WO2010010145A1 - Keratin-binding polypeptides and method for their identification - Google Patents

Abstract

The present invention pertains to keratin-binding polypeptides derived from the keratin-binding domain B (KBD-B) of desmoplakin, which have improved structural or functional properties in comparison to the native KBD-B. It furthermore pertains to the preparation of said polypeptides, to compositions comprising said polypeptides, and to their use in cosmetic and therapeutic applications. A method for identification of such improved keratin-binding proteins is also presented. Said method is based on a novel three dimensional model of keratin which is also part of present invention.

Description

Keratin-binding polypeptides and method for their identification

FIELD OF THE INVENTION

The present invention pertains to keratin-binding polypeptides derived from the keratin- binding domain B (KBD-B) of desmoplakin, which have improved structural or functional properties in comparison to the native KBD-B. It furthermore pertains to the preparation of said polypeptides, to compositions comprising said polypeptides, and to their use in cosmetic and therapeutic applications. A method for identification of such improved keratin-binding proteins is also presented. Said method is based on a novel threedimensional model of keratin which is also part of present invention.

BACKGROUND OF THE INVENTION

Keratins are a class of intermediate filaments occuring in vertebrate cells, hair, skin, hooves and nails. Specific proteins such as desmoplakin bind to keratin by means of special sequence motifs called keratin-binding domains (Fontao L et al., MoI Biol Cell. 2003; 14(5): 1978-92; Hopkinson SB and Jones JC, MoI Biol Cell. 2000;11 (1 ):277-86).

Keratins are the main constituents of structures that grow from the skin. In mammals, they occur in the hair (including wool), horns, nails, claws and hooves, but also as cytokeratins in the cytoskeleton of epithelial tissue.

Cytokeratins are intermediate filament keratins found in the intracytoplasmic cytoskeleton of epithelial tissue. There are two types of cytokeratins: the low weight, acidic type I cytokeratins and the high weight, basic or neutral type Il cytokeratins. Cytokeratins are usually found in pairs comprising a type I cytokeratin and a type Il cytokeratin. The group of high molecular weight cytokeratins, which are the basic or neutral cytokeratins, comprises subtypes CK1 , CK2, CK3, CK4, CK5, CK6, CK7, CK8 and CK9. The group of low molecular weight cytokeratins, which are the acidic cytokeratins, comprises subtypes CK10, CK12, CK 13, CK14, CK16, CK17, CK18, CK19 and CK20.

Cytokeratins do encompass skin keratins and are are structurally similar to hair keratins, as the latter do also form pairs comprising a type I and a type Il keratin. The group of acidic type I hair keratins comprises subtypes hHa1 (novel nomenclature: K31 ), hHa2 (K32), hHa3A (K33A), hHa3B (K33B), hHa4 (K34), hHa5 (K35), hHa6 (K36), hHa7 (K37) and hHaδ (K38). The group of basic type Il hair keratins comprises subtypes hHb1 (K81 ), hHb2 (K82), hHb3 (K83), hHb4 (K84), hHb5 (K85) and hHb6 (K86). The most important hair keratins are K32/82, K32/85, K35/85 and K35/82, the most important skin cytokeratins are CK5/14, CK1/10 and CK8/18. The structure of keratin in hair differs from keratin in skin mainly by the specific amino acid sequences. The coiled coil segments of their threedimensional structure resemble each other. Based on the particular functions, hair and nail keratins are further stabilized by associated matrix proteins not relevant in skin cells.

The close structural relationship between cytokeratins and hair keratins is demonstrated by the fact that desmoplakin does bind to the cytokeratin pair CK8/18 as well as to hair keratin (Choi et al., Nat Struct Biol. 2002, 9(8):612-620; Meng, JJ et al., J Bio Chem. 1997, 272:21495-21503; Norgett, EF et al., Human Molecular Genetics 2000, 9(18):2761 -2766). The pair cytokeratin 8 (neutral-basic) plus cytokeratin 18 (acidic) (cytokeratin 8/18, in short: CK8/18) forms keratin of the simple epithelium.

The present knowledge on keratin structure is summarized in Parry, DA and Steinert, PM, Q Rev Biophys 1999, 32:99-187. All cytokeratin chains are composed of a central α-helix-rich domain (with a 50-90% sequence identity among cytokeratins of the same type and around 30% between cytokeratins of different type) with non-α-helical N- and C-terminal domains. The central domain is generally called "rod domain", the N domain "head domain", the C domain "tail domain". The α-helical rod domain has 310-150 amino acids and comprises four segments in which a seven-residue pattern is repeated several times ("heptad repeat"). In this repeated pattern, the first and fourth residues are hydrophobic and the charged residues show alternate positive and negative polarity (especially the fifth and seventh residue are often basic or acidic), resulting in the location of the polar residues on one side of the helix. This central domain of the chain provides the molecular backbone of the keratin structure and makes the chains form coiled dimers in solution.

The four "heptad repeat" segments are designated 1A (35 amino acids), 1 B (101 amino acids in vertebrates), 2A (19 amino acids) and 2B (121 amino acids). 2B comprises a 4 amino acid discontinuity usually designated as "stutter". Moreover, there are two conserved regions in the C- and N-terminus of the complete heptad repeat sequence: 1 A contains a coserved sequence region designated as "helix initiation motiv" and represented by the amino acid sequence K/R-X-T/Q-M/l/L-K/Q-L-N-D-R-F-A-S-F/Y-l- D/E-K- V-R-F-L-E, and 2B contains a coserved sequence region designated as "helix termination motiv" and represented by the amino acid sequence E-Y-Q-X-L-L-D /N-V- K-X-R/A-L-D/E-X-E-I-A-T-Y-R-K/R-L-L-E-G-EE/D-X-R-L/N/I. The segments linking the heptad repeat segments are known as "linker" L1 , L12 and L2.

Up to now, no crystal structure of the head and tail domain exists, and merely short fragments of the rod domain have been characterized by X-ray structural analysis. The tertiary and quartary structure of keratin consist of pairs (heterodimers) comprising a type I cytokeratin and a type Il cytokeratin. In these dimers, the heptad repeat segments are aligned in parallel. The α-helical rod segments form a coiled coil stabilized by several interactions between the helices (Parry, DA and Steinert, PM, Q Rev Biophys 1999, 32:99-187; Strelkov, SV et al., Embo J 2002, 21 : 1255-66; Herrmann H and Aebi U, Annu Rev Biochem 2004, 73:749-89; Burkhard P et al., Structure 2000, 8:223-30). A threedimensional structure of a complete keratin coiled coil is lacking up to now.

Two dimers of cytokeratin group into a keratin tetramer by anti-parallel binding (Parry, DA and Steinert, PM, Q Rev Biophys 1999, 32:99-187). This cytokeratin tetramer is considered to be the main building block of the cytokeratin chain. By radial linking of eight cytokeratin tetramers, a cytokeratin filament is formed.

Desmoplakin, a protein of the plakin family, is a keratin binding protein. Human desmoplakin consists of a 1056 amino acid N terminal part, a 889 amino acid central "rod" part and a 926 amino acid C terminal part (the C-terminal part is also designated as DPCT). DPCT comprises three globular domains designated as domains A, B and C, respectively (Choi, HJ et al., Nat Struct Biol. 2002; 9:612-620). Domains A, B and C are responsible for the binding of desmoplakin to keratin in vivo. The native KBD-B and derivatives thereof, as well as their cosmetical and pharmaceutical use, are already mentioned in the prior art (WO 2005/115306, WO 2006/097432). Isolated KBD-B is able to bind to human hair and skin keratin.

The polypeptide sequence of human desmoplakin is given in SEQ ID NO:1. The native keratin-binding domain B of desmoplakin (KBD-B) is the polypeptide sequence represented by amino acids 2193 to 2481 of SEQ ID NO:1 (WO 2005/1 15306). A crystal structure of amino acids 2209 to 2456 of KBD-B is known (PDB-code:1 Im7, SEQ ID NO:49). A further keratin-binding domain (domain C, KBD-C) of desmoplakin is the polypeptide represented by amino acids 2606 to 2871 of SEQ ID NO:1 (WO 2005/115306). A crystal structure of amino acids 2609 to 2822 of KBD-C is known (PDB-code:1 lm5, SEQ ID NO:48).

The crystal structures of KBD-B and C have been published (Choi et al., Nat Struct Biol. 2002 9(8):612-620). It has been shown that KBD-B and KBD-C bind to the keratins CK8/18 and CK5/14, as well as to Vimentin (Choi, HJ et al., Nat Struc Biol 2002, 9:612-20; Fontao, I et al., MoI Biol Cell 2003, 14:1978-92; Meng et al., J Biol Chem 1997, 272:21495-503; Nicolic, B et al., J Cell Biol 1996, 134:1455-67). However, the location and mode of interaction between the KBDs and the bound keratin/vimentin structures remained unclear. For keratin, only a binding somewhere at the rod domain was proven, without any further detailed indication of the specific binding region inside the rod domain. Molecules binding to keratin are of considerable interest, especially for the pharmaceutical and cosmetic industry, as they allow the targeted transport and binding of active ingredients to keratin and keratin-comprising structures like skin, hair, leather, etc.. The targeted development of such keratin-binding molecules is, however, hampered by the fact that next to nothing is known about the exact target region on keratin, the three dimensional structure of said target region and the chemical properties of its surface. Thus, the molecular fit of a candidate compound to keratin is hard to predict. A prerequisite for a method allowing such prediction would be a reliable 3D model of the keratin target structure. As such model is lacking so far, there is a need for the development of such structure model and subsequently of said prediction method. This model would furthermore allow the search for molecules which are able to intercalate into keratin or to break a keratin barrier by disturbing the keratin spatial structure.

Isolated native KBD-B is able to bind to human hair and skin. However, up to now detailed informations on the mode and the exact location of interaction between keratin and KBD-B were lacking. Furthermore, due to the lack of data on the amino acids at the interface between KBD-B and keratin, a specific modification of the keratin-binding properties of the keratin-binding domain via amino acid mutations was not possible up to now. On the other hand, an inprovement of structural features like stability and solubility of the keratin-binding domain is desirable in order to increase its efficiency in pharmaceutical and cosmetic applications.

Thus, there is a need for a method allowing predictions on structural and functional properties of KBD-B, especially of its binding to keratin, and of modified KBD-B versions.

Up to date it is very difficult to identify interface residues of a protein complex using the available computational methods applied in the investigation of protein-protein interactions without any experimental data i.e. only based on the several structural coordinates of the complex partners. A fully rotational and conformational search in space is not feasible due to the multitude of combinatorial solutions and the computing time needed for such big systems. Rigid protein docking programs only produce static results not considering the induced fit adaption during complexation. Therefore, a critical assessment of every complex solution is required. Inclusion of water molecules, salts and appropriate pH value complicates the simulation protocols dramatically and has significant relevance to the transferability of the output. Last but not least the field of protein-protein-interactions is poorly understood. Thus, all predictions should be verified by experimental data. There is a need for a computer based model allowing the rational design of improved keratin-binding molecules.

OBJECT OF THE INVENTION

Thus, the objective of present invention is the provision of a method allowing the identification of keratin-binding molecules and of novel polypeptides identified by said method which have improved properties in comparison to the native keratin-binding domain B of desmoplakin.

SUMMARY OF THE INVENTION

According to one embodiment, novel keratin-binding polypeptides, compositions comprising one or more of said polypeptides, and the use of said polypeptides and compositions are provided.

According to another embodiment, a method for identifying keratin-binding molecules, especially keratin-binding polypeptides is provided. The keratin-binding polypeptides may be based on a known keratin-binding domain B (KBD-B), e.g. the amino acid sequence of KBD-B of desmoplakin, but possess improved properties in comparison to the native keratin-binding domain B of desmoplakin.

Improved properties of the novel peptides may be structural features like improved stability and/or solubility, or functional features like improved keratin-binding properties, increased mass efficiency or increased load density of keratin. Preferably, said polypeptides possess a high affinity to keratin or keratin-containing materials such as skin or hair. In one embodiment of present invention, the keratin affinity of the polypeptides is increased in comparison to native KBD-B. In a further embodiment of the invention, the peptides have an increased specifity for hair keratin in comparison to skin keratin or vice versa. The models used in present invention are based on CK8/18 (i.e. a skin keratin), but are suitable for identification of keratin-binding molecules with an improved binding to hair keratin, as demonstrated for the modified KDB-B molecules which are one embodiment of the invention. Thus, the models are applicable for identification of molecules binding to hair and/or skin keratin, and particularly of molecules having an increased hair or skin specifity. However, as outlined below, an increased hair specifity is especially preferred.

The keratin-binding polypeptides according to present invention are derived from the native keratin-binding domain B of desmoplakin as represented by amino acids 2250 to 2448, preferably by amino acids 2209 to 2448 of SEQ ID NO:1 by specific amino acid exchanges resulting in improved structural and/or functional properties of the modified KBD-B when compared to native KBD-B. Said polypeptides comprise an amino acid sequence wich differs from the sequence as represented by amino acids 2250 to 2448, preferably 2209 to 2448 of SEQ ID NO:1 by one or more amino acid exchanges as defined below in embodiment (1 ).

The polypeptides according to present invention are suitable for the treatment of keratin-comprising structures and tissues, in particular of hair and/or skin. Said treatment may be cosmetic or therapeutic.

The specific amino acid exchanges described in present invention may be derived from a model of the binding between KBD-B and keratin. Said model is provided according to another embodiment of the present invention and allows predictions on favourable and unfavourable amino acid exchanges in the amino acid sequence of native KBD-B. The accurateness of said predictions was confirmed by in vitro tests.

According to further embodiments, the keratin structure used in the model as well as its use in a method for identifying molecules which interact with keratin are provided.

In particular, the following embodiments of the invention are provided:

(1 ) an isolated keratin-binding polypeptide which comprises an amino acid sequence derived by at least one amino acid substitution from the native sequence of the desmoplakin keratin-binding domain B (KBD-B) as represented by amino acids no. 2250 to 2448 of SEQ ID NO:1 , wherein said at least one amino acid substitution conveys to the polypeptide at least one improved functional and/or structural property in comparison to native isolated KBD-B, or a homologue, functional variant, derivative or fragment of said keratin-binding polypeptide which comprises said at least one amino acid substitution and possesses the keratin-binding properties of said keratin-binding polypeptide;

(2) the keratin-binding polypeptide of embodiment (1 ), which comprises an amino acid sequence derived by at least one amino acid substitution from the native sequence of the desmoplakin keratin-binding domain B (KBD-B) as represented by amino acids no. 2209 to 2448, preferably 2193 to 2481 of SEQ ID NO:1 ;

(3) an isolated nucleic acid sequence encoding the keratin-binding polypeptide as defined in (1 ) or (2) above, or a nucleic acid complementary thereto;

(4) a vector comprising the nucleic acid sequence as defined in (3) above; (5) a cell being transformed or transfected with the vector as defined in (4) above and/or comprising the nucleic acid as defined in (3) above and/or being capable of expressing an keratin-binding polypeptide as defined in (1 ) or (2) above; (6) a composition comprising a keratin-binding polypeptide as defined in (1 ) or (2) above, or comprising a pharmaceutically and/or cosmetically acceptable functional variant thereof, which composition preferably is a pharmaceutical or cosmetic composition; (7) the use of the isolated keratin-binding polypeptide of (1 ) or (2) above or the composition (6) above for the treatment of keratin or a keratin-comprising material;

(8) the polypeptide according to embodiment (1 ) or (2) for use as a medicament; (9) a three-dimensional structure model of the rod domain of a keratin coiled coil formed by two keratin monomers (keratin model), comprising an amino acid sequence per monomer strand of at least 30, preferably at least 35, more preferably at least 39 consecutive amino acids of the native rod segment 1 B of said keratin; (10) use of the keratin structure model according to embodiment (9) for analysing the interaction between said keratin structure and a candidate molecule;

(1 1 ) a method for evaluating the interaction of a candidate molecule, preferably a candidate keratin-binding polypeptide, with keratin comprising the following steps:

(a) selecting a candidate molecule and a keratin;

(b) determining the interaction of the candidate molecule with the keratin structure model of embodiment (9) of said keratin by conducting a computer simulation of the interaction between said keratin structure model and a threedimensional model of the candidate molecule, wherein the steric and electrostatic interaction between the candidate molecule and the keratin structure are determined;

(12) the method according to embodiment (1 1 ), which is suitable for identification of keratin-binding polypetides with improved properties in comparison to KBD-B, and wherein the candidate molecule is a putative keratin-binding polypeptide, comprising the following steps:

(a) selecting a putative keratin-binding polypeptide and a keratin;

(b) determining the shape complementarity in a complex of said putative keratin-binding polypeptide with the rod domain of said keratin by conducting a computer simulation of the threedimensional arrangement of (i) the candidate keratin-binding polypeptide and (ii) the rod domain of said keratin;

(c) comparing the result to the result of the corresponding computer simulation of (i) native KBD-B and (ii) said keratin; and

(d) determining whether the differences between the putative keratin-binding polypeptide and KBD-B established in the comparison step (c) may lead to to the desired improvement; and

(13) a method for preparing the polypeptide as defined in (1 ) or (2) above or the polypeptide resulting from the method as defined in (12) above. FIGURE LEGENDS

Fig. 1 : Threedimensional model of the native keratin-binding domain B of human desmoplakin as represented by amino acids 2209 to 2448 of SEQ ID NO:1 ; two different perspectives are shown; light grey region: interface region.

Fig. 2: The rod sequences of CK8/18. Above each sequence, the coiled coil (light grey) and linker (dark grey) regions of the rod are indicated. Under the sequences, the heptad repeats are given ("abcdefg" is one complete hepad unit); therein, the positions of apolar residues are indicated in very light grey. In the amino acid sequences, acidic amino acids (E, D) and basic amino acids (R, K, H) are highlighted. Stut: stutter region. The rod of CK8/18 consists of 315 amino acids of each single cytokeratin chain. The first segment 1A begins respectively ends with the fourth amino acid in a heptad repeat. 1A consists of CK8 (SEQ ID NO:51 ) amino acids 83 to 125 and CK18 (SEQ ID NO:50) amino acids 73 to 1 15. The following linker L1 consists of 10 amino acids each. The next segment 1 B begins respectively ends on a third position of a heptad repeat and consists of CK8 amino acids 136 to 236 and CK18 amino acids 126 to 226. The following linker L12 consists of 17 amino acids each. The next segment 2A, positions 254 to 272 (CK8) and 244 to 262 (CK18), begins on a third position and ends on a seventh position of a heptad repeat. The linker L2 consists of 8 amino acids each. Segment 2B consists of amino acids 281 to 397 (CK8) and 271 to 387 (CK18), beginning respectively ending on a fourth position of a heptad repeat. Said segment is interrupted by the "stutter" discontinuity of amino acids 341 to 344 (CK8) and 331 to 334 (CK18), whereupon the heptad repeats are continued, starting on a first position.

Fig. 3: Alignment of keratin amino acid sequences forming the target region of KBD-B. Acidic, basic and aromatic amino acids are highlighted. The bottom line indicates the position of the heptad repeats.

Fig. 4: Final model of the rod segment of CK8/18.

Fig. 5: Paircoil Score indicating the ,,coiled coil" probability for the rod of CK8 (above) and CK18 (below). The segments wherein the score is below the dotted line have a high "coiled coil" probability, whilst the linker segment regions showing high peaks do probably not form coiled coils.

Fig. 6: Complex of KBD-B with the coiled coil of CK8/18. Above Left: complex geometry of coiled coil (up) and KBD-B (below), in horizontal constellation both keratin chains are supported by a KBD-B-loop. Below Left: same perspective as above, the coiled coil is located in a V-shaped valley of KBD-B; Right: lateral view of Below Left, the lower keratin chain is located lowly in the valley provided by KBD-B. Fig. 7: Region of CK8/18 bound by KBD-B. The figure shows segment 1 B. The region between the horizontal lines is the region bound by KBD-B. The horizontal lines designate the left and right border amino acids on K8 and K18: from K18-L159 and K8- G170 to K18-L197 and K8-V208.

Fig. 8: Molecular dynamics of complex between KBD-B F2416A and CK8/18. LJ: Lennard-Jones. When modeled with CK8/18 as keratin in Gromacs3.3 (molecular dynamics simulation), Hex4.1 and Sybyl (generation of complex), the interaction of F2416A KBD-B-mod. with CK8/18 results in a lower interaction energy (the sum of Coulomb potential and Lennard-Jones potential, which is a negative value, is higher than the sum for the native KBD-B) in comparison to native KBD-B. x-axis: time in ps, y-axis: interaction energy in kJ/mol.

Fig. 9: Localisation of amino acid exchanges in the interface of KBD-B. The interface is formed by the light grey and small black areas. All amino acid exchanges forming the small black surface areas led to decreased binding of keratin, exchange of L2358 and Y2339 led to degradation of the KBD-B-mod.

Fig. 10: Purification of KBD-B F2416A (compare example 7(C)). SDS-PAGE of protein fractions collected during purification by Ni-Sepharose (immobilized ion affinity chromatography). M, marker; 1 , cleared extract; 2, cleared extract after column; 3, first column wash; 4, second column wash; 5, eluted KBD-B F2416A protein fraction 1 ; 6, eluted KBD-B F2416A protein fraction 2; 7, eluted KBD-B F2416A protein fraction 3; 8, eluted KBD-B F2416A protein fraction 4; 9, eluted KBD-B F2416A protein fraction 5.

Fig. 11 : A) Fluorescence microscopy of KBD-B-Alexa Fluor 532-Conjugate bound to human hair (Excitation: 532 nm / Emission: 590 nm). B) Control-hair with Alexa Fluor 532 dye without KBD-B.

Fig. 12: Multiple sequence alignment using ClustalW of keratin and vimentin amino acid sequences (compare example 3).

TABLE LEGENDS The Protein Data Bank (pdb) file format used in the following tables is a textual file format describing the threedimensional structures of molecules held in the Protein Data Bank (for details see http://www.wwpdb.Org/documentation/format23/v2.3.html). As such, it contains atom position information (in the Coordinate Section) and sequence information along with information about the researchers who defined the structure and a citation. The Protein Data Bank (PDB) uses macromolecular Crystallographic Information File (mmCIF) data dictionaries to describe the information content of PDB entries (Chapter 3.6., Appendix 3.6.2. and Chapter 4.5 in International Tables for Crystallography G. Definition and exchange of crystallographic data, S. R. Hall and B. McMahon, Editors. 2005, Springer: Dordrecht, The Netherlands). Protein sequences in PDB are available for display and download in FASTA format (W. R. Pearson (1990) Methods in Enzymology 183, 63-98).

Legend to the tables is provided below and directly in the tables, especially in table 1. It is based on information from http://www-lehre.informatik.uni-osnabrueck.de/~okrone/ DIP/node25.html to ~ node27.html and http://www.wwpdb.Org/documentation/format2.3 -0108-a4.pdf: Header: indicates the name of the modeled protein chains

Remark: Name of the program used to generate the file and date of application SEQRES: List of all considered amino acid residues in 3-letter code ATOM: List of all atoms in the model.

Tab. 1 : Atom coordinates of the final threedimensional model of the rod domain without the linker regions of CK8/18 as generated by SYBYL. Chain A: CK 18 (SEQ ID NO:50), Chain B: CK 8 (SEQ ID NO:51 ), Chain segment sequences see Fig.2, Structure Visualization see Fig. 4.

Tab. 2: Atom coordinates of the final threedimensional model of the keratin backbone of CK8/18 as generated by SYBYL.

Tab. 3: Atom coordinates of the final threedimensional model of the rod domain of K35/85 as generated by SYBYL. Chain A: K35 (SEQ ID NO:58), Chain B: K85 (SEQ ID NO:62).

Tab. 4: Atom coordinates of the final threedimensional model of the protein-protein- complex between the rod domain of CK8/18 and KBD-B amino acids no. 2250 to 2448 of SEQ ID NO 1as generated by SYBYL. Chain A: CK8, Chain B: CK18, Chain C: KBD-B. Structure Visualization see Fig. 6. Chain A and B comprise the keratin segment bound by KBD-B and additionally 2 amino acids upstream and 4 amino acids downstream of said segment.

SEQUENCE LISTING, FREE TEXT

DEFINITIONS

The following abbreviations, terms and definitions are used herein:

KBD, keratin binding domain; KBD-B, keratin-binding domain B; the commonly used IUPAC one-letter symbols for amino acids; KBD-B-mod, modified keratin-binding domain B; CK, cytokeratin.

As used in the context of present invention, the singular forms of "a" and "an" also include the respective plurals unless the context clearly dictates otherwise. Thus, the term "a polypeptide" can include more than one peptide, namely two, three, four, five etc. peptide molecules.

The term "about" in context with a numerical value or parameter range denotes an interval of accuracy that the person skilled in the art will understand to still ensure the technical effect of the feature in question. The term typically indicates deviation from the indicated numerical value of +/- 10 %, preferably +/- 5 %.

Unless noted otherwise, all amino acid position numbers are the position numbers according to the native sequence of desmoplakin as represented by SEQ ID NO:1.

The abbreviations "CK8/18", "K8/18" and "K8/K18" (and corresponding groups of abbreviations using different integers) are synonyms for keratin heterodimers.

In the context of present invention, the term "keratin-binding domain B" (KBD-B) refers to the native keratin-binding domain B of desmoplakin as well as to the modified KBD-B introduced by present invention. Unless indicated otherwise, "native KBD-B" refers to the isolated native keratin-binding domain B of desmoplakin, i.e. the isolated domain B as represented by amino acids no. 2193 to 2481 (full-length native KBD-B) of SEQ ID NO:1 (SEQ ID NO:5), 2209 to 2456 (PDB 1 lm7) of SEQ ID NO:1 (SEQ ID NO:49), 2209 to 2448, or 2250 to 2448 (core KBD-B) of SEQ ID NO:1 without any single or multiple amino acid exchange. The latter sequences are encompassed by the former. They are all representing the native KBD-B, as its threedimensional properties and its binding affinity to keratin are not influenced by the segments represented by amino acids 2193 to 2249 and 2449 to 2481 of SEQ ID NO:1. The term "modified keratin- binding domain B" (KBD-B-mod) refers to the isolated keratin-binding polypeptide of embodiment (1 ) or (2) of the invention, i.e. an isolated KBD-B as represented by amino acids no. 2250 to 2448, 2209 to 2448 or 2193 to 2481 of SEQ ID NO:1 wherein at least one amino acid exchange according to present invention has occurred. The term "KBD- B" followed by an indication of an amino acid substitution (e.g. G2362I) refers to a KBD-B sequence modified by said amino acid exchange (e.g. "KBD-B G2352I").

The "interface" or "interface region" of a native or modified KBD-B is the region which hosts the bound keratin. The interface is further specified by those amino acids inside the interface region which are in immediate contact to keratin.

"Native" is a synonym for "naturally occurring".

The term "isolated" means "separate or purified from its organism of origin". More specifically, an isolated polypeptide, protein or nucleic acid is separate or has been purified from its organism of origin. This encompasses biochemically purified, recombinantly produced and chemically synthesized polypeptides, proteins or nucleic acids.

Whenever the size or relative size of an amino acid is mentioned in the context of present invention, this term pertains to the van der Waals volume of the amino acid side chain. The following table indicates the relevant van der Waals volumes and the amino acids considered as "small" (marked with "X"): Amino Acid Small van der Waals volume

Alanine X 67

Cysteine X 86

Aspartic acid X 91

Glutamic acid - 109

Phenylalanine - 135

Glycine X 48

Histidine - 118 lsoleucine - 124

Lysine - 135

Leucine - 124

Methionine - 124

Asparagine X 96

Proline X 90

Glutamine - 114

Arginine - 148

Serine X 73

Threonine X 93 Selenocysteine X

Valine X 105

Tryptophan - 163

Tyrosine - 141

A "homologue" in the context of present invention is a protein or polypeptide which possesses the at least one amino acid substitution indicated in embodiment (1 ) or (2), the keratin-binding properties and the further structural and functional properties of the polypeptide as defined in embodiment (1 ) or (2), but differs from said polypeptide in its amino acid sequence in that in addition to the at least one amino acid exchange, especially to the exchanges listed under (a) to (n) hereinafter in the "detailed description" section, one or more amino acids at positions different from the position of said at least one amino acid exchange are substituted. Preferably, the function and/or conformation of the polypeptide is not affected by the additional substitutions. More preferably, the said additional amino acid substitutions are conservative, i.e. said amino acids are substituted by amino acids with similar chemical properties, e.g. VaI by Ala (conservative amino acid exchange). The ratio of additional substituted amino acids in comparison to the polypeptide sequence as defined in embodiment (1 ) or (2) is preferably from 0 to 30 % of the total amino acids of KBD-B, more preferably from 0 to 15%, most preferably from 0 to 5%.

Conservative amino acid exchanges are preferably between the members of one of the follwing amino acid groups: - acidic amino acids (aspartic and glutamic acid); basic amino acids (lysine, arginine, histidine); hydrophobic amino acids (leucine, isoleucine, methionine, valine, alanine); hydrophilic amino acids (serine, glycine, alanine, threonine); amino acids having aliphatic side chains (glycine, alanine, valine, leucine, isoleucine); amino acids having aliphatic-hydroxyl side chains (serine, threonine); amino acids having amide-containing side chains (asparagine, glutamine); amino acids having aromatic side chains (phenylalanine, tyrosine, tryptophan); amino acids having basic side chains (lysine, arginine, histidine); - amino acids having sulfur-containing side chains (cysteine, methionine).

Specifically preferred conservative amino acid exchanges are as follows:

Native residue Substituting residue

Ala Ser

Arg Lys

Asn GIn; His

Asp GIu Cys Ser

GIn Asn

GIu Asp

GIy Pro

His Asn; GIn

Ne Leu; VaI

Leu lie; VaI

Lys Arg; GIn; GIu

Met Leu; Ne

Phe Met; Leu; Tyr

Ser Thr

Thr Ser

Trp Tyr

Tyr Trp; Phe

VaI lie; Leu

The homologues according to present invention can be generated by mutagenesis, e.g. by point mutations, site directed mutagenesis or random mutagenesis of the native KBD-B sequence, or by chemical polypeptide synthesis, preferably by site directed mutagenesis. Furthermore, homologues of the polypeptides according to the invention can be identified by screening combinatorial libraries of desmoplakin or KBD-B mutants, such as, for example, random mutants. For example, a library of protein variants can be generated by combinatorial mutagenesis at the nucleic acid level, such as, for example, by enzymatic ligation of a mixture of synthetic oligonucleotides. There is a large number of methods which can be used to prepare libraries of potential homologues from a degenerate oligonucleotide sequence. Chemical synthesis of a degenerate gene sequence can be carried out in an automatic DNA synthesizer, and the synthetic gene can then be ligated into a suitable expression vector. The use of a degenerate set of genes makes it possible to provide all the sequences which encode the desired set of potential protein or polypeptide sequences in one mixture. Methods for synthesizing degenerate oligonucleotides are known to a person skilled in the art (e.g. Narang, S.A. (1983) Tetrahedron 39:3; ltakura et al. (1984) Annu. Rev. Biochem. 53:323; ltakura et al. (1984) Science 198:1056; Ike et al. (1983) Nucleic Acids Res. 1 1 :477). Several techniques are known in the art for screening gene products in combinatorial libraries which have been prepared by point mutations or truncation, and for screening cDNA libraries for gene products having a selected property. These techniques can be adapted to the rapid screening of gene libraries which have been generated by combinatorial mutagenesis. The most commonly used techniques for screening large gene libraries, which are subject to high-throughput analysis, include the cloning of the gene library into replicable expression vectors, transformation of suitable cells with the resulting vector library and expression of the combinatorial nucleic acid sequences under conditions under which detection of the desired activity facilitates isolation of the vector which encodes the gene whose product has been detected. Recursive ensemble mutagenesis (REM), a technique which increases the frequency of functional mutants in the libraries, can be used in combination with the screening tests to identify homologues (Arkin and Yourvan (1992) PNAS 89:7811- 7815; Delgrave et al. (1993) Protein Engineering 6(3):327-331 ).

Further homologues encompassed by the invention are homologues of the specifically disclosed polypeptides according to embodiment (1 ) which have a homology of at least 50%, preferably at least 75%, more preferably at least 85%, such as, for example, 90%, 95% or 99%, to the amino acid sequence of the polypeptide of embodiment (1 ), in a preferred aspect of the invention to one of the specifically disclosed amino acid sequences according to embodiment (1 ) (calculated by the algorithm of Pearson and Lipman, Proc. Natl. Acad. Sci. (USA) 85(8), 1988, 2444-2448), under the proviso that said homologues possess the at least one amino acid substitution indicated in embodiment (1 ) or (2), as well as the keratin-binding properties and the further structural and functional properties of the polypeptide as defined in embodiment (1 ) or (2). A percentage homology of a homologous polypeptide of the invention means in particular the percentage identity of the amino acid residues at the corresponding amino acid positions in one of the amino acid sequences specifically described herein.

If it is desired that the polypeptide sequences are particularly suitable for binding to a keratin from a non-human organism, the amino acid exchanges in the homologue selected as suitable will preferably encompass specific amino acids from the keratin- binding protein, e.g. desmoplakin or plectin, of the corresponding organism. Further suitable homologues of the polypeptide of present invention with good binding to keratin do comprise sequence regions which show high homology or sequence identity in an alignment and can be regarded as consensus sequences of keratin-binding domains.

A "fragment" of the polypeptide as defined in embodiment (1 ) or (2) of the invention is the result of deletion of one or more consecutive amino acids at the N and/or C terminus of the polypeptide as defined in embodiment (1 ) or (2). Said fragment must still possess the at least one amino acid substitution, the keratin-binding properties and the further structural and functional properties of the initial polypeptide. Thus, the minimum length of said fragment is determined by its ability to bind keratin like the initial polypeptide. Preferably, said fragment comprises the complete interface region of the initial polypeptide. In a further preferred aspect, said fragment lacks up to 50 amino acids in comparison to KBD-B, more preferably up to 30 amino acids, even more preferably up to 10 amino acids and most preferably a maximum of 5 amino acids. The lacking amino acids are in a preferred aspect consecutive amino acids of the N- and/or C-terminus of KBD-B. Neither N- nor C-terminus of the native KBD-B are involved in binding keratin, as no amino acid of these regions is part of the interface between keratin and KBD-B. Thus, in a further preferred aspect, the complete or partial amino acid sequence as represented by amino acids 2193 to 2249 (preferably including the complete or partial sequence of amino acids 2193 to 2209) of SEQ ID NO:1 and by amino acids 2447 to 2481 (preferably including the partial or complete sequence of amino acids 2449 to 2481 ) of SEQ ID NO:1 are lacking in the fragment.

A "derivative" of the polypeptide as defined in embodiment (1 ) or (2) of the invention is a polypeptide derived from said polypeptide by addition and/or deletion of one or more amino acids, under the proviso that said derivative still possesses the at least one amino acid substitution indicated in embodiment (1 ) or (2), the keratin-binding properties and the further structural and functional properties of the polypeptide as defined in embodiment (1 ) or (2). However, the term "derivative" does not encompass fragments as defined in the preceding paragraph.

The addition products are polypeptides or proteins (including fusion proteins) resulting from addition of any number of amino acids, preferably from addition of 1-300, more preferably 1-100, even more preferably 1-40, even more preferably 1-20 amino acids to the polypeptide as defined in embodiment (1 ) or (2). The added amino acids may be added as single amino acids or in continuous segments containing 2 or more linked amino acids. Said addition may take place at the N and/or C terminus and/or inside of the polypeptide of embodiment (1 ) or (2). More than one addition per polypeptide is allowed, but a single addition is preferred. Moreover preferred is an addition at the N and/or C terminus.

A precursor of the polypeptide of embodiment (1 ) or (2) is also considered to be an addition derivative in the meaning of present invention under the proviso that the polypeptide resulting from the processing of said precursor possesses the properties as defined in embodiment (1 ) or (2).

The deletion products result from deletion of any number of amino acids, preferably from deletion of 1-50, more preferably 1-20 amino acids from the polypeptide of embodiment (1 ) or (2). The deleted amino acids may be deleted as single amino acids or in continuous segments containing 2 or more linked amino acids. Said deletion may take place inside the initial polypeptide, and may additionally encompass deletions at the N or C terminus. More than one deletion per polypeptide is allowed, but a single deletion is preferred. Especially preferred are derivatives wherein the additions and deletions took place solely outside of the interface region of KBD-B, i.e. outside of the region binding directly to keratin (compare Fig.1 and example 5). A "functional variant" of the polypeptide according to embodiment (1 ) or (2) of the invention is either a salt, or it is a fusion peptide of said polypeptide ("keratin-binding domain") with at least one second functional protein domain or functional non- proteinaceous component ("second domain"). The second domain is preferably conveying a specific functional property to the functional variant, and is more preferably selected from the group of active ingredients and effector molecules as described in detail below and in the "detailed description" section.

A second functional protein domain is preferably in functional N- or C-terminal linkage to the keratin-binding polypeptide (i.e. with negligable mutual functional impairment of both domains of the fusion peptide). Said second functional protein domain is more preferably a further desmoplakin domain, a marker protein, a signal peptide, an enzyme, or a proteinaceous active ingredient or effector molecule as described below in the "detailed description section". It is in one preferred aspect selected from the group consisting of oxidases, peroxidases, proteases, tyrosinases, lactoperoxidases, lysozymes, amyloglucosidases, glucose oxidases, superoxide dismutases, photolyases, katalases, silk proteins, small molecule binding proteins, functional peptides, inorganic material binding peptides, antimicrobial peptides and self assembling proteins.

Said non-proteinaceous second domain may be selected from non-native chemical compounds, polysaccharides and lipids. It is especially selected from the non- proteinaceous effector molecules and active ingredients as described below in the "detailed description" section.

The term "salt" encompasses salts of one or more carboxyl groups and/or acid addition salts of one or more amino groups of the polypeptides of present invention. Salts of carboxyl groups can be prepared in a manner known per se and encompass inorganic salts such as sodium, calcium, ammonium, iron and zinc salts, and salts with organic bases such as amines including triethanolamine, arginine, lysine, piperidine and the like. Acid addition salts are salts such as salts with mineral acids such as hydrochloric acid or sulfuric acid and salts with organic acids such as acetic acid and oxalic acid. Said salts include also the corresponding solvates. Preferred salts in the context of present invention are pharmaceutically and/or cosmetically acceptable salts.

A functional variant can be prepared by means of known techniques via derivatisation of functional amino acid side groups or of the N- or C-terminal end of the polypeptide according to embodiment (1 ). Such derivatives include esters or thioesters of carboxylic acid groups, amides of carboxylic acid groups, obtainable by reaction with ammonia or with a primary or secondary amine; N-acyl derivatives of free amino groups prepared by reaction with acylating agents; N-alkyl derivatives of free amino groups prepared by reaction with alkylating agents; S-acyl derivatives of free mercapto groups prepared by reaction with acylating agents; thioethers by reaction of free mercapto groups with alkylating agents; disulfides by reaction of free mercapto groups, for example with thiols; O-acyl derivatives of free hydroxy groups prepared by reaction with acylating agents; or ethers by reaction of free hydroxyl groups with alkylating agents.

In the case of possible protein glycosylation, the term "functional variant" includes proteins and polypeptides as defined above in deglycosylated or glycosylated form, and modified forms obtainable by altering the glycosylation pattern.

In the case of possible protein phosphorylation, the term "functional variant" includes proteins and polypeptides as defined above in dephosphorylated or phosphorylated form, and modified forms obtainable by altering the phosphorylation pattern.

The term "pharmaceutically/cosmetically acceptable" as used herein means that a compound which is safe and effective for topical or systemic use in mammals and that possesses the desired biologica activity. In a "pharmaceutically/cosmetically acceptable salt", the counter ion is suitable for the intended use, non-toxic, and it dos not interfere with the desired biological action. Pharmaceutically acceptable salts in the context of present invention include the salts reveiwed in the IUPAC Handbook of

Pharmaceutically Acceptable Salts (Wermith, CG and Stahl, PH, Pharmaceutical Salts: Properties, Selection and Use - A Handbook; Verlag Helvetica Chimica Acta (2002)). "Pharmaceutically/cosmetically acceptable functional variants" of the polypeptides of present invention are functional variants which are safe and effective for the intended pharmaceutal or cosmetic use.

A "functional" feature or property of a compound, in particular of a polypeptide, is a characteristic chemical or physical property of the molecule determining its function or parts thereof. Specific functional features of a polypeptide are its catalytic activity, binding to surfaces, binding of small ligands, solubility and stability in solution. Of these, one or more than one of the following are preferably improved for the poylpeptides of present invention: keratin-binding properties, load density, solubility, specifity for hair keratin in comparison to skin keratin, binding strength (i.e. permance on hair while washing (resistance)), and resistance against detergents. A "structural" feature or property of a compound, in particular of a polypeptide, is a characteristic chemical or physical property of the molecule determining its threedimensional form, the location and interaction of its amino acids, and its stability. Specific structural features of a polypeptide of present invention are the shape of the binding-site to keratin and interaction of amino acids within the binding site. Of these, the following are preferably improved for the poylpeptides of present invention: stability, monomer/dimer ratio, solubility, shape of the keratin binding site and the and interaction of amino acids within the binding site. Polypeptide "stability" is the ability of a polypeptide to retain its three-dimensional form and keratin-binding function under standard application conditions and preferably even under harsh conditions, i.e. at low or high temperature, in the presence of salt, detergents, organic solvents, thickeners, fatty acids, in the presence of cosmetic ingredients and cosmetic formulations as listed below in the "detailed description section" and as shown in examples 12-41 , or during and after the chemical coupling to a second molecule and in presence of such coupled molecule (second domain), e.g. of an effector molecule. Polypeptide stability can be determined by measuring the hair- binding activity using the colorimetric assay described in example 8 under specific test conditions. The higher the absorption the more polypeptide is bound to keratin and the higher is the stability of the polypeptide at the given condition. "Solubility" indicates the ability of a substance to dissolve in aqueous solutions or any other liquid material. It is defined as the maximum amount of polypeptide that will dissolve in a given amount of solvent at a given temperature, and especially in the presence of detergents, thickeners, fatty acids and other cosmetic ingredients or in cosmetic formulations as listed below in the "detailed description section" and as shown in examples 12-41.

"Load density" of a keratin is the maximum amount of polypeptide that binds to a given surface of keratin, especially to the surface of hair. Load density can be determined by measuring the maximum hair-binding activity of a polypeptide at saturating concentrations as described in example 8. The higher the absorbance, the higher is the load density at a given polypeptide concentration.

Generally, the structure of a polypeptide or protein determines its functional properties. Thus, structural and functional features in present invention are often, if not always, connected.

An "improvement" of a structural or functional property of a polypeptide is a positive change or outcome of a change of the initial polypeptide. Said change can preferably be predicted and/or be measured through assessment.

An "active ingredient" of a pharmaceutical or cosmetic composition is a compound in a medicament or cosmetic, respectively, which produces a specific effect for which the composition is designed. For example, a dyeing compound is the active ingredient of a hair dye (i.e. cosmetic composition), and an antifungal is the active ingredient of a medicament for the treatment of candidosis (i.e. pharmaceutical composition). Some cosmetics or medicaments may comprise more than one active ingredient.

A "candidate molecule" is a molecule which is tested on its binding to keratin in one of the methods using an interaction model according to present invention. Preferably, it is a molecule whose keratin-binding abilities are known, predicted or suspected. It may be non-proteinaceous or proteinaceous, and preferably is a polypeptide ("candidate polypeptide"). More preferably, it is derived from a known keratin-binding polypeptide, and it is tested in order to evaluate the influence of the modification on its keratin- binding properties.

The term "keratin-binding" indicates that a molecule, especially a polypeptide or protein is able to bind to keratin. The intensity of the keratin binding is characterized by the maximum amount of polypeptide that binds to a given quantity of keratin, e.g. hair. The "keratin-binding properties" of a polypeptide can be determined by one of the binding assays described in examples 8, 9 or 10, preferably by the assay described in example 8. Keratin-binding properties can be determined by measuring the minimum concentration of polypeptide that is necessary to achieve saturation of keratin binding. The binding of polypeptide at different concentrations and the maximum amount of polypeptide that binds to hair can be determined by the colorimetric assay described in example 8 at saturating concentration of the polypeptide. Saturation of keratin binding is achieved when an increase in polypeptide concentration does no longer lead to an increased absorbance. The higher the absorption, the more polypeptide is bound to the keratin, or the higher is the affinity between the keratin-binding peptide and the keratin. Thus, an absorption lower than 5% of the absorption achieved with native KBD-B ("relative absorption") means that a polypeptide is not keratin-binding, a relative absorption from 5% up to 50% means weak keratin-binding, from 50% up to 75% means medium keratin binding, from 75% up to 100% means normal keratin binding, from more than 100% means strong keratin binding, and from at least 130% means very strong keratin binding.

Preferred keratin-binding polypeptides in the context of present invention are at least weak keratin binding, more preferably medium keratin-binding, even more preferably normal keratin-binding or strong keratin-binding, most preferably very strong keratin- binding polypeptides.

A polypeptide according to present invention has "improved keratin-binding properties" (synonym: "increased keratin affinity") when in at least one of the quantitative binding assays described in examples 8 and 10, preferably in the assay described in example 8, it shows a quantitatively increased binding to keratin in comparison to a polypeptide consisting of the native amino acid sequence of KBD-B as represented by amino acids 2193 to 2481 of SEQ ID NO:1 , i.e. when it shows strong keratin binding. Said increase is measured in % of the reference value shown by said native isolated KBD-B (which is the 100% value). Thus, the keratin binding of a polypeptide with improved keratin- binding properties exceeds 100%. Preferably, the keratin binding of a polypeptide with improved keratin-binding properties is at least 105%, more preferably at least 110%, even more preferably at least 130%, 150%, most preferably at least 175% of the reference value for native KBD-B. Vice versa, a polypeptide according to present invention has "reduced keratin-binding properties" when in at least one of the quantitative binding assays described in examples 8 and 10, preferably in the assay decribed in example 8, it shows a quantitatively decreased binding to keratin in comparison to a polypeptide consisting of the native amino acid sequence of KBD-B as represented by amino acids 2193 to 2481 of SEQ ID NO:1. Said decrease is measured in % of the reference value shown by said native isolated KBD-B. Thus, the keratin binding of a polypeptide with reduced keratin- binding properties is lower than 100%. Preferably, the keratin binding of a polypeptide with reduced keratin-binding properties is at most 75%, more preferably at most 50%, even more preferably at most 10%, most preferably at most 5% of the reference value for native KBD-B.

DETAILED DESCRIPTION OF THE INVENTION The present invention pertains to an isolated keratin-binding polypeptide as defined in embodiment (1 ), preferably as defined in embodiment (2), its preparation and its use in cosmetical and therapeutical applications.

It is understood that, unless indicated otherwise, the term "keratin-binding polypeptide" does also encompass the homologues, functional variants, fragments and derivatives of the polypeptide as defined in embodiments (1 ) or (2) or a combination of said homologues, functional variants, fragments and derivatives. However, in each embodiment of present invention, the keratin-binding polypeptide according to embodiments (1 ) or (2) without any further modification to a homologue, functional variant, fragment or derivative is preferred, unless indicated otherwise.

The keratin-binding polypeptide according to present invention comprises, and preferably is a mutant of the native KBD-B, especially of the native KBD-B represented by amino acids no. 2250 to 2448 of SEQ ID NO:1 wherein one or more specific amino acid substitutions have occurred. Preferably, the number of amino acid substitions is 1 to 10, more preferably 1 to 5, even more preferably 1 or 2. In one most preferred aspect, only one amino acid substitution has occurred.

The present invention furthermore relates to compositions for treating keratin or keratin-containing materials, comprising at least one keratin-binding polypeptide as defined in embodiment (1 ) or (2). The treatment is preferably a cosmetic or pharmaceutical treatment.

The polypeptide according to embodiment (1 ) of the invention is a keratin-binding polypeptide. Its structural and/or functional properties are improved in comparison to the native isolated KBD-B as represented by amino acids 2250 to 2448, preferably 2209 to 2448, more preferably in comparison to the isolated KBD-B as represented by amino acids 2193 to 2481 of SEQ ID NO:1. In other words, it differs in at least one functional and/or structural property from the corresponding native KBD-B, and said difference constitutes an improvement.

Such improvement is preferably at least one improved property selected from the group consisting of an increased stability, improved keratin-binding properties, increased load density, an increased solubility, an increased specifity for hair keratin in comparison to skin keratin or vice versa, and/or such improvement resides in that the polypeptide according to embodiment (1 ) or (2) is not part of a KBD-B dimer (i.e. is a monomer). More preferably, only one or two improved properties are the result of the amino acid substitution in the native KBD-B sequence, most preferably only one structural and/or functional property is improved.

In a first especially preferred aspect, the improvement is an increased stability of the poylpeptide of present invention in comparison to the corresponding native isolated KBD-B. For definition of "stability", see above. An increase of stability is any stability increase in comparison to native isolated KBD-B. Said stability of the polypeptide of present invention is preferably at least 1 10 % of native KBD-B stability, more preferably at least 130 %, more preferably at least 150 %. Especially preferred is an increased stability (resistance) against detergents.

In a second especially preferred aspect, the improvement is an improved keratin- binding of the poylpeptide of present invention in comparison to corresponding native isolated KBD-B. For definition of "keratin-binding", see above. Generally, the keratin- binding of the polypeptide of present invention should amount to at least 75 % of the saturation concentration of native KBD-B binding to keratin, especially to hair keratin (e.g. saturation concentration as determined in example 8). However, when an improved keratin-binding is involved, said improved keratin-binding exceeds the keratin-binding (i.e. saturation concentration as determined in example 8) of native KBD-B as outlined above in the "definitions" section. Preferably, it exceeds the keratin- binding of native KBD-B by amounting to at least 110 % of native KBD-B keratin- binding, more preferably at least 130 %, more preferably at least 150 %. A specifically preferred aspect of the improved keratin-binding is an increase in binding strength, i.e. the permanence of the keratin-binding polypeptide on the keratin, especially on hair during washing is higher than that of native KBD-B.

In a third especially preferred aspect, the improvement is an increased load density of the keratin by the poylpeptide of present invention in comparison to corresponding native isolated KBD-B. For definition of "load density", see above. Generally, the load density should not sink below the load density of native KBD-B. An increased load density is at least 1 10 % of native KBD-B load density, more preferably at least 130 %, even more preferably at least 150 %. In a fourth especially preferred aspect, the improvement is an increased solubility of the poylpeptide of present invention in comparison to corresponding native isolated KBD-B. For definition of "solubility", see above. Generally, the solubility should not sink below the solubility of native KBD-B. An increased solubility is at least 1 10 % of native KBD-B solubility, more preferably at least 130 %, even more preferably at least 150 %.

In a fifth especially preferred aspect, the improvement is an increased specifity of the poylpeptide of present invention for hair keratin in comparison to skin keratin or vice versa. Specificity is the ability of the polypeptide to discriminate between hair and skin keratin. To test whether a polypeptide has an altered specificity its hair and skin binding properties can be determined using the assays described in examples 8 and 10.

A polypeptide with increased specificity for skin or hair, respectively, would lead to an increased difference between the amount of polypeptide bound to skin vs. hair and vice versa. Preferably, in the assay described in examples 8 and 10, the relative absorption for skin vs. hair or vice versa is increased. In a specific aspect, a polypeptide with increased specifity for skin would lead to a increased or unaltered absorption in the skin binding assay whereas the signal in the hair binding assay would be lower. A polypeptide with increased specificity for hair would lead to a increased or unaltered absorption in the hair binding assay whereas the signal in the skin binding assay would be lower.

In one preferred aspect, a polypeptide according to present invention with increased specificity for hair in comparison to skin is thus a polypeptide showing unaltered or increased absorption in the hair binding assay and a decrease of absorption in the skin binding assay in comparison to native KBD-B, said decrease preferably leading to 75 % or less of the absorption of native KBD-B, more preferably to 60 % or less, even more preferably to 40 % or less. Vice versa, in a second preferred aspect, a polypeptide according to present invention with increased specificity for skin in comparison to hair is thus a polypeptide showing unaltered or increased absorption in the skin binding assay and a decrease of absorption in the hair binding assay in comparison to native KBD-B, said decrease preferably leading to 75 % or less of the absorption of native KBD-B, more preferably to 60 % or less, even more preferably to 40 % or less. In a third preferred aspect, a polypeptide according to present invention with increased specificity for hair in comparison to skin is thus a polypeptide showing unaltered or decreased absorption in the skin binding assay and an increase of absorption in the hair binding assay in comparison to native KBD-B, said increase preferably leading to 1 10 % or more of the absorption of native KBD-B, more preferably to 130 % or more, even more preferably to 150 % or more. Vice versa, in a fourth preferred aspect, a polypeptide according to present invention with increased specificity for skin in comparison to hair is thus a polypeptide showing unaltered or decreased absorption in the hair binding assay and an increase of absorption in the skin binding assay in comparison to native KBD-B, said increase preferably leading to 1 10 % or more of the absorption of native KBD-B, more preferably to 130 % or more, even more preferably to 150 % or more.

In a sixth especially preferred aspect, the poylpeptide of present invention is a monomer. When the polypeptide is a monomer, it is able to bind to keratin as a monomer, and/or it is present as a monomer in solution and/or crystalline form. Preferably, it is present as a monomer in solution. This may improve the mass efficiency of the polypeptide (doubling it by reducing the mass binding to keratin), its solubility and/or its diffusion koefficient (leading to faster binding to keratin) in comparison to isolated native KBD-B which generally forms a dimer in solution.

A combination of two or more of the listed especially preferred improved properties in one polypeptide is also possible. Of these combinations, a combination wherein one of the improved properties are improved keratin-binding properties is most preferred.

Most preferably, the at least one improved property is selected from the group consisting of improved keratin-binding properties and increased specifity for hair keratin in comparison to skin keratin, more preferably is an improved keratin binding in comparison to the native isolated KBD-B.

The structural and/or functional improvement may be connected to the keratin-binding activity of the KBD-B-mod. In a first preferred aspect of embodiment (1 ) or (2), the structural or functional improvement is not accompanied by a loss of keratin-binding activity. More preferably, the improvement encompasses improved keratin-binding properties of the polypeptide in comparison to the native KBD-B.

However, there may be cases wherein a structural and/or functional improvement is advantageous even when the keratin-binding properties of the poylpeptide are reduced. A second preferred aspect of embodiment (1 ) or (2) encompasses these cases wherein the polypeptide has reduced keratin-binding properties.

The improved properties of the polypeptide according to present invention are the result of at least one amino acid substitution in the native amino acid sequence of KBD- B as represented by amino acids 2250 to 2448, preferably 2209 to 2448 of SEQ ID NO:1. In order to identify the most promising amino acid positions for such substitutions, a computer-based model for the interactions between KBD-B and keratin was established in the course of present invention (examples 5 and 6, table 4). The aim of the modeling project was the identification of the amino acids that form the keratin binding interface of the human desmoplakin keratin binding domain B. The resulting model allowed for the first time an identification of those amino acids which form the immediate interface between KBD-B and the bound keratin section. A representation of the interface is given in Fig. 1.

The following amino acids of the KBD-B amino acid sequence define the interface between native KBD-B and keratin ("keratin-binding interface"): R2284, P2285, G2286, T2287, L2289, E2290, E2293, E2327, K2328, S2331 , R2334, Y2339, N2340, P2342, E2343, G2345, E2357, L2358, I2359, E2360, G2362, H2363, R2366, D2410, D2411 , K2413, G2414, F2416, E2421 , E2422 and N2423. Said interface amino acids are therefore preferred locations of the one or more amino acid substitutions according to embodiments (1 ) and (2) in order to modify and especially improve the keratin-binding properties of KBD-B. Especially preferred locations for amino acid exchanges at the interface are selected from the group consisting of

(i) F2416, L2358, Y2339, K2328, S2331 , R2284, G2286, S2331 , R2334,

E2293, G2362, H2363, and E2421 , as a substitution of said amino acids has an immediate effect on the binding properties of KBD-B (compare examples 6 to 8); and (ii) I2359, P2342, F2416, L2358, Y2339, R2366, K2413, E2360, R2284,

K2328, E2421 , D2410, K2413 and F2416, as said amino acids form direct electrostatic (including lipophilic) links to keratin or are sterically favourable (compare table 5).

Members of the group (i) are more preferred, members of the intersection of groups (i) and (ii) are most preferred.

Table 5: Interactions between keratin and KBD-B. The lower case letters in column 3 indicate the heptad repeat position of the amino acid.

In an alternatively preferred aspect of embodiment (1 ) or (2), the location of the at least one amino acid substitution is selected from one or more amino acids of amino acids no. 2280-2430 of SEQ ID NO:1. This sequence part encompasses the interface amino acids listed above and its modification may therefore have immediate influence on the keratin-binding properties of the KBD-B.

Of most preference are substitutions of one or more of the amino acid residues R2284, P2285, G2286, T2287, L2289, E2290, E2293, E2327, K2328, S2331 , R2334, Y2339, N2340, P2342, E2343, G2345, E2357, L2358, I2359 , E2360, G2362, H2363, R2366, D2410, D2411 , K2413, G2414, F2416, E2421 , E2422, N2423 (reflecting the crucial binding interface) or subsitutions of their immediate neighbouring amino acids, i.e. amino acids at positions +/- 2 or 1 up- or downstream of the interface amino acids.

Further preferred are substitutions of one or more of the amino acid residues K2361 , E2324 and E2448 or substitutions of their immediate neighbouring amino acids, i.e. amino acids at positions +/- 2 or 1 up- or downstream of the interface amino acids, as said amino acids may be involved in the binding of KBD-B to keratin.

There exist further preferred regions of KBD-B which are suitable targets for improving the specific properties of isolated KBD-B. Such regions provide advantageous structural and/or functional properties to KBD-B. In a preferred aspect of present invention, they are responsible for stabilizing the secondary or tertiary structure of isolated KBD-B, for the solubility of isolated KBD-B, and/or for the formation of dimers by the isolated KBD-B in a solvent or during crystallisation. The amino acid exchanges according to embodiment (1 ) or (2) of present invention in said regions lead preferably to an increase in stability and/or solubility, and/or to a decrease in dimer formation. Preferred regions of amino acid exchange according to this aspect of embodiment (1 ) or (2) are: the surface of isolated KBD-B except the interface region, regions stabilizing the secondary or tertiary structure of isolated KBD-B, and regions responsible for the formation of KBD-B dimers in a solvent or during crystallization. More preferably, the at least one amino acid substitution according to embodiment (1 ) or (2) takes place at one or more of the amino acids D2407, E2422, E2403, S2406, R2249, R2229 and T2232 or at one of their immediate neighbouring amino acids, i.e. amino acids at positions +/- 2 or 1 up- or downstream of the interface amino acids.

Thus, a keratin-binding polypeptide according to embodiment (1 ) or (2), wherein at least one position of the at least one amino acid substitution is within one of the following regions:

- in the keratin binding interface of KBD-B,

- in a region stabilizing the secondary or tertiary structure of isolated KBD-B,

- at the surface of isolated KBD-B, or - in a region responsible for the formation of KBD-B dimers in a solvent or during crystallisation, is especially preferred. Of these, a keratin-binding poylpeptide wherein the at least one amino acid substitution is located in the keratin-binding interface of KBD-B is most preferred. In an even more preferred aspect, the latter substitution leads to (i) a keratin-binding polypeptide, which possesses (a) improved keratin-binding properties in comparison to native isolated KBD-B; and/or (b) increased specifity for hair keratin in comparison to skin keratin; and/or (ii) a keratin-binding polypeptide, which

(a) is able to bind as a monomer to keratin, and/or

(b) is present as a monomer in solution and/or crystalline form.

Embodiment (2) is a preferred embodiment of embodiment (1 ). In this preferred embodiment, the amino acid sequence of the native KBD-B wherefrom the polypeptide of present invention is derived encompasses amino acids 2209 to 2448, preferably 2193 to 2481 of SEQ ID NO:1 , i.e. the segment of the native KBD-B sequence used in establishing the model represented in Figure 1 or preferably the full-lenght native KBD- B sequence. Amino acids 2250 to 2448 of SEQ ID NO:1 form the core native KBD-B sequence and were basis for the binding model used in identifying the most relevant regions for improvement of KBD-B properties (compare table 4). The regions flanking said native KBD-B sequence are not necessary for the binding to keratin, thus, they were omitted in the interaction model underlying present invention. They were, however, part of the three dimensional model (amino acids 2209 to 2448, compare Figure 1 ) of KBD-B and of polypeptides prepared in vitro (amino acids 2193 to 2481 , compare example 7), and may therefore be present in a keratin-binding polypeptide according to present invention.

In a preferred aspect of any of embodiments (1 ) and (2), the at least one amino acid substitution in the polypeptide according to present invention is selected from the group consisting of (all amino acid positions are the positions in SEQ ID NO:1 ): (a) D2407X_a, wherein X_a = any amino acid except D; (b) E2293X_b, wherein X_b = I, L, V, M, A or F;

(c) E2422X_C, wherein X_c = I, L, V, M, A, F or Y;

(d) G2362X_d, wherein X_d =M, I, Q, V, L, F, A or N;

(e) H2363X_e, wherein X_e = any small hydrophobic amino acid, F, K, M, or S;

(f) E2421X_f, wherein X_f = I, M, V, L, F or A; (g) F2416X_g, wherein X₉ = any hydrophobic acid smaller than F;

(h) L2358X_h, wherein X_h = any aliphatic hydrophobic amino acid except L;

(i) Y2339X,, wherein X, = any hydrophobic aromatic amino acid except Y;

C) K2328X_j, wherein X_j = R, S, T or Y;

(k) S2331X_k, wherein X_k = R, S, T or Y; (I) R2334X,, wherein X, = R, S, T or Y;

(m) R2284X_m, wherein X_m = any basic amino acid except R; and

(n) G2286X_n, wherein X_n = any basic amino acid; or a homologue, functional variant, derivative or fragment thereof which comprises said at least one amino acid substitution and possesses the keratin-binding properties of said keratin-binding polypeptide.

The keratin-binding properties can be determined as outlined above in the "definitions" section using the assay of example 8 (hair) and/or 10 (skin). Unaltered binding activity as compared to the initial keratin-binding polypeptide would lead to similar absorption values in said assays.

More preferably, the at least one amino acid substitution in the polypeptide according to present invention is selected from the group consisting of

(a) D2407X_a, wherein X_a = any hydophobic amino acid, preferably any hydrophobic aliphatic amino acid, more preferably A, or K or R;

(b) E2293Xb, wherein X_b = any hydrophobic aliphatic amino acid, preferably I; (c) E2422X_C, wherein X₀ = I;

(d) G2362X_d, wherein X_d = M, I or Q, preferably M;

(e) H2363X_e, wherein X₆ = F, A, K, M, V or S, preferably F;

(f) E2421X_f, wherein X_f = I or M, preferably I;

(g) F2416X_g, wherein X₉ = W; (h) L2358X_h, wherein X_h = I or V;

(i) Y2339X,, wherein X, = W;

C + k) double substitution K2328X, and S2331X_k, wherein X_{J k} = R, S, T or Y, preferably

T;

(k + I) double substitution S2331X_k and R2334X,, wherein X _{k J} = R, S, T or Y, preferably X_k = T, X, = R; and

(m + n) double substitution R2284X_m and G2286X_n, wherein X_m, _n = K.

According to the predictions made by the method of embodiment (12), amino acid substitutions (a) to (f) may lead either to improved keratin-binding properties of KBD-B, i.e. to an increase of keratin affinity in the polypeptide according to present invention in comparison to native KBD-B, to a stabilisation of the KBD-B structure, to an increased solubility, to an increased specifity for hair keratin versus skin keratin, or to a decline in dimer formation. In a preferred aspect, amino acid substitution (a) leads to decreased electrostatic attractions and/or steric hindrance of the dimer, substitutions (c), (d), (e) and (f) lead to increased keratin affinity, substitution (c) leads to increased stability of the polypeptide, and substitution (b) does not only lead to increased keratin affinity, but preferably also increases the specifity for hair vs. skin keratin.

Without being bound by theory, the selection on the amino acids starting from the model results may be explained by similarities or differences, respectively, between certain amino acids as follows: Substitution (a) leads to replacement of D with a hydrophobic or bulky basic amino acid. Thus, dimer formation may be impeded due to decrease of electrostatic interactions and steric hindrance. A, K and R are most favoured. Substitution (b) leads to replacement of E with a hydrophobic amino acid, preferably with I L, V, M, A, or F. These replacement amino acids are hydrophobic and may therefore intensify hydrophobic interactions with keratin. I is most favoured by the model according to example 5.

Substitution (c) leads to replacement of E with I, F, L, V, M, A, or Y. These replacement amino acids are hydrophobic and may therefore intensify hydrophobic interactions with keratin. Y resembles F. F and I are most favoured by the model according to example 5.

Substitution (d) leads to replacement of G with M, I, Q, V, L, F, A or N. M, I and Q are most favoured by the model according to example 5. V, L, F and A resemble A in that they are hydrophobic amino acids. N differs from Q in just one CH₂-group. Substitution (e) leads to replacement of H with F, A, K, M, V or S. F is most favoured by the model according to example 5. A, K, M, V or S are found in proteins similar to desmoplakin at this position.

Substitution (f) leads to replacement of E with I, M, V, L, F or A. I and M are most favoured by the model according to example 5. V, L, F and A are also hydrophobic and may therefore intensify hydrophobic interactions with keratin.

Amino acid substitutions (g) to (n) are based on the predictions made by the method of embodiment (12) and on the in vitro results listed in example 6 to 8 for amino acid substitutions in the interface which result in destablization of the polypeptide or in a decrease of keratin binding. After in silico modeling the predicted interaction was analyzed by introducing selected mutations that would lead to weaker binding to keratin to the desmoplakin domain KBD-B. A weaker binding indicated that the selected amino acids were indeed involved in binding to keratin. The spatial and functional properties of the unfavourable substituting amino acids allowed conclusions on the properties of favourable substituting amino acids. For example, if a change from a lipophilic to an acidic amino acid (like L2358E) leads to destabilisation and even proteolytic cleavage of the resulting KBD-B-mod, then the conclusion that a conservative amino acid exchange against another aliphatic lipophilic amino acid, especially against a smaller amino acid, leads to improvements is admissible. Similar conclusions were made for the amino acid locations listed under (g) to (n) based on the results presented in example 6 to 8.

The amino acid substitutions which are most preferred in embodiments (1 ) and (2) are selected from the group consisting of: (a) D2407X_a, wherein X_a = A; (b) E2293X_b, wherein X_b = I; (C) E2422Xc, wherein Xc = I; (d) G2362X_d, wherein X_d = M;

(e) H2363X_e, wherein X₆ = F; and (f) E2421X_f, wherein X_f = I.

In addition to the amino acid substitutions listed above under (a) to (n), the amino acid sequence of the polypeptide according to embodiment (1 ) or (2) of the invention may differ from the native amino acid sequence of KBD-B in further amino acid exchanges, i.e. be a homologue as defined above. These additional exchanges are preferably conservative amino acid exchanges. The ratio of additional substituted amino acids is preferably from 0 to 30 % of the total amino acids of KBD-B, more preferably from 0 to 15%, most preferably from 0 to 5%. A number of additional amino acid exchanges not exceeding 10, preferably 5, more preferably 2 and most preferably 0 is most preferred.

In a preferred aspect of embodiment (2), the polypeptide according to present invention comprises an amino acid sequence selected from the group consisting of SEQ ID

NO:7, SEQ ID NO:10, SEQ ID NO:13, SEQ ID NO:16, SEQ ID NO:19, SEQ ID NO:22, SEQ ID NO:25, SEQ ID NO:28, SEQ ID NO:31 and SEQ ID NO:34. More preferably, the polypeptide according to present invention comprises an amino acid sequence selected from the group consisting of SEQ ID NO:7, SEQ ID NO:10, SEQ ID NO:13, SEQ ID NO:19, SEQ ID NO:28 and SEQ ID NO:31.

In a further preferred aspect of embodiment (2), the polypeptide according to present invention comprises an amino acid sequence selected from the group consisting of SEQ ID NO:6, SEQ ID NO:9, SEQ ID NO:12, SEQ ID NO:15, SEQ ID NO:18, SEQ ID NO:21 , SEQ ID NO:24, SEQ ID NO:27, SEQ ID NO:30 and SEQ ID NO:33. More preferably, the polypeptide according to present invention comprises an amino acid sequence selected from the group consisting of SEQ ID NO:6, SEQ ID NO:9, SEQ ID NO:12, SEQ ID NO:18, SEQ ID NO:27 and SEQ ID NO:30.

In an especially preferred aspect of embodiment (1 ) or (2), the polypeptide according to present invention does not only comprise an amino acid sequence derived by the at least one amino acid substitution from amino acids 2250 to 2448 of SEQ ID NO:1 , but consists of said amino acid sequence. In other words, it consists of the sequence represented by amino acids 2250 to 2448 of SEQ ID NO:1 , but differs from said sequence by the amino acid exchanges indicated in embodiment (1 ) and its preferred embodiments. The polypeptide according to this aspect may be part of a functional variant formed by the polypeptide as keratin-binding domain and a second functional domain, but its amino acid chain does not continue like SEQ ID NO:1 outside its borders defined by the amino acids corresponding to amino acids 2250 to 2448 of SEQ ID NO:1. In an equally preferred aspect of embodiment (1 ) or (2), the polypeptide according to present invention does not only comprise an amino acid sequence derived by the at least one amino acid substitution from amino acids 2209 to 2448 of SEQ ID NO:1 , but consists of said amino acid sequence. In other words, it consists of the sequence represented by amino acids 2209 to 2448 of SEQ ID NO:1 , but differs from said sequence by the amino acid exchanges indicated in embodiment (1 ) and its preferred embodiments. The polypeptide according to this aspect may be part of a functional variant formed by the polypeptide as keratin-binding domain and a second functional domain, but its amino acid chain does not continue like SEQ ID NO:1 outside its borders defined by the amino acids corresponding to amino acids 2209 to 2448 of SEQ ID NO:1.

In an equally preferred aspect of embodiment (1 ) or (2), the polypeptide according to present invention does not only comprise an amino acid sequence derived by the at least one amino acid substitution from amino acids 2193 to 2481 of SEQ ID NO:1 , but consists of said amino acid sequence. In other words, it consists of the sequence represented by amino acids 2193 to 2481 of SEQ ID NO:1 , but differs from said sequence by the amino acid exchanges indicated in embodiment (1 ) and its preferred embodiments. The polypeptide according to this aspect may be part of a functional variant formed by the polypeptide as keratin-binding domain and a second functional domain, but its amino acid chain does not continue like SEQ ID NO:1 outside its borders defined by the amino acids corresponding to amino acids 2193 to 2481 of SEQ ID NO:1.

In another equally preferred aspect of embodiment (1 ) or (2), the polypeptide according to present invention does not only comprise an amino acid sequence selected from the group consisting of SEQ ID NO:7, SEQ ID NO:10, SEQ ID NO:13, SEQ ID NO:16, SEQ ID NO:19, SEQ ID NO:22, SEQ ID NO:25, SEQ ID NO:28, SEQ ID NO:31 , SEQ ID NO:34, SEQ ID NO:6, SEQ ID NO:9, SEQ ID NO:12, SEQ ID NO:15, SEQ ID NO:18, SEQ ID NO:21 , SEQ ID NO:24, SEQ ID NO:27, SEQ ID NO:30 and SEQ ID NO:33, particularly an amino acid sequence selected from the group consisting of SEQ ID NO:7, SEQ ID NO:10, SEQ ID NO:13, SEQ ID NO:19, SEQ ID NO:28, SEQ ID NO:31 , SEQ ID NO:6, SEQ ID NO:9, SEQ ID NO:12, SEQ ID NO:18, SEQ ID NO:27 and SEQ ID NO:30, but consists of said amino acid sequence. In other words, it consists of the sequence represented by one of the listed SEQ ID NOs. The polypeptide according to this aspect may be part of a functional variant formed by the polypeptide as keratin-binding domain and a second functional domain, but its amino acid chain does not continue like SEQ ID NO:1 outside its borders defined by the listed SEQ ID NOs.

According to embodiment (1 ), any of the polypeptide homologues, derivatives, functional variants and fragments as defined above is also encompassed by present invention under the proviso that it comprises the at least one amino acid substitution as defined under embodiment (1 ) or (2) and possesses the keratin-binding properties of said keratin-binding polypeptide. Any peptide which is the result of combinations of the admissible modifications leading to a homologue, derivative, functional variant or fragment and fulfills said proviso is also part of present invention. However, in each embodiment of present invention, the keratin-binding polypeptide according to embodiments (1 ) or (2) without any further modification to a homologue, functional variant, fragment or derivative is preferred, unless indicated otherwise.

The nucleic acid sequence according to embodiment (3) of present invention may be any nucleic acid, preferably DNA or RNA, encoding any of the polypeptides of present invention, or any homologue, functional variant, derivative or fragment thereof as defined for embodiment (1 ) or (2). It preferably comprises one of the nucleic acid sequences encoding one of the polypeptides of present invention as comprised as ORF in the vectors having SEQ ID NO:8, SEQ ID NO:11 , SEQ ID NO:14, SEQ ID NO:17, SEQ ID NO:20, SEQ ID NO:23, SEQ ID NO:26, SEQ ID NO:29, SEQ ID NO:32 or SEQ ID NO:35, its RNA homologue or a nucleic acid sequence complementary thereto. More preferably, it comprises one of the nucleic acid sequences encoding the polypeptides of present invention as defined above comprised in the vectors having SEQ ID NO:8, SEQ ID NO:1 1 , SEQ ID NO:14, SEQ ID NO:20, SEQ ID NO:29 or SEQ ID NO:32. The vectors which have SEQ ID NO:8, SEQ ID NO:11 , SEQ ID NO:14, SEQ ID NO:17, SEQ ID NO:20, SEQ ID NO:23, SEQ ID NO:26, SEQ ID NO:29, SEQ ID NO:32 or SEQ ID NO:35 are a particularly preferred aspect of embodiment (3) and (4).

The vector of embodiment (4) may be any state of the art vector which is suitable for transformation or transfection of eucaryotic or procaryotic cells. It is preferably an expression vector, more preferably one of the vectors used in the examples section. Various expression vectors are suitable for the expression of the keratin-binding polypeptides of present invention (e.g. pQE30, pLib15, pLib16, etc.), pQE30 being preferred. In said vectors, various promoters (e.g. IPTG-inducible, rhamnose-inducible, arabinose-inducible, methanol-inducible, constitutive promoters, etc.) can be used. Constructs in which the KBD is expressed as fusion protein (e.g. as fusion with thioredoxin, or eGFP, or YaaD [B. subtilis, SWISS-PROT: P37527, PDX1], etc.) are also encompassed by embodiment (4).

The cell of embodiment (5) is preferably an isolated cell. For the expression of the KBD, various production hosts are suitable. In a preferred aspect of embodiment (5), they are bacterial or fungal host strains. Preferred bacterial host strains are E. coli strains (see example 7; e.g. XLI O-GoId [Stratagene], BL21-CodonPlus [Stratagene], and others). However, other bacterial production hosts, such as, for example, Bacillus megaterium or Bacillus subtilis, are also suitable (Barg, H., Malten, M. & Jahn, D. (2005) Protein and vitamin production in Bacillus megaterium. In Methods in Biotechnology-Microbial Products and Biotransformations, Barredo, J. -L., ed.). The preferred fungal production strains are Pichia pastoris (e.g. GS115 and KM71 [both from Invitrogen]; and others) and Aspergillus nidulans (e.g. RMS01 1 [Stringer, MA, Dean, RA, Sewall, TC, Timberlake, WE (1991 ) Genes Dev 5:1161-1 171] und

SRF200 [Karos, M, Fischer, R (1999) MoI Genet Genomics 260:510-521], and others). However, it is also possible to use other fungal production hosts, such as, for example, Aspergillus niger (KBD expression analogous to EP 0635574A1 and/or WO 98/46772) for the KBD expression.

The polypeptide of present invention may be preprared by any polypeptide or protein synthesis method known in the art including biochemical synthesis, e.g. by transgenic cells, and chemical synthesis, e.g. solid-phase synthesis. The preparation may use the vector of embodiment (4) and/or the cell of embodiment (5).

In a special aspect of present invention, the preparation according to embodiment (13) encompasses the use of the interaction model as defined in embodiment (12), i.e. the steps leading up to the identification of a keratin-binding polypeptide.

The use (7) and composition (6) are interrelated, as the composition (6) may be applied in the use (7), and as the use (7) defines the preferred kinds of composition (6). E.g., one of the preferred uses of a polypeptide of present invention is a cosmetic use, and one of the preferred compositions is a cosmetic composition. Thus, the preferred aspects described herein with regard to the composition (6) are preferred aspects of the use (7) as well where applicable, and vice versa.

In a preferred aspect, the use according to embodiment (7) and composition (6) is for

(a) prevention or treatment of diseases, preferably of the diseases as specified below;

(b) cosmetic treatment, preferably for the cosmetic treatment specified below; (c) the treatment of inanimate material in vitro, preferably of leather, wool, or horn.

The composition according to embodiment (6) comprises a keratin-binding polypeptide according to embodiment (1 ) or (2) of present invention as defined above. This encompasses compositions comprising a homologue, functional variant, derivative or fragment of the polypeptide as defined above. It does particularly encompass compositions comprising a pharmaceutically and/or cosmetically acceptable functional variant of said polypeptide. Such variant is preferably a pharmaceutically and/or cosmetically acceptable salt of a poylpeptide according to embodiment (1 ) or (2) of present invention, a variant comprising the poylpeptide linked to a second domain (which is preferably an active igredient or effector molecule as defined below), or a pharmaceutically and/or cosmetically acceptable salt of the latter. More preferably, it is a functional variant consisting of the poylpeptide linked to an active ingredient or effector molecule.

In a preferred aspect of the use (7) and of the composition (6), the keratin-binding polypeptide may be able to bind as a monomer to keratin, and/or may be present as a monomer in solution and/or crystalline form.

It is possible to use in the composition (6) or the use (7) either one or more than one kind of the polypeptide according to embodiment (1 ) or (2). The use of one kind is preferred, but present invention does also encompasse the use of more than one polypeptide of embodiment (1 ) or (2) in embodiments (6) and (7). For example, a poylpeptide having a specifity for human hair keratin and another poylpeptide having a specifity for human skin keratin may be used concurrently in one use (7) or in one composition (6). Moreover, a plurality (i.e. 2 or more) of copies of the same polypeptide according to present invention may be connected by a suitable linker (i.e. a linker not interfering with the structure and function of said polypeptides) in order to increase keratin affinity.

The composition according to embodiment (6) comprises the polypeptide according to present invention in any amount, preferably in an amount of from about 0.001 to 30% by weight, more preferably 0.01 to 20% by weight, very particularly preferably 0.1 to 12% by weight, based on the total weight of the composition. If it comrises more than one kind of polypeptide according to present invention, this amount is the total amount of said polypeptides.

The composition according to embodiment (6) which comprises a keratin-binding polypeptide according to embodiment (1 ) or (2) is suitable for the use according to embodiment (7), i.e. for the treatment of keratin or keratin-comprising material. It is therefore preferably used for the treatment of keratin or keratin-comprising tissue, especially of skin and/or hair. This includes the cosmetic treatment or pharmaceutical treatment of humans or animals, but also the treatment of keratin-comprising materials like leather, horn, wool etc.

The treatment of keratin or keratin-comprising tissue during the use (7), and for which the composition (6) is suitable, is performed in vivo or in vitro, preferably in vitro. In vitro treatments may be treatments of human or animal hair, e.g. for/in wigs, or leather treatment or wool treatment.

The keratin-binding polypeptides according to present invention have a wide area of application in human cosmetics (in particular in skin, nail and hair care), and as ingredients of pharmaceutical compositions, but also in animal care, leather care and leather processing. Preferably, they are used in cosmetic and pharmaceutical applications.

The composition according to embodiment (6) is preferably a pharmaceutical or cosmetic composition, more preferably a pharmaceutical or cosmetic composition for the treatment of a human subject.

For applications in the human sector, the preferred polypeptides are those having a particularly high affinity for human keratin. For applications in the pet sector, correspondingly, the preferred polypeptides are those having a particularly high affinity for the corresponding keratin, for example canine keratin or feline keratin.

In a first preferred aspect of embodiments (6) and (7) of present invention, the keratin- binding polypeptide (1 ) or (2) according to the invention is an ingredient of a cosmetic composition. A cosmetic composition according to present invention is a composition for cosmetic use, preferably for cosmetic treatment of the skin and/or hair of a subject. It will comprise a cosmetically effective amount of a cosmetic ingredient.

In a preferred aspect of said use as ingredient of a cosmetic composition, the keratin- binding polypeptides (1 ) or (2) according to the invention are used for skin cosmetics. They permit a high concentration and long action time of skin care or skin-protecting effectors on the area treated with the composition.

In a further preferred aspect of the use as ingredient of a cosmetics composition, the keratin-binding polypeptides (1 ) or (2) according to the invention are used for hair cosmetics. They permit a high concentration and long action time of hair care or hair- protecting effectors on the area treated with the composition.

In a second preferred aspect of embodiments (6) and (7) of present invention, the keratin-binding polypeptide (1 ) or (2) according to the invention is used as ingredient of a pharmaceutical composition. A pharmaceutical composition according to present invention is a composition for use as a medicament, i.e. in the treatment, alleviation or prevention of a disease. It will comprise a pharmaceutically effective amount of a pharmaceutically active ingredient.

In a preferred aspect of the use as ingredients of pharmaceutical compositions, the keratin-binding polypeptides (1 ) or (2) according to the invention are used for pharmaceutical compositions for treating the skin. They permit a high concentration and long action time of pharmaceutically active ingredients, skin care or skin-protecting effectors on the area treated with the composition. In a further preferred aspect of the use as ingredients of pharmaceutical compositions, the keratin-binding polypeptides (1 ) or (2) according to the invention are used as ingredients for hair treatment compositions. They permit a high concentration and long action time of pharmaceutically active ingredients, hair care or hair-protecting effectors on the area treated with the composition.

The pharmaceutical composition according to present invention is preferably for the treatment and/or prevention of skin and/or hair diseases or skin and/or hair clinical conditions. It may be especially suitable for treatments wherein (i) a tight binding of the active ingredient to hair and/or skin and/or (ii) a slow release of the pharmaceutically active effector molecule from the KBD-B by skin proteases is desirable.

More preferably, the pharmaceutical composition is suitable in the treatment or prevention of one or more of the following: hair loss, hair damage, acne, age marks, rash / allergy, atopic dermatitis, basalioma, candidosis, condylomata acuminata, dekubitus, molluscum contagiosum, perioral dermatitis, dermatophyte infections, erysipelas, pediculosis, furuncles, herpes zoster, human papilloma-virus infection, hyperhidrosis, ichthyosis, actinic keratosis, pityriasis versicolor, lichen ruber planus, scabies, herpes labialis, mycosis (especially madura mycosis), rosacea, seborreic rash, sun burn, thrush, vitiligo, diaper dermatitis, infestation with crab lice or hair lice, skin cancer, psoriasis and wounds. It may especially be suitable in wound healing and wound treatment.

The polypeptides according to embodiment (1 ) or (2) are preferably specific for certain target structures. Accordingly, for applications on skin, the polypeptides preferably employed in the composition of embodiment (6) or the use of embodiment (7) are polypeptides having a particularly high affinity for the keratin of skin. The polypeptide sequences preferred for applications on hair are those having a particularly high affinity for the keratin of hair.

Preferably, the composition according to embodiment (6)

(i) is suitable for the treatment of hair and preferably comprises a polypeptide according to embodiment (1 ) or (2) with an increased specifity for hair keratin in comparison to skin keratin; or (ii) is suitable for the treatment of skin and preferably comprises a polypeptide according to embodiment (1 ) or (2) with an increased specifity for skin keratin in comparison to hair keratin.

The compositions according to embodiment (6) of present invention preferably serve to care for or protect the skin or hair. They are in one preferred aspect skin cosmetic, nail cosmetic, hair cosmetic, hygiene or pharmaceutical compositions. Compositions for topical application are preferred, especially compositions for topical application on skin and/or hair. Topical application means in this context application of the composition onto a body surface. Body surfaces are outward surfaces of a human or animal body, including skin, mucous membranes, hair, nails and hooves. Preferred topical applications are selected from applications to skin, nails and hair, especially preferred are skin and/or hair applications.

The preferred hair cosmetic or skin cosmetic composition is ordinarily used for topical application to the skin or hair. A preferred topical pharmaceutical composition is a dermatological composition.

Preferably, a topical composition of present invention is suitable for applying the active substances to the skin in fine distribution and preferably in a form which can be absorbed through the skin. Examples suitable for this purpose are aqueous and hydroalcoholic solutions, sprays, foams, foam aerosols, ointments, aqueous gels, emulsions of the O/W or W/O type, microemulsions or cosmetic stick products.

The keratin-binding polypeptides according to the invention can also, if desired, easily be separated from the keratin again. For this purpose it is possible to employ for example washing with keratin or a keratin fragment like the CK8/18 rod domain, whereby the keratin-binding polypeptides are displaced from their existing binding to the keratin and are saturated with the keratin from the washing solution. Alternatively, a washing with a high content of detergent (e.g. SDS) is also possible for the washing out.

The keratin-binding polypeptide in a composition (6) or a use (7) may act either as

(i) a carrier or shuttle for a further compound; or

(ii) as an active ingredient of the composition.

In the composition according to embodiment (6) and the use of embodiment (7), the polypeptide of present invention is in one preferred aspect the active ingredient, in another preferred aspect the carrier of an active ingredient or effector molecule.

As active ingredient, the polypeptide of present invention is used for hair repair by binding to keratin structures, or as a preparatory means for preparing hair or skin for a consecutive treatment with an active ingredient binding to the polypeptide of present invention.

As a carrier of an active ingredient or effector molecule, the poylpeptide of present invention supports the transport of a further compound to keratin and/or the binding of said further compound to keratin. Thus, it works as a shuttle and/or permits a high concentration and long action time of said further compound on keratin. Preferably, said further compound is an active ingredient of the composition. It does either bind to the keratin-binding polypeptide during application of the composition, or it is bound to the polypeptide beforehand. A covalent binding between the active ingredient/effector molecule and the polypeptide via a linker is preferred, as this ensures a high concentration and long action time of the active ingredient/effector molecule on the area treated with the composition.

The pharmaceutical composition comprising the polypeptide of present invention is preferably a composition for treating keratin-comprising tissue like skin or hair, and for treating, alleviating or preventing conditions and diseases connected with keratin comprising tissues. This includes treatment of skin wounds and lesions, hair loss, hair damage, acne, age marks, rash / allergy, atopic dermatitis, basalioma, candidosis, condylomata acuminata, dekubitus, molluscum contagiosum, perioral dermatitis, dermatophyte infections, erysipelas, pediculosis, furuncles, herpes zoster, human papilloma-virus infection, hyperhidrosis, ichthyosis, actinic keratosis, pityriasis versicolor, lichen ruber planus, scabies, herpes labialis, mycosis (especially madura mycosis), rosacea, seborreic rash, sun burn, thrush, vitiligo, diaper dermatitis, infestation with crab lice or hair lice, skin cancer, and psoriasis.

The cosmetic use (7) of the composition according to embodiment (6) or of the polypeptide of present invention includes the improvement of hair and skin structure, prevention of hair loss, prevention and repair of hair damage, improvement of hair brilliance, ease of hair combing, improvement of hair gloss and color, reduction and prevention of skin wrinkles, and cosmetic treatment of unwanted cosmetic effects (e.g. scars and skin or hair alterations) of acne, age marks, rash / allergy, atopic dermatitis, basalioma, candidosis, condylomata acuminata, dekubitus, molluscum contagiosum, perioral dermatitis, dermatophyte infections, erysipelas, pediculosis, furuncles, herpes zoster, human papilloma-virus infection, hyperhidrosis, ichthyosis, actinic keratosis, pityriasis versicolor, lichen ruber planus, scabies, herpes labialis, madura mycosis, rosacea, seborreic rash, sun burn, thrush, vitiligo, diaper dermatitis, and wound scars.

In one preferred aspect, the cosmetic use is the repair of hair and skin keratin damages by binding of the polypeptide to the damaged keratin. In afuther preferred aspect, the cosmetic use resides in the repair of split hair ends, in shielding exposed hair cortex after stripping off hair cuticle, in repair of and/or protection of hair and skin against heat damage, in repair of and/or protection of hair and skin (preferably hair) against perm damage, in repair of and/or protection of hair and skin against damage after and/or during bleaching (hair or skin, preferably hair bleaching), in repair of and/or protection of skin against skin irritation, and/or in skin treatment after a peeling sun burn.

Preferred cosmetic compositions according to embodiment (6) are compositions for said preferred cosmetic uses (7). Particularly, the cosmecit composition is a hair tonic, hair conditioner, hair dye, skin cleansing lotion, shampoo, body mist, skin tanning lotion, skin whitening lotion or sun cream. Preferably, the compositions according to embodiment (6) are in the form of a gel, foam, spray, aerosol, ointment, cream, balsam, emulsion, suspension, dispersion, lotion, aqueous surfactant preparation, milk, granulation, dusting powder, stick product (lika a lipstick) or paste. If desired, liposomes or microspheres can also be used. Such formulations are very suitable for topical preparations. Suitable emulsions are oil-in- water emulsions and water-in-oil emulsions or microemulsions.

The cosmetical or pharmaceutical compositions according to the invention do in a preferred aspect of embodiment (6) additionally comprise a cosmetically and/or pharmaceutically active ingredient.

The cosmetical or pharmaceutical compositions according to the invention do in another preferred aspect of embodiment (6) additionally comprise a cosmetically and/or pharmaceutically active auxiliary or excipient.

The active ingredients, excipients and auxiliaries suitable for the composition of embodiment (6) are described in more detail in the following sections:

Suitable auxiliaries and additives for producing hair cosmetic, nail cosmetic or skin cosmetic or pharmaceutical compositions are known to the person skilled in the art and can be found in handbooks of cosmetics, for example Schrader, Grundlagen und Rezepturen der Kosmetika [Fundamentals and formulations of cosmetics], Hϋthig Verlag, Heidelberg, 1989, ISBN 3-7785-1491-1. The formulation base of pharmaceutical compositions according to the invention preferably comprises pharmaceutically acceptable auxiliaries. Pharmaceutically acceptable auxiliaries are those which are known for use in the field of pharmacy, food technology and related fields, in particular those listed in the relevant pharmacopeia (e.g. DAB Ph. Eur. BP NF) and other auxiliaries whose properties do not preclude a physiological application.

Suitable auxiliaries may be: lubricants, wetting agents, emulsifying and suspending agents, preserving agents, antioxidants, antiirritatives, chelating agents, emulsion stabilizers, film formers, gel formers, odor-masking agents, resins, hydrocolloids, solvents, solubility promoters, neutralizing agents, permeation accelerators, pigments, quaternary ammonium compounds, refatting and superfatting agents, ointment, cream or oil base substances, silicone derivatives, stabilizers, sterilizers, propellants, drying agents, opacifiers, thickeners, waxes, softeners, white oil. Formulation in this regard is based on specialist knowledge, as given, for example, in Fiedler, H. P. Lexikon der Hilfsstoffe fur Pharmazie, Kosmetik und angrenzende Gebiete [Lexicon of Auxiliaries for Pharmacy, Cosmetics and related fields], 4th ed., Aulendorf: ECV-Editio-Kantor-Verlag, 1996. To prepare the compositions according to the invention, the active ingredients can be mixed or diluted with a suitable auxiliary (excipient). Excipients may be solid, semisolid or liquid materials which can serve as a vehicle, carrier or medium for the active ingredient. Further auxiliaries are added, if desired, in the manner known to the person skilled in the art. In addition, the polymers and dispersions are suitable as auxiliaries in pharmacy, preferably as or in coating(s) or binder(s) for solid drug forms. They can also be used in creams and as tablet coatings and tablet binders.

In a preferred embodiment of the composition of the invention, the composition comprises a carrier. A preferred carrier is water, a gas, a water-based liquid, an oil, a gel, an emulsion or microemulsion, a dispersion or a mixture thereof. Said carriers are well tolerated by skin. Particularly advantageous for topical preparations are aqueous gels, emulsions or microemulsions.

Preferably, the compositions according to the invention comprise at least one keratin- binding polypeptide as defined above, and at least one constituent different therefrom which is chosen from cosmetically or pharmaceutically active ingredients, emulsifiers, surfactants, preservatives, perfume oils, thickeners, hair polymers, hair and skin conditioners, graft polymers, water-soluble or dispersible silicone-containing polymers, photoprotective agents, bleaches, gel formers, care agents, colorants, tints, tanning agents, dyes, pigments, consistency regulators, moisturizers, re-fatting agents, collagen, protein hydrolysates, lipids, antioxidants, antifoams, antistats, emollients and softeners. The keratin-binding polypeptide and/or the active ingredients may also be present in encapsulated form in the cosmetic preparations.

Advantageously, the antioxidants are chosen from the group consisting of amino acids (e.g. glycine, histidine, tyrosine, tryptophan) and derivatives thereof, imidazoles (e.g. urocanic acid) and derivatives thereof, peptides such as D,L-carnosine, D-carnosine, L-carnosine and derivaties thereof (e.g. anserine), carotenoids, carotenes (e.g. β- carotene, lycopene) and derivatives thereof, chlorogenic acid and derivatives thereof, lipoic acid and derivatives thereof (e.g. dihydrolipoic acid), aurothioglucose, propylthiouracil and other thiols (e.g. thioredoxin, glutathione, cysteine, cystine, cystamine and the glycosyl, N-acetyl, methyl, ethyl, propyl, amyl, butyl and lauryl, palmitoyl, oleyl, γ-linoleyl, cholesteryl and glyceryl esters thereof) and salts thereof, dilauryl thiodipropionate, distearyl thiodipropionate, thiodipropionic acid and derivatives thereof (esters, ethers, peptides, lipids, nucleotides, nucleosides and salts), and sulfoximine compounds (e.g. buthionine sulfoximines, homocysteine sulfoximines, buthionine sulfones, penta-, hexa-, heptathionine sulfoximine) in very low tolerated doses (e.g. pmol to μmol/kg), also (metal) chelating agents (e.g. α-hydroxy fatty acids, palmitic acid, phytic acid, lactoferrin), α-hydroxy acids (e.g. citric acid, lactic acid, malic acid), humic acid, bile acid, bile extracts, bilirubin, biliverdin, EDTA and derivatives thereof, unsaturated fatty acids and derivatives thereof (e.g. γ-linolenic acid, linoleic acid, oleic acid), folic acid and derivatives thereof, ubiquinone and ubiquinol and derivatives thereof, vitamin C and derivatives thereof (e.g. sodium ascorbate, ascorbyl palmitate, Mg ascorbyl phosphate, ascorbyl acetate), tocopherol and derivatives (e.g. vitamin E acetate, tocotrienol), vitamin A and derivatives (vitamin A palmitate), and coniferyl benzoate of benzoin resin, rutinic acid and derivatives thereof, α-glycosylrutin, ferulic acid, furfurylideneglucitol, carnosine, butylhydroxytoluene, butylhydroxyanisole, nordihydroguaiacic acid, nordihydroguaiaretic acid, trihydroxybutyrophenone, uric acid and derivatives thereof, mannose and derivatives thereof, zinc and derivatives thereof (e.g. ZnO, ZnSO₄), selenium and derivatives thereof (e.g. selenomethionine), stilbenes and derivatives thereof (e.g. stilbene oxide, trans-stilbene oxide).

Customary thickeners in such formulations are crosslinked polyacrylic acids and derivatives thereof, polysaccharides and derivatives thereof, such as xanthan gum, agar-agar, alginates or tyloses, cellulose derivatives, e.g. carboxymethylcellulose or hydroxycarboxymethylcellulose, fatty alcohols, monoglycerides and fatty acids, polyvinyl alcohol and polyvinylpyrrolidone. Preference is given to using nonionic thickeners.

Suitable cosmetically and/or pharmaceutically active ingredients are, for example, coloring active ingredients, skin and hair pigmentation agents, tinting agents, tanning agents, bleaches, keratin-hardening substances, antimicrobial active ingredients, photofilter active ingredients, repellent active ingredients, substances with a hyperemic effect, substances with a keratolytic and keratoplastic effect, antidandruff active ingredient, antiphlogistics, substances with a keratinizing effect, active ingredients with an antioxidative or free-radical-scavenging effect, substances which moisturize the skin or keep the skin moist, re-fatting active ingredients, antierythimatous or antiallergic active ingredients, branched fatty acids such as 18-methyleicosanoic acid, and mixtures thereof.

Active ingredients which tan the skin artificially and which are suitable for tanning the skin without natural or artificial irradiation with UV rays are, for example, dihydroxyacetone, alloxan and walnut shell extract. Suitable keratin-hardening substances are usually active ingredients as are also used in antiperspirants, such as, for example, potassium aluminum sulfate, aluminum hydroxychloride, aluminum lactate, etc.

Antimicrobial active ingredients are used to destroy microorganisms or to inhibit their growth and thus serve both as preservatives and also as deodorizing substance which reduces the formation or the intensity of body odor. These include, for example, customary preservatives known to the person skilled in the art, such as p- hydroxybenzoic esters, imidazolidinylurea, formaldehyde, sorbic acid, benzoic acid, salicylic acid, etc. Such deodorizing substances are, for example, zinc ricinoleate, triclosan, undecylenic alkylolamides, triethyl citrate, chlorhexidine etc.

Suitable preservatives to be used advantageously according to the invention are listed below with their E number.

Also suitable according to the invention are preservatives or preservative auxiliaries customary in cosmetics and pharmaceuticals including dibromodicyanobutane (2- bromo-2-bromomethylglutarodinitrile), 3-iodo-2-propynyl butylcarbamate, 2-bromo-2- nitropropane-1 ,3-diol, imidazolidinylurea, 5-chloro-2-methyl-4-isothiazolin-3-one, 2- chloroacetamide, benzalkonium chloride, benzyl alcohol and formaldehyde donors.

Also suitable as preservatives are phenyl hydroxyalkyl ethers, in particular the compound known under the name phenoxyethanol on account of its bactericidal and fungicidal effects on a number of microorganisms.

Other antimicrobial agents are likewise suitable for being incorporated into the compositions according to the invention. Advantageous substances are, for example, 2,4,4'-trichloro-2'-hydroxydiphenyl ether (irgasan), 1 ,6-di(4- chlorophenylbiguanido)hexane (chlorhexidine), 3,4,4'-trichlorocarbanilide, quaternary ammonium compounds, oil of cloves, mint oil, thyme oil, triethyl citrate, farnesol (3,7,1 1-trimethyl-2, 6,10-dodecatrien-1-ol), and the active ingredients or active ingredient combinations described in the patent laid-open specifications DE-37 40 186, DE-39 38 140, DE-42 04 321 , DE-42 29 707, DE-43 09 372, DE-44 1 1 664, DE- 195 41 967, DE-195 43 695, DE-195 43 696, DE-195 47 160, DE-196 02 108, DE-196 02 110, DE-196 02 11 1 , DE-196 31 003, DE-196 31 004 and DE-196 34 019 and the patent specifications DE-42 29 737, DE-42 37 081 , DE-43 24 219, DE-44 29 467, DE- 44 23 410 and DE-195 16 705. Sodium hydrogencarbonate is also to be used advantageously. Antimicrobial polypeptides can also likewise be used.

Suitable photofilter active ingredients are substances which absorb UV rays in the UV- B- and/or UV-A region. Suitable UV filters are, for example, 2,4,6-triaryl-1 ,3,5-triazines in which the aryl groups may in each case carry at least one substituent which is preferably chosen from hydroxy, alkoxy, specifically methoxy, alkoxycarbonyl, specifically methoxycarbonyl and ethoxycarbonyl and mixtures thereof. Also suitable are p-aminobenzoic esters, cinnamic esters, benzophenones, camphor derivatives, and pigments which stop UV rays, such as titanium dioxide, talc and zinc oxide.

Suitable UV filter substances are any UV-A and UV-B filter substances including:

The cosmetic and pharmaceutical (especially the dermatological) preparations according to the invention may advantageously additionally comprise inorganic pigments which stop UV rays based on metal oxides and/or other metal compounds which are insoluble or slightly soluble in water and chosen from the group of oxides of zinc (ZnO), titanium (TiO₂), iron (e.g. Fe₂O₃), zirconium (ZrO₂), silicon (SiO₂), manganese (e.g. MnO), aluminum (AI₂O₃), cerium (e.g. Ce₂O₃), mixed oxides of the corresponding metals and mixtures of such oxides.

The inorganic pigments can be present in coated form, i.e. are surface-treated. This surface treatment can consist, for example, in providing the pigments with a thin hydrophobic layer by a method known per se, as described in DE-A-33 14 742.

Suitable repellent active ingredients are compounds which are able to repel or drive away certain animals, in particular insects, from humans. These include, for example, 2-ethyl-1 ,3-hexanediol, N,N-diethyl-m-toluamide etc. Suitable hyperemic substances, which stimulate the flow of blood through the skin, are e.g. essential oils, such as dwarf pine extract, lavender extract, rosemary extract, juniperberry extract, horse chestnut extract, birch leaf extract, hayflower extract, ethyl acetate, camphor, menthol, peppermint oil, rosemary extract, eucalyptus oil, etc. Suitable keratolytic and keratoplastic substances are, for example, salicylic acid, calcium thioglycolate, thioglycolic acid and its salts, sulfur, etc. Suitable antidandruff active ingredients are, for example, sulfur, sulfur polyethylene glycol sorbitan monooleate, sulfur ricinol polyethoxylate, zinc pyrithione, aluminum pyrithione, etc. Suitable antiinflammatory agents, which counteract skin irritations, are, for example, allantoin, bisabolol, dragosantol, camomile extract, panthenol, etc.

The cosmetic and pharmaceutical compositions according to the invention can comprise, as cosmetic and/or pharmaceutical active ingredient (and also if appropriate as auxiliary), at least one cosmetically or pharmaceutically acceptable polymer which differs from the polymers which form the polyelectrolyte complex used according to the invention. These include, quite generally, cationic, amphoteric and neutral polymers.

Suitable polymers are, for example, cationic polymers with the INCI name PoIy- quaternium, e.g. copolymers of vinylpyrrolidone/N-vinylimidazolium salts (Luviquat FC, Luviquat HM, Luviquat MS, Luviquat&commat, Care), copolymers of N-vinylpyrrolidone/dimethylaminoethyl methacrylate, quaternized with diethyl sulfate (Luviquat PQ 11 ), copolymers of N-vinylcaprolactam/N-vinylpyrrolidone/N- vinylimidazolium salts (Luviquat E Hold), cationic cellulose derivatives (Polyquaternium-4 and -10), acrylamido copolymers (Polyquaternium-7) and chitosan.

Suitable cationic (quaternized) polymers are also Merquat (polymer based on dimethyldiallylammonium chloride), Gafquat (quaternary polymers which are produced by the reaction of polyvinylpyrrolidone with quaternary ammonium compounds), Polymer JR (hydroxyethylcellulose with cationic groups) and plant-based cationic polymers, e.g. guar polymers such as the Jaguar grades from Rhodia.

Further suitable polymers are also neutral polymers, such as polyvinylpyrrolidones, copolymers of N-vinylpyrrolidone and vinyl acetate and/or vinyl propionate, polysiloxanes, polyvinylcaprolactam and other copolymers with N-vinylpyrrolidone, polyethyleneimines and salts thereof, polyvinylamines and salts thereof, cellulose derivatives, polyaspartic acid salts and derivatives. These include, for example, Luviflex 0 Swing (partially saponified copolymer of polyvinyl acetate and polyethylene glycol, BASF).

Suitable polymers are also nonionic, water-soluble or water-dispersible polymers or oligomers, such as polyvinylcaprolactam, e.g. Luviskol 0 Plus (BASF), or polyvinylpyrrolidone and copolymers thereof, in particular with vinyl esters, such as vinyl acetate, e.g. Luviskol 0 VA 37 (BASF), polyamides, e.g. based on itaconic acid and aliphatic diamines, as are described, for example, in DE-A-43 33 238.

Suitable polymers are also amphoteric or zwitterionic polymers, such as the octylacrylamide/methyl methacrylate/tert-butylaminoethyl methacrylate/hydroxypropyl methacrylate copolymers obtainable under the names Amphomer (National Starch), and zwitterionic polymers as are disclosed, for example, in the German patent applications DE39 29 973, DE 21 50 557, DE28 17 369 and DE 3708 451. Acrylamidopropyltrimethylammonium chloride/acrylic acid or methacrylic acid copolymers and alkali metal and ammonium salts thereof are preferred zwitterionic polymers. Further suitable zwitterionic polymers are methacroylethylbetaine/ methacrylate copolymers, which are available commercially under the name Amersette (AMERCHOL), and copolymers of hydroxyethyl methacrylate, methyl methacrylate, N,N-dimethylaminoethyl methacrylate and acrylic acid (Jordapon (D)).

Suitable polymers are also nonionic, siloxane-containing, water-soluble or water- dispersible polymers, e.g. polyether siloxanes, such as Tegopren 0 (Goldschmidt) or Besi&commat (Wacker).

In a particularly preferred aspect of embodiment (6), the composition according to present invention is a skin-cleansing composition. In said composition, the keratin- binding polypeptide according to present invention may, e.g., be present in order to achieve an additional skin conditioning effect.

Preferred skin-cleansing compositions are soaps of liquid to gel-like consistency, such as transparent soaps, luxury soaps, deodorant soaps, cream soaps, baby soaps, skin protection soaps, abrasive soaps and syndets, pasty soaps, soft soaps and washing pastes, exfoliating soaps, moisturizing wipes, liquid washing, shower and bath preparations, such as washing lotions, shower baths and gels, foam baths, oil baths and scrub preparations, shaving foams, lotions and creams.

According to a further particularly preferred aspect, the compositions according to the invention are cosmetic compositions for the care and protection of the skin and hair, nail care compositions or preparations for decorative cosmetics.

Suitable skin cosmetic compositions are, for example, face tonics, face masks, deodorants and other cosmetic lotions. Compositions for use in decorative cosmetics comprise, for example, concealing sticks, stage makeup, mascara and eye shadows, lipsticks, kohl pencils, eyeliners, blushers, dusting powders and eyebrow pencils.

Furthermore, the polypeptides can be used in nose strips for pore cleansing, in antiacne compositions, repellents, shaving compositions, after-shave and pre-shave care compositions, aftersun care compositions, hair-removal compositions, hair colorants, intimate care compositions, foot care compositions, and in babycare.

The skincare compositions according to the invention are, in particular, W/O or O/W skin creams, day and night creams, eye creams, face creams, antiwrinkle creams, antisun creams, moisturizing creams, bleach creams, self-tanning creams, vitamin creams, skin lotions, care lotions and moisturizing lotions.

Particularly photoprotective compositions based on the polypeptide sequences (i) have the property of increasing the residence time of the UV-absorbing ingredients compared to customary auxiliaries such as polyvinylpyrrolidone.

Besides the polypeptide according to embodiment (1 ) or (2) and suitable carriers, the skin cosmetic preparations does preferably also comprise one or more further active ingredients and auxiliaries customary in skin cosmetics, as described above. These include preferably emulsifiers, preservatives, perfume oils, cosmetic active ingredients, such as phytantriol, vitamin A, E and C, retinol, bisabolol, panthenol, photoprotective agents, bleaches, colorants, tints, tanning agents, collagen, protein hydrolysates, stabilizers, pH regulators, dyes, salts, thickeners, gel formers, consistency regulators, silicones, moisturizers, re-fatting agents and further customary additives. Preferred oil and fat components of the cosmetic and pharmaceutical (especially the topical) compositions are the abovementioned mineral and synthetic oils, such as, for example, paraffins, silicone oils and aliphatic hydrocarbons having more than 8 carbon atoms, animal and vegetable oils, such as, for example, sunflower oil, coconut oil, avocado oil, olive oil, lanolin, or waxes, fatty acids, fatty acid esters, such as, for example, triglycerides of the C6-C30-fatty acids, wax esters, such as, for example, jojoba oil, fatty alcohols, vaseline, hydrogenated lanolin and acetylated lanolin, and mixtures thereof.

To establish certain properties, such as, for example, improvement in the feel to the touch, the spreading behavior, the water resistance and/or the binding of active ingredients and auxiliaries, such as pigments, the cosmetic and pharmaceutical preparations can additionally also comprise conditioning substances based on silicone compounds.

Suitable silicone compounds are, for example, polyalkylsiloxanes, polyarylsiloxanes, polyarylalkylsiloxanes, polyethersiloxanes or silicone resins.

The cosmetic or pharmaceutical compositions are prepared by customary methods known to the person skilled in the art.

Preferably, the cosmetic and pharmaceutical compositions are in the form of emulsions, in particular water-in-oil (VWO) or oil-in-water (O/W) emulsions.

It is, however, also possible to choose other types of formulations, for example gels, oils, oleogels, multiple emulsions, for example in the form of W/O/W or 0/W/O emulsions, anhydrous ointments or ointment bases, etc. Emulsifier-free formulations such as hydrodispersions, hydrogels or a Pickering emulsion are also advantageous embodiments.

The emulsions are prepared by known methods. Besides at least one polypeptide according to present invention, the emulsions generally comprise customary constituents, such as fatty alcohols, fatty acid esters and, in particular, fatty acid triglycerides, fatty acids, lanolin and derivatives thereof, natural or synthetic oils or waxes and emulsifiers in the presence of water. The selection of the additives specific to the type of emulsion and the preparation of suitable emulsions is described, for example, in Schrader, Grundlagen und Rezepturen der Kosmetika [Fundamentals and Formulations of Cosmetics], Hϋthig Buch Verlag, Heidelberg, 2nd edition, 1989, third part, which is hereby expressly incorporated by reference. A suitable emulsion as VWO emulsion, e.g. for a skin cream etc., generally comprises an aqueous phase which is emulsified by means of a suitable emulsifier system in an oil or fat phase. To provide the aqueous phase, a polyelectrolyte complex can be used.

Preferred fat components which may be present in the fatty phase of the emulsions are: hydrocarbon oils, such as paraffin oil, purcellin oil, perhydrosqualene and solutions of microcrystalline waxes in these oils; animal or vegetable oils, such as sweet almond oil, avocado oil, calophylum oil, lanolin and derivatives thereof, castor oil, sesame oil, olive oil, jojoba oil, karite oil, hoplostethus oil, mineral oils whose distillation start point under atmospheric pressure is about 250⁰C and whose distillation end point is 410⁰C, such as, for example, vaseline oil, esters of saturated or unsaturated fatty acids, such as alkyl myristates, e.g. isopropyl, butyl or cetyl myristate, hexadecyl stearate, ethyl or isopropyl palmitate, octanoic or decanoic acid triglycerides and cetyl ricinoleate.

The fatty phase can also comprise silicone oils soluble in other oils, such as dimethylpolysiloxane, methylphenylpolysiloxane and the silicone glycol copolymer, fatty acids and fatty alcohols.

It is also possible to use waxes, such as, for example, carnauba wax, candelilla wax, beeswax, microcrystalline wax, ozokerite wax and Ca, Mg and Al oleates, myristates, linoleates and stearates.

In addition, an emulsion according to the invention can be in the form of an O/W emulsion. Such an emulsion usually comprises an oil phase, emulsifiers which stabilize the oil phase in the water phase, and an aqueous phase, which is usually present in thickened form. Suitable emulsifiers are preferably O/W emulsifiers, such as polyglycerol esters, sorbitan esters or partially esterified glycerides.

The composition of embodiment (6) in one aspect of present invention comprises at least one eemulsifier. Emulsifiers which can be used in the composition according to embodiment (6) are nonionic surfactants, zwitterionic surfactants, ampholytic surfactants or anionic emulsifiers. The emulsifiers may be present in the composition of the invention in amounts of from 0.1 to 10, preferably 1 to 5% by weight based on the composition.

It is possible to use as nonionic surfactant for example a surfactant from at least one of the following groups: adducts of 2 to 30 mol of ethylene oxide and/or 0 to 5 mol of propylene oxide with linear fatty alcohols having 8 to 22 C atoms, with fatty acids having 12 to 22 C atoms and with alkylphenols having 8 to 15 C atoms in the alkyl group;

C-₁₂/₁8 fatty acid monoesters and diesters of adducts of 1 to 30 mol of ethylene oxide with glycerol; glycerol monoesters and diesters and sorbitan monoesters and diesters of saturated and unsaturated fatty acids having 6 to 22 carbon atoms and their ethylene oxide adducts; alkyl mono- and oligoglycosides having 8 to 22 carbon atoms in the alkyl radical and their ethoxylated analogs; adducts of 15 to 60 mol of ethylene oxide with castor oil and/or hardened castor oil; polyol esters and especially polyglycerol esters such as, for example, polyglycerol polyricinoleate, polyglycerol poly-12-hydroxystearate or polyglycerol dimerate. Likewise suitable are mixtures of compounds from a plurality of these substance classes; adducts of 2 to 15 mol of ethylene oxide with castor oil and/or hardened castor oil; partial esters based on linear, branched, unsaturated or saturated C₆/₂₂ fatty acids, ricinoleic acid and 12-hydroxystearic acid and glycerol, polyglycerol, pentaerythritol, dipentaerythritol, sugar alcohols (e.g. sorbitol), alkyl glucosides (e.g. methyl glucoside, butyl glucoside, lauryl glucoside) and polyglucosides (e.g. cellulose); mono-, di- and trialkyl phosphates and mono-, di- and/or tri-PEG-alkyl phosphates and the salts thereof; wool wax alcohols; polysiloxane-polyalkyl polyether copolymers and corresponding derivatives; mixed esters of pentaerythritol, fatty acids, citric acid and fatty alcohol as disclosed in DE 1 165574 and/or mixed esters of fatty acids having 6 to 22 carbon atoms, methyl glucose and polyols, preferably glycerol or polyglycerol, and polyalkylene glycols; betaines.

Zwitterionic surfactants can also be used as emulsifiers. The surface-active compounds referred to as zwitterionic surfactants are those having at least one quaternary ammonium group and at least one carboxylate or one sulfonate group in the molecule. Particularly suitable zwitterionic surfactants are the so-called betaines such as the N-alkyl-N,N-dimethylammonium glycinates, for example the cocoalkyldimethyl- ammonium glycinate, N-acylaminopropyl-N,N-dimethylammonium glycinates, for example the cocoacylaminopropyldimethylammonium glycinate, and 2-alkyl-3- carboxylmethyl-3-hydroxyethylimidazolines each having 8 to 18 C atoms in the alkyl or acyl group, and the cocoacylaminoethylhydroxyethylcarboxymethyl glycinate. A particularly preferred fatty amide derivative is that known under the CTFA name cocamidopropyl betaine.

Emulsifiers which are likewise suitable are ampholytic surfactants. Ampholytic surfactants means surface-active compounds which, apart from a Cs iβ-alkyl or -acyl group, comprise at least one free amino group and at least one -COOH or -SO₃H group in the molecule and are able to form inner salts. Examples of suitable ampholytic surfactants are N-alkylglycines, N-alkylpropionic acids, N-alkylaminobutyric acids, N- alkyliminodipropionic acids, N-hydroxyethyl-N-alkylamidopropylglycines, N- alkyltaurines, N-alkylsarcosines, 2-alkylaminopropionic acids and alkylaminoacetic acids each having about 8 to 18 C atoms in the alkyl group.

Particularly preferred ampholytic surfactants are N-cocoalkylaminopropionate, cocoacylaminoethylaminopropionate and Ci₂/i8-acylsarcosine. Besides the ampholytic emulsifiers, also suitable are quarternary emulsifiers, with particular preference for those of the ester quat type, preferably methyl-quaternized di-fatty acid triethanolamine ester salts. Anionic emulsifiers which can also be employed are alkyl ether sulfates, monoglyceride sulfates, fatty acid sulfates, sulfosuccinates and/or ether carboxylic acids.

Suitable oily substances are guerbet alcohols based on fatty alcohols having 6 to 18, preferably 8 to 10, carbon atoms, esters of linear C₆-C₂₂ fatty acids with linear C₆-C₂₂ fatty alcohols, esters of branched C₆-Ci₃ carboxylic acids with linear C₆-C₂₂ fatty alcohols, esters of linear C₆-C₂₂ fatty acids with branched alcohols, especially 2- ethylhexanol, esters of linear and/or branched fatty acids with polyhydric alcohols (such as, for example, propylene glycol, dimerdiol or trimertriol) and/or guerbet alcohols, triglycerides based on C₆-Ci₀ fatty acids, liquid mono/di-, triglyceride mixtures based on C₆-Ci₈ fatty acids, esters of C₆-C₂₂ fatty alcohols and/or guerbet alcohols with aromatic carboxylic acids, especially benzoic acid, esters of C₂-Ci₂ dicarboxylic acids with linear or branched alcohols having 1 to 22 carbon atoms or polyols having 2 to 10 carbon atoms and 2 to 6 hydroxyl groups, vegetable oils, branched primary alcohols, substituted cyclohexanes, linear C₆-C₂₂ fatty alcohol carbonates, guerbet carbonates, esters of benzoic acid with linear and/or branched C₆-C₂₂ alcohols (e.g. Finsolv^® TN), dialkyl ethers, ring-opened products of epoxidized fatty acid esters with polyols, silicone oils and/or aliphatic or naphthenic hydrocarbons. Further oily substances which can be employed are silicone compounds, for example dimethylpolysiloxanes, methylphenylpolysiloxanes, cyclic silicones and amino-, fatty acid-, alcohol-, polyether-, epoxy-, fluorine-, alkyl- and/or glycoside-modified silicone compounds which may at room temperature be both in liquid form and in the form of a resin. The oily substances may be present in the compositions of the invention in amounts of from 1 to 90, preferably 5 to 80, and in particular 10 to 50% by weight based on the composition.

According to a further preferred embodiment, the compositions according to the invention are a shower gel, a shampoo formulation or a bath preparation.

Such formulations comprise at least one polypeptide sequence according to embodiment (1 ) or (2) and customary anionic surfactants as base surfactants and amphoteric and/or nonionic surfactants. Further suitable active ingredients and/or auxiliaries are generally chosen from lipids, perfume oils, dyes, organic acids, preservatives and antioxidants, and thickeners/gel formers, skin conditioning agents and moisturizers. These formulations comprise preferably 2 to 50% by weight, preferably 5 to 40% by weight, particularly preferably 8 to 30% by weight, of surfactants, based on the total weight of the formulation.

In the washing, shower and bath preparations it is possible to use all anionic, neutral, amphoteric or cationic surfactants customarily used in body-cleansing compositions.

Suitable anionic surfactants are, for example, alkyl sulfates, alkyl ether sulfates, alkyl- sulfonates, alkylarylsulfonates, alkyl succinates, alkyl sulfosuccinates, N-alkoyl- sarcosinates, acyl taurates, acyl isethionates, alkyl phosphates, alkyl ether phosphates, alkyl ether carboxylates, alpha-olefinsulfonates, in particular the alkali metal and alkaline earth metal salts, e.g. sodium, potassium, magnesium, calcium, and ammonium and triethanolamine salts. The alkyl ether sulfates, alkyl ether phosphates and alkyl ether carboxylates can have between 1 and 10 ethylene oxide or propylene oxide units, preferably 1 to 3 ethylene oxide units, in the molecule.

These include, for example, sodium lauryl sulfate, ammonium tauryt sulfate, sodium lauryl ether sulfate, ammonium lauryl ether sulfate, sodium lauryl sarcosinate, sodium oleyl succinate, ammonium lauryl sulfosuccinate, sodium dodecylbenzenesulfonate, triethanolamine dodecylbenzenesulfonate.

Suitable amphoteric surfactants are, for example, alkylbetaines, alkylamidopropylbetaines, alkylsulfobetaines, alkyl glycinates, alkyl carboxyglycinates, alkyl amphoacetates or amphopropionates, alkyl amphodiacetates or amphodipropionates.

For example, cocodimethylsulfopropylbetaine, laurylbetaine, cocamidopropylbetaine or sodium cocamphopropionate can be used.

Suitable nonionic surfactants are, for example, the reaction products of aliphatic alcohols or alkylphenols having 6 to 20 carbon atoms in the alkyl chain, which may be linear or branched, with ethylene oxide and/or propylene oxide. The amount of alkylene oxide is about 6 to 60 moles per mole of alcohol. In addition, alkylamine oxides, mono- or dialkylalkanolamides, fatty acid esters of polyethylene glycols, ethoxylated fatty acid amides, alkyl polyglycosides or sorbitan ether esters are suitable.

Furthermore, the washing, shower and bath preparations can comprise customary cationic surfactants, such as, for example, quaternary ammonium compounds, for example cetyltrimethylammonium chloride.

In addition, the shower gel/shampoo formulations can comprise thickeners, such as, for example, sodium chloride, PEG-55, propylene glycol oleate, PEG-120 methylglucose dioleate and others, and preservatives, further active ingredients and auxiliaries and water.

According to a further preferred aspect of embodiment (6), a composition according to present invention is a hair-treatment composition.

Hair-treatment compositions according to the invention preferably comprise at least one polypeptide (1 ) or (2) in an amount in the range from about 0.01 to 30% by weight, preferably 0.5 to 20% by weight, based on the total weight of the composition.

Preferably, the hair-treatment compositions according to the invention are in the form of a setting foam, hair mousse, hair gel, shampoo, hair spray, hair foam, end fluids, neutralizers for permanent waves, hair colorants and bleaches or hot-oil treatments. Depending on the field of use, the hair cosmetic preparations can be applied as (aerosol) spray, (aerosol) foam, gel, gel spray, cream, lotion or wax. Hair sprays here comprise both aerosol sprays and also pump sprays without propellant gas. Hair foams comprise both aerosol foams and also pump foams without propellant gas. Hair sprays and hair foams comprise preferably predominantly or exclusively water-soluble or water-dispersible components. If the compounds used in the hair sprays and hair foams according to the invention are water-dispersible, they can be applied in the form of aqueous microdispersions with particle diameters of from usually 1 to 350 nm, preferably 1 to 250 nm. The solids contents of these preparations here are usually in a range from about 0.5 to 20% by weight. These microdispersions generally require no emulsifiers or surfactants for their stabilization.

The hair-treatment compositions according to present invention comprise, in a preferred embodiment, a) 0.01 to 30% by weight of at least one polypeptide according to embodiment (1 ) or (2), b) 20 to 99.95% by weight of water and/or alcohol, c) 0 to 50% by weight of at least one propellant gas, d) 0 to 5% by weight of at least one emulsifier, e) 0 to 3% by weight of at least one thickener, and up to 25% by weight of further constituents.

Alcohol is understood as meaning all alcohols customary in cosmetics or pharmaceutics, e.g. ethanol, isopropanol, n-propanol.

Further constituents are understood as meaning the additives customary in cosmetics or pharmaceutics, for example propellants, antifoams, inferface-active compounds, i.e. surfactants, emulsifiers, foam formers and solubilizers. The interface-active compounds used may be anionic, cationic, amphoteric or neutral. Further customary constituents may also be, for example, preservatives, perfume oils, opacifiers, active ingredients, UV filters, care substances, such as panthenol, collagen, vitamins, protein hydrolysates, alpha- and beta-hydroxycarboxylic acids, stabilizers, pH regulators, dyes, viscosity regulators, gel formers, salts, moisturizers, re-fatting agents, complexing agents and further customary additives.

These also include all styling and conditioner polymers known in cosmetics which can be used according to the invention if very specific properties are to be established.

Suitable conventional hair cosmetic polymers are, for example, the abovementioned cationic, anionic, neutral, nonionic and amphoteric polymers.

To establish certain properties, the compositions can additionally also comprise conditioning substances based on silicone compounds. Suitable silicone compounds are, for example, polyalkylsiloxanes, polyarylsiloxanes, polyarylalkylsiloxanes, polyethersiloxanes, silicone resins or dimethicone copolyols (CTFA) and aminofunctional silicone compounds, such as amodimethicones (CTFA).

The hair-treating composition according to embodiment (6) is in one preferred aspect a hair spray (aerosol spray or pump spray without propellant gas) or hair foam (aerosol foam or pump foam without propellant gas).

In a preferred embodiment, spray preparations comprise a) 0.01 to 30% by weight of at least one polypeptide according to embodiment (1 ) or (2), b) 20 to 99.9% by weight of water and/or alcohol, c) 0 to 70% by weight of at least one propellant, d) 0 to 20% by weight of further constituents.

Propellants are the propellants customarily used for hair sprays or aerosol foams. Preference is given to mixtures of propane/butane, pentane, dimethyl ether, 1 ,1- difluoroethane (HFC-152 a), carbon dioxide, nitrogen or compressed air.

A formulation for aerosol hair foams preferred according to the invention comprises a) 0.01 to 30% by weight of at least one polypeptide according to embodiment (1 ) or (2), b) 55 to 99.8% by weight of water and/or alcohol, c) 5 to 20% by weight of a propellant, d) 0.1 to 5% by weight of an emulsifier, e) 0 to 10% by weight of further constituents.

Emulsifiers which can be used are all of the emulsifiers customarily used in hair foams. Suitable emulsifiers may be nonionic, cationic or anionic or amphoteric.

Examples of nonionic emulsifiers (INCI nomenclature) are laureths, e.g. laureth-4; ceteths, e.g. cetheth-1 , polyethylene glycol cetyl ethers, ceteareths, e.g. cetheareth-25, polyglycol fatty acid glycerides, hydroxylated lecithin, lactyl esters of fatty acids, alkyl polyglycosides. Examples of cationic emulsifiers are cetyldimethyl-2-hydroxyethylammonium dihydrogenphosphate, cetyltrimonium chloride, cetyltrimonium bromide, cocotrimonium methyl sulfate, quaternium-1 to x (INCI).

Anionic emulsifiers can, for example, be chosen from the group of alkyl sulfates, alkyl ether sulfates, alkylsulfonates, alkylarylsulfonates, alkyl succinates, alkyl sulfosuccinates, N-alkoylsarcosinates, acyl taurates, acyl isethionates, alkyl phosphates, alkyl ether phosphates, alkyl ether carboxylates, alpha-olefinsulfonates, in particular the alkali metal and alkaline earth metal salts, e.g. sodium, potassium, magnesium, calcium, and ammonium and triethanolamine salts. The alkyl ether sulfates, alkyl ether phosphates and alkyl ether carboxylates can have between 1 and 10 ethylene oxide or propylene oxide units, preferably 1 to 3 ethylene oxide units, in the molecule.

A preparation suitable according to the invention for styling gels can, for example, have the following composition: a) 0.01 to 30% by weight of at least one polypeptide according to embodiment (1 ) or (2), b) 80 to 99.85% by weight of water and/or alcohol, c) 0 to 3% by weight, preferably 0.05 to 2% by weight, of a gel former, d) 0 to 20% by weight of further constituents.

Gel formers which may be used are all gel formers customary in cosmetics. These include slightly crosslinked polyacrylic acid, for example carbomer (INCI), cellulose derivatives, e.g. hydroxypropylcellulose, hydroxyethylcellulose, cationically modified celluloses, polysaccharides, e.g. xanthan gum, caprylic/capric triglyceride, sodium acrylate copolymers, polyquaternium-32 (and) Paraffinum Liquidum (INCI), sodium acrylate copolymers (and) Paraffinum Liquidum (and) PPG-1 trideceth-6, acrylamidopropyltrimonium chloride/acrylamide copolymers, steareth-10 allyl ether, acrylate copolymers, polyquaternium-37 (and) Paraffinum Liquidum (and) PPG-1 trideceth-6, polyquaternium 37 (and) propylene glycol dicaprate dicaprylate (and) PPG- 1 trideceth-6, polyquaternium-7, polyquaternium-44.

The polypeptides according to present invention are in one preferred aspect of embodiments (6) or (7) used as conditioners in shampoos. They may ease the combing of hair.

Preferred shampoo formulations comprise a) 0.01 to 30% by weight of at least one polypeptide (1 ) or (2), b) 25 to 94.95% by weight of water, c) 5 to 50% by weight of surfactants, c) 0 to 5% by weight of a further conditioner, d) 0 to 10% by weight of further cosmetic constituents.

In the shampoo formulations it is possible to use all of the anionic, neutral, amphoteric or cationic surfactants customarily used in shampoos. Suitable anionic surfactants are, for example, alkyl sulfates, alkyl ether sulfates, alkylsulfonates, alkylarylsulfonates, alkyl succinates, alkyl sulfosuccinates, N- alkoylsarcosinates, acyl taurates, acyl isethionates, alkyl phosphates, alkyl ether phosphates, alkyl ether carboxylates, alpha-olefinsulfonates, in particular the alkali metal and alkaline earth metal salts, e.g. sodium, potassium, magnesium, calcium, and ammonium and triethanolamine salts. The alkyl ether sulfates, alkyl ether phosphates and alkyl ether carboxylates can have between 1 and 10 ethylene oxide or propylene oxide units, preferably 1 to 3 ethylene oxide units, in the molecule.

Of suitability are, for example, sodium lauryl sulfate, ammonium lauryl sulfate, sodium lauryl ether sulfate, ammonium lauryl ether sulfate, sodium lauroyl sarcosinate, sodium oleyl succinate, ammonium lauryl sulfosuccinate, sodium dodecylbenzenesulfonate, triethanolamine dodecylbenzenesulfonate.

Suitable amphoteric surfactants are, for example, alkylbetaines, alkylamidopropyl- betaines, alkylsulfobetaines, alkyl glycinates, alkyl carboxyglyci nates, alkyl amphoacetates or amphopropionates, alkylamphodiacetates or amphodipropionates.

For example, cocodimethylsulfopropylbetaine, laurylbetaine, cocamidopropylbetaine or sodium cocamphopropionate can be used.

Suitable nonionic surfactants are, for example, the reaction products of aliphatic alcohols or alkylphenols having 6 to 20 carbon atoms in the alkyl chain, which may be linear or branched, with ethylene oxide and/or propylene oxide. The amount of alkylene oxide is about 6 to 60 moles per mole of alcohol. In addition, alkylamine oxides, mono- or dialkylalkanolamides, fatty acid esters of polyethylene glycols, alkyl polyglycosides or sorbitan ether esters are suitable.

Furthermore, the shampoo formulations can comprise customary cationic surfactants, such as, for example, quaternary ammonium compounds, for example cetyltrimethylammonium chloride.

In the shampoo formulations, customary conditioners can be used in combination with the polypeptide sequences (i) to achieve certain effects.

These include, for example, the abovementioned cationic polymers with the INCI name Polyquaternium, in particular copolymers of vinylpyrrolidone/N-vinylimidazolium salts (Luviquat FC, Luviquat&commat, HM, Luviquat MS, Luviquat Care), copolymers of N- vinylpyrrolidone/dimethylaminoethyl methacrylate, quaternized with diethyl sulfate (Luviquat D PQ 1 1 ), copolymers of N-vinylcaprolactam/N-vinylpyrrolidone/N- vinylimidazolium salts (Luviquat D Hold), cationic cellulose derivatives (Polyquaternium-4 and -10), acrylamide copolymers (Polyquaternium-7). In addition, protein hydrolysates can be used, and conditioning substances based on silicone compounds, for example polyalkylsiloxanes, polyarylsiloxanes, polyarylalkylsiloxanes, polyethersiloxanes or silicone resins. Further suitable silicone compounds are dimethicone copolyols (CTFA) and aminofunctional silicone compounds such as amodimethicones (CTFA). In addition, cationic guar derivatives, such as guar hydroxypropyltrimonium chloride (INCI) can be used.

The invention according to embodiments (1 ) and (2) further pertains to keratin-binding functional variants of the keratin-binding polypeptides comprising

(i) at least one keratin-binding polypeptide as defined above (first domain),

(ii) an effector molecule (ii) which is not naturally linked to the polypeptide (i) (second domain).

These functional variants are also designated as "keratin-binding effector molecules" in the following.

Thus, in a preferred aspect of embodiments (6) and (7), they pertain to compositions comprising said keratin-binding effector molecules and the use of such molecules.

The duration of action of an effector molecule on a keratin or keratin-comprising material can be signified prolonged by coupling an effector molecule to a keratin- binding polypeptide (i).

An effector molecule (ii) is a molecule which has a particular, predictable effect. Preferably, said effect is a cosmetic, therapeutic or preventive effect or a combination thereof. More preferably, it is a cosmetic or therapeutic effect.

The effector molecules (ii) are connected to a polypeptide sequence (i) which has a binding affinity for a keratin. The connection between (i) and (ii) can be both a covalent bond and based on ionic or van der Waals interactions.

A covalent linkage is preferred. This can take place for example via the side chains of the polypeptide sequence (i), in particular via amino functions or hydroxyl functions or carboxylate functions or thiol functions. Linkage via the amino functions of one or more lysine residues, one or more thiol groups of cysteine residues or via the N-terminal or C-terminal function of the polypeptide (i) is preferred. Apart from the amino acid functions present in the polypeptide sequence (i) it is also possible for amino acids with suitable functions (e.g. cysteines, lysines, aspartates, glutamates) to be attached to the sequence or for amino acids of the polypeptide sequence (i) to be substituted by such amino acid functions. Linkage of the effector molecules (N) to the polypeptide sequence (i) can take place either directly, i.e. as covalent linkage of two chemical functions already present in (i) and (ii), for example an amino function of (i) is linked to a carboxylate function of (ii) to give the amide. The linkage can, however, also take place via a so-called linker, i.e. an at least bifunctional molecule, which undergoes bonding with one function to (i) and is linked by one or more other functions to (ii).

If the effector molecule (ii) likewise consists of a polypeptide sequence, the linkage of (i) and (ii) can take place through a so-called fusion protein, i.e. a continuous polypeptide sequence consisting of the two partial sequences (i) and (ii).

It is also possible to incorporate so-called spacer elements between (i) and (ii), for example polypeptide sequences which have a potential cleavage site for a protease, lipase, esterase, phosphatase, hydrolase, or oligo- and polypeptide sequences which allow the fusion protein to be purified easily, for example so-called His tags, i.e. oligohistidine residues.

The spacer elements may further be composed of alkyl chains, ethylene glycol and polyethylene glycols.

Particularly preferred linker and/or spacer elements have a potential cleavage site for a protease, lipase, esterase, phosphatase, hydrolase, i.e. are enzymatically cleavable. Examples of enzymatically cleavable linkers which can be used in the molecules according to the invention are given, for example, in WO 98/01406, to the entire contents of which reference is hereby expressly made.

Particularly preferred linkers and spacers are thermally cleavable or photocleavable. Corresponding chemical structures are known to the person skilled in the art and are integrated between the molecular moieties (i) and (ii).

Linkage in the case of a non-proteinaceous effector molecule to the polypeptide sequence (i) preferably takes place with functionalizable residues (side groups, C or N terminus) on the polypeptide (i) which undergo covalent connection to the chemical function of the effector molecule.

The linkage in this case is preferably via an amino, thiol or hydroxyl function of the polypeptide (i), which are able to undergo a corresponding amide, thioester or ester bonding for example with a carboxyl function of the effector molecule (ii), where appropriate after activation.

A further preferred linkage of the polypeptide sequence (i) to an effector molecule (ii) is the use of a tailored linker. Such a linker has two or more so-called anchor groups with which it can link the polypeptide sequence (i) and one or more effector molecules (ii). For example, an anchor group for (i) may be a thiol function by means of which the linker can undergo disulfide bonding to a cysteine residue of the polypeptide (i). An anchor group for (ii) may be for example a carboxyl function by means of which the linker can undergo ester bonding to a hydroxyl function of the effector molecule (ii).

The use of such tailored linkers allows the linkage to be adapted accurately to the desired effector molecule. It is additionally possible thereby to link a plurality of effector molecules to a polypeptide sequence (i) in a defined manner.

The linker which is used depends on the functionality to be coupled. Suitable examples are molecules which couple to polypeptides (i) by means of sulfhydryl-reactive groups, e.g. maleimides, pyridyl disulfides, α-haloacetyls, vinyl sulfones, sulfatoalkyl sulfones (preferably sulfatoethyl sulfones) and to effector molecules (ii) by means of - sulfhydryl-reactive groups (e.g. maleimides, pyridyl disulfides, α-haloacetyls, vinyl sulfones, sulfatoalkyl sulfones (preferably sulfatoethyl sulfones) amine-reactive groups (e.g. succinimidyl esters, carbodiimides, hydroxymethylphosphine, imidoesters, PFP esters etc.) sugars or oxidized sugar-reactive groups (e.g. hydrazides etc.) - carboxy-reactive groups (e.g. carbodiimides etc.) hydroxyl-reactive groups (e.g. isocyanates etc.) thymine-reactive groups (e.g. psoralen etc.) nonselective groups (e.g. aryl azides etc.) photoactivatable groups (e.g. perfluorophenyl azide etc.) - metal-complexing groups (e.g. EDTA, hexahis, ferritin) antibodies and fragments thereof (e.g single-chain antibodies, F(ab) fragments of antibodies, catalytic antibodies).

An alternative possibility is direct coupling between active substance/effector and the keratin-binding domain, e.g. by means of carbodiimides, glutaraldehyde, the abovementioned crosslinkers or other crosslinkers known to the skilled worker.

The keratin-binding effector molecules of the invention have a wide area of application in human cosmetics, especially in skin and hair care, animal care, leather care and leather processing.

The keratin-binding effector molecules of the invention are preferably used in the same use and/or composition as outlined above more generally for the poylpeptide according to embodiment (1 ) or (2).

In a preferred aspect, they are used in cosmetics, especially in skin, nail or hair cosmetic compositions. They permit a high concentration and long duration and action time of a skin-, nail- and hair-care or skin-, nail- and hair-protecting effector molecule on the keratin.

In another preferred aspect, they are used as ingredient in a pharmaceutical composition. Preferably, in this aspect the effector molecule (ii) is a pharmaceutically active compound. The use of such keratin-binding effector-molecukes permits a high concentration and long duration of action of the effector molecule on the treated area.

A composition comprising such keratin-binding effector molecule may comprise other ingredients and may be formulated as described above generally for compositions comprising the polypeptide of present invention.

Effector molecules according to present invention may be either proteinaceous molecules such as enzymes or else non-proteinogenic molecules such as dyes, sunscreens, vitamins, provitamins, antioxidants and fatty acids, conditioners, or metal ion-containing compounds.

Among the proteinaceous effector molecules, preference is given to enzymes and antibodies. Among the enzymes, the following are preferred as effector molecules (ii): oxidases, peroxidases, proteases, glucanases, mutanase, tyrosinases, laccases, metal-binding enzymes, lactoperoxidase, lysozyme, amyloglycosidase, glucose oxidase, superoxide dismutase, photolyase, T4 endonuclease, catalase, thioredoxin, thioredoxin reductase.

The proteinaceous effector molecules (ii) without enzymatic activity which are preferred as effector molecules (ii) are the following: antimicrobial peptides, silk proteins, hydrophobins, collaten, carotenoid-binding proteins, heavy metal-binding proteins, odorant-binding proteins.

Also very suitable as proteinaceous effector molecules (ii) are hydrolysates of proteins from vegetable and animal sources, for example hydrolysates of proteins of marine origin or silk hydrolysates.

Among the non-proteinaceous effector molecules (ii), preference is given to dyes, more preferably hair dyes, food dyes, semipermanent dyes or reactive or oxidation dyes. In the case of oxidation dyes, it is preferred for one component to be coupled as effector molecule (ii) to the keratin-binding polypeptide according to embodiment (1 ) or (2) and then be oxidatively coupled to the second dye component at the site of action, i.e. after binding to the hair. It is further preferred with oxidation dyes to carry out the coupling of the color components before the linkage to the polypeptide according to embodiment (1 ) or (2). The reactive dyes may further preferably be linked as one component as effector molecule (ii) to the keratin-binding polypeptide according to embodiment (1 ) or (2) and then be bound to the hair. It is further possible for such dyes which are linked as effector molecule (ii) to the keratin-binding polypeptide according to embodiment (1 ) or (2) to be employed in decorative cosmetics through binding to nails or skin.

Suitable dyes for the molecules of the invention are all conventional hair dyes. Suitable dyes are known to the skilled worker from handbooks of cosmetics, for example Schrader, Grundlagen und Rezepturen der Kosmetika, Hϋthig Verlag, Heidelberg, 1989, ISBN 3-7785-1491-1.

Particularly advantageous dyes are those specified in the list below. The colour index numbers (CIN) are taken from the Rowe Colour Index, 3^rd edition, Society of Dyers and Colourists, Bradford, England, 1971.

Also very suitable as hair dyes are food dyes.

The abovementioned dyes can also be used as effector molecules (ii) to a skin- or nail- binding polypeptide according to embodiment (1 ) or (2) for the coloring of skin or nails e.g. in tattoos.

Further preferred effector molecules (ii) are fatty acids, in particular saturated fatty acids carrying an alkyl branch, particularly preferably branched eicosanoic acids, such as 18-methyleicosanoic acid. Further preferred effector molecules (N) are carotenoids. According to the invention, carotenoids are understood as meaning the following compounds and esterified or glycosylated derivatives thereof, β-carotene, lycopene, lutein, astaxanthin, zeaxanthin, cryptoxanthin, citranaxanthin, canthaxanthin, bixin, β-apo-4-carotenal, β-apo-8- carotenal, β-apo-8-carotenoic esters, neurosporene, echinenone, adonirubin, violaxanthin, torulene, torularhodin, singly or as mixture. Carotenoids which are preferably used are β-carotene, lycopene, lutein, astaxanthin, zeaxanthin, citranaxanthin and canthaxanthin.

Further preferred effector molecules (ii) are vitamins, especially vitamin A, retinoids and esters thereof.

Retinoids mean for the purposes of the present invention vitamin A alcohol (retinol) and its derivatives such as vitamin A aldehyde (retinal), vitamin A acid (retinoic acid) and vitamin A esters (e.g. retinyl acetate, retinyl propionate and retinyl palmitate). The term retinoic acid includes in this connection both all-trans-retinoic acid and 13-cis-retinoic acid. The terms retinol and retinal preferably include the all-trans compounds. The retinoid preferably used for the suspensions of the invention is all-trans-retinol, referred to as retinol hereinafter.

Further preferred effector molecules (ii) are vitamins, provitamins and vitamin precursors from the A, C, E and F groups, especially 3,4-didehydroretinol, β-carotene (provitamin of vitamin A), ascorbic acid (vitamin C), and the palmitic esters, glucosides or phosphates of ascorbic acid, tocopherols, especially α-tocopherol and its esters, e.g. the acetate, the nicotinate, the phosphate and the succinate; additionally vitamin F, by which are meant essential fatty acids, especially linoleic acid, linolenic acid and arachidonic acid.

The vitamins, provitamins or vitamin precursors of the vitamin B group or derivatives thereof, and the derivatives of 2-furanone which are preferably to be employed according to the invention include, inter alia:

Vitamin B₁, trivial name thiamine, chemical name 3-[(4'-amino-2'-methyl-5'-pyrimidinyl) methyl]-5-(2-hydroxyethyl)-4-methylthiazolium chloride. Vitamin B₂, trivial name riboflavin, chemical name 7,8-dimethyl-10-(1 -D-ribityl)- benzo[g]pteridine-2,4(3H,10H)-dione. Riboflavin occurs in free form for example in whey, and other riboflavin derivatives can be isolated from bacteria and yeasts. A riboflavin stereoisomer which is likewise suitable according to the invention is lyxoflavin which can be isolated from fish meal or liver and which has a D-arabityl radical in place of D-ribityl.

Vitamin B₃. The compounds nicotinic acid and nicotinamide (niacinamide) are frequently designated thus. Nicotinamide is preferred according to the invention. Vitamin B₅ (pantothenic acid and panthenol). Panthenol is preferably employed. Panthenol derivatives which can be employed according to the invention are, in particular, the esters and ethers of panthenol, and cationically derivatized panthenols. In a further preferred embodiment of the invention it is possible to employ in addition to pantothenic acid or panthenol also derivatives of 2-furanone. Particularly preferred derivatives are the substances, which are also commercially available, dihydro-3- hydroxy-4,4-dimethyl-2(3H)-furanone with the trivial name pantolactone (Merck), 4- hydroxymethyl-γ-butyrolactone (Merck), 3,3-dimethyl-2-hydroxy-γ-butyrolactone (Aldrich) and 2,5-dihydro-5-methoxy-2-furanone (Merck), with all stereoisomers being expressly included.

These compounds advantageously confer moisturizing and skin-soothing properties on the keratin-binding effector molecules of the invention.

Vitamin B₆, by which is meant not a uniform substance but the derivatives of 5- hydroxymethyl-2-methylpyridin-3-ol which are known under the trivial names of pyridoxine, pyridoxamine and pyridoxal.

Vitamin B₇ (biotin), also referred to as vitamin H or "skin vitamin". Biotin is (3aS,4S,

6aR)-2-oxohexahydrothienol[3,4-d]imidazole-4-valeric acid. Panthenol, pantolactone, nicotinamide and biotin are very particularly preferred according to the invention.

Preferred lipophilic, oil-soluble antioxidants suitable as effector molecules are tocopherol and its derivatives, gallic esters, flavonoids and carotenoids, and butylated hydroxytoluenel/anisole. Preferred water-soluble antioxidants are amino acids, e.g. tyrosine and cysteinee and derivatives thereof, and tannins especially those of vegetable origin.

Suitable effector molecules are also triterpenes, especially triterpene acids such as ursolic acid, rosmarinic acid, betulinic acid, boswellic acid and bryonolic acid.

A further preferred effector molecule (ii) is lipoic acid and suitable derivatives (salts, esters, sugars, nucleotides, nucleosides, peptides and lipids).

Further preferred effector molecules (ii) are UV light filters. By this are meant organic substances able to absorb ultraviolet rays and emit the absorbed energy again in the form of longer-wavelength radiation, e.g. heat. The organic substances may be oil- soluble or water-soluble.

Examples of oil-soluble UV-B filters which can be used are the following substances: 3-benzylidenecamphor and its derivatives, e.g. 3-(4-methylbenzylidene)camphor; 4-aminobenzoic acid derivatives, preferably 2-ethylhexyl 4-(dimethylamino)benzoate, 2-octyl 4-(dimethylamino)benzoate and amyl 4-(dimethylamino)benzoate; esters of cinnamic acid, preferably 2-ethylhexyl 4-methoxycinnamate, propyl 4- methoxycinnamate, isoamyl 4-methoxycinnamate, isopentyl 4-methoxycinnamate, 2- ethylhexyl 2-cyano-3-phenylcinnamate (octocrylene); esters of salicylic acid, preferably 2-ethylhexyl salicylate, 4-isopropylbenzyl salicylate, homomenthyl salicylate; derivatives of benzophenone, preferably 2-hydroxy-4-methoxybenzophenone, 2- hydroxy-4-methoxy-4'-methylbenzophenone, 2,2'-dihydroxy-4-methoxybenzophenone; esters of benzalmalonic acid, preferably 2-ethylhexyl 4-methoxybenzalmalonate; triazine derivatives such as, for example, 2,4,6-trianilino-(p-carbo-2'-ethyl-1 ^'-hexyloxy)- 1 ,3,5-triazine (octyl triazone) and dioctyl butamido triazone (Uvasorb^® HEB): propane-1 ,3-diones such as, for example, 1-(4-tert-butylphenyl)-3-(4'- methoxyphenyl)propane-1 ,3-dione.

Suitable water-soluble UV-filters are:

2-phenylbenzimidazole-5-sulfonic acid and the alkali metal, alkaline earth metal, ammonium, alkylammonium, alkanolammonium and glucammonium salts thereof; sulfonic acid derivatives of benzophenone, preferably 2-hydroxy-4- methoxybenzophenone-5-sulfonic acid and its salts; sulfonic acid derivatives of 3-benzylidenecamphor such as, for example, 4-(2-oxo-3- bornylidenemethyl)benzenesulfonic acid and 2-methyl-5-(2-oxo-3-bornylidene)sulfonic acid and salts thereof.

It is particularly preferred to use esters of cinnamic acid, preferably 2-ethylhexyl 4- methoxycinnamate, isopentyl 4-methoxycinnamate, 2-ethylhexyl 2-cyano-3- phenylcinnamate (octocrylene).

It is further preferred to use derivatives of benzophenone, in particular 2-hydroxy-4- methoxybenzophenone, 2-hydroxy-4-methoxy-4^"-methylbenzophenone, 2,2'-dihydroxy- 4-methoxybenzophenone and to use propane-1 ,3-diones such as, for example 1-(4- tert-butylphenyl)-3-(4'-methoxyphenyl)propane-1 ,3-dione.

Typical UV-A filters which are suitable are: derivatives of benzoylmethane such as, for example, 1-(4'-tert-butylphenyl)-3-(4'- methoxyphenyl)propane-1 ,3-dione, 4-tert-butyl-4'-methoxydibenzoylmethane or 1- phenyl-3-(4'-isopropylphenyl)propane-1 ,3-dione; amino-hydroxy-substituted derivatives of benzophenones such as, for example, N, N- diethylaminohydroxybenzoyl-n-hexyl benzoate.

The UV-A and UV-B filters can, of course, also be employed in mixtures. Further suitable UV filter substances are given in the table below.

Besides the two aforementioned groups of primary photoprotective substances it is also possible to employ secondary sunscreens of the antioxidant type which break the chain of photochemical reactions which is induced when UV rays penetrate into the skin. Typical examples thereof are superoxide dismutase, catalase, tocopherols (vitamin E) and ascorbic acid (vitamin C).

A further preferred group of effector molecules are anti-irritants which have an antiinflammatory effect on skin damaged by UV light. Examples of such substances are bisabolol, phytol and phytantriol.

A further preferred group of effector molecues are deodorant and antiperspirant compounds. Effector molecules (ii) suitable in particular for deodorants are: perfume oils, cyclodextrines, ion exchangers, zinc ricinoleate, antimicrobial/bacteriostatic compounds (e.g. DCMX, lrgasan DP 300, TCC ). Suitable for antipersipirants are: tannins, and zinc/aluminum salts.

A preferred area of application of the polypeptides and compositions of present invention is the therapeutic or prophylactic use for the treatment or prevention of certains disorders and deseases. Especially preferred areas of application are the therapeutic or prophylactic treatment of the skin, hair, and of the mucous membranes.

It is advantageous, especially in the oral, pharyngeal and nasal spaces, for pharmaceutically active substances for therapy/prophylaxis to be bound more strongly and for a longer time to skin and/or hair via the keratin-binding polypeptide. This prevents systemic uptake of a pharmaceutically active ingredient through the skin barrier when it is bound to a keratin-binding polypeptide of present invention. In a second preferred aspect, it allows a slow release of a pharmaceutically active ingredient bound to the keratin-binding polypeptide of present invention.

In another preferred aspect, the keratin-binding polypeptide itself is the pharmaceutically active ingredient of the composition.

In a preferred aspect of present invention, polypeptides and compositions of present invention are used for topical application of drugs or active ingredients that should only be present on skin and should not be taken up systemically due to possible side effects.

In a further preferred aspect, polypeptides and compositions of present invention are used to achieve a slow release of an active ingredient onto skin and/or hair, as the proteolytic degradation of the keratin-binding polypeptide takes some time.

Areas of pharmaceutical use and of use as ingredient of a pharmaceutical composition for the polypeptide and the keratin-binding effector molecules of present invention are, in particular: viral diseases (e.g. herpes, coxsackie, varicella zoster, cytomegalovirus etc) bacterial diseases (e.g. TB, syphilis etc.) fungal diseases (e.g. Candida, cryptococcus, histoplasmosis, aspergillus, mucormycosis etc.) neoplastic diseases (e.g. melanomas, adenomas etc.) autoimmune diseases (e.g. pemphigus vulgaris, bullous pemphgoid, systemic lupus erythematosis etc.) sunburn - parasitic infestation (e.g. ticks, mites, fleas etc.) prevention of insect contact and treatment of insect stings and bites (e.g. bloodsucking insects such as anopheles etc.) In a preferred aspect of embodiments (6) and (7), the polypeptide according to present invention comprises a pharmaceutically active ingredient suitable for therapy or prophylaxis (e.g. a corticoid, immunosuppressant compound, antibiotic, antimycotic, antiviral compound, insect repellent etc.) coupled via one of the linkers described above to a keratin-binding polypeptide according to embodiment (1 ) or (2).

The following table indicates pharmaceutically active ingredients which may preferably be coupled to a keratin-binding polypeptide of present invention:

Skin

Desease effector molecules / active ingredients benzoyl salicyclic acne peroxide acid antibiotics corticol retinoic acid age marks retinoic acid derivatives rash / glucoallergy corticoids antihistamine cortisole antiatopic antihistamin inflammatory dermatitis e drugs cortisole

5-Fluoro-

Basaliom Imiquimod uracil

Am op ho- Ke to- Flu- FIu-

Candidosis antifungals Nystatin Natamycin tericin B conazol conazol cytosin

Condylomata cytostatic Podophyll acuminata agents Imiquimod otoxin

Dekubitus antibiotics panthenol

Molluscum contagio- retinoic acid sum retinoic acid derivatives

Dermatitis, erythroglucoperioral antibiotics tetracyclin mycin corticoids dermatophyte infections antifungals tolnaftat

Erysipelas antibiotics penicilline

Pediculosis insecticides Allethrin Permethrin Pyrethrin

Ammoniu desinfectant Polyvidon mbitumino

Furuncles S iodine sulfat herpes zoster antivirals Brivudin Aciclovir Famciclovir

Typ 1 antivirals Aciclovir

Human-

Papilloma- cytostatic Podophyll

Virus agents Imiquimod otoxin

Hyper- botulinum hid rosis toxin retinoic acid salicyclic

Ichthyosis retinoic acid derivatives acid

Diclofenac-

Actinic 5-Fluoro hyaluronic keratosis uracil acid Pityriasis Keto- Fluconaversicolor antifungals conazole zole Itraconazole

Lichen ruber glucoplanus cortisole antihistamine corticoids

Skabies permethrin

Herpes labialis antivirals Aciclovir

Madura Peni- Sulfon- Cephalo- Ampho- Itra- mycosis antibiotics antifungals cillines amides sporines tericin conazo

MetroniErythro- benzoyl erythro-

Rosacea antibiotics dazole mycine peroxide tetracycline mycine

Seborreic antimfungal cortisole rash S derivatives

Sun burn cortisole diclofenac

Thrush antifungals cortisole glucocortico

Vitiligo ids

Diper Dex- Clotrimadermatitis panthenol antifungals Nystatin zole

Wound Dex- treatment panthenol Panthenol antibiotics antifungals

In a second preferred aspect, the polypeptide according to embodiment (1 ) or (2) acts as carrier for the pharmaceutically active ingredient, but is not coupled via a linker to the pharmaceutically active ingredient. The pharmaceutically active ingredient is preferably an ingredient as listed in the above table.

In a third preferred aspect, the polypeptide according to embodiment (1 ) or (2) itself is the pharmaceutically active ingredient. Preferred application fields of this pharmaceutical preparation are the treatment of ichtyosis, treatment of psoriasis, wound treatment and wound healing.

The polypeptide according to embodiment (8), i.e. for the use as a medicament, is preferably for use in the treatment of skin and/or hair diseases or skin and/or hair clinical conditions. It may be especially suitable for treatments wherein (i) a tight binding of the active ingredient to hair and/or skin and/or (ii) a slow release of the effecot molecule from the KBD-B by skin protease activity is desirable. More preferably, the polypeptide according to embodiment (8) is suitable in the treatment or prevention of one or more of the following: hair loss, hair damage, acne, age marks, rash / allergy, atopic dermatitis, basalioma, candidosis, condylomata acuminata, dekubitus, molluscum contagiosum, perioral dermatitis, dermatophyte infections, erysipelas, pediculosis, furuncles, herpes zoster, human papilloma-virus infection, hyperhidrosis, ichthyosis, actinic keratosis, pityriasis versicolor, lichen ruber planus, scabies, herpes labialis, mycosis (especially madura mycosis), rosacea, seborreic rash, sun burn, thrush, vitiligo, diaper dermatitis, infestation with crab lice or hair lice, skin cancer, psoriasis and wounds. It may especially be suitable in wound healing and wound treatment.

In preferred aspects of embodiment (8), the polypeptide is a polypeptide or keratin- binding effector molecule as described above in the context of embodiments (6) and (7).

One problem underlying the present invention was the lack of a complete crystal structure of a keratin. There existed only structural data on tiny keratin fragments, but no data on the complete keratin rod, let alone the rod segment bound by desmoplakin or isolated KBD-B. Thus, one of the aims of present invention was the creation of a model of a reference keratin for binding studies. The resulting model is the keratin model according to embodiment (9) of present invention.

The keratin model according to embodiment (9) is preferably a computer generated model, and may be displayed in one of the following programs: Sybyl, vmd v.1.8.5, Insight, Hex.

The problem underlying present invention was the provision of keratin-binding molecules. Thus, the target keratins of principal interest were the following keratins of skin and hair:

- eight known dimers in the kuticula of human hair: K32(previously: hHa2)/82(hHb2), K35(hHa5)/82, K39/82, K40/82, K32/85(hHb5), K35/85, K39/85, K40/85; and

- the prevalent dimers in keratinocytes of skin epidermis, K5/14 and K1/10.

CK8/18 was chosen as reference keratin because its composition resembles the composition of hair and skin keratin, and because it is bound by desmoplakin. As described in example 2, the present invention provides a homology model of CK8/18 whose creation did for the first time allow the modelling the interaction between keratin and KBD-B. The homology model of CK8/18 is based on the amino acid sequences of CK8 and CK18 and on the crystal structure 1d7m (PDB code) of cortexillin (SEQ ID NO:63) as a template (compare example 2). The choice of 1d7m as a structure template for the keratin coiled coil was one of the key steps in establishing the keratin structure model. The resulting atom coordinates for the region bound by KBD-B and the complete CK8/18 atom coordinates are listed in tables 2 and 1 , respectively.

Any amino acid sequence representing a complete or partial rod domain of a keratin heterodimer may be used in the models according to present invention, preferably a sequence representing the complete rod domain. The rod sequences of CK8/18, which are most preferred in the context of present invention, are given in Fig. 2. Even more preferred is the rod domain segment 1 B, especially the segment bound by KBD-B, namely G170 to V208 of CK8 and L159 to L197 of CK18. Present invention shows that KBD-B binds to the segment spanning amino acids G170 to V208 of the CK8 amino acid sequence (SEQ ID NO:51 ), which lie in the rod segment 1 B (Fig. 7). Thus, the exact keratin region which is bound by KBD-B is narrowed down considerably by present invention, namely to the region represented by the amino acids G170 to V208 of CK8 and L159 to L197 of CK18 and of the corresponding regions as indicated in the alignment in Fig. 3, i.e. to a region spanning only 39 amino acids of each of the two keratin monomers forming the coiled coil rod.

Thus, embodiment (9) of present invention is a three-dimensional structure model of the rod domain of a keratin coiled coil, which is formed by two polypeptide strands, comprising at least 30, preferably 35, more preferably 39 consecutive amino acids of the rod segment 1 B per strand of two keratin monomers forming a keratin heterodimer in vivo. Preferably, the region covered by said keratin structure model encompasses a coherent part of more than 50%, more preferably more than 75 %, most preferably all of the region bound by KBD-B. E.g., in case of CK8/18, a part of at least 30 amino acids of the 49 amino acid region bound by KBD-B (compare Fig. 7), i.e. the region from amino acid G170 to V208 of CK8 and L159 to L197 of CK18 is comprised in the model according to embodiment (9).

The side chain geometry of all amino acid residues in the keratin model is preferably adjusted using the internal rotamer library (version 3) of program SCWRL (Dunbrack Jr. R.L. and Karplus M., 1993, J. MoI. Biol. 230, 543-574).

In embodiment (9), one, several, or all of the the amino acids at positions of the amino acid sequence of the rod domain which correspond to the following positions in CK8 and 18 (compare Fig.3) remain preferably unchanged or are subject to homologous amino exchanges only: CK18V166, CK18T170, CK18M174, CK18E179, CK18D181 , CK18L185, CK18R186, CK18V188, CK18D191 , CK8F193, CK8V200, CK8D01 , CK8Y204. Without being bound by theory, it is assumed that said amino acids are important interface amino acids of the keratin in direct contact to KBD-B when the latter binds to keratin (compare table 5).

The heavy atom coordinates of the rod of CK 8/18 are given in table 1 , their backbone is given in table 2, and the coordinates of the rod region immediately binding to KBD-B are given in table 4. A keratin rod model relying on these coordinates inasfar as they are backbone atom coordinates, or deviating from said backbone coordinates only insignificantly is encompassed by embodiment (9) of present invention. A keratin rod model is preferred whose backbone heavy atoms lie within a rmsd range of 0 to 3 A, especially of 0 to 2,5 A, on the corresponding heavy atom coordinates as indicated in table 2 for the rod domain of CK8/18. The correspondence between the amino acid sequence forming the relevant part of the rod domain of CK8/18 and other keratin amino acid sequences is established by Fig. 3 and Fig. 12. E.g., a rod domain formed by amino acids 90 to 404 of K35 (SEQ ID NO:58) and amino acids 116 to 430 of K85 (SEQ ID NO:62) and whose backbone heavy atoms are aligned along the backbone coordinates given in table 2 and do not deviate from them by more than 3 A, is an embodiment of present invention.

The heavy atom coordinates of the rod of K35/85 are given in table 3. A keratin rod model relying on these coordinates inasfar as they are backbone atom coordinates, or deviating from said backbone coordinates only insignificantly is encompassed by embodiment (9) of present invention. A keratin rod model is preferred whose backbone heavy atoms lie within a rmsd range of 0 to 3 A, especially of 0 to 2,5 A, on the corresponding heavy atom coordinates as indicated in table 3 for the rod domain of K35/85. The correspondence between the amino acid sequence forming the relevant part of the rod domain of K35/85 and other keratin amino acid sequences is established by Fig. 3 and Fig. 12.

Most preferably, the backbone coordinates of the keratin dimer used in the keratin model of present invention are the backbone coordinates as indicated in table 2, or the coordinates of the backbone atoms as indicated in table 3. Utmost preferred are the backbone coordinates as indicated in table 2.

In the keratin rod model of present invention, any keratin rod coiled coil may be established based on the backbone coordinates of CK8/18 given in table 2, preferably on the coordinates given in table 1 , and on the amino acid sequence of a keratin dimer of interest. The amino acid residues of the keratin dimer of interest can then be arranged on the backbone established in present invention, preferably by using the internal rotamer library (version 3) of program SCWRL (Dunbrack Jr. R. L. and Karplus M., 1993, J. MoI. Biol. 230, 543-574).

In a preferred aspect of the model according to embodiment (9), the amino acid sequences may comprise an amino acid sequence starting at any of the amino acids of the 6th heptad repeat forming rod segment 1 B and ending with any amino acid of the 10th heptad repeat forming rod segment 1 B, preferably an amino acid sequence starting at any of the amino acids of the 4th heptad repeat forming rod segment 1 B and ending with any amino acid of the 12th heptad repeat forming rod segment 1 B. A start at the fourth amino acid of the 4th heptad repeat and/or an end at the sixth amino acid of the 12th heptad repeat is preferred. In the keratin structure model according to embodiment (9) of present invention, the keratin heterodimer may be any keratin heterodimer with a heptad repeat segment, preferably a heptad repeat segment whose amino acid sequence differs not more than 5%, preferably not more than 15%, more preferably not more than 25% from amino acids G170 to V208 of CK8 and/or L159 to L197 of CK18 based on amino acid homology when compared in a multiple sequence alignment using Clustal W. Preferred heterodimers are selected from the group consisting of heterodimers comprising the heptad repeat segments of K32 (previously: hHa2)/82(hHb2), K35(hHa5)/82, K39/82, K40/82, K32/85(hHb5), K35/85, K39/85, K40/85, K5/14 and K1/10, more preferably the rod domains or the complete heterodimers of said group. Accordingly, the amino acid sequences representing the rod domain of each of these heterodimers may be used in the model. This is due to the fact that the amino acid sequences representing the rod domain in each keratin monomer, i.e. the four heptad repeat segments, resemble each other. Thus, as for the rod domain based on CK8/18 a backbone model is provided in present invention, said backbone model can be used as backbone for other keratins as well (example 3). The threedimensional model of any of said keratin heterodimers is an embodiment of embodiment (9) of present invention. However, in a preferred aspect, the keratin model according to present invention is a model of CK8/18.

In a further preferred aspect, the keratin structure model of embodiment (9) is a model of the complete rod domain of a hair or skin keratin, preferably of a keratin selected from the group consisting of CK8/18, K32/82, K35/82, K39/82, K40/82, K32/85, K35/85, K39/85, K40/85, K5/14 and K1/10.

More preferably, the keratin structure model is

(i) a model of the CK8/18 rod domain, whose atom coordinates are preferably the coordinates as indicated in table 1 or coordinates deviating therefrom by not more than an rmsd value in the range from 0 to 3 A, preferably from 0 to 2.5 A; or (ii) a model of the CK35/85 rod domain, whose atom coordinates are preferably the coordinates as indicated in table 3 or coordinates deviating therefrom by not more than an rmsd value in the range from 0 to 3 A, preferably from 0 to 2.5 A.

The final model of CK8/18 is given in Fig. 4, the atom coordinates for CK8/18 are provided in Tab. 1. Both are preferred aspects of the keratin model according to embodiment (9) of the invention.

The use (10) of the keratin structure model according to embodiment (9) for analysing the interaction between said keratin structure and a candidate molecule is a further embodiment of present invention. The model may be used for the identification of:

- keratin binding molecules, especially keratin binding polypeptides;

- keratin disturbing molecules; or

- keratin intercalating molecules. Keratin disturbing molecules disturb the structure of keratin, thus breaking the keratin barrier. Keratin intercalating molecules intercalate between the amino acid chains of keratin and remain there. Thus, they are an alternative to keratin-binding molecules and have similar application fields.

The molecules identified by the use (10) of the keratin model may be applicable in

- cosmetics;

- pharmaceutical treatments; and/or

- keratin treatment in vitro, especially treatment of leather and animal hair (preferably wool).

Preferred molecules identified by the use of the keratin model are suitable for targeted transport of molecules to or through keratin and keratin comprising structures.

In one preferred aspect, a keratin binding molecule identified by the use of embodiment (10) is suitable as carrier of an active ingredient or is an active ingredient itself.

In a second preferred aspect, a keratin disturbing molecule identified by the use of embodiment (10) improves the uptake of further compounds through the skin due to a break in the cytokeratin barrier. Said molecule is preferable over the generally used DMSO as keratin barrier breaker, as DMSO destroys the skin.

In a third preferred aspect, a molecule intercalating into keratin is used to achieve a long-time stay of an active ingredient linked to the intercalating molecule.

The keratin model of embodiment (9) can easily be adapted to model different keratins of hair and skin by exchange of amino acid residues along the keratin rod backbone. Therefore, the search for keratin binding molecules in the use (10) can be specifically adapted to the search for molecules binding only to specific keratins of hair or skin, having a specifity for hair versus skin keratins, or vice versa.

Preferred candidate molecules in the use (10) are selected from the group consisting of desmoplakin, keratin-associated proteins (KAPs), envoplakin, periplakin, epiplakin, plectin, desmoglein, plakophilin, desmocollin, plakoglobin, desmoyokin, and their homologues, derivatives or functional variants. The method of embodiment (1 1 ) for evaluating the interaction of a candidate molecule with keratin is a further embodiment of present invention. It comprises the following steps: (a) selecting a candidate molecule and a keratin;

(b) determining the interaction of the candidate molecule with the keratin structure model of embodiment (9) of the selected keratin by conducting a computer simulation of the interaction between said keratin structure model and a threedimensional model of the candidate molecule, wherein the spatial, lipophilic and electrostatic interaction between the candidate molecule and the keratin structure are determined.

The keratin in steps (a) and (b) is preferably a keratin dimer, more preferably the rod domain of a keratin dimer, most preferably a rod domain as detailed above in the context of embodiment (9).

Step (b) of the method according to embodiment (11 ) may be based on the initial rigidly docked keratin/candidate molecule complex (Hex program) followed by the HADDOCK approach including a molecular dynamics simulation. During the zipper-like dimerization step in an explicit water environment (SPC-water model), intermolecular atom-atom interactions may be calculated (GROMOS96) (Berendsen, HJC et al., in: Intermolecular forces, edited by B. Pullman, Reidel, Dordrecht, p.331 (1981 ); Berendsen, HJC et al., J. Phys. Chem. 91 :6269 (1987)).

The method of embodiment (11 ) may additionally comprise the following step: (c) analyzing the interaction of the candidate molecule with keratin in vitro or in vivo, preferably in vitro. Thus, in order to verify the results of the model, the binding of the real candidate molecule to the real keratin is tested, e.g. by incubation of the candidate molecule with hair or skin under test conditions like the conditions described in examples 8, 9 or 10.

The method of embodiment (11 ) may additionally also comprise the following step: (d) in vitro testing of the structural and functional properties of the candidate molecule, preferably in comparison to native KBD-B.

In step (c) and (d), the interaction testing and the in vitro testing of the structural or functional properties of the candidate molecule is preferably performed according to the instructions given above for each feature in the "definitions" and "detailed description" section.

In a preferred aspect of present invention, any of the method steps may be reiterated. A reiteration of step (b) is recommendable whenever there seems to be more than one site and/or orientation of interaction on one or both partners offering itself. A reiteration of at least steps (a) to (b), but preferably of steps (a) to (c) is recommendable when an initial candidate molecule is slightly modified in each reiteration cycle in order to test the effects of such modifications onto the properties to be improved and/or to optimize the fit of the candidate molecule to the keratin.

The method according to embodiment (11 ) is not only suitable for identification of molecules binding to keratin. An interaction with keratin may also be an intercalation of a molecule into keratin, on even a disturbance of the keratin structure which allows a passage of the candidate molecules or further compounds through a keratin barrier. Thus, in the method according to embodiment (11 ), the interaction may comprise a binding of the candidate molecule to the keratin surface, and/or an intercalation of the candidate molecule into the keratin structure, and/or a disturbance of the keratin structure by the candidate molecule. A keratin-binding is the preferred interaction.

Therefore, the use of the method according to embodiment (1 1 ) for identifying molecules which

(a) disturb the keratin structure and are suitable as keratin barrier breaker and/or carrier for a further compound through the barrier as described above; or (b) bind to or intercalate into the keratin structure and are suitable as described above in the context of embodiments (6) and (7) is a further embodiment of present invention.

The most preferred application of the method according to embodiment (11 ) and the keratin rod model according to embodiment (9) is their use for identification of keratin- binding polypeptides, especially of keratin-binding polypeptides derived from KBD-B, in the method according to embodiment (12), as described in the following sections.

The availability of the keratin model according to embodiment (9) led in turn to a threedimensional model of the interaction between KBD-B and keratin (in the following: interaction model), and to the identification of the interface between keratin and KBD-B and of the amino acids forming said interface. The establishment of said interaction model and the identification of said interface are a major achievement of present invention, as the conventional modelling techniques for identifying molecular interactions did not and could not lead to reasonable results in a reasonable timeframe for the interaction between KBD-B and keratin.

As indicated above in the "background" section, it is a difficult task to identify the amino acids at the interface between two proteins without reliable structural data. The prediction of protein -protein interaction via computer aided modeling is hampered by too many false positive results when using computer-based structural predictions. Thus, all predictions should be verified by experimental data (as it was done in present invention, compare examples 6 to 8). The finding of a correct interaction prediction is no easy achievement.

There is no modeling program available which would be able to calculate the geometry of the keratin-KBD-B complex and to locate it at a position along the 315 amino acid (45 nm) long keratin rod domain. The complex itself consists of more than 200 amino acids. This opens up an endless number of possible complex geometries. Moreover, conventional approaches based on force field interaction energies are biased by the omission of water molecule effects in such complexes.

Some of the key points to be considered in the prediction of protein-protein-interactions are:

- shape complementarities and possible conformational changes due to improved shape complementarities It is to be noted that real protein complexes feature a good shape potential in all cases, but that many false complex solutions reached by computer simulations share good shape potentials too. A good shape potential is at least 400 kJ/mol (Hex-Shape- Potential).

- lipophilic complementarities (e.g., Meyer EE et al., PNAS 2006 103:15739-15746; Efremov, RG et al., Current Medicinal Chemistry 2007 14(4):393)

-electrostatic complementarities and repulsions necessary to avoid close contact of same charged amino acid residues.

However, there are several other restrictions to bear in mind (expressly the restrictions mentioned in example 5). Therefore, the protein-protein interface is usually not obvious even if the amino acid sequence and the threedimensional structure of both proteins are available. The development of the interaction model according to embodiment (12) was moreover complicated by the initial lack of a threedimensional keratin rod model which had to be developed first.

As the shape of the keratin model according to embodiment (9) is uniform, the use of mere shape complementarities (Hex-shape) would not have led to the localization of the region of keratin binding to KBD-B. Thus, lipophilic and electrostatic complementarities were the main guides to the establishement of the interaction model between KBD-B and keratin. The hydrophobic effects which are responsible for threedimensional folding of proteins and of the geometry of protein-protein complexes are hard to quantify. A "hydrophobic effect" is the formation of clusters of hydrophobic amino acid residues or of hydrophobic interfaces between strucutural elements of same or different proteins in order to minimize water contact of said regions.

The main key to success in developing the interaction model was, however, visual inspection of several threedimensional models suggested by SYBYL, several cycles of manual rearrangement of amino acid side chain conformations in the model, and of energy minimization in Hex4.1 in order to arrange amino acid side chains.

In the context of present invention, it was also demonstrated that reasonable predictions about the effects of amino acid exchanges in the KBD-B amino acid sequence are possible using the interaction model according to embodiment (1 1 ) or (12). Several predictions on the outcome of diverse amino acid exchanges were checked by prepraration of the corresponding polypeptides and testing their stability and their keratin-binding properties in vitro (examples 6 to 8). Based on these results, the model according to embodiment (12) of the invention was used to predict amino acid exchanges leading to an improvement of structural and/or functional features of the KBD-B derived polypeptide, specifically the exchanges listed above for embodiments (1 ) and (2).

The method according to embodiment (11 ) or (12) is especially useful to identify keratin-binding polypeptides with improved properties in comparison to KBD-B. Said improved properties may be at least one improved functional and/or structural property selected from the group consisting of

- increased stability, - improved keratin-binding properties,

- increased load density,

- increased solubility,

- decreased dimer formation, and

- increased specifity for hair keratin in comparison to skin keratin or vice versa.

Said method according to embodiment (12) is applied for identification of keratin- binding polypetides with improved properties in comparison to KBD-B, and wherein the candidate molecule is a putative keratin-binding polypeptide, comprising the following steps: (a) selecting a putative keratin-binding polypeptide and a keratin;

(b) determining the shape complementarity in a complex of said putative keratin- binding polypeptide with the rod domain of said keratin by conducting a computer simulation of the threedimensional arrangement of (i) the candidate keratin-binding polypeptide and (ii) the rod domain of said keratin; (c) comparing the result to the result of the corresponding computer simulation of (i) native KBD-B and (ii) said keratin;

(d) determining whether the differences between the putative keratin-binding polypeptide and KBD-B established in the comparison step (c) may lead to to the desired improvement.

In the computer simulation, the rod domain is preferably represented by the keratin model of embodiment (9). The method of embodiment (12) may additionally comprise the following steps in order to verify the results of steps (b) to (d):

(e) synthesis of the keratin-binding polypeptide amino acid sequence of the putative keratin-binding polypeptide; and/or

(f) in vitro testing the structural and functional properties of the keratin-binding polypeptide amino acid sequence of the keratin-binding polypeptide selected in step (d), preferably in comparison to native KBD-B.

In step (f), the in vitro testing of the structural or functional properties to be improved is preferably performed according to the instructions given above for each feature in the "definitions" and "detailed description" section.

In a preferred aspect of present invention, any of the method steps may be reiterated. A reiteration of steps (b) and (c) is recommendable whenever there seems to be more than one site and/or orientation of interaction on one or both partners offering itself. A reiteration of at least steps (a) to (d), but preferably of steps (a) to (f) is recommendable when an initial polypeptide is slightly modified in each reiteration cycle in order to test the effects of such modifications onto the properties to be improved and/or to optimize the fit of the polypeptide to the keratin.

In one preferred embodiment of the method (12), the putative keratin-binding polypeptide is derived by at least one amino acid exchange from a native keratin- binding domain, preferably from native KBD-B. The method may therefore be modified as follows:

(a) changing at least one amino acid in the native amino acid sequence of KBD-B as represented by amino acids by amino acids 2250 to 2448 of SEQ ID NO:1 and selecting the resulting polypeptide as putative keratin-binding polypeptide;

(b) fitting the changed amino acid(s) into the existing threedimensional structure of KBD-B as described above, subsequently establishing its interaction with a threedimensional model of the keratin rod domain of choice, and finally determining the shape complementarity;

(c) comparing the result to the corresponding result for the same threedimensional arrangement of native KBD-B and the keratin rod domain of choice; (d) determining whether the differences between the putative keratin-binding polypeptide and KBD-B established in the comparison step (c) may lead to to the desired improvement.

Most preferably, the putative keratin-binding polypeptide comprises an amino acid sequence as defined above for the polypeptides according to embodiment (1 ) or (2) of the invention. Particularly, it consists of said amino acid sequence. The putative keratin-binding polypeptide may additionally comprise the amino acid sequences represented by amino acids 2193 to 2249 and 2457 to 2481 of SEQ ID NO:1 , or a fragment of two or more consecutive amino acids thereof, as sequences flanking the sequence of KBD-B as represented by amino acids 2250 to 2448 of SEQ ID NO:1.

On the other hand, the keratin rod domain to be used in the model is preferably a rod domain model as defined under embodiment (9) above, and does more preferably comprise the coiled coil segment as defined by the coordinates and/or amino acid numbers indicated in table 1 , 2 or 4. Most preferably, it comprises the segment as defined by the coordinates and/or amino acid numbers indicated in table 4. In a specifically preferred aspect, the keratin used in the method according to embodiment (12) is selected from the group consisting of CK8/18, K32/82, K35/82, K39/82, K40/82, K32/85, K35/85, K39/85, K40/85, K5/14 and K1/10. More preferably, the keratin in the model is

(i) a model of the CK8/18 rod domain, whose atom coordinates are preferably the coordinates as indicated in table 1 or coordinates deviating therefrom by not more than an rmsd value in the range from 0 to 3 A, preferably from 0 to 2.5 A; or (ii) a model of the CK35/85 rod domain, whose atom coordinates are preferably the coordinates as indicated in table 3 or coordinates deviating therefrom by not more than an rmsd value in the range from 0 to 3 A, preferably from 0 to 2.5 A.

Specifically preferred is the use of CK8/18 as defined by the coordinates given in table 1 as skin keratin in the method (12) and the use of K35/85 as defined by the coordinates given in table 3 as hair keratin in the method (12).

Most specifically preferred is the use of the interaction model of KBD-B and CK8/18 (KBD-B/CK8/18 complex) with the coordinates as indicated in table 4 in the method of embodiment (12). This complex may be modified in step (a) by introduction of one or more amino acids into the amino acid sequence of KBD-B and subsequent evaluation of the steric, lipophilic and/or electrostatic effects this introduction has onto the complex geometry and the interaction between polypeptide and keratin. It may thus be performed as follows:

(a) changing at least one amino acid in the native amino acid sequence of KBD-B as represented by amino acids 2250 to 2448 of SEQ ID NO:1 and selecting the resulting polypeptide as putative keratin-binding polypeptide;

(b) fitting the changed amino acid(s) into the existing threedimensional structure of KBD-B as defined by the interaction model with the KBD-B coordinates provided in table 4, subsequently establishing its interaction with the CK8/18 keratin rod domain with the coordinates provided in table 4, and finally adjusting the orientation of the changes amino acid residues;

(c) comparing the result to the initial complex formed by KBD-B and CK8/18; (d) determining the steric, lipophilic and/or electrostatic effects the amino acid exchange has onto the complex geometry and the interaction between polypeptide and keratin and determining whether the differences between the keratin-binding polypeptide derived from KBD-B and the native KBD-B may lead to to the desired improvement.

Most preferably, the putative keratin-binding polypeptide comprises an amino acid sequence as defined above for the polypeptides according to embodiment (1 ) or (2) of the invention. Particularly, it consists of said amino acid sequence.

The putative keratin-binding polypeptide may additionally comprise the amino acid sequences represented by amino acids 2193 to 2208 and 2457 to 2481 of SEQ ID NO:1 , or a fragment of two or more consecutive amino acids thereof, as sequences flanking the sequence of KBD-B as represented by amino acids by amino acids 2209 to 2448.

Depending on the desired improved properties, the method of embodiment (12) may be modified accordingly, preferably as follows:

When the improved property in comparison to KBD-B is an improved keratin-binding: (a) selecting a putative keratin-binding polypeptide and a keratin; (b) determining the shape complementarity in a complex of said putative keratin- binding polypeptide with the rod domain of said keratin by conducting a computer simulation of the threedimensional arrangement of (i) the candidate keratin-binding polypeptide and (ii) the rod domain of said keratin, and additionally determining the interaction energy of said complex; (c) comparing the resulting interaction energy to the resulting interaction energy of the corresponding computer simulation of (i) native KBD-B and (ii) said keratin; (d) determining whether the interaction energy with the putative keratin-binding polypeptide is equal or higher than the interaction energy with KBD-B. Optionally: (e) synthesis of the keratin-binding polypeptide amino acid sequence of the putative keratin-binding polypeptide; and/or

(f) in vitro testing the keratin binding of the keratin-binding polypeptide amino acid sequence of the putative keratin-binding polypeptide in comparison to native KBD-B, preferably in an assay described in examples 8 to 10.

In the computer simulation, the rod domain is preferably represented by the keratin model of embodiment (9).

The interaction energy may be determined by any molecular dynamics calculation or molecular dynamics program, e.g. by Gromacs3.3. The interaction energy of the keratin-binding polypeptide is preferably higher than the interaction energy of KBD-B with the keratin. In another preferred aspect, the interaction energy has preferably a value of at least 350 kJ/mol, more preferably of at least 400 kJ/mol, even more preferably of at least 600 kJ/mol.

When the improved property in comparison to KBD-B is an increased specificity for either hair or skin keratin:

(a) selecting a putative keratin-binding polypeptide and a hair keratin and a skin keratin; (b) determining the shape complementarity in a complex of said putative keratin- binding polypeptide with the rod domain of said keratins by conducting a computer simulation of the threedimensional arrangement of (i) the candidate keratin-binding polypeptide and (ii) the rod domain of the hair keratin and (iii) the rod domain of the skin keratin, and additionally determining the interaction energy of the putative keratin- binding polypeptide and of native KBD-B with each of said rod domains;

(c) calculating the difference between the interaction energy of said hair and said skin keratin with the candidate keratin-binding polypeptide and the native KBD-B, i.e. the difference between hair and skin binding; and/or calculating the difference between the interaction energy of the candidate keratin- binding polypeptide and the native KBD-B with either hair or skin keratin, i.e. the difference between native KBD-B and the candidate keratin-binding polypeptide for one kind of keratin:

(d) comparing the resulting relative interaction energies for the candidate keratin- binding polypeptide and native KBD-B with each other; and (e) determining whether the comparison result indicates an increased specifity for one kind of keratin, and whether the affinity of the candidate is changed (i.e. decreased or increased) in comparison to native KBD-B.

Optionally: (f) synthesis of the keratin-binding polypeptide amino acid sequence of the putative keratin-binding polypeptide; and/or

(g) in vitro testing the keratin binding of the keratin-binding polypeptide amino acid sequence of the putative keratin-binding polypeptide in comparison to native KBD-B, preferably in an assay described in examples 8 to 10.

In said method regarding selection of polypeptides with increased specifity for hair or skin keratin, the interaction energy for each complex is determined and compared in steps (b) and (c). When the interaction energy for hair or skin deviates from the corresponding value of KBD-B, this hints to a modified specifity of the tested polypeptide. In the computer simulation used in said method, the rod domain is preferably represented by the keratin model of embodiment (9) as described above.

To test in step (f) whether a polypeptide has an altered specificity in its hair and skin binding properties can be determined using the assays described in examples 8 and 10. The preferred poylpeptides are the same as described above in the context of "specifity". A polypeptide with increased specificity for skin would preferably lead to a increased or unaltered absorption in the skin binding assay whereas the signal in the hair binding assay would be lower. A polypeptide with increased specificity for hair would lead to a increased or unaltered absorption in the hair binding assay whereas the signal in the skin binding assay would be lower.

The present invention is described in more detail by reference to the following examples. It should be understood that these examples are for illustrative purposes only and are not to be construed as limiting the invention.

EXAMPLES

In the following examples, standard techniques of recombinant DNA technology and molecular biology were used that were described in various publications, e.g. Sabrook et al. (2001 ), Molecular Cloning: A Laboratory Manual, 3^rd edition, Cold Spring Harbor Laboratory Press, or Ausubel et al. (1997), Current Protocols in Molecular Biology, Current Protocols in Protein Science, edition as of 2002, Wiley Interscience. Unless otherwise indicated, all cells, antibodies, reagents, devices and kits were used according to the manufacturer^'s instructions.

The following known sequences, partial sequences and crystal structures were used for modelling purposes:

Keratin-binding domains of desmoplakin: native KBD-B amino acids S2209 to S2456 respectively 2448 of SEQ ID NO:1 (amino acids 2449 to 2456 were not resoluted in PDB1 lm7) PDB-code:1 lm7 (DOI 10.2210/pdb1 lm7/pdb) (SEQ ID NO:48) native KBD-C amino acids F2609 to A2822 of SEQ ID NO:1 PDB-code:1 lm5 (DOI 10.2210/pdb1 lm5/pdb) (SEQ ID NO:49)

Keratin and vimentin sequences: NP_998821.2|K39 CAH10353.1 |K40 NP_002269.3|K32 NP_002271.3|K35 P13645|K1C10_HUMAN P02533|K1C14_HUMAN P05783|K1C18_HUMAN P04264|K2C1_HUMAN P13647|K2C5_HUMAN P05787|K2C8_HUMAN NP_149022.3|K82 NP_002274.1 |K85 P08670|VIME_HUMAN

Cortexillin x-ray structure:

PDB-code:1 d7m (DOI 10.2210/pdb1 d7m/pdb) (SEQ ID NO:63)

1 d7m was used as three dimensional template for keratin models.

Source databases for sequences and structures:

PDB http://www.rcsb.org/pdb/home/home.do

CCDS http://www.ncbi.nlm.nih.gov/CCDS/CcdsBrowse.cgi

Human intermediate filament database http://www.interfil.org/index.php ExPASy http://expasy.org/

UniProt http://www.expasy.ch/uniprot/

NCBI Protein http://www.ncbi. nlm.nih.gov/sites/entrez?db=protein

Programs used for modeling: PROCHECK3.4

CLUSTAL W-Server 2005-2007 with BLOSUM62 matrix (sequence alignment)

GROMACSS.I-S.S/GROMOSΘΘ-force field (molecular dymnamics)

INSIGHT Il Version 2005 (loop search) (Accelrys)

Paircoil2 (coiled coil prediction) Sybyl 7.1-7.2.3 (backbone construction of keratin model) (Tripos Inc.)

SCWRL3.0 (side chain placement of amino acids)

Hex4.1

Haddock1.3

The term "keratin-binding domain" as used in the following examples pertains to the polypeptides according to embodiment (1 ) of present invention and to native keratin- binding domains, especially to full-length native KBD-B. The latter was tested as reference material for comparative studies of binding to keratin. The term "keratin-binding domain active ingredient" as used in the follwing examples designates either a keratin binding polypeptide, or a functional variant of a keratin- binding polypeptide consisting of (i) a keratin-binding polypeptide (first domain), (ii) an effector molecule as defined above which is not naturally linked to the polypeptide (i) (second domain).

Example 1 : Skin and hair keratins of interest

The target keratins of principal interest were the following keratins of skin and hair: - eight known dimers in the kuticula of human hair: K32(previously: hHa2)/82(hHb2), K35(hHa5)/82, K39/82, K40/82, K32/85(hHb5), K35/85, K39/85, K40/85; and - the prevalent dimers in keratinocytes of skin epidermis, K5/14 and K1/10. CK8/18 was selected as keratin model as it is bound by KBD-B.

Example 2: Homology model of keratin CK8/18 A homology model of keratin based on the fact that KBD-B binds to the rod segment of CK8/18 keratin and on the published partial structural data for small rod regions was constructed.

Because no x-ray data for the complete CK8/18 was available and 1d7m is a coiled coil structure, the backbone coordinates of the crystal structure of the coiled-coil rod segments of PDB 1d7m (Cortexillin I; SEQ ID NO:63) were used as a template.

Cortexillin I is an actin bundling protein of D. discoideum which forms a homodimer. In contrast to Cortexillin I, keratins are heterodimers. The alignment of both sequences according to the four Keratin ,,coiled coN"-segments resulted from sequence alignments (Clustal W) and Pair Coil Scoring using Paircoil 2.

The Cortexillin homodimer comprises 14 "heptad repeat" units. It is composed of amino acids 1 to 101 of SEQ ID NO:63 and is therefore shorter than the rod of CK8/18.

The Cortexillin template was therefore extended up to the necessary length and spatial expansion using SYBYL. The extension was based on a multiple repeat of the template backbone sequence designated as 1 d7m.

Coserved regions between Cortexillin I and CK 8/18 were identified by sequence alignment (ClustalW) of 1 d7m and CK8/18. Then, the motif known as "heptad repeat" was assigned to said alignment using the Pair Coil Scoring algorithm (Paircoil2). This resulted in an unambiguous assignment of the CK8/18 peptide sequence backbone to the final template (control: position of heptad repeats in Paircoil and sequence alignments with known keratin sequences).

Fig. 2 shows a summary of said segment alignment.

The Paircoil Score indicating the ,,coiled coil" probability for the rod of CK8 and CK18 is given in Fig. 5. The length of the four Keratin ,,coiled coir-segments with correct ,,heptad repeaf- pattern was constructed by the following procedure:

In order to identify the rod segments of CK8/18, the ,,heptad-repeat"-pattern assigned by Pair Coil Scoring Form was compared with literature data (Parry, D. A. and Steinert, P. M. (1999) Q Rev Biophys 32:99-187; http://www.interfil.org/aboutDB.php, The

Human Intermediate Filament Database, Centre for Molecular Medicine and the

Bioinformatics Institute Singapore, 2007; Conway, J. F. and Parry, D. A. D (1988)

International Journal of Biological Macromolecules 10:79-98; Strelkov, S. V. et al.

(2002) Embo J 21 :1255-66) and controlled visually. Start and end positions of the segments were suggested by the positions of the linkers. Even though, the rod borders could not be determined definitely and were therefore assigned broadly.

Rod sequences of CK8/18 which were finally used for the modelling experiments are given in Fig. 2.

Its rod consists of 315 amino acids of each single cytokeratin chain. The first segment 1A begins respectively ends with the fourth amino acid in a heptad repeat. 1A consists of CK8 (SEQ ID NO:51 ) amino acids 83 to 125 and CK18 (SEQ ID NO:50) amino acids

73 to 115. The following linker L1 consists of 10 amino acids each. The next segment

1 B begins respectively ends on a third position of a heptad repeat and consists of CK8 amino acids 136 to 236 and CK18 amino acids 126 to 226. The following linker L12 consists of 17 amino acids each. The next segment 2A, positions 254 to 272 (CK8) and

244 to 262 (CK18), begins on a third position and ends on a seventh position of a heptad repeat. The linker L2 consists of 8 amino acids each. Segment 2B consists of amino acids 281 to 397 (CK8) and 271 to 387 (CK18), beginning respectively ending on a fourth position of a heptad repeat. Said segment is interrupted by the "stutter" discontinuity of amino acids 341 to 344 (CK8) and 331 to 334 (CK18), whereupon the heptad repeats are continued, starting on a first position.

The backbone template of Cortexillin I was then modified according to the four predicted "coiled coN"-segments using SYBYL.

In more detail, the coiled coil of PDB 1d7m was either shortened or extended in order to fit the segment length of the CK8/18 segments, taking into account the heptad repeat positions. The resulting segment assignments for PDB 1 d7m were:

1 A: amino acids no. 2 to 44 of SEQ ID NO:63 (correspond to sequence positions 244 to 286 of PDB entry 1d7m)

1 B: amino acids no. 6 to 101 plus 4 to 8 of SEQ ID NO:63 (correspond to sequence positions 248 to 343 and 246 to 250 of PDB entry)

2A: amino acids no. 1 to 19 of SEQ ID NO:63 (correspond to sequence positions 243 to 261 of PDB entry)

2B: amino acids no. 2 to 61 of SEQ ID NO:63, followed by the ,,stutter" from PDB 1 gk4 (4 amino acids), followed by amino acids no. 13 to 65 of SEQ ID NO:63 (first and final part correspond to sequence positions 244 to 303 and 255 to 307 of PDB entry 1 d7m).

Then, the spatial structure of the ,,stutter" region (Strelkov, S.V. et al. (2002) Embo J. 21 :1255-1266) of CK8/18 was supplemented by using the crystal structure coordinates of 1 GK4 (Vimentin, SEQ ID NO:52). All segments were arranged axially resulting in the keratin backbone modell whose coordinates are given in table 2.

Finally sidechains according to the sequence of each segment were attached to the backbone model using the program SCWRL. Stereochemical parameters were checked and ensured by the program Procheck.

The final model of CK8/18 is given in Fig. 4, the atom coordinates are provided in Tab. 1.

Example 3: Homology model of further hair and skin keratins of interest The length and the heptad repeat starting positions of segments 1 A, 1 B, 2A and 2B of all hair and skin keratins of interest for present invention, i.e. the proposed binding targets of KBD-B, are with all probability identical. This is the result of multiple sequence alignments using ClustalW (Fig. 12). Thus, the backbone model of CK8/18 (Tab. 2) was used as a template for all further keratin models. The insertion of the amino acids residues and the model control were performed as described beforehand for CK8/18. The rod models of the following additional keratins were constructed: Skin: CK1/10, CK5/14 Hair: K32/82, K35/82, K32/85, K35/85 K39 and K40 are very similar to K35 and K32, respectively. Thus, the corresponding models were transformed tho K39 and K40 by direct amino acid exchange in K35 and K32 models, respectively.

Examplarily, the coordinates of K35/85 are given in table 3.

Example 4: Completion of the threedimensional structure of desmoplakin KBD-B

The known crystal structure of isolated KBD-B (PDB 1 lm7) is a homodimer consisting of the monomers A and B, both represented by SEQ ID NO:49 (i.e. amino acids 2209 to 2448 of SEQ ID NO:1 ). The atomic coordinates have been determined completely, except for the same "loop" in each monomer (Choi, HJ. et al. (2002) Nature Struct Biol 9:612-620). As a loop region was missing in both monomers, a "loop search routine" was performed for each monomer and the resulting loop was inserted. This loop is part of the N-terminus and is therefore not part of the immediate keratin-binding region (i.e. the interface). In more detail: PDB 11m7 was chosen as starting point for modeling the complete 3D structure of KBD-B. The regions missing in the structure given in PDB 1 lm7 were inserted using "loop search" module (Insight Il 2000) followed by a molecular dynamics simulation under physiological conditions (GROMACS) and a final steepest descent minimization. "Loop search" takes into account the known atom coordinates of 5 amino acids before and after the amino acids of interest and bases its calculations on the assumption that the backbone and residue positions of the lacking atoms resemble each other.

As the dimensions of the missing amino acids in each monomer were slightliy different, a separate arrangement of the loop-search routin in INSIGHT Il was made for each monomer and for the insertion of the accordant loop.

The location of amino acids E 2239, E2240 and 12241 was missing in monomer A.

Inserted was the extracted threedimensional structure of a corresponding region from

PDB 1ABZ (Fezoui, Y., Connolly, PJ. , Osterhout, JJ. (1997) Protein Sci. 6:1869-

1877). Five amino acids before and after the lacking amino acid positions were considered in the search. The sequence of the resulting inserted backbone coordinates was ALEARGTDSNAEL, wherein GTD corresponded to the lacking amino acids. The resulting root mean square deviation value (rmsd) was 0.42 A.

Monomer B lacked the stereoposition of amino acids E2240 and 12241. Inserted was a structure region from PDB 3CEQ. Five amino acids before and after the lacking amino acids were considered in the model. The sequence of the resulting inserted backbone coordinates was FINNKLISDAEL, wherein LI corresponded to the lacking amino acids.

The resulting rmsd value was 0.83 A.

Stereochemistry of the inserted regions was checked and ensured by PROCHECK, a program for checking the quality of protein models.

The resulting KBD-B model is shown in Fig. 1.

Example 5: Model of interaction between KBD-B and CK8/18 and determination of the interface

The interaction between KBD-B and CK8/18 was determined using the foiling programs: Sybyl7.1 for minimizations and manual 3D docking HEX, a "rigid protein -protein docking" program Grid for calculation of interaction fields GROMACS for simulation of molecular dynamics - HADDOCK, a protein-protein docking program

The following initial constraints were included into the model: consideration of specifically complementary surfaces consideration of lipophilic complementarity - consideration of electrostatic complementarity

F, W and Y are preferably located in the interface, as they are hydrophobic and may lead to an hydrophobic effect (Efremov, R. G. et al. (2007) Curr Med Chem

14:393-415) consideration of reasonable conformative changes leading to improved complementary surfaces (estimation)

- the p rote in -protein interaction energy is at least 400 kJ/mol (Hex-shape potential)

The last of these constraints led to the surprising result that in spite of the fact that isolated KBD-B forms a homodimer in solution and under crytallization conditions (Choi, HJ et al., Nat Struct Biol. 2002; 9:612-620), a KBD-B-monomer seemed to be sufficient for binding keratin, as the protein-protein interaction energy values for KBD-B dimers were below 300 kJ/mol in the hex-shape-potential.

Thus, KBD-B may bind as a monomer to keratin. This "monomer hypothesis" is supported by the finding that isolated KBD-B C, which binds to keratin as well, does also form a homodimer, but in a different constellation as KBD-B. Thus, it seems that neither KBD-B nor KBD-C form a functional interface by dimerisation, but rather bind to keratin via an interface formed by the monomer. Further support to the "monomer hypothesis" was found in an unpublished crystal structure of isolated KBD-B which had a geometry completely different from the published structure of the homodimer.

The "monomer hypothesis" was examined further by performing the amino acid exchange D2407A in vitro.

As indicated in the previous section, isolated KBD-B does form a homodimer during purification and crystallization (Choi, HJ et al., Nat Struct Biol. 2002; 9:612-620). In said homodimer, the amino acid residue D2407 of monomer A is surrounded by 2 R and one T of monomer B and vice versa. The resulting salt bridges are protected from solvent influences. Thus, the dimer is very stable and does even resist treatment with SDS. The salt bridges indicated in the previous section were suspected to support dimerization. Thus, the amino acid exchange D2407A was performed in order to prevent dimerization and to test the "monomer hypothesis" by establishing the binding properties, solubility, and association constant with keratin of the isolated D2407A polypeptide.

Method: The amino acid exchange D 2407A was achieved by site directed mutagenesis of the native KBD-B sequence (amino acids 2193 to 2481 of SEQ ID NO:1 ) in the expression vector pQE30 (Qiagen) (pQE30 KBD-B, SEQ ID NO:3). Mutations were introduced according to the manufacturer's protocol using the the QuikChange Site Directed Mutagenesis Kit (Stratagene). Table 6 lists the primers.

Tab. 6: Plasmids and primer sequences for site-directed mutagenesis D2407A.

The numbers refer to the position of the mutation in the human desmoplakin amino acid sequence (SEQ ID NO:1 ). The D2407A mutation was confirmed by sequence analysis. The pQE30 expression vector carrying mutant KBD-B D2407A was introduced into competent E. coli XL10 (Stratagene) according to the manufacturer's protocol.

Expression, purification and analysis of hair-binding properties of mutant KBD-B D2407A were done as described in examples 7B, 7C and 8, respectively. Dimer formation was analyzed by SDS-PAGE (NuPAGE BT Gel, Invitrogen) and by western- blotting using a 0,45 μM PVDF-membrane (Invitrolon) and a anti-His-Tag-antibody alkaline-phosphatase-conjugate at a dilution of 1/5000 in TTBS buffer (20 mM Tris-HCI pH 7,5; 150 mM NaCI; 0,05 % Tween20) with NBT/CIP (nitro blue tetrazolium/5-bromo- 4-chloro-3-indolyl phosphate) as chromogenic substrate.

Results: In summary no significant differences in hair binding properties and dimer formation between KBD-B and KBD-B D2407A could be observed.

The modified KBD-B D2407A displayed a keratin binding which was similar to the native KBD-B.

Thus, a binding of KBD-B to keratin via a monomer seems possible by the results achieved with KBD-B D2407A.

The comparison of KBD-B and KBD-C led to the following further specification of the constraints on the interaction model: the binding regions and binding mode of KBD-B and KBD-C are similar - the binding region of KBD-B must not include the N terminal region represented by amino acids 2209 to 2249 od SEQ ID NO:1 , as KBD-B and KBD-C both use a similar binding mode, but have different N-termini, and as KBD-C is able to bind to keratin without involving the N terminus - the binding region is not completely covering the N- or C-terminus of KBD-B, as these regions are followed by further amino acid sequences in vivo and are therefore sterically hindered

- the binding region of KBD-B (and KBD-C) is freely accessible in the homodimer, as the KBD-B homdimer is able to bind to keratin in vitro.

As these constraints did not lead to satisfactory results, we concluded that conformative changes of the isolated KBD-B must happen during the binding process in order to increase the shape complementarity and thus allow the KBD-B to host a coiled coil structure of keratin. The backbone of the coiled coil was considered to be unchangeable due to the stabilizing interactions in vivo.

A model was then developed based on this hypothesis using mainly visual inspection of threedimensional models established by SYBYL. In the model, the coiled coil is located in a V shaped cavity (compare Fig. 6). Where the two monomer chains forming the coiled coil are aligned on top of each other through the perpendicular of the KBD-B surface, the lower monomer chain fits into the cavity of KBD-B. Where the two monomer chains are aligned horizontally in relation to the KBD-B-surface, they are supported by a horizontal loop element of KBD-B.

Considerations based on this hypothesis finally resulted in a first model for which Hex gave an interaction energy 440 kJ/mol. After minimization of this first model using "steepest descent" in SYBYL (Burkert,U., and Allinger,N. L. Molecular Mechanics. ACS Monograph 177. American Chemical Society: Washington D. C. 1982), a second docking using Hex was performed. This routine was repeated several times, until the model whose coordinates are given in table 4 was found. The interaction energy was 660 kJ/mol for this complex (Hex). The final model differed from the first model in slight modifications of the conformation of amino acid side chains, resulting in closer proximity of KBD-B and keratin.

The resulting conformation of KBD-B, which can host different keratin coild coil structures by only small conformation changes, is given in Fig. 6.

The final interaction model coordinates and amino acids are provided in table 4.

The resulting KBD-B interface, i.e. the region facing the bound keratin, is defined by the following KBD-B amino acids: R2284, P2285, G2286, T2287, L2289, E2290, E2293, E2327, K2328, S2331 , R2334, Y2339, N2340, P2342, E2343, G2345, E2357, L2358, I2359 , E2360, G2362, H2363, R2366, D2410, D241 1 , K2413, G2414, F2416, E2421 , E2422 and N2423.

It is represented by the light-coloured region in Fig. 1.

The KBD-B interface area has a size of about 670 A², i.e. is considerably increased in comparison to the interface of the homodimer (400 A²; calculated by Sybyl). It extends about 45 A along the bound keratin.

The corresponding keratin-interface lies in segment 1 B of the "coiled-coil-rod" segment of keratin (Fig. 7). The binding region was narrowed down to amino acids G170 to V208 with respect to the amino acid sequence of CK8 (SEQ ID NO:51 ) (compare Figure 7). This region can be found in other homologuous keratin proteins as well, with more or less deviations in the respective amino acid sequences (Fig. 3). These differences can influence the binding strenght and account for differences between different kinds of keratin like skin and hair keratin.

Each complex of KBD-B and the corresponding keratin section shows differences in its geometry due to differences in the amino acid sequence of the keratin section.

Example 6: Modeling and predicted effects of amino acid exchanges in KBD-B leading to impairment of keratin-binding The effects of single and double amino acid exchanges in KBD-B on the 3D structure of the resulting keratin-binding polypeptide, and on the interactions between the keratin-binding polypeptide and keratin in the model of the KBD-B-keratin complex as described in example 5 were studied using molecular modeling and molecular dynamics.

The following exchanges in the interface of KBD-B were studied in silico and in vitro using the methods described in examples 5, 7 and 8. All these exchanges should lead to deterioration of keratin binding when the model of example 5 was correct:

a) F2416A

Prediction: decrease of interaction energy between KBD-B-mod. and keratin (Fig. 8).

Modelling Result: When modeled with CK8/18 as keratin in GROMACS, the F2416A KBD-B-mod. produces a decreased interaction energy (the sum of Coulomb potential and Lennard-Jones potential, which is a negative value, is higher than the sum for the native KBD-B) in comparison to native KBD-B (Fig. 8). This supports the prediction that F2416A should lead to impairment of keratin binding.

In vitro result: see Table 10

b) L2358E

Prediction: conversion of a lipophilic into a negatively charged field of molecular interaction between KBD-B-mod. and keratin. This leads to a high risk of misfolding, as L2358 is part of a lipophilic cluster.

In vitro result: see Table 10

c) Y2339A

Prediction: decrease of interaction energy between KBD-B-mod. and keratin. This lead to a high risk of misfolding, as Y2339 is part of the same lipophilic cluster as L2358.

In vitro result: see Table 10

d) K2328A/S2331A Prediction: conversion of a positively charged into a small lipophilic field of molecular interaction between KBD-B-mod. and keratin. Additionally, a putative hydrogen bond is prevented.

In vitro result: see Table 10

e) S2331A/R2334A

Prediction: conversion of a positively charged into a small lipophilic field of molecular interaction between KBD-B-mod. and keratin. Additionally, a putative hydrogen bond is prevented.

In vitro result: see Table 10

f) R2284D/G2286D

Prediction: conversion of a positively charged into a negatively charged field of molecular interaction between KBD-B-mod. and keratin. KBD-C possesses an A at the position homologuous to R2284. Additionally, G2286 introduces a negatively charged field of molecular interaction and a sterical barrier.

In vitro result: see Table 10

All amino acid exchange mutants which were not prone to proteolytic degeneration showed impaired binding properties. Thus, the predictions based on the model of example 5 were confirmed. All mutant amino acids were located in the keratin-binding interface of KBD-B (Fig. 9).

Example 7: Generation and isolation of KBD-B mutants

After in silico modeling the predicted interaction was analyzed by introducing selected mutations that would lead to weaker binding to keratin into the desmoplakin domain B. A weaker binding would argue that the selected amino acids are indeed involved in binding to keratin.

The artificial native KBD-B comprises the native keratin binding domain B of human desmoplakin (amino acids 2193 to 2481 of SEQ ID NO:1 ). The cloning and expression of native KBD-B using the expression vector pQE30 KBD-B are described in example 2 of WO 2005/1 15306, its purification in examples 5 to 7 of WO 2005/1 15306.

After introducing the mutations the corresponding mutant KBD-B variants were expressed in E. coli, purified and tested for their hair binding properties.

(A) Generation of mutant variants of KBD-B in pQE30-KBD

Mutant variants of KBD-B were generated by site directed mutagenesis of the native KBD-B sequence (amino acids 2193 to 2481 of SEQ ID NO:1 ) in the expression vector pQE30 (Qiagen) (pQE30 KBD-B, SEQ ID NO:3). Double mutations (table 2) and single mutations (table 1 ) were introduced according to the manufacturer's protocol using the QuikChange Multi Site Directed Mutagenesis Kit (Stratagene) and the QuikChange Site Directed Mutagenesis Kit (Stratagene), respectively. Table 7 and 8 list the primers.

Tab. 7: Plasmids and primer sequences for single mutations. Mutated bases are shown in upper case.

Tab. 8: Plasmids and primer sequences for double mutations. Mutated bases are shown in upper case.

The numbers refer to the positions of the mutations in the human desmoplakin amino acid sequence (SEQ ID NO:1 ). All mutations were confirmed by sequence analysis. The pQE30 expression vectors containing the mutant KBD-B variants were introduced into competent E. coliXLIO (Stratagene) according to the manufacturer's protocol.

(B) Expression of KBD-B and its mutant variants in E. coli XL10

Shake flasks containing 50 ml of EC3 medium (23 g/L FS 65% o.S., 15 g/L bacto tryptone, 30 g/L glycerol, 2 g/L potassium phosphate monobasic, 5 g/L ammonium sulfate, 1 g/L magnesium sulfate and 0,1 g/L magnesium chloride) were started from pre-cultures of E. coli XL10 carrying the plasmids shown in tables 7 and 8. Pre-cultures were inoculated from a single colony from plate and grown on the same media as the shake flask cultures. Shake flask cultures were started by diluting the pre-cultures into the shake flask cultures yielding an ODΘOOnm of ~ 0.5. Shake flask cultures were induced at an ODΘOOnm of ~ 1.5 by adding 1 mM IPTG. After 3 h shaking at 220 rpm and 32°C the bacteria were harvested by centrifugation.

(C) Purification of KBD-B and its mutant variants from E. coli XL10 shake flask cultures

After harvesting the shake flasks cultures, the supernatants were discarded and the cell pellets were resuspended in 10 mM sodium phosphate buffer, pH 7.4. Cell disruption was conducted by sonication (Sonifier 250, Branson) at 60% of maximum power and 3 pulses of 2 min on ice. Cell debris was removed by centrifugation and the cleared extract was loaded on a Ni-Sepharose high performance column (diameter 2.6 cm; height 5 cm; Amersham Biosciences) using the Akta Explorer FPLC system (Amersham Biosciences).

Before loading the column was equilibrated with 96% puffer A (10 mM sodium phosphate, pH 7.5) and 4 % buffer B (10 mM sodium phosphate pH 7.5 and 300 mM imidazol). The same buffer conditions were used to wash the column and to remove weakly bound proteins. Under these conditions tightly bound KBD-B remained bound by its His-tag to the Ni-Sepharose. Elution of KBD-B from the column was done in 100% buffer B using a fraction collector (elution profile see Fig. 10). Immediately after elution, the fractions containing each KBD-B variant were pooled and diluted into one volume of ice cold purified water. Subsequently, the pooled fractions were extensively dialysed against 10 mM sodium phosphate buffer, pH 7.5. Native KBD-B, KBD-BF2416A, KBD-B K2328AS2331A, KBD-B S2331A/R2334A and KBD-B R2284D/G2286D could be successfully expressed and purified. In contrast, KBD-B L2358E and KBD-B Y2339A were degraded indicating protein instability and pointing toward incorrect folding. Degradation of these mutant KBD-B variants was confirmed by western Blotting using a anti-His-tag antibody.

Example 8: Hair binding properties of native KBD-B and its mutant variants

To test whether the mutant KBD-B variants show altered binding affinities to human hair in comparison to native KBD-B, human hair was incubated with the purified native or mutant KBD-B variants. After washing away unbound KBD-B protein, tightly bound KBD-B protein was quantified using a chromogenic assay based on the detection of KBD-B by an anti-His-tag antibody conjugated to horse radish peroxidase. Horse radish peroxidase catalyzes the oxidation of the chromogenic substrate 3, 5, 3, '5' Tetramethylbenzidin (TMB) into a dye enabling the quantification of bound KBD-B protein by measuring the absorbance of the dye at 405 nm.

In detail, 5 mg of human hair was cut into pieces of 5 mm in length and washed with 1 ml of Ethanol. The hair was then incubated for one hour at room temperature with 1% bovine serum albumine in PBS (phosphate buffered saline) to block unspecific binding sites on hair. Next, the hair was incubated with 10 μg/ml of the KBD-B (i.e native or mutant KBD-B) in 1 ml of PBS containing 0,05% Tween 20 for 1 hour at room temperature. After removal of the supernatant the KBD-B treated hair was washed three times with PBS containing 0,05% Tween 20 to remove unbound KBD-B. As the next step, the hair was treated with 1 ml of anti-HisTag-antibody horse radish peroxidase conjugate (Monoclonal AntipolyHistidine Peroxidase Conjugate, produced in mouse, lyophilized powder, Sigma) at a dilution of 1/2000 in PBS containing 0,05% Tween 20. After washing the hair three times with PBS containing 0,05% Tween 20, the amount of bound KBD-B was quantified by adding 1 ml of peroxidase substrate (see below). After 90 sec the chromogenic reaction was stopped by adding 100 μl 2M H₂SO₄ and the absorbance at 405 nm was determined photometrically.

Peroxidase substrate (prepare shortly beforehand): 0.1 ml TMB solution (42 mM TMB in DMSO) + 10 ml of substrate buffer (0.1 M sodium acetate pH 4.9) + 14.7 μl H₂O₂ 3% strength

BSA = Bovine serum albumin

PBS = Phosphate buffered salt solution

Tween 20 = polyoxyethylene sorbitan monolaurate, n about 20

TMB = 3,5,3',5'-tetramethylbenzidine For testing the binding of native KBD-B in comparisin to non-keratin-binding proteins, YaaD from B. subtilis was chosen, which likewise had - as is necessary for this test - a His tag for the detection. A binding test on hair carried out for native KBD-B demonstrated considerable superiority of the binding of KBD-B to hair compared with significantly poorer binding of the comparison protein YaaD:

Table 9: Quantitative KBD activity test Hair: 1 ) buffer; 2) comparison protein YaaD; 3) KBD-B denatured; 4) KBD-B renatured. The table shows the measured absorption values at 405 nm.

The absorbance of the mutant KBD-B variants (KBD-B-mod.) was compared to the absorbance of the native KBD-B that was used as a reference and set to 100% (Table 10).

Tab.10: Binding of mutant KBD-B variants (KBD-B-mod.) to hair in comparison to native KBD-B.

All mutant KBD-B variants that could be successfully purified showed reduced affinity to human hair indicating that the mutated amino acids are involved in keratin binding and supporting the in silico model. For all amino acid exchanges in table 10, a decline of binding activity had been predicted in the in silico model of example 5.

This finding leads to the conclusion that the model for keratin binding by modified KBD- B established in example 5 leads to correct predictions on the consequences of amino acid exchanges in the KBD-B amino acid sequence. Example 9: Qualitative binding test to skin keratin

A visual qualitative test was developed in order to examine whether the tested keratin- binding domain binds to skin keratin.

Solutions used:

Blocking solution: DIG Wash + Buffer set 1585762 Boehringer MA (10 x solution) diluted in TBS.

TBS: 20 mM Tris; 150 mM NaCI pH 7.5 TTBS: TBS + 0.05% Tween20

The first step is the transfer of the outer keratin layer of the skin to a stable support. For this purpose, a transparent adhesive tape is firmly applied to depilated human skin and removed again. The test can be carried out directly on the transparent adhesive strip, or the adhering keratin layer can be transferred to a glass slide through renewed adhesion. Binding is demonstrated as follows:

For incubation with the various reagents, transfer to a Falcon vessel

If appropriate addition of ethanol for degreasing, removal of ethanol and drying of the slide - Incubation with blocking buffer for 1 h at room temperature

2x washing for 5 min with TTBS

1x washing for 5 min with TBS

Incubation with the KBD-B to be tested (coupled to tag - e.g. His₆, HA etc.) or control protein in TBS / 0.05% Tween 20 for 2-4 h at room temperature - Removal of the supernatant

3x washing with TBS

Incubation for 1 h at room temperature with monoclonal anti-polyhistidine (or specific KBD rabbit) antibodies, diluted 1 :2000 in TBS + 0.01 % blocking

2x washing for 5 min with TTBS - 1x washing for 5 min with TBS

Incubation for 1 h at room temperature with anti-mouse IgG alkaline-phosphatase conjugate, diluted 1 :5000 in TBS + 0.01% blocking

2x washing for 5 min with TTBS

1x washing for 5 min with TBS - Addition of phosphatase substrate (NBT-BCIP; Boehringer MA 1 tablet/40 ml of water 2.5 min; stop: with water)

Optical detection of the colored precipitate with the naked eye or using a microscope. A blue colored precipitate indicates that the tested keratin-binding domain has bound to the skin. Example 10: Quantitative binding test to skin keratin

A quantitative test was developed with which the skin binding strength of a keratin- binding domain can be compared with a reference KBD-B or nonspecific proteins. For background information see also Example 8.

A 5 mm cork borer was used to bore a section out of a thawed dry piece of skin without hair (human or pig). Alternatively, in the case of a surface test, a section of skin was inserted into a Falcon lid. The sample of skin was then brought to a thickness of 2- 3 mm in order to remove any tissue present. The skin sample was then transferred to an Eppendorf vessel (protein low-bind) in order to carry out the binding test as follows: 2 x washing with PBS / 0.05% Tween 20

Addition of 1 ml of 1 % BSA in PBS and incubation for 1 h at room temperature, gentle swirling movements (900 rpm). Removal of the supernatant - Addition of 100 μg of the tested keratin-binding domain in PBS with 0.05% Tween 20; incubation for 2 h at room temperature and gentle swirling movements (900 rpm).

Removal of the supernatant 3x washing with PBS / 0.05% Tween 20 - Incubation with 1 ml of monoclonal mouse anti-tag (His₆ or HA or specific KBD) antibodies with peroxidase conjugate (1 :2000 in PBS with 0.05% Tween 20) [Monoclonal AntipolyHistidine Peroxidase Conjugate, produced in mouse, lyophilized powder, Sigma] for 2-4 h at room temperature, gentle swirling movement (900 rpm) - 3x washing with PBS / 0.05% Tween 20

Addition of peroxidase substrate (1 ml / Eppendorf vessel; composition see below) Allow reaction to run until blue coloration (about 90 seconds). Stop the reaction with 100 μl of 2 M H₂SO₄. The absorption is measured at 405 nm.

Peroxidase substrate (prepare shortly beforehand): 0.1 ml TMB solution (42 mM TMB in DMSO) + 10 ml substrate buffer (0.1 M sodium acetate pH 4.9) + 14.7 μl H₂O₂ 3% strength

Example 10a: Coupling of a dye to a keratin-binding domain In order to couple a fluorescent dye (Alexa Fluor 532, Molecular Probes/lnvitrogen) to a keratin-binding domain, the dye was coupled via a maleic acid diimide linker to a cysteine thiol group by the following protocol. The reaction is depicted in Figure 8 of WO 2005/115306. 1 mg of Alexa Fluor 532 was dissolved in 150 μl of PBS buffer of pH 7.0; this was followed by brief centrifugation to remove any undissolved constituents 10 μl of dissolved dye were added to 100 μg of the keratin-binding domain (1 mg/ml) - The mixture was incubated covered with Al foil, on a shaker at 450 pm and at

24°C for 1 hour

10 μl of 1 MDTT were added to inactivate the maleic acid diimide function of unreacted Alexa Fluor 532

Incubation was then carried out at 450 pm and at 24°C (covered with Al foil) for 30 minutes

Coupling of KBD with coupled Alexa Fluor 532 to skin/hair can be determined by an activity test (see example 9 and 10). The KBD-Alexa Fluor 532 coupling which is bound to skin or hair in analogy to example 9 or 10 can be detected very easily on hair under the fluorescence microscope (detection with absorption: 532 nm/emission: 590 nm, see figure 11 ) or with the naked eye on bleached hair.

Example 1 1 : Use of the KBD in an emulsion for daycare - O/W type

Al 1%:

% Ingredient (INCI)

A 1.7 Ceteareth-6, Stearyl Alcohol

0.7 Ceteareth-25

2.0 Diethylamino Hydroxybenzoyl Hexyl Benzoate 2.0 PEG-14 Dimethicone

3.6 Cetearyl Alcohol

6.0 Ethylhexyl Methoxycinnamate

2.0 Dibutyl Adipate

B 5.0 Glycerin 0.2 Disodium EDTA

1.0 Panthenol q.s. Preservative

67.8 Aqua dem.

C 4.0 Caprylic/Capric Triglyceride, Sodium Acrylates Copolymer D 0.2 Sodium Ascorbyl Phosphate

1.0 Tocopheryl Acetate

0.2 Bisabolol

1.0 Caprylic/Capric Triglyceride, Sodium Ascorbate, Tocopherol, Retinol

1.0 Aqueous solution with about 5% keratin-binding domain active ingredient E q.s. Sodium Hydroxide

Al 5%: % Ingredient (INCI)

A 1.7 Ceteareth-6, Stearyl Alcohol

0.7 Ceteareth-25

2.0 Diethylamino Hydroxybenzoyl Hexyl Benzoate

2.0 PEG-14 Dimethicone

3.6 Cetearyl Alcohol

6.0 Ethylhexyl Methoxycinnamate

2.0 Dibutyl Adipate

B 5.0 Glycerin

0.2 Disodium EDTA

1.0 Panthenol q.s. Preservative

63.8 Aqua dem.

C 4.0 Caprylic/Capric Triglyceride, Sodium Acrylates Copolymer

D 0.2 Sodium Ascorbyl Phosphate

1.0 Tocopheryl Acetate

0.2 Bisabolol

1.0 Caprylic/Capric Triglyceride, Sodium Ascorbate, Tocopherol, Retinol

5.0 Aqueous solution with about 5% keratin-binding domain active ingredient

E q.s. Sodium Hydroxide

Preparation: Heat phases A and B separately from one another to about 80⁰C. Stir Phase B into phase A and homogenize. Stir phase C into the combined phases A and B and homogenize again. Cool with stirring to about 40⁰C, add phase D, adjust the pH to about 6.5 using phase E, homogenize and cool to room temperature with stirring.

Note: The formulation is prepared without protective gas. Bottling must take place into oxygen-impermeable packagings, e.g. aluminum tubes.

Example 12: Use of the KBD in a protective day cream - O/W type Al 1%:

% Ingredient (INCI)

A 1.7 Ceteareth-6, Stearyl Alcohol

0.7 Ceteareth-25

2.0 Diethylamino Hydroxybenzoyl Hexyl Benzoate

2.0 PEG-14 Dimethicone

3.6 Cetearyl Alcohol

6.0 Ethylhexyl Methoxycinnamate

2.0 Dibutyl Adipate B 5.0 Glycerin

0.2 Disodium EDTA

1.0 Panthenol q.s. Preservative

68.6 Aqua dem.

C 4.0 Caprylic/Capric Triglyceride, Sodium Acrylates Copolymer

D 1.0 Sodium Ascorbyl Phosphate

1.0 Tocopheryl Acetate

0.2 Bisabolol

1.0 Aqueous solution with about 5% keratin-binding domain active ingredient

E q.s. Sodium Hydroxide

Al 5%:

% Ingredient (INCI)

A 1.7 Ceteareth-6, Stearyl Alcohol

0.7 Ceteareth-25

2.0 Diethylamino Hydroxybenzoyl Hexyl Benzoate

2.0 PEG-14 Dimethicone

3.6 Cetearyl Alcohol

6.0 Ethylhexyl Methoxycinnamate

2.0 Dibutyl Adipate

B 5.0 Glycerin

0.2 Disodium EDTA

1.0 Panthenol q.s. Preservative

64.6 Aqua dem.

C 4.0 Caprylic/Capric Triglyceride, Sodium Acrylates Copolymer

D 1.0 Sodium Ascorbyl Phosphate

1.0 Tocopheryl Acetate

0.2 Bisabolol

5.0 Aqueous solution with about 5% keratin-binding domain active ingredient

E q.s. Sodium Hydroxide

Preparation: Heat phases A and B separately from one another to about 80⁰C. Stir phase B into phase A and homogenize. Incorporate phase C into the combined phases A and B and homogenize. Cool with stirring to about 40⁰C. Add phase D, adjust the pH to about 6.5 using phase E and homogenize. Cool to room temperature with stirring.

Example 13: Use of the KBD in a face-cleansing lotion - O/W type Al 1%:

% Ingredient (INCI) A 10.0 Cetearyl Ethylhexanoate 10.0 Caprylic/Capric Triglyceride

1.5 Cyclopentasiloxane, Cyclohexasiloxane 2.0 PEG-40 Hydrogenated Castor Oil B 3.5 Caprylic/Capric Triglyceride, Sodium Acrylates Copolymer

C 1.0 Tocopheryl Acetate

0.2 Bisabolol q.s. Preservative q.s. Perfume oil

D 3.0 Polyquaternium-44

0.5 Cocotrimonium Methosulfate

0.5 Ceteareth-25

2.0 Panthenol, Propylene Glycol 44..00 Propylene Glycol

0.1 Disodium EDTA

1.0 Aqueous solution with about 5% keratin-binding domain active ingredient 60.7 Aqua dem.

Al 5%:

% Ingredient (INCI)

A 10.0 Cetearyl Ethylhexanoate

10.0 Caprylic/Capric Triglyceride

1.5 Cyclopentasiloxane, Cyclohexasiloxane

2.0 PEG-40 Hydrogenated Castor Oil

B 3.5 Caprylic/Capric Triglyceride, Sodium Acrylates Copolymer

C 1.0 Tocopheryl Acetate

0.2 Bisabolol q.s. Preservative q.s. Perfume oil

D 3.0 Polyquaternium-44

0.5 Cocotrimonium Methosulfate

0.5 Ceteareth-25

2.0 Panthenol, Propylene Glycol

4.0 Propylene Glycol

0.1 Disodium EDTA

5.0 Aqueous solution with about 5% keratin-binding domain active ingredient

56.7 Aqua dem.

Preparation: Dissolve phase A. Stir phase B into phase A. Incorporate phase C into the combined phases A and B. Dissolve phase D, stir into the combined phases A, B and C and homogenize. After-stir for 15 min.

Example 14: Use of the KBD in a daily care body spray Al 1 %:

% Ingredient (INCI)

A 3.0 Ethylhexyl Methoxycinnamate

2.0 Diethylamino Hydroxybenzoyl Hexyl Benzoate 1.0 Polyquaternium-44

3.0 Propylene Glycol

2.0 Panthenol, Propylene Glycol

1.0 Cyclopentasiloxane, Cyclohexasiloxane

10.0 Octyldodecanol 0.5 PVP

10.0 Caprylic/Capric Triglyceride

3.0 C12-15 Alkyl Benzoate

3.0 Glycerin

1.0 Tocopheryl Acetate 0.3 Bisabolol

1.0 Aqueous solution with about 5% keratin-binding domain active ingredient

59.2 Alcohol

Al 5%:

% Ingredient (INCI)

A 3.0 Ethylhexyl Methoxycinnamate

2.0 Diethylamino Hydroxybenzoyl Hexyl Benzoate

1.0 Polyquaternium-44 3.0 Propylene Glycol

2.0 Panthenol, Propylene Glycol

1.0 Cyclopentasiloxane, Cyclohexasiloxane

10.0 Octyldodecanol

0.5 PVP 10.0 Caprylic/Capric Triglyceride

3.0 C12-15 Alkyl Benzoate

3.0 Glycerin

1.0 Tocopheryl Acetate

0.3 Bisabolol 5.0 Aqueous solution with about 5% keratin-binding domain active ingredient

55.2 Alcohol

Preparation: Weigh in the components of phase A and dissolve until clear.

Example 15: Use of the KBD in a skin care gel Al 1%: % Ingredient (INCI)

A 3.6 PEG-40 Hydrogenated Castor Oil

15.0 Alcohol

0.1 Bisabolol

0.5 Tocopheryl Acetate q.s. Perfume oil

B 3.0 Panthenol

0.6 Carbomer

1.0 Aqueous solution with about 5% keratin-binding domain active ingredient

75.4 Aqua dem.

C 0.8 Triethanolamine

Al 5 %:

% Ingredient (INCI)

A 3.6 PEG-40 Hydrogenated Castor Oil

15.0 Alcohol

0.1 Bisabolol

0.5 Tocopheryl Acetate q.s. Perfume oil

B 3.0 Panthenol

0.6 Carbomer

5.0 Aqueous solution with about 5% keratin-binding domain active ingredient

71.4 Aqua dem.

C 0.8 Triethanolamine

Preparation: Dissolve phase A until clear. Allow phase B to swell and neutralize with phase C. Stir phase A into the homogenized phase B and homogenize.

Example 16: Use of the KBD in an after shave lotion

Al 1%:

% Ingredient (INCI) A 10.0 Cetearyl Ethylhexanoate

5.0 Tocopheryl Acetate

1.0 Bisabolol

0.1 Perfume oil

0.3 Acrylates/C 10-30 Alkyl Acrylate Crosspolymer B 15.0 Alcohol

1.0 Panthenol

3.0 Glycerin 1.0 Aqueous solution with about 5% keratin-binding domain active ingredient

0.1 Triethanolamine 63.5 Aqua dem.

Al 5%:

% Ingredient (INCI) A 10.0 Cetearyl Ethylhexanoate

5.0 Tocopheryl Acetate 1.0 Bisabolol

0.1 Perfume oil

0.3 Acrylates/C 10-30 Alkyl Acrylate Crosspolymer B 15.0 Alcohol

1.0 Panthenol 3.0 Glycerin

5.0 Aqueous solution with about 5% keratin-binding domain active ingredient

0.1 Triethanolamine 59.5 Aqua dem.

Preparation: Mix the components of phase A. Dissolve phase B, incorporate into phase A and homogenize.

Example 17: Use of the KBD in an after sun lotion Al 1%:

% Ingredient (INCI)

A 0.4 Acrylates/C 10-30 Alkyl Acrylate Crosspolymer

15.0 Cetearyl Ethylhexanoate

0.2 Bisabolol 1.0 Tocopheryl Acetate q.s. Perfume oil

B 1.0 Panthenol

15.0 Alcohol

3.0 Glycerin 1.0 Aqueous solution with about 5% keratin-binding domain active ingredient

63.2 Aqua dem.

C 0.2 Triethanolamine

Al 5%:

% Ingredient (INCI) A 0.4 Acrylates/C 10-30 Alkyl Acrylate Crosspolymer 15.0 Cetearyl Ethylhexanoate

0.2 Bisabolol

1.0 Tocopheryl Acetate q.s. Perfume oil

B 1.0 Panthenol

15.0 Alcohol

3.0 Glycerin

5.0 Aqueous solution with about 5% keratin-binding domain active ingredient

59.2 Aqua dem.

C 0.2 Triethanolamine

Preparation: Mix the components of phase A. Stir phase B into phase A with homogenization. Neutralize with phase C and homogenize again.

Example 18: Use of the KBD in a sunscreen lotion Al 1%:

% Ingredient (INCI)

A 4.5 Ethylhexyl Methoxycinnamate 2.0 Diethylamino Hydroxybenzoyl Hexyl Benzoate

3.0 Octocrylene

2.5 Di-C12-13 Alkyl Malate

0.5 Tocopheryl Acetate

4.0 Polyglyceryl-3 Methyl Glucose Distearate B 3.5 Cetearyl lsononanoate

1.0 VP/Eicosene Copolymer

5.0 Isohexadecane

2.5 Di-CI 2-13 Alkyl Malate

3.0 Titanium Dioxide, Trimethoxycaprylylsilane C 5.0 Glycerin

1.0 Sodium Cetearyl Sulfate

0.5 Xanthan Gum

59.7 Aqua dem.

D 1.0 Aqueous solution with about 5% keratin-binding domain active ingredient

1.0 Phenoxyethanol, Methylparaben, Ethylparaben, Butylparaben, Propylparaben, lsobutylparaben

0.3 Bisabolol

Al 5%:

% Ingredient (INCI)

A 4.5 Ethylhexyl Methoxycinnamate 2.0 Diethylamino Hydroxybenzoyl Hexyl Benzoate

3.0 Octocrylene

2.5 Di-C12-13 Alkyl Malate

0.5 Tocopheryl Acetate

4.0 Polyglyceryl-3 Methyl Glucose Distearate

B 3.5 Cetearyl lsononanoate

1.0 VP/Eicosene Copolymer

5.0 Isohexadecane

2.5 Di-CI 2-13 Alkyl Malate

3.0 Titanium Dioxide, Trimethoxycaprylylsilane

C 5.0 Glycerin

1.0 Sodium Cetearyl Sulfate

0.5 Xanthan Gum

55.7 Aqua dem.

D 5.0 Aqueous solution with about 5% keratin-binding domain active ingredient

1.0 Phenoxyethanol, Methylparaben, Ethylparaben, Butylparaben, Propylparaben, lsobutylparaben

0.3 Bisabolol

Preparation: Heat the components of phases A and B separately from one another to about 80⁰C. Stir phase B into phase A and homogenize. Heat phase C to about 80⁰C and stir into the combined phases A and B with homogenization. Cool to about 40°C with stirring, add phase D and homogenize again.

Example 19: Use of the KBD in a sunscreen lotion - O/W type Al 1%:

% Ingredient (INCI)

A 2.0 Ceteareth-6, Stearyl Alcohol

2.0 Ceteareth-25

3.0 Tribehenin

2.0 Cetearyl Alcohol

2.0 Cetearyl Ethylhexanoate

5.0 Ethylhexyl Methoxycinnamate

1.0 Ethylhexyl Triazone

1.0 VP/Eicosene Copolymer

7.0 lsopropyl Myristate

B 5.0 Zinc Oxide, Triethoxycaprylylsilane

C 0.2 Xanthan Gum

0.5 Hydroxyethyl Acrylate/Sodium Acryloyldimethyl Taurate Copolymer,

Squalane, Polysorbate 60

0.2 Disodium EDTA 5.0 Propylene Glycol

0.5 Panthenol

60.9 Aqua dem.

D 1.0 Aqueous solution with about 5% keratin-binding domain active ingredient

0.5 Phenoxyethanol, Methylparaben, Butylparaben, Ethylparaben, Propylparaben, lsopropylparaben

1.0 Tocopheryl Acetate

0.2 Bisabolol

Al 5%:

% Ingredient (INCI)

A 2.0 Ceteareth-6, Stearyl Alcohol

2.0 Ceteareth-25

3.0 Tribehenin

2.0 Cetearyl Alcohol

2.0 Cetearyl Ethylhexanoate

5.0 Ethylhexyl Methoxycinnamate

1.0 Ethylhexyl Triazone

1.0 VP/Eicosene Copolymer

7.0 lsopropyl Myristate

B 5.0 Zinc Oxide, Triethoxycaprylylsilane

C 0.2 Xanthan Gum

0.5 Hydroxyethyl Acrylate/Sodium Acryloyldimethyl Taurate Copolymer,

Squalane, Polysorbate 60

0.2 Disodium EDTA

5.0 Propylene Glycol

0.5 Panthenol

56.9 Aqua dem.

D 5.0 Aqueous solution with about 5% keratin-binding domain active ingredient

0.5 Phenoxyethanol, Methylparaben, Butylparaben, Ethylparaben, Propyl paraben, lsopropylparaben

1.0 Tocopheryl Acetate

0.2 Bisabolol

Preparation: Heat phase A to about 80⁰C, stir in phase B and homogenize for 3 min. Likewise heat phase C to 80⁰C and stir into the combined phases A and B with homogenization. Cool to about 40°C, stir in phase D and homogenize again.

Example 20: Use of the KBD in a sunscreen lotion - O/W type Al 1%

% Ingredient (INCI)

A 3 .5 Ceteareth-6, Stearyl Alcohol

1 .5 Ceteareth-25 l_{Ill C C C C}NNNN

7 .5 Ethylhexyl Methoxycinnamate

.0 Diethylamino Hydroxybenzoyl Hexyl Benzoate

.0 Cyclopentasiloxane, Cyclohexasiloxane

0 .5 Beeswax

3 .0 Cetearyl Alcohol

10 .0 Caprylic/Capric Triglyceride

B 5 .0 Titanium Dioxide, Silica, Methicone, Alumina

C 3 .0 Glycerin

0 .2 Disodium EDTA

0 .3 Xanthan Gum

1 .0 Decyl Glucoside

.0 Panthenol, Propylene Glycol

56 .3 Aqua dem.

D 1 .0 Aqueous solution with about 5% keratin-binding domain active ingredient

1 .0 Tocopheryl Acetate

0 .2 Bisabolol q- S. Perfume oil q- S. Preservative

Al 5%

% Ingredient (INCI)

A 3 .5 Ceteareth-6, Stearyl Alcohol

1 .5 Ceteareth-25

7 .5 Ethylhexyl Methoxycinnamate

2 .0 Diethylamino Hydroxybenzoyl Hexyl Benzoate

2 .0 Cyclopentasiloxane, Cyclohexasiloxane

0 .5 Beeswax

3 .0 Cetearyl Alcohol

10 .0 Caprylic/Capric Triglyceride

B 5 .0 Titanium Dioxide, Silica, Methicone, Alumina

C 3 .0 Glycerin

0 .2 Disodium EDTA

0 .3 Xanthan Gum

1 .0 Decyl Glucoside

.0 Panthenol, Propylene Glycol

52 .3 Aqua dem.

D 5 .0 Aqueous solution with about 5% keratin-binding domain active ingredient

1.0 Tocopheryl Acetate

0.2 Bisabolol q.s. Perfume oil q.s. Preservative

Preparation: Heat phase A to about 80⁰C, stir in phase B and homogenize for 3 min. Likewise heat phase C to 80⁰C and stir into the combined phases A and B with homogenization. Cool to about 40⁰C, stir in phase D and homogenize again.

Example 21 : Use of the KBD in a foot balsam

Al 1%:

% Ingredient (INCI) A 2.0 Ceteareth-6, Stearyl Alcohol

2.0 Ceteareth-25

5.0 Cetearyl Ethylhexanoate

4.0 Cetyl Alcohol

4.0 Glyceryl Stearate

5.0 Mineral Oil

0.2 Menthol

0.5 Camphor

B 69.3 Aqua dem. q.s. Preservative C 1.0 Bisabolol

1.0 Tocopheryl Acetate D 1.0 Aqueous solution with about 5% keratin-binding domain active ingredient

5.0 Witch Hazel Extract

Al 5%

% Ingredient (INCI) A 2.0 Ceteareth-6, Stearyl Alcohol

2.0 Ceteareth-25

5.0 Cetearyl Ethylhexanoate

4.0 Cetyl Alcohol

4.0 Glyceryl Stearate

5.0 Mineral Oil

0.2 Menthol

0.5 Camphor

B 65.3 Aqua dem. q.s. Preservative C 1..0 Bisabolol

1. .0 Tocopheryl Acetate

D 5. .0 Aqueous solution with about 5% keratin-binding domain active ingredient

5. .0 Witch Hazel Extract

Preparation: Heat the components of phases A and B separately from one another to about 80⁰C. Stir phase B into phase A with homogenization. Cool to about 40⁰C with stirring, add phases C and D and briefly after-homogenize. Cool to room temperature with stirring.

Example 22: Use of the KBD in a VWO emulsion with bisabolol

Al 1%:

% Ingredient (INCI)

6.0 PEG-7 Hydrogenated Castor Oil

8.0 Cetearyl Ethylhexanoate

5.0 lsopropyl Myristate

15.0 Mineral Oil

0.3 Magnesium Stearate

0.3 Aluminum Stearate

2.0 PEG-45/Dodecyl Glycol Copolymer

B 5.0 Glycerin

0.7 Magnesium Sulfate

55.6 Aqua dem.

1.0 Aqueous solution with about 5% keratin-binding domain active ingredient

0.5 Tocopheryl Acetate

0.6 Bisabolol Al 5%:

% Ingredient (INCI)

6.0 PEG-7 Hydrogenated Castor Oil

8.0 Cetearyl Ethylhexanoate

5.0 lsopropyl Myristate

15.0 Mineral Oil

0.3 Magnesium Stearate

0.3 Aluminum Stearate

2.0 PEG-45/Dodecyl Glycol Copolymer

B 5.0 Glycerin

0.7 Magnesium Sulfate

51.6 Aqua dem.

5.0 Aqueous solution with about 5% keratin-binding domain active ingredient 0.5 Tocopheryl Acetate

Preparation: Heat phases A and B separately from one another to about 85°C. Stir phase B into phase A and homogenize. Cool to about 40⁰C with stirring, add phase C and briefly homogenize again. Cool to room temperature with stirring. List of formulations for patent keratin-binding domain - haircare

Example 23: Foam conditioner with setting agent

Al 1 %

% Ingredient (INCI)

A 10.0 PVPA/A Copolymer 0.2 Hydroxyethyl Cetyldimonium Phosphate

0.2 Ceteareth-25

0.5 Dimethicone Copolyol q.s. Perfume oil

10.0 Alcohol 1.0 Aqueous solution with about 5% keratin-binding domain active ingredient

68.1 Aqua dem. 10.0 Propane/Butane

Al 5% % Ingredient (INCI)

A 10.0 PVPA/A Copolymer

0.2 Hydroxyethyl Cetyldimonium Phosphate

0.2 Ceteareth-25 0.5 Dimethicone Copolyol q.s. Perfume oil

10.0 Alcohol

5.0 Aqueous solution with about 5% keratin-binding domain active ingredient

64.1 Aqua dem. 10.0 Propane/Butane

Preparation: Weigh the components of phase A together, stir until everything has dissolved and bottle.

Example 24: Foam conditioner

Al 1 % % Ingredient (INCI)

A 1 .0 Polyquaternium-4

0 .5 Hydroxyethyl Cetyldimonium Phosphate

1 .0 Aqueous solution with about 5% keratin-binding domain active ingredient q- S. Perfume oil q- S. Preservative

91 .5 Aqua dem.

6 .0 Propane/Butane

Al 5%

% Ingredient (INCI)

A 1 .0 Polyquaternium-4

0 .5 Hydroxyethyl Cetyldimonium Phosphate

5 .0 Aqueous solution with about 5% keratin-binding domain active ingredient q- S. Perfume oil q- S. Preservative

87 .5 Aqua dem.

6 .0 Propane/Butane

Preparation: Weigh the components of phase A together, stir until everything has dissolved to give a clear solution and bottle.

Example 25: Foam conditioner

Al 1 %

% Ingredient (INCI)

A 1.0 Polyquaternium-1 1

0.5 Hydroxyethyl Cetyldimonium Phosphate

1.0 Aqueous solution with about 5% keratin-binding domain active ingredient q.s. Perfume oil q.s. Preservative 91.5 Aqua dem.

6.0 Propane/Butane

Al 5%

% Ingredient (INCI)

A 1.0 Polyquaternium-1 1

0.5 Hydroxyethyl Cetyldimonium Phosphate 5.0 Aqueous solution with about 5% keratin-binding domain active ingredient q- S. Perfume oil q- S. Preservative

87 .5 Aqua dem.

6 .0 Propane/Butane

Preparation: Weigh the components of phase A together, stir until everything has dissolved to give a clear solution and bottle.

Example 26: Styling foam

Al 1 %

% Ingredient (INCI)

A 0 .5 Laureth-4 q- S. Perfume oil

B 77 .3 Aqua dem.

10 .0 Polyquaternium-28

1 .0 Aqueous solution with about 5% keratin-binding domain active ingredient

0 .5 Dimethicone Copolyol

0 .2 Ceteareth-25

0 .2 Panthenol

0 .1 PEG-25 PABA

0 .2 Hydroxyethylcellulose

10.0 HFC 152 A

Al 5%

% Ingredient (INCI)

0 .5 Laureth-4 q- S. Perfume oil

B 73 .3 Aqua dem.

10 .0 Polyquaternium-28

5 .0 Aqueous solution with about 5% keratin-binding domain active ingredient

0 .5 Dimethicone Copolyol

0 .2 Ceteareth-25

0 .2 Panthenol

0 .1 PEG-25 PABA 0.2 Hydroxyethylcellulose

C 10.0 HFC 152 A

Preparation: Mix the components of phase A. Add the components of phase B one after the other and dissolve. Bottle with phase C.

Example 27: Styling foam

Al 1 %

% Ingredient (INCI)

A 2.0 Cocotrimonium Methosulfate q.s. Perfume oil

B 78 .5 Aqua dem.

6 .7 Acrylates Copolymer

0 .6 AMP

1 .0 Aqueous solution with about 5% keratin-binding domain active ingredient

0 .5 Dimethicone Copolyol

0 .2 Ceteareth-25

0 .2 Panthenol

0 .1 PEG-25 PABA

0 .2 Hydroxyethylcellulose

C 10 .0 HFC 152 A

Al 5%

% Ingredient (INCI)

A 2 .0 Cocotrimonium Methosulfate q- S. Perfume oil

B 74.5 Aqua dem. 6.7 Acrylates Copolymer

0.6 AMP

5.0 Aqueous solution with about 5% keratin-binding domain active ingredient

0.5 Dimethicone Copolyol

0.2 Ceteareth-25 0.2 Panthenol

0.1 PEG-25 PABA 0.2 Hydroxyethylcellulose

C 10.0 HFC 152 A

Preparation: Mix the components of phase A. Add the components of phase B one after the other and dissolve. Bottle with phase C.

Example 28: Styling foam

Al 1 %

% Ingredient (INCI)

A 2,0 Cocotrimonium Methosulfate q.s. Perfume oil

B 7.70 Polyquaternium-44

1.0 Aqueous solution with about 5% keratin-binding domain active ingredient q.s. Preservative

79.3 Aqua dem.

C 10.0 Propane/Butane

Al 5%

% Ingredient (INCI)

A 2.0 Cocotrimonium Methosulfate q.s. Perfume oil

B 7.70 Polyquaternium-44 5.0 Aqueous solution with about 5% keratin-binding domain active ingredient q.s. Preservative

75.3 Aqua dem.

C 10.0 Propane/Butane

Preparation: Mix the components of phase A. Dissolve the components of phase B until clear, then stir phase B into phase A. Adjust the pH to 6-7, bottle with phase C.

Example 29: Styling foam Al 1 %

% Ingredient (INCI)

A 2.00 Cocotrimonium Methosulfate q.s. Perfume oil

B 72.32 Aqua dem.

2.00 VP/Acrylates/Lauryl Methacrylate Copolymer

0.53 AMP 1.00 Aqueous solution with about 5% keratin-binding domain active ingredient

0.20 Ceteareth-25

0.50 Panthenol

0.05 Benzophenone-4

0.20 Amodimethicone, Cetrimonium Chloride, Trideceth-12 15.00 Alcohol

C 0.20 Hydroxyethylcellulose

D 6.00 Propane/Butane

Al 5%

% Ingredient (INCI)

A 2.00 Cocotrimonium Methosulfate q.s. Perfume oil

B 68.32 Aqua dem.

2.00 VP/Acrylates/Lauryl Methacrylate Copolymer

0.53 AMP 5.00 Aqueous solution with about 5% keratin-binding domain active ingredient

0.20 Ceteareth-25

0.50 Panthenol

0.05 Benzophenone-4

0.20 Amodimethicone, Cetrimonium Chloride, Trideceth-12 15.00 Alcohol

C 0.20 Hydroxyethylcellulose

D 6.00 Propane/Butane

Preparation: Mix the components of phase A. Add the components of phase B one after the other and dissolve. Dissolve phase C in the mixture of A and B, then adjust the pH to 6-7. Bottle with phase D.

Example 30: Styling foam

Al 1 %

% Ingredient (INCI)

A 2.00 Cetrimonium Chloride q.s. Perfume oil

B 67.85 Aqua dem.

7.00 Polyquaternium-46

1.00 Aqueous solution with about 5% keratin-binding domain active ingredient

0.20 Ceteareth-25 0.50 Panthenol

0.05 Benzophenone-4

0.20 Amodimethicone, Cetrimonium Chloride, Trideceth-12

15.00 Alcohol

C 0.20 Hydroxyethylcellulose

D 6.00 Propane/Butane

Al 5% % Ingredient (INCI)

A 2.00 Cetrimonium Chloride q.s. Perfume oil

B 63.85 Aqua dem.

7.00 Polyquaternium-46

5.00 Aqueous solution with about 5% keratin-binding domain active ingredient

0.20 Ceteareth-25

0.50 Panthenol 0.05 Benzophenone-4

0.20 Amodimethicone, Cetrimonium Chloride, Trideceth-12

15.00 Alcohol

C 0.20 Hydroxyethylcellulose

D 6.00 Propane/Butane Preparation: Mix the components of phase A. Add the components of phase B one after the other and dissolve. Dissolve phase C in the mixture of A and B, then adjust the pH to 6-7. Bottle with phase D.

Example 31 : Styling foam

Al 1 %

% Ingredient (INCI)

A q.s. PEG-40 Hydrogenated Castor Oil q.s. Perfume oil 85.5 Aqua dem.

B 7.0 Sodium Polystyrene Sulfonate 1.0 Aqueous solution with about 5% keratin-binding domain active ingredient

0.5 Cetrimonium Bromide q.s. Preservative

C 6.0 Propane/Butane

Styling foam

Al 5%

% Ingredient (INCI)

A q.s. PEG-40 Hydrogenated Castor Oil q.s. Perfume oil

81.5 Aqua dem.

B 7.0 Sodium Polystyrene Sulfonate

5.0 Aqueous solution with about 5% keratin-binding domain active ingredient

0.5 Cetrimonium Bromide q.s. Preservative

C 6.0 Propane/Butane

Preparation: Solubilize phase A. Weigh phase B into phase A and dissolve until clear. Adjust the pH to 6-7, bottle with phase C.

Example 32: Styling foam Al 1 %

% Ingredient (INCI)

A q.s. PEG-40 Hydrogenated Castor Oil q.s. Perfume oil

92.0 Aqua dem.

B 0.5 Polyquaternium-10

1.0 Aqueous solution with about 5% keratin-binding domain active ingredient 0.5 Cetrimonium Bromide q.s. Preservative

C 6.0 Propane/Butane

Al 5% o %. Ingredient (INCI)

A q.s. PEG-40 Hydrogenated Castor Oil q.s. Perfume oil 88.0 Aqua dem.

B 0.5 Polyquaternium-10

5.0 Aqueous solution with about 5% keratin-binding domain active ingredient

0.5 Cetrimonium Bromide q.s. Preservative

C 6.0 Propane/Butane

Preparation: Solubilize phase A. Weigh phase B into phase A and dissolve until clear. Adjust the pH to 6-7, bottle with phase C.

Example 32: Styling foam

Al 1 % % Ingredient (INCI)

A q.s. PEG-40 Hydrogenated Castor Oil q.s. Perfume oil

82.5 Aqua dem.

B 10.0 Polyquaternium-16

1.0 Aqueous solution with about 5% keratin-binding domain active ingredient 0.5 Hydroxyethyl Cetyldimonium Phosphate q.s. Preservative

C 6.0 Propane/Butane

Al 5%

% Ingredient (INCI)

A q.s. PEG-40 Hydrogenated Castor Oil q.s. Perfume oil

78.5 Aqua dem.

B 10.0 Polyquaternium-16

5.0 Aqueous solution with about 5% keratin-binding domain active ingredient 0.5 Hydroxyethyl Cetyldimonium Phosphate q.s. Preservative

C 6.0 Propane/Butane

Preparation: Solubilize phase A. Weigh phase B into phase A and dissolve until clear.

Adjust the pH to 6-7, bottle with phase C.

Example 33: Styling foam

Al 1 %

% Ingredient (INCI)

A 2.0 Cocotrimonium Methosulfate q.s. Perfume oil

B 84.0 Aqua dem.

2.0 Chitosan

1.0 Aqueous solution with about 5% keratin-binding domain active ingredient

0.5 Dimethicone Copolyol 0.2 Ceteareth-25

0.2 Panthenol

0.1 PEG-25 PABA

C 10.0 HFC 152 A

Al 5%

% Ingredient (INCI) A 2.0 Cocotrimonium Methosulfate q- S. Perfume oil

B 80 .0 Aqua dem.

2 .0 Chitosan

5 .0 Aqueous solution with about 5% keratin-binding domain active ingredient

0 .5 Dimethicone Copolyol

0 .2 Ceteareth-25

0 .2 Panthenol

0 .1 PEG-25 PABA

C 10.0 HFC 152 A

Preparation: Mix the components of phase A. Add the components of phase B one after the other and dissolve. Bottle with phase C.

Example 34: Care shampoo

Al 1 %

O V,o Ingredient (INCI)

A 30.0 Sodium Laureth Sulfate

6.0 Sodium Cocoamphoacetate 6.0 Cocamidopropyl Betaine

3.0 Sodium Laureth Sulfate, Glycol Distearate, Cocamide MEA, Laureth-10

1.0 Aqueous solution with about 5% keratin-binding domain active ingredient

7.7 Polyquaternium-44

2.0 Amodimethicone q.s. Perfume oil q.s. Preservative

1.0 Sodium Chloride

43.3 Aqua dem.

B q.s. Citric Acid

Al 5%

O V,o Ingredient (INCI)

A 30.0 Sodium Laureth Sulfate

6.0 Sodium Cocoamphoacetate

6.0 Cocamidopropyl Betaine 3.0 Sodium Laureth Sulfate, Glycol Distearate, Cocamide MEA, Laureth-10

5.0 Aqueous solution with about 5% keratin-binding domain active ingredient

7.7 Polyquaternium-44

2.0 Amodimethicone q.s. Perfume oil q.s. Preservative

1.0 Sodium Chloride

39.3 Aqua dem.

B q.s. Citric Acid

Preparation: Mix the components of phase A and dissolve. Adjust the pH to 6-7 with citric acid.

Example 35: Shower gel

Al 1 %

% Ingredient (INCI)

A 40 .0 Sodium Laureth Sulfate

5 .0 Decyl Glucoside

5 .0 Cocamidopropyl Betaine

1 .0 Aqueous solution with about 5% keratin-binding domain active ingredient

1 .0 Panthenol q- S. Perfume oil q- S. Preservative

2 .0 Sodium Chloride

46 .0 Aqua dem.

B q.s. Citric Acid

Al 5%

% Ingredient (INCI)

A 40 .0 Sodium Laureth Sulfate

5 .0 Decyl Glucoside

5 .0 Cocamidopropyl Betaine

5 .0 Aqueous solution with about 5% keratin-binding domain active ingredient

1 .0 Panthenol q- S. Perfume oil q- S. Preservative

2 .0 Sodium Chloride 42.0 Aqua dem.

B q.s. Citric Acid

Preparation: Mix the components of phase A and dissolve. Adjust the pH to 6-7 with citric acid.

Example 36: Shampoo

Al 1 %

% Ingredient (INCI)

A 40.0 Sodium Laureth Sulfate

5.0 Sodium C12-15 Pareth-15 Sulfonate 5.0 Decyl Glucoside q.s. Perfume oil

0.1 Phytantriol

44.6 Aqua dem.

1.0 Aqueous solution with about 5% keratin-binding domain active ingredient 0.3 Polyquaternium-10

1.0 Panthenol q.s. Preservative

1.0 Laureth-3

2.0 Sodium Chloride

Al 5%

% Ingredient (INCI)

A 40.0 Sodium Laureth Sulfate 5.0 Sodium C12-15 Pareth-15 Sulfonate

5.0 Decyl Glucoside q.s. Perfume oil

0.1 Phytantriol

40.6 Aqua dem. 5.0 Aqueous solution with about 5% keratin-binding domain active ingredient

0.3 Polyquaternium-10

1.0 Panthenol q.s. Preservative

1.0 Laureth-3 2.0 Sodium Chloride Preparation: Mix the components of phase A and dissolve. Adjust the pH to 6-7 with citric acid.

Example 37: Shampoo

Al 1 %

% Ingredient (INCI)

A 15.00 Cocamidopropyl Betaine 10.00 Disodium Cocoamphodiacetate

5.00 Polysorbate 20

5.00 Decyl Glucoside q.s. Perfume oil q.s. Preservative 1.00 Aqueous solution with about 5% keratin-binding domain active ingredient

0.15 Guar Hydroxypropyltrimonium Chloride

2.00 Laureth-3

58.00 Aqua dem. q.s. Citric Acid

B 3.00 PEG-150 Distearate

Al 5%

% Ingredient (INCI)

A 15. 00 Cocamidopropyl Betaine

10. 00 Disodium Cocoamphodiacetate

5. 00 Polysorbate 20

5. 00 Decyl Glucoside q .S. Perfume oil q .S. Preservative

5. 00 Aqueous solution with about 5% keratin-binding domain active ingredient

0. 15 Guar Hydroxypropyltrimonium Chloride

2. 00 Laureth-3

54. 00 Aqua dem. q .S. Citric Acid

B 3.00 PEG-150 Distearate

Preparation: Weigh in the components of phase A and dissolve. Adjust the pH to 6-7. Add phase B and heat to about 50⁰C. Cool to room temperature with stirring. Example 38: Moisturizing bodycare cream

Al 1 %

% Ingredient (INCI)

A 2.0 Ceteareth-25

2.0 Ceteareth-6, Stearyl Alcohol

3.0 Cetearyl Ethylhexanoate

1.0 Dimethicone 4.0 Cetearyl Alcohol

3.0 Glyceryl Stearate SE

5.0 Mineral Oil

4.0 Simmondsia Chinensis (Jojoba) Seed Oil

3.0 Mineral Oil, Lanolin Alcohol

B 5.0 Propylene Glycol

1.0 Aqueous solution with about 5% keratin-binding domain active ingredient

1.0 Panthenol

0.5 Magnesium Aluminum Silicate q.s Preservative

65.5 Aqua dem.

C q.s. Perfume oil

D q.s. Citric Acid

Al 5%

% Ingredient (INCI)

A 2.0 Ceteareth-25

2.0 Ceteareth-6, Stearyl Alcohol

3.0 Cetearyl Ethylhexanoate

1.0 Dimethicone

4.0 Cetearyl Alcohol 3.0 Glyceryl Stearate SE

5.0 Mineral Oil

4.0 Simmondsia Chinensis (Jojoba) Seed Oil

3.0 Mineral Oil, Lanolin Alcohol

B 5.0 Propylene Glycol

5.0 Aqueous solution with about 5% keratin-binding domain active ingredient

1.0 Panthenol 0.5 Magnesium Aluminum Silicate q.s Preservative 61.5 Aqua dem.

C q.s. Perfume oil

D q.s. Citric Acid

Preparation: Heat phases A and B separately to about 80⁰C. Briefly prehomogenize phase B, then stir phase B into phase A and homogenize again. Cool to about 40⁰C, add phase C and homogenize thoroughly again. Adjust the pH to 6-7 with citric acid.

Example 39: Moisturizing bodycare cream

Al 1 %

% Ingredient (INCI)

A 6.0 PEG-7 Hydrogenated Castor Oil

10.0 Cetearyl Ethylhexanoate

5.0 lsopropyl Myristate

7.0 Mineral Oil

0.5 Shea Butter (Butyrospermum Parkii)

0.5 Aluminum Stearate

0.5 Magnesium Stearate

0.2 Bisabolol

0.7 Quaternium-18-Hectorite

B 5.0 Dipropylene Glycol

0.7 Magnesium Sulfate q.s. Preservative

62.9 Aqua dem.

C q.s. Perfume oil

1.0 Aqueous solution with about 5% keratin-binding domain active ingredient

Al 5%

% Ingredient (INCI)

A 6.0 PEG-7 Hydrogenated Castor Oil 10.0 Cetearyl Ethylhexanoate

5.0 lsopropyl Myristate

7.0 Mineral Oil 0.5 Shea Butter (Butyrospermum Parkii)

0.5 Aluminum Stearate

0.5 Magnesium Stearate

0.2 Bisabolol

0.7 Quaternium-18-Hectorite

B 5.0 Dipropylene Glycol

0.7 Magnesium Sulfate q.s. Preservative

58.9 Aqua dem.

C q.s. Perfume oil

5.0 Aαueous solution with about 5% ken

Preparation: Heat phases A and B separately to about 80⁰C. Stir phase B into phase A and homogenize. Cool to about 40⁰C with stirring, add phase C and homogenize again. Allow to cool to room temperature with stirring.

Example 40: Liquid Make-up - CvW type

Al ' 1 %

% Ingredient (INCI)

A 2.0 Ceteareth-6, Stearyl Alcohol

2.0 Ceteareth-25

6.0 Glyceryl Stearate

1.0 Cetyl Alcohol

8.0 Mineral Oil

7.0 Cetearyl Ethylhexanoate

0.2 Dimethicone

B 3.0 Propylene Glycol

1.0 Panthenol q.s. Preservative

61.9 Aqua dem.

C 0.1 Bisabolol

1.0 Aqueous solution with about q.s. Perfume oil D 5.7 C. I. 77 891 , Titanium Dioxide

1.1 Iron Oxides

Al 5%

% Ingredient (INCI)

A 2.0 Ceteareth-6, Stearyl Alcohol

2.0 Ceteareth-25

6.0 Glyceryl Stearate

1.0 Cetyl Alcohol

8.0 Mineral Oil

7.0 Cetearyl Ethylhexanoate

0.2 Dimethicone

B 3.0 Propylene Glycol

1.0 Panthenol q.s. Preservative

57.9 Aqua dem.

C 0.1 Bisabolol

5.0 Aqueous solution with about 5% q.s. Perfume oil

D 5.7 C. I. 77 891 , Titanium Dioxide

1.1 Iron Oxides

Preparation: Heat phases A and B separately to about 80⁰C. Stir phase B into phase A and homogenize. Cool to about 40⁰C with stirring, add phases C and D and thoroughly homogenize again. Allow to cool to room temperature with stirring.

Example 41

The active ingredient employed in the following exemplary formulations was a 5% by weight aqueous solution of a keratin-binding domain active ingredient as defined above (i.e. a keratin-binding domain with or without an effector molecule). The following data are parts by weight.

Clear shampoo

Clear conditioner shampoo

Foam O/W emulsions

Conditioner Shampoo with pearlescence

adjust pH to 6.0

Clear conditioner shampoo

OW sunscreen formulation

Hydrodispersion

Sticks

PIT emulsion

Gel cream

Self-tanning hydrodispersion

After-sun hydrodispersion

WO emulsions

Sticks

Self-tanning PIT emulsions

Oil gel

1

Caprylic/Capric Triglyceride 12.00 10.00 6.00

Octyldodecanol 7.00 14.00 8.00 3.00

Butylene Glycol 12.00 Dicaprylate/Dicaprate

Pentaerythrityl Tetraisostearate 10.00 6.00 8.00 7.00

Polyglyceryl-3 Diisostearate 2.50

Bis-Diglyceryl Polyacyladipate-2 9.00 8.00 10.00 8.00

Myristyl Myristate 3.50 3.00 4.00 3.00

Benaufne-34 5.00 5.00 6.00 6.00

Propylene Carbonate 15.00 20.00 18.00 19.50

Aqueous solution with keratin- 1.0 0.5 3.0 5.0 binding domain active ingredient

Vitamin E Acetate 0.50 1.00

Ascorbyl Palmitate 0.05 0.05

Example 42: lipophilic candidosis emulsion (hypothetic)

100.000 IE Nystatin per g 55 % (w/w) basic cream DAC 15 % paraffin wax 5 % propylen glycol

25 % aqueous solution with about 4 % keratin-binding-domain-Nystatin- conjugate active ingredient equal to 10 E7 IE of Nystatin

Tables 1 to 4:

Tab 1 :

(Legend in brackets)

HEADER K18K8 (Chain A: K18; Chain B: K8)

COMPND K18K8

REMARK GENERATED BY SYBYL (TRIPOS, INC.) 10-MAR-08

(SEQRES 1-4 A 43: chain lines 1-4 listing 43 amino acid residues of chain A, namely segment 1A):

SEQRES I A 43 GLY MET GLY GLY ILE GLN ASN GLU LYS GLU THR MET GLN

SEQRES 2 A 43 SER LEU ASN ASP ARG LEU ALA SER TYR LEU ASP ARG VAL

SEQRES 3 A 43 ARG SER LEU GLU THR GLU ASN ARG ARG LEU GLU SER LYS

SEQRES 4 A 43 ILE ARG GLU HIS

(SEQRES 1-8 A 101 : chain lines 1-8 listing 101 amino acid residues of chain A, namely segment 1B):

SEQRES 101 TRP SER HIS TYR PHE LYS ILE ILE GLU ASP LEU ARG ALA SEQRES 101 GLN ILE PHE ALA ASN THR VAL ASP ASN ALA ARG ILE VAL SEQRES 101 LEU GLN ILE ASP ASN ALA ARG LEU ALA ALA ASP ASP PHE SEQRES 101 ARG VAL LYS TYR GLU THR GLU LEU ALA MET ARG GLN SER SEQRES 101 VAL GLU ASN ASP ILE HIS GLY LEU ARG LYS VAL ILE ASP SEQRES 101 ASP THR ASN ILE THR ARG LEU GLN LEU GLU THR GLU ILE SEQRES 101 GLU ALA LEU LYS GLU GLU LEU LEU PHE MET LYS LYS ASN SEQRES 101 HIS GLU GLU GLU VAL LYS GLY LEU GLN ALA

(chain A, segment 2A):

SEQRES 19 ASP LEU ALA LYS ILE MET ALA ASP ILE ARG ALA GLN TYR SEQRES 19 ASP GLU LEU ALA ARG LYS (chain A, segment 2B):

SEQRES 117 TRP SER GLN GLN ILE GLU GLU SER THR THR VAL VAL THR SEQRES 117 THR GLN SER ALA GLU VAL GLY ALA ALA GLU THR THR LEU SEQRES 117 THR GLU LEU ARG ARG THR VAL GLN SER LEU GLU ILE ASP SEQRES 4 A 117 LEU ASP SER MET ARG ASN LEU LYS ALA SER LEU GLU ASN SEQRES 5 A 117 SER LEU ARG GLU VAL GLU ALA ARG TYR ALA LEU GLN MET SEQRES 6 A 117 GLU GLN LEU ASN GLY ILE LEU LEU HIS LEU GLU SER GLU SEQRES 7 A 117 LEU ALA GLN THR ARG ALA GLU GLY GLN ARG GLN ALA GLN SEQRES 8 A 117 GLU TYR GLU ALA LEU LEU ASN ILE LYS VAL LYS LEU GLU SEQRES 9 A 117 ALA GLU ILE ALA THR TYR ARG ARG LEU LEU GLU ASP GLY (analogously: chain B, segments 1A to 2B):

SEQRES 1 B 43 ILE GLN ALA VAL ARG THR GLN GLU LYS GLU GLN ILE LYS

SEQRES 2 B 43 THR LEU ASN ASN LYS PHE ALA SER PHE ILE ASP LYS VAL

SEQRES 3 B 43 ARG PHE LEU GLU GLN GLN ASN LYS MET LEU GLU THR LYS

SEQRES 4 B 43 TRP SER LEU LEU

SEQRES 1 B 101 ASP ASN MET PHE GLU SER TYR ILE ASN ASN LEU ARG ARG

SEQRES B 101 GLN LEU GLU THR LEU GLY GLN GLU LYS LEU LYS LEU GLU

SEQRES 3 B 101 ALA GLU LEU GLY ASN MET GLN GLY LEU VAL GLU ASP PHE

SEQRES 4 B 101 LYS ASN LYS TYR GLU ASP GLU ILE ASN LYS ARG THR GLU

SEQRES 5 B 101 MET GLU ASN GLU PHE VAL LEU ILE LYS LYS ASP VAL ASP

SEQRES 6 B 101 GLU ALA TYR MET ASN LYS VAL GLU LEU GLU SER ARG LEU

SEQRES 7 B 101 GLU GLY LEU THR ASP GLU ILE ASN PHE LEU ARG GLN LEU

SEQRES 8 B 101 TYR GLU GLU GLU ILE ARG GLU LEU GLN SER

SEQRES 1 B 19 ASP MET ASP SER ILE ILE ALA GLU VAL LYS ALA GLN TYR

SEQRES B 19 GLU ASP ILE ALA ASN ARG

SEQRES 1 B 117 TYR GLN ILE LYS TYR GLU GLU LEU GLN SER LEU ALA GLY

SEQRES 2 B 117 LYS HIS GLY ASP ASP LEU ARG ARG THR LYS THR GLU ILE

SEQRES 3 B 117 SER GLU MET ASN ARG ASN ILE SER ARG LEU GLN ALA GLU

SEQRES 4 B 117 ILE GLU GLY LEU LYS GLY GLN ARG ALA SER LEU GLU ALA

SEQRES 5 B 117 ALA ILE ALA ASP ALA GLU GLN ARG GLY GLU LEU ALA ILE

SEQRES 6 B 117 LYS ASP ALA ASN ALA LYS LEU SER GLU LEU GLU ALA ALA

SEQRES 7 B 117 LEU GLN ARG ALA LYS GLN ASP MET ALA ARG GLN LEU ARG

SEQRES 8 B 117 GLU TYR GLN GLU LEU MET ASN VAL LYS LEU ALA LEU ASP

SEQRES 9 B 117 ILE GLU ILE ALA THR TYR ARG LYS LEU LEU GLU GLY GLU

(Coordinate Section:

The essential informations are provided in columns 1 to 54. In columns 7 to 11, to each atom in the complete protein a unique number is assigned. In columns 13 to 16, the IUPAC atom symbol and - if necessary - an additional identifier for its position in the respective amino acid are given. However, this identifier is only unequivocal in relation to said amino acid. As a protein generally comprises several identical amino acids, not even the amino acid name in comlumns 18 to 20 is sufficient for unequivocal identification of the atom. This identification is possible only by the amino acid number in columns 23 to 26, which provides the position of the amino acid in the amino acid sequence underlying the model (e.g. G73 of SEQ ID NO:50 for K18). In column 22, the chain (A or B) is indicated which comprises the atom. The spatial coordinates of the atoms are given in columns 31 to 54. The content of columns 57 and higher have no relevance.)

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ATOM 1 N GLY A 73 181.483 42.993 -33.125 1.00 0.00

ATOM 9 CA GLY A 73 180.788 42.153 -32.160 1.00 0.00

ATOM 3 C GLY A 73 179.956 43.012 -31.246 1.00 0.00

ATOM 4 O GLY A 73 178.904 42.580 -30.804 1.00 0.00

ATOM 5 N MET A 74 180.442 44.241 -30.977 1.00 0.00

ATOM 6 CA MET A 74 179.704 45.149 -30.115 1.00 0.00

ATOM 7 C MET A 74 178.381 45.506 -30.732 1.00 0.00

ATOM 8 O MET A 74 177.362 45.365 -30.077 1.00 0.00

ATOM 9 CB MET A 74 180.495 46.440 -29.893 1.00 0.00

ATOM 10 CG MET A 74 181.744 46.263 -29.045 1.00 0.00

ATOM 11 SD MET A 74 182.719 47.775 -28.917 1.00 0.00

ATOM 12 CE MET A 74 181.628 48.797 -27.930 1.00 0.00

ATOM 13 N GLY A 75 178.404 45.960 -32.003 1.00 0.00

ATOM 14 CA GLY A 75 177.156 46.312 -32.662 1.00 0.00

ATOM 15 C GLY A 75 176.182 45.168 -32.610 1.00 0.00

ATOM 16 O GLY A 75 175.022 45.387 -32.301 1.00 0.00

ATOM 17 N GLY A 76 176.665 43.941 -32.890 1.00 0.00

ATOM 18 CA GLY A 76 175.785 42.788 -32.813 1.00 0.00

ATOM 19 C GLY A 76 175.189 42.660 -31.437 1.00 0.00

ATOM 20 O GLY A 76 173.979 42.561 -31.313 1.00 0.00

ATOM 21 N ILE A 77 176.063 42.671 -30.410 1.00 0.00

ATOM 22 CA ILE A 77 175.604 42.522 -29.037 1.00 0.00

ATOM 23 C ILE A 77 174.515 43.504 -28.694 1.00 0.00

ATOM 24 O ILE A 77 173.519 43.113 -28.108 1.00 0.00

ATOM 25 CB ILE A 77 176.750 42.747 -28.033 1.00 0.00

ATOM 26 CGl ILE A 77 177.780 41.622 -28.137 1.00 0.00

ATOM 27 CG2 ILE A 77 176.211 42.777 -26.610 1.00 0.00

ATOM 28 CDl ILE A 77 179.066 41.899 -27.389 1.00 0.00

ATOM 29 N GLN A 78 174.714 44.784 -29.069 1.00 0.00

ATOM 30 CA GLN A 78 173.713 45.787 -28.748 1.00 0.00

ATOM 31 C GLN A 78 172.412 45.502 -29.448 1.00 0.00

ATOM 32 O GLN A 78 171.363 45.684 -28.850 1.00 0.00

ATOM 33 CB GLN A 78 174.188 47.176 -29.179 1.00 0.00

ATOM 34 CG GLN A 78 175.326 47.731 -28.339 1.00 0.00

ATOM 35 CD GLN A 78 175.847 49.054 -28.863 1.00 0.00

ATOM 36 OEl GLN A 78 175.418 49.527 -29.916 1.00 0.00

ATOM 37 NE2 GLN A 78 176.775 49.656 -28.129 1.00 0.00

ATOM 38 N ASN A 79 172.484 45.043 -30.713 1.00 0.00

ATOM 39 CA ASN A 79 171.261 44.740 -31.440 1.00 0.00

ATOM 40 C ASN A 79 170.467 43.678 -30.731 1.00 0.00

ATOM 41 O ASN A 79 169.269 43.842 -30.553 1.00 0.00

ATOM 42 CB ASN A 79 171.585 44.236 -32.848 1.00 0.00

ATOM 43 CG ASN A 79 172.075 45.341 -33.763 1.00 0.00

ATOM 44 ODl ASN A 79 171.853 46.523 -33.500 1.00 0.00

ATOM 45 ND2 ASN A 79 172.744 44.959 -34.845 1.00 0.00

ATOM 46 N GLU A 80 171.144 42.587 -30.323 1.00 0.00

ATOM 47 CA GLU A 80 170.432 41.499 -29.670 1.00 0.00

ATOM 48 C GLU A 80 169.898 41.912 -28.327 1.00 0.00

ATOM 49 O GLU A 80 168.806 41.493 -27.979 1.00 0.00

ATOM 50 CB GLU A 80 171.363 40.303 -29.455 1.00 0.00

ATOM 51 CG GLU A 80 171.756 39.584 -30.735 1.00 0.00

ATOM 52 CD GLU A 80 172.772 38.485 -30.498 1.00 0.00

ATOM 53 OEl GLU A 80 173.224 38.333 -29.344 1.00 0.00

ATOM 54 OE2 GLU A 80 173.118 37.776 -31.467 1.00 0.00

ATOM 55 N LYS A 81 170.659 42.728 -27.570 1.00 0.00

ATOM 56 CA LYS A 81 170.180 43.122 -26.256 1.00 0.00

ATOM 57 C LYS A 81 168.914 43.926 -26.373 1.00 0.00

ATOM 58 O LYS A 81 167.981 43.676 -25.627 1.00 0.00

ATOM 59 CB LYS A 81 171.228 43.975 -25.538 1.00 0.00

ATOM 60 CG LYS A 81 170.828 44.396 -24.132 1.00 0.00

ATOM 61 CD LYS A 81 171.943 45.171 -23.449 1.00 0.00

ATOM 62 CE LYS A 81 171.533 45.616 -22.056 1.00 0.00

ATOM 63 NZ LYS A 81 172.612 46.390 -21.380 1.00 0.00 ATOM 64 N GLU A 82 168.878 44.883 -27.322 1.00 0.00

ATOM 65 CA GLU A 82 167.667 45.667 -27.497 1.00 0.00

ATOM 66 C GLU A 82 166.517 44.778 -27.877 1.00 0.00

ATOM 67 O GLU A 82 165.441 44.920 -27.319 1.00 0.00

ATOM 68 CB GLU A 82 167.859 46.710 -28.600 1.00 0.00

ATOM 69 CG GLU A 82 168.797 47.845 -28.225 1.00 0.00

ATOM 70 CD GLU A 82 169.060 48.790 -29.381 1.00 0.00

ATOM 71 OEl GLU A 82 168.567 48.517 -30.495 1.00 0.00

ATOM 72 OE2 GLU A 82 169.758 49.805 -29.172 1.00 0.00

ATOM 73 N THR A 83 166.761 43.848 -28.822 1.00 0.00

ATOM 74 CA THR A 83 165.713 42.915 -29.205 1.00 0.00

ATOM 75 C THR A 83 165.224 42.161 -27.999 1.00 0.00

ATOM 76 O THR A 83 164.028 41.986 -27.843 1.00 0.00

ATOM 77 CB THR A 83 166.220 41.890 -30.237 1.00 0.00

ATOM 78 OGl THR A 83 166.633 42.571 -31.428 1.00 0.00

ATOM 79 CG2 THR A 83 165.119 40.902 -30.590 1.00 0.00

ATOM 80 N MET A 84 166.168 41.726 -27.138 1.00 0.00

ATOM 81 CA MET A 84 165.775 40.978 -25.956 1.00 0.00

ATOM 82 C MET A 84 164.922 41.806 -25.039 1.00 0.00

ATOM 83 O MET A 84 163.928 41.302 -24.539 1.00 0.00

ATOM 84 CB MET A 84 167.009 40.527 -25.172 1.00 0.00

ATOM 85 CG MET A 84 167.829 39.453 -25.868 1.00 0.00

ATOM 86 SD MET A 84 169.325 39.023 -24.961 1.00 0.00

ATOM 87 CE MET A 84 168.629 38.203 -23.528 1.00 0.00

ATOM 88 N GLN A 85 165.307 43.081 -24.825 1.00 0.00

ATOM 89 CA GLN A 85 164.510 43.944 -23.968 1.00 0.00

ATOM 90 C GLN A 85 163.089 43.990 -24.459 1.00 0.00

ATOM 91 O GLN A 85 162.175 43.827 -23.667 1.00 0.00

ATOM 92 CB GLN A 85 165.072 45.367 -23.968 1.00 0.00

ATOM 93 CG GLN A 85 166.399 45.510 -23.240 1.00 0.00

ATOM 94 CD GLN A 85 166.991 46.899 -23.374 1.00 0.00

ATOM 95 OEl GLN A 85 166.449 47.750 -24.080 1.00 0.00

ATOM 96 NE2 GLN A 85 168.107 47.134 -22.693 1.00 0.00

ATOM 97 N SER A 86 162.918 44.199 -25.780 1.00 0.00

ATOM 98 CA SER A 86 161.574 44.253 -26.333 1.00 0.00

ATOM 99 C SER A 86 160.833 42.964 -26.099 1.00 0.00

ATOM 100 O SER A 86 159.657 43.009 -25.780 1.00 0.00

ATOM 101 CB SER A 86 161.625 44.500 -27.843 1.00 0.00

ATOM 102 OG SER A 86 162.149 45.785 -28.131 1.00 0.00

ATOM 103 N LEU A 87 161.523 41.814 -26.247 1.00 0.00

ATOM 104 CA LEU A 87 160.847 40.547 -26.020 1.00 0.00

ATOM 105 C LEU A 87 160.408 40.433 -24.586 1.00 0.00

ATOM 106 O LEU A 87 159.280 40.045 -24.335 1.00 0.00

ATOM 107 CB LEU A 87 161.781 39.377 -26.334 1.00 0.00

ATOM 108 CG LEU A 87 162.123 39.160 -27.810 1.00 0.00

ATOM 109 CDl LEU A 87 163.201 38.097 -27.960 1.00 0.00

ATOM 110 CD2 LEU A 87 160.896 38.706 -28.584 1.00 0.00

ATOM 111 N ASN A 88 161.307 40.786 -23.644 1.00 0.00

ATOM 112 CA ASN A 88 160.962 40.677 -22.236 1.00 0.00

ATOM 113 C ASN A 88 159.769 41.518 -21.883 1.00 0.00

ATOM 114 O ASN A 88 158.910 41.054 -21.150 1.00 0.00

ATOM 115 CB ASN A 88 162.131 41.137 -21.362 1.00 0.00

ATOM 116 CG ASN A 88 163.274 40.143 -21.346 1.00 0.00

ATOM 117 ODl ASN A 88 163.093 38.968 -21.667 1.00 0.00

ATOM 118 ND2 ASN A 88 164.459 40.611 -20.972 1.00 0.00

ATOM 119 N ASP A 89 159.709 42.755 -22.418 1.00 0.00

ATOM 120 CA ASP A 89 158.561 43.603 -22.133 1.00 0.00

ATOM 121 C ASP A 89 157.313 42.967 -22.670 1.00 0.00

ATOM 122 O ASP A 89 156.318 42.910 -21.965 1.00 0.00

ATOM 123 CB ASP A 89 158.735 44.975 -22.787 1.00 0.00

ATOM 124 CG ASP A 89 159.779 45.825 -22.090 1.00 0.00

ATOM 125 ODl ASP A 89 160.194 45.457 -20.972 1.00 0.00

ATOM 126 OD2 ASP A 89 160.181 46.861 -22.662 1.00 0.00

ATOM 127 N ARG A 90 157.385 42.478 -23.926 1.00 0.00

ATOM 128 CA ARG A 90 156.240 41.794 -24.503 1.00 0.00

ATOM 129 C ARG A 90 155.799 40.691 -23.580 1.00 0.00

ATOM 130 O ARG A 90 154.622 40.587 -23.275 1.00 0.00

ATOM 131 CB ARG A 90 156.605 41.190 -25.861 1.00 0.00 ATOM 132 CG ARG A 90 156.805 42.217 -26.963 1.00 0.00

ATOM 133 CD ARG A 90 157.222 41.555 -28.266 1.00 0.00

ATOM 134 NE ARG A 90 157.464 42.533 -29.324 1.00 0.00

ATOM 135 CZ ARG A 90 157.952 42.231 -30.524 1.00 0.00

ATOM 136 NHl ARG A 90 158.138 43.188 -31.423 1.00 0.00

ATOM 137 NH2 ARG A 90 158.252 40.974 -30.820 1.00 0.00

ATOM 138 N LEU A 91 156.780 39.883 -23.136 1.00 0.00

ATOM 139 CA LEU A 91 156.490 38.752 -22.270 1.00 0.00

ATOM 140 C LEU A 91 155.730 39.148 -21.033 1.00 0.00

ATOM 141 O LEU A 91 154.663 38.606 -20.794 1.00 0.00

ATOM 142 CB LEU A 91 157.787 38.082 -21.811 1.00 0.00

ATOM 143 CG LEU A 91 157.636 36.895 -20.857 1.00 0.00

ATOM 144 CDl LEU A 91 156.885 35.756 -21.529 1.00 0.00

ATOM 145 CD2 LEU A 91 158.999 36.376 -20.425 1.00 0.00

ATOM 146 N ALA A 92 156.294 40.089 -20.248 1.00 0.00

ATOM 147 CA ALA A 92 155.635 40.501 -19.019 1.00 0.00

ATOM 148 C ALA A 92 154.222 40.926 -19.309 1.00 0.00

ATOM 149 O ALA A 92 153.307 40.490 -18.629 1.00 0.00

ATOM 150 CB ALA A 92 156.375 41.669 -18.385 1.00 0.00

ATOM 151 N SER A 93 154.067 41.772 -20.346 1.00 0.00

ATOM 152 CA SER A 93 152.743 42.241 -20.711 1.00 0.00

ATOM 153 C SER A 93 151.799 41.102 -20.986 1.00 0.00

ATOM 154 O SER A 93 150.752 41.040 -20.362 1.00 0.00

ATOM 155 CB SER A 93 152.810 43.106 -21.971 1.00 0.00

ATOM 156 OG SER A 93 153.516 44.309 -21.728 1.00 0.00

ATOM 157 N TYR A 94 152.175 40.202 -21.920 1.00 0.00

ATOM 158 CA TYR A 94 151.297 39.089 -22.256 1.00 0.00

ATOM 159 C TYR A 94 150.924 38.287 -21.040 1.00 0.00

ATOM 160 O TYR A 94 149.792 37.837 -20.945 1.00 0.00

ATOM 161 CB TYR A 94 151.983 38.146 -23.245 1.00 0.00

ATOM 162 CG TYR A 94 152.060 38.686 -24.655 1.00 0.00

ATOM 163 CDl TYR A 94 153.257 39.169 -25.168 1.00 0.00

ATOM 164 CD2 TYR A 94 150.935 38.712 -25.469 1.00 0.00

ATOM 165 CEl TYR A 94 153.336 39.666 -26.456 1.00 0.00

ATOM 166 CE2 TYR A 94 150.995 39.204 -26.758 1.00 0.00

ATOM 167 CZ TYR A 94 152.210 39.683 -27.248 1.00 0.00

ATOM 168 OH TYR A 94 152.286 40.177 -28.530 1.00 0.00

ATOM 169 N LEU A 95 151.882 38.114 -20.108 1.00 0.00

ATOM 170 CA LEU A 95 151.610 37.328 -18.915 1.00 0.00

ATOM 171 C LEU A 95 150.571 37.998 -18.060 1.00 0.00

ATOM 172 O LEU A 95 149.669 37.336 -17.575 1.00 0.00

ATOM 173 CB LEU A 95 152.883 37.162 -18.081 1.00 0.00

ATOM 174 CG LEU A 95 153.978 36.282 -18.685 1.00 0.00

ATOM 175 CDl LEU A 95 155.245 36.348 -17.844 1.00 0.00

ATOM 176 CD2 LEU A 95 153.527 34.831 -18.751 1.00 0.00

ATOM 177 N ASP A 96 150.711 39.327 -17.888 1.00 0.00

ATOM 178 CA ASP A 96 149.742 40.056 -17.089 1.00 0.00

ATOM 179 C ASP A 96 148.387 39.976 -17.734 1.00 0.00

ATOM 180 O ASP A 96 147.415 39.675 -17.059 1.00 0.00

ATOM 181 CB ASP A 96 150.144 41.528 -16.970 1.00 0.00

ATOM 182 CG ASP A 96 151.338 41.732 -16.058 1.00 0.00

ATOM 183 ODl ASP A 96 151.705 40.781 -15.337 1.00 0.00

ATOM 184 OD2 ASP A 96 151.908 42.844 -16.066 1.00 0.00

ATOM 185 N ARG A 97 148.338 40.238 -19.057 1.00 0.00

ATOM 186 CA ARG A 97 147.075 40.168 -19.775 1.00 0.00

ATOM 187 C ARG A 97 146.427 38.824 -19.588 1.00 0.00

ATOM 188 O ARG A 97 145.236 38.761 -19.331 1.00 0.00

ATOM 189 CB ARG A 97 147.297 40.389 -21.272 1.00 0.00

ATOM 190 CG ARG A 97 147.675 41.814 -21.641 1.00 0.00

ATOM 191 CD ARG A 97 147.925 41.951 -23.134 1.00 0.00

ATOM 192 NE ARG A 97 148.337 43.304 -23.499 1.00 0.00

ATOM 193 CZ ARG A 97 148.672 43.678 -24.729 1.00 0.00

ATOM 194 NHl ARG A 97 149.033 44.932 -24.966 1.00 0.00

ATOM 195 NH2 ARG A 97 148.643 42.797 -25.720 1.00 0.00

ATOM 196 N VAL A 98 147.230 37.751 -19.719 1.00 0.00

ATOM 197 CA VAL A 98 146.679 36.412 -19.591 1.00 0.00

ATOM 198 C VAL A 98 146.153 36.166 -18.205 1.00 0.00

ATOM 199 O VAL A 98 145.137 35.502 -18.070 1.00 0.00 ATOM 200 CB VAL A 98 147.741 35.334 -19.879 1.00 0.00

ATOM 201 CGl VAL A 98 147.202 33.953 -19.547 1.00 0.00

ATOM 202 CG2 VAL A 98 148.138 35.356 -21.347 1.00 0.00

ATOM 203 N ARG A 99 146.836 36.708 -17.175 1.00 0.00

ATOM 204 CA ARG A 99 146.341 36.519 -15.822 1.00 0.00

ATOM 205 C ARG A 99 144.964 37.111 -15.711 1.00 0.00

ATOM 206 O ARG A 99 144.062 36.451 -15.220 1.00 0.00

ATOM 207 CB ARG A 99 147.264 37.207 -14.813 1.00 0.00

ATOM 208 CG ARG A 99 148.613 36.529 -14.644 1.00 0.00

ATOM 209 CD ARG A 99 149.494 37.289 -13.665 1.00 0.00

ATOM 210 NE ARG A 99 150.813 36.678 -13.528 1.00 0.00

ATOM 211 CZ ARG A 99 151.793 37.174 -12.779 1.00 0.00

ATOM 212 NHl ARG A 99 152.960 36.550 -12.715 1.00 0.00

ATOM 213 NH2 ARG A 99 151.601 38.295 -12.095 1.00 0.00

ATOM 214 N SER A 100 144.815 38.362 -16.189 1.00 0.00

ATOM 215 CA SER A 100 143.513 39.003 -16.134 1.00 0.00

ATOM 216 C SER A 100 142.474 38.188 -16.857 1.00 0.00

ATOM 217 O SER A 100 141.420 37.941 -16.293 1.00 0.00

ATOM 218 CB SER A 100 143.569 40.387 -16.786 1.00 0.00

ATOM 219 OG SER A 100 144.386 41.269 -16.039 1.00 0.00

ATOM 220 N LEU A 101 142.771 37.769 -18.104 1.00 0.00

ATOM 221 CA LEU A 101 141.774 37.043 -18.874 1.00 0.00

ATOM 999 C LEU A 101 141.381 35.739 -18.241 1.00 0.00

ATOM 223 O LEU A 101 140.204 35.418 -18.253 1.00 0.00

ATOM 224 CB LEU A 101 142.305 36.723 -20.272 1.00 0.00

ATOM 225 CG LEU A 101 142.484 37.913 -21.218 1.00 0.00

ATOM 226 CDl LEU A 101 143.183 37.483 -22.498 1.00 0.00

ATOM 227 CD2 LEU A 101 141.135 38.510 -21.591 1.00 0.00

ATOM 228 N GLU A 102 142.349 34.981 -17.688 1.00 0.00

ATOM 229 CA GLU A 102 141.993 33.698 -17.099 1.00 0.00

ATOM 230 C GLU A 102 141.096 33.891 -15.911 1.00 0.00

ATOM 231 O GLU A 102 140.204 33.085 -15.694 1.00 0.00

ATOM 232 CB GLU A 102 143.248 32.954 -16.639 1.00 0.00

ATOM 233 CG GLU A 102 144.114 32.435 -17.774 1.00 0.00

ATOM 234 CD GLU A 102 145.407 31.812 -17.284 1.00 0.00

ATOM 235 OEl GLU A 102 145.660 31.853 -16.061 1.00 0.00

ATOM 236 OE2 GLU A 102 146.167 31.283 -18.122 1.00 0.00

ATOM 237 N THR A 103 141.330 34.976 -15.147 1.00 0.00

ATOM 238 CA THR A 103 140.453 35.253 -14.023 1.00 0.00

ATOM 239 C THR A 103 139.077 35.574 -14.537 1.00 0.00

ATOM 240 O THR A 103 138.103 35.037 -14.036 1.00 0.00

ATOM 241 CB THR A 103 140.959 36.447 -13.193 1.00 0.00

ATOM 242 OGl THR A 103 142.250 36.143 -12.651 1.00 0.00

ATOM 243 CG2 THR A 103 140.002 36.745 -12.049 1.00 0.00

ATOM 244 N GLU A 104 139.022 36.447 -15.563 1.00 0.00

ATOM 245 CA GLU A 104 137.743 36.811 -16.151 1.00 0.00

ATOM 246 C GLU A 104 137.028 35.604 -16.693 1.00 0.00

ATOM 247 O GLU A 104 135.819 35.513 -16.556 1.00 0.00

ATOM 248 CB GLU A 104 137.944 37.798 -17.303 1.00 0.00

ATOM 249 CG GLU A 104 138.379 39.186 -16.862 1.00 0.00

ATOM 250 CD GLU A 104 138.688 40.099 -18.032 1.00 0.00

ATOM 251 OEl GLU A 104 138.633 39.625 -19.186 1.00 0.00

ATOM 252 OE2 GLU A 104 138.985 41.288 -17.794 1.00 0.00

ATOM 253 N ASN A 105 137.785 34.672 -17.308 1.00 0.00

ATOM 254 CA ASN A 105 137.160 33.479 -17.859 1.00 0.00

ATOM 255 C ASN A 105 136.566 32.654 -16.757 1.00 0.00

ATOM 256 O ASN A 105 135.423 32.239 -16.872 1.00 0.00

ATOM 257 CB ASN A 105 138.191 32.629 -18.605 1.00 0.00

ATOM 258 CG ASN A 105 137.572 31.420 -19.277 1.00 0.00

ATOM 259 ODl ASN A 105 136.746 31.554 -20.180 1.00 0.00

ATOM 260 ND2 ASN A 105 137.972 30.232 -18.837 1.00 0.00

ATOM 261 N ARG A 106 137.353 32.426 -15.688 1.00 0.00

ATOM 262 CA ARG A 106 136.845 31.643 -14.576 1.00 0.00

ATOM 263 C ARG A 106 135.547 32.215 -14.077 1.00 0.00

ATOM 264 O ARG A 106 134.622 31.462 -13.820 1.00 0.00

ATOM 265 CB ARG A 106 137.847 31.640 -13.420 1.00 0.00

ATOM 266 CG ARG A 106 139.104 30.830 -13.691 1.00 0.00

ATOM 267 CD ARG A 106 140.077 30.912 -12.525 1.00 0.00 ATOM 268 NE ARG A 106 141.314 30.182 -12.792 1.00 0.00

ATOM 269 CZ ARG A 106 142.374 30.191 -11.990 1.00 0.00

ATOM 270 NHl ARG A 106 143.457 29.497 -12.314 1.00 0.00

ATOM 271 NH2 ARG A 106 142.350 30.895 -10.867 1.00 0.00

ATOM 272 N ARG A 107 135.481 33.557 -13.960 1.00 0.00

ATOM 273 CA ARG A 107 134.250 34.179 -13.498 1.00 0.00

ATOM 274 C ARG A 107 133.114 33.896 -14.442 1.00 0.00

ATOM 275 O ARG A 107 132.046 33.519 -13.990 1.00 0.00

ATOM 276 CB ARG A 107 134.420 35.696 -13.399 1.00 0.00

ATOM 277 CG ARG A 107 135.325 36.145 -12.264 1.00 0.00

ATOM 278 CD ARG A 107 135.487 37.657 -12.253 1.00 0.00

ATOM 279 NE ARG A 107 136.395 38.103 -11.198 1.00 0.00

ATOM 280 CZ ARG A 107 136.752 39.368 -11.005 1.00 0.00

ATOM 281 NHl ARG A 107 137.582 39.680 -10.019 1.00 0.00

ATOM 282 NH2 ARG A 107 136.278 40.319 -11.798 1.00 0.00

ATOM 283 N LEU A 108 133.354 34.081 -15.757 1.00 0.00

ATOM 284 CA LEU A 108 132.295 33.841 -16.723 1.00 0.00

ATOM 285 C LEU A 108 131.776 32.436 -16.609 1.00 0.00

ATOM 286 O LEU A 108 130.573 32.234 -16.663 1.00 0.00

ATOM 287 CB LEU A 108 132.813 34.047 -18.148 1.00 0.00

ATOM 288 CG LEU A 108 133.146 35.485 -18.547 1.00 0.00

ATOM 289 CDl LEU A 108 133.816 35.523 -19.913 1.00 0.00

ATOM 290 CD2 LEU A 108 131.883 36.331 -18.614 1.00 0.00

ATOM 291 N GLU A 109 132.703 31.470 -16.441 1.00 0.00

ATOM 292 CA GLU A 109 132.294 30.080 -16.330 1.00 0.00

ATOM 293 C GLU A 109 131.364 29.890 -15.165 1.00 0.00

ATOM 294 O GLU A 109 130.308 29.303 -15.335 1.00 0.00

ATOM 295 CB GLU A 109 133.513 29.177 -16.124 1.00 0.00

ATOM 296 CG GLU A 109 133.182 27.696 -16.043 1.00 0.00

ATOM 297 CD GLU A 109 134.416 26.832 -15.872 1.00 0.00

ATOM 298 OEl GLU A 109 135.531 27.392 -15.831 1.00 0.00

ATOM 299 OE2 GLU A 109 134.266 25.596 -15.780 1.00 0.00

ATOM 300 N SER A 110 131.759 30.405 -13.982 1.00 0.00

ATOM 301 CA SER A 110 130.893 30.283 -12.820 1.00 0.00

ATOM 302 C SER A 110 129.532 30.849 -13.123 1.00 0.00

ATOM 303 O SER A 110 128.543 30.169 -12.898 1.00 0.00

ATOM 304 CB SER A 110 131.482 31.043 -11.631 1.00 0.00

ATOM 305 OG SER A 110 132.685 30.442 -11.185 1.00 0.00

ATOM 306 N LYS A 111 129.495 32.089 -13.649 1.00 0.00

ATOM 307 CA LYS A 111 128.218 32.719 -13.951 1.00 0.00

ATOM 308 C LYS A 111 127.359 31.876 -14.855 1.00 0.00

ATOM 309 O LYS A 111 126.171 31.757 -14.596 1.00 0.00

ATOM 310 CB LYS A 111 128.435 34.062 -14.652 1.00 0.00

ATOM 311 CG LYS A 111 128.994 35.149 -13.748 1.00 0.00

ATOM 312 CD LYS A 111 129.162 36.459 -14.500 1.00 0.00

ATOM 313 CE LYS A 111 129.725 37.545 -13.598 1.00 0.00

ATOM 314 NZ LYS A 111 129.941 38.821 -14.334 1.00 0.00

ATOM 315 N ILE A 112 127.955 31.288 -15.911 1.00 0.00

ATOM 316 CA ILE A 112 127.157 30.482 -16.823 1.00 0.00

ATOM 317 C ILE A 112 126.627 29.258 -16.130 1.00 0.00

ATOM 318 O ILE A 112 125.516 28.845 -16.419 1.00 0.00

ATOM 319 CB ILE A 112 127.985 30.014 -18.034 1.00 0.00

ATOM 320 CGl ILE A 112 128.365 31.206 -18.914 1.00 0.00

ATOM 321 CG2 ILE A 112 127.188 29.029 -18.875 1.00 0.00

ATOM 322 CDl ILE A 112 129.392 30.879 -19.976 1.00 0.00

ATOM 323 N ARG A 113 127.418 28.686 -15.201 1.00 0.00

ATOM 324 CA ARG A 113 126.934 27.526 -14.470 1.00 0.00

ATOM 325 C ARG A 113 125.749 27.912 -13.630 1.00 0.00

ATOM 326 O ARG A 113 124.720 27.261 -13.706 1.00 0.00

ATOM 327 CB ARG A 113 128.029 26.975 -13.554 1.00 0.00

ATOM 328 CG ARG A 113 129.175 26.300 -14.292 1.00 0.00

ATOM 329 CD ARG A 113 130.245 25.819 -13.327 1.00 0.00

ATOM 330 NE ARG A 113 131.377 25.212 -14.024 1.00 0.00

ATOM 331 CZ ARG A 113 132.471 24.760 -13.420 1.00 0.00

ATOM 332 NHl ARG A 113 133.450 24.224 -14.135 1.00 0.00

ATOM 333 NH2 ARG A 113 132.584 24.846 -12.101 1.00 0.00

ATOM 334 N GLU A 114 125.913 28.986 -12.831 1.00 0.00

ATOM 335 CA GLU A 114 124.832 29.409 -11.959 1.00 0.00 ATOM 336 C GLU A 114 123.585 29.706 -12.741 1.00 0.00

ATOM 337 O GLU A 114 122.556 29.113 -12.466 1.00 0.00

ATOM 338 CB GLU A 114 125.224 30.676 -11.195 1.00 0.00

ATOM 339 CG GLU A 114 124.160 31.173 -10.231 1.00 0.00

ATOM 340 CD GLU A 114 124.562 32.455 -9.529 1.00 0.00

ATOM 341 OEl GLU A 114 125.682 32.947 -9.787 1.00 0.00

ATOM 342 OE2 GLU A 114 123.759 32.969 -8.724 1.00 0.00

ATOM 343 N HIS A 115 123.692 30.627 -13.720 1.00 0.00

ATOM 344 CA HIS A 115 122.517 30.997 -14.490 1.00 0.00

ATOM 345 C HIS A 115 121.891 29.794 -15.137 1.00 0.00

ATOM 346 O HIS A 115 120.707 29.563 -14.955 1.00 0.00

ATOM 347 CB HIS A 115 122.890 31.989 -15.594 1.00 0.00

ATOM 348 CG HIS A 115 123.350 33.318 -15.081 1.00 0.00

ATOM 349 NDl HIS A 115 124.655 33.563 -14.714 1.00 0.00

ATOM 350 CD2 HIS A 115 122.721 34.606 -14.822 1.00 0.00

ATOM 351 CEl HIS A 115 124.761 34.838 -14.298 1.00 0.00

ATOM 352 NE2 HIS A 115 123.604 35.469 -14.359 1.00 0.00

TER 353 HIS A 115

ATOM 354 N TRP A 126 104.979 31.505 -15.263 1.00 0.00

ATOM 355 CA TRP A 126 104.621 30.167 -14.792 1.00 0.00

ATOM 356 C TRP A 126 103.828 30.282 -13.468 1.00 0.00

ATOM 357 O TRP A 126 102.704 29.788 -13.371 1.00 0.00

ATOM 358 CB TRP A 126 105.879 29.331 -14.547 1.00 0.00

ATOM 359 CG TRP A 126 105.593 27.952 -14.036 1.00 0.00

ATOM 360 CDl TRP A 126 105.271 26.853 -14.780 1.00 0.00

ATOM 361 CD2 TRP A 126 105.603 27.524 -12.669 1.00 0.00

ATOM 362 NEl TRP A 126 105.080 25.767 -13.961 1.00 0.00

ATOM 363 CE2 TRP A 126 105.278 26.153 -12.659 1.00 0.00

ATOM 364 CE3 TRP A 126 105.854 28.165 -11.452 1.00 0.00

ATOM 365 CZ2 TRP A 126 105.198 25.412 -11.481 1.00 0.00

ATOM 366 CZ3 TRP A 126 105.774 27.427 -10.287 1.00 0.00

ATOM 367 CH2 TRP A 126 105.449 26.067 -10.306 1.00 0.00

ATOM 368 N SER A 127 104.398 30.941 -12.465 1.00 0.00

ATOM 369 CA SER A 127 103.721 31.113 -11.177 1.00 0.00

ATOM 370 C SER A 127 102.334 31.749 -11.316 1.00 0.00

ATOM 371 O SER A 127 101.362 31.317 -10.695 1.00 0.00

ATOM 372 CB SER A 127 104.543 32.017 -10.256 1.00 0.00

ATOM 373 OG SER A 127 105.775 31.408 -9.910 1.00 0.00

ATOM 374 N HIS A 128 102.246 32.795 -12.126 1.00 0.00

ATOM 375 CA HIS A 128 100.971 33.458 -12.297 1.00 0.00

ATOM 376 C HIS A 128 99.943 32.603 -13.002 1.00 0.00

ATOM 377 O HIS A 128 98.750 32.731 -12.734 1.00 0.00

ATOM 378 CB HIS A 128 101.137 34.733 -13.126 1.00 0.00

ATOM 379 CG HIS A 128 101.872 35.826 -12.413 1.00 0.00

ATOM 380 NDl HIS A 128 101.377 36.442 -11.284 1.00 0.00

ATOM 381 CD2 HIS A 128 103.138 36.520 -12.601 1.00 0.00

ATOM 382 CEl HIS A 128 102.254 37.376 -10.875 1.00 0.00

ATOM 383 NE2 HIS A 128 103.312 37.428 -11.660 1.00 0.00

ATOM 384 N TYR A 129 100.384 31.742 -13.912 1.00 0.00

ATOM 385 CA TYR A 129 99.429 30.907 -14.612 1.00 0.00

ATOM 386 C TYR A 129 98.893 29.876 -13.660 1.00 0.00

ATOM 387 O TYR A 129 97.706 29.581 -13.656 1.00 0.00

ATOM 388 CB TYR A 129 100.098 30.202 -15.793 1.00 0.00

ATOM 389 CG TYR A 129 100.504 31.134 -16.913 1.00 0.00

ATOM 390 CDl TYR A 129 99.992 32.423 -16.986 1.00 0.00

ATOM 391 CD2 TYR A 129 101.398 30.721 -17.892 1.00 0.00

ATOM 392 CEl TYR A 129 100.356 33.281 -18.006 1.00 0.00

ATOM 393 CE2 TYR A 129 101.775 31.565 -18.920 1.00 0.00

ATOM 394 CZ TYR A 129 101.244 32.854 -18.969 1.00 0.00

ATOM 395 OH TYR A 129 101.610 33.707 -19.986 1.00 0.00

ATOM 396 N PHE A 130 99.757 29.331 -12.829 1.00 0.00

ATOM 397 CA PHE A 130 99.272 28.369 -11.865 1.00 0.00

ATOM 398 C PHE A 130 98.275 29.085 -10.956 1.00 0.00

ATOM 399 O PHE A 130 97.254 28.513 -10.558 1.00 0.00

ATOM 400 CB PHE A 130 100.429 27.815 -11.031 1.00 0.00

ATOM 401 CG PHE A 130 100.005 26.811 -9.998 1.00 0.00

ATOM 402 CDl PHE A 130 99.735 25.501 -10.354 1.00 0.00

ATOM 403 CD2 PHE A 130 99.877 27.176 -8.669 1.00 0.00 ATOM 404 CEl PHE A 130 99.345 24.577 -9.403 1.00 0.00

ATOM 405 CE2 PHE A 130 99.487 26.251 -7.718 1.00 0.00

ATOM 406 CZ PHE A 130 q q 999 24.958 -8.080 1.00 0.00

ATOM 407 N LYS A 131 98.581 30.335 -10.630 1.00 0.00

ATOM 408 CA LYS A 131 97.731 31.106 -9.740 1.00 0.00

ATOM 409 C LYS A 131 96.350 31.248 -10.326 1.00 0.00

ATOM 410 O LYS A 131 95.341 31.059 -9.649 1.00 0.00

ATOM 411 CB LYS A 131 98.312 32.505 -9.523 1.00 0.00

ATOM 412 CG LYS A 131 99.582 32.527 -8.688 1.00 0.00

ATOM 413 CD LYS A 131 100.101 33.944 -8.511 1.00 0.00

ATOM 414 CE LYS A 131 101.385 33.964 -7.697 1.00 0.00

ATOM 415 NZ LYS A 131 101.924 35.344 -7.542 1.00 0.00

ATOM 416 N ILE A 132 96.343 31.555 -11.611 1.00 0.00

ATOM 417 CA ILE A 132 95.131 31.767 -12.375 1.00 0.00

ATOM 418 C ILE A 132 94.346 30.460 -12.498 1.00 0.00

ATOM 419 O ILE A 132 93.111 30.446 -12.512 1.00 0.00

ATOM 420 CB ILE A 132 95.440 32.272 -13.797 1.00 0.00

ATOM 421 CGl ILE A 132 96.033 33.682 -13.745 1.00 0.00

ATOM 422 CG2 ILE A 132 94.172 32.312 -14.635 1.00 0.00

ATOM 423 CDl ILE A 132 96.608 34.150 -15.063 1.00 0.00

ATOM 424 N ILE A 133 95.098 29.286 -12.664 1.00 0.00

ATOM 425 CA ILE A 133 94.631 27.900 -12.641 1.00 0.00

ATOM 426 C ILE A 133 93.890 27.629 -11.309 1.00 0.00

ATOM 427 O ILE A 133 92.728 27.220 -11.315 1.00 0.00

ATOM 428 CB ILE A 133 95.803 26.908 -12.757 1.00 0.00

ATOM 429 CGl ILE A 133 96.457 27.014 -14.136 1.00 0.00

ATOM 430 CG2 ILE A 133 95.316 25.480 -12.564 1.00 0.00

ATOM 431 CDl ILE A 133 97.785 26.295 -14.240 1.00 0.00

ATOM 432 N GLU A 134 94.548 27.869 -10.180 1.00 0.00

ATOM 433 CA GLU A 134 93.927 27.654 -8.869 1.00 0.00

ATOM 434 C GLU A 134 92.602 28.407 -8.711 1.00 0.00

ATOM 435 O GLU A 134 91.611 27.870 -8.212 1.00 0.00

ATOM 436 CB GLU A 134 94.855 28.132 -7.750 1.00 0.00

ATOM 437 CG GLU A 134 94.313 27.894 -6.350 1.00 0.00

ATOM 438 CD GLU A 134 95.286 28.323 -5.269 1.00 0.00

ATOM 439 OEl GLU A 134 96.395 28.784 -5.616 1.00 0.00

ATOM 440 OE2 GLU A 134 94.941 28.197 -4.075 1.00 0.00

ATOM 441 N ASP A 135 92.589 29.665 -9.124 1.00 0.00

ATOM 442 CA ASP A 135 91.376 30.446 -8.993 1.00 0.00

ATOM 443 C ASP A 135 90.253 29.959 -9.879 1.00 0.00

ATOM 444 O ASP A 135 89.084 30.082 -9.516 1.00 0.00

ATOM 445 CB ASP A 135 91.637 31.907 -9.366 1.00 0.00

ATOM 446 CG ASP A 135 92.436 32.644 -8.310 1.00 0.00

ATOM 447 ODl ASP A 135 92.580 32.108 -7.192 1.00 0.00

ATOM 448 OD2 ASP A 135 92.920 33.758 -8.601 1.00 0.00

ATOM 449 N LEU A 136 90.586 29.418 -11.048 1.00 0.00

ATOM 450 CA LEU A 136 89.538 28.941 -11.926 1.00 0.00

ATOM 451 C LEU A 136 88.935 27.697 -11.340 1.00 0.00

ATOM 452 O LEU A 136 87.725 27.511 -11.363 1.00 0.00

ATOM 453 CB LEU A 136 90.104 28.620 -13.311 1.00 0.00

ATOM 454 CG LEU A 136 90.570 29.814 -14.146 1.00 0.00

ATOM 455 CDl LEU A 136 91.269 29.344 -15.412 1.00 0.00

ATOM 456 CD2 LEU A 136 89.388 30.682 -14.550 1.00 0.00

ATOM 457 N ARG A 137 89.767 26.840 -10.784 1.00 0.00

ATOM 458 CA ARG A 137 89.224 25.654 -10.165 1.00 0.00

ATOM 459 C ARG A 137 88.323 26.100 -9.016 1.00 0.00

ATOM 460 O ARG A 137 87.267 25.511 -8.769 1.00 0.00

ATOM 461 CB ARG A 137 90.350 24.767 -9.629 1.00 0.00

ATOM 462 CG ARG A 137 91.169 24.081 -10.710 1.00 0.00

ATOM 463 CD ARG A 137 92.311 23.277 -10.111 1.00 0.00

ATOM 464 NE ARG A 137 93.126 22.633 -11.139 1.00 0.00

ATOM 465 CZ ARG A 137 94.228 21.933 -10.890 1.00 0.00

ATOM 466 NHl ARG A 137 94.904 21.383 -11.889 1.00 0.00

ATOM 467 NH2 ARG A 137 94.650 21.784 -9.642 1.00 0.00

ATOM 468 N ALA A 138 88.755 27.141 -8.314 1.00 0.00

ATOM 469 CA ALA A 138 88.006 27.637 -7.171 1.00 0.00

ATOM 470 C ALA A 138 86.628 28.072 -7.596 1.00 0.00

ATOM 471 O ALA A 138 85.625 27.749 -6.963 1.00 0.00 ATOM 472 CB ALA A 138 88.718 -6.547 00 0.00

ATOM 473 N GLN A 139 86.611 28.791 -8.706 00 0.00

ATOM 474 CA GLN A 139 85.403 29.340 -9.287 00 0.00

ATOM 475 C GLN A 139 84.496 28.214 -9.787 00 0.00

ATOM 476 O GLN A 139 83.266 28.302 -9.732 00 0.00

ATOM 477 CB GLN A 139 85.742 30.252 --1]0.467 00 0.00

ATOM 478 CG GLN A 139 86.422 31.552 -10.071 00 0.00

ATOM 479 CD GLN A 139 86.799 .401 -11.270 00 0.00

ATOM 480 OEl GLN A 139 86.589 .002 -12.415 00 0.00

ATOM 481 NE2 GLN A 139 87.357 33.577 -11.008 00 0.00

ATOM 482 N ILE A 140 85.122 27.144 -10.256 00 0.00

ATOM 483 CA ILE A 140 84.393 26.001 -10.783 00 0.00

ATOM 484 C ILE A 140 83.680 25.265 -9.648 00 0.00

ATOM 485 O ILE A 140 82.528 24.831 -9.784 00 0.00

ATOM 486 CB ILE A 140 85.336 25.005 11.483 00 0.00

ATOM 487 CGl ILE A 140 85.917 25.625 -12.755 00 0.00

ATOM 488 CG2 ILE A 140 84.585 23.738 11.864 00 0.00

ATOM 489 CDl ILE A 140 87.048 24.825 13.363 00 0.00

ATOM 490 N PHE A 141 84.374 25.148 -8.529 00 0.00

ATOM 491 CA PHE A 141 83.847 24.488 -7.349 00 0.00

ATOM 492 C PHE A 141 82.698 25.303 -6.736 1.00 0.00

ATOM 493 O PHE A 141 81.738 4. .747 -6. 14 1. .00 0.00

ATOM 494 CB PHE A 141 84.939 4. .329 -6. 90 1..00 0.00

ATOM 495 CG PHE A 141 84.476 3.637 -5.039 1..00 0.00

ATOM 496 CDl PHE A 141 84.317 22.262 -5.011 1.00 0.00

ATOM 497 CD2 PHE A 141 84.199 24.361 -3.893 1.00 0.00

ATOM 498 CEl PHE A 141 83.890 21.626 -3.861 1..00 0.00

ATOM 499 CE2 PHE A 141 83.774 23.724 -2.743 1..00 0.00

ATOM 500 CZ PHE A 141 83.618 22.363 -2.723 1.00 0.00

ATOM 501 N ALA A 142 82.799 26.624 -6.801 1.00 0.00

ATOM 502 CA ALA A 142 81.745 27.468 -6.248 1.00 0.00

ATOM 503 C ALA A 142 80.509 27.387 -7.146 1.00 0.00

ATOM 504 O ALA A 142 79.372 27.484 -6.676 1.00 0.00

ATOM 505 CB ALA A 142 82.210 28.914 -6.169 1.00 0.00

ATOM 506 N ASN A 143 80.734 27.214 -8.444 1..00 0.00

ATOM 507 CA ASN A 143 79.634 27.091 -9.385 1..00 0.00

ATOM 508 C ASN A 143 78.988 25.733 -9.165 1.00 0.00

ATOM 509 O ASN A 143 77.785 25.583 -9.324 1.00 0.00

ATOM 510 CB ASN A 143 80.145 27.197 -10.824 1.00 0.00

ATOM 511 CG ASN A 143 79.021 27.275 -11.837 1.00 0.00

ATOM 512 ODl ASN A 143 78.235 28.224 -11.835 1.00 0.00

ATOM 513 ND2 ASN A 143 78.940 26.278 -12.709 1.00 0.00

ATOM 514 N THR A 144 79.802 24.756 -8.782 1..00 0.00

ATOM 515 CA THR A 144 79.323 23.402 -8.512 1..00 0.00

ATOM 516 C THR A 144 78.362 23.434 -7.312 1.00 0.00

ATOM 517 O THR A 144 77.226 2 985 -7.410 1.00 0.00

ATOM 518 CB THR A 144 80.486 22.446 -8.185 1.00 0.00

ATOM 519 OGl THR A 144 81.376 22.372 -9.305 1.00 0.00

ATOM 520 CG2 THR A 144 79.961 21.053 -7.880 1.00 0.00

ATOM 521 N VAL A 145 78.818 23.963 -6.179 1.00 0.00

ATOM 522 CA VAL A 145 77.957 24.046 -5.006 1.00 0.00

ATOM 523 C VAL A 145 76.659 .742 -5.407 1..00 0.00

ATOM 524 O VAL A 145 75.587 .262 -5.078 1..00 0.00

ATOM 525 CB VAL A 145 78.623 24.847 -3.871 1.00 0.00

ATOM 526 CGl VAL A 145 77.633 25.100 -2.746 1.00 0.00

ATOM 527 CG2 VAL A 145 79.809 24.080 -3.304 1.00 0.00

ATOM 528 N ASP A 146 76.727 25.863 -6.120 1.00 0.00

ATOM 529 CA ASP A 146 75.483 26.522 -6.536 1.00 0.00

ATOM 530 C ASP A 146 74.564 25.561 -7.323 1.00 0.00

ATOM 531 O ASP A 146 73.384 25.353 -6.989 1..00 0.00

ATOM 532 CB ASP A 146 75.786 27.722 -7.436 1..00 0.00

ATOM 533 CG ASP A 146 76.376 28.890 -6.670 1.00 0.00

ATOM 534 ODl ASP A 146 76.330 28.866 -5.42; 1.00 0.00

ATOM 535 OD2 ASP A 146 76.885 29. 829 -7.318 00 0.00

ATOM 536 N ASN A 147 75.125 24 . 981 -8.373 00 0.00

ATOM 537 CA ASN A 147 74.436 24 . 028 -9.237 00 0.00

ATOM 538 C ASN A 147 73.706 >2.926 - 444 00 0.00

ATOM 539 O ASN A 147 72.522 22.64; -8.673 1.00 0.00 ATOM 540 CB ASN A 147 75.431 23.334 -10.170 00 0.00

ATOM 541 CG ASN A 147 75.933 24.248 -11.271 00 0.00

ATOM 542 ODl ASN A 147 75.340 25.292 -11.542 00 0.00

ATOM 543 ND2 ASN A 147 77.030 23.856 -11.908 00 0.00

ATOM 544 N ALA A 148 74.416 22.319 -7.498 00 0.00

ATOM 545 CA ALA A 148 73.837 21.259 -6.687 00 0.00

ATOM 546 C ALA A 148 72.681 21.811 -5.850 00 0.00

ATOM 547 O ALA A 148 71.656 21.144 -5.697 00 0.00

ATOM 548 CB ALA A 148 74.884 20.677 -5.749 1.00 0.00

ATOM 549 N ARG A 149 72.831 23.017 -5.314 .00 0.00

ATOM 550 CA ARG A 149 71.764 23.598 -4.500 .00 0.00

ATOM 551 C ARG A 149 70.496 23 ..772 -5.313 1.00 0.00

ATOM 552 O ARG A 149 69.409 23 .,399 -4.873 .00 0.00

ATOM 553 CB ARG A 149 72.182 24 . 970 -3.968 .00 0.00

ATOM 554 CG ARG A 149 73.262 24 . 919 -2.900 .00 0.00

ATOM 555 CD ARG A 149 73.662 26. , 315 -2.451 .00 0.00

ATOM 556 NE ARG A 149 74.734 26. ^?85 -1.459 .00 0.00

ATOM 557 CZ ARG A 149 75.306 27 . 369 -0.944 .00 0.00

ATOM 558 NHl ARG A 149 76.275 27 . 244 -0.047 .00 0.00

ATOM 559 NH2 ARG A 149 74.908 28 . 574 -1.327 1.00 0.00

ATOM 560 N ILE A 150 70.638 2244..334400 -6.503 1.00 0.00

ATOM 561 CA ILE A 150 69.485 24.. 554488 -7.361 1..00 0.00

ATOM 562 C ILE A 150 68.875 23.257 -7.862 1..00 0.00

ATOM 563 O ILE A 150 67.657 23.167 -7.992 1..00 0.00

ATOM 564 CB ILE A 150 69.852 25.370 -8.611 1.00 0.00

ATOM 565 CGl ILE A 150 70.217 26.803 -8.217 1.00 0.00

ATOM 566 CG2 ILE A 150 68.681 25.420 -9.580 1.00 0.00

ATOM 567 CDl ILE A 150 70.840 27.604 -9.340 1.00 0.00

ATOM 568 N VAL A 151 69.690 22.252 -8.155 1.00 0.00

ATOM 569 CA VAL A 151 69.096 21.012 .631 1.00 0.00

ATOM 570 C VAL A 151 68.298 20.348 -7.525 1..00 0.00

ATOM 571 O VAL A 151 67.207 19.854 -7.782 1..00 0.00

ATOM 572 CB VAL A 151 70.170 20.015 -9.104 1.00 0.00

ATOM 573 CGl VAL A 151 69.544 18.666 -9.417 1.00 0.00

ATOM 574 CG2 VAL A 151 70.856 20.530 -10.360 1.00 0.00

ATOM 575 N LEU A 152 68.809 20.329 -6.294 1.00 0.00

ATOM 576 CA LEU A 152 68.032 19.733 -5.204 1.00 0.00

ATOM 577 C LEU A 152 66.711 20.499 -5.042 1.00 0.00

ATOM 578 O LEU A 152 65.637 19.906 -4. .916 1..00 0.00

ATOM 579 CB LEU A 152 68.813 19.804 -3. 1..00 0.00

ATOM 580 CG LEU A 152 70.049 18.909 -3.786 1.00 0.00

ATOM 581 CDl LEU A 152 70.826 19.209 -2.514 1.00 0.00

ATOM 582 CD2 LEU A 152 69.649 17.441 -3.764 1.00 0.00

ATOM 583 N GLN A 153 66.792 21.830 -5.074 1.00 0.00

ATOM 584 CA GLN A 153 65.600 22.655 -4.950 1.00 0.00

ATOM 585 C GLN A 153 64.632 22.273 -6.072 1.00 0.00

ATOM 586 O GLN A 153 63.428 22 129 -5.826 1..00 0.00

ATOM 587 CB GLN A 153 65.961 24.138 -5.069 1..00 0.00

ATOM 588 CG GLN A 153 66.729 24.687 -3.877 1..00 0.00

ATOM 589 CD GLN A 153 67.167 26.124 -4.079 1..00 0.00

ATOM 590 OEl GLN A 153 66.976 26.697 -5.152 1.00 0.00

ATOM 591 NE2 GLN A 153 67.756 26.712 -3.044 1. .00 0.00

ATOM 592 N ILE A 154 65.154 22.089 -7.285 1..00 0.00

ATOM 593 CA ILE A 154 64.278 21.729 -8.403 1.00 0.00

ATOM 594 C ILE A 154 63.636 20.392 -8.182 1.00 0.00

ATOM 595 O ILE A 154 62.439 20.257 -8.408 1..00 0.00

ATOM 596 CB ILE A 154 65 . 057 21.656 -9.730 1..00 0.00

ATOM 597 CGl ILE A 154 65 . 536 23.048 -10.146 1.00 0.00

ATOM 598 CG2 ILE A 154 64 . 174 21.099 -10.836 1.00 0.00

ATOM 599 CDl ILE A 154 66. 529 23.036 -11.287 1.00 0.00

ATOM 600 N ASP A 155 64 . 408 19.405 -7.732 1.00 0.00

ATOM 601 CA ASP A 155 63 . 820 18.100 -7.459 1.00 0.00

ATOM 602 C ASP A 155 62 . 639 18.262 -6.521 1.00 0.00

ATOM 603 O ASP A 155 61 . 557 17.738 -6.767 00 0.00

ATOM 604 CB ASP A 155 64 . 849 17.176 -6.805 00 0.00

ATOM 605 CG ASP A 155 65 . 909 16.701 -7.780 00 0.00

ATOM 606 ODl ASP A 155 65 . 723 16.897 -9.001 00 0.00

ATOM 607 OD2 ASP A 155 66. 924 16.134 -7.325 1.00 0.00 ATOM 608 N ASN A 156 62.830 19.004 -5.447 1.00 0.00

ATOM 609 CA ASN A 156 61.728 19.171 -4.514 1.00 0.00

ATOM 610 C ASN A 156 60.535 19.859 -5.143 1.00 0.00

ATOM 611 O ASN A 156 59.384 19.516 -4.851 1.00 0.00

ATOM 612 CB ASN A 156 62.164 20.017 -3.316 1.00 0.00

ATOM 613 CG ASN A 156 63.085 19.266 -2.376 1.00 0.00

ATOM 614 ODl ASN A 156 63.128 18.035 -2.386 1.00 0.00

ATOM 615 ND2 ASN A 156 63.826 20.005 -1.560 1.00 0.00

ATOM 616 N ALA A 157 60.784 20.814 -6.030 1.00 0.00

ATOM 617 CA ALA A 157 59.647 21.473 -6.646 1.00 0.00

ATOM 618 C ALA A 157 58.948 20.503 -7.563 1.00 0.00

ATOM 619 O ALA A 157 57.726 20.427 -7.542 1.00 0.00

ATOM 620 CB ALA A 157 60.105 22.678 -7.452 1.00 0.00

ATOM 621 N ARG A 158 59.698 19.735 -8.347 1.00 0.00

ATOM 622 CA ARG A 158 59.053 18.779 -9.228 1.00 0.00

ATOM 623 C ARG A 158 58.190 17.772 -8.487 1.00 0.00

ATOM 624 O ARG A 158 57.100 17.444 -8.949 1.00 0.00

ATOM 625 CB ARG A 158 60.099 17.983 -10.011 1.00 0.00

ATOM 626 CG ARG A 158 60.824 18.789 -11.076 1.00 0.00

ATOM 627 CD ARG A 158 61.896 17.959 -11.763 1.00 0.00

ATOM 628 NE ARG A 158 62.621 18.728 -12.771 1.00 0.00

ATOM 629 CZ ARG A 158 63.655 18.263 -13.465 1.00 0.00

ATOM 630 NHl ARG A 158 64.254 19.035 -14.361 1.00 0.00

ATOM 631 NH2 ARG A 158 64.087 17.026 -13.261 1.00 0.00

ATOM 632 N LEU A 159 58.661 17.287 -7.338 1.00 0.00

ATOM 633 CA LEU A 159 57.871 16.340 -6.551 1.00 0.00

ATOM 634 C LEU A 159 56.608 17.012 -6.076 1.00 0.00

ATOM 635 O LEU A 159 55.512 16.463 -6.169 1.00 0.00

ATOM 636 CB LEU A 159 58.666 15.860 -5.336 1.00 0.00

ATOM 637 CG LEU A 159 57.955 14.872 -4.408 1.00 0.00

ATOM 638 CDl LEU A 159 57.610 13.590 -5.150 1.00 0.00

ATOM 639 CD2 LEU A 159 58.841 14.512 -3.225 1.00 0.00

ATOM 640 N ALA A 160 56.779 18.209 -5.557 1.00 0.00

ATOM 641 CA ALA A 160 55.653 18.981 -5.106 1.00 0.00

ATOM 642 C ALA A 160 54.622 19.044 -6.233 1.00 0.00

ATOM 643 O ALA A 160 53.460 18.718 -6.066 1.00 0.00

ATOM 644 CB ALA A 160 56.088 20.391 -4.740 1.00 0.00

ATOM 645 N ALA A 161 55.096 19.467 -7.390 1.00 0.00

ATOM 646 CA ALA A 161 54.306 19.600 -8.600 1.00 0.00

ATOM 647 C ALA A 161 53.477 18.345 -8.930 1.00 0.00

ATOM 648 O ALA A 161 52.250 18.383 -9.024 1.00 0.00

ATOM 649 CB ALA A 161 55.207 19.865 -9.796 1.00 0.00

ATOM 650 N ASP A 162 54.169 17.230 -9.134 1.00 0.00

ATOM 651 CA ASP A 162 53.504 15.979 -9.450 1.00 0.00

ATOM 652 C ASP A 162 52.400 15.705 -8.415 1.00 0.00

ATOM 653 O ASP A 162 51.232 15.466 -8.742 1.00 0.00

ATOM 654 CB ASP A 162 54.504 14.821 -9.425 1.00 0.00

ATOM 655 CG ASP A 162 55.444 14.838 -10.615 1.00 0.00

ATOM 656 ODl ASP A 162 55.181 15.600 -11.569 1.00 0.00

ATOM 657 OD2 ASP A 162 56.443 14.089 -10.593 1.00 0.00

ATOM 658 N ASP A 163 52.779 15.770 -7.149 1.00 0.00

ATOM 659 CA ASP A 163 51.856 15.560 -6.055 1.00 0.00

ATOM 660 C ASP A 163 50.611 16.456 -6.180 1.00 0.00

ATOM 661 O ASP A 163 49.499 15.953 -6.269 1.00 0.00

ATOM 662 CB ASP A 163 52.529 15.879 -4.719 1.00 0.00

ATOM 663 CG ASP A 163 53.524 14.815 -4.300 1.00 0.00

ATOM 664 ODl ASP A 163 53.553 13.743 -4.939 1.00 0.00

ATOM 665 OD2 ASP A 163 54.277 15.054 -3.332 1.00 0.00

ATOM 666 N PHE A 164 50.804 17.771 -6.192 1.00 0.00

ATOM 667 CA PHE A 164 49.682 18.696 -6.339 1.00 0.00

ATOM 668 C PHE A 164 48.791 18.389 -7.524 1.00 0.00

ATOM 669 O PHE A 164 47.586 18.553 -7.443 1.00 0.00

ATOM 670 CB PHE A 164 50.189 20.127 -6.527 1.00 0.00

ATOM 671 CG PHE A 164 50.797 20.722 -5.288 1.00 0.00

ATOM 672 CDl PHE A 164 50.607 20.129 -4.053 1.00 0.00

ATOM 673 CD2 PHE A 164 51.557 21.876 -5.359 1.00 0.00

ATOM 674 CEl PHE A 164 51.165 20.677 -2.913 1.00 0.00

ATOM 675 CE2 PHE A 164 52.116 22.425 -4.220 1.00 0.00 ATOM 676 CZ PHE A 164 51.923 21.829 -3.001 1.00 0.00

ATOM 677 N ARG A 165 49.393 17.979 -8.637 1.00 0.00

ATOM 678 CA ARG A 165 48.646 17.636 -9.848 1.00 0.00

ATOM 679 C ARG A 165 47.735 16.447 -9.625 1.00 0.00

ATOM 680 O ARG A 165 46.591 16.411 -10.067 1.00 0.00

ATOM 681 CB ARG A 165 49.604 17.284 -10.988 1.00 0.00

ATOM 682 CG ARG A 165 50.374 18.472 -11.540 1.00 0.00

ATOM 683 CD ARG A 165 51.339 18.044 -12.635 1.00 0.00

ATOM 684 NE ARG A 165 52.122 19.168 -13.144 1.00 0.00

ATOM 685 CZ ARG A 165 53.076 19.058 -14.063 1.00 0.00

ATOM 686 NHl ARG A 165 53.737 20.135 -14.465 1.00 0.00

ATOM 687 NH2 ARG A 165 53.366 17.871 -14.578 1.00 0.00

ATOM 688 N VAL A 166 48.300 15.433 -8.993 1.00 0.00

ATOM 689 CA VAL A 166 47.588 14.206 -8.704 1.00 0.00

ATOM 690 C VAL A 166 46.415 14.543 -7.778 1.00 0.00

ATOM 691 O VAL A 166 45.266 14.182 -8.051 1.00 0.00

ATOM 692 CB VAL A 166 48.498 13.174 -8.012 1.00 0.00

ATOM 693 CGl VAL A 166 47.685 11.978 -7.541 1.00 0.00

ATOM 694 CG2 VAL A 166 49.568 12.679 -8.973 1.00 0.00

ATOM 695 N LYS A 167 46.722 15.259 -6.696 1.00 0.00

ATOM 696 CA LYS A 167 45.737 15.707 -5.703 1.00 0.00

ATOM 697 C LYS A 167 44.610 16.433 -6.395 1.00 0.00

ATOM 698 O LYS A 167 43.444 16.172 -6.127 1.00 0.00

ATOM 699 CB LYS A 167 46.389 16.654 -4.693 1.00 0.00

ATOM 700 CG LYS A 167 47.367 15.976 -3.748 1.00 0.00

ATOM 701 CD LYS A 167 47.952 16.967 -2.755 1.00 0.00

ATOM 702 CE LYS A 167 48.912 16.284 -1.794 1.00 0.00

ATOM 703 NZ LYS A 167 49.535 17.252 -0.849 1.00 0.00

ATOM 704 N TYR A 168 44.978 17.375 -7.254 1.00 0.00

ATOM 705 CA TYR A 168 43.977 18.143 -7.973 1.00 0.00

ATOM 706 C TYR A 168 43.122 17.296 -8.891 1.00 0.00

ATOM 707 O TYR A 168 41.934 17.569 -9.051 1.00 0.00

ATOM 708 CB TYR A 168 44.643 19.211 -8.841 1.00 0.00

ATOM 709 CG TYR A 168 43.669 20.040 -9.649 1.00 0.00

ATOM 710 CDl TYR A 168 42.947 21.067 -9.055 1.00 0.00

ATOM 711 CD2 TYR A 168 43.477 19.792 -11.001 1.00 0.00

ATOM 712 CEl TYR A 168 42.054 21.828 -9.784 1.00 0.00

ATOM 713 CE2 TYR A 168 42.588 20.544 -11.748 1.00 0.00

ATOM 714 CZ TYR A 168 41.875 21.569 -11.126 1.00 0.00

ATOM 715 OH TYR A 168 40.987 22.326 -11.855 1.00 0.00

ATOM 716 N GLU A 169 43.709 16.270 -9.507 1.00 0.00

ATOM 717 CA GLU A 169 42.943 15.400 -10.394 1.00 0.00

ATOM 718 C GLU A 169 41.876 14.728 -9.551 1.00 0.00

ATOM 719 O GLU A 169 40.691 14.733 -9.894 1.00 0.00

ATOM 720 CB GLU A 169 43.853 14.347 -11.029 1.00 0.00

ATOM 721 CG GLU A 169 43.146 13.423 -12.007 1.00 0.00

ATOM n ₉₉ CD GLU A 169 44.085 12.416 -12.640 1.00 0.00

ATOM 723 OEl GLU A 169 45.292 12.449 -12.324 1.00 0.00

ATOM 724 OE2 GLU A 169 43.613 11.593 -13.453 1.00 0.00

ATOM 725 N THR A 170 42.299 14.161 -8.429 1.00 0.00

ATOM 726 CA THR A 170 41.350 13.512 -7.557 1.00 0.00

ATOM 727 C THR A 170 40.259 14.478 -7.115 1.00 0.00

ATOM 728 O THR A 170 39.074 14.165 -7.258 1.00 0.00

ATOM 729 CB THR A 170 42.030 12.967 -6.288 1.00 0.00

ATOM 730 OGl THR A 170 43.007 11.983 -6.651 1.00 0.00

ATOM 731 CG2 THR A 170 41.003 12.325 -5.368 1.00 0.00

ATOM 732 N GLU A 171 40.620 15.665 -6.636 1.00 0.00

ATOM 733 CA GLU A 171 39.569 16.572 -6.193 1.00 0.00

ATOM 734 C GLU A 171 38.632 17.058 -7.272 1.00 0.00

ATOM 735 O GLU A 171 37.459 17.228 -6.996 1.00 0.00

ATOM 736 CB GLU A 171 40.175 17.831 -5.570 1.00 0.00

ATOM 737 CG GLU A 171 40.833 17.601 -4.220 1.00 0.00

ATOM 738 CD GLU A 171 39.871 17.042 -3.191 1.00 0.00

ATOM 739 OEl GLU A 171 38.790 17.638 -3.001 1.00 0.00

ATOM 740 OE2 GLU A 171 40.197 16.006 -2.573 1.00 0.00

ATOM 741 N LEU A 172 39.116 17.286 -8.492 1.00 0.00

ATOM 742 CA LEU A 172 38.200 17.751 -9.521 1.00 0.00

ATOM 743 C LEU A 172 37.225 16.655 -9.870 1.00 0.00 ATOM 744 O LEU A 172 36.084 16.930 -10.224 1.00 0.00

ATOM 745 CB LEU A 172 38.970 18.147 -10.783 1.00 0.00

ATOM 746 CG LEU A 172 38.148 18.786 -11.905 1.00 0.00

ATOM 747 CDl LEU A 172 37.485 20.067 -11.423 1.00 0.00

ATOM 748 CD2 LEU A 172 39.035 19.127 -13.092 1.00 0.00

ATOM 749 N ALA A 173 37.673 15.415 -9.773 1.00 0.00

ATOM 750 CA ALA A 173 36.785 14.304 -10.082 1.00 0.00

ATOM 751 C ALA A 173 35.710 14.272 -9.001 1.00 0.00

ATOM 752 O ALA A 173 34.515 14.196 -9.283 1.00 0.00

ATOM 753 CB ALA A 173 37.558 12.995 -10.093 1.00 0.00

ATOM 754 N MET A 174 36.167 14.351 -7.762 1.00 0.00

ATOM 755 CA MET A 174 35.304 14.363 -6.597 1.00 0.00

ATOM 756 C MET A 174 34.287 15.517 -6.652 1.00 0.00

ATOM 757 O MET A 174 33.122 15.350 -6.289 1.00 0.00

ATOM 758 CB MET A 174 36.129 14.528 -5.320 1.00 0.00

ATOM 759 CG MET A 174 36.986 13.320 -4.973 1.00 0.00

ATOM 760 SD MET A 174 36.006 11.836 -4.680 1.00 0.00

ATOM 761 CE MET A 174 35.185 12.268 -3.149 1.00 0.00

ATOM 762 N ARG A 175 34.749 16.681 -7.101 1.00 0.00

ATOM 763 CA ARG A 175 33.896 17.866 -7.218 1.00 0.00

ATOM 764 C ARG A 175 32.848 17.589 -8.273 1.00 0.00

ATOM 765 O ARG A 175 31.665 17.799 -8.043 1.00 0.00

ATOM 766 CB ARG A 175 34.726 19.085 -7.625 1.00 0.00

ATOM 767 CG ARG A 175 33.926 20.373 -7.731 1.00 0.00

ATOM 768 CD ARG A 175 34.796 21.525 -8.206 1.00 0.00

ATOM 769 NE ARG A 175 35.274 21.323 -9.571 1.00 0.00

ATOM 770 CZ ARG A 175 34.538 21.524 -10.659 1.00 0.00

ATOM 771 NHl ARG A 175 35.057 21.314 -11.861 1.00 0.00

ATOM 772 NH2 ARG A 175 33.282 21.936 -10.542 1.00 0.00

ATOM 773 N GLN A 176 33.278 17.139 -9.444 1.00 0.00

ATOM 774 CA GLN A 176 32.317 16.828 -10.488 1.00 0.00

ATOM 775 C GLN A 176 31.214 15.895 -9.962 1.00 0.00

ATOM 776 O GLN A 176 30.027 16.112 -10.218 1.00 0.00

ATOM 111 CB GLN A 176 33.008 16.134 -11.663 1.00 0.00

ATOM 778 CG GLN A 176 32.085 15.823 -12.830 1.00 0.00

ATOM 779 CD GLN A 176 32.809 15.156 -13.984 1.00 0.00

ATOM 780 OEl GLN A 176 33.991 14.826 -13.880 1.00 0.00

ATOM 781 NE2 GLN A 176 32.100 14.954 -15.089 1.00 0.00

ATOM 782 N SER A 177 31.600 14.871 -9.212 1.00 0.00

ATOM 783 CA SER A 177 30.624 13.942 -8.646 1.00 0.00

ATOM 784 C SER A 177 29.665 14.646 -7.699 1.00 0.00

ATOM 785 O SER A 177 28.455 14.470 -7.792 1.00 0.00

ATOM 786 CB SER A 177 31.329 12.834 -7.861 1.00 0.00

ATOM 787 OG SER A 177 32.091 12.005 -8.722 1.00 0.00

ATOM 788 N VAL A 178 30.205 15.443 -6.787 1.00 0.00

ATOM 789 CA VAL A 178 29.368 16.187 -5.858 1.00 0.00

ATOM 790 C VAL A 178 28.347 17.035 -6.577 1.00 0.00

ATOM 791 O VAL A 178 27.191 17.095 -6.169 1.00 0.00

ATOM 792 CB VAL A 178 30.206 17.132 -4.978 1.00 0.00

ATOM 793 CGl VAL A 178 29.300 18.039 -4.158 1.00 0.00

ATOM 794 CG2 VAL A 178 31.080 16.335 -4.021 1.00 0.00

ATOM 795 N GLU A 179 28.787 17.711 -7.634 1.00 0.00

ATOM 796 CA GLU A 179 27.911 18.562 -8.424 1.00 0.00

ATOM 797 C GLU A 179 26.766 17.746 -9.003 1.00 0.00

ATOM 798 O GLU A 179 25.593 18.097 -8.854 1.00 0.00

ATOM 799 CB GLU A 179 28.685 19.203 -9.579 1.00 0.00

ATOM 800 CG GLU A 179 27.855 20.147 -10.432 1.00 0.00

ATOM 801 CD GLU A 179 28.663 20.788 -11.544 1.00 0.00

ATOM 802 OEl GLU A 179 29.875 20.503 -11.638 1.00 0.00

ATOM 803 OE2 GLU A 179 28.083 21.575 -12.321 1.00 0.00

ATOM 804 N ASN A 180 27.091 16.653 -9.670 1.00 0.00

ATOM 805 CA ASN A 180 26.030 15.826 -10.214 1.00 0.00

ATOM 806 C ASN A 180 25.056 15.473 -9.080 1.00 0.00

ATOM 807 O ASN A 180 23.857 15.714 -9.200 1.00 0.00

ATOM 808 CB ASN A 180 26.606 14.539 -10.809 1.00 0.00

ATOM 809 CG ASN A 180 27.338 14.777 -12.115 1.00 0.00

ATOM 810 ODl ASN A 180 27.178 15.823 -12.745 1.00 0.00

ATOM 811 ND2 ASN A 180 28.146 13.807 -12.524 1.00 0.00 ATOM 812 N ASP A 181 25.558 14.928 -7.978 1.00 0.00

ATOM 813 CA ASP A 181 24.677 14.556 -6.861 1.00 0.00

ATOM 814 C ASP A 181 23.783 15.691 -6.380 1.00 0.00

ATOM 815 O ASP A 181 22.606 15.478 -6.101 1.00 0.00

ATOM 816 CB ASP A 181 25.503 14.106 -5.654 1.00 0.00

ATOM 817 CG ASP A 181 26.137 12.744 -5.858 1.00 0.00

ATOM 818 ODl ASP A 181 25.761 12.052 -6.828 1.00 0.00

ATOM 819 OD2 ASP A 181 27.011 12.369 -5.048 1.00 0.00

ATOM 820 N ILE A 182 24.322 16.894 -6.265 1.00 0.00

ATOM 821 CA ILE A 182 23.482 17.992 -5.808 1.00 0.00

ATOM 822 C ILE A 182 22.411 18.305 -6.849 1.00 0.00

ATOM 823 O ILE A 182 21.311 18.725 -6.494 1.00 0.00

ATOM 824 CB ILE A 182 24.305 19.271 -5.569 1.00 0.00

ATOM 825 CGl ILE A 182 25.243 19.087 -4.374 1.00 0.00

ATOM 826 CG2 ILE A 182 23.387 20.450 -5.284 1.00 0.00

ATOM 827 CDl ILE A 182 26.269 20.189 -4.228 1.00 0.00

ATOM 828 N HIS A 183 22.723 18.115 -8.133 1.00 0.00

ATOM 829 CA HIS A 183 21.733 18.406 -9.168 1.00 0.00

ATOM 830 C HIS A 183 20.617 17.407 -9.026 1.00 0.00

ATOM 831 O HIS A 183 19.443 17.774 -8.948 1.00 0.00

ATOM 832 CB HIS A 183 22.362 18.289 -10.559 1.00 0.00

ATOM 833 CG HIS A 183 21.402 18.544 -11.679 1.00 0.00

ATOM 834 NDl HIS A 183 20.918 19.799 -11.975 1.00 0.00

ATOM 835 CD2 HIS A 183 20.741 17.726 -12.686 1.00 0.00

ATOM 836 CEl HIS A 183 20.082 19.711 -13.024 1.00 0.00

ATOM 837 NE2 HIS A 183 19.972 18.470 -13.456 1.00 0.00

ATOM 838 N GLY A 184 20.996 16.136 -8.995 1.00 0.00

ATOM 839 CA GLY A 184 20.007 15.083 -8.888 1.00 0.00

ATOM 840 C GLY A 184 19.125 15.268 -7.674 1.00 0.00

ATOM 841 O GLY A 184 17.908 15.406 -7.785 1.00 0.00

ATOM 842 N LEU A 185 19.747 15.267 -6.506 1.00 0.00

ATOM 843 CA LEU A 185 19.007 15.450 -5.277 1.00 0.00

ATOM 844 C LEU A 185 18.075 16.644 -5.427 1.00 0.00

ATOM 845 O LEU A 185 16.901 16.544 -5.108 1.00 0.00

ATOM 846 CB LEU A 185 19.962 15.704 -4.109 1.00 0.00

ATOM 847 CG LEU A 185 19.314 15.926 -2.740 1.00 0.00

ATOM 848 CDl LEU A 185 18.554 14.685 -2.298 1.00 0.00

ATOM 849 CD2 LEU A 185 20.370 16.234 -1.690 1.00 0.00

ATOM 850 N ARG A 186 18.581 17.759 -5.942 1.00 0.00

ATOM 851 CA ARG A 186 17.740 18.937 -6.131 1.00 0.00

ATOM 852 C ARG A 186 16.477 18.615 -6.940 1.00 0.00

ATOM 853 O ARG A 186 15.366 19.005 -6.572 1.00 0.00

ATOM 854 CB ARG A 186 18.506 20.028 -6.882 1.00 0.00

ATOM 855 CG ARG A 186 17.742 21.332 -7.031 1.00 0.00

ATOM 856 CD ARG A 186 18.505 22.324 -7.894 1.00 0.00

ATOM 857 NE ARG A 186 18.615 21.872 -9.279 1.00 0.00

ATOM 858 CZ ARG A 186 17.635 21.957 -10.172 1.00 0.00

ATOM 859 NHl ARG A 186 17.826 21.521 -11.410 1.00 0.00

ATOM 860 NH2 ARG A 186 16.465 22.478 -9.827 1.00 0.00

ATOM 861 N LYS A 187 16.663 17.917 -8.055 1.00 0.00

ATOM 862 CA LYS A 187 15.546 17.537 -8.904 1.00 0.00

ATOM 863 C LYS A 187 14.546 16.808 -8.023 1.00 0.00

ATOM 864 O LYS A 187 13.402 17.239 -7.865 1.00 0.00

ATOM 865 CB LYS A 187 16.020 16.623 -10.035 1.00 0.00

ATOM 866 CG LYS A 187 14.923 16.216 -11.005 1.00 0.00

ATOM 867 CD LYS A 187 15.471 15.350 -12.128 1.00 0.00

ATOM 868 CE LYS A 187 14.368 14.915 -13.079 1.00 0.00

ATOM 869 NZ LYS A 187 14.894 14.087 -14.199 1.00 0.00

ATOM 870 N VAL A 188 14.999 15.719 -7.421 1.00 0.00

ATOM 871 CA VAL A 188 14.143 14.934 -6.547 1.00 0.00

ATOM 872 C VAL A 188 13.429 15.725 -5.488 1.00 0.00

ATOM 873 O VAL A 188 12.241 15.516 -5.264 1.00 0.00

ATOM 874 CB VAL A 188 14.945 13.858 -5.790 1.00 0.00

ATOM 875 CGl VAL A 188 14.077 13.194 -4.732 1.00 0.00

ATOM 876 CG2 VAL A 188 15.437 12.786 -6.750 1.00 0.00

ATOM 877 N ILE A 189 14.136 16.624 -4.822 1.00 0.00

ATOM 878 CA ILE A 189 13.471 17.401 -3.799 1.00 0.00

ATOM 879 C ILE A 189 12.303 18.127 -4.428 1.00 0.00 ATOM 880 O ILE A 189 11.234 18.201 -3.847 1.00 0.00

ATOM 881 CB ILE A 189 14.421 18.437 -3.170 1.00 0.00

ATOM 882 CGl ILE A 189 15.516 17.734 -2.364 1.00 0.00

ATOM 883 CG2 ILE A 189 13.656 19.364 -2.238 1.00 0.00

ATOM 884 CDl ILE A 189 16.640 18.650 -1.932 1.00 0.00

ATOM 885 N ASP A 190 12.512 18.639 -5.635 1.00 0.00

ATOM 886 CA ASP A 190 11.468 19.373 -6.325 1.00 0.00

ATOM 887 C ASP A 190 10.257 18.502 -6.655 1.00 0.00

ATOM 888 O ASP A 190 9.115 18.845 -6.339 1.00 0.00

ATOM 889 CB ASP A 190 11.994 19.940 -7.646 1.00 0.00

ATOM 890 CG ASP A 190 12.945 21.103 -7.443 1.00 0.00

ATOM 891 ODl ASP A 190 13.013 21.624 -6.310 1.00 0.00

ATOM 892 OD2 ASP A 190 13.622 21.493 -8.418 1.00 0.00

ATOM 893 N ASP A 191 10.519 17.378 -7.302 1.00 0.00

ATOM 894 CA ASP A 191 9.466 16.439 -7.662 1.00 0.00

ATOM 895 C ASP A 191 8.663 16.088 -6.414 1.00 0.00

ATOM 896 O ASP A 191 7.428 15.994 -6.440 1.00 0.00

ATOM 897 CB ASP A 191 10.065 15.160 -8.249 1.00 0.00

ATOM 898 CG ASP A 191 10.622 15.365 -9.644 1.00 0.00

ATOM 899 ODl ASP A 191 10.347 16.425 -10.244 1.00 0.00

ATOM 900 OD2 ASP A 191 11.334 14.464 -10.138 1.00 0.00

ATOM 901 N THR A 192 9.360 15.919 -5.304 1.00 0.00

ATOM 902 CA THR A 192 8.652 15.527 -4.110 1.00 0.00

ATOM 903 C THR A 192 7.821 16.655 -3.534 1.00 0.00

ATOM 904 O THR A 192 6.786 16.398 -2.929 1.00 0.00

ATOM 905 CB THR A 192 9.622 15.076 -3.002 1.00 0.00

ATOM 906 OGl THR A 192 10.370 13.939 -3.451 1.00 0.00

ATOM 907 CG2 THR A 192 8.854 14.695 -1.744 1.00 0.00

ATOM 908 N ASN A 193 8.241 17.899 -3.716 1.00 0.00

ATOM 909 CA ASN A 193 7.427 18.990 -3.198 1.00 0.00

ATOM 910 C ASN A 193 6.121 19.057 -3.996 1.00 0.00

ATOM 911 O ASN A 193 5.044 19.237 -3.433 1.00 0.00

ATOM 912 CB ASN A 193 8.169 20.321 -3.331 1.00 0.00

ATOM 913 CG ASN A 193 9.309 20.455 -2.340 1.00 0.00

ATOM 914 ODl ASN A 193 9.338 19.772 -1.317 1.00 0.00

ATOM 915 ND2 ASN A 193 10.255 21.336 -2.644 1.00 0.00

ATOM 916 N ILE A 194 6.212 18.924 -5.316 1.00 0.00

ATOM 917 CA ILE A 194 4.996 18.935 -6.131 1.00 0.00

ATOM 918 C ILE A 194 4.063 17.853 -5.627 1.00 0.00

ATOM 919 O ILE A 194 2.900 18.108 -5.300 1.00 0.00

ATOM 920 CB ILE A 194 5.310 18.670 -7.615 1.00 0.00

ATOM 921 CGl ILE A 194 6.114 19.830 -8.206 1.00 0.00

ATOM 922 CG2 ILE A 194 4.022 18.520 -8.413 1.00 0.00

ATOM 923 CDl ILE A 194 6.712 19.530 -9.562 1.00 0.00

ATOM 924 N THR A 195 4.572 16.630 -5.611 1.00 0.00

ATOM 925 CA THR A 195 3.792 15.483 -5.172 1.00 0.00

ATOM 926 C THR A 195 3.097 15.747 -3.848 1.00 0.00

ATOM 927 O THR A 195 1.916 15.434 -3.679 1.00 0.00

ATOM 928 CB THR A 195 4.677 14.238 -4.982 1.00 0.00

ATOM 929 OGl THR A 195 5.295 13.892 -6.228 1.00 0.00

ATOM 930 CG2 THR A 195 3.843 13.059 -4.503 1.00 0.00

ATOM 931 N ARG A 196 3.840 16.318 -2.906 1.00 0.00

ATOM 932 CA ARG A 196 3.277 16.616 -1.595 1.00 0.00

ATOM 933 C ARG A 196 2.128 17.591 -1.688 1.00 0.00

ATOM 934 O ARG A 196 1.094 17.413 -1.062 1.00 0.00

ATOM 935 CB ARG A 196 4.340 17.231 -0.682 1.00 0.00

ATOM 936 CG ARG A 196 3.857 17.512 0.731 1.00 0.00

ATOM 937 CD ARG A 196 4.931 18.206 1.553 1.00 0.00

ATOM 938 NE ARG A 196 5.228 19.544 1.048 1.00 0.00

ATOM 939 CZ ARG A 196 4.466 20.611 1.268 1.00 0.00

ATOM 940 NHl ARG A 196 4.815 21.789 0.768 1.00 0.00

ATOM 941 NH2 ARG A 196 3.358 20.499 1.986 1.00 0.00

ATOM 942 N LEU A 197 2.314 18.644 -2.465 1.00 0.00

ATOM 943 CA LEU A 197 1.273 19.641 -2.580 1.00 0.00

ATOM 944 C LEU A 197 0.011 19.071 -3.212 1.00 0.00

ATOM 945 O LEU A 197 -1.116 19.359 -2.795 1.00 0.00

ATOM 946 CB LEU A 197 1.743 20.809 -3.449 1.00 0.00

ATOM 947 CG LEU A 197 2.832 21.703 -2.853 1.00 0.00 ATOM 948 CDl LEU A 197 3.331 22.704 883 .00 0.00

ATOM 949 CD2 LEU A 197 >97 22.478 658 .00 0.00

ATOM 950 N GLN A 198 >23 18.254 226 .00 0.00

ATOM 951 CA GLN A 198 -0.871 17.648 947 .00 0.00

ATOM 952 C GLN A 198 -1.656 16.796 946 .00 0.00

ATOM 953 O GLN A 198 -2.885 16.829 906 .00 0.00

ATOM 954 CB GLN A 198 -0.343 16.770 -6.083 .00 0.00

ATOM 955 CG GLN A 198 0.270 17.549 -7.236 .00 0.00

ATOM 956 CD GLN A 198 0.883 16.646 -8.288 .00 0.00

ATOM 957 OEl GLN A 198 0.934 15.428 -8.121 .00 0.00

ATOM 958 NE2 GLN A 198 1.351 17.244 -9.378 .00 0.00

ATOM 959 N LEU A 199 -0.940 16.076 -3.093 .00 0.00

ATOM 960 CA LEU A 199 -1.612 15.262 -2.109 .00 0.00

ATOM 961 C LEU A 199 -2.320 16.097 -1 042 .00 0.00

ATOM 962 O LEU A 199 -3.429 15.749 0.638 .00 0.00

ATOM 963 CB LEU A 199 -0.612 14.356 1.389 .00 0.00

ATOM 964 CG LEU A 199 0.009 13.234 2.224 .00 0.00

ATOM 965 CDl LEU A 199 1.109 12.529 1.446 .00 0.00

ATOM 966 CD2 LEU A 199 -1.042 12.201 2.603 .00 0.00

ATOM 967 N GLU A 200 -1.736 17.197 0.578 1.00 0.00

ATOM 968 CA GLU A 200 -2.453 17.974 0.438 1.00 0.00

ATOM 969 C GLU A 200 -3.801 18.419 0.121 1..00 0.00

ATOM 970 O GLU A 200 -4.811 18.4: 0.577 1..00 0.00

ATOM 971 CB GLU A 200 -1.645 19.213 0.833 1..00 0.00

ATOM 972 CG GLU A 200 -0.394 18.906 1.640 1.00 0.00

ATOM 973 CD GLU A 200 0.444 20.140 1.908 1.00 0.00

ATOM 974 OEl GLU A 200 0.085 1.399 1.00 0.00

ATOM 975 OE2 GLU A 200 1.460 20.025 9 626 1.00 0.00

ATOM 976 N THR A 201 -3.805 18.767 -1.402 1.00 0.00

ATOM 977 CA THR A 201 -5.015 19.187 _ 9 087 1.00 0.00

ATOM 978 C THR A 201 -6.013 18.030 -2.188 1..00 0.00

ATOM 979 O THR A 201 -7.157 18.146 -1.742 1..00 0.00

ATOM 980 CB THR A 201 -4.715 19.674 -3.517 1.00 0.00

ATOM 981 OGl THR A 201 -3.862 20.823 -3.464 1.00 0.00

ATOM 982 CG2 THR A 201 -6.003 20.050 -4.233 1.00 0.00

ATOM 983 N GLU A 202 -5.578 16.920 -2.797 1.00 0.00

ATOM 984 CA GLU A 202 -6.429 15.731 _ 9 954 1.00 0.00

ATOM 985 C GLU A 202 -7.030 15.328 -1.615 1.00 0.00

ATOM 986 O GLU A 202 -8.215 15.022 -1.518 1..00 0.00

ATOM 987 CB GLU A 202 -5.613 14.554 3.492 1..00 0.00

ATOM 988 CG GLU A 202 -5.221 14.689 4.955 1.00 0.00

ATOM 989 CD GLU A 202 -4.349 13.544 -5 432 1.00 0.00

ATOM 990 OEl GLU A 202 -3.986 12.687 4.599 1.00 0.00

ATOM 991 OE2 GLU A 202 -4.030 13.503 6.639 1.00 0.00

ATOM 992 N ILE A 203 -6.196 15.344 0.586 1.00 0.00

ATOM 993 CA ILE A 203 -6.642 15.020 0.753 1.00 0.00

ATOM 994 C ILE A 203 -7.739 15. 209 1..00 0.00

ATOM 995 O ILE A 203 -8.770 15.548 705 1..00 0.00

ATOM 996 CB ILE A 203 -5.488 15.106 768 1..00 0.00

ATOM 997 CGl ILE A 203 -4.461 14.004 503 1.00 0.00

ATOM 998 CG2 ILE A 203 -6.013 14.945 3.186 1.00 0.00

ATOM 999 CDl ILE A 203 -3.169 14.174 2.272 1.00 0.00

ATOM 1000 N GLU A 204 -7.549 17.293 1.066 1.00 0.00

ATOM 1001 CA GLU A 204 -8.625 18.179 1.499 1.00 0.00

ATOM 1002 C GLU A 204 -9.930 17.904 0.746 1.00 0.00

ATOM 1003 O GLU A 204 -10.998 17. 1.345 1..00 0.00

ATOM 1004 CB GLU A 204 -8.247 19.641 1.255 1..00 0.00

ATOM 1005 CG GLU A 204 -7.157 20.162 2.177 1.00 0.00

ATOM 1006 CD GLU A 204 -6.722 21.571 1.826 1.00 0.00

ATOM 1007 OEl GLU A 204 -7.220 22.113 0.817 1.00 0.00

ATOM 1008 OE2 GLU A 204 -5.882 22.135 2.560 1.00 0.00

ATOM 1009 N ALA A 205 -9.846 17.667 0.561 1.00 0.00

ATOM 1010 CA ALA A 205 -11.048 17.412 -1 338 1.00 0.00

ATOM 1011 C ALA A 205 -11.766 16.187 0.782 00 0.00

ATOM 1012 O ALA A 205 -I! ,978 16.214 0.552 00 0.00

ATOM 1013 CB ALA A 205 -10.693 17.157 2.796 00 0.00

ATOM 1014 N LEU A 206 -11.002 15.132 -0 526 00 0.00

ATOM 1015 CA LEU A 206 -11.573 13.891 -0.019 1.00 0.00 ATOM 1016 C LEU A 206 -12.158 14.056 1.365 .00 0.00

ATOM 1017 O LEU A 206 -13.236 13.549 1.638 .00 0.00

ATOM 1018 CB LEU A 206 -10.501 .801 0.061 .00 0.00

ATOM 1019 CG LEU A 206 -9.969 .275 -1 74 .00 0.00

ATOM 1020 CDl LEU A 206 -8.793 11.335 -1.051 .00 0.00

ATOM 1021 CD2 LEU A 206 -11.052 11.512 -2.021 .00 0.00

ATOM 1022 N LYS A 207 -11.452 14.778 2.226 .00 0.00

ATOM 1023 CA LYS A 207 -11.915 15.052 3.584 .00 0.00

ATOM 1024 C LYS A 207 -13. 264 15.769 3.566 .00 0.00

ATOM 1025 O LYS A 207 -14.162 15.474 4.353 .00 0.00

ATOM 1026 CB LYS A 207 -10.911 15.940 4.323 .00 0.00

ATOM 1027 CG LYS A 207 -11.291 16.240 5.764 .00 0.00

ATOM 1028 CD LYS A 207 -10.215 17.057 6.460 .00 0.00

ATOM 1029 CE LYS A 207 -10.609 17.383 7.892 .00 0.00

ATOM 1030 NZ LYS A 207 -9.570 18.197 8.582 .00 0.00

ATOM 1031 N GLU A 208 -13.374 16.733 2.657 .00 0.00

ATOM 1032 CA GLU A 208 -14.593 17.507 2.502 .00 0.00

ATOM 1033 C GLU A 208 -15.735 16.586 .054 .00 0.00

ATOM 1034 O GLU A 208 -16.838 16.629 .601 .00 0.00

ATOM 1035 CB GLU A 208 -14.401 18.605 .453 .00 0.00

ATOM 1036 CG GLU A 208 -13.487 19.735 .897 .00 0.00

ATOM 1037 CD GLU A 208 -13.211 20.730 0.788 1..00 0.00

ATOM 1038 OEl GLU A 208 -13.668 20.494 -0.350 1..00 0.00

ATOM 1039 OE2 GLU A 208 -12.537 21.748 1.057 1..00 0.00

ATOM 1040 N GLU A 209 -15.468 15.742 1.059 1.00 0.00

ATOM 1041 CA GLU A 209 -16.490 14.815 0.577 1.00 0.00

ATOM 1042 C GLU A 209 -16.938 13.902 .693 1.00 0.00

ATOM 1043 O GLU A 209 -18.122 13.625 .854 1.00 0.00

ATOM 1044 CB GLU A 209 -15.940 13.956 -0.562 1.00 0.00

ATOM 1045 CG GLU A 209 -15.711 14.715 -1.859 1.00 0.00

ATOM 1046 CD GLU A 209 -15.051 13.863 -2. .926 1..00 0.00

ATOM 1047 OEl GLU A 209 -14.706 12.700 -2..627 1..00 0.00

ATOM 1048 OE2 GLU A 209 -14. 14.357 -4.059 1.00 0.00

ATOM 1049 N LEU A 210 -15.974 13.412 2.449 1.00 0.00

ATOM 1050 CA LEU A 210 -16. 180 12.530 3.547 1.00 0.00

ATOM 1051 C LEU A 210 -17. 111 13. 224 4.544 1.00 0.00

ATOM 1052 O LEU A 210 -18.195 12.649 4.998 1.00 0.00

ATOM 1053 CB LEU A 210 -15.000 12.124 4.280 1.00 0.00

ATOM 1054 CG LEU A 210 -15.174 11.196 5.485 1..00 0.00

ATOM 1055 CDl LEU A 210 -15.789 9.872 5.059 1..00 0.00

ATOM 1056 CD2 LEU A 210 -13.832 10.909 6.140 1.00 0.00

ATOM 1057 N LEU A 211 -16.891 14.469 4.878 1.00 0.00

ATOM 1058 CA LEU A 211 -17.712 15.260 .795 1.00 0.00

ATOM 1059 C LEU A 211 -19.133 15.412 151 1.00 0.00

ATOM 1060 O LEU A 211 -20.125 15.227 .963 1.00 0.00

ATOM 1061 CB LEU A 211 -17.114 16.656 .981 1.00 0.00

ATOM 1062 CG LEU A 211 -17.882 17.604 .905 1. .00 0.00

ATOM 1063 CDl LEU A 211 -17.945 17.043 8.318 1..00 0.00

ATOM 1064 CD2 LEU A 211 -17.202 18.964 6.965 1..00 0.00

ATOM 1065 N PHE A 212 -19.210 15.772 3.967 1.00 0.00

ATOM 1066 CA PHE A 212 -20.481 15.968 3.273 1.00 0.00

ATOM 1067 C PHE A 212 -21.334 14.712 3.349 1..00 0.00

ATOM 1068 O PHE A 212 -22.539 14.796 3.570 1..00 0.00

ATOM 1069 CB PHE A 212 -20.241 16.298 1.799 1.00 0.00

ATOM 1070 CG PHE A 212 -19.626 17.651 1.573 1.00 0.00

ATOM 1071 CDl PHE A 91 9 -19.615 18.599 2.580 1.00 0.00

ATOM 1072 CD2 PHE A -19.059 17.973 0.352 1.00 0.00

ATOM 1073 CEl PHE A 212 -19.050 19.843 2.372 1.00 0.00

ATOM 1074 CE2 PHE A 212 -18.494 19.217 0.144 1.00 0.00

ATOM 1075 CZ PHE A 212 -18.488 20.150 1.148 1..00 0.00

ATOM 1076 N MET A 213 -20.713 13.549 3.164 1..00 0.00

ATOM 1077 CA MET A 213 -21.448 12.293 3.215 1.00 0.00

ATOM 1078 C MET A 213 -21.927 11.969 4.605 1.00 0.00

ATOM 1079 O MET A 213 -23.003 11.416 4.762 00 0.00

ATOM 1080 CB MET A 213 -20.561 11.135 2.752 00 0.00

ATOM 1081 CG MET A 213 -20.227 11.163 1.269 00 0.00

ATOM 1082 SD MET A 213 -21.692 11.063 0.223 00 0.00

ATOM 1083 CE MET A 213 -22.225 9.383 0.548 1.00 0.00 ATOM 1084 N LYS A 214 21.135 12.283 5.624 1.00 0.00

ATOM 1085 CA LYS A 214 21.580 11.986 6.974 1.00 0.00

ATOM 1086 C LYS A 214 22.830 12.805 7.227 1.00 0.00

ATOM 1087 O LYS A 214 23.811 12.304 7.774 1.00 0.00

ATOM 1088 CB LYS A 214 20.495 12.354 7.988 1.00 0.00

ATOM 1089 CG LYS A 214 19.276 11.447 7.952 1.00 0.00

ATOM 1090 CD LYS A 214 18.243 11.868 8.984 1.00 0.00

ATOM 1091 CE LYS A 214 17.014 10.975 8.931 1.00 0.00

ATOM 1092 NZ LYS A 214 15.980 11.397 9.915 1.00 0.00

ATOM 1093 N LYS A 215 22.797 14.065 6.806 1.00 0.00

ATOM 1094 CA LYS A 215 23.941 14.942 6.996 1.00 0.00

ATOM 1095 C LYS A 215 25.158 14.403 6.242 1.00 0.00

ATOM 1096 O LYS A 215 26.232 14.227 6.830 1.00 0.00

ATOM 1097 CB LYS A 215 23.633 16.346 6.474 1.00 0.00

ATOM 1098 CG LYS A 215 24.763 17.343 6.670 1.00 0.00

ATOM 1099 CD LYS A 215 24.364 18.731 6.196 1.00 0.00

ATOM 1100 CE LYS A 215 25.511 19.717 6.346 1.00 0.00

ATOM 1101 NZ LYS A 215 25.141 21.076 5.862 1.00 0.00

ATOM 1102 N ASN A 216 24.997 14.108 4.956 1.00 0.00

ATOM 1103 CA ASN A 216 26.110 13.573 4.180 1.00 0.00

ATOM 1104 C ASN A 216 26.660 12.299 4.827 1.00 0.00

ATOM 1105 O ASN A 216 27.878 12.116 4.924 1.00 0.00

ATOM 1106 CB ASN A 216 25.659 13.233 2.758 1.00 0.00

ATOM 1107 CG ASN A 216 25.424 14.467 1.911 1.00 0.00

ATOM 1108 ODl ASN A 216 25.923 15.549 2.221 1.00 0.00

ATOM 1109 ND2 ASN A 216 24.660 14.309 0.836 1.00 0.00

ATOM 1110 N HIS A 217 25.755 11.438 5.291 1.00 0.00

ATOM 1111 CA HIS A 217 26.156 10.205 5.956 1.00 0.00

ATOM 1112 C HIS A 217 27.083 10.593 7.089 1.00 0.00

ATOM 1113 O HIS A 217 28.252 10.245 7.059 1.00 0.00

ATOM 1114 CB HIS A 217 24.931 9.470 6.504 1.00 0.00

ATOM 1115 CG HIS A 217 25.265 8.230 7.273 1.00 0.00

ATOM 1116 NDl HIS A 217 25.636 7.052 6.664 1.00 0.00

ATOM 1117 CD2 HIS A 217 25.318 7.865 8.683 1.00 0.00

ATOM 1118 CEl HIS A 217 25.872 6.124 7.608 1.00 0.00

ATOM 1119 NE2 HIS A 217 25.683 6.605 8.822 1.00 0.00

ATOM 1120 N GLU A 218 26.570 11.323 8.079 1.00 0.00

ATOM 1121 CA GLU A 218 27.394 11.760 9.211 1.00 0.00

ATOM 1122 C GLU A 218 28.771 12.190 8.736 1.00 0.00

ATOM 1123 O GLU A 218 29.798 11.667 9.183 1.00 0.00

ATOM 1124 CB GLU A 218 26.738 12.943 9.925 1.00 0.00

ATOM 1125 CG GLU A 218 27.460 13.384 11.188 1.00 0.00

ATOM 1126 CD GLU A 218 26.712 14.466 11.940 1.00 0.00

ATOM 1127 OEl GLU A 218 25.629 14.876 11.470 1.00 0.00

ATOM 1128 OE2 GLU A 218 27.206 14.904 13.000 1.00 0.00

ATOM 1129 N GLU A 219 28.784 13.164 7.837 1.00 0.00

ATOM 1130 CA GLU A 219 30.034 13.673 7.300 1.00 0.00

ATOM 1131 C GLU A 219 30.981 12.542 6.903 1.00 0.00

ATOM 1132 O GLU A 219 32.176 12.582 7.201 1.00 0.00

ATOM 1133 CB GLU A 219 29.776 14.524 6.055 1.00 0.00

ATOM 1134 CG GLU A 219 31.028 15.146 5.458 1.00 0.00

ATOM 1135 CD GLU A 219 30.725 16.033 4.266 1.00 0.00

ATOM 1136 OEl GLU A 219 29.534 16.178 3.920 1.00 0.00

ATOM 1137 OE2 GLU A 219 31.680 16.581 3.676 1.00 0.00

ATOM 1138 N GLU A 220 30.440 11.522 6.247 1.00 0.00

ATOM 1139 CA GLU A 220 31.249 10.395 5.793 1.00 0.00

ATOM 1140 C GLU A 220 31.703 9.468 6.905 1.00 0.00

ATOM 1141 O GLU A 220 32.845 9.016 6.913 1.00 0.00

ATOM 1142 CB GLU A 220 30.461 9.534 4.804 1.00 0.00

ATOM 1143 CG GLU A 220 30.226 10.195 3.456 1.00 0.00

ATOM 1144 CD GLU A 220 31.518 10.575 2.761 1.00 0.00

ATOM 1145 OEl GLU A 220 32.396 9.699 2.620 1.00 0.00

ATOM 1146 OE2 GLU A 220 31.652 11.749 2.356 1.00 0.00

ATOM 1147 N VAL A 221 30.805 9.164 7.830 1.00 0.00

ATOM 1148 CA VAL A 221 31.188 8.268 8.904 1.00 0.00

ATOM 1149 C VAL A 221 32.277 8.979 9.702 1.00 0.00

ATOM 1150 O VAL A 221 33.124 8.350 10.345 1.00 0.00

ATOM 1151 CB VAL A 221 29.995 7.942 9.820 1.00 0.00 ATOM 1152 CGl VAL A 221 -30.458 7.166 11.043 .00 0.00

ATOM 1153 CG2 VAL A 221 -28.967 7.102 9.079 .00 0.00

ATOM 1154 N LYS A 999 -32.278 10.304 9.649 .00 0.00

ATOM 1155 CA LYS A 222 -33.303 11.000 10.395 .00 0.00

ATOM 1156 C LYS A 222 -34.610 11.101 9.652 .00 0.00

ATOM 1157 O LYS A 999 -35.664 10.923 10.250 .00 0.00

ATOM 1158 CB LYS A 999 -3 856 12.429 10.714 .00 0.00

ATOM 1159 CG LYS A 222 -31.712 12.513 11.711 .00 0.00

ATOM 1160 CD LYS A 222 -31.360 13.959 12.025 .00 0.00

ATOM 1161 CE LYS A 999 -30.202 14.043 13.006 .00 0.00

ATOM 1162 NZ LYS A 999 -29.837 15.454 13.313 .00 0.00

ATOM 1163 N GLY A 223 -34.567 11.423 8.366 .00 0.00

ATOM 1164 CA GLY A 223 -35.816 11.506 7.633 .00 0.00

ATOM 1165 C GLY A 990 -36.517 10.166 7.821 .00 0.00

ATOM 1166 O GLY A 990 -37.737 10.115 7.933 .00 0.00

ATOM 1167 N LEU A 224 -35.726 9.097 7.892 .00 0.00

ATOM 1168 CA LEU A 224 -36.231 7.738 8.122 ,00 0.00

ATOM 1169 C LEU A 224 -36.864 7.658 9.524 .00 0.00

ATOM 1170 O LEU A 224 -38.022 7.263 9.703 .00 0.00

ATOM 1171 CB LEU A 224 -35.092 6.721 8.031 1.00 0.00

ATOM 1172 CG LEU A 224 -35.463 5.262 8.305 1.00 0.00

ATOM 1173 CDl LEU A 224 -36.459 4.758 7.272 1..00 0.00

ATOM 1174 CD2 LEU A 224 -34.229 4.374 8.248 1..00 0.00

ATOM 1175 N GLN A 225 -36.177 7.860 10.491 1..00 0.00

ATOM 1176 CA GLN A 225 -36.897 7.856 11.769 1.00 0.00

ATOM 1177 C GLN A 225 -38.259 8.511 11.617 1.00 0.00

ATOM 1178 O GLN A 225 -39.299 7.908 11.908 1.00 0.00

ATOM 1179 CB GLN A 225 -36.108 8.625 12.831 1.00 0.00

ATOM 1180 CG GLN A 225 -36.777 8.661 14.195 1.00 0.00

ATOM 1181 CD GLN A 225 -35.941 9.381 15.235 1.00 0.00

ATOM 1182 OEl GLN A 225 -34.927 10.000 14.911 1..00 0.00

ATOM 1183 NE2 GLN A 225 -36.363 9.300 16.492 1..00 0.00

ATOM 1184 N ALA A 226 -38.245 9.759 11.173 1.00 0.00

ATOM 1185 CA ALA A 226 -39.479 10.503 10.983 1.00 0.00

ATOM 1186 C ALA A 226 -40.534 9.671 10.258 1.00 0.00

ATOM 1187 O ALA A 226 -41.703 9.652 10.646 1.00 0.00

ATOM 1188 CB ALA A 226 -39.221 11.753 10.156 1.00 0.00

TER 1189 ALA A 226

ATOM 1190 N ASP A 244 -55.241 9.223 .450 1.00 0.00

ATOM 1191 CA ASP A 244 -56.540 9.711 .038 1.00 0.00

ATOM 1192 C ASP A 244 -57.515 8.559 11.747 1.00 0.00

ATOM 1193 O ASP A 244 -58.556 8.455 12.386 1.00 0.00

ATOM 1194 CB ASP A 244 -56.418 10.551 10.765 1..00 0.00

ATOM 1195 CG ASP A 244 -55.770 11.899 11.016 1..00 0.00

ATOM 1196 ODl ASP A 244 -55.598 12.264 12.199 1.00 0.00

ATOM 1197 OD2 ASP A 244 -55.435 12.590 10.032 1.00 0.00

ATOM 1198 N LEU A 245 -57.176 7.695 10.793 1.00 0.00

ATOM 1199 CA LEU A 245 -58.028 6.552 10.471 1.00 0.00

ATOM 1200 C LEU A 245 -58.407 718 11.677 1.00 0.00

ATOM 1201 O LEU A 245 -59.518 221 11.751 1.00 0.00

ATOM 1202 CB LEU A 245 -57.319 615 9.491 1.00 0.00

ATOM 1203 CG LEU A 245 -57.135 139 8.065 1..00 0.00

ATOM 1204 CDl LEU A 245 -56.276 185 7.249 1..00 0.00

ATOM 1205 CD2 LEU A 245 -58.479 283 7.368 1.00 0.00

ATOM 1206 N ALA A 246 -57.468 541 12.601 1.00 0.00

ATOM 1207 CA ALA A 246 -57.713 767 13.822 1.00 0.00

ATOM 1208 C ALA A 246 -58.774 5.411 14.688 1.00 0.00

ATOM 1209 O ALA A 246 -59.647 4.753 15.249 1.00 0.00

ATOM 1210 CB ALA A 246 -56.439 4.661 14.646 1.00 0.00

ATOM 1211 N LYS A 247 -58.632 6.713 14.854 1..00 0.00

ATOM 1212 CA LYS A 247 -59.543 7.497 15.662 1..00 0.00

ATOM 1213 C LYS A 247 -60.936 7.408 15.032 1.00 0.00

ATOM 1214 O LYS A 247 -61.920 7.078 15.705 1.00 0.00

ATOM 1215 CB LYS A 247 -59.093 8.959 15.713 00 0.00

ATOM 1216 CG LYS A 247 -59.972 9.849 16.575 00 0.00

ATOM 1217 CD LYS A 247 -59.430 11.268 16.636 00 0.00

ATOM 1218 CE LYS A 247 -60.335 12.170 17.460 00 0.00

ATOM 1219 NZ LYS A 247 -59.827 13.569 17.509 1.00 0.00 ATOM 1220 N ILE A 248 60.998 681 13..727 .00 0.00

ATOM 1221 CA ILE A 248 62.234 624 ,936 .00 0.00

ATOM 1222 C ILE A 248 62.898 281 13.129 .00 0.00

ATOM 1223 O ILE A 248 64.096 6.209 13.363 .00 0.00

ATOM 1224 CB ILE A 248 61.952 7.815 11.433 .00 0.00

ATOM 1225 CGl ILE A 248 61.475 9.242 11.158 .00 0.00

ATOM 1226 CG2 ILE A 248 63.212 7.561 10.619 .00 0.00

ATOM 1227 CDl ILE A 248 60.918 9.441 9.765 .00 0.00

ATOM 1228 N MET A 249 62.109 .224 12.976 .00 0.00

ATOM 1229 CA MET A 249 62.644 .882 13.132 .00 0.00

ATOM 1230 C MET A 249 63.163 .606 14.529 .00 0.00

ATOM 1231 O MET A 249 64.147 .889 14.687 .00 0.00

ATOM 1232 CB MET A 249 61.564 2.838 12, 840 .00 0.00

ATOM 1233 CG MET A 249 61.155 2.761 11, 378 .00 0.00

ATOM 1234 SD MET A 249 59.812 1.592 11, 093 .00 0.00

ATOM 1235 CE MET A 249 60.642 0.038 11.415 .00 0.00

ATOM 1236 N ALA A 250 -6, 510 4.158 15.548 ,00 0.00

ATOM 1237 CA ALA A 250 62.961 3.946 16.919 .00 0.00

ATOM 1238 C ALA A 250 64.348 4.553 17.033 .00 0.00

ATOM 1239 O ALA A 250 -65. 289 3.914 17.505 1.00 0.00

ATOM 1240 CB ALA A 250 -62.012 4.618 17.900 1.00 0.00

ATOM 1241 N ASP A 251 -64.473 5.793 16.579 1..00 0.00

ATOM 1242 CA ASP A 251 -65.760 6.442 16.633 1..00 0.00

ATOM 1243 C ASP A 251 -66.813 5.646 15.874 1..00 0.00

ATOM 1244 O ASP A 251 -67.872 5.349 16.430 1.00 0.00

ATOM 1245 CB ASP A 251 -65.683 7.838 16.012 1.00 0.00

ATOM 1246 CG ASP A 251 -64.934 8.824 16.886 1.00 0.00

ATOM 1247 ODl ASP A 251 -64.683 8.501 18.066 1.00 0.00

ATOM 1248 OD2 ASP A 251 -64.597 9.920 16.391 1.00 0.00

ATOM 1249 N ILE A 252 -66.530 5.233 14.639 1.00 0.00

ATOM 1250 CA ILE A 252 -67.551 4.492 13.912 1..00 0.00

ATOM 1251 C ILE A 252 -67.919 3.153 14.500 1..00 0.00

ATOM 1252 O ILE A 252 -69.076 2.778 14.429 1.00 0.00

ATOM 1253 CB ILE A 252 -67.110 4.193 12.467 1.00 0.00

ATOM 1254 CGl ILE A 9 R 9 -67.029 5.488 11.656 1.00 0.00

ATOM 1255 CG2 ILE A -68.103 3.262 11.790 1.00 0.00

ATOM 1256 CDl ILE A 252 -66.353 5.325 10.312 1.00 0.00

ATOM 1257 N ARG A 253 -66.969 2.416 15.076 1.00 0.00

ATOM 1258 CA ARG A 253 -67.342 1.127 15.635 1..00 0.00

ATOM 1259 C ARG A 253 -68.221 1.328 16.841 1..00 0.00

ATOM 1260 O ARG A 253 -69.090 0.508 17.123 1.00 0.00

ATOM 1261 CB ARG A 253 -66.097 0.345 16.059 1.00 0.00

ATOM 1262 CG ARG A 253 -65.258 0.161 14.898 1.00 0.00

ATOM 1263 CD ARG A 253 -63.996 0.855 15.388 1.00 0.00

ATOM 1264 NE ARG A 253 -63.173 -1 340 14.283 1.00 0.00

ATOM 1265 CZ ARG A 253 -61.961 1.865 14.429 1.00 0.00

ATOM 1266 NHl ARG A 253 -61.287 2.280 13.367 1..00 0.00

ATOM 1267 NH2 ARG A 253 -61.426 -1 972 15.638 1..00 0.00

ATOM 1268 N ALA A 254 -68.005 2.422 17.557 1..00 0.00

ATOM 1269 CA ALA A 254 -68.826 2.692 18.724 1.00 0.00

ATOM 1270 C ALA A 254 -70.236 2.992 18.230 1.00 0.00

ATOM 1271 O ALA A 254 -71 .221 2.441 18.720 1.00 0.00

ATOM 1272 CB ALA A 254 -68.278 3.884 19.493 1.00 0.00

ATOM 1273 N GLN A 255 -70.299 3.863 17.234 1.00 0.00

ATOM 1274 CA GLN A 255 -71.543 4.260 16.606 1.00 0.00

ATOM 1275 C GLN A 255 -72.308 3.049 16.040 1..00 0.00

ATOM 1276 O GLN A 255 -73.534 2.972 16.145 1..00 0.00

ATOM 1277 CB GLN A 255 -71.276 5.226 15.450 1.00 0.00

ATOM 1278 CG GLN A 255 -70.806 6.603 15.890 1.00 0.00

ATOM 1279 CD GLN A 255 -70.443 7.495 14.719 1.00 0.00

ATOM 1280 OEl GLN A 255 -70.455 7.060 13.567 1.00 0.00

ATOM 1281 NE2 GLN A 255 -70.118 8.749 15.011 1.00 0.00

ATOM 1282 N TYR A 256 -71.569 2.123 15.435 1.00 0.00

ATOM 1283 CA TYR A 256 -72.156 0.911 14.856 00 0.00

ATOM 1284 C TYR A 256 -72.725 0.081 15.983 00 0.00

ATOM 1285 O TYR A 256 -73.868 -0.349 15.921 00 0.00

ATOM 1286 CB TYR A 256 -71.092 0.105 14.109 00 0.00

ATOM 1287 CG TYR A 256 -71.611 -1.178 13.500 1.00 0.00 ATOM 1288 CDl TYR A 256 -72.330 160 12.312 .00 0.00

ATOM 1289 CD2 TYR A 256 -71.380 401 14.114 .00 0.00

ATOM 1290 CEl TYR A 256 -72.809 -2.327 11.747 .00 0.00

ATOM 1291 CE2 TYR A 256 -71.851 -3.579 13.565 .00 0.00

ATOM 1292 CZ TYR A 256 -72.570 -3.533 12.371 .00 0.00

ATOM 1293 OH TYR A 256 -73.045 -4.696 11.811 .00 0.00

ATOM 1294 N ASP A 257 -71.927 -0.168 17.012 .00 0.00

ATOM 1295 CA ASP A 257 -72.42 -0.939 18.139 .00 0.00

ATOM 1296 C ASP A 257 -73.752 -0.358 18.659 .00 0.00

ATOM 1297 O ASP A 257 -74.705 -1..093 18.919 .00 0.00

ATOM 1298 CB ASP A 257 -71.419 -0.926 19.288 .00 0.00

ATOM 1299 CG ASP A 257 -70.199 -1.780 19.001 .00 0.00

ATOM 1300 ODl ASP A 257 -70.234 -2.556 18.023 .00 0.00

ATOM 1301 OD2 ASP A 257 -69.209 -1 675 19.755 .00 0.00

ATOM 1302 N GLU A 258 -73.821 0.963 18.784 .00 0.00

ATOM 1303 CA GLU A 258 -75.046 1.612 19.249 .00 0.00

ATOM 1304 C GLU A 258 -76.209 1.353 18.302 ,00 0.00

ATOM 1305 O GLU A 258 -77.295 0.984 18.736 .00 0.00

ATOM 1306 CB GLU A 258 -74.847 126 19.345 .00 0.00

ATOM 1307 CG GLU A 258 -76.060 880 19.866 1.00 0.00

ATOM 1308 CD GLU A 258 -75.815 371 19.979 1.00 0.00

ATOM 1309 OEl GLU A 258 -74.690 814 19.663 1..00 0.00

ATOM 1310 OE2 GLU A 258 -76.746 098 20.384 1..00 0.00

ATOM 1311 N LEU A 259 -75.981 548 17.012 1..00 0.00

ATOM 1312 CA LEU A 259 -77.020 297 16.024 1.00 0.00

ATOM 1313 C LEU A 259 -77.563 0.109 16.130 1.00 0.00

ATOM 1314 O LEU A 259 -78.768 0.315 16.042 1.00 0.00

ATOM 1315 CB LEU A 259 -76.469 1.481 14.608 1.00 0.00

ATOM 1316 CG LEU A 259 -76.123 2.913 14.196 1.00 0.00

ATOM 1317 CDl LEU A 259 -75.423 2.931 12.846 1.00 0.00

ATOM 1318 CD2 LEU A 259 -77.381 3.761 14.090 1. .00 0.00

ATOM 1319 N ALA A 260 -76.664 1.075 16.287 1..00 0.00

ATOM 1320 CA ALA A 260 -77.045 2.474 16.407 1.00 0.00

ATOM 1321 C ALA A 260 -77.958 -2 668 17.606 1.00 0.00

ATOM 1322 O ALA A 260 -79.042 -3.245 17.495 1..00 0.00

ATOM 1323 CB ALA A 260 -75.811 -3.345 16.589 1..00 0.00

ATOM 1324 N ARG A 261 -77.533 -2.191 18.764 1.00 0.00

ATOM 1325 CA ARG A 261 -78.383 -2.329 19.930 1.00 0.00

ATOM 1326 C ARG A 261 -79.759 -1.737 19.602 1.00 0.00

ATOM 1327 O ARG A 261 -80.776 -2.411 19.756 1.00 0.00

ATOM 1328 CB ARG A 261 -77.780 -1.585 21.123 1.00 0.00

ATOM 1329 CG ARG A 261 -78.552 -1.763 22.420 1.00 0.00

ATOM 1330 CD ARG A 261 -77.975 -0.898 23.529 1..00 0.00

ATOM 1331 NE ARG A 261 -78.152 0.527 23.260 1..00 0.00

ATOM 1332 CZ ARG A 261 -79.294 1.185 23.436 1.00 0.00

ATOM 1333 NHl ARG A 261 -79.362 2.480 23.165 1.00 0.00

ATOM 1334 NH2 ARG A 261 -80.365 0.544 23.883 1.00 0.00

ATOM 1335 N LYS A 262 -79.804 -0.494 19.128 1.00 0.00

ATOM 1336 CA LYS A 262 -81.091 0.137 18.807 1.00 0.00

ATOM 1337 C LYS A 262 -81.960 -0.687 17.863 1.00 0.00

ATOM 1338 O LYS A 262 -83.168 -0.791 18.059 1.00 0.00

ATOM 1339 CB LYS A 262 -80.870 1.492 18.132 1..00 0.00

ATOM 1340 CG LYS A 262 -82.152 2.249 17.824 1..00 0.00

ATOM 1341 CD LYS A 262 -81.857 3.613 17.222 1.00 0.00

ATOM 1342 CE LYS A 262 -83.139 4.365 16.902 1.00 0.00

ATOM 1343 NZ LYS A 262 -82.864 5.704 16.313 1.00 0.00

TER 1344 LYS A 262

ATOM 1345 N TRP A 271 -93.071 0.196 18.145 1.00 0.00

ATOM 1346 CA TRP A 271 -94.235 0.504 17.338 1.00 0.00

ATOM 1347 C TRP A 271 -94.678 -1 919 17.599 1..00 0.00

ATOM 1348 O TRP A 271 -95.847 2 224 17.434 1..00 0.00

ATOM 1349 CB TRP A 271 -93.909 0.357 15.850 1.00 0.00

ATOM 1350 CG TRP A 271 -93.702 062 15.419 1.00 0.00

ATOM 1351 CDl TRP A 271 -93.944 186 16.155 00 0.00

ATOM 1352 CD2 TRP A 271 -93.209 511 14 ,150 00 0.00

ATOM 1353 NEl TRP A 271 -93.634 307 15 ,424 00 0.00

ATOM 1354 CE2 TRP A 271 -93.180 2.919 14.188 00 0.00

ATOM 1355 CE3 TRP A 271 -92.791 0.860 12.985 1.00 0.00 ATOM 1356 CZ2 TRP A 271 -92.748 3.687 13.108 1.00 0.00

ATOM 1357 CZ3 TRP A 271 -92.363 1.626 11.917 1.00 0.00

ATOM 1358 CH2 TRP A 271 -92.344 3.023 11.982 1.00 0.00

ATOM 1359 N SER A 272 -93.758 -2.800 18.043 1.00 0.00

ATOM 1360 CA SER A 272 -94.191 -4.129 18.448 1.00 0.00

ATOM 1361 C SER A 272 -95.153 -4.018 19.599 1.00 0.00

ATOM 1362 O SER A 272 -96.176 -4.686 19.601 1.00 0.00

ATOM 1363 CB SER A 272 -92.992 -4.973 18.886 1.00 0.00

ATOM 1364 OG SER A 272 -92.123 -5.229 17.795 1.00 0.00

ATOM 1365 N GLN A 273 -94.816 -3.145 20.573 1.00 0.00

ATOM 1366 CA GLN A 273 -95.708 -2.932 21.702 1.00 0.00

ATOM 1367 C GLN A 273 -97.044 -2.444 21.220 1.00 0.00

ATOM 1368 O GLN A 273 -98.058 -2.965 21.655 1.00 0.00

ATOM 1369 CB GLN A 273 -95.125 -1.889 22.658 1.00 0.00

ATOM 1370 CG GLN A 273 -93.910 -2.370 23.433 1.00 0.00

ATOM 1371 CD GLN A 273 -93.279 -1.273 24.268 1.00 0.00

ATOM 1372 OEl GLN A 273 -93.701 -0.118 24.213 1.00 0.00

ATOM 1373 NE2 GLN A 273 -92.265 -1.632 25.046 1.00 0.00

ATOM 1374 N GLN A 274 -97.032 -1.447 20.314 1.00 0.00

ATOM 1375 CA GLN A 274 -98.287 -0.927 19.794 1.00 0.00

ATOM 1376 C GLN A 274 -99.076 -2.015 19.121 1.00 0.00

ATOM 1377 O GLN A 274 -100.277 -2.103 19.324 1.00 0.00

ATOM 1378 CB GLN A 274 -98.025 0.179 18.771 1.00 0.00

ATOM 1379 CG GLN A 274 -97.491 1.468 19.374 1.00 0.00

ATOM 1380 CD GLN A 274 -97.137 2.501 18.322 1.00 0.00

ATOM 1381 OEl GLN A 274 -97.205 2.229 17.123 1.00 0.00

ATOM 1382 NE2 GLN A 274 -96.756 3.692 18.768 1.00 0.00

ATOM 1383 N ILE A 275 -98.381 -2.856 18.332 1.00 0.00

ATOM 1384 CA ILE A 275 -99.065 -3.946 17.656 1.00 0.00

ATOM 1385 C ILE A 275 -99.697 -4.874 18.655 1.00 0.00

ATOM 1386 O ILE A 275 -100.839 -5.259 18.461 1.00 0.00

ATOM 1387 CB ILE A 275 -98.094 -4.773 16.792 1.00 0.00

ATOM 1388 CGl ILE A 275 -97.591 -3.941 15.611 1.00 0.00

ATOM 1389 CG2 ILE A 275 -98.787 -6.012 16.249 1.00 0.00

ATOM 1390 CDl ILE A 275 -96.437 -4.576 14.865 1.00 0.00

ATOM 1391 N GLU A 276 -98.953 -5.221 19.725 1.00 0.00

ATOM 1392 CA GLU A 276 -99.503 -6.118 20.729 1.00 0.00

ATOM 1393 C GLU A 276 -100.807 -5.588 21.252 1.00 0.00

ATOM 1394 O GLU A 276 -101.773 -6.331 21.324 1.00 0.00

ATOM 1395 CB GLU A 276 -98.536 -6.265 21.905 1.00 0.00

ATOM 1396 CG GLU A 276 -99.021 -7.208 22.993 1.00 0.00

ATOM 1397 CD GLU A 276 -98.020 -7.360 24.121 1.00 0.00

ATOM 1398 OEl GLU A 276 -96.931 -6.754 24.035 1.00 0.00

ATOM 1399 OE2 GLU A 276 -98.323 -8.086 25.091 1.00 0.00

ATOM 1400 N GLU A 277 -100.823 -4.287 21.604 1.00 0.00

ATOM 1401 CA GLU A 277 -102.052 -3.691 22.098 1.00 0.00

ATOM 1402 C GLU A 277 -103.146 -3.820 21.076 1.00 0.00

ATOM 1403 O GLU A 277 -104.253 -4.191 21.427 1.00 0.00

ATOM 1404 CB GLU A 277 -101.844 -2.206 22.400 1.00 0.00

ATOM 1405 CG GLU A 277 -103.071 -1.509 22.966 1.00 0.00

ATOM 1406 CD GLU A 277 -102.817 -0.049 23.284 1.00 0.00

ATOM 1407 OEl GLU A 277 -101.677 0.416 23.074 1.00 0.00

ATOM 1408 OE2 GLU A 277 -103.759 0.631 23.744 1.00 0.00

ATOM 1409 N SER A 278 -102.818 -3.520 19.802 1.00 0.00

ATOM 1410 CA SER A 278 -103.822 -3.608 18.757 1.00 0.00

ATOM 1411 C SER A 278 -104.392 -4.996 18.663 1.00 0.00

ATOM 1412 O SER A 278 -105.602 -5.142 18.610 1.00 0.00

ATOM 1413 CB SER A 278 -103.213 -3.253 17.399 1.00 0.00

ATOM 1414 OG SER A 278 -102.829 -1.889 17.352 1.00 0.00

ATOM 1415 N THR A 279 -103.508 -6.013 18.648 1.00 0.00

ATOM 1416 CA THR A 279 -103.982 -7.382 18.533 1.00 0.00

ATOM 1417 C THR A 279 -104.932 -7.717 19.649 1.00 0.00

ATOM 1418 O THR A 279 -105.984 -8.278 19.390 1.00 0.00

ATOM 1419 CB THR A 279 -102.819 -8.389 18.590 1.00 0.00

ATOM 1420 OGl THR A 279 -101.930 -8.160 17.491 1.00 0.00

ATOM 1421 CG2 THR A 279 -103.345 -9.814 18.509 1.00 0.00

ATOM 1422 N THR A 280 -104.557 -7.354 20.892 1.00 0.00

ATOM 1423 CA THR A 280 -105.437 -7.636 22.014 1.00 0.00 ATOM 1424 C THR A 280 -106.751 -6.925 21.845 1.00 0.00

ATOM 1425 O THR A 280 -107.786 -7.519 22.099 1.00 0.00

ATOM 1426 CB THR A 280 -104.817 -7.175 23.347 1.00 0.00

ATOM 1427 OGl THR A 280 -103.596 -7.885 23.581 1.00 0.00

ATOM 1428 CG2 THR A 280 -105.772 -7.445 24.499 1.00 0.00

ATOM 1429 N VAL A 281 -106.701 -5.651 21.406 1.00 0.00

ATOM 1430 CA VAL A 281 -107.937 -4.910 21.207 1.00 0.00

ATOM 1431 C VAL A 281 -108.825 -5.621 20.225 1.00 0.00

ATOM 1432 O VAL A 281 -110.014 -5.735 20.474 1.00 0.00

ATOM 1433 CB VAL A 281 -107.665 -3.495 20.663 1.00 0.00

ATOM 1434 CGl VAL A 281 -108.968 -2.813 20.276 1.00 0.00

ATOM 1435 CG2 VAL A 281 -106.970 -2.643 21.714 1.00 0.00

ATOM 1436 N VAL A 282 -108.228 -6.109 19.118 1.00 0.00

ATOM 1437 CA VAL A 282 -109.004 -6.861 18.145 1.00 0.00

ATOM 1438 C VAL A 282 -109.720 -7.988 18.840 1.00 0.00

ATOM 1439 O VAL A 282 -110.897 -8.200 18.598 1.00 0.00

ATOM 1440 CB VAL A 282 -108.106 -7.458 17.045 1.00 0.00

ATOM 1441 CGl VAL A 282 -108.901 -8.408 16.164 1.00 0.00

ATOM 1442 CG2 VAL A 282 -107.534 -6.354 16.169 1.00 0.00

ATOM 1443 N THR A 283 -108.985 -8.689 19.725 1.00 0.00

ATOM 1444 CA THR A 283 -109.591 -9.779 20.469 1.00 0.00

ATOM 1445 C THR A 283 -110.752 -9.282 21.288 1.00 0.00

ATOM 1446 O THR A 283 -111.817 -9.873 21.232 1.00 0.00

ATOM 1447 CB THR A 283 -108.583 -10.435 21.431 1.00 0.00

ATOM 1448 OGl THR A 283 -107.496 -10.991 20.681 1.00 0.00

ATOM 1449 CG2 THR A 283 -109.251 -11.544 22.228 1.00 0.00

ATOM 1450 N THR A 284 -110.536 -8.187 22.044 1.00 0.00

ATOM 1451 CA THR A 284 -111.599 -7.680 22.896 1.00 0.00

ATOM 1452 C THR A 284 -112.802 -7.278 22.091 1.00 0.00

ATOM 1453 O THR A 284 -113.914 -7.567 22.502 1.00 0.00

ATOM 1454 CB THR A 284 -111.142 -6.444 23.692 1.00 0.00

ATOM 1455 OGl THR A 284 -110.049 -6.800 24.548 1.00 0.00

ATOM 1456 CG2 THR A 284 -112.282 -5.909 24.545 1.00 0.00

ATOM 1457 N GLN A 285 -112.575 -6.618 20.938 1.00 0.00

ATOM 1458 CA GLN A 285 -113.697 -6.210 20.111 1.00 0.00

ATOM 1459 C GLN A 285 -114.503 -7.409 19.703 1.00 0.00

ATOM 1460 O GLN A 285 -115.716 -7.392 19.839 1.00 0.00

ATOM 1461 CB GLN A 285 -113.203 -5.502 18.848 1.00 0.00

ATOM 1462 CG GLN A 285 -112.611 -4.125 19.100 1.00 0.00

ATOM 1463 CD GLN A 285 -112.013 -3.509 17.850 1.00 0.00

ATOM 1464 OEl GLN A 285 -111.965 -4.145 16.796 1.00 0.00

ATOM 1465 NE2 GLN A 285 -111.553 -2.270 17.964 1.00 0.00

ATOM 1466 N SER A 286 -113.810 -8.458 19.216 1.00 0.00

ATOM 1467 CA SER A 286 -114.513 -9.671 18.835 1.00 0.00

ATOM 1468 C SER A 286 -115.265 -10.228 20.011 1.00 0.00

ATOM 1469 O SER A 286 -116.394 -10.662 19.852 1.00 0.00

ATOM 1470 CB SER A 286 -113.525 -10.731 18.343 1.00 0.00

ATOM 1471 OG SER A 286 -112.899 -10.324 17.139 1.00 0.00

ATOM 1472 N ALA A 287 -114.627 -10.195 21.199 1.00 0.00

ATOM 1473 CA ALA A 287 -115.294 -10.686 22.391 1.00 0.00

ATOM 1474 C ALA A 287 -116.566 -9.924 22.637 1.00 0.00

ATOM 1475 O ALA A 287 -117.591 -10.531 22.901 1.00 0.00

ATOM 1476 CB ALA A 287 -114.395 -10.525 23.607 1.00 0.00

ATOM 1477 N GLU A 288 -116.489 -8.583 22.531 1.00 0.00

ATOM 1478 CA GLU A 288 -117.677 -7.774 22.746 1.00 0.00

ATOM 1479 C GLU A 288 -118.736 -8.109 21.736 1.00 0.00

ATOM 1480 O GLU A 288 -119.904 -8.163 22.086 1.00 0.00

ATOM 1481 CB GLU A 288 -117.342 -6.287 22.616 1.00 0.00

ATOM 1482 CG GLU A 288 -116.500 -5.739 23.757 1.00 0.00

ATOM 1483 CD GLU A 288 -116.085 -4.298 23.535 1.00 0.00

ATOM 1484 OEl GLU A 288 -116.393 -3.751 22.455 1.00 0.00

ATOM 1485 OE2 GLU A 288 -115.451 -3.715 24.441 1.00 0.00

ATOM 1486 N VAL A 289 -118.313 -8.348 20.479 1.00 0.00

ATOM 1487 CA VAL A 289 -119.279 -8.687 19.448 1.00 0.00

ATOM 1488 C VAL A 289 -119.995 -9.966 19.792 1.00 0.00

ATOM 1489 O VAL A 289 -121.209 -10.015 19.672 1.00 0.00

ATOM 1490 CB VAL A 289 -118.599 -8.881 18.079 1.00 0.00

ATOM 1491 CGl VAL A 289 -119.591 -9.427 17.064 1.00 0.00 ATOM 1492 CG2 VAL A 289 -118.060 -7.557 17.561 1.00 0.00

ATOM 1493 N GLY A 290 -119.241 -10.996 20.225 1.00 0.00

ATOM 1494 CA GLY A 290 -119.881 -12.260 20.550 1.00 0.00

ATOM 1495 C GLY A 290 -120.843 -12.113 21.696 1.00 0.00

ATOM 1496 O GLY A 290 -121.884 -12.750 21.689 1.00 0.00

ATOM 1497 N ALA A 291 -120.489 -11.262 22.679 1.00 0.00

ATOM 1498 CA ALA A 291 -121.388 -11.057 23.803 1.00 0.00

ATOM 1499 C ALA A 291 -122.663 -10.421 23.325 1.00 0.00

ATOM 1500 O ALA A 291 -123.737 -10.836 23.734 1.00 0.00

ATOM 1501 CB ALA A 291 -120.745 -10.147 24.837 1.00 0.00

ATOM 1502 N ALA A 292 -122.529 -9.415 22.436 1.00 0.00

ATOM 1503 CA ALA A 292 -123.713 -8.784 21.877 1.00 0.00

ATOM 1504 C ALA A 292 -124.524 -9.793 21.114 1.00 0.00

ATOM 1505 O ALA A 292 -125.743 -9.729 21.141 1.00 0.00

ATOM 1506 CB ALA A 292 -123.318 -7.660 20.930 1.00 0.00

ATOM 1507 N GLU A 293 -123.829 -10.733 20.442 1.00 0.00

ATOM 1508 CA GLU A 293 -124.531 -11.749 19.677 1.00 0.00

ATOM 1509 C GLU A 293 -125.423 -12.571 20.563 1.00 0.00

ATOM 1510 O GLU A 293 -126.588 -12.744 20.242 1.00 0.00

ATOM 1511 CB GLU A 293 -123.536 -12.691 18.998 1.00 0.00

ATOM 1512 CG GLU A 293 -124.185 -13.763 18.136 1.00 0.00

ATOM 1513 CD GLU A 293 -123.167 -14.656 17.453 1.00 0.00

ATOM 1514 OEl GLU A 293 -121.954 -14.428 17.643 1.00 0.00

ATOM 1515 OE2 GLU A 293 -123.583 -15.583 16.728 1.00 0.00

ATOM 1516 N THR A 294 -124.865 -13.072 21.685 1.00 0.00

ATOM 1517 CA THR A 294 -125.664 -13.889 22.583 1.00 0.00

ATOM 1518 C THR A 294 -126.886 -13.139 23.036 1.00 0.00

ATOM 1519 O THR A 294 -127.969 -13.702 23.035 1.00 0.00

ATOM 1520 CB THR A 294 -124.866 -14.293 23.837 1.00 0.00

ATOM 1521 OGl THR A 294 -123.730 -15.076 23.453 1.00 0.00

ATOM 1522 CG2 THR A 294 -125.735 -15.112 24.779 1.00 0.00

ATOM 1523 N THR A 295 -126.700 -11.856 23.406 1.00 0.00

ATOM 1524 CA THR A 295 -127.836 -11.057 23.832 1.00 0.00

ATOM 1525 C THR A 295 -128.867 -10.987 22.741 1.00 0.00

ATOM 1526 O THR A 295 -130.038 -11.216 23.001 1.00 0.00

ATOM 1527 CB THR A 295 -127.414 -9.616 24.179 1.00 0.00

ATOM 1528 OGl THR A 295 -126.485 -9.637 25.268 1.00 0.00

ATOM 1529 CG2 THR A 295 -128.626 -8.789 24.581 1.00 0.00

ATOM 1530 N LEU A 296 -128.408 -10.668 21.514 1.00 0.00

ATOM 1531 CA LEU A 296 -129.331 -10.534 20.400 1.00 0.00

ATOM 1532 C LEU A 296 -130.160 -11.773 20.215 1.00 0.00

ATOM 1533 O LEU A 296 -131.367 -11.665 20.076 1.00 0.00

ATOM 1534 CB LEU A 296 -128.567 -10.282 19.099 1.00 0.00

ATOM 1535 CG LEU A 296 -129.413 -10.136 17.833 1.00 0.00

ATOM 1536 CDl LEU A 296 -130.348 -8.941 17.946 1.00 0.00

ATOM 1537 CD2 LEU A 296 -128.527 -9.932 16.614 1.00 0.00

ATOM 1538 N THR A 297 -129.504 -12.950 20.221 1.00 0.00

ATOM 1539 CA THR A 297 -130.245 -14.186 20.036 1.00 0.00

ATOM 1540 C THR A 297 -131.268 -14.357 21.124 1.00 0.00

ATOM 1541 O THR A 297 -132.390 -14.744 20.836 1.00 0.00

ATOM 1542 CB THR A 297 -129.314 -15.413 20.066 1.00 0.00

ATOM 1543 OGl THR A 297 -128.367 -15.324 18.994 1.00 0.00

ATOM 1544 CG2 THR A 297 -130.116 -16.695 19.910 1.00 0.00

ATOM 1545 N GLU A 298 -130.871 -14.057 22.377 1.00 0.00

ATOM 1546 CA GLU A 298 -131.803 -14.202 23.482 1.00 0.00

ATOM 1547 C GLU A 298 -133.037 -13.375 23.260 1.00 0.00

ATOM 1548 O GLU A 298 -134.134 -13.899 23.365 1.00 0.00

ATOM 1549 CB GLU A 298 -131.155 -13.748 24.793 1.00 0.00

ATOM 1550 CG GLU A 298 -132.046 -13.908 26.013 1.00 0.00

ATOM 1551 CD GLU A 298 -131.359 -13.481 27.296 1.00 0.00

ATOM 1552 OEl GLU A 298 -130.181 -13.072 27.231 1.00 0.00

ATOM 1553 OE2 GLU A 298 -132.000 -13.555 28.366 1.00 0.00

ATOM 1554 N LEU A 299 -132.846 -12.077 22.947 1.00 0.00

ATOM 1555 CA LEU A 299 -133.994 -11.212 22.739 1.00 0.00

ATOM 1556 C LEU A 299 -134.837 -11.696 21.595 1.00 0.00

ATOM 1557 O LEU A 299 -136.052 -11.719 21.717 1.00 0.00

ATOM 1558 CB LEU A 299 -133.540 -9.785 22.425 1.00 0.00

ATOM 1559 CG LEU A 299 -132.893 -9.011 23.575 1.00 0.00 ATOM 1560 CDl LEU A 299 -132.329 -7.687 23.082 1.00 0.00

ATOM 1561 CD2 LEU A 299 -133.912 -8.717 24.666 1.00 0.00

ATOM 1562 N ARG A 300 -134.179 -12.092 20.487 1.00 0.00

ATOM 1563 CA ARG A 300 -134.925 -12.544 19.326 1.00 0.00

ATOM 1564 C ARG A 300 -135.813 -13.708 19.665 1.00 0.00

ATOM 1565 O ARG A 300 -136.983 -13.687 19.317 1.00 0.00

ATOM 1566 CB ARG A 300 -133.971 -12.987 18.215 1.00 0.00

ATOM 1567 CG ARG A 300 -134.667 -13.415 16.934 1.00 0.00

ATOM 1568 CD ARG A 300 -133.669 -13.928 15.908 1.00 0.00

ATOM 1569 NE ARG A 300 -133.022 -15.163 16.344 1.00 0.00

ATOM 1570 CZ ARG A 300 -133.590 -16.363 16.291 1.00 0.00

ATOM 1571 NHl ARG A 300 -132.926 -17.431 16.711 1.00 0.00

ATOM 1572 NH2 ARG A 300 -134.823 -16.493 15.818 1.00 0.00

ATOM 1573 N ARG A 301 -135.249 -14.718 20.356 1.00 0.00

ATOM 1574 CA ARG A 301 -136.053 -15.873 20.724 1.00 0.00

ATOM 1575 C ARG A 301 -137.232 -15.445 21.551 1.00 0.00

ATOM 1576 O ARG A 301 -138.337 -15.900 21.306 1.00 0.00

ATOM 1577 CB ARG A 301 -135.222 -16.866 21.540 1.00 0.00

ATOM 1578 CG ARG A 301 -134.163 -17.598 20.733 1.00 0.00

ATOM 1579 CD ARG A 301 -133.329 -18.511 21.617 1.00 0.00

ATOM 1580 NE ARG A 301 -132.287 -19.202 20.862 1.00 0.00

ATOM 1581 CZ ARG A 301 -131.374 -20.002 21.406 1.00 0.00

ATOM 1582 NHl ARG A 301 -130.465 -20.588 20.639 1.00 0.00

ATOM 1583 NH2 ARG A 301 -131.375 -20.213 22.715 1.00 0.00

ATOM 1584 N THR A 302 -136.980 -14.551 22.527 1.00 0.00

ATOM 1585 CA THR A 302 -138.065 -14.069 23.365 1.00 0.00

ATOM 1586 C THR A 302 -139.126 -13.408 22.528 1.00 0.00

ATOM 1587 O THR A 302 -140.301 -13.660 22.744 1.00 0.00

ATOM 1588 CB THR A 302 -137.568 -13.040 24.396 1.00 0.00

ATOM 1589 OGl THR A 302 -136.607 -13.654 25.263 1.00 0.00

ATOM 1590 CG2 THR A 302 -138.728 -12.522 25.234 1.00 0.00

ATOM 1591 N VAL A 303 -138.699 -12.569 21.563 1.00 0.00

ATOM 1592 CA VAL A 303 -139.664 -11.894 20.713 1.00 0.00

ATOM 1593 C VAL A 303 -140.522 -12.892 19.987 1.00 0.00

ATOM 1594 O VAL A 303 -141.727 -12.716 19.943 1.00 0.00

ATOM 1595 CB VAL A 303 -138.968 -11.015 19.657 1.00 0.00

ATOM 1596 CGl VAL A 303 -139.982 -10.478 18.658 1.00 0.00

ATOM 1597 CG2 VAL A 303 -138.275 -9.834 20.319 1.00 0.00

ATOM 1598 N GLN A 304 -139.888 -13.941 19.426 1.00 0.00

ATOM 1599 CA GLN A 304 -140.650 -14.943 18.699 1.00 0.00

ATOM 1600 C GLN A 304 -141.746 -15.504 19.560 1.00 0.00

ATOM 1601 O GLN A 304 -142.877 -15.599 19.110 1.00 0.00

ATOM 1602 CB GLN A 304 -139.742 -16.095 18.264 1.00 0.00

ATOM 1603 CG GLN A 304 -140.449 -17.170 17.454 1.00 0.00

ATOM 1604 CD GLN A 304 -139.514 -18.284 17.024 1.00 0.00

ATOM 1605 OEl GLN A 304 -138.341 -18.302 17.396 1.00 0.00

ATOM 1606 NE2 GLN A 304 -140.032 -19.218 16.234 1.00 0.00

ATOM 1607 N SER A 305 -141.397 -15.865 20.811 1.00 0.00

ATOM 1608 CA SER A 305 -142.402 -16.404 21.709 1.00 0.00

ATOM 1609 C SER A 305 -143.500 -15.403 21.943 1.00 0.00

ATOM 1610 O SER A 305 -144.662 -15.777 21.922 1.00 0.00

ATOM 1611 CB SER A 305 -141.779 -16.757 23.061 1.00 0.00

ATOM 1612 OG SER A 305 -140.851 -17.822 22.933 1.00 0.00

ATOM 1613 N LEU A 306 -143.120 -14.126 22.149 1.00 0.00

ATOM 1614 CA LEU A 306 -144.130 -13.101 22.359 1.00 0.00

ATOM 1615 C LEU A 306 -145.054 -13.015 21.179 1.00 0.00

ATOM 1616 O LEU A 306 -146.260 -12.983 21.362 1.00 0.00

ATOM 1617 CB LEU A 306 -143.473 -11.733 22.555 1.00 0.00

ATOM 1618 CG LEU A 306 -142.706 -11.531 23.864 1.00 0.00

ATOM 1619 CDl LEU A 306 -141.949 -10.211 23.845 1.00 0.00

ATOM 1620 CD2 LEU A 306 -143.661 -11.514 25.048 1.00 0.00

ATOM 1621 N GLU A 307 -144.471 -12.985 19.963 1.00 0.00

ATOM 1622 CA GLU A 307 -145.286 -12.862 18.767 1.00 0.00

ATOM 1623 C GLU A 307 -146.278 -13.985 18.664 1.00 0.00

ATOM 1624 O GLU A 307 -147.441 -13.732 18.389 1.00 0.00

ATOM 1625 CB GLU A 307 -144.408 -12.891 17.514 1.00 0.00

ATOM 1626 CG GLU A 307 -145.176 -12.722 16.214 1.00 0.00

ATOM 1627 CD GLU A 307 -144.271 -12.723 14.998 1.00 0.00 ATOM 1628 OEl GLU A 307 -143.040 -12.842 15.175 1.00 0.00

ATOM 1629 OE2 GLU A 307 -144.792 -12.604 13.869 1.00 0.00

ATOM 1630 N ILE A 308 -145.808 -15.226 18.895 1.00 0.00

ATOM 1631 CA ILE A 308 -146.712 -16.362 18.812 1.00 0.00

ATOM 1632 C ILE A 308 -147.832 -16.204 19.802 1.00 0.00

ATOM 1633 O ILE A 308 -148.981 -16.383 19.435 1.00 0.00

ATOM 1634 CB ILE A 308 -145.985 -17.685 19.118 1.00 0.00

ATOM 1635 CGl ILE A 308 -144.974 -18.005 18.015 1.00 0.00

ATOM 1636 CG2 ILE A 308 -146.981 -18.831 19.207 1.00 0.00

ATOM 1637 CDl ILE A 308 -144.029 -19.135 18.363 1.00 0.00

ATOM 1638 N ASP A 309 -147.482 -15.848 21.054 1.00 0.00

ATOM 1639 CA ASP A 309 -148.512 -15.638 22.058 1.00 0.00

ATOM 1640 C ASP A 309 -149.497 -14.606 21.590 1.00 0.00

ATOM 1641 O ASP A 309 -150.693 -14.794 21.747 1.00 0.00

ATOM 1642 CB ASP A 309 -147.891 -15.155 23.371 1.00 0.00

ATOM 1643 CG ASP A 309 -147.143 -16.254 24.100 1.00 0.00

ATOM 1644 ODl ASP A 309 -147.299 -17.432 23.719 1.00 0.00

ATOM 1645 OD2 ASP A 309 -146.399 -15.934 25.051 1.00 0.00

ATOM 1646 N LEU A 310 -148.966 -13.516 20.999 1.00 0.00

ATOM 1647 CA LEU A 310 -149.829 -12.446 20.529 1.00 0.00

ATOM 1648 C LEU A 310 -150.833 -12.947 19.530 1.00 0.00

ATOM 1649 O LEU A 310 -152.019 -12.743 19.729 1.00 0.00

ATOM 1650 CB LEU A 310 -149.003 -11.347 19.856 1.00 0.00

ATOM 1651 CG LEU A 310 -149.786 -10.158 19.296 1.00 0.00

ATOM 1652 CDl LEU A 310 -150.527 -9.431 20.407 1.00 0.00

ATOM 1653 CD2 LEU A 310 -148.849 -9.167 18.622 1.00 0.00

ATOM 1654 N ASP A 311 -150.347 -13.600 18.455 1.00 0.00

ATOM 1655 CA ASP A 311 -151.258 -14.076 17.429 1.00 0.00

ATOM 1656 C ASP A 311 -152.301 -14.987 18.013 1.00 0.00

ATOM 1657 O ASP A 311 -153.469 -14.851 17.686 1.00 0.00

ATOM 1658 CB ASP A 311 -150.495 -14.854 16.354 1.00 0.00

ATOM 1659 CG ASP A 311 -149.665 -13.952 15.462 1.00 0.00

ATOM 1660 ODl ASP A 311 -149.859 -12.719 15.518 1.00 0.00

ATOM 1661 OD2 ASP A 311 -148.821 -14.478 14.707 1.00 0.00

ATOM 1662 N SER A 312 -151.860 -15.907 18.893 1.00 0.00

ATOM 1663 CA SER A 312 -152.798 -16.832 19.503 1.00 0.00

ATOM 1664 C SER A 312 -153.862 -16.093 20.264 1.00 0.00

ATOM 1665 O SER A 312 -155.036 -16.331 20.030 1.00 0.00

ATOM 1666 CB SER A 312 -152.074 -17.764 20.477 1.00 0.00

ATOM 1667 OG SER A 312 -151.184 -18.627 19.790 1.00 0.00

ATOM 1668 N MET A 313 -153.437 -15.193 21.175 1.00 0.00

ATOM 1669 CA MET A 313 -154.404 -14.458 21.974 1.00 0.00

ATOM 1670 C MET A 313 -155.375 -13.717 21.100 1.00 0.00

ATOM 1671 O MET A 313 -156.558 -13.706 21.395 1.00 0.00

ATOM 1672 CB MET A 313 -153.695 -13.439 22.869 1.00 0.00

ATOM 1673 CG MET A 313 -152.879 -14.061 23.991 1.00 0.00

ATOM 1674 SD MET A 313 -153.887 -15.029 25.130 1.00 0.00

ATOM 1675 CE MET A 313 -154.840 -13.735 25.922 1.00 0.00

ATOM 1676 N ARG A 314 -154.859 -13.106 20.015 1.00 0.00

ATOM 1677 CA ARG A 314 -155.736 -12.369 19.121 1.00 0.00

ATOM 1678 C ARG A 314 -156.790 -13.270 18.545 1.00 0.00

ATOM 1679 O ARG A 314 -157.959 -12.918 18.563 1.00 0.00

ATOM 1680 CB ARG A 314 -154.936 -11.765 17.964 1.00 0.00

ATOM 1681 CG ARG A 314 -154.029 -10.616 18.370 1.00 0.00

ATOM 1682 CD ARG A 314 -153.233 -10.095 17.184 1.00 0.00

ATOM 1683 NE ARG A 314 -152.318 -9.022 17.568 1.00 0.00

ATOM 1684 CZ ARG A 314 -151.468 -8.431 16.734 1.00 0.00

ATOM 1685 NHl ARG A 314 -150.674 -7.463 17.172 1.00 0.00

ATOM 1686 NH2 ARG A 314 -151.414 -8.810 15.465 1.00 0.00

ATOM 1687 N ASN A 315 -156.365 -14.446 18.039 1.00 0.00

ATOM 1688 CA ASN A 315 -157.323 -15.368 17.454 1.00 0.00

ATOM 1689 C ASN A 315 -158.340 -15.801 18.472 1.00 0.00

ATOM 1690 O ASN A 315 -159.525 -15.788 18.182 1.00 0.00

ATOM 1691 CB ASN A 315 -156.613 -16.617 16.926 1.00 0.00

ATOM 1692 CG ASN A 315 -155.822 -16.347 15.662 1.00 0.00

ATOM 1693 ODl ASN A 315 -156.061 -15.358 14.968 1.00 0.00

ATOM 1694 ND2 ASN A 315 -154.876 -17.227 15.358 1.00 0.00

ATOM 1695 N LEU A 316 -157.855 -16.175 19.673 1.00 0.00 ATOM 1696 CA LEU A 316 -158.763 -16.603 20.724 1.00 0.00

ATOM 1697 C LEU A 316 -159.773 -15.532 21.024 1.00 0.00

ATOM 1698 O LEU A 316 -160.952 -15.830 21.138 1.00 0.00

ATOM 1699 CB LEU A 316 -157.991 -16.908 22.008 1.00 0.00

ATOM 1700 CG LEU A 316 -158.823 -17.356 23.211 1.00 0.00

ATOM 1701 CDl LEU A 316 -159.552 -18.656 22.905 1.00 0.00

ATOM 1702 CD2 LEU A 316 -157.935 -17.584 24.425 1.00 0.00

ATOM 1703 N LYS A 317 -159.295 -14.279 21.143 1.00 0.00

ATOM 1704 CA LYS A 317 -160.201 -13.185 21.447 1.00 0.00

ATOM 1705 C LYS A 317 -161.243 -13.037 20.374 1.00 0.00

ATOM 1706 O LYS A 317 -162.401 -12.821 20.693 1.00 0.00

ATOM 1707 CB LYS A 317 -159.433 -11.865 21.551 1.00 0.00

ATOM 1708 CG LYS A 317 -160.299 -10.670 21.913 1.00 0.00

ATOM 1709 CD LYS A 317 -159.463 -9.412 22.078 1.00 0.00

ATOM 1710 CE LYS A 317 -160.333 -8.210 22.411 1.00 0.00

ATOM 1711 NZ LYS A 317 -159.528 -6.966 22.560 1.00 0.00

ATOM 1712 N ALA A 318 -160.823 -13.161 19.099 1.00 0.00

ATOM 1713 CA ALA A 318 -161.775 -13.028 18.010 1.00 0.00

ATOM 1714 C ALA A 318 -162.898 -14.016 18.163 1.00 0.00

ATOM 1715 O ALA A 318 -164.054 -13.640 18.036 1.00 0.00

ATOM 1716 CB ALA A 318 -161.092 -13.283 16.674 1.00 0.00

ATOM 1717 N SER A 319 -162.542 -15.283 18.452 1.00 0.00

ATOM 1718 CA SER A 319 -163.570 -16.295 18.627 1.00 0.00

ATOM 1719 C SER A 319 -164.473 -15.949 19.778 1.00 0.00

ATOM 1720 O SER A 319 -165.682 -16.006 19.627 1.00 0.00

ATOM 1721 CB SER A 319 -162.936 -17.659 18.908 1.00 0.00

ATOM 1722 OG SER A 319 -162.218 -18.130 17.782 1.00 0.00

ATOM 1723 N LEU A 320 -163.868 -15.585 20.926 1.00 0.00

ATOM 1724 CA LEU A 320 -164.668 -15.291 22.103 1.00 0.00

ATOM 1725 C LEU A 320 -165.629 -14.161 21.865 1.00 0.00

ATOM 1726 O LEU A 320 -166.791 -14.281 99 999 1.00 0.00

ATOM 1727 CB LEU A 320 -163.770 -14.895 23.277 1.00 0.00

ATOM 1728 CG LEU A 320 -162.921 -16.013 23.887 1.00 0.00

ATOM 1729 CDl LEU A 320 -161.942 -15.449 24.906 1.00 0.00

ATOM 1730 CD2 LEU A 320 -163.800 -17.036 24.588 1.00 0.00

ATOM 1731 N GLU A 321 -165.137 -13.064 21.255 1.00 0.00

ATOM 1732 CA GLU A 321 -165.999 -11.916 21.026 1.00 0.00

ATOM 1733 C GLU A 321 -167.198 -12.298 20.206 1.00 0.00

ATOM 1734 O GLU A 321 -168.304 -11.896 20.533 1.00 0.00

ATOM 1735 CB GLU A 321 -165.241 -10.817 20.279 1.00 0.00

ATOM 1736 CG GLU A 321 -164.175 -10.122 21.111 1.00 0.00

ATOM 1737 CD GLU A 321 -163.364 -9.128 20.305 1.00 0.00

ATOM 1738 OEl GLU A 321 -163.584 -9.035 19.079 1.00 0.00

ATOM 1739 OE2 GLU A 321 -162.506 -8.441 20.899 1.00 0.00

ATOM 1740 N ASN A 322 -166.964 -13.094 19.145 1.00 0.00

ATOM 1741 CA ASN A T 99 -168.078 -13.543 18.326 1.00 0.00

ATOM 1742 C ASN A 322 -169.055 -14.340 19.142 1.00 0.00

ATOM 1743 O ASN A 322 -170.251 -14.194 18.950 1.00 0.00

ATOM 1744 CB ASN A 322 -167.578 -14.427 17.181 1.00 0.00

ATOM 1745 CG ASN A -166.867 -13.635 16.101 1.00 0.00

ATOM 1746 ODl ASN A 322 -167.041 -12.422 15.992 1.00 0.00

ATOM 1747 ND2 ASN A 322 -166.061 -14.321 15.299 1.00 0.00

ATOM 1748 N SER A 323 -168.529 -15.175 20.062 1.00 0.00

ATOM 1749 CA SER A 323 -169.401 -16.018 20.866 1.00 0.00

ATOM 1750 C SER A 323 -170.320 -15.229 21.760 1.00 0.00

ATOM 1751 O SER A 323 -171.504 -15.523 21.791 1.00 0.00

ATOM 1752 CB SER A 323 -168.574 -16.937 21.767 1.00 0.00

ATOM 1753 OG SER A 323 -167.843 -17.880 21.002 1.00 0.00

ATOM 1754 N LEU A 324 -169.784 -14.228 22.490 1.00 0.00

ATOM 1755 CA LEU A 324 -170.640 -13.467 23.388 1.00 0.00

ATOM 1756 C LEU A 324 -171.649 -12.667 22.611 1.00 0.00

ATOM 1757 O LEU A 324 -172.826 -12.715 22.933 1.00 0.00

ATOM 1758 CB LEU A 324 -169.808 -12.500 24.231 1.00 0.00

ATOM 1759 CG LEU A 324 -168.899 -13.131 25.289 1.00 0.00

ATOM 1760 CDl LEU A 324 -167.996 -12.081 25.918 1.00 0.00

ATOM 1761 CD2 LEU A 324 -169.726 -13.772 26.393 1.00 0.00

ATOM 1762 N ARG A 325 -171.175 -11.946 21.574 1.00 0.00

ATOM 1763 CA ARG A 325 -172.092 -11.177 20.745 1.00 0.00 ATOM 1764 C ARG A 325 -173.210 -12.056 20.257 1.00 0.00

ATOM 1765 O ARG A 325 -174.337 -11.604 20.139 1.00 0.00

ATOM 1766 CB ARG A 325 -171.361 -10.599 19.531 1.00 0.00

ATOM 1767 CG ARG A 325 -170.370 -9.498 19.871 1.00 0.00

ATOM 1768 CD ARG A 325 -169.678 -8.974 18.623 1.00 0.00

ATOM 1769 NE ARG A 325 -168.679 -7.956 18.938 1.00 0.00

ATOM 1770 CZ ARG A 325 -167.849 -7.422 18.048 1.00 0.00

ATOM 1771 NHl ARG A 325 -166.973 -6.502 18.426 1.00 0.00

ATOM 1772 NH2 ARG A 325 -167.900 -7.809 16.780 1.00 0.00

ATOM 1773 N GLU A 326 -172.870 -13.334 19.996 1.00 0.00

ATOM 1774 CA GLU A 326 -173.875 -14.278 19.544 1.00 0.00

ATOM 1775 C GLU A 326 -174.926 -14.498 20.597 1.00 0.00

ATOM 1776 O GLU A 326 -176.098 -14.298 20.316 1.00 0.00

ATOM 1777 CB GLU A 326 -173.234 -15.630 19.225 1.00 0.00

ATOM 1778 CG GLU A 326 -174.211 -16.674 18.709 1.00 0.00

ATOM 1779 CD GLU A 326 -173.550 -18.014 18.451 1.00 0.00

ATOM 1780 OEl GLU A 326 -172.323 -18.121 18.660 1.00 0.00

ATOM 1781 OE2 GLU A 326 -174.259 -18.957 18.041 1.00 0.00

ATOM 1782 N VAL A 327 -174.500 -14.918 21.804 1.00 0.00

ATOM 1783 CA VAL A 327 -175.464 -15.228 22.851 1.00 0.00

ATOM 1784 C VAL A 327 -176.387 -14.070 23.107 1.00 0.00

ATOM 1785 O VAL A 327 -177.591 -14.262 23.153 1.00 0.00

ATOM 1786 CB VAL A 327 -174.764 -15.563 24.181 1.00 0.00

ATOM 1787 CGl VAL A 327 -175.783 -15.674 25.305 1.00 0.00

ATOM 1788 CG2 VAL A 327 -174.020 -16.885 24.073 1.00 0.00

ATOM 1789 N GLU A 328 -175.797 -12.868 23.269 1.00 0.00

ATOM 1790 CA GLU A 328 -176.598 -11.688 23.551 1.00 0.00

ATOM 1791 C GLU A 328 -177.729 -11.545 22.573 1.00 0.00

ATOM 1792 O GLU A 328 -178.865 -11.373 22.986 1.00 0.00

ATOM 1793 CB GLU A 328 -175.739 -10.424 23.465 1.00 0.00

ATOM 1794 CG GLU A 328 -176.491 -9.140 23.772 1.00 0.00

ATOM 1795 CD GLU A 328 -175.599 -7.916 23.717 1.00 0.00

ATOM 1796 OEl GLU A 328 -174.385 -8.075 23.472 1.00 0.00

ATOM 1797 OE2 GLU A 328 -176.115 -6.796 23.919 1.00 0.00

ATOM 1798 N ALA A 329 -177.405 -11.628 21.268 1.00 0.00

ATOM 1799 CA ALA A 329 -178.444 -11.491 20.261 1.00 0.00

ATOM 1800 C ALA A 329 -179.437 -12.616 20.341 1.00 0.00

ATOM 1801 O ALA A 329 -180.629 -12.364 20.282 1.00 0.00

ATOM 1802 CB ALA A 329 -177.835 -11.499 18.867 1.00 0.00

ATOM 1803 N ARG A 330 -178.935 -13.860 20.476 1.00 0.00

ATOM 1804 CA ARG A 330 -179.830 -15.006 20.484 1.00 0.00

ATOM 1805 C ARG A 330 -180.817 -14.944 21.618 1.00 0.00

ATOM 1806 O ARG A 330 -182.012 -14.992 21.375 1.00 0.00

ATOM 1807 CB ARG A 330 -179.035 -16.305 20.632 1.00 0.00

ATOM 1808 CG ARG A 330 -179.886 -17.563 20.583 1.00 0.00

ATOM 1809 CD ARG A 330 -179.055 -18.804 20.867 1.00 0.00

ATOM 1810 NE ARG A 330 -178.578 -18.838 22.247 1.00 0.00

ATOM 1811 CZ ARG A 330 -179.324 -19.195 23.288 1.00 0.00

ATOM 1812 NHl ARG A 330 -178.805 -19.196 24.507 1.00 0.00

ATOM 1813 NH2 ARG A 330 -180.588 -19.550 23.105 1.00 0.00

ATOM 1814 N TYR A 331 -180.300 -14.846 22.859 1.00 0.00

ATOM 1815 CA TYR A 331 -181.181 -14.841 24.013 1.00 0.00

ATOM 1816 C TYR A 331 -182.201 -13.740 23.917 1.00 0.00

ATOM 1817 O TYR A 331 -183.337 -13.947 24.314 1.00 0.00

ATOM 1818 CB TYR A 331 -180.378 -14.630 25.298 1.00 0.00

ATOM 1819 CG TYR A 331 -181.227 -14.583 26.549 1.00 0.00

ATOM 1820 CDl TYR A 331 -181.715 -15.751 27.122 1.00 0.00

ATOM 1821 CD2 TYR A 331 -181.537 -13.371 27.152 1.00 0.00

ATOM 1822 CEl TYR A 331 -182.491 -15.717 28.265 1.00 0.00

ATOM 1823 CE2 TYR A 331 -182.311 -13.318 28.296 1.00 0.00

ATOM 1824 CZ TYR A 331 -182.789 -14.506 28.850 1.00 0.00

ATOM 1825 OH TYR A 331 -183.562 -14.469 29.988 1.00 0.00

ATOM 1826 N ALA A 332 -181.788 -12.574 23.378 1.00 0.00

ATOM 1827 CA ALA A 332 -182.715 -11.460 23.268 1.00 0.00

ATOM 1828 C ALA A 332 -183.979 -11.862 22.560 1.00 0.00

ATOM 1829 O ALA A 332 -185.058 -11.595 23.063 1.00 0.00

ATOM 1830 CB ALA A 332 -182.082 -10.319 22.485 1.00 0.00

ATOM 1831 N LEU A 333 -183.835 -12.516 21.392 1.00 0.00 ATOM 1832 CA LEU A 333 -185.016 -12.943 20.660 1.00 0.00

ATOM 1833 C LEU A 333 -185.771 -13.989 21.426 1.00 0.00

ATOM 1834 O LEU A 333 -186.989 -13.935 21.476 1.00 0.00

ATOM 1835 CB LEU A 333 -184.622 -13.532 19.304 1.00 0.00

ATOM 1836 CG LEU A 333 -184.062 -12.550 18.274 1.00 0.00

ATOM 1837 CDl LEU A 333 -183.549 -13.290 17.049 1.00 0.00

ATOM 1838 CD2 LEU A 333 -185.137 -11.572 17.824 1.00 0.00

ATOM 1839 N GLN A 334 -185.033 -14.946 22.023 1.00 0.00

ATOM 1840 CA GLN A 334 -185.688 -16.035 22.729 1.00 0.00

ATOM 1841 C GLN A 334 -186.528 -15.532 23.867 1.00 0.00

ATOM 1842 O GLN A 334 -187.704 -15.853 23.933 1.00 0.00

ATOM 1843 CB GLN A 334 -184.650 -17.000 23.303 1.00 0.00

ATOM 1844 CG GLN A 334 -183.926 -17.829 22.256 1.00 0.00

ATOM 1845 CD GLN A 334 -182.815 -18.675 22.847 1.00 0.00

ATOM 1846 OEl GLN A 334 -182.526 -18.591 24.040 1.00 0.00

ATOM 1847 NE2 GLN A 334 -182.190 -19.497 22.011 1.00 0.00

ATOM 1848 N MET A 335 -185.909 -14.738 24.763 1.00 0.00

ATOM 1849 CA MET A 335 -186.651 -14.197 25.888 1.00 0.00

ATOM 1850 C MET A 335 -187.814 -13.390 25.387 1.00 0.00

ATOM 1851 O MET A 335 -188.886 -13.447 25.969 1.00 0.00

ATOM 1852 CB MET A 335 -185.753 -13.296 26.739 1.00 0.00

ATOM 1853 CG MET A 335 -186.444 -12.704 27.957 1.00 0.00

ATOM 1854 SD MET A 335 -185.357 -11.639 28.923 1.00 0.00

ATOM 1855 CE MET A 335 -185.256 -10.203 27.857 1.00 0.00

ATOM 1856 N GLU A 336 -187.583 -12.652 24.283 1.00 0.00

ATOM 1857 CA GLU A 336 -188.656 -11.880 23.681 1.00 0.00

ATOM 1858 C GLU A 336 -189.827 -12.774 23.370 1.00 0.00

ATOM 1859 O GLU A 336 -190.956 -12.407 23.650 1.00 0.00

ATOM 1860 CB GLU A 336 -188.183 -11.228 22.380 1.00 0.00

ATOM 1861 CG GLU A 336 -189.226 -10.347 21.712 1.00 0.00

ATOM 1862 CD GLU A 336 -188.702 -9.673 20.459 1.00 0.00

ATOM 1863 OEl GLU A 336 -187.517 -9.879 20.124 1.00 0.00

ATOM 1864 OE2 GLU A 336 -189.478 -8.937 19.812 1.00 0.00

ATOM 1865 N GLN A 337 -189.535 -13.958 22.798 1.00 0.00

ATOM 1866 CA GLN A 337 -190.605 -14.886 22.478 1.00 0.00

ATOM 1867 C GLN A 337 -191.220 -15.457 23.725 1.00 0.00

ATOM 1868 O GLN A 337 -192.430 -15.615 23.773 1.00 0.00

ATOM 1869 CB GLN A 337 -190.073 -16.048 21.637 1.00 0.00

ATOM 1870 CG GLN A 337 -189.673 -15.658 20.223 1.00 0.00

ATOM 1871 CD GLN A 337 -189.049 -16.807 19.456 1.00 0.00

ATOM 1872 OEl GLN A 337 -188.816 -17.882 20.010 1.00 0.00

ATOM 1873 NE2 GLN A 337 -188.775 -16.584 18.176 1.00 0.00

ATOM 1874 N LEU A 338 -190.378 -15.753 24.738 1.00 0.00

ATOM 1875 CA LEU A 338 -190.901 -16.301 25.979 1.00 0.00

ATOM 1876 C LEU A 338 -191.943 -15.386 26.557 1.00 0.00

ATOM 1877 O LEU A 338 -193.005 -15.843 26.950 1.00 0.00

ATOM 1878 CB LEU A 338 -189.778 -16.467 27.006 1.00 0.00

ATOM 1879 CG LEU A 338 -188.754 -17.566 26.718 1.00 0.00

ATOM 1880 CDl LEU A 338 -187.599 -17.495 27.706 1.00 0.00

ATOM 1881 CD2 LEU A 338 -189.394 -18.941 26.833 1.00 0.00

ATOM 1882 N ASN A 339 -191.620 -14.080 26.590 1.00 0.00

ATOM 1883 CA ASN A 339 -192.560 -13.113 27.129 1.00 0.00

ATOM 1884 C ASN A 339 -193.821 -13.078 26.312 1.00 0.00

ATOM 1885 O ASN A 339 -194.893 -12.924 26.877 1.00 0.00

ATOM 1886 CB ASN A 339 -191.948 -11.711 27.125 1.00 0.00

ATOM 1887 CG ASN A 339 -190.880 -11.538 28.188 1.00 0.00

ATOM 1888 ODl ASN A 339 -190.826 -12.297 29.156 1.00 0.00

ATOM 1889 ND2 ASN A 339 -190.026 -10.538 28.010 1.00 0.00

ATOM 1890 N GLY A 340 -193.688 -13.238 24.980 1.00 0.00

ATOM 1891 CA GLY A 340 -194.876 -13.226 24.141 1.00 0.00

ATOM 1892 C GLY A 340 -195.800 -14.351 24.509 1.00 0.00

ATOM 1893 O GLY A 340 -196.988 -14.119 24.662 1.00 0.00

ATOM 1894 N ILE A 341 -195.238 -15.568 24.658 1.00 0.00

ATOM 1895 CA ILE A 341 -196.064 -16.713 25.013 1.00 0.00

ATOM 1896 C ILE A 341 -196.811 -16.434 26.286 1.00 0.00

ATOM 1897 O ILE A 341 -197.994 -16.722 26.364 1.00 0.00

ATOM 1898 CB ILE A 341 -195.213 -17.979 25.224 1.00 0.00

ATOM 1899 CGl ILE A 341 -194.600 -18.436 23.898 1.00 0.00 ATOM 1900 CG2 ILE A 341 -196.068 -19.110 25.775 1.00 0.00

ATOM 1901 CDl ILE A 341 -193.543 -19.508 24.052 1.00 0.00

ATOM 1902 N LEU A 342 -196.106 -15.856 27.277 1.00 0.00

ATOM 1903 CA LEU A 342 -196.761 -15.547 28.533 1.00 0.00

ATOM 1904 C LEU A 342 -197.911 -14.606 28.307 1.00 0.00

ATOM 1905 O LEU A 342 -198.976 -14.815 28.866 1.00 0.00

ATOM 1906 CB LEU A 342 -195.778 -14.886 29.501 1.00 0.00

ATOM 1907 CG LEU A 342 -194.666 -15.780 30.054 1.00 0.00

ATOM 1908 CDl LEU A 342 -193.663 -14.960 30.851 1.00 0.00

ATOM 1909 CD2 LEU A 342 -195.241 -16.850 30.969 1.00 0.00

ATOM 1910 N LEU A 343 -197.688 -13.576 27.467 1.00 0.00

ATOM 1911 CA LEU A 343 -198.751 -12.623 27.197 1.00 0.00

ATOM 1912 C LEU A 343 -199.912 -13.283 26.507 1.00 0.00

ATOM 1913 O LEU A 343 -201.048 -13.028 26.869 1.00 0.00

ATOM 1914 CB LEU A 343 -198.242 -11.495 26.297 1.00 0.00

ATOM 1915 CG LEU A 343 -197.240 -10.526 26.926 1.00 0.00

ATOM 1916 CDl LEU A 343 -196.683 -9.573 25.878 1.00 0.00

ATOM 1917 CD2 LEU A 343 -197.902 -9.698 28.017 1.00 0.00

ATOM 1918 N HIS A 344 -199.611 -14.141 25.512 1.00 0.00

ATOM 1919 CA HIS A 344 -200.683 -14.816 24.800 1.00 0.00

ATOM 1920 C HIS A 344 -201.470 -15.684 25.742 1.00 0.00

ATOM 1921 O HIS A 344 -202.689 -15.696 25.670 1.00 0.00

ATOM 1922 CB HIS A 344 -200.114 -15.699 23.687 1.00 0.00

ATOM 1923 CG HIS A 344 -201.158 -16.429 22.902 1.00 0.00

ATOM 1924 NDl HIS A 344 -201.995 -15.797 22.008 1.00 0.00

ATOM 1925 CD2 HIS A 344 -201.603 -17.812 22.800 1.00 0.00

ATOM 1926 CEl HIS A 344 -202.820 -16.708 21.461 1.00 0.00

ATOM 1927 NE2 HIS A 344 -202.590 -17.919 21.932 1.00 0.00

ATOM 1928 N LEU A 345 -200.759 -16.394 26.638 1.00 0.00

ATOM 1929 CA LEU A 345 -201.452 -17.210 27.622 1.00 0.00

ATOM 1930 C LEU A 345 -202.301 -16.338 28.505 1.00 0.00

ATOM 1931 O LEU A 345 -203.388 -16.741 28.889 1.00 0.00

ATOM 1932 CB LEU A 345 -200.449 -17.965 28.496 1.00 0.00

ATOM 1933 CG LEU A 345 -199.657 -19.080 27.811 1.00 0.00

ATOM 1934 CDl LEU A 345 -198.577 -19.620 28.736 1.00 0.00

ATOM 1935 CD2 LEU A 345 -200.573 -20.232 27.428 1.00 0.00

ATOM 1936 N GLU A 346 -201.786 -15.130 28.808 1.00 0.00

ATOM 1937 CA GLU A 346 -202.515 -14.216 29.668 1.00 0.00

ATOM 1938 C GLU A 346 -203.850 -13.861 29.074 1.00 0.00

ATOM 1939 O GLU A 346 -204.854 -13.974 29.759 1.00 0.00

ATOM 1940 CB GLU A 346 -201.724 -12.922 29.868 1.00 0.00

ATOM 1941 CG GLU A 346 -202.394 -11.922 30.797 1.00 0.00

ATOM 1942 CD GLU A 346 -201.567 -10.668 30.997 1.00 0.00

ATOM 1943 OEl GLU A 346 -200.462 -10.587 30.420 1.00 0.00

ATOM 1944 OE2 GLU A 346 -202.023 -9.766 31.731 1.00 0.00

ATOM 1945 N SER A 347 -203.851 -13.437 27.794 1.00 0.00

ATOM 1946 CA SER A 347 -205.102 -13.054 27.160 1.00 0.00

ATOM 1947 C SER A 347 -206.094 -14.180 27.207 1.00 0.00

ATOM 1948 O SER A 347 -207.258 -13.951 27.499 1.00 0.00

ATOM 1949 CB SER A 347 -204.868 -12.685 25.694 1.00 0.00

ATOM 1950 OG SER A 347 -204.074 -11.517 25.582 1.00 0.00

ATOM 1951 N GLU A 348 -205.610 -15.407 26.930 1.00 0.00

ATOM 1952 CA GLU A 348 -206.487 -16.562 26.985 1.00 0.00

ATOM 1953 C GLU A 348 -207.066 -16.716 28.363 1.00 0.00

ATOM 1954 O GLU A 348 -208.268 -16.879 28.498 1.00 0.00

ATOM 1955 CB GLU A 348 -205.715 -17.838 26.638 1.00 0.00

ATOM 1956 CG GLU A 348 -205.316 -17.943 25.176 1.00 0.00

ATOM 1957 CD GLU A 348 -204.438 -19.147 24.898 1.00 0.00

ATOM 1958 OEl GLU A 348 -204.074 -19.853 25.862 1.00 0.00

ATOM 1959 OE2 GLU A 348 -204.113 -19.386 23.715 1.00 0.00

ATOM 1960 N LEU A 349 -206.184 -16.657 29.381 1.00 0.00

ATOM 1961 CA LEU A 349 -206.631 -16.819 30.755 1.00 0.00

ATOM 1962 C LEU A 349 -207.726 -15.846 31.091 1.00 0.00

ATOM 1963 O LEU A 349 -208.731 -16.247 31.656 1.00 0.00

ATOM 1964 CB LEU A 349 -205.473 -16.584 31.727 1.00 0.00

ATOM 1965 CG LEU A 349 -205.800 -16.713 33.215 1.00 0.00

ATOM 1966 CDl LEU A 349 -206.244 -18.130 33.548 1.00 0.00

ATOM 1967 CD2 LEU A 349 -204.582 -16.385 34.064 1.00 0.00 ATOM 1968 N ALA A 350 -207.522 -14.563 30.735 1.00 0.00

ATOM 1969 CA ALA A 350 -208.529 -13.562 31.038 1.00 0.00

ATOM 1970 C ALA A 350 -209.834 -13.888 30.368 1.00 0.00

ATOM 1971 O ALA A 350 -210.875 -13.755 30.993 1.00 0.00

ATOM 1972 CB ALA A 350 -208.077 -12.192 30.555 1.00 0.00

ATOM 1973 N GLN A 351 -209.767 -14.326 29.095 1.00 0.00

ATOM 1974 CA GLN A 351 -210.988 -14.644 28.373 1.00 0.00

ATOM 1975 C GLN A 351 -211.786 -15.698 29.088 1.00 0.00

ATOM 1976 O GLN A 351 -212.972 -15.512 29.304 1.00 0.00

ATOM 1977 CB GLN A 351 -210.661 -15.167 26.972 1.00 0.00

ATOM 1978 CG GLN A 351 -210.122 -14.108 26.024 1.00 0.00

ATOM 1979 CD GLN A 351 -209.685 -14.688 24.693 1.00 0.00

ATOM 1980 OEl GLN A 351 -209.710 -15.902 24.495 1.00 0.00

ATOM 1981 NE2 GLN A 351 -209.283 -13.816 23.775 1.00 0.00

ATOM 1982 N THR A 352 -211.117 -16.807 29.455 1.00 0.00

ATOM 1983 CA THR A 352 -211.830 -17.887 30.117 1.00 0.00

ATOM 1984 C THR A 352 -212.380 -17.441 31.442 1.00 0.00

ATOM 1985 O THR A 352 -213.511 -17.780 31.756 1.00 0.00

ATOM 1986 CB THR A 352 -210.909 -19.094 30.378 1.00 0.00

ATOM 1987 OGl THR A 352 -210.426 -19.609 29.131 1.00 0.00

ATOM 1988 CG2 THR A 352 -211.667 -20.194 31.105 1.00 0.00

ATOM 1989 N ARG A 353 -211.583 -16.673 32.211 1.00 0.00

ATOM 1990 CA ARG A 353 -212.050 -16.231 33.516 1.00 0.00

ATOM 1991 C ARG A 353 -213.323 -15.440 33.405 1.00 0.00

ATOM 1992 O ARG A 353 -214.255 -15.701 34.147 1.00 0.00

ATOM 1993 CB ARG A 353 -211.001 -15.344 34.189 1.00 0.00

ATOM 1994 CG ARG A 353 -211.377 -14.891 35.590 1.00 0.00

ATOM 1995 CD ARG A 353 -210.338 -13.941 36.161 1.00 0.00

ATOM 1996 NE ARG A 353 -210.284 -12.680 35.424 1.00 0.00

ATOM 1997 CZ ARG A 353 -211.163 -11.694 35.566 1.00 0.00

ATOM 1998 NHl ARG A 353 -211.034 -10.583 34.853 1.00 0.00

ATOM 1999 NH2 ARG A 353 -212.169 -11.820 36.421 1.00 0.00

ATOM 2000 N ALA A 354 -213.360 -14.478 32.460 1.00 0.00

ATOM 2001 CA ALA A 354 -214.570 -13.692 32.287 1.00 0.00

ATOM 2002 C ALA A 354 -215.724 -14.584 31.929 1.00 0.00

ATOM 2003 O ALA A 354 -216.804 -14.425 32.479 1.00 0.00

ATOM 2004 CB ALA A 354 -214.384 -12.671 31.175 1.00 0.00

ATOM 2005 N GLU A 355 -215.481 -15.535 31.005 1.00 0.00

ATOM 2006 CA GLU A 355 -216.536 -16.457 30.620 1.00 0.00

ATOM 2007 C GLU A 355 -217.040 -17.213 31.815 1.00 0.00

ATOM 2008 O GLU A 355 -218.242 -17.363 31.968 1.00 0.00

ATOM 2009 CB GLU A 355 -216.016 -17.467 29.594 1.00 0.00

ATOM 2010 CG GLU A 355 -215.739 -16.873 28.223 1.00 0.00

ATOM 2011 CD GLU A 355 -215.112 -17.872 27.271 1.00 0.00

ATOM 2012 OEl GLU A 355 -214.824 -19.007 27.706 1.00 0.00

ATOM 2013 OE2 GLU A 355 -214.906 -17.520 26.091 1.00 0.00

ATOM 2014 N GLY A 356 -216.107 -17.680 32.670 1.00 0.00

ATOM 2015 CA GLY A 356 -216.520 -18.433 33.841 1.00 0.00

ATOM 2016 C GLY A 356 -217.355 -17.587 34.761 1.00 0.00

ATOM 2017 O GLY A 356 -218.319 -18.090 35.317 1.00 0.00

ATOM 2018 N GLN A 357 -216.983 -16.300 34.915 1.00 0.00

ATOM 2019 CA GLN A 357 -217.755 -15.427 35.784 1.00 0.00

ATOM 2020 C GLN A 357 -219.181 -15.361 35.313 1.00 0.00

ATOM 2021 O GLN A 357 -220.089 -15.488 36.118 1.00 0.00

ATOM 2022 CB GLN A 357 -217.171 -14.013 35.777 1.00 0.00

ATOM 2023 CG GLN A 357 -215.831 -13.890 36.485 1.00 0.00

ATOM 2024 CD GLN A 357 -215.222 -12.510 36.345 1.00 0.00

ATOM 2025 OEl GLN A 357 -215.761 -11.651 35.648 1.00 0.00

ATOM 2026 NE2 GLN A 357 -214.093 -12.293 37.009 1.00 0.00

ATOM 2027 N ARG A 358 -219.360 -15.170 33.992 1.00 0.00

ATOM 2028 CA ARG A 358 -220.706 -15.111 33.451 1.00 0.00

ATOM 2029 C ARG A 358 -221.438 -16.396 33.720 1.00 0.00

ATOM 2030 O ARG A 358 -222.593 -16.354 34.115 1.00 0.00

ATOM 2031 CB ARG A 358 -220.667 -14.886 31.938 1.00 0.00

ATOM 2032 CG ARG A 358 -220.217 -13.492 31.530 1.00 0.00

ATOM 2033 CD ARG A 358 -220.130 -13.360 30.018 1.00 0.00

ATOM 2034 NE ARG A 358 -219.673 -12.035 29.609 1.00 0.00

ATOM 2035 CZ ARG A 358 -219.440 -11.679 28.350 1.00 0.00 ATOM 2036 NHl ARG A 358 -219.026 -10.451 28.074 1.00 0.00

ATOM 2037 NH2 ARG A 358 -219.624 -12.554 27.371 1.00 0.00

ATOM 2038 N GLN A 359 -220.750 -17.537 33.516 1.00 0.00

ATOM 2039 CA GLN A 359 -221.394 -18.818 33.755 1.00 0.00

ATOM 2040 C GLN A 359 -221.831 -18.938 35.187 1.00 0.00

ATOM 2041 O GLN A 359 -222.955 -19.340 35.436 1.00 0.00

ATOM 2042 CB GLN A 359 -220.432 -19.967 33.449 1.00 0.00

ATOM 2043 CG GLN A 359 -220.133 -20.151 31.971 1.00 0.00

ATOM 2044 CD GLN A 359 -219.077 -21.208 31.717 1.00 0.00

ATOM 2045 OEl GLN A 359 -218.500 -21.761 32.654 1.00 0.00

ATOM 2046 NE2 GLN A 359 -218.820 -21.493 30.445 1.00 0.00

ATOM 2047 N ALA A 360 -220.934 -18.572 36.125 1.00 0.00

ATOM 2048 CA ALA A 360 -221.276 -18.675 37.533 1.00 0.00

ATOM 2049 C ALA A 360 -222.486 -17.846 37.863 1.00 0.00

ATOM 2050 O ALA A 360 -223.366 -18.325 38.562 1.00 0.00

ATOM 2051 CB ALA A 360 -220.122 -18.188 38.396 1.00 0.00

ATOM 2052 N GLN A 361 -222.528 -16.603 37.344 1.00 0.00

ATOM 2053 CA GLN A 361 -223.676 -15.752 37.609 1.00 0.00

ATOM 2054 C GLN A 361 -224.935 -16.404 37.107 1.00 0.00

ATOM 2055 O GLN A 361 -225.914 -16.454 37.832 1.00 0.00

ATOM 2056 CB GLN A 361 -223.515 -14.402 36.907 1.00 0.00

ATOM 2057 CG GLN A 361 -222.443 -13.511 37.515 1.00 0.00

ATOM 2058 CD GLN A 361 _ 999 991 -12.242 36.716 1.00 0.00

ATOM 2059 OEl GLN A 361 -222.812 -12.053 35.654 1.00 0.00

ATOM 2060 NE2 GLN A 361 -221.363 -11.366 37.227 1.00 0.00

ATOM 2061 N GLU A 362 -224.886 -16.913 35.859 1.00 0.00

ATOM 2062 CA GLU A 362 -226.049 -17.592 35.308 1.00 0.00

ATOM 2063 C GLU A 362 -226.468 -18.717 36.208 1.00 0.00

ATOM 2064 O GLU A 362 -227.647 -18.878 36.474 1.00 0.00

ATOM 2065 CB GLU A 362 -225.729 -18.166 33.926 1.00 0.00

ATOM 2066 CG GLU A 362 -225.560 -17.114 32.841 1.00 0.00

ATOM 2067 CD GLU A 362 -225.123 -17.710 31.517 1.00 0.00

ATOM 2068 OEl GLU A 362 -224.881 -18.934 31.466 1.00 0.00

ATOM 2069 OE2 GLU A 362 -225.022 -16.951 30.529 1.00 0.00

ATOM 2070 N TYR A 363 -225.465 -19.485 36.674 1.00 0.00

ATOM 2071 CA TYR A 363 -225.746 -20.632 37.518 1.00 0.00

ATOM 2072 C TYR A 363 -226.511 -20.231 38.748 1.00 0.00

ATOM 2073 O TYR A 363 -227.566 -20.790 39.001 1.00 0.00

ATOM 2074 CB TYR A 363 -224.445 -21.299 37.966 1.00 0.00

ATOM 2075 CG TYR A 363 -224.649 -22.483 38.885 1.00 0.00

ATOM 2076 CDl TYR A 363 -225.004 -23.725 38.377 1.00 0.00

ATOM 2077 CD2 TYR A 363 -224.486 -22.354 40.259 1.00 0.00

ATOM 2078 CEl TYR A 363 -225.192 -24.812 39.208 1.00 0.00

ATOM 2079 CE2 TYR A 363 -224.670 -23.430 41.106 1.00 0.00

ATOM 2080 CZ TYR A 363 -225.026 -24.666 40.568 1.00 0.00

ATOM 2081 OH TYR A 363 -225.213 -25.747 41.399 1.00 0.00

ATOM 2082 N GLU A 364 -225.964 -19.261 39.506 1.00 0.00

ATOM 2083 CA GLU A 364 -226.624 -18.837 40.731 1.00 0.00

ATOM 2084 C GLU A 364 -228.037 -18.401 40.458 1.00 0.00

ATOM 2085 O GLU A 364 -228.936 -18.783 41.190 1.00 0.00

ATOM 2086 CB GLU A 364 -225.875 -17.662 41.364 1.00 0.00

ATOM 2087 CG GLU A 364 -224.529 -18.034 41.963 1.00 0.00

ATOM 2088 CD GLU A 364 -223.762 -16.827 42.470 1.00 0.00

ATOM 2089 OEl GLU A 364 -224.252 -15.694 42.285 1.00 0.00

ATOM 2090 OE2 GLU A 364 -222.674 -17.016 43.050 1.00 0.00

ATOM 2091 N ALA A 365 -228.215 -17.602 39.389 1.00 0.00

ATOM 2092 CA ALA A 365 -229.545 -17.117 39.062 1.00 0.00

ATOM 2093 C ALA A 365 -230.487 -18.256 38.786 1.00 0.00

ATOM 2094 O ALA A 365 -231.549 -18.309 39.385 1.00 0.00

ATOM 2095 CB ALA A 365 -229.498 -16.233 37.826 1.00 0.00

ATOM 2096 N LEU A 366 -230.081 -19.166 37.878 1.00 0.00

ATOM 2097 CA LEU A 366 -230.941 -20.289 37.539 1.00 0.00

ATOM 2098 C LEU A 366 -231.321 -21.063 38.769 1.00 0.00

ATOM 2099 O LEU A 366 -232.475 -21.436 38.912 1.00 0.00

ATOM 2100 CB LEU A 366 -230.226 -21.240 36.578 1.00 0.00

ATOM 2101 CG LEU A 366 -229.987 -20.718 35.160 1.00 0.00

ATOM 2102 CDl LEU A 366 -229.114 -21.683 34.371 1.00 0.00

ATOM 2103 CD2 LEU A 366 -231.305 -20.553 34.418 1.00 0.00 ATOM 2104 N LEU A 367 -230.334 -21.285 39.657 1.00 0.00

ATOM 2105 CA LEU A 367 -230.608 -22.027 40.877 1.00 0.00

ATOM 2106 C LEU A 367 -231.678 -21.348 41.685 1.00 0.00

ATOM 2107 O LEU A 367 -232.623 -22.002 42.098 1.00 0.00

ATOM 2108 CB LEU A 367 -229.346 -22.126 41.738 1.00 0.00

ATOM 2109 CG LEU A 367 -229.491 -22.870 43.068 1.00 0.00

ATOM 2110 CDl LEU A 367 -229.890 -24.318 42.832 1.00 0.00

ATOM 2111 CD2 LEU A 367 -228.178 -22.857 43.836 1.00 0.00

ATOM 2112 N ASN A 368 -231.519 -20.027 41.901 1.00 0.00

ATOM 2113 CA ASN A 368 -232.501 -19.300 42.688 1.00 0.00

ATOM 2114 C ASN A 368 -233.861 -19.384 42.055 1.00 0.00

ATOM 2115 O ASN A 368 -234.829 -19.661 42.745 1.00 0.00

ATOM 2116 CB ASN A 368 -232.114 -17.824 42.797 1.00 0.00

ATOM 2117 CG ASN A 368 -230.934 -17.598 43.721 1.00 0.00

ATOM 2118 ODl ASN A 368 -230.614 -18.447 44.554 1.00 0.00

ATOM 2119 ND2 ASN A 368 -230.283 -16.449 43.578 1.00 0.00

ATOM 2120 N ILE A 369 -233.914 -19.152 40.729 1.00 0.00

ATOM 2121 CA ILE A 369 -235.185 -19.221 40.025 1.00 0.00

ATOM 2122 C ILE A 369 -235.823 -20.568 40.221 1.00 0.00

ATOM 2123 O ILE A 369 -237.006 -20.639 40.515 1.00 0.00

ATOM 2124 CB ILE A 369 -235.005 -18.997 38.512 1.00 0.00

ATOM 2125 CGl ILE A 369 -234.569 -17.558 38.233 1.00 0.00

ATOM 2126 CG2 ILE A 369 -236.312 -19.254 37.777 1.00 0.00

ATOM 2127 CDl ILE A 369 -234.109 -17.324 36.811 1.00 0.00

ATOM 2128 N LYS A 370 -235.016 -21.633 40.056 1.00 0.00

ATOM 2129 CA LYS A 370 -235.550 -22.977 40.199 1.00 0.00

ATOM 2130 C LYS A 370 -236.128 -23.188 41.571 1.00 0.00

ATOM 2131 O LYS A 370 -237.189 -23.779 41.682 1.00 0.00

ATOM 2132 CB LYS A 370 -234.449 -24.017 39.983 1.00 0.00

ATOM 2133 CG LYS A 370 -234.930 -25.457 40.069 1.00 0.00

ATOM 2134 CD LYS A 370 -233.804 -26.433 39.769 1.00 0.00

ATOM 2135 CE LYS A 370 -234.278 -27.873 39.884 1.00 0.00

ATOM 2136 NZ LYS A 370 -233.182 -28.842 39.606 1.00 0.00

ATOM 2137 N VAL A 371 -235.426 -22.692 42.609 1.00 0.00

ATOM 2138 CA VAL A 371 -235.932 -22.854 43.962 1.00 0.00

ATOM 2139 C VAL A 371 -237.309 -22.258 44.075 1.00 0.00

ATOM 2140 O VAL A 371 -238.206 -22.906 44.588 1.00 0.00

ATOM 2141 CB VAL A 371 -235.023 -22.159 44.992 1.00 0.00

ATOM 2142 CGl VAL A 371 -235.672 -22.169 46.368 1.00 0.00

ATOM 2143 CG2 VAL A 371 -233.683 -22.871 45.087 1.00 0.00

ATOM 2144 N LYS A 372 -237.463 -21.016 43.576 1.00 0.00

ATOM 2145 CA LYS A 372 -238.761 -20.368 43.644 1.00 0.00

ATOM 2146 C LYS A 372 -239.803 -21.172 42.919 1.00 0.00

ATOM 2147 O LYS A 372 -240.867 -21.412 43.469 1.00 0.00

ATOM 2148 CB LYS A 372 -238.701 -18.979 43.005 1.00 0.00

ATOM 2149 CG LYS A 372 -240.010 -18.210 43.068 1.00 0.00

ATOM 2150 CD LYS A 372 -239.861 -16.816 42.481 1.00 0.00

ATOM 2151 CE LYS A 372 -241.182 -16.064 42.501 1.00 0.00

ATOM 2152 NZ LYS A 372 -241.055 -14.705 41.907 1.00 0.00

ATOM 2153 N LEU A 373 -239.486 -21.586 41.677 1.00 0.00

ATOM 2154 CA LEU A 373 -240.465 -22.314 40.889 1.00 0.00

ATOM 2155 C LEU A 373 -240.889 -23.587 41.561 1.00 0.00

ATOM 2156 O LEU A 373 -242.079 -23.840 41.645 1.00 0.00

ATOM 2157 CB LEU A 373 -239.886 -22.679 39.521 1.00 0.00

ATOM 2158 CG LEU A 373 -239.667 -21.521 38.546 1.00 0.00

ATOM 2159 CDl LEU A 373 -238.916 -21.993 37.310 1.00 0.00

ATOM 2160 CD2 LEU A 373 -240.996 -20.934 38.099 1.00 0.00

ATOM 2161 N GLU A 374 -239.911 -24.380 42.046 1.00 0.00

ATOM 2162 CA GLU A 374 -240.256 -25.640 42.684 1.00 0.00

ATOM 2163 C GLU A 374 -241.201 -25.422 43.832 1.00 0.00

ATOM 2164 O GLU A 374 -242.158 -26.168 43.968 1.00 0.00

ATOM 2165 CB GLU A 374 -239.001 -26.329 43.223 1.00 0.00

ATOM 2166 CG GLU A 374 -238.082 -26.879 42.143 1.00 0.00

ATOM 2167 CD GLU A 374 -236.793 -27.443 42.708 1.00 0.00

ATOM 2168 OEl GLU A 374 -236.585 -27.337 43.935 1.00 0.00

ATOM 2169 OE2 GLU A 374 -235.991 -27.991 41.923 1.00 0.00

ATOM 2170 N ALA A 375 -240.929 -24.382 44.647 1.00 0.00

ATOM 2171 CA ALA A 375 -241.827 -24.088 45.750 1.00 0.00 ATOM 2172 C ALA A 375 -243.200 -23.772 45.227 1.00 0.00

ATOM 2173 O ALA A 375 -244.176 -24.293 45.744 1.00 0.00

ATOM 2174 CB ALA A 375 -241.321 -22.892 46.542 1.00 0.00

ATOM 2175 N GLU A 376 -243.259 44.184 1.00 0.00

ATOM 2176 CA GLU A 376 -244.546 -22.568 43.607 1.00 0.00

ATOM 2177 C GLU A 376 -245.259 -23.790 43.097 1.00 0.00

ATOM 2178 O GLU A 376 -246.458 -23.910 43.294 1.00 0.00

ATOM 2179 CB GLU A 376 -244.360 -21.600 42.437 1.00 0.00

ATOM 2180 CG GLU A 376 -243.920 -20.204 42.849 1.00 0.00

ATOM 2181 CD GLU A 376 -243.627 -19.311 41.660 1.00 0.00

ATOM 2182 OEl GLU A 376 -243.698 -19.803 40.515 1.00 0.00

ATOM 2183 OE2 GLU A 376 -243.328 -18.117 41.874 1.00 0.00

ATOM 2184 N ILE A 377 -244.502 -24.698 42.450 1.00 0.00

ATOM 2185 CA ILE A 377 -245.110 -25.906 41.917 1.00 0.00

ATOM 2186 C ILE A 377 -245.718 -26.715 43.027 1.00 0.00

ATOM 2187 O ILE A 377 -246.859 -27.132 42.907 1.00 0.00

ATOM 2188 CB ILE A 377 -244.074 -26.789 41.197 1.00 0.00

ATOM 2189 CGl ILE A 377 -243.577 -26.099 39.924 1.00 0.00

ATOM 2190 CG2 ILE A 377 -244.688 -28.126 40.812 1.00 0.00

ATOM 2191 CDl ILE A 377 -242.370 -26.763 39.301 1.00 0.00

ATOM 2192 N ALA A 378 -244.941 -26.924 44.109 1.00 0.00

ATOM 2193 CA ALA A 378 -245.449 -27.704 45.227 1.00 0.00

ATOM 2194 C ALA A 378 -246.749 -27.136 45.724 1.00 0.00

ATOM 2195 O ALA A 378 -247.678 -27.886 45.977 1.00 0.00

ATOM 2196 CB ALA A 378 -244.453 -27.696 46.375 1.00 0.00

ATOM 2197 N THR A 379 -246.806 -25.795 45.842 1.00 0.00

ATOM 2198 CA THR A 379 -248.034 -25.164 46.300 1.00 0.00

ATOM 2199 C THR A 379 -249.160 -25.456 45.349 1.00 0.00

ATOM 2200 O THR A 379 -250.228 -25.847 45.791 1.00 0.00

ATOM 2201 CB THR A 379 -247.880 -23.635 46.398 1.00 0.00

ATOM 2202 OGl THR A 379 -246.862 -23.314 47.355 1.00 0.00

ATOM 2203 CG2 THR A 379 -249.188 -22.995 46.839 1.00 0.00

ATOM 2204 N TYR A 380 -248.904 -25.270 44.038 1.00 0.00

ATOM 2205 CA TYR A 380 -249.941 -25.531 43.054 1.00 0.00

ATOM 2206 C TYR A 380 -250.459 -26.936 43.180 1.00 0.00

ATOM 2207 O TYR A 380 -251.661 -27.139 43.148 1.00 0.00

ATOM 2208 CB TYR A 380 -249.394 -25.348 41.637 1.00 0.00

ATOM 2209 CG TYR A 380 -249.056 -23.915 41.291 1.00 0.00

ATOM 2210 CDl TYR A 380 -249.527 -22.865 42.069 1.00 0.00

ATOM 2211 CD2 TYR A 380 -248.266 -23.618 40.188 1.00 0.00

ATOM 2212 CEl TYR A 380 -249.223 -21.553 41.760 1.00 0.00

ATOM 2213 CE2 TYR A 380 -247.951 -22.312 39.864 1.00 0.00

ATOM 2214 CZ TYR A 380 -248.437 -21.277 40.661 1.00 0.00

ATOM 2215 OH TYR A 380 -248.133 -19.971 40.352 1.00 0.00

ATOM 2216 N ARG A 381 -249.533 -27.902 43.335 1.00 0.00

ATOM 2217 CA ARG A 381 -249.951 -29.289 43.451 1.00 0.00

ATOM 2218 C ARG A 381 -250.893 -29.474 44.609 1.00 0.00

ATOM 2219 O ARG A 381 -251.934 -30.090 44.447 1.00 0.00

ATOM 2220 CB ARG A 381 -248.739 -30.197 43.674 1.00 0.00

ATOM 2221 CG ARG A 381 -247.843 -30.345 42.455 1.00 0.00

ATOM 2222 CD ARG A 381 -246.638 -31.220 42.759 1.00 0.00

ATOM 2223 NE ARG A 381 -245.740 -31.332 41.612 1.00 0.00

ATOM 2224 CZ ARG A 381 -244.587 -31.992 41.628 1.00 0.00

ATOM 2225 NHl ARG A 381 -243.835 -32.041 40.536 1.00 0.00

ATOM 2226 NH2 ARG A 381 -244.187 -32.603 42.735 1.00 0.00

ATOM 2227 N ARG A 382 -250.521 -28.924 45.782 1.00 0.00

ATOM 2228 CA ARG A 382 -251.381 -29.064 46.946 1.00 0.00

ATOM 2229 C ARG A 382 -252.741 -28.482 46.675 1.00 0.00

ATOM 2230 O ARG A 382 -253.738 -29.116 46.982 1.00 0.00

ATOM 2231 CB ARG A 382 -250.777 -28.335 48.148 1.00 0.00

ATOM CG ARG A 382 -249.535 -29.001 48.718 1.00 0.00

ATOM 2233 CD ARG A 382 -248.963 -28.201 49.877 1.00 0.00

ATOM 2234 NE ARG A 382 -247.739 -28.802 50.404 1.00 0.00

ATOM 2235 CZ ARG A 382 -247.009 -28.274 51.381 1.00 0.00

ATOM 2236 NHl ARG A 382 -245.911 -28.891 51.796 1.00 0.00

ATOM 2237 NH2 ARG A 382 -247.378 -27.130 51.941 1.00 0.00

ATOM 2238 N LEU A 383 -252.763 -27.270 46.087 1.00 0.00

ATOM 2239 CA LEU A 383 -254.033 -26.625 45.808 1.00 0.00 ATOM 2240 C LEU A 383 -254.896 -27.489 44.934 1.00 0.00

ATOM 2241 O LEU A 383 -256.062 -27.676 45.243 1.00 0.00

ATOM 2242 CB LEU A 383 -253.811 -25.293 45.089 1.00 0.00

ATOM 2243 CG LEU A 383 -253.193 -24.168 45.922 1.00 0.00

ATOM 2244 CDl LEU A 383 -252.851 -22.973 45.045 1.00 0.00

ATOM 2245 CD2 LEU A 383 -254.160 -23.704 47.001 1.00 0.00

ATOM 2246 N LEU A 384 -254.306 -28.020 43.844 1.00 0.00

ATOM 2247 CA LEU A 384 -255.085 -28.855 42.948 1.00 0.00

ATOM 2248 C LEU A 384 -255.626 -30.056 43.671 1.00 0.00

ATOM 2249 O LEU A 384 -256.762 -30.431 43.433 1.00 0.00

ATOM 2250 CB LEU A 384 -254.219 -29.346 41.786 1.00 0.00

ATOM 2251 CG LEU A 384 -254.916 -30.228 40.747 1.00 0.00

ATOM 2252 CDl LEU A 384 -256.051 -29.473 40.075 1.00 0.00

ATOM 2253 CD2 LEU A 384 -253.934 -30.668 39.671 1.00 0.00

ATOM 2254 N GLU A 385 -254.811 -30.645 44.570 1.00 0.00

ATOM 2255 CA GLU A 385 -255.289 -31.792 45.323 1.00 0.00

ATOM 2256 C GLU A 385 -256.475 -31.411 46.160 1.00 0.00

ATOM 2257 O GLU A 385 -257.491 -32.088 46.113 1.00 0.00

ATOM 2258 CB GLU A 385 -254.192 -32.320 46.249 1.00 0.00

ATOM 2259 CG GLU A 385 -254.590 -33.553 47.044 1.00 0.00

ATOM 2260 CD GLU A 385 -253.467 -34.065 47.924 1.00 0.00

ATOM 2261 OEl GLU A 385 -252.373 -33.465 47.902 1.00 0.00

ATOM 2262 OE2 GLU A 385 -253.682 -35.069 48.637 1.00 0.00

ATOM 2263 N ASP A 386 -256.333 -30.313 46.929 1.00 0.00

ATOM 2264 CA ASP A 386 -257.412 -29.912 47.815 1.00 0.00

ATOM 2265 C ASP A 386 -258.665 -29.606 47.046 1.00 0.00

ATOM 2266 O ASP A 386 -259.708 -30.154 47.368 1.00 0.00

ATOM 2267 CB ASP A 386 -257.021 -28.658 48.600 1.00 0.00

ATOM 2268 CG ASP A 386 -255.987 -28.941 49.673 1.00 0.00

ATOM 2269 ODl ASP A 386 -255.749 -30.131 49.969 1.00 0.00

ATOM 2270 OD2 ASP A 386 -255.416 -27.973 50.216 1.00 0.00

ATOM 2271 N GLY A 387 -258.556 -28.727 46.031 1.00 0.00

ATOM 2272 CA GLY A 387 -259.745 -28.343 45.289 1.00 0.00

ATOM 2273 C GLY A 387 -260.320 -29.520 44.556 1.00 0.00

ATOM 2274 O GLY A 387 -261.463 -29.880 44.795 1.00 0.00

TER 2275 GLY A 387

ATOM 2276 N ILE B 84 183.610 37.279 -26.045 1.00 0.00

ATOM 2277 CA ILE B 84 182.494 38.031 -26.603 1.00 0.00

ATOM 2278 C ILE B 84 181.712 37.275 -27.641 1.00 0.00

ATOM 2279 O ILE B 84 180.499 37.411 -27.665 1.00 0.00

ATOM 2280 CB ILE B 84 182.972 39.326 -27.285 1.00 0.00

ATOM 2281 CGl ILE B 84 183.519 40.306 -26.245 1.00 0.00

ATOM 2282 CG2 ILE B 84 181.821 39.996 -28.021 1.00 0.00

ATOM 2283 CDl ILE B 84 184.250 41.487 -26.846 1.00 0.00

ATOM 2284 N GLN B 85 182.378 36.480 -28.503 1.00 0.00

ATOM 2285 CA GLN B 85 181.608 35.708 -29.467 1.00 0.00

ATOM 2286 C GLN B 85 180.769 34.708 -28.720 1.00 0.00

ATOM 2287 O GLN B 85 179.646 34.438 -29.115 1.00 0.00

ATOM 2288 CB GLN B 85 182.539 34.970 -30.430 1.00 0.00

ATOM 2289 CG GLN B 85 181.819 34.228 -31.544 1.00 0.00

ATOM 2290 CD GLN B 85 181.062 35.161 -32.470 1.00 0.00

ATOM 2291 OEl GLN B 85 181.587 36.188 -32.898 1.00 0.00

ATOM 2292 NE2 GLN B 85 179.820 34.804 -32.779 1.00 0.00

ATOM 2293 N ALA B 86 181.329 34.181 -27.613 1.00 0.00

ATOM 2294 CA ALA B 86 180.580 33.245 -26.791 1.00 0.00

ATOM 2295 C ALA B 86 179.342 33.894 -26.238 1.00 0.00

ATOM 2296 O ALA B 86 178.271 33.315 -26.332 1.00 0.00

ATOM 2297 CB ALA B 86 181.430 32.766 -25.625 1.00 0.00

ATOM 2298 N VAL B 87 179.497 35.105 -25.667 1.00 0.00

ATOM 2299 CA VAL B 87 178.343 35.802 -25.124 1.00 0.00

ATOM 2300 C VAL B 87 177.293 35.999 -26.180 1.00 0.00

ATOM 2301 O VAL B 87 176.123 35.792 -25.907 1.00 0.00

ATOM 2302 CB VAL B 87 178.727 37.191 -24.578 1.00 0.00

ATOM 2303 CGl VAL B 87 177.481 37.977 -24.200 1.00 0.00

ATOM 2304 CG2 VAL B 87 179.603 37.054 -23.343 1.00 0.00

ATOM 2305 N ARG B 88 177.728 36.389 -27.398 1.00 0.00

ATOM 2306 CA ARG B 88 176.776 36.590 -28.478 1.00 0.00

ATOM 2307 C ARG B 88 176.012 35.329 -28.775 1.00 0.00 ATOM 2308 O ARG B 88 174.820 35.406 -29.027 1.00 0.00

ATOM 2309 CB ARG B 88 177.499 37.018 -29.757 1.00 0.00

ATOM 2310 CG ARG B 88 178.049 38.435 -29.715 1.00 0.00

ATOM 2311 CD ARG B 88 178.485 38.897 -31.095 1.00 0.00

ATOM 2312 NE ARG B 88 179.606 38.113 -31.607 1.00 0.00

ATOM 2313 CZ ARG B 88 180.883 38.383 -31.360 1.00 0.00

ATOM 2314 NHl ARG B 88 181.835 37.613 -31.868 1.00 0.00

ATOM 2315 NH2 ARG B 88 181.205 39.424 -30.604 1.00 0.00

ATOM 2316 N THR B 89 176.691 34.163 -28.731 1.00 0.00

ATOM 2317 CA THR B 89 175.984 32.913 -28.968 1.00 0.00

ATOM 2318 C THR B 89 174.886 32.750 -27.953 1.00 0.00

ATOM 2319 O THR B 89 173.798 32.315 -28.295 1.00 0.00

ATOM 2320 CB THR B 89 176.927 31.701 -28.859 1.00 0.00

ATOM 2321 OGl THR B 89 177.953 31.799 -29.854 1.00 0.00

ATOM 9099 CG2 THR B 89 176.158 30.406 -29.071 1.00 0.00

ATOM 2323 N GLN B 90 175.197 33.123 -26.695 1.00 0.00

ATOM 2324 CA GLN B 90 174.224 32.985 -25.624 1.00 0.00

ATOM 2325 C GLN B 90 173.030 33.876 -25.823 1.00 0.00

ATOM 2326 O GLN B 90 171.913 33.421 -25.641 1.00 0.00

ATOM 2327 CB GLN B 90 174.853 33.350 -24.278 1.00 0.00

ATOM 2328 CG GLN B 90 175.885 32.349 -23.783 1.00 0.00

ATOM 2329 CD GLN B 90 176.566 32.799 -22.505 1.00 0.00

ATOM 2330 OEl GLN B 90 176.343 33.912 -22.031 1.00 0.00

ATOM 2331 NE2 GLN B 90 177.401 31.932 -21.944 1.00 0.00

ATOM 2332 N GLU B 91 173.264 35.152 -26.196 1.00 0.00

ATOM 2333 CA GLU B 91 172.145 36.068 -26.363 1.00 0.00

ATOM 2334 C GLU B 91 171.242 35.611 -27.473 1.00 0.00

ATOM 2335 O GLU B 91 170.033 35.717 -27.348 1.00 0.00

ATOM 2336 CB GLU B 91 172.648 37.472 -26.701 1.00 0.00

ATOM 2337 CG GLU B 91 173.334 38.181 -25.544 1.00 0.00

ATOM 2338 CD GLU B 91 173.926 39.517 -25.949 1.00 0.00

ATOM 2339 OEl GLU B 91 173.865 39.855 -27.150 1.00 0.00

ATOM 2340 OE2 GLU B 91 174.452 40.225 -25.064 1.00 0.00

ATOM 2341 N LYS B 92 171.848 35.089 -28.558 1.00 0.00

ATOM 2342 CA LYS B 92 171.042 34.583 -29.657 1.00 0.00

ATOM 2343 C LYS B 92 170.188 33.439 -29.188 1.00 0.00

ATOM 2344 O LYS B 92 169.056 33.309 -29.623 1.00 0.00

ATOM 2345 CB LYS B 92 171.938 34.090 -30.795 1.00 0.00

ATOM 2346 CG LYS B 92 172.660 35.199 -31.542 1.00 0.00

ATOM 2347 CD LYS B 92 173.528 34.640 -32.658 1.00 0.00

ATOM 2348 CE LYS B 92 174.269 35.748 -33.390 1.00 0.00

ATOM 2349 NZ LYS B 92 175.149 35.211 -34.463 1.00 0.00

ATOM 2350 N GLU B 93 170.752 32.613 -28.283 1.00 0.00

ATOM 2351 CA GLU B 93 170.004 31.475 -27.782 1.00 0.00

ATOM 2352 C GLU B 93 168.867 31.927 -26.908 1.00 0.00

ATOM 2353 O GLU B 93 167.750 31.475 -27.103 1.00 0.00

ATOM 2354 CB GLU B 93 170.910 30.560 -26.956 1.00 0.00

ATOM 2355 CG GLU B 93 171.946 29.809 -21.llξ> 1.00 0.00

ATOM 2356 CD GLU B 93 172.916 29.026 -26.913 1.00 0.00

ATOM 2357 OEl GLU B 93 172.819 29.124 -25.671 1.00 0.00

ATOM 2358 OE2 GLU B 93 173.771 28.312 -21.ill 1.00 0.00

ATOM 2359 N GLN B 94 169.156 32.826 -25.945 1.00 0.00

ATOM 2360 CA GLN B 94 168.099 33.292 -25.061 1.00 0.00

ATOM 2361 C GLN B 94 167.004 33.947 -25.854 1.00 0.00

ATOM 2362 O GLN B 94 165.836 33.727 -25.566 1.00 0.00

ATOM 2363 CB GLN B 94 168.647 34.310 -24.060 1.00 0.00

ATOM 2364 CG GLN B 94 169.564 33.711 -23.004 1.00 0.00

ATOM 2365 CD GLN B 94 170.177 34.762 -22.101 1.00 0.00

ATOM 2366 OEl GLN B 94 169.993 35.961 -22.312 1.00 0.00

ATOM 2367 NE2 GLN B 94 170.912 34.316 -21.088 1.00 0.00

ATOM 2368 N ILE B 95 167.399 34.744 -26.866 1.00 0.00

ATOM 2369 CA ILE B 95 166.411 35.407 -27.699 1.00 0.00

ATOM 2370 C ILE B 95 165.511 34.402 -28.362 1.00 0.00

ATOM 2371 O ILE B 95 164.303 34.576 -28.337 1.00 0.00

ATOM 2372 CB ILE B 95 167.078 36.243 -28.807 1.00 0.00

ATOM 2373 CGl ILE B 95 167.827 37.431 -28.202 1.00 0.00

ATOM 2374 CG2 ILE B 95 166.032 36.776 -29.774 1.00 0.00

ATOM 2375 CDl ILE B 95 168.730 38.149 -29.182 1.00 0.00 ATOM 2376 N LYS B 96 166.110 33.347 -28.951 1.00 0.00

ATOM 2377 CA LYS B 96 165.298 32.337 -29.610 1.00 0.00

ATOM 2378 C LYS B 96 164.295 31.749 -28.658 1.00 0.00

ATOM 2379 O LYS B 96 163.134 31.630 -29.015 1.00 0.00

ATOM 2380 CB LYS B 96 166.179 31.203 -30.139 1.00 0.00

ATOM 2381 CG LYS B 96 165.415 30.119 -30.881 1.00 0.00

ATOM 2382 CD LYS B 96 166.356 29.063 -31.438 1.00 0.00

ATOM 2383 CE LYS B 96 165.589 27.953 -32.138 1.00 0.00

ATOM 2384 NZ LYS B 96 166.497 26.899 -32.668 1.00 0.00

ATOM 2385 N THR B 97 164.749 31.397 -27.437 1.00 0.00

ATOM 2386 CA THR B 97 163.827 30.845 -26.456 1.00 0.00

ATOM 2387 C THR B 97 162.703 31.806 -26.181 1.00 0.00

ATOM 2388 O THR B 97 161.563 31.380 -26.086 1.00 0.00

ATOM 2389 CB THR B 97 164.533 30.554 -25.119 1.00 0.00

ATOM 2390 OGl THR B 97 165.565 29.579 -25.323 1.00 0.00

ATOM 2391 CG2 THR B 97 163.541 30.015 -24.099 1.00 0.00

ATOM 2392 N LEU B 98 163.031 33.110 -26.067 1.00 0.00

ATOM 2393 CA LEU B 98 161.994 34.095 -25.799 1.00 0.00

ATOM 2394 C LEU B 98 160.995 34.141 -26.922 1.00 0.00

ATOM 2395 O LEU B 98 159.804 34.109 -26.659 1.00 0.00

ATOM 2396 CB LEU B 98 162.606 35.488 -25.645 1.00 0.00

ATOM 2397 CG LEU B 98 163.440 35.727 -24.384 1.00 0.00

ATOM 2398 CDl LEU B 98 164.141 37.077 -24.451 1.00 0.00

ATOM 2399 CD2 LEU B 98 162.558 35.711 -23.145 1.00 0.00

ATOM 2400 N ASN B 99 161.488 34.210 -28.175 1.00 0.00

ATOM 2401 CA ASN B 99 160.581 34.285 -29.311 1.00 0.00

ATOM 2402 C ASN B 99 159.651 33.104 -29.351 1.00 0.00

ATOM 2403 O ASN B 99 158.472 33.284 -29.610 1.00 0.00

ATOM 2404 CB ASN B 99 161.368 34.310 -30.623 1.00 0.00

ATOM 2405 CG ASN B 99 162.065 35.634 -30.859 1.00 0.00

ATOM 2406 ODl ASN B 99 161.700 36.653 -30.271 1.00 0.00

ATOM 2407 ND2 ASN B 99 163.074 35.626 -31.724 1.00 0.00

ATOM 2408 N ASN B 100 160.187 31.894 -29.088 1.00 0.00

ATOM 2409 CA ASN B 100 159.340 30.713 -29.101 1.00 0.00

ATOM 2410 C ASN B 100 158.282 30.835 -28.040 1.00 0.00

ATOM 2411 O ASN B 100 157.121 30.573 -28.311 1.00 0.00

ATOM 2412 CB ASN B 100 160.168 29.455 -28.830 1.00 0.00

ATOM 2413 CG ASN B 100 161.041 29.068 -30.008 1.00 0.00

ATOM 2414 ODl ASN B 100 160.798 29.490 -31.138 1.00 0.00

ATOM 2415 ND2 ASN B 100 162.062 28.262 -29.745 1.00 0.00

ATOM 2416 N LYS B 101 158.708 31.255 -26.831 1.00 0.00

ATOM 2417 CA LYS B 101 157.755 31.462 -25.753 1.00 0.00

ATOM 2418 C LYS B 101 156.658 32.384 -26.208 1.00 0.00

ATOM 2419 O LYS B 101 155.491 32.060 -26.053 1.00 0.00

ATOM 2420 CB LYS B 101 158.447 32.083 -24.538 1.00 0.00

ATOM 2421 CG LYS B 101 159.398 31.144 -23.817 1.00 0.00

ATOM 2422 CD LYS B 101 160.026 31.815 -22.607 1.00 0.00

ATOM 2423 CE LYS B 101 160.960 30.868 -21.871 1.00 0.00

ATOM 2424 NZ LYS B 101 161.625 31.529 -20.715 1.00 0.00

ATOM 2425 N PHE B 102 157.060 33.535 -26.782 1.00 0.00

ATOM 2426 CA PHE B 102 156.090 34.514 -27.248 1.00 0.00

ATOM 2427 C PHE B 102 155.076 33.899 -28.175 1.00 0.00

ATOM 2428 O PHE B 102 153.894 34.144 -27.997 1.00 0.00

ATOM 2429 CB PHE B 102 156.790 35.644 -28.006 1.00 0.00

ATOM 2430 CG PHE B 102 157.443 36.660 -27.113 1.00 0.00

ATOM 2431 CDl PHE B 102 158.807 36.624 -26.882 1.00 0.00

ATOM 2432 CD2 PHE B 102 156.693 37.651 -26.504 1.00 0.00

ATOM 2433 CEl PHE B 102 159.408 37.559 -26.060 1.00 0.00

ATOM 2434 CE2 PHE B 102 157.294 38.585 -25.682 1.00 0.00

ATOM 2435 CZ PHE B 102 158.645 38.543 -25.459 1.00 0.00

ATOM 2436 N ALA B 103 155.541 33.100 -29.155 1.00 0.00

ATOM 2437 CA ALA B 103 154.601 32.474 -30.071 1.00 0.00

ATOM 2438 C ALA B 103 153.595 31.658 -29.306 1.00 0.00

ATOM 2439 O ALA B 103 152.404 31.807 -29.529 1.00 0.00

ATOM 2440 CB ALA B 103 155.333 31.558 -31.039 1.00 0.00

ATOM 2441 N SER B 104 154.097 30.802 -28.394 1.00 0.00

ATOM 2442 CA SER B 104 153.207 29.959 -27.613 1.00 0.00

ATOM 2443 C SER B 104 152.187 30.768 -26.861 1.00 0.00 ATOM 2444 O SER B 104 151.002 30.528 -27.029 1.00 0.00

ATOM 2445 CB SER B 104 154.002 29.144 -26.591 1.00 0.00

ATOM 2446 OG SER B 104 154.847 28.204 -27.233 1.00 0.00

ATOM 2447 N PHE B 105 152.652 31.728 -26.034 1.00 0.00

ATOM 2448 CA PHE B 105 151.721 32.520 -25.241 1.00 0.00

ATOM 2449 C PHE B 105 150.684 33.187 -26.101 1.00 0.00

ATOM 2450 O PHE B 105 149.538 33.273 -25.691 1.00 0.00

ATOM 2451 CB PHE B 105 152.467 33.615 -24.475 1.00 0.00

ATOM 2452 CG PHE B 105 153.174 33.120 -23.247 1.00 0.00

ATOM 2453 CDl PHE B 105 154.541 32.893 -23.260 1.00 0.00

ATOM 2454 CD2 PHE B 105 152.475 32.880 -22.077 1.00 0.00

ATOM 2455 CEl PHE B 105 155.192 32.438 -22.130 1.00 0.00

ATOM 2456 CE2 PHE B 105 153.127 32.425 -20.946 1.00 0.00

ATOM 2457 CZ PHE B 105 154.479 32.204 -20.969 1.00 0.00

ATOM 2458 N ILE B 106 151.085 33.659 -27.299 1.00 0.00

ATOM 2459 CA ILE B 106 150.129 34.341 -28.156 1.00 0.00

ATOM 2460 C ILE B 106 149.090 33.385 -28.676 1.00 0.00

ATOM 2461 O ILE B 106 147.925 33.741 -28.726 1.00 0.00

ATOM 2462 CB ILE B 106 150.819 34.985 -29.373 1.00 0.00

ATOM 2463 CGl ILE B 106 151.721 36.137 -28.925 1.00 0.00

ATOM 2464 CG2 ILE B 106 149.785 35.532 -30.344 1.00 0.00

ATOM 2465 CDl ILE B 106 152.636 36.654 -30.014 1.00 0.00

ATOM 2466 N ASP B 107 149.518 32.165 -29.055 1.00 0.00

ATOM 2467 CA ASP B 107 148.555 31.182 -29.520 1.00 0.00

ATOM 2468 C ASP B 107 147.598 30.846 -28.410 1.00 0.00

ATOM 2469 O ASP B 107 146.397 30.842 -28.630 1.00 0.00

ATOM 2470 CB ASP B 107 149.266 29.902 -29.963 1.00 0.00

ATOM 2471 CG ASP B 107 150.012 30.074 -31.272 1.00 0.00

ATOM 2472 ODl ASP B 107 149.789 31.097 -31.954 1.00 0.00

ATOM 2473 OD2 ASP B 107 150.821 29.186 -31.615 1.00 0.00

ATOM 2474 N LYS B 108 148.151 30.581 -27.209 1.00 0.00

ATOM 2475 CA LYS B 108 147.307 30.260 -26.066 1.00 0.00

ATOM 2476 C LYS B 108 146.310 31.357 -25.809 1.00 0.00

ATOM 2477 O LYS B 108 145.150 31.065 -25.567 1.00 0.00

ATOM 2478 CB LYS B 108 148.157 30.081 -24.807 1.00 0.00

ATOM 2479 CG LYS B 108 149.013 28.826 -24.808 1.00 0.00

ATOM 2480 CD LYS B 108 149.827 28.710 -23.529 1.00 0.00

ATOM 2481 CE LYS B 108 150.702 27.467 -23.542 1.00 0.00

ATOM 2482 NZ LYS B 108 151.530 27.359 -22.309 1.00 0.00

ATOM 2483 N VAL B 109 146.773 32.621 -25.870 1.00 0.00

ATOM 2484 CA VAL B 109 145.874 33.733 -25.610 1.00 0.00

ATOM 2485 C VAL B 109 144.793 33.816 -26.651 1.00 0.00

ATOM 2486 O VAL B 109 143.666 34.141 -26.312 1.00 0.00

ATOM 2487 CB VAL B 109 146.624 35.078 -25.614 1.00 0.00

ATOM 2488 CGl VAL B 109 145.641 36.237 -25.539 1.00 0.00

ATOM 2489 CG2 VAL B 109 147.564 35.167 -24.422 1.00 0.00

ATOM 2490 N ARG B 110 145.137 33.515 -27.920 1.00 0.00

ATOM 2491 CA ARG B 110 144.125 33.545 -28.963 1.00 0.00

ATOM 2492 C ARG B 110 143.037 32.566 -28.624 1.00 0.00

ATOM 2493 O ARG B 110 141.869 32.919 -28.676 1.00 0.00

ATOM 2494 CB ARG B 110 144.736 33.165 -30.313 1.00 0.00

ATOM 2495 CG ARG B 110 145.670 34.218 -30.889 1.00 0.00

ATOM 2496 CD ARG B 110 146.276 33.758 -32.205 1.00 0.00

ATOM 2497 NE ARG B 110 147.213 34.738 -32.748 1.00 0.00

ATOM 2498 CZ ARG B 110 147.922 34.559 -33.858 1.00 0.00

ATOM 2499 NHl ARG B 110 148.750 35.506 -34.276 1.00 0.00

ATOM 2500 NH2 ARG B 110 147.800 33.433 -34.547 1.00 0.00

ATOM 2501 N PHE B 111 143.438 31.332 -28.257 1.00 0.00

ATOM 2502 CA PHE B 111 142.454 30.330 -27.887 1.00 0.00

ATOM 2503 C PHE B 111 141.608 30.794 -26.733 1.00 0.00

ATOM 2504 O PHE B 111 140.393 30.727 -26.827 1.00 0.00

ATOM 2505 CB PHE B 111 143.144 29.028 -27.473 1.00 0.00

ATOM 2506 CG PHE B 111 142.193 27.951 -27.036 1.00 0.00

ATOM 2507 CDl PHE B 111 141.506 27.194 -27.969 1.00 0.00

ATOM 2508 CD2 PHE B 111 141.985 27.696 -25.692 1.00 0.00

ATOM 2509 CEl PHE B 111 140.631 26.202 -27.566 1.00 0.00

ATOM 2510 CE2 PHE B 111 141.110 26.705 -25.289 1.00 0.00

ATOM 2511 CZ PHE B 111 140.434 25.959 -26.219 1.00 0.00 ATOM 2512 N LEU B 112 142.256 31.267 -25.648 1.00 0.00

ATOM 2513 CA LEU B 112 141.500 31.696 -24.481 1.00 0.00

ATOM 2514 C LEU B 112 140.501 32.760 -24.839 1.00 0.00

ATOM 2515 O LEU B 112 139.410 32.755 -24.295 1.00 0.00

ATOM 2516 CB LEU B 112 142.437 32.267 -23.415 1.00 0.00

ATOM 2517 CG LEU B 112 143.358 31.265 -22.716 1.00 0.00

ATOM 2518 CDl LEU B 112 144.355 31.985 -21.820 1.00 0.00

ATOM 2519 CD2 LEU B 112 142.554 30.303 -21.856 1.00 0.00

ATOM 2520 N GLU B 113 140.871 33.669 -25.763 1.00 0.00

ATOM 2521 CA GLU B 113 139.939 34.718 -26.142 1.00 0.00

ATOM 2522 C GLU B 113 138.795 34.158 -26.938 1.00 0.00

ATOM 2523 O GLU B 113 137.687 34.657 -26.825 1.00 0.00

ATOM 2524 CB GLU B 113 140.642 35.776 -26.995 1.00 0.00

ATOM 2525 CG GLU B 113 141.643 36.627 -26.230 1.00 0.00

ATOM 2526 CD GLU B 113 142.385 37.601 -27.124 1.00 0.00

ATOM 2527 OEl GLU B 113 142.161 37.567 -28.352 1.00 0.00

ATOM 2528 OE2 GLU B 113 143.189 38.397 -26.597 1.00 0.00

ATOM 2529 N GLN B 114 139.064 33.107 -27.738 1.00 0.00

ATOM 2530 CA GLN B 114 137.983 32.481 -28.478 1.00 0.00

ATOM 2531 C GLN B 114 137.019 31.850 -27.512 1.00 0.00

ATOM 2532 O GLN B 114 135.823 32.060 -27.633 1.00 0.00

ATOM 2533 CB GLN B 114 138.531 31.402 -29.415 1.00 0.00

ATOM 2534 CG GLN B 114 139.334 31.944 -30.585 1.00 0.00

ATOM 2535 CD GLN B 114 139.984 30.846 -31.405 1.00 0.00

ATOM 2536 OEl GLN B 114 139.925 29.670 -31.043 1.00 0.00

ATOM 2537 NE2 GLN B 114 140.606 31.227 -32.514 1.00 0.00

ATOM 2538 N GLN B 115 137.557 31.082 -26.542 1.00 0.00

ATOM 2539 CA GLN B 115 136.698 30.438 -25.561 1.00 0.00

ATOM 2540 C GLN B 115 135.920 31.452 -24.770 1.00 0.00

ATOM 2541 O GLN B 115 134.761 31.212 -24.466 1.00 0.00

ATOM 2542 CB GLN B 115 137.531 29.609 -24.581 1.00 0.00

ATOM 2543 CG GLN B 115 136.705 28.806 -23.589 1.00 0.00

ATOM 2544 CD GLN B 115 135.847 27.753 -24.263 1.00 0.00

ATOM 2545 OEl GLN B 115 136.316 27.020 -25.133 1.00 0.00

ATOM 2546 NE2 GLN B 115 134.584 27.675 -23.860 1.00 0.00

ATOM 2547 N ASN B 116 136.563 32.591 -24.441 1.00 0.00

ATOM 2548 CA ASN B 116 135.865 33.620 -23.683 1.00 0.00

ATOM 2549 C ASN B 116 134.714 34.155 -24.484 1.00 0.00

ATOM 2550 O ASN B 116 133.617 34.256 -23.961 1.00 0.00

ATOM 2551 CB ASN B 116 136.812 34.775 -23.352 1.00 0.00

ATOM 2552 CG ASN B 116 137.822 34.413 -22.282 1.00 0.00

ATOM 2553 ODl ASN B 116 137.628 33.458 -21.529 1.00 0.00

ATOM 2554 ND2 ASN B 116 138.907 35.176 -22.211 1.00 0.00

ATOM 2555 N LYS B 117 134.979 34.489 -25.763 1.00 0.00

ATOM 2556 CA LYS B 117 133.913 34.995 -26.611 1.00 0.00

ATOM 2557 C LYS B 117 132.746 34.047 -26.621 1.00 0.00

ATOM 2558 O LYS B 117 131.614 34.490 -26.520 1.00 0.00

ATOM 2559 CB LYS B 117 134.407 35.164 -28.049 1.00 0.00

ATOM 2560 CG LYS B 117 133.361 35.721 -29.002 1.00 0.00

ATOM 2561 CD LYS B 117 133.939 35.934 -30.392 1.00 0.00

ATOM 2562 CE LYS B 117 132.886 36.459 -31.353 1.00 0.00

ATOM 2563 NZ LYS B 117 133.440 36.679 -32.718 1.00 0.00

ATOM 2564 N MET B 118 133.034 32.734 -26.723 1.00 0.00

ATOM 2565 CA MET B 118 131.958 31.756 -26.724 1.00 0.00

ATOM 2566 C MET B 118 131.185 31.797 -25.436 1.00 0.00

ATOM 2567 O MET B 118 129.964 31.828 -25.476 1.00 0.00

ATOM 2568 CB MET B 118 132.518 30.343 -26.896 1.00 0.00

ATOM 2569 CG MET B 118 133.097 30.068 -28.275 1.00 0.00

ATOM 2570 SD MET B 118 133.864 28.441 -28.395 1.00 0.00

ATOM 2571 CE MET B 118 132.426 27.379 -28.275 1.00 0.00

ATOM 2572 N LEU B 119 131.901 31.800 -24.295 1.00 0.00

ATOM 2573 CA LEU B 119 131.212 31.809 -23.014 1.00 0.00

ATOM 2574 C LEU B 119 130.310 33.006 -22.897 1.00 0.00

ATOM 2575 O LEU B 119 129.202 32.870 -22.403 1.00 0.00

ATOM 2576 CB LEU B 119 132.219 31.856 -21.864 1.00 0.00

ATOM 2577 CG LEU B 119 133.059 30.596 -21.646 1.00 0.00

ATOM 2578 CDl LEU B 119 134.135 30.842 -20.600 1.00 0.00

ATOM 2579 CD2 LEU B 119 132.187 29.445 -21.170 1.00 0.00 ATOM 2580 N GLU B 120 130.791 34.175 -23.364 1.00 0.00

ATOM 2581 CA GLU B 120 129.976 35.376 -23.277 1.00 0.00

ATOM 2582 C GLU B 120 128.696 35.209 -24.048 1.00 0.00

ATOM 2583 O GLU B 120 127.639 35.508 -23.513 1.00 0.00

ATOM 2584 CB GLU B 120 130.729 36.577 -23.851 1.00 0.00

ATOM 2585 CG GLU B 120 129.968 37.890 -23.758 1.00 0.00

ATOM 2586 CD GLU B 120 130.758 39.062 -24.306 1.00 0.00

ATOM 2587 OEl GLU B 120 131.908 38.850 -24.746 1.00 0.00

ATOM 2588 OE2 GLU B 120 130.228 40.193 -24.295 1.00 0.00

ATOM 2589 N THR B 121 128.789 34.717 -25.300 1.00 0.00

ATOM 2590 CA THR B 121 127.579 34.497 -26.077 1.00 0.00

ATOM 2591 C THR B 121 126.634 33.603 -25.322 1.00 0.00

ATOM 2592 O THR B 121 125.475 33.956 -25.171 1.00 0.00

ATOM 2593 CB THR B 121 127.891 33.831 -27.430 1.00 0.00

ATOM 2594 OGl THR B 121 128.737 34.689 -28.205 1.00 0.00

ATOM 2595 CG2 THR B 121 126.607 33.574 -28.205 1.00 0.00

ATOM 2596 N LYS B 122 127.144 32.453 -24.835 1.00 0.00

ATOM 2597 CA LYS B 122 126.291 31.527 -24.103 1.00 0.00

ATOM 2598 C LYS B 122 125.638 32.177 -22.913 1.00 0.00

ATOM 2599 O LYS B 122 124.455 31.968 -22.694 1.00 0.00

ATOM 2600 CB LYS B 122 127.106 30.339 -23.591 1.00 0.00

ATOM 2601 CG LYS B 122 127.575 29.391 -24.683 1.00 0.00

ATOM 2602 CD LYS B 122 128.374 28.234 -24.105 1.00 0.00

ATOM 2603 CE LYS B 122 128.864 27.300 -25.199 1.00 0.00

ATOM 2604 NZ LYS B 122 129.678 26.180 -24.649 1.00 0.00

ATOM 2605 N TRP B 123 126.416 32.965 -22.146 1.00 0.00

ATOM 2606 CA TRP B 123 125.873 33.581 -20.945 1.00 0.00

ATOM 2607 C TRP B 123 124.795 34.577 -21.274 1.00 0.00

ATOM 2608 O TRP B 123 123.844 34.694 -20.519 1.00 0.00

ATOM 2609 CB TRP B 123 126.973 34.316 -20.176 1.00 0.00

ATOM 2610 CG TRP B 123 126.478 35.026 -18.953 1.00 0.00

ATOM 2611 CDl TRP B 123 126.271 34.484 -17.718 1.00 0.00

ATOM 2612 CD2 TRP B 123 126.127 36.412 -18.848 1.00 0.00

ATOM 2613 NEl TRP B 123 125.814 35.444 -16.849 1.00 0.00

ATOM 2614 CE2 TRP B 123 125.716 36.638 -17.520 1.00 0.00

ATOM 2615 CE3 TRP B 123 126.119 37.483 -19.746 1.00 0.00

ATOM 2616 CZ2 TRP B 123 125.303 37.890 -17.068 1.00 0.00

ATOM 2617 CZ3 TRP B 123 125.709 38.723 -19.295 1.00 0.00

ATOM 2618 CH2 TRP B 123 125.306 38.919 -17.969 1.00 0.00

ATOM 2619 N SER B 124 124.940 35.289 -22.410 1.00 0.00

ATOM 2620 CA SER B 124 123.909 36.242 -22.783 1.00 0.00

ATOM 2621 C SER B 124 122.630 35.512 -23.074 1.00 0.00

ATOM 2622 O SER B 124 121.596 35.876 -22.539 1.00 0.00

ATOM 2623 CB SER B 124 124.328 37.024 -24.029 1.00 0.00

ATOM 2624 OG SER B 124 125.444 37.856 -23.759 1.00 0.00

ATOM 2625 N LEU B 125 122.720 34.472 -23.929 1.00 0.00

ATOM 2626 CA LEU B 125 121.523 33.735 -24.295 1.00 0.00

ATOM 2627 C LEU B 125 120.857 33.169 -23.077 1.00 0.00

ATOM 2628 O LEU B 125 119.693 33.458 -22.847 1.00 0.00

ATOM 2629 CB LEU B 125 121.873 32.578 -25.234 1.00 0.00

ATOM 2630 CG LEU B 125 120.712 31.677 -25.661 1.00 0.00

ATOM 2631 CDl LEU B 125 119.683 32.466 -26.455 1.00 0.00

ATOM 2632 CD2 LEU B 125 121.211 30.535 -26.532 1.00 0.00

ATOM 2633 N LEU B 126 121.610 32.370 -22.293 1.00 0.00

ATOM 2634 CA LEU B 126 121.045 31.822 -21.072 1.00 0.00

ATOM 2635 C LEU B 126 120.486 32.931 -20.226 1.00 0.00

ATOM 2636 O LEU B 126 119.286 32.985 -20.005 1.00 0.00

ATOM 2637 CB LEU B 126 122.119 31.084 -20.270 1.00 0.00

ATOM 2638 CG LEU B 126 122.762 29.874 -20.949 1.00 0.00

ATOM 2639 CDl LEU B 126 123.896 29.320 -20.101 1.00 0.00

ATOM 2640 CD2 LEU B 126 121.738 28.767 -21.155 1.00 0.00

TER 2641 LEU B 126

ATOM 2642 N ASP B 137 104.875 26.869 -20.649 1.00 0.00

ATOM 2643 CA ASP B 137 104.067 28.084 -20.667 1.00 0.00

ATOM 2644 C ASP B 137 102.867 27.955 -21.612 1.00 0.00

ATOM 2645 O ASP B 137 101.745 27.739 -21.158 1.00 0.00

ATOM 2646 CB ASP B 137 104.903 29.276 -21.136 1.00 0.00

ATOM 2647 CG ASP B 137 105.917 29.719 -20.099 1.00 0.00 ATOM 2648 ODl ASP B 137 105.837 29.243 -18.948 1.00 0.00

ATOM 2649 OD2 ASP B 137 106.792 30.544 -20.439 1.00 0.00

ATOM 2650 N ASN B 138 103.098 28.087 -22.923 1.00 0.00

ATOM 2651 CA ASN B 138 102.009 27.990 -23.901 1.00 0.00

ATOM 2652 C ASN B 138 101.072 26.853 -23.501 1.00 0.00

ATOM 2653 O ASN B 138 99.873 26.860 -23.812 1.00 0.00

ATOM 2654 CB ASN B 138 102.568 27.710 -25.298 1.00 0.00

ATOM 2655 CG ASN B 138 103.236 28.924 -25.913 1.00 0.00

ATOM 2656 ODl ASN B 138 103.031 30.051 -25.463 1.00 0.00

ATOM 2657 ND2 ASN B 138 104.039 28.696 -26.946 1.00 0.00

ATOM 2658 N MET B 139 101.645 25.887 -22.787 1.00 0.00

ATOM 2659 CA MET B 139 100.891 24.749 -22.299 1.00 0.00

ATOM 2660 C MET B 139 99.874 25.215 -21.284 1.00 0.00

ATOM 2661 O MET B 139 98.671 25.175 -21.532 1.00 0.00

ATOM 2662 CB MET B 139 101.824 23.732 -21.637 1.00 0.00

ATOM 2663 CG MET B 139 101.132 22.456 -21.190 1.00 0.00

ATOM 2664 SD MET B 139 102.266 21.283 -20.420 1.00 0.00

ATOM 2665 CE MET B 139 103.224 20.758 -21.839 1.00 0.00

ATOM 2666 N PHE B 140 100.344 25.677 -20.132 1.00 0.00

ATOM 2667 CA PHE B 140 99.413 26.143 -19.128 1.00 0.00

ATOM 2668 C PHE B 140 98.432 27.182 -19.649 1.00 0.00

ATOM 2669 O PHE B 140 97.335 27.313 -19.115 1.00 0.00

ATOM 2670 CB PHE B 140 100.162 26.786 -17.960 1.00 0.00

ATOM 2671 CG PHE B 140 100.839 25.796 -17.055 1.00 0.00

ATOM 2672 CDl PHE B 140 102.208 25.602 -17.118 1.00 0.00

ATOM 2673 CD2 PHE B 140 100.106 25.058 -16.142 1.00 0.00

ATOM 2674 CEl PHE B 140 102.830 24.691 -16.285 1.00 0.00

ATOM 2675 CE2 PHE B 140 100.728 24.146 -15.309 1.00 0.00

ATOM 2676 CZ PHE B 140 102.084 23.962 -15.378 1.00 0.00

ATOM 2677 N GLU B 141 98.799 27.925 -20.689 1.00 0.00

ATOM 2678 CA GLU B 141 97.858 28.905 -21.220 1.00 0.00

ATOM 2679 C GLU B 141 96.753 28.133 -21.909 1.00 0.00

ATOM 2680 O GLU B 141 95.613 28.578 -21.965 1.00 0.00

ATOM 2681 CB GLU B 141 98.556 29.830 -22.219 1.00 0.00

ATOM 2682 CG GLU B 141 99.549 30.790 -21.585 1.00 0.00

ATOM 2683 CD GLU B 141 100.287 31.627 -22.612 1.00 0.00

ATOM 2684 OEl GLU B 141 100.066 31.413 -23.822 1.00 0.00

ATOM 2685 OE2 GLU B 141 101.086 32.497 -22.207 1.00 0.00

ATOM 2686 N SER B 142 97.097 26.974 -22.450 1.00 0.00

ATOM 2687 CA SER B 142 96.088 26.171 -23.111 1.00 0.00

ATOM 2688 C SER B 142 95.109 25.651 -22.061 1.00 0.00

ATOM 2689 O SER B 142 93.893 25.738 -22.224 1.00 0.00

ATOM 2690 CB SER B 142 96.733 24.986 -23.832 1.00 0.00

ATOM 2691 OG SER B 142 97.547 25.425 -24.907 1.00 0.00

ATOM 2692 N TYR B 143 95.660 25.095 -20.986 1.00 0.00

ATOM 2693 CA TYR B 143 94.862 24.576 -19.882 1.00 0.00

ATOM 2694 C TYR B 143 93.904 25.666 -19.362 1.00 0.00

ATOM 2695 O TYR B 143 92.677 25.494 -19.379 1.00 0.00

ATOM 2696 CB TYR B 143 95.765 24.131 -18.730 1.00 0.00

ATOM 2697 CG TYR B 143 95.012 23.640 -17.515 1.00 0.00

ATOM 2698 CDl TYR B 143 94.479 22.357 -17.478 1.00 0.00

ATOM 2699 CD2 TYR B 143 94.834 24.460 -16.409 1.00 0.00

ATOM 2700 CEl TYR B 143 93.789 21.900 -16.371 1.00 0.00

ATOM 2701 CE2 TYR B 143 94.147 24.020 -15.293 1.00 0.00

ATOM 2702 CZ TYR B 143 93.623 22.728 -15.283 1.00 0.00

ATOM 2703 OH TYR B 143 92.937 22.274 -14.180 1.00 0.00

ATOM 2704 N ILE B 144 94.409 26.733 -19.261 1.00 0.00

ATOM 2705 CA ILE B 144 93.718 27.946 -18.831 1.00 0.00

ATOM 2706 C ILE B 144 92.484 28.233 -19.695 1.00 0.00

ATOM 2707 O ILE B 144 91.360 27.966 -19.273 1.00 0.00

ATOM 2708 CB ILE B 144 94.635 29.180 -18.921 1.00 0.00

ATOM 2709 CGl ILE B 144 95.795 29.055 -17.932 1.00 0.00

ATOM 2710 CG2 ILE B 144 93.858 30.446 -18.594 1.00 0.00

ATOM 2711 CDl ILE B 144 96.881 30.088 -18.131 1.00 0.00

ATOM 2712 N ASN B 145 92.689 28.776 -20.900 1.00 0.00

ATOM 2713 CA ASN B 145 91.569 29.097 -21.791 1.00 0.00

ATOM 2714 C ASN B 145 90.541 27.968 -21.734 1.00 0.00

ATOM 2715 O ASN B 145 89.340 28.172 -21.955 1.00 0.00 ATOM 2716 CB ASN B 145 92.058 29.256 -23.231 1.00 0.00

ATOM 2717 CG ASN B 145 92.820 30.548 -23.449 1.00 0.00

ATOM 2718 ODl ASN B 145 92.734 31.473 -22.641 1.00 0.00

ATOM 2719 ND2 ASN B 145 93.568 30.615 -24.544 1.00 0.00

ATOM 2720 N ASN B 146 91.040 26.777 -21.413 1.00 0.00

ATOM 2721 CA ASN B 146 90.200 25.605 -21.286 1.00 0.00

ATOM 2722 C ASN B 146 89.261 25.783 -20.115 1.00 0.00

ATOM 2723 O ASN B 146 88.053 25.924 -20.292 1.00 0.00

ATOM 2724 CB ASN B 146 91.054 24.356 -21.053 1.00 0.00

ATOM 2725 CG ASN B 146 90.239 23.078 -21.097 1.00 0.00

ATOM 2726 ODl ASN B 146 89.019 23.102 -20.933 1.00 0.00

ATOM 2727 ND2 ASN B 146 90.914 21.955 -21.316 1.00 0.00

ATOM 2728 N LEU B 147 89.804 25.797 -18.906 1.00 0.00

ATOM 2729 CA LEU B 147 88.948 25.972 -17.752 1.00 0.00

ATOM 2730 C LEU B 147 88.055 27.199 -17.844 1.00 0.00

ATOM 2731 O LEU B 147 86.990 27.231 -17.233 1.00 0.00

ATOM 2732 CB LEU B 147 89.787 26.125 -16.482 1.00 0.00

ATOM 2733 CG LEU B 147 90.556 24.885 -16.022 1.00 0.00

ATOM 2734 CDl LEU B 147 91.452 25.216 -14.839 1.00 0.00

ATOM 2735 CD2 LEU B 147 89.597 23.784 -15.599 1.00 0.00

ATOM 2736 N ARG B 148 88.458 28.216 -18.599 1.00 0.00

ATOM 2737 CA ARG B 148 87.599 29.386 -18.723 1.00 0.00

ATOM 2738 C ARG B 148 86.408 28.978 -19.561 1.00 0.00

ATOM 2739 O ARG B 148 85.312 29.503 -19.402 1.00 0.00

ATOM 2740 CB ARG B 148 88.351 30.534 -19.400 1.00 0.00

ATOM 2741 CG ARG B 148 89.437 31.158 -18.539 1.00 0.00

ATOM 2742 CD ARG B 148 90.196 32.232 -19.299 1.00 0.00

ATOM 2743 NE ARG B 148 91.250 32.836 -18.488 1.00 0.00

ATOM 2744 CZ ARG B 148 92.143 33.704 -18.951 1.00 0.00

ATOM 2745 NHl ARG B 148 93.067 34.202 -18.138 1.00 0.00

ATOM 2746 NH2 ARG B 148 92.112 34.074 -20.223 1.00 0.00

ATOM 2747 N ARG B 149 86.626 28.042 -20.475 1.00 0.00

ATOM 2748 CA ARG B 149 85.528 27.587 -21.303 1.00 0.00

ATOM 2749 C ARG B 149 84.536 26.826 -20.428 1.00 0.00

ATOM 2750 O ARG B 149 83.329 27.056 -20.483 1.00 0.00

ATOM 2751 CB ARG B 149 86.040 26.663 -22.410 1.00 0.00

ATOM 2752 CG ARG B 149 86.842 27.371 -23.489 1.00 0.00

ATOM 2753 CD ARG B 149 87.359 26.390 -24.528 1.00 0.00

ATOM 2754 NE ARG B 149 88.153 27.053 -25.560 1.00 0.00

ATOM 2755 CZ ARG B 149 88.739 26.421 -26.573 1.00 0.00

ATOM 2756 NHl ARG B 149 89.441 27.106 -27.463 1.00 0.00

ATOM 2757 NH2 ARG B 149 88.620 25.106 -26.690 1.00 0.00

ATOM 2758 N GLN B 150 85.064 25.901 -19.630 1.00 0.00

ATOM 2759 CA GLN B 150 84.252 25.108 -18.715 1.00 0.00

ATOM 2760 C GLN B 150 83.414 26.032 -17.810 1.00 0.00

ATOM 2761 O GLN B 150 82.177 25.973 -17.811 1.00 0.00

ATOM 2762 CB GLN B 150 85.141 24.233 -17.830 1.00 0.00

ATOM 2763 CG GLN B 150 84.375 23.360 -16.850 1.00 0.00

ATOM 2764 CD GLN B 150 85.288 22.483 -16.013 1.00 0.00

ATOM 2765 OEl GLN B 150 86.508 22.529 -16.156 1.00 0.00

ATOM 2766 NE2 GLN B 150 84.694 21.681 -15.138 1.00 0.00

ATOM 2767 N LEU B 151 84.092 26.895 -17.050 1.00 0.00

ATOM 2768 CA LEU B 151 83.398 27.840 -16.165 1.00 0.00

ATOM 2769 C LEU B 151 82.316 28.570 -16.961 1.00 0.00

ATOM 2770 O LEU B 151 81.218 28.811 -16.470 1.00 0.00

ATOM 2771 CB LEU B 151 84.383 28.866 -15.600 1.00 0.00

ATOM 2772 CG LEU B 151 83.801 29.909 -14.644 1.00 0.00

ATOM 2773 CDl LEU B 151 83.239 29.242 -13.398 1.00 0.00

ATOM 2774 CD2 LEU B 151 84.872 30.899 -14.212 1.00 0.00

ATOM 2775 N GLU B 152 82.634 28.911 -18.197 1.00 0.00

ATOM 2776 CA GLU B 152 81.693 29.609 -19.051 1.00 0.00

ATOM 2777 C GLU B 152 80.357 28.886 -19.234 1.00 0.00

ATOM 2778 O GLU B 152 79.283 29.359 -18.826 1.00 0.00

ATOM 2779 CB GLU B 152 82.281 29.798 -20.451 1.00 0.00

ATOM 2780 CG GLU B 152 81.377 30.564 -21.404 1.00 0.00

ATOM 2781 CD GLU B 152 81.996 30.744 -22.776 1.00 0.00

ATOM 2782 OEl GLU B 152 83.137 30.276 -22.979 1.00 0.00

ATOM 2783 OE2 GLU B 152 81.342 31.354 -23.648 1.00 0.00 ATOM 2784 N THR B 153 80.424 27.729 -19.868 .00 0.00

ATOM 2785 CA THR B 153 79.210 26.993 -20.117 .00 0.00

ATOM 2786 C THR B 153 78.475 26.753 -18.801 .00 0.00

ATOM 2787 O THR B 153 77.252 26.795 -18.768 .00 0.00

ATOM 2788 CB THR B 153 79.500 25.627 -20.765 .00 0.00

ATOM 2789 OGl THR B 153 80.142 25.822 -22.032 .00 0.00

ATOM 2790 CG2 THR B 153 78.209 24 . 853 - 20.981 .00 0.00

ATOM 2791 N LEU B 154 79.207 26 . 52 9 -17.711 .00 0.00

ATOM 2792 CA LEU B 154 78.556 26 . 2 97 16.425 .00 0.00

ATOM 2793 C LEU B 154 77.819 27 . 4 99 15.807 .00 0.00

ATOM 2794 O LEU B 154 76.811 27 . 320 15.124 .00 0.00

ATOM 2795 CB LEU B 154 79.583 25 . 868 15.375 .00 0.00

ATOM 2796 CG LEU B 154 80.225 24 . 4 94 -15.576 .00 0.00

ATOM 2797 CDl LEU B 154 81.329 24 . 2 62 14.557 .00 0.00

ATOM 2798 CD2 LEU B 154 79.191 23 . 389 15.418 .00 0.00

ATOM 2799 N GLY B 155 78.295 28 . 722 16.007 .00 0.00

ATOM 2800 CA GLY B 155 77.520 29. > 4 15.452 .00 0.00

ATOM 2801 C GLY B 155 76.242 29.. 891 16.284 .00 0.00

ATOM 2802 O GLY B 155 75.175 30. 999 15.775 .00 0.00

ATOM 2803 N GLN B 156 76.345 29.551 17.567 .00 0.00

ATOM 2804 CA GLN B 156 75.193 29.541 18.472 .00 0.00

ATOM 2805 C GLN B 156 74.131 28.541 17.942 1..00 0.00

ATOM 2806 O GLN B 156 72.945 28.871 17.770 1..00 0.00

ATOM 2807 CB GLN B 156 75.619 9.115 -19.878 1..00 0.00

ATOM 2808 CG GLN B 156 76.460 30.148 20.612 1.00 0.00

ATOM 2809 CD GLN B 156 76.975 29.642 -21.943 1.00 0.00

ATOM 2810 OEl GLN B 156 76.772 28.480 297 1.00 0.00

ATOM 2811 NE2 GLN B 156 77.644 30.513 689 1.00 0.00

ATOM 2812 N GLU B 157 74.578 27.323 - 17.663 1.00 0.00

ATOM 2813 CA GLU B 157 73.711 26. >76 17.129 1.00 0.00

ATOM 2814 C GLU B 157 73.022 26..766 15.873 1..00 0.00

ATOM 2815 O GLU B 157 71.819 26..591 15.706 1..00 0.00

ATOM 2816 CB GLU B 157 74.527 25.029 -16.785 1.00 0.00

ATOM 2817 CG GLU B 157 73.698 23.874 -16.245 1.00 0.00

ATOM 2818 CD GLU B 157 74.533 22.643 -15.954 1.00 0.00

ATOM 2819 OEl GLU B 157 75.756 22.681 -16.208 1.00 0.00

ATOM 2820 OE2 GLU B 157 73.966 21.639 -15.474 1.00 0.00

ATOM 2821 N LYS B 158 73.802 27.366 -14.979 1.00 0.00

ATOM 2822 CA LYS B 158 73.237 27.876 -13.747 1..00 0.00

ATOM 2823 C LYS B 158 72.146 28.924 -14.013 1..00 0.00

ATOM 2824 O LYS B 158 71.148 28.956 -13.300 1.00 0.00

ATOM 2825 CB LYS B 158 74.322 28.538 -1 895 1.00 0.00

ATOM 2826 CG LYS B 158 73.826 29.065 -11.558 1.00 0.00

ATOM 2827 CD LYS B 158 74.967 29.637 -10.732 1.00 0.00

ATOM 2828 CE LYS B 158 74.466 30.190 -9.408 1.00 0.00

ATOM 2829 NZ LYS B 158 75.572 30.768 -8.594 1.00 0.00

ATOM 2830 N LEU B 159 72.315 29.769 15.032 1..00 0.00

ATOM 2831 CA LEU B 159 71.292 30.774 15.341 1..00 0.00

ATOM 2832 C LEU B 159 70.002 30.059 15.686 1..00 0.00

ATOM 2833 O LEU B 159 68.899 30.459 15.297 1.00 0.00

ATOM 2834 CB LEU B 159 71.730 31.636 -16.528 1.00 0.00

ATOM 2835 CG LEU B 159 72.899 32.590 -16.277 1.00 0.00

ATOM 2836 CDl LEU B 159 73.344 33.246 -17.576 1.00 0.00

ATOM 2837 CD2 LEU B 159 72.500 33.687 -15.303 1.00 0.00

ATOM 2838 N LYS B 160 70.171 28.973 -16.422 1.00 0.00

ATOM 2839 CA LYS B 160 69.059 28.163 -16.844 1..00 0.00

ATOM 2840 C LYS B 160 68.322 27.485 -15.716 1..00 0.00

ATOM 2841 O LYS B 160 67.098 27.506 -15.696 1.00 0.00

ATOM 2842 CB LYS B 160 69.532 27.051 -17.782 1.00 0.00

ATOM 2843 CG LYS B 160 68.412 26.173 -18.317 1.00 0.00

ATOM 2844 CD LYS B 160 68.941 25 146 19.307 1.00 0.00

ATOM 2845 CE LYS B 160 67.826 24 245 19.816 1.00 0.00

ATOM 2846 NZ LYS B 160 68.338 23.200 20.744 1.00 0.00

ATOM 2847 N LEU B 161 69.046 26. 14.779 00 0.00

ATOM 2848 CA LEU B 161 68.400 26. 999 13.653 00 0.00

ATOM 2849 C LEU B 161 67.628 27.99-1 12.834 00 0.00

ATOM 2850 O LEU B 161 66.552 26.925 -12 .320 00 0.00

ATOM 2851 CB LEU B 161 69.444 25.556 -12.754 1.00 0.00 ATOM 2852 CG LEU B 161 70.164 24.339 -13.336 1.00 0.00

ATOM 2853 CDl LEU B 161 71.292 23.892 -12.420 1.00 0.00

ATOM 2854 CD2 LEU B 161 69.200 23.175 -13.508 1.00 0.00

ATOM 2855 N GLU B 162 68.197 28.403 -12.689 1.00 0.00

ATOM 2856 CA GLU B 162 67.542 29.443 -11.920 1.00 0.00

ATOM 2857 C GLU B 162 66.237 29.831 -12.558 1.00 0.00

ATOM 2858 O GLU B 162 65.256 30.162 -11.903 1.00 0.00

ATOM 2859 CB GLU B 162 68.427 30.689 -11.839 1.00 0.00

ATOM 2860 CG GLU B 162 69.659 30.518 -10.964 1.00 0.00

ATOM 2861 CD GLU B 162 70.574 31.726 -11.006 1.00 0.00

ATOM 2862 OEl GLU B 162 70.283 32.666 -11.775 1.00 0.00

ATOM 2863 OE2 GLU B 162 71.582 31.733 -10.269 1.00 0.00

ATOM 2864 N ALA B 163 66.267 29.834 -13.869 1.00 0.00

ATOM 2865 CA ALA B 163 65.117 30.209 -14.636 1.00 0.00

ATOM 2866 C ALA B 163 64.050 29.111 -14.537 1.00 0.00

ATOM 2867 O ALA B 163 62.868 29.397 -14.249 1.00 0.00

ATOM 2868 CB ALA B 163 65.493 30.400 -16.097 1.00 0.00

ATOM 2869 N GLU B 164 64.453 27.861 -14.751 1.00 0.00

ATOM 2870 CA GLU B 164 63.470 26.782 -14.669 1.00 0.00

ATOM 2871 C GLU B 164 62.847 26.749 -13.297 1.00 0.00

ATOM 2872 O GLU B 164 61.651 26.556 -13.165 1.00 0.00

ATOM 2873 CB GLU B 164 64.134 25.430 -14.935 1.00 0.00

ATOM 2874 CG GLU B 164 64.561 25.221 -16.379 1.00 0.00

ATOM 2875 CD GLU B 164 65.325 23.927 -16.580 1.00 0.00

ATOM 2876 OEl GLU B 164 65.584 23.229 -15.578 1.00 0.00

ATOM 2877 OE2 GLU B 164 65.664 23.611 -17.741 1.00 0.00

ATOM 2878 N LEU B 165 63.677 26.949 -12.282 1.00 0.00

ATOM 2879 CA LEU B 165 63.230 26.948 -10.901 1.00 0.00

ATOM 2880 C LEU B 165 62.170 28.035 -10.698 1.00 0.00

ATOM 2881 O LEU B 165 61.095 27.779 -10.145 1.00 0.00

ATOM 2882 CB LEU B 165 64.403 27.222 -9.958 1.00 0.00

ATOM 2883 CG LEU B 165 64.075 27.267 -8.464 1.00 0.00

ATOM 2884 CDl LEU B 165 63.529 25.927 -7.992 1.00 0.00

ATOM 2885 CD2 LEU B 165 65.319 27.587 -7.650 1.00 0.00

ATOM 2886 N GLY B 166 62.465 29.241 -11.153 1.00 0.00

ATOM 2887 CA GLY B 166 61.516 30.316 -11.010 1.00 0.00

ATOM 2888 C GLY B 166 60.183 29.935 -11.640 1.00 0.00

ATOM 2889 O GLY B 166 59.132 30.103 -11.023 1.00 0.00

ATOM 2890 N ASN B 167 60.221 29.375 -12.847 1.00 0.00

ATOM 2891 CA ASN B 167 58.974 28.985 -13.499 1.00 0.00

ATOM 2892 C ASN B 167 58.219 27.960 -12.658 1.00 0.00

ATOM 2893 O ASN B 167 56.996 27.999 -12.551 1.00 0.00

ATOM 2894 CB ASN B 167 59.257 28.366 -14.868 1.00 0.00

ATOM 2895 CG ASN B 167 59.684 29.394 -15.897 1.00 0.00

ATOM 2896 ODl ASN B 167 59.436 30.589 -15.733 1.00 0.00

ATOM 2897 ND2 ASN B 167 60.331 28.933 -16.961 1.00 0.00

ATOM 2898 N MET B 168 58.955 27.031 -12.067 1.00 0.00

ATOM 2899 CA MET B 168 58.323 26.017 -11.261 1.00 0.00

ATOM 2900 C MET B 168 57.674 26.636 -10.057 1.00 0.00

ATOM 2901 O MET B 168 56.521 26.347 -9.746 1.00 0.00

ATOM 2902 CB MET B 168 59.354 24.993 -10.783 1.00 0.00

ATOM 2903 CG MET B 168 59.887 24.089 -11.883 1.00 0.00

ATOM 2904 SD MET B 168 58.603 23.065 -12.626 1.00 0.00

ATOM 2905 CE MET B 168 58.221 21.963 -11.266 1.00 0.00

ATOM 2906 N GLN B 169 58.409 27.484 -9.364 1.00 0.00

ATOM 2907 CA GLN B 169 57.841 28.114 -8.191 1.00 0.00

ATOM 2908 C GLN B 169 56.565 28.894 -8.493 1.00 0.00

ATOM 2909 O GLN B 169 55.617 28.852 -7.717 1.00 0.00

ATOM 2910 CB GLN B 169 58.837 29.099 -7.576 1.00 0.00

ATOM 2911 CG GLN B 169 60.032 28.438 -6.909 1.00 0.00

ATOM 2912 CD GLN B 169 61.053 29.444 -6.413 1.00 0.00

ATOM 2913 OEl GLN B 169 60.916 30.646 -6.642 1.00 0.00

ATOM 2914 NE2 GLN B 169 62.080 28.954 -5.728 1.00 0.00

ATOM 2915 N GLY B 170 56.527 29.589 -9.632 1.00 0.00

ATOM 2916 CA GLY B 170 55.349 30.372 -10.013 1.00 0.00

ATOM 2917 C GLY B 170 54.190 29.408 -10.239 1.00 0.00

ATOM 2918 O GLY B 170 53.069 29.613 -9.776 1.00 0.00

ATOM 2919 N LEU B 171 54.492 28.359 -10.976 1.00 0.00 ATOM 2920 CA LEU B 171 53.537 27.315 -11.247 .00 0.00

ATOM 2921 C LEU B 171 52.938 26.860 -9.919 .00 0.00

ATOM 2922 O LEU B 171 51.719 26.870 -9.732 .00 0.00

ATOM 2923 CB LEU B 171 54.219 26.131 -11.934 .00 0.00

ATOM 2924 CG LEU B 171 54.617 26.334 -13.398 .00 0.00

ATOM 2925 CDl LEU B 171 55.520 25.205 -13.871 .00 0.00

ATOM 2926 CD2 LEU B 171 53.386 26.364 -14.290 .00 0.00

ATOM 2927 N VAL B 172 53.815 26.453 -9.007 .00 0.00

ATOM 2928 CA VAL B 172 53.415 25.991 -7.677 .00 0.00

ATOM 2929 C VAL B 172 52.459 26.969 -7.008 .00 0.00

ATOM 2930 O VAL B 172 51.424 26.561 -6.494 .00 0.00

ATOM 2931 CB VAL B 172 54.632 25.831 -6.747 .00 0.00

ATOM 2932 CGl VAL B 172 54.179 25.558 -5.320 .00 0.00

ATOM 2933 CG2 VAL B 172 55.504 24.672 -7.204 .00 0.00

ATOM 2934 N GLU B 173 52.793 28.257 -7.007 .00 0.00

ATOM 2935 CA GLU B 173 51.908 29.233 -6.382 .00 0.00

ATOM 2936 C GLU B 173 50.522 29.155 -7.029 .00 0.00

ATOM 2937 O GLU B 173 49.499 29.036 -6.342 .00 0.00

ATOM 2938 CB GLU B 173 52.460 30.648 -6.560 .00 0.00

ATOM 2939 CG GLU B 173 51.622 31.729 -5.898 .00 0.00

ATOM 2940 CD GLU B 173 52.217 33.114 -6.066 .00 0.00

ATOM 2941 OEl GLU B 173 53.295 33.225 -6.690 1..00 0.00

ATOM 2942 OE2 GLU B 173 51.609 34.087 -5.574 1..00 0.00

ATOM 2943 N ASP B 174 50.487 29.225 -8.354 1..00 0.00

ATOM 2944 CA ASP B 174 49.225 29.147 -9.079 1.00 0.00

ATOM 2945 C ASP B 174 48.421 27.906 -8.702 1.00 0.00

ATOM 2946 O ASP B 174 47.289 28.041 -8.235 1.00 0.00

ATOM 2947 CB ASP B 174 49.475 29.094 -10.587 1.00 0.00

ATOM 2948 CG ASP B 174 49.907 30.432 -11.154 1.00 0.00

ATOM 2949 ODl ASP B 174 49.825 31.442 -10.422 1.00 0.00

ATOM 2950 OD2 ASP B 174 50.328 30.473 -12.328 1..00 0.00

ATOM 2951 N PHE B 175 48.995 26.716 1..00 0.00

ATOM 2952 CA PHE B 175 48.287 25.482 -8.548 1.00 0.00

ATOM 2953 C PHE B 175 47.795 25.473 -7.125 1.00 0.00

ATOM 2954 O PHE B 175 46.715 .961 -6.863 1.00 0.00

ATOM 2955 CB PHE B 175 49.208 .271 -8.720 1.00 0.00

ATOM 2956 CG PHE B 175 49.396 23.851 -10.149 1.00 0.00

ATOM 2957 CDl PHE B 175 50.554 24.173 -10.834 1.00 0.00

ATOM 2958 CD2 PHE B 175 48.414 23.133 -10.809 1..00 0.00

ATOM 2959 CEl PHE B 175 50.727 23.786 -12.150 1..00 0.00

ATOM 2960 CE2 PHE B 175 48.586 22.745 -I- .124 1.00 0.00

ATOM 2961 CZ PHE B 175 49.737 23.070 -I- .795 1.00 0.00

ATOM 2962 N LYS B 176 48.554 26.031 -6. 101 1.00 0.00

ATOM 2963 CA LYS B 176 48.093 26.041 -4.321 1.00 0.00

ATOM 2964 C LYS B 176 46.905 26.971 -4.601 1.00 0.00

ATOM 2965 O LYS B 176 45.984 26.645 -3.856 1.00 0.00

ATOM 2966 CB LYS B 176 49.210 26.506 -3.886 1..00 0.00

ATOM 2967 CG LYS B 176 48.835 26.488 -2.412 1..00 0.00

ATOM 2968 CD LYS B 176 50.016 26.871 -1.537 1..00 0.00

ATOM 2969 CE LYS B 176 49.634 26.877 -0.066 1.00 0.00

ATOM 2970 NZ LYS B 176 50.777 27.271 0.803 1.00 0.00

ATOM 2971 N ASN B 177 46.921 28.113 -5.270 1.00 0.00

ATOM 2972 CA ASN B 177 45.820 29.054 -5.175 1.00 0.00

ATOM 2973 C ASN B 177 44.574 28.375 -5.746 1.00 0.00

ATOM 2974 O ASN B 177 43.514 28.370 -5.112 1.00 0.00

ATOM 2975 CB ASN B 177 46.129 30.324 -5.971 1..00 0.00

ATOM 2976 CG ASN B 177 47.173 31.193 -5.298 1..00 0.00

ATOM 2977 ODl ASN B 177 47.420 31.067 -4.098 1.00 0.00

ATOM 2978 ND2 ASN B 177 47.789 32.081 -6.069 1.00 0.00

ATOM 2979 N LYS B 178 44.731 27.802 -6.938 1.00 0.00

ATOM 2980 CA LYS B 178 43.654 27.118 -7.649 1.00 0.00

ATOM 2981 C LYS B 178 43.072 26.027 -6.770 1.00 0.00

ATOM 2982 O LYS B 178 41.860 25.907 -6.646 1.00 0.00

ATOM 2983 CB LYS B 178 44.181 26.485 -8.938 00 0.00

ATOM 2984 CG LYS B 178 44.563 27.491 -10.012 00 0.00

ATOM 2985 CD LYS B 178 45.079 26.795 -11.262 00 0.00

ATOM 2986 CE LYS B 178 45.484 27.800 12.327 00 0.00

ATOM 2987 NZ LYS B 178 46.026 27.134 13.542 1.00 0.00 ATOM 2988 N TYR B 179 43.946 25.239 -6.146 1.00 0.00

ATOM 2989 CA TYR B 179 43.487 24.181 -5.260 1.00 0.00

ATOM 2990 C TYR B 179 42.747 24.713 -4.041 1.00 0.00

ATOM 2991 O TYR B 179 41.800 24.087 -3.572 1.00 0.00

ATOM 2992 CB TYR B 179 44.671 23.360 -4.747 1.00 0.00

ATOM 2993 CG TYR B 179 44.281 22.252 -3.794 1.00 0.00

ATOM 2994 CDl TYR B 179 43.744 21.062 -4.268 1.00 0.00

ATOM 2995 CD2 TYR B 179 44.453 22.401 -2.424 1.00 0.00

ATOM 2996 CEl TYR B 179 43.386 20.045 -3.403 1.00 0.00

ATOM 2997 CE2 TYR B 179 44.101 21.395 -1.545 1.00 0.00

ATOM 2998 CZ TYR B 179 43.563 20.210 -2.047 1.00 0.00

ATOM 2999 OH TYR B 179 43.207 19.199 -1.183 1.00 0.00

ATOM 3000 N GLU B 180 43.180 25.855 -3.513 1.00 0.00

ATOM 3001 CA GLU B 180 42.518 26.439 -2.353 1.00 0.00

ATOM 3002 C GLU B 180 41.090 26.753 -2.775 1.00 0.00

ATOM 3003 O GLU B 180 40.130 26.387 -2.094 1.00 0.00

ATOM 3004 CB GLU B 180 43.235 27.717 -1.914 1.00 0.00

ATOM 3005 CG GLU B 180 42.638 28.371 -0.679 1.00 0.00

ATOM 3006 CD GLU B 180 43.395 29.614 -0.254 1.00 0.00

ATOM 3007 OEl GLU B 180 44.395 29.957 -0.919 1.00 0.00

ATOM 3008 OE2 GLU B 180 42.988 30.246 0.744 1.00 0.00

ATOM 3009 N ASP B 181 40.952 27.427 -3.908 1.00 0.00

ATOM 3010 CA ASP B 181 39.627 27.763 -4.418 1.00 0.00

ATOM 3011 C ASP B 181 38.786 26.510 -4.563 1.00 0.00

ATOM 3012 O ASP B 181 37.672 26.450 -4.055 1.00 0.00

ATOM 3013 CB ASP B 181 39.735 28.437 -5.787 1.00 0.00

ATOM 3014 CG ASP B 181 40.272 29.853 -5.698 1.00 0.00

ATOM 3015 ODl ASP B 181 40.334 30.394 -4.575 1.00 0.00

ATOM 3016 OD2 ASP B 181 40.629 30.419 -6.752 1.00 0.00

ATOM 3017 N GLU B 182 39.310 25.509 -5.271 1.00 0.00

ATOM 3018 CA GLU B 182 38.530 24.296 -5.502 1.00 0.00

ATOM 3019 C GLU B 182 38.099 23.647 -4.215 1.00 0.00

ATOM 3020 O GLU B 182 37.032 23.047 -4.156 1.00 0.00

ATOM 3021 CB GLU B 182 39.354 23.271 -6.283 1.00 0.00

ATOM 3022 CG GLU B 182 39.617 23.658 -7.729 1.00 0.00

ATOM 3023 CD GLU B 182 38.340 23.864 -8.520 1.00 0.00

ATOM 3024 OEl GLU B 182 37.480 22.957 -8.505 1.00 0.00

ATOM 3025 OE2 GLU B 182 38.198 24.930 -9.152 1.00 0.00

ATOM 3026 N ILE B 183 38.918 23.740 -3.188 1.00 0.00

ATOM 3027 CA ILE B 183 38.536 23.131 -1.933 1.00 0.00

ATOM 3028 C ILE B 183 37.462 23.944 -1.261 1.00 0.00

ATOM 3029 O ILE B 183 36.639 23.403 -0.535 1.00 0.00

ATOM 3030 CB ILE B 183 39.732 23.032 -0.967 1.00 0.00

ATOM 3031 CGl ILE B 183 40.826 22.142 -1.561 1.00 0.00

ATOM 3032 CG2 ILE B 183 39.294 22.436 0.363 1.00 0.00

ATOM 3033 CDl ILE B 183 40.365 20.735 -1.876 1.00 0.00

ATOM 3034 N ASN B 184 37.470 25.249 -1.495 1.00 0.00

ATOM 3035 CA ASN B 184 36.465 26.117 -0.906 1.00 0.00

ATOM 3036 C ASN B 184 35.140 25.760 -1.564 1.00 0.00

ATOM 3037 O ASN B 184 34.128 25.543 -0.886 1.00 0.00

ATOM 3038 CB ASN B 184 36.809 27.586 -1.163 1.00 0.00

ATOM 3039 CG ASN B 184 37.981 28.064 -0.330 1.00 0.00

ATOM 3040 ODl ASN B 184 38.311 27.467 0.695 1.00 0.00

ATOM 3041 ND2 ASN B 184 38.616 29.144 -0.769 1.00 0.00

ATOM 3042 N LYS B 185 35.158 25.683 -2.891 1.00 0.00

ATOM 3043 CA LYS B 185 33.951 25.359 -3.649 1.00 0.00

ATOM 3044 C LYS B 185 33.417 23.986 -3.283 1.00 0.00

ATOM 3045 O LYS B 185 32.211 23.805 -3.215 1.00 0.00

ATOM 3046 CB LYS B 185 34.243 25.364 -5.151 1.00 0.00

ATOM 3047 CG LYS B 185 34.501 26.747 -5.728 1.00 0.00

ATOM 3048 CD LYS B 185 34.780 26.680 -7.220 1.00 0.00

ATOM 3049 CE LYS B 185 35.062 28.059 -7.792 1.00 0.00

ATOM 3050 NZ LYS B 185 35.371 28.005 -9.248 1.00 0.00

ATOM 3051 N ARG B 186 34.318 23.034 -3.049 1.00 0.00

ATOM 3052 CA ARG B 186 33.951 21.665 -2.688 1.00 0.00

ATOM 3053 C ARG B 186 33.269 21.718 -1.311 1.00 0.00

ATOM 3054 O ARG B 186 32.178 21.185 -1.133 1.00 0.00

ATOM 3055 CB ARG B 186 35.195 20.777 -2.620 1.00 0.00 ATOM 3056 CG ARG B 186 34.902 19.322 -2.290 1.00 0.00

ATOM 3057 CD ARG B 186 36.184 18.515 -2.170 1.00 0.00

ATOM 3058 NE ARG B 186 37.002 18.950 -1.040 1.00 0.00

ATOM 3059 CZ ARG B 186 36.762 18.623 0.227 1.00 0.00

ATOM 3060 NHl ARG B 186 37.559 19.066 1.189 1.00 0.00

ATOM 3061 NH2 ARG B 186 35.724 17.854 0.526 1.00 0.00

ATOM 3062 N THR B 187 33.900 22.378 -0.348 1.00 0.00

ATOM 3063 CA THR B 187 33.314 22.523 0.986 1.00 0.00

ATOM 3064 C THR B 187 31.862 23.058 0.861 1.00 0.00

ATOM 3065 O THR B 187 30.939 22.548 1.497 1.00 0.00

ATOM 3066 CB THR B 187 34.122 23.506 1.853 1.00 0.00

ATOM 3067 OGl THR B 187 35.459 23.017 2.017 1.00 0.00

ATOM 3068 CG2 THR B 187 33.482 23.656 3.225 1.00 0.00

ATOM 3069 N GLU B 188 31.668 24.081 0.029 1.00 0.00

ATOM 3070 CA GLU B 188 30.341 24.666 -0.178 1.00 0.00

ATOM 3071 C GLU B 188 29.372 23.643 -0.746 1.00 0.00

ATOM 3072 O GLU B 188 28.259 23.487 -0.242 1.00 0.00

ATOM 3073 CB GLU B 188 30.418 25.838 -1.157 1.00 0.00

ATOM 3074 CG GLU B 188 29.090 26.536 -1.398 1.00 0.00

ATOM 3075 CD GLU B 188 29.212 27.713 -2.345 1.00 0.00

ATOM 3076 OEl GLU B 188 30.340 27.991 -2.805 1.00 0.00

ATOM 3077 OE2 GLU B 188 28.180 28.357 -2.629 1.00 0.00

ATOM 3078 N MET B 189 29.789 22.952 -1.800 1.00 0.00

ATOM 3079 CA MET B 189 28.915 21.949 -2.391 1.00 0.00

ATOM 3080 C MET B 189 28.501 20.897 -1.386 1.00 0.00

ATOM 3081 O MET B 189 27.343 20.486 -1.378 1.00 0.00

ATOM 3082 CB MET B 189 29.622 21.236 -3.545 1.00 0.00

ATOM 3083 CG MET B 189 29.830 22.103 -4.776 1.00 0.00

ATOM 3084 SD MET B 189 30.716 21.244 -6.090 1.00 0.00

ATOM 3085 CE MET B 189 30.837 22.540 -7.321 1.00 0.00

ATOM 3086 N GLU B 190 29.431 20.465 -0.539 1.00 0.00

ATOM 3087 CA GLU B 190 29.106 19.455 0.453 1.00 0.00

ATOM 3088 C GLU B 190 28.059 19.986 1.423 1.00 0.00

ATOM 3089 O GLU B 190 27.061 19.323 1.687 1.00 0.00

ATOM 3090 CB GLU B 190 30.353 19.065 1.250 1.00 0.00

ATOM 3091 CG GLU B 190 30.114 17.977 2.284 1.00 0.00

ATOM 3092 CD GLU B 190 31.378 17.593 3.028 1.00 0.00

ATOM 3093 OEl GLU B 190 32.444 18.170 2.726 1.00 0.00

ATOM 3094 OE2 GLU B 190 31.302 16.716 3.914 1.00 0.00

ATOM 3095 N ASN B 191 28.249 21.194 1.935 1.00 0.00

ATOM 3096 CA ASN B 191 27.241 21.731 2.832 1.00 0.00

ATOM 3097 C ASN B 191 25.888 21.718 2.111 1.00 0.00

ATOM 3098 O ASN B 191 24.907 21.195 2.634 1.00 0.00

ATOM 3099 CB ASN B 191 27.590 23.166 3.232 1.00 0.00

ATOM 3100 CG ASN B 191 28.753 23.234 4.202 1.00 0.00

ATOM 3101 ODl ASN B 191 29.086 22.247 4.857 1.00 0.00

ATOM 3102 ND2 ASN B 191 29.377 24.402 4.295 1.00 0.00

ATOM 3103 N GLU B 192 25.835 22.264 0.903 1.00 0.00

ATOM 3104 CA GLU B 192 24.576 22.304 0.157 1.00 0.00

ATOM 3105 C GLU B 192 23.935 20.929 -0.033 1.00 0.00

ATOM 3106 O GLU B 192 22.722 20.779 0.121 1.00 0.00

ATOM 3107 CB GLU B 192 24.799 22.885 -1.241 1.00 0.00

ATOM 3108 CG GLU B 192 25.102 24.375 -1.252 1.00 0.00

ATOM 3109 CD GLU B 192 25.438 24.890 -2.638 1.00 0.00

ATOM 3110 OEl GLU B 192 25.508 24.069 -3.576 1.00 0.00

ATOM 3111 OE2 GLU B 192 25.632 26.115 -2.785 1.00 0.00

ATOM 3112 N PHE B 193 24.750 19.937 -0.383 1.00 0.00

ATOM 3113 CA PHE B 193 24.257 18.577 -0.595 1.00 0.00

ATOM 3114 C PHE B 193 23.706 17.970 0.675 1.00 0.00

ATOM 3115 O PHE B 193 22.771 17.181 0.635 1.00 0.00

ATOM 3116 CB PHE B 193 25.385 17.669 -1.092 1.00 0.00

ATOM 3117 CG PHE B 193 24.932 16.285 -1.459 1.00 0.00

ATOM 3118 CDl PHE B 193 24.220 16.060 -2.625 1.00 0.00

ATOM 3119 CD2 PHE B 193 25.217 15.207 -0.639 1.00 0.00

ATOM 3120 CEl PHE B 193 23.804 14.787 -2.962 1.00 0.00

ATOM 3121 CE2 PHE B 193 24.801 13.934 -0.977 1.00 0.00

ATOM 3122 CZ PHE B 193 24.097 13.720 -2.132 1.00 0.00

ATOM 3123 N VAL B 194 24.295 18.317 1.808 1.00 0.00 ATOM 3124 CA VAL B 194 23.815 17.755 3 . 054 00 0.00

ATOM 3125 C VAL B 194 22.424 18.307 3 . 315 00 0.00

ATOM 3126 O VAL B 194 21.476 17.567 3 . 574 00 0.00

ATOM 3127 CB VAL B 194 24.735 18.126 4 . 232 00 0.00

ATOM 3128 CGl VAL B 194 24.117 17.687 5 . 550 00 0.00

ATOM 3129 CG2 VAL B 194 26. 17.447 4 . 086 00 0.00

ATOM 3130 N LEU B 195 22.308 19.624 3 . 225 00 0.00

ATOM 3131 CA LEU B 195 21.050 20.303 3 . 440 1.00 0.00

ATOM 3132 C LEU B 195 19.971 19.717 2 . 541 00 0.00

ATOM 3133 O LEU B 195 18.967 19.162 3 . 007 00 0.00

ATOM 3134 CB LEU B 195 21.186 21.794 3 . 127 00 0.00

ATOM 3135 CG LEU B 195 19.917 22.636 274 1.00 0.00

ATOM 3136 CDl LEU B 195 19.433 22.634 716 00 0.00

ATOM 3137 CD2 LEU B 195 20.176 24.076 861 00 0.00

ATOM 3138 N ILE B 196 20.186 19.855 242 00 0.00

ATOM 3139 CA ILE B 196 19.220 19.361 289 1.00 0.00

ATOM 3140 C ILE B 196 18.861 17.925 0.640 1.00 0.00

ATOM 3141 O ILE B 196 17.683 17.588 0.672 1.00 0.00

ATOM 3142 CB ILE B 196 19.778 19.390 -1 146 1.00 0.00

ATOM 3143 CGl ILE B 196 19.963 20.835 -1 616 1.00 0.00

ATOM 3144 CG2 ILE B 196 18.824 18.692 -2.103 1.00 0.00

ATOM 3145 CDl ILE B 196 20.755 20.963 -2.899 1..00 0.00

ATOM 3146 N LYS B 197 19.845 17.084 0.943 1..00 0.00

ATOM 3147 CA LYS B 197 19.531 15.701 1.297 1..00 0.00

ATOM 3148 C LYS B 197 18.556 15.616 2.468 1.00 0.00

ATOM 3149 O LYS B 197 17.597 14.835 2.424 1.00 0.00

ATOM 3150 CB LYS B 197 20.802 14.949 1.696 1.00 0.00

ATOM 3151 CG LYS B 197 20.575 13.486 2.041 1.00 0.00

ATOM 3152 CD LYS B 197 21.885 12.784 2.359 1.00 0.00

ATOM 3153 CE LYS B 197 21.652 11.333 2.753 1.00 0.00

ATOM 3154 NZ LYS B 197 22.926 10.639 3.090 1.00 0.00

ATOM 3155 N LYS B 198 18.800 16.408 3.518 1.00 0.00

ATOM 3156 CA LYS B 198 17.900 16.411 4.677 1.00 0.00

ATOM 3157 C LYS B 198 16.513 16.691 4.134 1.00 0.00

ATOM 3158 O LYS B 198 15.604 15.891 4.286 1..00 0.00

ATOM 3159 CB LYS B 198 18.317 17.492 5.676 1..00 0.00

ATOM 3160 CG LYS B 198 17.466 17.534 6.935 1..00 0.00

ATOM 3161 CD LYS B 198 17.964 18.595 7.904 1..00 0.00

ATOM 3162 CE LYS B 198 17.094 18.660 9.148 1..00 0.00

ATOM 3163 NZ LYS B 198 17.585 19.678 10.116 1..00 0.00

ATOM 3164 N ASP B 199 16.373 17.835 3.484 1.00 0.00

ATOM 3165 CA ASP B 199 15.112 18.253 2.904 1.00 0.00

ATOM 3166 C ASP B 199 14.419 17.173 2.079 .00 0.00

ATOM 3167 O ASP B 199 13.219 16.933 2.232 .00 0.00

ATOM 3168 CB ASP B 199 15.321 19.447 1.970 1.00 0.00

ATOM 3169 CG ASP B 199 15.612 20.730 2.723 .00 0.00

ATOM 3170 ODl ASP B 199 15.429 20.750 3.957 .00 0.00

ATOM 3171 OD2 ASP B 199 16.026 21.717 2..077 .00 0.00

ATOM 3172 N VAL B 200 15.169 16.530 l.:100 .00 0.00

ATOM 3173 CA VAL B 200 14.578 15.497 0.379 .00 0.00

ATOM 3174 C VAL B 200 13.952 14.463 292 1.00 0.00

ATOM 3175 O VAL B 200 12.844 14.002 050 1. .00 0.00

ATOM 3176 CB VAL B 200 15.631 14.811 -0.510 1..00 0.00

ATOM 3177 CGl VAL B 200 15.030 13.602 -1.212 1.00 0.00

ATOM 3178 CG2 VAL B 200 16.146 15.774 -1.568 1.00 0.00

ATOM 3179 N ASP B 201 14.668 14.111 2.355 1..00 0.00

ATOM 3180 CA ASP B 201 14.174 13.106 3.285 1..00 0.00

ATOM 3181 C ASP B 201 12.891 13.535 3.994 1.00 0.00

ATOM 3182 O ASP B 201 11.893 12.807 02; 1.00 0.00

ATOM 3183 CB ASP B 201 15.216 12.820 4 . 369 00 0.00

ATOM 3184 CG ASP B 201 16.400 12.031 3 . 845 00 0.00

ATOM 3185 ODl ASP B 201 16.309 11.503 2 . 717 00 0.00

ATOM 3186 OD2 ASP B 201 17.418 11.942 4 . 561 00 0.00

ATOM 3187 N GLU B 202 12.916 14.717 4 . 574 00 0.00

ATOM 3188 CA GLU B 202 11.731 15.219 5 . 244 00 0.00

ATOM 3189 C GLU B 202 10.516 15.292 4 . 326 00 0.00

ATOM 3190 O GLU B 202 9.435 14.846 4 . 684 00 0.00

ATOM 3191 CB GLU B 202 11.977 16.630 5 . 782 1.00 0.00 ATOM 3192 CG GLU B 202 10.798 17.218 6.542 1.00 0.00

ATOM 3193 CD GLU B 202 11.091 18.602 7.089 1.00 0.00

ATOM 3194 OEl GLU B 202 12.220 19.095 6.884 1.00 0.00

ATOM 3195 OE2 GLU B 202 10.190 19.192 7.721 1.00 0.00

ATOM 3196 N ALA B 203 10.685 15.863 3.136 1.00 0.00

ATOM 3197 CA ALA B 203 9.568 15.960 2.207 1.00 0.00

ATOM 3198 C ALA B 203 9.115 14.558 1.798 1.00 0.00

ATOM 3199 O ALA B 203 7.943 14.339 1.511 1.00 0.00

ATOM 3200 CB ALA B 203 9.979 16.728 0.961 1.00 0.00

ATOM 3201 N TYR B 204 10.030 13.598 1.764 1.00 0.00

ATOM 3202 CA TYR B 204 9.613 12.256 1.394 1.00 0.00

ATOM 3203 C TYR B 204 8.738 11.691 2.529 1.00 0.00

ATOM 3204 O TYR B 204 7.692 11.094 2.270 1.00 0.00

ATOM 3205 CB TYR B 204 10.831 11.354 1.189 1.00 0.00

ATOM 3206 CG TYR B 204 10.484 9.934 0.801 1.00 0.00

ATOM 3207 CDl TYR B 204 10.100 9.625 -0.498 1.00 0.00

ATOM 3208 CD2 TYR B 204 10.541 8.907 1.735 1.00 0.00

ATOM 3209 CEl TYR B 204 9.781 8.331 -0.862 1.00 0.00

ATOM 3210 CE2 TYR B 204 10.225 7.607 1.389 1.00 0.00

ATOM 3211 CZ TYR B 204 9.843 7.325 0.078 1.00 0.00

ATOM 3212 OH TYR B 204 9.526 6.035 -0.282 1.00 0.00

ATOM 3213 N MET B 205 9.137 11.885 3.783 1.00 0.00

ATOM 3214 CA MET B 205 8.286 11.393 4.870 1.00 0.00

ATOM 3215 C MET B 205 6.894 12.038 4.753 1.00 0.00

ATOM 3216 O MET B 205 5.878 11.344 4.745 1.00 0.00

ATOM 3217 CB MET B 205 8.892 11.751 6.229 1.00 0.00

ATOM 3218 CG MET B 205 10.169 10.994 6.557 1.00 0.00

ATOM 3219 SD MET B 205 10.921 11.539 8.103 1.00 0.00

ATOM 3220 CE MET B 205 9.715 10.954 9.292 1.00 0.00

ATOM 3221 N ASN B 206 6.847 13.363 4.656 1.00 0.00

ATOM 3222 CA ASN B 206 5.583 14.080 4.533 1.00 0.00

ATOM 3223 C ASN B 206 4.717 13.502 3.426 1.00 0.00

ATOM 3224 O ASN B 206 3.507 13.316 3.592 1.00 0.00

ATOM 3225 CB ASN B 206 5.834 15.555 4.210 1.00 0.00

ATOM 3226 CG ASN B 206 6.363 16.330 5.401 1.00 0.00

ATOM 3227 ODl ASN B 206 6.280 15.870 6.540 1.00 0.00

ATOM 3228 ND2 ASN B 206 6.908 17.512 5.141 1.00 0.00

ATOM 3229 N LYS B 207 5.339 13.209 2.284 1.00 0.00

ATOM 3230 CA LYS B 207 4.574 12.680 1.169 1.00 0.00

ATOM 3231 C LYS B 207 4.033 11.294 1.469 1.00 0.00

ATOM 3232 O LYS B 207 2.882 10.999 1.166 1.00 0.00

ATOM 3233 CB LYS B 207 5.449 12.582 -0.083 1.00 0.00

ATOM 3234 CG LYS B 207 4.721 12.055 -1.308 1.00 0.00

ATOM 3235 CD LYS B 207 5.622 12.065 -2.532 1.00 0.00

ATOM 3236 CE LYS B 207 6.728 11.030 -2.413 1.00 0.00

ATOM 3237 NZ LYS B 207 7.644 11.058 -3.587 1.00 0.00

ATOM 3238 N VAL B 208 4.829 10.445 2.095 1.00 0.00

ATOM 3239 CA VAL B 208 4.332 9.122 2.409 1.00 0.00

ATOM 3240 C VAL B 208 3.185 9.170 3.432 1.00 0.00

ATOM 3241 O VAL B 208 2.190 8.441 3.320 1.00 0.00

ATOM 3242 CB VAL B 208 5.437 8.230 3.005 1.00 0.00

ATOM 3243 CGl VAL B 208 4.852 6.916 3.500 1.00 0.00

ATOM 3244 CG2 VAL B 208 6.495 7.921 1.958 1.00 0.00

ATOM 3245 N GLU B 209 3.315 10.063 4.406 1.00 0.00

ATOM 3246 CA GLU B 209 2.280 10.224 5.417 1.00 0.00

ATOM 3247 C GLU B 209 0.995 10.607 4.702 1.00 0.00

ATOM 3248 O GLU B 209 -0.076 10.082 5.007 1.00 0.00

ATOM 3249 CB GLU B 209 2.670 11.319 6.412 1.00 0.00

ATOM 3250 CG GLU B 209 3.815 10.940 7.336 1.00 0.00

ATOM 3251 CD GLU B 209 4.254 12.089 8.222 1.00 0.00

ATOM 3252 OEl GLU B 209 3.712 13.203 8.062 1.00 0.00

ATOM 3253 OE2 GLU B 209 5.140 11.876 9.076 1.00 0.00

ATOM 3254 N LEU B 210 1.098 11.523 3.748 1.00 0.00

ATOM 3255 CA LEU B 210 -0.094 11.935 3.021 1.00 0.00

ATOM 3256 C LEU B 210 -0.658 10.813 2.147 1.00 0.00

ATOM 3257 O LEU B 210 -1.871 10.639 2.074 1.00 0.00

ATOM 3258 CB LEU B 210 0.221 13.118 2.103 1.00 0.00

ATOM 3259 CG LEU B 210 0.534 14.447 2.794 1.00 0.00 ATOM 3260 CDl LEU B 210 1.000 15.482 1.781 1.00 0.00

ATOM 3261 CD2 LEU B 210 -0.700 14.992 3.495 1.00 0.00

ATOM 3262 N GLU B 211 0.185 10.026 1.490 1.00 0.00

ATOM 3263 CA GLU B 211 -0.382 8.962 0.661 1.00 0.00

ATOM 3264 C GLU B 211 -1.231 8.042 1.519 1.00 0.00

ATOM 3265 O GLU B 211 -2.307 7.597 1.116 1.00 0.00

ATOM 3266 CB GLU B 211 0.732 8.141 0.009 1.00 0.00

ATOM 3267 CG GLU B 211 1.492 8.879 -1.081 1.00 0.00

ATOM 3268 CD GLU B 211 2.663 8.082 -1.618 1.00 0.00

ATOM 3269 OEl GLU B 211 2.926 6.982 -1.087 1.00 0.00

ATOM 3270 OE2 GLU B 211 3.319 8.556 -2.570 1.00 0.00

ATOM 3271 N SER B -0.750 7.782 2.722 1.00 0.00

ATOM 3272 CA SER B -1.467 6.922 3.645 1.00 0.00

ATOM 3273 C SER B 212 -2.764 7.584 4.069 1.00 0.00

ATOM 3274 O SER B 212 -3.844 6.983 4.006 1.00 0.00

ATOM 3275 CB SER B -0.623 6.653 4.892 1.00 0.00

ATOM 3276 OG SER B 0.528 5.891 4.575 1.00 0.00

ATOM 3277 N ARG B 213 -2.653 8.820 4.502 1.00 0.00

ATOM 3278 CA ARG B 213 -3.823 9.533 4.957 1.00 0.00

ATOM 3279 C ARG B 213 -4.907 9.577 3.899 1.00 0.00

ATOM 3280 O ARG B 213 -6.086 9.334 4.169 1.00 0.00

ATOM 3281 CB ARG B 213 -3.465 10.977 5.315 1.00 0.00

ATOM 3282 CG ARG B 213 -2.633 11.115 6.579 1.00 0.00

ATOM 3283 CD ARG B 213 -2.253 12.564 6.834 1.00 0.00

ATOM 3284 NE ARG B 213 -1.429 12.711 8.032 1.00 0.00

ATOM 3285 CZ ARG B 213 -0.901 13.860 8.439 1.00 0.00

ATOM 3286 NHl ARG B 213 -0.164 13.899 9.541 1.00 0.00

ATOM 3287 NH2 ARG B 213 -1.111 14.970 7.743 1.00 0.00

ATOM 3288 N LEU B 214 -4.480 9.873 2.680 1.00 0.00

ATOM 3289 CA LEU B 214 -5.387 9.941 1.557 1.00 0.00

ATOM 3290 C LEU B 214 -6.058 8.570 1.313 1.00 0.00

ATOM 3291 O LEU B 214 -7.277 8.488 1.174 1.00 0.00

ATOM 3292 CB LEU B 214 -4.637 10.342 0.286 1.00 0.00

ATOM 3293 CG LEU B 214 -5.472 10.440 -0.993 1.00 0.00

ATOM 3294 CDl LEU B 214 -6.550 11.503 -0.852 1.00 0.00

ATOM 3295 CD2 LEU B 214 -4.596 10.805 -2.181 1.00 0.00

ATOM 3296 N GLU B 215 -5.293 7.487 1.268 1.00 0.00

ATOM 3297 CA GLU B 215 -5.934 6.185 1.093 1.00 0.00

ATOM 3298 C GLU B 215 -6.983 5.929 2.190 1.00 0.00

ATOM 3299 O GLU B 215 -8.100 5.482 1.901 1.00 0.00

ATOM 3300 CB GLU B 215 -4.896 5.064 1.160 1.00 0.00

ATOM 3301 CG GLU B 215 -5.471 3.673 0.942 1.00 0.00

ATOM 3302 CD GLU B 215 -4.409 2.591 0.982 1.00 0.00

ATOM 3303 OEl GLU B 215 -3.220 2.931 1.165 1.00 0.00

ATOM 3304 OE2 GLU B 215 -4.764 1.404 0.828 1.00 0.00

ATOM 3305 N GLY B 216 -6.639 6.197 3.446 1.00 0.00

ATOM 3306 CA GLY B 216 -7.600 5.931 4.515 1.00 0.00

ATOM 3307 C GLY B 216 -8.869 6.701 4.306 1.00 0.00

ATOM 3308 O GLY B 216 -9.958 6.163 4.449 1.00 0.00

ATOM 3309 N LEU B 217 -8.706 7.971 3.958 1.00 0.00

ATOM 3310 CA LEU B 217 -9.846 8.834 3.739 1.00 0.00

ATOM 3311 C LEU B 217 10.696 8.363 2.575 1.00 0.00

ATOM 3312 O LEU B 217 11.925 8.335 2.673 1.00 0.00

ATOM 3313 CB LEU B 217 -9.386 10.261 3.432 1.00 0.00

ATOM 3314 CG LEU B 217 -8.752 11.033 4.590 1.00 0.00

ATOM 3315 CDl LEU B 217 -8.181 12.357 4.105 1.00 0.00

ATOM 3316 CD2 LEU B 217 -9.783 11.328 5.669 1.00 0.00

ATOM 3317 N THR B 218 10.045 7.988 1.479 1.00 0.00

ATOM 3318 CA THR B 218 10.766 7.523 0.305 1.00 0.00

ATOM 3319 C THR B 218 11.570 6.284 0.603 1.00 0.00

ATOM 3320 O THR B 218 12.700 6.136 0.140 1.00 0.00

ATOM 3321 CB THR B 218 -9.805 7.179 -0.848 1.00 0.00

ATOM 3322 OGl THR B 218 -9.081 8.354 -1.236 1.00 0.00

ATOM 3323 CG2 THR B 218 10.579 6.659 -2.049 1.00 0.00

ATOM 3324 N ASP B 219 10.994 5.400 1.400 1.00 0.00

ATOM 3325 CA ASP B 219 11.676 4.184 1.793 1.00 0.00

ATOM 3326 C ASP B 219 12.898 4.534 2.648 1.00 0.00

ATOM 3327 O ASP B 219 13.983 3.993 2.436 1.00 0.00 ATOM 3328 CB ASP B 219 -10.743 3.285 2.607 1.00 0.00

ATOM 3329 CG ASP B 219 -9.676 2.629 1.754 1.00 0.00

ATOM 3330 ODl ASP B 219 -9.801 2.668 0.512 1.00 0.00

ATOM 3331 OD2 ASP B 219 -8.714 2.076 2.328 1.00 0.00

ATOM 3332 N GLU B 220 -12.738 5.446 3.599 1.00 0.00

ATOM 3333 CA GLU B 220 -13.884 5.815 4.421 1.00 0.00

ATOM 3334 C GLU B 220 -14.966 6.450 3.591 1.00 0.00

ATOM 3335 O GLU B 220 -16.148 6.187 3.793 1.00 0.00

ATOM 3336 CB GLU B 220 -13.467 6.814 5.501 1.00 0.00

ATOM 3337 CG GLU B 220 -12.600 6.217 6.598 1.00 0.00

ATOM 3338 CD GLU B 220 -12.105 7.259 7.582 1.00 0.00

ATOM 3339 OEl GLU B 220 -12.379 8.459 7.365 1.00 0.00

ATOM 3340 OE2 GLU B 220 -11.443 6.877 8.570 1.00 0.00

ATOM 3341 N ILE B 991 -14.559 7.283 2.649 1.00 0.00

ATOM 3342 CA ILE B 221 -15.517 7.924 1.770 1.00 0.00

ATOM 3343 C ILE B 221 -16.307 6.852 0.997 1.00 0.00

ATOM 3344 O ILE B 221 -17.531 6.923 0.901 1.00 0.00

ATOM 3345 CB ILE B 221 -14.819 8.843 0.750 1.00 0.00

ATOM 3346 CGl ILE B 221 -14.188 10.044 1.458 1.00 0.00

ATOM 3347 CG2 ILE B 221 -15.819 9.358 -0.274 1.00 0.00

ATOM 3348 CDl ILE B 221 -13.258 10.851 0.578 1.00 0.00

ATOM 3349 N ASN B 222 -15.614 5.844 0.464 1.00 0.00

ATOM 3350 CA ASN B 222 -16.284 4.775 -0.286 1.00 0.00

ATOM 3351 C ASN B 222 -17.289 4.035 0.598 1.00 0.00

ATOM 3352 O ASN B 999 -18.414 3.765 0.184 1.00 0.00

ATOM 3353 CB ASN B 999 -15.260 3.760 -0.799 1.00 0.00

ATOM 3354 CG ASN B 222 -14.432 4.298 -1.949 1.00 0.00

ATOM 3355 ODl ASN B 999 -14.819 5.264 -2.607 1.00 0.00

ATOM 3356 ND2 ASN B 222 -13.285 3.673 -2.193 1.00 0.00

ATOM 3357 N PHE B -16.874 3.700 1.806 1.00 0.00

ATOM 3358 CA PHE B 223 -17.776 3.033 2.719 1.00 0.00

ATOM 3359 C PHE B 223 -18.980 3.938 3.020 1.00 0.00

ATOM 3360 O PHE B -20.100 3.451 3.147 1.00 0.00

ATOM 3361 CB PHE B 223 -17.065 2.708 4.033 1.00 0.00

ATOM 3362 CG PHE B 223 -16.169 1.504 3.956 1.00 0.00

ATOM 3363 CDl PHE B 223 -14.799 1.651 3.829 1.00 0.00

ATOM 3364 CD2 PHE B 223 -16.695 0.226 4.011 1.00 0.00

ATOM 3365 CEl PHE B 223 -13.974 0.545 3.758 1.00 0.00

ATOM 3366 CE2 PHE B 223 -15.871 -0.880 3.940 1.00 0.00

ATOM 3367 CZ PHE B 223 -14.515 -0.725 3.814 1.00 0.00

ATOM 3368 N LEU B 224 -18.757 5.249 3.101 1.00 0.00

ATOM 3369 CA LEU B 224 -19.866 6.158 3.366 1.00 0.00

ATOM 3370 C LEU B 224 -20.789 6.291 2.182 1.00 0.00

ATOM 3371 O LEU B 224 -21.986 6.451 2.374 1.00 0.00

ATOM 3372 CB LEU B 224 -19.344 7.556 3.702 1.00 0.00

ATOM 3373 CG LEU B 224 -18.589 7.698 5.025 1.00 0.00

ATOM 3374 CDl LEU B 224 -17.996 9.092 5.160 1.00 0.00

ATOM 3375 CD2 LEU B 224 -19.521 7.462 6.204 1.00 0.00

ATOM 3376 N ARG B 225 -20.269 6.231 0.959 1.00 0.00

ATOM 3377 CA ARG B 225 -21.173 6.349 -0.178 1.00 0.00

ATOM 3378 C ARG B 225 -22.094 5.158 -0.136 1.00 0.00

ATOM 3379 O ARG B 225 -23.289 5.289 -0.352 1.00 0.00

ATOM 3380 CB ARG B 225 -20.385 6.363 -1.490 1.00 0.00

ATOM 3381 CG ARG B 225 -19.589 7.636 -1.723 1.00 0.00

ATOM 3382 CD ARG B 225 -18.776 7.552 -3.004 1.00 0.00

ATOM 3383 NE ARG B 225 -17.983 8.757 -3.229 1.00 0.00

ATOM 3384 CZ ARG B 225 -17.129 8.913 -4.235 1.00 0.00

ATOM 3385 NHl ARG B 225 -16.450 10.045 -4.360 1.00 0.00

ATOM 3386 NH2 ARG B 225 -16.955 7.935 -5.115 1.00 0.00

ATOM 3387 N GLN B 226 -21.528 3.991 0.160 1.00 0.00

ATOM 3388 CA GLN B 226 -22 329 2.780 0.253 1.00 0.00

ATOM 3389 C GLN B 226 -23.393 2.914 1.336 1.00 0.00

ATOM 3390 O GLN B 226 -24.579 2.706 1.084 1.00 0.00

ATOM 3391 CB GLN B 226 -21.446 1.578 0.596 1.00 0.00

ATOM 3392 CG GLN B 226 -20.526 1.141 -0.533 1.00 0.00

ATOM 3393 CD GLN B 226 -19.575 0.037 -0.115 1.00 0.00

ATOM 3394 OEl GLN B 226 -19.541 -0.358 1.050 1.00 0.00

ATOM 3395 NE2 GLN B 226 -18.797 -0.463 -1.068 1.00 0.00 ATOM 3396 N LEU B 227 -22.971 3.263 2.542 .00 0.00

ATOM 3397 CA LEU B 227 -23.901 3.430 3.651 .00 0.00

ATOM 3398 C LEU B 99 n -25.004 4.398 3.253 .00 0.00

ATOM 3399 O LEU B 227 -26.190 4.158 3.511 .00 0.00

ATOM 3400 CB LEU B 227 -23.176 3.984 4.879 .00 0.00

ATOM 3401 CG LEU B 227 -22.217 3.027 5.590 .00 0.00

ATOM 3402 CDl LEU B 227 -21.428 3.757 6.667 .00 0.00

ATOM 3403 CD2 LEU B 227 _ 99 QQO .889 6.249 .00 0.00

ATOM 3404 N TYR B 228 -24.597 .506 2.643 .00 0.00

ATOM 3405 CA TYR B 228 -25.546 ,515 2.214 .00 0.00

ATOM 3406 C TYR B 228 -26.593 .835 1.355 .00 0.00

ATOM 3407 O TYR B 228 -27.761 .786 1.730 .00 0.00

ATOM 3408 CB TYR B 228 -24.842 ,604 1.405 .00 0.00

ATOM 3409 CG TYR B 228 -25.764 8.697 0.913 .00 0.00

ATOM 3410 CDl TYR B 228 -26.123 9.751 1.744 .00 0.00

ATOM 3411 CD2 TYR B 228 -26.273 8.670 -0.378 .00 0.00

ATOM 3412 CEl TYR B 228 -26.966 10.753 1.304 .00 0.00

ATOM 3413 CE2 TYR B 228 -27.117 9.664 -0.836 .00 0.00

ATOM 3414 CZ TYR B 228 -27.461 10.711 0.019 .00 0.00

ATOM 3415 OH TYR B 228 -28.302 11.709 -0.422 1.00 0.00

ATOM 3416 N GLU B 229 -26.177 5.295 0.213 1.00 0.00

ATOM 3417 CA GLU B 229 -27.101 4.596 -0.679 1..00 0.00

ATOM 3418 C GLU B 229 -28.066 .724 0.123 1..00 0.00

ATOM 3419 O GLU B 229 -29.287 .866 0.024 1..00 0.00

ATOM 3420 CB GLU B 229 -26.332 .697 -1 649 1.00 0.00

ATOM 3421 CG GLU B 229 -27.205 .025 2.697 1.00 0.00

ATOM 3422 CD GLU B 229 -26.395 >53 3.720 1.00 0.00

ATOM 3423 OEl GLU B 229 -25.152 >38 3.606 1.00 0.00

ATOM 3424 OE2 GLU B 229 -27.005 .662 4.637 1.00 0.00

ATOM 3425 N GLU B 230 -27.508 2.825 0.925 1.00 0.00

ATOM 3426 CA GLU B 230 -28.314 .937 1.751 1..00 0.00

ATOM 3427 C GLU B 230 -29.420 .699 2.483 1..00 0.00

ATOM 3428 O GLU B 230 -30.566 >59 2.540 1.00 0.00

ATOM 3429 CB GLU B 230 -27.444 >46 2.802 1.00 0.00

ATOM 3430 CG GLU B 230 -28.194 0.252 3.674 1.00 0.00

ATOM 3431 CD GLU B 230 -27.289 -0.457 4.661 1.00 0.00

ATOM 3432 OEl GLU B 230 -26.069 -0.189 4.647 1.00 0.00

ATOM 3433 OE2 GLU B 230 -27.798 -1. 282 448 1.00 0.00

ATOM 3434 N GLU B 231 -29.070 3.852 036 1..00 0.00

ATOM 3435 CA GLU B 231 -30.026 4.652 779 1..00 0.00

ATOM 3436 C GLU B 231 -31.047 5.370 2.913 1.00 0.00

ATOM 3437 O GLU B 231 -32.227 5.426 3.272 1.00 0.00

ATOM 3438 CB GLU B 231 -29.306 5.733 4.587 1.00 0.00

ATOM 3439 CG GLU B 231 -28.503 5.200 5.762 1.00 0.00

ATOM 3440 CD GLU B 231 -29.357 4.424 6.747 1.00 0.00

ATOM 3441 OEl GLU B 231 -30.390 4.966 7.192 1.00 0.00

ATOM 3442 OE2 GLU B 231 -28.992 3.275 7.074 1..00 0.00

ATOM 3443 N ILE B 232 -30.621 .938 1.789 1..00 0.00

ATOM 3444 CA ILE B 232 -31.619 .623 0.982 1..00 0.00

ATOM 3445 C ILE B 232 -32.565 .580 0.444 1.00 0.00

ATOM 3446 O ILE B 232 -33.704 .883 0.107 1.00 0.00

ATOM 3447 CB ILE B 232 -30.972 7.382 -0.191 1.00 0.00

ATOM 3448 CGl ILE B 909 -30.276 6.405 -1.140 1.00 0.00

ATOM 3449 CG2 ILE B 232 -29.940 8.375 0.321 1.00 0.00

ATOM 3450 CDl ILE B 232 -29.783 7.043 -2.420 1.00 0.00

ATOM 3451 N ARG B 233 -32.113 4.333 0.403 1..00 0.00

ATOM 3452 CA ARG B 233 -33.025 3.328 -0.076 1..00 0.00

ATOM 3453 C ARG B 233 -33.965 2.869 1.003 1.00 0.00

ATOM 3454 O ARG B 233 -35.126 2.583 0.728 1.00 0.00

ATOM 3455 CB ARG B 233 -32.257 .104 -0.578 1.00 0.00

ATOM 3456 CG ARG B 233 -31.487 .340 -1.869 1.00 0.00

ATOM 3457 CD ARG B 233 -30.674 .117 _ 9 257 1.00 0.00

ATOM 3458 NE ARG B 233 -29.967 .309 -3.521 1.00 0.00

ATOM 3459 CZ ARG B 233 -29.082 0.452 -4.021 00 0.00

ATOM 3460 NHl ARG B 233 -28.488 0.711 -5.177 00 0.00

ATOM 3461 NH2 ARG B 233 -28.792 -0.661 -3 361 00 0.00

ATOM 3462 N GLU B 234 -33.484 2.797 2.236 00 0.00

ATOM 3463 CA GLU B 234 -34.376 2.403 3.307 1.00 0.00 ATOM 3464 C GLU B 234 35.442 3.461 3.483 1.00 0.00

ATOM 3465 O GLU B 234 36.564 3.160 3.892 1.00 0.00

ATOM 3466 CB GLU B 234 33.604 2.249 4.619 1.00 0.00

ATOM 3467 CG GLU B 234 32.668 1.052 4.651 1.00 0.00

ATOM 3468 CD GLU B 234 31.853 0.983 5.927 1.00 0.00

ATOM 3469 OEl GLU B 234 31.976 1.906 6.760 1.00 0.00

ATOM 3470 OE2 GLU B 234 31.094 0.006 6.096 1.00 0.00

ATOM 3471 N LEU B 235 35.094 4.705 3.173 1.00 0.00

ATOM 3472 CA LEU B 235 36.057 5.788 3.254 1.00 0.00

ATOM 3473 C LEU B 235 37.072 5.459 2.147 1.00 0.00

ATOM 3474 O LEU B 235 38.253 5.272 2.422 1.00 0.00

ATOM 3475 CB LEU B 235 35.371 7.134 3.014 1.00 0.00

ATOM 3476 CG LEU B 235 36.274 8.370 3.042 1.00 0.00

ATOM 3477 CDl LEU B 235 36.916 8.535 4.410 1.00 0.00

ATOM 3478 CD2 LEU B 235 35.475 9.627 2.736 1.00 0.00

ATOM 3479 N GLN B 236 36.717 5.412 0.895 1.00 0.00

ATOM 3480 CA GLN B 236 37.744 5.171 -0.117 1.00 0.00

ATOM 3481 C GLN B 236 38.730 4.106 0.360 1.00 0.00

ATOM 3482 O GLN B 236 39.938 4.337 0.426 1.00 0.00

ATOM 3483 CB GLN B 236 37.107 4.689 -1.423 1.00 0.00

ATOM 3484 CG GLN B 236 38.104 4.423 -2.538 1.00 0.00

ATOM 3485 CD GLN B 236 37.433 4.003 -3.832 1.00 0.00

ATOM 3486 OEl GLN B 236 36.229 3.749 -3.862 1.00 0.00

ATOM 3487 NE2 GLN B 236 38.212 3.930 -4.904 1.00 0.00

ATOM 3488 N SER B 237 38.201 2.935 0.698 1.00 0.00

ATOM 3489 CA SER B 237 39.028 1.837 1.176 1.00 0.00

ATOM 3490 C SER B 237 40.025 2.304 2.239 1.00 0.00

ATOM 3491 O SER B 237 41.198 1.937 2.214 1.00 0.00

ATOM 3492 CB SER B 237 38.158 0.742 1.796 1.00 0.00

ATOM 3493 OG SER B 237 37.300 0.163 0.830 1.00 0.00

TER 3494 SER B 237

ATOM 3495 N ASP B 255 55.222 -1.786 4.294 1.00 0.00

ATOM 3496 CA ASP B 255 56.095 -2.631 5.101 1.00 0.00

ATOM 3497 C ASP B 255 57.125 -1.818 5.876 1.00 0.00

ATOM 3498 O ASP B 255 58.325 -2.036 5.695 1.00 0.00

ATOM 3499 CB ASP B 255 55.278 -3.431 6.117 1.00 0.00

ATOM 3500 CG ASP B 255 54.468 -4.539 5.472 1.00 0.00

ATOM 3501 ODl ASP B 255 54.690 -4.817 4.275 1.00 0.00

ATOM 3502 OD2 ASP B 255 53.612 -5.129 6.164 1.00 0.00

ATOM 3503 N MET B 256 56.675 -0.891 6.723 1.00 0.00

ATOM 3504 CA MET B 256 57.602 -0.071 7.499 1.00 0.00

ATOM 3505 C MET B 256 58.615 0.631 6.635 1.00 0.00

ATOM 3506 O MET B 256 59.761 0.764 7.033 1.00 0.00

ATOM 3507 CB MET B 256 56.841 1.006 8.277 1.00 0.00

ATOM 3508 CG MET B 256 55.995 0.466 9.418 1.00 0.00

ATOM 3509 SD MET B 256 54.999 1.744 10.210 1.00 0.00

ATOM 3510 CE MET B 256 56.278 2.770 10.932 1.00 0.00

ATOM 3511 N ASP B 257 58.220 1.082 5.455 1.00 0.00

ATOM 3512 CA ASP B 257 59.184 1.756 4.603 1.00 0.00

ATOM 3513 C ASP B 257 60.241 0.813 4.040 1.00 0.00

ATOM 3514 O ASP B 257 61.412 1.167 3.948 1.00 0.00

ATOM 3515 CB ASP B 257 58.482 2.411 3.411 1.00 0.00

ATOM 3516 CG ASP B 257 57.692 3.643 3.806 1.00 0.00

ATOM 3517 ODl ASP B 257 57.882 4.133 4.938 1.00 0.00

ATOM 3518 OD2 ASP B 257 56.884 4.119 2.981 1.00 0.00

ATOM 3519 N SER B 258 59.825 -0.395 3.692 1.00 0.00

ATOM 3520 CA SER B 258 60.749 -1.392 3.191 1.00 0.00

ATOM 3521 C SER B 258 61.740 -1.717 4.309 1.00 0.00

ATOM 3522 O SER B 258 62.956 -1.707 4.094 1.00 0.00

ATOM 3523 CB SER B 258 59.999 -2.660 2.780 1.00 0.00

ATOM 3524 OG SER B 258 59.161 -2.418 1.664 1.00 0.00

ATOM 3525 N ILE B 259 61.196 -1.990 5.494 1.00 0.00

ATOM 3526 CA ILE B 259 61.979 -2.335 6.679 1.00 0.00

ATOM 3527 C ILE B 259 62.987 -1.237 6.960 1.00 0.00

ATOM 3528 O ILE B 259 64.157 -1.515 7.205 1.00 0.00

ATOM 3529 CB ILE B 259 61.082 -2.500 7.920 1.00 0.00

ATOM 3530 CGl ILE B 259 60.182 -3.729 7.768 1.00 0.00

ATOM 3531 CG2 ILE B 259 61.930 -2.676 9.170 1.00 0.00 ATOM 3532 CDl ILE B 259 -59.086 -3.815 8.807 1.00 0.00

ATOM 3533 N ILE B 260 -62.534 0.012 6.912 1.00 0.00

ATOM 3534 CA ILE B 260 -63.430 1.135 7.143 1.00 0.00

ATOM 3535 C ILE B 260 -64.520 1.243 6.086 1.00 0.00

ATOM 3536 O ILE B 260 -65.643 1.631 6.398 1.00 0.00

ATOM 3537 CB ILE B 260 -62.669 2.475 7.134 1.00 0.00

ATOM 3538 CGl ILE B 260 -61.737 2.566 8.344 1.00 0.00

ATOM 3539 CG2 ILE B 260 -63.644 3.641 7.188 1.00 0.00

ATOM 3540 CDl ILE B 260 -60.762 3.722 8.277 1.00 0.00

ATOM 3541 N ALA B 261 -64.198 0.923 4.836 1.00 0.00

ATOM 3542 CA ALA B 261 -65.186 0.988 3.768 1.00 0.00

ATOM 3543 C ALA B 261 -66.283 -0.008 4.126 1.00 0.00

ATOM 3544 O ALA B 261 -67.469 0.321 4.113 1.00 0.00

ATOM 3545 CB ALA B 261 -64.552 0.622 2.435 1.00 0.00

ATOM 3546 N GLU B 262 -65.881 -1.227 4.455 1.00 0.00

ATOM 3547 CA GLU B 262 -66.843 -2.251 4.834 1.00 0.00

ATOM 3548 C GLU B 262 -67.704 -1.765 5.986 1.00 0.00

ATOM 3549 O GLU B 262 -68.927 -1.810 5.906 1.00 0.00

ATOM 3550 CB GLU B 262 -66.122 -3.528 5.270 1.00 0.00

ATOM 3551 CG GLU B 262 -67.054 -4.670 5.642 1.00 0.00

ATOM 3552 CD GLU B 262 -66.305 -5.928 6.037 1.00 0.00

ATOM 3553 OEl GLU B 262 -65.057 -5.910 6.008 1.00 0.00

ATOM 3554 OE2 GLU B 262 -66.967 -6.931 6.376 1.00 0.00

ATOM 3555 N VAL B 263 -67.069 -1.309 7.065 1.00 0.00

ATOM 3556 CA VAL B 263 -67.835 -0.878 8.232 1.00 0.00

ATOM 3557 C VAL B 263 -68.815 0.212 7.896 1.00 0.00

ATOM 3558 O VAL B 263 -69.882 0.285 8.494 1.00 0.00

ATOM 3559 CB VAL B 263 -66.916 -0.333 9.340 1.00 0.00

ATOM 3560 CGl VAL B 263 -67.739 0.288 10.458 1.00 0.00

ATOM 3561 CG2 VAL B 263 -66.071 -1.452 9.931 1.00 0.00

ATOM 3562 N LYS B 264 -68.462 1.071 6.964 1.00 0.00

ATOM 3563 CA LYS B 264 -69.379 2.133 6.609 1.00 0.00

ATOM 3564 C LYS B 264 -70.526 1.590 5.801 1.00 0.00

ATOM 3565 O LYS B 264 -71.626 2.119 5.851 1.00 0.00

ATOM 3566 CB LYS B 264 -68.665 3.203 5.780 1.00 0.00

ATOM 3567 CG LYS B 264 -67.657 4.028 6.564 1.00 0.00

ATOM 3568 CD LYS B 264 -66.984 5.064 5.681 1.00 0.00

ATOM 3569 CE LYS B 264 -65.977 5.888 6.465 1.00 0.00

ATOM 3570 NZ LYS B 264 -65.288 6.890 5.604 1.00 0.00

ATOM 3571 N ALA B 265 -70.269 0.533 5.042 1.00 0.00

ATOM 3572 CA ALA B 265 -71.309 -0.077 4.236 1.00 0.00

ATOM 3573 C ALA B 265 -72.299 -0.709 5.205 1.00 0.00

ATOM 3574 O ALA B 265 -73.515 -0.503 5.098 1.00 0.00

ATOM 3575 CB ALA B 265 -70.717 -1.134 3.317 1.00 0.00

ATOM 3576 N GLN B 266 -71.768 -1.466 6.159 1.00 0.00

ATOM 3577 CA GLN B 266 -72.607 -2.135 7.150 1.00 0.00

ATOM 3578 C GLN B 266 -73.404 -1.138 7.972 1.00 0.00

ATOM 3579 O GLN B 266 -74.552 -1.406 8.297 1.00 0.00

ATOM 3580 CB GLN B 266 -71.747 -2.956 8.114 1.00 0.00

ATOM 3581 CG GLN B 266 -71.123 -4.192 7.488 1.00 0.00

ATOM 3582 CD GLN B 266 -70.189 -4.917 8.437 1.00 0.00

ATOM 3583 OEl GLN B 266 -69.930 -4.450 9.546 1.00 0.00

ATOM 3584 NE2 GLN B 266 -69.680 -6.064 8.004 1.00 0.00

ATOM 3585 N TYR B 267 -72.794 -0.003 8.299 1.00 0.00

ATOM 3586 CA TYR B 267 -73.433 1.050 9.085 1.00 0.00

ATOM 3587 C TYR B 267 -74.595 1.613 8.247 1.00 0.00

ATOM 3588 O TYR B 267 -75.720 1.701 8.720 1.00 0.00

ATOM 3589 CB TYR B 267 -72.432 2.163 9.405 1.00 0.00

ATOM 3590 CG TYR B 267 -73.022 3.307 10.198 1.00 0.00

ATOM 3591 CDl TYR B 267 -73.224 3.193 11.568 1.00 0.00

ATOM 3592 CD2 TYR B 267 -73.374 4.497 9.575 1.00 0.00

ATOM 3593 CEl TYR B 267 -73.763 4.233 12.300 1.00 0.00

ATOM 3594 CE2 TYR B 267 -73.913 5.548 10.292 1.00 0.00

ATOM 3595 CZ TYR B 267 -74.106 5.407 11.666 1.00 0.00

ATOM 3596 OH TYR B 267 -74.642 6.445 12.394 1.00 0.00

ATOM 3597 N GLU B 268 -74.320 1.966 6.996 1.00 0.00

ATOM 3598 CA GLU B 268 -75.363 2.474 6.103 1.00 0.00

ATOM 3599 C GLU B 268 -76.571 1.499 6.110 1.00 0.00 ATOM 3600 O GLU B 268 77.725 1.916 6.219 1.00 0.00

ATOM 3601 CB GLU B 268 74.832 2.596 4.673 1.00 0.00

ATOM 3602 CG GLU B 268 75.843 3.143 3.680 1.00 0.00

ATOM 3603 CD GLU B 268 75.268 3.289 2.284 1.00 0.00

ATOM 3604 OEl GLU B 268 74.068 2.995 2.102 1.00 0.00

ATOM 3605 OE2 GLU B 268 76.018 3.698 1.372 1.00 0.00

ATOM 3606 N ASP B 269 76.292 0.200 5.999 1.00 0.00

ATOM 3607 CA ASP B 269 77.351 -0.817 5.999 1.00 0.00

ATOM 3608 C ASP B 269 78.131 -0.794 7.300 1.00 0.00

ATOM 3609 O ASP B 269 79.364 -0.777 7.292 1.00 0.00

ATOM 3610 CB ASP B 269 76.751 -2.214 5.829 1.00 0.00

ATOM 3611 CG ASP B 269 76.244 -2.464 4.422 1.00 0.00

ATOM 3612 ODl ASP B 269 76.567 -1.660 3.524 1.00 0.00

ATOM 3613 OD2 ASP B 269 75.525 -3.465 4.218 1.00 0.00

ATOM 3614 N ILE B 270 77.419 -0.806 8.420 1.00 0.00

ATOM 3615 CA ILE B 270 78.104 -0.783 9.706 1.00 0.00

ATOM 3616 C ILE B 270 79.004 0.424 9.841 1.00 0.00

ATOM 3617 O ILE B 270 80.113 0.303 10.358 1.00 0.00

ATOM 3618 CB ILE B 270 77.105 -0.740 10.877 1.00 0.00

ATOM 3619 CGl ILE B 270 76.265 -2.017 10.909 1.00 0.00

ATOM 3620 CG2 ILE B 270 77.842 -0.614 12.201 1.00 0.00

ATOM 3621 CDl ILE B 270 77.077 -3.278 11.112 1.00 0.00

ATOM 3622 N ALA B 271 78.544 1.582 9.378 1.00 0.00

ATOM 3623 CA ALA B 271 79.357 2.786 9.477 1.00 0.00

ATOM 3624 C ALA B 271 80.629 2.631 8.651 1.00 0.00

ATOM 3625 O ALA B 271 81.723 2.901 9.142 1.00 0.00

ATOM 3626 CB ALA B 271 78.586 3.991 8.959 1.00 0.00

ATOM 3627 N ASN B 272 80.513 2.167 7.416 1.00 0.00

ATOM 3628 CA ASN B 272 81.718 1.977 6.633 1.00 0.00

ATOM 3629 C ASN B 272 82.668 1.056 7.408 1.00 0.00

ATOM 3630 O ASN B 83.829 1.392 7.615 1.00 0.00

ATOM 3631 CB ASN B 272 81.384 1.340 5.283 1.00 0.00

ATOM 3632 CG ASN B 272 80.701 2.306 4.335 1.00 0.00

ATOM 3633 ODl ASN B 272 80.778 3.523 4.511 1.00 0.00

ATOM 3634 ND2 ASN B 80.028 1.768 3.325 1.00 0.00

ATOM 3635 N ARG B 273 82.171 -0.086 7.859 1.00 0.00

ATOM 3636 CA ARG B 273 83.020 -1.026 8.598 1.00 0.00

ATOM 3637 C ARG B 273 83.694 -0.411 9.821 1.00 0.00

ATOM 3638 O ARG B 273 84.877 -0.647 10.067 1.00 0.00

ATOM 3639 CB ARG B 273 82.194 -2.213 9.098 1.00 0.00

ATOM 3640 CG ARG B 273 81.672 -3.116 7.993 1.00 0.00

ATOM 3641 CD ARG B 273 80.840 -4.257 8.558 1.00 0.00

ATOM 3642 NE ARG B 273 80.307 -5.118 7.506 1.00 0.00

ATOM 3643 CZ ARG B 273 79.497 -6.149 7.724 1.00 0.00

ATOM 3644 NHl ARG B 273 79.061 -6.877 6.705 1.00 0.00

ATOM 3645 NH2 ARG B 273 79.124 -6.449 8.961 1.00 0.00

TER 3646 ARG B 273

ATOM 3647 N TYR B 282 93.407 -3.215 10.155 1.00 0.00

ATOM 3648 CA TYR B 282 94.347 -3.100 11.260 1.00 0.00

ATOM 3649 C TYR B 282 95.318 -1.977 11.045 1.00 0.00

ATOM 3650 O TYR B 282 96.500 -2.154 11.294 1.00 0.00

ATOM 3651 CB TYR B 282 93.603 -2.831 12.570 1.00 0.00

ATOM 3652 CG TYR B 282 92.890 -4.041 13.128 1.00 0.00

ATOM 3653 CDl TYR B 282 91.509 -4.158 13.035 1.00 0.00

ATOM 3654 CD2 TYR B 282 93.599 -5.063 13.747 1.00 0.00

ATOM 3655 CEl TYR B 282 90.848 -5.260 13.542 1.00 0.00

ATOM 3656 CE2 TYR B 282 92.954 -6.172 14.261 1.00 0.00

ATOM 3657 CZ TYR B 282 91.567 -6.265 14.153 1.00 0.00

ATOM 3658 OH TYR B 282 90.911 -7.363 14.659 1.00 0.00

ATOM 3659 N GLN B 283 94.801 -0.832 10.559 1.00 0.00

ATOM 3660 CA GLN B 283 95.670 0.310 10.330 1.00 0.00

ATOM 3661 C GLN B 283 96.840 -0.067 9.463 1.00 0.00

ATOM 3662 O GLN B 283 97.949 0.356 9.744 1.00 0.00

ATOM 3663 CB GLN B 283 94.903 1.436 9.631 1.00 0.00

ATOM 3664 CG GLN B 283 95.722 2.696 9.402 1.00 0.00

ATOM 3665 CD GLN B 283 94.925 3.794 8.729 1.00 0.00

ATOM 3666 OEl GLN B 283 93.777 3.589 8.333 1.00 0.00

ATOM 3667 NE2 GLN B 283 95.531 4.969 8.597 1.00 0.00 ATOM 3668 N ILE B 284 -96.586 -0.883 8.419 1.00 0.00

ATOM 3669 CA ILE B 284 -97.677 -1.285 7.547 1.00 0.00

ATOM 3670 C ILE B 284 -98.671 -2.141 8.284 1.00 0.00

ATOM 3671 O ILE B 284 -99.852 -1.838 8.253 1.00 0.00

ATOM 3672 CB ILE B 284 -97.166 -2.097 6.342 1.00 0.00

ATOM 3673 CGl ILE B 284 -96.324 -1.211 5.420 1.00 0.00

ATOM 3674 CG2 ILE B 284 -98.333 -2.653 5.541 1.00 0.00

ATOM 3675 CDl ILE B 284 -95.567 -1.980 4.360 1.00 0.00

ATOM 3676 N LYS B 285 -98.183 -3.210 8.946 1.00 0.00

ATOM 3677 CA LYS B 285 -99.093 -4.091 9.662 1.00 0.00

ATOM 3678 C LYS B 285 -99.905 -3.320 10.664 1.00 0.00

ATOM 3679 O LYS B 285 -101.104 -3.523 10.757 1.00 0.00

ATOM 3680 CB LYS B 285 -98.314 -5.175 10.409 1.00 0.00

ATOM 3681 CG LYS B 285 -97.670 -6.212 9.504 1.00 0.00

ATOM 3682 CD LYS B 285 -96.916 -7.256 10.310 1.00 0.00

ATOM 3683 CE LYS B 285 -96.252 -8.281 9.404 1.00 0.00

ATOM 3684 NZ LYS B 285 -95.481 -9.292 10.178 1.00 0.00

ATOM 3685 N TYR B 286 -99.226 -2.421 11.403 1.00 0.00

ATOM 3686 CA TYR B 286 -99.922 -1.620 12.395 1.00 0.00

ATOM 3687 C TYR B 286 -101.017 -0.814 11.753 1.00 0.00

ATOM 3688 O TYR B 286 -102.117 -0.779 12.281 1.00 0.00

ATOM 3689 CB TYR B 286 -98.952 -0.654 13.079 1.00 0.00

ATOM 3690 CG TYR B 286 -99.605 0.248 14.101 1.00 0.00

ATOM 3691 CDl TYR B 286 -99.899 -0.216 15.376 1.00 0.00

ATOM 3692 CD2 TYR B 286 -99.926 1.564 13.786 1.00 0.00

ATOM 3693 CEl TYR B 286 -100.495 0.603 16.316 1.00 0.00

ATOM 3694 CE2 TYR B 286 -100.524 2.396 14.713 1.00 0.00

ATOM 3695 CZ TYR B 286 -100.807 1.904 15.986 1.00 0.00

ATOM 3696 OH TYR B 286 -101.402 2.720 16.920 1.00 0.00

ATOM 3697 N GLU B 287 -100.707 -0.174 10.608 1.00 0.00

ATOM 3698 CA GLU B 287 -101.715 0.624 9.931 1.00 0.00

ATOM 3699 C GLU B 287 -102.924 -0.209 9.611 1.00 0.00

ATOM 3700 O GLU B 287 -104.036 0.222 9.872 1.00 0.00

ATOM 3701 CB GLU B 287 -101.160 1.189 8.622 1.00 0.00

ATOM 3702 CG GLU B 287 -102.136 2.078 7.867 1.00 0.00

ATOM 3703 CD GLU B 287 -101.540 2.646 6.594 1.00 0.00

ATOM 3704 OEl GLU B 287 -100.359 2.356 6.309 1.00 0.00

ATOM 3705 OE2 GLU B 287 -102.255 3.383 5.881 1.00 0.00

ATOM 3706 N GLU B 288 -102.690 -1.412 9.051 1.00 0.00

ATOM 3707 CA GLU B 288 -103.805 -2.287 8.729 1.00 0.00

ATOM 3708 C GLU B 288 -104.613 -2.583 9.961 1.00 0.00

ATOM 3709 O GLU B 288 -105.832 -2.531 9.905 1.00 0.00

ATOM 3710 CB GLU B 288 -103.298 -3.611 8.153 1.00 0.00

ATOM 3711 CG GLU B 288 -102.707 -3.495 6.758 1.00 0.00

ATOM 3712 CD GLU B 288 -102.105 -4.798 6.270 1.00 0.00

ATOM 3713 OEl GLU B 288 -102.084 -5.772 7.051 1.00 0.00

ATOM 3714 OE2 GLU B 288 -101.655 -4.845 5.105 1.00 0.00

ATOM 3715 N LEU B 289 -103.918 -2.884 11.074 1.00 0.00

ATOM 3716 CA LEU B 289 -104.623 -3.186 12.309 1.00 0.00

ATOM 3717 C LEU B 289 -105.497 -2.039 12.726 1.00 0.00

ATOM 3718 O LEU B 289 -106.663 -2.250 13.018 1.00 0.00

ATOM 3719 CB LEU B 289 -103.629 -3.461 13.440 1.00 0.00

ATOM 3720 CG LEU B 289 -102.833 -4.765 13.340 1.00 0.00

ATOM 3721 CDl LEU B 289 -101.756 -4.821 14.412 1.00 0.00

ATOM 3722 CD2 LEU B 289 -103.746 -5.967 13.520 1.00 0.00

ATOM 3723 N GLN B 290 -104.917 -0.823 12.745 1.00 0.00

ATOM 3724 CA GLN B 290 -105.678 0.334 13.184 1.00 0.00

ATOM 3725 C GLN B 290 -106.919 0.514 12.355 1.00 0.00

ATOM 3726 O GLN B 290 -107.980 0.743 12.911 1.00 0.00

ATOM 3727 CB GLN B 290 -104.836 1.607 13.062 1.00 0.00

ATOM 3728 CG GLN B 290 -105.543 2.866 13.538 1.00 0.00

ATOM 3729 CD GLN B 290 -104.673 4.101 13.420 1.00 0.00

ATOM 3730 OEl GLN B 290 -103.559 4.041 12.900 1.00 0.00

ATOM 3731 NE2 GLN B 290 -105.181 5.229 13.903 1.00 0.00

ATOM 3732 N SER B 291 -106.773 0.401 11.019 1.00 0.00

ATOM 3733 CA SER B 291 -107.935 0.551 10.160 1.00 0.00

ATOM 3734 C SER B 291 -108.973 -0.483 10.493 1.00 0.00

ATOM 3735 O SER B 291 -110.140 -0.150 10.613 1.00 0.00 ATOM 3736 CB SER B 291 -107.540 0.385 8.692 1.00 0.00

ATOM 3737 OG SER B 291 -106.695 1.440 8.267 1.00 0.00

ATOM 3738 N LEU B 292 -108.525 -1.745 10.655 1.00 0.00

ATOM 3739 CA LEU B 292 -109.458 -2.807 10.995 1.00 0.00

ATOM 3740 C LEU B 292 -110.171 -2.517 12.290 1.00 0.00

ATOM 3741 O LEU B 292 -111.350 -2.811 12.400 1.00 0.00

ATOM 3742 CB LEU B 292 -108.721 -4.139 11.149 1.00 0.00

ATOM 3743 CG LEU B 292 -108.155 -4.753 9.868 1.00 0.00

ATOM 3744 CDl LEU B 292 -107.299 -5.969 10.187 1.00 0.00

ATOM 3745 CD2 LEU B 292 -109.278 -5.192 8.941 1.00 0.00

ATOM 3746 N ALA B 293 -109.437 -1.938 13.263 1.00 0.00

ATOM 3747 CA ALA B 293 -110.026 -1.705 14.570 1.00 0.00

ATOM 3748 C ALA B 293 -111.251 -0.837 14.485 1.00 0.00

ATOM 3749 O ALA B 293 -112.295 -1.242 14.971 1.00 0.00

ATOM 3750 CB ALA B 293 -109.029 -1.012 15.485 1.00 0.00

ATOM 3751 N GLY B 294 -111.119 0.351 13.858 1.00 0.00

ATOM 3752 CA GLY B 294 -112.267 1.241 13.775 1.00 0.00

ATOM 3753 C GLY B 294 -113.425 0.585 13.075 1.00 0.00

ATOM 3754 O GLY B 294 -114.561 0.977 13.290 1.00 0.00

ATOM 3755 N LYS B 295 -113.123 -0.428 12.241 1.00 0.00

ATOM 3756 CA LYS B 295 -114.189 -1.145 11.566 1.00 0.00

ATOM 3757 C LYS B 295 -114.995 -1.933 12.561 1.00 0.00

ATOM 3758 O LYS B 295 -116.205 -1.776 12.609 1.00 0.00

ATOM 3759 CB LYS B 295 -113.613 -2.112 10.530 1.00 0.00

ATOM 3760 CG LYS B 295 -114.665 -2.873 9.739 1.00 0.00

ATOM 3761 CD LYS B 295 -114.028 -3.747 8.672 1.00 0.00

ATOM 3762 CE LYS B 295 -115.077 -4.534 7.904 1.00 0.00

ATOM 3763 NZ LYS B 295 -114.463 -5.438 6.891 1.00 0.00

ATOM 3764 N HIS B 296 -114.314 -2.786 13.353 1.00 0.00

ATOM 3765 CA HIS B 296 -115.030 -3.586 14.334 1.00 0.00

ATOM 3766 C HIS B 296 -115.776 -2.706 15.295 1.00 0.00

ATOM 3767 O HIS B 296 -116.862 -3.068 15.718 1.00 0.00

ATOM 3768 CB HIS B 296 -114.056 -4.453 15.135 1.00 0.00

ATOM 3769 CG HIS B 296 -113.451 -5.570 14.342 1.00 0.00

ATOM 3770 NDl HIS B 296 -114.203 -6.594 13.808 1.00 0.00

ATOM 3771 CD2 HIS B 296 -112.107 -5.934 13.918 1.00 0.00

ATOM 3772 CEl HIS B 296 -113.386 -7.442 13.156 1.00 0.00

ATOM 3773 NE2 HIS B 296 -112.128 -7.051 13.218 1.00 0.00

ATOM 3774 N GLY B 297 -115.194 -1.534 15.623 1.00 0.00

ATOM 3775 CA GLY B 297 -115.890 -0.616 16.509 1.00 0.00

ATOM 3776 C GLY B 297 -117.184 -0.166 15.895 1.00 0.00

ATOM 3777 O GLY B 297 -118.162 0.001 16.607 1.00 0.00

ATOM 3778 N ASP B 298 -117.186 0.021 14.560 1.00 0.00

ATOM 3779 CA ASP B 298 -118.417 0.413 13.895 1.00 0.00

ATOM 3780 C ASP B 298 -119.431 -0.691 13.994 1.00 0.00

ATOM 3781 O ASP B 298 -120.589 -0.417 14.262 1.00 0.00

ATOM 3782 CB ASP B 298 -118.156 0.707 12.416 1.00 0.00

ATOM 3783 CG ASP B 298 -117.409 2.009 12.204 1.00 0.00

ATOM 3784 ODl ASP B 298 -117.310 2.800 13.165 1.00 0.00

ATOM 3785 OD2 ASP B 298 -116.924 2.238 11.075 1.00 0.00

ATOM 3786 N ASP B 299 -118.977 -1.942 13.781 1.00 0.00

ATOM 3787 CA ASP B 299 -119.902 -3.063 13.846 1.00 0.00

ATOM 3788 C ASP B 299 -120.550 -3.144 15.197 1.00 0.00

ATOM 3789 O ASP B 299 -121.767 -3.177 15.277 1.00 0.00

ATOM 3790 CB ASP B 299 -119.168 -4.380 13.587 1.00 0.00

ATOM 3791 CG ASP B 299 -118.765 -4.547 12.135 1.00 0.00

ATOM 3792 ODl ASP B 299 -119.256 -3.769 11.290 1.00 0.00

ATOM 3793 OD2 ASP B 299 -117.960 -5.455 11.843 1.00 0.00

ATOM 3794 N LEU B 300 -119.717 -3.167 16.257 1.00 0.00

ATOM 3795 CA LEU B 300 -120.258 -3.218 17.604 1.00 0.00

ATOM 3796 C LEU B 300 -121.206 -2.076 17.837 1.00 0.00

ATOM 3797 O LEU B 300 -122.201 -2.252 18.522 1.00 0.00

ATOM 3798 CB LEU B 300 -119.132 -3.129 18.637 1.00 0.00

ATOM 3799 CG LEU B 300 -119.554 -3.187 20.107 1.00 0.00

ATOM 3800 CDl LEU B 300 -120.243 -4.508 20.416 1.00 0.00

ATOM 3801 CD2 LEU B 300 -118.345 -3.056 21.019 1.00 0.00

ATOM 3802 N ARG B 301 -120.888 -0.906 17.247 1.00 0.00

ATOM 3803 CA ARG B 301 -121.743 0.254 17.429 1.00 0.00 ATOM 3804 C ARG B 301 -123.148 -0.023 16.971 1.00 0.00

ATOM 3805 O ARG B 301 -124.067 0.076 17.769 1.00 0.00

ATOM 3806 CB ARG B 301 -121.212 1.443 16.626 1.00 0.00

ATOM 3807 CG ARG B 301 -122.009 2.723 16.811 1.00 0.00

ATOM 3808 CD ARG B 301 -121.509 3.824 15.889 1.00 0.00

ATOM 3809 NE ARG B 301 -121.775 3.523 14.484 1.00 0.00

ATOM 3810 CZ ARG B 301 -122.958 3.678 13.899 1.00 0.00

ATOM 3811 NHl ARG B 301 -123.106 3.379 12.615 1.00 0.00

ATOM 3812 NH2 ARG B 301 -123.989 4.132 14.597 1.00 0.00

ATOM 3813 N ARG B 302 -123.307 -0.371 15.678 1.00 0.00

ATOM 3814 CA ARG B 302 -124.641 -0.607 15.153 1.00 0.00

ATOM 3815 C ARG B 302 -125.344 -1.692 15.920 1.00 0.00

ATOM 3816 O ARG B 302 -126.540 -1.594 16.143 1.00 0.00

ATOM 3817 CB ARG B 302 -124.571 -1.033 13.685 1.00 0.00

ATOM 3818 CG ARG B 302 -124.168 0.082 12.734 1.00 0.00

ATOM 3819 CD ARG B 302 -124.048 -0.427 11.307 1.00 0.00

ATOM 3820 NE ARG B 302 -123.633 0.627 10.383 1.00 0.00

ATOM 3821 CZ ARG B 302 -123.383 0.432 9.092 1.00 0.00

ATOM 3822 NHl ARG B 302 -123.010 1.451 8.328 1.00 0.00

ATOM 3823 NH2 ARG B 302 -123.507 -0.780 8.567 1.00 0.00

ATOM 3824 N THR B 303 -124.583 -2.728 16.329 1.00 0.00

ATOM 3825 CA THR B 303 -125.199 -3.841 17.031 1.00 0.00

ATOM 3826 C THR B 303 -125.809 -3.409 18.336 1.00 0.00

ATOM 3827 O THR B 303 -126.934 -3.792 18.616 1.00 0.00

ATOM 3828 CB THR B 303 -124.173 -4.944 17.350 1.00 0.00

ATOM 3829 OGl THR B 303 -123.631 -5.464 16.128 1.00 0.00

ATOM 3830 CG2 THR B 303 -124.831 -6.078 18.119 1.00 0.00

ATOM 3831 N LYS B 304 -125.070 -2.605 19.129 1.00 0.00

ATOM 3832 CA LYS B 304 -125.623 -2.145 20.393 1.00 0.00

ATOM 3833 C LYS B 304 -126.921 -1.424 20.158 1.00 0.00

ATOM 3834 O LYS B 304 -127.860 -1.603 20.918 1.00 0.00

ATOM 3835 CB LYS B 304 -124.651 -1.187 21.086 1.00 0.00

ATOM 3836 CG LYS B 304 -123.397 -1.857 21.624 1.00 0.00

ATOM 3837 CD LYS B 304 -122.480 -0.851 22.298 1.00 0.00

ATOM 3838 CE LYS B 304 -121.214 -1.515 22.815 1.00 0.00

ATOM 3839 NZ LYS B 304 -120.291 -0.536 23.451 1.00 0.00

ATOM 3840 N THR B 305 -126.964 -0.621 19.077 1.00 0.00

ATOM 3841 CA THR B 305 -128.193 0.076 18.739 1.00 0.00

ATOM 3842 C THR B 305 -129.299 -0.910 18.480 1.00 0.00

ATOM 3843 O THR B 305 -130.389 -0.739 19.005 1.00 0.00

ATOM 3844 CB THR B 305 -128.023 0.941 17.476 1.00 0.00

ATOM 3845 OGl THR B 305 -127.025 1.942 17.711 1.00 0.00

ATOM 3846 CG2 THR B 305 -129.333 1.627 17.120 1.00 0.00

ATOM 3847 N GLU B 306 -129.005 -1.947 17.671 1.00 0.00

ATOM 3848 CA GLU B 306 -130.021 -2.941 17.365 1.00 0.00

ATOM 3849 C GLU B 306 -130.564 -3.561 18.620 1.00 0.00

ATOM 3850 O GLU B 306 -131.767 -3.721 18.739 1.00 0.00

ATOM 3851 CB GLU B 306 -129.435 -4.057 16.498 1.00 0.00

ATOM 3852 CG GLU B 306 -129.114 -3.632 15.074 1.00 0.00

ATOM 3853 CD GLU B 306 -128.423 -4.724 14.281 1.00 0.00

ATOM 3854 OEl GLU B 306 -128.128 -5.787 14.867 1.00 0.00

ATOM 3855 OE2 GLU B 306 -128.177 -4.517 13.074 1.00 0.00

ATOM 3856 N ILE B 307 -129.657 -3.901 19.557 1.00 0.00

ATOM 3857 CA ILE B 307 -130.096 -4.514 20.799 1.00 0.00

ATOM 3858 C ILE B 307 -131.064 -3.614 21.519 1.00 0.00

ATOM 3859 O ILE B 307 -132.074 -4.095 22.007 1.00 0.00

ATOM 3860 CB ILE B 307 -128.911 -4.787 21.744 1.00 0.00

ATOM 3861 CGl ILE B 307 -128.006 -5.875 21.163 1.00 0.00

ATOM 3862 CG2 ILE B 307 -129.411 -5.251 23.104 1.00 0.00

ATOM 3863 CDl ILE B 307 -126.685 -6.020 21.887 1.00 0.00

ATOM 3864 N SER B 308 -130.754 -2.303 21.562 1.00 0.00

ATOM 3865 CA SER B 308 -131.666 -1.369 22.205 1.00 0.00

ATOM 3866 C SER B 308 -133.033 -1.457 21.588 1.00 0.00

ATOM 3867 O SER B 308 -134.021 -1.444 22.305 1.00 0.00

ATOM 3868 CB SER B 308 -131.159 0.066 22.052 1.00 0.00

ATOM 3869 OG SER B 308 -129.944 0.257 22.758 1.00 0.00

ATOM 3870 N GLU B 309 -133.075 -1.561 20.246 1.00 0.00

ATOM 3871 CA GLU B 309 -134.359 -1.652 19.570 1.00 0.00 ATOM 3872 C GLU B 309 -135.098 -2.900 19.966 1.00 0.00

ATOM 3873 O GLU B 309 -136.272 -2.816 20.285 1.00 0.00

ATOM 3874 CB GLU B 309 -134.165 -1.679 18.053 1.00 0.00

ATOM 3875 CG GLU B 309 -135.463 -1.727 17.262 1.00 0.00

ATOM 3876 CD GLU B 309 -135.233 -1.718 15.764 1.00 0.00

ATOM 3877 OEl GLU B 309 -134.058 -1.660 15.344 1.00 0.00

ATOM 3878 OE2 GLU B 309 -136.227 -1.769 15.010 1.00 0.00

ATOM 3879 N MET B 310 -134.403 -4.055 19.941 1.00 0.00

ATOM 3880 CA MET B 310 -135.075 -5.302 20.270 1.00 0.00

ATOM 3881 C MET B 310 -135.667 -5.243 21.648 1.00 0.00

ATOM 3882 O MET B 310 -136.809 -5.635 21.827 1.00 0.00

ATOM 3883 CB MET B 310 -134.088 -6.470 20.222 1.00 0.00

ATOM 3884 CG MET B 310 -133.628 -6.838 18.821 1.00 0.00

ATOM 3885 SD MET B 310 -134.981 -7.401 17.770 1.00 0.00

ATOM 3886 CE MET B 310 -135.388 -8.961 18.549 1.00 0.00

ATOM 3887 N ASN B 311 -134.881 -4.731 22.616 1.00 0.00

ATOM 3888 CA ASN B 311 -135.397 -4.610 23.968 1.00 0.00

ATOM 3889 C ASN B 311 -136.630 -3.750 23.988 1.00 0.00

ATOM 3890 O ASN B 311 -137.577 -4.076 24.686 1.00 0.00

ATOM 3891 CB ASN B 311 -134.350 -3.974 24.885 1.00 0.00

ATOM 3892 CG ASN B 311 -134.782 -3.959 26.339 1.00 0.00

ATOM 3893 ODl ASN B 311 -134.970 -5.010 26.952 1.00 0.00

ATOM 3894 ND2 ASN B 311 -134.940 -2.764 26.895 1.00 0.00

ATOM 3895 N ARG B 312 -136.616 -2.653 23.204 1.00 0.00

ATOM 3896 CA ARG B 312 -137.779 -1.782 23.166 1.00 0.00

ATOM 3897 C ARG B 312 -138.977 -2.515 22.630 1.00 0.00

ATOM 3898 O ARG B 312 -140.029 -2.486 23.248 1.00 0.00

ATOM 3899 CB ARG B 312 -137.514 -0.573 22.267 1.00 0.00

ATOM 3900 CG ARG B 312 -136.519 0.422 22.843 1.00 0.00

ATOM 3901 CD ARG B 312 -136.269 1.572 21.881 1.00 0.00

ATOM 3902 NE ARG B 312 -135.278 2.512 22.399 1.00 0.00

ATOM 3903 CZ ARG B 312 -134.836 3.574 21.732 1.00 0.00

ATOM 3904 NHl ARG B 312 -133.933 4.374 22.282 1.00 0.00

ATOM 3905 NH2 ARG B 312 -135.298 3.833 20.516 1.00 0.00

ATOM 3906 N ASN B 313 -138.801 -3.177 21.469 1.00 0.00

ATOM 3907 CA ASN B 313 -139.914 -3.885 20.864 1.00 0.00

ATOM 3908 C ASN B 313 -140.458 -4.937 21.788 1.00 0.00

ATOM 3909 O ASN B 313 -141.666 -5.065 21.905 1.00 0.00

ATOM 3910 CB ASN B 313 -139.472 -4.574 19.571 1.00 0.00

ATOM 3911 CG ASN B 313 -139.242 -3.593 18.438 1.00 0.00

ATOM 3912 ODl ASN B 313 -139.740 -2.468 18.467 1.00 0.00

ATOM 3913 ND2 ASN B 313 -138.486 -4.019 17.433 1.00 0.00

ATOM 3914 N ILE B 314 -139.551 -5.679 22.454 1.00 0.00

ATOM 3915 CA ILE B 314 -139.996 -6.707 23.381 1.00 0.00

ATOM 3916 C ILE B 314 -140.847 -6.105 24.462 1.00 0.00

ATOM 3917 O ILE B 314 -141.896 -6.649 24.766 1.00 0.00

ATOM 3918 CB ILE B 314 -138.804 -7.414 24.054 1.00 0.00

ATOM 3919 CGl ILE B 314 -138.020 -8.233 23.026 1.00 0.00

ATOM 3920 CG2 ILE B 314 -139.290 -8.351 25.149 1.00 0.00

ATOM 3921 CDl ILE B 314 -136.690 -8.739 23.536 1.00 0.00

ATOM 3922 N SER B 315 -140.388 -4.972 25.031 1.00 0.00

ATOM 3923 CA SER B 315 -141.160 -4.330 26.082 1.00 0.00

ATOM 3924 C SER B 315 -142.549 -4.017 25.604 1.00 0.00

ATOM 3925 O SER B 315 -143.503 -4.306 26.309 1.00 0.00

ATOM 3926 CB SER B 315 -140.494 -3.023 26.513 1.00 0.00

ATOM 3927 OG SER B 315 -139.248 -3.269 27.143 1.00 0.00

ATOM 3928 N ARG B 316 -142.652 -3.438 24.392 1.00 0.00

ATOM 3929 CA ARG B 316 -143.965 -3.134 23.848 1.00 0.00

ATOM 3930 C ARG B 316 -144.801 -4.380 23.755 1.00 0.00

ATOM 3931 O ARG B 316 -145.963 -4.352 24.125 1.00 0.00

ATOM 3932 CB ARG B 316 -143.838 -2.533 22.447 1.00 0.00

ATOM 3933 CG ARG B 316 -143.273 -1.122 22.425 1.00 0.00

ATOM 3934 CD ARG B 316 -143.106 -0.616 21.001 1.00 0.00

ATOM 3935 NE ARG B 316 -142.537 0.729 20.961 1.00 0.00

ATOM 3936 CZ ARG B 316 -142.222 1.374 19.844 1.00 0.00

ATOM 3937 NHl ARG B 316 -141.709 2.596 19.905 1.00 0.00

ATOM 3938 NH2 ARG B 316 -142.421 0.797 18.667 1.00 0.00

ATOM 3939 N LEU B 317 -144.188 -5.478 23.266 1.00 0.00 ATOM 3940 CA LEU B 317 -144.928 -6.721 23.143 1.00 0.00

ATOM 3941 C LEU B 317 -145.442 -7.180 24.476 1.00 0.00

ATOM 3942 O LEU B 317 -146.613 -7.504 24.589 1.00 0.00

ATOM 3943 CB LEU B 317 -144.033 -7.824 22.573 1.00 0.00

ATOM 3944 CG LEU B 317 -143.634 -7.682 21.104 1.00 0.00

ATOM 3945 CDl LEU B 317 -142.599 -8.730 20.724 1.00 0.00

ATOM 3946 CD2 LEU B 317 -144.844 -7.859 20.199 1.00 0.00

ATOM 3947 N GLN B 318 -144.548 -7.198 25.485 1.00 0.00

ATOM 3948 CA GLN B 318 -144.947 -7.673 26.799 1.00 0.00

ATOM 3949 C GLN B 318 -146.118 -6.896 27.326 1.00 0.00

ATOM 3950 O GLN B 318 -147.072 -7.496 27.798 1.00 0.00

ATOM 3951 CB GLN B 318 -143.794 -7.527 27.794 1.00 0.00

ATOM 3952 CG GLN B 318 -142.643 -8.491 27.557 1.00 0.00

ATOM 3953 CD GLN B 318 -141.466 -8.230 28.476 1.00 0.00

ATOM 3954 OEl GLN B 318 -141.469 -7.270 29.247 1.00 0.00

ATOM 3955 NE2 GLN B 318 -140.452 -9.084 28.393 1.00 0.00

ATOM 3956 N ALA B 319 -146.039 -5.554 27.232 1.00 0.00

ATOM 3957 CA ALA B 319 -147.137 -4.732 27.713 1.00 0.00

ATOM 3958 C ALA B 319 -148.410 -5.098 27.002 1.00 0.00

ATOM 3959 O ALA B 319 -149.438 -5.240 27.646 1.00 0.00

ATOM 3960 CB ALA B 319 -146.847 -3.260 27.462 1.00 0.00

ATOM 3961 N GLU B 320 -148.319 -5.264 25.668 1.00 0.00

ATOM 3962 CA GLU B 320 -149.492 -5.646 24.900 1.00 0.00

ATOM 3963 C GLU B 320 -150.068 -6.934 25.415 1.00 0.00

ATOM 3964 O GLU B 320 -151.273 -7.024 25.593 1.00 0.00

ATOM 3965 CB GLU B 320 -149.129 -5.837 23.426 1.00 0.00

ATOM 3966 CG GLU B 320 -150.308 -6.193 22.537 1.00 0.00

ATOM 3967 CD GLU B 320 -149.916 -6.340 21.080 1.00 0.00

ATOM 3968 OEl GLU B 320 -148.722 -6.151 20.764 1.00 0.00

ATOM 3969 OE2 GLU B 320 -150.802 -6.646 20.254 1.00 0.00

ATOM 3970 N ILE B 321 -149.191 -7.929 25.657 1.00 0.00

ATOM 3971 CA ILE B 321 -149.665 -9.210 26.154 1.00 0.00

ATOM 3972 C ILE B 321 -150.441 -9.027 27.428 1.00 0.00

ATOM 3973 O ILE B 321 -151.513 -9.596 27.558 1.00 0.00

ATOM 3974 CB ILE B 321 -148.497 -10.169 26.446 1.00 0.00

ATOM 3975 CGl ILE B 321 -147.744 -10.502 25.155 1.00 0.00

ATOM 3976 CG2 ILE B 321 -149.011 -11.467 27.052 1.00 0.00

ATOM 3977 CDl ILE B 321 -148.590 -11.211 24.121 1.00 0.00

ATOM 3978 N GLU B 322 -149.893 -8.222 28.360 1.00 0.00

ATOM 3979 CA GLU B 322 -150.585 -7.997 29.617 1.00 0.00

ATOM 3980 C GLU B -151.973 -7.468 29.382 1.00 0.00

ATOM 3981 O GLU B -152.915 -7.990 29.955 1.00 0.00

ATOM 3982 CB GLU B 322 -149.827 -6.980 30.472 1.00 0.00

ATOM 3983 CG GLU B 322 -150.457 -6.717 31.829 1.00 0.00

ATOM 3984 CD GLU B -149.660 -5.731 32.662 1.00 0.00

ATOM 3985 OEl GLU B 322 -148.607 -5.264 32.181 1.00 0.00

ATOM 3986 OE2 GLU B 322 -150.089 -5.427 33.794 1.00 0.00

ATOM 3987 N GLY B 323 -152.089 -6.431 28.529 1.00 0.00

ATOM 3988 CA GLY B 323 -153.399 -5.847 28.289 1.00 0.00

ATOM 3989 C GLY B 323 -154.346 -6.844 27.685 1.00 0.00

ATOM 3990 O GLY B 323 -155.462 -6.971 28.162 1.00 0.00

ATOM 3991 N LEU B 324 -153.891 -7.553 26.633 1.00 0.00

ATOM 3992 CA LEU B 324 -154.760 -8.523 25.986 1.00 0.00

ATOM 3993 C LEU B 324 -155.234 -9.555 26.968 1.00 0.00

ATOM 3994 O LEU B 324 -156.403 -9.911 26.951 1.00 0.00

ATOM 3995 CB LEU B 324 -154.016 -9.241 24.859 1.00 0.00

ATOM 3996 CG LEU B 324 -153.678 -8.401 23.626 1.00 0.00

ATOM 3997 CDl LEU B 324 -152.788 -9.180 22.670 1.00 0.00

ATOM 3998 CD2 LEU B 324 -154.945 -8.005 22.881 1.00 0.00

ATOM 3999 N LYS B 325 -154.315 -10.024 27.834 1.00 0.00

ATOM 4000 CA LYS B 325 -154.694 -11.034 28.803 1.00 0.00

ATOM 4001 C LYS B 325 -155.757 -10.515 29.730 1.00 0.00

ATOM 4002 O LYS B 325 -156.737 -11.209 29.956 1.00 0.00

ATOM 4003 CB LYS B 325 -153.485 -11.448 29.645 1.00 0.00

ATOM 4004 CG LYS B 325 -153.782 -12.537 30.664 1.00 0.00

ATOM 4005 CD LYS B 325 -152.527 -12.948 31.414 1.00 0.00

ATOM 4006 CE LYS B 325 -152.832 -14.002 32.467 1.00 0.00

ATOM 4007 NZ LYS B 325 -151.614 -14.398 33.226 1.00 0.00 ATOM 4008 N GLY B 326 -155.564 -9.291 30.260 1.00 0.00

ATOM 4009 CA GLY B 326 -156.559 -8.747 31.171 1.00 0.00

ATOM 4010 C GLY B 326 -157.884 -8.590 30.482 1.00 0.00

ATOM 4011 O GLY B 326 -158.907 -8.916 31.063 1.00 0.00

ATOM 4012 N GLN B 327 -157.851 -8.095 29.229 1.00 0.00

ATOM 4013 CA GLN B 327 -159.088 -7.933 28.485 1.00 0.00

ATOM 4014 C GLN B 327 -159.778 -9.258 28.323 1.00 0.00

ATOM 4015 O GLN B 327 -160.976 -9.345 28.542 1.00 0.00

ATOM 4016 CB GLN B 327 -158.806 -7.360 27.094 1.00 0.00

ATOM 4017 CG GLN B 327 -158.367 -5.904 27.101 1.00 0.00

ATOM 4018 CD GLN B 327 -157.970 -5.410 25.723 1.00 0.00

ATOM 4019 OEl GLN B 327 -157.944 -6.178 24.761 1.00 0.00

ATOM 4020 NE2 GLN B 327 -157.658 -4.124 25.625 1.00 0.00

ATOM 4021 N ARG B 328 -158.998 -10.291 27.949 1.00 0.00

ATOM 4022 CA ARG B 328 -159.582 -11.606 27.761 1.00 0.00

ATOM 4023 C ARG B 328 -160.211 -12.095 29.036 1.00 0.00

ATOM 4024 O ARG B 328 -161.299 -12.645 28.989 1.00 0.00

ATOM 4025 CB ARG B 328 -158.510 -12.612 27.335 1.00 0.00

ATOM 4026 CG ARG B 328 -159.049 -14.001 27.033 1.00 0.00

ATOM 4027 CD ARG B 328 -157.931 -14.954 26.644 1.00 0.00

ATOM 4028 NE ARG B 328 -156.996 -15.180 27.745 1.00 0.00

ATOM 4029 CZ ARG B 328 -157.232 -15.992 28.770 1.00 0.00

ATOM 4030 NHl ARG B 328 -156.324 -16.136 29.725 1.00 0.00

ATOM 4031 NH2 ARG B 328 -158.376 -16.660 28.837 1.00 0.00

ATOM 4032 N ALA B 329 -159.522 -11.877 30.175 1.00 0.00

ATOM 4033 CA ALA B 329 -160.077 -12.311 31.445 1.00 0.00

ATOM 4034 C ALA B 329 -161.430 -11.695 31.665 1.00 0.00

ATOM 4035 O ALA B 329 -162.360 -12.398 32.027 1.00 0.00

ATOM 4036 CB ALA B 329 -159.167 -11.898 32.591 1.00 0.00

ATOM 4037 N SER B 330 -161.530 -10.372 31.429 1.00 0.00

ATOM 4038 CA SER B 330 -162.806 -9.703 31.613 1.00 0.00

ATOM 4039 C SER B 330 -163.849 -10.283 30.700 1.00 0.00

ATOM 4040 O SER B 330 -164.942 -10.583 31.153 1.00 0.00

ATOM 4041 CB SER B 330 -162.677 -8.210 31.306 1.00 0.00

ATOM 4042 OG SER B 330 -161.844 -7.564 32.253 1.00 0.00

ATOM 4043 N LEU B 331 -163.498 -10.446 29.409 1.00 0.00

ATOM 4044 CA LEU B 331 -164.456 -10.990 28.461 1.00 0.00

ATOM 4045 C LEU B 331 -164.962 -12.327 28.928 1.00 0.00

ATOM 4046 O LEU B 331 -166.145 -12.605 28.817 1.00 0.00

ATOM 4047 CB LEU B 331 -163.807 -11.173 27.088 1.00 0.00

ATOM 4048 CG LEU B 331 -163.456 -9.892 26.328 1.00 0.00

ATOM 4049 CDl LEU B 331 -162.659 -10.213 25.072 1.00 0.00

ATOM 4050 CD2 LEU B 331 -164.718 -9.151 25.913 1.00 0.00

ATOM 4051 N GLU B 332 -164.042 -13.145 29.471 1.00 0.00

ATOM 4052 CA GLU B 332 -164.439 -14.460 29.934 1.00 0.00

ATOM 4053 C GLU B 332 -165.331 -14.362 31.139 1.00 0.00

ATOM 4054 O GLU B 332 -166.248 -15.160 31.254 1.00 0.00

ATOM 4055 CB GLU B 332 -163.210 -15.287 30.317 1.00 0.00

ATOM 4056 CG GLU B 332 -162.352 -15.709 29.135 1.00 0.00

ATOM 4057 CD GLU B 332 -161.082 -16.419 29.561 1.00 0.00

ATOM 4058 OEl GLU B 332 -160.836 -16.517 30.782 1.00 0.00

ATOM 4059 OE2 GLU B 332 -160.331 -16.876 28.673 1.00 0.00

ATOM 4060 N ALA B 333 -165.081 -13.385 32.034 1.00 0.00

ATOM 4061 CA ALA B 333 -165.978 -13.220 33.167 1.00 0.00

ATOM 4062 C ALA B 333 -167.365 -12.923 32.670 1.00 0.00

ATOM 4063 O ALA B 333 -168.329 -13.506 33.143 1.00 0.00

ATOM 4064 CB ALA B 333 -165.512 -12.073 34.050 1.00 0.00

ATOM 4065 N ALA B 334 -167.441 -12.010 31.682 1.00 0.00

ATOM 4066 CA ALA B 334 -168.722 -11.718 31.063 1.00 0.00

ATOM 4067 C ALA B 334 -169.298 -12.958 30.439 1.00 0.00

ATOM 4068 O ALA B 334 -170.511 -13.085 30.386 1.00 0.00

ATOM 4069 CB ALA B 334 -168.560 -10.663 29.980 1.00 0.00

ATOM 4070 N ILE B 335 -168.415 -13.874 29.984 1.00 0.00

ATOM 4071 CA ILE B 335 -168.890 -15.124 29.411 1.00 0.00

ATOM 4072 C ILE B 335 -169.621 -15.909 30.465 1.00 0.00

ATOM 4073 O ILE B 335 -170.785 -16.227 30.271 1.00 0.00

ATOM 4074 CB ILE B 335 -167.724 -15.981 28.883 1.00 0.00

ATOM 4075 CGl ILE B 335 -167.061 -15.299 27.685 1.00 0.00 ATOM 4076 CG2 ILE B 335 -168.225 -17.348 28.444 1.00 0.00

ATOM 4077 CDl ILE B 335 -165.738 -15.916 27.286 1.00 0.00

ATOM 4078 N ALA B 336 -168.925 -16.219 31.576 1.00 0.00

ATOM 4079 CA ALA B 336 -169.529 -17.057 32.597 1.00 0.00

ATOM 4080 C ALA B 336 -170.793 -16.442 33.126 1.00 0.00

ATOM 4081 O ALA B 336 -171.810 -17.113 33.175 1.00 0.00

ATOM 4082 CB ALA B 336 -168.571 -17.245 33.763 1.00 0.00

ATOM 4083 N ASP B 337 -170.719 -15.152 33.508 1.00 0.00

ATOM 4084 CA ASP B 337 -171.902 -14.488 34.028 1.00 0.00

ATOM 4085 C ASP B 337 -173.030 -14.572 33.041 1.00 0.00

ATOM 4086 O ASP B 337 -174.150 -14.857 33.435 1.00 0.00

ATOM 4087 CB ASP B 337 -171.611 -13.012 34.303 1.00 0.00

ATOM 4088 CG ASP B 337 -170.733 -12.808 35.522 1.00 0.00

ATOM 4089 ODl ASP B 337 -170.545 -13.777 36.288 1.00 0.00

ATOM 4090 OD2 ASP B 337 -170.233 -11.680 35.712 1.00 0.00

ATOM 4091 N ALA B 338 -172.718 -14.331 31.753 1.00 0.00

ATOM 4092 CA ALA B 338 -173.759 -14.365 30.740 1.00 0.00

ATOM 4093 C ALA B 338 -174.404 -15.720 30.665 1.00 0.00

ATOM 4094 O ALA B 338 -175.616 -15.807 30.763 1.00 0.00

ATOM 4095 CB ALA B 338 -173.178 -14.044 29.372 1.00 0.00

ATOM 4096 N GLU B 339 -173.581 -16.775 30.493 1.00 0.00

ATOM 4097 CA GLU B 339 -174.140 -18.111 30.368 1.00 0.00

ATOM 4098 C GLU B 339 -174.962 -18.467 31.574 1.00 0.00

ATOM 4099 O GLU B 339 -176.049 -19.002 31.423 1.00 0.00

ATOM 4100 CB GLU B 339 -173.024 -19.148 30.230 1.00 0.00

ATOM 4101 CG GLU B 339 -172.291 -19.097 28.899 1.00 0.00

ATOM 4102 CD GLU B 339 -171.115 -20.053 28.844 1.00 0.00

ATOM 4103 OEl GLU B 339 -170.828 -20.700 29.872 1.00 0.00

ATOM 4104 OE2 GLU B 339 -170.481 -20.153 27.772 1.00 0.00

ATOM 4105 N GLN B 340 -174.435 -18.150 32.773 1.00 0.00

ATOM 4106 CA GLN B 340 -175.170 -18.459 33.988 1.00 0.00

ATOM 4107 C GLN B 340 -176.503 -17.764 34.001 1.00 0.00

ATOM 4108 O GLN B 340 -177.510 -18.400 34.264 1.00 0.00

ATOM 4109 CB GLN B 340 -174.383 -18.007 35.220 1.00 0.00

ATOM 4110 CG GLN B 340 -173.142 -18.837 35.503 1.00 0.00

ATOM 4111 CD GLN B 340 -172.317 -18.281 36.646 1.00 0.00

ATOM 4112 OEl GLN B 340 -172.627 -17.221 37.189 1.00 0.00

ATOM 4113 NE2 GLN B 340 -171.262 -18.998 37.016 1.00 0.00

ATOM 4114 N ARG B 341 -176.488 -16.448 33.714 1.00 0.00

ATOM 4115 CA ARG B 341 -177.721 -15.681 33.778 1.00 0.00

ATOM 4116 C ARG B 341 -178.752 -16.203 32.818 1.00 0.00

ATOM 4117 O ARG B 341 -179.883 -16.420 33.220 1.00 0.00

ATOM 4118 CB ARG B 341 -177.458 -14.215 33.429 1.00 0.00

ATOM 4119 CG ARG B 341 -176.678 -13.455 34.489 1.00 0.00

ATOM 4120 CD ARG B 341 -176.413 -12.022 34.057 1.00 0.00

ATOM 4121 NE ARG B 341 -175.620 -11.291 35.043 1.00 0.00

ATOM 4122 CZ ARG B 341 -175.203 -10.039 34.887 1.00 0.00

ATOM 4123 NHl ARG B 341 -174.487 -9.455 35.838 1.00 0.00

ATOM 4124 NH2 ARG B 341 -175.502 -9.374 33.779 1.00 0.00

ATOM 4125 N GLY B 342 -178.352 -16.404 31.545 1.00 0.00

ATOM 4126 CA GLY B 342 -179.315 -16.863 30.558 1.00 0.00

ATOM 4127 C GLY B 342 -179.927 -18.176 30.957 1.00 0.00

ATOM 4128 O GLY B 342 -181.108 -18.380 30.724 1.00 0.00

ATOM 4129 N GLU B 343 -179.118 -19.061 31.572 1.00 0.00

ATOM 4130 CA GLU B 343 -179.652 -20.344 31.996 1.00 0.00

ATOM 4131 C GLU B 343 -180.738 -20.156 33.018 1.00 0.00

ATOM 4132 O GLU B 343 -181.783 -20.778 32.908 1.00 0.00

ATOM 4133 CB GLU B 343 -178.550 -21.204 32.619 1.00 0.00

ATOM 4134 CG GLU B 343 -179.012 -22.586 33.051 1.00 0.00

ATOM 4135 CD GLU B 343 -177.887 -23.420 33.631 1.00 0.00

ATOM 4136 OEl GLU B 343 -176.742 -22.922 33.682 1.00 0.00

ATOM 4137 OE2 GLU B 343 -178.149 -24.573 34.034 1.00 0.00

ATOM 4138 N LEU B 344 -180.480 -19.282 34.011 1.00 0.00

ATOM 4139 CA LEU B 344 -181.465 -19.067 35.058 1.00 0.00

ATOM 4140 C LEU B 344 -182.744 -18.513 34.498 1.00 0.00

ATOM 4141 O LEU B 344 -183.809 -19.032 34.798 1.00 0.00

ATOM 4142 CB LEU B 344 -180.936 -18.075 36.097 1.00 0.00

ATOM 4143 CG LEU B 344 -181.877 -17.739 37.254 1.00 0.00 ATOM 4144 CDl LEU B 344 -182.198 -18.984 38.066 1.00 0.00

ATOM 4145 CD2 LEU B 344 -181.242 -16.715 38.183 1.00 0.00

ATOM 4146 N ALA B 345 -182.625 -17.448 33.683 1.00 0.00

ATOM 4147 CA ALA B 345 -183.817 -16.793 33.172 1.00 0.00

ATOM 4148 C ALA B 345 -184.622 -17.708 32.293 1.00 0.00

ATOM 4149 O ALA B 345 -185.834 -17.748 32.431 1.00 0.00

ATOM 4150 CB ALA B 345 -183.439 -15.572 32.349 1.00 0.00

ATOM 4151 N ILE B 346 -183.944 -18.453 31.397 1.00 0.00

ATOM 4152 CA ILE B 346 -184.667 -19.379 30.541 1.00 0.00

ATOM 4153 C ILE B 346 -185.414 -20.377 31.383 1.00 0.00

ATOM 4154 O ILE B 346 -186.544 -20.710 31.062 1.00 0.00

ATOM 4155 CB ILE B 346 -183.713 -20.151 29.611 1.00 0.00

ATOM 4156 CGl ILE B 346 -183.086 -19.204 28.586 1.00 0.00

ATOM 4157 CG2 ILE B 346 -184.464 -21.242 28.864 1.00 0.00

ATOM 4158 CDl ILE B 346 -181.943 -19.818 27.807 1.00 0.00

ATOM 4159 N LYS B 347 -184.772 -20.834 32.478 1.00 0.00

ATOM 4160 CA LYS B 347 -185.440 -21.767 33.368 1.00 0.00

ATOM 4161 C LYS B 347 -186.713 -21.170 33.902 1.00 0.00

ATOM 4162 O LYS B 347 -187.743 -21.822 33.864 1.00 0.00

ATOM 4163 CB LYS B 347 -184.538 -22.117 34.553 1.00 0.00

ATOM 4164 CG LYS B 347 -185.143 -23.122 35.519 1.00 0.00

ATOM 4165 CD LYS B 347 -184.169 -23.478 36.629 1.00 0.00

ATOM 4166 CE LYS B 347 -184.791 -24.446 37.622 1.00 0.00

ATOM 4167 NZ LYS B 347 -183.855 -24.784 38.729 1.00 0.00

ATOM 4168 N ASP B 348 -186.630 -19.919 34.397 1.00 0.00

ATOM 4169 CA ASP B 348 -187.810 -19.295 34.969 1.00 0.00

ATOM 4170 C ASP B 348 -188.903 -19.138 33.951 1.00 0.00

ATOM 4171 O ASP B 348 -190.038 -19.479 34.245 1.00 0.00

ATOM 4172 CB ASP B 348 -187.471 -17.904 35.510 1.00 0.00

ATOM 4173 CG ASP B 348 -186.646 -17.959 36.781 1.00 0.00

ATOM 4174 ODl ASP B 348 -186.539 -19.052 37.373 1.00 0.00

ATOM 4175 OD2 ASP B 348 -186.108 -16.906 37.185 1.00 0.00

ATOM 4176 N ALA B 349 -188.555 -18.628 32.752 1.00 0.00

ATOM 4177 CA ALA B 349 -189.565 -18.456 31.723 1.00 0.00

ATOM 4178 C ALA B 349 -190.251 -19.762 31.434 1.00 0.00

ATOM 4179 O ALA B 349 -191.470 -19.807 31.386 1.00 0.00

ATOM 4180 CB ALA B 349 -188.930 -17.951 30.436 1.00 0.00

ATOM 4181 N ASN B 350 -189.442 -20.824 31.259 1.00 0.00

ATOM 4182 CA ASN B 350 -190.008 -22.130 30.968 1.00 0.00

ATOM 4183 C ASN B 350 -190.934 -22.582 32.060 1.00 0.00

ATOM 4184 O ASN B 350 -192.019 -23.058 31.766 1.00 0.00

ATOM 4185 CB ASN B 350 -188.900 -23.174 30.826 1.00 0.00

ATOM 4186 CG ASN B 350 -188.116 -23.022 29.537 1.00 0.00

ATOM 4187 ODl ASN B 350 -188.584 -22.395 28.586 1.00 0.00

ATOM 4188 ND2 ASN B 350 -186.920 -23.597 29.501 1.00 0.00

ATOM 4189 N ALA B 351 -190.505 -22.425 33.327 1.00 0.00

ATOM 4190 CA ALA B 351 -191.355 -22.848 34.426 1.00 0.00

ATOM 4191 C ALA B 351 -192.657 -22.095 34.431 1.00 0.00

ATOM 4192 O ALA B 351 -193.702 -22.701 34.607 1.00 0.00

ATOM 4193 CB ALA B 351 -190.663 -22.600 35.758 1.00 0.00

ATOM 4194 N LYS B 352 -192.578 -20.765 34.232 1.00 0.00

ATOM 4195 CA LYS B 352 -193.780 -19.949 34.289 1.00 0.00

ATOM 4196 C LYS B 352 -194.784 -20.377 33.257 1.00 0.00

ATOM 4197 O LYS B 352 -195.888 -20.755 33.614 1.00 0.00

ATOM 4198 CB LYS B 352 -193.443 -18.478 34.037 1.00 0.00

ATOM 4199 CG LYS B 352 -194.645 -17.549 34.080 1.00 0.00

ATOM 4200 CD LYS B 352 -194.233 -16.103 33.859 1.00 0.00

ATOM 4201 CE LYS B 352 -195.437 -15.176 33.885 1.00 0.00

ATOM 4202 NZ LYS B 352 -195.053 -13.758 33.638 1.00 0.00

ATOM 4203 N LEU B 353 -194.387 -20.307 31.971 1.00 0.00

ATOM 4204 CA LEU B 353 -195.307 -20.681 30.909 1.00 0.00

ATOM 4205 C LEU B 353 -195.861 -22.061 31.129 1.00 0.00

ATOM 4206 O LEU B 353 -196.994 -22.323 30.757 1.00 0.00

ATOM 4207 CB LEU B 353 -194.596 -20.667 29.555 1.00 0.00

ATOM 4208 CG LEU B 353 -194.168 -19.296 29.029 1.00 0.00

ATOM 4209 CDl LEU B 353 -193.353 -19.440 27.752 1.00 0.00

ATOM 4210 CD2 LEU B 353 -195.383 -18.433 28.721 1.00 0.00

ATOM 4211 N SER B 354 -195.049 -22.935 31.757 1.00 0.00 ATOM 4212 CA SER B 354 -195.498 -24.291 32.002 1.00 0.00

ATOM 4213 C SER B 354 -196.713 -24.309 32.889 1.00 0.00

ATOM 4214 O SER B 354 -197.751 -24.795 32.471 1.00 0.00

ATOM 4215 CB SER B 354 -194.398 -25.105 32.688 1.00 0.00

ATOM 4216 OG SER B 354 -194.825 -26.433 32.937 1.00 0.00

ATOM 4217 N GLU B 355 -196.568 -23.773 34.119 1.00 0.00

ATOM 4218 CA GLU B 355 -197.687 -23.791 35.049 1.00 0.00

ATOM 4219 C GLU B 355 -198.886 -23.096 34.471 1.00 0.00

ATOM 4220 O GLU B 355 -200.002 -23.540 34.695 1.00 0.00

ATOM 4221 CB GLU B 355 -197.311 -23.084 36.352 1.00 0.00

ATOM 4222 CG GLU B 355 -196.309 -23.845 37.206 1.00 0.00

ATOM 4223 CD GLU B 355 -195.869 -23.060 38.426 1.00 0.00

ATOM 4224 OEl GLU B 355 -196.289 -21.893 38.565 1.00 0.00

ATOM 4225 OE2 GLU B 355 -195.103 -23.613 39.242 1.00 0.00

ATOM 4226 N LEU B 356 -198.643 -22.006 33.717 1.00 0.00

ATOM 4227 CA LEU B 356 -199.751 -21.251 33.161 1.00 0.00

ATOM 4228 C LEU B 356 -200.569 -22.071 32.202 1.00 0.00

ATOM 4229 O LEU B 356 -201.787 -22.045 32.289 1.00 0.00

ATOM 4230 CB LEU B 356 -199.238 -20.026 32.402 1.00 0.00

ATOM 4231 CG LEU B 356 -198.638 -18.905 33.251 1.00 0.00

ATOM 4232 CDl LEU B 356 -197.998 -17.844 32.369 1.00 0.00

ATOM 4233 CD2 LEU B 356 -199.713 -18.235 34.095 1.00 0.00

ATOM 4234 N GLU B 357 -199.894 -22.807 31.295 1.00 0.00

ATOM 4235 CA GLU B 357 -200.635 -23.637 30.358 1.00 0.00

ATOM 4236 C GLU B 357 -201.482 -24.634 31.099 1.00 0.00

ATOM 4237 O GLU B 357 -202.614 -24.874 30.708 1.00 0.00

ATOM 4238 CB GLU B 357 -199.675 -24.400 29.443 1.00 0.00

ATOM 4239 CG GLU B 357 -198.954 -23.525 28.431 1.00 0.00

ATOM 4240 CD GLU B 357 -197.924 -24.292 27.627 1.00 0.00

ATOM 4241 OEl GLU B 357 -197.720 -25.490 27.912 1.00 0.00

ATOM 4242 OE2 GLU B 357 -197.319 -23.694 26.711 1.00 0.00

ATOM 4243 N ALA B 358 -200.923 -25.195 32.190 1.00 0.00

ATOM 4244 CA ALA B 358 -201.688 -26.140 32.984 1.00 0.00

ATOM 4245 C ALA B 358 -202.924 -25.484 33.533 1.00 0.00

ATOM 4246 O ALA B 358 -203.996 -26.062 33.458 1.00 0.00

ATOM 4247 CB ALA B 358 -200.854 -26.651 34.149 1.00 0.00

ATOM 4248 N ALA B 359 -202.759 -24.263 34.079 1.00 0.00

ATOM 4249 CA ALA B 359 -203.905 -23.553 34.624 1.00 0.00

ATOM 4250 C ALA B 359 -204.955 -23.343 33.570 1.00 0.00

ATOM 4251 O ALA B 359 -206.128 -23.533 33.848 1.00 0.00

ATOM 4252 CB ALA B 359 -203.483 -22.192 35.154 1.00 0.00

ATOM 4253 N LEU B 360 -204.518 -22.959 32.353 1.00 0.00

ATOM 4254 CA LEU B 360 -205.471 -22.751 31.276 1.00 0.00

ATOM 4255 C LEU B 360 -206.264 -24.002 31.016 1.00 0.00

ATOM 4256 O LEU B 360 -207.466 -23.918 30.816 1.00 0.00

ATOM 4257 CB LEU B 360 -204.746 -22.365 29.985 1.00 0.00

ATOM 4258 CG LEU B 360 -205.630 -22.099 28.766 1.00 0.00

ATOM 4259 CDl LEU B 360 -206.571 -20.932 29.028 1.00 0.00

ATOM 4260 CD2 LEU B 360 -204.780 -21.759 27.551 1.00 0.00

ATOM 4261 N GLN B 361 -205.583 -25.165 31.043 1.00 0.00

ATOM 4262 CA GLN B 361 -206.290 -26.421 30.850 1.00 0.00

ATOM 4263 C GLN B 361 -207.382 -26.570 31.872 1.00 0.00

ATOM 4264 O GLN B 361 -208.485 -26.962 31.527 1.00 0.00

ATOM 4265 CB GLN B 361 -205.330 -27.603 30.990 1.00 0.00

ATOM 4266 CG GLN B 361 -204.336 -27.735 29.847 1.00 0.00

ATOM 4267 CD GLN B 361 -203.330 -28.846 30.075 1.00 0.00

ATOM 4268 OEl GLN B 361 -203.311 -29.472 31.135 1.00 0.00

ATOM 4269 NE2 GLN B 361 -202.489 -29.095 29.078 1.00 0.00

ATOM 4270 N ARG B 362 -207.057 -26.239 33.138 1.00 0.00

ATOM 4271 CA ARG B 362 -208.042 -26.374 34.196 1.00 0.00

ATOM 4272 C ARG B 362 -209.230 -25.485 33.956 1.00 0.00

ATOM 4273 O ARG B 362 -210.353 -25.947 34.073 1.00 0.00

ATOM 4274 CB ARG B 362 -207.433 -25.994 35.548 1.00 0.00

ATOM 4275 CG ARG B 362 -206.416 -26.993 36.073 1.00 0.00

ATOM 4276 CD ARG B 362 -205.818 -26.531 37.392 1.00 0.00

ATOM 4277 NE ARG B 362 -204.801 -27.456 37.886 1.00 0.00

ATOM 4278 CZ ARG B 362 -204.086 -27.261 38.989 1.00 0.00

ATOM 4279 NHl ARG B 362 -203.184 -28.158 39.362 1.00 0.00 ATOM 4280 NH2 ARG B 362 -204.274 -26.168 39.717 1.00 0.00

ATOM 4281 N ALA B 363 -208.970 -24.205 33.620 1.00 0.00

ATOM 4282 CA ALA B 363 -210.068 -23.275 33.416 1.00 0.00

ATOM 4283 C ALA B 363 -210.988 -23.759 32.331 1.00 0.00

ATOM 4284 O ALA B 363 -212.195 -23.695 32.492 1.00 0.00

ATOM 4285 CB ALA B 363 -209.537 -21.907 33.013 1.00 0.00

ATOM 4286 N LYS B 364 -210.397 -24.260 31.229 1.00 0.00

ATOM 4287 CA LYS B 364 -211.218 -24.789 30.152 1.00 0.00

ATOM 4288 C LYS B 364 -212.088 -25.905 30.661 1.00 0.00

ATOM 4289 O LYS B 364 -213.254 -25.970 30.307 1.00 0.00

ATOM 4290 CB LYS B 364 -210.338 -25.334 29.025 1.00 0.00

ATOM 4291 CG LYS B 364 -209.605 -24.261 28.237 1.00 0.00

ATOM 4292 CD LYS B 364 -208.753 -24.870 27.135 1.00 0.00

ATOM 4293 CE LYS B 364 -208.001 -23.799 26.362 1.00 0.00

ATOM 4294 NZ LYS B 364 -207.136 -24.383 25.301 1.00 0.00

ATOM 4295 N GLN B 365 -211.501 -26.774 31.508 1.00 0.00

ATOM 4296 CA GLN B 365 -212.259 -27.898 32.028 1.00 0.00

ATOM 4297 C GLN B 365 -213.408 -27.431 32.876 1.00 0.00

ATOM 4298 O GLN B 365 -214.528 -27.864 32.657 1.00 0.00

ATOM 4299 CB GLN B 365 -211.365 -28.793 32.890 1.00 0.00

ATOM 4300 CG GLN B 365 -210.330 -29.579 32.103 1.00 0.00

ATOM 4301 CD GLN B 365 -209.380 -30.350 32.997 1.00 0.00

ATOM 4302 OEl GLN B 365 -209.439 -30.241 34.222 1.00 0.00

ATOM 4303 NE2 GLN B 365 -208.498 -31.134 32.387 1.00 0.00

ATOM 4304 N ASP B 366 -213.119 -26.540 33.845 1.00 0.00

ATOM 4305 CA ASP B 366 -214.177 -26.064 34.721 1.00 0.00

ATOM 4306 C ASP B 366 -215.269 -25.405 33.930 1.00 0.00

ATOM 4307 O ASP B 366 -216.435 -25.627 34.214 1.00 0.00

ATOM 4308 CB ASP B 366 -213.627 -25.043 35.720 1.00 0.00

ATOM 4309 CG ASP B 366 -212.771 -25.684 36.795 1.00 0.00

ATOM 4310 ODl ASP B 366 -212.792 -26.926 36.910 1.00 0.00

ATOM 4311 OD2 ASP B 366 -212.077 -24.941 37.522 1.00 0.00

ATOM 4312 N MET B 367 -214.873 -24.599 32.926 1.00 0.00

ATOM 4313 CA MET B 367 -215.862 -23.932 32.098 1.00 0.00

ATOM 4314 C MET B 367 -216.760 -24.937 31.432 1.00 0.00

ATOM 4315 O MET B 367 -217.967 -24.757 31.441 1.00 0.00

ATOM 4316 CB MET B 367 -215.178 -23.102 31.009 1.00 0.00

ATOM 4317 CG MET B 367 -216.143 -22.383 30.079 1.00 0.00

ATOM 4318 SD MET B 367 -215.300 -21.474 28.771 1.00 0.00

ATOM 4319 CE MET B 367 -214.730 -22.819 27.735 1.00 0.00

ATOM 4320 N ALA B 368 -216.157 -25.999 30.862 1.00 0.00

ATOM 4321 CA ALA B 368 -216.957 -27.013 30.195 1.00 0.00

ATOM 4322 C ALA B 368 -217.965 -27.600 31.141 1.00 0.00

ATOM 4323 O ALA B 368 -219.122 -27.737 30.776 1.00 0.00

ATOM 4324 CB ALA B 368 -216.069 -28.136 29.681 1.00 0.00

ATOM 4325 N ARG B 369 -217.513 -27.935 32.366 1.00 0.00

ATOM 4326 CA ARG B 369 -218.431 -28.485 33.346 1.00 0.00

ATOM 4327 C ARG B 369 -219.561 -27.529 33.600 1.00 0.00

ATOM 4328 O ARG B 369 -220.706 -27.949 33.646 1.00 0.00

ATOM 4329 CB ARG B 369 -217.709 -28.745 34.670 1.00 0.00

ATOM 4330 CG ARG B 369 -216.731 -29.907 34.626 1.00 0.00

ATOM 4331 CD ARG B 369 -215.997 -30.062 35.948 1.00 0.00

ATOM 4332 NE ARG B 369 -215.032 -31.158 35.915 1.00 0.00

ATOM 4333 CZ ARG B 369 -214.209 -31.460 36.913 1.00 0.00

ATOM 4334 NHl ARG B 369 -213.364 -32.475 36.792 1.00 0.00

ATOM 4335 NH2 ARG B 369 -214.233 -30.747 38.030 1.00 0.00

ATOM 4336 N GLN B 370 -219.225 -26.232 33.751 1.00 0.00

ATOM 4337 CA GLN B 370 -220.260 -25.244 34.004 1.00 0.00

ATOM 4338 C GLN B 370 -221.252 -25.202 32.878 1.00 0.00

ATOM 4339 O GLN B 370 -222.445 -25.219 33.134 1.00 0.00

ATOM 4340 CB GLN B 370 -219.647 -23.850 34.151 1.00 0.00

ATOM 4341 CG GLN B 370 -218.846 -23.656 35.429 1.00 0.00

ATOM 4342 CD GLN B 370 -218.145 -22.312 35.477 1.00 0.00

ATOM 4343 OEl GLN B 370 -218.187 -21.543 34.517 1.00 0.00

ATOM 4344 NE2 GLN B 370 -217.495 -22.026 36.600 1.00 0.00

ATOM 4345 N LEU B 371 -220.748 -25.159 31.630 1.00 0.00

ATOM 4346 CA LEU B 371 -221.644 -25.097 30.487 1.00 0.00

ATOM 4347 C LEU B 371 -222.588 -26.264 30.472 1.00 0.00 ATOM 4348 O LEU B 371 -223.777 -26.071 30.265 1.00 0.00

ATOM 4349 CB LEU B 371 -220.848 -25.114 29.181 1.00 0.00

ATOM 4350 CG LEU B 371 -221.665 -25.070 27.889 1.00 0.00

ATOM 4351 CDl LEU B 371 -222.474 -23.784 27.808 1.00 0.00

ATOM 4352 CD2 LEU B 371 -220.754 -25.135 26.672 1.00 0.00

ATOM 4353 N ARG B 372 -222.049 -27.476 30.705 1.00 0.00

ATOM 4354 CA ARG B 372 -222.904 -28.652 30.720 1.00 0.00

ATOM 4355 C ARG B 372 -223.968 -28.508 31.771 1.00 0.00

ATOM 4356 O ARG B 372 -225.125 -28.781 31.494 1.00 0.00

ATOM 4357 CB ARG B 372 -222.084 -29.907 31.027 1.00 0.00

ATOM 4358 CG ARG B 372 -221.154 -30.331 29.902 1.00 0.00

ATOM 4359 CD ARG B 372 -220.339 -31.553 30.291 1.00 0.00

ATOM 4360 NE ARG B 372 -219.405 -31.945 29.238 1.00 0.00

ATOM 4361 CZ ARG B 372 -218.536 -32.946 29.344 1.00 0.00

ATOM 4362 NHl ARG B 372 -217.725 -33.231 28.335 1.00 0.00

ATOM 4363 NH2 ARG B 372 -218.481 -33.660 30.460 1.00 0.00

ATOM 4364 N GLU B 373 -223.562 -28.062 32.978 1.00 0.00

ATOM 4365 CA GLU B 373 -224.529 -27.873 34.046 1.00 0.00

ATOM 4366 C GLU B 373 -225.616 -26.934 33.605 1.00 0.00

ATOM 4367 O GLU B 373 -226.783 -27.218 33.812 1.00 0.00

ATOM 4368 CB GLU B 373 -223.851 -27.283 35.285 1.00 0.00

ATOM 4369 CG GLU B 373 -222.925 -28.251 36.005 1.00 0.00

ATOM 4370 CD GLU B 373 -222.167 -27.594 37.142 1.00 0.00

ATOM 4371 OEl GLU B 373 -222.304 -26.365 37.315 1.00 0.00

ATOM 4372 OE2 GLU B 373 -221.437 -28.309 37.860 1.00 0.00

ATOM 4373 N TYR B 374 -225.198 -25.812 32.985 1.00 0.00

ATOM 4374 CA TYR B 374 -226.159 -24.821 32.539 1.00 0.00

ATOM 4375 C TYR B 374 -227.187 -25.432 31.627 1.00 0.00

ATOM 4376 O TYR B 374 -228.368 -25.182 31.810 1.00 0.00

ATOM 4377 CB TYR B 374 -225.454 -23.697 31.774 1.00 0.00

ATOM 4378 CG TYR B 374 -226.392 -22.640 31.237 1.00 0.00

ATOM 4379 CDl TYR B 374 -226.886 -21.642 32.067 1.00 0.00

ATOM 4380 CD2 TYR B 374 -226.781 -22.644 29.904 1.00 0.00

ATOM 4381 CEl TYR B 374 -227.744 -20.670 31.585 1.00 0.00

ATOM 4382 CE2 TYR B 374 -227.637 -21.682 29.405 1.00 0.00

ATOM 4383 CZ TYR B 374 -228.119 -20.690 30.259 1.00 0.00

ATOM 4384 OH TYR B 374 -228.973 -19.725 29.777 1.00 0.00

ATOM 4385 N GLN B 375 -226.726 -26.239 30.652 1.00 0.00

ATOM 4386 CA GLN B 375 -227.663 -26.873 29.737 1.00 0.00

ATOM 4387 C GLN B 375 -228.666 -27.698 30.493 1.00 0.00

ATOM 4388 O GLN B 375 -229.854 -27.591 30.237 1.00 0.00

ATOM 4389 CB GLN B 375 -226.923 -27.791 28.762 1.00 0.00

ATOM 4390 CG GLN B 375 -226.082 -27.053 27.732 1.00 0.00

ATOM 4391 CD GLN B 375 -225.261 -27.991 26.870 1.00 0.00

ATOM 4392 OEl GLN B 375 -225.253 -29.203 27.088 1.00 0.00

ATOM 4393 NE2 GLN B 375 -224.566 -27.432 25.885 1.00 0.00

ATOM 4394 N GLU B 376 -228.159 -28.518 31.436 1.00 0.00

ATOM 4395 CA GLU B 376 -229.042 -29.379 32.202 1.00 0.00

ATOM 4396 C GLU B 376 -230.068 -28.576 32.951 1.00 0.00

ATOM 4397 O GLU B 376 -231.252 -28.846 32.816 1.00 0.00

ATOM 4398 CB GLU B 376 -228.243 -30.196 33.220 1.00 0.00

ATOM 4399 CG GLU B 376 -229.085 -31.162 34.038 1.00 0.00

ATOM 4400 CD GLU B 376 -228.256 -31.977 35.010 1.00 0.00

ATOM 4401 OEl GLU B 376 -227.020 -31.797 35.035 1.00 0.00

ATOM 4402 OE2 GLU B 376 -228.841 -32.798 35.748 1.00 0.00

ATOM 4403 N LEU B 377 -229.599 -27.590 33.740 1.00 0.00

ATOM 4404 CA LEU B 377 -230.522 -26.794 34.535 1.00 0.00

ATOM 4405 C LEU B 377 -231.575 -26.159 33.674 1.00 0.00

ATOM 4406 O LEU B 377 -232.737 -26.164 34.047 1.00 0.00

ATOM 4407 CB LEU B 377 -229.774 -25.678 35.267 1.00 0.00

ATOM 4408 CG LEU B 377 -228.840 -26.116 36.397 1.00 0.00

ATOM 4409 CDl LEU B 377 -228.030 -24.937 36.913 1.00 0.00

ATOM 4410 CD2 LEU B 377 -229.636 -26.691 37.559 1.00 0.00

ATOM 4411 N MET B 378 -231.157 -25.619 32.513 1.00 0.00

ATOM 4412 CA MET B 378 -232.121 -24.974 31.637 1.00 0.00

ATOM 4413 C MET B 378 -233.165 -25.951 31.171 1.00 0.00

ATOM 4414 O MET B 378 -234.340 -25.624 31.195 1.00 0.00

ATOM 4415 CB MET B 378 -231.423 -24.399 30.404 1.00 0.00 ATOM 4416 CG MET B 378 -230.553 -23.186 30.692 1.00 0.00

ATOM 4417 SD MET B 378 -231.497 -21.785 31.320 1.00 0.00

ATOM 4418 CE MET B 378 -232.447 -21.338 29.869 1.00 0.00

ATOM 4419 N ASN B 379 -232.727 -27.156 30.757 1.00 0.00

ATOM 4420 CA ASN B 379 -233.683 -28.152 30.302 1.00 0.00

ATOM 4421 C ASN B 379 -234.649 -28.493 31.400 1.00 0.00

ATOM 4422 O ASN B 379 -235.845 -28.527 31.164 1.00 0.00

ATOM 4423 CB ASN B 379 -232.961 -29.433 29.877 1.00 0.00

ATOM 4424 CG ASN B 379 -232.221 -29.275 28.564 1.00 0.00

ATOM 4425 ODl ASN B 379 -232.507 -28.366 27.783 1.00 0.00

ATOM 4426 ND2 ASN B 379 -231.265 -30.163 28.314 1.00 0.00

ATOM 4427 N VAL B 380 -234.105 -28.734 32.610 1.00 0.00

ATOM 4428 CA VAL B 380 -234.956 -29.066 33.741 1.00 0.00

ATOM 4429 C VAL B 380 -235.955 -27.970 33.985 1.00 0.00

ATOM 4430 O VAL B 380 -237.126 -28.254 34.181 1.00 0.00

ATOM 4431 CB VAL B 380 -234.134 -29.254 35.029 1.00 0.00

ATOM 4432 CGl VAL B 380 -235.054 -29.401 36.232 1.00 0.00

ATOM 4433 CG2 VAL B 380 -233.267 -30.500 34.932 1.00 0.00

ATOM 4434 N LYS B 381 -235.475 -26.712 33.966 1.00 0.00

ATOM 4435 CA LYS B 381 -236.369 -25.592 34.206 1.00 0.00

ATOM 4436 C LYS B 381 -237.467 -25.553 33.180 1.00 0.00

ATOM 4437 O LYS B 381 -238.608 -25.307 33.535 1.00 0.00

ATOM 4438 CB LYS B 381 -235.602 -24.269 34.136 1.00 0.00

ATOM 4439 CG LYS B 381 -236.454 -23.042 34.421 1.00 0.00

ATOM 4440 CD LYS B 381 -235.614 -21.775 34.413 1.00 0.00

ATOM 4441 CE LYS B 381 -236.470 -20.545 34.668 1.00 0.00

ATOM 4442 NZ LYS B 381 -235.664 -19.294 34.648 1.00 0.00

ATOM 4443 N LEU B 382 -237.109 -25.810 31.905 1.00 0.00

ATOM 4444 CA LEU B 382 -238.118 -25.812 30.859 1.00 0.00

ATOM 4445 C LEU B 382 -239.208 -26.795 31.184 1.00 0.00

ATOM 4446 O LEU B 382 -240.375 -26.450 31.096 1.00 0.00

ATOM 4447 CB LEU B 382 -237.498 -26.202 29.516 1.00 0.00

ATOM 4448 CG LEU B 382 -238.450 -26.262 28.321 1.00 0.00

ATOM 4449 CDl LEU B 382 -239.068 -24.896 28.057 1.00 0.00

ATOM 4450 CD2 LEU B 382 -237.712 -26.700 27.066 1.00 0.00

ATOM 4451 N ALA B 383 -238.808 -28.021 31.573 1.00 0.00

ATOM 4452 CA ALA B 383 -239.798 -29.030 31.907 1.00 0.00

ATOM 4453 C ALA B 383 -240.644 -28.588 33.068 1.00 0.00

ATOM 4454 O ALA B 383 -241.858 -28.700 32.997 1.00 0.00

ATOM 4455 CB ALA B 383 -239.117 -30.337 32.284 1.00 0.00

ATOM 4456 N LEU B 384 -239.991 -28.079 34.132 1.00 0.00

ATOM 4457 CA LEU B 384 -240.738 -27.647 35.301 1.00 0.00

ATOM 4458 C LEU B 384 -241.772 -26.625 34.924 1.00 0.00

ATOM 4459 O LEU B 384 -242.905 -26.728 35.364 1.00 0.00

ATOM 4460 CB LEU B 384 -239.800 -27.023 36.336 1.00 0.00

ATOM 4461 CG LEU B 384 -238.834 -27.979 37.039 1.00 0.00

ATOM 4462 CDl LEU B 384 -237.846 -27.207 37.900 1.00 0.00

ATOM 4463 CD2 LEU B 384 -239.592 -28.945 37.937 1.00 0.00

ATOM 4464 N ASP B 385 -241.371 -25.647 34.091 1.00 0.00

ATOM 4465 CA ASP B 385 -242.314 -24.618 33.689 1.00 0.00

ATOM 4466 C ASP B 385 -243.467 -25.210 32.928 1.00 0.00

ATOM 4467 O ASP B 385 -244.591 -24.771 33.117 1.00 0.00

ATOM 4468 CB ASP B 385 -241.630 -23.586 32.790 1.00 0.00

ATOM 4469 CG ASP B 385 -240.685 -22.681 33.556 1.00 0.00

ATOM 4470 ODl ASP B 385 -240.733 -22.693 34.804 1.00 0.00

ATOM 4471 OD2 ASP B 385 -239.896 -21.962 32.909 1.00 0.00

ATOM 4472 N ILE B 386 -243.186 -26.220 32.081 1.00 0.00

ATOM 4473 CA ILE B 386 -244.266 -26.862 31.350 1.00 0.00

ATOM 4474 C ILE B 386 -245.232 -27.493 32.317 1.00 0.00

ATOM 4475 O ILE B 386 -246.429 -27.294 32.186 1.00 0.00

ATOM 4476 CB ILE B 386 -243.737 -27.960 30.410 1.00 0.00

ATOM 4477 CGl ILE B 386 -242.915 -27.342 29.277 1.00 0.00

ATOM 4478 CG2 ILE B 386 -244.892 -28.739 29.798 1.00 0.00

ATOM 4479 CDl ILE B 386 -242.136 -28.355 28.466 1.00 0.00

ATOM 4480 N GLU B 387 -244.693 -28.246 33.297 1.00 0.00

ATOM 4481 CA GLU B 387 -245.557 -28.889 34.272 1.00 0.00

ATOM 4482 C GLU B 387 -246.356 -27.871 35.035 1.00 0.00

ATOM 4483 O GLU B 387 -247.532 -28.090 35.272 1.00 0.00 ATOM 4484 CB GLU B 387 -244.727 -29.694 35.275 1.00 0.00

ATOM 4485 CG GLU B 387 -244.092 -30.945 34.692 1.00 0.00

ATOM 4486 CD GLU B 387 -243.180 -31.649 35.677 1.00 0.00

ATOM 4487 OEl GLU B 387 -242.986 -31.118 36.790 1.00 0.00

ATOM 4488 OE2 GLU B 387 -242.659 -32.732 35.336 1.00 0.00

ATOM 4489 N ILE B 388 -245.704 -26.750 35.406 1.00 0.00

ATOM 4490 CA ILE B 388 -246.407 -25.713 36.145 1.00 0.00

ATOM 4491 C ILE B 388 -247.563 -25.195 35.339 1.00 0.00

ATOM 4492 O ILE B 388 -248.658 -25.085 35.866 1.00 0.00

ATOM 4493 CB ILE B 388 -245.481 -24.526 36.470 1.00 0.00

ATOM 4494 CGl ILE B 388 -244.402 -24.949 37.469 1.00 0.00

ATOM 4495 CG2 ILE B 388 -246.278 -23.381 37.076 1.00 0.00

ATOM 4496 CDl ILE B 388 -243.294 -23.932 37.638 1.00 0.00

ATOM 4497 N ALA B 389 -247.305 -24.886 34.052 1.00 0.00

ATOM 4498 CA ALA B 389 -248.368 -24.376 33.202 1.00 0.00

ATOM 4499 C ALA B 389 -249.537 -25.320 33.192 1.00 0.00

ATOM 4500 O ALA B 389 -250.670 -24.880 33.297 1.00 0.00

ATOM 4501 CB ALA B 389 -247.872 -24.212 31.773 1.00 0.00

ATOM 4502 N THR B 390 -249.242 -26.631 33.081 1.00 0.00

ATOM 4503 CA THR B 390 -250.311 -27.613 33.078 1.00 0.00

ATOM 4504 C THR B 390 -251.084 -27.558 34.366 1.00 0.00

ATOM 4505 O THR B 390 -252.303 -27.510 34.332 1.00 0.00

ATOM 4506 CB THR B 390 -249.763 -29.044 32.917 1.00 0.00

ATOM 4507 OGl THR B 390 -249.083 -29.159 31.660 1.00 0.00

ATOM 4508 CG2 THR B 390 -250.897 -30.057 32.958 1.00 0.00

ATOM 4509 N TYR B 391 -250.358 -27.559 35.502 1.00 0.00

ATOM 4510 CA TYR B 391 -251.030 -27.528 36.791 1.00 0.00

ATOM 4511 C TYR B 391 -251.941 -26.338 36.901 1.00 0.00

ATOM 4512 O TYR B 391 -253.057 -26.483 37.373 1.00 0.00

ATOM 4513 CB TYR B 391 -250.009 -27.450 37.927 1.00 0.00

ATOM 4514 CG TYR B 391 -249.178 -28.703 38.092 1.00 0.00

ATOM 4515 CDl TYR B 391 -249.564 -29.894 37.493 1.00 0.00

ATOM 4516 CD2 TYR B 391 -248.012 -28.689 38.847 1.00 0.00

ATOM 4517 CEl TYR B 391 -248.812 -31.045 37.638 1.00 0.00

ATOM 4518 CE2 TYR B 391 -247.248 -29.829 39.003 1.00 0.00

ATOM 4519 CZ TYR B 391 -247.658 -31.012 38.391 1.00 0.00

ATOM 4520 OH TYR B 391 -246.906 -32.157 38.537 1.00 0.00

ATOM 4521 N ARG B 392 -251.455 -25.164 36.453 1.00 0.00

ATOM 4522 CA ARG B 392 -252.274 -23.966 36.536 1.00 0.00

ATOM 4523 C ARG B 392 -253.560 -24.136 35.780 1.00 0.00

ATOM 4524 O ARG B 392 -254.611 -23.811 36.308 1.00 0.00

ATOM 4525 CB ARG B 392 -251.531 -22.766 35.945 1.00 0.00

ATOM 4526 CG ARG B 392 -250.360 -22.285 36.788 1.00 0.00

ATOM 4527 CD ARG B 392 -249.640 -21.124 36.121 1.00 0.00

ATOM 4528 NE ARG B 392 -248.483 -20.682 36.896 1.00 0.00

ATOM 4529 CZ ARG B 392 -247.649 -19.721 36.509 1.00 0.00

ATOM 4530 NHl ARG B 392 -246.623 -19.385 37.278 1.00 0.00

ATOM 4531 NH2 ARG B 392 -247.844 -19.099 35.354 1.00 0.00

ATOM 4532 N LYS B 393 -253.469 -24.661 34.541 1.00 0.00

ATOM 4533 CA LYS B 393 -254.677 -24.868 33.760 1.00 0.00

ATOM 4534 C LYS B 393 -255.630 -25.768 34.496 1.00 0.00

ATOM 4535 O LYS B 393 -256.802 -25.443 34.602 1.00 0.00

ATOM 4536 CB LYS B 393 -254.341 -25.515 32.414 1.00 0.00

ATOM 4537 CG LYS B 393 -255.545 -25.732 31.512 1.00 0.00

ATOM 4538 CD LYS B 393 -255.131 -26.311 30.169 1.00 0.00

ATOM 4539 CE LYS B 393 -256.340 -26.573 29.285 1.00 0.00

ATOM 4540 NZ LYS B 393 -255.951 -27.163 27.975 1.00 0.00

ATOM 4541 N LEU B 394 -255.105 -26.898 35.012 1.00 0.00

ATOM 4542 CA LEU B 394 -255.957 -27.832 35.730 1.00 0.00

ATOM 4543 C LEU B 394 -256.609 -27.166 36.906 1.00 0.00

ATOM 4544 O LEU B 394 -257.805 -27.317 37.097 1.00 0.00

ATOM 4545 CB LEU B 394 -255.138 -29.017 36.245 1.00 0.00

ATOM 4546 CG LEU B 394 -254.619 -29.993 35.188 1.00 0.00

ATOM 4547 CDl LEU B 394 -253.669 -31.005 35.811 1.00 0.00

ATOM 4548 CD2 LEU B 394 -255.770 -30.753 34.547 1.00 0.00

ATOM 4549 N LEU B 395 -255.803 -26.424 37.690 1.00 0.00

ATOM 4550 CA LEU B 395 -256.342 -25.774 38.870 1.00 0.00

ATOM 4551 C LEU B 395 -257.448 -24.823 38.506 1.00 0.00 ATOM 4552 O LEU B 395 -258.447 -24.781 39.207 1.00 0.00

ATOM 4553 CB LEU B 395 -255.249 -24.980 39.590 1.00 0.00

ATOM 4554 CG LEU B 395 -255.671 -24.252 40.868 1.00 0.00

ATOM 4555 CDl LEU B 395 -256.165 -25.241 41.912 1.00 0.00

ATOM 4556 CD2 LEU B 395 -254.501 -23.481 41.459 1.00 0.00

ATOM 4557 N GLU B 396 -257.269 -24.075 37.401 1.00 0.00

ATOM 4558 CA GLU B 396 -258.305 -23.141 36.992 1.00 0.00

ATOM 4559 C GLU B 396 -259.585 -23.871 36.703 1.00 0.00

ATOM 4560 O GLU B 396 -260.625 -23.483 37.212 1.00 0.00

ATOM 4561 CB GLU B 396 -257.880 -22.390 35.729 1.00 0.00

ATOM 4562 CG GLU B 396 -258.888 -21.354 35.253 1.00 0.00

ATOM 4563 CD GLU B 396 -258.417 -20.608 34.021 1.00 0.00

ATOM 4564 OEl GLU B 396 -257.298 -20.890 33.546 1.00 0.00

ATOM 4565 OE2 GLU B 396 -259.169 -19.740 33.530 1.00 0.00

ATOM 4566 N GLY B 397 -259.499 -24.938 35.884 1.00 0.00

ATOM 4567 CA GLY B 397 -260.704 -25.670 35.535 1.00 0.00

ATOM 4568 C GLY B 397 -261.369 -26.234 36.759 1.00 0.00

ATOM 4569 O GLY B 397 -262.565 -26.054 36.924 1.00 0.00

ATOM 4570 N GLU B 398 -260.582 -26.913 37.617 1.00 0.00

ATOM 4571 CA GLU B 398 -261.172 -27.496 38.810 1.00 0.00

ATOM 4572 C GLU B 398 -261.721 -26.414 39.695 1.00 0.00

ATOM 4573 O GLU B 398 -262.919 -26.363 39.923 1.00 0.00

ATOM 4574 CB GLU B 398 -260.124 -28.286 39.595 1.00 0.00

ATOM 4575 CG GLU B 398 -259.640 -29.545 38.894 1.00 0.00

ATOM 4576 CD GLU B 398 -260.758 -30.537 38.642 1.00 0.00

ATOM 4577 OEl GLU B 398 -261.473 -30.884 39.605 1.00 0.00

ATOM 4578 OE2 GLU B 398 -260.919 -30.968 37.481 1.00 0.00

TER 4579 GLU B 398

MASTER 0 0 0 0 0 0 0 0 4571 8 0 46

END

Tab. 2:

HEADER KERATINBACKBONE

COMPND KERATINBACKBONE

REMARK GENERATED BY SYBYL (TRIPOS, INC. ) 10-MAR-08

(Legend analogous tc ) legend of table 1 I. The names of the amino acids are of minor irelev only the backbone coordinates are provided)

SEQRES 1 A 43 ASP GLY LEU LEU VAL GLY SER GLU LYS VAL THR MET GLN

SEQRES 2 A 43 ASN LEU ASN ASP ARG LEU ALA SER TYR LEU ASP LYS VAL

SEQRES 3 A 43 ARG ALA LEU GLU GLU ALA ASN ALA ASP LEU GLU VAL LYS

SEQRES 4 A 43 ILE ARG ASP TRP

SEQRES 1 A 101 TYR SER PRO TYR PHE LYS THR ILE GLU ASP LEU ARG ASN

SEQRES 2 A 101 LYS ILE LEU THR ALA THR VAL ASP ASN ALA ASN VAL LEU

SEQRES 3 A 101 LEU GLN ILE ASP ASN ALA ARG LEU ALA ALA ASP ASP PHE

SEQRES 4 A 101 ARG THR LYS TYR GLU THR GLU LEU ASN LEU ARG MET SER

SEQRES 5 A 101 VAL GLU ALA ASP ILE ASN GLY LEU ARG ARG VAL LEU ASP

SEQRES 6 A 101 GLU LEU THR LEU ALA ARG ALA ASP LEU GLU MET GLN ILE

SEQRES 7 A 101 GLU SER LEU LYS GLU GLU LEU ALA TYR LEU LYS LYS ASN

SEQRES 8 A 101 HIS GLU GLU GLU MET ASN ALA LEU ARG GLY

SEQRES 1 A 19 ASP LEU SER ARG ILE LEU ASN GLU MET ARG ASP GLN TYR

SEQRES 2 A 19 GLU LYS MET ALA GLU LYS

SEQRES 1 A 117 PHE PHE THR LYS THR GLU GLU LEU ASN ARG GLU VAL ALA

SEQRES 9 A 117 THR ASN SER GLU LEU VAL GLN SER GLY LYS SER GLU ILE

SEQRES 3 A 117 SER GLU LEU ARG ARG THR MET GLN ASN LEU GLU ILE GLU

SEQRES 4 A 117 LEU GLN SER GLN LEU SER MET LYS ALA SER LEU GLU ASN

SEQRES 5 A 117 SER LEU GLU GLU THR LYS GLY ARG TYR CYS MET GLN LEU

SEQRES 6 A 117 ALA GLN ILE GLN GLU MET ILE GLY SER VAL GLU GLU GLN

SEQRES 7 A 117 LEU ALA GLN LEU ARG CYS GLU MET GLU GLN GLN ASN GLN

SEQRES 8 A 117 GLU TYR LYS ILE LEU LEU ASP VAL LYS THR ARG LEU GLU

SEQRES 9 A 117 GLN GLU ILE ALA THR TYR ARG ARG LEU LEU GLU GLY GLU

SEQRES 1 B 43 ILE GLN ARG VAL ARG THR GLU GLU ARG GLU GLN ILE LYS

SEQRES 9 B 43 THR LEU ASN ASN LYS PHE ALA SER PHE ILE ASP LYS VAL

SEQRES 3 B 43 ARG PHE LEU GLU GLN GLN ASN LYS VAL LEU ASP THR LYS

SEQRES 4 B 43 TRP THR LEU LEU

SEQRES 1 B 101 GLU PRO LEU PHE GLU GLN TYR ILE ASN ASN LEU ARG ARG

SEQRES 9 B 101 GLN LEU ASP SER ILE VAL GLY GLU ARG GLY ARG LEU ASP

SEQRES 3 B 101 SER GLU LEU ARG ASN MET GLN ASP LEU VAL GLU ASP PHE

SEQRES 4 B 101 LYS ASN LYS TYR GLU ASP GLU ILE ASN LYS ARG THR THR

SEQRES 5 B 101 ALA GLU ASN GLU PHE VAL MET LEU LYS LYS ASP VAL ASP

SEQRES 6 B 101 ALA ALA TYR MET ASN LYS VAL GLU LEU GLU ALA LYS VAL

SEQRES 7 B 101 ASP ALA LEU MET ASP GLU ILE ASN PHE MET LYS MET PHE

SEQRES 8 B 101 PHE ASP ALA GLU LEU SER GLN MET GLN THR

SEQRES 1 B 19 ASP LEU ASP SER ILE ILE ALA GLU VAL LYS ALA GLN TYR

SEQRES 2 B 19 GLU GLU ILE ALA ASN ARG

SEQRES 1 B 117 TYR GLN THR LYS TYR GLU GLU LEU GLN GLN THR ALA GLY

SEQRES 2 B 117 ARG HIS GLY ASP ASP LEU ARG ASN THR LYS HIS GLU ILE

SEQRES 3 B 117 SER GLU MET ASN ARG MET ILE GLN ARG LEU ARG ALA GLU

SEQRES 4 B 117 ILE ASP ASN VAL LYS LYS GLN CYS ALA ASN LEU GLN ASN

SEQRES 5 B 117 ALA ILE ALA ASP ALA GLU GLN ARG GLY GLU LEU ALA LEU

SEQRES 6 B 117 LYS ASP ALA ARG ASN LYS LEU ALA GLU LEU GLU GLU ALA

SEQRES 7 B 117 LEU GLN LYS ALA LYS GLN ASP MET ALA ARG LEU LEU ARG

SEQRES 8 B 117 GLU TYR GLN GLU LEU MET ASN THR LYS LEU ALA LEU ASP

SEQRES 9 B 117 VAL GLU ILE ALA THR TYR ARG LYS LEU LEU GLU GLY GLU

ATOM 1 N ASP A 1 181. 483 42. 993 -33 .125 1. 00 0.00

ATOM 2 CA ASP A 1 180. 788 42. 153 -32 .160 1. 00 0.00

ATOM 3 C ASP A 1 179. 956 43. 012 -31 .246 1. 00 0.00

ATOM 4 O ASP A 1 178. 904 42. 580 -30 .804 1. 00 0.00

ATOM 5 N GLY A 2 180. 442 44. 241 -30 .977 1. 00 0.00

ATOM 6 CA GLY A 2 179. 704 45. 149 -30 .115 1. 00 0.00

ATOM 7 C GLY A 9 178. 381 45. 506 -30 .732 1. 00 0.00

ATOM 8 O GLY A 2 177. 362 45. 365 -30 .077 1. 00 0.00

ATOM 9 N LEU A 3 178. 404 45. 960 -32 .003 1. 00 0.00

ATOM 10 CA LEU A 3 177. 156 46. 312 -32 .662 1. 00 0.00

ATOM 11 C LEU A 3 176. 182 45. 168 -32 .610 1. 00 0.00

ATOM 12 O LEU A 3 175. 022 45. 387 -32 .301 1. 00 0.00

ATOM 13 N LEU A 4 176. 665 43. 941 -32 .890 1. 00 0.00

ATOM 14 CA LEU A 4 175. 785 42. 788 -32 .813 1. 00 0.00

ATOM 15 C LEU A 4 175. 189 42. 660 -31 .437 1. 00 0.00 ATOM 16 O LEU A 4 173.979 42.561 -31.313 1.00 0.00

ATOM 17 N VAL A 5 176.063 42.671 -30.410 1.00 0.00

ATOM 18 CA VAL A 5 175.604 42.522 -29.037 1.00 0.00

ATOM 19 C VAL A 5 174.515 43.504 -28.694 1.00 0.00

ATOM 20 O VAL A 5 173.519 43.113 -28.108 1.00 0.00

ATOM 21 N GLY A 6 174.714 44.784 -29.069 1.00 0.00

ATOM 99 CA GLY A 6 173.713 45.787 -28.748 1.00 0.00

ATOM 23 C GLY A 6 172.412 45.502 -29.448 1.00 0.00

ATOM 24 O GLY A 6 171.363 45.684 -28.850 1.00 0.00

ATOM 25 N SER A 7 172.484 45.043 -30.713 1.00 0.00

ATOM 26 CA SER A 7 171.261 44.740 -31.440 1.00 0.00

ATOM 27 C SER A 7 170.467 43.678 -30.731 1.00 0.00

ATOM 28 O SER A 7 169.269 43.842 -30.553 1.00 0.00

ATOM 29 N GLU A 8 171.144 42.587 -30.323 1.00 0.00

ATOM 30 CA GLU A 8 170.432 41.499 -29.670 1.00 0.00

ATOM 31 C GLU A 8 169.898 41.912 -28.327 1.00 0.00

ATOM 32 O GLU A 8 168.806 41.493 -27.979 1.00 0.00

ATOM 33 N LYS A 9 170.659 42.728 -27.570 1.00 0.00

ATOM 34 CA LYS A 9 170.180 43.122 -26.256 1.00 0.00

ATOM 35 C LYS A 9 168.914 43.926 -26.373 1.00 0.00

ATOM 36 O LYS A 9 167.981 43.676 -25.627 1.00 0.00

ATOM 37 N VAL A 10 168.878 44.883 -27.322 1.00 0.00

ATOM 38 CA VAL A 10 167.667 45.667 -27.497 1.00 0.00

ATOM 39 C VAL A 10 166.517 44.778 -27.877 1.00 0.00

ATOM 40 O VAL A 10 165.441 44.920 -27.319 1.00 0.00

ATOM 41 N THR A 11 166.761 43.848 -28.822 1.00 0.00

ATOM 42 CA THR A 11 165.713 42.915 -29.205 1.00 0.00

ATOM 43 C THR A 11 165.224 42.161 -27.999 1.00 0.00

ATOM 44 O THR A 11 164.028 41.986 -27.843 1.00 0.00

ATOM 45 N MET A 12 166.168 41.726 -27.138 1.00 0.00

ATOM 46 CA MET A 12 165.775 40.978 -25.956 1.00 0.00

ATOM 47 C MET A 12 164.922 41.806 -25.039 1.00 0.00

ATOM 48 O MET A 12 163.928 41.302 -24.539 1.00 0.00

ATOM 49 N GLN A 13 165.307 43.081 -24.825 1.00 0.00

ATOM 50 CA GLN A 13 164.510 43.944 -23.968 1.00 0.00

ATOM 51 C GLN A 13 163.089 43.990 -24.459 1.00 0.00

ATOM 52 O GLN A 13 162.175 43.827 -23.667 1.00 0.00

ATOM 53 N ASN A 14 162.918 44.199 -25.780 1.00 0.00

ATOM 54 CA ASN A 14 161.574 44.253 -26.333 1.00 0.00

ATOM 55 C ASN A 14 160.833 42.964 -26.099 1.00 0.00

ATOM 56 O ASN A 14 159.657 43.009 -25.780 1.00 0.00

ATOM 57 N LEU A 15 161.523 41.814 -26.247 1.00 0.00

ATOM 58 CA LEU A 15 160.847 40.547 -26.020 1.00 0.00

ATOM 59 C LEU A 15 160.408 40.433 -24.586 1.00 0.00

ATOM 60 O LEU A 15 159.280 40.045 -24.335 1.00 0.00

ATOM 61 N ASN A 16 161.307 40.786 -23.644 1.00 0.00

ATOM 62 CA ASN A 16 160.962 40.677 -22.236 1.00 0.00

ATOM 63 C ASN A 16 159.769 41.518 -21.883 1.00 0.00

ATOM 64 O ASN A 16 158.910 41.054 -21.150 1.00 0.00

ATOM 65 N ASP A 17 159.709 42.755 -22.418 1.00 0.00

ATOM 66 CA ASP A 17 158.561 43.603 -22.133 1.00 0.00

ATOM 67 C ASP A 17 157.313 42.967 -22.670 1.00 0.00

ATOM 68 O ASP A 17 156.318 42.910 -21.965 1.00 0.00

ATOM 69 N ARG A 18 157.385 42.478 -23.926 1.00 0.00

ATOM 70 CA ARG A 18 156.240 41.794 -24.503 1.00 0.00

ATOM 71 C ARG A 18 155.799 40.691 -23.580 1.00 0.00

ATOM 72 O ARG A 18 154.622 40.587 -23.275 1.00 0.00

ATOM 73 N LEU A 19 156.780 39.883 -23.136 1.00 0.00

ATOM 74 CA LEU A 19 156.490 38.752 -22.270 1.00 0.00

ATOM 75 C LEU A 19 155.730 39.148 -21.033 1.00 0.00

ATOM 76 O LEU A 19 154.663 38.606 -20.794 1.00 0.00

ATOM 77 N ALA A 20 156.294 40.089 -20.248 1.00 0.00

ATOM 78 CA ALA A 20 155.635 40.501 -19.019 1.00 0.00

ATOM 79 C ALA A 20 154.222 40.926 -19.309 1.00 0.00

ATOM 80 O ALA A 20 153.307 40.490 -18.629 1.00 0.00

ATOM 81 N SER A 21 154.067 41.772 -20.346 1.00 0.00

ATOM 82 CA SER A 21 152.743 42.241 -20.711 1.00 0.00

ATOM 83 C SER A 21 151.799 41.102 -20.986 1.00 0.00 ATOM 84 O SER A 21 150.752 41.040 -20.362 1.00 0.00

ATOM 85 N TYR A 22 152.175 40.202 -21.920 1.00 0.00

ATOM 86 CA TYR A 22 151.297 39.089 -22.256 1.00 0.00

ATOM 87 C TYR A 22 150.924 38.287 -21.040 1.00 0.00

ATOM 88 O TYR A 22 149.792 37.837 -20.945 1.00 0.00

ATOM 89 N LEU A 23 151.882 38.114 -20.108 1.00 0.00

ATOM 90 CA LEU A 23 151.610 37.328 -18.915 1.00 0.00

ATOM 91 C LEU A 23 150.571 37.998 -18.060 1.00 0.00

ATOM 92 O LEU A 23 149.669 37.336 -17.575 1.00 0.00

ATOM 93 N ASP A 24 150.711 39.327 -17.888 1.00 0.00

ATOM 94 CA ASP A 24 149.742 40.056 -17.089 1.00 0.00

ATOM 95 C ASP A 24 148.387 39.976 -17.734 1.00 0.00

ATOM 96 O ASP A 24 147.415 39.675 -17.059 1.00 0.00

ATOM 97 N LYS A 25 148.338 40.238 -19.057 1.00 0.00

ATOM 98 CA LYS A 25 147.075 40.168 -19.775 1.00 0.00

ATOM 99 C LYS A 25 146.427 38.824 -19.588 1.00 0.00

ATOM 100 O LYS A 25 145.236 38.761 -19.331 1.00 0.00

ATOM 101 N VAL A 26 147.230 37.751 -19.719 1.00 0.00

ATOM 102 CA VAL A 26 146.679 36.412 -19.591 1.00 0.00

ATOM 103 C VAL A 26 146.153 36.166 -18.205 1.00 0.00

ATOM 104 O VAL A 26 145.137 35.502 -18.070 1.00 0.00

ATOM 105 N ARG A 27 146.836 36.708 -17.175 1.00 0.00

ATOM 106 CA ARG A 27 146.341 36.519 -15.822 1.00 0.00

ATOM 107 C ARG A 27 144.964 37.111 -15.711 1.00 0.00

ATOM 108 O ARG A 27 144.062 36.451 -15.220 1.00 0.00

ATOM 109 N ALA A 28 144.815 38.362 -16.189 1.00 0.00

ATOM 110 CA ALA A 28 143.513 39.003 -16.134 1.00 0.00

ATOM 111 C ALA A 28 142.474 38.188 -16.857 1.00 0.00

ATOM 112 O ALA A 28 141.420 37.941 -16.293 1.00 0.00

ATOM 113 N LEU A 29 142.771 37.769 -18.104 1.00 0.00

ATOM 114 CA LEU A 29 141.774 37.043 -18.874 1.00 0.00

ATOM 115 C LEU A 29 141.381 35.739 -18.241 1.00 0.00

ATOM 116 O LEU A 29 140.204 35.418 -18.253 1.00 0.00

ATOM 117 N GLU A 30 142.349 34.981 -17.688 1.00 0.00

ATOM 118 CA GLU A 30 141.993 33.698 -17.099 1.00 0.00

ATOM 119 C GLU A 30 141.096 33.891 -15.911 1.00 0.00

ATOM 120 O GLU A 30 140.204 33.085 -15.694 1.00 0.00

ATOM 121 N GLU A 31 141.330 34.976 -15.147 1.00 0.00

ATOM 1 99 CA GLU A 31 140.453 35.253 -14.023 1.00 0.00

ATOM 123 C GLU A 31 139.077 35.574 -14.537 1.00 0.00

ATOM 124 O GLU A 31 138.103 35.037 -14.036 1.00 0.00

ATOM 125 N ALA A 32 139.022 36.447 -15.563 1.00 0.00

ATOM 126 CA ALA A 32 137.743 36.811 -16.151 1.00 0.00

ATOM 127 C ALA A 32 137.028 35.604 -16.693 1.00 0.00

ATOM 128 O ALA A 32 135.819 35.513 -16.556 1.00 0.00

ATOM 129 N ASN A 33 137.785 34.672 -17.308 1.00 0.00

ATOM 130 CA ASN A 33 137.160 33.479 -17.859 1.00 0.00

ATOM 131 C ASN A 33 136.566 32.654 -16.757 1.00 0.00

ATOM 132 O ASN A 33 135.423 32.239 -16.872 1.00 0.00

ATOM 133 N ALA A 34 137.353 32.426 -15.688 1.00 0.00

ATOM 134 CA ALA A 34 136.845 31.643 -14.576 1.00 0.00

ATOM 135 C ALA A 34 135.547 32.215 -14.077 1.00 0.00

ATOM 136 O ALA A 34 134.622 31.462 -13.820 1.00 0.00

ATOM 137 N ASP A 35 135.481 33.557 -13.960 1.00 0.00

ATOM 138 CA ASP A 35 134.250 34.179 -13.498 1.00 0.00

ATOM 139 C ASP A 35 133.114 33.896 -14.442 1.00 0.00

ATOM 140 O ASP A 35 132.046 33.519 -13.990 1.00 0.00

ATOM 141 N LEU A 36 133.354 34.081 -15.757 1.00 0.00

ATOM 142 CA LEU A 36 132.295 33.841 -16.723 1.00 0.00

ATOM 143 C LEU A 36 131.776 32.436 -16.609 1.00 0.00

ATOM 144 O LEU A 36 130.573 32.234 -16.663 1.00 0.00

ATOM 145 N GLU A 37 132.703 31.470 -16.441 1.00 0.00

ATOM 146 CA GLU A 37 132.294 30.080 -16.330 1.00 0.00

ATOM 147 C GLU A 37 131.364 29.890 -15.165 1.00 0.00

ATOM 148 O GLU A 37 130.308 29.303 -15.335 1.00 0.00

ATOM 149 N VAL A 38 131.759 30.405 -13.982 1.00 0.00

ATOM 150 CA VAL A 38 130.893 30.283 -12.820 1.00 0.00

ATOM 151 C VAL A 38 129.532 30.849 -13.123 1.00 0.00 ATOM 152 O VAL A 38 128.543 30.169 -12.898 1.00 0.00

ATOM 153 N LYS A 39 129.495 32.089 -13.649 1.00 0.00

ATOM 154 CA LYS A 39 128.218 32.719 -13.951 1.00 0.00

ATOM 155 C LYS A 39 127.359 31.876 -14.855 1.00 0.00

ATOM 156 O LYS A 39 126.171 31.757 -14.596 1.00 0.00

ATOM 157 N ILE A 40 127.955 31.288 -15.911 1.00 0.00

ATOM 158 CA ILE A 40 127.157 30.482 -16.823 1.00 0.00

ATOM 159 C ILE A 40 126.627 29.258 -16.130 1.00 0.00

ATOM 160 O ILE A 40 125.516 28.845 -16.419 1.00 0.00

ATOM 161 N ARG A 41 127.418 28.686 -15.201 1.00 0.00

ATOM 162 CA ARG A 41 126.934 27.526 -14.470 1.00 0.00

ATOM 163 C ARG A 41 125.749 27.912 -13.630 1.00 0.00

ATOM 164 O ARG A 41 124.720 27.261 -13.706 1.00 0.00

ATOM 165 N ASP A 42 125.913 28.986 -12.831 1.00 0.00

ATOM 166 CA ASP A 42 124.832 29.409 -11.959 1.00 0.00

ATOM 167 C ASP A 42 123.585 29.706 -12.741 1.00 0.00

ATOM 168 O ASP A 42 122.556 29.113 -12.466 1.00 0.00

ATOM 169 N TRP A 43 123.692 30.627 -13.720 1.00 0.00

ATOM 170 CA TRP A 43 122.517 30.997 -14.490 1.00 0.00

ATOM 171 C TRP A 43 121.891 29.794 -15.137 1.00 0.00

ATOM 172 O TRP A 43 120.707 29.563 -14.955 1.00 0.00

TER 173 TRP A 43

ATOM 174 N TYR A 1 104.979 31.505 -15.263 1.00 0.00

ATOM 175 CA TYR A 1 104.621 30.167 -14.792 1.00 0.00

ATOM 176 C TYR A 1 103.828 30.282 -13.468 1.00 0.00

ATOM 177 O TYR A 1 102.704 29.788 -13.371 1.00 0.00

ATOM 178 N SER A 9 104.398 30.941 -12.465 1.00 0.00

ATOM 179 CA SER A 9 103.721 31.113 -11.177 1.00 0.00

ATOM 180 C SER A 2 102.334 31.749 -11.316 1.00 0.00

ATOM 181 O SER A 2 101.362 31.317 -10.695 1.00 0.00

ATOM 182 N PRO A 3 102.246 32.795 -12.126 1.00 0.00

ATOM 183 CA PRO A 3 100.971 33.458 -12.297 1.00 0.00

ATOM 184 C PRO A 3 99.943 32.603 -13.002 1.00 0.00

ATOM 185 O PRO A 3 98.750 32.731 -12.734 1.00 0.00

ATOM 186 N TYR A 4 100.384 31.742 -13.912 1.00 0.00

ATOM 187 CA TYR A 4 99.429 30.907 -14.612 1.00 0.00

ATOM 188 C TYR A 4 98.893 29.876 -13.660 1.00 0.00

ATOM 189 O TYR A 4 97.706 29.581 -13.656 1.00 0.00

ATOM 190 N PHE A 5 99.757 29.331 -12.829 1.00 0.00

ATOM 191 CA PHE A 5 99.272 28.369 -11.865 1.00 0.00

ATOM 192 C PHE A 5 98.275 29.085 -10.956 1.00 0.00

ATOM 193 O PHE A 5 97.254 28.513 -10.558 1.00 0.00

ATOM 194 N LYS A 6 98.581 30.335 -10.630 1.00 0.00

ATOM 195 CA LYS A 6 97.731 31.106 -9.740 1.00 0.00

ATOM 196 C LYS A 6 96.350 31.248 -10.326 1.00 0.00

ATOM 197 O LYS A 6 95.341 31.059 -9.649 1.00 0.00

ATOM 198 N THR A 7 96.343 31.555 -11.611 1.00 0.00

ATOM 199 CA THR A 7 95.131 31.767 -12.375 1.00 0.00

ATOM 200 C THR A 7 94.346 30.460 -12.498 1.00 0.00

ATOM 201 O THR A 7 93.111 30.446 -12.512 1.00 0.00

ATOM 202 N ILE A 8 95.098 29.286 -12.664 1.00 0.00

ATOM 203 CA ILE A 8 94.631 27.900 -12.641 1.00 0.00

ATOM 204 C ILE A 8 93.890 27.629 -11.309 1.00 0.00

ATOM 205 O ILE A 8 92.728 27.220 -11.315 1.00 0.00

ATOM 206 N GLU A 9 94.548 27.869 -10.180 1.00 0.00

ATOM 207 CA GLU A 9 93.927 27.654 -8.869 1.00 0.00

ATOM 208 C GLU A 9 92.602 28.407 -8.711 1.00 0.00

ATOM 209 O GLU A 9 91.611 27.870 -8.212 1.00 0.00

ATOM 210 N ASP A 10 92.589 29.665 -9.124 1.00 0.00

ATOM 211 CA ASP A 10 91.376 30.446 -8.993 1.00 0.00

ATOM 212 C ASP A 10 90.253 29.959 -9.879 1.00 0.00

ATOM 213 O ASP A 10 89.084 30.082 -9.516 1.00 0.00

ATOM 214 N LEU A 11 90.586 29.418 -11.048 1.00 0.00

ATOM 215 CA LEU A 11 89.538 28.941 -11.926 1.00 0.00

ATOM 216 C LEU A 11 88.935 27.697 -11.340 1.00 0.00

ATOM 217 O LEU A 11 87.725 27.511 -11.363 1.00 0.00

ATOM 218 N ARG A 12 89.767 26.840 -10.784 1.00 0.00

ATOM 219 CA ARG A 12 89.224 25.654 -10.165 1.00 0.00 ATOM 220 C ARG A 12 88.323 26.100 -9.016 1.00 0.00

ATOM 221 O ARG A 12 87.267 25.511 -8.769 1.00 0.00

ATOM 999 N ASN A 13 88.755 27.141 -8.314 1.00 0.00

ATOM 223 CA ASN A 13 88.006 27.637 -7.171 1.00 0.00

ATOM 224 C ASN A 13 86.628 28.072 -7.596 1.00 0.00

ATOM 225 O ASN A 13 85.625 27.749 -6.963 1.00 0.00

ATOM 226 N LYS A 14 86.611 28.791 -8.706 1.00 0.00

ATOM 227 CA LYS A 14 85.403 29.340 -9.287 1.00 0.00

ATOM 228 C LYS A 14 84.496 28.214 -9.787 1.00 0.00

ATOM 229 O LYS A 14 83.266 28.302 -9.732 1.00 0.00

ATOM 230 N ILE A 15 85.122 27.144 -10.256 1.00 0.00

ATOM 231 CA ILE A 15 84.393 26.001 -10.783 1.00 0.00

ATOM 232 C ILE A 15 83.680 25.265 -9.648 1.00 0.00

ATOM 233 O ILE A 15 82.528 24.831 -9.784 1.00 0.00

ATOM 234 N LEU A 16 84.374 25.148 -8.529 1.00 0.00

ATOM 235 CA LEU A 16 83.847 24.488 -7.349 1.00 0.00

ATOM 236 C LEU A 16 82.698 25.303 -6.736 1.00 0.00

ATOM 237 O LEU A 16 81.738 24.747 -6.214 1.00 0.00

ATOM 238 N THR A 17 82.799 26.624 -6.801 1.00 0.00

ATOM 239 CA THR A 17 81.745 27.468 -6.248 1.00 0.00

ATOM 240 C THR A 17 80.509 27.387 -7.146 1.00 0.00

ATOM 241 O THR A 17 79.372 27.484 -6.676 1.00 0.00

ATOM 242 N ALA A 18 80.734 27.214 -8.444 1.00 0.00

ATOM 243 CA ALA A 18 79.634 27.091 -9.385 1.00 0.00

ATOM 244 C ALA A 18 78.988 25.733 -9.165 1.00 0.00

ATOM 245 O ALA A 18 77.785 25.583 -9.324 1.00 0.00

ATOM 246 N THR A 19 79.802 24.756 -8.782 1.00 0.00

ATOM 247 CA THR A 19 79.323 23.402 -8.512 1.00 0.00

ATOM 248 C THR A 19 78.362 23.434 -7.312 1.00 0.00

ATOM 249 O THR A 19 77.226 22.985 -7.410 1.00 0.00

ATOM 250 N VAL A 20 78.818 23.963 -6.179 1.00 0.00

ATOM 251 CA VAL A 20 77.957 24.046 -5.006 1.00 0.00

ATOM 252 C VAL A 20 76.659 24.742 -5.407 1.00 0.00

ATOM 253 O VAL A 20 75.587 24.262 -5.078 1.00 0.00

ATOM 254 N ASP A 21 IS.121 25.863 -6.120 1.00 0.00

ATOM 255 CA ASP A 21 75.483 26.522 -6.536 1.00 0.00

ATOM 256 C ASP A 21 74.564 25.561 -7.323 1.00 0.00

ATOM 257 O ASP A 21 73.384 25.353 -6.989 1.00 0.00

ATOM 258 N ASN A 99 75.125 24.981 -8.373 1.00 0.00

ATOM 259 CA ASN A 22 74.436 24.028 -9.237 1.00 0.00

ATOM 260 C ASN A 22 73.706 22.926 -8.444 1.00 0.00

ATOM 261 O ASN A 22 72.522 22.642 -8.673 1.00 0.00

ATOM 262 N ALA A 23 74.416 22.319 -7.498 1.00 0.00

ATOM 263 CA ALA A 23 73.837 21.259 -6.687 1.00 0.00

ATOM 264 C ALA A 23 72.681 21.811 -5.850 1.00 0.00

ATOM 265 O ALA A 23 71.656 21.144 -5.697 1.00 0.00

ATOM 266 N ASN A 24 72.831 23.017 -5.314 1.00 0.00

ATOM 267 CA ASN A 24 71.764 23.598 -4.500 1.00 0.00

ATOM 268 C ASN A 24 70.496 23.772 -5.313 1.00 0.00

ATOM 269 O ASN A 24 69.409 23.399 -4.873 1.00 0.00

ATOM 270 N VAL A 25 70.638 24.340 -6.503 1.00 0.00

ATOM 271 CA VAL A 25 69.485 24.548 -7.361 1.00 0.00

ATOM 272 C VAL A 25 68.875 23.257 -7.862 1.00 0.00

ATOM 273 O VAL A 25 67.657 23.167 -7.992 1.00 0.00

ATOM 274 N LEU A 26 69.690 22.252 -8.155 1.00 0.00

ATOM 275 CA LEU A 26 69.096 21.012 -8.631 1.00 0.00

ATOM 276 C LEU A 26 68.298 20.348 -7.525 1.00 0.00

ATOM 277 O LEU A 26 67.207 19.854 -7.782 1.00 0.00

ATOM 278 N LEU A 27 68.809 20.329 -6.294 1.00 0.00

ATOM 279 CA LEU A 27 68.032 19.733 -5.204 1.00 0.00

ATOM 280 C LEU A 27 66.711 20.499 -5.042 1.00 0.00

ATOM 281 O LEU A 27 65.637 19.906 -4.916 1.00 0.00

ATOM 282 N GLN A 28 66.792 21.830 -5.074 1.00 0.00

ATOM 283 CA GLN A 28 65.600 22.655 -4.950 1.00 0.00

ATOM 284 C GLN A 28 64.632 22.273 -6.072 1.00 0.00

ATOM 285 O GLN A 28 63.428 22.129 -5.826 1.00 0.00

ATOM 286 N ILE A 29 65.154 22.089 -7.285 1.00 0.00

ATOM 287 CA ILE A 29 64.278 21.729 -8.403 1.00 0.00 ATOM 288 C ILE A 29 63.636 20.392 -8.182 1.00 0.00

ATOM 289 O ILE A 29 62.439 20.257 -8.408 1.00 0.00

ATOM 290 N ASP A 30 64.408 19.405 -7.732 1.00 0.00

ATOM 291 CA ASP A 30 63.820 18.100 -7.459 1.00 0.00

ATOM 292 C ASP A 30 62.639 18.262 -6.521 1.00 0.00

ATOM 293 O ASP A 30 61.557 17.738 -6.767 1.00 0.00

ATOM 294 N ASN A 31 62.830 19.004 -5.447 1.00 0.00

ATOM 295 CA ASN A 31 61.728 19.171 -4.514 1.00 0.00

ATOM 296 C ASN A 31 60.535 19.859 -5.143 1.00 0.00

ATOM 297 O ASN A 31 59.384 19.516 -4.851 1.00 0.00

ATOM 298 N ALA A 32 60.784 20.814 -6.030 1.00 0.00

ATOM 299 CA ALA A 32 59.647 21.473 -6.646 1.00 0.00

ATOM 300 C ALA A 32 58.948 20.503 -7.563 1.00 0.00

ATOM 301 O ALA A 32 57.726 20.427 -7.542 1.00 0.00

ATOM 302 N ARG A 33 59.698 19.735 -8.347 1.00 0.00

ATOM 303 CA ARG A 33 59.053 18.779 -9.228 1.00 0.00

ATOM 304 C ARG A 33 58.190 17.772 -8.487 1.00 0.00

ATOM 305 O ARG A 33 57.100 17.444 -8.949 1.00 0.00

ATOM 306 N LEU A 34 58.661 17.287 -7.338 1.00 0.00

ATOM 307 CA LEU A 34 57.871 16.340 -6.551 1.00 0.00

ATOM 308 C LEU A 34 56.608 17.012 -6.076 1.00 0.00

ATOM 309 O LEU A 34 55.512 16.463 -6.169 1.00 0.00

ATOM 310 N ALA A 35 56.779 18.209 -5.557 1.00 0.00

ATOM 311 CA ALA A 35 55.653 18.981 -5.106 1.00 0.00

ATOM 312 C ALA A 35 54.622 19.044 -6.233 1.00 0.00

ATOM 313 O ALA A 35 53.460 18.718 -6.066 1.00 0.00

ATOM 314 N ALA A 36 55.096 19.467 -7.390 1.00 0.00

ATOM 315 CA ALA A 36 54.306 19.600 -8.600 1.00 0.00

ATOM 316 C ALA A 36 53.477 18.345 -8.930 1.00 0.00

ATOM 317 O ALA A 36 52.250 18.383 -9.024 1.00 0.00

ATOM 318 N ASP A 37 54.169 17.230 -9.134 1.00 0.00

ATOM 319 CA ASP A 37 53.504 15.979 -9.450 1.00 0.00

ATOM 320 C ASP A 37 52.400 15.705 -8.415 1.00 0.00

ATOM 321 O ASP A 37 51.232 15.466 -8.742 1.00 0.00

ATOM 322 N ASP A 38 52.779 15.770 -7.149 1.00 0.00

ATOM 323 CA ASP A 38 51.856 15.560 -6.055 1.00 0.00

ATOM 324 C ASP A 38 50.611 16.456 -6.180 1.00 0.00

ATOM 325 O ASP A 38 49.499 15.953 -6.269 1.00 0.00

ATOM 326 N PHE A 39 50.804 17.771 -6.192 1.00 0.00

ATOM 327 CA PHE A 39 49.682 18.696 -6.339 1.00 0.00

ATOM 328 C PHE A 39 48.791 18.389 -7.524 1.00 0.00

ATOM 329 O PHE A 39 47.586 18.553 -7.443 1.00 0.00

ATOM 330 N ARG A 40 49.393 17.979 -8.637 1.00 0.00

ATOM 331 CA ARG A 40 48.646 17.636 -9.848 1.00 0.00

ATOM 332 C ARG A 40 47.735 16.447 -9.625 1.00 0.00

ATOM 333 O ARG A 40 46.591 16.411 -10.067 1.00 0.00

ATOM 334 N THR A 41 48.300 15.433 -8.993 1.00 0.00

ATOM 335 CA THR A 41 47.588 14.206 -8.704 1.00 0.00

ATOM 336 C THR A 41 46.415 14.543 -7.778 1.00 0.00

ATOM 337 O THR A 41 45.266 14.182 -8.051 1.00 0.00

ATOM 338 N LYS A 42 46.722 15.259 -6.696 1.00 0.00

ATOM 339 CA LYS A 42 45.737 15.707 -5.703 1.00 0.00

ATOM 340 C LYS A 42 44.610 16.433 -6.395 1.00 0.00

ATOM 341 O LYS A 42 43.444 16.172 -6.127 1.00 0.00

ATOM 342 N TYR A 43 44.978 17.375 -7.254 1.00 0.00

ATOM 343 CA TYR A 43 43.977 18.143 -7.973 1.00 0.00

ATOM 344 C TYR A 43 43.122 17.296 -8.891 1.00 0.00

ATOM 345 O TYR A 43 41.934 17.569 -9.051 1.00 0.00

ATOM 346 N GLU A 44 43.709 16.270 -9.507 1.00 0.00

ATOM 347 CA GLU A 44 42.943 15.400 -10.394 1.00 0.00

ATOM 348 C GLU A 44 41.876 14.728 -9.551 1.00 0.00

ATOM 349 O GLU A 44 40.691 14.733 -9.894 1.00 0.00

ATOM 350 N THR A 45 42.299 14.161 -8.429 1.00 0.00

ATOM 351 CA THR A 45 41.350 13.512 -7.557 1.00 0.00

ATOM 352 C THR A 45 40.259 14.478 -7.115 1.00 0.00

ATOM 353 O THR A 45 39.074 14.165 -7.258 1.00 0.00

ATOM 354 N GLU A 46 40.620 15.665 -6.636 1.00 0.00

ATOM 355 CA GLU A 46 39.569 16.572 -6.193 1.00 0.00 ATOM 356 C GLU A 46 38.632 17.058 -7.272 ,00 0.00

ATOM 357 O GLU A 46 37.459 17.228 -6.996 ,00 0.00

ATOM 358 N LEU A 47 39.116 17.286 -8.492 ,00 0.00

ATOM 359 CA LEU A 47 38.200 17.751 -9.521 ,00 0.00

ATOM 360 C LEU A 47 37.225 16.655 -9.870 ,00 0.00

ATOM 361 O LEU A 47 36.084 16.930 -10.224 ,00 0.00

ATOM 362 N ASN A 48 37.673 15.415 -9.773 ,00 0.00

ATOM 363 CA ASN A 48 36.785 14.304 -10.082 ,00 0.00

ATOM 364 C ASN A 48 35.710 14.272 -9.001 ,00 0.00

ATOM 365 O ASN A 48 34.515 14.196 -9. 283 ,00 0.00

ATOM 366 N LEU A 49 36.167 14.351 -7.762 ,00 0.00

ATOM 367 CA LEU A 49 35.304 14.363 -6.597 ,00 0.00

ATOM 368 C LEU A 49 34.287 15.517 -6. ,652 ,00 0.00

ATOM 369 O LEU A 49 33.122 15.350 -6. ^?89 ,00 0.00

ATOM 370 N ARG A 50 34.749 16.681 -7.101 ,00 0.00

ATOM 371 CA ARG A 50 33.896 17.866 -7.218 ,00 0.00

ATOM 372 C ARG A 50 32.848 17.589 -8.273 ,00 0.00

ATOM 373 O ARG A 50 31.665 17.799 -8.043 ,00 0.00

ATOM 374 N MET A 51 33.278 17.139 -9.444 ,00 0.00

ATOM 375 CA MET A 51 32.317 16.828 -10.488 ,00 0.00

ATOM 376 C MET A 51 31.214 15.895 -9. ,962 ,00 0.00

ATOM 377 O MET A 51 30.027 16.112 -10. -18 ,00 0.00

ATOM 378 N SER A 52 31.600 14.871 -9..12 ,00 0.00

ATOM 379 CA SER A 52 30.624 13.942 -8.646 ,00 0.00

ATOM 380 C SER A 52 29.665 14.646 -7.699 ,00 0.00

ATOM 381 O SER A 52 28.455 14.470 -7.792 ,00 0.00

ATOM 382 N VAL A 53 30.205 15.443 -6.787 ,00 0.00

ATOM 383 CA VAL A 53 29.368 16.187 -5.858 ,00 0.00

ATOM 384 C VAL A 53 28.347 17.035 -6.577 ,00 0.00

ATOM 385 O VAL A 53 27.191 17.095 -6.169 ,00 0.00

ATOM 386 N GLU A 54 28.787 17.711 -7.634 ,00 0.00

ATOM 387 CA GLU A 54 27.911 18.562 -8.424 ,00 0.00

ATOM 388 C GLU A 54 26.766 17.746 -9.003 ,00 0.00

ATOM 389 O GLU A 54 25.593 18.097 -8.854 ,00 0.00

ATOM 390 N ALA A 55 27.091 16.653 -9.670 ,00 0.00

ATOM 391 CA ALA A 55 26.030 15.826 -10.214 ,00 0.00

ATOM 392 C ALA A 55 25.056 15.473 -9.080 ,00 0.00

ATOM 393 O ALA A 55 23.857 15.714 -9.200 ,00 0.00

ATOM 394 N ASP A 56 25.558 14.928 -7.978 ,00 0.00

ATOM 395 CA ASP A 56 24.677 14.556 -6.861 ,00 0.00

ATOM 396 C ASP A 56 23.783 15.691 -6.380 ,00 0.00

ATOM 397 O ASP A 56 22.606 15.478 -6.101 ,00 0.00

ATOM 398 N ILE A 57 24.322 16.894 -6.265 ,00 0.00

ATOM 399 CA ILE A 57 23.482 17.992 -5.808 ,00 0.00

ATOM 400 C ILE A 57 22.411 18.305 -6.849 ,00 0.00

ATOM 401 O ILE A 57 21.311 18.725 -6.494 ,00 0.00

ATOM 402 N ASN A 58 22.723 18.115 -8.133 ,00 0.00

ATOM 403 CA ASN A 58 21.733 18.406 -9.168 ,00 0.00

ATOM 404 C ASN A 58 20.617 17.407 -9.026 ,00 0.00

ATOM 405 O ASN A 58 19.443 17.774 -8.948 ,00 0.00

ATOM 406 N GLY A 59 20.996 16.136 -8.995 ,00 0.00

ATOM 407 CA GLY A 59 20.007 15.083 ,00 0.00

ATOM 408 C GLY A 59 19. .125 15.268 -7.674 ,00 0.00

ATOM 409 O GLY A 59 17.,908 15.406 -7.785 ,00 0.00

ATOM 410 N LEU A 60 19.747 15.267 -6.506 ,00 0.00

ATOM 411 CA LEU A 60 19.007 15.450 -5.277 ,00 0.00

ATOM 412 C LEU A 60 18.075 16.644 -5.427 ,00 0.00

ATOM 413 O LEU A 60 16.901 16.544 -5.108 ,00 0.00

ATOM 414 N ARG A 61 18.581 17.759 -5.942 ,00 0.00

ATOM 415 CA ARG A 61 17.740 18.937 -6.131 ,00 0.00

ATOM 416 C ARG A 61 16.477 18.615 -6.940 ,00 0.00

ATOM 417 O ARG A 61 15.366 19.005 -6.572 ,00 0.00

ATOM 418 N ARG A 62 16.663 17.917 -8.055 ,00 0.00

ATOM 419 CA ARG A 62 15.546 17.537 -8.904 ,00 0.00

ATOM 420 C ARG A 62 14.546 16.808 -8.023 ,00 0.00

ATOM 421 O ARG A 62 13.402 17.239 -7.865 ,00 0.00

ATOM 422 N VAL A 63 14.999 15.719 -7.421 ,00 0.00

ATOM 423 CA VAL A 63 14.143 14.934 -6.547 1.00 0.00 ATOM 424 C VAL A 63 13.429 15.725 -5 488 .00 0.00

ATOM 425 O VAL A 63 12.241 15.516 5.264 .00 0.00

ATOM 426 N LEU A 64 14.136 16.624 4.822 .00 0.00

ATOM 427 CA LEU A 64 13.471 17.401 3.799 .00 0.00

ATOM 428 C LEU A 64 12.303 18.127 .428 .00 0.00

ATOM 429 O LEU A 64 11.234 18.201 .847 .00 0.00

ATOM 430 N ASP A 65 12.512 18.639 ,635 .00 0.00

ATOM 431 CA ASP A 65 11.468 19.373 ,325 .00 0.00

ATOM 432 C ASP A 65 10.257 18.502 -6 655 .00 0.00

ATOM 433 O ASP A 65 9.115 18.845 6.339 .00 0.00

ATOM 434 N GLU A 66 10.519 17.378 7.302 .00 0.00

ATOM 435 CA GLU A 66 9.466 16.439 662 .00 0.00

ATOM 436 C GLU A 66 8.663 16.088 414 .00 0.00

ATOM 437 O GLU A 66 7.428 15.994 440 .00 0.00

ATOM 438 N LEU A 67 9.360 15.919 304 .00 0.00

ATOM 439 CA LEU A 67 8.652 15.527 110 .00 0.00

ATOM 440 C LEU A 67 1 16.655 -3.534 .00 0.00

ATOM 441 O LEU A 67 6 . 786 16.398 -2.929 .00 0.00

ATOM 442 N THR A 68 8 . 241 17.899 -3.716 .00 0.00

ATOM 443 CA THR A 68 7 . 427 18.990 -3.198 1.00 0.00

ATOM 444 C THR A 68 6 . 121 19.057 -3.996 1.00 0.00

ATOM 445 O THR A 68 5 . 044 19.237 -3.433 1..00 0.00

ATOM 446 N LEU A 69 6 . 212 18.924 -5.316 1..00 0.00

ATOM 447 CA LEU A 69 4.996 18.935 -6.131 1..00 0.00

ATOM 448 C LEU A 69 4.063 17.853 -5.627 1.00 0.00

ATOM 449 O LEU A 69 900 18.108 -5.300 1.00 0.00

ATOM 450 N ALA A 70 572 16.630 -5.611 1.00 0.00

ATOM 451 CA ALA A 70 3 . 792 15.483 172 1.00 0.00

ATOM 452 C ALA A 70 3 . 097 15.747 1.00 0.00

ATOM 453 O ALA A 70 1 . 916 15.434 679 1.00 0.00

ATOM 454 N ARG A 71 840 16.318 906 1..00 0.00

ATOM 455 CA ARG A 71 277 16.616 595 1..00 0.00

ATOM 456 C ARG A 71 2 . 128 17.591 1.00 0.00

ATOM 457 O ARG A 71 1 . 094 17.413 062 1.00 0.00

ATOM 458 N ALA A 72 2 . 314 18.644 465 1.00 0.00

ATOM 459 CA ALA A 72 1 . 273 19.641 580 1.00 0.00

ATOM 460 C ALA A 72 0 . 011 19.071 3.212 1.00 0.00

ATOM 461 O ALA A 72 -1 . 116 19.359 2.795 1.00 0.00

ATOM 462 N ASP A 73 0. 13 18.254 226 1..00 0.00

ATOM 463 CA ASP A 73 -0.871 17.648 947 1..00 0.00

ATOM 464 C ASP A 73 -1.656 16.796 946 1.00 0.00

ATOM 465 O ASP A 73 -2.885 16.829 906 1.00 0.00

ATOM 466 N LEU A 74 -0.940 16.076 -3.093 1.00 0.00

ATOM 467 CA LEU A 74 -1.612 15.262 -2.109 1.00 0.00

ATOM 468 C LEU A 74 -2.320 16.097 -1.042 1.00 0.00

ATOM 469 O LEU A 74 -3.429 15.749 -0.638 1.00 0.00

ATOM 470 N GLU A 75 -1.736 17.197 -0.578 1..00 0.00

ATOM 471 CA GLU A 75 -2.453 17.974 0.438 1..00 0.00

ATOM 472 C GLU A 75 -3.801 18.419 -0.121 1..00 0.00

ATOM 473 O GLU A 75 -4.811 18.422 0.577 1.00 0.00

ATOM 474 N MET A 76 -3.805 18.767 .402 1.00 0.00

ATOM 475 CA MET A 76 -5.015 19.187 .087 1.00 0.00

ATOM 476 C MET A 76 -6.013 18.030 .188 1.00 0.00

ATOM 477 O MET A 76 -7.157 18.146 .742 1.00 0.00

ATOM 478 N GLN A 77 -5.578 16.920 .797 1.00 0.00

ATOM 479 CA GLN A 77 -6.429 15.731 .954 1..00 0.00

ATOM 480 C GLN A 77 -7.030 15.328 .615 1..00 0.00

ATOM 481 O GLN A 77 -8.215 15.022 .518 1.00 0.00

ATOM 482 N ILE A 78 -6.196 15.344 -0.586 1.00 0.00

ATOM 483 CA ILE A 78 -6.642 15.020 0.753 1.00 0.00

ATOM 484 C ILE A 78 -7.739 15.988 1.209 1.00 0.00

ATOM 485 O ILE A 78 -8.770 15.548 1.705 1.00 0.00

ATOM 486 N GLU A 79 -7.549 17.293 1.066 1.00 0.00

ATOM 487 CA GLU A 79 -8.625 18.179 1.499 00 0.00

ATOM 488 C GLU A 79 -9.930 17.904 0.746 00 0.00

ATOM 489 O GLU A 79 -10.998 17.889 1.345 00 0.00

ATOM 490 N SER A 80 -9.846 17.667 -0.561 00 0.00

ATOM 491 CA SER A 80 -11.048 17.412 -1.338 1.00 0.00 ATOM 492 C SER A 80 -11.766 16.187 -0.782 ,00 0.00

ATOM 493 O SER A 80 -12.978 16.214 -0.552 ,00 0.00

ATOM 494 N LEU A 81 -11.002 15.132 -0.526 ,00 0.00

ATOM 495 CA LEU A 81 -11.573 13.891 -0.019 ,00 0.00

ATOM 496 C LEU A 81 ,158 14.056 1.365 ,00 0.00

ATOM 497 O LEU A 81 -13. >36 13.549 1.638 ,00 0.00

ATOM 498 N LYS A 82 -11.452 14.778 2.226 ,00 0.00

ATOM 499 CA LYS A 82 -11.915 15.052 3.584 00 0.00

ATOM 500 C LYS A 82 -13.264 15.769 3.566 ,00 0.00

ATOM 501 O LYS A 82 -14.162 15.474 4.353 ,00 0.00

ATOM 502 N GLU A 83 -13.374 16.733 2.657 ,00 0.00

ATOM 503 CA GLU A 83 -14.593 17.507 2.502 ,00 0.00

ATOM 504 C GLU A 83 -15.735 16.586 2.054 ,00 0.00

ATOM 505 O GLU A 83 -16.838 16.629 601 ,00 0.00

ATOM 506 N GLU A 84 -15.468 15.742 1.059 ,00 0.00

ATOM 507 CA GLU A 84 -16.490 14.815 0.577 ,00 0.00

ATOM 508 C GLU A 84 -16.938 13.902 1.693 ,00 0.00

ATOM 509 O GLU A 84 -18.122 13.625 1.854 ,00 0.00

ATOM 510 N LEU A 85 -15.974 13.412 2.449 ,00 0.00

ATOM 511 CA LEU A 85 -16.280 12.530 3.547 ,00 0.00

ATOM 512 C LEU A 85 -17.211 13.224 4.544 ,00 0.00

ATOM 513 O LEU A 85 -18.195 12.649 4.998 ,00 0.00

ATOM 514 N ALA A 86 -16.891 14.469 4.878 ,00 0.00

ATOM 515 CA ALA A 86 -17.712 15.260 5.795 ,00 0.00

ATOM 516 C ALA A 86 -19.133 15.412 5.251 ,00 0.00

ATOM 517 O ALA A 86 -20.125 15.227 963 ,00 0.00

ATOM 518 N TYR A 87 -19.210 15.772 967 ,00 0.00

ATOM 519 CA TYR A 87 -20.481 15.968 273 ,00 0.00

ATOM 520 C TYR A 87 -21.334 14.712 349 ,00 0.00

ATOM 521 O TYR A 87 -22.539 14.796 570 ,00 0.00

ATOM 522 N LEU A 88 -20.713 13.549 164 ,00 0.00

ATOM 523 CA LEU A 88 -21.448 12.293 215 ,00 0.00

ATOM 524 C LEU A 88 -21.927 11.969 605 ,00 0.00

ATOM 525 O LEU A 88 -23.003 11.416 4.762 ,00 0.00

ATOM 526 N LYS A 89 -21.135 12.283 5.624 ,00 0.00

ATOM 527 CA LYS A 89 -21.580 11.986 6.974 ,00 0.00

ATOM 528 C LYS A 89 -22.830 .805 7.227 ,00 0.00

ATOM 529 O LYS A 89 -23.811 .304 7.774 ,00 0.00

ATOM 530 N LYS A 90 -22.797 14.065 6.806 ,00 0.00

ATOM 531 CA LYS A 90 -23.941 14.942 6.996 ,00 0.00

ATOM 532 C LYS A 90 -25.158 14.403 6.242 ,00 0.00

ATOM 533 O LYS A 90 -26.232 14.227 6.830 ,00 0.00

ATOM 534 N ASN A 91 997 14.108 956 ,00 0.00

ATOM 535 CA ASN A 91 110 13.573 180 ,00 0.00

ATOM 536 C ASN A 91 -26.660 12.299 4.827 ,00 0.00

ATOM 537 O ASN A 91 -27.878 12.116 .924 00 0.00

ATOM 538 N HIS A 92 -25.755 11.438 >91 ,00 0.00

ATOM 539 CA HIS A 92 -26.156 10.205 ,956 ,00 0.00

ATOM 540 C HIS A 92 -27.083 10.593 .089 ,00 0.00

ATOM 541 O HIS A 92 -28.252 10.245 7.059 ,00 0.00

ATOM 542 N GLU A 93 -26.570 11.323 8.079 ,00 0.00

ATOM 543 CA GLU A 93 -27.394 11.760 9.211 ,00 0.00

ATOM 544 C GLU A 93 -28.771 12.190 8.736 ,00 0.00

ATOM 545 O GLU A 93 -29.798 11.667 9.183 ,00 0.00

ATOM 546 N GLU A 94 -28.784 13.164 7.837 ,00 0.00

ATOM 547 CA GLU A 94 -30.034 13.673 7.300 ,00 0.00

ATOM 548 C GLU A 94 -30.981 12.542 6.903 ,00 0.00

ATOM 549 O GLU A 94 -32.176 12.582 7.201 ,00 0.00

ATOM 550 N GLU A 95 -30.440 11.522 6.247 ,00 0.00

ATOM 551 CA GLU A 95 -31.249 10.395 5.793 ,00 0.00

ATOM 552 C GLU A 95 -31.703 9.468 6.905 00 0.00

ATOM 553 O GLU A 95 -32.845 9.016 6.913 00 0.00

ATOM 554 N MET A 96 -30.805 9.164 7.830 00 0.00

ATOM 555 CA MET A 96 -31.188 8.268 8.904 00 0.00

ATOM 556 C MET A 96 -32.277 8.979 9.702 ,00 0.00

ATOM 557 O MET A 96 -33.124 8.350 10.345 00 0.00

ATOM 558 N ASN A 97 -32.278 10.304 9.649 ,00 0.00

ATOM 559 CA ASN A 97 -33.303 11.000 10.395 1.00 0.00 ATOM 560 C ASN A 97 34.610 11.101 9.652 1.00 0.00

ATOM 561 O ASN A 97 35.664 10.923 10.250 1.00 0.00

ATOM 562 N ALA A 98 34.567 11.423 8.366 1.00 0.00

ATOM 563 CA ALA A 98 35.816 11.506 7.633 1.00 0.00

ATOM 564 C ALA A 98 36.517 10.166 7.821 1.00 0.00

ATOM 565 O ALA A 98 37.737 10.115 7.933 1.00 0.00

ATOM 566 N LEU A 99 35.726 9.097 7.892 1.00 0.00

ATOM 567 CA LEU A 99 36.231 7.738 8.122 1.00 0.00

ATOM 568 C LEU A 99 36.864 7.658 9.524 1.00 0.00

ATOM 569 O LEU A 99 38.022 7.263 9.703 1.00 0.00

ATOM 570 N ARG A 100 36.177 7.860 10.491 1.00 0.00

ATOM 571 CA ARG A 100 36.897 7.856 11.769 1.00 0.00

ATOM 572 C ARG A 100 38.259 8.511 11.617 1.00 0.00

ATOM 573 O ARG A 100 39.299 7.908 11.908 1.00 0.00

ATOM 574 N GLY A 101 38.245 9.759 11.173 1.00 0.00

ATOM 575 CA GLY A 101 39.479 10.503 10.983 1.00 0.00

ATOM 576 C GLY A 101 40.534 9.671 10.258 1.00 0.00

ATOM 577 O GLY A 101 41.703 9.652 10.646 1.00 0.00

TER 578 GLY A 101

ATOM 579 N ASP A 1 55.241 9.223 12.450 1.00 0.00

ATOM 580 CA ASP A 1 56.540 9.711 12.038 1.00 0.00

ATOM 581 C ASP A 1 57.515 8.559 11.747 1.00 0.00

ATOM 582 O ASP A 1 58.556 8.455 12.386 1.00 0.00

ATOM 583 N LEU A 9 57.176 7.695 10.793 1.00 0.00

ATOM 584 CA LEU A 9 58.028 6.552 10.471 1.00 0.00

ATOM 585 C LEU A 2 58.407 5.718 11.677 1.00 0.00

ATOM 586 O LEU A 9 59.518 5.221 11.751 1.00 0.00

ATOM 587 N SER A 3 57.468 5.541 12.601 1.00 0.00

ATOM 588 CA SER A 3 57.713 4.767 13.822 1.00 0.00

ATOM 589 C SER A 3 58.774 5.411 14.688 1.00 0.00

ATOM 590 O SER A 3 59.647 4.753 15.249 1.00 0.00

ATOM 591 N ARG A 4 58.632 6.713 14.854 1.00 0.00

ATOM 592 CA ARG A 4 59.543 7.497 15.662 1.00 0.00

ATOM 593 C ARG A 4 60.936 7.408 15.032 1.00 0.00

ATOM 594 O ARG A 4 61.920 7.078 15.705 1.00 0.00

ATOM 595 N ILE A 5 60.998 7.681 13.727 1.00 0.00

ATOM 596 CA ILE A 5 62.234 7.624 12.936 1.00 0.00

ATOM 597 C ILE A 5 62.898 6.281 13.129 1.00 0.00

ATOM 598 O ILE A 5 64.096 6.209 13.363 1.00 0.00

ATOM 599 N LEU A 6 62.109 5.224 12.976 1.00 0.00

ATOM 600 CA LEU A 6 62.644 3.882 13.132 1.00 0.00

ATOM 601 C LEU A 6 63.163 3.606 14.529 1.00 0.00

ATOM 602 O LEU A 6 64.147 2.889 14.687 1.00 0.00

ATOM 603 N ASN A 7 62.510 4.158 15.548 1.00 0.00

ATOM 604 CA ASN A 7 62.961 3.946 16.919 1.00 0.00

ATOM 605 C ASN A 7 64.348 4.553 17.033 1.00 0.00

ATOM 606 O ASN A 7 65.289 3.914 17.505 1.00 0.00

ATOM 607 N GLU A 8 64.473 5.793 16.579 1.00 0.00

ATOM 608 CA GLU A 8 65.760 6.442 16.633 1.00 0.00

ATOM 609 C GLU A 8 66.813 5.646 15.874 1.00 0.00

ATOM 610 O GLU A 8 67.872 5.349 16.430 1.00 0.00

ATOM 611 N MET A 9 66.530 5.233 14.639 1.00 0.00

ATOM 612 CA MET A 9 67.551 4.492 13.912 1.00 0.00

ATOM 613 C MET A 9 67.919 3.153 14.500 1.00 0.00

ATOM 614 O MET A 9 69.076 2.778 14.429 1.00 0.00

ATOM 615 N ARG A 10 66.969 2.416 15.076 1.00 0.00

ATOM 616 CA ARG A 10 67.342 1.127 15.635 1.00 0.00

ATOM 617 C ARG A 10 68.221 1.328 16.841 1.00 0.00

ATOM 618 O ARG A 10 69.090 0.508 17.123 1.00 0.00

ATOM 619 N ASP A 11 68.005 2.422 17.557 1.00 0.00

ATOM 620 CA ASP A 11 68.826 2.692 18.724 1.00 0.00

ATOM 621 C ASP A 11 70.236 2.992 18.230 1.00 0.00

ATOM 622 O ASP A 11 71.221 2.441 18.720 1.00 0.00

ATOM 623 N GLN A 12 70.299 3.863 17.234 1.00 0.00

ATOM 624 CA GLN A 12 71.543 4.260 16.606 1.00 0.00

ATOM 625 C GLN A 12 72.308 3.049 16.040 1.00 0.00

ATOM 626 O GLN A 12 73.534 2.972 16.145 1.00 0.00

ATOM 627 N TYR A 13 71.569 2.123 15.435 1.00 0.00 ATOM 628 CA TYR A 13 -72.156 0.911 14.856 1.00 0.00

ATOM 629 C TYR A 13 -72.725 0.081 15.983 1.00 0.00

ATOM 630 O TYR A 13 -73.868 -0.349 15.921 1.00 0.00

ATOM 631 N GLU A 14 -71.927 -0.168 17.012 1.00 0.00

ATOM 632 CA GLU A 14 -72.428 -0.939 18.139 1.00 0.00

ATOM 633 C GLU A 14 -73.752 -0.358 18.659 1.00 0.00

ATOM 634 O GLU A 14 -74.705 -1.093 18.919 1.00 0.00

ATOM 635 N LYS A 15 -73.821 0.963 18.784 1.00 0.00

ATOM 636 CA LYS A 15 -75.046 1.612 19.249 1.00 0.00

ATOM 637 C LYS A 15 -76.209 1.353 18.302 1.00 0.00

ATOM 638 O LYS A 15 -77.295 0.984 18.736 1.00 0.00

ATOM 639 N MET A 16 -75.981 1.548 17.012 1.00 0.00

ATOM 640 CA MET A 16 -77.020 1.297 16.024 1.00 0.00

ATOM 641 C MET A 16 -77.563 -0.109 16.130 1.00 0.00

ATOM 642 O MET A 16 -78.768 -0.315 16.042 1.00 0.00

ATOM 643 N ALA A 17 -76.664 -1.075 16.287 1.00 0.00

ATOM 644 CA ALA A 17 -77.045 -2.474 16.407 1.00 0.00

ATOM 645 C ALA A 17 -77.958 -2.668 17.606 1.00 0.00

ATOM 646 O ALA A 17 -79.042 -3.245 17.495 1.00 0.00

ATOM 647 N GLU A 18 -77.533 -2.191 18.764 1.00 0.00

ATOM 648 CA GLU A 18 -78.383 -2.329 19.930 1.00 0.00

ATOM 649 C GLU A 18 -79.759 -1.737 19.602 1.00 0.00

ATOM 650 O GLU A 18 -80.776 -2.411 19.756 1.00 0.00

ATOM 651 N LYS A 19 -79.804 -0.494 19.128 1.00 0.00

ATOM 652 CA LYS A 19 -81.091 0.137 18.807 1.00 0.00

ATOM 653 C LYS A 19 -81.960 -0.687 17.863 1.00 0.00

ATOM 654 O LYS A 19 -83.168 -0.791 18.059 1.00 0.00

TER 655 LYS A 19

ATOM 656 N PHE A 1 -93.071 -0.196 18.145 1.00 0.00

ATOM 657 CA PHE A 1 -94.235 -0.504 17.338 1.00 0.00

ATOM 658 C PHE A 1 -94.678 -1.919 17.599 1.00 0.00

ATOM 659 O PHE A 1 -95.847 -2.224 17.434 1.00 0.00

ATOM 660 N PHE A 9 -93.758 -2.800 18.043 1.00 0.00

ATOM 661 CA PHE A 2 -94.191 -4.129 18.448 1.00 0.00

ATOM 662 C PHE A 2 -95.153 -4.018 19.599 1.00 0.00

ATOM 663 O PHE A 2 -96.176 -4.686 19.601 1.00 0.00

ATOM 664 N THR A 3 -94.816 -3.145 20.573 1.00 0.00

ATOM 665 CA THR A 3 -95.708 -2.932 21.702 1.00 0.00

ATOM 666 C THR A 3 -97.044 -2.444 21.220 1.00 0.00

ATOM 667 O THR A 3 -98.058 -2.965 21.655 1.00 0.00

ATOM 668 N LYS A 4 -97.032 -1.447 20.314 1.00 0.00

ATOM 669 CA LYS A 4 -98.287 -0.927 19.794 1.00 0.00

ATOM 670 C LYS A 4 -99.076 -2.015 19.121 1.00 0.00

ATOM 671 O LYS A 4 -100.277 -2.103 19.324 1.00 0.00

ATOM 672 N THR A 5 -98.381 -2.856 18.332 1.00 0.00

ATOM 673 CA THR A 5 -99.065 -3.946 17.656 1.00 0.00

ATOM 674 C THR A 5 -99.697 -4.874 18.655 1.00 0.00

ATOM 675 O THR A 5 -100.839 -5.259 18.461 1.00 0.00

ATOM 676 N GLU A 6 -98.953 -5.221 19.725 1.00 0.00

ATOM 677 CA GLU A 6 -99.503 -6.118 20.729 1.00 0.00

ATOM 678 C GLU A 6 -100.807 -5.588 21.252 1.00 0.00

ATOM 679 O GLU A 6 -101.773 -6.331 21.324 1.00 0.00

ATOM 680 N GLU A 7 -100.823 -4.287 21.604 1.00 0.00

ATOM 681 CA GLU A 7 -102.052 -3.691 22.098 1.00 0.00

ATOM 682 C GLU A 7 -103.146 -3.820 21.076 1.00 0.00

ATOM 683 O GLU A 7 -104.253 -4.191 21.427 1.00 0.00

ATOM 684 N LEU A 8 -102.818 -3.520 19.802 1.00 0.00

ATOM 685 CA LEU A 8 -103.822 -3.608 18.757 1.00 0.00

ATOM 686 C LEU A 8 -104.392 -4.996 18.663 1.00 0.00

ATOM 687 O LEU A 8 -105.602 -5.142 18.610 1.00 0.00

ATOM 688 N ASN A 9 -103.508 -6.013 18.648 1.00 0.00

ATOM 689 CA ASN A 9 -103.982 -7.382 18.533 1.00 0.00

ATOM 690 C ASN A 9 -104.932 -7.717 19.649 1.00 0.00

ATOM 691 O ASN A 9 -105.984 -8.278 19.390 1.00 0.00

ATOM 692 N ARG A 10 -104.557 -7.354 20.892 1.00 0.00

ATOM 693 CA ARG A 10 -105.437 -7.636 22.014 1.00 0.00

ATOM 694 C ARG A 10 -106.751 -6.925 21.845 1.00 0.00

ATOM 695 O ARG A 10 -107.786 -7.519 22.099 1.00 0.00 ATOM 696 N GLU A 11 -106.701 -5.651 21.406 1.00 0.00

ATOM 697 CA GLU A 11 -107.937 -4.910 21.207 1.00 0.00

ATOM 698 C GLU A 11 -108.825 -5.621 20.225 1.00 0.00

ATOM 699 O GLU A 11 -110.014 -5.735 20.474 1.00 0.00

ATOM 700 N VAL A 12 -108.228 -6.109 19.118 1.00 0.00

ATOM 701 CA VAL A 12 -109.004 -6.861 18.145 1.00 0.00

ATOM 702 C VAL A 12 -109.720 -7.988 18.840 1.00 0.00

ATOM 703 O VAL A 12 -110.897 -8.200 18.598 1.00 0.00

ATOM 704 N ALA A 13 -108.985 -8.689 19.725 1.00 0.00

ATOM 705 CA ALA A 13 -109.591 -9.779 20.469 1.00 0.00

ATOM 706 C ALA A 13 -110.752 -9.282 21.288 1.00 0.00

ATOM 707 O ALA A 13 -111.817 -9.873 21.232 1.00 0.00

ATOM 708 N THR A 14 -110.536 -8.187 22.044 1.00 0.00

ATOM 709 CA THR A 14 -111.599 -7.680 22.896 1.00 0.00

ATOM 710 C THR A 14 -112.802 -7.278 22.091 1.00 0.00

ATOM 711 O THR A 14 -113.914 -7.567 22.502 1.00 0.00

ATOM 712 N ASN A 15 -112.575 -6.618 20.938 1.00 0.00

ATOM 713 CA ASN A 15 -113.697 -6.210 20.111 1.00 0.00

ATOM 714 C ASN A 15 -114.503 -7.409 19.703 1.00 0.00

ATOM 715 O ASN A 15 -115.716 -7.392 19.839 1.00 0.00

ATOM 716 N SER A 16 -113.810 -8.458 19.216 1.00 0.00

ATOM 717 CA SER A 16 -114.513 -9.671 18.835 1.00 0.00

ATOM 718 C SER A 16 -115.265 -10.228 20.011 1.00 0.00

ATOM 719 O SER A 16 -116.394 -10.662 19.852 1.00 0.00

ATOM 720 N GLU A 17 -114.627 -10.195 21.199 1.00 0.00

ATOM 721 CA GLU A 17 -115.294 -10.686 22.391 1.00 0.00

ATOM 722 C GLU A 17 -116.566 -9.924 22.637 1.00 0.00

ATOM 723 O GLU A 17 -117.591 -10.531 22.901 1.00 0.00

ATOM 724 N LEU A 18 -116.489 -8.583 22.531 1.00 0.00

ATOM 725 CA LEU A 18 -117.677 -7.774 22.746 1.00 0.00

ATOM 726 C LEU A 18 -118.736 -8.109 21.736 1.00 0.00

ATOM 727 O LEU A 18 -119.904 -8.163 22.086 1.00 0.00

ATOM 728 N VAL A 19 -118.313 -8.348 20.479 1.00 0.00

ATOM 729 CA VAL A 19 -119.279 -8.687 19.448 1.00 0.00

ATOM 730 C VAL A 19 -119.995 -9.966 19.792 1.00 0.00

ATOM 731 O VAL A 19 -121.209 -10.015 19.672 1.00 0.00

ATOM 732 N GLN A 20 -119.241 -10.996 20.225 1.00 0.00

ATOM 733 CA GLN A 20 -119.881 -12.260 20.550 1.00 0.00

ATOM 734 C GLN A 20 -120.843 -12.113 21.696 1.00 0.00

ATOM 735 O GLN A 20 -121.884 -12.750 21.689 1.00 0.00

ATOM 736 N SER A 21 -120.489 -11.262 22.679 1.00 0.00

ATOM 737 CA SER A 21 -121.388 -11.057 23.803 1.00 0.00

ATOM 738 C SER A 21 -122.663 -10.421 23.325 1.00 0.00

ATOM 739 O SER A 21 -123.737 -10.836 23.734 1.00 0.00

ATOM 740 N GLY A 22 -122.529 -9.415 22.436 1.00 0.00

ATOM 741 CA GLY A 22 -123.713 -8.784 21.877 1.00 0.00

ATOM 742 C GLY A 99 -124.524 -9.793 21.114 1.00 0.00

ATOM 743 O GLY A 99 -125.743 -9.729 21.141 1.00 0.00

ATOM 744 N LYS A 23 -123.829 -10.733 20.442 1.00 0.00

ATOM 745 CA LYS A 23 -124.531 -11.749 19.677 1.00 0.00

ATOM 746 C LYS A 23 -125.423 -12.571 20.563 1.00 0.00

ATOM 747 O LYS A 23 -126.588 -12.744 20.242 1.00 0.00

ATOM 748 N SER A 24 -124.865 -13.072 21.685 1.00 0.00

ATOM 749 CA SER A 24 -125.664 -13.889 22.583 1.00 0.00

ATOM 750 C SER A 24 -126.886 -13.139 23.036 1.00 0.00

ATOM 751 O SER A 24 -127.969 -13.702 23.035 1.00 0.00

ATOM 752 N GLU A 25 -126.700 -11.856 23.406 1.00 0.00

ATOM 753 CA GLU A 25 -127.836 -11.057 23.832 1.00 0.00

ATOM 754 C GLU A 25 -128.867 -10.987 22.741 1.00 0.00

ATOM 755 O GLU A 25 -130.038 -11.216 23.001 1.00 0.00

ATOM 756 N ILE A 26 -128.408 -10.668 21.514 1.00 0.00

ATOM 757 CA ILE A 26 -129.331 -10.534 20.400 1.00 0.00

ATOM 758 C ILE A 26 -130.160 -11.773 20.215 1.00 0.00

ATOM 759 O ILE A 26 -131.367 -11.665 20.076 1.00 0.00

ATOM 760 N SER A 27 -129.504 -12.950 20.221 1.00 0.00

ATOM 761 CA SER A 27 -130.245 -14.186 20.036 1.00 0.00

ATOM 762 C SER A 27 -131.268 -14.357 21.124 1.00 0.00

ATOM 763 O SER A 27 -132.390 -14.744 20.836 1.00 0.00 ATOM 764 N GLU A 28 -130.871 -14.057 22.377 1.00 0.00

ATOM 765 CA GLU A 28 -131.803 -14.202 23.482 1.00 0.00

ATOM 766 C GLU A 28 -133.037 -13.375 23.260 1.00 0.00

ATOM 767 O GLU A 28 -134.134 -13.899 23.365 1.00 0.00

ATOM 768 N LEU A 29 -132.846 -12.077 22.947 1.00 0.00

ATOM 769 CA LEU A 29 -133.994 -11.212 22.739 1.00 0.00

ATOM 770 C LEU A 29 -134.837 -11.696 21.595 1.00 0.00

ATOM 771 O LEU A 29 -136.052 -11.719 21.717 1.00 0.00

ATOM 772 N ARG A 30 -134.179 -12.092 20.487 1.00 0.00

ATOM 773 CA ARG A 30 -134.925 -12.544 19.326 1.00 0.00

ATOM 774 C ARG A 30 -135.813 -13.708 19.665 1.00 0.00

ATOM 775 O ARG A 30 -136.983 -13.687 19.317 1.00 0.00

ATOM 776 N ARG A 31 -135.249 -14.718 20.356 1.00 0.00

ATOM 111 CA ARG A 31 -136.053 -15.873 20.724 1.00 0.00

ATOM 778 C ARG A 31 -137.232 -15.445 21.551 1.00 0.00

ATOM 779 O ARG A 31 -138.337 -15.900 21.306 1.00 0.00

ATOM 780 N THR A 32 -136.980 -14.551 22.527 1.00 0.00

ATOM 781 CA THR A 32 -138.065 -14.069 23.365 1.00 0.00

ATOM 782 C THR A 32 -139.126 -13.408 22.528 1.00 0.00

ATOM 783 O THR A 32 -140.301 -13.660 22.744 1.00 0.00

ATOM 784 N MET A 33 -138.699 -12.569 21.563 1.00 0.00

ATOM 785 CA MET A 33 -139.664 -11.894 20.713 1.00 0.00

ATOM 786 C MET A 33 -140.522 -12.892 19.987 1.00 0.00

ATOM 787 O MET A 33 -141.727 -12.716 19.943 1.00 0.00

ATOM 788 N GLN A 34 -139.888 -13.941 19.426 1.00 0.00

ATOM 789 CA GLN A 34 -140.650 -14.943 18.699 1.00 0.00

ATOM 790 C GLN A 34 -141.746 -15.504 19.560 1.00 0.00

ATOM 791 O GLN A 34 -142.877 -15.599 19.110 1.00 0.00

ATOM 792 N ASN A 35 -141.397 -15.865 20.811 1.00 0.00

ATOM 793 CA ASN A 35 -142.402 -16.404 21.709 1.00 0.00

ATOM 794 C ASN A 35 -143.500 -15.403 21.943 1.00 0.00

ATOM 795 O ASN A 35 -144.662 -15.777 21.922 1.00 0.00

ATOM 796 N LEU A 36 -143.120 -14.126 22.149 1.00 0.00

ATOM 797 CA LEU A 36 -144.130 -13.101 22.359 1.00 0.00

ATOM 798 C LEU A 36 -145.054 -13.015 21.179 1.00 0.00

ATOM 799 O LEU A 36 -146.260 -12.983 21.362 1.00 0.00

ATOM 800 N GLU A 37 -144.471 -12.985 19.963 1.00 0.00

ATOM 801 CA GLU A 37 -145.286 -12.862 18.767 1.00 0.00

ATOM 802 C GLU A 37 -146.278 -13.985 18.664 1.00 0.00

ATOM 803 O GLU A 37 -147.441 -13.732 18.389 1.00 0.00

ATOM 804 N ILE A 38 -145.808 -15.226 18.895 1.00 0.00

ATOM 805 CA ILE A 38 -146.712 -16.362 18.812 1.00 0.00

ATOM 806 C ILE A 38 -147.832 -16.204 19.802 1.00 0.00

ATOM 807 O ILE A 38 -148.981 -16.383 19.435 1.00 0.00

ATOM 808 N GLU A 39 -147.482 -15.848 21.054 1.00 0.00

ATOM 809 CA GLU A 39 -148.512 -15.638 22.058 1.00 0.00

ATOM 810 C GLU A 39 -149.497 -14.606 21.590 1.00 0.00

ATOM 811 O GLU A 39 -150.693 -14.794 21.747 1.00 0.00

ATOM 812 N LEU A 40 -148.966 -13.516 20.999 1.00 0.00

ATOM 813 CA LEU A 40 -149.829 -12.446 20.529 1.00 0.00

ATOM 814 C LEU A 40 -150.833 -12.947 19.530 1.00 0.00

ATOM 815 O LEU A 40 -152.019 -12.743 19.729 1.00 0.00

ATOM 816 N GLN A 41 -150.347 -13.600 18.455 1.00 0.00

ATOM 817 CA GLN A 41 -151.258 -14.076 17.429 1.00 0.00

ATOM 818 C GLN A 41 -152.301 -14.987 18.013 1.00 0.00

ATOM 819 O GLN A 41 -153.469 -14.851 17.686 1.00 0.00

ATOM 820 N SER A 42 -151.860 -15.907 18.893 1.00 0.00

ATOM 821 CA SER A 42 -152.798 -16.832 19.503 1.00 0.00

ATOM 822 C SER A 42 -153.862 -16.093 20.264 1.00 0.00

ATOM 823 O SER A 42 -155.036 -16.331 20.030 1.00 0.00

ATOM 824 N GLN A 43 -153.437 -15.193 21.175 1.00 0.00

ATOM 825 CA GLN A 43 -154.404 -14.458 21.974 1.00 0.00

ATOM 826 C GLN A 43 -155.375 -13.717 21.100 1.00 0.00

ATOM 827 O GLN A 43 -156.558 -13.706 21.395 1.00 0.00

ATOM 828 N LEU A 44 -154.859 -13.106 20.015 1.00 0.00

ATOM 829 CA LEU A 44 -155.736 -12.369 19.121 1.00 0.00

ATOM 830 C LEU A 44 -156.790 -13.270 18.545 1.00 0.00

ATOM 831 O LEU A 44 -157.959 -12.918 18.563 1.00 0.00 ATOM 832 N SER A 45 -156.365 -14.446 18.039 1.00 0.00

ATOM 833 CA SER A 45 -157.323 -15.368 17.454 1.00 0.00

ATOM 834 C SER A 45 -158.340 -15.801 18.472 1.00 0.00

ATOM 835 O SER A 45 -159.525 -15.788 18.182 1.00 0.00

ATOM 836 N MET A 46 -157.855 -16.175 19.673 1.00 0.00

ATOM 837 CA MET A 46 -158.763 -16.603 20.724 1.00 0.00

ATOM 838 C MET A 46 -159.773 -15.532 21.024 1.00 0.00

ATOM 839 O MET A 46 -160.952 -15.830 21.138 1.00 0.00

ATOM 840 N LYS A 47 -159.295 -14.279 21.143 1.00 0.00

ATOM 841 CA LYS A 47 -160.201 -13.185 21.447 1.00 0.00

ATOM 842 C LYS A 47 -161.243 -13.037 20.374 1.00 0.00

ATOM 843 O LYS A 47 -162.401 -12.821 20.693 1.00 0.00

ATOM 844 N ALA A 48 -160.823 -13.161 19.099 1.00 0.00

ATOM 845 CA ALA A 48 -161.775 -13.028 18.010 1.00 0.00

ATOM 846 C ALA A 48 -162.898 -14.016 18.163 1.00 0.00

ATOM 847 O ALA A 48 -164.054 -13.640 18.036 1.00 0.00

ATOM 848 N SER A 49 -162.542 -15.283 18.452 1.00 0.00

ATOM 849 CA SER A 49 -163.570 -16.295 18.627 1.00 0.00

ATOM 850 C SER A 49 -164.473 -15.949 19.778 1.00 0.00

ATOM 851 O SER A 49 -165.682 -16.006 19.627 1.00 0.00

ATOM 852 N LEU A 50 -163.868 -15.585 20.926 1.00 0.00

ATOM 853 CA LEU A 50 -164.668 -15.291 22.103 1.00 0.00

ATOM 854 C LEU A 50 -165.629 -14.161 21.865 1.00 0.00

ATOM 855 O LEU A 50 -166.791 -14.281 99 999 1.00 0.00

ATOM 856 N GLU A 51 -165.137 -13.064 21.255 1.00 0.00

ATOM 857 CA GLU A 51 -165.999 -11.916 21.026 1.00 0.00

ATOM 858 C GLU A 51 -167.198 -12.298 20.206 1.00 0.00

ATOM 859 O GLU A 51 -168.304 -11.896 20.533 1.00 0.00

ATOM 860 N ASN A 52 -166.964 -13.094 19.145 1.00 0.00

ATOM 861 CA ASN A 52 -168.078 -13.543 18.326 1.00 0.00

ATOM 862 C ASN A 52 -169.055 -14.340 19.142 1.00 0.00

ATOM 863 O ASN A 52 -170.251 -14.194 18.950 1.00 0.00

ATOM 864 N SER A 53 -168.529 -15.175 20.062 1.00 0.00

ATOM 865 CA SER A 53 -169.401 -16.018 20.866 1.00 0.00

ATOM 866 C SER A 53 -170.320 -15.229 21.760 1.00 0.00

ATOM 867 O SER A 53 -171.504 -15.523 21.791 1.00 0.00

ATOM 868 N LEU A 54 -169.784 -14.228 22.490 1.00 0.00

ATOM 869 CA LEU A 54 -170.640 -13.467 23.388 1.00 0.00

ATOM 870 C LEU A 54 -171.649 -12.667 22.611 1.00 0.00

ATOM 871 O LEU A 54 -172.826 -12.715 22.933 1.00 0.00

ATOM 872 N GLU A 55 -171.175 -11.946 21.574 1.00 0.00

ATOM 873 CA GLU A 55 -172.092 -11.177 20.745 1.00 0.00

ATOM 874 C GLU A 55 -173.210 -12.056 20.257 1.00 0.00

ATOM 875 O GLU A 55 -174.337 -11.604 20.139 1.00 0.00

ATOM 876 N GLU A 56 -172.870 -13.334 19.996 1.00 0.00

ATOM 877 CA GLU A 56 -173.875 -14.278 19.544 1.00 0.00

ATOM 878 C GLU A 56 -174.926 -14.498 20.597 1.00 0.00

ATOM 879 O GLU A 56 -176.098 -14.298 20.316 1.00 0.00

ATOM 880 N THR A 57 -174.500 -14.918 21.804 1.00 0.00

ATOM 881 CA THR A 57 -175.464 -15.228 22.851 1.00 0.00

ATOM 882 C THR A 57 -176.387 -14.070 23.107 1.00 0.00

ATOM 883 O THR A 57 -177.591 -14.262 23.153 1.00 0.00

ATOM 884 N LYS A 58 -175.797 -12.868 23.269 1.00 0.00

ATOM 885 CA LYS A 58 -176.598 -11.688 23.551 1.00 0.00

ATOM 886 C LYS A 58 -177.729 -11.545 22.573 1.00 0.00

ATOM 887 O LYS A 58 -178.865 -11.373 22.986 1.00 0.00

ATOM 888 N GLY A 59 -177.405 -11.628 21.268 1.00 0.00

ATOM 889 CA GLY A 59 -178.444 -11.491 20.261 1.00 0.00

ATOM 890 C GLY A 59 -179.437 -12.616 20.341 1.00 0.00

ATOM 891 O GLY A 59 -180.629 -12.364 20.282 1.00 0.00

ATOM 892 N ARG A 60 -178.935 -13.860 20.476 1.00 0.00

ATOM 893 CA ARG A 60 -179.830 -15.006 20.484 1.00 0.00

ATOM 894 C ARG A 60 -180.817 -14.944 21.618 1.00 0.00

ATOM 895 O ARG A 60 -182.012 -14.992 21.375 1.00 0.00

ATOM 896 N TYR A 61 -180.300 -14.846 22.859 1.00 0.00

ATOM 897 CA TYR A 61 -181.181 -14.841 24.013 1.00 0.00

ATOM 898 C TYR A 61 -182.201 -13.740 23.917 1.00 0.00

ATOM 899 O TYR A 61 -183.337 -13.947 24.314 1.00 0.00 ATOM 900 N CYS A 62 -181.788 -12.574 23.378 1.00 0.00

ATOM 901 CA CYS A 62 -182.715 -11.460 23.268 1.00 0.00

ATOM 902 C CYS A 62 -183.979 -11.862 22.560 1.00 0.00

ATOM 903 O CYS A 62 -185.058 -11.595 23.063 1.00 0.00

ATOM 904 N MET A 63 -183.835 -12.516 21.392 1.00 0.00

ATOM 905 CA MET A 63 -185.016 -12.943 20.660 1.00 0.00

ATOM 906 C MET A 63 -185.771 -13.989 21.426 1.00 0.00

ATOM 907 O MET A 63 -186.989 -13.935 21.476 1.00 0.00

ATOM 908 N GLN A 64 -185.033 -14.946 22.023 1.00 0.00

ATOM 909 CA GLN A 64 -185.688 -16.035 22.729 1.00 0.00

ATOM 910 C GLN A 64 -186.528 -15.532 23.867 1.00 0.00

ATOM 911 O GLN A 64 -187.704 -15.853 23.933 1.00 0.00

ATOM 912 N LEU A 65 -185.909 -14.738 24.763 1.00 0.00

ATOM 913 CA LEU A 65 -186.651 -14.197 25.888 1.00 0.00

ATOM 914 C LEU A 65 -187.814 -13.390 25.387 1.00 0.00

ATOM 915 O LEU A 65 -188.886 -13.447 25.969 1.00 0.00

ATOM 916 N ALA A 66 -187.583 -12.652 24.283 1.00 0.00

ATOM 917 CA ALA A 66 -188.656 -11.880 23.681 1.00 0.00

ATOM 918 C ALA A 66 -189.827 -12.774 23.370 1.00 0.00

ATOM 919 O ALA A 66 -190.956 -12.407 23.650 1.00 0.00

ATOM 920 N GLN A 67 -189.535 -13.958 22.798 1.00 0.00

ATOM 921 CA GLN A 67 -190.605 -14.886 22.478 1.00 0.00

ATOM 922 C GLN A 67 -191.220 -15.457 23.725 1.00 0.00

ATOM 923 O GLN A 67 -192.430 -15.615 23.773 1.00 0.00

ATOM 924 N ILE A 68 -190.378 -15.753 24.738 1.00 0.00

ATOM 925 CA ILE A 68 -190.901 -16.301 25.979 1.00 0.00

ATOM 926 C ILE A 68 -191.943 -15.386 26.557 1.00 0.00

ATOM 927 O ILE A 68 -193.005 -15.843 26.950 1.00 0.00

ATOM 928 N GLN A 69 -191.620 -14.080 26.590 1.00 0.00

ATOM 929 CA GLN A 69 -192.560 -13.113 27.129 1.00 0.00

ATOM 930 C GLN A 69 -193.821 -13.078 26.312 1.00 0.00

ATOM 931 O GLN A 69 -194.893 -12.924 26.877 1.00 0.00

ATOM 932 N GLU A 70 -193.688 -13.238 24.980 1.00 0.00

ATOM 933 CA GLU A 70 -194.876 -13.226 24.141 1.00 0.00

ATOM 934 C GLU A 70 -195.800 -14.351 24.509 1.00 0.00

ATOM 935 O GLU A 70 -196.988 -14.119 24.662 1.00 0.00

ATOM 936 N MET A 71 -195.238 -15.568 24.658 1.00 0.00

ATOM 937 CA MET A 71 -196.064 -16.713 25.013 1.00 0.00

ATOM 938 C MET A 71 -196.811 -16.434 26.286 1.00 0.00

ATOM 939 O MET A 71 -197.994 -16.722 26.364 1.00 0.00

ATOM 940 N ILE A 72 -196.106 -15.856 27.277 1.00 0.00

ATOM 941 CA ILE A 72 -196.761 -15.547 28.533 1.00 0.00

ATOM 942 C ILE A 72 -197.911 -14.606 28.307 1.00 0.00

ATOM 943 O ILE A 72 -198.976 -14.815 28.866 1.00 0.00

ATOM 944 N GLY A 73 -197.688 -13.576 27.467 1.00 0.00

ATOM 945 CA GLY A 73 -198.751 -12.623 27.197 1.00 0.00

ATOM 946 C GLY A 73 -199.912 -13.283 26.507 1.00 0.00

ATOM 947 O GLY A 73 -201.048 -13.028 26.869 1.00 0.00

ATOM 948 N SER A 74 -199.611 -14.141 25.512 1.00 0.00

ATOM 949 CA SER A 74 -200.683 -14.816 24.800 1.00 0.00

ATOM 950 C SER A 74 -201.470 -15.684 25.742 1.00 0.00

ATOM 951 O SER A 74 -202.689 -15.696 25.670 1.00 0.00

ATOM 952 N VAL A 75 -200.759 -16.394 26.638 1.00 0.00

ATOM 953 CA VAL A 75 -201.452 -17.210 27.622 1.00 0.00

ATOM 954 C VAL A 75 -202.301 -16.338 28.505 1.00 0.00

ATOM 955 O VAL A 75 -203.388 -16.741 28.889 1.00 0.00

ATOM 956 N GLU A 76 -201.786 -15.130 28.808 1.00 0.00

ATOM 957 CA GLU A 76 -202.515 -14.216 29.668 1.00 0.00

ATOM 958 C GLU A 76 -203.850 -13.861 29.074 1.00 0.00

ATOM 959 O GLU A 76 -204.854 -13.974 29.759 1.00 0.00

ATOM 960 N GLU A 77 -203.851 -13.437 27.794 1.00 0.00

ATOM 961 CA GLU A 77 -205.102 -13.054 27.160 1.00 0.00

ATOM 962 C GLU A 77 -206.094 -14.180 27.207 1.00 0.00

ATOM 963 O GLU A 77 -207.258 -13.951 27.499 1.00 0.00

ATOM 964 N GLN A 78 -205.610 -15.407 26.930 1.00 0.00

ATOM 965 CA GLN A 78 -206.487 -16.562 26.985 1.00 0.00

ATOM 966 C GLN A 78 -207.066 -16.716 28.363 1.00 0.00

ATOM 967 O GLN A 78 -208.268 -16.879 28.498 1.00 0.00 ATOM 968 N LEU A 79 -206.184 -16.657 29.381 1.00 0.00

ATOM 969 CA LEU A 79 -206.631 -16.819 30.755 1.00 0.00

ATOM 970 C LEU A 79 -207.726 -15.846 31.091 1.00 0.00

ATOM 971 O LEU A 79 -208.731 -16.247 31.656 1.00 0.00

ATOM 972 N ALA A 80 -207.522 -14.563 30.735 1.00 0.00

ATOM 973 CA ALA A 80 -208.529 -13.562 31.038 1.00 0.00

ATOM 974 C ALA A 80 -209.834 -13.888 30.368 1.00 0.00

ATOM 975 O ALA A 80 -210.875 -13.755 30.993 1.00 0.00

ATOM 976 N GLN A 81 -209.767 -14.326 29.095 1.00 0.00

ATOM 977 CA GLN A 81 -210.988 -14.644 28.373 1.00 0.00

ATOM 978 C GLN A 81 -211.786 -15.698 29.088 1.00 0.00

ATOM 979 O GLN A 81 -212.972 -15.512 29.304 1.00 0.00

ATOM 980 N LEU A 82 -211.117 -16.807 29.455 1.00 0.00

ATOM 981 CA LEU A 82 -211.830 -17.887 30.117 1.00 0.00

ATOM 982 C LEU A 82 -212.380 -17.441 31.442 1.00 0.00

ATOM 983 O LEU A 82 -213.511 -17.780 31.756 1.00 0.00

ATOM 984 N ARG A 83 -211.583 -16.673 32.211 1.00 0.00

ATOM 985 CA ARG A 83 -212.050 -16.231 33.516 1.00 0.00

ATOM 986 C ARG A 83 -213.323 -15.440 33.405 1.00 0.00

ATOM 987 O ARG A 83 -214.255 -15.701 34.147 1.00 0.00

ATOM 988 N CYS A 84 -213.360 -14.478 32.460 1.00 0.00

ATOM 989 CA CYS A 84 -214.570 -13.692 32.287 1.00 0.00

ATOM 990 C CYS A 84 -215.724 -14.584 31.929 1.00 0.00

ATOM 991 O CYS A 84 -216.804 -14.425 32.479 1.00 0.00

ATOM 992 N GLU A 85 -215.481 -15.535 31.005 1.00 0.00

ATOM 993 CA GLU A 85 -216.536 -16.457 30.620 1.00 0.00

ATOM 994 C GLU A 85 -217.040 -17.213 31.815 1.00 0.00

ATOM 995 O GLU A 85 -218.242 -17.363 31.968 1.00 0.00

ATOM 996 N MET A 86 -216.107 -17.680 32.670 1.00 0.00

ATOM 997 CA MET A 86 -216.520 -18.433 33.841 1.00 0.00

ATOM 998 C MET A 86 -217.355 -17.587 34.761 1.00 0.00

ATOM 999 O MET A 86 -218.319 -18.090 35.317 1.00 0.00

ATOM 1000 N GLU A 87 -216.983 -16.300 34.915 1.00 0.00

ATOM 1001 CA GLU A 87 -217.755 -15.427 35.784 1.00 0.00

ATOM 1002 C GLU A 87 -219.181 -15.361 35.313 1.00 0.00

ATOM 1003 O GLU A 87 -220.089 -15.488 36.118 1.00 0.00

ATOM 1004 N GLN A 88 -219.360 -15.170 33.992 1.00 0.00

ATOM 1005 CA GLN A 88 -220.706 -15.111 33.451 1.00 0.00

ATOM 1006 C GLN A 88 -221.438 -16.396 33.720 1.00 0.00

ATOM 1007 O GLN A 88 -222.593 -16.354 34.115 1.00 0.00

ATOM 1008 N GLN A 89 -220.750 -17.537 33.516 1.00 0.00

ATOM 1009 CA GLN A 89 -221.394 -18.818 33.755 1.00 0.00

ATOM 1010 C GLN A 89 -221.831 -18.938 35.187 1.00 0.00

ATOM 1011 O GLN A 89 -222.955 -19.340 35.436 1.00 0.00

ATOM 1012 N ASN A 90 -220.934 -18.572 36.125 1.00 0.00

ATOM 1013 CA ASN A 90 -221.276 -18.675 37.533 1.00 0.00

ATOM 1014 C ASN A 90 -222.486 -17.846 37.863 1.00 0.00

ATOM 1015 O ASN A 90 -223.366 -18.325 38.562 1.00 0.00

ATOM 1016 N GLN A 91 -222.528 -16.603 37.344 1.00 0.00

ATOM 1017 CA GLN A 91 -223.676 -15.752 37.609 1.00 0.00

ATOM 1018 C GLN A 91 -224.935 -16.404 37.107 1.00 0.00

ATOM 1019 O GLN A 91 -225.914 -16.454 37.832 1.00 0.00

ATOM 1020 N GLU A 92 -224.886 -16.913 35.859 1.00 0.00

ATOM 1021 CA GLU A 92 -226.049 -17.592 35.308 1.00 0.00

ATOM 1022 C GLU A 92 -226.468 -18.717 36.208 1.00 0.00

ATOM 1023 O GLU A 92 -227.647 -18.878 36.474 1.00 0.00

ATOM 1024 N TYR A 93 -225.465 -19.485 36.674 1.00 0.00

ATOM 1025 CA TYR A 93 -225.746 -20.632 37.518 1.00 0.00

ATOM 1026 C TYR A 93 -226.511 -20.231 38.748 1.00 0.00

ATOM 1027 O TYR A 93 -227.566 -20.790 39.001 1.00 0.00

ATOM 1028 N LYS A 94 -225.964 -19.261 39.506 1.00 0.00

ATOM 1029 CA LYS A 94 -226.624 -18.837 40.731 1.00 0.00

ATOM 1030 C LYS A 94 -228.037 -18.401 40.458 1.00 0.00

ATOM 1031 O LYS A 94 -228.936 -18.783 41.190 1.00 0.00

ATOM 1032 N ILE A 95 -228.215 -17.602 39.389 1.00 0.00

ATOM 1033 CA ILE A 95 -229.545 -17.117 39.062 1.00 0.00

ATOM 1034 C ILE A 95 -230.487 -18.256 38.786 1.00 0.00

ATOM 1035 O ILE A 95 -231.549 -18.309 39.385 1.00 0.00 ATOM 1036 N LEU A 96 -230.081 -19.166 37.878 1.00 0.00

ATOM 1037 CA LEU A 96 -230.941 -20.289 37.539 1.00 0.00

ATOM 1038 C LEU A 96 -231.321 -21.063 38.769 1.00 0.00

ATOM 1039 O LEU A 96 -232.475 -21.436 38.912 1.00 0.00

ATOM 1040 N LEU A 97 -230.334 -21.285 39.657 1.00 0.00

ATOM 1041 CA LEU A 97 -230.608 -22.027 40.877 1.00 0.00

ATOM 1042 C LEU A 97 -231.678 -21.348 41.685 1.00 0.00

ATOM 1043 O LEU A 97 -232.623 -22.002 42.098 1.00 0.00

ATOM 1044 N ASP A 98 -231.519 -20.027 41.901 1.00 0.00

ATOM 1045 CA ASP A 98 -232.501 -19.300 42.688 1.00 0.00

ATOM 1046 C ASP A 98 -233.861 -19.384 42.055 1.00 0.00

ATOM 1047 O ASP A 98 -234.829 -19.661 42.745 1.00 0.00

ATOM 1048 N VAL A 99 -233.914 -19.152 40.729 1.00 0.00

ATOM 1049 CA VAL A 99 -235.185 -19.221 40.025 1.00 0.00

ATOM 1050 C VAL A 99 -235.823 -20.568 40.221 1.00 0.00

ATOM 1051 O VAL A 99 -237.006 -20.639 40.515 1.00 0.00

ATOM 1052 N LYS A 100 -235.016 -21.633 40.056 1.00 0.00

ATOM 1053 CA LYS A 100 -235.550 -22.977 40.199 1.00 0.00

ATOM 1054 C LYS A 100 -236.128 -23.188 41.571 1.00 0.00

ATOM 1055 O LYS A 100 -237.189 -23.779 41.682 1.00 0.00

ATOM 1056 N THR A 101 -235.426 -22.692 42.609 1.00 0.00

ATOM 1057 CA THR A 101 -235.932 -22.854 43.962 1.00 0.00

ATOM 1058 C THR A 101 -237.309 -22.258 44.075 1.00 0.00

ATOM 1059 O THR A 101 -238.206 -22.906 44.588 1.00 0.00

ATOM 1060 N ARG A 102 -237.463 -21.016 43.576 1.00 0.00

ATOM 1061 CA ARG A 102 -238.761 -20.368 43.644 1.00 0.00

ATOM 1062 C ARG A 102 -239.803 -21.172 42.919 1.00 0.00

ATOM 1063 O ARG A 102 -240.867 -21.412 43.469 1.00 0.00

ATOM 1064 N LEU A 103 -239.486 -21.586 41.677 1.00 0.00

ATOM 1065 CA LEU A 103 -240.465 -22.314 40.889 1.00 0.00

ATOM 1066 C LEU A 103 -240.889 -23.587 41.561 1.00 0.00

ATOM 1067 O LEU A 103 -242.079 -23.840 41.645 1.00 0.00

ATOM 1068 N GLU A 104 -239.911 -24.380 42.046 1.00 0.00

ATOM 1069 CA GLU A 104 -240.256 -25.640 42.684 1.00 0.00

ATOM 1070 C GLU A 104 -241.201 -25.422 43.832 1.00 0.00

ATOM 1071 O GLU A 104 -242.158 -26.168 43.968 1.00 0.00

ATOM 1072 N GLN A 105 -240.929 -24.382 44.647 1.00 0.00

ATOM 1073 CA GLN A 105 -241.827 -24.088 45.750 1.00 0.00

ATOM 1074 C GLN A 105 -243.200 -23.772 45.227 1.00 0.00

ATOM 1075 O GLN A 105 -244.176 -24.293 45.744 1.00 0.00

ATOM 1076 N GLU A 106 -243.259 -22.922 44.184 1.00 0.00

ATOM 1077 CA GLU A 106 -244.546 -22.568 43.607 1.00 0.00

ATOM 1078 C GLU A 106 -245.259 -23.790 43.097 1.00 0.00

ATOM 1079 O GLU A 106 -246.458 -23.910 43.294 1.00 0.00

ATOM 1080 N ILE A 107 -244.502 -24.698 42.450 1.00 0.00

ATOM 1081 CA ILE A 107 -245.110 -25.906 41.917 1.00 0.00

ATOM 1082 C ILE A 107 -245.718 -26.715 43.027 1.00 0.00

ATOM 1083 O ILE A 107 -246.859 -27.132 42.907 1.00 0.00

ATOM 1084 N ALA A 108 -244.941 -26.924 44.109 1.00 0.00

ATOM 1085 CA ALA A 108 -245.449 -27.704 45.227 1.00 0.00

ATOM 1086 C ALA A 108 -246.749 -27.136 45.724 1.00 0.00

ATOM 1087 O ALA A 108 -247.678 -27.886 45.977 1.00 0.00

ATOM 1088 N THR A 109 -246.806 -25.795 45.842 1.00 0.00

ATOM 1089 CA THR A 109 -248.034 -25.164 46.300 1.00 0.00

ATOM 1090 C THR A 109 -249.160 -25.456 45.349 1.00 0.00

ATOM 1091 O THR A 109 -250.228 -25.847 45.791 1.00 0.00

ATOM 1092 N TYR A 110 -248.904 -25.270 44.038 1.00 0.00

ATOM 1093 CA TYR A 110 -249.941 -25.531 43.054 1.00 0.00

ATOM 1094 C TYR A 110 -250.459 -26.936 43.180 1.00 0.00

ATOM 1095 O TYR A 110 -251.661 -27.139 43.148 1.00 0.00

ATOM 1096 N ARG A 111 -249.533 -27.902 43.335 1.00 0.00

ATOM 1097 CA ARG A 111 -249.951 -29.289 43.451 1.00 0.00

ATOM 1098 C ARG A 111 -250.893 -29.474 44.609 1.00 0.00

ATOM 1099 O ARG A 111 -251.934 -30.090 44.447 1.00 0.00

ATOM 1100 N ARG A 112 -250.521 -28.924 45.782 1.00 0.00

ATOM 1101 CA ARG A 112 -251.381 -29.064 46.946 1.00 0.00

ATOM 1102 C ARG A 112 -252.741 -28.482 46.675 1.00 0.00

ATOM 1103 O ARG A 112 -253.738 -29.116 46.982 1.00 0.00 ATOM 1104 N LEU A 113 -252.763 -27.270 46.087 1.00 0.00

ATOM 1105 CA LEU A 113 -254.033 -26.625 45.808 1.00 0.00

ATOM 1106 C LEU A 113 -254.896 -27.489 44.934 1.00 0.00

ATOM 1107 O LEU A 113 -256.062 -27.676 45.243 1.00 0.00

ATOM 1108 N LEU A 114 -254.306 -28.020 43.844 1.00 0.00

ATOM 1109 CA LEU A 114 -255.085 -28.855 42.948 1.00 0.00

ATOM 1110 C LEU A 114 -255.626 -30.056 43.671 1.00 0.00

ATOM 1111 O LEU A 114 -256.762 -30.431 43.433 1.00 0.00

ATOM 1112 N GLU A 115 -254.811 -30.645 44.570 1.00 0.00

ATOM 1113 CA GLU A 115 -255.289 -31.792 45.323 1.00 0.00

ATOM 1114 C GLU A 115 -256.475 -31.411 46.160 1.00 0.00

ATOM 1115 O GLU A 115 -257.491 -32.088 46.113 1.00 0.00

ATOM 1116 N GLY A 116 -256.333 -30.313 46.929 1.00 0.00

ATOM 1117 CA GLY A 116 -257.412 -29.912 47.815 1.00 0.00

ATOM 1118 C GLY A 116 -258.665 -29.606 47.046 1.00 0.00

ATOM 1119 O GLY A 116 -259.708 -30.154 47.368 1.00 0.00

ATOM 1120 N GLU A 117 -258.556 -28.727 46.031 1.00 0.00

ATOM 1121 CA GLU A 117 -259.745 -28.343 45.289 1.00 0.00

ATOM 1122 C GLU A 117 -260.320 -29.520 44.556 1.00 0.00

ATOM 1123 O GLU A 117 -261.463 -29.880 44.795 1.00 0.00

TER 1124 GLU A 117

ATOM 1125 N ILE B 1 183.610 37.279 -26.045 1.00 0.00

ATOM 1126 CA ILE B 1 182.494 38.031 -26.603 1.00 0.00

ATOM 1127 C ILE B 1 181.712 37.275 -27.641 1.00 0.00

ATOM 1128 O ILE B 1 180.499 37.411 -27.665 1.00 0.00

ATOM 1129 N GLN B 9 182.378 36.480 -28.503 1.00 0.00

ATOM 1130 CA GLN B 2 181.608 35.708 -29.467 1.00 0.00

ATOM 1131 C GLN B 2 180.769 34.708 -28.720 1.00 0.00

ATOM 1132 O GLN B 9 179.646 34.438 -29.115 1.00 0.00

ATOM 1133 N ARG B 3 181.329 34.181 -27.613 1.00 0.00

ATOM 1134 CA ARG B 3 180.580 33.245 -26.791 1.00 0.00

ATOM 1135 C ARG B 3 179.342 33.894 -26.238 1.00 0.00

ATOM 1136 O ARG B 3 178.271 33.315 -26.332 1.00 0.00

ATOM 1137 N VAL B 4 179.497 35.105 -25.667 1.00 0.00

ATOM 1138 CA VAL B 4 178.343 35.802 -25.124 1.00 0.00

ATOM 1139 C VAL B 4 177.293 35.999 -26.180 1.00 0.00

ATOM 1140 O VAL B 4 176.123 35.792 -25.907 1.00 0.00

ATOM 1141 N ARG B 5 177.728 36.389 -27.398 1.00 0.00

ATOM 1142 CA ARG B 5 176.776 36.590 -28.478 1.00 0.00

ATOM 1143 C ARG B 5 176.012 35.329 -28.775 1.00 0.00

ATOM 1144 O ARG B 5 174.820 35.406 -29.027 1.00 0.00

ATOM 1145 N THR B 6 176.691 34.163 -28.731 1.00 0.00

ATOM 1146 CA THR B 6 175.984 32.913 -28.968 1.00 0.00

ATOM 1147 C THR B 6 174.886 32.750 -27.953 1.00 0.00

ATOM 1148 O THR B 6 173.798 32.315 -28.295 1.00 0.00

ATOM 1149 N GLU B 7 175.197 33.123 -26.695 1.00 0.00

ATOM 1150 CA GLU B 7 174.224 32.985 -25.624 1.00 0.00

ATOM 1151 C GLU B 7 173.030 33.876 -25.823 1.00 0.00

ATOM 1152 O GLU B 7 171.913 33.421 -25.641 1.00 0.00

ATOM 1153 N GLU B 8 173.264 35.152 -26.196 1.00 0.00

ATOM 1154 CA GLU B 8 172.145 36.068 -26.363 1.00 0.00

ATOM 1155 C GLU B 8 171.242 35.611 -27.473 1.00 0.00

ATOM 1156 O GLU B 8 170.033 35.717 -27.348 1.00 0.00

ATOM 1157 N ARG B 9 171.848 35.089 -28.558 1.00 0.00

ATOM 1158 CA ARG B 9 171.042 34.583 -29.657 1.00 0.00

ATOM 1159 C ARG B 9 170.188 33.439 -29.188 1.00 0.00

ATOM 1160 O ARG B 9 169.056 33.309 -29.623 1.00 0.00

ATOM 1161 N GLU B 10 170.752 32.613 -28.283 1.00 0.00

ATOM 1162 CA GLU B 10 170.004 31.475 -27.782 1.00 0.00

ATOM 1163 C GLU B 10 168.867 31.927 -26.908 1.00 0.00

ATOM 1164 O GLU B 10 167.750 31.475 -27.103 1.00 0.00

ATOM 1165 N GLN B 11 169.156 32.826 -25.945 1.00 0.00

ATOM 1166 CA GLN B 11 168.099 33.292 -25.061 1.00 0.00

ATOM 1167 C GLN B 11 167.004 33.947 -25.854 1.00 0.00

ATOM 1168 O GLN B 11 165.836 33.727 -25.566 1.00 0.00

ATOM 1169 N ILE B 12 167.399 34.744 -26.866 1.00 0.00

ATOM 1170 CA ILE B 12 166.411 35.407 -27.699 1.00 0.00

ATOM 1171 C ILE B 12 165.511 34.402 -28.362 1.00 0.00 ATOM 1172 O ILE B 12 164.303 34.576 -28.337 1.00 0.00

ATOM 1173 N LYS B 13 166.110 33.347 -28.951 1.00 0.00

ATOM 1174 CA LYS B 13 165.298 32.337 -29.610 1.00 0.00

ATOM 1175 C LYS B 13 164.295 31.749 -28.658 1.00 0.00

ATOM 1176 O LYS B 13 163.134 31.630 -29.015 1.00 0.00

ATOM 1177 N THR B 14 164.749 31.397 -27.437 1.00 0.00

ATOM 1178 CA THR B 14 163.827 30.845 -26.456 1.00 0.00

ATOM 1179 C THR B 14 162.703 31.806 -26.181 1.00 0.00

ATOM 1180 O THR B 14 161.563 31.380 -26.086 1.00 0.00

ATOM 1181 N LEU B 15 163.031 33.110 -26.067 1.00 0.00

ATOM 1182 CA LEU B 15 161.994 34.095 -25.799 1.00 0.00

ATOM 1183 C LEU B 15 160.995 34.141 -26.922 1.00 0.00

ATOM 1184 O LEU B 15 159.804 34.109 -26.659 1.00 0.00

ATOM 1185 N ASN B 16 161.488 34.210 -28.175 1.00 0.00

ATOM 1186 CA ASN B 16 160.581 34.285 -29.311 1.00 0.00

ATOM 1187 C ASN B 16 159.651 33.104 -29.351 1.00 0.00

ATOM 1188 O ASN B 16 158.472 33.284 -29.610 1.00 0.00

ATOM 1189 N ASN B 17 160.187 31.894 -29.088 1.00 0.00

ATOM 1190 CA ASN B 17 159.340 30.713 -29.101 1.00 0.00

ATOM 1191 C ASN B 17 158.282 30.835 -28.040 1.00 0.00

ATOM 1192 O ASN B 17 157.121 30.573 -28.311 1.00 0.00

ATOM 1193 N LYS B 18 158.708 31.255 -26.831 1.00 0.00

ATOM 1194 CA LYS B 18 157.755 31.462 -25.753 1.00 0.00

ATOM 1195 C LYS B 18 156.658 32.384 -26.208 1.00 0.00

ATOM 1196 O LYS B 18 155.491 32.060 -26.053 1.00 0.00

ATOM 1197 N PHE B 19 157.060 33.535 -26.782 1.00 0.00

ATOM 1198 CA PHE B 19 156.090 34.514 -27.248 1.00 0.00

ATOM 1199 C PHE B 19 155.076 33.899 -28.175 1.00 0.00

ATOM 1200 O PHE B 19 153.894 34.144 -27.997 1.00 0.00

ATOM 1201 N ALA B 20 155.541 33.100 -29.155 1.00 0.00

ATOM 1202 CA ALA B 20 154.601 32.474 -30.071 1.00 0.00

ATOM 1203 C ALA B 20 153.595 31.658 -29.306 1.00 0.00

ATOM 1204 O ALA B 20 152.404 31.807 -29.529 1.00 0.00

ATOM 1205 N SER B 21 154.097 30.802 -28.394 1.00 0.00

ATOM 1206 CA SER B 21 153.207 29.959 -27.613 1.00 0.00

ATOM 1207 C SER B 21 152.187 30.768 -26.861 1.00 0.00

ATOM 1208 O SER B 21 151.002 30.528 -27.029 1.00 0.00

ATOM 1209 N PHE B 99 152.652 31.728 -26.034 1.00 0.00

ATOM 1210 CA PHE B 22 151.721 32.520 -25.241 1.00 0.00

ATOM 1211 C PHE B 22 150.684 33.187 -26.101 1.00 0.00

ATOM 1212 O PHE B 99 149.538 33.273 -25.691 1.00 0.00

ATOM 1213 N ILE B 23 151.085 33.659 -27.299 1.00 0.00

ATOM 1214 CA ILE B 23 150.129 34.341 -28.156 1.00 0.00

ATOM 1215 C ILE B 23 149.090 33.385 -28.676 1.00 0.00

ATOM 1216 O ILE B 23 147.925 33.741 -28.726 1.00 0.00

ATOM 1217 N ASP B 24 149.518 32.165 -29.055 1.00 0.00

ATOM 1218 CA ASP B 24 148.555 31.182 -29.520 1.00 0.00

ATOM 1219 C ASP B 24 147.598 30.846 -28.410 1.00 0.00

ATOM 1220 O ASP B 24 146.397 30.842 -28.630 1.00 0.00

ATOM 1221 N LYS B 25 148.151 30.581 -27.209 1.00 0.00

ATOM 1222 CA LYS B 25 147.307 30.260 -26.066 1.00 0.00

ATOM 1223 C LYS B 25 146.310 31.357 -25.809 1.00 0.00

ATOM 1224 O LYS B 25 145.150 31.065 -25.567 1.00 0.00

ATOM 1225 N VAL B 26 146.773 32.621 -25.870 1.00 0.00

ATOM 1226 CA VAL B 26 145.874 33.733 -25.610 1.00 0.00

ATOM 1227 C VAL B 26 144.793 33.816 -26.651 1.00 0.00

ATOM 1228 O VAL B 26 143.666 34.141 -26.312 1.00 0.00

ATOM 1229 N ARG B 27 145.137 33.515 -27.920 1.00 0.00

ATOM 1230 CA ARG B 27 144.125 33.545 -28.963 1.00 0.00

ATOM 1231 C ARG B 27 143.037 32.566 -28.624 1.00 0.00

ATOM 1232 O ARG B 27 141.869 32.919 -28.676 1.00 0.00

ATOM 1233 N PHE B 28 143.438 31.332 -28.257 1.00 0.00

ATOM 1234 CA PHE B 28 142.454 30.330 -27.887 1.00 0.00

ATOM 1235 C PHE B 28 141.608 30.794 -26.733 1.00 0.00

ATOM 1236 O PHE B 28 140.393 30.727 -26.827 1.00 0.00

ATOM 1237 N LEU B 29 142.256 31.267 -25.648 1.00 0.00

ATOM 1238 CA LEU B 29 141.500 31.696 -24.481 1.00 0.00

ATOM 1239 C LEU B 29 140.501 32.760 -24.839 1.00 0.00 ATOM 1240 O LEU B 29 139.410 32.755 -24.295 1.00 0.00

ATOM 1241 N GLU B 30 140.871 33.669 -25.763 1.00 0.00

ATOM 1242 CA GLU B 30 139.939 34.718 -26.142 1.00 0.00

ATOM 1243 C GLU B 30 138.795 34.158 -26.938 1.00 0.00

ATOM 1244 O GLU B 30 137.687 34.657 -26.825 1.00 0.00

ATOM 1245 N GLN B 31 139.064 33.107 -27.738 1.00 0.00

ATOM 1246 CA GLN B 31 137.983 32.481 -28.478 1.00 0.00

ATOM 1247 C GLN B 31 137.019 31.850 -27.512 1.00 0.00

ATOM 1248 O GLN B 31 135.823 32.060 -27.633 1.00 0.00

ATOM 1249 N GLN B 32 137.557 31.082 -26.542 1.00 0.00

ATOM 1250 CA GLN B 32 136.698 30.438 -25.561 1.00 0.00

ATOM 1251 C GLN B 32 135.920 31.452 -24.770 1.00 0.00

ATOM 1252 O GLN B 32 134.761 31.212 -24.466 1.00 0.00

ATOM 1253 N ASN B 33 136.563 32.591 -24.441 1.00 0.00

ATOM 1254 CA ASN B 33 135.865 33.620 -23.683 1.00 0.00

ATOM 1255 C ASN B 33 134.714 34.155 -24.484 1.00 0.00

ATOM 1256 O ASN B 33 133.617 34.256 -23.961 1.00 0.00

ATOM 1257 N LYS B 34 134.979 34.489 -25.763 1.00 0.00

ATOM 1258 CA LYS B 34 133.913 34.995 -26.611 1.00 0.00

ATOM 1259 C LYS B 34 132.746 34.047 -26.621 1.00 0.00

ATOM 1260 O LYS B 34 131.614 34.490 -26.520 1.00 0.00

ATOM 1261 N VAL B 35 133.034 32.734 -26.723 1.00 0.00

ATOM 1262 CA VAL B 35 131.958 31.756 -26.724 1.00 0.00

ATOM 1263 C VAL B 35 131.185 31.797 -25.436 1.00 0.00

ATOM 1264 O VAL B 35 129.964 31.828 -25.476 1.00 0.00

ATOM 1265 N LEU B 36 131.901 31.800 -24.295 1.00 0.00

ATOM 1266 CA LEU B 36 131.212 31.809 -23.014 1.00 0.00

ATOM 1267 C LEU B 36 130.310 33.006 -22.897 1.00 0.00

ATOM 1268 O LEU B 36 129.202 32.870 -22.403 1.00 0.00

ATOM 1269 N ASP B 37 130.791 34.175 -23.364 1.00 0.00

ATOM 1270 CA ASP B 37 129.976 35.376 -23.277 1.00 0.00

ATOM 1271 C ASP B 37 128.696 35.209 -24.048 1.00 0.00

ATOM 1272 O ASP B 37 127.639 35.508 -23.513 1.00 0.00

ATOM 1273 N THR B 38 128.789 34.717 -25.300 1.00 0.00

ATOM 1274 CA THR B 38 127.579 34.497 -26.077 1.00 0.00

ATOM 1275 C THR B 38 126.634 33.603 -25.322 1.00 0.00

ATOM 1276 O THR B 38 125.475 33.956 -25.171 1.00 0.00

ATOM 1277 N LYS B 39 127.144 32.453 -24.835 1.00 0.00

ATOM 1278 CA LYS B 39 126.291 31.527 -24.103 1.00 0.00

ATOM 1279 C LYS B 39 125.638 32.177 -22.913 1.00 0.00

ATOM 1280 O LYS B 39 124.455 31.968 -22.694 1.00 0.00

ATOM 1281 N TRP B 40 126.416 32.965 -22.146 1.00 0.00

ATOM 1282 CA TRP B 40 125.873 33.581 -20.945 1.00 0.00

ATOM 1283 C TRP B 40 124.795 34.577 -21.274 1.00 0.00

ATOM 1284 O TRP B 40 123.844 34.694 -20.519 1.00 0.00

ATOM 1285 N THR B 41 124.940 35.289 -22.410 1.00 0.00

ATOM 1286 CA THR B 41 123.909 36.242 -22.783 1.00 0.00

ATOM 1287 C THR B 41 122.630 35.512 -23.074 1.00 0.00

ATOM 1288 O THR B 41 121.596 35.876 -22.539 1.00 0.00

ATOM 1289 N LEU B 42 122.720 34.472 -23.929 1.00 0.00

ATOM 1290 CA LEU B 42 121.523 33.735 -24.295 1.00 0.00

ATOM 1291 C LEU B 42 120.857 33.169 -23.077 1.00 0.00

ATOM 1292 O LEU B 42 119.693 33.458 -22.847 1.00 0.00

ATOM 1293 N LEU B 43 121.610 32.370 -22.293 1.00 0.00

ATOM 1294 CA LEU B 43 121.045 31.822 -21.072 1.00 0.00

ATOM 1295 C LEU B 43 120.486 32.931 -20.226 1.00 0.00

ATOM 1296 O LEU B 43 119.286 32.985 -20.005 1.00 0.00

TER 1297 LEU B 43

ATOM 1298 N GLU B 1 104.875 26.869 -20.649 1.00 0.00

ATOM 1299 CA GLU B 1 104.067 28.084 -20.667 1.00 0.00

ATOM 1300 C GLU B 1 102.867 27.955 -21.612 1.00 0.00

ATOM 1301 O GLU B 1 101.745 27.739 -21.158 1.00 0.00

ATOM 1302 N PRO B 9 103.098 28.087 -22.923 1.00 0.00

ATOM 1303 CA PRO B 2 102.009 27.990 -23.901 1.00 0.00

ATOM 1304 C PRO B 9 101.072 26.853 -23.501 1.00 0.00

ATOM 1305 O PRO B 2 99.873 26.860 -23.812 1.00 0.00

ATOM 1306 N LEU B 3 101.645 25.887 -22.787 1.00 0.00

ATOM 1307 CA LEU B 3 100.891 24.749 -22.299 1.00 0.00 ATOM 1308 C LEU B 3 99.874 25.215 -21.284 1.00 0.00

ATOM 1309 O LEU B 3 98.671 25.175 -21.532 1.00 0.00

ATOM 1310 N PHE B 4 100.344 25.677 -20.132 1.00 0.00

ATOM 1311 CA PHE B 4 99.413 26.143 -19.128 1.00 0.00

ATOM 1312 C PHE B 4 98.432 27.182 -19.649 1.00 0.00

ATOM 1313 O PHE B 4 97.335 27.313 -19.115 1.00 0.00

ATOM 1314 N GLU B 5 98.799 27.925 -20.689 1.00 0.00

ATOM 1315 CA GLU B 5 97.858 28.905 -21.220 1.00 0.00

ATOM 1316 C GLU B 5 96.753 28.133 -21.909 1.00 0.00

ATOM 1317 O GLU B 5 95.613 28.578 -21.965 1.00 0.00

ATOM 1318 N GLN B 6 97.097 26.974 -22.450 1.00 0.00

ATOM 1319 CA GLN B 6 96.088 26.171 -23.111 1.00 0.00

ATOM 1320 C GLN B 6 95.109 25.651 -22.061 1.00 0.00

ATOM 1321 O GLN B 6 93.893 25.738 -22.224 1.00 0.00

ATOM 1322 N TYR B 7 95.660 25.095 -20.986 1.00 0.00

ATOM 1323 CA TYR B 7 94.862 24.576 -19.882 1.00 0.00

ATOM 1324 C TYR B 7 93.904 25.666 -19.362 1.00 0.00

ATOM 1325 O TYR B 7 92.677 25.494 -19.379 1.00 0.00

ATOM 1326 N ILE B 8 94.409 26.733 -19.261 1.00 0.00

ATOM 1327 CA ILE B 8 93.718 27.946 -18.831 1.00 0.00

ATOM 1328 C ILE B 8 92.484 28.233 -19.695 1.00 0.00

ATOM 1329 O ILE B 8 91.360 27.966 -19.273 1.00 0.00

ATOM 1330 N ASN B 9 92.689 28.776 -20.900 1.00 0.00

ATOM 1331 CA ASN B 9 91.569 29.097 -21.791 1.00 0.00

ATOM 1332 C ASN B 9 90.541 27.968 -21.734 1.00 0.00

ATOM 1333 O ASN B 9 89.340 28.172 -21.955 1.00 0.00

ATOM 1334 N ASN B 10 91.040 26.777 -21.413 1.00 0.00

ATOM 1335 CA ASN B 10 90.200 25.605 -21.286 1.00 0.00

ATOM 1336 C ASN B 10 89.261 25.783 -20.115 1.00 0.00

ATOM 1337 O ASN B 10 88.053 25.924 -20.292 1.00 0.00

ATOM 1338 N LEU B 11 89.804 25.797 -18.906 1.00 0.00

ATOM 1339 CA LEU B 11 88.948 25.972 -17.752 1.00 0.00

ATOM 1340 C LEU B 11 88.055 27.199 -17.844 1.00 0.00

ATOM 1341 O LEU B 11 86.990 27.231 -17.233 1.00 0.00

ATOM 1342 N ARG B 12 88.458 28.216 -18.599 1.00 0.00

ATOM 1343 CA ARG B 12 87.599 29.386 -18.723 1.00 0.00

ATOM 1344 C ARG B 12 86.408 28.978 -19.561 1.00 0.00

ATOM 1345 O ARG B 12 85.312 29.503 -19.402 1.00 0.00

ATOM 1346 N ARG B 13 86.626 28.042 -20.475 1.00 0.00

ATOM 1347 CA ARG B 13 85.528 27.587 -21.303 1.00 0.00

ATOM 1348 C ARG B 13 84.536 26.826 -20.428 1.00 0.00

ATOM 1349 O ARG B 13 83.329 27.056 -20.483 1.00 0.00

ATOM 1350 N GLN B 14 85.064 25.901 -19.630 1.00 0.00

ATOM 1351 CA GLN B 14 84.252 25.108 -18.715 1.00 0.00

ATOM 1352 C GLN B 14 83.414 26.032 -17.810 1.00 0.00

ATOM 1353 O GLN B 14 82.177 25.973 -17.811 1.00 0.00

ATOM 1354 N LEU B 15 84.092 26.895 -17.050 1.00 0.00

ATOM 1355 CA LEU B 15 83.398 27.840 -16.165 1.00 0.00

ATOM 1356 C LEU B 15 82.316 28.570 -16.961 1.00 0.00

ATOM 1357 O LEU B 15 81.218 28.811 -16.470 1.00 0.00

ATOM 1358 N ASP B 16 82.634 28.911 -18.197 1.00 0.00

ATOM 1359 CA ASP B 16 81.693 29.609 -19.051 1.00 0.00

ATOM 1360 C ASP B 16 80.357 28.886 -19.234 1.00 0.00

ATOM 1361 O ASP B 16 79.283 29.359 -18.826 1.00 0.00

ATOM 1362 N SER B 17 80.424 27.729 -19.868 1.00 0.00

ATOM 1363 CA SER B 17 79.210 26.993 -20.117 1.00 0.00

ATOM 1364 C SER B 17 78.475 26.753 -18.801 1.00 0.00

ATOM 1365 O SER B 17 77.252 26.795 -18.768 1.00 0.00

ATOM 1366 N ILE B 18 79.207 26.529 -17.711 1.00 0.00

ATOM 1367 CA ILE B 18 78.556 26.297 -16.425 1.00 0.00

ATOM 1368 C ILE B 18 77.819 27.499 -15.807 1.00 0.00

ATOM 1369 O ILE B 18 76.811 27.320 -15.124 1.00 0.00

ATOM 1370 N VAL B 19 78.295 28.722 -16.007 1.00 0.00

ATOM 1371 CA VAL B 19 77.520 29.824 -15.452 1.00 0.00

ATOM 1372 C VAL B 19 76.242 29.891 -16.284 1.00 0.00

ATOM 1373 O VAL B 19 75.175 30.222 -15.775 1.00 0.00

ATOM 1374 N GLY B 20 76.345 29.551 -17.567 1.00 0.00

ATOM 1375 CA GLY B 20 75.193 29.541 -18.472 1.00 0.00 ATOM 1376 C GLY B 20 74.131 28.541 -17, 942 .00 0.00

ATOM 1377 O GLY B 20 72.945 28.871 -17, 770 .00 0.00

ATOM 1378 N GLU B 21 74.578 27.323 -17, 663 .00 0.00

ATOM 1379 CA GLU B 21 73.711 26.276 -17, 129 .00 0.00

ATOM 1380 C GLU B 21 73.022 26.766 -15, 873 .00 0.00

ATOM 1381 O GLU B 21 71.819 26.591 -15, 706 .00 0.00

ATOM 1382 N ARG B 99 73.802 27.366 -14, 979 .00 0.00

ATOM 1383 CA ARG B 22 73.237 27.876 -13, 747 .00 0.00

ATOM 1384 C ARG B 22 .146 28 924 -14, 013 .00 0.00

ATOM 1385 O ARG B 99 71.148 28.956 -13, 300 .00 0.00

ATOM 1386 N GLY B 23 72.315 29.769 -15, 032 .00 0.00

ATOM 1387 CA GLY B 23 71.292 30.774 -15, 341 .00 0.00

ATOM 1388 C GLY B 23 70.002 30.059 -15, 686 .00 0.00

ATOM 1389 O GLY B 23 68.899 30.459 -15, 297 .00 0.00

ATOM 1390 N ARG B 24 70.171 28.973 -16, 422 .00 0.00

ATOM 1391 CA ARG B 24 69.059 28.163 -16, 844 .00 0.00

ATOM 1392 C ARG B 24 68.322 27.485 -15.716 .00 0.00

ATOM 1393 O ARG B 24 67.098 27.506 -15.696 .00 0.00

ATOM 1394 N LEU B 25 69.046 26. -14.779 .00 0.00

ATOM 1395 CA LEU B 25 68.400 26.222 -13.653 .00 0.00

ATOM 1396 C LEU B 25 67.628 27.221 -12.834 .00 0.00

ATOM 1397 O LEU B 25 66.552 26.925 -12.320 1..00 0.00

ATOM 1398 N ASP B 26 68.197 28.403 -12.689 1..00 0.00

ATOM 1399 CA ASP B 26 67.542 29.443 -11.920 1..00 0.00

ATOM 1400 C ASP B 26 66.237 29.831 -12.558 1.00 0.00

ATOM 1401 O ASP B 26 65.256 30.162 -11.903 1.00 0.00

ATOM 1402 N SER B 27 66.267 29. .834 -13.869 1.00 0.00

ATOM 1403 CA SER B 27 65.117 30. 109 -14.636 1.00 0.00

ATOM 1404 C SER B 27 64.050 29.111 -14.537 1.00 0.00

ATOM 1405 O SER B 27 62.868 29.397 -14.249 1.00 0.00

ATOM 1406 N GLU B 28 64.453 27.861 -14.751 1..00 0.00

ATOM 1407 CA GLU B 28 63.470 26.782 -14.669 1..00 0.00

ATOM 1408 C GLU B 28 62.847 26.749 -13.297 1.00 0.00

ATOM 1409 O GLU B 28 61.651 26.556 - 13.165 1.00 0.00

ATOM 1410 N LEU B 29 63.677 26.949 - 12.282 1.00 0.00

ATOM 1411 CA LEU B 29 63.230 26.948 - 10.901 1.00 0.00

ATOM 1412 C LEU B 29 62.170 28.035 - 10.698 1.00 0.00

ATOM 1413 O LEU B 29 61.095 27.779 - 10.145 1.00 0.00

ATOM 1414 N ARG B 30 62.465 9.241 -11.153 1..00 0.00

ATOM 1415 CA ARG B 30 61.516 30.316 11.010 1..00 0.00

ATOM 1416 C ARG B 30 60.183 29.935 -11 . 640 1.00 0.00

ATOM 1417 O ARG B 30 59.132 30.103 -11 . 023 1.00 0.00

ATOM 1418 N ASN B 31 60.221 29.375 -12 . 847 1.00 0.00

ATOM 1419 CA ASN B 31 58.974 28.985 -13 . 499 1.00 0.00

ATOM 1420 C ASN B 31 58.219 27.960 -12 . 658 1.00 0.00

ATOM 1421 O ASN B 31 56.996 27.999 . 551 1.00 0.00

ATOM 1422 N MET B 32 58.955 11 . 031 -12 . 067 1..00 0.00

ATOM 1423 CA MET B 32 58.323 26 . 017 -11 . 261 1..00 0.00

ATOM 1424 C MET B 32 57.674 26 . 636 -10 . 057 1..00 0.00

ATOM 1425 O MET B 32 56.521 26.347 - 9. 746 1.00 0.00

ATOM 1426 N GLN B 33 58.409 27.484 -9.364 1.00 0.00

ATOM 1427 CA GLN B 33 57.841 28.114 -8.191 1.00 0.00

ATOM 1428 C GLN B 33 56.565 28.894 -8.493 1.00 0.00

ATOM 1429 O GLN B 33 55.617 28.852 -7.717 1.00 0.00

ATOM 1430 N ASP B 34 56.527 29.589 -9.632 1.00 0.00

ATOM 1431 CA ASP B 34 55.349 30.372 -10.013 1..00 0.00

ATOM 1432 C ASP B 34 54.190 29.408 -10.239 1..00 0.00

ATOM 1433 O ASP B 34 53.069 29.613 -9.776 1.00 0.00

ATOM 1434 N LEU B 35 54.492 28.359 -10.976 1.00 0.00

ATOM 1435 CA LEU B 35 53.537 27.315 -11.247 1.00 0.00

ATOM 1436 C LEU B 35 52.938 26.860 -9.919 1.00 0.00

ATOM 1437 O LEU B 35 51.719 26.870 -9.732 1.00 0.00

ATOM 1438 N VAL B 36 53.815 26.453 -9.007 1.00 0.00

ATOM 1439 CA VAL B 36 53.415 25.991 -7.677 00 0.00

ATOM 1440 C VAL B 36 52.459 26.969 -7.008 00 0.00

ATOM 1441 O VAL B 36 51.424 26.561 -6.494 00 0.00

ATOM 1442 N GLU B 37 52.793 28.257 -7.007 00 0.00

ATOM 1443 CA GLU B 37 51.908 29.233 -6.382 1.00 0.00 ATOM 1444 C GLU B 37 50.522 29.155 -7.029 1.00 0.00

ATOM 1445 O GLU B 37 49.499 29.036 -6.342 1.00 0.00

ATOM 1446 N ASP B 38 50.487 29.225 -8.354 1.00 0.00

ATOM 1447 CA ASP B 38 49.225 29.147 -9.079 1.00 0.00

ATOM 1448 C ASP B 38 48.421 27.906 -8.702 1.00 0.00

ATOM 1449 O ASP B 38 47.289 28.041 -8.235 1.00 0.00

ATOM 1450 N PHE B 39 48.995 26.716 -8.889 1.00 0.00

ATOM 1451 CA PHE B 39 48.287 25.482 -8.548 1.00 0.00

ATOM 1452 C PHE B 39 47.795 25.473 -7.125 1.00 0.00

ATOM 1453 O PHE B 39 46.715 24.961 -6.863 1.00 0.00

ATOM 1454 N LYS B 40 48.554 26.031 -6.201 1.00 0.00

ATOM 1455 CA LYS B 40 48.093 26.041 -4.821 1.00 0.00

ATOM 1456 C LYS B 40 46.905 26.971 -4.601 1.00 0.00

ATOM 1457 O LYS B 40 45.984 26.645 -3.856 1.00 0.00

ATOM 1458 N ASN B 41 46.921 28.113 -5.270 1.00 0.00

ATOM 1459 CA ASN B 41 45.820 29.054 -5.175 1.00 0.00

ATOM 1460 C ASN B 41 44.574 28.375 -5.746 1.00 0.00

ATOM 1461 O ASN B 41 43.514 28.370 -5.112 1.00 0.00

ATOM 1462 N LYS B 42 44.731 27.802 -6.938 1.00 0.00

ATOM 1463 CA LYS B 42 43.654 27.118 -7.649 1.00 0.00

ATOM 1464 C LYS B 42 43.072 26.027 -6.770 1.00 0.00

ATOM 1465 O LYS B 42 41.860 25.907 -6.646 1.00 0.00

ATOM 1466 N TYR B 43 43.946 25.239 -6.146 1.00 0.00

ATOM 1467 CA TYR B 43 43.487 24.181 -5.260 1.00 0.00

ATOM 1468 C TYR B 43 42.747 24.713 -4.041 1.00 0.00

ATOM 1469 O TYR B 43 41.800 24.087 -3.572 1.00 0.00

ATOM 1470 N GLU B 44 43.180 25.855 -3.513 1.00 0.00

ATOM 1471 CA GLU B 44 42.518 26.439 -2.353 1.00 0.00

ATOM 1472 C GLU B 44 41.090 26.753 -2.775 1.00 0.00

ATOM 1473 O GLU B 44 40.130 26.387 -2.094 1.00 0.00

ATOM 1474 N ASP B 45 40.952 27.427 -3.908 1.00 0.00

ATOM 1475 CA ASP B 45 39.627 27.763 -4.418 1.00 0.00

ATOM 1476 C ASP B 45 38.786 26.510 -4.563 1.00 0.00

ATOM 1477 O ASP B 45 37.672 26.450 -4.055 1.00 0.00

ATOM 1478 N GLU B 46 39.310 25.509 -5.271 1.00 0.00

ATOM 1479 CA GLU B 46 38.530 24.296 -5.502 1.00 0.00

ATOM 1480 C GLU B 46 38.099 23.647 -4.215 1.00 0.00

ATOM 1481 O GLU B 46 37.032 23.047 -4.156 1.00 0.00

ATOM 1482 N ILE B 47 38.918 23.740 -3.188 1.00 0.00

ATOM 1483 CA ILE B 47 38.536 23.131 -1.933 1.00 0.00

ATOM 1484 C ILE B 47 37.462 23.944 -1.261 1.00 0.00

ATOM 1485 O ILE B 47 36.639 23.403 -0.535 1.00 0.00

ATOM 1486 N ASN B 48 37.470 25.249 -1.495 1.00 0.00

ATOM 1487 CA ASN B 48 36.465 26.117 -0.906 1.00 0.00

ATOM 1488 C ASN B 48 35.140 25.760 -1.564 1.00 0.00

ATOM 1489 O ASN B 48 34.128 25.543 -0.886 1.00 0.00

ATOM 1490 N LYS B 49 35.158 25.683 -2.891 1.00 0.00

ATOM 1491 CA LYS B 49 33.951 25.359 -3.649 1.00 0.00

ATOM 1492 C LYS B 49 33.417 23.986 -3.283 1.00 0.00

ATOM 1493 O LYS B 49 32.211 23.805 -3.215 1.00 0.00

ATOM 1494 N ARG B 50 34.318 23.034 -3.049 1.00 0.00

ATOM 1495 CA ARG B 50 33.951 21.665 -2.688 1.00 0.00

ATOM 1496 C ARG B 50 33.269 21.718 -1.311 1.00 0.00

ATOM 1497 O ARG B 50 32.178 21.185 -1.133 1.00 0.00

ATOM 1498 N THR B 51 33.900 22.378 -0.348 1.00 0.00

ATOM 1499 CA THR B 51 33.314 22 523 0.986 1.00 0.00

ATOM 1500 C THR B 51 31.862 23.058 0.861 1.00 0.00

ATOM 1501 O THR B 51 30.939 22.548 1.497 1.00 0.00

ATOM 1502 N THR B 52 31.668 24.081 0.029 1.00 0.00

ATOM 1503 CA THR B 52 30.341 24.666 -0.178 1.00 0.00

ATOM 1504 C THR B 52 29.372 23.643 -0.746 1.00 0.00

ATOM 1505 O THR B 52 28.259 23.487 -0.242 1.00 0.00

ATOM 1506 N ALA B 53 29.789 22.952 -1.800 1.00 0.00

ATOM 1507 CA ALA B 53 28.915 21.949 -2.391 1.00 0.00

ATOM 1508 C ALA B 53 28.501 20.897 -1.386 1.00 0.00

ATOM 1509 O ALA B 53 27.343 20.486 -1.378 1.00 0.00

ATOM 1510 N GLU B 54 29.431 20.465 -0.539 1.00 0.00

ATOM 1511 CA GLU B 54 29.106 19.455 0.453 1.00 0.00 ATOM 1512 C GLU B 54 28.059 19.986 1.423 .00 0.00

ATOM 1513 O GLU B 54 27.061 19.323 1.687 .00 0.00

ATOM 1514 N ASN B 55 28.249 21.194 1.935 .00 0.00

ATOM 1515 CA ASN B 55 27.241 21.731 2.832 .00 0.00

ATOM 1516 C ASN B 55 25.888 21.718 2.111 .00 0.00

ATOM 1517 O ASN B 55 24.907 21.195 2.634 .00 0.00

ATOM 1518 N GLU B 56 25.835 22.264 0.903 .00 0.00

ATOM 1519 CA GLU B 56 24.576 22.304 0.157 .00 0.00

ATOM 1520 C GLU B 56 23.935 20.929 -0.033 .00 0.00

ATOM 1521 O GLU B 56 22.722 20.779 0.121 .00 0.00

ATOM 1522 N PHE B 57 24.750 19.937 -0.383 .00 0.00

ATOM 1523 CA PHE B 57 24.257 18.577 -0.595 .00 0.00

ATOM 1524 C PHE B 57 23.706 17.970 0.675 .00 0.00

ATOM 1525 O PHE B 57 22.771 17.181 0.635 .00 0.00

ATOM 1526 N VAL B 58 24.295 18.317 1.808 .00 0.00

ATOM 1527 CA VAL B 58 23.815 17.755 3.054 .00 0.00

ATOM 1528 C VAL B 58 22.424 18.307 3.315 .00 0.00

ATOM 1529 O VAL B 58 21.476 17.567 3.574 .00 0.00

ATOM 1530 N MET B 59 22.308 19.624 225 .00 0.00

ATOM 1531 CA MET B 59 21.050 20.303 440 1.00 0.00

ATOM 1532 C MET B 59 19.971 19.717 541 1.00 0.00

ATOM 1533 O MET B 59 18.967 19.162 007 1..00 0.00

ATOM 1534 N LEU B 60 20.186 19.855 242 1..00 0.00

ATOM 1535 CA LEU B 60 19.220 19.361 0.289 1..00 0.00

ATOM 1536 C LEU B 60 18.861 17.925 0.640 1.00 0.00

ATOM 1537 O LEU B 60 17.683 17.588 0.672 1.00 0.00

ATOM 1538 N LYS B 61 19.845 17.084 0.943 1.00 0.00

ATOM 1539 CA LYS B 61 19.531 15.701 1.297 1.00 0.00

ATOM 1540 C LYS B 61 18.556 15.616 2.468 1.00 0.00

ATOM 1541 O LYS B 61 17.597 14.835 2.424 1.00 0.00

ATOM 1542 N LYS B 62 18.800 16.408 3.518 1..00 0.00

ATOM 1543 CA LYS B 62 17.900 16.411 4.677 1..00 0.00

ATOM 1544 C LYS B 62 16.513 16.691 4.134 1.00 0.00

ATOM 1545 O LYS B 62 15.604 15.891 4.286 1.00 0.00

ATOM 1546 N ASP B 63 16.373 17.835 3.484 1.00 0.00

ATOM 1547 CA ASP B 63 15.112 18.253 2.904 1.00 0.00

ATOM 1548 C ASP B 63 14.419 17.173 2.079 1.00 0.00

ATOM 1549 O ASP B 63 13.219 16.933 2.232 1.00 0.00

ATOM 1550 N VAL B 64 15.169 16.530 1.200 1..00 0.00

ATOM 1551 CA VAL B 64 14.578 15.497 0.379 1..00 0.00

ATOM 1552 C VAL B 64 13.952 14.463 1.292 1.00 0.00

ATOM 1553 O VAL B 64 12.844 14.002 1 050 1.00 0.00

ATOM 1554 N ASP B 65 14.668 14.111 2.355 1.00 0.00

ATOM 1555 CA ASP B 65 14.174 13.106 3.285 1.00 0.00

ATOM 1556 C ASP B 65 12.891 13.535 3.994 1.00 0.00

ATOM 1557 O ASP B 65 11.893 12.807 4.022 1.00 0.00

ATOM 1558 N ALA B 66 12.916 14.717 4.574 1..00 0.00

ATOM 1559 CA ALA B 66 11.731 15.219 5.244 1..00 0.00

ATOM 1560 C ALA B 66 10.516 15.292 .326 1..00 0.00

ATOM 1561 O ALA B 66 9.435 14.846 .684 1.00 0.00

ATOM 1562 N ALA B 67 10.685 15.863 .136 1.00 0.00

ATOM 1563 CA ALA B 67 9.568 15.960 101 1.00 0.00

ATOM 1564 C ALA B 67 9.115 14.558 .798 1.00 0.00

ATOM 1565 O ALA B 67 7.943 14.339 1.511 1.00 0.00

ATOM 1566 N TYR B 68 10.030 13.598 1.764 1.00 0.00

ATOM 1567 CA TYR B 68 9.613 12.256 1.394 1..00 0.00

ATOM 1568 C TYR B 68 8.738 11.691 2.529 1..00 0.00

ATOM 1569 O TYR B 68 7.692 11.094 2.270 1.00 0.00

ATOM 1570 N MET B 69 9.137 11.885 3.783 1.00 0.00

ATOM 1571 CA MET B 69 8.286 11.393 4.870 1.00 0.00

ATOM 1572 C MET B 69 6.894 12.038 4.753 1.00 0.00

ATOM 1573 O MET B 69 5.878 11.344 4.745 1.00 0.00

ATOM 1574 N ASN B 70 6.847 13.363 4.656 00 0.00

ATOM 1575 CA ASN B 70 5.583 14.080 4.533 00 0.00

ATOM 1576 C ASN B 70 4.717 13.502 3.426 00 0.00

ATOM 1577 O ASN B 70 3.507 13.316 3.592 00 0.00

ATOM 1578 N LYS B 71 5.339 13.209 2.284 00 0.00

ATOM 1579 CA LYS B 71 4.574 12.680 1.169 1.00 0.00 ATOM 1580 C LYS B 71 4.033 11.294 1.469 1.00 0.00

ATOM 1581 O LYS B 71 2.882 10.999 1.166 1.00 0.00

ATOM 1582 N VAL B 72 4.829 10.445 2.095 1.00 0.00

ATOM 1583 CA VAL B 72 4.332 9.122 2.409 1.00 0.00

ATOM 1584 C VAL B 72 3.185 9.170 3.432 1.00 0.00

ATOM 1585 O VAL B 72 2.190 8.441 3.320 1.00 0.00

ATOM 1586 N GLU B 73 3.315 10.063 4.406 1.00 0.00

ATOM 1587 CA GLU B 73 2.280 10.224 5.417 1.00 0.00

ATOM 1588 C GLU B 73 0.995 10.607 4.702 1.00 0.00

ATOM 1589 O GLU B 73 -0.076 10.082 5.007 1.00 0.00

ATOM 1590 N LEU B 74 1.098 11.523 3.748 1.00 0.00

ATOM 1591 CA LEU B 74 -0.094 11.935 3.021 1.00 0.00

ATOM 1592 C LEU B 74 -0.658 10.813 2.147 1.00 0.00

ATOM 1593 O LEU B 74 -1.871 10.639 2.074 1.00 0.00

ATOM 1594 N GLU B 75 0.185 10.026 1.490 1.00 0.00

ATOM 1595 CA GLU B 75 -0.382 8.962 0.661 1.00 0.00

ATOM 1596 C GLU B 75 -1.231 8.042 1.519 1.00 0.00

ATOM 1597 O GLU B 75 -2.307 7.597 1.116 1.00 0.00

ATOM 1598 N ALA B 76 -0.750 7.782 2.722 1.00 0.00

ATOM 1599 CA ALA B 76 -1.467 6.922 3.645 1.00 0.00

ATOM 1600 C ALA B 76 -2.764 7.584 4.069 1.00 0.00

ATOM 1601 O ALA B 76 -3.844 6.983 4.006 1.00 0.00

ATOM 1602 N LYS B 77 -2.653 8.820 4.502 1.00 0.00

ATOM 1603 CA LYS B 77 -3.823 9.533 4.957 1.00 0.00

ATOM 1604 C LYS B 77 -4.907 9.577 3.899 1.00 0.00

ATOM 1605 O LYS B 77 -6.086 9.334 4.169 1.00 0.00

ATOM 1606 N VAL B 78 -4.480 9.873 2.680 1.00 0.00

ATOM 1607 CA VAL B 78 -5.387 9.941 1.557 1.00 0.00

ATOM 1608 C VAL B 78 -6.058 8.570 1.313 1.00 0.00

ATOM 1609 O VAL B 78 -7.277 8.488 1.174 1.00 0.00

ATOM 1610 N ASP B 79 -5.293 7.487 1.268 1.00 0.00

ATOM 1611 CA ASP B 79 -5.934 6.185 1.093 1.00 0.00

ATOM 1612 C ASP B 79 -6.983 5.929 2.190 1.00 0.00

ATOM 1613 O ASP B 79 -8.100 5.482 1.901 1.00 0.00

ATOM 1614 N ALA B 80 -6.639 6.197 3.446 1.00 0.00

ATOM 1615 CA ALA B 80 -7.600 5.931 4.515 1.00 0.00

ATOM 1616 C ALA B 80 -8.869 6.701 4.306 1.00 0.00

ATOM 1617 O ALA B 80 -9.958 6.163 4.449 1.00 0.00

ATOM 1618 N LEU B 81 -8.706 7.971 3.958 1.00 0.00

ATOM 1619 CA LEU B 81 -9.846 8.834 3.739 1.00 0.00

ATOM 1620 C LEU B 81 -10.696 8.363 2.575 1.00 0.00

ATOM 1621 O LEU B 81 -11.925 8.335 2.673 1.00 0.00

ATOM 1622 N MET B 82 -10.045 7.988 1.479 1.00 0.00

ATOM 1623 CA MET B 82 -10.766 7.523 0.305 1.00 0.00

ATOM 1624 C MET B 82 -11.570 6.284 0.603 1.00 0.00

ATOM 1625 O MET B 82 -12.700 6.136 0.140 1.00 0.00

ATOM 1626 N ASP B 83 -10.994 5.400 1.400 1.00 0.00

ATOM 1627 CA ASP B 83 -11.676 4.184 1.793 1.00 0.00

ATOM 1628 C ASP B 83 -12.898 4.534 2.648 1.00 0.00

ATOM 1629 O ASP B 83 -13.983 3.993 2.436 1.00 0.00

ATOM 1630 N GLU B 84 -12.738 5.446 3.599 1.00 0.00

ATOM 1631 CA GLU B 84 -13.884 5.815 4.421 1.00 0.00

ATOM 1632 C GLU B 84 -14.966 6.450 3.591 1.00 0.00

ATOM 1633 O GLU B 84 -16.148 6.187 3.793 1.00 0.00

ATOM 1634 N ILE B 85 -14.559 7.283 2.649 1.00 0.00

ATOM 1635 CA ILE B 85 -15.517 7.924 1.770 1.00 0.00

ATOM 1636 C ILE B 85 -16.307 6.852 0.997 1.00 0.00

ATOM 1637 O ILE B 85 -17.531 6.923 0.901 1.00 0.00

ATOM 1638 N ASN B 86 -15.614 5.844 0.464 1.00 0.00

ATOM 1639 CA ASN B 86 -16.284 4.775 -0.286 1.00 0.00

ATOM 1640 C ASN B 86 -17.289 4.035 0.598 1.00 0.00

ATOM 1641 O ASN B 86 -18.414 3.765 0.184 1.00 0.00

ATOM 1642 N PHE B 87 -16.874 3.700 1.806 1.00 0.00

ATOM 1643 CA PHE B 87 -17.776 3.033 2.719 1.00 0.00

ATOM 1644 C PHE B 87 -18.980 3.938 3.020 1.00 0.00

ATOM 1645 O PHE B 87 -20.100 3.451 3.147 1.00 0.00

ATOM 1646 N MET B 88 -18.757 5.249 3.101 1.00 0.00

ATOM 1647 CA MET B 88 -19.866 6.158 3.366 1.00 0.00 ATOM 1648 C MET B 88 20.789 6.291 2.182 1.00 0.00

ATOM 1649 O MET B 88 21.986 6.451 2.374 1.00 0.00

ATOM 1650 N LYS B 89 20.269 6.231 0.959 1.00 0.00

ATOM 1651 CA LYS B 89 21.173 6.349 -0.178 1.00 0.00

ATOM 1652 C LYS B 89 22.094 5.158 -0.136 1.00 0.00

ATOM 1653 O LYS B 89 23.289 5.289 -0.352 1.00 0.00

ATOM 1654 N MET B 90 21.528 3.991 0.160 1.00 0.00

ATOM 1655 CA MET B 90 99 Q 9 q 2.780 0.253 1.00 0.00

ATOM 1656 C MET B 90 23.393 2.914 1.336 1.00 0.00

ATOM 1657 O MET B 90 24.579 2.706 1.084 1.00 0.00

ATOM 1658 N PHE B 91 22.971 3.263 2.542 1.00 0.00

ATOM 1659 CA PHE B 91 23.901 3.430 3.651 1.00 0.00

ATOM 1660 C PHE B 91 25.004 4.398 3.253 1.00 0.00

ATOM 1661 O PHE B 91 26.190 4.158 3.511 1.00 0.00

ATOM 1662 N PHE B 92 24.597 5.506 2.643 1.00 0.00

ATOM 1663 CA PHE B 92 25.546 6.515 2.214 1.00 0.00

ATOM 1664 C PHE B 92 26.593 5.835 1.355 1.00 0.00

ATOM 1665 O PHE B 92 27.761 5.786 1.730 1.00 0.00

ATOM 1666 N ASP B 93 26.177 5.295 0.213 1.00 0.00

ATOM 1667 CA ASP B 93 27.101 4.596 -0.679 1.00 0.00

ATOM 1668 C ASP B 93 28.066 3.724 0.123 1.00 0.00

ATOM 1669 O ASP B 93 29.287 3.866 0.024 1.00 0.00

ATOM 1670 N ALA B 94 27.508 2.825 0.925 1.00 0.00

ATOM 1671 CA ALA B 94 28.314 1.937 1.751 1.00 0.00

ATOM 1672 C ALA B 94 29.420 2.699 2.483 1.00 0.00

ATOM 1673 O ALA B 94 30.566 2.259 2.540 1.00 0.00

ATOM 1674 N GLU B 95 29.070 3.852 3.036 1.00 0.00

ATOM 1675 CA GLU B 95 30.026 4.652 3.779 1.00 0.00

ATOM 1676 C GLU B 95 31.047 5.370 2.913 1.00 0.00

ATOM 1677 O GLU B 95 32.227 5.426 3.272 1.00 0.00

ATOM 1678 N LEU B 96 30.621 5.938 1.789 1.00 0.00

ATOM 1679 CA LEU B 96 31.619 6.623 0.982 1.00 0.00

ATOM 1680 C LEU B 96 32.565 5.580 0.444 1.00 0.00

ATOM 1681 O LEU B 96 33.704 5.883 0.107 1.00 0.00

ATOM 1682 N SER B 97 32.113 4.333 0.403 1.00 0.00

ATOM 1683 CA SER B 97 33.025 3.328 -0.076 1.00 0.00

ATOM 1684 C SER B 97 33.965 2.869 1.003 1.00 0.00

ATOM 1685 O SER B 97 35.126 2.583 0.728 1.00 0.00

ATOM 1686 N GLN B 98 33.484 2.797 2.236 1.00 0.00

ATOM 1687 CA GLN B 98 34.376 2.403 3.307 1.00 0.00

ATOM 1688 C GLN B 98 35.442 3.461 3.483 1.00 0.00

ATOM 1689 O GLN B 98 36.564 3.160 3.892 1.00 0.00

ATOM 1690 N MET B 99 35.094 4.705 3.173 1.00 0.00

ATOM 1691 CA MET B 99 36.057 5.788 3.254 1.00 0.00

ATOM 1692 C MET B 99 37.072 5.459 2.147 1.00 0.00

ATOM 1693 O MET B 99 38.253 5.272 2.422 1.00 0.00

ATOM 1694 N GLN B 100 36.717 5.412 0.895 1.00 0.00

ATOM 1695 CA GLN B 100 37.744 5.171 -0.117 1.00 0.00

ATOM 1696 C GLN B 100 38.730 4.106 0.360 1.00 0.00

ATOM 1697 O GLN B 100 39.938 4.337 0.426 1.00 0.00

ATOM 1698 N THR B 101 38.201 2.935 0.698 1.00 0.00

ATOM 1699 CA THR B 101 39.028 1.837 1.176 1.00 0.00

ATOM 1700 C THR B 101 40.025 2.304 2.239 1.00 0.00

ATOM 1701 O THR B 101 41.198 1.937 2.214 1.00 0.00

TER 1702 THR B 101

ATOM 1703 N ASP B 1 55.222 -1.786 4.294 1.00 0.00

ATOM 1704 CA ASP B 1 56.095 -2.631 5.101 1.00 0.00

ATOM 1705 C ASP B 1 57.125 -1.818 5.876 1.00 0.00

ATOM 1706 O ASP B 1 58.325 -2.036 5.695 1.00 0.00

ATOM 1707 N LEU B 56.675 -0.891 6.723 1.00 0.00

ATOM 1708 CA LEU B 57.602 -0.071 7.499 1.00 0.00

ATOM 1709 C LEU B 2 58.615 0.631 6.635 1.00 0.00

ATOM 1710 O LEU B 59.761 0.764 7.033 1.00 0.00

ATOM 1711 N ASP B 3 58.220 1.082 5.455 1.00 0.00

ATOM 1712 CA ASP B 3 59.184 1.756 4.603 1.00 0.00

ATOM 1713 C ASP B 3 60.241 0.813 4.040 1.00 0.00

ATOM 1714 O ASP B 3 61.412 1.167 3.948 1.00 0.00

ATOM 1715 N SER B 4 59.825 -0.395 3.692 1.00 0.00 ATOM 1716 CA SER B 4 60.749 -1.392 3.191 1.00 0.00

ATOM 1717 C SER B 4 61.740 -1.717 4.309 1.00 0.00

ATOM 1718 O SER B 4 62.956 -1.707 4.094 1.00 0.00

ATOM 1719 N ILE B 5 61.196 -1.990 5.494 1.00 0.00

ATOM 1720 CA ILE B 5 61.979 -2.335 6.679 1.00 0.00

ATOM 1721 C ILE B 5 62.987 -1.237 6.960 1.00 0.00

ATOM 1722 O ILE B 5 64.157 -1.515 7.205 1.00 0.00

ATOM 1723 N ILE B 6 62.534 0.012 6.912 1.00 0.00

ATOM 1724 CA ILE B 6 63.430 1.135 7.143 1.00 0.00

ATOM 1725 C ILE B 6 64.520 1.243 6.086 1.00 0.00

ATOM 1726 O ILE B 6 65.643 1.631 6.398 1.00 0.00

ATOM 1727 N ALA B 7 64.198 0.923 4.836 1.00 0.00

ATOM 1728 CA ALA B 7 65.186 0.988 3.768 1.00 0.00

ATOM 1729 C ALA B 7 66.283 -0.008 4.126 1.00 0.00

ATOM 1730 O ALA B 7 67.469 0.321 4.113 1.00 0.00

ATOM 1731 N GLU B 8 65.881 -1.227 4.455 1.00 0.00

ATOM 1732 CA GLU B 8 66.843 -2.251 4.834 1.00 0.00

ATOM 1733 C GLU B 8 67.704 -1.765 5.986 1.00 0.00

ATOM 1734 O GLU B 8 68.927 -1.810 5.906 1.00 0.00

ATOM 1735 N VAL B 9 67.069 -1.309 7.065 1.00 0.00

ATOM 1736 CA VAL B 9 67.835 -0.878 8.232 1.00 0.00

ATOM 1737 C VAL B 9 68.815 0.212 7.896 1.00 0.00

ATOM 1738 O VAL B 9 69.882 0.285 8.494 1.00 0.00

ATOM 1739 N LYS B 10 68.462 1.071 6.964 1.00 0.00

ATOM 1740 CA LYS B 10 69.379 2.133 6.609 1.00 0.00

ATOM 1741 C LYS B 10 70.526 1.590 5.801 1.00 0.00

ATOM 1742 O LYS B 10 71.626 2.119 5.851 1.00 0.00

ATOM 1743 N ALA B 11 70.269 0.533 5.042 1.00 0.00

ATOM 1744 CA ALA B 11 71.309 -0.077 4.236 1.00 0.00

ATOM 1745 C ALA B 11 72.299 -0.709 5.205 1.00 0.00

ATOM 1746 O ALA B 11 73.515 -0.503 5.098 1.00 0.00

ATOM 1747 N GLN B 12 71.768 -1.466 6.159 1.00 0.00

ATOM 1748 CA GLN B 12 72.607 -2.135 7.150 1.00 0.00

ATOM 1749 C GLN B 12 73.404 -1.138 7.972 1.00 0.00

ATOM 1750 O GLN B 12 74.552 -1.406 8.297 1.00 0.00

ATOM 1751 N TYR B 13 72.794 -0.003 8.299 1.00 0.00

ATOM 1752 CA TYR B 13 73.433 1.050 9.085 1.00 0.00

ATOM 1753 C TYR B 13 74.595 1.613 8.247 1.00 0.00

ATOM 1754 O TYR B 13 75.720 1.701 8.720 1.00 0.00

ATOM 1755 N GLU B 14 74.320 1.966 6.996 1.00 0.00

ATOM 1756 CA GLU B 14 75.363 2.474 6.103 1.00 0.00

ATOM 1757 C GLU B 14 76.571 1.499 6.110 1.00 0.00

ATOM 1758 O GLU B 14 77.725 1.916 6.219 1.00 0.00

ATOM 1759 N GLU B 15 76.292 0.200 5.999 1.00 0.00

ATOM 1760 CA GLU B 15 77.351 -0.817 5.999 1.00 0.00

ATOM 1761 C GLU B 15 78.131 -0.794 7.300 1.00 0.00

ATOM 1762 O GLU B 15 79.364 -0.777 7.292 1.00 0.00

ATOM 1763 N ILE B 16 77.419 -0.806 8.420 1.00 0.00

ATOM 1764 CA ILE B 16 78.104 -0.783 9.706 1.00 0.00

ATOM 1765 C ILE B 16 79.004 0.424 9.841 1.00 0.00

ATOM 1766 O ILE B 16 80.113 0.303 10.358 1.00 0.00

ATOM 1767 N ALA B 17 78.544 1.582 9.378 1.00 0.00

ATOM 1768 CA ALA B 17 79.357 2.786 9.477 1.00 0.00

ATOM 1769 C ALA B 17 80.629 2.631 8.651 1.00 0.00

ATOM 1770 O ALA B 17 81.723 2.901 9.142 1.00 0.00

ATOM 1771 N ASN B 18 80.513 2.167 7.416 1.00 0.00

ATOM 1772 CA ASN B 18 81.718 1.977 6.633 1.00 0.00

ATOM 1773 C ASN B 18 82.668 1.056 7.408 1.00 0.00

ATOM 1774 O ASN B 18 83.829 1.392 7.615 1.00 0.00

ATOM 1775 N ARG B 19 82.171 -0.086 7.859 1.00 0.00

ATOM 1776 CA ARG B 19 83.020 -1.026 8.598 1.00 0.00

ATOM 1777 C ARG B 19 83.694 -0.411 9.821 1.00 0.00

ATOM 1778 O ARG B 19 84.877 -0.647 10.067 1.00 0.00

TER 1779 ARG B 19

ATOM 1780 N TYR B 1 - 93 . 407 -3 . 215 10 . 155 1 . 00 0 . 00

ATOM 1781 CA TYR B 1 - 94 . 347 -3 . 100 11 . 260 1 . 00 0 . 00

ATOM 1782 C TYR B 1 - 95 . 318 -1 . 977 11 . 045 1 . 00 0 . 00

ATOM 1783 O TYR B 1 - 96. 500 -2 . 154 11 . 294 1 . 00 0 . 00 ATOM 1784 N GLN B 2 -94.801 -0.832 10.559 1.00 0.00

ATOM 1785 CA GLN B 2 -95.670 0.310 10.330 1.00 0.00

ATOM 1786 C GLN B 9 -96.840 -0.067 9.463 1.00 0.00

ATOM 1787 O GLN B 2 -97.949 0.356 9.744 1.00 0.00

ATOM 1788 N THR B 3 -96.586 -0.883 8.419 1.00 0.00

ATOM 1789 CA THR B 3 -97.677 -1.285 7.547 1.00 0.00

ATOM 1790 C THR B 3 -98.671 -2.141 8.284 1.00 0.00

ATOM 1791 O THR B 3 -99.852 -1.838 8.253 1.00 0.00

ATOM 1792 N LYS B 4 -98.183 -3.210 8.946 1.00 0.00

ATOM 1793 CA LYS B 4 -99.093 -4.091 9.662 1.00 0.00

ATOM 1794 C LYS B 4 -99.905 -3.320 10.664 1.00 0.00

ATOM 1795 O LYS B 4 -101.104 -3.523 10.757 1.00 0.00

ATOM 1796 N TYR B 5 -99.226 -2.421 11.403 1.00 0.00

ATOM 1797 CA TYR B 5 -99.922 -1.620 12.395 1.00 0.00

ATOM 1798 C TYR B 5 -101.017 -0.814 11.753 1.00 0.00

ATOM 1799 O TYR B 5 -102.117 -0.779 12.281 1.00 0.00

ATOM 1800 N GLU B 6 -100.707 -0.174 10.608 1.00 0.00

ATOM 1801 CA GLU B 6 -101.715 0.624 9.931 1.00 0.00

ATOM 1802 C GLU B 6 -102.924 -0.209 9.611 1.00 0.00

ATOM 1803 O GLU B 6 -104.036 0.222 9.872 1.00 0.00

ATOM 1804 N GLU B 7 -102.690 -1.412 9.051 1.00 0.00

ATOM 1805 CA GLU B 7 -103.805 -2.287 8.729 1.00 0.00

ATOM 1806 C GLU B 7 -104.613 -2.583 9.961 1.00 0.00

ATOM 1807 O GLU B 7 -105.832 -2.531 9.905 1.00 0.00

ATOM 1808 N LEU B 8 -103.918 -2.884 11.074 1.00 0.00

ATOM 1809 CA LEU B 8 -104.623 -3.186 12.309 1.00 0.00

ATOM 1810 C LEU B 8 -105.497 -2.039 12.726 1.00 0.00

ATOM 1811 O LEU B 8 -106.663 -2.250 13.018 1.00 0.00

ATOM 1812 N GLN B 9 -104.917 -0.823 12.745 1.00 0.00

ATOM 1813 CA GLN B 9 -105.678 0.334 13.184 1.00 0.00

ATOM 1814 C GLN B 9 -106.919 0.514 12.355 1.00 0.00

ATOM 1815 O GLN B 9 -107.980 0.743 12.911 1.00 0.00

ATOM 1816 N GLN B 10 -106.773 0.401 11.019 1.00 0.00

ATOM 1817 CA GLN B 10 -107.935 0.551 10.160 1.00 0.00

ATOM 1818 C GLN B 10 -108.973 -0.483 10.493 1.00 0.00

ATOM 1819 O GLN B 10 -110.140 -0.150 10.613 1.00 0.00

ATOM 1820 N THR B 11 -108.525 -1.745 10.655 1.00 0.00

ATOM 1821 CA THR B 11 -109.458 -2.807 10.995 1.00 0.00

ATOM 1822 C THR B 11 -110.171 -2.517 12.290 1.00 0.00

ATOM 1823 O THR B 11 -111.350 -2.811 12.400 1.00 0.00

ATOM 1824 N ALA B 12 -109.437 -1.938 13.263 1.00 0.00

ATOM 1825 CA ALA B 12 -110.026 -1.705 14.570 1.00 0.00

ATOM 1826 C ALA B 12 -111.251 -0.837 14.485 1.00 0.00

ATOM 1827 O ALA B 12 -112.295 -1.242 14.971 1.00 0.00

ATOM 1828 N GLY B 13 -111.119 0.351 13.858 1.00 0.00

ATOM 1829 CA GLY B 13 -112.267 1.241 13.775 1.00 0.00

ATOM 1830 C GLY B 13 -113.425 0.585 13.075 1.00 0.00

ATOM 1831 O GLY B 13 -114.561 0.977 13.290 1.00 0.00

ATOM 1832 N ARG B 14 -113.123 -0.428 12.241 1.00 0.00

ATOM 1833 CA ARG B 14 -114.189 -1.145 11.566 1.00 0.00

ATOM 1834 C ARG B 14 -114.995 -1.933 12.561 1.00 0.00

ATOM 1835 O ARG B 14 -116.205 -1.776 12.609 1.00 0.00

ATOM 1836 N HIS B 15 -114.314 -2.786 13.353 1.00 0.00

ATOM 1837 CA HIS B 15 -115.030 -3.586 14.334 1.00 0.00

ATOM 1838 C HIS B 15 -115.776 -2.706 15.295 1.00 0.00

ATOM 1839 O HIS B 15 -116.862 -3.068 15.718 1.00 0.00

ATOM 1840 N GLY B 16 -115.194 -1.534 15.623 1.00 0.00

ATOM 1841 CA GLY B 16 -115.890 -0.616 16.509 1.00 0.00

ATOM 1842 C GLY B 16 -117.184 -0.166 15.895 1.00 0.00

ATOM 1843 O GLY B 16 -118.162 0.001 16.607 1.00 0.00

ATOM 1844 N ASP B 17 -117.186 0.021 14.560 1.00 0.00

ATOM 1845 CA ASP B 17 -118.417 0.413 13.895 1.00 0.00

ATOM 1846 C ASP B 17 -119.431 -0.691 13.994 1.00 0.00

ATOM 1847 O ASP B 17 -120.589 -0.417 14.262 1.00 0.00

ATOM 1848 N ASP B 18 -118.977 -1.942 13.781 1.00 0.00

ATOM 1849 CA ASP B 18 -119.902 -3.063 13.846 1.00 0.00

ATOM 1850 C ASP B 18 -120.550 -3.144 15.197 1.00 0.00

ATOM 1851 O ASP B 18 -121.767 -3.177 15.277 1.00 0.00 ATOM 1852 N LEU B 19 -119.717 -3.167 16.257 1.00 0.00

ATOM 1853 CA LEU B 19 -120.258 -3.218 17.604 1.00 0.00

ATOM 1854 C LEU B 19 -121.206 -2.076 17.837 1.00 0.00

ATOM 1855 O LEU B 19 -122.201 -2.252 18.522 1.00 0.00

ATOM 1856 N ARG B 20 -120.888 -0.906 17.247 1.00 0.00

ATOM 1857 CA ARG B 20 -121.743 0.254 17.429 1.00 0.00

ATOM 1858 C ARG B 20 -123.148 -0.023 16.971 1.00 0.00

ATOM 1859 O ARG B 20 -124.067 0.076 17.769 1.00 0.00

ATOM 1860 N ASN B 21 -123.307 -0.371 15.678 1.00 0.00

ATOM 1861 CA ASN B 21 -124.641 -0.607 15.153 1.00 0.00

ATOM 1862 C ASN B 21 -125.344 -1.692 15.920 1.00 0.00

ATOM 1863 O ASN B 21 -126.540 -1.594 16.143 1.00 0.00

ATOM 1864 N THR B 22 -124.583 -2.728 16.329 1.00 0.00

ATOM 1865 CA THR B 22 -125.199 -3.841 17.031 1.00 0.00

ATOM 1866 C THR B 99 -125.809 -3.409 18.336 1.00 0.00

ATOM 1867 O THR B 22 -126.934 -3.792 18.616 1.00 0.00

ATOM 1868 N LYS B 23 -125.070 -2.605 19.129 1.00 0.00

ATOM 1869 CA LYS B 23 -125.623 -2.145 20.393 1.00 0.00

ATOM 1870 C LYS B 23 -126.921 -1.424 20.158 1.00 0.00

ATOM 1871 O LYS B 23 -127.860 -1.603 20.918 1.00 0.00

ATOM 1872 N HIS B 24 -126.964 -0.621 19.077 1.00 0.00

ATOM 1873 CA HIS B 24 -128.193 0.076 18.739 1.00 0.00

ATOM 1874 C HIS B 24 -129.299 -0.910 18.480 1.00 0.00

ATOM 1875 O HIS B 24 -130.389 -0.739 19.005 1.00 0.00

ATOM 1876 N GLU B 25 -129.005 -1.947 17.671 1.00 0.00

ATOM 1877 CA GLU B 25 -130.021 -2.941 17.365 1.00 0.00

ATOM 1878 C GLU B 25 -130.564 -3.561 18.620 1.00 0.00

ATOM 1879 O GLU B 25 -131.767 -3.721 18.739 1.00 0.00

ATOM 1880 N ILE B 26 -129.657 -3.901 19.557 1.00 0.00

ATOM 1881 CA ILE B 26 -130.096 -4.514 20.799 1.00 0.00

ATOM 1882 C ILE B 26 -131.064 -3.614 21.519 1.00 0.00

ATOM 1883 O ILE B 26 -132.074 -4.095 22.007 1.00 0.00

ATOM 1884 N SER B 27 -130.754 -2.303 21.562 1.00 0.00

ATOM 1885 CA SER B 27 -131.666 -1.369 22.205 1.00 0.00

ATOM 1886 C SER B 27 -133.033 -1.457 21.588 1.00 0.00

ATOM 1887 O SER B 27 -134.021 -1.444 22.305 1.00 0.00

ATOM 1888 N GLU B 28 -133.075 -1.561 20.246 1.00 0.00

ATOM 1889 CA GLU B 28 -134.359 -1.652 19.570 1.00 0.00

ATOM 1890 C GLU B 28 -135.098 -2.900 19.966 1.00 0.00

ATOM 1891 O GLU B 28 -136.272 -2.816 20.285 1.00 0.00

ATOM 1892 N MET B 29 -134.403 -4.055 19.941 1.00 0.00

ATOM 1893 CA MET B 29 -135.075 -5.302 20.270 1.00 0.00

ATOM 1894 C MET B 29 -135.667 -5.243 21.648 1.00 0.00

ATOM 1895 O MET B 29 -136.809 -5.635 21.827 1.00 0.00

ATOM 1896 N ASN B 30 -134.881 -4.731 22.616 1.00 0.00

ATOM 1897 CA ASN B 30 -135.397 -4.610 23.968 1.00 0.00

ATOM 1898 C ASN B 30 -136.630 -3.750 23.988 1.00 0.00

ATOM 1899 O ASN B 30 -137.577 -4.076 24.686 1.00 0.00

ATOM 1900 N ARG B 31 -136.616 -2.653 23.204 1.00 0.00

ATOM 1901 CA ARG B 31 -137.779 -1.782 23.166 1.00 0.00

ATOM 1902 C ARG B 31 -138.977 -2.515 22.630 1.00 0.00

ATOM 1903 O ARG B 31 -140.029 -2.486 23.248 1.00 0.00

ATOM 1904 N MET B 32 -138.801 -3.177 21.469 1.00 0.00

ATOM 1905 CA MET B 32 -139.914 -3.885 20.864 1.00 0.00

ATOM 1906 C MET B 32 -140.458 -4.937 21.788 1.00 0.00

ATOM 1907 O MET B 32 -141.666 -5.065 21.905 1.00 0.00

ATOM 1908 N ILE B 33 -139.551 -5.679 22.454 1.00 0.00

ATOM 1909 CA ILE B 33 -139.996 -6.707 23.381 1.00 0.00

ATOM 1910 C ILE B 33 -140.847 -6.105 24.462 1.00 0.00

ATOM 1911 O ILE B 33 -141.896 -6.649 24.766 1.00 0.00

ATOM 1912 N GLN B 34 -140.388 -4.972 25.031 1.00 0.00

ATOM 1913 CA GLN B 34 -141.160 -4.330 26.082 1.00 0.00

ATOM 1914 C GLN B 34 -142.549 -4.017 25.604 1.00 0.00

ATOM 1915 O GLN B 34 -143.503 -4.306 26.309 1.00 0.00

ATOM 1916 N ARG B 35 -142.652 -3.438 24.392 1.00 0.00

ATOM 1917 CA ARG B 35 -143.965 -3.134 23.848 1.00 0.00

ATOM 1918 C ARG B 35 -144.801 -4.380 23.755 1.00 0.00

ATOM 1919 O ARG B 35 -145.963 -4.352 24.125 1.00 0.00 ATOM 1920 N LEU B 36 -144.188 -5.478 23.266 1.00 0.00

ATOM 1921 CA LEU B 36 -144.928 -6.721 23.143 1.00 0.00

ATOM 1922 C LEU B 36 -145.442 -7.180 24.476 1.00 0.00

ATOM 1923 O LEU B 36 -146.613 -7.504 24.589 1.00 0.00

ATOM 1924 N ARG B 37 -144.548 -7.198 25.485 1.00 0.00

ATOM 1925 CA ARG B 37 -144.947 -7.673 26.799 1.00 0.00

ATOM 1926 C ARG B 37 -146.118 -6.896 27.326 1.00 0.00

ATOM 1927 O ARG B 37 -147.072 -7.496 27.798 1.00 0.00

ATOM 1928 N ALA B 38 -146.039 -5.554 27.232 1.00 0.00

ATOM 1929 CA ALA B 38 -147.137 -4.732 27.713 1.00 0.00

ATOM 1930 C ALA B 38 -148.410 -5.098 27.002 1.00 0.00

ATOM 1931 O ALA B 38 -149.438 -5.240 27.646 1.00 0.00

ATOM 1932 N GLU B 39 -148.319 -5.264 25.668 1.00 0.00

ATOM 1933 CA GLU B 39 -149.492 -5.646 24.900 1.00 0.00

ATOM 1934 C GLU B 39 -150.068 -6.934 25.415 1.00 0.00

ATOM 1935 O GLU B 39 -151.273 -7.024 25.593 1.00 0.00

ATOM 1936 N ILE B 40 -149.191 -7.929 25.657 1.00 0.00

ATOM 1937 CA ILE B 40 -149.665 -9.210 26.154 1.00 0.00

ATOM 1938 C ILE B 40 -150.441 -9.027 27.428 1.00 0.00

ATOM 1939 O ILE B 40 -151.513 -9.596 27.558 1.00 0.00

ATOM 1940 N ASP B 41 -149.893 -8.222 28.360 1.00 0.00

ATOM 1941 CA ASP B 41 -150.585 -7.997 29.617 1.00 0.00

ATOM 1942 C ASP B 41 -151.973 -7.468 29.382 1.00 0.00

ATOM 1943 O ASP B 41 -152.915 -7.990 29.955 1.00 0.00

ATOM 1944 N ASN B 42 -152.089 -6.431 28.529 1.00 0.00

ATOM 1945 CA ASN B 42 -153.399 -5.847 28.289 1.00 0.00

ATOM 1946 C ASN B 42 -154.346 -6.844 27.685 1.00 0.00

ATOM 1947 O ASN B 42 -155.462 -6.971 28.162 1.00 0.00

ATOM 1948 N VAL B 43 -153.891 -7.553 26.633 1.00 0.00

ATOM 1949 CA VAL B 43 -154.760 -8.523 25.986 1.00 0.00

ATOM 1950 C VAL B 43 -155.234 -9.555 26.968 1.00 0.00

ATOM 1951 O VAL B 43 -156.403 -9.911 26.951 1.00 0.00

ATOM 1952 N LYS B 44 -154.315 -10.024 27.834 1.00 0.00

ATOM 1953 CA LYS B 44 -154.694 -11.034 28.803 1.00 0.00

ATOM 1954 C LYS B 44 -155.757 -10.515 29.730 1.00 0.00

ATOM 1955 O LYS B 44 -156.737 -11.209 29.956 1.00 0.00

ATOM 1956 N LYS B 45 -155.564 -9.291 30.260 1.00 0.00

ATOM 1957 CA LYS B 45 -156.559 -8.747 31.171 1.00 0.00

ATOM 1958 C LYS B 45 -157.884 -8.590 30.482 1.00 0.00

ATOM 1959 O LYS B 45 -158.907 -8.916 31.063 1.00 0.00

ATOM 1960 N GLN B 46 -157.851 -8.095 29.229 1.00 0.00

ATOM 1961 CA GLN B 46 -159.088 -7.933 28.485 1.00 0.00

ATOM 1962 C GLN B 46 -159.778 -9.258 28.323 1.00 0.00

ATOM 1963 O GLN B 46 -160.976 -9.345 28.542 1.00 0.00

ATOM 1964 N CYS B 47 -158.998 -10.291 27.949 1.00 0.00

ATOM 1965 CA CYS B 47 -159.582 -11.606 27.761 1.00 0.00

ATOM 1966 C CYS B 47 -160.211 -12.095 29.036 1.00 0.00

ATOM 1967 O CYS B 47 -161.299 -12.645 28.989 1.00 0.00

ATOM 1968 N ALA B 48 -159.522 -11.877 30.175 1.00 0.00

ATOM 1969 CA ALA B 48 -160.077 -12.311 31.445 1.00 0.00

ATOM 1970 C ALA B 48 -161.430 -11.695 31.665 1.00 0.00

ATOM 1971 O ALA B 48 -162.360 -12.398 32.027 1.00 0.00

ATOM 1972 N ASN B 49 -161.530 -10.372 31.429 1.00 0.00

ATOM 1973 CA ASN B 49 -162.806 -9.703 31.613 1.00 0.00

ATOM 1974 C ASN B 49 -163.849 -10.283 30.700 1.00 0.00

ATOM 1975 O ASN B 49 -164.942 -10.583 31.153 1.00 0.00

ATOM 1976 N LEU B 50 -163.498 -10.446 29.409 1.00 0.00

ATOM 1977 CA LEU B 50 -164.456 -10.990 28.461 1.00 0.00

ATOM 1978 C LEU B 50 -164.962 -12.327 28.928 1.00 0.00

ATOM 1979 O LEU B 50 -166.145 -12.605 28.817 1.00 0.00

ATOM 1980 N GLN B 51 -164.042 -13.145 29.471 1.00 0.00

ATOM 1981 CA GLN B 51 -164.439 -14.460 29.934 1.00 0.00

ATOM 1982 C GLN B 51 -165.331 -14.362 31.139 1.00 0.00

ATOM 1983 O GLN B 51 -166.248 -15.160 31.254 1.00 0.00

ATOM 1984 N ASN B 52 -165.081 -13.385 32.034 1.00 0.00

ATOM 1985 CA ASN B 52 -165.978 -13.220 33.167 1.00 0.00

ATOM 1986 C ASN B 52 -167.365 -12.923 32.670 1.00 0.00

ATOM 1987 O ASN B 52 -168.329 -13.506 33.143 1.00 0.00 ATOM 1988 N ALA B 53 -167.441 -12.010 31.682 1.00 0.00

ATOM 1989 CA ALA B 53 -168.722 -11.718 31.063 1.00 0.00

ATOM 1990 C ALA B 53 -169.298 -12.958 30.439 1.00 0.00

ATOM 1991 O ALA B 53 -170.511 -13.085 30.386 1.00 0.00

ATOM 1992 N ILE B 54 -168.415 -13.874 29.984 1.00 0.00

ATOM 1993 CA ILE B 54 -168.890 -15.124 29.411 1.00 0.00

ATOM 1994 C ILE B 54 -169.621 -15.909 30.465 1.00 0.00

ATOM 1995 O ILE B 54 -170.785 -16.227 30.271 1.00 0.00

ATOM 1996 N ALA B 55 -168.925 -16.219 31.576 1.00 0.00

ATOM 1997 CA ALA B 55 -169.529 -17.057 32.597 1.00 0.00

ATOM 1998 C ALA B 55 -170.793 -16.442 33.126 1.00 0.00

ATOM 1999 O ALA B 55 -171.810 -17.113 33.175 1.00 0.00

ATOM 2000 N ASP B 56 -170.719 -15.152 33.508 1.00 0.00

ATOM 2001 CA ASP B 56 -171.902 -14.488 34.028 1.00 0.00

ATOM 2002 C ASP B 56 -173.030 -14.572 33.041 1.00 0.00

ATOM 2003 O ASP B 56 -174.150 -14.857 33.435 1.00 0.00

ATOM 2004 N ALA B 57 -172.718 -14.331 31.753 1.00 0.00

ATOM 2005 CA ALA B 57 -173.759 -14.365 30.740 1.00 0.00

ATOM 2006 C ALA B 57 -174.404 -15.720 30.665 1.00 0.00

ATOM 2007 O ALA B 57 -175.616 -15.807 30.763 1.00 0.00

ATOM 2008 N GLU B 58 -173.581 -16.775 30.493 1.00 0.00

ATOM 2009 CA GLU B 58 -174.140 -18.111 30.368 1.00 0.00

ATOM 2010 C GLU B 58 -174.962 -18.467 31.574 1.00 0.00

ATOM 2011 O GLU B 58 -176.049 -19.002 31.423 1.00 0.00

ATOM 2012 N GLN B 59 -174.435 -18.150 32.773 1.00 0.00

ATOM 2013 CA GLN B 59 -175.170 -18.459 33.988 1.00 0.00

ATOM 2014 C GLN B 59 -176.503 -17.764 34.001 1.00 0.00

ATOM 2015 O GLN B 59 -177.510 -18.400 34.264 1.00 0.00

ATOM 2016 N ARG B 60 -176.488 -16.448 33.714 1.00 0.00

ATOM 2017 CA ARG B 60 -177.721 -15.681 33.778 1.00 0.00

ATOM 2018 C ARG B 60 -178.752 -16.203 32.818 1.00 0.00

ATOM 2019 O ARG B 60 -179.883 -16.420 33.220 1.00 0.00

ATOM 2020 N GLY B 61 -178.352 -16.404 31.545 1.00 0.00

ATOM 2021 CA GLY B 61 -179.315 -16.863 30.558 1.00 0.00

ATOM 2022 C GLY B 61 -179.927 -18.176 30.957 1.00 0.00

ATOM 2023 O GLY B 61 -181.108 -18.380 30.724 1.00 0.00

ATOM 2024 N GLU B 62 -179.118 -19.061 31.572 1.00 0.00

ATOM 2025 CA GLU B 62 -179.652 -20.344 31.996 1.00 0.00

ATOM 2026 C GLU B 62 -180.738 -20.156 33.018 1.00 0.00

ATOM 2027 O GLU B 62 -181.783 -20.778 32.908 1.00 0.00

ATOM 2028 N LEU B 63 -180.480 -19.282 34.011 1.00 0.00

ATOM 2029 CA LEU B 63 -181.465 -19.067 35.058 1.00 0.00

ATOM 2030 C LEU B 63 -182.744 -18.513 34.498 1.00 0.00

ATOM 2031 O LEU B 63 -183.809 -19.032 34.798 1.00 0.00

ATOM 2032 N ALA B 64 -182.625 -17.448 33.683 1.00 0.00

ATOM 2033 CA ALA B 64 -183.817 -16.793 33.172 1.00 0.00

ATOM 2034 C ALA B 64 -184.622 -17.708 32.293 1.00 0.00

ATOM 2035 O ALA B 64 -185.834 -17.748 32.431 1.00 0.00

ATOM 2036 N LEU B 65 -183.944 -18.453 31.397 1.00 0.00

ATOM 2037 CA LEU B 65 -184.667 -19.379 30.541 1.00 0.00

ATOM 2038 C LEU B 65 -185.414 -20.377 31.383 1.00 0.00

ATOM 2039 O LEU B 65 -186.544 -20.710 31.062 1.00 0.00

ATOM 2040 N LYS B 66 -184.772 -20.834 32.478 1.00 0.00

ATOM 2041 CA LYS B 66 -185.440 -21.767 33.368 1.00 0.00

ATOM 2042 C LYS B 66 -186.713 -21.170 33.902 1.00 0.00

ATOM 2043 O LYS B 66 -187.743 -21.822 33.864 1.00 0.00

ATOM 2044 N ASP B 67 -186.630 -19.919 34.397 1.00 0.00

ATOM 2045 CA ASP B 67 -187.810 -19.295 34.969 1.00 0.00

ATOM 2046 C ASP B 67 -188.903 -19.138 33.951 1.00 0.00

ATOM 2047 O ASP B 67 -190.038 -19.479 34.245 1.00 0.00

ATOM 2048 N ALA B 68 -188.555 -18.628 32.752 1.00 0.00

ATOM 2049 CA ALA B 68 -189.565 -18.456 31.723 1.00 0.00

ATOM 2050 C ALA B 68 -190.251 -19.762 31.434 1.00 0.00

ATOM 2051 O ALA B 68 -191.470 -19.807 31.386 1.00 0.00

ATOM 2052 N ARG B 69 -189.442 -20.824 31.259 1.00 0.00

ATOM 2053 CA ARG B 69 -190.008 -22.130 30.968 1.00 0.00

ATOM 2054 C ARG B 69 -190.934 -22.582 32.060 1.00 0.00

ATOM 2055 O ARG B 69 -192.019 -23.058 31.766 1.00 0.00 ATOM 2056 N ASN B 70 -190.505 -22.425 33.327 1.00 0.00

ATOM 2057 CA ASN B 70 -191.355 -22.848 34.426 1.00 0.00

ATOM 2058 C ASN B 70 -192.657 -22.095 34.431 1.00 0.00

ATOM 2059 O ASN B 70 -193.702 -22.701 34.607 1.00 0.00

ATOM 2060 N LYS B 71 -192.578 -20.765 34.232 1.00 0.00

ATOM 2061 CA LYS B 71 -193.780 -19.949 34.289 1.00 0.00

ATOM 2062 C LYS B 71 -194.784 -20.377 33.257 1.00 0.00

ATOM 2063 O LYS B 71 -195.888 -20.755 33.614 1.00 0.00

ATOM 2064 N LEU B 72 -194.387 -20.307 31.971 1.00 0.00

ATOM 2065 CA LEU B 72 -195.307 -20.681 30.909 1.00 0.00

ATOM 2066 C LEU B 72 -195.861 -22.061 31.129 1.00 0.00

ATOM 2067 O LEU B 72 -196.994 -22.323 30.757 1.00 0.00

ATOM 2068 N ALA B 73 -195.049 -22.935 31.757 1.00 0.00

ATOM 2069 CA ALA B 73 -195.498 -24.291 32.002 1.00 0.00

ATOM 2070 C ALA B 73 -196.713 -24.309 32.889 1.00 0.00

ATOM 2071 O ALA B 73 -197.751 -24.795 32.471 1.00 0.00

ATOM 2072 N GLU B 74 -196.568 -23.773 34.119 1.00 0.00

ATOM 2073 CA GLU B 74 -197.687 -23.791 35.049 1.00 0.00

ATOM 2074 C GLU B 74 -198.886 -23.096 34.471 1.00 0.00

ATOM 2075 O GLU B 74 -200.002 -23.540 34.695 1.00 0.00

ATOM 2076 N LEU B 75 -198.643 -22.006 33.717 1.00 0.00

ATOM 2077 CA LEU B 75 -199.751 -21.251 33.161 1.00 0.00

ATOM 2078 C LEU B 75 -200.569 -22.071 32.202 1.00 0.00

ATOM 2079 O LEU B 75 -201.787 -22.045 32.289 1.00 0.00

ATOM 2080 N GLU B 76 -199.894 -22.807 31.295 1.00 0.00

ATOM 2081 CA GLU B 76 -200.635 -23.637 30.358 1.00 0.00

ATOM 2082 C GLU B 76 -201.482 -24.634 31.099 1.00 0.00

ATOM 2083 O GLU B 76 -202.614 -24.874 30.708 1.00 0.00

ATOM 2084 N GLU B 77 -200.923 -25.195 32.190 1.00 0.00

ATOM 2085 CA GLU B 77 -201.688 -26.140 32.984 1.00 0.00

ATOM 2086 C GLU B 77 -202.924 -25.484 33.533 1.00 0.00

ATOM 2087 O GLU B 77 -203.996 -26.062 33.458 1.00 0.00

ATOM 2088 N ALA B 78 -202.759 -24.263 34.079 1.00 0.00

ATOM 2089 CA ALA B 78 -203.905 -23.553 34.624 1.00 0.00

ATOM 2090 C ALA B 78 -204.955 -23.343 33.570 1.00 0.00

ATOM 2091 O ALA B 78 -206.128 -23.533 33.848 1.00 0.00

ATOM 2092 N LEU B 79 -204.518 -22.959 32.353 1.00 0.00

ATOM 2093 CA LEU B 79 -205.471 -22.751 31.276 1.00 0.00

ATOM 2094 C LEU B 79 -206.264 -24.002 31.016 1.00 0.00

ATOM 2095 O LEU B 79 -207.466 -23.918 30.816 1.00 0.00

ATOM 2096 N GLN B 80 -205.583 -25.165 31.043 1.00 0.00

ATOM 2097 CA GLN B 80 -206.290 -26.421 30.850 1.00 0.00

ATOM 2098 C GLN B 80 -207.382 -26.570 31.872 1.00 0.00

ATOM 2099 O GLN B 80 -208.485 -26.962 31.527 1.00 0.00

ATOM 2100 N LYS B 81 -207.057 -26.239 33.138 1.00 0.00

ATOM 2101 CA LYS B 81 -208.042 -26.374 34.196 1.00 0.00

ATOM 2102 C LYS B 81 -209.230 -25.485 33.956 1.00 0.00

ATOM 2103 O LYS B 81 -210.353 -25.947 34.073 1.00 0.00

ATOM 2104 N ALA B 82 -208.970 -24.205 33.620 1.00 0.00

ATOM 2105 CA ALA B 82 -210.068 -23.275 33.416 1.00 0.00

ATOM 2106 C ALA B 82 -210.988 -23.759 32.331 1.00 0.00

ATOM 2107 O ALA B 82 -212.195 -23.695 32.492 1.00 0.00

ATOM 2108 N LYS B 83 -210.397 -24.260 31.229 1.00 0.00

ATOM 2109 CA LYS B 83 -211.218 -24.789 30.152 1.00 0.00

ATOM 2110 C LYS B 83 -212.088 -25.905 30.661 1.00 0.00

ATOM 2111 O LYS B 83 -213.254 -25.970 30.307 1.00 0.00

ATOM 2112 N GLN B 84 -211.501 -26.774 31.508 1.00 0.00

ATOM 2113 CA GLN B 84 -212.259 -27.898 32.028 1.00 0.00

ATOM 2114 C GLN B 84 -213.408 -27.431 32.876 1.00 0.00

ATOM 2115 O GLN B 84 -214.528 -27.864 32.657 1.00 0.00

ATOM 2116 N ASP B 85 -213.119 -26.540 33.845 1.00 0.00

ATOM 2117 CA ASP B 85 -214.177 -26.064 34.721 1.00 0.00

ATOM 2118 C ASP B 85 -215.269 -25.405 33.930 1.00 0.00

ATOM 2119 O ASP B 85 -216.435 -25.627 34.214 1.00 0.00

ATOM 2120 N MET B 86 -214.873 -24.599 32.926 1.00 0.00

ATOM 2121 CA MET B 86 -215.862 -23.932 32.098 1.00 0.00

ATOM 2122 C MET B 86 -216.760 -24.937 31.432 1.00 0.00

ATOM 2123 O MET B 86 -217.967 -24.757 31.441 1.00 0.00 ATOM 2124 N ALA B 87 -216.157 -25.999 30.862 1.00 0.00

ATOM 2125 CA ALA B 87 -216.957 -27.013 30.195 1.00 0.00

ATOM 2126 C ALA B 87 -217.965 -27.600 31.141 1.00 0.00

ATOM 2127 O ALA B 87 -219.122 -27.737 30.776 1.00 0.00

ATOM 2128 N ARG B 88 -217.513 -27.935 32.366 1.00 0.00

ATOM 2129 CA ARG B 88 -218.431 -28.485 33.346 1.00 0.00

ATOM 2130 C ARG B 88 -219.561 -27.529 33.600 1.00 0.00

ATOM 2131 O ARG B 88 -220.706 -27.949 33.646 1.00 0.00

ATOM 2132 N LEU B 89 -219.225 -26.232 33.751 1.00 0.00

ATOM 2133 CA LEU B 89 -220.260 -25.244 34.004 1.00 0.00

ATOM 2134 C LEU B 89 -221.252 -25.202 32.878 1.00 0.00

ATOM 2135 O LEU B 89 -222.445 -25.219 33.134 1.00 0.00

ATOM 2136 N LEU B 90 -220.748 -25.159 31.630 1.00 0.00

ATOM 2137 CA LEU B 90 -221.644 -25.097 30.487 1.00 0.00

ATOM 2138 C LEU B 90 -222.588 -26.264 30.472 1.00 0.00

ATOM 2139 O LEU B 90 -223.777 -26.071 30.265 1.00 0.00

ATOM 2140 N ARG B 91 -222.049 -27.476 30.705 1.00 0.00

ATOM 2141 CA ARG B 91 -222.904 -28.652 30.720 1.00 0.00

ATOM 2142 C ARG B 91 -223.968 -28.508 31.771 1.00 0.00

ATOM 2143 O ARG B 91 -225.125 -28.781 31.494 1.00 0.00

ATOM 2144 N GLU B 92 -223.562 -28.062 32.978 1.00 0.00

ATOM 2145 CA GLU B 92 -224.529 -27.873 34.046 1.00 0.00

ATOM 2146 C GLU B 92 -225.616 -26.934 33.605 1.00 0.00

ATOM 2147 O GLU B 92 -226.783 -27.218 33.812 1.00 0.00

ATOM 2148 N TYR B 93 -225.198 -25.812 32.985 1.00 0.00

ATOM 2149 CA TYR B 93 -226.159 -24.821 32.539 1.00 0.00

ATOM 2150 C TYR B 93 -227.187 -25.432 31.627 1.00 0.00

ATOM 2151 O TYR B 93 -228.368 -25.182 31.810 1.00 0.00

ATOM 2152 N GLN B 94 -226.726 -26.239 30.652 1.00 0.00

ATOM 2153 CA GLN B 94 -227.663 -26.873 29.737 1.00 0.00

ATOM 2154 C GLN B 94 -228.666 -27.698 30.493 1.00 0.00

ATOM 2155 O GLN B 94 -229.854 -27.591 30.237 1.00 0.00

ATOM 2156 N GLU B 95 -228.159 -28.518 31.436 1.00 0.00

ATOM 2157 CA GLU B 95 -229.042 -29.379 32.202 1.00 0.00

ATOM 2158 C GLU B 95 -230.068 -28.576 32.951 1.00 0.00

ATOM 2159 O GLU B 95 -231.252 -28.846 32.816 1.00 0.00

ATOM 2160 N LEU B 96 -229.599 -27.590 33.740 1.00 0.00

ATOM 2161 CA LEU B 96 -230.522 -26.794 34.535 1.00 0.00

ATOM 2162 C LEU B 96 -231.575 -26.159 33.674 1.00 0.00

ATOM 2163 O LEU B 96 -232.737 -26.164 34.047 1.00 0.00

ATOM 2164 N MET B 97 -231.157 -25.619 32.513 1.00 0.00

ATOM 2165 CA MET B 97 -232.121 -24.974 31.637 1.00 0.00

ATOM 2166 C MET B 97 -233.165 -25.951 31.171 1.00 0.00

ATOM 2167 O MET B 97 -234.340 -25.624 31.195 1.00 0.00

ATOM 2168 N ASN B 98 -232.727 -27.156 30.757 1.00 0.00

ATOM 2169 CA ASN B 98 -233.683 -28.152 30.302 1.00 0.00

ATOM 2170 C ASN B 98 -234.649 -28.493 31.400 1.00 0.00

ATOM 2171 O ASN B 98 -235.845 -28.527 31.164 1.00 0.00

ATOM 2172 N THR B 99 -234.105 -28.734 32.610 1.00 0.00

ATOM 2173 CA THR B 99 -234.956 -29.066 33.741 1.00 0.00

ATOM 2174 C THR B 99 -235.955 -27.970 33.985 1.00 0.00

ATOM 2175 O THR B 99 -237.126 -28.254 34.181 1.00 0.00

ATOM 2176 N LYS B 100 -235.475 -26.712 33.966 1.00 0.00

ATOM 2177 CA LYS B 100 -236.369 -25.592 34.206 1.00 0.00

ATOM 2178 C LYS B 100 -237.467 -25.553 33.180 1.00 0.00

ATOM 2179 O LYS B 100 -238.608 -25.307 33.535 1.00 0.00

ATOM 2180 N LEU B 101 -237.109 -25.810 31.905 1.00 0.00

ATOM 2181 CA LEU B 101 -238.118 -25.812 30.859 1.00 0.00

ATOM 2182 C LEU B 101 -239.208 -26.795 31.184 1.00 0.00

ATOM 2183 O LEU B 101 -240.375 -26.450 31.096 1.00 0.00

ATOM 2184 N ALA B 102 -238.808 -28.021 31.573 1.00 0.00

ATOM 2185 CA ALA B 102 -239.798 -29.030 31.907 1.00 0.00

ATOM 2186 C ALA B 102 -240.644 -28.588 33.068 1.00 0.00

ATOM 2187 O ALA B 102 -241.858 -28.700 32.997 1.00 0.00

ATOM 2188 N LEU B 103 -239.991 -28.079 34.132 1.00 0.00

ATOM 2189 CA LEU B 103 -240.738 -27.647 35.301 1.00 0.00

ATOM 2190 C LEU B 103 -241.772 -26.625 34.924 1.00 0.00

ATOM 2191 O LEU B 103 -242.905 -26.728 35.364 1.00 0.00 ATOM 2192 N ASP B 104 -241.371 -25.647 34.091 1.00 0.00

ATOM 2193 CA ASP B 104 -242.314 -24.618 33.689 1.00 0.00

ATOM 2194 C ASP B 104 -243.467 -25.210 32.928 1.00 0.00

ATOM 2195 O ASP B 104 -244.591 -24.771 33.117 1.00 0.00

ATOM 2196 N VAL B 105 -243.186 -26.220 32.081 1.00 0.00

ATOM 2197 CA VAL B 105 -244.266 -26.862 31.350 1.00 0.00

ATOM 2198 C VAL B 105 -245.232 -27.493 32.317 1.00 0.00

ATOM 2199 O VAL B 105 -246.429 -27.294 32.186 1.00 0.00

ATOM 2200 N GLU B 106 -244.693 -28.246 33.297 1.00 0.00

ATOM 2201 CA GLU B 106 -245.557 -28.889 34.272 1.00 0.00

ATOM 2202 C GLU B 106 -246.356 -27.871 35.035 1.00 0.00

ATOM 2203 O GLU B 106 -247.532 -28.090 35.272 1.00 0.00

ATOM 2204 N ILE B 107 -245.704 -26.750 35.406 1.00 0.00

ATOM 2205 CA ILE B 107 -246.407 -25.713 36.145 1.00 0.00

ATOM 2206 C ILE B 107 -247.563 -25.195 35.339 1.00 0.00

ATOM 2207 O ILE B 107 -248.658 -25.085 35.866 1.00 0.00

ATOM 2208 N ALA B 108 -247.305 -24.886 34.052 1.00 0.00

ATOM 2209 CA ALA B 108 -248.368 -24.376 33.202 1.00 0.00

ATOM 2210 C ALA B 108 -249.537 -25.320 33.192 1.00 0.00

ATOM 2211 O ALA B 108 -250.670 -24.880 33.297 1.00 0.00

ATOM 2212 N THR B 109 -249.242 -26.631 33.081 1.00 0.00

ATOM 2213 CA THR B 109 -250.311 -27.613 33.078 1.00 0.00

ATOM 2214 C THR B 109 -251.084 -27.558 34.366 1.00 0.00

ATOM 2215 O THR B 109 -252.303 -27.510 34.332 1.00 0.00

ATOM 2216 N TYR B 110 -250.358 -27.559 35.502 1.00 0.00

ATOM 2217 CA TYR B 110 -251.030 -27.528 36.791 1.00 0.00

ATOM 2218 C TYR B 110 -251.941 -26.338 36.901 1.00 0.00

ATOM 2219 O TYR B 110 -253.057 -26.483 37.373 1.00 0.00

ATOM 2220 N ARG B 111 -251.455 -25.164 36.453 1.00 0.00

ATOM 2221 CA ARG B 111 -252.274 -23.966 36.536 1.00 0.00

ATOM 9999 C ARG B 111 -253.560 -24.136 35.780 1.00 0.00

ATOM 2223 O ARG B 111 -254.611 -23.811 36.308 1.00 0.00

ATOM 2224 N LYS B 112 -253.469 -24.661 34.541 1.00 0.00

ATOM 2225 CA LYS B 112 -254.677 -24.868 33.760 1.00 0.00

ATOM 2226 C LYS B 112 -255.630 -25.768 34.496 1.00 0.00

ATOM 2227 O LYS B 112 -256.802 -25.443 34.602 1.00 0.00

ATOM 2228 N LEU B 113 -255.105 -26.898 35.012 1.00 0.00

ATOM 2229 CA LEU B 113 -255.957 -27.832 35.730 1.00 0.00

ATOM 2230 C LEU B 113 -256.609 -27.166 36.906 1.00 0.00

ATOM 2231 O LEU B 113 -257.805 -27.317 37.097 1.00 0.00

ATOM 2232 N LEU B 114 -255.803 -26.424 37.690 1.00 0.00

ATOM 2233 CA LEU B 114 -256.342 -25.774 38.870 1.00 0.00

ATOM 2234 C LEU B 114 -257.448 -24.823 38.506 1.00 0.00

ATOM 2235 O LEU B 114 -258.447 -24.781 39.207 1.00 0.00

ATOM 2236 N GLU B 115 -257.269 -24.075 37.401 1.00 0.00

ATOM 2237 CA GLU B 115 -258.305 -23.141 36.992 1.00 0.00

ATOM 2238 C GLU B 115 -259.585 -23.871 36.703 1.00 0.00

ATOM 2239 O GLU B 115 -260.625 -23.483 37.212 1.00 0.00

ATOM 2240 N GLY B 116 -259.499 -24.938 35.884 1.00 0.00

ATOM 2241 CA GLY B 116 -260.704 -25.670 35.535 1.00 0.00

ATOM 2242 C GLY B 116 -261.369 -26.234 36.759 1.00 0.00

ATOM 2243 O GLY B 116 -262.565 -26.054 36.924 1.00 0.00

ATOM 2244 N GLU B 117 -260.582 -26.913 37.617 1.00 0.00

ATOM 2245 CA GLU B 117 -261.172 -27.496 38.810 1.00 0.00

ATOM 2246 C GLU B 117 -261.721 -26.414 39.695 1.00 0.00

ATOM 2247 O GLU B 117 -262.919 -26.363 39.923 1.00 0.00

TER 2248 GLU B 117

MASTER 0 0 0 0 0 0 0 0 2240 8 0 46

END Tab. 3:

HEADER K35 K85 (Chain A: K35; chain B : K85)

COMPND K35_ K85

REMARK GENERATED BY SYBYL (TRIPOS, INC. ) 10-MAR-08

(Legend analogous to table ' 1)

SEQRES 1 A 43 GLU GLY ILE LEU THR GLY ASN GLU LYS GLU THR MET GLN

SEQRES 9 A 43 SER LEU ASN ASP ARG LEU ALA GLY TYR LEU GLU LYS VAL

SEQRES 3 A 43 ARG GLN LEU GLU GLN GLU ASN ALA SER LEU GLU SER ARG

SEQRES 4 A 43 ILE ARG GLU TRP

SEQRES 1 A 101 TYR GLN SER TYR PHE ARG THR ILE GLU GLU LEU GLN LYS

SEQRES 9 A 101 LYS THR LEU CYS SER LYS ALA GLU ASN ALA ARG LEU VAL

SEQRES 3 A 101 VAL GLU ILE ASP ASN ALA LYS LEU ALA ALA ASP ASP PHE

SEQRES 4 A 101 ARG THR LYS TYR GLU THR GLU VAL SER LEU ARG GLN LEU

SEQRES 5 A 101 VAL GLU SER ASP ILE ASN GLY LEU ARG ARG ILE LEU ASP

SEQRES 6 A 101 ASP LEU THR LEU CYS LYS SER ASP LEU GLU ALA GLN VAL

SEQRES 7 A 101 GLU SER LEU LYS GLU GLU LEU LEU CYS LEU LYS LYS ASN

SEQRES 8 A 101 HIS GLU GLU GLU VAL ASN SER LEU ARG CYS

SEQRES 1 A 19 ASP LEU ASN ARG VAL LEU GLU GLU MET ARG CYS GLN TYR

SEQRES 9 A 19 GLU THR LEU VAL GLU ASN

SEQRES 1 A 117 LEU ASP THR GLN SER GLU GLU LEU ASN GLN GLN VAL VAL

SEQRES 9 A 117 SER SER SER GLU GLN LEU GLN SER CYS GLN ALA GLU ILE

SEQRES 3 A 117 ILE GLU LEU ARG ARG THR VAL ASN ALA LEU GLU ILE GLU

SEQRES 4 A 117 LEU GLN ALA GLN HIS SER MET ARG ASP ALA LEU GLU SER

SEQRES 5 A 117 THR LEU ALA GLU THR GLU ALA ARG TYR SER SER GLN LEU

SEQRES 6 A 117 ALA GLN MET GLN CYS MET ILE THR ASN VAL GLU ALA GLN

SEQRES 7 A 117 LEU ALA GLU ILE ARG ALA ASP LEU GLU ARG GLN ASN GLN

SEQRES 8 A 117 GLU TYR GLN VAL LEU LEU ASP VAL ARG ALA ARG LEU GLU

SEQRES 9 A 117 CYS GLU ILE ASN THR TYR ARG GLY LEU LEU GLU SER GLU

SEQRES 1 B 43 ALA GLN CYS VAL LYS GLN GLU GLU LYS GLU GLN ILE LYS

SEQRES 2 B 43 SER LEU ASN SER ARG PHE ALA ALA PHE ILE ASP LYS VAL

SEQRES 3 B 43 ARG PHE LEU GLU GLN GLN ASN LYS LEU LEU GLU THR LYS

SEQRES 4 B 43 TRP GLN PHE TYR

SEQRES 1 B 101 GLU PRO LEU PHE SER GLY TYR ILE GLU THR LEU ARG ARG

SEQRES 2 B 101 GLU ALA GLU CYS VAL GLU ALA ASP SER GLY ARG LEU ALA

SEQRES 3 B 101 SER GLU LEU ASN HIS VAL GLN GLU VAL LEU GLU GLY TYR

SEQRES 4 B 101 LYS LYS LYS TYR GLU GLU GLU VAL ALA LEU ARG ALA THR

SEQRES 5 B 101 ALA GLU ASN GLU PHE VAL VAL LEU LYS LYS ASP VAL ASP

SEQRES 6 B 101 CYS ALA TYR LEU ARG LYS SER ASP LEU GLU ALA ASN VAL

SEQRES 7 B 101 GLU ALA LEU VAL GLU GLU SER SER PHE LEU ARG ARG LEU

SEQRES 8 B 101 TYR GLU GLU GLU ILE ARG VAL LEU GLN ALA

SEQRES 1 B 19 ASN MET ASP CYS ILE ILE ALA GLU ILE LYS ALA GLN TYR

SEQRES 9 B 19 ASP ASP VAL ALA SER ARG

SEQRES 1 B 117 TYR ARG SER LYS CYS GLU GLU MET LYS ALA THR VAL ILE

SEQRES 2 B 117 ARG HIS GLY GLU THR LEU ARG ARG THR LYS GLU GLU ILE

SEQRES 3 B 117 ASN GLU LEU ASN ARG MET ILE GLN ARG LEU THR ALA GLU

SEQRES 4 B 117 ILE GLU ASN ALA LYS CYS GLN ARG ALA LYS LEU GLU ALA

SEQRES 5 B 117 ALA VAL ALA GLU ALA GLU GLN GLN GLY GLU ALA ALA LEU

SEQRES 6 B 117 SER ASP ALA ARG CYS LYS LEU ALA GLU LEU GLU GLY ALA

SEQRES 7 B 117 LEU GLN LYS ALA LYS GLN ASP MET ALA CYS LEU LEU LYS

SEQRES 8 B 117 GLU TYR GLN GLU VAL MET ASN SER LYS LEU GLY LEU ASP

SEQRES 9 B 117 ILE GLU ILE ALA THR TYR ARG ARG LEU LEU GLU GLY GLU

ATOM 1 N GLU A 90 181. 483 42. 993 -33. 125 1. 00 0.00

ATOM 9 CA GLU A 90 180. 788 42. 153 -32. 160 1. 00 0.00

ATOM 3 C GLU A 90 179. 956 43. 012 -31. 246 1. 00 0.00

ATOM 4 O GLU A 90 178. 904 42. 580 -30. 804 1. 00 0.00

ATOM 5 CB GLU A 90 181. 791 41. 363 -31. 318 1. 00 0.00

ATOM 6 CG GLU A 90 182. 508 40. 259 -32. 079 1. 00 0.00

ATOM 7 CD GLU A 90 183. 561 39. 561 -31. 239 1. 00 0.00

ATOM 8 OEl GLU A 90 183. 778 39. 986 -30. 086 1. 00 0.00

ATOM 9 OE2 GLU A 90 184. 167 38. 589 -31. 736 1. 00 0.00

ATOM 10 N GLY A 91 180. 442 44. 241 -30. 977 1. 00 0.00

ATOM 11 CA GLY A 91 179. 704 45. 149 -30. 115 1. 00 0.00

ATOM 12 C GLY A 91 178. 381 45. 506 -30. 732 1. 00 0.00

ATOM 13 O GLY A 91 177. 362 45. 365 -30. 077 1. 00 0.00

ATOM 14 N ILE A 92 178. 404 45. 960 -32. 003 1. 00 0.00

ATOM 15 CA ILE A 92 177. 156 46. 312 -32. 662 1. 00 0.00

ATOM 16 C ILE A 92 176. 182 45. 168 -32. 610 1. 00 0.00 ATOM 17 O ILE A 92 175.022 45.387 -32.301 1.00 0.00

ATOM 18 CB ILE A 92 177.382 46.669 -34.144 1.00 0.00

ATOM 19 CGl ILE A 92 178.165 47.977 -34.264 1.00 0.00

ATOM 20 CG2 ILE A 92 176.050 46.835 -34.860 1.00 0.00

ATOM 21 CDl ILE A 92 178.662 48.264 -35.664 1.00 0.00

ATOM 22 N LEU A 93 176.665 43.941 -32.890 1.00 0.00

ATOM 23 CA LEU A 93 175.785 42.788 -32.813 1.00 0.00

ATOM 24 C LEU A 93 175.189 42.660 -31.437 1.00 0.00

ATOM 25 O LEU A 93 173.979 42.561 -31.313 1.00 0.00

ATOM 26 CB LEU A 93 176.557 41.503 -33.121 1.00 0.00

ATOM 27 CG LEU A 93 177.007 41.314 -34.571 1.00 0.00

ATOM 28 CDl LEU A 93 177.920 40.103 -34.698 1.00 0.00

ATOM 29 CD2 LEU A 93 175.808 41.103 -35.483 1.00 0.00

ATOM 30 N THR A 94 176.063 42.671 -30.410 1.00 0.00

ATOM 31 CA THR A 94 175.604 42.522 -29.037 1.00 0.00

ATOM 32 C THR A 94 174.515 43.504 -28.694 1.00 0.00

ATOM 33 O THR A 94 173.519 43.113 -28.108 1.00 0.00

ATOM 34 CB THR A 94 176.750 42.747 -28.033 1.00 0.00

ATOM 35 OGl THR A 94 177.781 41.778 -28.254 1.00 0.00

ATOM 36 CG2 THR A 94 176.241 42.609 -26.606 1.00 0.00

ATOM 37 N GLY A 95 174.714 44.784 -29.069 1.00 0.00

ATOM 38 CA GLY A 95 173.713 45.787 -28.748 1.00 0.00

ATOM 39 C GLY A 95 172.412 45.502 -29.448 1.00 0.00

ATOM 40 O GLY A 95 171.363 45.684 -28.850 1.00 0.00

ATOM 41 N ASN A 96 172.484 45.043 -30.713 1.00 0.00

ATOM 42 CA ASN A 96 171.261 44.740 -31.440 1.00 0.00

ATOM 43 C ASN A 96 170.467 43.678 -30.731 1.00 0.00

ATOM 44 O ASN A 96 169.269 43.842 -30.553 1.00 0.00

ATOM 45 CB ASN A 96 171.585 44.236 -32.848 1.00 0.00

ATOM 46 CG ASN A 96 172.075 45.341 -33.763 1.00 0.00

ATOM 47 ODl ASN A 96 171.853 46.523 -33.500 1.00 0.00

ATOM 48 ND2 ASN A 96 172.744 44.959 -34.845 1.00 0.00

ATOM 49 N GLU A 97 171.144 42.587 -30.323 1.00 0.00

ATOM 50 CA GLU A 97 170.432 41.499 -29.670 1.00 0.00

ATOM 51 C GLU A 97 169.898 41.912 -28.327 1.00 0.00

ATOM 52 O GLU A 97 168.806 41.493 -27.979 1.00 0.00

ATOM 53 CB GLU A 97 171.363 40.303 -29.455 1.00 0.00

ATOM 54 CG GLU A 97 171.756 39.584 -30.735 1.00 0.00

ATOM 55 CD GLU A 97 172.772 38.485 -30.498 1.00 0.00

ATOM 56 OEl GLU A 97 173.224 38.333 -29.344 1.00 0.00

ATOM 57 OE2 GLU A 97 173.118 37.776 -31.467 1.00 0.00

ATOM 58 N LYS A 98 170.659 42.728 -27.570 1.00 0.00

ATOM 59 CA LYS A 98 170.180 43.122 -26.256 1.00 0.00

ATOM 60 C LYS A 98 168.914 43.926 -26.373 1.00 0.00

ATOM 61 O LYS A 98 167.981 43.676 -25.627 1.00 0.00

ATOM 62 CB LYS A 98 171.228 43.975 -25.538 1.00 0.00

ATOM 63 CG LYS A 98 170.828 44.396 -24.132 1.00 0.00

ATOM 64 CD LYS A 98 171.943 45.171 -23.449 1.00 0.00

ATOM 65 CE LYS A 98 171.533 45.616 -22.056 1.00 0.00

ATOM 66 NZ LYS A 98 172.612 46.390 -21.380 1.00 0.00

ATOM 67 N GLU A 99 168.878 44.883 -27.322 1.00 0.00

ATOM 68 CA GLU A 99 167.667 45.667 -27.497 1.00 0.00

ATOM 69 C GLU A 99 166.517 44.778 -27.877 1.00 0.00

ATOM 70 O GLU A 99 165.441 44.920 -27.319 1.00 0.00

ATOM 71 CB GLU A 99 167.859 46.710 -28.600 1.00 0.00

ATOM 72 CG GLU A 99 168.797 47.845 -28.225 1.00 0.00

ATOM 73 CD GLU A 99 169.060 48.790 -29.381 1.00 0.00

ATOM 74 OEl GLU A 99 168.567 48.517 -30.495 1.00 0.00

ATOM 75 OE2 GLU A 99 169.758 49.805 -29.172 1.00 0.00

ATOM 76 N THR A 100 166.761 43.848 -28.822 1.00 0.00

ATOM 77 CA THR A 100 165.713 42.915 -29.205 1.00 0.00

ATOM 78 C THR A 100 165.224 42.161 -27.999 1.00 0.00

ATOM 79 O THR A 100 164.028 41.986 -27.843 1.00 0.00

ATOM 80 CB THR A 100 166.220 41.890 -30.237 1.00 0.00

ATOM 81 OGl THR A 100 166.633 42.571 -31.428 1.00 0.00

ATOM 82 CG2 THR A 100 165.119 40.902 -30.590 1.00 0.00

ATOM 83 N MET A 101 166.168 41.726 -27.138 1.00 0.00

ATOM 84 CA MET A 101 165.775 40.978 -25.956 1.00 0.00 ATOM 85 C MET A 101 164.922 41.806 -25.039 1.00 0.00

ATOM 86 O MET A 101 163.928 41.302 -24.539 1.00 0.00

ATOM 87 CB MET A 101 167.009 40.527 -25.172 1.00 0.00

ATOM 88 CG MET A 101 167.829 39.453 -25.868 1.00 0.00

ATOM 89 SD MET A 101 169.325 39.023 -24.961 1.00 0.00

ATOM 90 CE MET A 101 168.629 38.203 -23.528 1.00 0.00

ATOM 91 N GLN A 102 165.307 43.081 -24.825 1.00 0.00

ATOM 92 CA GLN A 102 164.510 43.944 -23.968 1.00 0.00

ATOM 93 C GLN A 102 163.089 43.990 -24.459 1.00 0.00

ATOM 94 O GLN A 102 162.175 43.827 -23.667 1.00 0.00

ATOM 95 CB GLN A 102 165.072 45.367 -23.968 1.00 0.00

ATOM 96 CG GLN A 102 166.399 45.510 -23.240 1.00 0.00

ATOM 97 CD GLN A 102 166.991 46.899 -23.374 1.00 0.00

ATOM 98 OEl GLN A 102 166.449 47.750 -24.080 1.00 0.00

ATOM 99 NE2 GLN A 102 168.107 47.134 -22.693 1.00 0.00

ATOM 100 N SER A 103 162.918 44.199 -25.780 1.00 0.00

ATOM 101 CA SER A 103 161.574 44.253 -26.333 1.00 0.00

ATOM 102 C SER A 103 160.833 42.964 -26.099 1.00 0.00

ATOM 103 O SER A 103 159.657 43.009 -25.780 1.00 0.00

ATOM 104 CB SER A 103 161.625 44.500 -27.843 1.00 0.00

ATOM 105 OG SER A 103 162.149 45.785 -28.131 1.00 0.00

ATOM 106 N LEU A 104 161.523 41.814 -26.247 1.00 0.00

ATOM 107 CA LEU A 104 160.847 40.547 -26.020 1.00 0.00

ATOM 108 C LEU A 104 160.408 40.433 -24.586 1.00 0.00

ATOM 109 O LEU A 104 159.280 40.045 -24.335 1.00 0.00

ATOM 110 CB LEU A 104 161.781 39.377 -26.334 1.00 0.00

ATOM 111 CG LEU A 104 162.123 39.160 -27.810 1.00 0.00

ATOM 112 CDl LEU A 104 163.201 38.097 -27.960 1.00 0.00

ATOM 113 CD2 LEU A 104 160.896 38.706 -28.584 1.00 0.00

ATOM 114 N ASN A 105 161.307 40.786 -23.644 1.00 0.00

ATOM 115 CA ASN A 105 160.962 40.677 -22.236 1.00 0.00

ATOM 116 C ASN A 105 159.769 41.518 -21.883 1.00 0.00

ATOM 117 O ASN A 105 158.910 41.054 -21.150 1.00 0.00

ATOM 118 CB ASN A 105 162.131 41.137 -21.362 1.00 0.00

ATOM 119 CG ASN A 105 163.274 40.143 -21.346 1.00 0.00

ATOM 120 ODl ASN A 105 163.093 38.968 -21.667 1.00 0.00

ATOM 121 ND2 ASN A 105 164.459 40.611 -20.972 1.00 0.00

ATOM 1 99 N ASP A 106 159.709 42.755 -22.418 1.00 0.00

ATOM 123 CA ASP A 106 158.561 43.603 -22.133 1.00 0.00

ATOM 124 C ASP A 106 157.313 42.967 -22.670 1.00 0.00

ATOM 125 O ASP A 106 156.318 42.910 -21.965 1.00 0.00

ATOM 126 CB ASP A 106 158.735 44.975 -22.787 1.00 0.00

ATOM 127 CG ASP A 106 159.779 45.825 -22.090 1.00 0.00

ATOM 128 ODl ASP A 106 160.194 45.457 -20.972 1.00 0.00

ATOM 129 OD2 ASP A 106 160.181 46.861 -22.662 1.00 0.00

ATOM 130 N ARG A 107 157.385 42.478 -23.926 1.00 0.00

ATOM 131 CA ARG A 107 156.240 41.794 -24.503 1.00 0.00

ATOM 132 C ARG A 107 155.799 40.691 -23.580 1.00 0.00

ATOM 133 O ARG A 107 154.622 40.587 -23.275 1.00 0.00

ATOM 134 CB ARG A 107 156.605 41.190 -25.861 1.00 0.00

ATOM 135 CG ARG A 107 156.805 42.217 -26.963 1.00 0.00

ATOM 136 CD ARG A 107 157.222 41.555 -28.266 1.00 0.00

ATOM 137 NE ARG A 107 157.464 42.533 -29.324 1.00 0.00

ATOM 138 CZ ARG A 107 157.952 42.231 -30.524 1.00 0.00

ATOM 139 NHl ARG A 107 158.138 43.188 -31.423 1.00 0.00

ATOM 140 NH2 ARG A 107 158.252 40.974 -30.820 1.00 0.00

ATOM 141 N LEU A 108 156.780 39.883 -23.136 1.00 0.00

ATOM 142 CA LEU A 108 156.490 38.752 -22.270 1.00 0.00

ATOM 143 C LEU A 108 155.730 39.148 -21.033 1.00 0.00

ATOM 144 O LEU A 108 154.663 38.606 -20.794 1.00 0.00

ATOM 145 CB LEU A 108 157.787 38.082 -21.811 1.00 0.00

ATOM 146 CG LEU A 108 157.636 36.895 -20.857 1.00 0.00

ATOM 147 CDl LEU A 108 156.885 35.756 -21.529 1.00 0.00

ATOM 148 CD2 LEU A 108 158.999 36.376 -20.425 1.00 0.00

ATOM 149 N ALA A 109 156.294 40.089 -20.248 1.00 0.00

ATOM 150 CA ALA A 109 155.635 40.501 -19.019 1.00 0.00

ATOM 151 C ALA A 109 154.222 40.926 -19.309 1.00 0.00

ATOM 152 O ALA A 109 153.307 40.490 -18.629 1.00 0.00 ATOM 153 CB ALA A 109 156.375 41.669 -18.385 1.00 0.00

ATOM 154 N GLY A 110 154.067 41.772 -20.346 1.00 0.00

ATOM 155 CA GLY A 110 152.743 42.241 -20.711 1.00 0.00

ATOM 156 C GLY A 110 151.799 41.102 -20.986 1.00 0.00

ATOM 157 O GLY A 110 150.752 41.040 -20.362 1.00 0.00

ATOM 158 N TYR A 111 152.175 40.202 -21.920 1.00 0.00

ATOM 159 CA TYR A 111 151.297 39.089 -22.256 1.00 0.00

ATOM 160 C TYR A 111 150.924 38.287 -21.040 1.00 0.00

ATOM 161 O TYR A 111 149.792 37.837 -20.945 1.00 0.00

ATOM 162 CB TYR A 111 151.983 38.146 -23.245 1.00 0.00

ATOM 163 CG TYR A 111 152.060 38.686 -24.655 1.00 0.00

ATOM 164 CDl TYR A 111 153.257 39.169 -25.168 1.00 0.00

ATOM 165 CD2 TYR A 111 150.935 38.712 -25.469 1.00 0.00

ATOM 166 CEl TYR A 111 153.336 39.666 -26.456 1.00 0.00

ATOM 167 CE2 TYR A 111 150.995 39.204 -26.758 1.00 0.00

ATOM 168 CZ TYR A 111 152.210 39.683 -27.248 1.00 0.00

ATOM 169 OH TYR A 111 152.286 40.177 -28.530 1.00 0.00

ATOM 170 N LEU A 112 151.882 38.114 -20.108 1.00 0.00

ATOM 171 CA LEU A 112 151.610 37.328 -18.915 1.00 0.00

ATOM 172 C LEU A 112 150.571 37.998 -18.060 1.00 0.00

ATOM 173 O LEU A 112 149.669 37.336 -17.575 1.00 0.00

ATOM 174 CB LEU A 112 152.883 37.162 -18.081 1.00 0.00

ATOM 175 CG LEU A 112 153.978 36.282 -18.685 1.00 0.00

ATOM 176 CDl LEU A 112 155.245 36.348 -17.844 1.00 0.00

ATOM 177 CD2 LEU A 112 153.527 34.831 -18.751 1.00 0.00

ATOM 178 N GLU A 113 150.711 39.327 -17.888 1.00 0.00

ATOM 179 CA GLU A 113 149.742 40.056 -17.089 1.00 0.00

ATOM 180 C GLU A 113 148.387 39.976 -17.734 1.00 0.00

ATOM 181 O GLU A 113 147.415 39.675 -17.059 1.00 0.00

ATOM 182 CB GLU A 113 150.144 41.528 -16.970 1.00 0.00

ATOM 183 CG GLU A 113 149.207 42.359 -16.109 1.00 0.00

ATOM 184 CD GLU A 113 149.656 43.802 -15.987 1.00 0.00

ATOM 185 OEl GLU A 113 150.708 44.148 -16.564 1.00 0.00

ATOM 186 OE2 GLU A 113 148.955 44.587 -15.312 1.00 0.00

ATOM 187 N LYS A 114 148.338 40.238 -19.057 1.00 0.00

ATOM 188 CA LYS A 114 147.075 40.168 -19.775 1.00 0.00

ATOM 189 C LYS A 114 146.427 38.824 -19.588 1.00 0.00

ATOM 190 O LYS A 114 145.236 38.761 -19.331 1.00 0.00

ATOM 191 CB LYS A 114 147.297 40.389 -21.272 1.00 0.00

ATOM 192 CG LYS A 114 146.021 40.372 -22.098 1.00 0.00

ATOM 193 CD LYS A 114 146.308 40.668 -23.562 1.00 0.00

ATOM 194 CE LYS A 114 145.038 40.603 -24.396 1.00 0.00

ATOM 195 NZ LYS A 114 145.306 40.866 -25.837 1.00 0.00

ATOM 196 N VAL A 115 147.230 37.751 -19.719 1.00 0.00

ATOM 197 CA VAL A 115 146.679 36.412 -19.591 1.00 0.00

ATOM 198 C VAL A 115 146.153 36.166 -18.205 1.00 0.00

ATOM 199 O VAL A 115 145.137 35.502 -18.070 1.00 0.00

ATOM 200 CB VAL A 115 147.741 35.334 -19.879 1.00 0.00

ATOM 201 CGl VAL A 115 147.202 33.953 -19.547 1.00 0.00

ATOM 202 CG2 VAL A 115 148.138 35.356 -21.347 1.00 0.00

ATOM 203 N ARG A 116 146.836 36.708 -17.175 1.00 0.00

ATOM 204 CA ARG A 116 146.341 36.519 -15.822 1.00 0.00

ATOM 205 C ARG A 116 144.964 37.111 -15.711 1.00 0.00

ATOM 206 O ARG A 116 144.062 36.451 -15.220 1.00 0.00

ATOM 207 CB ARG A 116 147.264 37.207 -14.813 1.00 0.00

ATOM 208 CG ARG A 116 148.613 36.529 -14.644 1.00 0.00

ATOM 209 CD ARG A 116 149.494 37.289 -13.665 1.00 0.00

ATOM 210 NE ARG A 116 150.813 36.678 -13.528 1.00 0.00

ATOM 211 CZ ARG A 116 151.793 37.174 -12.779 1.00 0.00

ATOM 212 NHl ARG A 116 152.960 36.550 -12.715 1.00 0.00

ATOM 213 NH2 ARG A 116 151.601 38.295 -12.095 1.00 0.00

ATOM 214 N GLN A 117 144.815 38.362 -16.189 1.00 0.00

ATOM 215 CA GLN A 117 143.513 39.003 -16.134 1.00 0.00

ATOM 216 C GLN A 117 142.474 38.188 -16.857 1.00 0.00

ATOM 217 O GLN A 117 141.420 37.941 -16.293 1.00 0.00

ATOM 218 CB GLN A 117 143.569 40.395 -16.790 1.00 0.00

ATOM 219 CG GLN A 117 142.190 41.057 -16.791 1.00 0.00

ATOM 220 CD GLN A 117 141.816 41.549 -15.391 1.00 0.00 ATOM 221 OEl GLN A 117 140.756 42.108 -15.164 1.00 0.00

ATOM 999 NE2 GLN A 117 142.744 41.310 -14.469 1.00 0.00

ATOM 223 HBl GLN A 117 143.932 40.290 -17.812 1.00 0.00

ATOM 224 HB2 GLN A 117 144.263 41.022 -16.230 1.00 0.00

ATOM 225 HGl GLN A 117 141.452 40.335 -17.141 1.00 0.00

ATOM 226 HG2 GLN A 117 142.206 41.907 -17.474 1.00 0.00

ATOM 227 HE22 GLN A 117 142.589 41.600 -13.503 1.00 0.00

ATOM 228 HE21 GLN A 117 143.610 40.837 -14.727 1.00 0.00

ATOM 229 N LEU A 118 142.771 37.769 -18.104 1.00 0.00

ATOM 230 CA LEU A 118 141.774 37.043 -18.874 1.00 0.00

ATOM 231 C LEU A 118 141.381 35.739 -18.241 1.00 0.00

ATOM 232 O LEU A 118 140.204 35.418 -18.253 1.00 0.00

ATOM 233 CB LEU A 118 142.286 36.709 -20.287 1.00 0.00

ATOM 234 CG LEU A 118 141.399 35.782 -21.121 1.00 0.00

ATOM 235 CDl LEU A 118 142.014 35.527 -22.498 1.00 0.00

ATOM 236 CD2 LEU A 118 141.111 34.480 -20.372 1.00 0.00

ATOM 237 HBl LEU A 118 143.272 36.262 -20.158 1.00 0.00

ATOM 238 HB2 LEU A 118 142.394 37.660 -20.808 1.00 0.00

ATOM 239 HG LEU A 118 140.465 36.328 -21.256 1.00 0.00

ATOM 240 HD21 LEU A 118 140.608 34.696 -19.429 1.00 0.00

ATOM 241 HD22 LEU A 118 142.044 33.956 -20.165 1.00 0.00

ATOM 242 HD23 LEU A 118 140.478 33.846 -20.993 1.00 0.00

ATOM 243 HDIl LEU A 118 142.997 35.070 -22.388 1.00 0.00

ATOM 244 HD12 LEU A 118 142.118 36.468 -23.038 1.00 0.00

ATOM 245 HD13 LEU A 118 141.357 34.866 -23.063 1.00 0.00

ATOM 246 N GLU A 119 142.349 34.981 -17.688 1.00 0.00

ATOM 247 CA GLU A 119 141.993 33.698 -17.099 1.00 0.00

ATOM 248 C GLU A 119 141.096 33.891 -15.911 1.00 0.00

ATOM 249 O GLU A 119 140.204 33.085 -15.694 1.00 0.00

ATOM 250 CB GLU A 119 143.248 32.954 -16.639 1.00 0.00

ATOM 251 CG GLU A 119 144.114 32.435 -17.774 1.00 0.00

ATOM 252 CD GLU A 119 145.407 31.812 -17.284 1.00 0.00

ATOM 253 OEl GLU A 119 145.660 31.853 -16.061 1.00 0.00

ATOM 254 OE2 GLU A 119 146.167 31.283 -18.122 1.00 0.00

ATOM 255 N GLN A 120 141.330 34.976 -15.147 1.00 0.00

ATOM 256 CA GLN A 120 140.453 35.253 -14.023 1.00 0.00

ATOM 257 C GLN A 120 139.077 35.574 -14.537 1.00 0.00

ATOM 258 O GLN A 120 138.103 35.037 -14.036 1.00 0.00

ATOM 259 CB GLN A 120 140.976 36.442 -13.215 1.00 0.00

ATOM 260 CG GLN A 120 142.259 36.157 -12.450 1.00 0.00

ATOM 261 CD GLN A 120 142.826 37.394 -11.783 1.00 0.00

ATOM 262 OEl GLN A 120 142.323 38.501 -11.974 1.00 0.00

ATOM 263 NE2 GLN A 120 143.879 37.210 -10.996 1.00 0.00

ATOM 264 N GLU A 121 139.022 36.447 -15.563 1.00 0.00

ATOM 265 CA GLU A 121 137.743 36.811 -16.151 1.00 0.00

ATOM 266 C GLU A 121 137.028 35.604 -16.693 1.00 0.00

ATOM 267 O GLU A 121 135.819 35.513 -16.556 1.00 0.00

ATOM 268 CB GLU A 121 137.944 37.798 -17.303 1.00 0.00

ATOM 269 CG GLU A 121 136.651 38.281 -17.939 1.00 0.00

ATOM 270 CD GLU A 121 136.888 39.301 -19.036 1.00 0.00

ATOM 271 OEl GLU A 121 138.062 39.643 -19.286 1.00 0.00

ATOM 272 OE2 GLU A 121 135.898 39.757 -19.645 1.00 0.00

ATOM 273 N ASN A 122 137.785 34.672 -17.308 1.00 0.00

ATOM 274 CA ASN A 122 137.160 33.479 -17.859 1.00 0.00

ATOM 275 C ASN A 122 136.566 32.654 -16.757 1.00 0.00

ATOM 276 O ASN A 122 135.423 32.239 -16.872 1.00 0.00

ATOM 277 CB ASN A 122 138.191 32.629 -18.605 1.00 0.00

ATOM 278 CG ASN A 122 138.608 33.245 -19.925 1.00 0.00

ATOM 279 ODl ASN A 122 137.907 34.098 -20.473 1.00 0.00

ATOM 280 ND2 ASN A 122 139.753 32.814 -20.443 1.00 0.00

ATOM 281 N ALA A 123 137.353 32.426 -15.688 1.00 0.00

ATOM 282 CA ALA A 123 136.845 31.643 -14.576 1.00 0.00

ATOM 283 C ALA A 123 135.547 32.215 -14.077 1.00 0.00

ATOM 284 O ALA A 123 134.622 31.462 -13.820 1.00 0.00

ATOM 285 CB ALA A 123 137.843 31.641 -13.428 1.00 0.00

ATOM 286 N SER A 124 135.481 33.557 -13.960 1.00 0.00

ATOM 287 CA SER A 124 134.250 34.179 -13.498 1.00 0.00

ATOM 288 C SER A 124 133.114 33.896 -14.442 1.00 0.00 ATOM 289 O SER A 124 132.046 33.519 -13.990 1.00 0.00

ATOM 290 CB SER A 124 134.420 35.696 -13.399 1.00 0.00

ATOM 291 OG SER A 124 135.347 36.039 -12.383 1.00 0.00

ATOM 292 N LEU A 125 133.354 34.081 -15.757 1.00 0.00

ATOM 293 CA LEU A 125 132.295 33.841 -16.723 1.00 0.00

ATOM 294 C LEU A 125 131.776 32.436 -16.609 1.00 0.00

ATOM 295 O LEU A 125 130.573 32.234 -16.663 1.00 0.00

ATOM 296 CB LEU A 125 132.813 34.047 -18.148 1.00 0.00

ATOM 297 CG LEU A 125 133.146 35.485 -18.547 1.00 0.00

ATOM 298 CDl LEU A 125 133.816 35.523 -19.913 1.00 0.00

ATOM 299 CD2 LEU A 125 131.883 36.331 -18.614 1.00 0.00

ATOM 300 N GLU A 126 132.703 31.470 -16.441 1.00 0.00

ATOM 301 CA GLU A 126 132.294 30.080 -16.330 1.00 0.00

ATOM 302 C GLU A 126 131.364 29.890 -15.165 1.00 0.00

ATOM 303 O GLU A 126 130.308 29.303 -15.335 1.00 0.00

ATOM 304 CB GLU A 126 133.513 29.177 -16.124 1.00 0.00

ATOM 305 CG GLU A 126 133.182 27.696 -16.043 1.00 0.00

ATOM 306 CD GLU A 126 134.416 26.832 -15.872 1.00 0.00

ATOM 307 OEl GLU A 126 135.531 27.392 -15.831 1.00 0.00

ATOM 308 OE2 GLU A 126 134.266 25.596 -15.780 1.00 0.00

ATOM 309 N SER A 127 131.759 30.405 -13.982 1.00 0.00

ATOM 310 CA SER A 127 130.893 30.283 -12.820 1.00 0.00

ATOM 311 C SER A 127 129.532 30.849 -13.123 1.00 0.00

ATOM 312 O SER A 127 128.543 30.169 -12.898 1.00 0.00

ATOM 313 CB SER A 127 131.482 31.043 -11.631 1.00 0.00

ATOM 314 OG SER A 127 132.685 30.442 -11.185 1.00 0.00

ATOM 315 N ARG A 128 129.495 32.089 -13.649 1.00 0.00

ATOM 316 CA ARG A 128 128.218 32.719 -13.951 1.00 0.00

ATOM 317 C ARG A 128 127.359 31.876 -14.855 1.00 0.00

ATOM 318 O ARG A 128 126.171 31.757 -14.596 1.00 0.00

ATOM 319 CB ARG A 128 128.435 34.062 -14.652 1.00 0.00

ATOM 320 CG ARG A 128 128.996 35.148 -13.749 1.00 0.00

ATOM 321 CD ARG A 128 129.235 36.437 -14.518 1.00 0.00

ATOM 322 NE ARG A 128 129.825 37.476 -13.678 1.00 0.00

ATOM 323 CZ ARG A 128 130.241 38.655 -14.128 1.00 0.00

ATOM 324 NHl ARG A 128 130.765 39.538 -13.290 1.00 0.00

ATOM 325 NH2 ARG A 128 130.133 38.948 -15.417 1.00 0.00

ATOM 326 N ILE A 129 127.955 31.288 -15.911 1.00 0.00

ATOM 327 CA ILE A 129 127.157 30.482 -16.823 1.00 0.00

ATOM 328 C ILE A 129 126.627 29.258 -16.130 1.00 0.00

ATOM 329 O ILE A 129 125.516 28.845 -16.419 1.00 0.00

ATOM 330 CB ILE A 129 127.985 30.014 -18.034 1.00 0.00

ATOM 331 CGl ILE A 129 128.365 31.206 -18.914 1.00 0.00

ATOM 332 CG2 ILE A 129 127.188 29.029 -18.875 1.00 0.00

ATOM 333 CDl ILE A 129 129.392 30.879 -19.976 1.00 0.00

ATOM 334 N ARG A 130 127.418 28.686 -15.201 1.00 0.00

ATOM 335 CA ARG A 130 126.934 27.526 -14.470 1.00 0.00

ATOM 336 C ARG A 130 125.749 27.912 -13.630 1.00 0.00

ATOM 337 O ARG A 130 124.720 27.261 -13.706 1.00 0.00

ATOM 338 CB ARG A 130 128.029 26.975 -13.554 1.00 0.00

ATOM 339 CG ARG A 130 129.175 26.300 -14.292 1.00 0.00

ATOM 340 CD ARG A 130 130.245 25.819 -13.327 1.00 0.00

ATOM 341 NE ARG A 130 131.377 25.212 -14.024 1.00 0.00

ATOM 342 CZ ARG A 130 132.471 24.760 -13.420 1.00 0.00

ATOM 343 NHl ARG A 130 133.450 24.224 -14.135 1.00 0.00

ATOM 344 NH2 ARG A 130 132.584 24.846 -12.101 1.00 0.00

ATOM 345 N GLU A 131 125.913 28.986 -12.831 1.00 0.00

ATOM 346 CA GLU A 131 124.832 29.409 -11.959 1.00 0.00

ATOM 347 C GLU A 131 123.585 29.706 -12.741 1.00 0.00

ATOM 348 O GLU A 131 122.556 29.113 -12.466 1.00 0.00

ATOM 349 CB GLU A 131 125.224 30.676 -11.195 1.00 0.00

ATOM 350 CG GLU A 131 124.160 31.173 -10.231 1.00 0.00

ATOM 351 CD GLU A 131 124.562 32.455 -9.529 1.00 0.00

ATOM 352 OEl GLU A 131 125.682 32.947 -9.787 1.00 0.00

ATOM 353 OE2 GLU A 131 123.759 32.969 -8.724 1.00 0.00

ATOM 354 N TRP A 132 123.692 30.627 -13.720 1.00 0.00

ATOM 355 CA TRP A 132 122.517 30.997 -14.490 1.00 0.00

ATOM 356 C TRP A 132 121.891 29.794 -15.137 1.00 0.00 ATOM 357 O TRP A 132 120.707 29.563 -14.955 1.00 0.00

ATOM 358 CB TRP A 132 122.890 31.989 -15.594 1.00 0.00

ATOM 359 CG TRP A 132 123.281 33.340 -15.078 1.00 0.00

ATOM 360 CDl TRP A 132 124.548 33.832 -14.948 1.00 0.00

ATOM 361 CD2 TRP A 132 122.400 34.373 -14.622 1.00 0.00

ATOM 362 NEl TRP A 132 124.511 35.109 -14.440 1.00 0.00

ATOM 363 CE2 TRP A 132 123.202 35.463 -14.232 1.00 0.00

ATOM 364 CE3 TRP A 132 121.010 34.483 -14.506 1.00 0.00

ATOM 365 CZ2 TRP A 132 122.662 36.648 -13.733 1.00 0.00

ATOM 366 CZ3 TRP A 132 120.479 35.660 -14.011 1.00 0.00

ATOM 367 CH2 TRP A 132 121.300 36.727 -13.630 1.00 0.00

TER 368 TRP A 132

ATOM 369 N TYR A 144 104.979 31.505 -15.263 1.00 0.00

ATOM 370 CA TYR A 144 104.621 30.167 -14.792 1.00 0.00

ATOM 371 C TYR A 144 103.828 30.282 -13.468 1.00 0.00

ATOM 372 O TYR A 144 102.704 29.788 -13.371 1.00 0.00

ATOM 373 CB TYR A 144 105.879 29.331 -14.547 1.00 0.00

ATOM 374 CG TYR A 144 105.599 27.941 -14.022 1.00 0.00

ATOM 375 CDl TYR A 144 105.248 26.912 -14.887 1.00 0.00

ATOM 376 CD2 TYR A 144 105.686 27.662 -12.664 1.00 0.00

ATOM 377 CEl TYR A 144 104.989 25.638 -14.416 1.00 0.00

ATOM 378 CE2 TYR A 144 105.432 26.395 -12.176 1.00 0.00

ATOM 379 CZ TYR A 144 105.081 25.380 -13.065 1.00 0.00

ATOM 380 OH TYR A 144 104.824 24.113 -12.594 1.00 0.00

ATOM 381 N GLN A 145 104.398 30.941 -12.465 1.00 0.00

ATOM 382 CA GLN A 145 103.721 31.113 -11.177 1.00 0.00

ATOM 383 C GLN A 145 102.334 31.749 -11.316 1.00 0.00

ATOM 384 O GLN A 145 101.362 31.317 -10.695 1.00 0.00

ATOM 385 CB GLN A 145 104.543 32.017 -10.256 1.00 0.00

ATOM 386 CG GLN A 145 103.943 32.204 -8.872 1.00 0.00

ATOM 387 CD GLN A 145 104.795 33.087 -7.981 1.00 0.00

ATOM 388 OEl GLN A 145 105.795 33.651 -8.425 1.00 0.00

ATOM 389 NE2 GLN A 145 104.400 33.209 -6.719 1.00 0.00

ATOM 390 N SER A 146 102.246 32.795 -12.126 1.00 0.00

ATOM 391 CA SER A 146 100.971 33.458 -12.297 1.00 0.00

ATOM 392 C SER A 146 99.943 32.603 -13.002 1.00 0.00

ATOM 393 O SER A 146 98.750 32.731 -12.734 1.00 0.00

ATOM 394 CB SER A 146 101.137 34.733 -13.126 1.00 0.00

ATOM 395 OG SER A 146 101.529 34.430 -14.454 1.00 0.00

ATOM 396 N TYR A 147 100.384 31.742 -13.912 1.00 0.00

ATOM 397 CA TYR A 147 99.429 30.907 -14.612 1.00 0.00

ATOM 398 C TYR A 147 98.893 29.876 -13.660 1.00 0.00

ATOM 399 O TYR A 147 97.706 29.581 -13.656 1.00 0.00

ATOM 400 CB TYR A 147 100.098 30.202 -15.793 1.00 0.00

ATOM 401 CG TYR A 147 100.504 31.134 -16.913 1.00 0.00

ATOM 402 CDl TYR A 147 99.992 32.423 -16.986 1.00 0.00

ATOM 403 CD2 TYR A 147 101.398 30.721 -17.892 1.00 0.00

ATOM 404 CEl TYR A 147 100.356 33.281 -18.006 1.00 0.00

ATOM 405 CE2 TYR A 147 101.775 31.565 -18.920 1.00 0.00

ATOM 406 CZ TYR A 147 101.244 32.854 -18.969 1.00 0.00

ATOM 407 OH TYR A 147 101.610 33.707 -19.986 1.00 0.00

ATOM 408 N PHE A 148 99.757 29.331 -12.829 1.00 0.00

ATOM 409 CA PHE A 148 99.272 28.369 -11.865 1.00 0.00

ATOM 410 C PHE A 148 98.275 29.085 -10.956 1.00 0.00

ATOM 411 O PHE A 148 97.254 28.513 -10.558 1.00 0.00

ATOM 412 CB PHE A 148 100.429 27.815 -11.031 1.00 0.00

ATOM 413 CG PHE A 148 100.005 26.811 -9.998 1.00 0.00

ATOM 414 CDl PHE A 148 99.735 25.501 -10.354 1.00 0.00

ATOM 415 CD2 PHE A 148 99.877 27.176 -8.669 1.00 0.00

ATOM 416 CEl PHE A 148 99.345 24.577 -9.403 1.00 0.00

ATOM 417 CE2 PHE A 148 99.487 26.251 -7.718 1.00 0.00

ATOM 418 CZ PHE A 148 99.222 24.958 -8.080 1.00 0.00

ATOM 419 N ARG A 149 98.581 30.335 -10.630 1.00 0.00

ATOM 420 CA ARG A 149 97.731 31.106 -9.740 1.00 0.00

ATOM 421 C ARG A 149 96.350 31.248 -10.326 1.00 0.00

ATOM 422 O ARG A 149 95.341 31.059 -9.649 1.00 0.00

ATOM 423 CB ARG A 149 98.312 32.505 -9.523 1.00 0.00

ATOM 424 CG ARG A 149 99.574 32.528 -8.677 1.00 0.00 ATOM 425 CD ARG A 149 100.136 33.936 -8.562 1.00 0.00

ATOM 426 NE ARG A 149 101.366 33.972 -7.775 1.00 0.00

ATOM 427 CZ ARG A 149 102.098 35.063 -7.583 1.00 0.00

ATOM 428 NHl ARG A 149 103.202 35.002 -6.850 1.00 0.00

ATOM 429 NH2 ARG A 149 101.725 36.216 -8.122 1.00 0.00

ATOM 430 N THR A 150 96.343 31.555 -11.611 1.00 0.00

ATOM 431 CA THR A 150 95.131 31.767 -12.375 1.00 0.00

ATOM 432 C THR A 150 94.346 30.460 -12.498 1.00 0.00

ATOM 433 O THR A 150 93.111 30.446 -12.512 1.00 0.00

ATOM 434 CB THR A 150 95.440 32.272 -13.797 1.00 0.00

ATOM 435 OGl THR A 150 96.117 33.532 -13.723 1.00 0.00

ATOM 436 CG2 THR A 150 94.156 32.449 -14.591 1.00 0.00

ATOM 437 N ILE A 151 95.098 29.286 -12.664 1.00 0.00

ATOM 438 CA ILE A 151 94.631 27.900 -12.641 1.00 0.00

ATOM 439 C ILE A 151 93.890 27.629 -11.309 1.00 0.00

ATOM 440 O ILE A 151 92.728 27.220 -11.315 1.00 0.00

ATOM 441 CB ILE A 151 95.803 26.908 -12.757 1.00 0.00

ATOM 442 CGl ILE A 151 96.457 27.014 -14.136 1.00 0.00

ATOM 443 CG2 ILE A 151 95.316 25.480 -12.564 1.00 0.00

ATOM 444 CDl ILE A 151 97.785 26.295 -14.240 1.00 0.00

ATOM 445 N GLU A 152 94.548 27.869 -10.180 1.00 0.00

ATOM 446 CA GLU A 152 93.927 27.654 -8.869 1.00 0.00

ATOM 447 C GLU A 152 92.602 28.407 -8.711 1.00 0.00

ATOM 448 O GLU A 152 91.611 27.870 -8.212 1.00 0.00

ATOM 449 CB GLU A 152 94.855 28.132 -7.750 1.00 0.00

ATOM 450 CG GLU A 152 94.313 27.894 -6.350 1.00 0.00

ATOM 451 CD GLU A 152 95.286 28.323 -5.269 1.00 0.00

ATOM 452 OEl GLU A 152 96.395 28.784 -5.616 1.00 0.00

ATOM 453 OE2 GLU A 152 94.941 28.197 -4.075 1.00 0.00

ATOM 454 N GLU A 153 92.589 29.665 -9.124 1.00 0.00

ATOM 455 CA GLU A 153 91.376 30.446 -8.993 1.00 0.00

ATOM 456 C GLU A 153 90.253 29.959 -9.879 1.00 0.00

ATOM 457 O GLU A 153 89.084 30.082 -9.516 1.00 0.00

ATOM 458 CB GLU A 153 91.637 31.907 -9.366 1.00 0.00

ATOM 459 CG GLU A 153 92.500 32.659 -8.366 1.00 0.00

ATOM 460 CD GLU A 153 92.813 34.073 -8.813 1.00 0.00

ATOM 461 OEl GLU A 153 92.406 34.445 -9.935 1.00 0.00

ATOM 462 OE2 GLU A 153 93.463 34.809 -8.043 1.00 0.00

ATOM 463 N LEU A 154 90.586 29.418 -11.048 1.00 0.00

ATOM 464 CA LEU A 154 89.538 28.941 -11.926 1.00 0.00

ATOM 465 C LEU A 154 88.935 27.697 -11.340 1.00 0.00

ATOM 466 O LEU A 154 87.725 27.511 -11.363 1.00 0.00

ATOM 467 CB LEU A 154 90.104 28.620 -13.311 1.00 0.00

ATOM 468 CG LEU A 154 90.570 29.814 -14.146 1.00 0.00

ATOM 469 CDl LEU A 154 91.269 29.344 -15.412 1.00 0.00

ATOM 470 CD2 LEU A 154 89.388 30.682 -14.550 1.00 0.00

ATOM 471 N GLN A 155 89.767 26.840 -10.784 1.00 0.00

ATOM 472 CA GLN A 155 89.224 25.654 -10.165 1.00 0.00

ATOM 473 C GLN A 155 88.323 26.100 -9.016 1.00 0.00

ATOM 474 O GLN A 155 87.267 25.511 -8.769 1.00 0.00

ATOM 475 CB GLN A 155 90.350 24.767 -9.629 1.00 0.00

ATOM 476 CG GLN A 155 91.175 24.089 -10.710 1.00 0.00

ATOM 477 CD GLN A 155 92.347 23.311 -10.147 1.00 0.00

ATOM 478 OEl GLN A 155 92.608 23.346 -8.944 1.00 0.00

ATOM 479 NE2 GLN A 155 93.061 22.605 -11.016 1.00 0.00

ATOM 480 N LYS A 156 88.755 27.141 -8.314 1.00 0.00

ATOM 481 CA LYS A 156 88.006 27.637 -7.171 1.00 0.00

ATOM 482 C LYS A 156 86.628 28.072 -7.596 1.00 0.00

ATOM 483 O LYS A 156 85.625 27.749 -6.963 1.00 0.00

ATOM 484 CB LYS A 156 88.720 28.835 -6.542 1.00 0.00

ATOM 485 CG LYS A 156 90.011 28.480 -5.822 1.00 0.00

ATOM 486 CD LYS A 156 90.666 29.714 -5.221 1.00 0.00

ATOM 487 CE LYS A 156 91.969 29.362 -4.522 1.00 0.00

ATOM 488 NZ LYS A 156 92.638 30.566 -3.957 1.00 0.00

ATOM 489 N LYS A 157 86.611 28.791 -8.706 1.00 0.00

ATOM 490 CA LYS A 157 85.403 29.340 -9.287 1.00 0.00

ATOM 491 C LYS A 157 84.496 28.214 -9.787 1.00 0.00

ATOM 492 O LYS A 157 83.266 28.302 -9.732 1.00 0.00 ATOM 493 CB LYS A 157 85.742 30.252 -10.467 1.00 0.00

ATOM 494 CG LYS A 157 86.413 31.557 -10.071 1.00 0.00

ATOM 495 CD LYS A 157 86.725 32.409 -11.290 1.00 0.00

ATOM 496 CE LYS A 157 87.396 33.715 -10.892 1.00 0.00

ATOM 497 NZ LYS A 157 87.734 34.549 -12.079 1.00 0.00

ATOM 498 N THR A 158 85.122 27.144 -10.256 1.00 0.00

ATOM 499 CA THR A 158 84.393 26.001 -10.783 1.00 0.00

ATOM 500 C THR A 158 83.680 25.265 -9.648 1.00 0.00

ATOM 501 O THR A 158 82.528 24.831 -9.784 1.00 0.00

ATOM 502 CB THR A 158 85.336 25.005 -11.483 1.00 0.00

ATOM 503 OGl THR A 158 85.974 25.646 -12.594 1.00 0.00

ATOM 504 CG2 THR A 158 84.557 23.801 -11.991 1.00 0.00

ATOM 505 N LEU A 159 84.374 25.148 -8.529 1.00 0.00

ATOM 506 CA LEU A 159 83.847 24.488 -7.349 1.00 0.00

ATOM 507 C LEU A 159 82.698 25.303 -6.736 1.00 0.00

ATOM 508 O LEU A 159 81.738 24.747 -6.214 1.00 0.00

ATOM 509 CB LEU A 159 84.939 24.329 -6.290 1.00 0.00

ATOM 510 CG LEU A 159 86.062 23.341 -6.617 1.00 0.00

ATOM 511 CDl LEU A 159 87.164 23.414 -5.571 1.00 0.00

ATOM 512 CD2 LEU A 159 85.531 21.916 -6.651 1.00 0.00

ATOM 513 N CYS A 160 82.799 26.624 -6.801 1.00 0.00

ATOM 514 CA CYS A 160 81.745 27.468 -6.248 1.00 0.00

ATOM 515 C CYS A 160 80.509 27.387 -7.146 1.00 0.00

ATOM 516 O CYS A 160 79.372 27.484 -6.676 1.00 0.00

ATOM 517 CB CYS A 160 82.210 28.923 -6.168 1.00 0.00

ATOM 518 SG CYS A 160 83.506 29.227 -4.944 1.00 0.00

ATOM 519 N SER A 161 80.734 27.214 -8.444 1.00 0.00

ATOM 520 CA SER A 161 79.634 27.091 -9.385 1.00 0.00

ATOM 521 C SER A 161 78.988 25.733 -9.165 1.00 0.00

ATOM 522 O SER A 161 77.785 25.583 -9.324 1.00 0.00

ATOM 523 CB SER A 161 80.145 27.197 -10.824 1.00 0.00

ATOM 524 OG SER A 161 80.676 28.484 -11.083 1.00 0.00

ATOM 525 N LYS A 162 79.802 24.756 -8.782 1.00 0.00

ATOM 526 CA LYS A 162 79.323 23.402 -8.512 1.00 0.00

ATOM 527 C LYS A 162 78.362 23.434 -7.312 1.00 0.00

ATOM 528 O LYS A 162 77.226 22.985 -7.410 1.00 0.00

ATOM 529 CB LYS A 162 80.496 22.473 -8.190 1.00 0.00

ATOM 530 CG LYS A 162 80.089 21.038 -7.898 1.00 0.00

ATOM 531 CD LYS A 162 81.302 20.165 -7.623 1.00 0.00

ATOM 532 CE LYS A 162 80.894 18.734 -7.314 1.00 0.00

ATOM 533 NZ LYS A 162 82.072 17.873 -7.012 1.00 0.00

ATOM 534 N ALA A 163 78.818 23.963 -6.179 1.00 0.00

ATOM 535 CA ALA A 163 77.957 24.046 -5.006 1.00 0.00

ATOM 536 C ALA A 163 76.659 24.742 -5.407 1.00 0.00

ATOM 537 O ALA A 163 75.587 24.262 -5.078 1.00 0.00

ATOM 538 CB ALA A 163 78.639 24.841 -3.903 1.00 0.00

ATOM 539 N GLU A 164 76.727 25.863 -6.120 1.00 0.00

ATOM 540 CA GLU A 164 75.483 26.522 -6.536 1.00 0.00

ATOM 541 C GLU A 164 74.564 25.561 -7.323 1.00 0.00

ATOM 542 O GLU A 164 73.384 25.353 -6.989 1.00 0.00

ATOM 543 CB GLU A 164 75.786 27.722 -7.436 1.00 0.00

ATOM 544 CG GLU A 164 74.554 28.494 -7.878 1.00 0.00

ATOM 545 CD GLU A 164 74.896 29.693 -8.739 1.00 0.00

ATOM 546 OEl GLU A 164 76.099 29.929 -8.979 1.00 0.00

ATOM 547 OE2 GLU A 164 73.961 30.399 -9.174 1.00 0.00

ATOM 548 N ASN A 165 75.125 24.981 -8.373 1.00 0.00

ATOM 549 CA ASN A 165 74.436 24.028 -9.237 1.00 0.00

ATOM 550 C ASN A 165 73.706 22.926 -8.444 1.00 0.00

ATOM 551 O ASN A 165 72.522 22.642 -8.673 1.00 0.00

ATOM 552 CB ASN A 165 75.431 23.334 -10.170 1.00 0.00

ATOM 553 CG ASN A 165 75.933 24.248 -11.271 1.00 0.00

ATOM 554 ODl ASN A 165 75.340 25.292 -11.542 1.00 0.00

ATOM 555 ND2 ASN A 165 77.030 23.856 -11.908 1.00 0.00

ATOM 556 N ALA A 166 74.416 22.319 -7.498 1.00 0.00

ATOM 557 CA ALA A 166 73.837 21.259 -6.687 1.00 0.00

ATOM 558 C ALA A 166 72.681 21.811 -5.850 1.00 0.00

ATOM 559 O ALA A 166 71.656 21.144 -5.697 1.00 0.00

ATOM 560 CB ALA A 166 74.884 20.677 -5.749 1.00 0.00 ATOM 561 N ARG A 167 72.831 23.017 -5.314 .00 0.00

ATOM 562 CA ARG A 167 71.764 23.598 -4.500 .00 0.00

ATOM 563 C ARG A 167 70.496 23.772 -5.313 .00 0.00

ATOM 564 O ARG A 167 69.409 399 -4.873 .00 0.00

ATOM 565 CB ARG A 167 72.182 970 -3.968 .00 0.00

ATOM 566 CG ARG A 167 73.262 24.919 -2.900 .00 0.00

ATOM 567 CD ARG A 167 73.662 26.315 -2.451 .00 0.00

ATOM 568 NE ARG A 167 74.734 26.285 -1.459 .00 0.00

ATOM 569 CZ ARG A 167 75.306 27.369 -0.944 .00 0.00

ATOM 570 NHl ARG A 167 76.275 27.244 -0.047 .00 0.00

ATOM 571 NH2 ARG A 167 74.908 28.574 -1.327 .00 0.00

ATOM 572 N LEU A 168 70.638 24.340 -6.503 .00 0.00

ATOM 573 CA LEU A 168 69.485 24.548 -7.361 .00 0.00

ATOM 574 C LEU A 168 68.875 23.257 -7.862 .00 0.00

ATOM 575 O LEU A 168 67.657 23.167 -7.992 .00 0.00

ATOM 576 CB LEU A 168 69.875 25.366 -8.594 .00 0.00

ATOM 577 CG LEU A 168 70.239 26.832 -8.347 .00 0.00

ATOM 578 CDl LEU A 168 70.775 27.473 -9.617 .00 0.00

ATOM 579 CD2 LEU A 168 69.019 27.619 -7.895 .00 0.00

ATOM 580 N VAL A 169 69.690 22.252 -8.155 .00 0.00

ATOM 581 CA VAL A 169 69.096 21.012 -8.631 .00 0.00

ATOM 582 C VAL A 169 68.298 20.348 -7.525 1..00 0.00

ATOM 583 O VAL A 169 67.207 19.854 -7.782 1..00 0.00

ATOM 584 CB VAL A 169 70.170 20.015 -9.104 1..00 0.00

ATOM 585 CGl VAL A 169 69.544 18.666 -9.417 1.00 0.00

ATOM 586 CG2 VAL A 169 70.856 20.530 -10.360 1.00 0.00

ATOM 587 N VAL A 170 68.809 20.329 -6.294 1.00 0.00

ATOM 588 CA VAL A 170 68.032 19.733 -5.204 1.00 0.00

ATOM 589 C VAL A 170 66.711 20.499 -5.042 1.00 0.00

ATOM 590 O VAL A 170 65.637 19.906 -4.916 1.00 0.00

ATOM 591 CB VAL A 170 68.797 19.792 -3.869 1..00 0.00

ATOM 592 CGl VAL A 170 67.900 19.354 -2.720 1..00 0.00

ATOM 593 CG2 VAL A 170 70.010 18.874 -3.908 1.00 0.00

ATOM 594 N GLU A 171 66.792 21.830 -5.074 1.00 0.00

ATOM 595 CA GLU A 171 65.600 22.655 -4.950 1.00 0.00

ATOM 596 C GLU A 171 64.632 22.273 -6.072 1.00 0.00

ATOM 597 O GLU A 171 63.428 2 ,' .129 -5.826 1.00 0.00

ATOM 598 CB GLU A 171 65.961 24 . 138 -5.069 1.00 0.00

ATOM 599 CG GLU A 171 66.726 687 -3.877 1..00 0.00

ATOM 600 CD GLU A 171 67.173 122 -4.082 1..00 0.00

ATOM 601 OEl GLU A 171 66.948 26. 662 -5.185 1..00 0.00

ATOM 602 OE2 GLU A 171 67.748 26. 705 -3.139 1.00 0.00

ATOM 603 N ILE A 172 65.154 22.089 -7.285 1.00 0.00

ATOM 604 CA ILE A 172 64.278 21.729 -8.403 1.00 0.00

ATOM 605 C ILE A 172 63.636 20.392 -8.182 1.00 0.00

ATOM 606 O ILE A 172 62.439 20.257 -8.408 1.00 0.00

ATOM 607 CB ILE A 172 65.057 .656 -9.730 1..00 0.00

ATOM 608 CGl ILE A 172 65.536 .048 -10.146 1..00 0.00

ATOM 609 CG2 ILE A 172 64.174 .099 -10.836 1..00 0.00

ATOM 610 CDl ILE A 172 66.529 23.036 -11.287 1.00 0.00

ATOM 611 N ASP A 173 64.408 19.405 -7.732 1.00 0.00

ATOM 612 CA ASP A 173 63.820 18.100 -7.459 1.00 0.00

ATOM 613 C ASP A 173 .639 18 62 -6.521 1.00 0.00

ATOM 614 O ASP A 173 61 . 557 17.738 -6.767 1.00 0.00

ATOM 615 CB ASP A 173 64 . 849 17.176 -6.805 1.00 0.00

ATOM 616 CG ASP A 173 65 . 909 16.701 -7.780 1..00 0.00

ATOM 617 ODl ASP A 173 65 . 723 16.897 -9.001 1..00 0.00

ATOM 618 OD2 ASP A 173 66. 924 16.134 -7.325 1.00 0.00

ATOM 619 N ASN A 174 62 . 830 19.004 -5.447 1.00 0.00

ATOM 620 CA ASN A 174 61 . 728 19.171 -4.514 1.00 0.00

ATOM 621 C ASN A 174 60 . 535 19.859 -5.143 1.00 0.00

ATOM 622 O ASN A 174 59 . 384 19.516 -4.851 1.00 0.00

ATOM 623 CB ASN A 174 62 . 164 20.017 -3.316 1.00 0.00

ATOM 624 CG ASN A 174 63 . 085 19.266 -2.376 00 0.00

ATOM 625 ODl ASN A 174 63 . 128 18.035 -2.386 00 0.00

ATOM 626 ND2 ASN A 174 63 . 826 20.005 -1.560 00 0.00

ATOM 627 N ALA A 175 60 . 784 20.814 -6.030 00 0.00

ATOM 628 CA ALA A 175 59 . 647 21.473 -6.646 1.00 0.00 ATOM 629 C ALA A 175 58.948 20.503 -7.563 1.00 0.00

ATOM 630 O ALA A 175 57.726 20.427 -7.542 1.00 0.00

ATOM 631 CB ALA A 175 60.105 22.678 -7.452 1.00 0.00

ATOM 632 N LYS A 176 59.698 19.735 -8.347 1.00 0.00

ATOM 633 CA LYS A 176 59.053 18.779 -9.228 1.00 0.00

ATOM 634 C LYS A 176 58.190 17.772 -8.487 1.00 0.00

ATOM 635 O LYS A 176 57.100 17.444 -8.949 1.00 0.00

ATOM 636 CB LYS A 176 60.099 17.983 -10.011 1.00 0.00

ATOM 637 CG LYS A 176 60.834 18.793 -11.066 1.00 0.00

ATOM 638 CD LYS A 176 61.853 17.941 -11.806 1.00 0.00

ATOM 639 CE LYS A 176 62.605 18.758 -12.844 1.00 0.00

ATOM 640 NZ LYS A 176 63.630 17.944 -13.554 1.00 0.00

ATOM 641 N LEU A 177 58.661 17.287 -7.338 1.00 0.00

ATOM 642 CA LEU A 177 57.871 16.340 -6.551 1.00 0.00

ATOM 643 C LEU A 177 56.608 17.012 -6.076 1.00 0.00

ATOM 644 O LEU A 177 55.512 16.463 -6.169 1.00 0.00

ATOM 645 CB LEU A 177 58.666 15.860 -5.336 1.00 0.00

ATOM 646 CG LEU A 177 57.955 14.872 -4.408 1.00 0.00

ATOM 647 CDl LEU A 177 57.610 13.590 -5.150 1.00 0.00

ATOM 648 CD2 LEU A 177 58.841 14.512 -3.225 1.00 0.00

ATOM 649 N ALA A 178 56.779 18.209 -5.557 1.00 0.00

ATOM 650 CA ALA A 178 55.653 18.981 -5.106 1.00 0.00

ATOM 651 C ALA A 178 54.622 19.044 -6.233 1.00 0.00

ATOM 652 O ALA A 178 53.460 18.718 -6.066 1.00 0.00

ATOM 653 CB ALA A 178 56.088 20.391 -4.740 1.00 0.00

ATOM 654 N ALA A 179 55.096 19.467 -7.390 1.00 0.00

ATOM 655 CA ALA A 179 54.306 19.600 -8.600 1.00 0.00

ATOM 656 C ALA A 179 53.477 18.345 -8.930 1.00 0.00

ATOM 657 O ALA A 179 52.250 18.383 -9.024 1.00 0.00

ATOM 658 CB ALA A 179 55.207 19.865 -9.796 1.00 0.00

ATOM 659 N ASP A 180 54.169 17.230 -9.134 1.00 0.00

ATOM 660 CA ASP A 180 53.504 15.979 -9.450 1.00 0.00

ATOM 661 C ASP A 180 52.400 15.705 -8.415 1.00 0.00

ATOM 662 O ASP A 180 51.232 15.466 -8.742 1.00 0.00

ATOM 663 CB ASP A 180 54.504 14.821 -9.425 1.00 0.00

ATOM 664 CG ASP A 180 55.444 14.838 -10.615 1.00 0.00

ATOM 665 ODl ASP A 180 55.181 15.600 -11.569 1.00 0.00

ATOM 666 OD2 ASP A 180 56.443 14.089 -10.593 1.00 0.00

ATOM 667 N ASP A 181 52.779 15.770 -7.149 1.00 0.00

ATOM 668 CA ASP A 181 51.856 15.560 -6.055 1.00 0.00

ATOM 669 C ASP A 181 50.611 16.456 -6.180 1.00 0.00

ATOM 670 O ASP A 181 49.499 15.953 -6.269 1.00 0.00

ATOM 671 CB ASP A 181 52.529 15.879 -4.719 1.00 0.00

ATOM 672 CG ASP A 181 53.524 14.815 -4.300 1.00 0.00

ATOM 673 ODl ASP A 181 53.553 13.743 -4.939 1.00 0.00

ATOM 674 OD2 ASP A 181 54.277 15.054 -3.332 1.00 0.00

ATOM 675 N PHE A 182 50.804 17.771 -6.192 1.00 0.00

ATOM 676 CA PHE A 182 49.682 18.696 -6.339 1.00 0.00

ATOM 677 C PHE A 182 48.791 18.389 -7.524 1.00 0.00

ATOM 678 O PHE A 182 47.586 18.553 -7.443 1.00 0.00

ATOM 679 CB PHE A 182 50.189 20.127 -6.527 1.00 0.00

ATOM 680 CG PHE A 182 50.650 20.779 -5.254 1.00 0.00

ATOM 681 CDl PHE A 182 51.999 20.893 -4.967 1.00 0.00

ATOM 682 CD2 PHE A 182 49.734 21.277 -4.343 1.00 0.00

ATOM 683 CEl PHE A 182 52.423 21.493 -3.796 1.00 0.00

ATOM 684 CE2 PHE A 182 50.158 21.877 -3.173 1.00 0.00

ATOM 685 CZ PHE A 182 51.496 21.986 -2.897 1.00 0.00

ATOM 686 N ARG A 183 49.393 17.979 -8.637 1.00 0.00

ATOM 687 CA ARG A 183 48.646 17.636 -9.848 1.00 0.00

ATOM 688 C ARG A 183 47.735 16.447 -9.625 1.00 0.00

ATOM 689 O ARG A 183 46.591 16.411 -10.067 1.00 0.00

ATOM 690 CB ARG A 183 49.604 17.284 -10.988 1.00 0.00

ATOM 691 CG ARG A 183 50.374 18.472 -11.540 1.00 0.00

ATOM 692 CD ARG A 183 51.339 18.044 -12.635 1.00 0.00

ATOM 693 NE ARG A 183 52.122 19.168 -13.144 1.00 0.00

ATOM 694 CZ ARG A 183 53.076 19.058 -14.063 1.00 0.00

ATOM 695 NHl ARG A 183 53.737 20.135 -14.465 1.00 0.00

ATOM 696 NH2 ARG A 183 53.366 17.871 -14.578 1.00 0.00 ATOM 697 N THR A 184 48.300 15.433 -8.993 ,00 0.00

ATOM 698 CA THR A 184 47.588 14.206 -8.704 ,00 0.00

ATOM 699 C THR A 184 46.415 14.543 -7.778 ,00 0.00

ATOM 700 O THR A 184 45.266 14.182 -8.051 ,00 0.00

ATOM 701 CB THR A 184 48.498 13.174 -8.012 ,00 0.00

ATOM 702 OGl THR A 184 49.585 12.833 -8.881 1.00 0.00

ATOM 703 CG2 THR A 184 47.717 11.911 -7 682 00 0.00

ATOM 704 N LYS A 185 46.722 15.259 -6.696 00 0.00

ATOM 705 CA LYS A 185 45.737 15.707 -5.703 00 0.00

ATOM 706 C LYS A 185 44.610 16.433 -6.395 00 0.00

ATOM 707 O LYS A 185 43.444 16.172 -6.127 00 0.00

ATOM 708 CB LYS A 185 46.389 16.654 -4.693 00 0.00

ATOM 709 CG LYS A 185 47.367 15.976 -3.748 00 0.00

ATOM 710 CD LYS A 185 47.952 16.967 -2.755 00 0.00

ATOM 711 CE LYS A 185 48.912 16.284 -1.794 00 0.00

ATOM 712 NZ LYS A 185 49.535 17.252 -0.849 00 0.00

ATOM 713 N TYR A 186 44.978 17.375 -7.254 00 0.00

ATOM 714 CA TYR A 186 43.977 18.143 -7.973 00 0.00

ATOM 715 C TYR A 186 43.122 17.296 -8.891 00 0.00

ATOM 716 O TYR A 186 41.934 17.569 -9.051 00 0.00

ATOM 717 CB TYR A 186 44.643 19.211 -8.841 00 0.00

ATOM 718 CG TYR A 186 43.669 20.040 -9.649 00 0.00

ATOM 719 CDl TYR A 186 42.947 21.067 -9.055 00 0.00

ATOM 720 CD2 TYR A 186 43.477 19.792 -11.001 00 0.00

ATOM 721 CEl TYR A 186 42.054 21.828 -9.784 00 0.00

ATOM 722 CE2 TYR A 186 42.588 20.544 -11.748 00 0.00

ATOM 723 CZ TYR A 186 41.875 21.569 -11.126 00 0.00

ATOM 724 OH TYR A 186 40.987 22.326 -11.855 00 0.00

ATOM 725 N GLU A 187 43.709 16.270 -9.507 00 0.00

ATOM 726 CA GLU A 187 42.943 15.400 -10.394 00 0.00

ATOM 727 C GLU A 187 41.876 14.728 -9.551 00 0.00

ATOM 728 O GLU A 187 40.691 14.733 -9.894 00 0.00

ATOM 729 CB GLU A 187 43.853 14.347 -11.029 00 0.00

ATOM 730 CG GLU A 187 43.146 13.423 -12, 007 00 0.00

ATOM 731 CD GLU A 187 44.085 12.416 12, 640 00 0.00

ATOM 732 OEl GLU A 187 45.292 12.449 12, 324 00 0.00

ATOM 733 OE2 GLU A 187 43.613 11.593 -13.453 00 0.00

ATOM 734 N THR A 188 42.299 14.161 -8.429 00 0.00

ATOM 735 CA THR A 188 41.350 13.512 -7.557 00 0.00

ATOM 736 C THR A 188 40.259 14.478 -7.115 00 0.00

ATOM 737 O THR A 188 39.074 14.165 -7.258 00 0.00

ATOM 738 CB THR A 188 42.030 12.967 -6.288 00 0.00

ATOM 739 OGl THR A 188 43.007 11.983 -6.651 00 0.00

ATOM 740 CG2 THR A 188 41.003 12.325 -5.368 1.00 0.00

ATOM 741 N GLU A 189 40.620 15.665 -6.636 ,00 0.00

ATOM 742 CA GLU A 189 39.569 16.572 -6.193 ,00 0.00

ATOM 743 C GLU A 189 38.632 17.058 -7.272 ,00 0.00

ATOM 744 O GLU A 189 37.459 17.228 -6.996 ,00 0.00

ATOM 745 CB GLU A 189 40.175 17.831 -5.570 ,00 0.00

ATOM 746 CG GLU A 189 39.147 18.808 -5.022 ,00 0.00

ATOM 747 CD GLU A 189 39.785 20.015 -4.362 ,00 0.00

ATOM 748 OEl GLU A 189 41.032 20.077 -4.316 ,00 0.00

ATOM 749 OE2 GLU A 189 39.038 20.898 -3.890 ,00 0.00

ATOM 750 N VAL A 190 39.116 17.286 -8.492 ,00 0.00

ATOM 751 CA VAL A 190 38.200 17.751 -9.521 ,00 0.00

ATOM 752 C VAL A 190 37.225 16.655 -9.870 ,00 0.00

ATOM 753 O VAL A 190 36.084 16.930 -10.224 ,00 0.00

ATOM 754 CB VAL A 190 38.951 18.156 -10.803 ,00 0.00

ATOM 755 CGl VAL A 190 37.967 18.464 -11.921 ,00 0.00

ATOM 756 CG2 VAL A 190 39.800 19.394 -10.555 ,00 0.00

ATOM 757 N SER A 191 37.673 15.415 -9.773 ,00 0.00

ATOM 758 CA SER A 191 36.785 14.304 -10.082 ,00 0.00

ATOM 759 C SER A 191 35.710 14.272 -9.001 ,00 0.00

ATOM 760 O SER A 191 34.515 14.196 -9.283 ,00 0.00

ATOM 761 CB SER A 191 37.560 12.985 -10.093 ,00 0.00

ATOM 762 OG SER A 191 38.495 12.952 -11.157 ,00 0.00

ATOM 763 N LEU A 192 36.167 14.351 -7.762 ,00 0.00

ATOM 764 CA LEU A 192 35.304 14.363 -6.597 1.00 0.00 ATOM 765 C LEU A 192 34.287 15.517 -6.652 1.00 0.00

ATOM 766 O LEU A 192 33.122 15.350 -6.289 1.00 0.00

ATOM 767 CB LEU A 192 36.129 14.528 -5.320 1.00 0.00

ATOM 768 CG LEU A 192 37.010 13.341 -4.923 1.00 0.00

ATOM 769 CDl LEU A 192 37.906 13.705 -3.749 1.00 0.00

ATOM 770 CD2 LEU A 192 36.156 12.150 -4.518 1.00 0.00

ATOM 771 N ARG A 193 34.749 16.681 -7.101 1.00 0.00

ATOM 772 CA ARG A 193 33.896 17.866 -7.218 1.00 0.00

ATOM 773 C ARG A 193 32.848 17.589 -8.273 1.00 0.00

ATOM 774 O ARG A 193 31.665 17.799 -8.043 1.00 0.00

ATOM 775 CB ARG A 193 34.726 19.085 -7.625 1.00 0.00

ATOM 776 CG ARG A 193 33.926 20.373 -7.731 1.00 0.00

ATOM 111 CD ARG A 193 34.796 21.525 -8.206 1.00 0.00

ATOM 778 NE ARG A 193 35.274 21.323 -9.571 1.00 0.00

ATOM 779 CZ ARG A 193 34.538 21.524 -10.659 1.00 0.00

ATOM 780 NHl ARG A 193 35.057 21.314 -11.861 1.00 0.00

ATOM 781 NH2 ARG A 193 33.282 21.936 -10.542 1.00 0.00

ATOM 782 N GLN A 194 33.278 17.139 -9.444 1.00 0.00

ATOM 783 CA GLN A 194 32.317 16.828 -10.488 1.00 0.00

ATOM 784 C GLN A 194 31.214 15.895 -9.962 1.00 0.00

ATOM 785 O GLN A 194 30.027 16.112 -10.218 1.00 0.00

ATOM 786 CB GLN A 194 33.008 16.134 -11.663 1.00 0.00

ATOM 787 CG GLN A 194 32.085 15.823 -12.830 1.00 0.00

ATOM 788 CD GLN A 194 32.809 15.156 -13.984 1.00 0.00

ATOM 789 OEl GLN A 194 33.991 14.826 -13.880 1.00 0.00

ATOM 790 NE2 GLN A 194 32.100 14.954 -15.089 1.00 0.00

ATOM 791 N LEU A 195 31.600 14.871 -9.212 1.00 0.00

ATOM 792 CA LEU A 195 30.624 13.942 -8.646 1.00 0.00

ATOM 793 C LEU A 195 29.665 14.646 -7.699 1.00 0.00

ATOM 794 O LEU A 195 28.455 14.470 -7.792 1.00 0.00

ATOM 795 CB LEU A 195 31.329 12.834 -7.861 1.00 0.00

ATOM 796 CG LEU A 195 30.426 11.794 -7.196 1.00 0.00

ATOM 797 CDl LEU A 195 29.613 11.044 -8.238 1.00 0.00

ATOM 798 CD2 LEU A 195 31.254 10.782 -6.419 1.00 0.00

ATOM 799 N VAL A 196 30.205 15.443 -6.787 1.00 0.00

ATOM 800 CA VAL A 196 29.368 16.187 -5.858 1.00 0.00

ATOM 801 C VAL A 196 28.347 17.035 -6.577 1.00 0.00

ATOM 802 O VAL A 196 27.191 17.095 -6.169 1.00 0.00

ATOM 803 CB VAL A 196 30.206 17.132 -4.978 1.00 0.00

ATOM 804 CGl VAL A 196 29.300 18.039 -4.158 1.00 0.00

ATOM 805 CG2 VAL A 196 31.080 16.335 -4.021 1.00 0.00

ATOM 806 N GLU A 197 28.787 17.711 -7.634 1.00 0.00

ATOM 807 CA GLU A 197 27.911 18.562 -8.424 1.00 0.00

ATOM 808 C GLU A 197 26.766 17.746 -9.003 1.00 0.00

ATOM 809 O GLU A 197 25.593 18.097 -8.854 1.00 0.00

ATOM 810 CB GLU A 197 28.685 19.203 -9.579 1.00 0.00

ATOM 811 CG GLU A 197 27.855 20.147 -10.432 1.00 0.00

ATOM 812 CD GLU A 197 28.663 20.788 -11.544 1.00 0.00

ATOM 813 OEl GLU A 197 29.875 20.503 -11.638 1.00 0.00

ATOM 814 OE2 GLU A 197 28.083 21.575 -12.321 1.00 0.00

ATOM 815 N SER A 198 27.091 16.653 -9.670 1.00 0.00

ATOM 816 CA SER A 198 26.030 15.826 -10.214 1.00 0.00

ATOM 817 C SER A 198 25.056 15.473 -9.080 1.00 0.00

ATOM 818 O SER A 198 23.857 15.714 -9.200 1.00 0.00

ATOM 819 CB SER A 198 26.606 14.539 -10.809 1.00 0.00

ATOM 820 OG SER A 198 27.401 14.815 -11.949 1.00 0.00

ATOM 821 N ASP A 199 25.558 14.928 -7.978 1.00 0.00

ATOM 822 CA ASP A 199 24.677 14.556 -6.861 1.00 0.00

ATOM 823 C ASP A 199 23.783 15.691 -6.380 1.00 0.00

ATOM 824 O ASP A 199 22.606 15.478 -6.101 1.00 0.00

ATOM 825 CB ASP A 199 25.503 14.106 -5.654 1.00 0.00

ATOM 826 CG ASP A 199 26.137 12.744 -5.858 1.00 0.00

ATOM 827 ODl ASP A 199 25.761 12.052 -6.828 1.00 0.00

ATOM 828 OD2 ASP A 199 27.011 12.369 -5.048 1.00 0.00

ATOM 829 N ILE A 200 24.322 16.894 -6.265 1.00 0.00

ATOM 830 CA ILE A 200 23.482 17.992 -5.808 1.00 0.00

ATOM 831 C ILE A 200 22.411 18.305 -6.849 1.00 0.00

ATOM 832 O ILE A 200 21.311 18.725 -6.494 1.00 0.00 ATOM 833 CB ILE A 200 24.305 19.271 -5.569 1.00 0.00

ATOM 834 CGl ILE A 200 25.243 19.087 -4.374 1.00 0.00

ATOM 835 CG2 ILE A 200 23.387 20.450 -5.284 1.00 0.00

ATOM 836 CDl ILE A 200 26.269 20.189 -4.228 1.00 0.00

ATOM 837 N ASN A 201 99 n 9 o 18.115 -8.133 1.00 0.00

ATOM 838 CA ASN A 201 21.733 18.406 -9.168 1.00 0.00

ATOM 839 C ASN A 201 20.617 17.407 -9.026 1.00 0.00

ATOM 840 O ASN A 201 19.443 17.774 -8.948 1.00 0.00

ATOM 841 CB ASN A 201 22.362 18.289 -10.559 1.00 0.00

ATOM 842 CG ASN A 201 23.303 19.437 -10.871 1.00 0.00

ATOM 843 ODl ASN A 201 23.223 20.502 -10.258 1.00 0.00

ATOM 844 ND2 ASN A 201 24.199 19.223 -11.827 1.00 0.00

ATOM 845 N GLY A 202 20.996 16.136 -8.995 1.00 0.00

ATOM 846 CA GLY A 202 20.007 15.083 -8.888 1.00 0.00

ATOM 847 C GLY A 202 19.125 15.268 -7.674 1.00 0.00

ATOM 848 O GLY A 202 17.908 15.406 -7.785 1.00 0.00

ATOM 849 N LEU A 203 19.747 15.267 -6.506 1.00 0.00

ATOM 850 CA LEU A 203 19.007 15.450 -5.277 1.00 0.00

ATOM 851 C LEU A 203 18.075 16.644 -5.427 1.00 0.00

ATOM 852 O LEU A 203 16.901 16.544 -5.108 1.00 0.00

ATOM 853 CB LEU A 203 19.962 15.704 -4.109 1.00 0.00

ATOM 854 CG LEU A 203 19.314 15.926 -2.740 1.00 0.00

ATOM 855 CDl LEU A 203 18.554 14.685 -2.298 1.00 0.00

ATOM 856 CD2 LEU A 203 20.370 16.234 -1.690 1.00 0.00

ATOM 857 N ARG A 204 18.581 17.759 -5.942 1.00 0.00

ATOM 858 CA ARG A 204 17.740 18.937 -6.131 1.00 0.00

ATOM 859 C ARG A 204 16.477 18.615 -6.940 1.00 0.00

ATOM 860 O ARG A 204 15.366 19.005 -6.572 1.00 0.00

ATOM 861 CB ARG A 204 18.506 20.028 -6.882 1.00 0.00

ATOM 862 CG ARG A 204 17.742 21.332 -7.031 1.00 0.00

ATOM 863 CD ARG A 204 18.505 22.324 -7.894 1.00 0.00

ATOM 864 NE ARG A 204 18.615 21.872 -9.279 1.00 0.00

ATOM 865 CZ ARG A 204 17.635 21.957 -10.172 1.00 0.00

ATOM 866 NHl ARG A 204 17.826 21.521 -11.410 1.00 0.00

ATOM 867 NH2 ARG A 204 16.465 22.478 -9.827 1.00 0.00

ATOM 868 N ARG A 205 16.663 17.917 -8.055 1.00 0.00

ATOM 869 CA ARG A 205 15.546 17.537 -8.904 1.00 0.00

ATOM 870 C ARG A 205 14.546 16.808 -8.023 1.00 0.00

ATOM 871 O ARG A 205 13.402 17.239 -7.865 1.00 0.00

ATOM 872 CB ARG A 205 16.020 16.623 -10.035 1.00 0.00

ATOM 873 CG ARG A 205 14.922 16.212 -11.003 1.00 0.00

ATOM 874 CD ARG A 205 15.461 15.308 -12.099 1.00 0.00

ATOM 875 NE ARG A 205 14.423 14.925 -13.053 1.00 0.00

ATOM 876 CZ ARG A 205 14.583 14.011 -14.004 1.00 0.00

ATOM 877 NHl ARG A 205 13.582 13.727 -14.826 1.00 0.00

ATOM 878 NH2 ARG A 205 15.743 13.383 -14.132 1.00 0.00

ATOM 879 N ILE A 206 14.999 15.719 -7.421 1.00 0.00

ATOM 880 CA ILE A 206 14.143 14.934 -6.547 1.00 0.00

ATOM 881 C ILE A 206 13.429 15.725 -5.488 1.00 0.00

ATOM 882 O ILE A 206 12.241 15.516 -5.264 1.00 0.00

ATOM 883 CB ILE A 206 14.945 13.858 -5.790 1.00 0.00

ATOM 884 CGl ILE A 206 15.456 12.792 -6.760 1.00 0.00

ATOM 885 CG2 ILE A 206 14.071 13.181 -4.745 1.00 0.00

ATOM 886 CDl ILE A 206 16.474 11.852 -6.153 1.00 0.00

ATOM 887 N LEU A 207 14.136 16.624 -4.822 1.00 0.00

ATOM 888 CA LEU A 207 13.471 17.401 -3.799 1.00 0.00

ATOM 889 C LEU A 207 12.303 18.127 -4.428 1.00 0.00

ATOM 890 O LEU A 207 11.234 18.201 -3.847 1.00 0.00

ATOM 891 CB LEU A 207 14.435 18.421 -3.190 1.00 0.00

ATOM 892 CG LEU A 207 13.869 19.307 -2.077 1.00 0.00

ATOM 893 CDl LEU A 207 13.420 18.463 -0.895 1.00 0.00

ATOM 894 CD2 LEU A 207 14.921 20.290 -1.588 1.00 0.00

ATOM 895 N ASP A 208 12.512 18.639 -5.635 1.00 0.00

ATOM 896 CA ASP A 208 11.468 19.373 -6.325 1.00 0.00

ATOM 897 C ASP A 208 10.257 18.502 -6.655 1.00 0.00

ATOM 898 O ASP A 208 9.115 18.845 -6.339 1.00 0.00

ATOM 899 CB ASP A 208 11.994 19.940 -7.646 1.00 0.00

ATOM 900 CG ASP A 208 12.945 21.103 -7.443 1.00 0.00 ATOM 901 ODl ASP A 208 13.013 21.624 -6.310 1.00 0.00

ATOM 902 OD2 ASP A 208 13.622 21.493 -8.418 1.00 0.00

ATOM 903 N ASP A 209 10.519 17.378 -7.302 1.00 0.00

ATOM 904 CA ASP A 209 9.466 16.439 -7.662 1.00 0.00

ATOM 905 C ASP A 209 8.663 16.088 -6.414 1.00 0.00

ATOM 906 O ASP A 209 7.428 15.994 -6.440 1.00 0.00

ATOM 907 CB ASP A 209 10.065 15.160 -8.249 1.00 0.00

ATOM 908 CG ASP A 209 10.622 15.365 -9.644 1.00 0.00

ATOM 909 ODl ASP A 209 10.347 16.425 -10.244 1.00 0.00

ATOM 910 OD2 ASP A 209 11.334 14.464 -10.138 1.00 0.00

ATOM 911 N LEU A 210 9.360 15.919 -5.304 1.00 0.00

ATOM 912 CA LEU A 210 8.652 15.527 -4.110 1.00 0.00

ATOM 913 C LEU A 210 7.821 16.655 -3.534 1.00 0.00

ATOM 914 O LEU A 210 6.786 16.398 -2.929 1.00 0.00

ATOM 915 CB LEU A 210 9.636 15.083 -3.025 1.00 0.00

ATOM 916 CG LEU A 210 10.403 13.786 -3.294 1.00 0.00

ATOM 917 CDl LEU A 210 11.450 13.548 -2.217 1.00 0.00

ATOM 918 CD2 LEU A 210 9.456 12.596 -3.310 1.00 0.00

ATOM 919 N THR A 211 8.241 17.899 -3.716 1.00 0.00

ATOM 920 CA THR A 211 7.427 18.990 -3.198 1.00 0.00

ATOM 921 C THR A 211 6.121 19.057 -3.996 1.00 0.00

ATOM 922 O THR A 211 5.044 19.237 -3.433 1.00 0.00

ATOM 923 CB THR A 211 8.152 20.343 -3.320 1.00 0.00

ATOM 924 OGl THR A 211 9.358 20.313 -2.547 1.00 0.00

ATOM 925 CG2 THR A 211 7.268 21.470 -2.810 1.00 0.00

ATOM 926 N LEU A 212 6.212 18.924 -5.316 1.00 0.00

ATOM 927 CA LEU A 212 4.996 18.935 -6.131 1.00 0.00

ATOM 928 C LEU A 212 4.063 17.853 -5.627 1.00 0.00

ATOM 929 O LEU A 212 2.900 18.108 -5.300 1.00 0.00

ATOM 930 CB LEU A 212 5.334 18.669 -7.599 1.00 0.00

ATOM 931 CG LEU A 212 4.149 18.597 -8.564 1.00 0.00

ATOM 932 CDl LEU A 212 3.414 19.929 -8.615 1.00 0.00

ATOM 933 CD2 LEU A 212 4.620 18.263 -9.971 1.00 0.00

ATOM 934 N CYS A 213 4.572 16.630 -5.611 1.00 0.00

ATOM 935 CA CYS A 213 3.792 15.483 -5.172 1.00 0.00

ATOM 936 C CYS A 213 3.097 15.747 -3.848 1.00 0.00

ATOM 937 O CYS A 213 1.916 15.434 -3.679 1.00 0.00

ATOM 938 CB CYS A 213 4.693 14.259 -4.991 1.00 0.00

ATOM 939 SG CYS A 213 5.463 13.667 -6.514 1.00 0.00

ATOM 940 N LYS A 214 3.840 16.318 -2.906 1.00 0.00

ATOM 941 CA LYS A 214 3.277 16.616 -1.595 1.00 0.00

ATOM 942 C LYS A 214 2.128 17.591 -1.688 1.00 0.00

ATOM 943 O LYS A 214 1.094 17.413 -1.062 1.00 0.00

ATOM 944 CB LYS A 214 4.340 17.231 -0.682 1.00 0.00

ATOM 945 CG LYS A 214 3.844 17.554 0.718 1.00 0.00

ATOM 946 CD LYS A 214 4.972 18.067 1.597 1.00 0.00

ATOM 947 CE LYS A 214 4.447 18.562 2.936 1.00 0.00

ATOM 948 NZ LYS A 214 3.853 17.460 3.742 1.00 0.00

ATOM 949 N SER A 215 2.314 18.644 -2.465 1.00 0.00

ATOM 950 CA SER A 215 1.273 19.641 -2.580 1.00 0.00

ATOM 951 C SER A 215 0.011 19.071 -3.212 1.00 0.00

ATOM 952 O SER A 215 -1.116 19.359 -2.795 1.00 0.00

ATOM 953 CB SER A 215 1.743 20.809 -3.449 1.00 0.00

ATOM 954 OG SER A 215 2.804 21.514 -2.827 1.00 0.00

ATOM 955 N ASP A 216 0.223 18.254 -4.226 1.00 0.00

ATOM 956 CA ASP A 216 -0.871 17.648 -4.947 1.00 0.00

ATOM 957 C ASP A 216 -1.656 16.796 -3.946 1.00 0.00

ATOM 958 O ASP A 216 -2.885 16.829 -3.906 1.00 0.00

ATOM 959 CB ASP A 216 -0.343 16.770 -6.083 1.00 0.00

ATOM 960 CG ASP A 216 0.212 17.582 -7.237 1.00 0.00

ATOM 961 ODl ASP A 216 -0.024 18.808 -7.267 1.00 0.00

ATOM 962 OD2 ASP A 216 0.882 16.992 -8.111 1.00 0.00

ATOM 963 N LEU A 217 -0.940 16.076 -3.093 1.00 0.00

ATOM 964 CA LEU A 217 -1.612 15.262 -2.109 1.00 0.00

ATOM 965 C LEU A 217 -2.320 16.097 -1.042 1.00 0.00

ATOM 966 O LEU A 217 -3.429 15.749 -0.638 1.00 0.00

ATOM 967 CB LEU A 217 -0.612 14.356 -1.389 1.00 0.00

ATOM 968 CG LEU A 217 0.009 13.234 -2.224 1.00 0.00 ATOM 969 CDl LEU A 217 1..109 12.529 1.446 .00 0.00

ATOM 970 CD2 LEU A 217 -1..042 12.201 2.603 .00 0.00

ATOM 971 N GLU A 218 -1..736 17.197 0.578 .00 0.00

ATOM 972 CA GLU A 218 -2.453 17.974 0.438 .00 0.00

ATOM 973 C GLU A 218 -3.801 18.419 -0 121 .00 0.00

ATOM 974 O GLU A 218 -4.811 18.422 0.577 .00 0.00

ATOM 975 CB GLU A 218 -1.645 19.213 0.833 .00 0.00

ATOM 976 CG GLU A 218 -0.394 18.906 1.640 .00 0.00

ATOM 977 CD GLU A 218 0.444 20.140 1.908 .00 0.00

ATOM 978 OEl GLU A 218 0.085 21.223 1.399 .00 0.00

ATOM 979 OE2 GLU A 218 1.460 20.025 2.626 .00 0.00

ATOM 980 N ALA A 219 -3.805 18.767 1.402 .00 0.00

ATOM 981 CA ALA A 219 -5.015 19.187 2.087 .00 0.00

ATOM 982 C ALA A 219 -6.013 18.030 2.188 .00 0.00

ATOM 983 O ALA A 219 -7.157 18.146 -1 742 .00 0.00

ATOM 984 CB ALA A 219 -4.690 19.663 3.495 .00 0.00

ATOM 985 N GLN A 220 -5.578 16.920 2.797 .00 0.00

ATOM 986 CA GLN A 220 -6.429 15.731 954 .00 0.00

ATOM 987 C GLN A 220 -7.030 15.328 615 .00 0.00

ATOM 988 O GLN A 220 -8.215 15.022 518 1.00 0.00

ATOM 989 CB GLN A 220 -5.613 14.554 492 1.00 0.00

ATOM 990 CG GLN A 220 -6.4 8 13 95 3.740 1..00 0.00

ATOM 991 CD GLN A 220 -5.590 12.159 4.294 1..00 0.00

ATOM 992 OEl GLN A 220 -4.369 12.271 4.401 1..00 0.00

ATOM 993 NE2 GLN A 220 -6.246 11.059 4.646 1.00 0.00

ATOM 994 N VAL A 221 -6.196 15.344 0.586 1.00 0.00

ATOM 995 CA VAL A 221 -6.642 15.020 0.753 1.00 0.00

ATOM 996 C VAL A 221 -7.739 15.988 1.209 1.00 0.00

ATOM 997 O VAL A 221 -8.770 15.548 1.705 1.00 0.00

ATOM 998 CB VAL A 221 -5.488 15.106 1.768 1.00 0.00

ATOM 999 CGl VAL A 221 -6.015 14.959 3.188 1..00 0.00

ATOM 1000 CG2 VAL A 221 -4.473 14.001 1.516 1..00 0.00

ATOM 1001 N GLU A 222 -7.549 17.293 1.066 1.00 0.00

ATOM 1002 CA GLU A 222 -8.625 18.179 1.499 1.00 0.00

ATOM 1003 C GLU A 999 -9.930 17.904 0.746 1.00 0.00

ATOM 1004 O GLU A 222 -10.998 17. 1.345 1.00 0.00

ATOM 1005 CB GLU A 222 -8.247 19.641 1 55 1.00 0.00

ATOM 1006 CG GLU A 222 -7.157 20.162 2.177 1.00 0.00

ATOM 1007 CD GLU A 999 -6.722 21.571 1.826 1..00 0.00

ATOM 1008 OEl GLU A 999 -7.220 22.113 0.817 1..00 0.00

ATOM 1009 OE2 GLU A 222 -5.882 22.135 2.560 1.00 0.00

ATOM 1010 N SER A 223 -9.846 17.667 0.561 1.00 0.00

ATOM 1011 CA SER A 223 -11.048 17.412 -1 338 1.00 0.00

ATOM 1012 C SER A 223 -11.766 16.187 -0.782 1.00 0.00

ATOM 1013 O SER A -12.978 16.214 -0.552 1.00 0.00

ATOM 1014 CB SER A 223 -10.693 17.155 -2.805 1.00 0.00

ATOM 1015 OG SER A 223 -10.166 18.322 -3.414 1..00 0.00

ATOM 1016 N LEU A 224 -11.002 15.132 -0.526 1..00 0.00

ATOM 1017 CA LEU A 224 -11.573 13.891 -0.019 1..00 0.00

ATOM 1018 C LEU A 224 -12.158 14.056 365 1.00 0.00

ATOM 1019 O LEU A 224 -13.236 13.549 638 1.00 0.00

ATOM 1020 CB LEU A 224 -10.501 12.801 0.061 1.00 0.00

ATOM 1021 CG LEU A 224 -9.969 12.275 -1.274 1.00 0.00

ATOM 1022 CDl LEU A 224 -8.793 11.335 -1.051 1.00 0.00

ATOM 1023 CD2 LEU A 224 -11.052 11.512 -2.021 1.00 0.00

ATOM 1024 N LYS A 225 -11.452 14.778 2.226 1..00 0.00

ATOM 1025 CA LYS A 225 -11.915 15.052 3.584 1..00 0.00

ATOM 1026 C LYS A 225 -13.264 15.769 3.566 1.00 0.00

ATOM 1027 O LYS A 225 -14.162 15.474 4.353 1.00 0.00

ATOM 1028 CB LYS A -10.911 15.940 4.323 1.00 0.00

ATOM 1029 CG LYS A 225 -11.291 16.240 5.764 1.00 0.00

ATOM 1030 CD LYS A 225 -10.215 17.057 6.460 1.00 0.00

ATOM 1031 CE LYS A 225 -10.609 17.383 7.892 1.00 0.00

ATOM 1032 NZ LYS A 225 -9.570 18.197 8.582 00 0.00

ATOM 1033 N GLU A 226 -13.374 16.733 2.657 00 0.00

ATOM 1034 CA GLU A 226 -14.593 17.507 2.502 00 0.00

ATOM 1035 C GLU A 226 -15.735 16.586 2.054 00 0.00

ATOM 1036 O GLU A 226 -16.838 16.629 2.601 1.00 0.00 ATOM 1037 CB GLU A 226 14.401 18.605 1.453 1.00 0.00

ATOM 1038 CG GLU A 226 15.617 19.496 1.258 1.00 0.00

ATOM 1039 CD GLU A 226 15.379 20.591 0.237 1.00 0.00

ATOM 1040 OEl GLU A 226 14.257 20.660 -0.309 1.00 0.00

ATOM 1041 OE2 GLU A 226 16.313 21.380 -0.017 1.00 0.00

ATOM 1042 N GLU A 99 n 15.468 15.742 1.059 1.00 0.00

ATOM 1043 CA GLU A 227 16.490 14.815 0.577 1.00 0.00

ATOM 1044 C GLU A 227 16.938 13.902 1.693 1.00 0.00

ATOM 1045 O GLU A 227 18.122 13.625 1.854 1.00 0.00

ATOM 1046 CB GLU A 227 15.940 13.956 -0.562 1.00 0.00

ATOM 1047 CG GLU A 227 15.711 14.715 -1.859 1.00 0.00

ATOM 1048 CD GLU A 227 15.051 13.863 -2.926 1.00 0.00

ATOM 1049 OEl GLU A 227 14.706 12.700 -2.627 1.00 0.00

ATOM 1050 OE2 GLU A 227 14.880 14.357 -4.059 1.00 0.00

ATOM 1051 N LEU A 228 15.974 13.412 2.449 1.00 0.00

ATOM 1052 CA LEU A 228 16.280 12.530 3.547 1.00 0.00

ATOM 1053 C LEU A 228 17.211 13.224 4.544 1.00 0.00

ATOM 1054 O LEU A 228 18.195 12.649 4.998 1.00 0.00

ATOM 1055 CB LEU A 228 15.000 12.124 4.280 1.00 0.00

ATOM 1056 CG LEU A 228 15.174 11.196 5.485 1.00 0.00

ATOM 1057 CDl LEU A 228 15.789 9.872 5.059 1.00 0.00

ATOM 1058 CD2 LEU A 228 13.832 10.909 6.140 1.00 0.00

ATOM 1059 N LEU A 229 16.891 14.469 4.878 1.00 0.00

ATOM 1060 CA LEU A 229 17.712 15.260 5.795 1.00 0.00

ATOM 1061 C LEU A 229 19.133 15.412 5.251 1.00 0.00

ATOM 1062 O LEU A 229 20.125 15.227 5.963 1.00 0.00

ATOM 1063 CB LEU A 229 17.114 16.656 5.981 1.00 0.00

ATOM 1064 CG LEU A 229 17.882 17.604 6.905 1.00 0.00

ATOM 1065 CDl LEU A 229 17.945 17.043 8.318 1.00 0.00

ATOM 1066 CD2 LEU A 229 17.202 18.964 6.965 1.00 0.00

ATOM 1067 N CYS A 230 19.210 15.772 3.967 1.00 0.00

ATOM 1068 CA CYS A 230 20.481 15.968 3.273 1.00 0.00

ATOM 1069 C CYS A 230 21.334 14.712 3.349 1.00 0.00

ATOM 1070 O CYS A 230 22.539 14.796 3.570 1.00 0.00

ATOM 1071 CB CYS A 230 20.241 16.298 1.799 1.00 0.00

ATOM 1072 SG CYS A 230 19.499 17.921 1.508 1.00 0.00

ATOM 1073 N LEU A 231 20.713 13.549 3.164 1.00 0.00

ATOM 1074 CA LEU A 231 21.448 12.293 3.215 1.00 0.00

ATOM 1075 C LEU A 231 21.927 11.969 4.605 1.00 0.00

ATOM 1076 O LEU A 231 23.003 11.416 4.762 1.00 0.00

ATOM 1077 CB LEU A 231 20.561 11.135 2.752 1.00 0.00

ATOM 1078 CG LEU A 231 20.188 11.119 1.268 1.00 0.00

ATOM 1079 CDl LEU A 231 19.167 10.028 0.983 1.00 0.00

ATOM 1080 CD2 LEU A 231 21.414 10.858 0.408 1.00 0.00

ATOM 1081 N LYS A 232 21.135 12.283 5.624 1.00 0.00

ATOM 1082 CA LYS A 232 21.580 11.986 6.974 1.00 0.00

ATOM 1083 C LYS A 232 22.830 12.805 7.227 1.00 0.00

ATOM 1084 O LYS A 232 23.811 12.304 7.774 1.00 0.00

ATOM 1085 CB LYS A 232 20.495 12.354 7.988 1.00 0.00

ATOM 1086 CG LYS A 232 19.276 11.447 7.952 1.00 0.00

ATOM 1087 CD LYS A 232 18.243 11.868 8.984 1.00 0.00

ATOM 1088 CE LYS A 232 17.014 10.975 8.931 1.00 0.00

ATOM 1089 NZ LYS A 232 15.980 11.397 9.915 1.00 0.00

ATOM 1090 N LYS A 233 22.797 14.065 6.806 1.00 0.00

ATOM 1091 CA LYS A 233 23.941 14.942 6.996 1.00 0.00

ATOM 1092 C LYS A 233 25.158 14.403 6.242 1.00 0.00

ATOM 1093 O LYS A 233 26.232 14.227 6.830 1.00 0.00

ATOM 1094 CB LYS A 233 23.633 16.346 6.474 1.00 0.00

ATOM 1095 CG LYS A 233 24.763 17.343 6.670 1.00 0.00

ATOM 1096 CD LYS A 233 24.364 18.731 6.196 1.00 0.00

ATOM 1097 CE LYS A 233 25.511 19.717 6.346 1.00 0.00

ATOM 1098 NZ LYS A 233 25.141 21.076 5.862 1.00 0.00

ATOM 1099 N ASN A 234 24.997 14.108 4.956 1.00 0.00

ATOM 1100 CA ASN A 234 26.110 13.573 4.180 1.00 0.00

ATOM 1101 C ASN A 234 26.660 12.299 4.827 1.00 0.00

ATOM 1102 O ASN A 234 27.878 12.116 4.924 1.00 0.00

ATOM 1103 CB ASN A 234 25.659 13.233 2.758 1.00 0.00

ATOM 1104 CG ASN A 234 25.424 14.467 1.911 1.00 0.00 ATOM 1105 ODl ASN A 234 25.923 15.549 2.221 1.00 0.00

ATOM 1106 ND2 ASN A 234 24.660 14.309 0.836 1.00 0.00

ATOM 1107 N HIS A 235 25.755 11.438 5.291 1.00 0.00

ATOM 1108 CA HIS A 235 26.156 10.205 5.956 1.00 0.00

ATOM 1109 C HIS A 235 27.083 10.593 7.089 1.00 0.00

ATOM 1110 O HIS A 235 28.252 10.245 7.059 1.00 0.00

ATOM 1111 CB HIS A 235 24.931 9.470 6.504 1.00 0.00

ATOM 1112 CG HIS A 235 25.265 8.230 7.273 1.00 0.00

ATOM 1113 NDl HIS A 235 25.636 7.052 6.664 1.00 0.00

ATOM 1114 CD2 HIS A 235 25.318 7.865 8.683 1.00 0.00

ATOM 1115 CEl HIS A 235 25.872 6.124 7.608 1.00 0.00

ATOM 1116 NE2 HIS A 235 25.683 6.605 8.822 1.00 0.00

ATOM 1117 N GLU A 236 26.570 11.323 8.079 1.00 0.00

ATOM 1118 CA GLU A 236 27.394 11.760 9.211 1.00 0.00

ATOM 1119 C GLU A 236 28.771 12.190 8.736 1.00 0.00

ATOM 1120 O GLU A 236 29.798 11.667 9.183 1.00 0.00

ATOM 1121 CB GLU A 236 26.738 12.943 9.925 1.00 0.00

ATOM 1122 CG GLU A 236 27.460 13.384 11.188 1.00 0.00

ATOM 1123 CD GLU A 236 26.712 14.466 11.940 1.00 0.00

ATOM 1124 OEl GLU A 236 25.629 14.876 11.470 1.00 0.00

ATOM 1125 OE2 GLU A 236 27.206 14.904 13.000 1.00 0.00

ATOM 1126 N GLU A 237 28.784 13.164 7.837 1.00 0.00

ATOM 1127 CA GLU A 237 30.034 13.673 7.300 1.00 0.00

ATOM 1128 C GLU A 237 30.981 12.542 6.903 1.00 0.00

ATOM 1129 O GLU A 237 32.176 12.582 7.201 1.00 0.00

ATOM 1130 CB GLU A 237 29.776 14.524 6.055 1.00 0.00

ATOM 1131 CG GLU A 237 31.028 15.146 5.458 1.00 0.00

ATOM 1132 CD GLU A 237 30.725 16.033 4.266 1.00 0.00

ATOM 1133 OEl GLU A 237 29.534 16.178 3.920 1.00 0.00

ATOM 1134 OE2 GLU A 237 31.680 16.581 3.676 1.00 0.00

ATOM 1135 N GLU A 238 30.440 11.522 6.247 1.00 0.00

ATOM 1136 CA GLU A 238 31.249 10.395 5.793 1.00 0.00

ATOM 1137 C GLU A 238 31.703 9.468 6.905 1.00 0.00

ATOM 1138 O GLU A 238 32.845 9.016 6.913 1.00 0.00

ATOM 1139 CB GLU A 238 30.461 9.534 4.804 1.00 0.00

ATOM 1140 CG GLU A 238 30.226 10.195 3.456 1.00 0.00

ATOM 1141 CD GLU A 238 31.518 10.575 2.761 1.00 0.00

ATOM 1142 OEl GLU A 238 32.396 9.699 2.620 1.00 0.00

ATOM 1143 OE2 GLU A 238 31.652 11.749 2.356 1.00 0.00

ATOM 1144 N VAL A 239 30.805 9.164 7.830 1.00 0.00

ATOM 1145 CA VAL A 239 31.188 8.268 8.904 1.00 0.00

ATOM 1146 C VAL A 239 32.277 8.979 9.702 1.00 0.00

ATOM 1147 O VAL A 239 33.124 8.350 10.345 1.00 0.00

ATOM 1148 CB VAL A 239 29.995 7.942 9.820 1.00 0.00

ATOM 1149 CGl VAL A 239 30.458 7.166 11.043 1.00 0.00

ATOM 1150 CG2 VAL A 239 28.967 7.102 9.079 1.00 0.00

ATOM 1151 N ASN A 240 32.278 10.304 9.649 1.00 0.00

ATOM 1152 CA ASN A 240 33.303 11.000 10.395 1.00 0.00

ATOM 1153 C ASN A 240 34.610 11.101 9.652 1.00 0.00

ATOM 1154 O ASN A 240 35.664 10.923 10.250 1.00 0.00

ATOM 1155 CB ASN A 240 32.856 12.429 10.714 1.00 0.00

ATOM 1156 CG ASN A 240 31.746 12.476 11.744 1.00 0.00

ATOM 1157 ODl ASN A 240 31.559 11.533 12.514 1.00 0.00

ATOM 1158 ND2 ASN A 240 31.004 13.576 11.761 1.00 0.00

ATOM 1159 N SER A 241 34.567 11.423 8.366 1.00 0.00

ATOM 1160 CA SER A 241 35.816 11.506 7.633 1.00 0.00

ATOM 1161 C SER A 241 36.517 10.166 7.821 1.00 0.00

ATOM 1162 O SER A 241 37.737 10.115 7.933 1.00 0.00

ATOM 1163 CB SER A 241 35.550 11.767 6.149 1.00 0.00

ATOM 1164 OG SER A 241 34.883 10.670 5.549 1.00 0.00

ATOM 1165 N LEU A 242 35.726 9.097 7.892 1.00 0.00

ATOM 1166 CA LEU A 242 36.231 7.738 8.122 1.00 0.00

ATOM 1167 C LEU A 242 36.864 7.658 9.524 1.00 0.00

ATOM 1168 O LEU A 242 38.022 7.263 9.703 1.00 0.00

ATOM 1169 CB LEU A 242 35.092 6.721 8.031 1.00 0.00

ATOM 1170 CG LEU A 242 35.463 5.262 8.305 1.00 0.00

ATOM 1171 CDl LEU A 242 36.459 4.758 7.272 1.00 0.00

ATOM 1172 CD2 LEU A 242 34.229 4.374 8.248 1.00 0.00 ATOM 1173 N ARG A 243 36.177 7.860 10.491 1.00 0.00

ATOM 1174 CA ARG A 243 36.897 7.856 11.769 1.00 0.00

ATOM 1175 C ARG A 243 38.259 8.511 11.617 1.00 0.00

ATOM 1176 O ARG A 243 39.299 7.908 11.908 1.00 0.00

ATOM 1177 CB ARG A 243 36.108 8.625 12.831 1.00 0.00

ATOM 1178 CG ARG A 243 36.618 8.424 14.249 1.00 0.00

ATOM 1179 CD ARG A 243 35.707 9.096 15.264 1.00 0.00

ATOM 1180 NE ARG A 243 34.469 8.347 15.468 1.00 0.00

ATOM 1181 CZ ARG A 243 33.474 8.748 16.253 1.00 0.00

ATOM 1182 NHl ARG A 243 32.387 8.001 16.378 1.00 0.00

ATOM 1183 NH2 ARG A 243 33.570 9.896 16.910 1.00 0.00

ATOM 1184 N CYS A 244 38.245 9.759 11.173 1.00 0.00

ATOM 1185 CA CYS A 244 39.479 10.503 10.983 1.00 0.00

ATOM 1186 C CYS A 244 40.534 9.671 10.258 1.00 0.00

ATOM 1187 O CYS A 244 41.703 9.652 10.646 1.00 0.00

ATOM 1188 CB CYS A 244 39.223 11.761 10.152 1.00 0.00

ATOM 1189 SG CYS A 244 38.137 12.973 10.943 1.00 0.00

TER 1190 CYS A 244

ATOM 1191 N ASP A 261 55.241 9.223 12.450 1.00 0.00

ATOM 1192 CA ASP A 261 56.540 9.711 12.038 1.00 0.00

ATOM 1193 C ASP A 261 57.515 8.559 11.747 1.00 0.00

ATOM 1194 O ASP A 261 58.556 8.455 12.386 1.00 0.00

ATOM 1195 CB ASP A 261 56.418 10.551 10.765 1.00 0.00

ATOM 1196 CG ASP A 261 55.770 11.899 11.016 1.00 0.00

ATOM 1197 ODl ASP A 261 55.598 12.264 12.199 1.00 0.00

ATOM 1198 OD2 ASP A 261 55.435 12.590 10.032 1.00 0.00

ATOM 1199 N LEU A 262 57.176 7.695 10.793 1.00 0.00

ATOM 1200 CA LEU A 262 58.028 6.552 10.471 1.00 0.00

ATOM 1201 C LEU A 262 58.407 5.718 11.677 1.00 0.00

ATOM 1202 O LEU A 262 59.518 5.221 11.751 1.00 0.00

ATOM 1203 CB LEU A 262 57.319 5.615 9.491 1.00 0.00

ATOM 1204 CG LEU A 262 57.135 6.139 8.065 1.00 0.00

ATOM 1205 CDl LEU A 262 56.276 5.185 7.249 1.00 0.00

ATOM 1206 CD2 LEU A 262 58.479 6.283 7.368 1.00 0.00

ATOM 1207 N ASN A 263 57.468 5.541 12.601 1.00 0.00

ATOM 1208 CA ASN A 263 57.713 4.767 13.822 1.00 0.00

ATOM 1209 C ASN A 263 58.774 5.411 14.688 1.00 0.00

ATOM 1210 O ASN A 263 59.647 4.753 15.249 1.00 0.00

ATOM 1211 CB ASN A 263 56.433 4.658 14.653 1.00 0.00

ATOM 1212 CG ASN A 263 56.609 3.789 15.883 1.00 0.00

ATOM 1213 ODl ASN A 263 56.871 2.591 15.776 1.00 0.00

ATOM 1214 ND2 ASN A 263 56.465 4.391 17.057 1.00 0.00

ATOM 1215 N ARG A 264 58.632 6.713 14.854 1.00 0.00

ATOM 1216 CA ARG A 264 59.543 7.497 15.662 1.00 0.00

ATOM 1217 C ARG A 264 60.936 7.408 15.032 1.00 0.00

ATOM 1218 O ARG A 264 61.920 7.078 15.705 1.00 0.00

ATOM 1219 CB ARG A 264 59.093 8.959 15.713 1.00 0.00

ATOM 1220 CG ARG A 264 57.831 9.192 16.525 1.00 0.00

ATOM 1221 CD ARG A 264 57.417 10.655 16.493 1.00 0.00

ATOM 1222 NE ARG A 264 56.176 10.888 17.230 1.00 0.00

ATOM 1223 CZ ARG A 264 55.567 12.066 17.312 1.00 0.00

ATOM 1224 NHl ARG A 264 54.443 12.184 18.005 1.00 0.00

ATOM 1225 NH2 ARG A 264 56.084 13.124 16.701 1.00 0.00

ATOM 1226 N VAL A 265 60.998 7.681 13.727 1.00 0.00

ATOM 1227 CA VAL A 265 62.234 7.624 12.936 1.00 0.00

ATOM 1228 C VAL A 265 62.898 6.281 13.129 1.00 0.00

ATOM 1229 O VAL A 265 64.096 6.209 13.363 1.00 0.00

ATOM 1230 CB VAL A 265 61.952 7.815 11.433 1.00 0.00

ATOM 1231 CGl VAL A 265 63.207 7.542 10.618 1.00 0.00

ATOM 1232 CG2 VAL A 265 61.497 9.239 11.154 1.00 0.00

ATOM 1233 N LEU A 266 62.109 5.224 12.976 1.00 0.00

ATOM 1234 CA LEU A 266 62.644 3.882 13.132 1.00 0.00

ATOM 1235 C LEU A 266 63.163 3.606 14.529 1.00 0.00

ATOM 1236 O LEU A 266 64.147 2.889 14.687 1.00 0.00

ATOM 1237 CB LEU A 266 61.564 2.838 12.840 1.00 0.00

ATOM 1238 CG LEU A 266 61.991 1.373 12.950 1.00 0.00

ATOM 1239 CDl LEU A 266 63.095 1.059 11.951 1.00 0.00

ATOM 1240 CD2 LEU A 266 60.817 0.449 12.666 1.00 0.00 ATOM 1241 N GLU A 267 62.510 4.158 15.548 1.00 0.00

ATOM 1242 CA GLU A 267 62.961 3.946 16.919 1.00 0.00

ATOM 1243 C GLU A 267 64.348 4.553 17.033 1.00 0.00

ATOM 1244 O GLU A 267 65.289 3.914 17.505 1.00 0.00

ATOM 1245 CB GLU A 267 62.008 4.621 17.907 1.00 0.00

ATOM 1246 CG GLU A 267 62.377 4.413 19.367 1.00 0.00

ATOM 1247 CD GLU A 267 61.392 5.067 20.315 1.00 0.00

ATOM 1248 OEl GLU A 267 60.413 5.673 19.831 1.00 0.00

ATOM 1249 OE2 GLU A 267 61.600 4.974 21.545 1.00 0.00

ATOM 1250 N GLU A 268 64.473 5.793 16.579 1.00 0.00

ATOM 1251 CA GLU A 268 65.760 6.442 16.633 1.00 0.00

ATOM 1252 C GLU A 268 66.813 5.646 15.874 1.00 0.00

ATOM 1253 O GLU A 268 67.872 5.349 16.430 1.00 0.00

ATOM 1254 CB GLU A 268 65.683 7.838 16.012 1.00 0.00

ATOM 1255 CG GLU A 268 66.989 8.614 16.067 1.00 0.00

ATOM 1256 CD GLU A 268 66.865 10.004 15.473 1.00 0.00

ATOM 1257 OEl GLU A 268 65.755 10.364 15.031 1.00 0.00

ATOM 1258 OE2 GLU A 268 67.880 10.733 15.451 1.00 0.00

ATOM 1259 N MET A 269 66.530 5.233 14.639 1.00 0.00

ATOM 1260 CA MET A 269 67.551 4.492 13.912 1.00 0.00

ATOM 1261 C MET A 269 67.919 3.153 14.500 1.00 0.00

ATOM 1262 O MET A 269 69.076 2.778 14.429 1.00 0.00

ATOM 1263 CB MET A 269 67.090 4.208 12.481 1.00 0.00

ATOM 1264 CG MET A 269 67.014 5.442 11.597 1.00 0.00

ATOM 1265 SD MET A 269 68.611 6.254 11.397 1.00 0.00

ATOM 1266 CE MET A 269 69.486 5.041 10.413 1.00 0.00

ATOM 1267 N ARG A 270 66.969 2.416 15.076 1.00 0.00

ATOM 1268 CA ARG A 270 67.342 1.127 15.635 1.00 0.00

ATOM 1269 C ARG A 270 68.221 1.328 16.841 1.00 0.00

ATOM 1270 O ARG A 270 69.090 0.508 17.123 1.00 0.00

ATOM 1271 CB ARG A 270 66.097 0.345 16.059 1.00 0.00

ATOM 1272 CG ARG A 270 65.258 -0.161 14.898 1.00 0.00

ATOM 1273 CD ARG A 270 63.996 -0.855 15.388 1.00 0.00

ATOM 1274 NE ARG A 270 63.173 -1.340 14.283 1.00 0.00

ATOM 1275 CZ ARG A 270 61.961 -1.865 14.429 1.00 0.00

ATOM 1276 NHl ARG A 270 61.287 -2.280 13.367 1.00 0.00

ATOM 1277 NH2 ARG A 270 61.426 -1.972 15.638 1.00 0.00

ATOM 1278 N CYS A 271 68.005 2.422 17.557 1.00 0.00

ATOM 1279 CA CYS A 271 68.826 2.692 18.724 1.00 0.00

ATOM 1280 C CYS A 271 70.236 2.992 18.230 1.00 0.00

ATOM 1281 O CYS A 271 71.221 2.441 18.720 1.00 0.00

ATOM 1282 CB CYS A 271 68.276 3.890 19.500 1.00 0.00

ATOM 1283 SG CYS A 271 66.711 3.577 20.349 1.00 0.00

ATOM 1284 N GLN A 272 70.299 3.863 17.234 1.00 0.00

ATOM 1285 CA GLN A 272 71.543 4.260 16.606 1.00 0.00

ATOM 1286 C GLN A 272 72.308 3.049 16.040 1.00 0.00

ATOM 1287 O GLN A 272 73.534 2.972 16.145 1.00 0.00

ATOM 1288 CB GLN A 272 71.276 5.226 15.450 1.00 0.00

ATOM 1289 CG GLN A 272 70.806 6.603 15.890 1.00 0.00

ATOM 1290 CD GLN A 272 70.443 7.495 14.719 1.00 0.00

ATOM 1291 OEl GLN A 272 70.455 7.060 13.567 1.00 0.00

ATOM 1292 NE2 GLN A 70.118 8.749 15.011 1.00 0.00

ATOM 1293 N TYR A 273 71.569 2.123 15.435 1.00 0.00

ATOM 1294 CA TYR A 273 72.156 0.911 14.856 1.00 0.00

ATOM 1295 C TYR A 273 72.725 0.081 15.983 1.00 0.00

ATOM 1296 O TYR A 273 73.868 -0.349 15.921 1.00 0.00

ATOM 1297 CB TYR A 273 71.092 0.105 14.109 1.00 0.00

ATOM 1298 CG TYR A 273 71.611 -1.178 13.500 1.00 0.00

ATOM 1299 CDl TYR A 273 72.330 -1.160 12.312 1.00 0.00

ATOM 1300 CD2 TYR A 273 71.380 -2.401 14.114 1.00 0.00

ATOM 1301 CEl TYR A 273 72.809 -2.327 11.747 1.00 0.00

ATOM 1302 CE2 TYR A 273 71.851 -3.579 13.565 1.00 0.00

ATOM 1303 CZ TYR A 273 72.570 -3.533 12.371 1.00 0.00

ATOM 1304 OH TYR A 273 73.045 -4.696 11.811 1.00 0.00

ATOM 1305 N GLU A 274 71.927 -0.168 17.012 1.00 0.00

ATOM 1306 CA GLU A 274 72.428 -0.939 18.139 1.00 0.00

ATOM 1307 C GLU A 274 73.752 -0.358 18.659 1.00 0.00

ATOM 1308 O GLU A 274 74.705 -1.093 18.919 1.00 0.00 ATOM 1309 CB GLU A 274 -71.419 -0.926 19.288 1.00 0.00

ATOM 1310 CG GLU A 274 -71.836 -1.757 20.490 1.00 0.00

ATOM 1311 CD GLU A 274 -70.784 -1.772 21.583 1.00 0.00

ATOM 1312 OEl GLU A 274 -69.718 -1.151 21.388 1.00 0.00

ATOM 1313 OE2 GLU A 274 -71.026 -2.406 22.631 1.00 0.00

ATOM 1314 N THR A 275 -73.821 0.963 18.784 1.00 0.00

ATOM 1315 CA THR A 275 -75.046 1.612 19.249 1.00 0.00

ATOM 1316 C THR A 275 -76.209 1.353 18.302 1.00 0.00

ATOM 1317 O THR A 275 -77.295 0.984 18.736 1.00 0.00

ATOM 1318 CB THR A 275 -74.871 3.139 19.355 1.00 0.00

ATOM 1319 OGl THR A 275 -73.847 3.441 20.311 1.00 0.00

ATOM 1320 CG2 THR A 275 -76.169 3.794 19.798 1.00 0.00

ATOM 1321 N LEU A 276 -75.981 1.548 17.012 1.00 0.00

ATOM 1322 CA LEU A 276 -77.020 1.297 16.024 1.00 0.00

ATOM 1323 C LEU A 276 -77.563 -0.109 16.130 1.00 0.00

ATOM 1324 O LEU A 276 -78.768 -0.315 16.042 1.00 0.00

ATOM 1325 CB LEU A 276 -76.469 1.481 14.608 1.00 0.00

ATOM 1326 CG LEU A 276 -76.123 2.913 14.196 1.00 0.00

ATOM 1327 CDl LEU A 276 -75.423 2.931 12.846 1.00 0.00

ATOM 1328 CD2 LEU A 276 -77.381 3.761 14.090 1.00 0.00

ATOM 1329 N VAL A 277 -76.664 -1.075 16.287 1.00 0.00

ATOM 1330 CA VAL A 277 -77.045 -2.474 16.407 1.00 0.00

ATOM 1331 C VAL A 277 -77.958 -2.668 17.606 1.00 0.00

ATOM 1332 O VAL A 277 -79.042 -3.245 17.495 1.00 0.00

ATOM 1333 CB VAL A 277 -75.813 -3.380 16.592 1.00 0.00

ATOM 1334 CGl VAL A 277 -76.244 -4.804 16.913 1.00 0.00

ATOM 1335 CG2 VAL A 277 -74.975 -3.406 15.324 1.00 0.00

ATOM 1336 N GLU A 278 -77.533 -2.191 18.764 1.00 0.00

ATOM 1337 CA GLU A 278 -78.383 -2.329 19.930 1.00 0.00

ATOM 1338 C GLU A 278 -79.759 -1.737 19.602 1.00 0.00

ATOM 1339 O GLU A 278 -80.776 -2.411 19.756 1.00 0.00

ATOM 1340 CB GLU A 278 -77.780 -1.585 21.123 1.00 0.00

ATOM 1341 CG GLU A 278 -78.594 -1.698 22.402 1.00 0.00

ATOM 1342 CD GLU A 278 -77.945 -0.984 23.571 1.00 0.00

ATOM 1343 OEl GLU A 278 -76.841 -0.429 23.390 1.00 0.00

ATOM 1344 OE2 GLU A 278 -78.542 -0.979 24.668 1.00 0.00

ATOM 1345 N ASN A 279 -79.804 -0.494 19.128 1.00 0.00

ATOM 1346 CA ASN A 279 -81.091 0.137 18.807 1.00 0.00

ATOM 1347 C ASN A 279 -81.960 -0.687 17.863 1.00 0.00

ATOM 1348 O ASN A 279 -83.168 -0.791 18.059 1.00 0.00

ATOM 1349 CB ASN A 279 -80.870 1.492 18.132 1.00 0.00

ATOM 1350 CG ASN A 279 -82.148 2.299 18.014 1.00 0.00

ATOM 1351 ODl ASN A 279 -83.090 2.105 18.782 1.00 0.00

ATOM 1352 ND2 ASN A 279 -82.183 3.211 17.048 1.00 0.00

TER 1353 ASN A 279

ATOM 1354 N LEU A 288 -93.071 -0.196 18.145 1.00 0.00

ATOM 1355 CA LEU A 288 -94.235 -0.504 17.338 1.00 0.00

ATOM 1356 C LEU A 288 -94.678 -1.919 17.599 1.00 0.00

ATOM 1357 O LEU A 288 -95.847 -2 224 17.434 1.00 0.00

ATOM 1358 CB LEU A 288 -93.909 -0.357 15.850 1.00 0.00

ATOM 1359 CG LEU A 288 -93.647 1.065 15.351 1.00 0.00

ATOM 1360 CDl LEU A 288 -93.176 1.049 13.905 1.00 0.00

ATOM 1361 CD2 LEU A 288 -94.915 1.903 15.427 1.00 0.00

ATOM 1362 N ASP A 289 -93.758 -2.800 18.043 1.00 0.00

ATOM 1363 CA ASP A 289 -94.191 -4.129 18.448 1.00 0.00

ATOM 1364 C ASP A 289 -95.153 -4.018 19.599 1.00 0.00

ATOM 1365 O ASP A 289 -96.176 -4.686 19.601 1.00 0.00

ATOM 1366 CB ASP A 289 -92.992 -4.973 18.886 1.00 0.00

ATOM 1367 CG ASP A 289 -93.372 -6.407 19.200 1.00 0.00

ATOM 1368 ODl ASP A 289 -93.849 -7.110 18.284 1.00 0.00

ATOM 1369 OD2 ASP A 289 -93.193 -6.828 20.362 1.00 0.00

ATOM 1370 N THR A 290 -94.816 -3.145 20.573 1.00 0.00

ATOM 1371 CA THR A 290 -95.708 -2.932 21.702 1.00 0.00

ATOM 1372 C THR A 290 -97.044 -2.444 21.220 1.00 0.00

ATOM 1373 O THR A 290 -98.058 -2.965 21.655 1.00 0.00

ATOM 1374 CB THR A 290 -95.142 -1.885 22.679 1.00 0.00

ATOM 1375 OGl THR A 290 -93.896 -2.350 23.212 1.00 0.00

ATOM 1376 CG2 THR A 290 -96.111 -1.649 23.827 1.00 0.00 ATOM 1377 N GLN A 291 -97.032 -1.447 20.314 1.00 0.00

ATOM 1378 CA GLN A 291 -98.287 -0.927 19.794 1.00 0.00

ATOM 1379 C GLN A 291 -99.076 -2.015 19.121 1.00 0.00

ATOM 1380 O GLN A 291 -100.277 -2.103 19.324 1.00 0.00

ATOM 1381 CB GLN A 291 -98.025 0.179 18.771 1.00 0.00

ATOM 1382 CG GLN A 291 -97.491 1.468 19.374 1.00 0.00

ATOM 1383 CD GLN A 291 -97.137 2.501 18.322 1.00 0.00

ATOM 1384 OEl GLN A 291 -97.205 2.229 17.123 1.00 0.00

ATOM 1385 NE2 GLN A 291 -96.756 3.692 18.768 1.00 0.00

ATOM 1386 N SER A 292 -98.381 -2.856 18.332 1.00 0.00

ATOM 1387 CA SER A 292 -99.065 -3.946 17.656 1.00 0.00

ATOM 1388 C SER A 292 -99.697 -4.874 18.655 1.00 0.00

ATOM 1389 O SER A 292 -100.839 -5.259 18.461 1.00 0.00

ATOM 1390 CB SER A 292 -98.080 -4.751 16.805 1.00 0.00

ATOM 1391 OG SER A 292 -97.572 -3.972 15.737 1.00 0.00

ATOM 1392 N GLU A 293 -98.953 -5.221 19.725 1.00 0.00

ATOM 1393 CA GLU A 293 -99.503 -6.118 20.729 1.00 0.00

ATOM 1394 C GLU A 293 -100.807 -5.588 21.252 1.00 0.00

ATOM 1395 O GLU A 293 -101.773 -6.331 21.324 1.00 0.00

ATOM 1396 CB GLU A 293 -98.536 -6.265 21.905 1.00 0.00

ATOM 1397 CG GLU A 293 -99.021 -7.208 22.993 1.00 0.00

ATOM 1398 CD GLU A 293 -98.020 -7.360 24.121 1.00 0.00

ATOM 1399 OEl GLU A 293 -96.931 -6.754 24.035 1.00 0.00

ATOM 1400 OE2 GLU A 293 -98.323 -8.086 25.091 1.00 0.00

ATOM 1401 N GLU A 294 -100.823 -4.287 21.604 1.00 0.00

ATOM 1402 CA GLU A 294 -102.052 -3.691 22.098 1.00 0.00

ATOM 1403 C GLU A 294 -103.146 -3.820 21.076 1.00 0.00

ATOM 1404 O GLU A 294 -104.253 -4.191 21.427 1.00 0.00

ATOM 1405 CB GLU A 294 -101.844 -2.206 22.400 1.00 0.00

ATOM 1406 CG GLU A 294 -103.071 -1.509 22.966 1.00 0.00

ATOM 1407 CD GLU A 294 -102.817 -0.049 23.284 1.00 0.00

ATOM 1408 OEl GLU A 294 -101.677 0.416 23.074 1.00 0.00

ATOM 1409 OE2 GLU A 294 -103.759 0.631 23.744 1.00 0.00

ATOM 1410 N LEU A 295 -102.818 -3.520 19.802 1.00 0.00

ATOM 1411 CA LEU A 295 -103.822 -3.608 18.757 1.00 0.00

ATOM 1412 C LEU A 295 -104.392 -4.996 18.663 1.00 0.00

ATOM 1413 O LEU A 295 -105.602 -5.142 18.610 1.00 0.00

ATOM 1414 CB LEU A 295 -103.213 -3.253 17.399 1.00 0.00

ATOM 1415 CG LEU A 295 -102.834 -1.785 17.188 1.00 0.00

ATOM 1416 CDl LEU A 295 -102.072 -1.609 15.885 1.00 0.00

ATOM 1417 CD2 LEU A 295 -104.078 -0.910 17.135 1.00 0.00

ATOM 1418 N ASN A 296 -103.508 -6.013 18.648 1.00 0.00

ATOM 1419 CA ASN A 296 -103.982 -7.382 18.533 1.00 0.00

ATOM 1420 C ASN A 296 -104.932 -7.717 19.649 1.00 0.00

ATOM 1421 O ASN A 296 -105.984 -8.278 19.390 1.00 0.00

ATOM 1422 CB ASN A 296 -102.809 -8.362 18.592 1.00 0.00

ATOM 1423 CG ASN A 296 -101.975 -8.350 17.327 1.00 0.00

ATOM 1424 ODl ASN A 296 -102.431 -7.900 16.276 1.00 0.00

ATOM 1425 ND2 ASN A 296 -100.746 -8.845 17.426 1.00 0.00

ATOM 1426 N GLN A 297 -104.557 -7.354 20.892 1.00 0.00

ATOM 1427 CA GLN A 297 -105.437 -7.636 22.014 1.00 0.00

ATOM 1428 C GLN A 297 -106.751 -6.925 21.845 1.00 0.00

ATOM 1429 O GLN A 297 -107.786 -7.519 22.099 1.00 0.00

ATOM 1430 CB GLN A 297 -104.799 -7.169 23.325 1.00 0.00

ATOM 1431 CG GLN A 297 -103.609 -8.004 23.768 1.00 0.00

ATOM 1432 CD GLN A 297 -102.935 -7.445 25.005 1.00 0.00

ATOM 1433 OEl GLN A 297 -103.299 -6.376 25.493 1.00 0.00

ATOM 1434 NE2 GLN A 297 -101.948 -8.170 25.518 1.00 0.00

ATOM 1435 N GLN A 298 -106.701 -5.651 21.406 1.00 0.00

ATOM 1436 CA GLN A 298 -107.937 -4.910 21.207 1.00 0.00

ATOM 1437 C GLN A 298 -108.825 -5.621 20.225 1.00 0.00

ATOM 1438 O GLN A 298 -110.014 -5.735 20.474 1.00 0.00

ATOM 1439 CB GLN A 298 -107.641 -3.510 20.667 1.00 0.00

ATOM 1440 CG GLN A 298 -106.989 -2.579 21.676 1.00 0.00

ATOM 1441 CD GLN A 298 -106.607 -1.241 21.074 1.00 0.00

ATOM 1442 OEl GLN A 298 -106.745 -1.029 19.870 1.00 0.00

ATOM 1443 NE2 GLN A 298 -106.124 -0.332 21.914 1.00 0.00

ATOM 1444 N VAL A 299 -108.228 -6.109 19.118 1.00 0.00 ATOM 1445 CA VAL A 299 -109.004 -6.861 18.145 1.00 0.00

ATOM 1446 C VAL A 299 -109.720 -7.988 18.840 1.00 0.00

ATOM 1447 O VAL A 299 -110.897 -8.200 18.598 1.00 0.00

ATOM 1448 CB VAL A 299 -108.106 -7.458 17.045 1.00 0.00

ATOM 1449 CGl VAL A 299 -108.901 -8.408 16.164 1.00 0.00

ATOM 1450 CG2 VAL A 299 -107.534 -6.354 16.169 1.00 0.00

ATOM 1451 N VAL A 300 -108.985 -8.689 19.725 1.00 0.00

ATOM 1452 CA VAL A 300 -109.591 -9.779 20.469 1.00 0.00

ATOM 1453 C VAL A 300 -110.752 -9.282 21.288 1.00 0.00

ATOM 1454 O VAL A 300 -111.817 -9.873 21.232 1.00 0.00

ATOM 1455 CB VAL A 300 -108.583 -10.435 21.431 1.00 0.00

ATOM 1456 CGl VAL A 300 -109.284 -11.434 22.338 1.00 0.00

ATOM 1457 CG2 VAL A 300 -107.503 -11.168 20.650 1.00 0.00

ATOM 1458 N SER A 301 -110.536 -8.187 22.044 1.00 0.00

ATOM 1459 CA SER A 301 -111.599 -7.680 22.896 1.00 0.00

ATOM 1460 C SER A 301 -112.802 -7.278 22.091 1.00 0.00

ATOM 1461 O SER A 301 -113.914 -7.567 22.502 1.00 0.00

ATOM 1462 CB SER A 301 -111.121 -6.453 23.675 1.00 0.00

ATOM 1463 OG SER A 301 -110.100 -6.799 24.595 1.00 0.00

ATOM 1464 N SER A 302 -112.575 -6.618 20.938 1.00 0.00

ATOM 1465 CA SER A 302 -113.697 -6.210 20.111 1.00 0.00

ATOM 1466 C SER A 302 -114.503 -7.409 19.703 1.00 0.00

ATOM 1467 O SER A 302 -115.716 -7.392 19.839 1.00 0.00

ATOM 1468 CB SER A 302 -113.203 -5.502 18.848 1.00 0.00

ATOM 1469 OG SER A 302 -112.581 -4.268 19.165 1.00 0.00

ATOM 1470 N SER A 303 -113.810 -8.458 19.216 1.00 0.00

ATOM 1471 CA SER A 303 -114.513 -9.671 18.835 1.00 0.00

ATOM 1472 C SER A 303 -115.265 -10.228 20.011 1.00 0.00

ATOM 1473 O SER A 303 -116.394 -10.662 19.852 1.00 0.00

ATOM 1474 CB SER A 303 -113.525 -10.731 18.343 1.00 0.00

ATOM 1475 OG SER A 303 -112.899 -10.324 17.139 1.00 0.00

ATOM 1476 N GLU A 304 -114.627 -10.195 21.199 1.00 0.00

ATOM 1477 CA GLU A 304 -115.294 -10.686 22.391 1.00 0.00

ATOM 1478 C GLU A 304 -116.566 -9.924 22.637 1.00 0.00

ATOM 1479 O GLU A 304 -117.591 -10.531 22.901 1.00 0.00

ATOM 1480 CB GLU A 304 -114.391 -10.525 23.616 1.00 0.00

ATOM 1481 CG GLU A 304 -114.993 -11.058 24.905 1.00 0.00

ATOM 1482 CD GLU A 304 -114.058 -10.911 26.090 1.00 0.00

ATOM 1483 OEl GLU A 304 -112.932 -10.406 25.898 1.00 0.00

ATOM 1484 OE2 GLU A 304 -114.450 -11.303 27.209 1.00 0.00

ATOM 1485 N GLN A 305 -116.489 -8.583 22.531 1.00 0.00

ATOM 1486 CA GLN A 305 -117.677 -7.774 22.746 1.00 0.00

ATOM 1487 C GLN A 305 -118.736 -8.109 21.736 1.00 0.00

ATOM 1488 O GLN A 305 -119.904 -8.163 22.086 1.00 0.00

ATOM 1489 CB GLN A 305 -117.342 -6.287 22.616 1.00 0.00

ATOM 1490 CG GLN A 305 -116.498 -5.739 23.756 1.00 0.00

ATOM 1491 CD GLN A 305 -116.091 -4.295 23.538 1.00 0.00

ATOM 1492 OEl GLN A 305 -116.363 -3.715 22.487 1.00 0.00

ATOM 1493 NE2 GLN A 305 -115.436 -3.709 24.534 1.00 0.00

ATOM 1494 N LEU A 306 -118.313 -8.348 20.479 1.00 0.00

ATOM 1495 CA LEU A 306 -119.279 -8.687 19.448 1.00 0.00

ATOM 1496 C LEU A 306 -119.995 -9.966 19.792 1.00 0.00

ATOM 1497 O LEU A 306 -121.209 -10.015 19.672 1.00 0.00

ATOM 1498 CB LEU A 306 -118.580 -8.874 18.099 1.00 0.00

ATOM 1499 CG LEU A 306 -119.476 -9.253 16.918 1.00 0.00

ATOM 1500 CDl LEU A 306 -120.502 -8.163 16.651 1.00 0.00

ATOM 1501 CD2 LEU A 306 -118.648 -9.447 15.657 1.00 0.00

ATOM 1502 N GLN A 307 -119.241 -10.996 20.225 1.00 0.00

ATOM 1503 CA GLN A 307 -119.881 -12.260 20.550 1.00 0.00

ATOM 1504 C GLN A 307 -120.843 -12.113 21.696 1.00 0.00

ATOM 1505 O GLN A 307 -121.884 -12.750 21.689 1.00 0.00

ATOM 1506 CB GLN A 307 -118.834 -13.303 20.947 1.00 0.00

ATOM 1507 CG GLN A 307 -117.972 -13.787 19.793 1.00 0.00

ATOM 1508 CD GLN A 307 -116.875 -14.733 20.241 1.00 0.00

ATOM 1509 OEl GLN A 307 -116.694 -14.965 21.436 1.00 0.00

ATOM 1510 NE2 GLN A 307 -116.139 -15.282 19.281 1.00 0.00

ATOM 1511 N SER A 308 -120.489 -11.262 22.679 1.00 0.00

ATOM 1512 CA SER A 308 -121.388 -11.057 23.803 1.00 0.00 ATOM 1513 C SER A 308 -122.663 -10.421 23.325 1.00 0.00

ATOM 1514 O SER A 308 -123.737 -10.836 23.734 1.00 0.00

ATOM 1515 CB SER A 308 -120.743 -10.142 24.845 1.00 0.00

ATOM 1516 OG SER A 308 -119.614 -10.761 25.439 1.00 0.00

ATOM 1517 N CYS A 309 _ -l 99 R 9 Q -9.415 22.436 1.00 0.00

ATOM 1518 CA CYS A 309 -123.713 -8.784 21.877 1.00 0.00

ATOM 1519 C CYS A 309 -124.524 -9.793 21.114 1.00 0.00

ATOM 1520 O CYS A 309 -125.743 -9.729 21.141 1.00 0.00

ATOM 1521 CB CYS A 309 -123.318 -7.653 20.924 1.00 0.00

ATOM 1522 SG CYS A 309 -122.581 -6.216 21.737 1.00 0.00

ATOM 1523 N GLN A 310 -123.829 -10.733 20.442 1.00 0.00

ATOM 1524 CA GLN A 310 -124.531 -11.749 19.677 1.00 0.00

ATOM 1525 C GLN A 310 -125.423 -12.571 20.563 1.00 0.00

ATOM 1526 O GLN A 310 -126.588 -12.744 20.242 1.00 0.00

ATOM 1527 CB GLN A 310 -123.536 -12.691 18.998 1.00 0.00

ATOM 1528 CG GLN A 310 -122.763 -12.058 17.853 1.00 0.00

ATOM 1529 CD GLN A 310 -121.696 -12.976 17.291 1.00 0.00

ATOM 1530 OEl GLN A 310 -121.471 -14.071 17.807 1.00 0.00

ATOM 1531 NE2 GLN A 310 -121.033 -12.531 16.229 1.00 0.00

ATOM 1532 N ALA A 311 -124.865 -13.072 21.685 1.00 0.00

ATOM 1533 CA ALA A 311 -125.664 -13.889 22.583 1.00 0.00

ATOM 1534 C ALA A 311 -126.886 -13.139 23.036 1.00 0.00

ATOM 1535 O ALA A 311 -127.969 -13.702 23.035 1.00 0.00

ATOM 1536 CB ALA A 311 -124.854 -14.273 23.812 1.00 0.00

ATOM 1537 N GLU A 312 -126.700 -11.856 23.406 1.00 0.00

ATOM 1538 CA GLU A 312 -127.836 -11.057 23.832 1.00 0.00

ATOM 1539 C GLU A 312 -128.867 -10.987 22.741 1.00 0.00

ATOM 1540 O GLU A 312 -130.038 -11.216 23.001 1.00 0.00

ATOM 1541 CB GLU A 312 -127.392 -9.632 24.171 1.00 0.00

ATOM 1542 CG GLU A 312 -126.568 -9.524 25.443 1.00 0.00

ATOM 1543 CD GLU A 312 -126.031 -8.125 25.674 1.00 0.00

ATOM 1544 OEl GLU A 312 -126.234 -7.260 24.796 1.00 0.00

ATOM 1545 OE2 GLU A 312 -125.407 -7.896 26.730 1.00 0.00

ATOM 1546 N ILE A 313 -128.408 -10.668 21.514 1.00 0.00

ATOM 1547 CA ILE A 313 -129.331 -10.534 20.400 1.00 0.00

ATOM 1548 C ILE A 313 -130.160 -11.773 20.215 1.00 0.00

ATOM 1549 O ILE A 313 -131.367 -11.665 20.076 1.00 0.00

ATOM 1550 CB ILE A 313 -128.585 -10.280 19.077 1.00 0.00

ATOM 1551 CGl ILE A 313 -127.914 -8.904 19.099 1.00 0.00

ATOM 1552 CG2 ILE A 313 -129.551 -10.326 17.903 1.00 0.00

ATOM 1553 CDl ILE A 313 -126.942 -8.681 17.961 1.00 0.00

ATOM 1554 N ILE A 314 -129.504 -12.950 20.221 1.00 0.00

ATOM 1555 CA ILE A 314 -130.245 -14.186 20.036 1.00 0.00

ATOM 1556 C ILE A 314 -131.268 -14.357 21.124 1.00 0.00

ATOM 1557 O ILE A 314 -132.390 -14.744 20.836 1.00 0.00

ATOM 1558 CB ILE A 314 -129.314 -15.413 20.066 1.00 0.00

ATOM 1559 CGl ILE A 314 -128.395 -15.414 18.843 1.00 0.00

ATOM 1560 CG2 ILE A 314 -130.126 -16.699 20.061 1.00 0.00

ATOM 1561 CDl ILE A 314 -127.274 -16.428 18.923 1.00 0.00

ATOM 1562 N GLU A 315 -130.871 -14.057 22.377 1.00 0.00

ATOM 1563 CA GLU A 315 -131.803 -14.202 23.482 1.00 0.00

ATOM 1564 C GLU A 315 -133.037 -13.375 23.260 1.00 0.00

ATOM 1565 O GLU A 315 -134.134 -13.899 23.365 1.00 0.00

ATOM 1566 CB GLU A 315 -131.155 -13.748 24.793 1.00 0.00

ATOM 1567 CG GLU A 315 -132.046 -13.908 26.013 1.00 0.00

ATOM 1568 CD GLU A 315 -131.359 -13.481 27.296 1.00 0.00

ATOM 1569 OEl GLU A 315 -130.181 -13.072 27.231 1.00 0.00

ATOM 1570 OE2 GLU A 315 -132.000 -13.555 28.366 1.00 0.00

ATOM 1571 N LEU A 316 -132.846 -12.077 22.947 1.00 0.00

ATOM 1572 CA LEU A 316 -133.994 -11.212 22.739 1.00 0.00

ATOM 1573 C LEU A 316 -134.837 -11.696 21.595 1.00 0.00

ATOM 1574 O LEU A 316 -136.052 -11.719 21.717 1.00 0.00

ATOM 1575 CB LEU A 316 -133.540 -9.785 22.425 1.00 0.00

ATOM 1576 CG LEU A 316 -132.893 -9.011 23.575 1.00 0.00

ATOM 1577 CDl LEU A 316 -132.329 -7.687 23.082 1.00 0.00

ATOM 1578 CD2 LEU A 316 -133.912 -8.717 24.666 1.00 0.00

ATOM 1579 N ARG A 317 -134.179 -12.092 20.487 1.00 0.00

ATOM 1580 CA ARG A 317 -134.925 -12.544 19.326 1.00 0.00 ATOM 1581 C ARG A 317 -135.813 -13.708 19.665 1.00 0.00

ATOM 1582 O ARG A 317 -136.983 -13.687 19.317 1.00 0.00

ATOM 1583 CB ARG A 317 -133.971 -12.987 18.215 1.00 0.00

ATOM 1584 CG ARG A 317 -133.217 -11.845 17.553 1.00 0.00

ATOM 1585 CD ARG A 317 -132.256 -12.358 16.494 1.00 0.00

ATOM 1586 NE ARG A 317 -131.487 -11.277 15.882 1.00 0.00

ATOM 1587 CZ ARG A 317 -130.539 -11.459 14.968 1.00 0.00

ATOM 1588 NHl ARG A 317 -129.893 -10.415 14.467 1.00 0.00

ATOM 1589 NH2 ARG A 317 -130.240 -12.683 14.557 1.00 0.00

ATOM 1590 N ARG A 318 -135.249 -14.718 20.356 1.00 0.00

ATOM 1591 CA ARG A 318 -136.053 -15.873 20.724 1.00 0.00

ATOM 1592 C ARG A 318 -137.232 -15.445 21.551 1.00 0.00

ATOM 1593 O ARG A 318 -138.337 -15.900 21.306 1.00 0.00

ATOM 1594 CB ARG A 318 -135.222 -16.866 21.540 1.00 0.00

ATOM 1595 CG ARG A 318 -134.163 -17.598 20.733 1.00 0.00

ATOM 1596 CD ARG A 318 -133.329 -18.511 21.617 1.00 0.00

ATOM 1597 NE ARG A 318 -132.287 -19.202 20.862 1.00 0.00

ATOM 1598 CZ ARG A 318 -131.374 -20.002 21.406 1.00 0.00

ATOM 1599 NHl ARG A 318 -130.465 -20.588 20.639 1.00 0.00

ATOM 1600 NH2 ARG A 318 -131.375 -20.213 22.715 1.00 0.00

ATOM 1601 N THR A 319 -136.980 -14.551 22.527 1.00 0.00

ATOM 1602 CA THR A 319 -138.065 -14.069 23.365 1.00 0.00

ATOM 1603 C THR A 319 -139.126 -13.408 22.528 1.00 0.00

ATOM 1604 O THR A 319 -140.301 -13.660 22.744 1.00 0.00

ATOM 1605 CB THR A 319 -137.568 -13.040 24.396 1.00 0.00

ATOM 1606 OGl THR A 319 -136.607 -13.654 25.263 1.00 0.00

ATOM 1607 CG2 THR A 319 -138.728 -12.522 25.234 1.00 0.00

ATOM 1608 N VAL A 320 -138.699 -12.569 21.563 1.00 0.00

ATOM 1609 CA VAL A 320 -139.664 -11.894 20.713 1.00 0.00

ATOM 1610 C VAL A 320 -140.522 -12.892 19.987 1.00 0.00

ATOM 1611 O VAL A 320 -141.727 -12.716 19.943 1.00 0.00

ATOM 1612 CB VAL A 320 -138.968 -11.015 19.657 1.00 0.00

ATOM 1613 CGl VAL A 320 -139.982 -10.478 18.658 1.00 0.00

ATOM 1614 CG2 VAL A 320 -138.275 -9.834 20.319 1.00 0.00

ATOM 1615 N ASN A 321 -139.888 -13.941 19.426 1.00 0.00

ATOM 1616 CA ASN A 321 -140.650 -14.943 18.699 1.00 0.00

ATOM 1617 C ASN A 321 -141.746 -15.504 19.560 1.00 0.00

ATOM 1618 O ASN A 321 -142.877 -15.599 19.110 1.00 0.00

ATOM 1619 CB ASN A 321 -139.742 -16.095 18.264 1.00 0.00

ATOM 1620 CG ASN A 321 -138.817 -15.710 17.126 1.00 0.00

ATOM 1621 ODl ASN A 321 -139.034 -14.705 16.450 1.00 0.00

ATOM 1622 ND2 ASN A 321 -137.780 -16.511 16.912 1.00 0.00

ATOM 1623 N ALA A 322 -141.397 -15.865 20.811 1.00 0.00

ATOM 1624 CA ALA A 322 -142.402 -16.404 21.709 1.00 0.00

ATOM 1625 C ALA A -143.500 -15.403 21.943 1.00 0.00

ATOM 1626 O ALA A -144.662 -15.777 21.922 1.00 0.00

ATOM 1627 CB ALA A 322 -141.780 -16.755 23.052 1.00 0.00

ATOM 1628 N LEU A 323 -143.120 -14.126 22.149 1.00 0.00

ATOM 1629 CA LEU A 323 -144.130 -13.101 22.359 1.00 0.00

ATOM 1630 C LEU A 323 -145.054 -13.015 21.179 1.00 0.00

ATOM 1631 O LEU A 323 -146.260 -12.983 21.362 1.00 0.00

ATOM 1632 CB LEU A 323 -143.473 -11.733 22.555 1.00 0.00

ATOM 1633 CG LEU A 323 -142.706 -11.531 23.864 1.00 0.00

ATOM 1634 CDl LEU A 323 -141.949 -10.211 23.845 1.00 0.00

ATOM 1635 CD2 LEU A 323 -143.661 -11.514 25.048 1.00 0.00

ATOM 1636 N GLU A 324 -144.471 -12.985 19.963 1.00 0.00

ATOM 1637 CA GLU A 324 -145.286 -12.862 18.767 1.00 0.00

ATOM 1638 C GLU A 324 -146.278 -13.985 18.664 1.00 0.00

ATOM 1639 O GLU A 324 -147.441 -13.732 18.389 1.00 0.00

ATOM 1640 CB GLU A 324 -144.408 -12.891 17.514 1.00 0.00

ATOM 1641 CG GLU A 324 -145.176 -12.722 16.214 1.00 0.00

ATOM 1642 CD GLU A 324 -144.271 -12.723 14.998 1.00 0.00

ATOM 1643 OEl GLU A 324 -143.040 -12.842 15.175 1.00 0.00

ATOM 1644 OE2 GLU A 324 -144.792 -12.604 13.869 1.00 0.00

ATOM 1645 N ILE A 325 -145.808 -15.226 18.895 1.00 0.00

ATOM 1646 CA ILE A 325 -146.712 -16.362 18.812 1.00 0.00

ATOM 1647 C ILE A 325 -147.832 -16.204 19.802 1.00 0.00

ATOM 1648 O ILE A 325 -148.981 -16.383 19.435 1.00 0.00 ATOM 1649 CB ILE A 325 -145.985 -17.685 19.118 1.00 0.00

ATOM 1650 CGl ILE A 325 -144.974 -18.005 18.015 1.00 0.00

ATOM 1651 CG2 ILE A 325 -146.981 -18.831 19.207 1.00 0.00

ATOM 1652 CDl ILE A 325 -144.029 -19.135 18.363 1.00 0.00

ATOM 1653 N GLU A 326 -147.482 -15.848 21.054 1.00 0.00

ATOM 1654 CA GLU A 326 -148.512 -15.638 22.058 1.00 0.00

ATOM 1655 C GLU A 326 -149.497 -14.606 21.590 1.00 0.00

ATOM 1656 O GLU A 326 -150.693 -14.794 21.747 1.00 0.00

ATOM 1657 CB GLU A 326 -147.891 -15.155 23.371 1.00 0.00

ATOM 1658 CG GLU A 326 -147.089 -16.216 24.106 1.00 0.00

ATOM 1659 CD GLU A 326 -146.389 -15.671 25.334 1.00 0.00

ATOM 1660 OEl GLU A 326 -146.470 -14.447 25.570 1.00 0.00

ATOM 1661 OE2 GLU A 326 -145.758 -16.467 26.061 1.00 0.00

ATOM 1662 N LEU A 327 -148.966 -13.516 20.999 1.00 0.00

ATOM 1663 CA LEU A 327 -149.829 -12.446 20.529 1.00 0.00

ATOM 1664 C LEU A 327 -150.833 -12.947 19.530 1.00 0.00

ATOM 1665 O LEU A 327 -152.019 -12.743 19.729 1.00 0.00

ATOM 1666 CB LEU A 327 -149.003 -11.347 19.856 1.00 0.00

ATOM 1667 CG LEU A 327 -149.786 -10.158 19.296 1.00 0.00

ATOM 1668 CDl LEU A 327 -150.527 -9.431 20.407 1.00 0.00

ATOM 1669 CD2 LEU A 327 -148.849 -9.167 18.622 1.00 0.00

ATOM 1670 N GLN A 328 -150.347 -13.600 18.455 1.00 0.00

ATOM 1671 CA GLN A 328 -151.258 -14.076 17.429 1.00 0.00

ATOM 1672 C GLN A 328 -152.301 -14.987 18.013 1.00 0.00

ATOM 1673 O GLN A 328 -153.469 -14.851 17.686 1.00 0.00

ATOM 1674 CB GLN A 328 -150.495 -14.854 16.354 1.00 0.00

ATOM 1675 CG GLN A 328 -149.610 -13.987 15.473 1.00 0.00

ATOM 1676 CD GLN A 328 -148.785 -14.803 14.496 1.00 0.00

ATOM 1677 OEl GLN A 328 -148.802 -16.033 14.531 1.00 0.00

ATOM 1678 NE2 GLN A 328 -148.059 -14.116 13.621 1.00 0.00

ATOM 1679 N ALA A 329 -151.860 -15.907 18.893 1.00 0.00

ATOM 1680 CA ALA A 329 -152.798 -16.832 19.503 1.00 0.00

ATOM 1681 C ALA A 329 -153.862 -16.093 20.264 1.00 0.00

ATOM 1682 O ALA A 329 -155.036 -16.331 20.030 1.00 0.00

ATOM 1683 CB ALA A 329 -152.076 -17.758 20.471 1.00 0.00

ATOM 1684 N GLN A 330 -153.437 -15.193 21.175 1.00 0.00

ATOM 1685 CA GLN A 330 -154.404 -14.458 21.974 1.00 0.00

ATOM 1686 C GLN A 330 -155.375 -13.717 21.100 1.00 0.00

ATOM 1687 O GLN A 330 -156.558 -13.706 21.395 1.00 0.00

ATOM 1688 CB GLN A 330 -153.695 -13.439 22.869 1.00 0.00

ATOM 1689 CG GLN A 330 -152.900 -14.059 24.007 1.00 0.00

ATOM 1690 CD GLN A 330 -152.121 -13.031 24.802 1.00 0.00

ATOM 1691 OEl GLN A 330 -152.099 -11.850 24.454 1.00 0.00

ATOM 1692 NE2 GLN A 330 -151.481 -13.476 25.876 1.00 0.00

ATOM 1693 N HIS A 331 -154.859 -13.106 20.015 1.00 0.00

ATOM 1694 CA HIS A 331 -155.736 -12.369 19.121 1.00 0.00

ATOM 1695 C HIS A 331 -156.790 -13.270 18.545 1.00 0.00

ATOM 1696 O HIS A 331 -157.959 -12.918 18.563 1.00 0.00

ATOM 1697 CB HIS A 331 -154.936 -11.765 17.964 1.00 0.00

ATOM 1698 CG HIS A 331 -155.779 -11.035 16.964 1.00 0.00

ATOM 1699 NDl HIS A 331 -156.327 -9.797 17.216 1.00 0.00

ATOM 1700 CD2 HIS A 331 -156.247 -11.299 15.612 1.00 0.00

ATOM 1701 CEl HIS A 331 -157.026 -9.399 16.137 1.00 0.00

ATOM 1702 NE2 HIS A 331 -156.983 -10.296 15.172 1.00 0.00

ATOM 1703 N SER A 332 -156.365 -14.446 18.039 1.00 0.00

ATOM 1704 CA SER A 332 -157.323 -15.368 17.454 1.00 0.00

ATOM 1705 C SER A 332 -158.340 -15.801 18.472 1.00 0.00

ATOM 1706 O SER A 332 -159.525 -15.788 18.182 1.00 0.00

ATOM 1707 CB SER A 332 -156.613 -16.617 16.926 1.00 0.00

ATOM 1708 OG SER A 332 -155.771 -16.300 15.832 1.00 0.00

ATOM 1709 N MET A 333 -157.855 -16.175 19.673 1.00 0.00

ATOM 1710 CA MET A 333 -158.763 -16.603 20.724 1.00 0.00

ATOM 1711 C MET A 333 -159.773 -15.532 21.024 1.00 0.00

ATOM 1712 O MET A 333 -160.952 -15.830 21.138 1.00 0.00

ATOM 1713 CB MET A 333 -157.991 -16.908 22.008 1.00 0.00

ATOM 1714 CG MET A 333 -157.113 -18.147 21.927 1.00 0.00

ATOM 1715 SD MET A 333 -156.120 -18.396 23.410 1.00 0.00

ATOM 1716 CE MET A 333 -157.391 -18.806 24.603 1.00 0.00 ATOM 1717 N ARG A 334 -159.295 -14.279 21.143 1.00 0.00

ATOM 1718 CA ARG A 334 -160.201 -13.185 21.447 1.00 0.00

ATOM 1719 C ARG A 334 -161.243 -13.037 20.374 1.00 0.00

ATOM 1720 O ARG A 334 -162.401 -12.821 20.693 1.00 0.00

ATOM 1721 CB ARG A 334 -159.433 -11.865 21.551 1.00 0.00

ATOM 1722 CG ARG A 334 -158.565 -11.750 22.794 1.00 0.00

ATOM 1723 CD ARG A 334 -158.069 -10.327 22.991 1.00 0.00

ATOM 1724 NE ARG A 334 -157.179 -9.903 21.913 1.00 0.00

ATOM 1725 CZ ARG A 334 -155.867 -10.118 21.899 1.00 0.00

ATOM 1726 NHl ARG A 334 -155.137 -9.697 20.875 1.00 0.00

ATOM 1727 NH2 ARG A 334 -155.289 -10.754 22.909 1.00 0.00

ATOM 1728 N ASP A 335 -160.823 -13.161 19.099 1.00 0.00

ATOM 1729 CA ASP A 335 -161.775 -13.028 18.010 1.00 0.00

ATOM 1730 C ASP A 335 -162.898 -14.016 18.163 1.00 0.00

ATOM 1731 O ASP A 335 -164.054 -13.640 18.036 1.00 0.00

ATOM 1732 CB ASP A 335 -161.090 -13.284 16.666 1.00 0.00

ATOM 1733 CG ASP A 335 -160.170 -12.152 16.255 1.00 0.00

ATOM 1734 ODl ASP A 335 -160.241 -11.072 16.882 1.00 0.00

ATOM 1735 OD2 ASP A 335 -159.378 -12.341 15.309 1.00 0.00

ATOM 1736 N ALA A 336 -162.542 -15.283 18.452 1.00 0.00

ATOM 1737 CA ALA A 336 -163.570 -16.295 18.627 1.00 0.00

ATOM 1738 C ALA A 336 -164.473 -15.949 19.778 1.00 0.00

ATOM 1739 O ALA A 336 -165.682 -16.006 19.627 1.00 0.00

ATOM 1740 CB ALA A 336 -162.938 -17.650 18.907 1.00 0.00

ATOM 1741 N LEU A 337 -163.868 -15.585 20.926 1.00 0.00

ATOM 1742 CA LEU A 337 -164.668 -15.291 22.103 1.00 0.00

ATOM 1743 C LEU A 337 -165.629 -14.161 21.865 1.00 0.00

ATOM 1744 O LEU A 337 -166.791 -14.281 99 999 1.00 0.00

ATOM 1745 CB LEU A 337 -163.770 -14.895 23.277 1.00 0.00

ATOM 1746 CG LEU A 337 -162.921 -16.013 23.887 1.00 0.00

ATOM 1747 CDl LEU A 337 -161.942 -15.449 24.906 1.00 0.00

ATOM 1748 CD2 LEU A 337 -163.800 -17.036 24.588 1.00 0.00

ATOM 1749 N GLU A 338 -165.137 -13.064 21.255 1.00 0.00

ATOM 1750 CA GLU A 338 -165.999 -11.916 21.026 1.00 0.00

ATOM 1751 C GLU A 338 -167.198 -12.298 20.206 1.00 0.00

ATOM 1752 O GLU A 338 -168.304 -11.896 20.533 1.00 0.00

ATOM 1753 CB GLU A 338 -165.241 -10.817 20.279 1.00 0.00

ATOM 1754 CG GLU A 338 -164.175 -10.122 21.111 1.00 0.00

ATOM 1755 CD GLU A 338 -163.364 -9.128 20.305 1.00 0.00

ATOM 1756 OEl GLU A 338 -163.584 -9.035 19.079 1.00 0.00

ATOM 1757 OE2 GLU A 338 -162.506 -8.441 20.899 1.00 0.00

ATOM 1758 N SER A 339 -166.964 -13.094 19.145 1.00 0.00

ATOM 1759 CA SER A 339 -168.078 -13.543 18.326 1.00 0.00

ATOM 1760 C SER A 339 -169.055 -14.340 19.142 1.00 0.00

ATOM 1761 O SER A 339 -170.251 -14.194 18.950 1.00 0.00

ATOM 1762 CB SER A 339 -167.578 -14.427 17.181 1.00 0.00

ATOM 1763 OG SER A 339 -166.784 -13.684 16.273 1.00 0.00

ATOM 1764 N THR A 340 -168.529 -15.175 20.062 1.00 0.00

ATOM 1765 CA THR A 340 -169.401 -16.018 20.866 1.00 0.00

ATOM 1766 C THR A 340 -170.320 -15.229 21.760 1.00 0.00

ATOM 1767 O THR A 340 -171.504 -15.523 21.791 1.00 0.00

ATOM 1768 CB THR A 340 -168.591 -16.954 21.783 1.00 0.00

ATOM 1769 OGl THR A 340 -167.783 -17.827 20.985 1.00 0.00

ATOM 1770 CG2 THR A 340 -169.524 -17.794 22.642 1.00 0.00

ATOM 1771 N LEU A 341 -169.784 -14.228 22.490 1.00 0.00

ATOM 1772 CA LEU A 341 -170.640 -13.467 23.388 1.00 0.00

ATOM 1773 C LEU A 341 -171.649 -12.667 22.611 1.00 0.00

ATOM 1774 O LEU A 341 -172.826 -12.715 22.933 1.00 0.00

ATOM 1775 CB LEU A 341 -169.808 -12.500 24.231 1.00 0.00

ATOM 1776 CG LEU A 341 -168.899 -13.131 25.289 1.00 0.00

ATOM 1777 CDl LEU A 341 -167.996 -12.081 25.918 1.00 0.00

ATOM 1778 CD2 LEU A 341 -169.726 -13.772 26.393 1.00 0.00

ATOM 1779 N ALA A 342 -171.175 -11.946 21.574 1.00 0.00

ATOM 1780 CA ALA A 342 -172.092 -11.177 20.745 1.00 0.00

ATOM 1781 C ALA A 342 -173.210 -12.056 20.257 1.00 0.00

ATOM 1782 O ALA A 342 -174.337 -11.604 20.139 1.00 0.00

ATOM 1783 CB ALA A 342 -171.363 -10.603 19.540 1.00 0.00

ATOM 1784 N GLU A 343 -172.870 -13.334 19.996 1.00 0.00 ATOM 1785 CA GLU A 343 -173.875 -14.278 19.544 1.00 0.00

ATOM 1786 C GLU A 343 -174.926 -14.498 20.597 1.00 0.00

ATOM 1787 O GLU A 343 -176.098 -14.298 20.316 1.00 0.00

ATOM 1788 CB GLU A 343 -173.234 -15.630 19.225 1.00 0.00

ATOM 1789 CG GLU A 343 -174.211 -16.674 18.709 1.00 0.00

ATOM 1790 CD GLU A 343 -173.550 -18.014 18.451 1.00 0.00

ATOM 1791 OEl GLU A 343 -172.323 -18.121 18.660 1.00 0.00

ATOM 1792 OE2 GLU A 343 -174.259 -18.957 18.041 1.00 0.00

ATOM 1793 N THR A 344 -174.500 -14.918 21.804 1.00 0.00

ATOM 1794 CA THR A 344 -175.464 -15.228 22.851 1.00 0.00

ATOM 1795 C THR A 344 -176.387 -14.070 23.107 1.00 0.00

ATOM 1796 O THR A 344 -177.591 -14.262 23.153 1.00 0.00

ATOM 1797 CB THR A 344 -174.764 -15.563 24.181 1.00 0.00

ATOM 1798 OGl THR A 344 -173.927 -16.712 24.008 1.00 0.00

ATOM 1799 CG2 THR A 344 -175.791 -15.861 25.263 1.00 0.00

ATOM 1800 N GLU A 345 -175.797 -12.868 23.269 1.00 0.00

ATOM 1801 CA GLU A 345 -176.598 -11.688 23.551 1.00 0.00

ATOM 1802 C GLU A 345 -177.729 -11.545 22.573 1.00 0.00

ATOM 1803 O GLU A 345 -178.865 -11.373 22.986 1.00 0.00

ATOM 1804 CB GLU A 345 -175.739 -10.424 23.465 1.00 0.00

ATOM 1805 CG GLU A 345 -176.491 -9.140 23.772 1.00 0.00

ATOM 1806 CD GLU A 345 -175.599 -7.916 23.717 1.00 0.00

ATOM 1807 OEl GLU A 345 -174.385 -8.075 23.472 1.00 0.00

ATOM 1808 OE2 GLU A 345 -176.115 -6.796 23.919 1.00 0.00

ATOM 1809 N ALA A 346 -177.405 -11.628 21.268 1.00 0.00

ATOM 1810 CA ALA A 346 -178.444 -11.491 20.261 1.00 0.00

ATOM 1811 C ALA A 346 -179.437 -12.616 20.341 1.00 0.00

ATOM 1812 O ALA A 346 -180.629 -12.364 20.282 1.00 0.00

ATOM 1813 CB ALA A 346 -177.835 -11.499 18.867 1.00 0.00

ATOM 1814 N ARG A 347 -178.935 -13.860 20.476 1.00 0.00

ATOM 1815 CA ARG A 347 -179.830 -15.006 20.484 1.00 0.00

ATOM 1816 C ARG A 347 -180.817 -14.944 21.618 1.00 0.00

ATOM 1817 O ARG A 347 -182.012 -14.992 21.375 1.00 0.00

ATOM 1818 CB ARG A 347 -179.035 -16.305 20.632 1.00 0.00

ATOM 1819 CG ARG A 347 -179.886 -17.563 20.583 1.00 0.00

ATOM 1820 CD ARG A 347 -179.055 -18.804 20.867 1.00 0.00

ATOM 1821 NE ARG A 347 -178.578 -18.838 22.247 1.00 0.00

ATOM 1822 CZ ARG A 347 -179.324 -19.195 23.288 1.00 0.00

ATOM 1823 NHl ARG A 347 -178.805 -19.196 24.507 1.00 0.00

ATOM 1824 NH2 ARG A 347 -180.588 -19.550 23.105 1.00 0.00

ATOM 1825 N TYR A 348 -180.300 -14.846 22.859 1.00 0.00

ATOM 1826 CA TYR A 348 -181.181 -14.841 24.013 1.00 0.00

ATOM 1827 C TYR A 348 -182.201 -13.740 23.917 1.00 0.00

ATOM 1828 O TYR A 348 -183.337 -13.947 24.314 1.00 0.00

ATOM 1829 CB TYR A 348 -180.378 -14.630 25.298 1.00 0.00

ATOM 1830 CG TYR A 348 -181.227 -14.583 26.549 1.00 0.00

ATOM 1831 CDl TYR A 348 -181.715 -15.751 27.122 1.00 0.00

ATOM 1832 CD2 TYR A 348 -181.537 -13.371 27.152 1.00 0.00

ATOM 1833 CEl TYR A 348 -182.491 -15.717 28.265 1.00 0.00

ATOM 1834 CE2 TYR A 348 -182.311 -13.318 28.296 1.00 0.00

ATOM 1835 CZ TYR A 348 -182.789 -14.506 28.850 1.00 0.00

ATOM 1836 OH TYR A 348 -183.562 -14.469 29.988 1.00 0.00

ATOM 1837 N SER A 349 -181.788 -12.574 23.378 1.00 0.00

ATOM 1838 CA SER A 349 -182.715 -11.460 23.268 1.00 0.00

ATOM 1839 C SER A 349 -183.979 -11.862 22.560 1.00 0.00

ATOM 1840 O SER A 349 -185.058 -11.595 23.063 1.00 0.00

ATOM 1841 CB SER A 349 -182.080 -10.312 22.481 1.00 0.00

ATOM 1842 OG SER A 349 -180.995 -9.744 23.193 1.00 0.00

ATOM 1843 N SER A 350 -183.835 -12.516 21.392 1.00 0.00

ATOM 1844 CA SER A 350 -185.016 -12.943 20.660 1.00 0.00

ATOM 1845 C SER A 350 -185.771 -13.989 21.426 1.00 0.00

ATOM 1846 O SER A 350 -186.989 -13.935 21.476 1.00 0.00

ATOM 1847 CB SER A 350 -184.622 -13.532 19.304 1.00 0.00

ATOM 1848 OG SER A 350 -184.056 -12.543 18.463 1.00 0.00

ATOM 1849 N GLN A 351 -185.033 -14.946 22.023 1.00 0.00

ATOM 1850 CA GLN A 351 -185.688 -16.035 22.729 1.00 0.00

ATOM 1851 C GLN A 351 -186.528 -15.532 23.867 1.00 0.00

ATOM 1852 O GLN A 351 -187.704 -15.853 23.933 1.00 0.00 ATOM 1853 CB GLN A 351 -184.650 -17.000 23.303 1.00 0.00

ATOM 1854 CG GLN A 351 -183.926 -17.829 22.256 1.00 0.00

ATOM 1855 CD GLN A 351 -182.815 -18.675 22.847 1.00 0.00

ATOM 1856 OEl GLN A 351 -182.526 -18.591 24.040 1.00 0.00

ATOM 1857 NE2 GLN A 351 -182.190 -19.497 22.011 1.00 0.00

ATOM 1858 N LEU A 352 -185.909 -14.738 24.763 1.00 0.00

ATOM 1859 CA LEU A 352 -186.651 -14.197 25.888 1.00 0.00

ATOM 1860 C LEU A 352 -187.814 -13.390 25.387 1.00 0.00

ATOM 1861 O LEU A 352 -188.886 -13.447 25.969 1.00 0.00

ATOM 1862 CB LEU A 352 -185.753 -13.296 26.739 1.00 0.00

ATOM 1863 CG LEU A 352 -186.400 -12.667 27.975 1.00 0.00

ATOM 1864 CDl LEU A 352 -186.872 -13.744 28.940 1.00 0.00

ATOM 1865 CD2 LEU A 352 -185.408 -11.775 28.706 1.00 0.00

ATOM 1866 N ALA A 353 -187.583 -12.652 24.283 1.00 0.00

ATOM 1867 CA ALA A 353 -188.656 -11.880 23.681 1.00 0.00

ATOM 1868 C ALA A 353 -189.827 -12.774 23.370 1.00 0.00

ATOM 1869 O ALA A 353 -190.956 -12.407 23.650 1.00 0.00

ATOM 1870 CB ALA A 353 -188.183 -11.232 22.388 1.00 0.00

ATOM 1871 N GLN A 354 -189.535 -13.958 22.798 1.00 0.00

ATOM 1872 CA GLN A 354 -190.605 -14.886 22.478 1.00 0.00

ATOM 1873 C GLN A 354 -191.220 -15.457 23.725 1.00 0.00

ATOM 1874 O GLN A 354 -192.430 -15.615 23.773 1.00 0.00

ATOM 1875 CB GLN A 354 -190.073 -16.048 21.637 1.00 0.00

ATOM 1876 CG GLN A 354 -189.673 -15.658 20.223 1.00 0.00

ATOM 1877 CD GLN A 354 -189.049 -16.807 19.456 1.00 0.00

ATOM 1878 OEl GLN A 354 -188.816 -17.882 20.010 1.00 0.00

ATOM 1879 NE2 GLN A 354 -188.775 -16.584 18.176 1.00 0.00

ATOM 1880 N MET A 355 -190.378 -15.753 24.738 1.00 0.00

ATOM 1881 CA MET A 355 -190.901 -16.301 25.979 1.00 0.00

ATOM 1882 C MET A 355 -191.943 -15.386 26.557 1.00 0.00

ATOM 1883 O MET A 355 -193.005 -15.843 26.950 1.00 0.00

ATOM 1884 CB MET A 355 -189.778 -16.467 27.006 1.00 0.00

ATOM 1885 CG MET A 355 -188.797 -17.579 26.677 1.00 0.00

ATOM 1886 SD MET A 355 -189.573 -19.207 26.652 1.00 0.00

ATOM 1887 CE MET A 355 -189.958 -19.426 28.387 1.00 0.00

ATOM 1888 N GLN A 356 -191.620 -14.080 26.590 1.00 0.00

ATOM 1889 CA GLN A 356 -192.560 -13.113 27.129 1.00 0.00

ATOM 1890 C GLN A 356 -193.821 -13.078 26.312 1.00 0.00

ATOM 1891 O GLN A 356 -194.893 -12.924 26.877 1.00 0.00

ATOM 1892 CB GLN A 356 -191.948 -11.711 27.125 1.00 0.00

ATOM 1893 CG GLN A 356 -190.833 -11.518 28.140 1.00 0.00

ATOM 1894 CD GLN A 356 -190.175 -10.156 28.031 1.00 0.00

ATOM 1895 OEl GLN A 356 -190.489 -9.375 27.133 1.00 0.00

ATOM 1896 NE2 GLN A 356 -189.258 -9.868 28.947 1.00 0.00

ATOM 1897 N CYS A 357 -193.688 -13.238 24.980 1.00 0.00

ATOM 1898 CA CYS A 357 -194.876 -13.226 24.141 1.00 0.00

ATOM 1899 C CYS A 357 -195.800 -14.351 24.509 1.00 0.00

ATOM 1900 O CYS A 357 -196.988 -14.119 24.662 1.00 0.00

ATOM 1901 CB CYS A 357 -194.494 -13.381 22.668 1.00 0.00

ATOM 1902 SG CYS A 357 -193.633 -11.955 21.965 1.00 0.00

ATOM 1903 N MET A 358 -195.238 -15.568 24.658 1.00 0.00

ATOM 1904 CA MET A 358 -196.064 -16.713 25.013 1.00 0.00

ATOM 1905 C MET A 358 -196.811 -16.434 26.286 1.00 0.00

ATOM 1906 O MET A 358 -197.994 -16.722 26.364 1.00 0.00

ATOM 1907 CB MET A 358 -195.197 -17.957 25.217 1.00 0.00

ATOM 1908 CG MET A 358 -194.575 -18.496 23.939 1.00 0.00

ATOM 1909 SD MET A 358 -195.808 -19.007 22.727 1.00 0.00

ATOM 1910 CE MET A 358 -196.504 -20.444 23.537 1.00 0.00

ATOM 1911 N ILE A 359 -196.106 -15.856 27.277 1.00 0.00

ATOM 1912 CA ILE A 359 -196.761 -15.547 28.533 1.00 0.00

ATOM 1913 C ILE A 359 -197.911 -14.606 28.307 1.00 0.00

ATOM 1914 O ILE A 359 -198.976 -14.815 28.866 1.00 0.00

ATOM 1915 CB ILE A 359 -195.790 -14.879 29.527 1.00 0.00

ATOM 1916 CGl ILE A 359 -194.717 -15.875 29.972 1.00 0.00

ATOM 1917 CG2 ILE A 359 -196.540 -14.395 30.758 1.00 0.00

ATOM 1918 CDl ILE A 359 -193.575 -15.239 30.735 1.00 0.00

ATOM 1919 N THR A 360 -197.688 -13.576 27.467 1.00 0.00

ATOM 1920 CA THR A 360 -198.751 -12.623 27.197 1.00 0.00 ATOM 1921 C THR A 360 -199.912 -13.283 26.507 1.00 0.00

ATOM 1922 O THR A 360 -201.048 -13.028 26.869 1.00 0.00

ATOM 1923 CB THR A 360 -198.263 -11.477 26.292 1.00 0.00

ATOM 1924 OGl THR A 360 -197.211 -10.759 26.949 1.00 0.00

ATOM 1925 CG2 THR A 360 -199.403 -10.514 25.992 1.00 0.00

ATOM 1926 N ASN A 361 -199.611 -14.141 25.512 1.00 0.00

ATOM 1927 CA ASN A 361 -200.683 -14.816 24.800 1.00 0.00

ATOM 1928 C ASN A 361 -201.470 -15.684 25.742 1.00 0.00

ATOM 1929 O ASN A 361 -202.689 -15.696 25.670 1.00 0.00

ATOM 1930 CB ASN A 361 -200.114 -15.699 23.687 1.00 0.00

ATOM 1931 CG ASN A 361 -199.595 -14.892 22.513 1.00 0.00

ATOM 1932 ODl ASN A 361 -199.963 -13.732 22.333 1.00 0.00

ATOM 1933 ND2 ASN A 361 -198.736 -15.508 21.708 1.00 0.00

ATOM 1934 N VAL A 362 -200.759 -16.394 26.638 1.00 0.00

ATOM 1935 CA VAL A 362 -201.452 -17.210 27.622 1.00 0.00

ATOM 1936 C VAL A 362 -202.301 -16.338 28.505 1.00 0.00

ATOM 1937 O VAL A 362 -203.388 -16.741 28.889 1.00 0.00

ATOM 1938 CB VAL A 362 -200.462 -17.980 28.515 1.00 0.00

ATOM 1939 CGl VAL A 362 -201.198 -18.666 29.657 1.00 0.00

ATOM 1940 CG2 VAL A 362 -199.731 -19.042 27.708 1.00 0.00

ATOM 1941 N GLU A 363 -201.786 -15.130 28.808 1.00 0.00

ATOM 1942 CA GLU A 363 -202.515 -14.216 29.668 1.00 0.00

ATOM 1943 C GLU A 363 -203.850 -13.861 29.074 1.00 0.00

ATOM 1944 O GLU A 363 -204.854 -13.974 29.759 1.00 0.00

ATOM 1945 CB GLU A 363 -201.724 -12.922 29.868 1.00 0.00

ATOM 1946 CG GLU A 363 -202.394 -11.922 30.797 1.00 0.00

ATOM 1947 CD GLU A 363 -201.567 -10.668 30.997 1.00 0.00

ATOM 1948 OEl GLU A 363 -200.462 -10.587 30.420 1.00 0.00

ATOM 1949 OE2 GLU A 363 -202.023 -9.766 31.731 1.00 0.00

ATOM 1950 N ALA A 364 -203.851 -13.437 27.794 1.00 0.00

ATOM 1951 CA ALA A 364 -205.102 -13.054 27.160 1.00 0.00

ATOM 1952 C ALA A 364 -206.094 -14.180 27.207 1.00 0.00

ATOM 1953 O ALA A 364 -207.258 -13.951 27.499 1.00 0.00

ATOM 1954 CB ALA A 364 -204.867 -12.688 25.703 1.00 0.00

ATOM 1955 N GLN A 365 -205.610 -15.407 26.930 1.00 0.00

ATOM 1956 CA GLN A 365 -206.487 -16.562 26.985 1.00 0.00

ATOM 1957 C GLN A 365 -207.066 -16.716 28.363 1.00 0.00

ATOM 1958 O GLN A 365 -208.268 -16.879 28.498 1.00 0.00

ATOM 1959 CB GLN A 365 -205.715 -17.838 26.638 1.00 0.00

ATOM 1960 CG GLN A 365 -205.313 -17.943 25.177 1.00 0.00

ATOM 1961 CD GLN A 365 -204.440 -19.149 24.897 1.00 0.00

ATOM 1962 OEl GLN A 365 -204.059 -19.878 25.814 1.00 0.00

ATOM 1963 NE2 GLN A 365 -204.117 -19.364 23.627 1.00 0.00

ATOM 1964 N LEU A 366 -206.184 -16.657 29.381 1.00 0.00

ATOM 1965 CA LEU A 366 -206.631 -16.819 30.755 1.00 0.00

ATOM 1966 C LEU A 366 -207.726 -15.846 31.091 1.00 0.00

ATOM 1967 O LEU A 366 -208.731 -16.247 31.656 1.00 0.00

ATOM 1968 CB LEU A 366 -205.473 -16.584 31.727 1.00 0.00

ATOM 1969 CG LEU A 366 -205.800 -16.713 33.215 1.00 0.00

ATOM 1970 CDl LEU A 366 -206.244 -18.130 33.548 1.00 0.00

ATOM 1971 CD2 LEU A 366 -204.582 -16.385 34.064 1.00 0.00

ATOM 1972 N ALA A 367 -207.522 -14.563 30.735 1.00 0.00

ATOM 1973 CA ALA A 367 -208.529 -13.562 31.038 1.00 0.00

ATOM 1974 C ALA A 367 -209.834 -13.888 30.368 1.00 0.00

ATOM 1975 O ALA A 367 -210.875 -13.755 30.993 1.00 0.00

ATOM 1976 CB ALA A 367 -208.077 -12.192 30.555 1.00 0.00

ATOM 1977 N GLU A 368 -209.767 -14.326 29.095 1.00 0.00

ATOM 1978 CA GLU A 368 -210.988 -14.644 28.373 1.00 0.00

ATOM 1979 C GLU A 368 -211.786 -15.698 29.088 1.00 0.00

ATOM 1980 O GLU A 368 -212.972 -15.512 29.304 1.00 0.00

ATOM 1981 CB GLU A 368 -210.661 -15.167 26.972 1.00 0.00

ATOM 1982 CG GLU A 368 -211.884 -15.484 26.127 1.00 0.00

ATOM 1983 CD GLU A 368 -211.522 -15.967 24.737 1.00 0.00

ATOM 1984 OEl GLU A 368 -210.314 -16.042 24.429 1.00 0.00

ATOM 1985 OE2 GLU A 368 -212.447 -16.270 23.954 1.00 0.00

ATOM 1986 N ILE A 369 -211.117 -16.807 29.455 1.00 0.00

ATOM 1987 CA ILE A 369 -211.830 -17.887 30.117 1.00 0.00

ATOM 1988 C ILE A 369 -212.380 -17.441 31.442 1.00 0.00 ATOM 1989 O ILE A 369 -213.511 -17.780 31.756 1.00 0.00

ATOM 1990 CB ILE A 369 -210.909 -19.094 30.378 1.00 0.00

ATOM 1991 CGl ILE A 369 -210.504 -19.752 29.057 1.00 0.00

ATOM 1992 CG2 ILE A 369 -211.620 -20.130 31.235 1.00 0.00

ATOM 1993 CDl ILE A 369 -209.396 -20.773 29.199 1.00 0.00

ATOM 1994 N ARG A 370 -211.583 -16.673 32.211 1.00 0.00

ATOM 1995 CA ARG A 370 -212.050 -16.231 33.516 1.00 0.00

ATOM 1996 C ARG A 370 -213.323 -15.440 33.405 1.00 0.00

ATOM 1997 O ARG A 370 -214.255 -15.701 34.147 1.00 0.00

ATOM 1998 CB ARG A 370 -211.001 -15.344 34.189 1.00 0.00

ATOM 1999 CG ARG A 370 -211.377 -14.891 35.590 1.00 0.00

ATOM 2000 CD ARG A 370 -210.338 -13.941 36.161 1.00 0.00

ATOM 2001 NE ARG A 370 -210.284 -12.680 35.424 1.00 0.00

ATOM 2002 CZ ARG A 370 -211.163 -11.694 35.566 1.00 0.00

ATOM 2003 NHl ARG A 370 -211.034 -10.583 34.853 1.00 0.00

ATOM 2004 NH2 ARG A 370 -212.169 -11.820 36.421 1.00 0.00

ATOM 2005 N ALA A 371 -213.360 -14.478 32.460 1.00 0.00

ATOM 2006 CA ALA A 371 -214.570 -13.692 32.287 1.00 0.00

ATOM 2007 C ALA A 371 -215.724 -14.584 31.929 1.00 0.00

ATOM 2008 O ALA A 371 -216.804 -14.425 32.479 1.00 0.00

ATOM 2009 CB ALA A 371 -214.384 -12.671 31.175 1.00 0.00

ATOM 2010 N ASP A 372 -215.481 -15.535 31.005 1.00 0.00

ATOM 2011 CA ASP A 372 -216.536 -16.457 30.620 1.00 0.00

ATOM 2012 C ASP A 372 -217.040 -17.213 31.815 1.00 0.00

ATOM 2013 O ASP A 372 -218.242 -17.363 31.968 1.00 0.00

ATOM 2014 CB ASP A 372 -216.016 -17.467 29.594 1.00 0.00

ATOM 2015 CG ASP A 372 -215.800 -16.850 28.227 1.00 0.00

ATOM 2016 ODl ASP A 372 -216.269 -15.714 28.007 1.00 0.00

ATOM 2017 OD2 ASP A 372 -215.161 -17.503 27.375 1.00 0.00

ATOM 2018 N LEU A 373 -216.107 -17.680 32.670 1.00 0.00

ATOM 2019 CA LEU A 373 -216.520 -18.433 33.841 1.00 0.00

ATOM 2020 C LEU A 373 -217.355 -17.587 34.761 1.00 0.00

ATOM 2021 O LEU A 373 -218.319 -18.090 35.317 1.00 0.00

ATOM 2022 CB LEU A 373 -215.299 -18.922 34.623 1.00 0.00

ATOM 2023 CG LEU A 373 -214.458 -20.010 33.954 1.00 0.00

ATOM 2024 CDl LEU A 373 -213.186 -20.271 34.746 1.00 0.00

ATOM 2025 CD2 LEU A 373 -215.238 -21.313 33.864 1.00 0.00

ATOM 2026 N GLU A 374 -216.983 -16.300 34.915 1.00 0.00

ATOM 2027 CA GLU A 374 -217.755 -15.427 35.784 1.00 0.00

ATOM 2028 C GLU A 374 -219.181 -15.361 35.313 1.00 0.00

ATOM 2029 O GLU A 374 -220.089 -15.488 36.118 1.00 0.00

ATOM 2030 CB GLU A 374 -217.171 -14.013 35.777 1.00 0.00

ATOM 2031 CG GLU A 374 -217.891 -13.040 36.697 1.00 0.00

ATOM 2032 CD GLU A 374 -217.264 -11.660 36.690 1.00 0.00

ATOM 2033 OEl GLU A 374 -216.259 -11.467 35.975 1.00 0.00

ATOM 2034 OE2 GLU A 374 -217.779 -10.770 37.400 1.00 0.00

ATOM 2035 N ARG A 375 -219.360 -15.170 33.992 1.00 0.00

ATOM 2036 CA ARG A 375 -220.706 -15.111 33.451 1.00 0.00

ATOM 2037 C ARG A 375 -221.438 -16.396 33.720 1.00 0.00

ATOM 2038 O ARG A 375 -222.593 -16.354 34.115 1.00 0.00

ATOM 2039 CB ARG A 375 -220.667 -14.886 31.938 1.00 0.00

ATOM 2040 CG ARG A 375 -220.217 -13.492 31.530 1.00 0.00

ATOM 2041 CD ARG A 375 -220.130 -13.360 30.018 1.00 0.00

ATOM 2042 NE ARG A 375 -219.673 -12.035 29.609 1.00 0.00

ATOM 2043 CZ ARG A 375 -219.440 -11.679 28.350 1.00 0.00

ATOM 2044 NHl ARG A 375 -219.026 -10.451 28.074 1.00 0.00

ATOM 2045 NH2 ARG A 375 -219.624 -12.554 27.371 1.00 0.00

ATOM 2046 N GLN A 376 -220.750 -17.537 33.516 1.00 0.00

ATOM 2047 CA GLN A 376 -221.394 -18.818 33.755 1.00 0.00

ATOM 2048 C GLN A 376 -221.831 -18.938 35.187 1.00 0.00

ATOM 2049 O GLN A 376 -222.955 -19.340 35.436 1.00 0.00

ATOM 2050 CB GLN A 376 -220.432 -19.967 33.449 1.00 0.00

ATOM 2051 CG GLN A 376 -220.133 -20.151 31.971 1.00 0.00

ATOM 2052 CD GLN A 376 -219.077 -21.208 31.717 1.00 0.00

ATOM 2053 OEl GLN A 376 -218.500 -21.761 32.654 1.00 0.00

ATOM 2054 NE2 GLN A 376 -218.820 -21.493 30.445 1.00 0.00

ATOM 2055 N ASN A 377 -220.934 -18.572 36.125 1.00 0.00

ATOM 2056 CA ASN A 377 -221.276 -18.675 37.533 1.00 0.00 ATOM 2057 C ASN A 377 -222.486 -17.846 37.863 1.00 0.00

ATOM 2058 O ASN A 377 -223.366 -18.325 38.562 1.00 0.00

ATOM 2059 CB ASN A 377 -220.116 -18.185 38.403 1.00 0.00

ATOM 2060 CG ASN A 377 -218.954 -19.159 38.428 1.00 0.00

ATOM 2061 ODl ASN A 377 -219.115 -20.339 38.117 1.00 0.00

ATOM 2062 ND2 ASN A 377 -217.778 -18.666 38.797 1.00 0.00

ATOM 2063 N GLN A 378 -222.528 -16.603 37.344 1.00 0.00

ATOM 2064 CA GLN A 378 -223.676 -15.752 37.609 1.00 0.00

ATOM 2065 C GLN A 378 -224.935 -16.404 37.107 1.00 0.00

ATOM 2066 O GLN A 378 -225.914 -16.454 37.832 1.00 0.00

ATOM 2067 CB GLN A 378 -223.515 -14.402 36.907 1.00 0.00

ATOM 2068 CG GLN A 378 -222.443 -13.511 37.515 1.00 0.00

ATOM 2069 CD GLN A 378 -222.221 -12.242 36.716 1.00 0.00

ATOM 2070 OEl GLN A 378 -222.812 -12.053 35.654 1.00 0.00

ATOM 2071 NE2 GLN A 378 -221.363 -11.366 37.227 1.00 0.00

ATOM 2072 N GLU A 379 -224.886 -16.913 35.859 1.00 0.00

ATOM 2073 CA GLU A 379 -226.049 -17.592 35.308 1.00 0.00

ATOM 2074 C GLU A 379 -226.468 -18.717 36.208 1.00 0.00

ATOM 2075 O GLU A 379 -227.647 -18.878 36.474 1.00 0.00

ATOM 2076 CB GLU A 379 -225.729 -18.166 33.926 1.00 0.00

ATOM 2077 CG GLU A 379 -225.560 -17.114 32.841 1.00 0.00

ATOM 2078 CD GLU A 379 -225.123 -17.710 31.517 1.00 0.00

ATOM 2079 OEl GLU A 379 -224.881 -18.934 31.466 1.00 0.00

ATOM 2080 OE2 GLU A 379 -225.022 -16.951 30.529 1.00 0.00

ATOM 2081 N TYR A 380 -225.465 -19.485 36.674 1.00 0.00

ATOM 2082 CA TYR A 380 -225.746 -20.632 37.518 1.00 0.00

ATOM 2083 C TYR A 380 -226.511 -20.231 38.748 1.00 0.00

ATOM 2084 O TYR A 380 -227.566 -20.790 39.001 1.00 0.00

ATOM 2085 CB TYR A 380 -224.445 -21.299 37.966 1.00 0.00

ATOM 2086 CG TYR A 380 -224.649 -22.483 38.885 1.00 0.00

ATOM 2087 CDl TYR A 380 -225.004 -23.725 38.377 1.00 0.00

ATOM 2088 CD2 TYR A 380 -224.486 -22.354 40.259 1.00 0.00

ATOM 2089 CEl TYR A 380 -225.192 -24.812 39.208 1.00 0.00

ATOM 2090 CE2 TYR A 380 -224.670 -23.430 41.106 1.00 0.00

ATOM 2091 CZ TYR A 380 -225.026 -24.666 40.568 1.00 0.00

ATOM 2092 OH TYR A 380 -225.213 -25.747 41.399 1.00 0.00

ATOM 2093 N GLN A 381 -225.964 -19.261 39.506 1.00 0.00

ATOM 2094 CA GLN A 381 -226.624 -18.837 40.731 1.00 0.00

ATOM 2095 C GLN A 381 -228.037 -18.401 40.458 1.00 0.00

ATOM 2096 O GLN A 381 -228.936 -18.783 41.190 1.00 0.00

ATOM 2097 CB GLN A 381 -225.875 -17.662 41.364 1.00 0.00

ATOM 2098 CG GLN A 381 -224.527 -18.034 41.961 1.00 0.00

ATOM 2099 CD GLN A 381 -223.766 -16.828 42.476 1.00 0.00

ATOM 2100 OEl GLN A 381 -224.203 -15.689 42.310 1.00 0.00

ATOM 2101 NE2 GLN A 381 -222.623 -17.076 43.104 1.00 0.00

ATOM 2102 N VAL A 382 -228.215 -17.602 39.389 1.00 0.00

ATOM 2103 CA VAL A 382 -229.545 -17.117 39.062 1.00 0.00

ATOM 2104 C VAL A 382 -230.487 -18.256 38.786 1.00 0.00

ATOM 2105 O VAL A 382 -231.549 -18.309 39.385 1.00 0.00

ATOM 2106 CB VAL A 382 -229.526 -16.217 37.813 1.00 0.00

ATOM 2107 CGl VAL A 382 -230.944 -15.886 37.374 1.00 0.00

ATOM 2108 CG2 VAL A 382 -228.796 -14.915 38.105 1.00 0.00

ATOM 2109 N LEU A 383 -230.081 -19.166 37.878 1.00 0.00

ATOM 2110 CA LEU A 383 -230.941 -20.289 37.539 1.00 0.00

ATOM 2111 C LEU A 383 -231.321 -21.063 38.769 1.00 0.00

ATOM 2112 O LEU A 383 -232.475 -21.436 38.912 1.00 0.00

ATOM 2113 CB LEU A 383 -230.226 -21.240 36.578 1.00 0.00

ATOM 2114 CG LEU A 383 -229.987 -20.718 35.160 1.00 0.00

ATOM 2115 CDl LEU A 383 -229.114 -21.683 34.371 1.00 0.00

ATOM 2116 CD2 LEU A 383 -231.305 -20.553 34.418 1.00 0.00

ATOM 2117 N LEU A 384 -230.334 -21.285 39.657 1.00 0.00

ATOM 2118 CA LEU A 384 -230.608 -22.027 40.877 1.00 0.00

ATOM 2119 C LEU A 384 -231.678 -21.348 41.685 1.00 0.00

ATOM 2120 O LEU A 384 -232.623 -22.002 42.098 1.00 0.00

ATOM 2121 CB LEU A 384 -229.346 -22.126 41.738 1.00 0.00

ATOM 2122 CG LEU A 384 -229.491 -22.870 43.068 1.00 0.00

ATOM 2123 CDl LEU A 384 -229.890 -24.318 42.832 1.00 0.00

ATOM 2124 CD2 LEU A 384 -228.178 -22.857 43.836 1.00 0.00 ATOM 2125 N ASP A 385 -231.519 -20.027 41.901 1.00 0.00

ATOM 2126 CA ASP A 385 -232.501 -19.300 42.688 1.00 0.00

ATOM 2127 C ASP A 385 -233.861 -19.384 42.055 1.00 0.00

ATOM 2128 O ASP A 385 -234.829 -19.661 42.745 1.00 0.00

ATOM 2129 CB ASP A 385 -232.114 -17.824 42.797 1.00 0.00

ATOM 2130 CG ASP A 385 -230.928 -17.599 43.714 1.00 0.00

ATOM 2131 ODl ASP A 385 -230.557 -18.541 44.447 1.00 0.00

ATOM 2132 OD2 ASP A 385 -230.370 -16.482 43.700 1.00 0.00

ATOM 2133 N VAL A 386 -233.914 -19.152 40.729 1.00 0.00

ATOM 2134 CA VAL A 386 -235.185 -19.221 40.025 1.00 0.00

ATOM 2135 C VAL A 386 -235.823 -20.568 40.221 1.00 0.00

ATOM 2136 O VAL A 386 -237.006 -20.639 40.515 1.00 0.00

ATOM 2137 CB VAL A 386 -235.005 -18.997 38.512 1.00 0.00

ATOM 2138 CGl VAL A 386 -236.308 -19.269 37.775 1.00 0.00

ATOM 2139 CG2 VAL A 386 -234.584 -17.562 38.232 1.00 0.00

ATOM 2140 N ARG A 387 -235.016 -21.633 40.056 1.00 0.00

ATOM 2141 CA ARG A 387 -235.550 -22.977 40.199 1.00 0.00

ATOM 2142 C ARG A 387 -236.128 -23.188 41.571 1.00 0.00

ATOM 2143 O ARG A 387 -237.189 -23.779 41.682 1.00 0.00

ATOM 2144 CB ARG A 387 -234.449 -24.017 39.983 1.00 0.00

ATOM 2145 CG ARG A 387 -234.928 -25.457 40.077 1.00 0.00

ATOM 2146 CD ARG A 387 -233.813 -26.432 39.740 1.00 0.00

ATOM 2147 NE ARG A 387 -234.245 -27.823 39.866 1.00 0.00

ATOM 2148 CZ ARG A 387 -233.452 -28.872 39.677 1.00 0.00

ATOM 2149 NHl ARG A 387 -233.933 -30.100 39.814 1.00 0.00

ATOM 2150 NH2 ARG A 387 -232.179 -28.691 39.352 1.00 0.00

ATOM 2151 N ALA A 388 -235.426 -22.692 42.609 1.00 0.00

ATOM 2152 CA ALA A 388 -235.932 -22.854 43.962 1.00 0.00

ATOM 2153 C ALA A 388 -237.309 -22.258 44.075 1.00 0.00

ATOM 2154 O ALA A 388 -238.206 -22.906 44.588 1.00 0.00

ATOM 2155 CB ALA A 388 -235.017 -22.158 44.958 1.00 0.00

ATOM 2156 N ARG A 389 -237.463 -21.016 43.576 1.00 0.00

ATOM 2157 CA ARG A 389 -238.761 -20.368 43.644 1.00 0.00

ATOM 2158 C ARG A 389 -239.803 -21.172 42.919 1.00 0.00

ATOM 2159 O ARG A 389 -240.867 -21.412 43.469 1.00 0.00

ATOM 2160 CB ARG A 389 -238.701 -18.979 43.005 1.00 0.00

ATOM 2161 CG ARG A 389 -237.911 -17.960 43.810 1.00 0.00

ATOM 2162 CD ARG A 389 -237.852 -16.619 43.097 1.00 0.00

ATOM 2163 NE ARG A 389 -237.054 -15.642 43.834 1.00 0.00

ATOM 2164 CZ ARG A 389 -236.798 -14.411 43.404 1.00 0.00

ATOM 2165 NHl ARG A 389 -236.062 -13.591 44.142 1.00 0.00

ATOM 2166 NH2 ARG A 389 -237.278 -14.002 42.238 1.00 0.00

ATOM 2167 N LEU A 390 -239.486 -21.586 41.677 1.00 0.00

ATOM 2168 CA LEU A 390 -240.465 -22.314 40.889 1.00 0.00

ATOM 2169 C LEU A 390 -240.889 -23.587 41.561 1.00 0.00

ATOM 2170 O LEU A 390 -242.079 -23.840 41.645 1.00 0.00

ATOM 2171 CB LEU A 390 -239.886 -22.679 39.521 1.00 0.00

ATOM 2172 CG LEU A 390 -239.667 -21.521 38.546 1.00 0.00

ATOM 2173 CDl LEU A 390 -238.916 -21.993 37.310 1.00 0.00

ATOM 2174 CD2 LEU A 390 -240.996 -20.934 38.099 1.00 0.00

ATOM 2175 N GLU A 391 -239.911 -24.380 42.046 1.00 0.00

ATOM 2176 CA GLU A 391 -240.256 -25.640 42.684 1.00 0.00

ATOM 2177 C GLU A 391 -241.201 -25.422 43.832 1.00 0.00

ATOM 2178 O GLU A 391 -242.158 -26.168 43.968 1.00 0.00

ATOM 2179 CB GLU A 391 -239.001 -26.329 43.223 1.00 0.00

ATOM 2180 CG GLU A 391 -238.082 -26.879 42.143 1.00 0.00

ATOM 2181 CD GLU A 391 -236.793 -27.443 42.708 1.00 0.00

ATOM 2182 OEl GLU A 391 -236.585 -27.337 43.935 1.00 0.00

ATOM 2183 OE2 GLU A 391 -235.991 -27.991 41.923 1.00 0.00

ATOM 2184 N CYS A 392 -240.929 -24.382 44.647 1.00 0.00

ATOM 2185 CA CYS A 392 -241.827 -24.088 45.750 1.00 0.00

ATOM 2186 C CYS A 392 -243.200 -23.772 45.227 1.00 0.00

ATOM 2187 O CYS A 392 -244.176 -24.293 45.744 1.00 0.00

ATOM 2188 CB CYS A 392 -241.320 -22.885 46.548 1.00 0.00

ATOM 2189 SG CYS A 392 -239.805 -23.198 47.486 1.00 0.00

ATOM 2190 N GLU A 393 -243.259 _ 99 no 9 44.184 1.00 0.00

ATOM 2191 CA GLU A 393 -244.546 -22.568 43.607 1.00 0.00

ATOM 2192 C GLU A 393 -245.259 -23.790 43.097 1.00 0.00 ATOM 2193 O GLU A 393 -246.458 -23.910 43.294 1.00 0.00

ATOM 2194 CB GLU A 393 -244.360 -21.600 42.437 1.00 0.00

ATOM 2195 CG GLU A 393 -243.920 -20.204 42.849 1.00 0.00

ATOM 2196 CD GLU A 393 -243.627 -19.311 41.660 1.00 0.00

ATOM 2197 OEl GLU A 393 -243.698 -19.803 40.515 1.00 0.00

ATOM 2198 OE2 GLU A 393 -243.328 -18.117 41.874 1.00 0.00

ATOM 2199 N ILE A 394 -244.502 -24.698 42.450 1.00 0.00

ATOM 2200 CA ILE A 394 -245.110 -25.906 41.917 1.00 0.00

ATOM 2201 C ILE A 394 -245.718 -26.715 43.027 1.00 0.00

ATOM 2202 O ILE A 394 -246.859 -27.132 42.907 1.00 0.00

ATOM 2203 CB ILE A 394 -244.074 -26.789 41.197 1.00 0.00

ATOM 2204 CGl ILE A 394 -243.577 -26.099 39.924 1.00 0.00

ATOM 2205 CG2 ILE A 394 -244.688 -28.126 40.812 1.00 0.00

ATOM 2206 CDl ILE A 394 -242.370 -26.763 39.301 1.00 0.00

ATOM 2207 N ASN A 395 -244.941 -26.924 44.109 1.00 0.00

ATOM 2208 CA ASN A 395 -245.449 -27.704 45.227 1.00 0.00

ATOM 2209 C ASN A 395 -246.749 -27.136 45.724 1.00 0.00

ATOM 2210 O ASN A 395 -247.678 -27.886 45.977 1.00 0.00

ATOM 2211 CB ASN A 395 -244.448 -27.698 46.383 1.00 0.00

ATOM 2212 CG ASN A 395 -243.232 -28.559 46.106 1.00 0.00

ATOM 2213 ODl ASN A 395 -243.240 -29.388 45.195 1.00 0.00

ATOM 2214 ND2 ASN A 395 -242.178 -28.363 46.891 1.00 0.00

ATOM 2215 N THR A 396 -246.806 -25.795 45.842 1.00 0.00

ATOM 2216 CA THR A 396 -248.034 -25.164 46.300 1.00 0.00

ATOM 2217 C THR A 396 -249.160 -25.456 45.349 1.00 0.00

ATOM 2218 O THR A 396 -250.228 -25.847 45.791 1.00 0.00

ATOM 2219 CB THR A 396 -247.880 -23.635 46.398 1.00 0.00

ATOM 2220 OGl THR A 396 -246.862 -23.314 47.355 1.00 0.00

ATOM 2221 CG2 THR A 396 -249.188 -22.995 46.839 1.00 0.00

ATOM 2222 N TYR A 397 -248.904 -25.270 44.038 1.00 0.00

ATOM 2223 CA TYR A 397 -249.941 -25.531 43.054 1.00 0.00

ATOM 2224 C TYR A 397 -250.459 -26.936 43.180 1.00 0.00

ATOM 2225 O TYR A 397 -251.661 -27.139 43.148 1.00 0.00

ATOM 2226 CB TYR A 397 -249.394 -25.348 41.637 1.00 0.00

ATOM 2227 CG TYR A 397 -249.056 -23.915 41.291 1.00 0.00

ATOM 2228 CDl TYR A 397 -249.527 -22.865 42.069 1.00 0.00

ATOM 2229 CD2 TYR A 397 -248.266 -23.618 40.188 1.00 0.00

ATOM 2230 CEl TYR A 397 -249.223 -21.553 41.760 1.00 0.00

ATOM 2231 CE2 TYR A 397 -247.951 -22.312 39.864 1.00 0.00

ATOM 9909 CZ TYR A 397 -248.437 -21.277 40.661 1.00 0.00

ATOM 2233 OH TYR A 397 -248.133 -19.971 40.352 1.00 0.00

ATOM 2234 N ARG A 398 -249.533 -27.902 43.335 1.00 0.00

ATOM 2235 CA ARG A 398 -249.951 -29.289 43.451 1.00 0.00

ATOM 2236 C ARG A 398 -250.893 -29.474 44.609 1.00 0.00

ATOM 2237 O ARG A 398 -251.934 -30.090 44.447 1.00 0.00

ATOM 2238 CB ARG A 398 -248.739 -30.197 43.674 1.00 0.00

ATOM 2239 CG ARG A 398 -247.843 -30.345 42.455 1.00 0.00

ATOM 2240 CD ARG A 398 -246.638 -31.220 42.759 1.00 0.00

ATOM 2241 NE ARG A 398 -245.740 -31.332 41.612 1.00 0.00

ATOM 2242 CZ ARG A 398 -244.587 -31.992 41.628 1.00 0.00

ATOM 2243 NHl ARG A 398 -243.835 -32.041 40.536 1.00 0.00

ATOM 2244 NH2 ARG A 398 -244.187 -32.603 42.735 1.00 0.00

ATOM 2245 N GLY A 399 -250.521 -28.924 45.782 1.00 0.00

ATOM 2246 CA GLY A 399 -251.381 -29.064 46.946 1.00 0.00

ATOM 2247 C GLY A 399 -252.741 -28.482 46.675 1.00 0.00

ATOM 2248 O GLY A 399 -253.738 -29.116 46.982 1.00 0.00

ATOM 2249 N LEU A 400 -252.763 -27.270 46.087 1.00 0.00

ATOM 2250 CA LEU A 400 -254.033 -26.625 45.808 1.00 0.00

ATOM 2251 C LEU A 400 -254.896 -27.489 44.934 1.00 0.00

ATOM 99 c 9 O LEU A 400 -256.062 -27.676 45.243 1.00 0.00

ATOM 2253 CB LEU A 400 -253.811 -25.293 45.089 1.00 0.00

ATOM 2254 CG LEU A 400 -253.193 -24.168 45.922 1.00 0.00

ATOM 2255 CDl LEU A 400 -252.851 -22.973 45.045 1.00 0.00

ATOM 2256 CD2 LEU A 400 -254.160 -23.704 47.001 1.00 0.00

ATOM 2257 N LEU A 401 -254.306 -28.020 43.844 1.00 0.00

ATOM 2258 CA LEU A 401 -255.085 -28.855 42.948 1.00 0.00

ATOM 2259 C LEU A 401 -255.626 -30.056 43.671 1.00 0.00

ATOM 2260 O LEU A 401 -256.762 -30.431 43.433 1.00 0.00 ATOM 2261 CB LEU A 401 -254.219 -29.346 41.786 1.00 0.00

ATOM 2262 CG LEU A 401 -254.916 -30.228 40.747 1.00 0.00

ATOM 2263 CDl LEU A 401 -256.051 -29.473 40.075 1.00 0.00

ATOM 2264 CD2 LEU A 401 -253.934 -30.668 39.671 1.00 0.00

ATOM 2265 N GLU A 402 -254.811 -30.645 44.570 1.00 0.00

ATOM 2266 CA GLU A 402 -255.289 -31.792 45.323 1.00 0.00

ATOM 2267 C GLU A 402 -256.475 -31.411 46.160 1.00 0.00

ATOM 2268 O GLU A 402 -257.491 -32.088 46.113 1.00 0.00

ATOM 2269 CB GLU A 402 -254.192 -32.320 46.249 1.00 0.00

ATOM 2270 CG GLU A 402 -254.590 -33.553 47.044 1.00 0.00

ATOM 2271 CD GLU A 402 -253.467 -34.065 47.924 1.00 0.00

ATOM 2272 OEl GLU A 402 -252.373 -33.465 47.902 1.00 0.00

ATOM 2273 OE2 GLU A 402 -253.682 -35.069 48.637 1.00 0.00

ATOM 2274 N SER A 403 -256.333 -30.313 46.929 1.00 0.00

ATOM 2275 CA SER A 403 -257.412 -29.912 47.815 1.00 0.00

ATOM 2276 C SER A 403 -258.665 -29.606 47.046 1.00 0.00

ATOM 2277 O SER A 403 -259.708 -30.154 47.368 1.00 0.00

ATOM 2278 CB SER A 403 -257.021 -28.658 48.600 1.00 0.00

ATOM 2279 OG SER A 403 -255.960 -28.930 49.499 1.00 0.00

ATOM 2280 N GLU A 404 -258.556 -28.727 46.031 1.00 0.00

ATOM 2281 CA GLU A 404 -259.745 -28.343 45.289 1.00 0.00

ATOM 99 Q o C GLU A 404 -260.320 -29.520 44.556 1.00 0.00

ATOM 2283 O GLU A 404 -261.463 -29.880 44.795 1.00 0.00

ATOM 2284 CB GLU A 404 -259.410 -27.258 44.265 1.00 0.00

ATOM 2285 CG GLU A 404 -258.924 -25.955 44.877 1.00 0.00

ATOM 2286 CD GLU A 404 -258.515 -24.936 43.831 1.00 0.00

ATOM 2287 OEl GLU A 404 -258.594 -25.257 42.627 1.00 0.00

ATOM 2288 OE2 GLU A 404 -258.118 -23.817 44.216 1.00 0.00

TER 2289 GLU A 404

ATOM 2290 N ALA B 116 183.610 37.279 -26.045 1.00 0.00

ATOM 2291 CA ALA B 116 182.494 38.031 -26.603 1.00 0.00

ATOM 2292 C ALA B 116 181.712 37.275 -27.641 1.00 0.00

ATOM 2293 O ALA B 116 180.499 37.411 -27.665 1.00 0.00

ATOM 2294 CB ALA B 116 182.993 39.303 -27.269 1.00 0.00

ATOM 2295 N GLN B 117 182.378 36.480 -28.503 1.00 0.00

ATOM 2296 CA GLN B 117 181.608 35.708 -29.467 1.00 0.00

ATOM 2297 C GLN B 117 180.769 34.708 -28.720 1.00 0.00

ATOM 2298 O GLN B 117 179.646 34.438 -29.115 1.00 0.00

ATOM 2299 CB GLN B 117 182.539 34.970 -30.430 1.00 0.00

ATOM 2300 CG GLN B 117 183.264 35.879 -31.410 1.00 0.00

ATOM 2301 CD GLN B 117 184.261 35.128 -32.271 1.00 0.00

ATOM 2302 OEl GLN B 117 184.484 33.933 -32.081 1.00 0.00

ATOM 2303 NE2 GLN B 117 184.864 35.830 -33.223 1.00 0.00

ATOM 2304 N CYS B 118 181.329 34.181 -27.613 1.00 0.00

ATOM 2305 CA CYS B 118 180.580 33.245 -26.791 1.00 0.00

ATOM 2306 C CYS B 118 179.342 33.894 -26.238 1.00 0.00

ATOM 2307 O CYS B 118 178.271 33.315 -26.332 1.00 0.00

ATOM 2308 CB CYS B 118 181.433 32.761 -25.617 1.00 0.00

ATOM 2309 SG CYS B 118 182.811 31.689 -26.087 1.00 0.00

ATOM 2310 N VAL B 119 179.497 35.105 -25.667 1.00 0.00

ATOM 2311 CA VAL B 119 178.343 35.802 -25.124 1.00 0.00

ATOM 2312 C VAL B 119 177.293 35.999 -26.180 1.00 0.00

ATOM 2313 O VAL B 119 176.123 35.792 -25.907 1.00 0.00

ATOM 2314 CB VAL B 119 178.727 37.191 -24.578 1.00 0.00

ATOM 2315 CGl VAL B 119 177.481 37.977 -24.200 1.00 0.00

ATOM 2316 CG2 VAL B 119 179.603 37.054 -23.343 1.00 0.00

ATOM 2317 N LYS B 120 177.728 36.389 -27.398 1.00 0.00

ATOM 2318 CA LYS B 120 176.776 36.590 -28.478 1.00 0.00

ATOM 2319 C LYS B 120 176.012 35.329 -28.775 1.00 0.00

ATOM 2320 O LYS B 120 174.820 35.406 -29.027 1.00 0.00

ATOM 2321 CB LYS B 120 177.499 37.018 -29.757 1.00 0.00

ATOM 2322 CG LYS B 120 178.047 38.435 -29.716 1.00 0.00

ATOM 2323 CD LYS B 120 178.631 38.840 -31.059 1.00 0.00

ATOM 2324 CE LYS B 120 179.957 38.143 -31.317 1.00 0.00

ATOM 2325 NZ LYS B 120 180.585 38.597 -32.589 1.00 0.00

ATOM 2326 N GLN B 121 176.691 34.163 -28.731 1.00 0.00

ATOM 2327 CA GLN B 121 175.984 32.913 -28.968 1.00 0.00

ATOM 2328 C GLN B 121 174.886 32.750 -27.953 1.00 0.00 ATOM 2329 O GLN B 121 173.798 32.315 -28.295 1.00 0.00

ATOM 2330 CB GLN B 121 176.941 31.726 -28.855 1.00 0.00

ATOM 2331 CG GLN B 121 177.944 31.626 -29.993 1.00 0.00

ATOM 2332 CD GLN B 121 178.947 30.507 -29.788 1.00 0.00

ATOM 2333 OEl GLN B 121 178.956 29.851 -28.747 1.00 0.00

ATOM 2334 NE2 GLN B 121 179.797 30.287 -30.785 1.00 0.00

ATOM 2335 N GLU B 122 175.197 33.123 -26.695 1.00 0.00

ATOM 2336 CA GLU B 122 174.224 32.985 -25.624 1.00 0.00

ATOM 2337 C GLU B 122 173.030 33.876 -25.823 1.00 0.00

ATOM 2338 O GLU B 122 171.913 33.421 -25.641 1.00 0.00

ATOM 2339 CB GLU B 122 174.853 33.350 -24.278 1.00 0.00

ATOM 2340 CG GLU B 122 175.884 32.348 -23.782 1.00 0.00

ATOM 2341 CD GLU B 122 176.573 32.803 -22.510 1.00 0.00

ATOM 2342 OEl GLU B 1 99 176.298 33.933 -22.057 1.00 0.00

ATOM 2343 OE2 GLU B -1 99 177.389 32.029 -21.969 1.00 0.00

ATOM 2344 N GLU B 123 173.264 35.152 -26.196 1.00 0.00

ATOM 2345 CA GLU B 123 172.145 36.068 -26.363 1.00 0.00

ATOM 2346 C GLU B 123 171.242 35.611 -27.473 1.00 0.00

ATOM 2347 O GLU B 123 170.033 35.717 -27.348 1.00 0.00

ATOM 2348 CB GLU B 123 172.648 37.472 -26.701 1.00 0.00

ATOM 2349 CG GLU B 123 173.334 38.181 -25.544 1.00 0.00

ATOM 2350 CD GLU B 123 173.926 39.517 -25.949 1.00 0.00

ATOM 2351 OEl GLU B 123 173.865 39.855 -27.150 1.00 0.00

ATOM 2352 OE2 GLU B 123 174.452 40.225 -25.064 1.00 0.00

ATOM 2353 N LYS B 124 171.848 35.089 -28.558 1.00 0.00

ATOM 2354 CA LYS B 124 171.042 34.583 -29.657 1.00 0.00

ATOM 2355 C LYS B 124 170.188 33.439 -29.188 1.00 0.00

ATOM 2356 O LYS B 124 169.056 33.309 -29.623 1.00 0.00

ATOM 2357 CB LYS B 124 171.938 34.090 -30.795 1.00 0.00

ATOM 2358 CG LYS B 124 172.660 35.199 -31.542 1.00 0.00

ATOM 2359 CD LYS B 124 173.528 34.640 -32.658 1.00 0.00

ATOM 2360 CE LYS B 124 174.269 35.748 -33.390 1.00 0.00

ATOM 2361 NZ LYS B 124 175.149 35.211 -34.463 1.00 0.00

ATOM 2362 N GLU B 125 170.752 32.613 -28.283 1.00 0.00

ATOM 2363 CA GLU B 125 170.004 31.475 -27.782 1.00 0.00

ATOM 2364 C GLU B 125 168.867 31.927 -26.908 1.00 0.00

ATOM 2365 O GLU B 125 167.750 31.475 -27.103 1.00 0.00

ATOM 2366 CB GLU B 125 170.910 30.560 -26.956 1.00 0.00

ATOM 2367 CG GLU B 125 171.946 29.809 -21.llξ> 1.00 0.00

ATOM 2368 CD GLU B 125 172.916 29.026 -26.913 1.00 0.00

ATOM 2369 OEl GLU B 125 172.819 29.124 -25.671 1.00 0.00

ATOM 2370 OE2 GLU B 125 173.771 28.312 -21.ill 1.00 0.00

ATOM 2371 N GLN B 126 169.156 32.826 -25.945 1.00 0.00

ATOM 2372 CA GLN B 126 168.099 33.292 -25.061 1.00 0.00

ATOM 2373 C GLN B 126 167.004 33.947 -25.854 1.00 0.00

ATOM 2374 O GLN B 126 165.836 33.727 -25.566 1.00 0.00

ATOM 2375 CB GLN B 126 168.647 34.310 -24.060 1.00 0.00

ATOM 2376 CG GLN B 126 169.564 33.711 -23.004 1.00 0.00

ATOM 2377 CD GLN B 126 170.177 34.762 -22.101 1.00 0.00

ATOM 2378 OEl GLN B 126 169.993 35.961 -22.312 1.00 0.00

ATOM 2379 NE2 GLN B 126 170.912 34.316 -21.088 1.00 0.00

ATOM 2380 N ILE B 127 167.399 34.744 -26.866 1.00 0.00

ATOM 2381 CA ILE B 127 166.411 35.407 -27.699 1.00 0.00

ATOM 2382 C ILE B 127 165.511 34.402 -28.362 1.00 0.00

ATOM 2383 O ILE B 127 164.303 34.576 -28.337 1.00 0.00

ATOM 2384 CB ILE B 127 167.078 36.243 -28.807 1.00 0.00

ATOM 2385 CGl ILE B 127 167.827 37.431 -28.202 1.00 0.00

ATOM 2386 CG2 ILE B 127 166.032 36.776 -29.774 1.00 0.00

ATOM 2387 CDl ILE B 127 168.730 38.149 -29.182 1.00 0.00

ATOM 2388 N LYS B 128 166.110 33.347 -28.951 1.00 0.00

ATOM 2389 CA LYS B 128 165.298 32.337 -29.610 1.00 0.00

ATOM 2390 C LYS B 128 164.295 31.749 -28.658 1.00 0.00

ATOM 2391 O LYS B 128 163.134 31.630 -29.015 1.00 0.00

ATOM 2392 CB LYS B 128 166.179 31.203 -30.139 1.00 0.00

ATOM 2393 CG LYS B 128 165.415 30.119 -30.881 1.00 0.00

ATOM 2394 CD LYS B 128 166.356 29.063 -31.438 1.00 0.00

ATOM 2395 CE LYS B 128 165.589 27.953 -32.138 1.00 0.00

ATOM 2396 NZ LYS B 128 166.497 26.899 -32.668 1.00 0.00 ATOM 2397 N SER B 129 164.749 31.397 -27.437 1.00 0.00

ATOM 2398 CA SER B 129 163.827 30.845 -26.456 1.00 0.00

ATOM 2399 C SER B 129 162.703 31.806 -26.181 1.00 0.00

ATOM 2400 O SER B 129 161.563 31.380 -26.086 1.00 0.00

ATOM 2401 CB SER B 129 164.552 30.565 -25.138 1.00 0.00

ATOM 2402 OG SER B 129 165.515 29.538 -25.295 1.00 0.00

ATOM 2403 N LEU B 130 163.031 33.110 -26.067 1.00 0.00

ATOM 2404 CA LEU B 130 161.994 34.095 -25.799 1.00 0.00

ATOM 2405 C LEU B 130 160.995 34.141 -26.922 1.00 0.00

ATOM 2406 O LEU B 130 159.804 34.109 -26.659 1.00 0.00

ATOM 2407 CB LEU B 130 162.606 35.488 -25.645 1.00 0.00

ATOM 2408 CG LEU B 130 163.440 35.727 -24.384 1.00 0.00

ATOM 2409 CDl LEU B 130 164.141 37.077 -24.451 1.00 0.00

ATOM 2410 CD2 LEU B 130 162.558 35.711 -23.145 1.00 0.00

ATOM 2411 N ASN B 131 161.488 34.210 -28.175 1.00 0.00

ATOM 2412 CA ASN B 131 160.581 34.285 -29.311 1.00 0.00

ATOM 2413 C ASN B 131 159.651 33.104 -29.351 1.00 0.00

ATOM 2414 O ASN B 131 158.472 33.284 -29.610 1.00 0.00

ATOM 2415 CB ASN B 131 161.368 34.310 -30.623 1.00 0.00

ATOM 2416 CG ASN B 131 162.065 35.634 -30.859 1.00 0.00

ATOM 2417 ODl ASN B 131 161.700 36.653 -30.271 1.00 0.00

ATOM 2418 ND2 ASN B 131 163.074 35.626 -31.724 1.00 0.00

ATOM 2419 N SER B 132 160.187 31.894 -29.088 1.00 0.00

ATOM 2420 CA SER B 132 159.340 30.713 -29.101 1.00 0.00

ATOM 2421 C SER B 132 158.282 30.835 -28.040 1.00 0.00

ATOM 2422 O SER B 132 157.121 30.573 -28.311 1.00 0.00

ATOM 2423 CB SER B 132 160.168 29.455 -28.830 1.00 0.00

ATOM 2424 OG SER B 132 161.075 29.204 -29.890 1.00 0.00

ATOM 2425 N ARG B 133 158.708 31.255 -26.831 1.00 0.00

ATOM 2426 CA ARG B 133 157.755 31.462 -25.753 1.00 0.00

ATOM 2427 C ARG B 133 156.658 32.384 -26.208 1.00 0.00

ATOM 2428 O ARG B 133 155.491 32.060 -26.053 1.00 0.00

ATOM 2429 CB ARG B 133 158.447 32.083 -24.538 1.00 0.00

ATOM 2430 CG ARG B 133 159.382 31.137 -23.804 1.00 0.00

ATOM 2431 CD ARG B 133 160.078 31.835 -22.647 1.00 0.00

ATOM 2432 NE ARG B 133 161.016 30.952 -21.959 1.00 0.00

ATOM 2433 CZ ARG B 133 161.839 31.344 -20.992 1.00 0.00

ATOM 2434 NHl ARG B 133 162.659 30.469 -20.423 1.00 0.00

ATOM 2435 NH2 ARG B 133 161.840 32.609 -20.594 1.00 0.00

ATOM 2436 N PHE B 134 157.060 33.535 -26.782 1.00 0.00

ATOM 2437 CA PHE B 134 156.090 34.514 -27.248 1.00 0.00

ATOM 2438 C PHE B 134 155.076 33.899 -28.175 1.00 0.00

ATOM 2439 O PHE B 134 153.894 34.144 -27.997 1.00 0.00

ATOM 2440 CB PHE B 134 156.790 35.644 -28.006 1.00 0.00

ATOM 2441 CG PHE B 134 157.443 36.660 -27.113 1.00 0.00

ATOM 2442 CDl PHE B 134 158.807 36.624 -26.882 1.00 0.00

ATOM 2443 CD2 PHE B 134 156.693 37.651 -26.504 1.00 0.00

ATOM 2444 CEl PHE B 134 159.408 37.559 -26.060 1.00 0.00

ATOM 2445 CE2 PHE B 134 157.294 38.585 -25.682 1.00 0.00

ATOM 2446 CZ PHE B 134 158.645 38.543 -25.459 1.00 0.00

ATOM 2447 N ALA B 135 155.541 33.100 -29.155 1.00 0.00

ATOM 2448 CA ALA B 135 154.601 32.474 -30.071 1.00 0.00

ATOM 2449 C ALA B 135 153.595 31.658 -29.306 1.00 0.00

ATOM 2450 O ALA B 135 152.404 31.807 -29.529 1.00 0.00

ATOM 2451 CB ALA B 135 155.333 31.558 -31.039 1.00 0.00

ATOM 2452 N ALA B 136 154.097 30.802 -28.394 1.00 0.00

ATOM 2453 CA ALA B 136 153.207 29.959 -27.613 1.00 0.00

ATOM 2454 C ALA B 136 152.187 30.768 -26.861 1.00 0.00

ATOM 2455 O ALA B 136 151.002 30.528 -27.029 1.00 0.00

ATOM 2456 CB ALA B 136 153.999 29.149 -26.598 1.00 0.00

ATOM 2457 N PHE B 137 152.652 31.728 -26.034 1.00 0.00

ATOM 2458 CA PHE B 137 151.721 32.520 -25.241 1.00 0.00

ATOM 2459 C PHE B 137 150.684 33.187 -26.101 1.00 0.00

ATOM 2460 O PHE B 137 149.538 33.273 -25.691 1.00 0.00

ATOM 2461 CB PHE B 137 152.467 33.615 -24.475 1.00 0.00

ATOM 2462 CG PHE B 137 153.174 33.120 -23.247 1.00 0.00

ATOM 2463 CDl PHE B 137 154.541 32.893 -23.260 1.00 0.00

ATOM 2464 CD2 PHE B 137 152.475 32.880 -22.077 1.00 0.00 ATOM 2465 CEl PHE B 137 155.192 32.438 -22.130 1.00 0.00

ATOM 2466 CE2 PHE B 137 153.127 32.425 -20.946 1.00 0.00

ATOM 2467 CZ PHE B 137 154.479 32.204 -20.969 1.00 0.00

ATOM 2468 N ILE B 138 151.085 33.659 -27.299 1.00 0.00

ATOM 2469 CA ILE B 138 150.129 34.341 -28.156 1.00 0.00

ATOM 2470 C ILE B 138 149.090 33.385 -28.676 1.00 0.00

ATOM 2471 O ILE B 138 147.925 33.741 -28.726 1.00 0.00

ATOM 2472 CB ILE B 138 150.819 34.985 -29.373 1.00 0.00

ATOM 2473 CGl ILE B 138 151.721 36.137 -28.925 1.00 0.00

ATOM 2474 CG2 ILE B 138 149.785 35.532 -30.344 1.00 0.00

ATOM 2475 CDl ILE B 138 152.636 36.654 -30.014 1.00 0.00

ATOM 2476 N ASP B 139 149.518 32.165 -29.055 1.00 0.00

ATOM 2477 CA ASP B 139 148.555 31.182 -29.520 1.00 0.00

ATOM 2478 C ASP B 139 147.598 30.846 -28.410 1.00 0.00

ATOM 2479 O ASP B 139 146.397 30.842 -28.630 1.00 0.00

ATOM 2480 CB ASP B 139 149.266 29.902 -29.963 1.00 0.00

ATOM 2481 CG ASP B 139 150.012 30.074 -31.272 1.00 0.00

ATOM 2482 ODl ASP B 139 149.789 31.097 -31.954 1.00 0.00

ATOM 2483 OD2 ASP B 139 150.821 29.186 -31.615 1.00 0.00

ATOM 2484 N LYS B 140 148.151 30.581 -27.209 1.00 0.00

ATOM 2485 CA LYS B 140 147.307 30.260 -26.066 1.00 0.00

ATOM 2486 C LYS B 140 146.310 31.357 -25.809 1.00 0.00

ATOM 2487 O LYS B 140 145.150 31.065 -25.567 1.00 0.00

ATOM 2488 CB LYS B 140 148.157 30.081 -24.807 1.00 0.00

ATOM 2489 CG LYS B 140 149.013 28.826 -24.808 1.00 0.00

ATOM 2490 CD LYS B 140 149.827 28.710 -23.529 1.00 0.00

ATOM 2491 CE LYS B 140 150.702 27.467 -23.542 1.00 0.00

ATOM 2492 NZ LYS B 140 151.530 27.359 -22.309 1.00 0.00

ATOM 2493 N VAL B 141 146.773 32.621 -25.870 1.00 0.00

ATOM 2494 CA VAL B 141 145.874 33.733 -25.610 1.00 0.00

ATOM 2495 C VAL B 141 144.793 33.816 -26.651 1.00 0.00

ATOM 2496 O VAL B 141 143.666 34.141 -26.312 1.00 0.00

ATOM 2497 CB VAL B 141 146.624 35.078 -25.614 1.00 0.00

ATOM 2498 CGl VAL B 141 145.641 36.237 -25.539 1.00 0.00

ATOM 2499 CG2 VAL B 141 147.564 35.167 -24.422 1.00 0.00

ATOM 2500 N ARG B 142 145.137 33.515 -27.920 1.00 0.00

ATOM 2501 CA ARG B 142 144.125 33.545 -28.963 1.00 0.00

ATOM 2502 C ARG B 142 143.037 32.566 -28.624 1.00 0.00

ATOM 2503 O ARG B 142 141.869 32.919 -28.676 1.00 0.00

ATOM 2504 CB ARG B 142 144.736 33.165 -30.313 1.00 0.00

ATOM 2505 CG ARG B 142 145.670 34.218 -30.889 1.00 0.00

ATOM 2506 CD ARG B 142 146.276 33.758 -32.205 1.00 0.00

ATOM 2507 NE ARG B 142 147.213 34.738 -32.748 1.00 0.00

ATOM 2508 CZ ARG B 142 147.922 34.559 -33.858 1.00 0.00

ATOM 2509 NHl ARG B 142 148.750 35.506 -34.276 1.00 0.00

ATOM 2510 NH2 ARG B 142 147.800 33.433 -34.547 1.00 0.00

ATOM 2511 N PHE B 143 143.438 31.332 -28.257 1.00 0.00

ATOM 2512 CA PHE B 143 142.454 30.330 -27.887 1.00 0.00

ATOM 2513 C PHE B 143 141.608 30.794 -26.733 1.00 0.00

ATOM 2514 O PHE B 143 140.393 30.727 -26.827 1.00 0.00

ATOM 2515 CB PHE B 143 143.144 29.028 -27.473 1.00 0.00

ATOM 2516 CG PHE B 143 142.193 27.951 -27.036 1.00 0.00

ATOM 2517 CDl PHE B 143 141.506 27.194 -27.969 1.00 0.00

ATOM 2518 CD2 PHE B 143 141.985 27.696 -25.692 1.00 0.00

ATOM 2519 CEl PHE B 143 140.631 26.202 -27.566 1.00 0.00

ATOM 2520 CE2 PHE B 143 141.110 26.705 -25.289 1.00 0.00

ATOM 2521 CZ PHE B 143 140.434 25.959 -26.219 1.00 0.00

ATOM 2522 N LEU B 144 142.256 31.267 -25.648 1.00 0.00

ATOM 2523 CA LEU B 144 141.500 31.696 -24.481 1.00 0.00

ATOM 2524 C LEU B 144 140.501 32.760 -24.839 1.00 0.00

ATOM 2525 O LEU B 144 139.410 32.755 -24.295 1.00 0.00

ATOM 2526 CB LEU B 144 142.437 32.267 -23.415 1.00 0.00

ATOM 2527 CG LEU B 144 143.358 31.265 -22.716 1.00 0.00

ATOM 2528 CDl LEU B 144 144.355 31.985 -21.820 1.00 0.00

ATOM 2529 CD2 LEU B 144 142.554 30.303 -21.856 1.00 0.00

ATOM 2530 N GLU B 145 140.871 33.669 -25.763 1.00 0.00

ATOM 2531 CA GLU B 145 139.939 34.718 -26.142 1.00 0.00

ATOM 2532 C GLU B 145 138.795 34.158 -26.938 1.00 0.00 ATOM 2533 O GLU B 145 137.687 34.657 -26.825 1.00 0.00

ATOM 2534 CB GLU B 145 140.642 35.776 -26.995 1.00 0.00

ATOM 2535 CG GLU B 145 141.643 36.627 -26.230 1.00 0.00

ATOM 2536 CD GLU B 145 142.385 37.601 -27.124 1.00 0.00

ATOM 2537 OEl GLU B 145 142.161 37.567 -28.352 1.00 0.00

ATOM 2538 OE2 GLU B 145 143.189 38.397 -26.597 1.00 0.00

ATOM 2539 N GLN B 146 139.064 33.107 -27.738 1.00 0.00

ATOM 2540 CA GLN B 146 137.983 32.481 -28.478 1.00 0.00

ATOM 2541 C GLN B 146 137.019 31.850 -27.512 1.00 0.00

ATOM 2542 O GLN B 146 135.823 32.060 -27.633 1.00 0.00

ATOM 2543 CB GLN B 146 138.531 31.402 -29.415 1.00 0.00

ATOM 2544 CG GLN B 146 139.334 31.944 -30.585 1.00 0.00

ATOM 2545 CD GLN B 146 139.984 30.846 -31.405 1.00 0.00

ATOM 2546 OEl GLN B 146 139.925 29.670 -31.043 1.00 0.00

ATOM 2547 NE2 GLN B 146 140.606 31.227 -32.514 1.00 0.00

ATOM 2548 N GLN B 147 137.557 31.082 -26.542 1.00 0.00

ATOM 2549 CA GLN B 147 136.698 30.438 -25.561 1.00 0.00

ATOM 2550 C GLN B 147 135.920 31.452 -24.770 1.00 0.00

ATOM 2551 O GLN B 147 134.761 31.212 -24.466 1.00 0.00

ATOM 2552 CB GLN B 147 137.531 29.609 -24.581 1.00 0.00

ATOM 2553 CG GLN B 147 136.705 28.806 -23.589 1.00 0.00

ATOM 2554 CD GLN B 147 135.847 27.753 -24.263 1.00 0.00

ATOM 2555 OEl GLN B 147 136.316 27.020 -25.133 1.00 0.00

ATOM 2556 NE2 GLN B 147 134.584 27.675 -23.860 1.00 0.00

ATOM 2557 N ASN B 148 136.563 32.591 -24.441 1.00 0.00

ATOM 2558 CA ASN B 148 135.865 33.620 -23.683 1.00 0.00

ATOM 2559 C ASN B 148 134.714 34.155 -24.484 1.00 0.00

ATOM 2560 O ASN B 148 133.617 34.256 -23.961 1.00 0.00

ATOM 2561 CB ASN B 148 136.812 34.775 -23.352 1.00 0.00

ATOM 2562 CG ASN B 148 136.150 35.848 -22.508 1.00 0.00

ATOM 2563 ODl ASN B 148 135.311 36.605 -22.996 1.00 0.00

ATOM 2564 ND2 ASN B 148 136.525 35.913 -21.236 1.00 0.00

ATOM 2565 N LYS B 149 134.979 34.489 -25.763 1.00 0.00

ATOM 2566 CA LYS B 149 133.913 34.995 -26.611 1.00 0.00

ATOM 2567 C LYS B 149 132.746 34.047 -26.621 1.00 0.00

ATOM 2568 O LYS B 149 131.614 34.490 -26.520 1.00 0.00

ATOM 2569 CB LYS B 149 134.407 35.164 -28.049 1.00 0.00

ATOM 2570 CG LYS B 149 133.361 35.721 -29.002 1.00 0.00

ATOM 2571 CD LYS B 149 133.939 35.934 -30.392 1.00 0.00

ATOM 2572 CE LYS B 149 132.886 36.459 -31.353 1.00 0.00

ATOM 2573 NZ LYS B 149 133.440 36.679 -32.718 1.00 0.00

ATOM 2574 N LEU B 150 133.034 32.734 -26.723 1.00 0.00

ATOM 2575 CA LEU B 150 131.958 31.756 -26.724 1.00 0.00

ATOM 2576 C LEU B 150 131.185 31.797 -25.436 1.00 0.00

ATOM 2577 O LEU B 150 129.964 31.828 -25.476 1.00 0.00

ATOM 2578 CB LEU B 150 132.518 30.343 -26.896 1.00 0.00

ATOM 2579 CG LEU B 150 131.496 29.204 -26.900 1.00 0.00

ATOM 2580 CDl LEU B 150 130.525 29.358 -28.059 1.00 0.00

ATOM 2581 CD2 LEU B 150 132.190 27.859 -27.035 1.00 0.00

ATOM 2582 N LEU B 151 131.901 31.800 -24.295 1.00 0.00

ATOM 2583 CA LEU B 151 131.212 31.809 -23.014 1.00 0.00

ATOM 2584 C LEU B 151 130.310 33.006 -22.897 1.00 0.00

ATOM 2585 O LEU B 151 129.202 32.870 -22.403 1.00 0.00

ATOM 2586 CB LEU B 151 132.219 31.856 -21.864 1.00 0.00

ATOM 2587 CG LEU B 151 133.059 30.596 -21.646 1.00 0.00

ATOM 2588 CDl LEU B 151 134.135 30.842 -20.600 1.00 0.00

ATOM 2589 CD2 LEU B 151 132.187 29.445 -21.170 1.00 0.00

ATOM 2590 N GLU B 152 130.791 34.175 -23.364 1.00 0.00

ATOM 2591 CA GLU B 152 129.976 35.376 -23.277 1.00 0.00

ATOM 2592 C GLU B 152 128.696 35.209 -24.048 1.00 0.00

ATOM 2593 O GLU B 152 127.639 35.508 -23.513 1.00 0.00

ATOM 2594 CB GLU B 152 130.729 36.577 -23.851 1.00 0.00

ATOM 2595 CG GLU B 152 129.968 37.890 -23.758 1.00 0.00

ATOM 2596 CD GLU B 152 130.758 39.062 -24.306 1.00 0.00

ATOM 2597 OEl GLU B 152 131.908 38.850 -24.746 1.00 0.00

ATOM 2598 OE2 GLU B 152 130.228 40.193 -24.295 1.00 0.00

ATOM 2599 N THR B 153 128.789 34.717 -25.300 1.00 0.00

ATOM 2600 CA THR B 153 127.579 34.497 -26.077 1.00 0.00 ATOM 2601 C THR B 153 126.634 33.603 -25.322 1.00 0.00

ATOM 2602 O THR B 153 125.475 33.956 -25.171 1.00 0.00

ATOM 2603 CB THR B 153 127.891 33.831 -27.430 1.00 0.00

ATOM 2604 OGl THR B 153 128.737 34.689 -28.205 1.00 0.00

ATOM 2605 CG2 THR B 153 126.607 33.574 -28.205 1.00 0.00

ATOM 2606 N LYS B 154 127.144 32.453 -24.835 1.00 0.00

ATOM 2607 CA LYS B 154 126.291 31.527 -24.103 1.00 0.00

ATOM 2608 C LYS B 154 125.638 32.177 -22.913 1.00 0.00

ATOM 2609 O LYS B 154 124.455 31.968 -22.694 1.00 0.00

ATOM 2610 CB LYS B 154 127.106 30.339 -23.591 1.00 0.00

ATOM 2611 CG LYS B 154 127.575 29.391 -24.683 1.00 0.00

ATOM 2612 CD LYS B 154 128.374 28.234 -24.105 1.00 0.00

ATOM 2613 CE LYS B 154 128.864 27.300 -25.199 1.00 0.00

ATOM 2614 NZ LYS B 154 129.678 26.180 -24.649 1.00 0.00

ATOM 2615 N TRP B 155 126.416 32.965 -22.146 1.00 0.00

ATOM 2616 CA TRP B 155 125.873 33.581 -20.945 1.00 0.00

ATOM 2617 C TRP B 155 124.795 34.577 -21.274 1.00 0.00

ATOM 2618 O TRP B 155 123.844 34.694 -20.519 1.00 0.00

ATOM 2619 CB TRP B 155 126.973 34.316 -20.176 1.00 0.00

ATOM 2620 CG TRP B 155 126.478 35.026 -18.953 1.00 0.00

ATOM 2621 CDl TRP B 155 126.271 34.484 -17.718 1.00 0.00

ATOM 2622 CD2 TRP B 155 126.127 36.412 -18.848 1.00 0.00

ATOM 2623 NEl TRP B 155 125.814 35.444 -16.849 1.00 0.00

ATOM 2624 CE2 TRP B 155 125.716 36.638 -17.520 1.00 0.00

ATOM 2625 CE3 TRP B 155 126.119 37.483 -19.746 1.00 0.00

ATOM 2626 CZ2 TRP B 155 125.303 37.890 -17.068 1.00 0.00

ATOM 2627 CZ3 TRP B 155 125.709 38.723 -19.295 1.00 0.00

ATOM 2628 CH2 TRP B 155 125.306 38.919 -17.969 1.00 0.00

ATOM 2629 N GLN B 156 124.940 35.289 -22.410 1.00 0.00

ATOM 2630 CA GLN B 156 123.909 36.242 -22.783 1.00 0.00

ATOM 2631 C GLN B 156 122.630 35.512 -23.074 1.00 0.00

ATOM 2632 O GLN B 156 121.596 35.876 -22.539 1.00 0.00

ATOM 2633 CB GLN B 156 124.328 37.024 -24.029 1.00 0.00

ATOM 2634 CG GLN B 156 125.458 38.012 -23.791 1.00 0.00

ATOM 2635 CD GLN B 156 125.936 38.671 -25.071 1.00 0.00

ATOM 2636 OEl GLN B 156 125.476 38.334 -26.162 1.00 0.00

ATOM 2637 NE2 GLN B 156 126.862 39.614 -24.940 1.00 0.00

ATOM 2638 N PHE B 157 122.720 34.472 -23.929 1.00 0.00

ATOM 2639 CA PHE B 157 121.523 33.735 -24.295 1.00 0.00

ATOM 2640 C PHE B 157 120.857 33.169 -23.077 1.00 0.00

ATOM 2641 O PHE B 157 119.693 33.458 -22.847 1.00 0.00

ATOM 2642 CB PHE B 157 121.873 32.578 -25.234 1.00 0.00

ATOM 2643 CG PHE B 157 120.696 31.719 -25.602 1.00 0.00

ATOM 2644 CDl PHE B 157 119.781 32.143 -26.549 1.00 0.00

ATOM 2645 CD2 PHE B 157 120.505 30.488 -25.000 1.00 0.00

ATOM 2646 CEl PHE B 157 118.700 31.353 -26.888 1.00 0.00

ATOM 2647 CE2 PHE B 157 119.423 29.697 -25.339 1.00 0.00

ATOM 2648 CZ PHE B 157 118.522 30.126 -26.279 1.00 0.00

ATOM 2649 N TYR B 158 121.610 32.370 -22.293 1.00 0.00

ATOM 2650 CA TYR B 158 121.045 31.822 -21.072 1.00 0.00

ATOM 2651 C TYR B 158 120.486 32.931 -20.226 1.00 0.00

ATOM 2652 O TYR B 158 119.286 32.985 -20.005 1.00 0.00

ATOM 2653 CB TYR B 158 122.119 31.084 -20.270 1.00 0.00

ATOM 2654 CG TYR B 158 122.653 29.846 -20.954 1.00 0.00

ATOM 2655 CDl TYR B 158 123.841 29.889 -21.675 1.00 0.00

ATOM 2656 CD2 TYR B 158 121.970 28.640 -20.878 1.00 0.00

ATOM 2657 CEl TYR B 158 124.337 28.763 -22.303 1.00 0.00

ATOM 2658 CE2 TYR B 158 122.451 27.504 -21.501 1.00 0.00

ATOM 2659 CZ TYR B 158 123.645 27.575 -22.217 1.00 0.00

ATOM 2660 OH TYR B 158 124.138 26.452 -22.842 1.00 0.00

TER 2661 TYR B 158

ATOM 2662 N GLU B 169 104.875 26.869 -20.649 1.00 0.00

ATOM 2663 CA GLU B 169 104.067 28.084 -20.667 1.00 0.00

ATOM 2664 C GLU B 169 102.867 27.955 -21.612 1.00 0.00

ATOM 2665 O GLU B 169 101.745 27.739 -21.158 1.00 0.00

ATOM 2666 CB GLU B 169 104.903 29.276 -21.136 1.00 0.00

ATOM 2667 CG GLU B 169 104.158 30.601 -21.125 1.00 0.00

ATOM 2668 CD GLU B 169 105.027 31.764 -21.560 1.00 0.00 ATOM 2669 OEl GLU B 169 106.216 31.533 -21.869 1.00 0.00

ATOM 2670 OE2 GLU B 169 104.522 32.905 -21.592 1.00 0.00

ATOM 2671 N PRO B 170 103.098 28.087 -22.923 1.00 0.00

ATOM 2672 CA PRO B 170 102.009 27.990 -23.901 1.00 0.00

ATOM 2673 C PRO B 170 101.072 26.853 -23.501 1.00 0.00

ATOM 2674 O PRO B 170 99.873 26.860 -23.812 1.00 0.00

ATOM 2675 CB PRO B 170 102.725 27.712 -25.225 1.00 0.00

ATOM 2676 CG PRO B 170 104.051 28.377 -25.079 1.00 0.00

ATOM 2677 CD PRO B 170 104.476 28.156 -23.654 1.00 0.00

ATOM 2678 N LEU B 171 101.645 25.887 -22.787 1.00 0.00

ATOM 2679 CA LEU B 171 100.891 24.749 -22.299 1.00 0.00

ATOM 2680 C LEU B 171 99.874 25.215 -21.284 1.00 0.00

ATOM 2681 O LEU B 171 98.671 25.175 -21.532 1.00 0.00

ATOM 2682 CB LEU B 171 101.824 23.732 -21.637 1.00 0.00

ATOM 2683 CG LEU B 171 101.167 22.460 -21.099 1.00 0.00

ATOM 2684 CDl LEU B 171 100.567 21.643 -22.232 1.00 0.00

ATOM 2685 CD2 LEU B 171 102.187 21.594 -20.374 1.00 0.00

ATOM 2686 N PHE B 172 100.344 25.677 -20.132 1.00 0.00

ATOM 2687 CA PHE B 172 99.413 26.143 -19.128 1.00 0.00

ATOM 2688 C PHE B 172 98.432 27.182 -19.649 1.00 0.00

ATOM 2689 O PHE B 172 97.335 27.313 -19.115 1.00 0.00

ATOM 2690 CB PHE B 172 100.162 26.786 -17.960 1.00 0.00

ATOM 2691 CG PHE B 172 100.839 25.796 -17.055 1.00 0.00

ATOM 2692 CDl PHE B 172 102.208 25.602 -17.118 1.00 0.00

ATOM 2693 CD2 PHE B 172 100.106 25.058 -16.142 1.00 0.00

ATOM 2694 CEl PHE B 172 102.830 24.691 -16.285 1.00 0.00

ATOM 2695 CE2 PHE B 172 100.728 24.146 -15.309 1.00 0.00

ATOM 2696 CZ PHE B 172 102.084 23.962 -15.378 1.00 0.00

ATOM 2697 N SER B 173 98.799 27.925 -20.689 1.00 0.00

ATOM 2698 CA SER B 173 97.858 28.905 -21.220 1.00 0.00

ATOM 2699 C SER B 173 96.753 28.133 -21.909 1.00 0.00

ATOM 2700 O SER B 173 95.613 28.578 -21.965 1.00 0.00

ATOM 2701 CB SER B 173 98.556 29.830 -22.219 1.00 0.00

ATOM 2702 OG SER B 173 99.546 30.618 -21.579 1.00 0.00

ATOM 2703 N GLY B 174 97.097 26.974 -22.450 1.00 0.00

ATOM 2704 CA GLY B 174 96.088 26.171 -23.111 1.00 0.00

ATOM 2705 C GLY B 174 95.109 25.651 -22.061 1.00 0.00

ATOM 2706 O GLY B 174 93.893 25.738 -22.224 1.00 0.00

ATOM 2707 N TYR B 175 95.660 25.095 -20.986 1.00 0.00

ATOM 2708 CA TYR B 175 94.862 24.576 -19.882 1.00 0.00

ATOM 2709 C TYR B 175 93.904 25.666 -19.362 1.00 0.00

ATOM 2710 O TYR B 175 92.677 25.494 -19.379 1.00 0.00

ATOM 2711 CB TYR B 175 95.765 24.131 -18.730 1.00 0.00

ATOM 2712 CG TYR B 175 95.012 23.640 -17.515 1.00 0.00

ATOM 2713 CDl TYR B 175 94.479 22.357 -17.478 1.00 0.00

ATOM 2714 CD2 TYR B 175 94.834 24.460 -16.409 1.00 0.00

ATOM 2715 CEl TYR B 175 93.789 21.900 -16.371 1.00 0.00

ATOM 2716 CE2 TYR B 175 94.147 24.020 -15.293 1.00 0.00

ATOM 2717 CZ TYR B 175 93.623 22.728 -15.283 1.00 0.00

ATOM 2718 OH TYR B 175 92.937 22.274 -14.180 1.00 0.00

ATOM 2719 N ILE B 176 94.409 26.733 -19.261 1.00 0.00

ATOM 2720 CA ILE B 176 93.718 27.946 -18.831 1.00 0.00

ATOM 2721 C ILE B 176 92.484 28.233 -19.695 1.00 0.00

ATOM 2722 O ILE B 176 91.360 27.966 -19.273 1.00 0.00

ATOM 2723 CB ILE B 176 94.635 29.180 -18.921 1.00 0.00

ATOM 2724 CGl ILE B 176 95.795 29.055 -17.932 1.00 0.00

ATOM 2725 CG2 ILE B 176 93.858 30.446 -18.594 1.00 0.00

ATOM 2726 CDl ILE B 176 96.881 30.088 -18.131 1.00 0.00

ATOM 2727 N GLU B 177 92.689 28.776 -20.900 1.00 0.00

ATOM 2728 CA GLU B 177 91.569 29.097 -21.791 1.00 0.00

ATOM 2729 C GLU B 177 90.541 27.968 -21.734 1.00 0.00

ATOM 2730 O GLU B 177 89.340 28.172 -21.955 1.00 0.00

ATOM 2731 CB GLU B 177 92.058 29.256 -23.231 1.00 0.00

ATOM 2732 CG GLU B 177 90.980 29.698 -24.208 1.00 0.00

ATOM 2733 CD GLU B 177 91.520 29.928 -25.606 1.00 0.00

ATOM 2734 OEl GLU B 177 92.735 29.723 -25.816 1.00 0.00

ATOM 2735 OE2 GLU B 177 90.729 30.314 -26.492 1.00 0.00

ATOM 2736 N THR B 178 91.040 26.777 -21.413 1.00 0.00 ATOM 2737 CA THR B 178 90.200 25.605 -21.286 1.00 0.00

ATOM 2738 C THR B 178 89.261 25.783 -20.115 1.00 0.00

ATOM 2739 O THR B 178 88.053 25.924 -20.292 1.00 0.00

ATOM 2740 CB THR B 178 91.036 24.333 -21.051 1.00 0.00

ATOM 2741 OGl THR B 178 91.877 24.094 -22.187 1.00 0.00

ATOM 2742 CG2 THR B 178 90.129 23.129 -20.847 1.00 0.00

ATOM 2743 N LEU B 179 89.804 25.797 -18.906 1.00 0.00

ATOM 2744 CA LEU B 179 88.948 25.972 -17.752 1.00 0.00

ATOM 2745 C LEU B 179 88.055 27.199 -17.844 1.00 0.00

ATOM 2746 O LEU B 179 86.990 27.231 -17.233 1.00 0.00

ATOM 2747 CB LEU B 179 89.787 26.125 -16.482 1.00 0.00

ATOM 2748 CG LEU B 179 90.556 24.885 -16.022 1.00 0.00

ATOM 2749 CDl LEU B 179 91.452 25.216 -14.839 1.00 0.00

ATOM 2750 CD2 LEU B 179 89.597 23.784 -15.599 1.00 0.00

ATOM 2751 N ARG B 180 88.458 28.216 -18.599 1.00 0.00

ATOM 2752 CA ARG B 180 87.599 29.386 -18.723 1.00 0.00

ATOM 2753 C ARG B 180 86.408 28.978 -19.561 1.00 0.00

ATOM 2754 O ARG B 180 85.312 29.503 -19.402 1.00 0.00

ATOM 2755 CB ARG B 180 88.351 30.534 -19.400 1.00 0.00

ATOM 2756 CG ARG B 180 89.437 31.158 -18.539 1.00 0.00

ATOM 2757 CD ARG B 180 90.196 32.232 -19.299 1.00 0.00

ATOM 2758 NE ARG B 180 91.250 32.836 -18.488 1.00 0.00

ATOM 2759 CZ ARG B 180 92.143 33.704 -18.951 1.00 0.00

ATOM 2760 NHl ARG B 180 93.067 34.202 -18.138 1.00 0.00

ATOM 2761 NH2 ARG B 180 92.112 34.074 -20.223 1.00 0.00

ATOM 2762 N ARG B 181 86.626 28.042 -20.475 1.00 0.00

ATOM 2763 CA ARG B 181 85.528 27.587 -21.303 1.00 0.00

ATOM 2764 C ARG B 181 84.536 26.826 -20.428 1.00 0.00

ATOM 2765 O ARG B 181 83.329 27.056 -20.483 1.00 0.00

ATOM 2766 CB ARG B 181 86.040 26.663 -22.410 1.00 0.00

ATOM 2767 CG ARG B 181 86.842 27.371 -23.489 1.00 0.00

ATOM 2768 CD ARG B 181 87.359 26.390 -24.528 1.00 0.00

ATOM 2769 NE ARG B 181 88.153 27.053 -25.560 1.00 0.00

ATOM 2770 CZ ARG B 181 88.739 26.421 -26.573 1.00 0.00

ATOM 2771 NHl ARG B 181 89.441 27.106 -27.463 1.00 0.00

ATOM 2772 NH2 ARG B 181 88.620 25.106 -26.690 1.00 0.00

ATOM 2773 N GLU B 182 85.064 25.901 -19.630 1.00 0.00

ATOM 2774 CA GLU B 182 84.252 25.108 -18.715 1.00 0.00

ATOM 2775 C GLU B 182 83.414 26.032 -17.810 1.00 0.00

ATOM 2776 O GLU B 182 82.177 25.973 -17.811 1.00 0.00

ATOM 2777 CB GLU B 182 85.141 24.233 -17.830 1.00 0.00

ATOM 2778 CG GLU B 182 84.374 23.337 -16.871 1.00 0.00

ATOM 2779 CD GLU B 182 85.287 22.463 -16.033 1.00 0.00

ATOM 2780 OEl GLU B 182 86.520 22.545 -16.217 1.00 0.00

ATOM 2781 OE2 GLU B 182 84.769 21.697 -15.194 1.00 0.00

ATOM 2782 N ALA B 183 84.092 26.895 -17.050 1.00 0.00

ATOM 2783 CA ALA B 183 83.398 27.840 -16.165 1.00 0.00

ATOM 2784 C ALA B 183 82.316 28.570 -16.961 1.00 0.00

ATOM 2785 O ALA B 183 81.218 28.811 -16.470 1.00 0.00

ATOM 2786 CB ALA B 183 84.380 28.859 -15.605 1.00 0.00

ATOM 2787 N GLU B 184 82.634 28.911 -18.197 1.00 0.00

ATOM 2788 CA GLU B 184 81.693 29.609 -19.051 1.00 0.00

ATOM 2789 C GLU B 184 80.357 28.886 -19.234 1.00 0.00

ATOM 2790 O GLU B 184 79.283 29.359 -18.826 1.00 0.00

ATOM 2791 CB GLU B 184 82.281 29.798 -20.451 1.00 0.00

ATOM 2792 CG GLU B 184 81.377 30.564 -21.404 1.00 0.00

ATOM 2793 CD GLU B 184 81.996 30.744 -22.776 1.00 0.00

ATOM 2794 OEl GLU B 184 83.137 30.276 -22.979 1.00 0.00

ATOM 2795 OE2 GLU B 184 81.342 31.354 -23.648 1.00 0.00

ATOM 2796 N CYS B 185 80.424 27.729 -19.868 1.00 0.00

ATOM 2797 CA CYS B 185 79.210 26.993 -20.117 1.00 0.00

ATOM 2798 C CYS B 185 78.475 26.753 -18.801 1.00 0.00

ATOM 2799 O CYS B 185 77.252 26.795 -18.768 1.00 0.00

ATOM 2800 CB CYS B 185 79.526 25.641 -20.761 1.00 0.00

ATOM 2801 SG CYS B 185 80.150 25.747 -22.453 1.00 0.00

ATOM 2802 N VAL B 186 79.207 26.529 -17.711 1.00 0.00

ATOM 2803 CA VAL B 186 78.556 26.297 -16.425 1.00 0.00

ATOM 2804 C VAL B 186 77.819 27.499 -15.807 1.00 0.00 ATOM 2805 O VAL B 186 76.811 27.320 15.124 .00 0.00

ATOM 2806 CB VAL B 186 79.570 25.864 15.349 .00 0.00

ATOM 2807 CGl VAL B 186 78.904 25.805 13.984 .00 0.00

ATOM 2808 CG2 VAL B 186 80.131 24.487 15.671 .00 0.00

ATOM 2809 N GLU B 187 78.295 28.722 16.007 .00 0.00

ATOM 2810 CA GLU B 187 77.520 29.824 15.452 .00 0.00

ATOM 2811 C GLU B 187 76.242 29.891 16.284 .00 0.00

ATOM 2812 O GLU B 187 75.175 30.222 15.775 .00 0.00

ATOM 2813 CB GLU B 187 78.305 31.134 15.553 .00 0.00

ATOM 2814 CG GLU B 187 79.506 31.212 14.625 .00 0.00

ATOM 2815 CD GLU B 187 80.311 32.482 14.817 .00 0.00

ATOM 2816 OEl GLU B 187 79.964 33.273 15.720 .00 0.00

ATOM 2817 OE2 GLU B 187 81.287 32.685 14.067 .00 0.00

ATOM 2818 N ALA B 188 76.345 29.551 17.567 .00 0.00

ATOM 2819 CA ALA B 188 75.193 29.541 18.472 .00 0.00

ATOM 2820 C ALA B 188 74.131 28.541 17.942 .00 0.00

ATOM 2821 O ALA B 188 72.945 28.871 17.770 .00 0.00

ATOM 2822 CB ALA B 188 75.620 29. 117 19.869 .00 0.00

ATOM 2823 N ASP B 189 74.578 27.323 17.663 .00 0.00

ATOM 2824 CA ASP B 189 73.711 26.276 17.129 .00 0.00

ATOM 2825 C ASP B 189 73.022 26.766 -15.873 .00 0.00

ATOM 2826 O ASP B 189 71.819 .591 15.706 1..00 0.00

ATOM 2827 CB ASP B 189 74.527 .029 16.785 1..00 0.00

ATOM 2828 CG ASP B 189 74.988 .275 18.018 1..00 0.00

ATOM 2829 ODl ASP B 189 74.492 .583 19.122 1.00 0.00

ATOM 2830 OD2 ASP B 189 75.847 23.379 17. 1.00 0.00

ATOM 2831 N SER B 190 73.802 27.366 -14.979 1.00 0.00

ATOM 2832 CA SER B 190 73.237 27.876 -13.747 1.00 0.00

ATOM 2833 C SER B 190 72.146 28.924 -14.013 1.00 0.00

ATOM 2834 O SER B 190 71.148 28.956 -13.300 1.00 0.00

ATOM 2835 CB SER B 190 74.322 28.538 -12.895 1..00 0.00

ATOM 2836 OG SER B 190 73.780 29.057 -11.693 1..00 0.00

ATOM 2837 N GLY B 191 72.315 29.769 -15.032 1.00 0.00

ATOM 2838 CA GLY B 191 71.292 30.774 -15.341 1.00 0.00

ATOM 2839 C GLY B 191 70.002 30.059 -15.686 1.00 0.00

ATOM 2840 O GLY B 191 68.899 30.459 -15.297 1.00 0.00

ATOM 2841 N ARG B 192 70.171 28.973 -16.422 1.00 0.00

ATOM 2842 CA ARG B 192 69.059 28.163 -16.844 1.00 0.00

ATOM 2843 C ARG B 192 68.322 27.485 -15.716 1..00 0.00

ATOM 2844 O ARG B 192 67.098 27.506 -15.696 1..00 0.00

ATOM 2845 CB ARG B 192 69.532 27.051 -17.782 1.00 0.00

ATOM 2846 CG ARG B 192 69.970 27.540 -19.153 1.00 0.00

ATOM 2847 CD ARG B 192 70.472 26 ..339922 -20.014 1.00 0.00

ATOM 2848 NE ARG B 192 70.922 26 ..885500 -21 .327 1.00 0.00

ATOM 2849 CZ ARG B 192 71.426 26 .052 -22.263 1.00 0.00

ATOM 2850 NHl ARG B 192 71.809 26 .557 -23.427 1.00 0.00

ATOM 2851 NH2 ARG B 192 71.546 24 .752 -22.032 1..00 0.00

ATOM 2852 N LEU B 193 69.046 26 .886 -14.779 1..00 0.00

ATOM 2853 CA LEU B 193 68.400 26 .222222 -13.653 1..00 0.00

ATOM 2854 C LEU B 193 67.628 27 221 .834 1.00 0.00

ATOM 2855 O LEU B 193 66.552 26, 925 .320 1.00 0.00

ATOM 2856 CB LEU B 193 69.444 >5.556 -12.754 1.00 0.00

ATOM 2857 CG LEU B 193 70.164 14.339 -13.336 1.00 0.00

ATOM 2858 CDl LEU B 193 71. >92 23.892 -12.420 1.00 0.00

ATOM 2859 CD2 LEU B 193 69. ^?00 23.175 -13.508 1.00 0.00

ATOM 2860 N ALA B 194 68.197 28.403 -12.689 1..00 0.00

ATOM 2861 CA ALA B 194 67.542 29.443 -11.920 1..00 0.00

ATOM 2862 C ALA B 194 66.237 29.831 -12.558 1.00 0.00

ATOM 2863 O ALA B 194 65.256 30.162 -11.903 1.00 0.00

ATOM 2864 CB ALA B 194 68.424 30.680 -11.841 1.00 0.00

ATOM 2865 N SER B 195 66.267 29. .834 -13.869 1.00 0.00

ATOM 2866 CA SER B 195 65.117 30. >09 -14.636 1.00 0.00

ATOM 2867 C SER B 195 64.050 29.111 -14.537 1.00 0.00

ATOM 2868 O SER B 195 62.868 29.397 -14.249 00 0.00

ATOM 2869 CB SER B 195 65.493 30.402 -16.106 00 0.00

ATOM 2870 OG SER B 195 66.361 31.509 -16.270 00 0.00

ATOM 2871 N GLU B 196 64.453 27.861 -14.751 00 0.00

ATOM 2872 CA GLU B 196 63.470 26.782 -14.669 1.00 0.00 ATOM 2873 C GLU B 196 62.847 26.749 -13.297 1.00 0.00

ATOM 2874 O GLU B 196 61.651 26.556 -13.165 1.00 0.00

ATOM 2875 CB GLU B 196 64.134 25.430 -14.935 1.00 0.00

ATOM 2876 CG GLU B 196 64.561 25.221 -16.379 1.00 0.00

ATOM 2877 CD GLU B 196 65.325 23.927 -16.580 1.00 0.00

ATOM 2878 OEl GLU B 196 65.584 23.229 -15.578 1.00 0.00

ATOM 2879 OE2 GLU B 196 65.664 23.611 -17.741 1.00 0.00

ATOM 2880 N LEU B 197 63.677 26.949 -12.282 1.00 0.00

ATOM 2881 CA LEU B 197 63.230 26.948 -10.901 1.00 0.00

ATOM 2882 C LEU B 197 62.170 28.035 -10.698 1.00 0.00

ATOM 2883 O LEU B 197 61.095 27.779 -10.145 1.00 0.00

ATOM 2884 CB LEU B 197 64.403 27.222 -9.958 1.00 0.00

ATOM 2885 CG LEU B 197 64.075 27.267 -8.464 1.00 0.00

ATOM 2886 CDl LEU B 197 63.529 25.927 -7.992 1.00 0.00

ATOM 2887 CD2 LEU B 197 65.319 27.587 -7.650 1.00 0.00

ATOM 2888 N ASN B 198 62.465 29.241 -11.153 1.00 0.00

ATOM 2889 CA ASN B 198 61.516 30.316 -11.010 1.00 0.00

ATOM 2890 C ASN B 198 60.183 29.935 -11.640 1.00 0.00

ATOM 2891 O ASN B 198 59.132 30.103 -11.023 1.00 0.00

ATOM 2892 CB ASN B 198 62.032 31.582 -11.697 1.00 0.00

ATOM 2893 CG ASN B 198 63.167 32.237 -10.934 1.00 0.00

ATOM 2894 ODl ASN B 198 63.353 31.986 -9.743 1.00 0.00

ATOM 2895 ND2 ASN B 198 63.931 33.079 -11.620 1.00 0.00

ATOM 2896 N HIS B 199 60.221 29.375 -12.847 1.00 0.00

ATOM 2897 CA HIS B 199 58.974 28.985 -13.499 1.00 0.00

ATOM 2898 C HIS B 199 58.219 27.960 -12.658 1.00 0.00

ATOM 2899 O HIS B 199 56.996 27.999 -12.551 1.00 0.00

ATOM 2900 CB HIS B 199 59.257 28.366 -14.868 1.00 0.00

ATOM 2901 CG HIS B 199 58.025 27.940 -15.605 1.00 0.00

ATOM 2902 NDl HIS B 199 57.144 28.839 -16.165 1.00 0.00

ATOM 2903 CD2 HIS B 199 57.407 26.666 -15.945 1.00 0.00

ATOM 2904 CEl HIS B 199 56.142 28.162 -16.754 1.00 0.00

ATOM 2905 NE2 HIS B 199 56.294 26.858 -16.626 1.00 0.00

ATOM 2906 N VAL B 200 58.955 27.031 -12.067 1.00 0.00

ATOM 2907 CA VAL B 200 58.323 26.017 -11.261 1.00 0.00

ATOM 2908 C VAL B 200 57.674 26.636 -10.057 1.00 0.00

ATOM 2909 O VAL B 200 56.521 26.347 -9.746 1.00 0.00

ATOM 2910 CB VAL B 200 59.341 24.972 -10.768 1.00 0.00

ATOM 2911 CGl VAL B 200 58.694 24.032 -9.762 1.00 0.00

ATOM 2912 CG2 VAL B 200 59.863 24.146 -11.932 1.00 0.00

ATOM 2913 N GLN B 201 58.409 27.484 -9.364 1.00 0.00

ATOM 2914 CA GLN B 201 57.841 28.114 -8.191 1.00 0.00

ATOM 2915 C GLN B 201 56.565 28.894 -8.493 1.00 0.00

ATOM 2916 O GLN B 201 55.617 28.852 -7.717 1.00 0.00

ATOM 2917 CB GLN B 201 58.837 29.099 -7.576 1.00 0.00

ATOM 2918 CG GLN B 201 60.032 28.438 -6.909 1.00 0.00

ATOM 2919 CD GLN B 201 61.053 29.444 -6.413 1.00 0.00

ATOM 2920 OEl GLN B 201 60.916 30.646 -6.642 1.00 0.00

ATOM 2921 NE2 GLN B 201 62.080 28.954 -5.728 1.00 0.00

ATOM 2922 N GLU B 202 56.527 29.589 -9.632 1.00 0.00

ATOM 2923 CA GLU B 202 55.349 30.372 -10.013 1.00 0.00

ATOM 2924 C GLU B 202 54.190 29.408 -10.239 1.00 0.00

ATOM 2925 O GLU B 202 53.069 29.613 -9.776 1.00 0.00

ATOM 2926 CB GLU B 202 55.620 31.159 -11.296 1.00 0.00

ATOM 2927 CG GLU B 202 54.463 32.039 -11.742 1.00 0.00

ATOM 2928 CD GLU B 202 54.781 32.829 -12.996 1.00 0.00

ATOM 2929 OEl GLU B 202 55.911 32.697 -13.510 1.00 0.00

ATOM 2930 OE2 GLU B 202 53.899 33.578 -13.466 1.00 0.00

ATOM 2931 N VAL B 203 54.492 28.359 -10.976 1.00 0.00

ATOM 2932 CA VAL B 203 53.537 27.315 -11.247 1.00 0.00

ATOM 2933 C VAL B 203 52.938 26.860 -9.919 1.00 0.00

ATOM 2934 O VAL B 203 51.719 26.870 -9.732 1.00 0.00

ATOM 2935 CB VAL B 203 54.200 26.110 -11.940 1.00 0.00

ATOM 2936 CGl VAL B 203 53.226 24.946 -12.031 1.00 0.00

ATOM 2937 CG2 VAL B 203 54.639 26.481 -13.348 1.00 0.00

ATOM 2938 N LEU B 204 53.815 26.453 -9.007 1.00 0.00

ATOM 2939 CA LEU B 204 53.415 25.991 -7.677 1.00 0.00

ATOM 2940 C LEU B 204 52.459 26.969 -7.008 1.00 0.00 ATOM 2941 O LEU B 204 51.424 26.561 -6.494 .00 0.00

ATOM 2942 CB LEU B 204 54.640 25.841 -6.772 .00 0.00

ATOM 2943 CG LEU B 204 55.580 24.676 -7.092 .00 0.00

ATOM 2944 CDl LEU B 204 56.842 24.755 -6.246 .00 0.00

ATOM 2945 CD2 LEU B 204 54.901 23.345 -6.812 .00 0.00

ATOM 2946 N GLU B 205 52.793 28.257 -7.007 .00 0.00

ATOM 2947 CA GLU B 205 51.908 29.233 -6.382 .00 0.00

ATOM 2948 C GLU B 205 50.522 29.155 -7.029 .00 0.00

ATOM 2949 O GLU B 205 49.499 29.036 -6.342 .00 0.00

ATOM 2950 CB GLU B 205 52.460 30.648 -6.560 .00 0.00

ATOM 2951 CG GLU B 205 51.622 31.729 -5.898 .00 0.00

ATOM 2952 CD GLU B 205 52.217 33.114 -6.066 .00 0.00

ATOM 2953 OEl GLU B 205 53.295 33.225 -6.690 .00 0.00

ATOM 2954 OE2 GLU B 205 51.609 34.087 -5.574 .00 0.00

ATOM 2955 N GLY B 206 50.487 29.225 -8.354 .00 0.00

ATOM 2956 CA GLY B 206 49 99 R 29.147 -9.079 .00 0.00

ATOM 2957 C GLY B 206 48.4 1 27.906 -8.702 .00 0.00

ATOM 2958 O GLY B 206 47.289 28.041 -8.235 .00 0.00

ATOM 2959 N TYR B 207 48.995 26.716 .00 0.00

ATOM 2960 CA TYR B 207 48.287 25.482 -8.548 .00 0.00

ATOM 2961 C TYR B 207 47.795 25.473 -7.125 .00 0.00

ATOM 2962 O TYR B 207 46.715 .961 -6.863 1..00 0.00

ATOM 2963 CB TYR B 207 49.208 .271 -8.720 1..00 0.00

ATOM 2964 CG TYR B 207 49.577 .982 -10.157 1..00 0.00

ATOM 2965 CDl TYR B 207 48.882 .575 -11.203 1.00 0.00

ATOM 2966 CD2 TYR B 207 50.620 23.116 -10.463 1.00 0.00

ATOM 2967 CEl TYR B 207 49.212 24.316 -12.520 1.00 0.00

ATOM 2968 CE2 TYR B 207 50.963 22.845 -11.774 1.00 0.00

ATOM 2969 CZ TYR B 207 50.249 23.454 -12.805 1.00 0.00

ATOM 2970 OH TYR B 207 50.580 23.194 -14.115 1.00 0.00

ATOM 2971 N LYS B 208 48.554 26.031 -6.201 1..00 0.00

ATOM 2972 CA LYS B 208 48.093 26.041 -4.821 1..00 0.00

ATOM 2973 C LYS B 208 46.905 26.971 -4.601 1.00 0.00

ATOM 2974 O LYS B 208 45.984 26.645 -3.856 1.00 0.00

ATOM 2975 CB LYS B 208 49.210 26.506 -3. 1.00 0.00

ATOM 2976 CG LYS B 208 50.347 25.509 -3.733 1.00 0.00

ATOM 2977 CD LYS B 208 51.418 26.032 -2.789 1.00 0.00

ATOM 2978 CE LYS B 208 52.570 25.050 -2.662 1.00 0.00

ATOM 2979 NZ LYS B 208 53.638 25.559 -1 759 1..00 0.00

ATOM 2980 N LYS B 209 46.921 28.113 -5 270 1..00 0.00

ATOM 2981 CA LYS B 209 45.820 29.054 -5.175 1.00 0.00

ATOM 2982 C LYS B 209 44.574 28.375 -5.746 1.00 0.00

ATOM 2983 O LYS B 209 43.514 28.370 -5.112 1.00 0.00

ATOM 2984 CB LYS B 209 46.129 30.324 -5.971 1.00 0.00

ATOM 2985 CG LYS B 209 45.044 31.384 -5.893 1.00 0.00

ATOM 2986 CD LYS B 209 45.447 32.642 -6.646 1.00 0.00

ATOM 2987 CE LYS B 209 44.341 33.685 -6.609 1..00 0.00

ATOM 2988 NZ LYS B 209 44.713 34.914 -7.363 1..00 0.00

ATOM 2989 N LYS B 210 44.731 27.802 -6.938 1..00 0.00

ATOM 2990 CA LYS B 210 43.654 27.118 -7.649 1.00 0.00

ATOM 2991 C LYS B 210 43.072 26.027 -6.770 1.00 0.00

ATOM 2992 O LYS B 210 41.860 25.907 -6.646 1.00 0.00

ATOM 2993 CB LYS B 210 44.181 26.485 -8.938 1.00 0.00

ATOM 2994 CG LYS B 210 44.563 27.491 -10.012 1.00 0.00

ATOM 2995 CD LYS B 210 45.079 26.795 -11.262 1.00 0.00

ATOM 2996 CE LYS B 210 45.484 27.800 -12.327 1..00 0.00

ATOM 2997 NZ LYS B 210 46.026 27.134 -13.542 1..00 0.00

ATOM 2998 N TYR B 211 43.946 25.239 -6.146 1.00 0.00

ATOM 2999 CA TYR B 211 43.487 24.181 -5.260 1.00 0.00

ATOM 3000 C TYR B 211 42.747 24.713 -4.041 1.00 0.00

ATOM 3001 O TYR B 211 41.800 24.087 -3.572 1.00 0.00

ATOM 3002 CB TYR B 211 44.671 23.360 -4.747 1.00 0.00

ATOM 3003 CG TYR B 211 44.281 22.252 -3.794 1.00 0.00

ATOM 3004 CDl TYR B 211 43.744 21.062 -4.268 1..00 0.00

ATOM 3005 CD2 TYR B 211 44.453 22.401 -2.424 1,.00 0.00

ATOM 3006 CEl TYR B 211 43.386 20.045 -3.403 1.00 0.00

ATOM 3007 CE2 TYR B 211 44.101 21.395 -1.545 1.00 0.00

ATOM 3008 CZ TYR B 211 43.563 20.210 -2.047 1.00 0.00 ATOM 3009 OH TYR B 211 43.207 19.199 -1.183 1.00 0.00

ATOM 3010 N GLU B 212 43.180 25.855 -3.513 1.00 0.00

ATOM 3011 CA GLU B 212 42.518 26.439 -2.353 1.00 0.00

ATOM 3012 C GLU B 212 41.090 26.753 -2.775 1.00 0.00

ATOM 3013 O GLU B 212 40.130 26.387 -2.094 1.00 0.00

ATOM 3014 CB GLU B 212 43.235 27.717 -1.914 1.00 0.00

ATOM 3015 CG GLU B 212 42.638 28.371 -0.679 1.00 0.00

ATOM 3016 CD GLU B 212 43.395 29.614 -0.254 1.00 0.00

ATOM 3017 OEl GLU B 212 44.395 29.957 -0.919 1.00 0.00

ATOM 3018 OE2 GLU B 212 42.988 30.246 0.744 1.00 0.00

ATOM 3019 N GLU B 213 40.952 27.427 -3.908 1.00 0.00

ATOM 3020 CA GLU B 213 39.627 27.763 -4.418 1.00 0.00

ATOM 3021 C GLU B 213 38.786 26.510 -4.563 1.00 0.00

ATOM 3022 O GLU B 213 37.672 26.450 -4.055 1.00 0.00

ATOM 3023 CB GLU B 213 39.735 28.437 -5.787 1.00 0.00

ATOM 3024 CG GLU B 213 38.400 28.865 -6.374 1.00 0.00

ATOM 3025 CD GLU B 213 38.549 29.559 -7.715 1.00 0.00

ATOM 3026 OEl GLU B 213 39.698 29.718 -8.177 1.00 0.00

ATOM 3027 OE2 GLU B 213 37.517 29.944 -8.301 1.00 0.00

ATOM 3028 N GLU B 214 39.310 25.509 -5.271 1.00 0.00

ATOM 3029 CA GLU B 214 38.530 24.296 -5.502 1.00 0.00

ATOM 3030 C GLU B 214 38.099 23.647 -4.215 1.00 0.00

ATOM 3031 O GLU B 214 37.032 23.047 -4.156 1.00 0.00

ATOM 3032 CB GLU B 214 39.354 23.271 -6.283 1.00 0.00

ATOM 3033 CG GLU B 214 38.587 22.013 -6.658 1.00 0.00

ATOM 3034 CD GLU B 214 39.402 21.065 -7.514 1.00 0.00

ATOM 3035 OEl GLU B 214 40.563 21.402 -7.832 1.00 0.00

ATOM 3036 OE2 GLU B 214 38.883 19.985 -7.866 1.00 0.00

ATOM 3037 N VAL B 215 38.918 23.740 -3.188 1.00 0.00

ATOM 3038 CA VAL B 215 38.536 23.131 -1.933 1.00 0.00

ATOM 3039 C VAL B 215 37.462 23.944 -1.261 1.00 0.00

ATOM 3040 O VAL B 215 36.639 23.403 -0.535 1.00 0.00

ATOM 3041 CB VAL B 215 39.732 23.032 -0.967 1.00 0.00

ATOM 3042 CGl VAL B 215 39.271 22.559 0.404 1.00 0.00

ATOM 3043 CG2 VAL B 215 40.763 22.046 -1.495 1.00 0.00

ATOM 3044 N ALA B 216 37.470 25.249 -1.495 1.00 0.00

ATOM 3045 CA ALA B 216 36.465 26.117 -0.906 1.00 0.00

ATOM 3046 C ALA B 216 35.140 25.760 -1.564 1.00 0.00

ATOM 3047 O ALA B 216 34.128 25.543 -0.886 1.00 0.00

ATOM 3048 CB ALA B 216 36.809 27.576 -1.163 1.00 0.00

ATOM 3049 N LEU B 217 35.158 25.683 -2.891 1.00 0.00

ATOM 3050 CA LEU B 217 33.951 25.359 -3.649 1.00 0.00

ATOM 3051 C LEU B 217 33.417 23.986 -3.283 1.00 0.00

ATOM 3052 O LEU B 217 32.211 23.805 -3.215 1.00 0.00

ATOM 3053 CB LEU B 217 34.243 25.364 -5.151 1.00 0.00

ATOM 3054 CG LEU B 217 34.531 26.729 -5.780 1.00 0.00

ATOM 3055 CDl LEU B 217 34.980 26.572 -7.224 1.00 0.00

ATOM 3056 CD2 LEU B 217 33.285 27.602 -5.762 1.00 0.00

ATOM 3057 N ARG B 218 34.318 23.034 -3.049 1.00 0.00

ATOM 3058 CA ARG B 218 33.951 21.665 -2.688 1.00 0.00

ATOM 3059 C ARG B 218 33.269 21.718 -1.311 1.00 0.00

ATOM 3060 O ARG B 218 32.178 21.185 -1.133 1.00 0.00

ATOM 3061 CB ARG B 218 35.195 20.777 -2.620 1.00 0.00

ATOM 3062 CG ARG B 218 34.902 19.322 -2.290 1.00 0.00

ATOM 3063 CD ARG B 218 36.184 18.515 -2.170 1.00 0.00

ATOM 3064 NE ARG B 218 37.002 18.950 -1.040 1.00 0.00

ATOM 3065 CZ ARG B 218 36.762 18.623 0.227 1.00 0.00

ATOM 3066 NHl ARG B 218 37.559 19.066 1.189 1.00 0.00

ATOM 3067 NH2 ARG B 218 35.724 17.854 0.526 1.00 0.00

ATOM 3068 N ALA B 219 33.900 22.378 -0.348 1.00 0.00

ATOM 3069 CA ALA B 219 33.314 22.523 0.986 1.00 0.00

ATOM 3070 C ALA B 219 31.862 23.058 0.861 1.00 0.00

ATOM 3071 O ALA B 219 30.939 22.548 1.497 1.00 0.00

ATOM 3072 CB ALA B 219 34.130 23.498 1.821 1.00 0.00

ATOM 3073 N THR B 220 31.668 24.081 0.029 1.00 0.00

ATOM 3074 CA THR B 220 30.341 24.666 -0.178 1.00 0.00

ATOM 3075 C THR B 220 29.372 23.643 -0.746 1.00 0.00

ATOM 3076 O THR B 220 28.259 23.487 -0.242 1.00 0.00 ATOM 3077 CB THR B 220 30.392 25.850 1.161 00 0.00

ATOM 3078 OGl THR B 220 31.227 26.884 0.624 00 0.00

ATOM 3079 CG2 THR B 220 28.998 26.412 -1 392 00 0.00

ATOM 3080 N ALA B 221 29.789 22.952 -1.800 00 0.00

ATOM 3081 CA ALA B 221 28.915 949 -2.391 00 0.00

ATOM 3082 C ALA B 221 28.501 20.897 -1.386 00 0.00

ATOM 3083 O ALA B 221 27.343 20.486 -1.378 00 0.00

ATOM 3084 CB ALA B 221 29.620 21.242 -3.539 00 0.00

ATOM 3085 N GLU B 222 29.431 20.465 -0.539 00 0.00

ATOM 3086 CA GLU B 999 29.106 19.455 0.453 00 0.00

ATOM 3087 C GLU B 999 28.059 19.986 1.423 00 0.00

ATOM 3088 O GLU B 222 27.061 19.323 1.687 00 0.00

ATOM 3089 CB GLU B 222 30.353 19.065 1.250 1.00 0.00

ATOM 3090 CG GLU B 999 30.114 17.977 2.284 ,00 0.00

ATOM 3091 CD GLU B 999 31.378 17.593 3.028 ,00 0.00

ATOM 3092 OEl GLU B 222 32.444 18.170 2.726 1.00 0.00

ATOM 3093 OE2 GLU B 222 31.302 16.716 3.914 1.00 0.00

ATOM 3094 N ASN B 223 28.249 21.194 1.935 1.00 0.00

ATOM 3095 CA ASN B 223 27.241 21.731 2.832 1.00 0.00

ATOM 3096 C ASN B 223 25.888 21.718 2.111 1.00 0.00

ATOM 3097 O ASN B 223 24.907 21.195 2.634 1.00 0.00

ATOM 3098 CB ASN B 223 27.590 23.166 3.232 1..00 0.00

ATOM 3099 CG ASN B 223 28.753 >34 4.202 1..00 0.00

ATOM 3100 ODl ASN B 223 29.086 >47 4.857 1..00 0.00

ATOM 3101 ND2 ASN B 223 29.377 24.402 4.295 1.00 0.00

ATOM 3102 N GLU B 224 25.835 22. 264 0.903 1.00 0.00

ATOM 3103 CA GLU B 224 24.576 22.304 0.157 1.00 0.00

ATOM 3104 C GLU B 224 23.935 20.929 -0.033 1.00 0.00

ATOM 3105 O GLU B 224 22.722 20.779 0.121 1.00 0.00

ATOM 3106 CB GLU B 224 24.799 22.885 241 1.00 0.00

ATOM 3107 CG GLU B 224 25.102 24.375 252 1..00 0.00

ATOM 3108 CD GLU B 224 25.438 24.890 638 1..00 0.00

ATOM 3109 OEl GLU B 224 25.508 24.069 576 1.00 0.00

ATOM 3110 OE2 GLU B 224 25.632 26.115 2.785 1.00 0.00

ATOM 3111 N PHE B 225 24.750 19.937 0.383 1.00 0.00

ATOM 3112 CA PHE B 225 24.257 18.577 0.595 1.00 0.00

ATOM 3113 C PHE B 225 23.706 17.970 0.675 1.00 0.00

ATOM 3114 O PHE B 225 22.771 17.181 0.635 1.00 0.00

ATOM 3115 CB PHE B 225 25.385 17.669 1.092 1.00 0.00

ATOM 3116 CG PHE B 225 24.932 16.285 1.459 1.00 0.00

ATOM 3117 CDl PHE B 225 24.220 16.060 2.625 1.00 0.00

ATOM 3118 CD2 PHE B 225 25.217 15.207 0.639 1.00 0.00

ATOM 3119 CEl PHE B 225 23.804 14.787 -2 962 1..00 0.00

ATOM 3120 CE2 PHE B 99c 24.801 13.934 -0.977 1..00 0.00

ATOM 3121 CZ PHE B 225 24.097 13.720 -2.132 1.00 0.00

ATOM 3122 N VAL B 226 24.295 18.317 1.808 1.00 0.00

ATOM 3123 CA VAL B 226 23.815 17.755 3.054 1.00 0.00

ATOM 3124 C VAL B 226 22 424 18.307 3.315 1.00 0.00

ATOM 3125 O VAL B 226 21.476 17.567 3.574 1.00 0.00

ATOM 3126 CB VAL B 226 24.735 18.126 4.232 1.00 0.00

ATOM 3127 CGl VAL B 226 24.117 17.687 5.550 1.00 0.00

ATOM 3128 CG2 VAL B 226 26.088 17.447 4.086 1.00 0.00

ATOM 3129 N VAL B 227 22.308 19.624 3.225 1.00 0.00

ATOM 3130 CA VAL B 227 21.050 20.303 3.440 1.00 0.00

ATOM 3131 C VAL B 227 19.971 19.717 2.541 1.00 0.00

ATOM 3132 O VAL B 227 18.967 19.162 3.007 1..00 0.00

ATOM 3133 CB VAL B 227 21.161 21.807 3.132 1..00 0.00

ATOM 3134 CGl VAL B 227 19.788 2,' .461 3.167 1..00 0.00

ATOM 3135 CG2 VAL B 227 22.048 22.497 4.157 1..00 0.00

ATOM 3136 N LEU B 228 20.186 19.855 1.242 1..00 0.00

ATOM 3137 CA LEU B 228 19.220 19.361 0.289 1..00 0.00

ATOM 3138 C LEU B 228 18.861 17.925 0.640 1.00 0.00

ATOM 3139 O LEU B 228 17.683 17.588 0.672 1.00 0.00

ATOM 3140 CB LEU B 228 19.797 19.401 -1.128 .00 0.00

ATOM 3141 CG LEU B 228 19.971 20.788 -1.750 ,00 0.00

ATOM 3142 CDl LEU B 228 20.722 20.694 -3.069 ,00 0.00

ATOM 3143 CD2 LEU B 228 18.619 21.431 -2.016 ,00 0.00

ATOM 3144 N LYS B 229 19.845 17.084 0.943 1.00 0.00 ATOM 3145 CA LYS B 229 19.531 15.701 1.297 1.00 0.00

ATOM 3146 C LYS B 229 18.556 15.616 2.468 1.00 0.00

ATOM 3147 O LYS B 229 17.597 14.835 2.424 1.00 0.00

ATOM 3148 CB LYS B 229 20.802 14.949 1.696 1.00 0.00

ATOM 3149 CG LYS B 229 20.575 13.486 2.041 1.00 0.00

ATOM 3150 CD LYS B 229 21.885 12.784 2.359 1.00 0.00

ATOM 3151 CE LYS B 229 21.652 11.333 2.753 1.00 0.00

ATOM 3152 NZ LYS B 229 22.926 10.639 3.090 1.00 0.00

ATOM 3153 N LYS B 230 18.800 16.408 3.518 1.00 0.00

ATOM 3154 CA LYS B 230 17.900 16.411 4.677 1.00 0.00

ATOM 3155 C LYS B 230 16.513 16.691 4.134 1.00 0.00

ATOM 3156 O LYS B 230 15.604 15.891 4.286 1.00 0.00

ATOM 3157 CB LYS B 230 18.317 17.492 5.676 1.00 0.00

ATOM 3158 CG LYS B 230 17.466 17.534 6.935 1.00 0.00

ATOM 3159 CD LYS B 230 17.964 18.595 7.904 1.00 0.00

ATOM 3160 CE LYS B 230 17.094 18.660 9.148 1.00 0.00

ATOM 3161 NZ LYS B 230 17.585 19.678 10.116 1.00 0.00

ATOM 3162 N ASP B 231 16.373 17.835 3.484 1.00 0.00

ATOM 3163 CA ASP B 231 15.112 18.253 2.904 1.00 0.00

ATOM 3164 C ASP B 231 14.419 17.173 2.079 1.00 0.00

ATOM 3165 O ASP B 231 13.219 16.933 2.232 1.00 0.00

ATOM 3166 CB ASP B 231 15.321 19.447 1.970 1.00 0.00

ATOM 3167 CG ASP B 231 15.612 20.730 2.723 1.00 0.00

ATOM 3168 ODl ASP B 231 15.429 20.750 3.957 1.00 0.00

ATOM 3169 OD2 ASP B 231 16.026 21.717 2.077 1.00 0.00

ATOM 3170 N VAL B 232 15.169 16.530 1.200 1.00 0.00

ATOM 3171 CA VAL B 232 14.578 15.497 0.379 1.00 0.00

ATOM 3172 C VAL B 232 13.952 14.463 1.292 1.00 0.00

ATOM 3173 O VAL B 232 12.844 14.002 1.050 1.00 0.00

ATOM 3174 CB VAL B 232 15.631 14.811 -0.510 1.00 0.00

ATOM 3175 CGl VAL B 232 15.030 13.602 -1.212 1.00 0.00

ATOM 3176 CG2 VAL B 232 16.146 15.774 -1.568 1.00 0.00

ATOM 3177 N ASP B 233 14.668 14.111 2.355 1.00 0.00

ATOM 3178 CA ASP B 233 14.174 13.106 3.285 1.00 0.00

ATOM 3179 C ASP B 233 12.891 13.535 3.994 1.00 0.00

ATOM 3180 O ASP B 233 11.893 12.807 4.022 1.00 0.00

ATOM 3181 CB ASP B 233 15.216 12.820 4.369 1.00 0.00

ATOM 3182 CG ASP B 233 16.400 12.031 3.845 1.00 0.00

ATOM 3183 ODl ASP B 233 16.309 11.503 2.717 1.00 0.00

ATOM 3184 OD2 ASP B 233 17.418 11.942 4.561 1.00 0.00

ATOM 3185 N CYS B 234 12.916 14.717 4.574 1.00 0.00

ATOM 3186 CA CYS B 234 11.731 15.219 5.244 1.00 0.00

ATOM 3187 C CYS B 234 10.516 15.292 4.326 1.00 0.00

ATOM 3188 O CYS B 234 9.435 14.846 4.684 1.00 0.00

ATOM 3189 CB CYS B 234 11.977 16.630 5.782 1.00 0.00

ATOM 3190 SG CYS B 234 13.142 16.711 7.162 1.00 0.00

ATOM 3191 N ALA B 235 10.685 15.863 3.136 1.00 0.00

ATOM 3192 CA ALA B 235 9.568 15.960 2.207 1.00 0.00

ATOM 3193 C ALA B 235 9.115 14.558 1.798 1.00 0.00

ATOM 3194 O ALA B 235 7.943 14.339 1.511 1.00 0.00

ATOM 3195 CB ALA B 235 9.979 16.728 0.961 1.00 0.00

ATOM 3196 N TYR B 236 10.030 13.598 1.764 1.00 0.00

ATOM 3197 CA TYR B 236 9.613 12.256 1.394 1.00 0.00

ATOM 3198 C TYR B 236 8.738 11.691 2.529 1.00 0.00

ATOM 3199 O TYR B 236 7.692 11.094 2.270 1.00 0.00

ATOM 3200 CB TYR B 236 10.831 11.354 1.189 1.00 0.00

ATOM 3201 CG TYR B 236 10.484 9.934 0.801 1.00 0.00

ATOM 3202 CDl TYR B 236 10.100 9.625 -0.498 1.00 0.00

ATOM 3203 CD2 TYR B 236 10.541 8.907 1.735 1.00 0.00

ATOM 3204 CEl TYR B 236 9.781 8.331 -0.862 1.00 0.00

ATOM 3205 CE2 TYR B 236 10.225 7.607 1.389 1.00 0.00

ATOM 3206 CZ TYR B 236 9.843 7.325 0.078 1.00 0.00

ATOM 3207 OH TYR B 236 9.526 6.035 -0.282 1.00 0.00

ATOM 3208 N LEU B 237 9.137 11.885 3.783 1.00 0.00

ATOM 3209 CA LEU B 237 8.286 11.393 4.870 1.00 0.00

ATOM 3210 C LEU B 237 6.894 12.038 4.753 1.00 0.00

ATOM 3211 O LEU B 237 5.878 11.344 4.745 1.00 0.00

ATOM 3212 CB LEU B 237 8.892 11.751 6.229 1.00 0.00 ATOM 3213 CG LEU B 237 8.099 11.312 7.461 1.00 0.00

ATOM 3214 CDl LEU B 237 7.970 9.797 7.505 1.00 0.00

ATOM 3215 CD2 LEU B 237 8.793 11.768 8.737 1.00 0.00

ATOM 3216 N ARG B 238 6.847 13.363 4.656 1.00 0.00

ATOM 3217 CA ARG B 238 5.583 14.080 4.533 1.00 0.00

ATOM 3218 C ARG B 238 4.717 13.502 3.426 1.00 0.00

ATOM 3219 O ARG B 238 3.507 13.316 3.592 1.00 0.00

ATOM 3220 CB ARG B 238 5.834 15.555 4.210 1.00 0.00

ATOM 3221 CG ARG B 238 6.416 16.353 5.365 1.00 0.00

ATOM 3222 CD ARG B 238 6.688 17.792 4.962 1.00 0.00

ATOM 3223 NE ARG B 238 7.298 18.560 6.045 1.00 0.00

ATOM 3224 CZ ARG B 238 7.743 19.805 5.919 1.00 0.00

ATOM 3225 NHl ARG B 238 8.284 20.424 6.959 1.00 0.00

ATOM 3226 NH2 ARG B 238 7.646 20.430 4.753 1.00 0.00

ATOM 3227 N LYS B 239 5.339 13.209 2.284 1.00 0.00

ATOM 3228 CA LYS B 239 4.574 12.680 1.169 1.00 0.00

ATOM 3229 C LYS B 239 4.033 11.294 1.469 1.00 0.00

ATOM 3230 O LYS B 239 2.882 10.999 1.166 1.00 0.00

ATOM 3231 CB LYS B 239 5.449 12.582 -0.083 1.00 0.00

ATOM 3232 CG LYS B 239 4.710 12.096 -1.319 1.00 0.00

ATOM 3233 CD LYS B 239 5.613 12.110 -2.542 1.00 0.00

ATOM 3234 CE LYS B 239 4.882 11.601 -3.773 1.00 0.00

ATOM 3235 NZ LYS B 239 5.761 11.589 -4.975 1.00 0.00

ATOM 3236 N SER B 240 4.829 10.445 2.095 1.00 0.00

ATOM 3237 CA SER B 240 4.332 9.122 2.409 1.00 0.00

ATOM 3238 C SER B 240 3.185 9.170 3.432 1.00 0.00

ATOM 3239 O SER B 240 2.190 8.441 3.320 1.00 0.00

ATOM 3240 CB SER B 240 5.447 8.257 2.999 1.00 0.00

ATOM 3241 OG SER B 240 6.460 8.007 2.040 1.00 0.00

ATOM 3242 N ASP B 241 3.315 10.063 4.406 1.00 0.00

ATOM 3243 CA ASP B 241 2.280 10.224 5.417 1.00 0.00

ATOM 3244 C ASP B 241 0.995 10.607 4.702 1.00 0.00

ATOM 3245 O ASP B 241 0.076 10.082 5.007 1.00 0.00

ATOM 3246 CB ASP B 241 2.670 11.319 6.412 1.00 0.00

ATOM 3247 CG ASP B 241 3.781 10.887 7.349 1.00 0.00

ATOM 3248 ODl ASP B 241 4.085 9.676 7.390 1.00 0.00

ATOM 3249 OD2 ASP B 241 4.345 11.759 8.042 1.00 0.00

ATOM 3250 N LEU B 242 1.098 11.523 3.748 1.00 0.00

ATOM 3251 CA LEU B 242 0.094 11.935 3.021 1.00 0.00

ATOM 3252 C LEU B 242 0.658 10.813 2.147 1.00 0.00

ATOM 3253 O LEU B 242 1.871 10.639 2.074 1.00 0.00

ATOM 3254 CB LEU B 242 0.221 13.118 2.103 1.00 0.00

ATOM 3255 CG LEU B 242 0.534 14.447 2.794 1.00 0.00

ATOM 3256 CDl LEU B 242 1.000 15.482 1.781 1.00 0.00

ATOM 3257 CD2 LEU B 242 0.700 14.992 3.495 1.00 0.00

ATOM 3258 N GLU B 243 0.185 10.026 1.490 1.00 0.00

ATOM 3259 CA GLU B 243 0.382 8.962 0.661 1.00 0.00

ATOM 3260 C GLU B 243 1.231 8.042 1.519 1.00 0.00

ATOM 3261 O GLU B 243 2.307 7.597 1.116 1.00 0.00

ATOM 3262 CB GLU B 243 0.732 8.141 0.009 1.00 0.00

ATOM 3263 CG GLU B 243 1.492 8.879 -1.081 1.00 0.00

ATOM 3264 CD GLU B 243 2.663 8.082 -1.618 1.00 0.00

ATOM 3265 OEl GLU B 243 2.926 6.982 -1.087 1.00 0.00

ATOM 3266 OE2 GLU B 243 3.319 8.556 -2.570 1.00 0.00

ATOM 3267 N ALA B 244 0.750 7.782 2.722 1.00 0.00

ATOM 3268 CA ALA B 244 1.467 6.922 3.645 1.00 0.00

ATOM 3269 C ALA B 244 2.764 7.584 4.069 1.00 0.00

ATOM 3270 O ALA B 244 3.844 6.983 4.006 1.00 0.00

ATOM 3271 CB ALA B 244 0.626 6.657 4.884 1.00 0.00

ATOM 3272 N ASN B 245 2.653 8.820 4.502 1.00 0.00

ATOM 3273 CA ASN B 245 3.823 9.533 4.957 1.00 0.00

ATOM 3274 C ASN B 245 4.907 9.577 3.899 1.00 0.00

ATOM 3275 O ASN B 245 6.086 9.334 4.169 1.00 0.00

ATOM 3276 CB ASN B 245 3.465 10.977 5.315 1.00 0.00

ATOM 3277 CG ASN B 245 2.678 11.079 6.605 1.00 0.00

ATOM 3278 ODl ASN B 245 2.694 10.163 7.429 1.00 0.00

ATOM 3279 ND2 ASN B 245 1.984 12.197 6.788 1.00 0.00

ATOM 3280 N VAL B 246 4.480 9.873 2.680 1.00 0.00 ATOM 3281 CA VAL B 246 -5.387 9.941 1.557 1.00 0.00

ATOM 3282 C VAL B 246 -6.058 8.570 1.313 1.00 0.00

ATOM 3283 O VAL B 246 -7.277 8.488 1.174 1.00 0.00

ATOM 3284 CB VAL B 246 -4.655 10.344 0.263 1.00 0.00

ATOM 3285 CGl VAL B 246 -5.582 10.216 -0.936 1.00 0.00

ATOM 3286 CG2 VAL B 246 -4.176 11.786 0.350 1.00 0.00

ATOM 3287 N GLU B 247 -5.293 7.487 1.268 1.00 0.00

ATOM 3288 CA GLU B 247 -5.934 6.185 1.093 1.00 0.00

ATOM 3289 C GLU B 247 -6.983 5.929 2.190 1.00 0.00

ATOM 3290 O GLU B 247 -8.100 5.482 1.901 1.00 0.00

ATOM 3291 CB GLU B 247 -4.896 5.064 1.160 1.00 0.00

ATOM 3292 CG GLU B 247 -5.471 3.673 0.942 1.00 0.00

ATOM 3293 CD GLU B 247 -4.409 2.591 0.982 1.00 0.00

ATOM 3294 OEl GLU B 247 -3.220 2.931 1.165 1.00 0.00

ATOM 3295 OE2 GLU B 247 -4.764 1.404 0.828 1.00 0.00

ATOM 3296 N ALA B 248 -6.639 6.197 3.446 1.00 0.00

ATOM 3297 CA ALA B 248 -7.600 5.931 4.515 1.00 0.00

ATOM 3298 C ALA B 248 -8.869 6.701 4.306 1.00 0.00

ATOM 3299 O ALA B 248 -9.958 6.163 4.449 1.00 0.00

ATOM 3300 CB ALA B 248 -7.019 6.332 5.862 1.00 0.00

ATOM 3301 N LEU B 249 -8.706 7.971 3.958 1.00 0.00

ATOM 3302 CA LEU B 249 -9.846 8.834 3.739 1.00 0.00

ATOM 3303 C LEU B 249 10.696 8.363 2.575 1.00 0.00

ATOM 3304 O LEU B 249 11.925 8.335 2.673 1.00 0.00

ATOM 3305 CB LEU B 249 -9.386 10.261 3.432 1.00 0.00

ATOM 3306 CG LEU B 249 -8.752 11.033 4.590 1.00 0.00

ATOM 3307 CDl LEU B 249 -8.181 12.357 4.105 1.00 0.00

ATOM 3308 CD2 LEU B 249 -9.783 11.328 5.669 1.00 0.00

ATOM 3309 N VAL B 250 10.045 7.988 1.479 1.00 0.00

ATOM 3310 CA VAL B 250 10.766 7.523 0.305 1.00 0.00

ATOM 3311 C VAL B 250 11.570 6.284 0.603 1.00 0.00

ATOM 3312 O VAL B 250 12.700 6.136 0.140 1.00 0.00

ATOM 3313 CB VAL B 250 -9.805 7.179 -0.848 1.00 0.00

ATOM 3314 CGl VAL B 250 10.558 6.511 -1.988 1.00 0.00

ATOM 3315 CG2 VAL B 250 -9.143 8.440 -1.383 1.00 0.00

ATOM 3316 N GLU B 251 10.994 5.400 1.400 1.00 0.00

ATOM 3317 CA GLU B 251 11.676 4.184 1.793 1.00 0.00

ATOM 3318 C GLU B 251 12.898 4.534 2.648 1.00 0.00

ATOM 3319 O GLU B 251 13.983 3.993 2.436 1.00 0.00

ATOM 3320 CB GLU B 251 10.743 3.285 2.607 1.00 0.00

ATOM 3321 CG GLU B 251 -9.616 2.665 1.797 1.00 0.00

ATOM 3322 CD GLU B 251 -8.644 1.883 2.657 1.00 0.00

ATOM 3323 OEl GLU B 251 -8.810 1.885 3.895 1.00 0.00

ATOM 3324 OE2 GLU B 251 -7.715 1.266 2.093 1.00 0.00

ATOM 3325 N GLU B 252 12.738 5.446 3.599 1.00 0.00

ATOM 3326 CA GLU B 252 13.884 5.815 4.421 1.00 0.00

ATOM 3327 C GLU B 252 14.966 6.450 3.591 1.00 0.00

ATOM 3328 O GLU B 252 16.148 6.187 3.793 1.00 0.00

ATOM 3329 CB GLU B 252 13.467 6.814 5.501 1.00 0.00

ATOM 3330 CG GLU B 252 12.600 6.217 6.598 1.00 0.00

ATOM 3331 CD GLU B 252 12.105 7.259 7.582 1.00 0.00

ATOM 3332 OEl GLU B 252 12.379 8.459 7.365 1.00 0.00

ATOM 3333 OE2 GLU B 9 R 9 11.443 6.877 8.570 1.00 0.00

ATOM 3334 N SER B 253 14.559 7.283 2.649 1.00 0.00

ATOM 3335 CA SER B 253 15.517 7.924 1.770 1.00 0.00

ATOM 3336 C SER B 253 16.307 6.852 0.997 1.00 0.00

ATOM 3337 O SER B 253 17.531 6.923 0.901 1.00 0.00

ATOM 3338 CB SER B 253 14.800 8.830 0.767 1.00 0.00

ATOM 3339 OG SER B 253 14.187 9.928 1.419 1.00 0.00

ATOM 3340 N SER B 254 15.614 5.844 0.464 1.00 0.00

ATOM 3341 CA SER B 254 16.284 4.775 -0.286 1.00 0.00

ATOM 3342 C SER B 254 17.289 4.035 0.598 1.00 0.00

ATOM 3343 O SER B 254 18.414 3.765 0.184 1.00 0.00

ATOM 3344 CB SER B 254 15.260 3.760 -0.799 1.00 0.00

ATOM 3345 OG SER B 254 14.409 4.341 -1.771 1.00 0.00

ATOM 3346 N PHE B 255 16.874 3.700 1.806 1.00 0.00

ATOM 3347 CA PHE B 255 17.776 3.033 2.719 1.00 0.00

ATOM 3348 C PHE B 255 18.980 3.938 3.020 1.00 0.00 ATOM 3349 O PHE B 255 -20.100 3.451 3.147 1.00 0.00

ATOM 3350 CB PHE B 255 -17.065 2.708 4.033 1.00 0.00

ATOM 3351 CG PHE B 255 -16.169 1.504 3.956 1.00 0.00

ATOM 3352 CDl PHE B 255 -14.799 1.651 3.829 1.00 0.00

ATOM 3353 CD2 PHE B 255 -16.695 0.226 4.011 1.00 0.00

ATOM 3354 CEl PHE B 255 -13.974 0.545 3.758 1.00 0.00

ATOM 3355 CE2 PHE B 255 -15.871 -0.880 3.940 1.00 0.00

ATOM 3356 CZ PHE B 255 -14.515 -0.725 3.814 1.00 0.00

ATOM 3357 N LEU B 256 -18.757 5.249 3.101 1.00 0.00

ATOM 3358 CA LEU B 256 -19.866 6.158 3.366 1.00 0.00

ATOM 3359 C LEU B 256 -20.789 6.291 2.182 1.00 0.00

ATOM 3360 O LEU B 256 -21.986 6.451 2.374 1.00 0.00

ATOM 3361 CB LEU B 256 -19.344 7.556 3.702 1.00 0.00

ATOM 3362 CG LEU B 256 -18.589 7.698 5.025 1.00 0.00

ATOM 3363 CDl LEU B 256 -17.996 9.092 5.160 1.00 0.00

ATOM 3364 CD2 LEU B 256 -19.521 7.462 6.204 1.00 0.00

ATOM 3365 N ARG B 257 -20.269 6.231 0.959 1.00 0.00

ATOM 3366 CA ARG B 257 -21.173 6.349 -0.178 1.00 0.00

ATOM 3367 C ARG B 257 -22.094 5.158 -0.136 1.00 0.00

ATOM 3368 O ARG B 257 -23.289 5.289 -0.352 1.00 0.00

ATOM 3369 CB ARG B 257 -20.385 6.363 -1.490 1.00 0.00

ATOM 3370 CG ARG B 257 -19.589 7.636 -1.723 1.00 0.00

ATOM 3371 CD ARG B 257 -18.776 7.552 -3.004 1.00 0.00

ATOM 3372 NE ARG B 257 -17.983 8.757 -3.229 1.00 0.00

ATOM 3373 CZ ARG B 257 -17.129 8.913 -4.235 1.00 0.00

ATOM 3374 NHl ARG B 257 -16.450 10.045 -4.360 1.00 0.00

ATOM 3375 NH2 ARG B 257 -16.955 7.935 -5.115 1.00 0.00

ATOM 3376 N ARG B 258 -21.528 3.991 0.160 1.00 0.00

ATOM 3377 CA ARG B 258 -22.329 2.780 0.253 1.00 0.00

ATOM 3378 C ARG B 258 -23.393 2.914 1.336 1.00 0.00

ATOM 3379 O ARG B 258 -24.579 2.706 1.084 1.00 0.00

ATOM 3380 CB ARG B 258 -21.446 1.578 0.596 1.00 0.00

ATOM 3381 CG ARG B 258 -20.526 1.141 -0.533 1.00 0.00

ATOM 3382 CD ARG B 258 -19.647 -0.023 -0.109 1.00 0.00

ATOM 3383 NE ARG B 258 -18.723 -0.425 -1.167 1.00 0.00

ATOM 3384 CZ ARG B 258 -17.808 -1.380 -1.037 1.00 0.00

ATOM 3385 NHl ARG B 258 -17.009 -1.677 -2.054 1.00 0.00

ATOM 3386 NH2 ARG B 258 -17.692 -2.036 0.109 1.00 0.00

ATOM 3387 N LEU B 259 -22.971 3.263 2.542 1.00 0.00

ATOM 3388 CA LEU B 259 -23.901 3.430 3.651 1.00 0.00

ATOM 3389 C LEU B 259 -25.004 4.398 3.253 1.00 0.00

ATOM 3390 O LEU B 259 -26.190 4.158 3.511 1.00 0.00

ATOM 3391 CB LEU B 259 -23.176 3.984 4.879 1.00 0.00

ATOM 3392 CG LEU B 259 -22.217 3.027 5.590 1.00 0.00

ATOM 3393 CDl LEU B 259 -21.428 3.757 6.667 1.00 0.00

ATOM 3394 CD2 LEU B 259 -22.982 1.889 6.249 1.00 0.00

ATOM 3395 N TYR B 260 -24.597 5.506 2.643 1.00 0.00

ATOM 3396 CA TYR B 260 -25.546 6.515 2.214 1.00 0.00

ATOM 3397 C TYR B 260 -26.593 5.835 1.355 1.00 0.00

ATOM 3398 O TYR B 260 -27.761 5.786 1.730 1.00 0.00

ATOM 3399 CB TYR B 260 -24.842 7.604 1.405 1.00 0.00

ATOM 3400 CG TYR B 260 -25.764 8.697 0.913 1.00 0.00

ATOM 3401 CDl TYR B 260 -26.123 9.751 1.744 1.00 0.00

ATOM 3402 CD2 TYR B 260 -26.273 8.670 -0.378 1.00 0.00

ATOM 3403 CEl TYR B 260 -26.966 10.753 1.304 1.00 0.00

ATOM 3404 CE2 TYR B 260 -27.117 9.664 -0.836 1.00 0.00

ATOM 3405 CZ TYR B 260 -27.461 10.711 0.019 1.00 0.00

ATOM 3406 OH TYR B 260 -28.302 11.709 -0.422 1.00 0.00

ATOM 3407 N GLU B 261 -26.177 5.295 0.213 1.00 0.00

ATOM 3408 CA GLU B 261 -27.101 4.596 -0.679 1.00 0.00

ATOM 3409 C GLU B 261 -28.066 3.724 0.123 1.00 0.00

ATOM 3410 O GLU B 261 -29.287 3.866 0.024 1.00 0.00

ATOM 3411 CB GLU B 261 -26.332 3.697 -1.649 1.00 0.00

ATOM 3412 CG GLU B 261 -27.205 3.025 -2.697 1.00 0.00

ATOM 3413 CD GLU B 261 -26.395 2.253 -3.720 1.00 0.00

ATOM 3414 OEl GLU B 261 -25.152 2.238 -3.606 1.00 0.00

ATOM 3415 OE2 GLU B 261 -27.005 1.662 -4.637 1.00 0.00

ATOM 3416 N GLU B 262 -27.508 2.825 0.925 1.00 0.00 ATOM 3417 CA GLU B 262 -28.314 ,937 1.751 00 0.00

ATOM 3418 C GLU B 262 -29.420 .699 483 .00 0.00

ATOM 3419 O GLU B 262 -30.566 >59 540 .00 0.00

ATOM 3420 CB GLU B 262 -27.444 >46 2.802 .00 0.00

ATOM 3421 CG GLU B 262 -28.194 0.252 3.674 .00 0.00

ATOM 3422 CD GLU B 262 -27.289 -0.457 4.661 .00 0.00

ATOM 3423 OEl GLU B 262 -26.069 -0.189 4.647 .00 0.00

ATOM 3424 OE2 GLU B 262 -27.798 -1.282 5.448 .00 0.00

ATOM 3425 N GLU B 263 -29.070 3.852 3.036 .00 0.00

ATOM 3426 CA GLU B 263 -30.026 4.652 3.779 .00 0.00

ATOM 3427 C GLU B 263 -31.047 5.370 2.913 .00 0.00

ATOM 3428 O GLU B 263 -32 ,227 5.426 3.272 .00 0.00

ATOM 3429 CB GLU B 263 -29 ,306 5.733 4.587 .00 0.00

ATOM 3430 CG GLU B 263 28.503 5.200 5.762 .00 0.00

ATOM 3431 CD GLU B 263 29.357 4.424 6.747 .00 0.00

ATOM 3432 OEl GLU B 263 30.390 4.966 7.192 .00 0.00

ATOM 3433 OE2 GLU B 263 28.992 3.275 7.074 .00 0.00

ATOM 3434 N ILE B 264 -30 621 .938 1.789 .00 0.00

ATOM 3435 CA ILE B 264 -31.619 .623 0.982 .00 0.00

ATOM 3436 C ILE B 264 -32.565 .580 0.444 1.00 0.00

ATOM 3437 O ILE B 264 -33.704 .883 0.107 1.00 0.00

ATOM 3438 CB ILE B 264 -30.972 7.382 -0.191 1..00 0.00

ATOM 3439 CGl ILE B 264 -30.276 6.405 -1.140 1..00 0.00

ATOM 3440 CG2 ILE B 264 -29.940 8.375 0.321 1..00 0.00

ATOM 3441 CDl ILE B 264 -29.783 7.043 -2.420 1.00 0.00

ATOM 3442 N ARG B 265 -32.113 4.333 0.403 1.00 0.00

ATOM 3443 CA ARG B 265 -33.025 3.328 -0.076 1.00 0.00

ATOM 3444 C ARG B 265 -33.965 2.869 1.003 1.00 0.00

ATOM 3445 O ARG B 265 -35.126 2.583 0.728 1.00 0.00

ATOM 3446 CB ARG B 265 -32.257 2.104 -0.578 1.00 0.00

ATOM 3447 CG ARG B 265 -31.487 2.340 .869 1..00 0.00

ATOM 3448 CD ARG B 265 -30.674 1.117 >57 1..00 0.00

ATOM 3449 NE ARG B 265 -29.967 1.309 .521 1.00 0.00

ATOM 3450 CZ ARG B 265 -29.082 0.452 .021 1.00 0.00

ATOM 3451 NHl ARG B 265 -28.488 0.711 .177 1.00 0.00

ATOM 3452 NH2 ARG B 265 -28.792 -0.661 -3.361 1.00 0.00

ATOM 3453 N VAL B 266 -33.484 2.797 2.236 1.00 0.00

ATOM 3454 CA VAL B 266 -34.376 2.403 3.307 1.00 0.00

ATOM 3455 C VAL B 266 -35.442 3.461 3.483 1..00 0.00

ATOM 3456 O VAL B 266 -36.564 3.160 3.892 1..00 0.00

ATOM 3457 CB VAL B 266 -33.622 241 4.640 1.00 0.00

ATOM 3458 CGl VAL B 266 -34.600 007 5.780 1.00 0.00

ATOM 3459 CG2 VAL B 266 -32.670 057 4.572 1.00 0.00

ATOM 3460 N LEU B 267 -35.094 705 3.173 1.00 0.00

ATOM 3461 CA LEU B 267 -36.057 788 3.254 1.00 0.00

ATOM 3462 C LEU B 267 -37.072 5.459 2.147 1.00 0.00

ATOM 3463 O LEU B 267 -38.253 5.272 2 422 1..00 0.00

ATOM 3464 CB LEU B 267 -35.371 7.134 3.014 1..00 0.00

ATOM 3465 CG LEU B 267 -36.274 8.370 3.042 1..00 0.00

ATOM 3466 CDl LEU B 267 -36.916 8.535 4.410 1.00 0.00

ATOM 3467 CD2 LEU B 267 -35.475 9.627 2.736 1.00 0.00

ATOM 3468 N GLN B 268 -36.717 5.412 0.895 1.00 0.00

ATOM 3469 CA GLN B 268 -37.744 5.171 -0.117 1.00 0.00

ATOM 3470 C GLN B 268 -38.730 4.106 0.360 1.00 0.00

ATOM 3471 O GLN B 268 -39.938 4.337 0.426 1.00 0.00

ATOM 3472 CB GLN B 268 -37.107 4.689 -1.423 1..00 0.00

ATOM 3473 CG GLN B 268 -38.104 4.423 -2.538 1..00 0.00

ATOM 3474 CD GLN B 268 -37.433 4.003 -3.832 1.00 0.00

ATOM 3475 OEl GLN B 268 -36.229 3.749 -3.862 1.00 0.00

ATOM 3476 NE2 GLN B 268 -38.212 3.930 -4 904 1.00 0.00

ATOM 3477 N ALA B 269 -38.201 2.935 0.698 1.00 0.00

ATOM 3478 CA ALA B 269 -39.028 1.837 1.176 1.00 0.00

ATOM 3479 C ALA B 269 -40.025 2.304 2. 39 1.00 0.00

ATOM 3480 O ALA B 269 -41.198 1.937 2. 14 1.00 0.00

ATOM 3481 CB ALA B 269 -38.161 0.750 1.793 1.00 0.00

TER 3482 ALA B 269

ATOM 3483 N ASN B 287 -55.222 -1.786 4.294 1.00 0.00

ATOM 3484 CA ASN B 287 -56.095 -2.631 5.101 1.00 0.00 ATOM 3485 C ASN B 287 -57.125 1.818 5.876 .00 0.00

ATOM 3486 O ASN B 287 -58.325 2.036 5.695 .00 0.00

ATOM 3487 CB ASN B 287 -55.278 3.431 6.117 .00 0.00

ATOM 3488 CG ASN B 287 -54.459 4.531 5.471 .00 0.00

ATOM 3489 ODl ASN B 287 -54.712 4.917 4.330 .00 0.00

ATOM 3490 ND2 ASN B 287 -53.473 -5 040 6.200 .00 0.00

ATOM 3491 N MET B 288 -56.675 0.891 6.723 .00 0.00

ATOM 3492 CA MET B 288 -57.602 0.071 7.499 .00 0.00

ATOM 3493 C MET B 288 -58.615 0.631 6.635 .00 0.00

ATOM 3494 O MET B 288 -59.761 0.764 7.033 .00 0.00

ATOM 3495 CB MET B 288 -56.841 1.006 8.277 .00 0.00

ATOM 3496 CG MET B OQQ

ZOO -55.995 0.466 9.418 .00 0.00

ATOM 3497 SD MET B 288 -54.999 1.744 10.210 .00 0.00

ATOM 3498 CE MET B 288 -56.278 2.770 10.932 .00 0.00

ATOM 3499 N ASP B 289 -58.220 1.082 5.455 .00 0.00

ATOM 3500 CA ASP B 289 -59.184 1.756 603 .00 0.00

ATOM 3501 C ASP B 289 -60.241 0.813 040 ,00 0.00

ATOM 3502 O ASP B 289 -61.412 1.167 948 .00 0.00

ATOM 3503 CB ASP B 289 -58.482 2.411 3.411 .00 0.00

ATOM 3504 CG ASP B 289 -57.692 3.643 3.806 1.00 0.00

ATOM 3505 ODl ASP B 289 -57.882 4.133 4.938 1.00 0.00

ATOM 3506 OD2 ASP B 289 -56.884 4.119 2.981 1..00 0.00

ATOM 3507 N CYS B 290 -59.825 -0.395 3.692 1..00 0.00

ATOM 3508 CA CYS B 290 -60.749 -1.392 3.191 1..00 0.00

ATOM 3509 C CYS B 290 -61.740 -1.717 4.309 1.00 0.00

ATOM 3510 O CYS B 290 -62.956 1.707 4.094 1.00 0.00

ATOM 3511 CB CYS B 290 -59.999 -2.660 2.780 1.00 0.00

ATOM 3512 SG CYS B 290 -58.960 -2.471 1.313 1.00 0.00

ATOM 3513 N ILE B 291 -61.196 -1.990 5.494 1.00 0.00

ATOM 3514 CA ILE B 291 -61.979 -2.335 6.679 1.00 0.00

ATOM 3515 C ILE B 291 -62.987 .237 6.960 1..00 0.00

ATOM 3516 O ILE B 291 -64. .157 .515 7.205 1..00 0.00

ATOM 3517 CB ILE B 291 -61.082 -2.500 7.920 1.00 0.00

ATOM 3518 CGl ILE B 291 -60.182 -3 729 7.768 1.00 0.00

ATOM 3519 CG2 ILE B 291 -61.930 2.676 9.170 1.00 0.00

ATOM 3520 CDl ILE B 291 -59.086 3.815 8.807 1.00 0.00

ATOM 3521 N ILE B 292 -62.534 0.012 6.912 1.00 0.00

ATOM 3522 CA ILE B 292 -63.430 1.135 7.143 1.00 0.00

ATOM 3523 C ILE B 292 -64.520 1.243 6.086 1..00 0.00

ATOM 3524 O ILE B 292 -65.643 1.631 6.398 1..00 0.00

ATOM 3525 CB ILE B 292 -62.669 2.475 7.134 1.00 0.00

ATOM 3526 CGl ILE B 292 -61.737 2.566 8.344 1.00 0.00

ATOM 3527 CG2 ILE B 292 -63.644 3.641 7.188 1.00 0.00

ATOM 3528 CDl ILE B 292 -60.762 3.722 8.277 1.00 0.00

ATOM 3529 N ALA B 293 -64.198 0.923 .836 1.00 0.00

ATOM 3530 CA ALA B 293 -65.186 0.988 .768 1.00 0.00

ATOM 3531 C ALA B 293 -66.283 0.008 .126 1..00 0.00

ATOM 3532 O ALA B 293 -67.469 0.321 .113 1..00 0.00

ATOM 3533 CB ALA B 293 -64.552 622 2.435 1..00 0.00

ATOM 3534 N GLU B 294 -65.881 227 4.455 1.00 0.00

ATOM 3535 CA GLU B 294 -66.843 251 4.834 1.00 0.00

ATOM 3536 C GLU B 294 -67.704 765 .986 1.00 0.00

ATOM 3537 O GLU B 294 -68.927 810 .906 1.00 0.00

ATOM 3538 CB GLU B 294 -66.122 528 >70 1.00 0.00

ATOM 3539 CG GLU B 294 -67.054 -4.670 .642 1.00 0.00

ATOM 3540 CD GLU B 294 -66.305 -5 928 6.037 1..00 0.00

ATOM 3541 OEl GLU B 294 -65.057 -5 910 6.008 1..00 0.00

ATOM 3542 OE2 GLU B 294 -66.967 -6.931 6.376 1.00 0.00

ATOM 3543 N ILE B 295 -67.069 -1.309 7.065 1.00 0.00

ATOM 3544 CA ILE B 295 -67.835 -0.878 8.232 1.00 0.00

ATOM 3545 C ILE B 295 -68.815 0.212 7.896 1.00 0.00

ATOM 3546 O ILE B 295 -69.882 0.285 8.494 1.00 0.00

ATOM 3547 CB ILE B 295 -66.916 -0.333 9.340 1.00 0.00

ATOM 3548 CGl ILE B 295 -66.071 .461 9.936 00 0.00

ATOM 3549 CG2 ILE B 295 -67.739 ,293 10.456 00 0.00

ATOM 3550 CDl ILE B 295 -64.961 -0.979 10.843 00 0.00

ATOM 3551 N LYS B 296 -68.462 1.071 6.964 00 0.00

ATOM 3552 CA LYS B 296 -69.379 2.133 6.609 1.00 0.00 ATOM 3553 C LYS B 296 70.526 1.590 5.801 1.00 0.00

ATOM 3554 O LYS B 296 71.626 2.119 5.851 1.00 0.00

ATOM 3555 CB LYS B 296 68.665 3.203 5.780 1.00 0.00

ATOM 3556 CG LYS B 296 67.657 4.028 6.564 1.00 0.00

ATOM 3557 CD LYS B 296 66.984 5.064 5.681 1.00 0.00

ATOM 3558 CE LYS B 296 65.977 5.888 6.465 1.00 0.00

ATOM 3559 NZ LYS B 296 65.288 6.890 5.604 1.00 0.00

ATOM 3560 N ALA B 297 70.269 0.533 5.042 1.00 0.00

ATOM 3561 CA ALA B 297 71.309 -0.077 4.236 1.00 0.00

ATOM 3562 C ALA B 297 72.299 -0.709 5.205 1.00 0.00

ATOM 3563 O ALA B 297 73.515 -0.503 5.098 1.00 0.00

ATOM 3564 CB ALA B 297 70.717 -1.134 3.317 1.00 0.00

ATOM 3565 N GLN B 298 71.768 -1.466 6.159 1.00 0.00

ATOM 3566 CA GLN B 298 72.607 -2.135 7.150 1.00 0.00

ATOM 3567 C GLN B 298 73.404 -1.138 7.972 1.00 0.00

ATOM 3568 O GLN B 298 74.552 -1.406 8.297 1.00 0.00

ATOM 3569 CB GLN B 298 71.747 -2.956 8.114 1.00 0.00

ATOM 3570 CG GLN B 298 71.123 -4.192 7.488 1.00 0.00

ATOM 3571 CD GLN B 298 70.189 -4.917 8.437 1.00 0.00

ATOM 3572 OEl GLN B 298 69.930 -4.450 9.546 1.00 0.00

ATOM 3573 NE2 GLN B 298 69.680 -6.064 8.004 1.00 0.00

ATOM 3574 N TYR B 299 72.794 -0.003 8.299 1.00 0.00

ATOM 3575 CA TYR B 299 73.433 1.050 9.085 1.00 0.00

ATOM 3576 C TYR B 299 74.595 1.613 8.247 1.00 0.00

ATOM 3577 O TYR B 299 75.720 1.701 8.720 1.00 0.00

ATOM 3578 CB TYR B 299 72.432 2.163 9.405 1.00 0.00

ATOM 3579 CG TYR B 299 73.022 3.307 10.198 1.00 0.00

ATOM 3580 CDl TYR B 299 73.224 3.193 11.568 1.00 0.00

ATOM 3581 CD2 TYR B 299 73.374 4.497 9.575 1.00 0.00

ATOM 3582 CEl TYR B 299 73.763 4.233 12.300 1.00 0.00

ATOM 3583 CE2 TYR B 299 73.913 5.548 10.292 1.00 0.00

ATOM 3584 CZ TYR B 299 74.106 5.407 11.666 1.00 0.00

ATOM 3585 OH TYR B 299 74.642 6.445 12.394 1.00 0.00

ATOM 3586 N ASP B 300 74.320 1.966 6.996 1.00 0.00

ATOM 3587 CA ASP B 300 75.363 2.474 6.103 1.00 0.00

ATOM 3588 C ASP B 300 76.571 1.499 6.110 1.00 0.00

ATOM 3589 O ASP B 300 77.725 1.916 6.219 1.00 0.00

ATOM 3590 CB ASP B 300 74.832 2.596 4.673 1.00 0.00

ATOM 3591 CG ASP B 300 73.865 3.753 4.509 1.00 0.00

ATOM 3592 ODl ASP B 300 73.782 4.594 5.428 1.00 0.00

ATOM 3593 OD2 ASP B 300 73.191 3.819 3.459 1.00 0.00

ATOM 3594 N ASP B 301 76.292 0.200 5.999 1.00 0.00

ATOM 3595 CA ASP B 301 77.351 -0.817 5.999 1.00 0.00

ATOM 3596 C ASP B 301 78.131 -0.794 7.300 1.00 0.00

ATOM 3597 O ASP B 301 79.364 -0.777 7.292 1.00 0.00

ATOM 3598 CB ASP B 301 76.751 -2.214 5.829 1.00 0.00

ATOM 3599 CG ASP B 301 76.244 -2.464 4.422 1.00 0.00

ATOM 3600 ODl ASP B 301 76.567 -1.660 3.524 1.00 0.00

ATOM 3601 OD2 ASP B 301 75.525 -3.465 4.218 1.00 0.00

ATOM 3602 N VAL B 302 77.419 -0.806 8.420 1.00 0.00

ATOM 3603 CA VAL B 302 78.104 -0.783 9.706 1.00 0.00

ATOM 3604 C VAL B 302 79.004 0.424 9.841 1.00 0.00

ATOM 3605 O VAL B 302 80.113 0.303 10.358 1.00 0.00

ATOM 3606 CB VAL B 302 77.105 -0.740 10.877 1.00 0.00

ATOM 3607 CGl VAL B 302 77.835 -0.515 12.192 1.00 0.00

ATOM 3608 CG2 VAL B 302 76.337 -2.049 10.971 1.00 0.00

ATOM 3609 N ALA B 303 78.544 1.582 9.378 1.00 0.00

ATOM 3610 CA ALA B 303 79.357 2.786 9.477 1.00 0.00

ATOM 3611 C ALA B 303 80.629 2.631 8.651 1.00 0.00

ATOM 3612 O ALA B 303 81.723 2.901 9.142 1.00 0.00

ATOM 3613 CB ALA B 303 78.586 3.991 8.959 1.00 0.00

ATOM 3614 N SER B 304 80.513 2.167 7.416 1.00 0.00

ATOM 3615 CA SER B 304 81.718 1.977 6.633 1.00 0.00

ATOM 3616 C SER B 304 82.668 1.056 7.408 1.00 0.00

ATOM 3617 O SER B 304 83.829 1.392 7.615 1.00 0.00

ATOM 3618 CB SER B 304 81.384 1.340 5.283 1.00 0.00

ATOM 3619 OG SER B 304 80.622 9 999 4.477 1.00 0.00

ATOM 3620 N ARG B 305 82.171 -0.086 7.859 1.00 0.00 ATOM 3621 CA ARG B 305 -83.020 -1.026 8.598 1.00 0.00

ATOM 3622 C ARG B 305 -83.694 -0.411 9.821 1.00 0.00

ATOM 3623 O ARG B 305 -84.877 -0.647 10.067 1.00 0.00

ATOM 3624 CB ARG B 305 -82.194 -2.213 9.098 1.00 0.00

ATOM 3625 CG ARG B 305 -81.672 -3.116 7.993 1.00 0.00

ATOM 3626 CD ARG B 305 -80.840 -4.257 8.558 1.00 0.00

ATOM 3627 NE ARG B 305 -80.307 -5.118 7.506 1.00 0.00

ATOM 3628 CZ ARG B 305 -79.497 -6.149 7.724 1.00 0.00

ATOM 3629 NHl ARG B 305 -79.061 -6.877 6.705 1.00 0.00

ATOM 3630 NH2 ARG B 305 -79.124 -6.449 8.961 1.00 0.00

TER 3631 ARG B 305

ATOM 3632 N TYR B 314 -93.407 -3.215 10.155 1.00 0.00

ATOM 3633 CA TYR B 314 -94.347 -3.100 11.260 1.00 0.00

ATOM 3634 C TYR B 314 -95.318 -1.977 11.045 1.00 0.00

ATOM 3635 O TYR B 314 -96.500 -2.154 11.294 1.00 0.00

ATOM 3636 CB TYR B 314 -93.603 -2.831 12.570 1.00 0.00

ATOM 3637 CG TYR B 314 -92.890 -4.041 13.128 1.00 0.00

ATOM 3638 CDl TYR B 314 -91.509 -4.158 13.035 1.00 0.00

ATOM 3639 CD2 TYR B 314 -93.599 -5.063 13.747 1.00 0.00

ATOM 3640 CEl TYR B 314 -90.848 -5.260 13.542 1.00 0.00

ATOM 3641 CE2 TYR B 314 -92.954 -6.172 14.261 1.00 0.00

ATOM 3642 CZ TYR B 314 -91.567 -6.265 14.153 1.00 0.00

ATOM 3643 OH TYR B 314 -90.911 -7.363 14.659 1.00 0.00

ATOM 3644 N ARG B 315 -94.801 -0.832 10.559 1.00 0.00

ATOM 3645 CA ARG B 315 -95.670 0.310 10.330 1.00 0.00

ATOM 3646 C ARG B 315 -96.840 -0.067 9.463 1.00 0.00

ATOM 3647 O ARG B 315 -97.949 0.356 9.744 1.00 0.00

ATOM 3648 CB ARG B 315 -94.903 1.436 9.631 1.00 0.00

ATOM 3649 CG ARG B 315 -93.876 2.128 10.512 1.00 0.00

ATOM 3650 CD ARG B 315 -93.119 3.196 9.743 1.00 0.00

ATOM 3651 NE ARG B 315 -92.091 3.835 10.562 1.00 0.00

ATOM 3652 CZ ARG B 315 -91.209 4.715 10.100 1.00 0.00

ATOM 3653 NHl ARG B 315 -90.309 5.244 10.918 1.00 0.00

ATOM 3654 NH2 ARG B 315 -91.229 5.066 8.822 1.00 0.00

ATOM 3655 N SER B 316 -96.586 -0.883 8.419 1.00 0.00

ATOM 3656 CA SER B 316 -97.677 -1.285 7.547 1.00 0.00

ATOM 3657 C SER B 316 -98.671 -2.141 8.284 1.00 0.00

ATOM 3658 O SER B 316 -99.852 -1.838 8.253 1.00 0.00

ATOM 3659 CB SER B 316 -97.144 -2.089 6.359 1.00 0.00

ATOM 3660 OG SER B 316 -96.343 -1.281 5.515 1.00 0.00

ATOM 3661 N LYS B 317 -98.183 -3.210 8.946 1.00 0.00

ATOM 3662 CA LYS B 317 -99.093 -4.091 9.662 1.00 0.00

ATOM 3663 C LYS B 317 -99.905 -3.320 10.664 1.00 0.00

ATOM 3664 O LYS B 317 -101.104 -3.523 10.757 1.00 0.00

ATOM 3665 CB LYS B 317 -98.314 -5.175 10.409 1.00 0.00

ATOM 3666 CG LYS B 317 -97.670 -6.212 9.504 1.00 0.00

ATOM 3667 CD LYS B 317 -96.916 -7.256 10.310 1.00 0.00

ATOM 3668 CE LYS B 317 -96.252 -8.281 9.404 1.00 0.00

ATOM 3669 NZ LYS B 317 -95.481 -9.292 10.178 1.00 0.00

ATOM 3670 N CYS B 318 -99.226 -2.421 11.403 1.00 0.00

ATOM 3671 CA CYS B 318 -99.922 -1.620 12.395 1.00 0.00

ATOM 3672 C CYS B 318 -101.017 -0.814 11.753 1.00 0.00

ATOM 3673 O CYS B 318 -102.117 -0.779 12.281 1.00 0.00

ATOM 3674 CB CYS B 318 -98.952 -0.654 13.079 1.00 0.00

ATOM 3675 SG CYS B 318 -97.738 -1.453 14.156 1.00 0.00

ATOM 3676 N GLU B 319 -100.707 -0.174 10.608 1.00 0.00

ATOM 3677 CA GLU B 319 -101.715 0.624 9.931 1.00 0.00

ATOM 3678 C GLU B 319 -102.924 -0.209 9.611 1.00 0.00

ATOM 3679 O GLU B 319 -104.036 0.222 9.872 1.00 0.00

ATOM 3680 CB GLU B 319 -101.160 1.189 8.622 1.00 0.00

ATOM 3681 CG GLU B 319 -102.136 2.078 7.867 1.00 0.00

ATOM 3682 CD GLU B 319 -101.540 2.646 6.594 1.00 0.00

ATOM 3683 OEl GLU B 319 -100.359 2.356 6.309 1.00 0.00

ATOM 3684 OE2 GLU B 319 -102.255 3.383 5.881 1.00 0.00

ATOM 3685 N GLU B 320 -102.690 -1.412 9.051 1.00 0.00

ATOM 3686 CA GLU B 320 -103.805 -2.287 8.729 1.00 0.00

ATOM 3687 C GLU B 320 -104.613 -2.583 9.961 1.00 0.00

ATOM 3688 O GLU B 320 -105.832 -2.531 9.905 1.00 0.00 ATOM 3689 CB GLU B 320 -103.298 -3.611 8.153 1.00 0.00

ATOM 3690 CG GLU B 320 -102.707 -3.495 6.758 1.00 0.00

ATOM 3691 CD GLU B 320 -102.105 -4.798 6.270 1.00 0.00

ATOM 3692 OEl GLU B 320 -102.084 -5.772 7.051 1.00 0.00

ATOM 3693 OE2 GLU B 320 -101.655 -4.845 5.105 1.00 0.00

ATOM 3694 N MET B 321 -103.918 -2.884 11.074 1.00 0.00

ATOM 3695 CA MET B 321 -104.623 -3.186 12.309 1.00 0.00

ATOM 3696 C MET B 321 -105.497 -2.039 12.726 1.00 0.00

ATOM 3697 O MET B 321 -106.663 -2.250 13.018 1.00 0.00

ATOM 3698 CB MET B 321 -103.629 -3.461 13.440 1.00 0.00

ATOM 3699 CG MET B 321 -102.875 -4.774 13.297 1.00 0.00

ATOM 3700 SD MET B 321 -103.963 -6.210 13.348 1.00 0.00

ATOM 3701 CE MET B 321 -104.500 -6.167 15.056 1.00 0.00

ATOM 3702 N LYS B 322 -104.917 -0.823 12.745 1.00 0.00

ATOM 3703 CA LYS B -105.678 0.334 13.184 1.00 0.00

ATOM 3704 C LYS B 322 -106.919 0.514 12.355 1.00 0.00

ATOM 3705 O LYS B 322 -107.980 0.743 12.911 1.00 0.00

ATOM 3706 CB LYS B 322 -104.836 1.607 13.062 1.00 0.00

ATOM 3707 CG LYS B 322 -105.543 2.865 13.540 1.00 0.00

ATOM 3708 CD LYS B -104.627 4.076 13.457 1.00 0.00

ATOM 3709 CE LYS B -105.348 5.343 13.888 1.00 0.00

ATOM 3710 NZ LYS B 322 -104.471 6.542 13.789 1.00 0.00

ATOM 3711 N ALA B 323 -106.773 0.401 11.019 1.00 0.00

ATOM 3712 CA ALA B 323 -107.935 0.551 10.160 1.00 0.00

ATOM 3713 C ALA B 323 -108.973 -0.483 10.493 1.00 0.00

ATOM 3714 O ALA B 323 -110.140 -0.150 10.613 1.00 0.00

ATOM 3715 CB ALA B 323 -107.539 0.385 8.701 1.00 0.00

ATOM 3716 N THR B 324 -108.525 -1.745 10.655 1.00 0.00

ATOM 3717 CA THR B 324 -109.458 -2.807 10.995 1.00 0.00

ATOM 3718 C THR B 324 -110.171 -2.517 12.290 1.00 0.00

ATOM 3719 O THR B 324 -111.350 -2.811 12.400 1.00 0.00

ATOM 3720 CB THR B 324 -108.740 -4.159 11.156 1.00 0.00

ATOM 3721 OGl THR B 324 -108.119 -4.524 9.918 1.00 0.00

ATOM 3722 CG2 THR B 324 -109.729 -5.244 11.550 1.00 0.00

ATOM 3723 N VAL B 325 -109.437 -1.938 13.263 1.00 0.00

ATOM 3724 CA VAL B 325 -110.026 -1.705 14.570 1.00 0.00

ATOM 3725 C VAL B 325 -111.251 -0.837 14.485 1.00 0.00

ATOM 3726 O VAL B 325 -112.295 -1.242 14.971 1.00 0.00

ATOM 3727 CB VAL B 325 -109.036 -1.003 15.519 1.00 0.00

ATOM 3728 CGl VAL B 325 -109.734 -0.592 16.807 1.00 0.00

ATOM 3729 CG2 VAL B 325 -107.885 -1.934 15.871 1.00 0.00

ATOM 3730 N ILE B 326 -111.119 0.351 13.858 1.00 0.00

ATOM 3731 CA ILE B 326 -112.267 1.241 13.775 1.00 0.00

ATOM 3732 C ILE B 326 -113.425 0.585 13.075 1.00 0.00

ATOM 3733 O ILE B 326 -114.561 0.977 13.290 1.00 0.00

ATOM 3734 CB ILE B 326 -111.930 2.527 12.998 1.00 0.00

ATOM 3735 CGl ILE B 326 -112.986 3.601 13.261 1.00 0.00

ATOM 3736 CG2 ILE B 326 -111.885 2.250 11.503 1.00 0.00

ATOM 3737 CDl ILE B 326 -112.580 4.983 12.799 1.00 0.00

ATOM 3738 N ARG B 327 -113.123 -0.428 12.241 1.00 0.00

ATOM 3739 CA ARG B 327 -114.189 -1.145 11.566 1.00 0.00

ATOM 3740 C ARG B 327 -114.995 -1.933 12.561 1.00 0.00

ATOM 3741 O ARG B 327 -116.205 -1.776 12.609 1.00 0.00

ATOM 3742 CB ARG B 327 -113.613 -2.112 10.530 1.00 0.00

ATOM 3743 CG ARG B 327 -113.012 -1.430 9.312 1.00 0.00

ATOM 3744 CD ARG B 327 -112.417 -2.443 8.349 1.00 0.00

ATOM 3745 NE ARG B 327 -111.812 -1.803 7.183 1.00 0.00

ATOM 3746 CZ ARG B 327 -111.204 -2.459 6.201 1.00 0.00

ATOM 3747 NHl ARG B 327 -110.682 -1.791 5.181 1.00 0.00

ATOM 3748 NH2 ARG B 327 -111.118 -3.782 6.242 1.00 0.00

ATOM 3749 N HIS B 328 -114.314 -2.786 13.353 1.00 0.00

ATOM 3750 CA HIS B 328 -115.030 -3.586 14.334 1.00 0.00

ATOM 3751 C HIS B 328 -115.776 -2.706 15.295 1.00 0.00

ATOM 3752 O HIS B 328 -116.862 -3.068 15.718 1.00 0.00

ATOM 3753 CB HIS B 328 -114.056 -4.453 15.135 1.00 0.00

ATOM 3754 CG HIS B 328 -113.451 -5.570 14.342 1.00 0.00

ATOM 3755 NDl HIS B 328 -114.203 -6.594 13.808 1.00 0.00

ATOM 3756 CD2 HIS B 328 -112.107 -5.934 13.918 1.00 0.00 ATOM 3757 CEl HIS B 328 -113.386 -7.442 13.156 1.00 0.00

ATOM 3758 NE2 HIS B 328 -112.128 -7.051 13.218 1.00 0.00

ATOM 3759 N GLY B 329 -115.194 -1.534 15.623 1.00 0.00

ATOM 3760 CA GLY B 329 -115.890 -0.616 16.509 1.00 0.00

ATOM 3761 C GLY B 329 -117.184 -0.166 15.895 1.00 0.00

ATOM 3762 O GLY B 329 -118.162 0.001 16.607 1.00 0.00

ATOM 3763 N GLU B 330 -117.186 0.021 14.560 1.00 0.00

ATOM 3764 CA GLU B 330 -118.417 0.413 13.895 1.00 0.00

ATOM 3765 C GLU B 330 -119.431 -0.691 13.994 1.00 0.00

ATOM 3766 O GLU B 330 -120.589 -0.417 14.262 1.00 0.00

ATOM 3767 CB GLU B 330 -118.156 0.707 12.416 1.00 0.00

ATOM 3768 CG GLU B 330 -117.349 1.971 12.167 1.00 0.00

ATOM 3769 CD GLU B 330 -117.006 2.164 10.703 1.00 0.00

ATOM 3770 OEl GLU B 330 -117.337 1.273 9.893 1.00 0.00

ATOM 3771 OE2 GLU B 330 -116.405 3.206 10.366 1.00 0.00

ATOM 3772 N THR B 331 -118.977 -1.942 13.781 1.00 0.00

ATOM 3773 CA THR B 331 -119.902 -3.063 13.846 1.00 0.00

ATOM 3774 C THR B 331 -120.550 -3.144 15.197 1.00 0.00

ATOM 3775 O THR B 331 -121.767 -3.177 15.277 1.00 0.00

ATOM 3776 CB THR B 331 -119.186 -4.402 13.588 1.00 0.00

ATOM 3777 OGl THR B 331 -118.623 -4.400 12.271 1.00 0.00

ATOM 3778 CG2 THR B 331 -120.165 -5.560 13.702 1.00 0.00

ATOM 3779 N LEU B 332 -119.717 -3.167 16.257 1.00 0.00

ATOM 3780 CA LEU B 332 -120.258 -3.218 17.604 1.00 0.00

ATOM 3781 C LEU B 332 -121.206 -2.076 17.837 1.00 0.00

ATOM 3782 O LEU B 332 -122.201 -2.252 18.522 1.00 0.00

ATOM 3783 CB LEU B 332 -119.132 -3.129 18.637 1.00 0.00

ATOM 3784 CG LEU B 332 -118.203 -4.340 18.733 1.00 0.00

ATOM 3785 CDl LEU B 332 -117.032 -4.047 19.659 1.00 0.00

ATOM 3786 CD2 LEU B 332 -118.948 -5.548 19.277 1.00 0.00

ATOM 3787 N ARG B 333 -120.888 -0.906 17.247 1.00 0.00

ATOM 3788 CA ARG B 333 -121.743 0.254 17.429 1.00 0.00

ATOM 3789 C ARG B 333 -123.148 -0.023 16.971 1.00 0.00

ATOM 3790 O ARG B 333 -124.067 0.076 17.769 1.00 0.00

ATOM 3791 CB ARG B 333 -121.212 1.443 16.626 1.00 0.00

ATOM 3792 CG ARG B 333 -122.009 2.723 16.811 1.00 0.00

ATOM 3793 CD ARG B 333 -121.509 3.824 15.889 1.00 0.00

ATOM 3794 NE ARG B 333 -121.775 3.523 14.484 1.00 0.00

ATOM 3795 CZ ARG B 333 -122.958 3.678 13.899 1.00 0.00

ATOM 3796 NHl ARG B 333 -123.106 3.379 12.615 1.00 0.00

ATOM 3797 NH2 ARG B 333 -123.989 4.132 14.597 1.00 0.00

ATOM 3798 N ARG B 334 -123.307 -0.371 15.678 1.00 0.00

ATOM 3799 CA ARG B 334 -124.641 -0.607 15.153 1.00 0.00

ATOM 3800 C ARG B 334 -125.344 -1.692 15.920 1.00 0.00

ATOM 3801 O ARG B 334 -126.540 -1.594 16.143 1.00 0.00

ATOM 3802 CB ARG B 334 -124.571 -1.033 13.685 1.00 0.00

ATOM 3803 CG ARG B 334 -124.168 0.082 12.734 1.00 0.00

ATOM 3804 CD ARG B 334 -124.048 -0.427 11.307 1.00 0.00

ATOM 3805 NE ARG B 334 -123.633 0.627 10.383 1.00 0.00

ATOM 3806 CZ ARG B 334 -123.383 0.432 9.092 1.00 0.00

ATOM 3807 NHl ARG B 334 -123.010 1.451 8.328 1.00 0.00

ATOM 3808 NH2 ARG B 334 -123.507 -0.780 8.567 1.00 0.00

ATOM 3809 N THR B 335 -124.583 -2.728 16.329 1.00 0.00

ATOM 3810 CA THR B 335 -125.199 -3.841 17.031 1.00 0.00

ATOM 3811 C THR B 335 -125.809 -3.409 18.336 1.00 0.00

ATOM 3812 O THR B 335 -126.934 -3.792 18.616 1.00 0.00

ATOM 3813 CB THR B 335 -124.173 -4.944 17.350 1.00 0.00

ATOM 3814 OGl THR B 335 -123.631 -5.464 16.128 1.00 0.00

ATOM 3815 CG2 THR B 335 -124.831 -6.078 18.119 1.00 0.00

ATOM 3816 N LYS B 336 -125.070 -2.605 19.129 1.00 0.00

ATOM 3817 CA LYS B 336 -125.623 -2.145 20.393 1.00 0.00

ATOM 3818 C LYS B 336 -126.921 -1.424 20.158 1.00 0.00

ATOM 3819 O LYS B 336 -127.860 -1.603 20.918 1.00 0.00

ATOM 3820 CB LYS B 336 -124.651 -1.187 21.086 1.00 0.00

ATOM 3821 CG LYS B 336 -123.397 -1.857 21.624 1.00 0.00

ATOM 3822 CD LYS B 336 -122.480 -0.851 22.298 1.00 0.00

ATOM 3823 CE LYS B 336 -121.214 -1.515 22.815 1.00 0.00

ATOM 3824 NZ LYS B 336 -120.291 -0.536 23.451 1.00 0.00 ATOM 3825 N GLU B 337 -126.964 -0.621 19.077 1.00 0.00

ATOM 3826 CA GLU B 337 -128.193 0.076 18.739 1.00 0.00

ATOM 3827 C GLU B 337 -129.299 -0.910 18.480 1.00 0.00

ATOM 3828 O GLU B 337 -130.389 -0.739 19.005 1.00 0.00

ATOM 3829 CB GLU B 337 -127.999 0.927 17.483 1.00 0.00

ATOM 3830 CG GLU B 337 -129.225 1.731 17.081 1.00 0.00

ATOM 3831 CD GLU B 337 -128.984 2.587 15.854 1.00 0.00

ATOM 3832 OEl GLU B 337 -127.853 2.563 15.325 1.00 0.00

ATOM 3833 OE2 GLU B 337 -129.927 3.282 15.420 1.00 0.00

ATOM 3834 N GLU B 338 -129.005 -1.947 17.671 1.00 0.00

ATOM 3835 CA GLU B 338 -130.021 -2.941 17.365 1.00 0.00

ATOM 3836 C GLU B 338 -130.564 -3.561 18.620 1.00 0.00

ATOM 3837 O GLU B 338 -131.767 -3.721 18.739 1.00 0.00

ATOM 3838 CB GLU B 338 -129.435 -4.057 16.498 1.00 0.00

ATOM 3839 CG GLU B 338 -129.114 -3.632 15.074 1.00 0.00

ATOM 3840 CD GLU B 338 -128.423 -4.724 14.281 1.00 0.00

ATOM 3841 OEl GLU B 338 -128.128 -5.787 14.867 1.00 0.00

ATOM 3842 OE2 GLU B 338 -128.177 -4.517 13.074 1.00 0.00

ATOM 3843 N ILE B 339 -129.657 -3.901 19.557 1.00 0.00

ATOM 3844 CA ILE B 339 -130.096 -4.514 20.799 1.00 0.00

ATOM 3845 C ILE B 339 -131.064 -3.614 21.519 1.00 0.00

ATOM 3846 O ILE B 339 -132.074 -4.095 22.007 1.00 0.00

ATOM 3847 CB ILE B 339 -128.911 -4.787 21.744 1.00 0.00

ATOM 3848 CGl ILE B 339 -128.006 -5.875 21.163 1.00 0.00

ATOM 3849 CG2 ILE B 339 -129.411 -5.251 23.104 1.00 0.00

ATOM 3850 CDl ILE B 339 -126.685 -6.020 21.887 1.00 0.00

ATOM 3851 N ASN B 340 -130.754 -2.303 21.562 1.00 0.00

ATOM 3852 CA ASN B 340 -131.666 -1.369 22.205 1.00 0.00

ATOM 3853 C ASN B 340 -133.033 -1.457 21.588 1.00 0.00

ATOM 3854 O ASN B 340 -134.021 -1.444 22.305 1.00 0.00

ATOM 3855 CB ASN B 340 -131.159 0.066 22.052 1.00 0.00

ATOM 3856 CG ASN B 340 -129.956 0.355 22.928 1.00 0.00

ATOM 3857 ODl ASN B 340 -129.702 -0.350 23.905 1.00 0.00

ATOM 3858 ND2 ASN B 340 -129.209 1.397 22.580 1.00 0.00

ATOM 3859 N GLU B 341 -133.075 -1.561 20.246 1.00 0.00

ATOM 3860 CA GLU B 341 -134.359 -1.652 19.570 1.00 0.00

ATOM 3861 C GLU B 341 -135.098 -2.900 19.966 1.00 0.00

ATOM 3862 O GLU B 341 -136.272 -2.816 20.285 1.00 0.00

ATOM 3863 CB GLU B 341 -134.165 -1.679 18.053 1.00 0.00

ATOM 3864 CG GLU B 341 -135.463 -1.727 17.262 1.00 0.00

ATOM 3865 CD GLU B 341 -135.233 -1.718 15.764 1.00 0.00

ATOM 3866 OEl GLU B 341 -134.058 -1.660 15.344 1.00 0.00

ATOM 3867 OE2 GLU B 341 -136.227 -1.769 15.010 1.00 0.00

ATOM 3868 N LEU B 342 -134.403 -4.055 19.941 1.00 0.00

ATOM 3869 CA LEU B 342 -135.075 -5.302 20.270 1.00 0.00

ATOM 3870 C LEU B 342 -135.667 -5.243 21.648 1.00 0.00

ATOM 3871 O LEU B 342 -136.809 -5.635 21.827 1.00 0.00

ATOM 3872 CB LEU B 342 -134.088 -6.470 20.222 1.00 0.00

ATOM 3873 CG LEU B 342 -133.582 -6.875 18.837 1.00 0.00

ATOM 3874 CDl LEU B 342 -132.474 -7.910 18.949 1.00 0.00

ATOM 3875 CD2 LEU B 342 -134.709 -7.474 18.007 1.00 0.00

ATOM 3876 N ASN B 343 -134.881 -4.731 22.616 1.00 0.00

ATOM 3877 CA ASN B 343 -135.397 -4.610 23.968 1.00 0.00

ATOM 3878 C ASN B 343 -136.630 -3.750 23.988 1.00 0.00

ATOM 3879 O ASN B 343 -137.577 -4.076 24.686 1.00 0.00

ATOM 3880 CB ASN B 343 -134.350 -3.974 24.885 1.00 0.00

ATOM 3881 CG ASN B 343 -134.782 -3.959 26.339 1.00 0.00

ATOM 3882 ODl ASN B 343 -134.970 -5.010 26.952 1.00 0.00

ATOM 3883 ND2 ASN B 343 -134.940 -2.764 26.895 1.00 0.00

ATOM 3884 N ARG B 344 -136.616 -2.653 23.204 1.00 0.00

ATOM 3885 CA ARG B 344 -137.779 -1.782 23.166 1.00 0.00

ATOM 3886 C ARG B 344 -138.977 -2.515 22.630 1.00 0.00

ATOM 3887 O ARG B 344 -140.029 -2.486 23.248 1.00 0.00

ATOM 3888 CB ARG B 344 -137.514 -0.573 22.267 1.00 0.00

ATOM 3889 CG ARG B 344 -136.519 0.422 22.843 1.00 0.00

ATOM 3890 CD ARG B 344 -136.269 1.572 21.881 1.00 0.00

ATOM 3891 NE ARG B 344 -135.278 2.512 22.399 1.00 0.00

ATOM 3892 CZ ARG B 344 -134.836 3.574 21.732 1.00 0.00 ATOM 3893 NHl ARG B 344 -133.933 4.374 22.282 1.00 0.00

ATOM 3894 NH2 ARG B 344 -135.298 3.833 20.516 1.00 0.00

ATOM 3895 N MET B 345 -138.801 -3.177 21.469 1.00 0.00

ATOM 3896 CA MET B 345 -139.914 -3.885 20.864 1.00 0.00

ATOM 3897 C MET B 345 -140.458 -4.937 21.788 1.00 0.00

ATOM 3898 O MET B 345 -141.666 -5.065 21.905 1.00 0.00

ATOM 3899 CB MET B 345 -139.472 -4.574 19.571 1.00 0.00

ATOM 3900 CG MET B 345 -139.151 -3.616 18.436 1.00 0.00

ATOM 3901 SD MET B 345 -140.570 -2.619 17.945 1.00 0.00

ATOM 3902 CE MET B 345 -141.621 -3.866 17.205 1.00 0.00

ATOM 3903 N ILE B 346 -139.551 -5.679 22.454 1.00 0.00

ATOM 3904 CA ILE B 346 -139.996 -6.707 23.381 1.00 0.00

ATOM 3905 C ILE B 346 -140.847 -6.105 24.462 1.00 0.00

ATOM 3906 O ILE B 346 -141.896 -6.649 24.766 1.00 0.00

ATOM 3907 CB ILE B 346 -138.804 -7.414 24.054 1.00 0.00

ATOM 3908 CGl ILE B 346 -138.020 -8.233 23.026 1.00 0.00

ATOM 3909 CG2 ILE B 346 -139.290 -8.351 25.149 1.00 0.00

ATOM 3910 CDl ILE B 346 -136.690 -8.739 23.536 1.00 0.00

ATOM 3911 N GLN B 347 -140.388 -4.972 25.031 1.00 0.00

ATOM 3912 CA GLN B 347 -141.160 -4.330 26.082 1.00 0.00

ATOM 3913 C GLN B 347 -142.549 -4.017 25.604 1.00 0.00

ATOM 3914 O GLN B 347 -143.503 -4.306 26.309 1.00 0.00

ATOM 3915 CB GLN B 347 -140.494 -3.023 26.513 1.00 0.00

ATOM 3916 CG GLN B 347 -139.197 -3.212 27.285 1.00 0.00

ATOM 3917 CD GLN B 347 -138.498 -1.899 27.580 1.00 0.00

ATOM 3918 OEl GLN B 347 -138.938 -0.838 27.140 1.00 0.00

ATOM 3919 NE2 GLN B 347 -137.402 -1.970 28.327 1.00 0.00

ATOM 3920 N ARG B 348 -142.652 -3.438 24.392 1.00 0.00

ATOM 3921 CA ARG B 348 -143.965 -3.134 23.848 1.00 0.00

ATOM 3922 C ARG B 348 -144.801 -4.380 23.755 1.00 0.00

ATOM 3923 O ARG B 348 -145.963 -4.352 24.125 1.00 0.00

ATOM 3924 CB ARG B 348 -143.838 -2.533 22.447 1.00 0.00

ATOM 3925 CG ARG B 348 -143.273 -1.122 22.425 1.00 0.00

ATOM 3926 CD ARG B 348 -143.106 -0.616 21.001 1.00 0.00

ATOM 3927 NE ARG B 348 -142.537 0.729 20.961 1.00 0.00

ATOM 3928 CZ ARG B 348 -142.222 1.374 19.844 1.00 0.00

ATOM 3929 NHl ARG B 348 -141.709 2.596 19.905 1.00 0.00

ATOM 3930 NH2 ARG B 348 -142.421 0.797 18.667 1.00 0.00

ATOM 3931 N LEU B 349 -144.188 -5.478 23.266 1.00 0.00

ATOM 3932 CA LEU B 349 -144.928 -6.721 23.143 1.00 0.00

ATOM 3933 C LEU B 349 -145.442 -7.180 24.476 1.00 0.00

ATOM 3934 O LEU B 349 -146.613 -7.504 24.589 1.00 0.00

ATOM 3935 CB LEU B 349 -144.033 -7.824 22.573 1.00 0.00

ATOM 3936 CG LEU B 349 -143.634 -7.682 21.104 1.00 0.00

ATOM 3937 CDl LEU B 349 -142.599 -8.730 20.724 1.00 0.00

ATOM 3938 CD2 LEU B 349 -144.844 -7.859 20.199 1.00 0.00

ATOM 3939 N THR B 350 -144.548 -7.198 25.485 1.00 0.00

ATOM 3940 CA THR B 350 -144.947 -7.673 26.799 1.00 0.00

ATOM 3941 C THR B 350 -146.118 -6.896 27.326 1.00 0.00

ATOM 3942 O THR B 350 -147.072 -7.496 27.798 1.00 0.00

ATOM 3943 CB THR B 350 -143.801 -7.537 27.820 1.00 0.00

ATOM 3944 OGl THR B 350 -142.689 -8.337 27.404 1.00 0.00

ATOM 3945 CG2 THR B 350 -144.257 -8.001 29.195 1.00 0.00

ATOM 3946 N ALA B 351 -146.039 -5.554 27.232 1.00 0.00

ATOM 3947 CA ALA B 351 -147.137 -4.732 27.713 1.00 0.00

ATOM 3948 C ALA B 351 -148.410 -5.098 27.002 1.00 0.00

ATOM 3949 O ALA B 351 -149.438 -5.240 27.646 1.00 0.00

ATOM 3950 CB ALA B 351 -146.847 -3.260 27.462 1.00 0.00

ATOM 3951 N GLU B 352 -148.319 -5.264 25.668 1.00 0.00

ATOM 3952 CA GLU B 352 -149.492 -5.646 24.900 1.00 0.00

ATOM 3953 C GLU B 352 -150.068 -6.934 25.415 1.00 0.00

ATOM 3954 O GLU B 352 -151.273 -7.024 25.593 1.00 0.00

ATOM 3955 CB GLU B 352 -149.129 -5.837 23.426 1.00 0.00

ATOM 3956 CG GLU B 352 -150.308 -6.193 22.537 1.00 0.00

ATOM 3957 CD GLU B 352 -149.916 -6.340 21.080 1.00 0.00

ATOM 3958 OEl GLU B 352 -148.722 -6.151 20.764 1.00 0.00

ATOM 3959 OE2 GLU B 352 -150.802 -6.646 20.254 1.00 0.00

ATOM 3960 N ILE B 353 -149.191 -7.929 25.657 1.00 0.00 ATOM 3961 CA ILE B 353 -149.665 -9.210 26.154 1.00 0.00

ATOM 3962 C ILE B 353 -150.441 -9.027 27.428 1.00 0.00

ATOM 3963 O ILE B 353 -151.513 -9.596 27.558 1.00 0.00

ATOM 3964 CB ILE B 353 -148.497 -10.169 26.446 1.00 0.00

ATOM 3965 CGl ILE B 353 -147.744 -10.502 25.155 1.00 0.00

ATOM 3966 CG2 ILE B 353 -149.011 -11.467 27.052 1.00 0.00

ATOM 3967 CDl ILE B 353 -148.590 -11.211 24.121 1.00 0.00

ATOM 3968 N GLU B 354 -149.893 -8.222 28.360 1.00 0.00

ATOM 3969 CA GLU B 354 -150.585 -7.997 29.617 1.00 0.00

ATOM 3970 C GLU B 354 -151.973 -7.468 29.382 1.00 0.00

ATOM 3971 O GLU B 354 -152.915 -7.990 29.955 1.00 0.00

ATOM 3972 CB GLU B 354 -149.827 -6.980 30.472 1.00 0.00

ATOM 3973 CG GLU B 354 -150.457 -6.717 31.829 1.00 0.00

ATOM 3974 CD GLU B 354 -149.660 -5.731 32.662 1.00 0.00

ATOM 3975 OEl GLU B 354 -148.607 -5.264 32.181 1.00 0.00

ATOM 3976 OE2 GLU B 354 -150.089 -5.427 33.794 1.00 0.00

ATOM 3977 N ASN B 355 -152.089 -6.431 28.529 1.00 0.00

ATOM 3978 CA ASN B 355 -153.399 -5.847 28.289 1.00 0.00

ATOM 3979 C ASN B 355 -154.346 -6.844 27.685 1.00 0.00

ATOM 3980 O ASN B 355 -155.462 -6.971 28.162 1.00 0.00

ATOM 3981 CB ASN B 355 -153.290 -4.663 27.327 1.00 0.00

ATOM 3982 CG ASN B 355 -152.661 -3.443 27.974 1.00 0.00

ATOM 3983 ODl ASN B 355 -152.623 -3.329 29.199 1.00 0.00

ATOM 3984 ND2 ASN B 355 -152.165 -2.528 27.150 1.00 0.00

ATOM 3985 N ALA B 356 -153.891 -7.553 26.633 1.00 0.00

ATOM 3986 CA ALA B 356 -154.760 -8.523 25.986 1.00 0.00

ATOM 3987 C ALA B 356 -155.234 -9.555 26.968 1.00 0.00

ATOM 3988 O ALA B 356 -156.403 -9.911 26.951 1.00 0.00

ATOM 3989 CB ALA B 356 -154.018 -9.236 24.865 1.00 0.00

ATOM 3990 N LYS B 357 -154.315 -10.024 27.834 1.00 0.00

ATOM 3991 CA LYS B 357 -154.694 -11.034 28.803 1.00 0.00

ATOM 3992 C LYS B 357 -155.757 -10.515 29.730 1.00 0.00

ATOM 3993 O LYS B 357 -156.737 -11.209 29.956 1.00 0.00

ATOM 3994 CB LYS B 357 -153.485 -11.448 29.645 1.00 0.00

ATOM 3995 CG LYS B 357 -153.782 -12.537 30.664 1.00 0.00

ATOM 3996 CD LYS B 357 -152.527 -12.948 31.414 1.00 0.00

ATOM 3997 CE LYS B 357 -152.832 -14.002 32.467 1.00 0.00

ATOM 3998 NZ LYS B 357 -151.614 -14.398 33.226 1.00 0.00

ATOM 3999 N CYS B 358 -155.564 -9.291 30.260 1.00 0.00

ATOM 4000 CA CYS B 358 -156.559 -8.747 31.171 1.00 0.00

ATOM 4001 C CYS B 358 -157.884 -8.590 30.482 1.00 0.00

ATOM 4002 O CYS B 358 -158.907 -8.916 31.063 1.00 0.00

ATOM 4003 CB CYS B 358 -156.120 -7.375 31.686 1.00 0.00

ATOM 4004 SG CYS B 358 -154.698 -7.415 32.801 1.00 0.00

ATOM 4005 N GLN B 359 -157.851 -8.095 29.229 1.00 0.00

ATOM 4006 CA GLN B 359 -159.088 -7.933 28.485 1.00 0.00

ATOM 4007 C GLN B 359 -159.778 -9.258 28.323 1.00 0.00

ATOM 4008 O GLN B 359 -160.976 -9.345 28.542 1.00 0.00

ATOM 4009 CB GLN B 359 -158.806 -7.360 27.094 1.00 0.00

ATOM 4010 CG GLN B 359 -158.367 -5.904 27.101 1.00 0.00

ATOM 4011 CD GLN B 359 -157.970 -5.410 25.723 1.00 0.00

ATOM 4012 OEl GLN B 359 -157.944 -6.178 24.761 1.00 0.00

ATOM 4013 NE2 GLN B 359 -157.658 -4.124 25.625 1.00 0.00

ATOM 4014 N ARG B 360 -158.998 -10.291 27.949 1.00 0.00

ATOM 4015 CA ARG B 360 -159.582 -11.606 27.761 1.00 0.00

ATOM 4016 C ARG B 360 -160.211 -12.095 29.036 1.00 0.00

ATOM 4017 O ARG B 360 -161.299 -12.645 28.989 1.00 0.00

ATOM 4018 CB ARG B 360 -158.510 -12.612 27.335 1.00 0.00

ATOM 4019 CG ARG B 360 -159.049 -14.001 27.033 1.00 0.00

ATOM 4020 CD ARG B 360 -157.931 -14.954 26.644 1.00 0.00

ATOM 4021 NE ARG B 360 -156.996 -15.180 27.745 1.00 0.00

ATOM 4022 CZ ARG B 360 -157.232 -15.992 28.770 1.00 0.00

ATOM 4023 NHl ARG B 360 -156.324 -16.136 29.725 1.00 0.00

ATOM 4024 NH2 ARG B 360 -158.376 -16.660 28.837 1.00 0.00

ATOM 4025 N ALA B 361 -159.522 -11.877 30.175 1.00 0.00

ATOM 4026 CA ALA B 361 -160.077 -12.311 31.445 1.00 0.00

ATOM 4027 C ALA B 361 -161.430 -11.695 31.665 1.00 0.00

ATOM 4028 O ALA B 361 -162.360 -12.398 32.027 1.00 0.00 ATOM 4029 CB ALA B 361 -159.167 -11.898 32.591 1.00 0.00

ATOM 4030 N LYS B 362 -161.530 -10.372 31.429 1.00 0.00

ATOM 4031 CA LYS B 362 -162.806 -9.703 31.613 1.00 0.00

ATOM 4032 C LYS B 362 -163.849 -10.283 30.700 1.00 0.00

ATOM 4033 O LYS B 362 -164.942 -10.583 31.153 1.00 0.00

ATOM 4034 CB LYS B 362 -162.677 -8.210 31.306 1.00 0.00

ATOM 4035 CG LYS B 362 -163.959 -7.421 31.512 1.00 0.00

ATOM 4036 CD LYS B 362 -163.743 -5.938 31.258 1.00 0.00

ATOM 4037 CE LYS B 362 -165.036 -5.155 31.417 1.00 0.00

ATOM 4038 NZ LYS B 362 -164.843 -3.704 31.148 1.00 0.00

ATOM 4039 N LEU B 363 -163.498 -10.446 29.409 1.00 0.00

ATOM 4040 CA LEU B 363 -164.456 -10.990 28.461 1.00 0.00

ATOM 4041 C LEU B 363 -164.962 -12.327 28.928 1.00 0.00

ATOM 4042 O LEU B 363 -166.145 -12.605 28.817 1.00 0.00

ATOM 4043 CB LEU B 363 -163.807 -11.173 27.088 1.00 0.00

ATOM 4044 CG LEU B 363 -163.456 -9.892 26.328 1.00 0.00

ATOM 4045 CDl LEU B 363 -162.659 -10.213 25.072 1.00 0.00

ATOM 4046 CD2 LEU B 363 -164.718 -9.151 25.913 1.00 0.00

ATOM 4047 N GLU B 364 -164.042 -13.145 29.471 1.00 0.00

ATOM 4048 CA GLU B 364 -164.439 -14.460 29.934 1.00 0.00

ATOM 4049 C GLU B 364 -165.331 -14.362 31.139 1.00 0.00

ATOM 4050 O GLU B 364 -166.248 -15.160 31.254 1.00 0.00

ATOM 4051 CB GLU B 364 -163.210 -15.287 30.317 1.00 0.00

ATOM 4052 CG GLU B 364 -162.352 -15.709 29.135 1.00 0.00

ATOM 4053 CD GLU B 364 -161.082 -16.419 29.561 1.00 0.00

ATOM 4054 OEl GLU B 364 -160.836 -16.517 30.782 1.00 0.00

ATOM 4055 OE2 GLU B 364 -160.331 -16.876 28.673 1.00 0.00

ATOM 4056 N ALA B 365 -165.081 -13.385 32.034 1.00 0.00

ATOM 4057 CA ALA B 365 -165.978 -13.220 33.167 1.00 0.00

ATOM 4058 C ALA B 365 -167.365 -12.923 32.670 1.00 0.00

ATOM 4059 O ALA B 365 -168.329 -13.506 33.143 1.00 0.00

ATOM 4060 CB ALA B 365 -165.512 -12.073 34.050 1.00 0.00

ATOM 4061 N ALA B 366 -167.441 -12.010 31.682 1.00 0.00

ATOM 4062 CA ALA B 366 -168.722 -11.718 31.063 1.00 0.00

ATOM 4063 C ALA B 366 -169.298 -12.958 30.439 1.00 0.00

ATOM 4064 O ALA B 366 -170.511 -13.085 30.386 1.00 0.00

ATOM 4065 CB ALA B 366 -168.560 -10.663 29.980 1.00 0.00

ATOM 4066 N VAL B 367 -168.415 -13.874 29.984 1.00 0.00

ATOM 4067 CA VAL B 367 -168.890 -15.124 29.411 1.00 0.00

ATOM 4068 C VAL B 367 -169.621 -15.909 30.465 1.00 0.00

ATOM 4069 O VAL B 367 -170.785 -16.227 30.271 1.00 0.00

ATOM 4070 CB VAL B 367 -167.724 -15.981 28.883 1.00 0.00

ATOM 4071 CGl VAL B 367 -168.222 -17.353 28.455 1.00 0.00

ATOM 4072 CG2 VAL B 367 -167.071 -15.311 27.684 1.00 0.00

ATOM 4073 N ALA B 368 -168.925 -16.219 31.576 1.00 0.00

ATOM 4074 CA ALA B 368 -169.529 -17.057 32.597 1.00 0.00

ATOM 4075 C ALA B 368 -170.793 -16.442 33.126 1.00 0.00

ATOM 4076 O ALA B 368 -171.810 -17.113 33.175 1.00 0.00

ATOM 4077 CB ALA B 368 -168.571 -17.245 33.763 1.00 0.00

ATOM 4078 N GLU B 369 -170.719 -15.152 33.508 1.00 0.00

ATOM 4079 CA GLU B 369 -171.902 -14.488 34.028 1.00 0.00

ATOM 4080 C GLU B 369 -173.030 -14.572 33.041 1.00 0.00

ATOM 4081 O GLU B 369 -174.150 -14.857 33.435 1.00 0.00

ATOM 4082 CB GLU B 369 -171.611 -13.012 34.303 1.00 0.00

ATOM 4083 CG GLU B 369 -170.691 -12.771 35.489 1.00 0.00

ATOM 4084 CD GLU B 369 -170.327 -11.309 35.657 1.00 0.00

ATOM 4085 OEl GLU B 369 -170.732 -10.494 34.802 1.00 0.00

ATOM 4086 OE2 GLU B 369 -169.635 -10.978 36.642 1.00 0.00

ATOM 4087 N ALA B 370 -172.718 -14.331 31.753 1.00 0.00

ATOM 4088 CA ALA B 370 -173.759 -14.365 30.740 1.00 0.00

ATOM 4089 C ALA B 370 -174.404 -15.720 30.665 1.00 0.00

ATOM 4090 O ALA B 370 -175.616 -15.807 30.763 1.00 0.00

ATOM 4091 CB ALA B 370 -173.178 -14.044 29.372 1.00 0.00

ATOM 4092 N GLU B 371 -173.581 -16.775 30.493 1.00 0.00

ATOM 4093 CA GLU B 371 -174.140 -18.111 30.368 1.00 0.00

ATOM 4094 C GLU B 371 -174.962 -18.467 31.574 1.00 0.00

ATOM 4095 O GLU B 371 -176.049 -19.002 31.423 1.00 0.00

ATOM 4096 CB GLU B 371 -173.024 -19.148 30.230 1.00 0.00 ATOM 4097 CG GLU B 371 -172.291 -19.097 28.899 1.00 0.00

ATOM 4098 CD GLU B 371 -171.115 -20.053 28.844 1.00 0.00

ATOM 4099 OEl GLU B 371 -170.828 -20.700 29.872 1.00 0.00

ATOM 4100 OE2 GLU B 371 -170.481 -20.153 27.772 1.00 0.00

ATOM 4101 N GLN B 372 -174.435 -18.150 32.773 1.00 0.00

ATOM 4102 CA GLN B 372 -175.170 -18.459 33.988 1.00 0.00

ATOM 4103 C GLN B 372 -176.503 -17.764 34.001 1.00 0.00

ATOM 4104 O GLN B 372 -177.510 -18.400 34.264 1.00 0.00

ATOM 4105 CB GLN B 372 -174.383 -18.007 35.220 1.00 0.00

ATOM 4106 CG GLN B 372 -173.142 -18.837 35.503 1.00 0.00

ATOM 4107 CD GLN B 372 -172.317 -18.281 36.646 1.00 0.00

ATOM 4108 OEl GLN B 372 -172.627 -17.221 37.189 1.00 0.00

ATOM 4109 NE2 GLN B 372 -171.262 -18.998 37.016 1.00 0.00

ATOM 4110 N GLN B 373 -176.488 -16.448 33.714 1.00 0.00

ATOM 4111 CA GLN B 373 -177.721 -15.681 33.778 1.00 0.00

ATOM 4112 C GLN B 373 -178.752 -16.203 32.818 1.00 0.00

ATOM 4113 O GLN B 373 -179.883 -16.420 33.220 1.00 0.00

ATOM 4114 CB GLN B 373 -177.458 -14.215 33.429 1.00 0.00

ATOM 4115 CG GLN B 373 -176.678 -13.455 34.489 1.00 0.00

ATOM 4116 CD GLN B 373 -176.321 -12.047 34.051 1.00 0.00

ATOM 4117 OEl GLN B 373 -176.588 -11.652 32.917 1.00 0.00

ATOM 4118 NE2 GLN B 373 -175.715 -11.285 34.954 1.00 0.00

ATOM 4119 N GLY B 374 -178.352 -16.404 31.545 1.00 0.00

ATOM 4120 CA GLY B 374 -179.315 -16.863 30.558 1.00 0.00

ATOM 4121 C GLY B 374 -179.927 -18.176 30.957 1.00 0.00

ATOM 4122 O GLY B 374 -181.108 -18.380 30.724 1.00 0.00

ATOM 4123 N GLU B 375 -179.118 -19.061 31.572 1.00 0.00

ATOM 4124 CA GLU B 375 -179.652 -20.344 31.996 1.00 0.00

ATOM 4125 C GLU B 375 -180.738 -20.156 33.018 1.00 0.00

ATOM 4126 O GLU B 375 -181.783 -20.778 32.908 1.00 0.00

ATOM 4127 CB GLU B 375 -178.550 -21.204 32.619 1.00 0.00

ATOM 4128 CG GLU B 375 -179.012 -22.586 33.051 1.00 0.00

ATOM 4129 CD GLU B 375 -177.887 -23.420 33.631 1.00 0.00

ATOM 4130 OEl GLU B 375 -176.742 -22.922 33.682 1.00 0.00

ATOM 4131 OE2 GLU B 375 -178.149 -24.573 34.034 1.00 0.00

ATOM 4132 N ALA B 376 -180.480 -19.282 34.011 1.00 0.00

ATOM 4133 CA ALA B 376 -181.465 -19.067 35.058 1.00 0.00

ATOM 4134 C ALA B 376 -182.744 -18.513 34.498 1.00 0.00

ATOM 4135 O ALA B 376 -183.809 -19.032 34.798 1.00 0.00

ATOM 4136 CB ALA B 376 -180.936 -18.081 36.089 1.00 0.00

ATOM 4137 N ALA B 377 -182.625 -17.448 33.683 1.00 0.00

ATOM 4138 CA ALA B 377 -183.817 -16.793 33.172 1.00 0.00

ATOM 4139 C ALA B 377 -184.622 -17.708 32.293 1.00 0.00

ATOM 4140 O ALA B 377 -185.834 -17.748 32.431 1.00 0.00

ATOM 4141 CB ALA B 377 -183.439 -15.572 32.349 1.00 0.00

ATOM 4142 N LEU B 378 -183.944 -18.453 31.397 1.00 0.00

ATOM 4143 CA LEU B 378 -184.667 -19.379 30.541 1.00 0.00

ATOM 4144 C LEU B 378 -185.414 -20.377 31.383 1.00 0.00

ATOM 4145 O LEU B 378 -186.544 -20.710 31.062 1.00 0.00

ATOM 4146 CB LEU B 378 -183.699 -20.133 29.628 1.00 0.00

ATOM 4147 CG LEU B 378 -183.022 -19.309 28.530 1.00 0.00

ATOM 4148 CDl LEU B 378 -181.958 -20.132 27.819 1.00 0.00

ATOM 4149 CD2 LEU B 378 -184.039 -18.853 27.496 1.00 0.00

ATOM 4150 N SER B 379 -184.772 -20.834 32.478 1.00 0.00

ATOM 4151 CA SER B 379 -185.440 -21.767 33.368 1.00 0.00

ATOM 4152 C SER B 379 -186.713 -21.170 33.902 1.00 0.00

ATOM 4153 O SER B 379 -187.743 -21.822 33.864 1.00 0.00

ATOM 4154 CB SER B 379 -184.538 -22.117 34.553 1.00 0.00

ATOM 4155 OG SER B 379 -183.399 -22.847 34.129 1.00 0.00

ATOM 4156 N ASP B 380 -186.630 -19.919 34.397 1.00 0.00

ATOM 4157 CA ASP B 380 -187.810 -19.295 34.969 1.00 0.00

ATOM 4158 C ASP B 380 -188.903 -19.138 33.951 1.00 0.00

ATOM 4159 O ASP B 380 -190.038 -19.479 34.245 1.00 0.00

ATOM 4160 CB ASP B 380 -187.471 -17.904 35.510 1.00 0.00

ATOM 4161 CG ASP B 380 -186.646 -17.959 36.781 1.00 0.00

ATOM 4162 ODl ASP B 380 -186.539 -19.052 37.373 1.00 0.00

ATOM 4163 OD2 ASP B 380 -186.108 -16.906 37.185 1.00 0.00

ATOM 4164 N ALA B 381 -188.555 -18.628 32.752 1.00 0.00 ATOM 4165 CA ALA B 381 -189.565 -18.456 31.723 1.00 0.00

ATOM 4166 C ALA B 381 -190.251 -19.762 31.434 1.00 0.00

ATOM 4167 O ALA B 381 -191.470 -19.807 31.386 1.00 0.00

ATOM 4168 CB ALA B 381 -188.930 -17.951 30.436 1.00 0.00

ATOM 4169 N ARG B 382 -189.442 -20.824 31.259 1.00 0.00

ATOM 4170 CA ARG B 382 -190.008 -22.130 30.968 1.00 0.00

ATOM 4171 C ARG B 382 -190.934 -22.582 32.060 1.00 0.00

ATOM 4172 O ARG B 382 -192.019 -23.058 31.766 1.00 0.00

ATOM 4173 CB ARG B 382 -188.900 -23.174 30.826 1.00 0.00

ATOM 4174 CG ARG B 382 -188.058 -23.020 29.569 1.00 0.00

ATOM 4175 CD ARG B 382 -186.951 -24.060 29.516 1.00 0.00

ATOM 4176 NE ARG B 382 -186.102 -23.895 28.338 1.00 0.00

ATOM 4177 CZ ARG B 382 -185.029 -24.636 28.081 1.00 0.00

ATOM 4178 NHl ARG B 382 -184.318 -24.414 26.984 1.00 0.00

ATOM 4179 NH2 ARG B 382 -184.671 -25.598 28.920 1.00 0.00

ATOM 4180 N CYS B 383 -190.505 -22.425 33.327 1.00 0.00

ATOM 4181 CA CYS B 383 -191.355 -22.848 34.426 1.00 0.00

ATOM 4182 C CYS B 383 -192.657 -22.095 34.431 1.00 0.00

ATOM 4183 O CYS B 383 -193.702 -22.701 34.607 1.00 0.00

ATOM 4184 CB CYS B 383 -190.662 -22.599 35.767 1.00 0.00

ATOM 4185 SG CYS B 383 -189.235 -23.666 36.078 1.00 0.00

ATOM 4186 N LYS B 384 -192.578 -20.765 34.232 1.00 0.00

ATOM 4187 CA LYS B 384 -193.780 -19.949 34.289 1.00 0.00

ATOM 4188 C LYS B 384 -194.784 -20.377 33.257 1.00 0.00

ATOM 4189 O LYS B 384 -195.888 -20.755 33.614 1.00 0.00

ATOM 4190 CB LYS B 384 -193.443 -18.478 34.037 1.00 0.00

ATOM 4191 CG LYS B 384 -194.645 -17.549 34.080 1.00 0.00

ATOM 4192 CD LYS B 384 -194.233 -16.103 33.859 1.00 0.00

ATOM 4193 CE LYS B 384 -195.437 -15.176 33.885 1.00 0.00

ATOM 4194 NZ LYS B 384 -195.053 -13.758 33.638 1.00 0.00

ATOM 4195 N LEU B 385 -194.387 -20.307 31.971 1.00 0.00

ATOM 4196 CA LEU B 385 -195.307 -20.681 30.909 1.00 0.00

ATOM 4197 C LEU B 385 -195.861 -22.061 31.129 1.00 0.00

ATOM 4198 O LEU B 385 -196.994 -22.323 30.757 1.00 0.00

ATOM 4199 CB LEU B 385 -194.596 -20.667 29.555 1.00 0.00

ATOM 4200 CG LEU B 385 -195.467 -20.954 28.329 1.00 0.00

ATOM 4201 CDl LEU B 385 -196.555 -19.902 28.185 1.00 0.00

ATOM 4202 CD2 LEU B 385 -194.628 -20.946 27.060 1.00 0.00

ATOM 4203 N ALA B 386 -195.049 -22.935 31.757 1.00 0.00

ATOM 4204 CA ALA B 386 -195.498 -24.291 32.002 1.00 0.00

ATOM 4205 C ALA B 386 -196.713 -24.309 32.889 1.00 0.00

ATOM 4206 O ALA B 386 -197.751 -24.795 32.471 1.00 0.00

ATOM 4207 CB ALA B 386 -194.403 -25.097 32.684 1.00 0.00

ATOM 4208 N GLU B 387 -196.568 -23.773 34.119 1.00 0.00

ATOM 4209 CA GLU B 387 -197.687 -23.791 35.049 1.00 0.00

ATOM 4210 C GLU B 387 -198.886 -23.096 34.471 1.00 0.00

ATOM 4211 O GLU B 387 -200.002 -23.540 34.695 1.00 0.00

ATOM 4212 CB GLU B 387 -197.311 -23.084 36.352 1.00 0.00

ATOM 4213 CG GLU B 387 -196.309 -23.845 37.206 1.00 0.00

ATOM 4214 CD GLU B 387 -195.869 -23.060 38.426 1.00 0.00

ATOM 4215 OEl GLU B 387 -196.289 -21.893 38.565 1.00 0.00

ATOM 4216 OE2 GLU B 387 -195.103 -23.613 39.242 1.00 0.00

ATOM 4217 N LEU B 388 -198.643 -22.006 33.717 1.00 0.00

ATOM 4218 CA LEU B 388 -199.751 -21.251 33.161 1.00 0.00

ATOM 4219 C LEU B 388 -200.569 -22.071 32.202 1.00 0.00

ATOM 4220 O LEU B 388 -201.787 -22.045 32.289 1.00 0.00

ATOM 4221 CB LEU B 388 -199.238 -20.026 32.402 1.00 0.00

ATOM 4222 CG LEU B 388 -198.638 -18.905 33.251 1.00 0.00

ATOM 4223 CDl LEU B 388 -197.998 -17.844 32.369 1.00 0.00

ATOM 4224 CD2 LEU B 388 -199.713 -18.235 34.095 1.00 0.00

ATOM 4225 N GLU B 389 -199.894 -22.807 31.295 1.00 0.00

ATOM 4226 CA GLU B 389 -200.635 -23.637 30.358 1.00 0.00

ATOM 4227 C GLU B 389 -201.482 -24.634 31.099 1.00 0.00

ATOM 4228 O GLU B 389 -202.614 -24.874 30.708 1.00 0.00

ATOM 4229 CB GLU B 389 -199.675 -24.400 29.443 1.00 0.00

ATOM 4230 CG GLU B 389 -198.954 -23.525 28.431 1.00 0.00

ATOM 4231 CD GLU B 389 -197.924 -24.292 27.627 1.00 0.00

ATOM 4232 OEl GLU B 389 -197.720 -25.490 27.912 1.00 0.00 ATOM 4233 OE2 GLU B 389 -197.319 -23.694 26.711 1.00 0.00

ATOM 4234 N GLY B 390 -200.923 -25.195 32.190 1.00 0.00

ATOM 4235 CA GLY B 390 -201.688 -26.140 32.984 1.00 0.00

ATOM 4236 C GLY B 390 -202.924 -25.484 33.533 1.00 0.00

ATOM 4237 O GLY B 390 -203.996 -26.062 33.458 1.00 0.00

ATOM 4238 N ALA B 391 -202.759 -24.263 34.079 1.00 0.00

ATOM 4239 CA ALA B 391 -203.905 -23.553 34.624 1.00 0.00

ATOM 4240 C ALA B 391 -204.955 -23.343 33.570 1.00 0.00

ATOM 4241 O ALA B 391 -206.128 -23.533 33.848 1.00 0.00

ATOM 4242 CB ALA B 391 -203.483 -22.192 35.154 1.00 0.00

ATOM 4243 N LEU B 392 -204.518 -22.959 32.353 1.00 0.00

ATOM 4244 CA LEU B 392 -205.471 -22.751 31.276 1.00 0.00

ATOM 4245 C LEU B 392 -206.264 -24.002 31.016 1.00 0.00

ATOM 4246 O LEU B 392 -207.466 -23.918 30.816 1.00 0.00

ATOM 4247 CB LEU B 392 -204.746 -22.365 29.985 1.00 0.00

ATOM 4248 CG LEU B 392 -204.092 -20.983 29.963 1.00 0.00

ATOM 4249 CDl LEU B 392 -203.259 -20.803 28.702 1.00 0.00

ATOM 4250 CD2 LEU B 392 -205.146 -19.888 29.995 1.00 0.00

ATOM 4251 N GLN B 393 -205.583 -25.165 31.043 1.00 0.00

ATOM 4252 CA GLN B 393 -206.290 -26.421 30.850 1.00 0.00

ATOM 4253 C GLN B 393 -207.382 -26.570 31.872 1.00 0.00

ATOM 4254 O GLN B 393 -208.485 -26.962 31.527 1.00 0.00

ATOM 4255 CB GLN B 393 -205.330 -27.603 30.990 1.00 0.00

ATOM 4256 CG GLN B 393 -204.336 -27.735 29.847 1.00 0.00

ATOM 4257 CD GLN B 393 -203.330 -28.846 30.075 1.00 0.00

ATOM 4258 OEl GLN B 393 -203.311 -29.472 31.135 1.00 0.00

ATOM 4259 NE2 GLN B 393 -202.489 -29.095 29.078 1.00 0.00

ATOM 4260 N LYS B 394 -207.057 -26.239 33.138 1.00 0.00

ATOM 4261 CA LYS B 394 -208.042 -26.374 34.196 1.00 0.00

ATOM 4262 C LYS B 394 -209.230 -25.485 33.956 1.00 0.00

ATOM 4263 O LYS B 394 -210.353 -25.947 34.073 1.00 0.00

ATOM 4264 CB LYS B 394 -207.433 -25.994 35.548 1.00 0.00

ATOM 4265 CG LYS B 394 -208.385 -26.145 36.723 1.00 0.00

ATOM 4266 CD LYS B 394 -207.696 -25.819 38.037 1.00 0.00

ATOM 4267 CE LYS B 394 -208.661 -25.923 39.207 1.00 0.00

ATOM 4268 NZ LYS B 394 -208.005 -25.584 40.500 1.00 0.00

ATOM 4269 N ALA B 395 -208.970 -24.205 33.620 1.00 0.00

ATOM 4270 CA ALA B 395 -210.068 -23.275 33.416 1.00 0.00

ATOM 4271 C ALA B 395 -210.988 -23.759 32.331 1.00 0.00

ATOM 4272 O ALA B 395 -212.195 -23.695 32.492 1.00 0.00

ATOM 4273 CB ALA B 395 -209.537 -21.907 33.013 1.00 0.00

ATOM 4274 N LYS B 396 -210.397 -24.260 31.229 1.00 0.00

ATOM 4275 CA LYS B 396 -211.218 -24.789 30.152 1.00 0.00

ATOM 4276 C LYS B 396 -212.088 -25.905 30.661 1.00 0.00

ATOM 4277 O LYS B 396 -213.254 -25.970 30.307 1.00 0.00

ATOM 4278 CB LYS B 396 -210.338 -25.334 29.025 1.00 0.00

ATOM 4279 CG LYS B 396 -209.605 -24.261 28.237 1.00 0.00

ATOM 4280 CD LYS B 396 -208.753 -24.870 27.135 1.00 0.00

ATOM 4281 CE LYS B 396 -208.001 -23.799 26.362 1.00 0.00

ATOM 4282 NZ LYS B 396 -207.136 -24.383 25.301 1.00 0.00

ATOM 4283 N GLN B 397 -211.501 -26.774 31.508 1.00 0.00

ATOM 4284 CA GLN B 397 -212.259 -27.898 32.028 1.00 0.00

ATOM 4285 C GLN B 397 -213.408 -27.431 32.876 1.00 0.00

ATOM 4286 O GLN B 397 -214.528 -27.864 32.657 1.00 0.00

ATOM 4287 CB GLN B 397 -211.365 -28.793 32.890 1.00 0.00

ATOM 4288 CG GLN B 397 -210.330 -29.579 32.103 1.00 0.00

ATOM 4289 CD GLN B 397 -209.380 -30.350 32.997 1.00 0.00

ATOM 4290 OEl GLN B 397 -209.439 -30.241 34.222 1.00 0.00

ATOM 4291 NE2 GLN B 397 -208.498 -31.134 32.387 1.00 0.00

ATOM 4292 N ASP B 398 -213.119 -26.540 33.845 1.00 0.00

ATOM 4293 CA ASP B 398 -214.177 -26.064 34.721 1.00 0.00

ATOM 4294 C ASP B 398 -215.269 -25.405 33.930 1.00 0.00

ATOM 4295 O ASP B 398 -216.435 -25.627 34.214 1.00 0.00

ATOM 4296 CB ASP B 398 -213.627 -25.043 35.720 1.00 0.00

ATOM 4297 CG ASP B 398 -212.771 -25.684 36.795 1.00 0.00

ATOM 4298 ODl ASP B 398 -212.792 -26.926 36.910 1.00 0.00

ATOM 4299 OD2 ASP B 398 -212.077 -24.941 37.522 1.00 0.00

ATOM 4300 N MET B 399 -214.873 -24.599 32.926 1.00 0.00 ATOM 4301 CA MET B 399 -215.862 -23.932 32.098 1.00 0.00

ATOM 4302 C MET B 399 -216.760 -24.937 31.432 1.00 0.00

ATOM 4303 O MET B 399 -217.967 -24.757 31.441 1.00 0.00

ATOM 4304 CB MET B 399 -215.178 -23.102 31.009 1.00 0.00

ATOM 4305 CG MET B 399 -216.143 -22.383 30.079 1.00 0.00

ATOM 4306 SD MET B 399 -215.300 -21.474 28.771 1.00 0.00

ATOM 4307 CE MET B 399 -214.730 -22.819 27.735 1.00 0.00

ATOM 4308 N ALA B 400 -216.157 -25.999 30.862 1.00 0.00

ATOM 4309 CA ALA B 400 -216.957 -27.013 30.195 1.00 0.00

ATOM 4310 C ALA B 400 -217.965 -27.600 31.141 1.00 0.00

ATOM 4311 O ALA B 400 -219.122 -27.737 30.776 1.00 0.00

ATOM 4312 CB ALA B 400 -216.069 -28.136 29.681 1.00 0.00

ATOM 4313 N CYS B 401 -217.513 -27.935 32.366 1.00 0.00

ATOM 4314 CA CYS B 401 -218.431 -28.485 33.346 1.00 0.00

ATOM 4315 C CYS B 401 -219.561 -27.529 33.600 1.00 0.00

ATOM 4316 O CYS B 401 -220.706 -27.949 33.646 1.00 0.00

ATOM 4317 CB CYS B 401 -217.709 -28.745 34.670 1.00 0.00

ATOM 4318 SG CYS B 401 -216.506 -30.092 34.613 1.00 0.00

ATOM 4319 N LEU B 402 -219.225 -26.232 33.751 1.00 0.00

ATOM 4320 CA LEU B 402 -220.260 -25.244 34.004 1.00 0.00

ATOM 4321 C LEU B 402 -221.252 -25.202 32.878 1.00 0.00

ATOM 4322 O LEU B 402 -222.445 -25.219 33.134 1.00 0.00

ATOM 4323 CB LEU B 402 -219.647 -23.850 34.151 1.00 0.00

ATOM 4324 CG LEU B 402 -218.820 -23.603 35.414 1.00 0.00

ATOM 4325 CDl LEU B 402 -218.116 -22.256 35.342 1.00 0.00

ATOM 4326 CD2 LEU B 402 -219.709 -23.608 36.648 1.00 0.00

ATOM 4327 N LEU B 403 -220.748 -25.159 31.630 1.00 0.00

ATOM 4328 CA LEU B 403 -221.644 -25.097 30.487 1.00 0.00

ATOM 4329 C LEU B 403 -222.588 -26.264 30.472 1.00 0.00

ATOM 4330 O LEU B 403 -223.777 -26.071 30.265 1.00 0.00

ATOM 4331 CB LEU B 403 -220.848 -25.114 29.181 1.00 0.00

ATOM 4332 CG LEU B 403 -221.665 -25.070 27.889 1.00 0.00

ATOM 4333 CDl LEU B 403 -222.474 -23.784 27.808 1.00 0.00

ATOM 4334 CD2 LEU B 403 -220.754 -25.135 26.672 1.00 0.00

ATOM 4335 N LYS B 404 -222.049 -27.476 30.705 1.00 0.00

ATOM 4336 CA LYS B 404 -222.904 -28.652 30.720 1.00 0.00

ATOM 4337 C LYS B 404 -223.968 -28.508 31.771 1.00 0.00

ATOM 4338 O LYS B 404 -225.125 -28.781 31.494 1.00 0.00

ATOM 4339 CB LYS B 404 -222.084 -29.907 31.027 1.00 0.00

ATOM 4340 CG LYS B 404 -222.893 -31.193 31.023 1.00 0.00

ATOM 4341 CD LYS B 404 -222.006 -32.404 31.264 1.00 0.00

ATOM 4342 CE LYS B 404 -222.821 -33.685 31.308 1.00 0.00

ATOM 4343 NZ LYS B 404 -221.968 -34.878 31.568 1.00 0.00

ATOM 4344 N GLU B 405 -223.562 -28.062 32.978 1.00 0.00

ATOM 4345 CA GLU B 405 -224.529 -27.873 34.046 1.00 0.00

ATOM 4346 C GLU B 405 -225.616 -26.934 33.605 1.00 0.00

ATOM 4347 O GLU B 405 -226.783 -27.218 33.812 1.00 0.00

ATOM 4348 CB GLU B 405 -223.851 -27.283 35.285 1.00 0.00

ATOM 4349 CG GLU B 405 -222 925 -28.251 36.005 1.00 0.00

ATOM 4350 CD GLU B 405 -222.167 -27.594 37.142 1.00 0.00

ATOM 4351 OEl GLU B 405 -222.304 -26.365 37.315 1.00 0.00

ATOM 4352 OE2 GLU B 405 -221.437 -28.309 37.860 1.00 0.00

ATOM 4353 N TYR B 406 -225.198 -25.812 32.985 1.00 0.00

ATOM 4354 CA TYR B 406 -226.159 -24.821 32.539 1.00 0.00

ATOM 4355 C TYR B 406 -227.187 -25.432 31.627 1.00 0.00

ATOM 4356 O TYR B 406 -228.368 -25.182 31.810 1.00 0.00

ATOM 4357 CB TYR B 406 -225.454 -23.697 31.774 1.00 0.00

ATOM 4358 CG TYR B 406 -226.392 -22.640 31.237 1.00 0.00

ATOM 4359 CDl TYR B 406 -226.886 -21.642 32.067 1.00 0.00

ATOM 4360 CD2 TYR B 406 -226.781 -22.644 29.904 1.00 0.00

ATOM 4361 CEl TYR B 406 -227.744 -20.670 31.585 1.00 0.00

ATOM 4362 CE2 TYR B 406 -227.637 -21.682 29.405 1.00 0.00

ATOM 4363 CZ TYR B 406 -228.119 -20.690 30.259 1.00 0.00

ATOM 4364 OH TYR B 406 -228.973 -19.725 29.777 1.00 0.00

ATOM 4365 N GLN B 407 -226.726 -26.239 30.652 1.00 0.00

ATOM 4366 CA GLN B 407 -227.663 -26.873 29.737 1.00 0.00

ATOM 4367 C GLN B 407 -228.666 -27.698 30.493 1.00 0.00

ATOM 4368 O GLN B 407 -229.854 -27.591 30.237 1.00 0.00 ATOM 4369 CB GLN B 407 -226.923 -27.791 28.762 1.00 0.00

ATOM 4370 CG GLN B 407 -226.082 -27.053 27.732 1.00 0.00

ATOM 4371 CD GLN B 407 -225.261 -27.991 26.870 1.00 0.00

ATOM 4372 OEl GLN B 407 -225.253 -29.203 27.088 1.00 0.00

ATOM 4373 NE2 GLN B 407 -224.566 -27.432 25.885 1.00 0.00

ATOM 4374 N GLU B 408 -228.159 -28.518 31.436 1.00 0.00

ATOM 4375 CA GLU B 408 -229.042 -29.379 32.202 1.00 0.00

ATOM 4376 C GLU B 408 -230.068 -28.576 32.951 1.00 0.00

ATOM 4377 O GLU B 408 -231.252 -28.846 32.816 1.00 0.00

ATOM 4378 CB GLU B 408 -228.243 -30.196 33.220 1.00 0.00

ATOM 4379 CG GLU B 408 -229.085 -31.162 34.038 1.00 0.00

ATOM 4380 CD GLU B 408 -228.256 -31.977 35.010 1.00 0.00

ATOM 4381 OEl GLU B 408 -227.020 -31.797 35.035 1.00 0.00

ATOM 4382 OE2 GLU B 408 -228.841 -32.798 35.748 1.00 0.00

ATOM 4383 N VAL B 409 -229.599 -27.590 33.740 1.00 0.00

ATOM 4384 CA VAL B 409 -230.522 -26.794 34.535 1.00 0.00

ATOM 4385 C VAL B 409 -231.575 -26.159 33.674 1.00 0.00

ATOM 4386 O VAL B 409 -232.737 -26.164 34.047 1.00 0.00

ATOM 4387 CB VAL B 409 -229.792 -25.663 35.283 1.00 0.00

ATOM 4388 CGl VAL B 409 -230.794 -24.728 35.943 1.00 0.00

ATOM 4389 CG2 VAL B 409 -228.886 -26.235 36.361 1.00 0.00

ATOM 4390 N MET B 410 -231.157 -25.619 32.513 1.00 0.00

ATOM 4391 CA MET B 410 -232.121 -24.974 31.637 1.00 0.00

ATOM 4392 C MET B 410 -233.165 -25.951 31.171 1.00 0.00

ATOM 4393 O MET B 410 -234.340 -25.624 31.195 1.00 0.00

ATOM 4394 CB MET B 410 -231.423 -24.399 30.404 1.00 0.00

ATOM 4395 CG MET B 410 -230.553 -23.186 30.692 1.00 0.00

ATOM 4396 SD MET B 410 -231.497 -21.785 31.320 1.00 0.00

ATOM 4397 CE MET B 410 -232.447 -21.338 29.869 1.00 0.00

ATOM 4398 N ASN B 411 -232.727 -27.156 30.757 1.00 0.00

ATOM 4399 CA ASN B 411 -233.683 -28.152 30.302 1.00 0.00

ATOM 4400 C ASN B 411 -234.649 -28.493 31.400 1.00 0.00

ATOM 4401 O ASN B 411 -235.845 -28.527 31.164 1.00 0.00

ATOM 4402 CB ASN B 411 -232.961 -29.433 29.877 1.00 0.00

ATOM 4403 CG ASN B 411 -232.221 -29.275 28.564 1.00 0.00

ATOM 4404 ODl ASN B 411 -232.507 -28.366 27.783 1.00 0.00

ATOM 4405 ND2 ASN B 411 -231.265 -30.163 28.314 1.00 0.00

ATOM 4406 N SER B 412 -234.105 -28.734 32.610 1.00 0.00

ATOM 4407 CA SER B 412 -234.956 -29.066 33.741 1.00 0.00

ATOM 4408 C SER B 412 -235.955 -27.970 33.985 1.00 0.00

ATOM 4409 O SER B 412 -237.126 -28.254 34.181 1.00 0.00

ATOM 4410 CB SER B 412 -234.117 -29.247 35.007 1.00 0.00

ATOM 4411 OG SER B 412 -233.275 -30.383 34.903 1.00 0.00

ATOM 4412 N LYS B 413 -235.475 -26.712 33.966 1.00 0.00

ATOM 4413 CA LYS B 413 -236.369 -25.592 34.206 1.00 0.00

ATOM 4414 C LYS B 413 -237.467 -25.553 33.180 1.00 0.00

ATOM 4415 O LYS B 413 -238.608 -25.307 33.535 1.00 0.00

ATOM 4416 CB LYS B 413 -235.602 -24.269 34.136 1.00 0.00

ATOM 4417 CG LYS B 413 -236.454 -23.042 34.421 1.00 0.00

ATOM 4418 CD LYS B 413 -235.614 -21.775 34.413 1.00 0.00

ATOM 4419 CE LYS B 413 -236.470 -20.545 34.668 1.00 0.00

ATOM 4420 NZ LYS B 413 -235.664 -19.294 34.648 1.00 0.00

ATOM 4421 N LEU B 414 -237.109 -25.810 31.905 1.00 0.00

ATOM 4422 CA LEU B 414 -238.118 -25.812 30.859 1.00 0.00

ATOM 4423 C LEU B 414 -239.208 -26.795 31.184 1.00 0.00

ATOM 4424 O LEU B 414 -240.375 -26.450 31.096 1.00 0.00

ATOM 4425 CB LEU B 414 -237.498 -26.202 29.516 1.00 0.00

ATOM 4426 CG LEU B 414 -238.450 -26.262 28.321 1.00 0.00

ATOM 4427 CDl LEU B 414 -239.068 -24.896 28.057 1.00 0.00

ATOM 4428 CD2 LEU B 414 -237.712 -26.700 27.066 1.00 0.00

ATOM 4429 N GLY B 415 -238.808 -28.021 31.573 1.00 0.00

ATOM 4430 CA GLY B 415 -239.798 -29.030 31.907 1.00 0.00

ATOM 4431 C GLY B 415 -240.644 -28.588 33.068 1.00 0.00

ATOM 4432 O GLY B 415 -241.858 -28.700 32.997 1.00 0.00

ATOM 4433 N LEU B 416 -239.991 -28.079 34.132 1.00 0.00

ATOM 4434 CA LEU B 416 -240.738 -27.647 35.301 1.00 0.00

ATOM 4435 C LEU B 416 -241.772 -26.625 34.924 1.00 0.00

ATOM 4436 O LEU B 416 -242.905 -26.728 35.364 1.00 0.00 ATOM 4437 CB LEU B 416 -239.800 -27.023 36.336 1.00 0.00

ATOM 4438 CG LEU B 416 -238.834 -27.979 37.039 1.00 0.00

ATOM 4439 CDl LEU B 416 -237.846 -27.207 37.900 1.00 0.00

ATOM 4440 CD2 LEU B 416 -239.592 -28.945 37.937 1.00 0.00

ATOM 4441 N ASP B 417 -241.371 -25.647 34.091 1.00 0.00

ATOM 4442 CA ASP B 417 -242.314 -24.618 33.689 1.00 0.00

ATOM 4443 C ASP B 417 -243.467 -25.210 32.928 1.00 0.00

ATOM 4444 O ASP B 417 -244.591 -24.771 33.117 1.00 0.00

ATOM 4445 CB ASP B 417 -241.630 -23.586 32.790 1.00 0.00

ATOM 4446 CG ASP B 417 -240.685 -22.681 33.556 1.00 0.00

ATOM 4447 ODl ASP B 417 -240.733 -22.693 34.804 1.00 0.00

ATOM 4448 OD2 ASP B 417 -239.896 -21.962 32.909 1.00 0.00

ATOM 4449 N ILE B 418 -243.186 -26.220 32.081 1.00 0.00

ATOM 4450 CA ILE B 418 -244.266 -26.862 31.350 1.00 0.00

ATOM 4451 C ILE B 418 -245.232 -27.493 32.317 1.00 0.00

ATOM 4452 O ILE B 418 -246.429 -27.294 32.186 1.00 0.00

ATOM 4453 CB ILE B 418 -243.737 -27.960 30.410 1.00 0.00

ATOM 4454 CGl ILE B 418 -242.915 -27.342 29.277 1.00 0.00

ATOM 4455 CG2 ILE B 418 -244.892 -28.739 29.798 1.00 0.00

ATOM 4456 CDl ILE B 418 -242.136 -28.355 28.466 1.00 0.00

ATOM 4457 N GLU B 419 -244.693 -28.246 33.297 1.00 0.00

ATOM 4458 CA GLU B 419 -245.557 -28.889 34.272 1.00 0.00

ATOM 4459 C GLU B 419 -246.356 -27.871 35.035 1.00 0.00

ATOM 4460 O GLU B 419 -247.532 -28.090 35.272 1.00 0.00

ATOM 4461 CB GLU B 419 -244.727 -29.694 35.275 1.00 0.00

ATOM 4462 CG GLU B 419 -244.092 -30.945 34.692 1.00 0.00

ATOM 4463 CD GLU B 419 -243.180 -31.649 35.677 1.00 0.00

ATOM 4464 OEl GLU B 419 -242.986 -31.118 36.790 1.00 0.00

ATOM 4465 OE2 GLU B 419 -242.659 -32.732 35.336 1.00 0.00

ATOM 4466 N ILE B 420 -245.704 -26.750 35.406 1.00 0.00

ATOM 4467 CA ILE B 420 -246.407 -25.713 36.145 1.00 0.00

ATOM 4468 C ILE B 420 -247.563 -25.195 35.339 1.00 0.00

ATOM 4469 O ILE B 420 -248.658 -25.085 35.866 1.00 0.00

ATOM 4470 CB ILE B 420 -245.481 -24.526 36.470 1.00 0.00

ATOM 4471 CGl ILE B 420 -244.402 -24.949 37.469 1.00 0.00

ATOM 4472 CG2 ILE B 420 -246.278 -23.381 37.076 1.00 0.00

ATOM 4473 CDl ILE B 420 -243.294 -23.932 37.638 1.00 0.00

ATOM 4474 N ALA B 421 -247.305 -24.886 34.052 1.00 0.00

ATOM 4475 CA ALA B 421 -248.368 -24.376 33.202 1.00 0.00

ATOM 4476 C ALA B 421 -249.537 -25.320 33.192 1.00 0.00

ATOM 4477 O ALA B 421 -250.670 -24.880 33.297 1.00 0.00

ATOM 4478 CB ALA B 421 -247.872 -24.212 31.773 1.00 0.00

ATOM 4479 N THR B 422 -249.242 -26.631 33.081 1.00 0.00

ATOM 4480 CA THR B 422 -250.311 -27.613 33.078 1.00 0.00

ATOM 4481 C THR B 422 -251.084 -27.558 34.366 1.00 0.00

ATOM 4482 O THR B 422 -252.303 -27.510 34.332 1.00 0.00

ATOM 4483 CB THR B 422 -249.763 -29.044 32.917 1.00 0.00

ATOM 4484 OGl THR B 422 -249.083 -29.159 31.660 1.00 0.00

ATOM 4485 CG2 THR B 422 -250.897 -30.057 32.958 1.00 0.00

ATOM 4486 N TYR B 423 -250.358 -27.559 35.502 1.00 0.00

ATOM 4487 CA TYR B 423 -251.030 -27.528 36.791 1.00 0.00

ATOM 4488 C TYR B 423 -251.941 -26.338 36.901 1.00 0.00

ATOM 4489 O TYR B 423 -253.057 -26.483 37.373 1.00 0.00

ATOM 4490 CB TYR B 423 -250.009 -27.450 37.927 1.00 0.00

ATOM 4491 CG TYR B 423 -249.178 -28.703 38.092 1.00 0.00

ATOM 4492 CDl TYR B 423 -249.564 -29.894 37.493 1.00 0.00

ATOM 4493 CD2 TYR B 423 -248.012 -28.689 38.847 1.00 0.00

ATOM 4494 CEl TYR B 423 -248.812 -31.045 37.638 1.00 0.00

ATOM 4495 CE2 TYR B 423 -247.248 -29.829 39.003 1.00 0.00

ATOM 4496 CZ TYR B 423 -247.658 -31.012 38.391 1.00 0.00

ATOM 4497 OH TYR B 423 -246.906 -32.157 38.537 1.00 0.00

ATOM 4498 N ARG B 424 -251.455 -25.164 36.453 1.00 0.00

ATOM 4499 CA ARG B 424 -252.274 -23.966 36.536 1.00 0.00

ATOM 4500 C ARG B 424 -253.560 -24.136 35.780 1.00 0.00

ATOM 4501 O ARG B 424 -254.611 -23.811 36.308 1.00 0.00

ATOM 4502 CB ARG B 424 -251.531 -22.766 35.945 1.00 0.00

ATOM 4503 CG ARG B 424 -250.360 -22.285 36.788 1.00 0.00

ATOM 4504 CD ARG B 424 -249.640 -21.124 36.121 1.00 0.00 ATOM 4505 NE ARG B 424 -248.483 -20.682 36.896 1.00 0.00

ATOM 4506 CZ ARG B 424 -247.649 -19.721 36.509 1.00 0.00

ATOM 4507 NHl ARG B 424 -246.623 -19.385 37.278 1.00 0.00

ATOM 4508 NH2 ARG B 424 -247.844 -19.099 35.354 1.00 0.00

ATOM 4509 N ARG B 425 -253.469 -24.661 34.541 1.00 0.00

ATOM 4510 CA ARG B 425 -254.677 -24.868 33.760 1.00 0.00

ATOM 4511 C ARG B 425 -255.630 -25.768 34.496 1.00 0.00

ATOM 4512 O ARG B 425 -256.802 -25.443 34.602 1.00 0.00

ATOM 4513 CB ARG B 425 -254.341 -25.515 32.414 1.00 0.00

ATOM 4514 CG ARG B 425 -253.615 -24.595 31.448 1.00 0.00

ATOM 4515 CD ARG B 425 -253.272 -25.313 30.153 1.00 0.00

ATOM 4516 NE ARG B 425 -252.530 -24.457 29.231 1.00 0.00

ATOM 4517 CZ ARG B 425 -252.062 -24.856 28.053 1.00 0.00

ATOM 4518 NHl ARG B 425 -251.398 -24.007 27.280 1.00 0.00

ATOM 4519 NH2 ARG B 425 -252.257 -26.105 27.650 1.00 0.00

ATOM 4520 N LEU B 426 -255.105 -26.898 35.012 1.00 0.00

ATOM 4521 CA LEU B 426 -255.957 -27.832 35.730 1.00 0.00

ATOM 4522 C LEU B 426 -256.609 -27.166 36.906 1.00 0.00

ATOM 4523 O LEU B 426 -257.805 -27.317 37.097 1.00 0.00

ATOM 4524 CB LEU B 426 -255.138 -29.017 36.245 1.00 0.00

ATOM 4525 CG LEU B 426 -254.619 -29.993 35.188 1.00 0.00

ATOM 4526 CDl LEU B 426 -253.669 -31.005 35.811 1.00 0.00

ATOM 4527 CD2 LEU B 426 -255.770 -30.753 34.547 1.00 0.00

ATOM 4528 N LEU B 427 -255.803 -26.424 37.690 1.00 0.00

ATOM 4529 CA LEU B 427 -256.342 -25.774 38.870 1.00 0.00

ATOM 4530 C LEU B 427 -257.448 -24.823 38.506 1.00 0.00

ATOM 4531 O LEU B 427 -258.447 -24.781 39.207 1.00 0.00

ATOM 4532 CB LEU B 427 -255.249 -24.980 39.590 1.00 0.00

ATOM 4533 CG LEU B 427 -255.671 -24.252 40.868 1.00 0.00

ATOM 4534 CDl LEU B 427 -256.165 -25.241 41.912 1.00 0.00

ATOM 4535 CD2 LEU B 427 -254.501 -23.481 41.459 1.00 0.00

ATOM 4536 N GLU B 428 -257.269 -24.075 37.401 1.00 0.00

ATOM 4537 CA GLU B 428 -258.305 -23.141 36.992 1.00 0.00

ATOM 4538 C GLU B 428 -259.585 -23.871 36.703 1.00 0.00

ATOM 4539 O GLU B 428 -260.625 -23.483 37.212 1.00 0.00

ATOM 4540 CB GLU B 428 -257.880 -22.390 35.729 1.00 0.00

ATOM 4541 CG GLU B 428 -258.888 -21.354 35.253 1.00 0.00

ATOM 4542 CD GLU B 428 -258.417 -20.608 34.021 1.00 0.00

ATOM 4543 OEl GLU B 428 -257.298 -20.890 33.546 1.00 0.00

ATOM 4544 OE2 GLU B 428 -259.169 -19.740 33.530 1.00 0.00

ATOM 4545 N GLY B 429 -259.499 -24.938 35.884 1.00 0.00

ATOM 4546 CA GLY B 429 -260.704 -25.670 35.535 1.00 0.00

ATOM 4547 C GLY B 429 -261.369 -26.234 36.759 1.00 0.00

ATOM 4548 O GLY B 429 -262.565 -26.054 36.924 1.00 0.00

ATOM 4549 N GLU B 430 -260.582 -26.913 37.617 1.00 0.00

ATOM 4550 CA GLU B 430 -261.172 -27.496 38.810 1.00 0.00

ATOM 4551 C GLU B 430 -261.721 -26.414 39.695 1.00 0.00

ATOM 4552 O GLU B 430 -262.919 -26.363 39.923 1.00 0.00

ATOM 4553 CB GLU B 430 -260.124 -28.286 39.595 1.00 0.00

ATOM 4554 CG GLU B 430 -259.640 -29.545 38.894 1.00 0.00

ATOM 4555 CD GLU B 430 -260.758 -30.537 38.642 1.00 0.00

ATOM 4556 OEl GLU B 430 -261.473 -30.884 39.605 1.00 0.00

ATOM 4557 OE2 GLU B 430 -260.919 -30.968 37.481 1.00 0.00

TER 4558 GLU B 430

MASTER 0 0 0 0 0 0 0 0 4550 8 0 46

END Tab. 4:

HEADER KBD_B_K8_K18 (Chain A: K8; chain B: K18; chain C: KBD-B) COMPND KBD_B_K8_K18 REMARK GENERATED BY SYBYL (TRI POS , INC . ) 10-MAR- 08

(Legend analogous to table 1 . CONECT indicates bonds via non-standard groups: the first number in a line designates the atom to which the subsequent atoms established a bond.)

SEQRES 45 MET GLN GLY LEU VAL GLU ASP PHE LYS ASN LYS TYR GLU

SEQRES 45 ASP GLU ILE ASN LYS ARG THR GLU MET GLU ASN GLU PHE

SEQRES 45 VAL LEU ILE LYS LYS ASP VAL ASP GLU ALA TYR MET ASN

SEQRES 45 LYS VAL GLU LEU GLU SER

SEQRES 45 ALA ARG LEU ALA ALA ASP ASP PHE ARG VAL LYS TYR GLU

SEQRES 45 THR GLU LEU ALA MET ARG GLN SER VAL GLU ASN ASP ILE

SEQRES 45 HIS GLY LEU ARG LYS VAL ILE ASP ASP THR ASN ILE THR

SEQRES 45 ARG LEU GLN LEU GLU THR

SEQRES 199 ILE LYS ASP PHE LEU GLN GLY SER SER CYS ILE ALA GLY

SEQRES 199 ILE TYR ASN GLU THR THR LYS GLN LYS LEU GLY ILE TYR

SEQRES 3 C 199 GLU ALA MET LYS ILE GLY LEU VAL ARG PRO GLY THR ALA

SEQRES 4 C 199 LEU GLU LEU LEU GLU ALA GLN ALA ALA THR GLY PHE ILE

SEQRES 5 C 199 VAL ASP PRO VAL SER ASN LEU ARG LEU PRO VAL GLU GLU

SEQRES 6 C 199 ALA TYR LYS ARG GLY LEU VAL GLY ILE GLU PHE LYS GLU

SEQRES 7 C 199 LYS LEU LEU SER ALA GLU ARG ALA VAL THR GLY TYR ASN

SEQRES 8 C 199 ASP PRO GLU THR GLY ASN ILE ILE SER LEU PHE GLN ALA

SEQRES 9 C 199 MET ASN LYS GLU LEU ILE GLU LYS GLY HIS GLY ILE ARG

SEQRES 10 C 199 LEU LEU GLU ALA GLN ILE ALA THR GLY GLY ILE ILE ASP

SEQRES 11 C 199 PRO LYS GLU SER HIS ARG LEU PRO VAL ASP ILE ALA TYR

SEQRES 12 C 199 LYS ARG GLY TYR PHE ASN GLU GLU LEU SER GLU ILE LEU

SEQRES 13 C 199 SER ASP PRO SER ASP ASP THR LYS GLY PHE PHE ASP PRO

SEQRES 14 C 199 ASN THR GLU GLU ASN LEU THR TYR LEU GLN LEU LYS GLU

SEQRES 15 C 199 ARG CYS ILE LYS ASP GLU GLU THR GLY LEU CYS LEU LEU

SEQRES 16 C 199 PRO LEU LYS GLU

ATOM N MET A 168 12.353 45.936 40.930

ATOM CA MET A 168 13.218 45.545 39.820

ATOM C MET A 168 13.885 46.729 39.140

ATOM O MET A 168 15.080 46.679 38.899

ATOM CB MET A 168 12.479 44.724 38.730

ATOM CG MET A 168 11.910 43.371 39.232

ATOM SD MET A 168 13.279 42.295 39.780

ATOM CE MET A 168 12.370 41.093 40.796

ATOM 9 HA MET A 168 14.017 44.917 40.243

ATOM 10 HBl MET A 168 11.662 45.332 38.309

ATOM 11 HB2 MET A 168 13.204 44.499 37.933

ATOM 12 HGl MET A 168 11.193 43.532 40.049

ATOM 13 HG2 MET A 168 11.387 42.856 38.411

ATOM 14 HEl MET A 168 11.589 40.605 40.194

ATOM 15 HE2 MET A 168 13.075 40.335 41.167

ATOM 16 HE3 MET A 168 11.909 41.608 41.652

ATOM 17 LPDl MET A 168 13.736 42.638 40.147

ATOM 18 LPD2 MET A 168 13.588 41.996 39.255

ATOM 19 HNCA MET A 168 11.942 45.234 41.512

ATOM 20 HH MET A 168 12.222 46.905 41.147

ATOM 21 NN GLN A 169 13.142 47.806 38.800

ATOM CCAA GLN A 169 13.767 48.948 38.128

ATOM 23 CC GLN A 169 14.971 49.466 38.888

ATOM 24 OO GLN A 169 15.980 49.742 38.259

ATOM 25 CCBB GLN A 169 12.794 50.139 37.897

ATOM 26 CCGG GLN A 169 11.672 49.813 36.874

ATOM 27 CCDD GLN A 169 10.929 51.078 36.509

ATOM 28 OEl GLN A 169 10.060 51.482 37.266

ATOM 29 NE2 GLN A 169 11.248 51.734 35.370

ATOM 30 HA GLN A 169 14.109 48.618 37.133

ATOM 31 HBl GLN A 169 12.348 50.443 38.858

ATOM 32 HB2 GLN A 169 13.373 50.992 37.503

ATOM 33 HGl GLN A 169 12.109 49.361 35.969

ATOM 34 HG2 GLN A 169 10.959 49.088 37.294

ATOM 35 HEE2222 GLN A 169 10.759 52.574 35.128

ATOM 36 HEE2211 GLN A 169 11.964 51.401 34.754

ATOM 37 HH GLN A 169 12.159 47.828 38.982 ATOM 38 N GLY A 170 14.895 49.620 40.230

ATOM 39 CA GLY A 170 16.048 50.135 40.968

ATOM 40 C GLY A 170 17.153 49.105 41.014

ATOM 41 O GLY A 170 18.315 49.471 40.954

ATOM 42 HA2 GLY A 170 15.770 50.372 42.008

ATOM 43 HAl GLY A 170 16.397 51.066 40.495

ATOM 44 H GLY A 170 14.068 49.367 40.739

ATOM 45 N LEU A 171 16.810 47.804 41.136

ATOM 46 CA LEU A 171 17.839 46.759 41.153

ATOM 47 C LEU A 171 18.647 46.845 39.874

ATOM 48 O LEU A 171 19.866 46.770 39.914

ATOM 49 CB LEU A 171 17.148 45.369 41.284

ATOM 50 CG LEU A 171 18.084 44.128 41.373

ATOM 51 CDl LEU A 171 19.032 44.193 42.602

ATOM 52 CD2 LEU A 171 17.209 42.844 41.456

ATOM 53 HA LEU A 171 18.485 46.917 42.032

ATOM 54 HBl LEU A 171 16.509 45.389 42.183

ATOM 55 HB2 LEU A 171 16.498 45.230 40.409

ATOM 56 HG LEU A 171 18.697 44.069 40.457

ATOM 57 HD21 LEU A 171 16.557 42.760 40.572

ATOM 58 HD22 LEU A 171 17.838 41.942 41.502

ATOM 59 HD23 LEU A 171 16.573 42.869 42.356

ATOM 60 HDIl LEU A 171 18.456 44.369 43.524

ATOM 61 HD12 LEU A 171 19.583 43.246 42.713

ATOM 62 HDl 3 LEU A 171 19.774 44.996 42.485

ATOM 63 H LEU A 171 15.847 47.538 41.216

ATOM 64 N VAL A 172 17.961 47.023 38.722

ATOM 65 CA VAL A 172 18.657 47.174 37.442

ATOM 66 C VAL A 172 19.510 48.427 37.497

ATOM 67 O VAL A 172 20.655 48.399 37.078

ATOM 68 CB VAL A 172 17.638 47.233 36.261

ATOM 69 CGl VAL A 172 18.315 47.688 34.941

ATOM 70 CG2 VAL A 172 16.958 45.850 36.047

ATOM 71 HA VAL A 172 19.306 46.296 37.292

ATOM 72 HB VAL A 172 16.855 47.974 36.497

ATOM 73 HGIl VAL A 172 19.142 47.009 34.695

ATOM 74 HGl 2 VAL A 172 17.589 47.679 34.113

ATOM 75 HGl 3 VAL A 172 18.714 48.710 35.029

ATOM 76 HG21 VAL A 172 16.456 45.502 36.962

ATOM 77 HG22 VAL A 172 16.205 45.918 35.247

ATOM 78 HG23 VAL A 172 17.703 45.096 35.753

ATOM 79 H VAL A 172 16.962 47.095 38.739

ATOM 80 N GLU A 173 18.947 49.541 38.013

ATOM 81 CA GLU A 173 19.667 50.819 38.070

ATOM 82 C GLU A 173 20.979 50.656 38.809

ATOM 83 O GLU A 173 22.008 51.088 38.314

ATOM 84 CB GLU A 173 18.763 51.885 38.757

ATOM 85 CG GLU A 173 19.269 53.345 38.646

ATOM 86 CD GLU A 173 18.276 54.256 39.329

ATOM 87 OEl GLU A 173 18.654 54.930 40.325

ATOM 88 OE2 GLU A 173 17.098 54.300 38.877

ATOM 89 HA GLU A 173 19.862 51.167 37.042

ATOM 90 HBl GLU A 173 17.762 51.849 38.295

ATOM 91 HB2 GLU A 173 18.662 51.647 39.825

ATOM 92 HGl GLU A 173 20.262 53.437 39.115

ATOM 93 HG2 GLU A 173 19.353 53.641 37.589

ATOM 94 H GLU A 173 18.006 49.497 38.345

ATOM 95 N ASP A 174 20.930 50.023 40.006

ATOM 96 CA ASP A 174 22.136 49.805 40.805

ATOM 97 C ASP A 174 23.104 48.923 40.060

ATOM 98 O ASP A 174 24.282 49.236 40.001

ATOM 99 CB ASP A 174 21.811 49.144 42.175

ATOM 100 CG ASP A 174 21.044 50.094 43.060

ATOM 101 ODl ASP A 174 19.836 49.841 43.320

ATOM 102 OD2 ASP A 174 21.650 51.105 43.507

ATOM 103 HA ASP A 174 22.623 50.772 41.016

ATOM 104 HBl ASP A 174 21.233 48.218 42.029

ATOM 105 HB2 ASP A 174 22.748 48.878 42.690 ATOM 106 H ASP A 174 20.058 49.684 40.363

ATOM 107 N PHE A 175 22.591 47.843 39.459

ATOM 108 CA PHE A 175 23.476 46.921 38.751

ATOM 109 C PHE A 175 24.194 47.727 37. 694

ATOM 110 O PHE A 175 25.409 47.702 37.600

ATOM 111 CB PHE A 175 22.726 45.735 38.075

ATOM 112 CG PHE A 175 23.006 44.437 38.845

ATOM 113 CDl PHE A 175 204 44.067 39.930

ATOM 114 CD2 PHE A 175 083 43.623 38.476

ATOM 115 CEl PHE A 175 2. 500 42.917 40.665

ATOM 116 CE2 PHE A 175 24.386 4 .478 39.217

ATOM 117 CZ PHE A 175 23.600 4 .128 40.317

ATOM 118 HA PHE A 175 24.222 4 6 . 527 39.465

ATOM 119 HBl PHE A 175 21.645 45 . 9 38.021

ATOM 120 HB2 PHE A 175 23.069 45 . 606 37.037

ATOM 121 HD2 PHE A 175 24.696 43 37.618

ATOM 122 HE2 PHE A 175 25.232 41 . 860 38.943

ATOM 123 HZ PHE A 175 23.844 41 . >45 40.899

ATOM 124 HEl PHE A 175 21.879 42 .636 41.510

ATOM 125 HDl PHE A 175 21.351 44.675 40.209

ATOM 126 H PHE A 175 21.673 47.557 39.739

ATOM 127 N LYS A 176 23.464 48.373 36.841

ATOM 128 CA LYS A 176 23.989 49.168 35.729

ATOM 129 C LYS A 176 25.005 50.190 36.205

ATOM 130 O LYS A 176 26.087 50.283 35.645

ATOM 131 CB LYS A 176 22.756 49.815 35.024

ATOM 132 CG LYS A 176 23.017 50.685 33.764

ATOM 133 CD LYS A 176 23.575 52.105 34.068

ATOM 134 CE LYS A 176 23.338 53.059 32.862

ATOM 135 NZ LYS A 176 23.858 54.422 33.111

ATOM 136 HA LYS A 176 24.471 48.496 35.000

ATOM 137 HBl LYS A 176 22.108 48.980 34.701

ATOM 138 HB2 LYS A 176 22.186 50.412 35.753

ATOM 139 HGl LYS A 176 23.677 50.151 33.061

ATOM 140 HG2 LYS A 176 22.037 50.813 33.271

ATOM 141 HDl LYS A 176 23.068 52.531 34.949

ATOM 142 HD2 LYS A 176 24.653 52.050 34.283

ATOM 143 HEl LYS A 176 23.819 52.635 31.964

ATOM 144 HE2 LYS A 176 2. .254 53.131 32.665

ATOM 145 HZl LYS A 176 24..926 54.419 33. lib

ATOM 146 HZ2 LYS A 176 23.668 55.072 3: .266

ATOM 147 HZ3 LYS A 176 23.394 54.881 33.973

ATOM 148 H LYS A 176 22.469 48.306 36.967

ATOM 149 N ASN A 177 24.665 50.976 37.251

ATOM 150 CA ASN A 177 25.603 51.960 37.799

ATOM 151 C ASN A 177 26.896 51.286 38.202

ATOM 152 O ASN A 177 27.969 51.756 37.854

ATOM 153 CB ASN A 177 25.020 52.676 39.052

ATOM 154 CG ASN A 177 23.878 53.613 38.737

ATOM 155 ODl ASN A 177 23.571 53.832 37.575

ATOM 156 ND2 ASN A 177 23.232 54.194 39.773

ATOM 157 HA ASN A 177 25.828 52.728 37.040

ATOM 158 HBl ASN A 177 24.678 51.927 39.782

ATOM 159 HB2 ASN A 177 25.813 53.277 39.525

ATOM 160 HD22 ASN A 177 22.486 54.838 39.598

ATOM 161 HD21 ASN A 177 23.491 53.997 40.720

ATOM 162 H ASN A 177 23.761 50.888 37.671

ATOM 163 N LYS A 178 26.772 50.176 38.962

ATOM 164 CA LYS A 178 27.944 49.482 39.497

ATOM 165 C LYS A 178 28.712 48.801 38.381

ATOM 166 O LYS A 178 29.926 48.700 38.415

ATOM 167 CB LYS A 178 27.462 48.459 40.567

ATOM 168 CG LYS A 178 28.603 47.789 41.378

ATOM 169 CD LYS A 178 29.549 48.825 42.039

ATOM 170 CE LYS A 178 30.451 48.218 43.142

ATOM 171 NZ LYS A 178 31.384 49.249 43.649

ATOM 172 HA LYS A 178 28.578 50.238 39.976

ATOM 173 HBl LYS A 178 26.813 48.988 41.284 ATOM 174 HB2 LYS A 178 26.860 47.678 40.073

ATOM 175 HGl LYS A 178 28.149 47.148 42.152

ATOM 176 HG2 LYS A 178 29.192 47.153 40.709

ATOM 177 HDl LYS A 178 30.217 49.233 41.269

ATOM 178 HD2 LYS A 178 28.960 49.648 42.474

ATOM 179 HEl LYS A 178 29.824 47.841 43.967

ATOM 180 HE2 LYS A 178 31.020 47.370 42.729

ATOM 181 HZl LYS A 178 30.854 50.079 44.098

ATOM 182 HZ2 LYS A 178 32.058 48.849 44.393

ATOM 183 HZ3 LYS A 178 31.992 49.656 42.853

ATOM 184 H LYS A 178 25.862 49.805 39.162

ATOM 185 N TYR A 179 27.985 48.322 37.355

ATOM 186 CA TYR A 179 28.600 47.673 36.190

ATOM 187 C TYR A 179 29.472 48.658 35.455

ATOM 188 O TYR A 179 30.597 48.318 35.122

ATOM 189 CB TYR A 179 27.432 47.119 35.318

ATOM 190 CG TYR A 179 27.705 46.707 33.866

ATOM 191 CDl TYR A 179 28.531 45.618 33.580

ATOM 192 CD2 TYR A 179 27.083 47.393 32.814

ATOM 193 CEl TYR A 179 28.620 45.145 32.265

ATOM 194 CE2 TYR A 179 27.162 46.911 31.506

ATOM 195 CZ TYR A 179 27.948 45.791 31.224

ATOM 196 OH TYR A 179 28.060 45.351 29. 904

ATOM 197 HA TYR A 179 227 46.829 36.518

ATOM 198 HB2 TYR A 179 975 46.258 35.834

ATOM 199 HBl TYR A 179 26.669 47.896 35.252

ATOM 200 HD2 TYR A 179 26.519 48.304 32.994

ATOM 201 HE2 TYR A 179 26.619 47.403 30.706

ATOM 202 HEl TYR A 179 29.210 44.266 32.048

ATOM 203 HDl TYR A 179 29.090 45.133 34.372

ATOM 204 HH TYR A 179 28.885 44.910 29.733

ATOM 205 H TYR A 179 26.994 48.427 37.389

ATOM 206 N GLU A 180 28.974 49.892 35.217

ATOM 207 CA GLU A 180 29.833 50.917 34.636

ATOM 208 C GLU A 180 30.990 51.195 35.571

ATOM 209 O GLU A 180 32.118 51. 154 35.108

ATOM 210 CB GLU A 180 29.092 .219 34.224

ATOM 211 CG GLU A 180 28.245 5: .006 32.937

ATOM 212 CD GLU A 180 27.692 53.319 32.442

ATOM 213 OEl GLU A 180 28.152 53.805 31.372

ATOM 214 OE2 GLU A 180 26.791 53.877 33.123

ATOM 215 HA GLU A 180 30.260 50.505 33.717

ATOM 216 HBl GLU A 180 28.457 52.571 35.052

ATOM 217 HB2 GLU A 180 29.843 52.997 34.009

ATOM 218 HGl GLU A 180 28.871 51.572 32.140

ATOM 219 HG2 GLU A 180 27.416 51.309 33.137

ATOM 220 H GLU A 180 28.038 50.135 35.471

ATOM 221 N ASP A 181 30.744 51.354 36.890

ATOM 999 CA ASP A 181 31.846 51.562 37.835

ATOM 223 C ASP A 181 32.918 50.502 37.661

ATOM 224 O ASP A 181 34.087 50.852 37.726

ATOM 225 CB ASP A 181 31.323 51.593 39.293

ATOM 226 CG ASP A 181 32.407 51.842 40.307

ATOM 227 ODl ASP A 181 32.712 53.035 40.573

ATOM 228 OD2 ASP A 181 32.953 50.845 40.854

ATOM 229 HA ASP A 181 32.293 52.547 37.622

ATOM 230 HBl ASP A 181 30.541 52.363 39.397

ATOM 231 HB2 ASP A 181 30.874 50.622 39.509

ATOM 232 H ASP A 181 29.802 51.344 37.231

ATOM 233 N GLU A 182 32.569 49. 111 37.427

ATOM 234 CA GLU A 182 33.612 48.101 37.195

ATOM 235 C GLU A 182 34.206 48.338 35.800

ATOM 236 O GLU A 182 35.404 48.152 35.661

ATOM 237 CB GLU A 182 33.141 46.748 37.435

ATOM 238 CG GLU A 182 32.578 46.530 38.867

ATOM 239 CD GLU A 182 33.476 46.989 39.989

ATOM 240 OEl GLU A 182 34.724 46.913 39.845

ATOM 241 OE2 GLU A 182 32.944 47.425 41.044 ATOM 242 HA GLU A 182 34.413 48.401 37.917

ATOM 243 HBl GLU A 182 32.367 46.490 36.693

ATOM 244 HB2 GLU A 182 33.998 46.069 37.284

ATOM 245 HGl GLU A 182 31.633 47.075 38.963

ATOM 246 HG2 GLU A 182 32.367 45.458 39.008

ATOM 247 H GLU A 182 31.609 48.930 37.382

ATOM 248 N ILE A 183 33.405 48.656 34.752

ATOM 249 CA ILE A 183 33.956 48.836 33.398

ATOM 250 C ILE A 183 35.028 49.911 33.443

ATOM 251 O ILE A 183 36.098 49.716 32.883

ATOM 252 CB ILE A 183 32.847 49.123 32.346

ATOM 253 CGl ILE A 183 32.024 47.820 32.105

ATOM 254 CG2 ILE A 183 33.434 49.690 31.022

ATOM 255 CDl ILE A 183 30.621 48.070 31.496

ATOM 256 HA ILE A 183 34.451 47.895 33.108

ATOM 257 HB ILE A 183 32.204 49.909 32.756

ATOM 258 HGIl ILE A 183 32.594 47.151 31.439

ATOM 259 HG12 ILE A 183 31.869 47.280 33.053

ATOM 260 HDIl ILE A 183 30.670 48.629 30.553

ATOM 261 HD12 ILE A 183 30.160 47.098 31.284

ATOM 262 HD13 ILE A 183 29.976 48.614 32.203

ATOM 263 HG21 ILE A 183 34.141 48.975 30.576

ATOM 264 HG22 ILE A 183 32.635 49.896 30.296

ATOM 265 HG23 ILE A 183 33.961 50.640 31.202

ATOM 266 H ILE A 183 32.424 48.782 34.899

ATOM 267 N ASN A 184 34.760 51.046 34.130

ATOM 268 CA ASN A 184 35.782 52.084 34.311

ATOM 269 C ASN A 184 37.020 51.495 34.957

ATOM 270 O ASN A 184 38.131 51.785 34.541

ATOM 271 CB ASN A 184 35.231 53.210 35.230

ATOM 272 CG ASN A 184 36.262 54.276 35.514

ATOM 273 ODl ASN A 184 36.720 54.375 36.642

ATOM 274 ND2 ASN A 184 36.647 55.092 34.509

ATOM 275 HA ASN A 184 36.024 52.518 33.328

ATOM 276 HBl ASN A 184 34.354 53.678 34.753

ATOM 277 HB2 ASN A 184 34.896 52.775 36.184

ATOM 278 HD22 ASN A 184 37.326 55.806 34.682

ATOM 279 HD21 ASN A 184 36.260 55.003 33.590

ATOM 280 H ASN A 184 33.860 51.184 34.545

ATOM 281 N LYS A 185 36.825 50.663 36.004

ATOM 282 CA LYS A 185 37.960 50.119 36.763

ATOM 283 C LYS A 185 38.815 49.291 35.836

ATOM 284 O LYS A 185 40.030 49.402 35.886

ATOM 285 CB LYS A 185 37.493 49.273 37.993

ATOM 286 CG LYS A 185 38.119 49.693 39.355

ATOM 287 CD LYS A 185 37.301 49.221 40.596

ATOM 288 CE LYS A 185 35.948 49.961 40.805

ATOM 289 NZ LYS A 185 35.221 49.434 41.982

ATOM 290 HA LYS A 185 38.574 50.964 37.117

ATOM 291 HBl LYS A 185 36.425 49.422 38.111

ATOM 292 HB2 LYS A 185 37.636 48.195 37.817

ATOM 293 HGl LYS A 185 39.132 49.263 39.399

ATOM 294 HG2 LYS A 185 38.211 50.788 39.426

ATOM 295 HDl LYS A 185 37.094 48.152 40.518

ATOM 296 HD2 LYS A 185 37.912 49.373 41.501

ATOM 297 HEl LYS A 185 36.144 51.038 40.936

ATOM 298 HE2 LYS A 185 35.274 49.844 39.945

ATOM 299 HZl LYS A 185 35.782 49.556 .897

ATOM 300 HZ2 LYS A 185 34.286 49.959 .113

ATOM 301 HZ3 LYS A 185 34.983 48.384 41.876

ATOM 302 H LYS A 185 35.884 50.433 36.256

ATOM 303 N ARG A 186 38.193 48.442 34.979

ATOM 304 CA ARG A 186 39.003 47.535 34.177

ATOM 305 C ARG A 186 39.651 48.295 33.052

ATOM 306 O ARG A 186 40.792 48.000 32.740

ATOM 307 CB ARG A 186 38.314 46.273 33.638

ATOM 308 CG ARG A 186 39.411 45.231 33.186

ATOM 309 CD ARG A 186 38.712 44.079 32.423 ATOM 310 NE ARG A 186 38.299 44.627 31.124

ATOM 311 CZ ARG A 186 37.221 44.284 30.455

ATOM 312 NHl ARG A 186 36.930 44.993 29.385

ATOM 313 NH2 ARG A 186 36.430 43.292 30.788

ATOM 314 HA ARG A 186 39.776 47.155 34.857

ATOM 315 HBl ARG A 186 37.606 45.947 34.427

ATOM 316 HB2 ARG A 186 37.696 46.566 32.779

ATOM 317 HGl ARG A 186 40.169 45.631 32.501

ATOM 318 HG2 ARG A 186 40.031 44.860 34.012

ATOM 319 HDl ARG A 186 39.388 43.220 32.282

ATOM 320 HD2 ARG A 186 37.888 43.785 33.088

ATOM 321 HE ARG A 186 38.878 45.386 30.735

ATOM 322 HHl 2 ARG A 186 36.109 44.771 28.807

ATOM 323 HHIl ARG A 186 37.510 45.798 29.095

ATOM 324 HH22 ARG A 186 35.580 43.093 30.237

ATOM 325 HH21 ARG A 186 36.628 42.683 31.592

ATOM 326 H ARG A 186 37.196 48.399 34.892

ATOM 327 N THR A 187 39.004 49.239 32.337

ATOM 328 CA THR A 187 39.681 49.996 31.284

ATOM 329 C THR A 187 40.939 50.620 31.849

ATOM 330 O THR A 187 41.973 50.626 31.198

ATOM 331 CB THR A 187 38.765 51.118 30.729

ATOM 332 OGl THR A 187 38.376 51.937 31.844

ATOM 333 CG2 THR A 187 37.528 50.527 29.999

ATOM 334 HA THR A 187 39.948 49.293 30.477

ATOM 335 HB THR A 187 39.343 51.729 30.013

ATOM 336 HGl THR A 187 37.877 52.703 31.582

ATOM 337 HG23 THR A 187 37.829 50.104 29.028

ATOM 338 HG21 THR A 187 37.060 49.726 30.587

ATOM 339 HG22 THR A 187 36.776 51.311 29.821

ATOM 340 H THR A 187 38.229 49.654 32.815

ATOM 341 N GLU A 188 40.929 51.112 33.130

ATOM 342 CA GLU A 188 42.134 51.659 33.747

ATOM 343 C GLU A 188 43.144 50.566 34.039

ATOM 344 O GLU A 188 44.332 50.806 33.892

ATOM 345 CB GLU A 188 41.850 52.540 34.995

ATOM 346 CG GLU A 188 41.119 53.857 34.605

ATOM 347 CD GLU A 188 41.194 54.858 35.730

ATOM 348 OEl GLU A 188 41.868 55.912 35.557

ATOM 349 OE2 GLU A 188 40.581 54.597 36.799

ATOM 350 HA GLU A 188 42.626 52.325 33.018

ATOM 351 HBl GLU A 188 41. >62 51.975 35.737

ATOM 352 HB2 GLU A 188 4: .817 52.806 35.453

ATOM 353 HGl GLU A 188 41.588 54.309 33.716

ATOM 354 HG2 GLU A 188 40.064 53.657 34.363

ATOM 355 H GLU A 188 40.084 51.084 33.670

ATOM 356 N MET A 189 42.701 49.354 34.436

ATOM 357 CA MET A 189 43.643 48.247 34.637

ATOM 358 C MET A 189 44.256 47.852 33.312

ATOM 359 O MET A 189 45.463 47.695 33.220

ATOM 360 CB MET A 189 42.887 47.099 35.348

ATOM 361 CG MET A 189 42.620 47.461 36.826

ATOM 362 SD MET A 189 41.520 46.248 37.616

ATOM 363 CE MET A 189 41.471 47.065 39.243

ATOM 364 HA MET A 189 44.460 48.579 35.297

ATOM 365 HBl MET A 189 41.981 46.872 34.769

ATOM 366 HB2 MET A 189 43.502 46.201 35.422

ATOM 367 HGl MET A 189 43.570 47.469 37.386

ATOM 368 HG2 MET A 189 42.172 48.459 36.889

ATOM 369 HEl MET A 189 41.245 48.135 39.129

ATOM 370 HE2 MET A 189 40.703 46.601 39.876

ATOM 371 HE3 MET A 189 42.454 46.968 39.723

ATOM 372 LPDl MET A 189 41.792 45.626 37.644

ATOM 373 LPD2 MET A 189 40.910 46.215 37.321

ATOM 374 H MET A 189 41.721 49.192 34.564

ATOM 375 N GLU A 190 43.432 47.705 32. 256

ATOM 376 CA GLU A 190 43.964 47.423 30.927

ATOM 377 C GLU A 190 45 . 051 48 . 42 9 30 . 614 ATOM 378 O GLU A 190 46.111 48.031 30.168

ATOM 379 CB GLU A 190 42.892 47.490 29.803

ATOM 380 CG GLU A 190 41.963 46.257 29.850

ATOM 381 CD GLU A 190 40.760 46.403 28.953

ATOM 382 OEl GLU A 190 40.866 46.039 27.752

ATOM 383 OE2 GLU A 190 39.696 46.874 29.443

ATOM 384 HA GLU A 190 44.403 46.411 30.927

ATOM 385 HBl GLU A 190 42.303 48.412 29.908

ATOM 386 HB2 GLU A 190 43.378 47.500 28.813

ATOM 387 HGl GLU A 190 42.546 45.368 29.565

ATOM 388 HG2 GLU A 190 41.624 46.121 30.880

ATOM 389 H GLU A 190 42.451 47.820 32.368

ATOM 390 N ASN A 191 44.840 49.745 30.834

ATOM 391 CA ASN A 191 45.904 50.705 30.521

ATOM 392 C ASN A 191 47.141 50.411 31.343

ATOM 393 O ASN A 191 48.225 50.343 30.787

ATOM 394 CB ASN A 191 45.411 52.157 30.768

ATOM 395 CG ASN A 191 46. O99 53.182 30.134

ATOM 396 ODl ASN A 191 46. 5 0 53.113 28.930

ATOM 397 ND2 ASN A 191 46.881 54.153 30.

ATOM 398 HA ASN A 191 46.141 50.602 29.448

ATOM 399 HBl ASN A 191 44.427 52.285 30.290

ATOM 400 HB2 ASN A 191 45.279 .331 31.847

ATOM 401 HD22 ASN A 191 47.450 54.845 30.443

ATOM 402 HD21 ASN A 191 46.733 54.209 31.876

ATOM 403 H ASN A 191 43.961 50.073 31.,188

ATOM 404 N GLU A 192 46.989 50.230 32. 676

ATOM 405 CA GLU A 192 48.139 49.911 33.524

ATOM 406 C GLU A 192 48.880 48.744 32.913

ATOM 407 O GLU A 192 50.037 48.872 32.544

ATOM 408 CB GLU A 192 47.719 49.634 35.004

ATOM 409 CG GLU A 192 47.405 50.907 35.834

ATOM 410 CD GLU A 192 48.650 51.724 36.065

ATOM 411 OEl GLU A 192 49.421 51.378 37.001

ATOM 412 OE2 GLU A 192 48.866 52.717 35.319

ATOM 413 HA GLU A 192 48.822 50.774 33.544

ATOM 414 HBl GLU A 192 46.814 49.015 35.021

ATOM 415 HB2 GLU A 192 48.510 49.074 35.522

ATOM 416 HGl GLU A 192 46.633 51.513 35.333

ATOM 417 HG2 GLU A 192 47.009 50.607 36.819

ATOM 418 H GLU A 192 46.083 50.311 33.095

ATOM 419 N PHE A 193 48.286 47.656 32.697

ATOM 420 CA PHE A 193 48.664 46.362 32.138

ATOM 421 C PHE A 193 49.434 46.625 30.865

ATOM 422 O PHE A 193 50.651 46.557 30.864

ATOM 423 CB PHE A 193 47.384 45.519 31.903

ATOM 424 CG PHE A 193 47.666 44.137 31.309

ATOM 425 CDl PHE A 193 48.177 43.139 32.139

ATOM 426 CD2 PHE A 193 47.400 43.860 29.961

ATOM 427 CEl PHE A 193 48.427 41.860 31.631

ATOM 428 CE2 PHE A 193 47.639 42.580 29.453

ATOM 429 CZ PHE A 193 48.224 41.613 30.276

ATOM 430 HA PHE A 193 49.297 45.817 32.861

ATOM 431 HBl PHE A 193 46.856 45.383 32.858

ATOM 432 HB2 PHE A 193 46.704 46.055 31.243

ATOM 433 HD2 PHE A 193 47.014 44.632 29.301

ATOM 434 HE2 PHE A 193 47.383 42.340 28.426

ATOM 435 HZ PHE A 193 48.536 40.666 29.866

ATOM 436 HEl PHE A 193 48.781 41.066 32.282

ATOM 437 HDl PHE A 193 48.382 43.350 33.181

ATOM 438 H PHE A 193 47.510 47.725 33.316

ATOM 439 N VAL A 194 48.950 47.574 29.934

ATOM 440 CA VAL A 194 49.659 47.992 28.720

ATOM 441 C VAL A 194 50.936 48.751 29.031

ATOM 442 O VAL A 194 51.979 48.458 28.469

ATOM 443 CB VAL A 194 48.767 48.857 27.768

ATOM 444 CGl VAL A 194 49.582 49.478 26.596

ATOM 445 CG2 VAL A 194 47.588 48.043 27.158 ATOM 446 HA VAL A 194 49.950 47.105 28.150

ATOM 447 HB VAL A 194 48.345 49.688 28.355

ATOM 448 HGIl VAL A 194 50.053 48.685 25.995

ATOM 449 HGl 2 VAL A 194 48.919 50.063 25.940

ATOM 450 HGl 3 VAL A 194 50.366 50.157 26.962

ATOM 451 HG21 VAL A 194 46.997 47.530 27.926

ATOM 452 HG22 VAL A 194 46.911 48.714 26.606

ATOM 453 HG23 VAL A 194 47.967 47.281 26.460

ATOM 454 H VAL A 194 47.984 47.818 30.048

ATOM 455 N LEU A 195 50.849 49.777 29.902

ATOM 456 CA LEU A 195 52.008 50.628 30.211

ATOM 457 C LEU A 195 53.137 49.797 30.777

ATOM 458 O LEU A 195 54.241 49.776 30.256

ATOM 459 CB LEU A 195 51.639 51.705 31.286

ATOM 460 CG LEU A 195 50.881 52.944 30.723

ATOM 461 CDl LEU A 195 50.045 53.616 31.850

ATOM 462 CD2 LEU A 195 51.875 53.983 30.131

ATOM 463 HA LEU A 195 52.358 51.151 29.305

ATOM 464 HBl LEU A 195 51.008 51.247 32.061

ATOM 465 HB2 LEU A 195 52.550 52.060 31.794

ATOM 466 HG LEU A 195 50.186 .618 29.930

ATOM 467 HD21 LEU A 195 52.488 53.536 29.335

ATOM 468 HD22 LEU A 195 51.328 54.837 29.703

ATOM 469 HD23 LEU A 195 52.547 54.363 30.917

ATOM 470 HDIl LEU A 195 50.675 53.824 32.729

ATOM 471 HD12 LEU A 195 49.616 54.567 31.504

ATOM 472 HD13 LEU A 195 49.218 52.956 32.158

ATOM 473 H LEU A 195 49.964 49.963 30.333

ATOM 474 N ILE A 196 52.807 49.124 31.890

ATOM 475 CA ILE A 196 53.781 48.377 32.675

ATOM 476 C ILE A 196 54.410 47.311 31.794

ATOM 477 O ILE A 196 55.613 47.136 31.869

ATOM 478 CB ILE A 196 53.013 47.964 33.978

ATOM 479 CGl ILE A 196 52.971 49.208 34.924

ATOM 480 CG2 ILE A 196 53.545 46.681 34.648

ATOM 481 CDl ILE A 196 51.681 49.308 35.766

ATOM 482 HA ILE A 196 54.604 49.052 32.988

ATOM 483 HB ILE A 196 51.983 47.649 33.730

ATOM 484 HGIl ILE A 196 53.860 49.207 35.574

ATOM 485 HG12 ILE A 196 52.988 50.143 34.340

ATOM 486 HDIl ILE A 196 51.579 48.416 36.384

ATOM 487 HD12 ILE A 196 51.712 50.190 36.424

ATOM 488 HD13 ILE A 196 50.811 49.395 35.100

ATOM 489 HG21 ILE A 196 54.532 46.794 35.104

ATOM 490 HG22 ILE A 196 52.849 46.312 35.417

ATOM 491 HG23 ILE A 196 53.603 45.949 33.839

ATOM 492 H ILE A 196 51.856 49.138 32.182

ATOM 493 N LYS A 197 53.638 46.613 30.932

ATOM 494 CA LYS A 197 54.210 45.643 29.996

ATOM 495 C LYS A 197 55.395 46.183 29.225

ATOM 496 O LYS A 197 56.299 45.410 28.952

ATOM 497 CB LYS A 197 53.096 45.229 28.980

ATOM 498 CG LYS A 197 52.120 44.165 29.562

ATOM 499 CD LYS A 197 50.848 43.987 28.684

ATOM 500 CE LYS A 197 50.986 42.907 27.579

ATOM 501 NZ LYS A 197 50.257 43.288 26.349

ATOM 502 HA LYS A 197 54.536 44.766 30.589

ATOM 503 HBl LYS A 197 52.548 46.135 28.689

ATOM 504 HB2 LYS A 197 53.496 44.845 28.040

ATOM 505 HGl LYS A 197 52.623 43.196 29.709

ATOM 506 HG2 LYS A 197 51.805 44.508 30.552

ATOM 507 HDl LYS A 197 49.999 43.722 29.328

ATOM 508 HD2 LYS A 197 50.595 44.941 28.210

ATOM 509 HEl LYS A 197 52.045 42.763 27.333

ATOM 510 HE2 LYS A 197 50.608 41.942 27.956

ATOM 511 HZl LYS A 197 50.657 44.190 25.903

ATOM 512 HZ2 LYS A 197 50.366 42.507 25.613

ATOM 513 HZ3 LYS A 197 49.200 43.438 26.522 ATOM 514 H LYS A 197 52.659 46.781 30.912

ATOM 515 N LYS A 198 55.420 47.475 28.825

ATOM 516 CA LYS A 198 56.526 47.971 27.998

ATOM 517 C LYS A 198 57.724 48.186 28.890

ATOM 518 O LYS A 198 58.812 47.744 28.559

ATOM 519 CB LYS A 198 56.153 49.314 27.312

ATOM 520 CG LYS A 198 57.033 49.595 26.062

ATOM 521 CD LYS A 198 57.113 51.121 25.787

ATOM 522 CE LYS A 198 57.755 51.444 24.411

ATOM 523 NZ LYS A 198 57.556 52.872 24.069

ATOM 524 HA LYS A 198 56.762 47.234 27.211

ATOM 525 HBl LYS A 198 55.098 49.284 26.991

ATOM 526 HB2 LYS A 198 56.249 50.136 28.038

ATOM 527 HGl LYS A 198 58.052 49.204 26.205

ATOM 528 HG2 LYS A 198 56.590 49.073 25.196

ATOM 529 HDl LYS A 198 56.095 51.541 25.814

ATOM 530 HD2 LYS A 198 57.705 51.603 26.584

ATOM 531 HEl LYS A 198 58.831 51.202 24.441

ATOM 532 HE2 LYS A 198 57.286 50.823 23.630

ATOM 533 HZl LYS A 198 57.971 53.527 24.822

ATOM 534 HZ2 LYS A 198 58.023 53.124 23.126

ATOM 535 HZ3 LYS A 198 56.506 53.113 23.970

ATOM 536 H LYS A 198 54.689 48.112 29.085

ATOM 537 N ASP A 199 57.511 48.870 30.037

ATOM 538 CA ASP A 199 58.582 49.062 31.012

ATOM 539 C ASP A 199 59.262 47.747 31.325

ATOM 540 O ASP A 199 60.465 47.744 31.537

ATOM 541 CB ASP A 199 58.058 49.714 32.311

ATOM 542 CG ASP A 199 57.574 51.117 32.049

ATOM 543 ODl ASP A 199 56.376 51.276 31.686

ATOM 544 OD2 ASP A 199 58.387 52.068 32.202

ATOM 545 HA ASP A 199 59.331 49.749 30.584

ATOM 546 HBl ASP A 199 57.220 49.110 32.672

ATOM 547 HB2 ASP A 199 58.851 49.727 33.076

ATOM 548 H ASP A 199 56.611 49.256 30.246

ATOM 549 N VAL A 200 58.509 46.623 31.343

ATOM 550 CA VAL A 200 59.149 45.326 31.537

ATOM 551 C VAL A 200 60.045 45.043 30.345

ATOM 552 O VAL A 200 61.207 44.730 30.554

ATOM 553 CB VAL A 200 58.150 44.160 31.745

ATOM 554 CGl VAL A 200 58.933 42.814 31.843

ATOM 555 CG2 VAL A 200 57.249 44.312 32.996

ATOM 556 HA VAL A 200 59.766 45.374 32.447

ATOM 557 HB VAL A 200 57.470 44.226 30.889

ATOM 558 HGIl VAL A 200 59.672 42.864 32.654

ATOM 559 HGl 2 VAL A 200 58.252 41.976 32.055

ATOM 560 HG13 VAL A 200 59.476 42.589 30.912

ATOM 561 HG21 VAL A 200 56.705 45.264 33.006

ATOM 562 HG22 VAL A 200 56.511 43.496 33.041

ATOM 563 HG23 VAL A 200 57.875 44.260 33.

ATOM 564 H VAL A 200 57.519 46.657 31.201

ATOM 565 N ASP A 201 59.540 45.128 29.089

ATOM 566 CA ASP A 201 60.367 44.755 27.937

ATOM 567 C ASP A 201 61.601 45.616 27.798

ATOM 568 O ASP A 201 62.649 45.083 27.476

ATOM 569 CB ASP A 201 59.642 44.973 26.583

ATOM 570 CG ASP A 201 58.322 44.267 26.504

ATOM 571 ODl ASP A 201 57.375 44.913 25.989

ATOM 572 OD2 ASP A 201 58.222 43.089 26.944

ATOM 573 HA ASP A 201 60.648 43.693 28.044

ATOM 574 HBl ASP A 201 59.467 46.050 26.424

ATOM 575 HB2 ASP A 201 60.271 44.610 25.758

ATOM 576 H ASP A 201 58.590 45.405 28.930

ATOM 577 N GLU A 202 61.488 46.948 27.996

ATOM 578 CA GLU A 202 62.643 47.823 27.785

ATOM 579 C GLU A 202 63.709 47.451 28.792

ATOM 580 O GLU A 202 64. 47.386 28.453

ATOM 581 CB GLU A 202 62. ?46 49.312 28.021 ATOM 582 CG GLU A 202 61.178 49.844 27.019

ATOM 583 CD GLU A 202 61.805 50.544 25.840

ATOM 584 OEl GLU A 202 61.877 49.934 24.739

ATOM 585 OE2 GLU A 202 62.228 51.720 26.009

ATOM 586 HA GLU A 202 63.026 47.692 26.760

ATOM 587 HBl GLU A 202 61.841 49.392 29.043

ATOM 588 HB2 GLU A 202 63.145 49.949 27.973

ATOM 589 HGl GLU A 202 60.529 49.033 26.657

ATOM 590 HG2 GLU A 202 60.530 50.579 27.524

ATOM 591 H GLU A 202 60.620 47.343 28.300

ATOM 592 N ALA A 203 63.294 47.212 30.056

ATOM 593 CA ALA A 203 64.254 46.881 31.104

ATOM 594 C ALA A 203 64.900 45.550 30.782

ATOM 595 O ALA A 203 66.116 45.467 30.782

ATOM 596 CB ALA A 203 63.574 46.850 32.495

ATOM 597 HA ALA A 203 65.030 47.665 31.143

ATOM 598 HBl ALA A 203 64.308 46.588 33.272

ATOM 599 HB2 ALA A 203 63.146 47.836 32.733

ATOM 600 HB3 ALA A 203 62.762 46.110 32.489

ATOM 601 H ALA A 203 62.322 47.258 30.297

ATOM 602 N TYR A 204 64.094 44.505 30.491

ATOM 603 CA TYR A 204 64.640 43.211 30.069

ATOM 604 C TYR A 204 65.652 43.368 28.953

ATOM 605 O TYR A 204 66.753 42.850 29.051

ATOM 606 CB TYR A 204 63.482 42.324 29.541

ATOM 607 CG TYR A 204 64.029 41.121 28.760

ATOM 608 CDl TYR A 204 64.836 40.169 29.397

ATOM 609 CD2 TYR A 204 63.738 40.975 27.401

ATOM 610 CEl TYR A 204 65.364 39.099 28.675

ATOM 611 CE2 TYR A 204 64.282 39.912 26.674

ATOM 612 CZ TYR A 204 65.098 38.972 27.302

ATOM 613 OH TYR A 204 65.633 37.925 26.547

ATOM 614 HA TYR A 204 65.107 42.715 30.934

ATOM 615 HB2 TYR A 204 62.845 42.014 30.379

ATOM 616 HBl TYR A 204 62.844 42.917 28.874

ATOM 617 HD2 TYR A 204 63.091 41.682 26.892

ATOM 618 HE2 TYR A 204 64.069 39.816 25.614

ATOM 619 HEl TYR A 204 65.982 38.370 29.186

ATOM 620 HDl TYR A 204 65.056 40.260 30.456

ATOM 621 HH TYR A 204 66.212 37.349 27.031

ATOM 622 H TYR A 204 63.101 44.606 30.564

ATOM 623 N MET A 205 65.282 44.082 27.870

ATOM 624 CA MET A 205 66.209 44.296 26.755

ATOM 625 C MET A 205 67.508 44.873 27.277

ATOM 626 O MET A 205 68.572 44.372 26.949

ATOM 627 CB MET A 205 65.573 45.233 25.690

ATOM 628 CG MET A 205 64.480 44.469 24.893

ATOM 629 SD MET A 205 63.234 45.612 24.217

ATOM 630 CE MET A 205 62.122 44.386 23.457

ATOM 631 HA MET A 205 66.419 43.335 26.254

ATOM 632 HBl MET A 205 65.139 46.108 26.197

ATOM 633 HB2 MET A 205 66.340 45.600 .989

ATOM 634 HGl MET A 205 64.937 43.895 .072

ATOM 635 HG2 MET A 205 63.943 43.765 25.545

ATOM 636 HEl MET A 205 61.852 43.605 24.184

ATOM 637 HE2 MET A 205 61.208 44.890 23.112

ATOM 638 HE3 MET A 205 62.627 43.918 22.600

ATOM 639 LPDl MET A 205 63.499 46.036 23.758

ATOM 640 LPD2 MET A 205 62.925 45.971 24.704

ATOM 641 H MET A 205 64.364 44.480 27.831

ATOM 642 N ASN A 206 67.417 45.932 28.110

ATOM 643 CA ASN A 206 68.619 46.564 28.659

ATOM 644 C ASN A 206 69.408 45.530 29.443

ATOM 645 O ASN A 206 70.620 45.454 29.318

ATOM 646 CB ASN A 206 68.233 47.748 29.599

ATOM 647 CG ASN A 206 69.363 48.738 29.742

ATOM 648 ODl ASN A 206 70.227 48.521 30.574

ATOM 649 ND2 ASN A 206 69.392 49.833 28.948 ATOM 650 HA ASN A 206 69.227 46.951 27.823

ATOM 651 HBl ASN A 206 67.362 48.289 29.198

ATOM 652 HB2 ASN A 206 67.947 47.376 30.595

ATOM 653 HD22 ASN A 206 70.140 50.492 29.040

ATOM 654 HD21 ASN A 206 68.678 50.011 28.270

ATOM 655 H ASN A 206 66.517 46.288 28.365

ATOM 656 N LYS A 207 68.696 44.721 30.262

ATOM 657 CA LYS A 207 69.326 43.742 31.153

ATOM 658 C LYS A 207 70.152 42.769 30.335

ATOM 659 O LYS A 207 71.294 42.514 30.682

ATOM 660 CB LYS A 207 68.217 43.107 32.051

ATOM 661 CG LYS A 207 68.702 42.226 33.236

ATOM 662 CD LYS A 207 69.142 40.788 32.844

ATOM 663 CE LYS A 207 67.968 39.866 32.412

ATOM 664 NZ LYS A 207 68.419 38.465 .247

ATOM 665 HA LYS A 207 70.018 44.278 31.817

ATOM 666 HBl LYS A 207 67.658 43.945 32.504

ATOM 667 HB2 LYS A 207 67.514 42.540 31.430

ATOM 668 HGl LYS A 207 69.529 42.751 33.740

ATOM 669 HG2 LYS A 207 67.881 42.129 33.966

ATOM 670 HDl LYS A 207 69.872 40.826 32.029

ATOM 671 HD2 LYS A 207 69.633 40.335 33.720

ATOM 672 HEl LYS A 207 67.171 39.902 33.174

ATOM 673 HE2 LYS A 207 67.544 40.208 31.453

ATOM 674 HZl LYS A 207 68.842 38.064 33.159

ATOM 675 HZ2 LYS A 207 67.598 37.820 31.968

ATOM 676 HZ3 LYS A 207 69.160 38.378 31.465

ATOM 677 H LYS A 207 67.701 44.802 30.277

ATOM 678 N VAL A 208 69.611 42.217 29.227

ATOM 679 CA VAL A 208 70.364 41.237 28.426

ATOM 680 C VAL A 208 71.,632 41.838 27.866

ATOM 681 O VAL A 208 72.680 41.214 27.937

ATOM 682 CB VAL A 208 69.475 40.662 27.279

ATOM 683 CGl VAL A 208 70.295 40.104 26.082

ATOM 684 CG2 VAL A 208 68.557 39.552 27.855

ATOM 685 HA VAL A 208 70.671 40.405 29.082

ATOM 686 HB VAL A 208 68.843 41.468 26.867

ATOM 687 HGIl VAL A 208 71.005 39.337 26.426

ATOM 688 HG12 VAL A 208 69.622 39.652 25.337

ATOM 689 HGl 3 VAL A 208 70.854 40.909 25.579

ATOM 690 HG21 VAL A 208 67.981 39.942 28.708

ATOM 691 HG22 VAL A 208 67.861 39.213 27.077

ATOM 692 HG23 VAL A 208 69.148 38.687 28.194

ATOM 693 H VAL A 208 68.684 42.482 28.955

ATOM 694 N GLU A 209 71.554 43.058 27.295

ATOM 695 CA GLU A 209 72.761 43.694 26.759

ATOM 696 C GLU A 209 73.807 43.754 27.860

ATOM 697 O GLU A 209 74.968 43.443 27.637

ATOM 698 CB GLU A 209 72.469 45.145 26.270

ATOM 699 CG GLU A 209 71.487 45.233 25.067

ATOM 700 CD GLU A 209 72.103 44.678 23.810

ATOM 701 OEl GLU A 209 72.851 45.434 23.131

ATOM 702 OE2 GLU A 209 71.844 43.487 23.486

ATOM 703 HA GLU A 209 73.152 43.101 25.915

ATOM 704 HBl GLU A 209 72.045 45.722 27.107

ATOM 705 HB2 GLU A 209 73.417 45.625 25. .975

ATOM 706 HGl GLU A 209 70.542 44.709 25. 110

ATOM 707 HG2 GLU A 209 71.235 46.292 24.

ATOM 708 H GLU A 209 70.675 43.536 27.257

ATOM 709 N LEU A 210 73.375 44.160 29.077

ATOM 710 CA LEU A 210 74.292 44.286 30.209

ATOM 711 C LEU A 210 74.879 42.945 30.603

ATOM 712 O LEU A 210 76.020 42.913 31.040

ATOM 713 CB LEU A 210 73.570 44.925 31.427

ATOM 714 CG LEU A 210 73.194 46.425 31.245

ATOM 715 CDl LEU A 210 72. 109 46.819 32.282

ATOM 716 CD2 LEU A 210 74. 421 47.360 31.423

ATOM 717 HA LEU A 210 75.128 44.935 29.906 ATOM 718 HBl LEU A 210 72.666 44.339 31.641

ATOM 719 HB2 LEU A 210 74.229 44.850 32.295

ATOM 720 HG LEU A 210 72.779 46.584 30.235

ATOM 721 HD21 LEU A 210 75.242 47.091 30.747

ATOM 722 HD22 LEU A 210 74.137 48.397 31.195

ATOM 723 HD23 LEU A 210 74.786 47.314 32.460

ATOM 724 HDIl LEU A 210 72.419 46.544 33.299

ATOM 725 HD12 LEU A 210 71.928 47.902 32.257

ATOM 726 HDl 3 LEU A 210 71.169 46.303 32.049

ATOM 727 H LEU A 210 72.411 44.380 29.225

ATOM 728 N GLU A 211 74.130 41.828 30.463

ATOM 729 CA GLU A 211 74.704 40.512 30.753

ATOM 730 C GLU A 211 75.696 40.084 29.697

ATOM 731 O GLU A 211 76.692 39.471 30.049

ATOM 732 CB GLU A 211 73.651 39.371 30.806

ATOM 733 CG GLU A 211 72.728 39.494 32.043

ATOM 734 CD GLU A 211 71.764 38.336 32.103

ATOM 735 OEl GLU A 211 71.164 37.998 31.046

ATOM 736 OE2 GLU A 211 71.593 37.749 33.207

ATOM 737 HA GLU A 211 75.209 40.534 31.733

ATOM 738 HBl GLU A 211 73.060 39.371 29.877

ATOM 739 HB2 GLU A 211 74.167 38.397 30.881

ATOM 740 HGl GLU A 211 73.336 39.513 32.961

ATOM 741 HG2 GLU A 211 72.172 40.438 31.987

ATOM 742 H GLU A 211 73.187 41.882 30.132

ATOM 743 N SER A 212 75.414 40.347 28.402

ATOM 744 CA SER A 212 76.184 39.703 27.338

ATOM 745 C SER A 212 77.393 40.529 26.981

ATOM 746 O SER A 212 77.780 41.402 27.733

ATOM 747 CB SER A 212 75.256 39.470 26.118

ATOM 748 OG SER A 212 74.755 40.740 25.671

ATOM 749 HA SER A 212 76.544 38.718 27.680

ATOM 750 OT SER A 212 77.989 40.336 25.934

ATOM 751 HBl SER A 212 75.808 38.962 25.309

ATOM 752 HB2 SER A 74.414 38. Il 26.430

ATOM 753 HG SER A 212 74.158 40.655 24.934

ATOM 754 H SER A 212 74.646 40.938 28.147

TER 755 SER A 212

ATOM 756 N ALA B 157 11.384 43.624 33.565

ATOM 757 CA ALA B 157 12.817 43.762 33.820

ATOM 758 C ALA B 157 13.623 42.545 34.252

ATOM 759 O ALA B 157 14.809 .720 34.482

ATOM 760 CB ALA B 157 12.872 44.809 34.961

ATOM 761 HA ALA B 157 13.293 44.185 32.921

ATOM 762 HBl ALA B 157 13.902 44.991 35.302

ATOM 763 HB2 ALA B 157 12.439 45.766 34.632

ATOM 764 HB3 ALA B 157 12.274 44.434 35.803

ATOM 765 HNCA ALA B 157 10.910 44.324 33.027

ATOM 766 H ALA B 157 10.872 42.856 33.943

ATOM 767 N ARG B 158 13.066 41.320 34.396

ATOM 768 CA ARG B 158 13.845 40.219 34.968

ATOM 769 C ARG B 158 14.868 39.741 33.969

ATOM 770 O ARG B 158 15.935 39.317 34.382

ATOM 771 CB ARG B 158 12.919 39.069 35.406

ATOM 772 CG ARG B 158 11.999 39.510 36.547

ATOM 773 CD ARG B 158 10.784 38.587 36.660

ATOM 774 NE ARG B 158 9.911 39.033 37.768

ATOM 775 CZ ARG B 158 8.760 38.421 38.118

ATOM 776 NHl ARG B 158 8.364 37.340 37.432

ATOM 111 NH2 ARG B 158 8.024 38.887 39.136

ATOM 778 HA ARG B 158 14.381 40.588 35.859

ATOM 779 HBl ARG B 158 13.530 38.225 35.727

ATOM 780 HB2 ARG B 158 12.309 38.763 34.557

ATOM 781 HGl ARG B 158 11.673 40.533 36.362

ATOM 782 HG2 ARG B 158 12.557 39.479 37.483

ATOM 783 HDl ARG B 158 11.120 37.566 36.839

ATOM 784 HD2 ARG B 158 10.219 38.616 35.728

ATOM 785 HE ARG B 158 10.226 39.857 38.280 ATOM 786 HHl 2 ARG I5 158 7.497 36.865 37.683

ATOM 787 HHIl ARG Ii 158 8.931 36.991 36.658

ATOM 788 HH22 ARG I 5 158 7.155 38.418 39.394

ATOM 789 HH21 ARG I I 158 8.332 39.710 39.653

ATOM 790 H ARG I I 158 12.129 41.129 34.118

ATOM 791 N LEU Ii 159 14.560 39.802 32.655

ATOM 792 CA LEU I 5 159 15.519 39.345 31.655

ATOM 793 C LEU I I 159 16.671 40.315 31.782

ATOM 794 O LEU I I 159 17.773 39.888 3 074

ATOM 795 CB LEU Ii 159 14.920 39.335 30.214

ATOM 796 CG LEU I 5 159 13.660 38.426 30.049

ATOM 797 CDl LEU I I 159 12.773 38.927 28.873

ATOM 798 CD2 LEU I I 159 14.043 36.937 29.827

ATOM 799 HA LEU Ii 159 15.853 38.324 31.903

ATOM 800 HBl LEU I 5 159 14.633 40.362 29.949

ATOM 801 HB2 LEU I I 159 15.699 39.024 29.499

ATOM 802 HG LEU I I 159 13.035 38.470 30.956

ATOM 803 HD21 LEU Ii 159 14.652 36.562 30.662

ATOM 804 HD22 LEU I 5 159 13.135 36.316 29.758

ATOM 805 HD23 LEU I I 159 14.612 36.821 28.892

ATOM 806 HDIl LEU I I 159 13.344 38.,931 27.932

ATOM 807 HD12 LEU Ii 159 11.890 38.,280 28.748

ATOM 808 HD13 LEU I 5 159 12.415 39.950 29.071

ATOM 809 H LEU I 5 159 13.700 40.206 32.346

ATOM 810 N ALA I I 160 16.412 41.,630 31.599

ATOM 811 CA ALA I I 160 17.458 42..647 31.733

ATOM 812 C ALA Ii 160 18.254 4: .479 33.011

ATOM 813 O ALA I 5 160 19.463 42.644 32.989

ATOM 814 CB ALA I I 160 16.845 44.073 31.751

ATOM 815 HA ALA I I 160 18.137 42.584 30.867

ATOM 816 HBl ALA Ii 160 17.636 44.830 31.869

ATOM 817 HB2 ALA I 5 160 16.311 44.267 30.807

ATOM 818 HB3 ALA I I 160 16.134 44, ,174 32.585

ATOM 819 H ALA I I 160 15.486 41 ,932 31.371

ATOM 820 N ALA Ii 161 17.596 42 ,150 34.143

ATOM 821 CA ALA Ii 161 18.331 41.923 35.388

ATOM 822 C ALA Ii 161 19.247 40.725 35.252

ATOM 823 O ALA I I 161 20.419 40.819 35.582

ATOM 824 CB ALA Ii 161 17.381 41.693 36.593

ATOM 825 HA ALA Ii 161 18.931 42.816 35.635

ATOM 826 HBl ALA Ii 161 17.965 41.577 37.519

ATOM 827 HB2 ALA I I 161 16.701 42.551 36.710

ATOM 828 HB3 ALA Ii 161 16.780 40.784 36.449

ATOM 829 H ALA Ii 161 16.599 42.049 34.143

ATOM 830 N ASP Ii 162 18.722 39.576 34.772

ATOM 831 CA ASP I I 162 19.544 38.364 34.681

ATOM 832 C ASP Ii 162 20.655 38.629 33.684

ATOM 833 O ASP Ii 162 21.783 38.236 33.935

ATOM 834 CB ASP Ii 162 18.676 37.141 34.276

ATOM 835 CG ASP Ii 162 19.299 35.854 34.754

ATOM 836 ODl ASP I I 162 18.714 35.208 35.668

ATOM 837 OD2 ASP Ii 162 20.379 35.482 34.225

ATOM 838 HA ASP Ii 162 19.986 38.170 35.674

ATOM 839 HBl ASP Ii 162 17.682 37.221 34.746

ATOM 840 HB2 ASP I I 162 18.531 37.116 33.185

ATOM 841 H ASP Ii 162 17.770 39.549 34.464

ATOM 842 N ASP Ii 163 20.348 39.326 32.561

ATOM 843 CA ASP I I 163 21.382 39.767 31.630

ATOM 844 C ASP I I 163 22.460 40.433 32.451

ATOM 845 O ASP Ii 163 23.597 39.995 32.431

ATOM 846 CB ASP I 5 163 20.886 40.769 30.546

ATOM 847 CG ASP I I 163 20.036 40.131 29.479

ATOM 848 ODl ASP I I 163 20.272 40.415 28.273

ATOM 849 OD2 ASP Ii 163 19.117 39.346 29.837

ATOM 850 HA ASP I 5 163 790 38.890 31.106

ATOM 851 HBl ASP I I 163 274 41.555 30.992

ATOM 852 HB2 ASP I I 163 747 41.275 30.087

ATOM 853 H ASP Ii 163 19.410 39.588 32.363 ATOM 854 N PHE I5 164 22.040 41.448 33.306

ATOM 855 CA PHE Ii 164 23.069 42.220 33.990

ATOM 856 C PHE Ii 164 23.814 41.322 34.945

ATOM 857 O PHE Ii 164 24.996 41.510 35.180

ATOM 858 CB PHE I I 164 22.505 43.424 34.793

ATOM 859 CG PHE Ii 164 22.316 44.646 33.882

ATOM 860 CDl PHE Ii 164 21.044 45.135 33.566

ATOM 861 CD2 PHE Ii 164 23.444 45.284 33.353

ATOM 862 CEl PHE I I 164 20.897 46.133 32.598

ATOM 863 CE2 PHE Ii 164 23.302 46.309 32.414

ATOM 864 CZ PHE Ii 164 22.026 46.717 32.017

ATOM 865 HA PHE Ii 164 23.771 42.591 33.229

ATOM 866 HBl PHE I I 164 21.576 43.140 35.310

ATOM 867 HB2 PHE Ii 164 23.236 43.718 35.558

ATOM 868 HD2 PHE Ii 164 24.439 44.985 33.668

ATOM 869 HE2 PHE Ii 164 24.181 46.785 31.993

ATOM 870 HZ PHE I I 164 21.913 47.486 31.259

ATOM 871 HEl PHE Ii 164 19.905 46.456 32.295

ATOM 872 HDl PHE Ii 164 20.167 44.747 34.071

ATOM 873 H PHE Ii 164 21.182 41.906 33.062

ATOM 874 N ARG I I 165 23.244 40.371 35.521

ATOM 875 CA ARG Ii 165 23.998 39.544 36.454

ATOM 876 C ARG I 5 165 25.095 38.798 35.736

ATOM 877 O ARG I 5 165 26.179 38.687 36.285

ATOM 878 CB ARG I I 165 23.107 38.546 37.239

ATOM 879 CG ARG I I 165 22.177 39.286 38.240

ATOM 880 CD ARG Ii 165 21.405 38.296 39.155

ATOM 881 NE ARG I 5 165 22.289 37.640 40.124

ATOM 882 CZ ARG I I 165 21.890 36.690 40.944

ATOM 883 NHl ARG I I 165 22.762 36.162 41.774

ATOM 884 NH2 ARG Ii 165 20.654 36.246 40.970

ATOM 885 HA ARG I 5 165 24.485 40.206 37.189

ATOM 886 HBl ARG I I 165 22.514 37.948 36.530

ATOM 887 HB2 ARG I I 165 23.764 37.857 37.794

ATOM 888 HGl ARG Ii 165 22.769 39.960 38.877

ATOM 889 HG2 ARG I 5 165 21.456 39.904 37.685

ATOM 890 HDl ARG I I 165 20.633 38.861 39.706

ATOM 891 HD2 ARG I I 165 20.918 37.557 38.498

ATOM 892 HE ARG Ii 165 23.273 37.948 40.158

ATOM 893 HHl 2 ARG I 5 165 22.487 35.418 42.432

ATOM 894 HHIl ARG I I 165 23.744 36.479 41.791

ATOM 895 HH22 ARG I I 165 20.376 35.498 41.622

ATOM 896 HH21 ARG Ii 165 19.928 36.627 40.351

ATOM 897 H ARG I 5 165 22.275 40.180 35.348

ATOM 898 N VAL I I 166 24.855 38.280 34.513

ATOM 899 CA VAL I I 166 25.920 37.554 33.819

ATOM 900 C VAL Ii 166 26.981 38.576 33.474

ATOM 901 O VAL I 5 166 28.149 38.359 33.759

ATOM 902 CB VAL I 5 166 25.442 36.852 32.511

ATOM 903 CGl VAL I I 166 26.640 36.139 31.829

ATOM 904 CG2 VAL I I 166 24.299 35.827 32.760

ATOM 905 HA VAL Ii 166 26.339 36.782 34.488

ATOM 906 HB VAL I 5 166 25.053 37.611 31.811

ATOM 907 HGIl VAL I I 166 27.064 35.363 32.485

ATOM 908 HG12 VAL I I 166 26.301 35.665 30.903

ATOM 909 HGl 3 VAL Ii 166 27.432 36.853 31.564

ATOM 910 HG21 VAL I 5 166 23.417 36.304 33.209

ATOM 911 HG22 VAL I I 166 23.980 35.380 31.805

ATOM 912 HG23 VAL I I 166 24.638 35.022 33.429

ATOM 913 H VAL Ii 166 23.978 38.437 34.056

ATOM 914 N LYS I 5 167 26.541 39.696 32.849

ATOM 915 CA LYS Ii 167 27.436 40.789 32.475

ATOM 916 C LYS I I 167 28.383 41.060 33.630

ATOM 917 O LYS Ii 167 29.590 40.915 33.525

ATOM 918 CB LYS Ii 167 26.632 42.084 32.140

ATOM 919 CG LYS Ii 167 25.748 42.087 30.857

ATOM 920 CD LYS I I 167 26.591 42.239 29.565

ATOM 921 CE LYS Ii 167 25.744 42.716 28.356 ATOM 922 NZ LYS I5 167 26.605 42.931 27.170

ATOM 923 HA LYS Ii 167 28.021 40.503 31.597

ATOM 924 HBl LYS Ii 167 25.970 42.319 32.974

ATOM 925 HB2 LYS Ii 167 27.334 42.918 32.075

ATOM 926 HGl LYS I I 167 25.116 41.190 30.782

ATOM 927 HG2 LYS Ii 167 25.075 42,.959 30.922

ATOM 928 HDl LYS Ii 167 27.388 42,.974 29.725

ATOM 929 HD2 LYS Ii 167 27.071 41, >84 29.329

ATOM 930 HEl LYS I I 167 24.963 41.972 28.138

ATOM 931 HE2 LYS Ii 167 25.239 43.664 28.606

ATOM 932 HZl LYS Ii 167 27.179 42.051 26.918

ATOM 933 HZ2 LYS Ii 167 26.021 43.191 26.298

ATOM 934 HZ3 LYS I I 167 27.307 43.739 27.335

ATOM 935 H LYS Ii 167 25.571 39.790 32.634

ATOM 936 N TYR Ii 168 27.805 41.449 34.781

ATOM 937 CA TYR I I 168 28.597 41.810 35.953

ATOM 938 C TYR I I 168 29.473 40.655 36.385

ATOM 939 O TYR Ii 168 30.665 40.854 36.553

ATOM 940 CB TYR I 5 168 27.580 42.173 37.069

ATOM 941 CG TYR I I 168 28.260 42.694 38.329

ATOM 942 CDl TYR I I 168 28.822 43.972 38.300

ATOM 943 CD2 TYR Ii 168 28.313 41.934 39.502

ATOM 944 CEl TYR I 5 168 29.414 44.495 39.448

ATOM 945 CE2 TYR I 5 168 28.830 42.498 40.672

ATOM 946 CZ TYR I I 168 29.374 43.785 40.654

ATOM 947 OH TYR I I 168 29.869 44.338 41.838

ATOM 948 HA TYR Ii 168 29.231 42.687 35.722

ATOM 949 HB2 TYR I 5 168 26.914 .972 36.704

ATOM 950 HBl TYR I I 168 26.953 41.303 37.309

ATOM 951 HD2 TYR I I 168 27.951 40.911 39.511

ATOM 952 HE2 TYR Ii 168 28.810 41.935 41.600

ATOM 953 HEl TYR I 5 168 29.899 45.455 39.379

ATOM 954 HDl TYR I I 168 28.797 44.560 37.389

ATOM 955 HH TYR I I 168 30.327 45.160 41.713

ATOM 956 H TYR Ii 168 26.809 41.510 34.844

ATOM 957 N GLU I 5 169 28.900 39.443 36.566

ATOM 958 CA GLU I I 169 29.686 38.289 37.011

ATOM 959 C GLU I I 169 30.938 38.130 36.178

ATOM 960 O GLU Ii 169 31.982 37.809 36.724

ATOM 961 CB GLU I 5 169 28.883 36.959 36.971

ATOM 962 CG GLU I I 169 27.919 36.835 38.183

ATOM 963 CD GLU I I 169 27.013 35.644 38.007

ATOM 964 OEl GLU Ii 169 27.521 34.493 38.099

ATOM 965 OE2 GLU I 5 169 25.790 35.845 37.774

ATOM 966 HA GLU I I 169 29.990 38.464 38.057

ATOM 967 HBl GLU I I 169 28.329 36.901 36.022

ATOM 968 HB2 GLU Ii 169 29.576 36.102 37.008

ATOM 969 HGl GLU I 5 169 28.503 36.703 39.108

ATOM 970 HG2 GLU I 5 169 27.318 37.749 38.301

ATOM 971 H GLU I I 169 27.919 39.326 36.416

ATOM 972 N THR I I 170 30.833 38.310 34.807

ATOM 973 CA THR Ii 170 32.040 38.209 33.991

ATOM 974 C THR Ii 170 32.964 39.351 34.316

ATOM 975 O THR Ii 170 34.105 39.141 34.695

ATOM 976 CB THR I I 170 31.734 38.265 32.438

ATOM 977 OGl THR Ii 170 31.302 39.605 32.133

ATOM 978 CG2 THR Ii 170 30.580 37.283 32.090

ATOM 979 HA THR Ii 170 32.543 37.256 34.225

ATOM 980 HB THR I I 170 32.585 38.090 31.732

ATOM 981 HGl THR Ii 170 31.103 39.768 31.216

ATOM 982 HG23 THR Ii 170 30.937 36.485 31.441

ATOM 983 HG21 THR Ii 170 30.135 36.805 32.973

ATOM 984 HG22 THR I I 170 29.778 37.796 31.548

ATOM 985 H THR Ii 170 30.056 38.840 34.453

ATOM 986 N GLU Ii 111 32.463 40.605 34.163

ATOM 987 CA GLU Ii 111 33.318 41.786 34.190

ATOM 988 C GLU I I 111 34.077 41.822 35.500

ATOM 989 O GLU Ii 111 35.285 41.993 35.495 ATOM 990 CB GLU B 171 32.542 43.122 34.011

ATOM 991 CG GLU B 171 31.924 43.326 32.599

ATOM 992 CD GLU B 171 32.893 43.438 31.452

ATOM 993 OEl GLU B 171 32.438 43.378 30.276

ATOM 994 OE2 GLU B 171 34.111 43.606 31.710

ATOM 995 HA GLU B 171 34.045 41.709 33.366

ATOM 996 HBl GLU B 171 31.730 43.165 34.756

ATOM 997 HB2 GLU B 171 33.227 43.963 34.209

ATOM 998 HGl GLU B 171 31.198 42.531 32.376

ATOM 999 HG2 GLU B 171 31.402 44.293 32.620

ATOM 1000 H GLU B 171 31.484 40.706 33.974

ATOM 1001 N LEU B 172 33.342 41.642 36.619

ATOM 1002 CA LEU B 172 33.942 41.566 37.953

ATOM 1003 C LEU B 172 35.136 40.648 37.952

ATOM 1004 O LEU B 172 36.193 41.044 38.408

ATOM 1005 CB LEU B 172 32.867 41.097 38.984

ATOM 1006 CG LEU B 172 33.280 40.825 40.472

ATOM 1007 CDl LEU B 172 32.028 41.171 41.334

ATOM 1008 CD2 LEU B 172 33.675 39.326 40.764

ATOM 1009 HA LEU B 172 34.267 42.573 38.269

ATOM 1010 HBl LEU B 172 32.082 41.873 38.927

ATOM 1011 HB2 LEU B 172 32.399 40.171 38.632

ATOM 1012 HG LEU B 172 34.082 41.514 40.807

ATOM 1013 HD21 LEU B 172 34.572 38.959 40.243

ATOM 1014 HD22 LEU B 172 33. 39.282 41.839

ATOM 1015 HD23 LEU B 172 32. 38.575 40.575

ATOM 1016 HDIl LEU B 172 31.162 40.564 41.026

ATOM 1017 HD12 LEU B 172 32.223 40.982 42.397

ATOM 1018 HD13 LEU B 172 31.749 42.233 41.232

ATOM 1019 H LEU B 172 32.349 41.556 36.540

ATOM 1020 N ALA B 173 35.011 39.405 37.451

ATOM 1021 CA ALA B 173 36.150 38.500 37.545

ATOM 1022 C ALA B 173 37.311 38.832 36.636

ATOM 1023 O ALA B 173 38.434 38.513 36.993

ATOM 1024 CB ALA B 173 35.756 37.048 37.236

ATOM 1025 HA ALA B 173 36.521 38.504 38.584

ATOM 1026 HBl ALA B 173 36.673 36.449 37.330

ATOM 1027 HB2 ALA B 173 35.010 36.698 37.965

ATOM 1028 HB3 ALA B 173 35.355 36.960 36.213

ATOM 1029 H ALA B 173 34.149 39.072 37.058

ATOM 1030 N MET B 174 37.084 39.440 35.453

ATOM 1031 CA MET B 174 38.207 39.759 34.574

ATOM 1032 C MET B 174 38.886 41.036 35.013

ATOM 1033 O MET B 174 40.077 41.193 34.793

ATOM 1034 CB MET B 174 37.766 39.722 33.086

ATOM 1035 CG MET B 174 37.430 38.266 32.644

ATOM 1036 SD MET B 174 35.742 37.681 32.985

ATOM 1037 CE MET B 174 36.044 35.881 32.933

ATOM 1038 HA MET B 174 38.978 38.989 34.711

ATOM 1039 HBl MET B 174 36.917 40.402 32.906

ATOM 1040 HB2 MET B 174 38.619 40.075 32.482

ATOM 1041 HGl MET B 174 37.611 38.145 31.575

ATOM 1042 HG2 MET B 174 38.081 37.547 33.139

ATOM 1043 HEl MET B 174 36.702 35.590 33.766

ATOM 1044 HE2 MET B 174 35.094 35.338 33.025

ATOM 1045 HE3 MET B 174 36.523 35.613 31.979

ATOM 1046 LPDl MET B 174 35.303 37.879 32.506

ATOM 1047 LPD2 MET B 174 35.520 37.884 33.594

ATOM 1048 H MET B 174 36.160 39.709 35.180

ATOM 1049 N ARG B 175 38.142 41.937 35.685

ATOM 1050 CA ARG B 175 38.779 42.991 36.469

ATOM 1051 C ARG B 175 39.752 42.362 37.437

ATOM 1052 O ARG B 175 40.912 42.741 37.469

ATOM 1053 CB ARG B 175 37.706 43.817 37. 10

ATOM 1054 CG ARG B 175 38.230 44.927 38.167

ATOM 1055 CD ARG B 175 37.115 45.126 39.256

ATOM 1056 NE ARG B 175 37.107 44.115 40.348

ATOM 1057 CZ ARG B 175 36.064 43.728 41.076 ATOM 1058 NHl ARG B 175 36.223 42.934 42.121

ATOM 1059 NH2 ARG B 175 34.826 44.096 40.843

ATOM 1060 HA ARG B 175 39.335 43.669 35.835

ATOM 1061 HBl ARG B 175 37.006 44.259 36.491

ATOM 1062 HB2 ARG B 175 37.137 43.119 37.840

ATOM 1063 HGl ARG B 175 39.188 44.649 38.634

ATOM 1064 HG2 ARG B 175 38.435 45.825 37.550

ATOM 1065 HDl ARG B 175 37.285 46.089 39.745

ATOM 1066 HD2 ARG B 175 36.178 45.206 38.690

ATOM 1067 HE ARG B 175 38.017 43.683 40.560

ATOM 1068 HH12 ARG B 175 35.412 42.561 42.645

ATOM 1069 HHIl ARG B 175 37.154 42.686 42.481

ATOM 1070 HH22 ARG B 175 34.055 43.818 41.471

ATOM 1071 HH21 ARG B 175 34.580 44.678 40.045

ATOM 1072 H ARG B 175 37.146 41.851 35.715

ATOM 1073 N GLN B 176 39.279 41.386 38. >39

ATOM 1074 CA GLN B 176 40.144 40.797 39. ^?55

ATOM 1075 C GLN B 176 41.374 40.191 38.619

ATOM 1076 O GLN B 176 42.469 40.334 39.136

ATOM 1077 CB GLN B 176 39.375 39.768 40.118

ATOM 1078 CG GLN B 176 38.273 40.384 41.020

ATOM 1079 CD GLN B 176 37.540 39.306 41.788

ATOM 1080 OEl GLN B 176 37.115 38.340 41.173

ATOM 1081 NE2 GLN B 176 37.366 39.439 43.123

ATOM 1082 HA GLN B 176 40.455 41.588 39.960

ATOM 1083 HBl GLN B 176 38.986 38.957 39.486

ATOM 1084 HB2 GLN B 176 40.103 39.365 40.821

ATOM 1085 HGl GLN B 176 38.744 41.107 41.703

ATOM 1086 HG2 GLN B 176 37.531 40.926 40.423

ATOM 1087 HE22 GLN B 176 36.855 38.747 43.632

ATOM 1088 HE21 GLN B 176 37.733 40.220 43.628

ATOM 1089 H GLN B 176 38.334 41.070 38.153

ATOM 1090 N SER B 177 41.213 39.472 37.492

ATOM 1091 CA SER B 177 42.377 38.902 36.821

ATOM 1092 C SER B 177 43.414 39.960 36.502

ATOM 1093 O SER B 177 44.522 39.877 37.010

ATOM 1094 CB SER B 177 41.997 38.152 35.531

ATOM 1095 OG SER B 177 41.109 37.066 35.787

ATOM 1096 HA SER B 177 42.833 38.141 37.476

ATOM 1097 HBl SER B 177 42.911 37.783 35.065

ATOM 1098 HB2 SER B 177 41.512 38.854 34.853

ATOM 1099 HG SER B 177 40.902 36.630 34.957

ATOM 1100 H SER B 177 40.299 39.289 37.128

ATOM 1101 N VAL B 178 43.066 40.951 35.649

ATOM 1102 CA VAL B 178 44.064 41.897 35.140

ATOM 1103 C VAL B 178 44.611 42.664 36.334

ATOM 1104 O VAL B 178 45.815 42 849 36.402

ATOM 1105 CB VAL B 178 43.476 42 769 33.990

ATOM 1106 CGl VAL B 178 44.495 43 829 33.493

ATOM 1107 CG2 VAL B 178 43.071 41.878 32.778

ATOM 1108 HA VAL B 178 44.909 41.325 34.719

ATOM 1109 HB VAL B 178 42.585 43.292 34.376

ATOM 1110 HGIl VAL B 178 45.379 43.341 33.055

ATOM 1111 HG12 VAL B 178 44.035 44.477 32.731

ATOM 1112 HG13 VAL B 178 44.826 44.457 34.326

ATOM 1113 HG21 VAL B 178 42.430 41.032 33.064

ATOM 1114 HG22 VAL B 178 42.526 .476 32.036

ATOM 1115 HG23 VAL B 178 43.970 41.474 32.293

ATOM 1116 H VAL B 178 42.111 41.054 35.365

ATOM 1117 N GLU B 179 43.756 43.069 37.308

ATOM 1118 CA GLU B 179 44.225 43.700 38.553

ATOM 1119 C GLU B 179 45.562 43.177 39.049

ATOM 1120 O GLU B 179 46.401 43.996 39.388

ATOM 1121 CB GLU B 179 43.205 43.493 39.714

ATOM 1122 CG GLU B 179 43.604 44.102 41.091

ATOM 1123 CD GLU B 179 42.881 43.361 42.191

ATOM 1124 OEl GLU B 179 41.811 43.849 42.645

ATOM 1125 OE2 GLU B 179 43.379 42.276 42.603 ATOM 1126 HA GLU B 179 44.289 44.784 38.381

ATOM 1127 HBl GLU B 179 42.211 43.880 39.441

ATOM 1128 HB2 GLU B 179 43.117 42.414 39.861

ATOM 1129 HGl GLU B 179 44.681 44.023 41.291

ATOM 1130 HG2 GLU B 179 43.342 45.169 41.133

ATOM 1131 H GLU B 179 42.767 42.971 37.183

ATOM 1132 N ASN B 180 45.767 41.842 39.149

ATOM 1133 CA ASN B 180 46.963 41.303 39.815

ATOM 1134 C ASN B 180 48.057 40.916 38.862

ATOM 1135 O ASN B 180 49.209 41.007 39.255

ATOM 1136 CB ASN B 180 46.467 40.157 40.721

ATOM 1137 CG ASN B 180 47.467 39.461 41.601

ATOM 1138 ODl ASN B 180 47.734 39.869 42.719

ATOM 1139 ND2 ASN B 180 48.027 38.346 41.123

ATOM 1140 HA ASN B 180 47.395 42.080 40.454

ATOM 1141 HBl ASN B 180 45.698 40.580 41.382

ATOM 1142 HB2 ASN B 180 46.008 39.398 40.069

ATOM 1143 HD22 ASN B 180 48.633 37.835 41.734

ATOM 1144 HD21 ASN B 180 47.937 38.102 40.152

ATOM 1145 H ASN B 180 45.063 41.207 38.826

ATOM 1146 N ASP B 181 47.758 40.530 37.604

ATOM 1147 CA ASP B 181 48.854 40.374 36.653

ATOM 1148 C ASP B 181 49.578 41.705 36.595

ATOM 1149 O ASP B 181 50.778 41.716 36.381

ATOM 1150 CB ASP B 181 48.310 39.915 35.279

ATOM 1151 CG ASP B 181 47.392 38.732 35.487

ATOM 1152 ODl ASP B 181 47.852 37.694 36.033

ATOM 1153 OD2 ASP B 181 46.194 38.832 35.105

ATOM 1154 HA ASP B 181 49.533 39.597 37.043

ATOM 1155 HBl ASP B 181 47.759 40.747 34.812

ATOM 1156 HB2 ASP B 181 49.148 39.637 34.620

ATOM 1157 H ASP B 181 46.812 40.450 37.288

ATOM 1158 N ILE B 182 48.867 42.840 36.820

ATOM 1159 CA ILE B 182 49.546 44.132 36.919

ATOM 1160 C ILE B 182 50.488 44.094 38.105

ATOM 1161 O ILE B 182 51.667 44.342 37.909

ATOM 1162 CB ILE B 182 48.568 45.328 37.042

ATOM 1163 CGl ILE B 182 47.727 45.504 35.741

ATOM 1164 CG2 ILE B 182 49.329 46.648 37.337

ATOM 1165 CDl ILE B 182 46.416 46.239 36.098

ATOM 1166 HA ILE B 182 50.131 44.292 35.999

ATOM 1167 HB ILE B 182 47.923 45.132 37.910

ATOM 1168 HGIl ILE B 182 48.287 46.113 35.024

ATOM 1169 HG12 ILE B 182 47.502 44.565 35.204

ATOM 1170 HDIl ILE B 182 46.555 47.219 36.572

ATOM 1171 HD12 ILE B 182 45.828 46.378 35.189

ATOM 1172 HD13 ILE B 182 45.869 45.612 36.810

ATOM 1173 HG21 ILE B 182 49.953 46.871 36.464

ATOM 1174 HG22 ILE B 182 48.644 47.489 37.507

ATOM 1175 HG23 ILE B 182 49.975 46.575 38.223

ATOM 1176 H ILE B 182 47.876 42.826 36.968

ATOM 1177 N HIS B 183 50.002 43.795 39.337

ATOM 1178 CA HIS B 183 50.897 43.703 40.497

ATOM 1179 C HIS B 183 52.117 42.882 40.130

ATOM 1180 O HIS B 183 53.223 43.255 40.492

ATOM 1181 CB HIS B 183 50.193 43.118 41.753

ATOM 1182 CG HIS B 183 48.904 43.827 42.114

ATOM 1183 NDl HIS B 183 48.624 45.090 41.865

ATOM 1184 CD2 HIS B 183 47.858 43.256 42.744

ATOM 1185 CEl HIS B 183 47.434 45.371 42.292

ATOM 1186 NE2 HIS B 183 46.930 44.350 42.815

ATOM 1187 HA HIS B 183 51.238 44.721 40.749

ATOM 1188 HBl HIS B 183 49.979 42.051 41.584

ATOM 1189 HB2 HIS B 183 50.878 43.194 42.612

ATOM 1190 HD2 HIS B 183 47.729 42.242 43.109

ATOM 1191 HEl HIS B 183 46.935 46.337 42.218

ATOM 1192 HDl HIS B 183 49.247 45.764 41.398

ATOM 1193 H HIS B 183 49.023 43.650 39.481 ATOM 1194 N GLY B 184 51.927 41.770 39.383

ATOM 1195 CA GLY B 184 53.067 40.954 38.981

ATOM 1196 C GLY B 184 53.957 41.739 38.086

ATOM 1197 O GLY B 184 55.066 42.068 38.467

ATOM 1198 HA2 GLY B 184 52.799 40.088 38.354

ATOM 1199 HAl GLY B 184 53.593 40.599 39.876

ATOM 1200 H GLY B 184 51.010 41.495 39.091

ATOM 1201 N LEU B 185 53.430 42.038 36.882

ATOM 1202 CA LEU B 185 54.207 42.771 35.899

ATOM 1203 C LEU B 185 54.916 43.957 36.538

ATOM 1204 O LEU B 185 55.964 44.322 36.036

ATOM 1205 CB LEU B 185 53.343 43.233 34.707

ATOM 1206 CG LEU B 185 52.783 42.108 33.783

ATOM 1207 CDl LEU B 185 51.502 42.641 33.088

ATOM 1208 CD2 LEU B 185 53. Il 41.659 32.717

ATOM 1209 HA LEU B 185 54.944 42.076 35.474

ATOM 1210 HBl LEU B 185 52.534 43.855 35.119

ATOM 1211 HB2 LEU B 185 54.000 43.841 34.077

ATOM 1212 HG LEU B 185 52.502 41.216 34.366

ATOM 1213 HD21 LEU B 185 54.731 41.259 33.200

ATOM 1214 HD22 LEU B 185 53.408 40.870 32.073

ATOM 1215 HD23 LEU B 185 54.118 42.504 32.074

ATOM 1216 HDIl LEU B 185 51.697 43.634 32.664

ATOM 1217 HD12 LEU B 185 51.173 41.966 32.284

ATOM 1218 HD13 LEU B 185 50.687 42.740 33.821

ATOM 1219 H LEU B 185 52.507 41.736 36.643

ATOM 1220 N ARG B 186 54.395 44.583 37.623

ATOM 1221 CA ARG B 186 55.131 45.648 38.319

ATOM 1222 C ARG B 186 56.282 45.090 39.135

ATOM 1223 O ARG B 186 57.421 45.465 38.907

ATOM 1224 CB ARG B 186 54.237 46.507 39.256

ATOM 1225 CG ARG B 186 53.319 47.470 38.458

ATOM 1226 CD ARG B 186 52.417 48.304 39.410

ATOM 1227 NE ARG B 186 53.210 49.186 40.272

ATOM 1228 CZ ARG B 186 52.767 49.706 41.399

ATOM 1229 NHl ARG B 186 53.593 50.422 42.129

ATOM 1230 NH2 ARG B 186 51.536 49.548 41.831

ATOM 1231 HA ARG B 186 55.557 46.337 37.578

ATOM 1232 HBl ARG B 186 53.616 45.858 39.892

ATOM 1233 HB2 ARG B 186 54.889 47.099 39.919

ATOM 1234 HGl ARG B 186 53.928 48.152 37.844

ATOM 1235 HG2 ARG B 186 52.692 46.861 37.790

ATOM 1236 HDl ARG B 186 51.721 48.929 38.827

ATOM 1237 HD2 ARG B 186 51.842 47.562 39.984

ATOM 1238 HE ARG B 186 54.181 49.383 39.981

ATOM 1239 HH12 ARG B 186 53.287 50.845 43.018

ATOM 1240 HHIl ARG B 186 54.570 50.577 41.836

ATOM 1241 HH22 ARG B 186 51.235 49.961 42.726

ATOM 1242 HH21 ARG B 186 50.831 49.033 41.291

ATOM 1243 H ARG B 186 53.509 44.303 37.990

ATOM 1244 N LYS B 187 55.987 44.194 40.103

ATOM 1245 CA LYS B 187 57.037 43.521 40.887

ATOM 1246 C LYS B 187 58.138 42.989 39.988

ATOM 1247 O LYS B 187 59.317 43.044 40.304

ATOM 1248 CB LYS B 187 56.359 42.457 41.789

ATOM 1249 CG LYS B 187 55.621 43.146 42.981

ATOM 1250 CD LYS B 187 54.502 4. .239 43.549

ATOM 1251 CE LYS B 187 53.908 42. 677 44.913

ATOM 1252 NZ LYS B 187 54.865 42.468 46.027

ATOM 1253 HA LYS B 187 57.512 44.245 41.558

ATOM 1254 HBl LYS B 187 55.647 41.893 41.171

ATOM 1255 HB2 LYS B 187 57.106 41.743 42.175

ATOM 1256 HGl LYS B 187 56.368 43.370 43.758

ATOM 1257 HG2 LYS B 187 55.159 44.099 42.677

ATOM 1258 HDl LYS B 187 53.696 42.140 42.801

ATOM 1259 HD2 LYS B 187 54.951 41.263 43.718

ATOM 1260 HEl LYS B 187 53.582 43.729 44.864

ATOM 1261 HE2 LYS B 187 53.016 42.054 45.106 ATOM 1262 HZl LYS B 187 55.681 43.175 46.009

ATOM 1263 HZ2 LYS B 187 54.380 42 .578 46.987

ATOM 1264 HZ3 LYS B 187 55.296 41.476 46.029

ATOM 1265 H LYS B 187 55.025 43.966 40.265

ATOM 1266 N VAL B 188 57.729 42.489 38.809

ATOM 1267 CA VAL B 188 58.678 42.079 37.773

ATOM 1268 C VAL B 188 59.594 43.217 37.361

ATOM 1269 O VAL B 188 60.792 43.002 37.251

ATOM 1270 CB VAL B 188 57.885 41.538 36.552

ATOM 1271 CGl VAL B 188 58.711 41.597 35.247

ATOM 1272 CG2 VAL B 188 57.330 40.118 36.849

ATOM 1273 HA VAL B 188 59.308 41.264 38.165

ATOM 1274 HB VAL B 188 57.039 42.205 36.374

ATOM 1275 HGIl VAL B 188 59.645 41.040 35.360

ATOM 1276 HG12 VAL B 188 58.110 41 .200 34.417

ATOM 1277 HG13 VAL B 188 58.985 42.629 35.000

ATOM 1278 HG21 VAL B 188 56.681 40.121 37.736

ATOM 1279 HG22 VAL B 188 56.748 39.734 35.997

ATOM 1280 HG23 VAL B 188 58.164 39.435 37.053

ATOM 1281 H VAL B 188 56.749 42.408 38.636

ATOM 1282 N ILE B 189 59.067 44.439 37.106

ATOM 1283 CA ILE B 189 59.936 45.539 36.671

ATOM 1284 C ILE B 189 60.921 45.769 37.796

ATOM 1285 O ILE B 189 62.112 45.874 37.552

ATOM 1286 CB ILE B 189 59.228 46.904 36.374

ATOM 1287 CGl ILE B 189 58.164 46.806 35.247

ATOM 1288 CG2 ILE B 189 60.285 47.970 35.973

ATOM 1289 CDl ILE B 189 57.146 47.976 35.232

ATOM 1290 HA ILE B 189 60.465 45. >04 35.763

ATOM 1291 HB ILE B 189 58.716 47. >34 37.293

ATOM 1292 HGIl ILE B 189 58.652 46.718 34.264

ATOM 1293 HG12 ILE B 189 57.567 45.911 35.415

ATOM 1294 HDIl ILE B 189 57.622 48.952 35.091

ATOM 1295 HD12 ILE B 189 56.444 47.814 34.402

ATOM 1296 HD13 ILE B 189 56.572 48.013 36.168

ATOM 1297 HG21 ILE B 189 60.850 47.644 35.085

ATOM 1298 HG22 ILE B 189 59.829 48.945 35.755

ATOM 1299 HG23 ILE B 189 60.986 48.120 36.800

ATOM 1300 H ILE B 189 58.091 44.607 37.230

ATOM 1301 N ASP B 190 60.434 45.852 39.054

ATOM 1302 CA ASP B 190 61.338 46.054 40.188

ATOM 1303 C ASP B 190 62.477 45.056 40.144

ATOM 1304 O ASP B 190 63.619 45.423 40.368

ATOM 1305 CB ASP B 190 60.603 45.961 41.551

ATOM 1306 CG ASP B 190 59.508 46.997 41.625

ATOM 1307 ODl ASP B 190 58.308 46.615 41.675

ATOM 1308 OD2 ASP B 190 59.841 48.213 41.630

ATOM 1309 HA ASP B 190 61.752 47.073 40.123

ATOM 1310 HBl ASP B 190 60.187 44.953 41.688

ATOM 1311 HB2 ASP B 190 61.316 46.146 42.370

ATOM 1312 H ASP B 190 59.450 45.791 39.225

ATOM 1313 N ASP B 191 62.179 43.769 39.852

ATOM 1314 CA ASP B 191 63.247 42.767 39.790

ATOM 1315 C ASP B 191 64.208 43.078 38.659

ATOM 1316 O ASP B 191 65.392 43.250 38.907

ATOM 1317 CB ASP B 191 62.742 41.300 39.711

ATOM 1318 CG ASP B 191 62.366 40.794 41.083

ATOM 1319 ODl ASP B 191 63.072 39.887 41.606

ATOM 1320 OD2 ASP B 191 61.366 41.306 41.655

ATOM 1321 HA ASP B 191 63.835 42.823 40.719

ATOM 1322 HBl ASP B 191 61.885 41.217 39.026

ATOM 1323 HB2 ASP B 191 63.551 40.661 39.322

ATOM 1324 H ASP B 191 61.233 43.490 39.673

ATOM 1325 N THR B 192 63.802 43.119 37.396

ATOM 1326 CA THR B 192 64.649 43.485 36.259

ATOM 1327 C THR B 192 65.487 44.690 36.632

ATOM 1328 O THR B 192 66.671 44.717 36.343

ATOM 1329 CB THR B 192 63.843 43.875 34.991 ATOM 1330 OGl THR B 192 62.973 44.944 35.380

ATOM 1331 CG2 THR B 192 63.040 42.688 34.394

ATOM 1332 HA THR B 192 65.312 42.628 36.039

ATOM 1333 HB THR B 192 64.544 44.245 34 220

ATOM 1334 HGl THR B 192 62.488 45.311 34 653

ATOM 1335 HG23 THR B 192 63.706 42.080 33.763

ATOM 1336 HG21 THR B 192 62.616 42.056 35.186

ATOM 1337 HG22 THR B 192 62 212 43.051 33.766

ATOM 1338 H THR B 192 62 804 43.126 37.303

ATOM 1339 N ASN B 193 64 827 45.781 37.217

ATOM 1340 CA ASN B 193 65.524 47.018 37.565

ATOM 1341 C ASN B 193 66.674 46.730 38.502

ATOM 1342 O ASN B 193 67.763 47.251 38.316

ATOM 1343 CB ASN B 193 64.637 48.059 38.304

ATOM 1344 CG ASN B 193 63.597 48.725 37.439

ATOM 1345 ODl ASN B 193 63.514 48.439 36.255

ATOM 1346 ND2 ASN B 193 62.795 49.641 38.030

ATOM 1347 HA ASN B 193 65.904 47.492 36.647

ATOM 1348 HBl ASN B 193 64.143 47.587 39.165

ATOM 1349 HB2 ASN B 193 65.280 48.869 38.685

ATOM 1350 HD22 ASN B 193 62.115 50.140 37.492

ATOM 1351 HD21 ASN B 193 62.875 49.842 39.008

ATOM 1352 H ASN B 193 63.851 45.719 37.427

ATOM 1353 N ILE B 194 66.425 45.911 39.546

ATOM 1354 CA ILE B 194 67.492 45.584 40.492

ATOM 1355 C ILE B 194 68.620 44.952 39.707

ATOM 1356 O ILE B 194 69.750 45.408 39.792

ATOM 1357 CB ILE B 194 66.944 44.679 41.645

ATOM 1358 CGl ILE B 194 66.016 45.510 42.587

ATOM 1359 CG2 ILE B 194 68.097 44.003 42.438

ATOM 1360 CDl ILE B 194 65.024 44.649 43.416

ATOM 1361 HA ILE B 194 67.871 46.518 40.944

ATOM 1362 HB ILE B 194 66.351 43.865 41.199

ATOM 1363 HGIl ILE B 194 66.630 46.114 43.274

ATOM 1364 HG12 ILE B 194 65.413 46.213 41.991

ATOM 1365 HDIl ILE B 194 65.554 43.971 44.101

ATOM 1366 HD12 ILE B 194 64.370 45.300 44.018

ATOM 1367 HD13 ILE B 194 64.385 44.051 42.752

ATOM 1368 HG21 ILE B 194 68.745 44.763 42.901

ATOM 1369 HG22 ILE B 194 67.699 43.350 43.228

ATOM 1370 HG23 ILE B 194 68.710 43.378 41.772

ATOM 1371 H ILE B 194 65.512 45.516 39.676

ATOM 1372 N THR B 195 68.313 44.051 38.730

ATOM 1373 CA THR B 195 69.340 43.220 38.100

ATOM 1374 C THR B 195 70.183 44.089 37.192

ATOM 1375 O THR B 195 71.392 44.164 37.332

ATOM 1376 CB THR B 195 68.637 42.084 37.308

ATOM 1377 OGl THR B 195 67.670 41.472 38.181

ATOM 1378 CG2 THR B 195 69.660 41.034 36.805

ATOM 1379 HA THR B 195 69.966 42.780 38.897

ATOM 1380 HB THR B 195 68.106 42.520 36.445

ATOM 1381 HGl THR B 195 67.152 40.802 37.747

ATOM 1382 HG23 THR B 195 70.350 41.503 36.092

ATOM 1383 HG21 THR B 195 70.239 40.628 37.649

ATOM 1384 HG22 THR B 195 69.140 40.204 36.303

ATOM 1385 H THR B 195 67.454 43.620 39.020

ATOM 1386 N ARG B 196 69.408 45.068 36.565

ATOM 1387 CA ARG B 196 69.989 46.117 35.725

ATOM 1388 C ARG B 196 70.928 46.992 36.538

ATOM 1389 O ARG B 196 72.032 47.259 36.092

ATOM 1390 CB ARG B 196 68.801 46.926 35.122

ATOM 1391 CG ARG B 196 69.168 48.099 34.181

ATOM 1392 CD ARG B 196 67.879 48.813 33.679

ATOM 1393 NE ARG B 196 68.172 49.850 32.689

ATOM 1394 CZ ARG B 196 67.243 50.473 31.993

ATOM 1395 NHl ARG B 196 67.616 51.361 31.099

ATOM 1396 NH2 ARG B 196 65.957 50.252 32.152

ATOM 1397 HA ARG B 196 70.560 45.651 34.904 ATOM 1398 HBl ARG B 196 68.158 46.224 34.563

ATOM 1399 HB2 ARG B 196 68.213 47.350 35.943

ATOM 1400 HGl ARG B 196 69.824 48.817 34.700

ATOM 1401 HG2 ARG B 196 69.697 47.701 33.308

ATOM 1402 HDl ARG B 196 67.237 48.041 33.222

ATOM 1403 HD2 ARG B 196 67.357 49.268 34.537

ATOM 1404 HE ARG B 196 69.166 50.079 32. 524

ATOM 1405 HH12 ARG B 196 66.921 51.867 30.529

ATOM 1406 HHIl ARG B 196 68.611 51.579 30.946

ATOM 1407 HH22 ARG B 196 65.261 50.754 31.579

ATOM 1408 HH21 ARG B 196 65.601 49.591 3 853

ATOM 1409 H ARG B 196 68.407 44.982 36.611

ATOM 1410 N LEU B 197 70.494 47.443 37.738

ATOM 1411 CA LEU B 197 71.296 48.358 38.560

ATOM 1412 C LEU B 197 72.556 47.655 39.014

ATOM 1413 O LEU B 197 73.618 48.257 38.999

ATOM 1414 CB LEU B 197 70.418 48.905 39.725

ATOM 1415 CG LEU B 197 71.027 50.123 40.489

ATOM 1416 CDl LEU B 197 69.901 51.087 40.965

ATOM 1417 CD2 LEU B 197 71.875 49.670 41.709

ATOM 1418 HA LEU B 197 71.574 49.221 37.933

ATOM 1419 HBl LEU B 197 69.475 49.236 39.258

ATOM 1420 HB2 LEU B 197 70.169 48.093 40.426

ATOM 1421 HG LEU B 197 71.677 50.698 39.807

ATOM 1422 HD21 LEU B 197 72.684 48.993 41.399

ATOM 1423 HD22 LEU B 197 72.327 50.545 42.203

ATOM 1424 HD23 LEU B 197 71.243 49.148 42.444

ATOM 1425 HDIl LEU B 197 69.193 50.560 41.623

ATOM 1426 HD12 LEU B 197 70.326 51.940 41.516

ATOM 1427 HD13 LEU B 197 69.345 51.487 40.102

ATOM 1428 H LEU B 197 69.604 47.147 38.083

ATOM 1429 N GLN B 198 72.456 46.366 39.407

ATOM 1430 CA GLN B 198 73.649 45.614 39.797

ATOM 1431 C GLN B 198 74.641 45.554 38.653

ATOM 1432 O GLN B 198 75.817 45.807 38.867

ATOM 1433 CB GLN B 198 73.328 44.156 40.233

ATOM 1434 CG GLN B 198 72.526 44.087 41.560

ATOM 1435 CD GLN B 198 72.290 42.646 41.949

ATOM 1436 OEl GLN B 198 71.167 42.176 41.847

ATOM 1437 NE2 GLN B 198 73.336 41.916 42.396

ATOM 1438 HA GLN B 198 74.128 46.114 40.656

ATOM 1439 HBl GLN B 198 72.763 43.643 39.439

ATOM 1440 HB2 GLN B 198 74.280 43.617 40.371

ATOM 1441 HGl GLN B 198 73.085 44.587 42.366

ATOM 1442 HG2 GLN B 198 71.559 44.602 41.456

ATOM 1443 HE22 GLN B 198 73.201 40.958 42.653

ATOM 1444 HE21 GLN B 198 74.251 42.314 42.481

ATOM 1445 H GLN B 198 71.570 45.903 39.414

ATOM 1446 N LEU B 199 74.181 45.197 37.432

ATOM 1447 CA LEU B 199 75.111 44.993 36.319

ATOM 1448 C LEU B 199 75.725 46.317 35.911

ATOM 1449 O LEU B 199 76.925 46.385 35.698

ATOM 1450 CB LEU B 199 74.403 44.345 35.099

ATOM 1451 CG LEU B 199 73.878 42.897 35.348

ATOM 1452 CDl LEU B 199 72.640 42.595 34.458

ATOM 1453 CD2 LEU B 199 74.981 41.841 35.059

ATOM 1454 HA LEU B 199 75.914 44.312 36.647

ATOM 1455 HBl LEU B 199 73.570 45.003 34.812

ATOM 1456 HB2 LEU B 199 75.134 44.323 34.278

ATOM 1457 HG LEU B 199 73.563 42.793 36.401

ATOM 1458 HD21 LEU B 199 75.872 42.027 35.675

ATOM 1459 HD22 LEU B 199 74.612 40.827 35.280

ATOM 1460 HD23 LEU B 199 75.273 41.877 33.998

ATOM 1461 HDIl LEU B 199 72.894 42.702 33.395

ATOM 1462 HD12 LEU B 199 72.288 41.566 34.621

ATOM 1463 HD13 LEU B 199 71.819 43.287 34.698

ATOM 1464 H LEU B 199 73.201 45.063 37.275

ATOM 1465 N GLU B 200 74.893 47.377 35.802 ATOM 1466 CA GLU B 200 75.401 48.721 35.517

ATOM 1467 C GLU B 200 76.604 49.064 36.370

ATOM 1468 O GLU B 200 77.557 49.627 35.852

ATOM 1469 CB GLU B 200 74.306 49.794 35.790

ATOM 1470 CG GLU B 200 73.240 49.873 34.658

ATOM 1471 CD GLU B 200 73.618 50.840 33.561

ATOM 1472 OEl GLU B 200 74.009 51.994 33.883

ATOM 1473 OE2 GLU B 200 73.514 50.470 32.362

ATOM 1474 HA GLU B 200 75.706 48.767 34.459

ATOM 1475 HBl GLU B 200 73.816 49.539 36.743

ATOM 1476 HB2 GLU B 200 74.765 50.786 35.926

ATOM 1477 HGl GLU B 200 73.070 48.872 34.236

ATOM 1478 HG2 GLU B 200 72.283 50.228 35.072

ATOM 1479 H GLU B 200 73.907 47.247 35.909

ATOM 1480 N THR B 201 76.624 48.852 37.688

ATOM 1481 CA THR B 201 77.747 49.126 38.577

ATOM 1482 C THR B 201 78.657 47.920 38.581

ATOM 1483 O THR B 201 79.669 47.921 37.897

ATOM 1484 CB THR B 201 77.197 49.437 39.996

ATOM 1485 OGl THR B 201 76.159 48.481 40.279

ATOM 1486 CG2 THR B 201 76.645 50.887 40.057

ATOM 1487 HA THR B 201 78.309 50.000 38.210

ATOM 1488 OT THR B 201 78.391 46.944 39.265

ATOM 1489 HB THR B 201 78.010 49.337 40.737

ATOM 1490 HGl THR B 201 75.776 48.594 41.143

ATOM 1491 HG23 THR B 201 77.471 51.610 39.967

ATOM 1492 HG21 THR B 201 75.931 51.059 39.237

ATOM 1493 HG22 THR B 201 76.133 51.065 41.015

ATOM 1494 H THR B 201 75.934 48.192 37.994

TER 1495 THR B 201

ATOM 1496 N ILE C2250 43.801 9.502 22.116

ATOM 1497 CA ILE C2250 43.324 10.871 21.939

ATOM 1498 C ILE C2250 43.276 11.596 23.276

ATOM 1499 O ILE C2250 42.319 12.293 23.571

ATOM 1500 CB ILE C2250 41.989 10.853 21.127

ATOM 1501 CGl ILE C2250 41.041 9.737 21.661

ATOM 1502 CG2 ILE C2250 42.268 10.688 19.604

ATOM 1503 CDl ILE C2250 39.621 9.763 21.036

ATOM 1504 HA ILE C2250 44.071 11.426 21.345

ATOM 1505 HB ILE C2250 41.492 11.828 21.243

ATOM 1506 HGIl ILE C2250 41.477 8.743 21.471

ATOM 1507 HG12 ILE C2250 40.943 9.861 22.750

ATOM 1508 HDIl ILE C2250 39.642 9.469 19.977

ATOM 1509 HD12 ILE C2250 38.970 9.050 21.567

ATOM 1510 HD13 ILE C2250 39.179 10.767 21.116

ATOM 1511 HG21 ILE C2250 42.730 9.711 19.395

ATOM 1512 HG22 ILE C2250 41.342 10.771 19.017

ATOM 1513 HG23 ILE C2250 42.946 11.478 19.243

ATOM 1514 HNCA ILE C2250 44.211 9.013 21.345

ATOM 1515 H ILE C2250 43.696 9.059 23.013

ATOM 1516 N LYS C2251 44.337 11.439 24.105

ATOM 1517 CA LYS C2251 44.352 12.047 25.443

ATOM 1518 C LYS C2251 44.365 13.557 25.339

ATOM 1519 O LYS C2251 43.648 14.217 26.076

ATOM 1520 CB LYS C2251 45.568 11.508 26.246

ATOM 1521 CG LYS C2251 45.496 11.841 27.762

ATOM 1522 CD LYS C2251 46.586 11.091 28.585

ATOM 1523 CE LYS C2251 46.256 9.587 28.823

ATOM 1524 NZ LYS C2251 47.338 8.893 29.559

ATOM 1525 HA LYS C2251 43.441 11.727 25.974

ATOM 1526 HBl LYS C2251 45.572 10.416 26.116

ATOM 1527 HB2 LYS C2251 46.502 11.904 25.816

ATOM 1528 HGl LYS C2251 45.632 12.929 27.878

ATOM 1529 HG2 LYS C2251 44.505 11.581 28.168

ATOM 1530 HDl LYS C2251 47.558 11.184 28.074

ATOM 1531 HD2 LYS C2251 46.676 11.572 29.573

ATOM 1532 HEl LYS C2251 45.318 9.513 29.400

ATOM 1533 HE2 LYS C2251 46.106 9.056 27.871 ATOM 1534 HZl LYS C2251 47.529 9.348 30.521

ATOM 1535 HZ2 LYS C2251 47.087 7.856 29.742

ATOM 1536 HZ3 LYS C2251 48.264 8.898 28.999

ATOM 1537 H LYS C2251 45.119 10.885 23.808

ATOM 1538 N ASP C2252 45.183 14.113 24.416

ATOM 1539 CA ASP C2252 45.294 15.568 24.293

ATOM 1540 C ASP C2252 43.980 16.176 23.857

ATOM 1541 O ASP C2252 43.752 17.340 24.142

ATOM 1542 CB ASP C2252 46.435 15.948 23.310

ATOM 1543 CG ASP C2252 47.718 15.223 23.650

ATOM 1544 ODl ASP C2252 47.689 13.965 23.733

ATOM 1545 OD2 ASP C2252 48.771 15.887 23.831

ATOM 1546 HA ASP C2252 45.547 15.974 25.285

ATOM 1547 HBl ASP C2252 46.143 15.662 22.287

ATOM 1548 HB2 ASP C2252 46.594 17.039 23.332

ATOM 1549 H ASP C2252 45.735 13.530 23.814

ATOM 1550 N PHE C2253 43.091 15.461 23.111

ATOM 1551 CA PHE C2253 41.734 15.928 22.838

ATOM 1552 C PHE C2253 40.827 15.685 24.019

ATOM 1553 O PHE C2253 40.087 16.570 24.422

ATOM 1554 CB PHE C2253 41.156 15.250 21.573

ATOM 1555 CG PHE C2253 41.957 15.753 20.366

ATOM 1556 CDl PHE C2253 43.051 15.030 19.878

ATOM 1557 CD2 PHE C2253 41.599 16.960 19.756

ATOM 1558 CEl PHE C2253 43.825 15.553 18.837

ATOM 1559 CE2 PHE C2253 42.381 17.492 18.727

ATOM 1560 CZ PHE C2253 43.502 16.792 18.276

ATOM 1561 HA PHE C2253 41.769 17.011 22.638

ATOM 1562 HBl PHE C2253 41.212 14.157 21.669

ATOM 1563 HB2 PHE C2253 40.095 15.521 21.452

ATOM 1564 HD2 PHE C2253 40.715 17.495 20.082

ATOM 1565 HE2 PHE C2253 42.116 18.448 18.283

ATOM 1566 HZ PHE C2253 44.122 17.211 17.489

ATOM 1567 HEl PHE C2253 44.679 14.996 18.465

ATOM 1568 HDl PHE C2253 43.307 14.067 20.308

ATOM 1569 H PHE C2253 43.273 14.475 23.100

ATOM 1570 N LEU C2254 40.753 14.601 24.637

ATOM 1571 CA LEU C2254 39.822 14.349 25.737

ATOM 1572 C LEU C2254 40.020 15.317 26.885

ATOM 1573 O LEU C2254 39.033 15.706 27.489

ATOM 1574 CB LEU C2254 39.976 12.890 26.258

ATOM 1575 CG LEU C2254 39.192 11.794 25.458

ATOM 1576 CDl LEU C2254 38.985 12.052 23.936

ATOM 1577 CD2 LEU C2254 39.889 10.419 25.664

ATOM 1578 HA LEU C2254 38.785 14.492 25.392

ATOM 1579 HBl LEU C2254 41.051 12.661 26.302

ATOM 1580 HB2 LEU C2254 39.609 12.841 27.297

ATOM 1581 HG LEU C2254 38.173 11.726 25.881

ATOM 1582 HD21 LEU C2254 39.983 10.194 26.738

ATOM 1583 HD22 LEU C2254 39.314 9.609 25.189

ATOM 1584 HD23 LEU C2254 40.898 10.434 25.223

ATOM 1585 HDIl LEU C2254 39.934 12.142 23.400

ATOM 1586 HD12 LEU C2254 38.430 11.208 23.499

ATOM 1587 HDl 3 LEU C2254 38.391 12.956 23.743

ATOM 1588 H LEU C2254 41.378 13.873 24.340

ATOM 1589 N GLN C2255 41.280 15.693 27.207

ATOM 1590 CA GLN C2255 41.540 16.556 28.363

ATOM 1591 C GLN C2255 42.435 17.713 27.975

ATOM 1592 O GLN C2255 42.047 18.854 28.177

ATOM 1593 CB GLN C2255 42.190 15.740 29.513

ATOM 1594 CG GLN C2255 41.370 14.468 29.859

ATOM 1595 CD GLN C2255 41.972 13.696 31.010

ATOM 1596 OEl GLN C2255 42.958 14.132 31.583

ATOM 1597 NE2 GLN C2255 41.392 12.531 31.371

ATOM 1598 HA GLN C2255 40.602 16.983 28.759

ATOM 1599 HBl GLN C2255 43.207 15.423 29.235

ATOM 1600 HB2 GLN C2255 42.259 16.389 30.401

ATOM 1601 HGl GLN C2255 40.338 14.751 30.119 ATOM 1602 HG2 GLN C2255 41.343 13.801 28.983

ATOM 1603 HE22 GLN C2255 41.772 12.000 32.130

ATOM 1604 HE21 GLN C2255 40.585 12.184 30.890

ATOM 1605 H GLN C2255 42.053 15.333 26.685

ATOM 1606 N GLY C2256 43.642 17.430 27.429

ATOM 1607 CA GLY C2256 44.585 18.493 27.097

ATOM 1608 C GLY C2256 45.989 18.014 27.366

ATOM 1609 O GLY C2256 46.136 17.058 28.112

ATOM 1610 HA2 GLY C2256 44.447 19.373 27.739

ATOM 1611 HAl GLY C2256 44.459 18.795 26.048

ATOM 1612 H GLY C2256 43.935 16.492 27.243

ATOM 1613 N SER C2257 47.025 18.671 26.794

ATOM 1614 CA SER C2257 48.395 18.310 27.142

ATOM 1615 C SER C2257 48.783 19.112 28.356

ATOM 1616 O SER C2257 48.077 20.035 28.734

ATOM 1617 CB SER C2257 49.371 18.495 25.953

ATOM 1618 OG SER C2257 49.526 19.880 25.632

ATOM 1619 HA SER C2257 48.448 17.242 27.413

ATOM 1620 HBl SER C2257 50.360 18.065 26.185

ATOM 1621 HB2 SER C2257 48.945 17.969 25.086

ATOM 1622 HG SER C2257 50.035 20.012 24.837

ATOM 1623 H SER C2257 46.875 19.456 26.190

ATOM 1624 N SER C2258 49.902 18.742 29.012

ATOM 1625 CA SER C2258 50.167 19.320 30.317

ATOM 1626 C SER C2258 50.510 20.788 30.251

ATOM 1627 O SER C2258 51.240 21.189 29.361

ATOM 1628 CB SER C2258 51.221 18.610 31.194

ATOM 1629 OG SER C2258 51.111 19.253 32.475

ATOM 1630 HA SER C2258 49.241 19.198 30.901

ATOM 1631 HBl SER C2258 50.981 17.535 31.274

ATOM 1632 HB2 SER C2258 52.231 18.724 30.769

ATOM 1633 HG SER C2258 51.639 18.848 33.145

ATOM 1634 H SER C2258 50.511 18.025 28.673

ATOM 1635 N CYS C2259 49.978 21.576 31.212

ATOM 1636 CA CYS C2259 50.237 23.008 31.256

ATOM 1637 C CYS C2259 51.373 23.259 32.212

ATOM 1638 O CYS C2259 51.925 22.310 32.747

ATOM 1639 CB CYS C2259 48.914 23.658 31.755

ATOM 1640 SG CYS C2259 48.668 23.260 33.523

ATOM 1641 HA CYS C2259 50.493 23.409 30.260

ATOM 1642 HBl CYS C2259 48.914 24.748 31.635

ATOM 1643 HB2 CYS C2259 48.070 23.258 31.171

ATOM 1644 HG CYS C2259 47.696 23.517 33.602

ATOM 1645 LPGl CYS C2259 49.065 23.635 33.927

ATOM 1646 LPG2 CYS C2259 48.770 22.602 33.653

ATOM 1647 H CYS C2259 49.407 21.183 31.937

ATOM 1648 N ILE C2260 51.699 24.546 32.456

ATOM 1649 CA ILE C2260 52.638 24.873 33.517

ATOM 1650 C ILE C2260 51.920 24.485 34.790

ATOM 1651 O ILE C2260 51.124 25.243 35.321

ATOM 1652 CB ILE C2260 53.115 26.345 33.438

ATOM 1653 CGl ILE C2260 53.760 26.578 32.033

ATOM 1654 CG2 ILE C2260 54.090 26.603 34.619

ATOM 1655 CDl ILE C2260 54.335 27.996 31.831

ATOM 1656 HA ILE C2260 53.542 24.250 33.388

ATOM 1657 HB ILE C2260 52.240 27.004 33.551

ATOM 1658 HGIl ILE C2260 54.548 25.836 31.848

ATOM 1659 HG12 ILE C2260 53.015 26.450 31.235

ATOM 1660 HDIl ILE C2260 55.181 28.186 32.506

ATOM 1661 HD12 ILE C2260 54.681 28.105 30.793

ATOM 1662 HD13 ILE C2260 53.545 28.736 32.007

ATOM 1663 HG21 ILE C2260 54.963 25.940 34.526

ATOM 1664 HG22 ILE C2260 54.424 27.649 34.647

ATOM 1665 HG23 ILE C2260 53.600 26.392 35.581

ATOM 1666 H ILE C2260 51.245 25.284 31.970

ATOM 1667 N ALA C2261 52.204 23.251 35.252

ATOM 1668 CA ALA C2261 51.565 22.684 36.432

ATOM 1669 C ALA C2261 52.072 23.303 37.711 ATOM 1670 O ALA C2261 51.347 23.287 38.694

ATOM 1671 CB ALA C2261 51.870 21.171 36.525

ATOM 1672 HA ALA C2261 50.469 22.771 36.356

ATOM 1673 HBl ALA C2261 51.456 20.756 37.454

ATOM 1674 HB2 ALA C2261 51.418 20.654 35.664

ATOM 1675 HB3 ALA C2261 52.957 21.001 36.528

ATOM 1676 H ALA C2261 52.868 22.689 34.762

ATOM 1677 N GLY C2262 53.330 23.803 37.723

ATOM 1678 CA GLY C2262 54.023 23.965 38.991

ATOM 1679 C GLY C2262 55.378 24.598 38.796

ATOM 1680 O GLY C2262 55.679 25.007 37.685

ATOM 1681 HA2 GLY C2262 54.165 22.970 39.423

ATOM 1682 HAl GLY C2262 53.419 24.576 39.673

ATOM 1683 H GLY C2262 53.851 23.960 36.882

ATOM 1684 N ILE C2263 56.190 24.677 39.876

ATOM 1685 CA ILE C2263 57.525 25.268 39.783

ATOM 1686 C ILE C2263 58.574 24.337 40.339

ATOM 1687 O ILE C2263 58.301 23.721 41.357

ATOM 1688 CB ILE C2263 57.497 26.633 40.530

ATOM 1689 CGl ILE C2263 56.766 27.710 39.669

ATOM 1690 CG2 ILE C2263 58.928 27.104 40.893

ATOM 1691 CDl ILE C2263 56.101 28.813 40.529

ATOM 1692 HA ILE C2263 57.798 25.472 38.742

ATOM 1693 HB ILE C2263 56.952 26.484 41.478

ATOM 1694 HGIl ILE C2263 57.477 28.181 38.973

ATOM 1695 HG12 ILE C2263 55.970 27.241 39.069

ATOM 1696 HDIl ILE C2263 56.839 29.387 41.106

ATOM 1697 HD12 ILE C2263 55.532 29.507 39.890

ATOM 1698 HD13 ILE C2263 55.409 28.337 41.231

ATOM 1699 HG21 ILE C2263 59.542 27.111 39.983

ATOM 1700 HG22 ILE C2263 58.910 28.115 41.322

ATOM 1701 HG23 ILE C2263 59.397 26.428 41.623

ATOM 1702 H ILE C2263 55.879 24.370 40.776

ATOM 1703 N TYR C2264 59.762 24.258 39.686

ATOM 1704 CA TYR C2264 60.845 23.398 40.154

ATOM 1705 C TYR C2264 62.000 24.266 40.605

ATOM 1706 O TYR C2264 62.611 24.876 39.748

ATOM 1707 CB TYR C2264 61.306 22.469 39.003

ATOM 1708 CG TYR C2264 62.516 21.667 39.492

ATOM 1709 CDl TYR C2264 63.816 22.030 39.114

ATOM 1710 CD2 TYR C2264 62.322 20.567 40.332

ATOM 1711 CEl TYR C2264 64.905 21.261 39.523

ATOM 1712 CE2 TYR C2264 63.414 19.794 40.739

ATOM 1713 CZ TYR C2264 64.695 20.100 40.281

ATOM 1714 OH TYR C2264 65.754 19.243 40.577

ATOM 1715 HA TYR C2264 60.519 22.754 40.979

ATOM 1716 HB2 TYR C2264 60.492 21.783 38.723

ATOM 1717 HBl TYR C2264 61.566 23.054 38.106

ATOM 1718 HD2 TYR C2264 61.324 20.307 40.671

ATOM 1719 HE2 TYR C2264 63.265 18.951 41.406

ATOM 1720 HEl TYR C2264 65.912 21.560 39.252

ATOM 1721 HDl TYR C2264 63.985 22.911 38.503

ATOM 1722 HH TYR C2264 66.398 19.214 39.878

ATOM 1723 H TYR C2264 59.946 24.804 38.867

ATOM 1724 N ASN C2265 62.340 24.364 41.915

ATOM 1725 CA ASN C2265 63.371 25.321 42.321

ATOM 1726 C ASN C2265 64.742 24.677 42.328

ATOM 1727 O ASN C2265 64.946 23.707 43.040

ATOM 1728 CB ASN C2265 63.072 26.041 43.662

ATOM 1729 CG ASN C2265 63.148 25.171 44.890

ATOM 1730 ODl ASN C2265 62.976 23.967 44.787

ATOM 1731 ND2 ASN C2265 63.392 25.775 46.075

ATOM 1732 HA ASN C2265 63.381 26.154 41.603

ATOM 1733 HBl ASN C2265 63.764 26.894 43.770

ATOM 1734 HB2 ASN C2265 62.048 26.434 43.612

ATOM 1735 HD22 ASN C2265 63.442 25.234 46.909

ATOM 1736 HD21 ASN C2265 63.526 26.764 46.144

ATOM 1737 H ASN C2265 61.904 23.803 42.621 ATOM 1738 N GLU C2266 65.700 25.208 41.529

ATOM 1739 CA GLU C2266 67.040 24.622 41.466

ATOM 1740 C GLU C2266 67.639 24.550 42.854

ATOM 1741 O GLU C2266 68.258 23.552 43.188

ATOM 1742 CB GLU C2266 67.993 25.440 40.548

ATOM 1743 CG GLU C2266 67.567 25.483 39.052

ATOM 1744 CD GLU C2266 67.563 24.115 38.418

ATOM 1745 OEl GLU C2266 66.594 23.802 37.674

ATOM 1746 OE2 GLU C2266 68.530 23.341 38.655

ATOM 1747 HA GLU C2266 66.967 23.606 41.047

ATOM 1748 HBl GLU C2266 68.029 26.461 40.939

ATOM 1749 HB2 GLU C2266 69.015 25.037 40.610

ATOM 1750 HGl GLU C2266 66.576 25.947 38.934

ATOM 1751 HG2 GLU C2266 68.284 26.106 38.495

ATOM 1752 H GLU C2266 65.512 26.016 40.971

ATOM 1753 N THR C2267 67.215 25.446 43.816

ATOM 1754 CA THR C2267 67.886 25.613 45.102

ATOM 1755 C THR C2267 67.777 24.337 45.915

ATOM 1756 O THR C2267 68.789 23.693 46.109

ATOM 1757 CB THR C2267 67.293 26.847 45.832

ATOM 1758 OGl THR C2267 67.527 27.980 44.988

ATOM 1759 CG2 THR C2267 67.941 27.079 47.223

ATOM 1760 HA THR C2267 68.959 25.813 44.914

ATOM 1761 HB THR C2267 66.201 26.737 45.946

ATOM 1762 HGl THR C2267 67.142 28.751 45.382

ATOM 1763 HG23 THR C2267 67.619 26.307 47.932

ATOM 1764 HG21 THR C2267 69.038 27.048 47.145

ATOM 1765 HG22 THR C2267 67.646 28.059 47.632

ATOM 1766 H THR C2267 67.151 26.233 43.208

ATOM 1767 N THR C2268 66.561 23.946 46.385

ATOM 1768 CA THR C2268 66.407 22.685 47.112

ATOM 1769 C THR C2268 65.985 21.611 46.131

ATOM 1770 O THR C2268 65.756 20.485 46.541

ATOM 1771 CB THR C2268 65.352 22.822 48.247

ATOM 1772 OGl THR C2268 64.138 23.344 47.679

ATOM 1773 CG2 THR C2268 65.867 23.749 49.382

ATOM 1774 HA THR C2268 67.350 22.364 47.588

ATOM 1775 HB THR C2268 65.152 21.829 48.688

ATOM 1776 HGl THR C2268 63.444 23.413 48.328

ATOM 1777 HG23 THR C2268 66.605 90 999 50.007

ATOM 1778 HG21 THR C2268 66.344 24.637 48.953

ATOM 1779 HG22 THR C2268 65.040 24.082 50.028

ATOM 1780 H THR C2268 65.749 24.493 46.198

ATOM 1781 N LYS C2269 65.942 21.744 44.794

ATOM 1782 CA LYS C2269 65.521 20.666 43.896

ATOM 1783 C LYS C2269 64.135 20.158 44.269

ATOM 1784 O LYS C2269 63.962 18.954 44.383

ATOM 1785 CB LYS C2269 66.557 19.500 43.856

ATOM 1786 CG LYS C2269 68.032 19.956 43.674

ATOM 1787 CD LYS C2269 68.320 20.566 42.277

ATOM 1788 CE LYS C2269 69.789 21.060 42.164

ATOM 1789 NZ LYS C2269 70.007 21.816 40.910

ATOM 1790 HA LYS C2269 65.431 21.075 42.878

ATOM 1791 HBl LYS C2269 66.506 18.942 44.804

ATOM 1792 HB2 LYS C2269 66.292 18.795 43.052

ATOM 1793 HGl LYS C2269 68.284 20.682 44.463

ATOM 1794 HG2 LYS C2269 68.690 19.079 43.800

ATOM 1795 HDl LYS C2269 68.145 19.808 41.498

ATOM 1796 HD2 LYS C2269 67.637 21.405 42.092

ATOM 1797 HEl LYS C2269 70.034 21.709 43.022

ATOM 1798 HE2 LYS C2269 70.469 20.192 42.196

ATOM 1799 HZl LYS C2269 69.365 22.681 40.862

ATOM 1800 HZ2 LYS C2269 71.025 22.175 40.830

ATOM 1801 HZ3 LYS C2269 69.799 21.217 40.035

ATOM 1802 H LYS C2269 66.211 22.621 44.382

ATOM 1803 N GLN C2270 63.132 21.054 44.467

ATOM 1804 CA GLN C2270 61.789 20.621 44.877

ATOM 1805 C GLN C2270 60.744 21.071 43.887 ATOM 1806 O GLN C2270 60.932 22.117 43.286

ATOM 1807 CB GLN C2270 61.393 21.228 46.253

ATOM 1808 CG GLN C2270 62.329 20.750 47.392

ATOM 1809 CD GLN C2270 62.096 19.304 47.756

ATOM 1810 OEl GLN C2270 62.772 18.441 47.219

ATOM 1811 NE2 GLN C2270 61.142 19.011 48.669

ATOM 1812 HA GLN C2270 61.734 19.525 44.960

ATOM 1813 HBl GLN C2270 61.447 22.326 46.181

ATOM 1814 HB2 GLN C2270 60.355 20.958 46.510

ATOM 1815 HGl GLN C2270 63.372 20.895 47.088

ATOM 1816 HG2 GLN C2270 62.153 21.364 48.289

ATOM 1817 HE22 GLN C2270 60.978 18.058 48.926

ATOM 1818 HE21 GLN C2270 60.595 19.728 49.105

ATOM 1819 H GLN C2270 63.291 22.038 44.357

ATOM 1820 N LYS C2271 59.645 20.285 43.755

ATOM 1821 CA LYS C2271 58.518 20.696 42.925

ATOM 1822 C LYS C2271 57.472 21.283 43.851

ATOM 1823 O LYS C2271 57.279 20.738 44.926

ATOM 1824 CB LYS C2271 57.971 19.592 41.973

ATOM 1825 CG LYS C2271 57.565 18.274 42.684

ATOM 1826 CD LYS C2271 57.018 17.209 41.694

ATOM 1827 CE LYS C2271 56.810 15.832 42.392

ATOM 1828 NZ LYS C2271 57.735 14.823 41.830

ATOM 1829 HA LYS C2271 58.858 21.492 42.250

ATOM 1830 HBl LYS C2271 57.107 19.995 41.420

ATOM 1831 HB2 LYS C2271 58.763 19.346 41.246

ATOM 1832 HGl LYS C2271 58.455 17.831 43.157

ATOM 1833 HG2 LYS C2271 56.813 18.481 43.461

ATOM 1834 HDl LYS C2271 56.066 17.531 41.258

ATOM 1835 HD2 LYS C2271 57.723 17.112 40.854

ATOM 1836 HEl LYS C2271 56.976 15.911 43.479

ATOM 1837 HE2 LYS C2271 55.773 15.480 42.265

ATOM 1838 HZl LYS C2271 58.769 15.109 41.969

ATOM 1839 HZ2 LYS C2271 57.595 13.873 42.322

ATOM 1840 HZ3 LYS C2271 57.569 14.682 40.771

ATOM 1841 H LYS C2271 59.544 19.453 44.302

ATOM 1842 N LEU C2272 56.810 22.401 43.459

ATOM 1843 CA LEU C2272 55.786 23.033 44.295

ATOM 1844 C LEU C2272 54.653 23.488 43.414

ATOM 1845 O LEU C2272 54.903 23.703 42.240

ATOM 1846 CB LEU C2272 56.322 24.367 44.892

ATOM 1847 CG LEU C2272 57.368 24.198 46.028

ATOM 1848 CDl LEU p 99 n 9 58.128 25.537 46.232

ATOM 1849 CD2 LEU C2272 56.691 23.786 47.365

ATOM 1850 HA LEU C2272 55.412 22.340 45.064

ATOM 1851 HBl LEU C2272 56.776 24.931 44.061

ATOM 1852 HB2 LEU p 99 n 9 55.493 24.979 45.286

ATOM 1853 HG LEU C2272 58.100 23.426 45.733

ATOM 1854 HD21 LEU C2272 56.154 22.832 47.267

ATOM 1855 HD22 LEU C2272 57.447 23.673 48.157

ATOM 1856 HD23 LEU C2272 55.977 24.561 47.680

ATOM 1857 HDIl LEU C2272 57.427 26.348 46.486

ATOM 1858 HD12 LEU C2272 58.867 25.438 47.041

ATOM 1859 HDl 3 LEU C2272 58.663 25.810 45.311

ATOM 1860 H LEU C2272 57.014 22.833 42.578

ATOM 1861 N GLY C2273 53.440 23.693 43.975

ATOM 1862 CA GLY C2273 52.395 24.335 43.195

ATOM 1863 C GLY C2273 52.648 25.823 43.142

ATOM 1864 O GLY C2273 53.399 26.369 43.937

ATOM 1865 HA2 GLY C2273 51.399 24.146 43.625

ATOM 1866 HAl GLY C2273 52.411 23.948 42.165

ATOM 1867 H GLY C2273 53.261 23.500 44.942

ATOM 1868 N ILE C2274 51.991 26.486 42.166

ATOM 1869 CA ILE C2274 52.179 27.922 41.986

ATOM 1870 C ILE C2274 51.828 28.671 43.254

ATOM 1871 O ILE C2274 52.570 29.539 43.688

ATOM 1872 CB ILE C2274 51.349 28.524 40.808

ATOM 1873 CGl ILE C2274 51.241 27.688 39.489 ATOM 1874 CG2 ILE C2274 51.923 29.926 40.493

ATOM 1875 CDl ILE C2274 52.610 27.365 38.837

ATOM 1876 HA ILE C2274 53.239 28.102 41.793

ATOM 1877 HB ILE C2274 50.314 28.646 41.167

ATOM 1878 HGIl ILE C2274 50.684 26.755 39.644

ATOM 1879 HG12 ILE C2274 50.635 28.246 38.760

ATOM 1880 HDIl ILE C2274 53.290 26.928 39.580

ATOM 1881 HD12 ILE C2274 52.475 26.649 38.010

ATOM 1882 HD13 ILE C2274 53.079 28.271 38.428

ATOM 1883 HG21 ILE C2274 52.966 29.884 40.149

ATOM 1884 HG22 ILE C2274 51.317 30.382 39.707

ATOM 1885 HG23 ILE C2274 51.893 30.559 41.387

ATOM 1886 H ILE C2274 51.381 25.988 41.558

ATOM 1887 N TYR C2275 50.661 28.359 43.857

ATOM 1888 CA TYR C2275 50.215 29.147 45.003

ATOM 1889 C TYR C2275 51.172 28.978 46.167

ATOM 1890 O TYR C2275 51.576 29.960 46.771

ATOM 1891 CB TYR C2275 48.773 28.778 45.430

ATOM 1892 CG TYR C2275 48.324 29.682 46.584

ATOM 1893 CDl TYR C2275 48.043 31.032 46.342

ATOM 1894 CD2 TYR C2275 48.196 29.178 47.882

ATOM 1895 CEl TYR C2275 47.715 31.887 47.396

ATOM 1896 CE2 TYR C2275 47.853 30.031 48.936

ATOM 1897 CZ TYR C2275 47.637 31.391 48.704

ATOM 1898 OH TYR C2275 47.345 32.231 49.784

ATOM 1899 HA TYR C2275 50.205 30.191 44.678

ATOM 1900 HB2 TYR C2275 48.081 28.900 44.581

ATOM 1901 HBl TYR C2275 48.765 27.722 45.734

ATOM 1902 HD2 TYR C2275 48.363 28.124 48.082

ATOM 1903 HE2 TYR C2275 47.756 29.633 49.941

ATOM 1904 HEl TYR C2275 47.520 32.935 47.190

ATOM 1905 HDl TYR C2275 48.079 31.421 45.330

ATOM 1906 HH TYR C2275 47.257 33.148 49.550

ATOM 1907 H TYR C2275 50.076 27.620 43.518

ATOM 1908 N GLU C2276 51.547 27.718 46.485

ATOM 1909 CA GLU C2276 52.494 27.445 47.577

ATOM 1910 C GLU C2276 53.803 28.177 47.347

ATOM 1911 O GLU C2276 54.432 28.630 48.290

ATOM 1912 CB GLU C2276 52.768 25.913 47.641

ATOM 1913 CG GLU C2276 53.455 25.471 48.961

ATOM 1914 CD GLU C2276 52.560 25.628 50.165

ATOM 1915 OEl GLU C2276 53.100 25.856 51.281

ATOM 1916 OE2 GLU C2276 51.312 25.522 50.019

ATOM 1917 HA GLU C2276 52.036 27.778 48.522

ATOM 1918 HBl GLU C2276 51.821 25.356 47.555

ATOM 1919 HB2 GLU C2276 53.399 25.628 46.783

ATOM 1920 HGl GLU C2276 53.714 24.402 48.890

ATOM 1921 HG2 GLU C2276 54.383 26.044 49.106

ATOM 1922 H GLU C2276 51.177 26.952 45.956

ATOM 1923 N ALA C2277 54.224 28.292 46.068

ATOM 1924 CA ALA C2277 55.447 29.023 45.745

ATOM 1925 C ALA C2277 55.292 30.495 46.075

ATOM 1926 O ALA C2277 56.221 31.086 46.604

ATOM 1927 CB ALA C2277 55.817 28.818 44.251

ATOM 1928 HA ALA C2277 56.271 28.631 46.361

ATOM 1929 HBl ALA C2277 56.693 29.419 43.973

ATOM 1930 HB2 ALA C2277 56.040 27.757 44.058

ATOM 1931 HB3 ALA C2277 54.986 29.122 43.604

ATOM 1932 H ALA C2277 53.701 27.880 45.322

ATOM 1933 N MET C2278 54.135 31.131 45.778

ATOM 1934 CA MET C2278 54.000 32.556 46.078

ATOM 1935 C MET C2278 53.999 32.822 47.565

ATOM 1936 O MET C2278 54.522 33.834 48.006

ATOM 1937 CB MET C2278 52.776 33.276 45.441

ATOM 1938 CG MET C2278 51.390 32.925 46.052

ATOM 1939 SD MET C2278 50.199 34.288 45.902

ATOM 1940 CE MET C2278 50.740 35.285 47.324

ATOM 1941 HA MET C2278 54.908 33.028 45.702 ATOM 1942 HBl MET C2278 52.949 34.359 45.528

ATOM 1943 HB2 MET C2278 52.742 33.033 44.375

ATOM 1944 HGl MET C2278 50.952 32.086 45.512

ATOM 1945 HG2 MET C2278 51.420 32.672 47.116

ATOM 1946 HEl MET C2278 51.804 35.541 47.228

ATOM 1947 HE2 MET C2278 50.140 36.205 47.367

ATOM 1948 HE3 MET C2278 50.596 34.717 48.254

ATOM 1949 LPDl MET C2278 49.558 34.075 45.968

ATOM 1950 LPD2 MET C2278 50.267 34.623 45.315

ATOM 1951 H MET C2278 53.365 30.651 45.358

ATOM 1952 N LYS C2279 53.398 31.890 48.332

ATOM 1953 CA LYS C2279 53.330 32.024 49.786

ATOM 1954 C LYS C2279 54.732 32.100 50.340

ATOM 1955 O LYS C2279 54.974 32.934 51.199

ATOM 1956 CB LYS C2279 52.565 30.772 50.307

ATOM 1957 CG LYS C2279 52.378 30.657 51.841

ATOM 1958 CD LYS C2279 51.876 29.234 52.240

ATOM 1959 CE LYS C2279 50.562 28.806 51.525

ATOM 1960 NZ LYS C2279 50.065 27.496 52.007

ATOM 1961 HA LYS C2279 52.779 32.948 50.034

ATOM 1962 HBl LYS C2279 51.571 30.785 49.830

ATOM 1963 HB2 LYS C2279 53.105 29.873 49.976

ATOM 1964 HGl LYS C2279 53.344 30.837 52.341

ATOM 1965 HG2 LYS C2279 51.665 31.424 52.183

ATOM 1966 HDl LYS C2279 52.660 28.494 52.004

ATOM 1967 HD2 LYS C2279 51.710 29.212 53.329

ATOM 1968 HEl LYS C2279 49.792 29.577 51.693

ATOM 1969 HE2 LYS C2279 50.728 28.714 50.440

ATOM 1970 HZl LYS C2279 49.811 27.521 53.057

ATOM 1971 HZ2 LYS C2279 49.175 27.191 51.472

ATOM 1972 HZ3 LYS C2279 50.795 26.711 51.870

ATOM 1973 H LYS C2279 52.967 31.097 47.895

ATOM 1974 N ILE C2280 55.670 31.257 49.841

ATOM 1975 CA ILE C2280 57.051 31.292 50.329

ATOM 1976 C ILE C2280 57.906 32.209 49.468

ATOM 1977 O ILE C2280 59.048 31.876 49.193

ATOM 1978 CB ILE C2280 57.632 29.860 50.515

ATOM 1979 CGl ILE C2280 57.740 29.086 49.164

ATOM 1980 CG2 ILE C2280 56.774 29.076 51.551

ATOM 1981 CDl ILE C2280 59.031 28.232 49.087

ATOM 1982 HA ILE C2280 57.077 31.754 51.330

ATOM 1983 HB ILE C2280 58.643 29.978 50.943

ATOM 1984 HGIl ILE C2280 56.869 28.426 49.031

ATOM 1985 HG12 ILE C2280 57.761 29.781 48.312

ATOM 1986 HDIl ILE C2280 59.071 27.511 49.918

ATOM 1987 HD12 ILE C2280 59.063 27.681 48.136

ATOM 1988 HD13 ILE C2280 59.920 28.881 49.134

ATOM 1989 HG21 ILE C2280 55.731 28.989 51.210

ATOM 1990 HG22 ILE C2280 57.179 28.064 51.700

ATOM 1991 HG23 ILE C2280 56.774 29.593 52.524

ATOM 1992 H ILE C2280 55.438 30.608 49.115

ATOM 1993 N GLY C2281 57.373 33.384 49.039

ATOM 1994 CA GLY C2281 58.155 34.393 48.310

ATOM 1995 C GLY C2281 58.996 33.937 47.136

ATOM 1996 O GLY C2281 59.819 34.715 46.677

ATOM 1997 HA2 GLY C2281 58.821 34.887 49.035

ATOM 1998 HAl GLY C2281 57.465 35.159 47.912

ATOM 1999 H GLY C2281 56.433 33.631 49.277

ATOM 2000 N LEU C2282 58.801 32.702 46.625

ATOM 2001 CA LEU C2282 59.581 32.212 45.481

ATOM 2002 C LEU C2282 59.044 32.839 44.208

ATOM 2003 O LEU C2282 59.820 33.063 43.291

ATOM 2004 CB LEU C2282 59.427 30.659 45.476

ATOM 2005 CG LEU C2282 60.137 29.878 44.335

ATOM 2006 CDl LEU C2282 61.681 30.017 44.421

ATOM 2007 CD2 LEU C2282 59.762 28.372 44.422

ATOM 2008 HA LEU C2282 60.643 32.489 45.606

ATOM 2009 HBl LEU C2282 59.783 30.272 46.446 ATOM 2010 HB2 LEU C2282 58.355 30.431 45.401

ATOM 2011 HG LEU C2282 59.783 30.260 43.362

ATOM 2012 HD21 LEU C2282 58.675 28.220 44.406

ATOM 2013 HD22 LEU C2282 60.178 27.837 43.559

ATOM 2014 HD23 LEU C2282 60.159 27.924 45.346

ATOM 2015 HDIl LEU C2282 62.030 29.776 45.436

ATOM 2016 HD12 LEU C2282 62.176 29.322 43.729

ATOM 2017 HDl 3 LEU C2282 61.988 31.040 44.161

ATOM 2018 H LEU C2282 58.079 32.117 46.995

ATOM 2019 N VAL C2283 57.727 33.152 44.136

ATOM 2020 CA VAL C2283 57.173 33.870 42.983

ATOM 2021 C VAL C2283 56.246 34.968 43.475

ATOM 2022 O VAL C2283 55.474 34.761 44.391

ATOM 2023 CB VAL C2283 56.473 32.898 41.984

ATOM 2024 CGl VAL C2283 55.309 32.115 42.641

ATOM 2025 CG2 VAL C2283 55.932 33.648 40.737

ATOM 2026 HA VAL C2283 57.994 34.357 42.427

ATOM 2027 HB VAL C2283 57.225 32.163 41.647

ATOM 2028 HGIl VAL C2283 54.526 32.816 42.949

ATOM 2029 HGl 2 VAL C2283 54.868 31.393 41.937

ATOM 2030 HGl 3 VAL C2283 55.659 31.569 43.523

ATOM 2031 HG21 VAL C2283 56.750 34. .177 40.231

ATOM 2032 HG22 VAL C2283 55.485 32.940 40.022

ATOM 2033 HG23 VAL C2283 55.161 34.377 41.025

ATOM 2034 H VAL C2283 57.101 32.910 44.874

ATOM 2035 N ARG C2284 56.291 36.184 42.899

ATOM 2036 CA ARG C2284 55.359 37.231 43.305

ATOM 2037 C ARG C2284 53.889 36.853 43.142

ATOM 2038 O ARG C2284 53.648 35.971 4; .335

ATOM 2039 CB ARG C2284 55.698 38.535 4; .526

ATOM 2040 CG ARG C2284 55.447 38.586 40.

ATOM 2041 CD ARG C2284 56.353 37.718 40.074

ATOM 2042 NE ARG C2284 57.775 38.026 40.260

ATOM 2043 CZ ARG C2284 58.756 37.272 39.809

ATOM 2044 NHl ARG C2284 58.554 36.189 39.100

ATOM 2045 NH2 ARG C2284 59.995 37.618 40.075

ATOM 2046 HA ARG C2284 55.556 37.397 44.376

ATOM 2047 HBl ARG C2284 55.010 39.271 42.928

ATOM 2048 HB2 ARG C2284 56.722 38.858 42.770

ATOM 2049 HGl ARG C2284 54.393 38.346 40.804

ATOM 2050 HG2 ARG C2284 55.618 39.621 40.658

ATOM 2051 HDl ARG C2284 56.080 36.673 40.259

ATOM 2052 HD2 ARG C2284 56.115 37.938 39.025

ATOM 2053 HE ARG C2284 58.011 38.878 40.790

ATOM 2054 HHl 2 ARG C2284 59.345 35.608 38.794

ATOM 2055 HHIl ARG C2284 57.616 35.897 38.817

ATOM 2056 HH22 ARG C2284 60.790 37.054 39.735

ATOM 2057 HH21 ARG C2284 60.208 38.463 40.624

ATOM 2058 H ARG C2284 57.013 36.401 42.253

ATOM 2059 N PRO C2285 52.868 37.442 43.841

ATOM 2060 CA PRO C2285 51.482 37.007 43.657

ATOM 2061 C PRO C2285 50.956 37.176 42.259

ATOM 2062 O PRO C2285 50.062 36.458 41.838

ATOM 2063 CB PRO C2285 50.726 38.027 44.555

ATOM 2064 CG PRO C2285 51.771 38.505 45.586

ATOM 2065 CD PRO C2285 53.081 38.549 44.772

ATOM 2066 HA PRO C2285 51.359 35.973 44.010

ATOM 2067 HD2 PRO C2285 53.115 39.507 44.232

ATOM 2068 HDl PRO C2285 53.937 38.465 45.456

ATOM 2069 HG2 PRO C2285 51.516 39.475 46.044

ATOM 2070 HGl PRO C2285 51.870 37.759 46.386

ATOM 2071 HBl PRO C2285 50.417 38.912 43.971

ATOM 2072 HB2 PRO C2285 49.830 37.600 45.031

ATOM 2073 N GLY C2286 51.473 38.193 41.550

ATOM 2074 CA GLY C2286 50.906 38.526 40.256

ATOM 2075 C GLY C2286 50.995 37.447 39.217

ATOM 2076 O GLY C2286 49.987 36.934 38.762

ATOM 2077 HA2 GLY C2286 51.451 39.366 39.878 ATOM 2078 HAl GLY C2286 49.899 38.910 40.366

ATOM 2079 H GLY C2286 52.170 38.799 41.942

ATOM 2080 N THR C2287 52.281 37.184 38.755

ATOM 2081 CA THR C2287 52.405 36.151 37.737

ATOM 2082 C THR C2287 51.889 34.858 38.312

ATOM 2083 O THR C2287 51.463 34.000 37.558

ATOM 2084 CB THR C2287 53.867 35.991 37.268

ATOM 2085 OGl THR C2287 54.606 35.435 38.368

ATOM 2086 CG2 THR C2287 54.427 37.364 36.807

ATOM 2087 HA THR C2287 51.792 36.425 36.858

ATOM 2088 HB THR C2287 53.885 35.280 36.421

ATOM 2089 HGl THR C2287 55.482 35.171 38.112

ATOM 2090 HG23 THR C2287 53.905 37.700 35.899

ATOM 2091 HG21 THR C2287 54.282 38.137 37.574

ATOM 2092 HG22 THR C2287 55.501 37.288 36.596

ATOM 2093 H THR C2287 52.931 37.168 39.514

ATOM 2094 N ALA Lzz Oo 51.947 34.598 39.671

ATOM 2095 CA ALA Lzz Oo 51.354 33.375 40.198

ATOM 2096 C ALA C2288 49.987 33.160 39.581

ATOM 2097 O ALA C2288 49.627 32.024 39.315

ATOM 2098 CB ALA C2288 51.228 33.378 41.741

ATOM 2099 HA ALA 52.037 32.563 39.906

ATOM 2100 HBl ALA LZZ O O 50.775 32.448 42.113

ATOM 2101 HB2 ALA C2288 52.231 33.495 42.171

ATOM 2102 HB3 ALA C2288 50.597 34.199 42.087

ATOM 2103 H ALA C2288 52.370 35.234 40.317

ATOM 2104 N LEU C2289 49.198 34.235 39.337

ATOM 2105 CA LEU C2289 47.888 34.030 38.723

ATOM 2106 C LEU C2289 47.975 33.733 37.255

ATOM 2107 O LEU C2289 47.438 32.710 36.876

ATOM 2108 CB LEU C2289 46.936 35.186 39.135

ATOM 2109 CG LEU C2289 46.113 34.924 40.426

ATOM 2110 CDl LEU C2289 45.500 36.255 40.930

ATOM 2111 CD2 LEU C2289 44.952 33.916 40.194

ATOM 2112 HA LEU C2289 47.505 33.115 39.171

ATOM 2113 HBl LEU C2289 47.491 36.121 39.230

ATOM 2114 HB2 LEU C2289 46.218 35.367 38.355

ATOM 2115 HG LEU C2289 46.801 34.527 41.188

ATOM 2116 HD21 LEU C2289 45.296 32.999 39.716

ATOM 2117 HD22 LEU C2289 44.505 33.629 41.150

ATOM 2118 HD23 LEU C2289 44.165 34.360 39.567

ATOM 2119 HDIl LEU C2289 45.087 36.823 40.083

ATOM 2120 HD12 LEU C2289 44.709 36.066 41.666

ATOM 2121 HDl 3 LEU C2289 46.259 36.865 41.422

ATOM 2122 H LEU C2289 49.494 35.163 39.567

ATOM 2123 N GLU C2290 48.636 34.565 36.424

ATOM 2124 CA GLU C2290 48.881 34.200 35.022

ATOM 2125 C GLU C2290 48.903 32.687 34.836

ATOM 2126 O GLU C2290 48.193 32.161 33.990

ATOM 2127 CB GLU C2290 50.252 34.764 34.533

ATOM 2128 CG GLU C2290 50.283 36.301 34.302

ATOM 2129 CD GLU C2290 51.606 36.778 33.753

ATOM 2130 OEl GLU C2290 51.619 37.808 33.025

ATOM 2131 OE2 GLU C2290 52.647 36.134 34.053

ATOM 2132 HA GLU C2290 48.084 34.627 34.386

ATOM 2133 HBl GLU C2290 51.036 34.500 35.251

ATOM 2134 HB2 GLU C2290 50.520 34.293 33.582

ATOM 2135 HGl GLU C2290 49.469 36.586 33.618

ATOM 2136 HG2 GLU C2290 50.151 36.846 35.244

ATOM 2137 H GLU C2290 48.949 35.450 36.761

ATOM 2138 N LEU C2291 49.713 31.976 35.662

ATOM 2139 CA LEU C2291 49.764 30.519 35.570

ATOM 2140 C LEU C2291 48.464 29.876 36.027

ATOM 2141 O LEU C2291 47.906 29.084 35.285

ATOM 2142 CB LEU C2291 50.952 29.870 36.339

ATOM 2143 CG LEU C2291 52.404 30.150 35.830

ATOM 2144 CDl LEU C2291 52.507 30.206 34.285

ATOM 2145 CD2 LEU C2291 53.081 31.407 36.444 ATOM 2146 HA LEU C2291 49.876 30.253 34.508

ATOM 2147 HBl LEU C2291 50.879 30.171 37.391

ATOM 2148 HB2 LEU C2291 50.790 28.779 36.283

ATOM 2149 HG LEU C2291 53.022 29.296 36.165

ATOM 2150 HD21 LEU C2291 53.019 31.392 37.544

ATOM 2151 HD22 LEU C2291 54.147 31.430 36.164

ATOM 2152 HD23 LEU C2291 52.621 32.329 36.067

ATOM 2153 HDIl LEU C2291 52.065 31.134 33.889

ATOM 2154 HD12 LEU C2291 53.566 30.175 33.996

ATOM 2155 HDl 3 LEU C2291 51.995 29.346 33.833

ATOM 2156 H LEU C2291 50.282 32.424 36.356

ATOM 2157 N LEU C2292 47.954 30.183 37.241

ATOM 2158 CA LEU C2292 46.740 29.518 37.729

ATOM 2159 C LEU C2292 45.539 29.834 36.851

ATOM 2160 O LEU C2292 44.666 28.994 36.717

ATOM 2161 CB LEU C2292 46.404 29.916 39.205

ATOM 2162 CG LEU C2292 47.441 29.670 40.340

ATOM 2163 CDl LEU C2292 47.250 30.696 41.508

ATOM 2164 CD2 LEU 47.231 28.236 40.901

ATOM 2165 HA LEU C2292 46.919 28.433 37.752

ATOM 2166 HBl LEU C2292 46.234 30.991 39.217

ATOM 2167 HB2 LEU C2292 45.478 29.401 39.508

ATOM 2168 HG LEU C2292 48.461 29.769 39.936

ATOM 2169 HD21 LEU C2292 47.359 27.496 40.098

ATOM 2170 HD22 LEU C2292 47.953 28.027 41.701

ATOM 2171 HD23 LEU C2292 46.218 28.127 41.326

ATOM 2172 HDIl LEU 46.196 30.680 41.823

ATOM 2173 HD12 LEU C2292 47.883 30.417 42.362

ATOM 2174 HDl 3 LEU C2292 47.513 31.740 41.269

ATOM 2175 H LEU C2292 48.399 30.873 37.813

ATOM 2176 N GLU C2293 45.527 31.031 36.288

ATOM 2177 CA GLU C2293 44.424 31.404 35.455

ATOM 2178 C GLU C2293 44.445 30.554 34.215

ATOM 2179 O GLU C2293 43.410 30.035 33.834

ATOM 2180 CB GLU C2293 44.633 32.909 35.201

ATOM 2181 CG GLU C2293 44.434 33.715 36.486

ATOM 2182 CD GLU C2293 44.872 35.169 36.294

ATOM 2183 OEl GLU C2293 45.317 35.543 35.199

ATOM 2184 OE2 GLU C2293 44.735 35.921 37.333

ATOM 2185 HA GLU C2293 43.480 31.256 35.971

ATOM 2186 HBl GLU C2293 43.926 33.240 34.440

ATOM 2187 HB2 GLU C2293 45.648 33.068 34.836

ATOM 2188 HGl GLU C2293 45.014 33.255 37.286

ATOM 2189 HG2 GLU C2293 43.378 33.695 36.756

ATOM 2190 H GLU C2293 46.300 31.640 36.402

ATOM 2191 N ALA C2294 45.633 30.385 33.597

ATOM 2192 CA ALA C2294 45.799 29.441 32.497

ATOM 2193 C ALA C2294 45.392 28.051 32.958

ATOM 2194 O ALA C2294 44.754 27.348 32.189

ATOM 2195 CB ALA C2294 47.277 29.485 31.946

ATOM 2196 HA ALA C2294 45.128 29.736 31.672

ATOM 2197 HBl ALA C2294 47.388 28.693 31.197

ATOM 2198 HB2 ALA C2294 47.670 30.414 31.477

ATOM 2199 HB3 ALA C2294 47.963 29.244 32.765

ATOM 2200 H ALA C2294 46.446 30.818 33.992

ATOM 2201 N GLN C2295 45.729 27.632 34.203

ATOM 2202 CA GLN C2295 45.313 26.310 34.682

ATOM 2203 C GLN C2295 43.796 26.222 34.652

ATOM 2204 O GLN C2295 43.243 25.323 34.036

ATOM 2205 CB GLN C2295 45.911 26.020 36.088

ATOM 2206 CG GLN C2295 47.454 25.848 36.141

ATOM 2207 CD GLN C2295 47.935 25.411 37.506

ATOM 2208 OEl GLN C2295 47.160 25.392 38.449

ATOM 2209 NE2 GLN C2295 49.226 25.042 37.640

ATOM 2210 HA GLN C2295 45.723 25.551 33.995

ATOM 2211 HBl GLN C2295 45.582 26.765 36.818

ATOM 2212 HB2 GLN C2295 45.522 25.063 36.412

ATOM 2213 HGl GLN C2295 47.749 25.071 35.427 ATOM 2214 HG2 GLN C2295 47.980 26.769 35.868

ATOM 2215 HE22 GLN C2295 49.560 24.707 38.523

ATOM 2216 HE21 GLN C2295 49.856 25.094 36.866

ATOM 2217 H GLN C2295 46.260 28.217 34.815

ATOM 2218 N ALA C2296 43.111 27.177 35.319

ATOM 2219 CA ALA C2296 41.650 27.221 35.309

ATOM 2220 C ALA C2296 41.114 27.168 33.894

ATOM 2221 O ALA C2296 40.291 26.321 33.584

ATOM 9999 CB ALA C2296 41.108 28.467 36.049

ATOM 2223 HA ALA C2296 41.250 26.374 35.891

ATOM 2224 HBl ALA C2296 40.010 28.498 36.001

ATOM 2225 HB2 ALA C2296 41.400 28.448 37.106

ATOM 2226 HB3 ALA C2296 41.525 29.372 35.593

ATOM 2227 H ALA C2296 43.599 27.871 35.844

ATOM 2228 N ALA C2297 41.578 28.085 33.019

ATOM 2229 CA ALA C2297 40.983 28.209 31.689

ATOM 2230 C ALA C2297 41.192 27.029 30.779

ATOM 2231 O ALA C2297 40.551 26.980 29.740

ATOM 2232 CB ALA C2297 41.566 29.411 30.940

ATOM 2233 HA ALA C2297 39.898 28.332 31.807

ATOM 2234 HBl ALA C2297 41.107 29.501 29.946

ATOM 2235 HB2 ALA C2297 41.333 30.290 31.552

ATOM 2236 HB3 ALA C2297 42.654 29.283 30.825

ATOM 2237 H ALA C2297 42.312 28.713 33.284

ATOM 2238 N THR C2298 42.005 26.088 31.132

ATOM 2239 CA THR C2298 42.252 24.889 30.342

ATOM 2240 C THR C2298 41.584 23.699 30.988

ATOM 2241 O THR C2298 41.192 22.778 30.287

ATOM 2242 CB THR C2298 43.785 24.672 30.298

ATOM 2243 OGl THR C2298 44.285 24.630 31.646

ATOM 2244 CG2 THR C2298 44.462 25.812 29.494

ATOM 2245 HA THR C2298 41.854 25.020 29.323

ATOM 2246 HB THR C2298 43.994 23.705 29.814

ATOM 2247 HGl THR C2298 45.220 24.456 31.684

ATOM 2248 HG23 THR C2298 44.131 25.771 28.449

ATOM 2249 HG21 THR C2298 44.190 26.799 29.889

ATOM 2250 HG22 THR C2298 45.556 25.703 29.526

ATOM 2251 H THR C2298 42.464 26.186 32.020

ATOM 2252 N GLY C2299 41.152 23.749 32.255

ATOM 2253 CA GLY C2299 40.492 22.604 32.866

ATOM 2254 C GLY C2299 40.640 22.641 34.368

ATOM 2255 O GLY C2299 39.672 22.926 35.054

ATOM 2256 HA2 GLY C2299 40.934 21.658 32.513

ATOM 2257 HAl GLY C2299 39.424 22.603 32.590

ATOM 2258 H GLY C2299 41.312 24.552 32.832

ATOM 2259 N PHE C2300 41.888 22.348 34.893

ATOM 2260 CA PHE C2300 42.107 22.118 36.317

ATOM 2261 C PHE C2300 43.110 23.056 36.931

ATOM 2262 O PHE C2300 44.122 23.341 36.317

ATOM 2263 CB PHE C2300 42.608 20.670 36.542

ATOM 2264 CG PHE C2300 41.651 19.695 35.849

ATOM 2265 CDl PHE C2300 42.001 19.084 34.639

ATOM 2266 CD2 PHE C2300 40.408 19.419 36.427

ATOM 2267 CEl PHE C2300 41.098 18.235 33.992

ATOM 2268 CE2 PHE C2300 39.501 18.577 35.778

ATOM 2269 CZ PHE C2300 39.843 17.992 34.556

ATOM 2270 HA PHE C2300 41.165 22.259 36.868

ATOM 2271 HBl PHE C2300 43.626 20.563 36.135

ATOM 2272 HB2 PHE C2300 42.652 20.450 37.618

ATOM 2273 HD2 PHE C2300 40.142 19.863 37.381

ATOM 2274 HE2 PHE C2300 38.531 18.379 36.223

ATOM 2275 HZ PHE C2300 39.134 17.348 34.044

ATOM 2276 HEl PHE C2300 41.372 17.767 33.051

ATOM 2277 HDl PHE C2300 42.973 19.266 34.192

ATOM 2278 H PHE C2300 42.664 22.261 34.265

ATOM 2279 N ILE C2301 42.948 23.321 38.263

ATOM 2280 CA ILE C2301 44.100 23.760 39.043

ATOM 2281 C ILE C2301 44.878 22.510 39.354 ATOM 2282 O ILE C2301 44.247 21.501 39.627

ATOM 2283 CB ILE C2301 43.710 24.501 40.349

ATOM 2284 CGl ILE C2301 42.701 25.656 40.087

ATOM 2285 CG2 ILE C2301 44.953 24.981 41.150

ATOM 2286 CDl ILE C2301 43.178 26.683 39.030

ATOM 2287 HA ILE C2301 44.730 24.432 38.448

ATOM 2288 HB ILE C2301 43.197 23.760 40.974

ATOM 2289 HGIl ILE C2301 41.745 25.237 39.735

ATOM 2290 HG12 ILE C2301 42.502 26.184 41.034

ATOM 2291 HDIl ILE C2301 43.277 26.229 38.033

ATOM 2292 HD12 ILE C2301 42.419 27.466 38.958

ATOM 2293 HD13 ILE C2301 44.129 27.153 39.316

ATOM 2294 HG21 ILE C2301 45.566 25.660 40.544

ATOM 2295 HG22 ILE C2301 44.645 25.510 42.066

ATOM 2296 HG23 ILE C2301 45.577 24.125 41.451

ATOM 2297 H ILE C2301 42.101 23.120 38.762

ATOM 2298 N VAL C2302 46.230 22.551 39.300

ATOM 2299 CA VAL C2302 47.017 21.326 39.413

ATOM 2300 C VAL C2302 47.943 21.375 40.602

ATOM 2301 O VAL C2302 48.490 22.437 40.852

ATOM 2302 CB VAL C2302 47.838 21.117 38.107

ATOM 2303 CGl VAL C2302 48.738 19.852 38.188

ATOM 2304 CG2 VAL C2302 46.880 21.034 36.886

ATOM 2305 HA VAL C2302 46.353 20.463 39.539

ATOM 2306 HB VAL C2302 48.498 21.990 37.962

ATOM 2307 HGIl VAL C2302 48.141 18.961 38.425

ATOM 2308 HG12 VAL C2302 49.240 19.681 37.223

ATOM 2309 HGl 3 VAL C2302 49.514 19.972 38.960

ATOM 2310 HG21 VAL C2302 46.345 21.986 36.754

ATOM 2311 HG22 VAL C2302 47.441 20.827 35.961

ATOM 2312 HG23 VAL C2302 46.137 20.237 37.031

ATOM 2313 H VAL C2302 46.723 23.401 39.118

ATOM 2314 N ASP C2303 48.133 20.231 41.312

ATOM 2315 CA ASP C2303 49.148 20.134 42.356

ATOM 2316 C ASP C2303 50.250 19.223 41.841

ATOM 2317 O ASP C2303 49.979 18.041 41.712

ATOM 2318 CB ASP C2303 48.612 19.483 43.657

ATOM 2319 CG ASP C2303 49.667 19.318 44.723

ATOM 2320 ODl ASP C2303 50.730 19.993 44.644

ATOM 2321 OD2 ASP C2303 49.447 18.496 45.654

ATOM 2322 HA ASP C2303 49.451 21.137 42.672

ATOM 2323 HBl ASP C2303 47.790 20.093 44.028

ATOM 2324 HB2 ASP C2303 48.195 18.494 43.466

ATOM 2325 H ASP C2303 47.637 19.389 41.097

ATOM 2326 N PRO C2304 51.495 19.651 41.530

ATOM 2327 CA PRO C2304 52.528 18.682 41.185

ATOM 2328 C PRO C2304 52.892 17.667 42.246

ATOM 2329 O PRO C2304 53.287 16.568 41.891

ATOM 2330 CB PRO C2304 53.718 19.637 40.930

ATOM 2331 CG PRO C2304 53.366 20.917 41.701

ATOM 2332 CD PRO C2304 51.854 21.061 41.476

ATOM 2333 HA PRO C2304 52.243 18.160 40.261

ATOM 2334 HD2 PRO C2304 51.468 21.728 42.254

ATOM 2335 HDl PRO C2304 51.626 21.459 40.475

ATOM 2336 HG2 PRO C2304 53.573 20.791 42.775

ATOM 2337 HGl PRO C2304 53.937 21.770 41.331

ATOM 2338 HBl PRO C2304 54.686 19.265 41.278

ATOM 2339 HB2 PRO C2304 53.782 19.875 39.858

ATOM 2340 N VAL C2305 52.795 18.023 43.544

ATOM 2341 CA VAL C2305 53.444 17.230 44.587

ATOM 2342 C VAL C2305 52.683 15.933 44.756

ATOM 2343 O VAL C2305 53.293 14.877 44.689

ATOM 2344 CB VAL C2305 53.558 18.009 45.936

ATOM 2345 CGl VAL C2305 54.308 17.156 46.996

ATOM 2346 CG2 VAL C2305 54.301 19.368 45.773

ATOM 2347 HA VAL C2305 54.473 17.005 44.257

ATOM 2348 HB VAL C2305 52.543 18.221 46.314

ATOM 2349 HGIl VAL C2305 55.332 16.935 46.654 ATOM 2350 HGl 2 VAL C2305 54.371 17.700 47.952

ATOM 2351 HGl 3 VAL C2305 53.784 16.206 47.178

ATOM 2352 HG21 VAL C2305 53.765 20.059 45.110

ATOM 2353 HG22 VAL C2305 54.405 19.872 46.747

ATOM 2354 HG23 VAL C2305 55.305 19.199 45.362

ATOM 2355 H VAL C2305 52.312 18.857 43.794

ATOM 2356 N SER C2306 51.345 16.000 44.958

ATOM 2357 CA SER C2306 50.515 14.792 44.998

ATOM 2358 C SER C2306 49.916 14.487 43.632

ATOM 2359 O SER C2306 49.053 13.628 43.547

ATOM 2360 CB SER C2306 49.416 14.994 46.074

ATOM 2361 OG SER C2306 48.666 13.780 46.247

ATOM 2362 HA SER C2306 51.117 13.923 45.311

ATOM 2363 HBl SER C2306 49.901 15.272 47.025

ATOM 2364 HB2 SER C2306 48.750 15.817 45.770

ATOM 2365 HG SER C2306 47.994 13.862 46.916

ATOM 2366 H SER C2306 50.884 16.886 45.008

ATOM 2367 N ASN C2307 50.362 15.170 42.549

ATOM 2368 CA ASN C2307 49.832 14.946 41.200

ATOM 2369 C ASN C2307 48.316 14.979 41.162

ATOM 2370 O ASN C2307 47.712 14.042 40.663

ATOM 2371 CB ASN C2307 50.383 13.624 40.605

ATOM 2372 CG ASN C2307 50.434 13.566 39.091

ATOM 2373 ODl ASN C2307 51.249 12.806 38.592

ATOM 2374 ND2 ASN C2307 49.618 14.306 38.305

ATOM 2375 HA ASN C2307 50.192 15.783 40.579

ATOM 2376 HBl ASN C2307 51.410 13.514 40.980

ATOM 2377 HB2 ASN C2307 49.818 12.760 40.986

ATOM 2378 HD22 ASN C2307 49.706 14.234 37.310

ATOM 2379 HD21 ASN C2307 48.926 14.928 38.666

ATOM 2380 H ASN C2307 51.098 15.838 42.636

ATOM 2381 N LEU C2308 47.698 16.069 41.674

ATOM 2382 CA LEU C2308 46.237 16.201 41.684

ATOM 2383 C LEU C2308 45.824 17.210 40.633

ATOM 2384 O LEU C2308 46.568 18.147 40.398

ATOM 2385 CB LEU C2308 45.652 16.598 43.065

ATOM 2386 CG LEU C2308 45.931 15.552 44.185

ATOM 2387 CDl LEU C2308 45.656 16.185 45.577

ATOM 2388 CD2 LEU C2308 45.065 14.268 44.026

ATOM 2389 HA LEU C2308 45.772 15.241 41.423

ATOM 2390 HBl LEU C2308 46.066 17.576 43.340

ATOM 2391 HB2 LEU C2308 44.564 16.722 42.978

ATOM 2392 HG LEU C2308 46.993 15.264 44.141

ATOM 2393 HD21 LEU C2308 45.317 13.722 43.106

ATOM 2394 HD22 LEU C2308 45.239 13.583 44.871

ATOM 2395 HD23 LEU C2308 43.994 14.522 44.004

ATOM 2396 HDIl LEU C2308 44.608 16.510 45.645

ATOM 2397 HD12 LEU C2308 45.850 15.458 46.380

ATOM 2398 HDl 3 LEU C2308 46.305 17.059 45.740

ATOM 2399 H LEU C2308 48.250 16.826 42.008

ATOM 2400 N ARG C2309 44.647 17.011 39.991

ATOM 2401 CA ARG C2309 44.186 17.858 38.888

ATOM 2402 C ARG C2309 42.754 18.210 39.227

ATOM 2403 O ARG C2309 41.868 17.470 38.828

ATOM 2404 CB ARG C2309 44.346 17.066 37.560

ATOM 2405 CG ARG C2309 45.848 16.845 37.216

ATOM 2406 CD ARG C2309 46.034 15.842 36.046

ATOM 2407 NE ARG C2309 45.535 16.391 34.778

ATOM 2408 CZ ARG C2309 44.899 15.711 33.842

ATOM 2409 NHl ARG C2309 44.606 14.430 33.908

ATOM 2410 NH2 ARG C2309 44.535 16.354 32.754

ATOM 2411 HA ARG C2309 44.771 18.783 38.790

ATOM 2412 HBl ARG C2309 43.845 16.092 37.671

ATOM 2413 HB2 ARG C2309 43.858 17.613 36.736

ATOM 2414 HGl ARG C2309 46.319 17.806 36.958

ATOM 2415 HG2 ARG C2309 46.376 16.440 38.095

ATOM 2416 HDl ARG C2309 47.111 15.652 35.904

ATOM 2417 HD2 ARG C2309 45.574 14.915 36.407 ATOM 2418 HE ARG C2309 45.708 17.398 34.625

ATOM 2419 HHl 2 ARG C2309 44.096 13.965 33.142

ATOM 2420 HHIl ARG C2309 44.868 13.845 34.704

ATOM 2421 HH22 ARG C2309 44.048 15.868 31.988

ATOM 2422 HH21 ARG C2309 44.738 17.357 32.626

ATOM 2423 H ARG C2309 44.068 16.232 40.235

ATOM 2424 N LEU C2310 42.532 19.308 39.994

ATOM 2425 CA LEU C2310 41.225 19.539 40.613

ATOM 2426 C LEU C2310 40.601 20.844 40.173

ATOM 2427 O LEU C2310 41.371 21.782 40.039

ATOM 2428 CB LEU C2310 41.415 19.510 42.152

ATOM 2429 CG LEU C2310 41.765 18.084 42.674

ATOM 2430 CDl LEU C2310 42.208 18.163 44.159

ATOM 2431 CD2 LEU C2310 40.586 17.079 42.515

ATOM 2432 HA LEU C2310 40.553 18.721 40.365

ATOM 2433 HBl LEU C2310 42.226 20.209 42.413

ATOM 2434 HB2 LEU C2310 40.506 19.870 42.650

ATOM 2435 HG LEU C2310 42.614 17.696 42.089

ATOM 2436 HD21 LEU C2310 40.484 16.740 41.474

ATOM 2437 HD22 LEU C2310 40.747 16.178 43.127

ATOM 2438 HD23 LEU C2310 39.638 17.541 42.823

ATOM 2439 HDIl LEU C2310 41.416 18.615 44.771

ATOM 2440 HD12 LEU C2310 42.423 17.156 44.546

ATOM 2441 HDl 3 LEU C2310 43.120 18.772 44.261

ATOM 2442 H LEU C2310 43.277 19.938 40.225

ATOM 2443 N PRO C2311 39.265 20.991 39.938

ATOM 2444 CA PRO C2311 38.727 22 299 39.602

ATOM 2445 C PRO C2311 38.985 23.342 40.658

ATOM 2446 O PRO C2311 39.499 23.030 41.719

ATOM 2447 CB PRO C2311 37.208 21.996 39.534

ATOM 2448 CG PRO C2311 37.153 20.506 39.146

ATOM 2449 CD PRO C2311 38.312 19.882 39.956

ATOM 2450 HA PRO C2311 39.128 22.626 38.627

ATOM 2451 HD2 PRO C2311 38.007 19.656 40.989

ATOM 2452 HDl PRO C2311 38.610 18.964 39.428

ATOM 2453 HG2 PRO C2311 36.178 20.037 39.357

ATOM 2454 HGl PRO C2311 37.365 20.418 38.066

ATOM 2455 HBl PRO C2311 36.750 22.110 40.531

ATOM 2456 HB2 PRO C2311 36.661 22.630 38.820

ATOM 2457 N VAL C2312 38.602 24.593 40.337

ATOM 2458 CA VAL C2312 38.878 25.729 41.214

ATOM 2459 C VAL C2312 38.307 25.496 42.595

ATOM 2460 O VAL C2312 39.009 25.718 43.570

ATOM 2461 CB VAL C2312 38.316 27.052 40.638

ATOM 2462 CGl VAL C2312 38.510 28.203 41.673

ATOM 2463 CG2 VAL C2312 39.055 27.367 39.309

ATOM 2464 HA VAL C2312 39.967 25.843 41.324

ATOM 2465 HB VAL C2312 37.236 26.934 40.434

ATOM 2466 HGIl VAL C2312 39.580 28.335 41.900

ATOM 2467 HGl 2 VAL C2312 38.118 29.156 41.303

ATOM 2468 HG13 VAL C2312 37.964 27.999 42.606

ATOM 2469 HG21 VAL C2312 38.879 26.641 38.503

ATOM 2470 HG22 VAL C2312 38.703 28.338 38.956

ATOM 2471 HG23 VAL C2312 40.137 27.431 39.477

ATOM 2472 H VAL C2312 38.125 24.740 39.472

ATOM 2473 N GLU C2313 37.031 25.064 42.706

ATOM 2474 CA GLU C2313 36.431 24.884 44.030

ATOM 2475 C GLU C2313 37.119 23.754 44.767

ATOM 2476 O GLU C2313 37.596 23.985 45.863

ATOM 2477 CB GLU C2313 34.893 24.638 43.975

ATOM 2478 CG GLU C2313 34.067 25.963 43.935

ATOM 2479 CD GLU C2313 33.354 26.201 45.245

ATOM 2480 OEl GLU C2313 34.031 26.163 46.310

ATOM 2481 OE2 GLU C2313 32.113 26.427 45.228

ATOM 2482 HA GLU C2313 36.614 25.793 44.628

ATOM 2483 HBl GLU C2313 34.657 24.011 43.100

ATOM 2484 HB2 GLU C2313 34.588 24.055 44.860

ATOM 2485 HGl GLU C2313 34.707 26.835 43.731 ATOM 2486 HG2 GLU C2313 33.319 25.919 43.127

ATOM 2487 H GLU C2313 36.491 24.866 41.887

ATOM 2488 N GLU C2314 37.206 22.515 44.235

ATOM 2489 CA GLU C2314 37.848 21.455 45.021

ATOM 2490 C GLU C2314 39.288 21.827 45.322

ATOM 2491 O GLU C2314 39.786 21.459 46.372

ATOM 2492 CB GLU C2314 37.718 20.081 44.313

ATOM 2493 CG GLU C2314 38.167 18.897 45.210

ATOM 2494 CD GLU C2314 37.259 18.722 46.400

ATOM 2495 OEl GLU C2314 36.094 18.283 46.199

ATOM 2496 OE2 GLU C2314 37.699 19.018 47.544

ATOM 2497 HA GLU C2314 37.298 21.365 45.973

ATOM 2498 HBl GLU C2314 36.666 19.917 44.026

ATOM 2499 HB2 GLU C2314 38.316 20.110 43.394

ATOM 2500 HGl GLU C2314 38.134 17.964 44.627

ATOM 2501 HG2 GLU C2314 39.201 19.049 45.549

ATOM 2502 H GLU C2314 36.840 22.312 43.325

ATOM 2503 N ALA C2315 39.984 22.565 44.430

ATOM 2504 CA ALA C2315 41.364 22.980 44.706

ATOM 2505 C ALA C2315 41.426 23.938 45.878

ATOM 2506 O ALA C2315 42.234 23.772 46.780

ATOM 2507 CB ALA C2315 41.941 23.615 43.416

ATOM 2508 HA ALA C2315 41.969 22.092 44.947

ATOM 2509 HBl ALA C2315 42.974 23.950 43.544

ATOM 2510 HB2 ALA C2315 41.914 22.843 42.632

ATOM 2511 HB3 ALA C2315 41.347 24.480 43.089

ATOM 2512 H ALA C2315 39.557 22.844 43.570

ATOM 2513 N TYR C2316 40.533 24.949 45.861

ATOM 2514 CA TYR C2316 40.370 25.857 46.998

ATOM 2515 C TYR C2316 40.186 25.073 48.284

ATOM 2516 O TYR C2316 40.783 25.418 49.293

ATOM 2517 CB TYR C2316 39.151 26.775 46.699

ATOM 2518 CG TYR C2316 38.792 27.639 47.903

ATOM 2519 CDl TYR C2316 39.654 28.674 48.268

ATOM 2520 CD2 TYR C2316 37.626 27.410 48.643

ATOM 2521 CEl TYR C2316 39.422 29.378 49.449

ATOM 2522 CE2 TYR C2316 37.344 28.194 49.764

ATOM 2523 CZ TYR C2316 38.249 29.172 50.184

ATOM 2524 OH TYR C2316 37.958 29.918 51.328

ATOM 2525 HA TYR C2316 41.263 26.493 47.105

ATOM 2526 HB2 TYR C2316 39.379 27.420 45.836

ATOM 2527 HBl TYR C2316 38.273 26.176 46.438

ATOM 2528 HD2 TYR C2316 36.933 26.626 48.356

ATOM 2529 HE2 TYR C2316 36.422 28.043 50.316

ATOM 2530 HEl TYR C2316 40.175 30.076 49.777

ATOM 2531 HDl TYR C2316 40.504 28.928 47.644

ATOM 2532 HH TYR C2316 38.670 30.470 51.625

ATOM 2533 H TYR C2316 39.944 25.073 45.062

ATOM 2534 N LYS C2317 39.368 23.996 48.258

ATOM 2535 CA LYS C2317 39.147 23.192 49.467

ATOM 2536 C LYS C2317 40.431 22.481 49.827

ATOM 2537 O LYS C2317 40.825 22.421 50.982

ATOM 2538 CB LYS C2317 38.043 22.112 49.259

ATOM 2539 CG LYS C2317 36.647 22.687 48.878

ATOM 2540 CD LYS C2317 35.904 23.329 50.079

ATOM 2541 CE LYS C2317 34.643 24.101 49.606

ATOM 2542 NZ LYS C2317 33.917 24.684 50.756

ATOM 2543 HA LYS C2317 38.860 23.849 50.301

ATOM 2544 HBl LYS C2317 38.369 21.444 48.449

ATOM 2545 HB2 LYS C2317 37.941 21.502 50.170

ATOM 2546 HGl LYS C2317 36.750 23.437 48.086

ATOM 2547 HG2 LYS C2317 36.017 21.872 48.483

ATOM 2548 HDl LYS C2317 35.612 22.538 50.789

ATOM 2549 HD2 LYS C2317 36.560 24.038 50.604

ATOM 2550 HEl LYS C2317 34.949 24.912 48.922

ATOM 2551 HE2 LYS C2317 33.975 23.421 49.050

ATOM 2552 HZl LYS C2317 34.544 25.361 51.320

ATOM 2553 HZ2 LYS C2317 33.053 25.248 50.431 ATOM 2554 HZ3 LYS C2317 33.567 23.917 51.433

ATOM 2555 H LYS C2317 38.953 23.713 47.391

ATOM 2556 N ARG C2318 41.105 21.935 48.791

ATOM 2557 CA ARG C2318 42.357 21.206 49.000

ATOM 2558 C ARG C2318 43.477 22.116 49.489

ATOM 2559 O ARG C2318 44.544 21.609 49.799

ATOM 2560 CB ARG C2318 42.709 20.466 47.672

ATOM 2561 CG ARG C2318 43.580 19.196 47.884

ATOM 2562 CD ARG C2318 42.710 17.907 47.999

ATOM 2563 NE ARG C2318 43.414 16.905 48.803

ATOM 2564 CZ ARG C2318 43.260 16.742 50.103

ATOM 2565 NHl ARG C2318 42.461 17.466 50.856

ATOM 2566 NH2 ARG C2318 43.951 15.791 50.692

ATOM 2567 HA ARG C2318 42.184 20.446 49.775

ATOM 2568 HBl ARG C2318 41.804 20.136 47.139

ATOM 2569 HB2 ARG C2318 43.190 21.194 47.013

ATOM 2570 HGl ARG C2318 44.274 19.081 47.034

ATOM 2571 HG2 ARG C2318 44.193 19.311 48.790

ATOM 2572 HDl ARG C2318 41.685 18.100 48.340

ATOM 2573 HD2 ARG C2318 42.573 17.498 46.985

ATOM 2574 HE ARG C2318 44.060 16.280 48.292

ATOM 2575 HHl 2 ARG C2318 42.379 17.287 51.868

ATOM 2576 HHIl ARG C2318 41.896 18.230 50.478

ATOM 2577 HH22 ARG C2318 43.869 15.622 51.706

ATOM 2578 HH21 ARG C2318 44.598 15.191 50.160

ATOM 2579 H ARG C2318 40.746 22.026 47.862

ATOM 2580 N GLY C2319 43.277 23.457 49.577

ATOM 2581 CA GLY C2319 44.345 24.354 50.014

ATOM 2582 C GLY C2319 45.336 24.633 48.908

ATOM 2583 O GLY C2319 46.408 25.143 49.198

ATOM 2584 HA2 GLY C2319 44.876 23.911 50.872

ATOM 2585 HAl GLY C2319 43.919 25.315 50.354

ATOM 2586 H GLY C2319 42.421 23.890 49.301

ATOM 2587 N LEU C2320 44.997 24.312 47.637

ATOM 2588 CA LEU C2320 45.921 24.568 46.535

ATOM 2589 C LEU C2320 45.799 25.987 46.047

ATOM 2590 O LEU C2320 46.728 26.418 45.382

ATOM 2591 CB LEU C2320 45.686 23.605 45.348

ATOM 2592 CG LEU C2320 45.860 22.106 45.720

ATOM 2593 CDl LEU C2320 45.335 21.235 44.543

ATOM 2594 CD2 LEU C2320 47.318 21.747 46.118

ATOM 2595 HA LEU C2320 46.957 24.416 46.876

ATOM 2596 HBl LEU C2320 44.656 23.779 45.020

ATOM 2597 HB2 LEU C2320 46.361 23.855 44.513

ATOM 2598 HG LEU C2320 45.257 21.888 46.609

ATOM 2599 HD21 LEU C2320 47.604 22.225 47.065

ATOM 2600 HD22 LEU C2320 47.408 20.662 46.279

ATOM 2601 HD23 LEU C2320 48.027 22.066 45.339

ATOM 2602 HDIl LEU C2320 45.890 21.459 43.619

ATOM 2603 HD12 LEU C2320 45.428 20.163 44.775

ATOM 2604 HD13 LEU C2320 44.272 21.446 44.355

ATOM 2605 H LEU C2320 44.099 23.933 47.410

ATOM 2606 N VAL C2321 44.698 26.716 46.353

ATOM 2607 CA VAL C2321 44.653 28.129 46.008

ATOM 2608 C VAL C2321 44.091 28.951 47.145

ATOM 2609 O VAL C2321 43.232 28.471 47.869

ATOM 2610 CB VAL C2321 43.929 28.361 44.665

ATOM 2611 CGl VAL C2321 42.409 28.051 44.731

ATOM 2612 CG2 VAL C2321 44.168 29.833 44.278

ATOM 2613 HA VAL C2321 45.687 28.483 45.878

ATOM 2614 HB VAL C2321 44.391 27.710 43.902

ATOM 2615 HGIl VAL C2321 41.918 28.656 45.508

ATOM 2616 HG12 VAL C2321 41.929 28.279 43.766

ATOM 2617 HGl 3 VAL C2321 42.252 26.985 44.946

ATOM 2618 HG21 VAL C2321 45.235 30.092 44.244

ATOM 2619 HG22 VAL C2321 43.778 29.967 43.286

ATOM 2620 HG23 VAL C2321 43.626 30.503 44.956

ATOM 2621 H VAL C2321 43.901 26.323 46.813 ATOM 2622 N GLY C2322 44.586 30.199 47.325

ATOM 2623 CA GLY C2322 44.098 31.026 48.414

ATOM 2624 C GLY C2322 42.706 31.586 48.214

ATOM 2625 O GLY C2322 41.981 31.217 47.304

ATOM 2626 HA2 GLY C2322 44.800 31.863 48.564

ATOM 2627 HAl GLY C2322 44.098 30.426 49.335

ATOM 2628 H GLY C2322 45.307 30.582 46.742

ATOM 2629 N ILE C2323 42.355 32.498 49.143

ATOM 2630 CA ILE C2323 41.000 33.022 49.275

ATOM 2631 C ILE C2323 40.845 34.183 48.312

ATOM 2632 O ILE C2323 39.843 34.307 47.627

ATOM 2633 CB ILE C2323 40.800 33.466 50.768

ATOM 2634 CGl ILE C2323 41.132 32.376 51.852

ATOM 2635 CG2 ILE C2323 39.336 33.958 50.952

ATOM 2636 CDl ILE C2323 42.612 32.208 52.315

ATOM 2637 HA ILE C2323 40.246 32.260 49.016

ATOM 2638 HB ILE C2323 41.450 34.331 50.981

ATOM 2639 HGIl ILE C2323 40.572 32.621 52.769

ATOM 2640 HG12 ILE C2323 40.791 31.392 51.520

ATOM 2641 HDIl ILE C2323 43.087 33.187 52.482

ATOM 2642 HD12 ILE C2323 42.641 31.651 53.266

ATOM 2643 HD13 ILE C2323 43.219 31.623 51.610

ATOM 2644 HG21 ILE C2323 38.632 33.126 50.800

ATOM 2645 HG22 ILE C2323 39.184 34.365 51.965

ATOM 2646 HG23 ILE C2323 39.098 34.759 50.237

ATOM 2647 H ILE C2323 43.054 32.843 49.758

ATOM 2648 N GLU C2324 41.879 35.047 48.264

ATOM 2649 CA GLU C2324 41.934 36.216 47.382

ATOM 2650 C GLU C2324 41.643 35.816 45.950

ATOM 2651 O GLU C2324 40.779 36.374 45.292

ATOM 2652 CB GLU C2324 43.325 36.951 47.398

ATOM 2653 CG GLU C2324 44.207 36.843 48.680

ATOM 2654 CD GLU C2324 44.950 35.526 48.771

ATOM 2655 OEl GLU C2324 44.592 34.699 49.655

ATOM 2656 OE2 GLU C2324 45.886 35.300 47.955

ATOM 2657 HA GLU C2324 41.171 36.948 47.710

ATOM 2658 HBl GLU C2324 43.971 36.583 46.594

ATOM 2659 HB2 GLU C2324 43.148 38.020 47.188

ATOM 2660 HGl GLU C2324 44.987 37.621 48.648

ATOM 2661 HG2 GLU C2324 43.595 37.027 49.578

ATOM 2662 H GLU C2324 42.621 34.896 48.894

ATOM 2663 N PHE C2325 42.367 34.913 45.395

ATOM 2664 CA PHE C2325 42.377 34.429 44.021

ATOM 2665 C PHE C2325 41.133 33.623 43.729

ATOM 2666 O PHE C2325 40.757 33.461 42.578

ATOM 2667 CB PHE C2325 43.623 33.492 43.936

ATOM 2668 CG PHE C2325 44.998 34.186 43.973

ATOM 2669 CDl PHE C2325 45.192 35.562 44.215

ATOM 2670 CD2 PHE C2325 46.117 33.388 43.747

ATOM 2671 CEl PHE C2325 46.470 36.106 44.227

ATOM 2672 CE2 PHE C2325 47.409 33.932 43.734

ATOM 2673 CZ PHE C2325 47.585 35. 190 43.969

ATOM 2674 HA PHE C2325 42.373 35. >85 43.331

ATOM 2675 HBl PHE C2325 43.602 32.788 44.780

ATOM 2676 HB2 PHE C2325 43.576 32.845 43.056

ATOM 2677 HD2 PHE C2325 45.993 32.327 43.576

ATOM 2678 HE2 PHE C2325 48.264 33.292 43.536

ATOM 2679 HZ PHE C2325 48.577 35.722 43.954

ATOM 2680 HEl PHE C2325 46.613 37.164 44.430

ATOM 2681 HDl PHE C2325 44.356 36.226 44.384

ATOM 2682 H PHE C2325 42.936 34.455 46.079

ATOM 2683 N LYS C2326 40.364 33.136 44.611

ATOM 2684 CA LYS C2326 39.335 .163 44.266

ATOM 2685 C LYS C2326 38.353 32.696 43. 235

ATOM 2686 O LYS C2326 38.156 32.062 42.210

ATOM 2687 CB LYS C2326 38.561 31.702 45.533

ATOM 2688 CG LYS C2326 37.635 30.490 45.230

ATOM 2689 CD LYS C2326 36.468 30.407 46.248 ATOM 2690 CE LYS C2326 35.537 29.202 45.946

ATOM 2691 NZ LYS C2326 34.285 29.298 46.731

ATOM 2692 HA LYS C2326 39.842 31.278 43.850

ATOM 2693 HBl LYS C2326 39.267 31.411 46.329

ATOM 2694 HB2 LYS C2326 37.974 32.553 45.911

ATOM 2695 HGl LYS C2326 37.198 30.585 44.994

ATOM 2696 HG2 LYS C2326 38.226 29.560 45. ?52

ATOM 2697 HDl LYS C2326 36.859 30.331 47.276

ATOM 2698 HD2 LYS C2326 35.877 31.335 46.169

ATOM 2699 HEl LYS C2326 35.282 29.196 44.874

ATOM 2700 HE2 LYS C2326 36.066 28.262 46.175

ATOM 2701 HZl LYS C2326 33.727 30.192 46.487

ATOM 2702 HZ2 LYS C2326 33.621 28.470 46.534

ATOM 2703 HZ3 LYS C2326 34.481 29.306 47.794

ATOM 2704 H LYS C2326 40.551 33.331 45.577

ATOM 2705 N GLU C2327 37.710 33.855 43.509

ATOM 2706 CA GLU C2327 36.615 34.342 42.656

ATOM 2707 C GLU C2327 37.055 34.525 41.215

ATOM 2708 O GLU C2327 36.283 34.301 40.296

ATOM 2709 CB GLU C2327 36.146 35.725 43.205

ATOM 2710 CG GLU C2327 34.748 36.157 42.686

ATOM 2711 CD GLU C2327 33.677 35.678 43.638

ATOM 2712 OEl GLU C2327 33.318 34.472 43.605

ATOM 2713 OE2 GLU C2327 33.197 36.515 44.455

ATOM 2714 HA GLU C2327 35.770 33.633 42.706

ATOM 2715 HBl GLU C2327 36.100 35.728 44.307

ATOM 2716 HB2 GLU C2327 36.910 36.466 42.930

ATOM 2717 HGl GLU C2327 34.668 37.249 42.749

ATOM 2718 HG2 GLU C2327 34.605 35.881 41.626

ATOM 2719 H GLU C2327 37.958 34.373 44.329

ATOM 2720 N LYS C2328 38.316 34.973 41.024

ATOM 2721 CA LYS C2328 38.818 35.286 39.683

ATOM 2722 C LYS C2328 38.835 33.994 38.907

ATOM 2723 O LYS C2328 38.292 33.873 37.820

ATOM 2724 CB LYS C2328 40.252 35.898 39.628

ATOM 2725 CG LYS C2328 40.697 36.579 40.945

ATOM 2726 CD LYS C2328 41.983 37.408 40.754

ATOM 2727 CE LYS C2328 42.357 38.183 42.051

ATOM 2728 NZ LYS C2328 43.357 39.229 41.772

ATOM 2729 HA LYS C2328 38.135 36.021 39.223

ATOM 2730 HBl LYS C2328 41.011 35.132 39.398

ATOM 2731 HB2 LYS C2328 40.266 36.645 38.818

ATOM 2732 HGl LYS C2328 39.870 37.187 41.339

ATOM 2733 HG2 LYS C2328 40.953 35.821 41.690

ATOM 2734 HDl LYS C2328 42.788 36.732 40.443

ATOM 2735 HD2 LYS C2328 41.829 38.097 39.923

ATOM 2736 HEl LYS C2328 41.476 38.655 42.512

ATOM 2737 HE2 LYS C2328 42.767 37.486 42.796

ATOM 2738 HZl LYS C2328 43.009 39.968 41.062

ATOM 2739 HZ2 LYS C2328 43.661 39.750 42.670

ATOM 2740 HZ3 LYS C2328 44.220 38.734 41.365

ATOM 2741 H LYS C2328 38.900 35.088 41.820

ATOM 2742 N LEU C2329 39.519 33.009 39.529

ATOM 2743 CA LEU C2329 39.765 31.735 38.865

ATOM 2744 C LEU C2329 38.475 31.050 38.522

ATOM 2745 O LEU C2329 38.317 30.531 37.429

ATOM 2746 CB LEU C2329 40.580 30.799 39.807

ATOM 2747 CG LEU C2329 42.064 31.239 39.950

ATOM 2748 CDl LEU C2329 42.678 30.673 41.244

ATOM 2749 CD2 LEU C2329 42.902 30.738 38.750

ATOM 2750 HA LEU C2329 40.329 31.933 37.943

ATOM 2751 HBl LEU C2329 40.094 30.774 40.794

ATOM 2752 HB2 LEU C2329 40.579 29.776 39.414

ATOM 2753 HG LEU C2329 .131 32.338 40.005

ATOM 2754 HD21 LEU C2329 .363 30.961 37.830

ATOM 2755 HD22 LEU C2329 43.883 31.225 38.718

ATOM 2756 HD23 LEU C2329 43.055 29.654 38.793

ATOM 2757 HDIl LEU C2329 42.631 29.571 41.260 ATOM 2758 HD12 LEU C2329 43.732 30.992 41.292

ATOM 2759 HDl 3 LEU C2329 42.133 31.066 42.118

ATOM 2760 H LEU C2329 39.913 33.158 40.441

ATOM 2761 N LEU C2330 37.556 31.062 39.506

ATOM 2762 CA LEU C2330 36.248 30.436 39.342

ATOM 2763 C LEU C2330 35.694 30.796 37.981

ATOM 2764 O LEU C2330 35.114 29.947 37.323

ATOM 2765 CB LEU C2330 35.283 30.964 40.453

ATOM 2766 CG LEU C2330 33.913 30.273 40.670

ATOM 2767 CDl LEU C2330 34.101 28.959 41.485

ATOM 2768 CD2 LEU C2330 32.995 31.252 41.467

ATOM 2769 HA LEU C2330 36.341 29.342 39.426

ATOM 2770 HBl LEU C2330 35.763 30.849 41.433

ATOM 2771 HB2 LEU C2330 35.100 32.032 40.269

ATOM 2772 HG LEU C2330 33.464 30.064 39.685

ATOM 2773 HD21 LEU C2330 32.802 32.170 40.887

ATOM 2774 HD22 LEU C2330 32.028 30.775 41.679

ATOM 2775 HD23 LEU C2330 33.459 31.548 42.423

ATOM 2776 HDIl LEU C2330 34.517 29.167 42.484

ATOM 2777 HD12 LEU C2330 33.129 28.464 41.621

ATOM 2778 HDl 3 LEU C2330 34.784 28.271 40.966

ATOM 2779 H LEU C2330 37.776 31.505 40.377

ATOM 2780 N SER C2331 35.897 32.065 37.554

ATOM 2781 CA SER C2331 35.451 32.496 36.234

ATOM 2782 C SER C2331 36.449 32.299 35.123

ATOM 2783 O SER C2331 36.002 32.083 34.008

ATOM 2784 CB SER C2331 35.028 33.973 36.261

ATOM 2785 OG SER C2331 33.840 34.119 37.058

ATOM 2786 HA SER C2331 34.546 31.944 35.982

ATOM 2787 HBl SER C2331 35.879 34.509 36.679

ATOM 2788 HB2 SER C2331 34.862 34.335 35.239

ATOM 2789 HG SER C2331 33.516 35.014 37.074

ATOM 2790 H SER C2331 36.365 32.730 38.137

ATOM 2791 N ALA C2332 37.776 32.369 35.350

ATOM 2792 CA ALA C2332 38.698 31.966 34.285

ATOM 2793 C ALA C2332 38.311 30.573 33.819

ATOM 2794 O ALA C2332 38.337 30.298 32.630

ATOM 2795 CB ALA C2332 40.168 31.972 34.748

ATOM 2796 HA ALA C2332 38.591 32.669 33.443

ATOM 2797 HBl ALA C2332 40.804 31.591 33.935

ATOM 2798 HB2 ALA C2332 40.465 32.996 35.018

ATOM 2799 HB3 ALA C2332 40.285 31.329 35.626

ATOM 2800 H ALA C2332 38.134 32.636 36.246

ATOM 2801 N GLU C2333 37.908 29.707 34.781

ATOM 2802 CA GLU C2333 37.397 28.364 34.475

ATOM 2803 C GLU C2333 36.271 28.369 33.447

ATOM 2804 O GLU C2333 36.026 27.342 32.836

ATOM 2805 CB GLU C2333 36.834 27.670 35.786

ATOM 2806 CG GLU C2333 37.031 26.131 35.765

ATOM 2807 CD GLU C2333 36.428 25.536 37.014

ATOM 2808 OEl GLU C2333 35.209 25.758 37.249

ATOM 2809 OE2 GLU C2333 37.166 24.858 37.777

ATOM 2810 HA GLU C2333 38.249 27.782 34.091

ATOM 2811 HBl GLU C2333 37.250 27.939 36.779

ATOM 2812 HB2 GLU C2333 35.764 27.914 35.861

ATOM 2813 HGl GLU C2333 36.552 25.692 34.877

ATOM 2814 HG2 GLU C2333 38.111 25.901 35.729

ATOM 2815 H GLU C2333 37.972 29.994 35.736

ATOM 2816 N ARG C2334 35.544 29.499 33.248

ATOM 2817 CA ARG C2334 34.416 29.558 32.307

ATOM 2818 C ARG C2334 34.852 29.604 30.854

ATOM 2819 O ARG C2334 34.028 29.372 29.982

ATOM 2820 CB ARG C2334 33.329 30.621 32.705

ATOM 2821 CG ARG C2334 32.697 30.260 34.089

ATOM 2822 CD ARG C2334 31.514 31.148 34.589

ATOM 2823 NE ARG C2334 31.887 32.567 34.642

ATOM 2824 CZ ARG C2334 31.687 33.441 33.672

ATOM 2825 NHl ARG C2334 30.908 33.239 32.641 ATOM 2826 NH2 ARG C2334 32.274 34.611 33.698

ATOM 2827 HA ARG C2334 33.906 28.590 32.394

ATOM 2828 HBl ARG C2334 33.730 31.648 32.714

ATOM 2829 HB2 ARG C2334 32.530 30.616 31.952

ATOM 2830 HGl ARG C2334 32.297 29.239 34.035

ATOM 2831 HG2 ARG C2334 33.492 30.245 34.848

ATOM 2832 HDl ARG C2334 30.596 30.910 34.041

ATOM 2833 HD2 ARG C2334 31.302 30.833 35.626

ATOM 2834 HE ARG C2334 32.355 32.879 35.508

ATOM 2835 HHl 2 ARG C2334 30.744 33.979 31.941

ATOM 2836 HHIl ARG C2334 30.344 32.400 32.570

ATOM 2837 HH22 ARG C2334 32.242 35.242 32.885

ATOM 2838 HH21 ARG C2334 32.808 34.915 34.512

ATOM 2839 H ARG C2334 35.758 30.327 33.747

ATOM 2840 N ALA C2335 36.156 29.832 30.578

ATOM 2841 CA ALA C2335 36.716 29.483 29.268

ATOM 2842 C ALA C2335 36.497 28.021 28.919

ATOM 2843 O ALA C2335 36.516 27.667 27.749

ATOM 2844 CB ALA C2335 38.220 29.760 29.141

ATOM 2845 HA ALA C2335 36.260 30.085 28.475

ATOM 2846 HBl ALA C2335 38.672 29.510 28.180

ATOM 2847 HB2 ALA C2335 38.365 30.834 29 299

ATOM 2848 HB3 ALA C2335 38.698 29.142 29.904

ATOM 2849 H ALA C2335 36.777 30.148 31.298

ATOM 2850 N VAL C2336 36.291 27.158 29.940

ATOM 2851 CA VAL C2336 36.095 25.722 29.731

ATOM 2852 C VAL C2336 34.606 25.454 29.703

ATOM 2853 O VAL C2336 34.108 24.911 28.731

ATOM 2854 CB VAL C2336 36.730 24.924 30.925

ATOM 2855 CGl VAL C2336 36.710 23.387 30.706

ATOM 2856 CG2 VAL C2336 38.169 25.393 31.282

ATOM 2857 HA VAL C2336 36.565 25.402 28.784

ATOM 2858 HB VAL C2336 36.130 25.098 31.832

ATOM 2859 HGIl VAL C2336 37.476 23.084 29.984

ATOM 2860 HG12 VAL C2336 36.927 22.865 31.652

ATOM 2861 HGl 3 VAL C2336 35.726 23.054 30.345

ATOM 2862 HG21 VAL C2336 38.199 26.448 31.583

ATOM 2863 HG22 VAL C2336 38.555 24.806 32.127

ATOM 2864 HG23 VAL C2336 38.842 25.259 30.428

ATOM 2865 H VAL C2336 36.251 27.493 30.876

ATOM 2866 N THR C2337 33.873 25.724 30.770

ATOM 2867 CA THR C2337 32.480 25.356 30.995

ATOM 2868 C THR C2337 31.581 26.261 30.190

ATOM 2869 O THR C2337 30.585 25.781 29.669

ATOM 2870 CB THR C2337 32.116 25.459 32.501

ATOM 2871 OGl THR C2337 32.336 26.811 32.919

ATOM 2872 CG2 THR C2337 32.959 24.480 33.365

ATOM 2873 HA THR C2337 32.315 24.307 30.687

ATOM 2874 HB THR C2337 31.044 25 221 32.628

ATOM 2875 HGl THR C2337 32.093 26.944 33.829

ATOM 2876 HG23 THR C2337 32.577 23.453 33.261

ATOM 2877 HG21 THR C2337 34.015 24.494 33.059

ATOM 2878 HG22 THR C2337 32.909 24.759 34.430

ATOM 2879 H THR C2337 34.258 26.469 31.313

ATOM 2880 N GLY C2338 31.892 27.568 29.951

ATOM 2881 CA GLY C2338 31.093 28.424 29.088

ATOM 2882 C GLY C2338 30.695 29.731 29.732

ATOM 2883 O GLY C2338 30.488 29.775 30.935

ATOM 2884 HA2 GLY C2338 30.163 27.935 28.806

ATOM 2885 HAl GLY C2338 31.641 28.605 28.151

ATOM 2886 H GLY C2338 32.721 27.962 30.345

ATOM 2887 N TYR C2339 30.537 30.786 28.897

ATOM 2888 CA TYR C2339 29.940 32.038 29.346

ATOM 2889 C TYR C2339 28.471 31.929 29.033

ATOM 2890 O TYR C2339 28.148 31.102 28.199

ATOM 2891 CB TYR C2339 30.540 33.244 28.577

ATOM 2892 CG TYR C2339 32.038 33.384 28.835

ATOM 2893 CDl TYR C2339 32.976 32.510 28.272 ATOM 2894 CD2 TYR C2339 32.513 34.415 29.645

ATOM 2895 CEl TYR C2339 34.283 32.502 28.739

ATOM 2896 CE2 TYR C2339 33.812 34.385 30.145

ATOM 2897 CZ TYR C2339 34.691 33.377 29.770

ATOM 2898 OH TYR C2339 35.932 33.273 30.406

ATOM 2899 HA TYR C2339 30.098 32.184 30.420

ATOM 2900 HB2 TYR C2339 30.441 33.093 27.500

ATOM 2901 HBl TYR C2339 30.004 34.168 28.847

ATOM 2902 HD2 TYR C2339 31.875 35.247 29.881

ATOM 2903 HE2 TYR C2339 34.128 35.165 30.825

ATOM 2904 HEl TYR C2339 34.968 31.818 28.280

ATOM 2905 HDl TYR C2339 32.688 31.843 27.464

ATOM 2906 HH TYR C2339 36.435 32.494 30.206

ATOM 2907 H TYR C2339 30.698 30.693 27.916

ATOM 2908 N ASN C2340 27.567 32.716 29.657

ATOM 2909 CA ASN C2340 26.142 32.581 29.344

ATOM 2910 C ASN C2340 25.693 33.771 28.513

ATOM 2911 O ASN C2340 26.276 34.827 28.681

ATOM 2912 CB ASN C2340 25.395 32.436 30.692

ATOM 2913 CG ASN C2340 23.936 32.131 30.493

ATOM 2914 ODl ASN C2340 23.155 33.067 30.482

ATOM 2915 ND2 ASN C2340 23.546 30.845 30.340

ATOM 2916 HA ASN C2340 25.947 31.668 28.761

ATOM 2917 HBl ASN C2340 25.860 31.625 31.277

ATOM 2918 HB2 ASN C2340 25.500 33.360 31.278

ATOM 2919 HD22 ASN C2340 22.576 30.628 30.228

ATOM 2920 HD21 ASN C2340 24.208 30.094 30.353

ATOM 2921 H ASN C2340 27.846 33.399 30.336

ATOM 2922 N ASP C2341 24.702 33.644 27.593

ATOM 2923 CA ASP C2341 24.341 34.775 26.724

ATOM 2924 C ASP C2341 23.422 35.702 27.489

ATOM 2925 O ASP C2341 22.415 35.195 27.960

ATOM 2926 CB ASP C2341 23.609 34.309 25.432

ATOM 2927 CG ASP C2341 23.470 35.303 24.308

ATOM 2928 ODl ASP C2341 22.938 34.903 23.236

ATOM 2929 OD2 ASP C2341 23..872 36.484 24.462

ATOM 2930 HA ASP C2341 25. ?59 35.280 26.383

ATOM 2931 HBl ASP C2341 24.116 33.419 25.037

ATOM 2932 HB2 ASP C2341 22.581 34.032 25.678

ATOM 2933 H ASP C2341 24.213 32.777 27.481

ATOM 2934 N PRO C2342 23.683 37.027 27.640

ATOM 2935 CA PRO C2342 22.709 37.901 28.271

ATOM 2936 C PRO C2342 21.295 37.704 27.769

ATOM 2937 O PRO C2342 20.450 37.389 28.593

ATOM 2938 CB PRO C2342 23.309 39.290 27.930

ATOM 2939 CG PRO C2342 24.830 39.036 27.876

ATOM 2940 CD PRO C2342 24.951 37.630 27.250

ATOM 2941 HA PRO C2342 22.758 37.715 29.354

ATOM 2942 HD2 PRO C2342 25.038 37.716 26.158

ATOM 2943 HDl PRO C2342 25.829 37.115 27.670

ATOM 2944 HG2 PRO C2342 25.387 39.790 27.298

ATOM 2945 HGl PRO C2342 25.201 39.025 28.914

ATOM 2946 HBl PRO C2342 22.978 39.650 26.945

ATOM 2947 HB2 PRO C2342 23.062 40.053 28.676

ATOM 2948 N GLU C2343 21.014 37.865 26.451

ATOM 2949 CA GLU C2343 19.662 37.615 25.941

ATOM 2950 C GLU C2343 19.555 36.122 25.739

ATOM 2951 O GLU C2343 20.581 35.515 25.464

ATOM 2952 CB GLU C2343 19.422 38.448 24.649

ATOM 2953 CG GLU C2343 17.928 38.618 24.255

ATOM 2954 CD GLU C2343 17.348 37.386 23.607

ATOM 2955 OEl GLU C2343 16.647 36.608 24.308

ATOM 2956 OE2 GLU C2343 17.581 37.193 22.382

ATOM 2957 HA GLU C2343 18.923 37.949 26.688

ATOM 2958 HBl GLU C2343 19.822 39.458 24.844

ATOM 2959 HB2 GLU C2343 19.990 38.017 23.809

ATOM 2960 HGl GLU C2343 17.329 38.904 25.134

ATOM 2961 HG2 GLU C2343 17.845 39.439 23.523 ATOM 2962 H GLU C2343 21.735 38.089 25.791

ATOM 2963 N THR C2344 18.506 35.389 25.726

ATOM 2964 CA THR C2344 18.119 33.976 25.744

ATOM 2965 C THR C2344 18.816 33.202 26.854

ATOM 2966 O THR C2344 18.442 32.070 27.127

ATOM 2967 CB THR C2344 18.328 33.317 24.348

ATOM 2968 OGl THR C2344 17.753 31.999 24.414

ATOM 2969 CG2 THR C2344 19.809 33.233 23.880

ATOM 2970 HA THR C2344 17.040 33.909 25.959

ATOM 2971 HB THR C2344 17.767 33.911 23.604

ATOM 2972 HGl THR C2344 17.743 31.550 23.574

ATOM 2973 HG23 THR C2344 20.165 34.199 23.492

ATOM 2974 HG21 THR C2344 20.464 32.912 24.701

ATOM 2975 HG22 THR C2344 19.906 32.503 23.061

ATOM 2976 H THR C2344 17.838 36.051 26.047

ATOM 2977 N GLY C2345 19.925 33.504 27.549

ATOM 2978 CA GLY C2345 20.393 32.642 28.631

ATOM 2979 C GLY C2345 21.003 31.324 28.189

ATOM 2980 O GLY C2345 20.778 30.330 28.862

ATOM 2981 HA2 GLY C2345 19.544 32.429 29.302

ATOM 2982 HAl GLY C2345 21.119 33.187 29.244

ATOM 2983 H GLY C2345 20.388 34.380 27.396

ATOM 2984 N ASN C2346 21.783 31.293 27.083

ATOM 2985 CA ASN C2346 22.340 30.047 26.544

ATOM 2986 C ASN C2346 23.848 30.006 26.661

ATOM 2987 O ASN C2346 24.471 31.048 26.786

ATOM 2988 CB ASN C2346 21.917 29.828 25.064

ATOM 2989 CG ASN C2346 20.563 29.160 24.968

ATOM 2990 ODl ASN C2346 20.493 28.029 24.511

ATOM 2991 ND2 ASN C2346 19.467 29.822 25.397

ATOM 2992 HA ASN C2346 21.970 29.179 27.115

ATOM 2993 HBl ASN C2346 21.905 30.786 24.522

ATOM 2994 HB2 ASN C2346 22.649 29.180 24.556

ATOM 2995 HD22 ASN C2346 18.570 29.380 25.346

ATOM 2996 HD21 ASN C2346 19.532 30.747 25.766

ATOM 2997 H ASN C2346 21.978 32.135 26.598

ATOM 2998 N ILE C2347 24.448 28.789 26.631

ATOM 2999 CA ILE C2347 25.869 28.656 26.945

ATOM 3000 C ILE C2347 26.686 29.046 25.730

ATOM 3001 O ILE C2347 26.639 28.333 24.740

ATOM 3002 CB ILE C2347 26.201 27.235 27.496

ATOM 3003 CGl ILE C2347 25.437 26.990 28.838

ATOM 3004 CG2 ILE C2347 27.730 27.113 27.702

ATOM 3005 CDl ILE C2347 25.681 25.590 29.464

ATOM 3006 HA ILE C2347 26.107 29.333 27.781

ATOM 3007 HB ILE C2347 25.891 26.478 26.760

ATOM 3008 HGIl ILE C2347 25.729 27.749 29.583

ATOM 3009 HG12 ILE C2347 24.355 27.095 28.661

ATOM 3010 HDIl ILE C2347 26.716 25.483 29.821

ATOM 3011 HD12 ILE C2347 25.017 25.447 30.331

ATOM 3012 HD13 ILE C2347 25.471 24.798 28.730

ATOM 3013 HG21 ILE C2347 27.988 27.818 28.502

ATOM 3014 HG22 ILE C2347 28.030 26.096 27.993

ATOM 3015 HG23 ILE C2347 28.294 27.371 26.793

ATOM 3016 H ILE C2347 23.931 27.958 26.411

ATOM 3017 N ILE C2348 27.435 30.174 25.809

ATOM 3018 CA ILE C2348 28.235 30.673 24.692

ATOM 3019 C ILE C2348 29.717 30.510 24.976

ATOM 3020 O ILE C2348 30.108 30.290 26.112

ATOM 3021 CB ILE C2348 27.819 32.131 24.322

ATOM 3022 CGl ILE C2348 27.888 33.068 25.557

ATOM 3023 CG2 ILE C2348 26.400 32.159 23.693

ATOM 3024 CDl ILE C2348 28.121 34.559 25.214

ATOM 3025 HA ILE C2348 28.029 30.064 23.798

ATOM 3026 HB ILE C2348 28.518 32.509 23.562

ATOM 3027 HGIl ILE C2348 26.979 32.972 26.170

ATOM 3028 HG12 ILE C2348 28.739 32.745 26.159

ATOM 3029 HDIl ILE C2348 27.294 34.976 24.622 ATOM 3030 HD12 ILE C2348 28.191 35.115 26.159

ATOM 3031 HD13 ILE C2348 29.064 34.690 24.659

ATOM 3032 HG21 ILE C2348 25.673 31.709 24.385

ATOM 3033 HG22 ILE C2348 26.092 33.192 23.468

ATOM 3034 HG23 ILE C2348 26.381 31.587 22.754

ATOM 3035 H ILE C2348 27.465 30.693 26.656

ATOM 3036 N SER C2349 30.539 30.604 23.903

ATOM 3037 CA SER C2349 31.979 30.356 23.995

ATOM 3038 C SER C2349 32.789 31.584 24.317

ATOM 3039 O SER C2349 32.327 32.689 24.095

ATOM 3040 CB SER C2349 32.535 29.792 22.657

ATOM 3041 OG SER C2349 33.974 29.794 22.656

ATOM 3042 HA SER C2349 32.188 29.642 24.803

ATOM 3043 HBl SER C2349 32.156 28.769 22.501

ATOM 3044 HB2 SER C2349 32.191 30.427 21.825

ATOM 3045 HG SER C2349 34.343 29.512 21.825

ATOM 3046 H SER C2349 30.154 30.818 23.007

ATOM 3047 N LEU C2350 34.027 31.355 24.819

ATOM 3048 CA LEU C2350 34.991 32.430 25.069

ATOM 3049 C LEU C2350 35.046 33.385 23.904

ATOM 3050 O LEU C2350 34.981 34.589 24.100

ATOM 3051 CB LEU C2350 36.353 31.692 25.283

ATOM 3052 CG LEU C2350 37.594 32.576 25.515

ATOM 3053 CDl LEU C2350 37.292 33.491 26.698

ATOM 3054 CD2 LEU C2350 38.817 31.709 25.906

ATOM 3055 HA LEU C2350 34.677 32.987 25.963

ATOM 3056 HBl LEU C2350 36.247 31.032 26.159

ATOM 3057 HB2 LEU C2350 36.594 31.063 24.415

ATOM 3058 HG LEU C2350 37.829 33.185 24.624

ATOM 3059 HD21 LEU C2350 38.998 30.919 25.171

ATOM 3060 HD22 LEU C2350 39.723 32.313 26.020

ATOM 3061 HD23 LEU C2350 38.627 31.251 26.873

ATOM 3062 HDIl LEU C2350 36.890 32.909 27.544

ATOM 3063 HD12 LEU C2350 38.252 33.959 26.939

ATOM 3064 HD13 LEU C2350 36.574 34.243 26.365

ATOM 3065 H LEU C2350 34.317 30.415 25.013

ATOM 3066 N PHE C2351 35.103 32.928 22.686

ATOM 3067 CA PHE C2351 35.206 33.701 21.453

ATOM 3068 C PHE C2351 33.925 34.472 21.257

ATOM 3069 O PHE C2351 33.961 35.683 21.114

ATOM 3070 CB PHE C2351 35.464 32.782 20.233

ATOM 3071 CG PHE C2351 35.383 33.525 18.890

ATOM 3072 CDl PHE C2351 34.570 33.047 17.856

ATOM 3073 CD2 PHE C2351 36.128 34.689 18.674

ATOM 3074 CEl PHE C2351 34.603 33.636 16.588

ATOM 3075 CE2 PHE C2351 36.135 35.308 17.422

ATOM 3076 CZ PHE C2351 35.394 34.766 16.368

ATOM 3077 HA PHE C2351 36.056 34.395 21.572

ATOM 3078 HBl PHE C2351 36.474 32.353 20.324

ATOM 3079 HB2 PHE C2351 34.735 31.958 20.260

ATOM 3080 HD2 PHE C2351 36.708 35.120 19.479

ATOM 3081 HE2 PHE C2351 36.718 36.210 17.267

ATOM 3082 HZ PHE C2351 35.423 35.228 15.387

ATOM 3083 HEl PHE C2351 34.009 33.221 15.780

ATOM 3084 HDl PHE C2351 33.905 32.214 18.031

ATOM 3085 H PHE C2351 35.237 31.938 22.679

ATOM 3086 N GLN C2352 32.748 33.862 21.393

ATOM 3087 CA GLN C2352 31.490 34.594 21.243

ATOM 3088 C GLN C2352 31.348 35.637 22.332

ATOM 3089 O GLN C2352 30.841 36.718 22.075

ATOM 3090 CB GLN C2352 30.257 33.658 21.300

ATOM 3091 CG GLN C2352 30.132 32.769 20.035

ATOM 3092 CD GLN C2352 28.972 31.814 20.209

ATOM 3093 OEl GLN C2352 27.837 32.262 20.171

ATOM 3094 NE2 GLN C2352 29.212 30.500 20.410

ATOM 3095 HA GLN C2352 31.491 35.110 20.270

ATOM 3096 HBl GLN C2352 30.360 33.034 22.196

ATOM 3097 HB2 GLN C2352 29.336 34.257 21.398 ATOM 3098 HGl GLN C2352 29.939 33.403 19.154

ATOM 3099 HG2 GLN C2352 31.073 32.228 19.854

ATOM 3100 HE22 GLN C2352 28.447 29.867 20.532

ATOM 3101 HE21 GLN C2352 30.142 30.143 20.440

ATOM 3102 H GLN C2352 32.734 32.873 21.562

ATOM 3103 N ALA C2353 31.797 35.320 23.564

ATOM 3104 CA ALA C2353 31.795 36.303 24.646

ATOM 3105 C ALA C2353 32.685 37.470 24.280

ATOM 3106 O ALA C2353 32.253 38.605 24.421

ATOM 3107 CB ALA C2353 32.212 35.615 25.971

ATOM 3108 HA ALA C2353 30.768 36.681 24.780

ATOM 3109 HBl ALA C2353 32.241 36.321 26.811

ATOM 3110 HB2 ALA C2353 31.479 34.833 26.207

ATOM 3111 HB3 ALA C2353 33.197 35.142 25.870

ATOM 3112 H ALA C2353 32.153 34.404 23.745

ATOM 3113 N MET C2354 33.921 37.219 23.788

ATOM 3114 CA MET C2354 34.768 38.328 23.339

ATOM 3115 C MET C2354 33.967 39.141 22.336

ATOM 3116 O MET C2354 33.882 40.353 22.460

ATOM 3117 CB MET C2354 36.089 37.856 22.663

ATOM 3118 CG MET C2354 37.075 37.206 23.668

ATOM 3119 SD MET C2354 38.283 36.116 22.841

ATOM 3120 CE MET C2354 39.200 37.253 21.761

ATOM 3121 HA MET C2354 35.010 38.953 24.216

ATOM 3122 HBl MET C2354 35.857 37.133 21.868

ATOM 3123 HB2 MET C2354 36.587 38.723 22.197

ATOM 3124 HGl MET C2354 37.585 37.984 24.254

ATOM 3125 HG2 MET C2354 36.543 36.548 24.364

ATOM 3126 HEl MET C2354 39.618 38.062 22.373

ATOM 3127 HE2 MET C2354 40.021 36.704 21.280

ATOM 3128 HE3 MET C2354 38.541 37.668 20.984

ATOM 3129 LPDl MET C2354 37.969 35.636 22.478

ATOM 3130 LPD2 MET C2354 38.697 35.824 23.293

ATOM 3131 H MET C2354 34.251 36.279 23.696

ATOM 3132 N ASN C2355 33.365 38.459 21.333

ATOM 3133 CA ASN C2355 32.606 39.144 20.284

ATOM 3134 C ASN C2355 31.444 39.943 20.821

ATOM 3135 O ASN C2355 31.172 41.001 20.274

ATOM 3136 CB ASN C2355 31.985 38.165 19.253

ATOM 3137 CG ASN C2355 32.996 37.263 18.595

ATOM 3138 ODl ASN C2355 34.189 37.425 18.797

ATOM 3139 ND2 ASN C2355 32.514 36.294 17.787

ATOM 3140 HA ASN C2355 33.286 39.824 19.743

ATOM 3141 HBl ASN C2355 31.225 37.542 19.747

ATOM 3142 HB2 ASN C2355 31.483 38.743 18.460

ATOM 3143 HD22 ASN C2355 33.144 35.679 17.325

ATOM 3144 HD21 ASN C2355 31.532 36.179 17.637

ATOM 3145 H ASN C2355 33.454 37.465 21.275

ATOM 3146 N LYS C2356 30.752 39.463 21.882

ATOM 3147 CA LYS C2356 29.630 40.208 22.460

ATOM 3148 C LYS C2356 30.122 41.084 23.603

ATOM 3149 O LYS C2356 29.415 41.247 24.586

ATOM 3150 CB LYS C2356 28.491 39.212 22.823

ATOM 3151 CG LYS C2356 27.737 38.709 21.562

ATOM 3152 CD LYS C2356 26.736 37.575 21.925

ATOM 3153 CE LYS C2356 25.774 37.264 20.747

ATOM 3154 NZ LYS C2356 24.827 36.179 21.089

ATOM 3155 HA LYS C2356 29.209 40.904 21.717

ATOM 3156 HBl LYS C2356 28.917 38.335 23.327

ATOM 3157 HB2 LYS C2356 27.763 39.689 23.499

ATOM 3158 HGl LYS C2356 27.190 39.557 21.118

ATOM 3159 HG2 LYS C2356 28.458 38.335 20.816

ATOM 3160 HDl LYS C2356 27.298 36.664 22.193

ATOM 3161 HD2 LYS C2356 26.136 37.877 22.799

ATOM 3162 HEl LYS C2356 25.202 38.175 20.500

ATOM 3163 HE2 LYS C2356 26.362 36.978 19.858

ATOM 3164 HZl LYS C2356 24.224 36.439 21.947

ATOM 3165 HZ2 LYS C2356 24.142 35.982 20.275 ATOM 3166 HZ3 LYS C2356 25.339 35.252 21.310

ATOM 3167 H LYS C2356 31.025 38.602 22.312

ATOM 3168 N GLU C2357 31.345 41.664 23.467

ATOM 3169 CA GLU C2357 31.917 42.592 24.447

ATOM 3170 C GLU C2357 31.608 42.240 25.884

ATOM 3171 O GLU C2357 31.400 43.118 26.706

ATOM 3172 CB GLU C2357 31.594 44.054 24.036

ATOM 3173 CG GLU C2357 32.185 44.390 22.637

ATOM 3174 CD GLU C2357 31.979 45.843 22.294

ATOM 3175 OEl GLU C2357 30.823 46.215 21.956

ATOM 3176 OE2 GLU C2357 32.968 46.623 22.354

ATOM 3177 HA GLU C2357 33.017 42.491 24.405

ATOM 3178 HBl GLU C2357 30.501 44.192 24.023

ATOM 3179 HB2 GLU C2357 32.028 44.749 24.773

ATOM 3180 HGl GLU C2357 33.264 44.165 22.624

ATOM 3181 HG2 GLU C2357 31.702 43.782 21.855

ATOM 3182 H GLU C2357 31.902 41.502 22.655

ATOM 3183 N LEU C2358 31.617 40.921 26.173

ATOM 3184 CA LEU C2358 31.546 40.442 27.551

ATOM 3185 C LEU C2358 32.924 40.318 28.146

ATOM 3186 O LEU C2358 33.010 40.240 29.362

ATOM 3187 CB LEU C2358 30.828 39.066 27.610

ATOM 3188 CG LEU C2358 29.276 39.228 27.565

ATOM 3189 CDl LEU C2358 28.626 38.249 26.562

ATOM 3190 CD2 LEU C2358 28.677 38.979 28.972

ATOM 3191 HA LEU C2358 30.985 41.148 28.186

ATOM 3192 HBl LEU C2358 31.181 38.449 26.775

ATOM 3193 HB2 LEU C2358 31.126 38.530 28.526

ATOM 3194 HG LEU C2358 29.006 40.245 27.229

ATOM 3195 HD21 LEU C2358 29.101 39.707 29.676

ATOM 3196 HD22 LEU C2358 27.585 39.069 28.964

ATOM 3197 HD23 LEU C2358 28.917 37.961 29.311

ATOM 3198 HDIl LEU C2358 28.791 37.218 26.897

ATOM 3199 HD12 LEU C2358 27.548 38.438 26.466

ATOM 3200 HD13 LEU C2358 29.085 38.384 25.579

ATOM 3201 H LEU C2358 31.756 40.250 25.441

ATOM 3202 N ILE C2359 33.999 40.292 27.323

ATOM 3203 CA ILE C2359 35.335 40.217 27.890

ATOM 3204 C ILE C2359 36.256 41.070 27.060

ATOM 3205 O ILE C2359 36.142 41.072 25.843

ATOM 3206 CB ILE C2359 35.924 38.755 27.818

ATOM 3207 CGl ILE C2359 34.851 37.644 28.021

ATOM 3208 CG2 ILE C2359 37.025 38.580 28.897

ATOM 3209 CDl ILE C2359 35.356 36.279 27.479

ATOM 3210 HA ILE C2359 35.298 40.631 28.910

ATOM 3211 HB ILE C2359 36.389 38.586 26.826

ATOM 3212 HGIl ILE C2359 34.589 37.543 29.085

ATOM 3213 HG12 ILE C2359 33.922 37.897 27.486

ATOM 3214 HDIl ILE C2359 36.357 35.955 27.809

ATOM 3215 HD12 ILE C2359 34.651 35.491 27.767

ATOM 3216 HD13 ILE C2359 35.356 36.365 26.384

ATOM 3217 HG21 ILE C2359 36.517 38.880 29.819

ATOM 3218 HG22 ILE C2359 37.456 37.575 29.059

ATOM 3219 HG23 ILE C2359 37.851 39.270 28.688

ATOM 3220 H ILE C2359 33.919 40.288 26.326

ATOM 3221 N GLU C2360 37.199 41.763 27.724

ATOM 3222 CA GLU C2360 38.271 42.395 26.981

ATOM 3223 C GLU C2360 38.928 41.392 26.057

ATOM 3224 O GLU C2360 38.871 40.196 26.306

ATOM 3225 CB GLU C2360 39.364 42.998 27.916

ATOM 3226 CG GLU C2360 39.934 42.018 28.982

ATOM 3227 CD GLU C2360 41.180 42.649 29.540

ATOM 3228 OEl GLU C2360 42.295 42.149 29.236

ATOM 3229 OE2 GLU C2360 41.041 43.657 30.280

ATOM 3230 HA GLU C2360 37.834 43.209 26.379

ATOM 3231 HBl GLU C2360 40.196 43.327 27.270

ATOM 3232 HB2 GLU C2360 38.988 43.888 28.431

ATOM 3233 HGl GLU C2360 39.298 41.726 29.839 ATOM 3234 HG2 GLU C2360 40.166 41.107 28.422

ATOM 3235 H GLU C2360 37.193 41.820 28.719

ATOM 3236 N LYS C2361 39.568 41.899 24.978

ATOM 3237 CA LYS C2361 40.289 41.013 24.072

ATOM 3238 C LYS C2361 41.572 40.561 24.726

ATOM 3239 O LYS C2361 41.905 39.401 24.554

ATOM 3240 CB LYS C2361 40.585 41.584 22.648

ATOM 3241 CG LYS C2361 39.413 41.335 21.651

ATOM 3242 CD LYS C2361 39.793 41.491 20.146

ATOM 3243 CE LYS C2361 39.636 42.935 19.599

ATOM 3244 NZ LYS C2361 39.836 42.963 18.130

ATOM 3245 HA LYS C2361 39.692 40.095 23.950

ATOM 3246 HBl LYS C2361 40.837 42.654 22.705

ATOM 3247 HB2 LYS C2361 41.467 41.054 22.253

ATOM 3248 HGl LYS C2361 39.085 40.291 21.762

ATOM 3249 HG2 LYS C2361 38.555 41.973 21.913

ATOM 3250 HDl LYS C2361 40.820 41.136 19.963

ATOM 3251 HD2 LYS C2361 39.118 40.852 19.550

ATOM 3252 HEl LYS C2361 38.619 43.299 19.825

ATOM 3253 HE2 LYS C2361 40.360 43.603 20.096

ATOM 3254 HZl LYS C2361 39.130 42.329 17.608

ATOM 3255 HZ2 LYS C2361 39.704 43.958 17.726

ATOM 3256 HZ3 LYS C2361 40.827 42.633 17.850

ATOM 3257 H LYS C2361 39.593 42.887 24.816

ATOM 3258 N GLY C2362 42.307 41.420 25.470

ATOM 3259 CA GLY C2362 43.548 40.964 26.098

ATOM 3260 C GLY C2362 43.334 39.624 26.757

ATOM 3261 O GLY C2362 43.709 38.616 26.181

ATOM 3262 HA2 GLY C2362 43.903 41.691 26.847

ATOM 3263 HAl GLY C2362 44.331 40.865 25.330

ATOM 3264 H GLY C2362 42.045 42.383 25.565

ATOM 3265 N HIS C2363 42.712 39.605 27.953

ATOM 3266 CA HIS C2363 42.483 38.349 28.662

ATOM 3267 C HIS C2363 41.769 37.303 27.851

ATOM 3268 O HIS C2363 42.065 36.135 28.043

ATOM 3269 CB HIS C2363 41.701 38.597 29.973

ATOM 3270 CG HIS C2363 41.722 37.297 30.711

ATOM 3271 NDl HIS C2363 42.836 36.772 31.157

ATOM 3272 CD2 HIS C2363 40.669 36.507 30.991

ATOM 3273 CEl HIS C2363 42.573 35.648 31.714

ATOM 3274 NE2 HIS C2363 41.339 35.428 31.663

ATOM 3275 HA HIS C2363 43.461 37.932 28.898

ATOM 3276 HBl HIS C2363 42.195 39.362 30.592

ATOM 3277 HB2 HIS C2363 40.670 38.915 29.756

ATOM 3278 HD2 HIS C2363 39.614 36.644 30.764

ATOM 3279 HEl HIS C2363 43.358 35.056 32.142

ATOM 3280 HDl HIS C2363 43.779 37.168 31.075

ATOM 3281 H HIS C2363 42.456 40.463 28.395

ATOM 3282 N GLY C2364 40.844 37.679 26.942

ATOM 3283 CA GLY C2364 40.198 36.647 26.139

ATOM 3284 C GLY C2364 41.261 35.878 25.397

ATOM 3285 O GLY C2364 41.288 34.658 25.437

ATOM 3286 HA2 GLY C2364 39.501 37.082 25.411

ATOM 3287 HAl GLY C2364 39.639 35.986 26.812

ATOM 3288 H GLY C2364 40.598 38.641 26.797

ATOM 3289 N ILE C2365 42.156 36.630 24.720

ATOM 3290 CA ILE C2365 43.240 36.007 23.966

ATOM 3291 C ILE C2365 44.112 35.242 24.939

ATOM 3292 O ILE C2365 44.380 34.076 24.703

ATOM 3293 CB ILE C2365 44.012 37.057 23.109

ATOM 3294 CGl ILE C2365 43.053 37.638 22.022

ATOM 3295 CG2 ILE C2365 45.282 36.430 22.467

ATOM 3296 CDl ILE C2365 43.596 38.900 21.307

ATOM 3297 HA ILE C2365 42.817 35.274 23.268

ATOM 3298 HB ILE C2365 44.344 37.872 23.773

ATOM 3299 HGIl ILE C2365 42.830 36.861 21.276

ATOM 3300 HG12 ILE C2365 42.097 37.933 22.474

ATOM 3301 HDIl ILE C2365 44.484 38.653 20.717 ATOM 3302 HD12 ILE C2365 42.836 39.306 20.621

ATOM 3303 HD13 ILE C2365 43.862 39.677 22.040

ATOM 3304 HG21 ILE C2365 45.005 35.642 21.750

ATOM 3305 HG22 ILE C2365 45.869 37.195 21.941

ATOM 3306 HG23 ILE C2365 45.935 35.990 23.236

ATOM 3307 H ILE C2365 42.109 37.630 24.758

ATOM 3308 N ARG C2366 44.557 35.879 26.045

ATOM 3309 CA ARG C2366 45.472 35.215 26.980

ATOM 3310 C ARG C2366 44.986 33.837 27.367

ATOM 3311 O ARG C2366 45.785 32.920 27.475

ATOM 3312 CB ARG C2366 45.829 36.012 28.267

ATOM 3313 CG ARG C2366 46.465 37.398 27.945

ATOM 3314 CD ARG C2366 47.151 38.041 29.182

ATOM 3315 NE ARG C2366 46.201 38.552 30.178

ATOM 3316 CZ ARG C2366 46.414 38.584 31.478

ATOM 3317 NHl ARG C2366 47.560 38.269 32.034

ATOM 3318 NH2 ARG C2366 45.430 38.954 32.270

ATOM 3319 HA ARG C2366 46.440 35.102 26.464

ATOM 3320 HBl ARG C2366 44.946 36.116 28.910

ATOM 3321 HB2 ARG C2366 46.566 35.410 28.822

ATOM 3322 HGl ARG C2366 47.231 37.257 27.165

ATOM 3323 HG2 ARG C2366 45.732 38.106 27.538

ATOM 3324 HDl ARG C2366 47.841 37.270 29.552

ATOM 3325 HD2 ARG C2366 47.736 38.892 28.816

ATOM 3326 HE ARG C2366 45.297 38.883 29.821

ATOM 3327 HHl 2 ARG C2366 47.663 38.276 33.052

ATOM 3328 HHIl ARG C2366 48.394 38.036 31.486

ATOM 3329 HH22 ARG C2366 45.550 38.995 33.292

ATOM 3330 HH21 ARG C2366 44.508 39.210 31.892

ATOM 3331 H ARG C2366 44.294 36.828 26.200

ATOM 3332 N LEU C2367 43.665 33.676 27.581

ATOM 3333 CA LEU C2367 43.143 32.359 27.917

ATOM 3334 C LEU C2367 43.150 31.493 26.676

ATOM 3335 O LEU C2367 43.636 30.377 26.757

ATOM 3336 CB LEU C2367 41.703 32.384 28.478

ATOM 3337 CG LEU C2367 41.585 33.123 29.834

ATOM 3338 CDl LEU C2367 40.153 32.941 30.416

ATOM 3339 CD2 LEU C2367 42.692 32.693 30.832

ATOM 3340 HA LEU C2367 43.805 31.878 28.655

ATOM 3341 HBl LEU C2367 41.045 32.886 27.761

ATOM 3342 HB2 LEU C2367 41.361 31.346 28.584

ATOM 3343 HG LEU C2367 41.726 34.193 29.628

ATOM 3344 HD21 LEU C2367 43.627 33.246 30.646

ATOM 3345 HD22 LEU C2367 42.332 32.888 31.846

ATOM 3346 HD23 LEU C2367 42.947 31.634 30.773

ATOM 3347 HDIl LEU C2367 39.931 31.883 30.585

ATOM 3348 HD12 LEU C2367 40.024 33.450 31.381

ATOM 3349 HDl 3 LEU C2367 39.410 33.350 29.713

ATOM 3350 H LEU C2367 43.030 34.444 27.478

ATOM 3351 N LEU C2368 42.633 31.986 25.524

ATOM 3352 CA LEU C2368 42.590 31.160 24.312

ATOM 3353 C LEU C2368 43.926 30.487 24.080

ATOM 3354 O LEU C2368 43.978 29.288 23.864

ATOM 3355 CB LEU C2368 42.209 31.957 23.027

ATOM 3356 CG LEU C2368 40.688 32.287 22.921

ATOM 3357 CDl LEU C2368 40.420 33.476 21.965

ATOM 3358 CD2 LEU C2368 39.856 31.059 22.450

ATOM 3359 HA LEU C2368 41.828 30.385 24.459

ATOM 3360 HBl LEU C2368 42.799 32.883 23.013

ATOM 3361 HB2 LEU C2368 42.492 31.378 22.133

ATOM 3362 HG LEU C2368 40.333 32.628 23.897

ATOM 3363 HD21 LEU C2368 39.970 30.192 23.113

ATOM 3364 HD22 LEU C2368 38.785 31.311 22.403

ATOM 3365 HD23 LEU C2368 40.188 30.761 21.448

ATOM 3366 HDIl LEU C2368 40.894 33.265 21.006

ATOM 3367 HD12 LEU C2368 39.340 33.623 21.808

ATOM 3368 HD13 LEU C2368 40.839 34.410 22.361

ATOM 3369 H LEU C2368 42.250 32.911 25.489 ATOM 3370 N GLU C2369 45.024 31.271 24.122

ATOM 3371 CA GLU C2369 46.345 30.701 23.844

ATOM 3372 C GLU C2369 46.681 29.559 24.774

ATOM 3373 O GLU C2369 47.198 28.557 24.304

ATOM 3374 CB GLU C2369 47.535 31.699 23.758

ATOM 3375 CG GLU C2369 47.615 32.733 24.903

ATOM 3376 CD GLU C2369 48.701 33.745 24.651

ATOM 3377 OEl GLU C2369 48.453 34.730 23.905

ATOM 3378 OE2 GLU C2369 49.812 33.569 25.204

ATOM 3379 HA GLU C2369 46.264 30.271 22.835

ATOM 3380 HBl GLU C2369 48.487 31.144 23.705

ATOM 3381 HB2 GLU C2369 47.422 32.261 22.828

ATOM 3382 HGl GLU C2369 46.699 33.321 24.967

ATOM 3383 HG2 GLU C2369 47.759 32.200 25.852

ATOM 3384 H GLU C2369 44.909 32.245 24.293

ATOM 3385 N ALA C2370 46.403 29.659 26.091

ATOM 3386 CA ALA C2370 46.680 28.521 26.970

ATOM 3387 C ALA C2370 45.940 27.300 26.468

ATOM 3388 O ALA C2370 46.472 26.202 26.527

ATOM 3389 CB ALA C2370 46.274 28.823 28.433

ATOM 3390 HA ALA C2370 47.761 28.312 26.942

ATOM 3391 HBl ALA C2370 46.526 27.961 29.066

ATOM 3392 HB2 ALA C2370 46.820 29.707 28.800

ATOM 3393 HB3 ALA C2370 45.193 29.015 28.507

ATOM 3394 H ALA C2370 45.978 30.483 26.472

ATOM 3395 N GLN C2371 44.708 27.489 25.950

ATOM 3396 CA GLN C2371 43.965 26.367 25.381

ATOM 3397 C GLN C2371 44.700 25.862 24.154

ATOM 3398 O GLN C2371 44.927 24.668 24.036

ATOM 3399 CB GLN C2371 42.490 26.720 25.047

ATOM 3400 CG GLN C2371 41.739 27.484 26.169

ATOM 3401 CD GLN C2371 40.258 27.571 25.885

ATOM 3402 OEl GLN C2371 39.859 27.624 24.733

ATOM 3403 NE2 GLN C2371 39.409 27.597 26.931

ATOM 3404 HA GLN C2371 43.916 25.554 26.122

ATOM 3405 HBl GLN C2371 42.452 27.309 24.119

ATOM 3406 HB2 GLN C2371 41.950 25.772 24.905

ATOM 3407 HGl GLN C2371 41.931 26.985 27.132

ATOM 3408 HG2 GLN C2371 42.077 28.524 26.244

ATOM 3409 HE22 GLN C2371 38.423 27.654 26.765

ATOM 3410 HE21 GLN C2371 39.755 27.555 27.871

ATOM 3411 H GLN C2371 44.321 28.408 25.909

ATOM 3412 N ILE C2372 45.084 26.776 23.232

ATOM 3413 CA ILE C2372 45.748 26.376 21.986

ATOM 3414 C ILE C2372 46.979 25.546 22.307

ATOM 3415 O ILE C2372 47.107 24.435 21.816

ATOM 3416 CB ILE C2372 46.080 27.609 21.087

ATOM 3417 CGl ILE C2372 44.809 28.346 20.551

ATOM 3418 CG2 ILE C2372 47.073 27.269 19.941

ATOM 3419 CDl ILE C2372 44.028 27.611 19.429

ATOM 3420 HA ILE C2372 45.052 25.746 21.422

ATOM 3421 HB ILE C2372 46.622 28.319 21.725

ATOM 3422 HGIl ILE C2372 44.104 28.547 21.371

ATOM 3423 HG12 ILE C2372 45.114 29.323 20.144

ATOM 3424 HDIl ILE C2372 43.631 26.647 19.775

ATOM 3425 HD12 ILE C2372 43.177 28.234 19.114

ATOM 3426 HD13 ILE C2372 44.659 27.444 18.544

ATOM 3427 HG21 ILE C2372 46.694 26.440 19.327

ATOM 3428 HG22 ILE C2372 47.225 28.152 19.299

ATOM 3429 HG23 ILE C2372 48.053 26.977 20.348

ATOM 3430 H ILE C2372 44.904 27.744 23.399

ATOM 3431 N ALA C2373 47.894 26.078 23.145

ATOM 3432 CA ALA C2373 49.106 25.344 23.511

ATOM 3433 C ALA C2373 48.842 24.033 24.205

ATOM 3434 O ALA C2373 49.756 23.224 24.218

ATOM 3435 CB ALA C2373 49.931 26.190 24.515

ATOM 3436 HA ALA C2373 49.694 25.153 22.597

ATOM 3437 HBl ALA C2373 50.858 25.672 24.807 ATOM 3438 HB2 ALA C2373 50.193 27.165 24.079

ATOM 3439 HB3 ALA C2373 49.317 26.359 25.413

ATOM 3440 H ALA C2373 47.763 26.998 23.515

ATOM 3441 N THR C2374 47.643 23.788 24.803

ATOM 3442 CA THR C2374 47.436 22.492 25.446

ATOM 3443 C THR C2374 46.362 21.732 24.706

ATOM 3444 O THR C2374 45.544 21.062 25.319

ATOM 3445 CB THR C2374 47.090 22.752 26.942

ATOM 3446 OGl THR C2374 45.967 23.649 26.982

ATOM 3447 CG2 THR C2374 48.289 23.366 27.720

ATOM 3448 HA THR C2374 48.339 21.868 25.378

ATOM 3449 HB THR C2374 46.802 21.807 27.432

ATOM 3450 HGl THR C2374 45.701 23.851 27.872

ATOM 3451 HG23 THR C2374 49.045 22.596 27.920

ATOM 3452 HG21 THR C2374 48.749 24.187 27.150

ATOM 3453 HG22 THR C2374 47.964 23.765 28.692

ATOM 3454 H THR C2374 46.894 24.456 24.813

ATOM 3455 N GLY C2375 46.568 21.737 23.276

ATOM 3456 CA GLY C2375 45.821 20.861 22.376

ATOM 3457 C GLY C2375 44.569 21.466 21.789

ATOM 3458 O GLY C2375 43.796 20.695 21.241

ATOM 3459 HA2 GLY C2375 45.554 19.932 22.905

ATOM 3460 HAl GLY C2375 46.465 20.587 21.523

ATOM 3461 H GLY C2375 47.248 22.353 22.869

ATOM 3462 N GLY C2376 44.363 22.804 21.859

ATOM 3463 CA GLY C2376 43.283 23.441 21.103

ATOM 3464 C GLY C2376 42.318 24.171 21.998

ATOM 3465 O GLY C2376 42.429 24.064 23.208

ATOM 3466 HA2 GLY C2376 42.687 22.712 20.533

ATOM 3467 HAl GLY C2376 43.710 24.146 20.371

ATOM 3468 H GLY C2376 44.976 23.390 22.391

ATOM 3469 N ILE C2377 41.354 24.900 21.386

ATOM 3470 CA ILE C2377 40.294 25.559 22.155

ATOM 3471 C ILE C2377 39.370 24.530 22.752

ATOM 3472 O ILE C2377 39.382 23.418 22.251

ATOM 3473 CB ILE C2377 39.478 26.616 21.346

ATOM 3474 CGl ILE C2377 38.656 26.004 20.169

ATOM 3475 CG2 ILE C2377 40.423 27.738 20.826

ATOM 3476 CDl ILE C2377 37.257 25.467 20.570

ATOM 3477 HA ILE C2377 40.774 26.104 22.971

ATOM 3478 HB ILE C2377 38.768 27.116 22.028

ATOM 3479 HGIl ILE C2377 38.476 26.798 19.430

ATOM 3480 HG12 ILE C2377 39.204 25.198 19.660

ATOM 3481 HDIl ILE C2377 36.678 26.234 21.105

ATOM 3482 HD12 ILE C2377 36.723 25.218 19.644

ATOM 3483 HD13 ILE C2377 37.304 24.561 21.189

ATOM 3484 HG21 ILE C2377 41.115 27.341 20.074

ATOM 3485 HG22 ILE C2377 39.839 28.544 20.356

ATOM 3486 HG23 ILE C2377 41.007 28.177 21.649

ATOM 3487 H ILE C2377 41.355 24.969 20.390

ATOM 3488 N ILE C2378 38.574 24.883 23.795

ATOM 3489 CA ILE C2378 37.670 23.918 24.427

ATOM 3490 C ILE C2378 36.245 24.156 23.983

ATOM 3491 O ILE C2378 35.802 25.290 24.050

ATOM 3492 CB ILE C2378 37.776 23.995 25.974

ATOM 3493 CGl ILE C2378 39.206 23.526 26.370

ATOM 3494 CG2 ILE C2378 36.681 23.107 26.636

ATOM 3495 CDl ILE C2378 39.750 24.137 27.673

ATOM 3496 HA ILE C2378 37.975 22.898 24.156

ATOM 3497 HB ILE C2378 37.620 25.041 26.286

ATOM 3498 HGIl ILE C2378 39.190 22.437 26.507

ATOM 3499 HG12 ILE C2378 39.937 23.783 25.587

ATOM 3500 HDIl ILE C2378 39.072 23.932 28.504

ATOM 3501 HD12 ILE C2378 40.728 23.679 27.879

ATOM 3502 HD13 ILE C2378 39.878 25.219 27.566

ATOM 3503 HG21 ILE C2378 36.746 22.070 26.269

ATOM 3504 HG22 ILE C2378 36.804 23.092 27.724

ATOM 3505 HG23 ILE C2378 35.671 23.489 26.422 ATOM 3506 H ILE C2378 38.585 25.814 24.165

ATOM 3507 N ASP C2379 35.523 23.092 23.554

ATOM 3508 CA ASP C2379 34.106 23.223 23.203

ATOM 3509 C ASP C2379 33.307 23.364 24.486

ATOM 3510 O ASP C2379 33.324 22.395 oc 99 R

ATOM 3511 CB ASP C2379 33.666 21.945 22.432

ATOM 3512 CG ASP C2379 32.275 22.012 21.867

ATOM 3513 ODl ASP C2379 32.048 21.441 20.765

ATOM 3514 OD2 ASP C2379 31.392 22.630 22.519

ATOM 3515 HA ASP C2379 33.974 24.075 22.521

ATOM 3516 HBl ASP C2379 34.363 21.788 21.601

ATOM 3517 HB2 ASP C2379 33.724 21.060 23.080

ATOM 3518 H ASP C2379 35.937 22.181 23.507

ATOM 3519 N PRO C2380 32.603 24.470 24.848

ATOM 3520 CA PRO C2380 31.835 24.462 26.087

ATOM 3521 C PRO C2380 30.800 23.363 26.133

ATOM 3522 O PRO C2380 30.625 22.754 27.177

ATOM 3523 CB PRO C2380 31.120 25.832 26.029

ATOM 3524 CG PRO C2380 32.021 26.676 25.105

ATOM 3525 CD PRO C2380 32.541 25.680 24.043

ATOM 3526 HA PRO C2380 32.525 24.388 26.939

ATOM 3527 HD2 PRO C2380 31.809 25.549 23.234

ATOM 3528 HDl PRO C2380 33.497 26.036 23.633

ATOM 3529 HG2 PRO C2380 31.457 27.503 24.653

ATOM 3530 HGl PRO C2380 32.865 27.075 25.695

ATOM 3531 HBl PRO C2380 30.130 25.744 25.551

ATOM 3532 HB2 PRO C2380 30.986 26.276 27.027

ATOM 3533 N LYS C2381 30.097 23.120 25.003

ATOM 3534 CA LYS C2381 29.026 22.125 25.004

ATOM 3535 C LYS C2381 29.562 20.725 25.168

ATOM 3536 O LYS C2381 29.251 20.047 26.135

ATOM 3537 CB LYS C2381 28.145 22.190 23.719

ATOM 3538 CG LYS C2381 27.159 23.393 23.698

ATOM 3539 CD LYS C2381 26.009 23.216 24.729

ATOM 3540 CE LYS C2381 24.904 24.294 24.595

ATOM 3541 NZ LYS C2381 23.845 24.059 25.604

ATOM 3542 HA LYS C2381 28.397 22.296 25.884

ATOM 3543 HBl LYS C2381 28.795 22.250 22.832

ATOM 3544 HB2 LYS C2381 27.558 21.261 23.626

ATOM 3545 HGl LYS C2381 27.705 24.332 23.886

ATOM 3546 HG2 LYS C2381 26.712 23.454 22.691

ATOM 3547 HDl LYS C2381 25.543 22.226 24.599

ATOM 3548 HD2 LYS C2381 26.398 23.286 25.755

ATOM 3549 HEl LYS C2381 25.350 25.292 24.732

ATOM 3550 HE2 LYS C2381 24.467 24.254 23.584

ATOM 3551 HZl LYS C2381 24.239 24.006 26.610

ATOM 3552 HZ2 LYS C2381 23.107 24.850 25.601

ATOM 3553 HZ3 LYS C2381 23.326 23.129 25.417

ATOM 3554 H LYS C2381 30.285 23.637 24.165

ATOM 3555 N GLU C2382 30.363 20.287 24.178

ATOM 3556 CA GLU C2382 30.797 18.895 24.127

ATOM 3557 C GLU C2382 31.889 18.657 25.165

ATOM 3558 O GLU C2382 32.081 17.520 25.568

ATOM 3559 CB GLU C2382 31.220 18.544 22.672

ATOM 3560 CG GLU C2382 30.163 18.883 21.576

ATOM 3561 CD GLU C2382 28.822 18.213 21.722

ATOM 3562 OEl GLU C2382 28.745 17.127 22.355

ATOM 3563 OE2 GLU C2382 27.825 18.770 21.183

ATOM 3564 HA GLU C2382 29.948 18.250 24.406

ATOM 3565 HBl GLU C2382 32.116 19.134 22.437

ATOM 3566 HB2 GLU C2382 31.477 17.474 22.620

ATOM 3567 HGl GLU C2382 29.994 19.968 21.508

ATOM 3568 HG2 GLU C2382 30.561 18.559 20.603

ATOM 3569 H GLU C2382 30.677 20.924 23.479

ATOM 3570 N SER C2383 32.585 19.724 25.632

ATOM 3571 CA SER C2383 33.529 19.637 26.756

ATOM 3572 C SER C2383 34.796 18.871 26.428

ATOM 3573 O SER C2383 35.151 17.935 27.130 ATOM 3574 CB SER C2383 32.824 19.165 28.052

ATOM 3575 OG SER C2383 33.670 19.470 29.176

ATOM 3576 HA SER C2383 33.861 20.667 26.981

ATOM 3577 HBl SER C2383 31.867 19.706 28.151

ATOM 3578 HB2 SER C2383 32.617 18.084 28.013

ATOM 3579 HG SER C2383 33.272 19.242 30.010

ATOM 3580 H SER C2383 32.432 20.634 25.246

ATOM 3581 N HIS C2384 35.491 19.307 25.348

ATOM 3582 CA HIS C2384 36.736 18.664 24.916

ATOM 3583 C HIS C2384 37.433 19.546 23.897

ATOM 3584 O HIS C2384 36.852 20.554 23.524

ATOM 3585 CB HIS C2384 36.471 17.237 24.356

ATOM 3586 CG HIS C2384 35.840 17.224 22.986

ATOM 3587 NDl HIS C2384 34.737 17.864 22.674

ATOM 3588 CD2 HIS C2384 36.304 16.559 21.908

ATOM 3589 CEl HIS C2384 34.450 17.660 21.427

ATOM 3590 NE2 HIS C2384 35.318 16.909 20.922

ATOM 3591 HA HIS C2384 37.400 18.575 25.793

ATOM 3592 HBl HIS C2384 37.422 16.685 24.304

ATOM 3593 HB2 HIS C2384 35.809 16.680 25.035

ATOM 3594 HD2 HIS C2384 37.183 15.924 21.804

ATOM 3595 HEl HIS C2384 33.600 18.060 20.876

ATOM 3596 HDl HIS C2384 34.184 18.437 23.323

ATOM 3597 H HIS C2384 35.156 20.093 24.825

ATOM 3598 N ARG C2385 38.666 19.224 23.435

ATOM 3599 CA ARG C2385 39.373 20.156 22.553

ATOM 3600 C ARG C2385 38.923 19.985 21.127

ATOM 3601 O ARG C2385 38.603 18.857 20.786

ATOM 3602 CB ARG C2385 40.927 20.059 22.550

ATOM 3603 CG ARG C2385 41.574 19.997 23.961

ATOM 3604 CD ARG C2385 41.066 21.151 24.854

ATOM 3605 NE ARG C2385 41.674 21.086 26.183

ATOM 3606 CZ ARG C2385 42.759 21.737 26.550

ATOM 3607 NHl ARG C2385 43.461 22.512 25.753

ATOM 3608 NH2 ARG C2385 43.167 21.596 27.791

ATOM 3609 HA ARG C2385 39.119 21.174 22.861

ATOM 3610 HBl ARG C2385 41.237 19.171 21.983

ATOM 3611 HB2 ARG C2385 41.324 20.941 22.020

ATOM 3612 HGl ARG C2385 41.333 19.040 24.451

ATOM 3613 HG2 ARG C2385 42.671 20.060 23.870

ATOM 3614 HDl ARG C2385 41.150 22.121 24.347

ATOM 3615 HD2 ARG C2385 39.991 20.973 24.991

ATOM 3616 HE ARG C2385 41.186 20.497 26.880

ATOM 3617 HHl 2 ARG C2385 44.295 23.002 26.101

ATOM 3618 HHIl ARG C2385 43.224 22.644 24.765

ATOM 3619 HH22 ARG C2385 44.027 22.050 28.121

ATOM 3620 HH21 ARG C2385 42.649 21.012 28.466

ATOM 3621 H ARG C2385 39.104 18.358 23.674

ATOM 3622 N LEU C2386 38.912 21.067 20.302

ATOM 3623 CA LEU C2386 38.577 20.904 18.887

ATOM 3624 C LEU C2386 39.744 21.227 17.979

ATOM 3625 O LEU C2386 40.479 22.141 18.319

ATOM 3626 CB LEU C2386 37.413 21.813 18.432

ATOM 3627 CG LEU C2386 36.060 21.466 19.112

ATOM 3628 CDl LEU C2386 35.017 22.511 18.647

ATOM 3629 CD2 LEU C2386 35.512 20.049 18.771

ATOM 3630 HA LEU C2386 38.217 19.890 18.720

ATOM 3631 HBl LEU C2386 37.702 22.848 18.676

ATOM 3632 HB2 LEU C2386 37.287 21.745 17.339

ATOM 3633 HG LEU C2386 36.212 21.541 20.201

ATOM 3634 HD21 LEU C2386 36.097 19.250 19.246

ATOM 3635 HD22 LEU C2386 34.480 19.951 19.140

ATOM 3636 HD23 LEU C2386 35.506 19.889 17.682

ATOM 3637 HDIl LEU C2386 34.817 22.386 17.576

ATOM 3638 HD12 LEU C2386 34.078 22.416 19.211

ATOM 3639 HDl 3 LEU C2386 35.410 23.519 18.789

ATOM 3640 H LEU C2386 39.150 21.988 20.628

ATOM 3641 N PRO C2387 39.938 20.555 16.813 ATOM 3642 CA PRO C2387 40.898 21.049 15.839

ATOM 3643 C PRO C2387 40.581 22.448 15.361

ATOM 3644 O PRO C2387 39.458 22.902 15.512

ATOM 3645 CB PRO C2387 40.717 20.063 14.659

ATOM 3646 CG PRO C2387 40.136 18.794 15.317

ATOM 3647 CD PRO C2387 39.234 19.327 16.458

ATOM 3648 HA PRO C2387 41.914 20.999 16.268

ATOM 3649 HD2 PRO C2387 38.218 19.552 16.098

ATOM 3650 HDl PRO C2387 39.204 18.562 17.250

ATOM 3651 HG2 PRO C2387 39.589 18.154 14.605

ATOM 3652 HGl PRO C2387 40.972 18.214 15.745

ATOM 3653 HBl PRO C2387 39.970 20.454 13.952

ATOM 3654 HB2 PRO C2387 41.654 19.880 14.110

ATOM 3655 N VAL C2388 41.586 23.138 14.780

ATOM 3656 CA VAL C2388 41.416 24.550 14.416

ATOM 3657 C VAL C2388 40.327 24.741 13.371

ATOM 3658 O VAL C2388 39.541 25.671 13.474

ATOM 3659 CB VAL C2388 42.795 25.183 14.031

ATOM 3660 CGl VAL C2388 43.200 24.889 12.561

ATOM 3661 CG2 VAL C2388 42.830 26.709 14.318

ATOM 3662 HA VAL C2388 41.094 25.082 15.325

ATOM 3663 HB VAL C2388 43.573 24.750 14.685

ATOM 3664 HGIl VAL C2388 42.484 25.347 11.861

ATOM 3665 HGl 2 VAL C2388 44.199 25.300 12.348

ATOM 3666 HGl 3 VAL C2388 43.239 23.804 12.382

ATOM 3667 HG21 VAL C2388 42.714 26.906 15.395

ATOM 3668 HG22 VAL C2388 43.785 27.151 13.994

ATOM 3669 HG23 VAL C2388 42.009 27.201 13.785

ATOM 3670 H VAL C2388 42.474 22.693 14.640

ATOM 3671 N ASP C2389 40.264 23.857 12.348

ATOM 3672 CA ASP C2389 39.235 23.955 11.309

ATOM 3673 C ASP C2389 37.842 23.786 11.874

ATOM 3674 O ASP C2389 36.969 24.585 11.574

ATOM 3675 CB ASP C2389 39.466 22.913 10.177

ATOM 3676 CG ASP C2389 39.642 21.514 10.712

ATOM 3677 ODl ASP C2389 40.674 21.272 11.397

ATOM 3678 OD2 ASP C2389 38.764 20.646 10.459

ATOM 3679 HA ASP C2389 39.298 24.953 10.853

ATOM 3680 HBl ASP C2389 38.624 22.945 9.465

ATOM 3681 HB2 ASP C2389 40.384 23.176 9.627

ATOM 3682 H ASP C2389 40.929 23.113 12.288

ATOM 3683 N ILE C2390 37.619 22.735 12.693

ATOM 3684 CA ILE C2390 36.285 22.500 13.251

ATOM 3685 C ILE C2390 35.931 23.688 14.123

ATOM 3686 O ILE C2390 34.817 24.182 14.065

ATOM 3687 CB ILE C2390 36.224 21.155 14.039

ATOM 3688 CGl ILE C2390 36.693 19.904 13.222

ATOM 3689 CG2 ILE C2390 34.800 20.929 14.612

ATOM 3690 CDl ILE C2390 35.985 19.704 11.856

ATOM 3691 HA ILE C2390 35.546 22.452 12.435

ATOM 3692 HB ILE C2390 36.911 21.254 14.896

ATOM 3693 HGIl ILE C2390 37.773 19.948 13.023

ATOM 3694 HG12 ILE C2390 36.530 19.000 13.831

ATOM 3695 HDIl ILE C2390 36.188 20.546 11.178

ATOM 3696 HD12 ILE C2390 36.362 18.787 11.374

ATOM 3697 HD13 ILE C2390 34.898 19.599 11.982

ATOM 3698 HG21 ILE C2390 34.055 20.895 13.805

ATOM 3699 HG22 ILE C2390 34.750 19.988 15.180

ATOM 3700 HG23 ILE C2390 34.530 21.747 15.292

ATOM 3701 H ILE C2390 38.376 22.141 12.962

ATOM 3702 N ALA C2391 36.892 24.172 14.940

ATOM 3703 CA ALA C2391 36.632 25.338 15.781

ATOM 3704 C ALA C2391 36.173 26.520 14.953

ATOM 3705 O ALA C2391 35.209 27.166 15.334

ATOM 3706 CB ALA C2391 37.880 25.765 16.590

ATOM 3707 HA ALA C2391 35.835 25.072 16.497

ATOM 3708 HBl ALA C2391 37.627 26.641 17.204

ATOM 3709 HB2 ALA C2391 38.207 24.946 17.248 ATOM 3710 HB3 ALA C2391 38.711 26.033 15.922

ATOM 3711 H ALA C2391 37.791 23.736 14.992

ATOM 3712 N TYR C2392 36.835 26.817 13.809

ATOM 3713 CA TYR C2392 36.324 27.868 12.927

ATOM 3714 C TYR C2392 34.892 27.539 12.538

ATOM 3715 O TYR C2392 34.026 28.400 12.556

ATOM 3716 CB TYR C2392 37.133 28.006 11.606

ATOM 3717 CG TYR C2392 38.651 28.222 11.744

ATOM 3718 CDl TYR C2392 39.227 28.916 12.815

ATOM 3719 CD2 TYR C2392 39.495 27.721 10.745

ATOM 3720 CEl TYR C2392 40.575 29.281 12.779

ATOM 3721 CE2 TYR C2392 40.873 27.934 10.800

ATOM 3722 CZ TYR C2392 41.413 28.770 11.777

ATOM 3723 OH TYR C2392 42.775 29.072 11.741

ATOM 3724 HA TYR C2392 36.337 28.827 13.465

ATOM 3725 HB2 TYR C2392 36.963 27.102 11.003

ATOM 3726 HBl TYR C2392 36.741 28.864 11.037

ATOM 3727 HD2 TYR C2392 39.084 27.167 9.908

ATOM 3728 HE2 TYR C2392 41.529 27.457 10.077

ATOM 3729 HEl TYR C2392 40.969 29.955 13.532

ATOM 3730 HDl TYR C2392 38.639 29.185 13.683

ATOM 3731 HH TYR C2392 43.016 29.799 12.301

ATOM 3732 H TYR C2392 37.647 26.304 13.527

ATOM 3733 N LYS C2393 34.664 26.260 12.166

ATOM 3734 CA LYS C2393 33.375 25.828 11.615

ATOM 3735 C LYS C2393 32.275 25.974 12.647

ATOM 3736 O LYS C2393 31.167 26.312 12.260

ATOM 3737 CB LYS C2393 33.529 24.357 11.115

ATOM 3738 CG LYS C2393 32.567 23.913 9.981

ATOM 3739 CD LYS C2393 32.844 22.446 9.519

ATOM 3740 CE LYS C2393 34.192 22.182 8.775

ATOM 3741 NZ LYS C2393 34.257 22.783 7.422

ATOM 3742 HA LYS C2393 33.145 26.481 10.756

ATOM 3743 HBl LYS C2393 34.534 24.255 10.688

ATOM 3744 HB2 LYS C2393 33.435 23.672 11.971

ATOM 3745 HGl LYS C2393 31.536 23.980 10.368

ATOM 3746 HG2 LYS C2393 32.649 24.599 9.124

ATOM 3747 HDl LYS C2393 32.808 21.796 10.409

ATOM 3748 HD2 LYS C2393 32.030 22.134 8.844

ATOM 3749 HEl LYS C2393 35.058 22.511 9.370

ATOM 3750 HE2 LYS C2393 34.301 21.089 8.655

ATOM 3751 HZl LYS C2393 34.167 23.859 7.433

ATOM 3752 HZ2 LYS C2393 35.202 22.566 6.939

ATOM 3753 HZ3 LYS C2393 33.484 22.391 6.775

ATOM 3754 H LYS C2393 35.413 25.600 12.240

ATOM 3755 N ARG C2394 32.560 25.752 13.958

ATOM 3756 CA ARG C2394 31.552 25.946 15.007

ATOM 3757 C ARG C2394 31.565 27.371 15.530

ATOM 3758 O ARG C2394 30.996 27.610 16.584

ATOM 3759 CB ARG C2394 31.726 24.923 16.163

ATOM 3760 CG ARG C2394 31.690 23.472 15.610

ATOM 3761 CD ARG C2394 31.647 22.405 16.736

ATOM 3762 NE ARG C2394 31.852 21.060 16.191

ATOM 3763 CZ ARG C2394 31.981 19.982 16.933

ATOM 3764 NHl ARG C2394 31.893 20.004 18.243

ATOM 3765 NH2 ARG C2394 32.205 18.830 16.342

ATOM 3766 HA ARG C2394 30.546 25.760 14.591

ATOM 3767 HBl ARG C2394 32.686 25.107 16.675

ATOM 3768 HB2 ARG C2394 30.914 25.047 16.899

ATOM 3769 HGl ARG C2394 30.808 23.329 14.965

ATOM 3770 HG2 ARG C2394 32.589 23.310 14.997

ATOM 3771 HDl ARG C2394 32.440 22.653 17.452

ATOM 3772 HD2 ARG C2394 30.672 22.460 17.247

ATOM 3773 HE ARG C2394 31.909 20.969 15.164

ATOM 3774 HHl 2 ARG C2394 32.008 19.138 18.789

ATOM 3775 HHIl ARG C2394 31.702 20.870 18.761

ATOM 3776 HH22 ARG C2394 32.307 17.961 16.889

ATOM 3777 HH21 ARG C2394 32.287 18.762 15.316 ATOM 3778 H ARG C2394 33.485 25.500 14.244

ATOM 3779 N GLY C2395 32.195 28.340 14.823

ATOM 3780 CA GLY C2395 32.218 29.718 15.301

ATOM 3781 C GLY C2395 32.725 29.829 16.718

ATOM 3782 O GLY C2395 32.156 30.598 17.476

ATOM 3783 HA2 GLY C2395 31.197 30.128 15.230

ATOM 3784 HAl GLY C2395 32.876 30.333 14.663

ATOM 3785 H GLY C2395 32.634 28.156 13.946

ATOM 3786 N TYR C2396 33.798 29.080 17.069

ATOM 3787 CA TYR C2396 34.456 29.246 18.370

ATOM 3788 C TYR C2396 35.842 29.853 18.266

ATOM 3789 O TYR C2396 36.459 30.065 19.302

ATOM 3790 CB TYR C2396 34.603 27.864 19.059

ATOM 3791 CG TYR C2396 33.309 27.171 19.524

ATOM 3792 CDl TYR C2396 33.381 25.802 19.780

ATOM 3793 CD2 TYR C2396 32.080 27.813 19.729

ATOM 3794 CEl TYR C2396 32.272 25.085 20.236

ATOM 3795 CE2 TYR C2396 31.012 27.130 20.319

ATOM 3796 CZ TYR C2396 31.105 25.761 20.589

ATOM 3797 OH TYR C2396 30.038 25.099 21.204

ATOM 3798 HA TYR C2396 33.891 29.901 19.051

ATOM 3799 HB2 TYR C2396 35.146 27.204 18.364

ATOM 3800 HBl TYR C2396 35.211 27.970 19.969

ATOM 3801 HD2 TYR C2396 31.935 28.844 19.445

ATOM 3802 HE2 TYR C2396 30.099 27.656 20.574

ATOM 3803 HEl TYR C2396 32.336 24.010 20.309

ATOM 3804 HDl TYR C2396 34.311 25.283 19.634

ATOM 3805 HH TYR C2396 30.259 24.225 21.508

ATOM 3806 H TYR C2396 34.175 28.408 16.426

ATOM 3807 N PHE C2397 36.353 30.304 17.094

ATOM 3808 CA PHE C2397 37.739 30.745 16.953

ATOM 3809 C PHE C2397 37.934 31.262 15.552

ATOM 3810 O PHE C2397 37.058 31.082 14.722

ATOM 3811 CB PHE C2397 38.723 29.586 17.257

ATOM 3812 CG PHE C2397 40.170 30.051 17.473

ATOM 3813 CDl PHE C2397 41.196 29.555 16.658

ATOM 3814 CD2 PHE C2397 40.489 30.948 18.499

ATOM 3815 CEl PHE C2397 42.527 29.867 16.934

ATOM 3816 CE2 PHE C2397 41.820 31.312 18.729

ATOM 3817 CZ PHE C2397 42.838 30.791 17.934

ATOM 3818 HA PHE C2397 37.898 31.593 17.637

ATOM 3819 HBl PHE C2397 38.433 29.071 18.184

ATOM 3820 HB2 PHE C2397 38.654 28.854 16.438

ATOM 3821 HD2 PHE C2397 39.711 31.363 19.130

ATOM 3822 HE2 PHE C2397 42.077 31.996 19.526

ATOM 3823 HZ PHE C2397 43.864 31.098 18.095

ATOM 3824 HEl PHE C2397 43.323 29.384 16.383

ATOM 3825 HDl PHE C2397 40.964 28.916 15.814

ATOM 3826 H PHE C2397 35.939 29.788 16.352

ATOM 3827 N ASN C2398 38.740 32.076 15.056

ATOM 3828 CA ASN C2398 38.737 32.437 13.641

ATOM 3829 C ASN C2398 40.125 32.772 13.172

ATOM 3830 O ASN C2398 41.008 32.929 14.001

ATOM 3831 CB ASN C2398 37.696 33.526 13.264

ATOM 3832 CG ASN C2398 38.223 34.926 13.436

ATOM 3833 ODl ASN C2398 38.582 35.545 12.448

ATOM 3834 ND2 ASN C2398 38.269 35.452 14.676

ATOM 3835 HA ASN C2398 38.472 31.534 13.071

ATOM 3836 HBl ASN C2398 37.394 33.404 12.210

ATOM 3837 HB2 ASN C2398 36.787 33.412 13.872

ATOM 3838 HD22 ASN C2398 38.538 36.405 14.801

ATOM 3839 HD21 ASN C2398 38.022 34.905 15.473

ATOM 3840 H ASN C2398 39.462 32.418 15.660

ATOM 3841 N GLU C2399 40.322 32.859 11.838

ATOM 3842 CA GLU C2399 41.667 33.045 11.313

ATOM 3843 C GLU C2399 42.264 34.323 11.862

ATOM 3844 O GLU C2399 43.447 34.315 12.159

ATOM 3845 CB GLU C2399 41.731 33.062 9.759 ATOM 3846 CG GLU C2399 41.383 31.689 9.111

ATOM 3847 CD GLU C2399 39.932 31.288 9.198

ATOM 3848 OEl GLU C2399 39.642 30.066 9.091

ATOM 3849 OE2 GLU C2399 39.063 32.186 9.370

ATOM 3850 HA GLU C2399 42.281 32.200 11.668

ATOM 3851 HBl GLU C2399 41.071 33.852 9.367

ATOM 3852 HB2 GLU C2399 42.766 33.313 9.471

ATOM 3853 HGl GLU C2399 41.628 31.733 8.037

ATOM 3854 HG2 GLU C2399 42.004 30.901 9.566

ATOM 3855 H GLU C2399 39.560 32.778 11.195

ATOM 3856 N GLU C2400 41.499 35.429 12.024

ATOM 3857 CA GLU C2400 42.098 36.643 12.588

ATOM 3858 C GLU C2400 42.826 36.305 13.874

ATOM 3859 O GLU C2400 43.916 36.798 14.116

ATOM 3860 CB GLU C2400 41.102 37.761 13.012

ATOM 3861 CG GLU C2400 40.235 38.354 11.872

ATOM 3862 CD GLU C2400 39.336 39.426 12.440

ATOM 3863 OEl GLU C2400 39.437 40.601 11.993

ATOM 3864 OE2 GLU C2400 38.519 39.102 13.345

ATOM 3865 HA GLU C2400 42.804 37.040 11.842

ATOM 3866 HBl GLU C2400 40.443 37.365 13.797

ATOM 3867 HB2 GLU C2400 41.680 38.595 13.449

ATOM 3868 HGl GLU C2400 40.887 38.771 11.089

ATOM 3869 HG2 GLU C2400 39.595 37.590 11.410

ATOM 3870 H GLU C2400 40.537 35.431 11.753

ATOM 3871 N LEU C2401 42.209 35.468 14.736

ATOM 3872 CA LEU C2401 42.836 35.155 16.018

ATOM 3873 C LEU C2401 44.060 34.288 15.802

ATOM 3874 O LEU C2401 45.063 34.531 16.455

ATOM 3875 CB LEU C2401 41.847 34.527 17.036

ATOM 3876 CG LEU C2401 40.701 35.505 17.446

ATOM 3877 CDl LEU C2401 39.631 34.752 18.276

ATOM 3878 CD2 LEU C2401 41.206 36.731 18.262

ATOM 3879 HA LEU C2401 43.190 36.088 16.478

ATOM 3880 HBl LEU C2401 41.430 33.615 16.585

ATOM 3881 HB2 LEU C2401 42.403 34.227 17.939

ATOM 3882 HG LEU C2401 40.204 35.889 16.542

ATOM 3883 HD21 LEU C2401 41.733 37.447 17.620

ATOM 3884 HD22 LEU C2401 40.370 37.283 18.717

ATOM 3885 HD23 LEU C2401 41.884 36.403 19.063

ATOM 3886 HDIl LEU C2401 40.098 34.308 19.159

ATOM 3887 HD12 LEU C2401 38.856 35.451 18.614

ATOM 3888 HD13 LEU C2401 39.153 33.954 17.690

ATOM 3889 H LEU C2401 41.326 35.052 14.508

ATOM 3890 N SER C2402 44.029 33.288 14.890

ATOM 3891 CA SER C2402 45.253 32.541 14.584

ATOM 3892 C SER C2402 46.363 33.479 14.153

ATOM 3893 O SER C2402 47.486 33.334 14.612

ATOM 3894 CB SER C2402 45.056 31.551 13.404

ATOM 3895 OG SER C2402 44.064 30.560 13.701

ATOM 3896 HA SER C2402 45.568 31.984 15.484

ATOM 3897 HBl SER C2402 44.717 32.096 12.511

ATOM 3898 HB2 SER C2402 46.011 31.057 13.154

ATOM 3899 HG SER C2402 44.337 30.000 14.417

ATOM 3900 H SER C2402 43.186 33.055 14.399

ATOM 3901 N GLU C2403 46.053 34.450 13.261

ATOM 3902 CA GLU C2403 47.069 35.391 12.779

ATOM 3903 C GLU C2403 47.747 36.057 13.955

ATOM 3904 O GLU C2403 48.957 36.225 13.961

ATOM 3905 CB GLU C2403 46.487 36.486 11.839

ATOM 3906 CG GLU C2403 46.049 35.920 10.458

ATOM 3907 CD GLU C2403 45.401 36.977 9.597

ATOM 3908 OEl GLU C2403 45.691 37.017 8.370

ATOM 3909 OE2 GLU C2403 44.590 37.780 10.133

ATOM 3910 HA GLU C2403 47.822 34.831 12.202

ATOM 3911 HBl GLU C2403 45.637 36.972 12.338

ATOM 3912 HB2 GLU C2403 47.255 37.255 11.656

ATOM 3913 HGl GLU C2403 46.934 35.518 9.937 ATOM 3914 HG2 GLU C2403 45.328 35.100 10.579

ATOM 3915 H GLU C2403 45.116 34.544 12.924

ATOM 3916 N ILE C2404 46.945 36.445 14.967

ATOM 3917 CA ILE C2404 47.488 37.140 16.133

ATOM 3918 C ILE C2404 48.444 36.259 16.928

ATOM 3919 O ILE C2404 49.332 36.799 17.569

ATOM 3920 CB ILE C2404 46.305 37.736 16.959

ATOM 3921 CGl ILE C2404 45.666 38.929 16.177

ATOM 3922 CG2 ILE C2404 46.784 38.164 18.367

ATOM 3923 CDl ILE C2404 44.289 39.394 16.720

ATOM 3924 HA ILE C2404 48.073 38.006 15.775

ATOM 3925 HB ILE C2404 45.543 36.955 17.111

ATOM 3926 HGIl ILE C2404 46.358 39.787 16.185

ATOM 3927 HG12 ILE C2404 45.509 38.641 15.125

ATOM 3928 HDIl ILE C2404 44.360 39.790 17.743

ATOM 3929 HD12 ILE C2404 43.874 40.188 16.079

ATOM 3930 HD13 ILE C2404 43.587 38.551 16.711

ATOM 3931 HG21 ILE C2404 47.584 38.917 18.300

ATOM 3932 HG22 ILE C2404 45.945 38.587 18.927

ATOM 3933 HG23 ILE C2404 47.149 37.294 18.933

ATOM 3934 H ILE C2404 45.960 36.274 14.913

ATOM 3935 N LEU C2405 48.291 34.912 16.908

ATOM 3936 CA LEU C2405 49.170 34.023 17.681

ATOM 3937 C LEU C2405 50.355 33.491 16.918

ATOM 3938 O LEU C2405 51.368 33.233 17.546

ATOM 3939 CB LEU C2405 48.417 32.747 18.156

ATOM 3940 CG LEU C2405 47.273 33.013 19.174

ATOM 3941 CDl LEU C2405 46.580 31.668 19.529

ATOM 3942 CD2 LEU C2405 47.800 33.669 20.477

ATOM 3943 HA LEU C2405 49.593 34.546 18.551

ATOM 3944 HBl LEU C2405 48.002 32.244 17.267

ATOM 3945 HB2 LEU C2405 49.133 32.053 18.628

ATOM 3946 HG LEU C2405 46.529 33.688 18.716

ATOM 3947 HD21 LEU C2405 48.204 34.665 20.285

ATOM 3948 HD22 LEU C2405 46.975 33.800 21.191

ATOM 3949 HD23 LEU C2405 48.596 33.052 20.924

ATOM 3950 HDIl LEU C2405 47.288 30.981 20.018

ATOM 3951 HD12 LEU C2405 45.731 31.839 20.210

ATOM 3952 HD13 LEU C2405 46.207 31.184 18.615

ATOM 3953 H LEU C2405 47.564 34.502 16.358

ATOM 3954 N SER C2406 50.244 33.285 15.591

ATOM 3955 CA SER C2406 51.418 32.885 14.825

ATOM 3956 C SER C2406 52 322 34.093 14.663

ATOM 3957 O SER C2406 53.512 33.881 14.482

ATOM 3958 CB SER C2406 50.964 32.330 13.452

ATOM 3959 OG SER C2406 50.181 33.329 12.777

ATOM 3960 HA SER C2406 51.973 32.095 15.363

ATOM 3961 HBl SER C2406 51.843 32.052 12.847

ATOM 3962 HB2 SER C2406 50.346 31.430 13.620

ATOM 3963 HG SER C2406 49.854 33.023 11.936

ATOM 3964 H SER C2406 49.385 33.455 15.106

ATOM 3965 N ASP C2407 51.797 35.347 14.749

ATOM 3966 CA ASP C2407 52.640 36.544 14.719

ATOM 3967 C ASP C2407 52.430 37.353 15.992

ATOM 3968 O ASP C2407 51.752 38.368 15.930

ATOM 3969 CB ASP C2407 52.291 37.379 13.456

ATOM 3970 CG ASP C2407 53.114 38.644 13.400

ATOM 3971 ODl ASP C2407 52.518 39.746 13.250

ATOM 3972 OD2 ASP C2407 54.367 38.549 13.510

ATOM 3973 HA ASP C2407 53.703 36.284 14.624

ATOM 3974 HBl ASP C2407 52.496 36.784 12.552

ATOM 3975 HB2 ASP C2407 51.219 37.632 13.460

ATOM 3976 H ASP C2407 50.815 35.508 14.854

ATOM 3977 N PRO C2408 52.971 36.963 17.176

ATOM 3978 CA PRO C2408 52.705 37.729 18.388

ATOM 3979 C PRO C2408 53.355 39.100 18.435

ATOM 3980 O PRO C2408 54.455 39.262 17.930

ATOM 3981 CB PRO C2408 53.215 36.764 19.484 ATOM 3982 CG PRO C2408 54.279 35.897 18.774 ATOM 3983 CD PRO C2408 53.763 35.751 17.321 ATOM 3984 HA PRO C2408 51.613 37.839 18.499 ATOM 3985 HD2 PRO C2408 54.611 35.666 16.625 ATOM 3986 HDl PRO C2408 53.110 34.875 17.226 ATOM 3987 HG2 PRO C2408 55.234 36.447 18.771 ATOM 3988 HGl PRO C2408 54.432 34.924 19.271 ATOM 3989 HBl PRO C2408 53.620 37.286 20.365 ATOM 3990 HB2 PRO C2408 52.384 36.115 19.802 ATOM 3991 N SER C2409 52.663 40.093 19.049 ATOM 3992 CA SER C2409 53.146 41.472 19.122 ATOM 3993 C SER C2409 53.267 41.940 20.555 ATOM 3994 O SER C2409 52.880 41.214 21.459 ATOM 3995 CB SER C2409 52.063 42.329 18.417 ATOM 3996 OG SER C2409 50.814 42.106 19.094 ATOM 3997 HA SER C2409 54.109 41.605 18.606 ATOM 3998 HBl SER C2409 52.321 43.401 18.443 ATOM 3999 HB2 SER C2409 51.981 42.011 17.364 ATOM 4000 HG SER C2409 50.091 42.578 18.694 ATOM 4001 H SER C2409 51.764 39.921 19.450 ATOM 4002 N ASP C2410 53.767 43.187 20.754 ATOM 4003 CA ASP C2410 53.680 43.826 22.067 ATOM 4004 C ASP C2410 52.355 43.568 22.753 ATOM 4005 O ASP C2410 52.334 43.454 23.968 ATOM 4006 CB ASP C2410 53.914 45.360 22.007 ATOM 4007 CG ASP C2410 55.364 45.695 21.749 ATOM 4008 ODl ASP C2410 56.035 44.932 21.003 ATOM 4009 OD2 ASP C2410 55.848 46.724 22.297 ATOM 4010 HA ASP C2410 54.485 43.421 22.673 ATOM 4011 HBl ASP C2410 53.285 45.803 21.220 ATOM 4012 HB2 ASP C2410 53.628 45.808 22.973 ATOM 4013 H ASP C2410 54.208 43.700 20.013 ATOM 4014 N ASP C2411 51.238 43.482 21.999 ATOM 4015 CA ASP C2411 49.943 43.248 22.629 ATOM 4016 C ASP C2411 49.871 41.816 23.100 ATOM 4017 O ASP C2411 49.574 41.593 24.263 ATOM 4018 CB ASP C2411 48.766 43.570 21.671 ATOM 4019 CG ASP C2411 48.958 44.954 21.104 ATOM 4020 ODl ASP C2411 49.624 45.072 20.039 ATOM 4021 OD2 ASP C2411 48.456 45.932 21.721 ATOM 4022 HA ASP C2411 49.853 43.936 23.486 ATOM 4023 HBl ASP C2411 48.728 42.837 20.851 ATOM 4024 HB2 ASP C2411 47.811 43.513 22.218 ATOM 4025 H ASP C2411 51.282 43.580 21.005 ATOM 4026 N THR C2412 50.121 40.840 22.248 ATOM 4027 CA THR C2412 50.005 39.429 22.587 ATOM 4028 C THR C2412 51.370 38.877 22.919 ATOM 4029 O THR C2412 52.006 38.213 22.115 ATOM 4030 CB THR C2412 49.228 38.731 21.450 ATOM 4031 OGl THR C2412 47.951 39.395 21.453 ATOM 4032 CG2 THR C2412 49.083 37.214 21.724 ATOM 4033 HA THR C2412 49.386 39.323 23.495 ATOM 4034 HB THR C2412 49.733 38.882 20.480 ATOM 4035 HGl THR C2412 47.354 39.077 20.790 ATOM 4036 HG23 THR C2412 50.021 36.681 21.509 ATOM 4037 HG21 THR C2412 48.795 37.030 22.769 ATOM 4038 HG22 THR C2412 48.300 36.815 21.072 ATOM 4039 H THR C2412 50.553 41.098 21.388 ATOM 4040 N LYS C2413 51.649 39.024 24.347 ATOM 4041 CA LYS C2413 52.875 38.460 24.907 ATOM 4042 C LYS C2413 52.684 38.183 26.381 ATOM 4043 O LYS C2413 53.658 38.206 27.114 ATOM 4044 CB LYS C2413 54.024 39.471 24.702 ATOM 4045 CG LYS C2413 53.757 40.785 25.488 ATOM 4046 CD LYS C2413 54.909 41.777 25.223 ATOM 4047 CE LYS C2413 54.756 43.104 26.016 ATOM 4048 NZ LYS C2413 55.193 42.932 27.419 ATOM 4049 HA LYS C2413 53.121 37.506 24.412 ATOM 4050 HBl LYS C2413 54.974 39.023 25.036 ATOM 4051 HB2 LYS C2413 54.104 39.687 23.624 ATOM 4052 HGl LYS C2413 52. 41.235 25.159 ATOM 4053 HG2 LYS C2413 53. 40.610 26.570 ATOM 4054 HDl LYS C2413 55.882 41.319 25.434 ATOM 4055 HD2 LYS C2413 54.908 41.952 24.149 ATOM 4056 HEl LYS C2413 55.370 43.860 25.515 ATOM 4057 HE2 LYS C2413 53.729 43.484 25.978 ATOM 4058 HZl LYS C2413 56.163 42.484 27.413 ATOM 4059 HZ2 LYS C2413 55.447 43.838 27.941 ATOM 4060 HZ3 LYS C2413 54.508 42.350 28.021 ATOM 4061 H LYS C2413 51.044 39.582 24.933 ATOM 4062 N GLY C2414 51.431 37.970 26.850 ATOM 4063 CA GLY C2414 51.115 38.357 28.223 ATOM 4064 C GLY C2414 52.016 37.697 29.231 ATOM 4065 O GLY C2414 52.716 38.367 29.973 ATOM 4066 HA2 GLY C2414 50.076 38.093 28.470 ATOM 4067 HAl GLY C2414 51.198 39.456 28.287 ATOM 4068 H GLY C2414 50.669 37.721 26.243 ATOM 4069 N PHE C2415 52.106 36.398 29.168 ATOM 4070 CA PHE C2415 52.645 35.556 30.229 ATOM 4071 C PHE C2415 54.071 35.973 30.479 ATOM 4072 O PHE C2415 54.699 36.441 29.546 ATOM 4073 CB PHE C2415 52.516 34.050 29.855 ATOM 4074 CG PHE C2415 51.026 33.670 29.728 ATOM 4075 CDl PHE C2415 50.352 33.709 28.502 ATOM 4076 CD2 PHE C2415 50.302 33.294 30.855 ATOM 4077 CEl PHE C2415 48.962 33.562 28.443 ATOM 4078 CE2 PHE C2415 48.896 33.274 30.812 ATOM 4079 CZ PHE C2415 48.226 33.268 29.595 ATOM 4080 HA PHE C2415 52.069 35.742 31.154 ATOM 4081 HBl PHE C2415 53.063 33.832 28.925 ATOM 4082 HB2 PHE C2415 52.962 33.451 30.657 ATOM 4083 HD2 PHE C2415 50.825 33.014 31.760 ATOM 4084 HE2 PHE C2415 48.332 33.274 31.731 ATOM 4085 HZ PHE C2415 47.158 33.048 29.538 ATOM 4086 HEl PHE C2415 48.447 33.690 27.505 ATOM 4087 HDl PHE C2415 50.910 33.867 27.590 ATOM 4088 H PHE C2415 51.350 36.070 28.611 ATOM 4089 N PHE C2416 54.594 35.837 31.723 ATOM 4090 CA PHE C2416 55.928 36.344 32.035 ATOM 4091 C PHE C2416 56.836 35.198 .407 ATOM 4092 O PHE C2416 56.356 34.164 32.845 ATOM 4093 CB PHE C2416 55.814 37.351 33.202 ATOM 4094 CG PHE C2416 57.211 37.744 33.689 ATOM 4095 CDl PHE C2416 57.745 37.129 34.825 ATOM 4096 CD2 PHE C2416 57.961 38.706 33.004 ATOM 4097 CEl PHE C2416 58. 920 37.622 35.391 ATOM 4098 CE2 PHE C2416 59.229 39.062 33.472 ATOM 4099 CZ PHE C2416 59.683 38.560 34.696 ATOM 4100 HA PHE C2416 56.396 36.866 31.187 ATOM 4101 HBl PHE C2416 55.251 38.243 32.883 ATOM 4102 HB2 PHE C2416 55.260 36.879 34.025 ATOM 4103 HD2 PHE C2416 57.564 39.175 .108 ATOM 4104 HE2 PHE C2416 59.850 39.741 .896 ATOM 4105 HZ PHE C2416 60. 0 38.902 35.122 ATOM 4106 HEl PHE C2416 59.228 37.291 36.373 ATOM 4107 HDl PHE C2416 57.255 36.273 35.276 ATOM 4108 H PHE C2416 54.079 35.395 32.459 ATOM 4109 N ASP C2417 58.252 35.451 32.235 ATOM 4110 CA ASP C2417 59.250 34.430 32.562 ATOM 4111 C ASP C2417 60.101 34.830 33.757 ATOM 4112 O ASP C2417 60.958 35.678 33.589 ATOM 4113 CB ASP C2417 60.216 34.065 31.397 ATOM 4114 CG ASP C2417 61..234 33.032 31.815 ATOM 4115 ODl ASP C2417 62,.168 33.387 32.582 ATOM 4116 OD2 ASP C2417 61.119 31.854 31.379 ATOM 4117 HA ASP C2417 58.725 33.489 32.754 ATOM 4118 HBl ASP C2417 59.663 33.647 30.549 ATOM 4119 HB2 ASP C2417 60.745 34.954 31.035 ATOM 4120 H ASP C2417 58.594 36.315 31.862 ATOM 4121 N PRO C2418 59.936 34. ^?43 34.967 ATOM 4122 CA PRO C2418 60.823 34..522 36.094 ATOM 4123 C PRO C2418 62.326 34.559 35.909 ATOM 4124 O PRO C2418 62.940 35.459 36.463 ATOM 4125 CB PRO C2418 60.407 33.383 37.049 ATOM 4126 CG PRO C2418 58.898 33.240 36.758 ATOM 4127 CD PRO C2418 58.861 33.298 35.219 ATOM 4128 HA PRO C2418 60.510 35.466 36.556 ATOM 4129 HD2 PRO C2418 59.149 32.332 34.777 ATOM 4130 HDl PRO C2418 57.865 33. 622 34.880 ATOM 4131 HG2 PRO C2418 58.442 32.327 37.163 ATOM 4132 HGl PRO C2418 58.353 34.108 37.160 ATOM 4133 HBl PRO C2418 60..924 32.453 36.766 ATOM 4134 HB2 PRO C2418 60..629 33.613 38.100 ATOM 4135 N ASN C2419 62.957 33.607 35.184 ATOM 4136 CA ASN C2419 64.425 33.556 35.153 ATOM 4137 C ASN C2419 65.034 34.563 34.208 ATOM 4138 O ASN C2419 65.798 35.410 34.645 ATOM 4139 CB ASN C2419 64.934 32.132 34.781 ATOM 4140 CG ASN C2419 64.567 31.082 35.804 ATOM 4141 ODl ASN C2419 63.955 31.403 36.810 ATOM 4142 ND2 ASN C2419 64.940 29.805 35.564 ATOM 4143 HA ASN C2419 64.811 33.773 36.166 ATOM 4144 HBl ASN C2419 64.522 31.823 33.808 ATOM 4145 HB2 ASN C2419 66.032 32.151 34.696 ATOM 4146 HD22 ASN C2419 64.726 29.090 36.230 ATOM 4147 HD21 ASN C2419 65.432 29.558 34.727 ATOM 4148 H ASN C2419 62.431 32.907 34.699 ATOM 4149 N THR C2420 64.913 34.308 32.837 ATOM 4150 CA THR C2420 65.420 35.309 31.896 ATOM 4151 C THR C2420 64.605 36.579 32. .023 ATOM 4152 O THR C2420 65.162 37.658 31. ATOM 4153 CB THR C2420 65.455 34.751 30.447 ATOM 4154 OGl THR C2420 65.679 35.860 29.562 ATOM 4155 CG2 THR C2420 64.170 33.976 30.055 ATOM 4156 HA THR C2420 66.466 35.558 32.155 ATOM 4157 HB THR C2420 66.305 34.049 30.360 ATOM 4158 HGl THR C2420 65.784 35.588 28.657 ATOM 4159 HG23 THR C2420 64.145 32.989 30.542 ATOM 4160 HG21 THR C2420 63.276 34.536 30.354 ATOM 4161 HG22 THR C2420 64.143 33.815 28.967 ATOM 4162 H THR C2420 63.965 33.994 32.741 ATOM 4163 N GLU C2421 63.457 36.826 32.551 ATOM 4164 CA GLU C2421 62.841 38.091 32.943 ATOM 4165 C GLU C2421 62.289 38.809 31.733 ATOM 4166 O GLU C2421 62.666 39.937 31.468 ATOM 4167 CB GLU C2421 63.624 39.026 33.902 ATOM 4168 CG GLU C2421 63.929 38.373 35.274 ATOM 4169 CD GLU C2421 64.433 39.431 36.223 ATOM 4170 OEl GLU C2421 65.677 39.575 36.368 ATOM 4171 OE2 GLU C2421 63.578 40.134 36.827 ATOM 4172 HA GLU C2421 61.955 37.849 33.543 ATOM 4173 HBl GLU C2421 64.546 39.408 33.441 ATOM 4174 HB2 GLU C2421 62.963 39.882 34.104 ATOM 4175 HGl GLU C2421 63.016 37.930 35.703 ATOM 4176 HG2 GLU C2421 64.676 37.576 35.155 ATOM 4177 H GLU C2421 62.900 35.995 32.652 ATOM 4178 N GLU C2422 61.367 38.130 31.014 ATOM 4179 CA GLU C2422 60.811 38.661 29.772 ATOM 4180 C GLU C2422 59.383 38.210 29.588 ATOM 4181 O GLU C2422 58.958 37.298 30.280 ATOM 4182 CB GLU C2422 61.674 38.255 28.563 ATOM 4183 CG GLU C2422 61.761 36.733 28.438 ATOM 4184 CD GLU C2422 62.617 36.330 27.236 ATOM 4185 OEl GLU C2422 63.129 37.202 26.519 ATOM 4186 OE2 GLU C2422 62.743 35.058 27.058 ATOM 4187 HA GLU C2422 60.799 39.764 29.797 ATOM 4188 HBl GLU C2422 62.672 38.676 28.685 ATOM 4189 HB2 GLU C2422 61.226 38.661 27.656 ATOM 4190 HGl GLU C2422 60.754 36.329 28.330 ATOM 4191 HG2 GLU C2422 62.210 36.328 29.345 ATOM 4192 H GLU C2422 61.074 37.223 31.308 ATOM 4193 N ASN C2423 58.648 38.857 28.656 ATOM 4194 CA ASN C2423 57.254 38.503 28.419 ATOM 4195 C ASN C2423 57.123 37.689 27.166 ATOM 4196 O ASN C2423 57.993 37.816 26.319 ATOM 4197 CB ASN C2423 56.375 39.734 28.176 ATOM 4198 CG ASN C2423 56.448 40.673 29.332 ATOM 4199 ODl ASN C2423 55.657 40.568 30.259 ATOM 4200 ND2 ASN C2423 57.391 41.624 29.268 ATOM 4201 HA ASN C2423 56.823 37.968 29.275 ATOM 4202 HBl ASN C2423 56.727 40.210 27.253 ATOM 4203 HB2 ASN C2423 55.325 39.465 28.051 ATOM 4204 HD22 ASN C2423 57.314 42.322 29.946 ATOM 4205 HD21 ASN C2423 58.082 41.711 28.548 ATOM 4206 H ASN C2423 59.049 39.578 28.087 ATOM 4207 N LEU C2424 56.058 36.861 27.056 ATOM 4208 CA LEU C2424 55.972 35.935 25.934 ATOM 4209 C LEU C2424 54.647 35.206 25.967 ATOM 4210 O LEU C2424 53.924 35.341 26.943 ATOM 4211 CB LEU C2424 57.214 34.989 25.907 ATOM 4212 CG LEU C2424 57.399 34.090 27.167 ATOM 4213 CDl LEU C2424 58.655 33.193 27.004 ATOM 4214 CD2 LEU C2424 57.614 34.915 28.462 ATOM 4215 HA LEU C2424 55.965 36.536 25.007 ATOM 4216 HBl LEU C2424 57.157 34.360 25.013 ATOM 4217 HB2 LEU C2424 58.138 35.566 25.774 ATOM 4218 HG LEU C2424 56.512 33.447 27.281 ATOM 4219 HD21 LEU C2424 56.688 35.354 28.829 ATOM 4220 HD22 LEU C2424 57.955 34.273 29.270 ATOM 4221 HD23 LEU C2424 58.374 35.693 28.311 ATOM 4222 HDIl LEU C2424 59.525 33.839 26.831 ATOM 4223 HD12 LEU C2424 58.849 32.585 27.899 ATOM 4224 HD13 LEU C2424 58.550 32.509 26.159 ATOM 4225 H LEU C2424 55.326 36.846 27.746 ATOM 4226 N THR C2425 54.232 34.515 24.911 ATOM 4227 CA THR C2425 52.953 33.815 24.846 ATOM 4228 C THR C2425 53.018 32.549 25.666 ATOM 4229 O THR C2425 54.096 32.122 26.051 ATOM 4230 CB THR C2425 52.608 33.433 23.383 ATOM 4231 OGl THR C2425 53.672 32.610 22.878 ATOM 4232 CG2 THR C2425 52.414 34.705 22.522 ATOM 4233 HA THR C2425 52.158 34.464 25.253 ATOM 4234 HB THR C2425 51.670 32.851 23.352 ATOM 4235 HGl THR C2425 53.484 32.268 22.009 ATOM 4236 HG23 THR C2425 51.511 35.239 22.855 ATOM 4237 HG21 THR C2425 53.277 35.383 22.606 ATOM 4238 HG22 THR C2425 52.288 34.415 21.470 ATOM 4239 H THR C2425 54.969 34.202 24.316 ATOM 4240 N TYR C2426 51.828 31.938 25.928 ATOM 4241 CA TYR C2426 51.775 30.747 26.762 ATOM 4242 C TYR C2426 52.583 29.638 26.136 ATOM 4243 O TYR C2426 53.248 28.904 26.850 ATOM 4244 CB TYR C2426 50.331 30.222 26.964 ATOM 4245 CG TYR C2426 50.373 29.281 28.172 ATOM 4246 CDl TYR C2426 50.334 29.836 29.454 ATOM 4247 CD2 TYR C2426 50.475 27.895 28.023 ATOM 4248 CEl TYR C2426 50.382 29.014 30.580 ATOM 4249 CE2 TYR C2426 50.427 27.065 29.147 ATOM 4250 CZ TYR C2426 50.360 27.624 30.426 ATOM 4251 OH TYR C2426 50.271 26.794 31.542 ATOM 4252 HA TYR C2426 52.198 31.007 27.748 ATOM 4253 HB2 TYR C2426 49 . 645 31 . 053 27 . 192 ATOM 4254 HBl TYR C2426 49.956 29.718 26.059 ATOM 4255 HD2 TYR C2426 50.599 27.464 27.038 ATOM 4256 HE2 TYR C2426 50.443 25.986 29.026 ATOM 4257 HEl TYR C2426 50.435 29.460 31.567 ATOM 4258 HDl TYR C2426 50.275 30.909 29.581 ATOM 4259 HH TYR C2426 49.871 27.224 32.291 ATOM 4260 H TYR C2426 50.970 32.300 25.566 ATOM 4261 N LEU C2427 52.513 29.508 24.793 ATOM 4262 CA LEU C2427 53.252 28.451 24.104 ATOM 4263 C LEU C2427 54.726 28.660 24.342 ATOM 4264 O LEU C2427 55.421 27.701 24.641 ATOM 4265 CB LEU C2427 52.889 28.467 22.588 ATOM 4266 CG LEU C2427 53.588 27.415 21.670 ATOM 4267 CDl LEU C2427 55.010 27.851 21.218 ATOM 4268 CD2 LEU C2427 53.602 25.991 22.291 ATOM 4269 HA LEU C2427 52.949 27.484 24.540 ATOM 4270 HBl LEU C2427 51.801 28.295 22.527 ATOM 4271 HB2 LEU C2427 53.086 29.470 22.178 ATOM 4272 HG LEU C2427 52.985 27.357 20.744 ATOM 4273 HD21 LEU C2427 52.590 25.706 22.616 ATOM 4274 HD22 LEU C2427 53.947 25.257 21.546 ATOM 4275 HD23 LEU C2427 54.282 25.941 23.154 ATOM 4276 HDIl LEU C2427 55.708 27.920 22.061 ATOM 4277 HD12 LEU C2427 55.414 27.117 20.503 ATOM 4278 HD13 LEU C2427 54.969 28.830 20.716 ATOM 4279 H LEU C2427 51.955 30.140 24.251 ATOM 4280 N GLN C2428 55.232 29.906 24.213 ATOM 4281 CA GLN C2428 56.668 30.111 24.383 ATOM 4282 C GLN C2428 57.053 29.904 25.837 ATOM 4283 O GLN C2428 58.097 29.333 26.110 ATOM 4284 CB GLN C2428 57.113 31.516 23.913 ATOM 4285 CG GLN C2428 56.912 31.802 22.401 ATOM 4286 CD GLN C2428 57.234 33.260 22.151 ATOM 4287 OEl GLN C2428 58.389 33.626 22.304 ATOM 4288 NE2 GLN C2428 56.262 34.126 21.784 ATOM 4289 HA GLN C2428 57.183 29.388 23.737 ATOM 4290 HBl GLN C2428 56.542 32.237 24.511 ATOM 4291 HB2 GLN C2428 58.189 31.628 24.112 ATOM 4292 HGl GLN C2428 57.600 31.178 21.808 ATOM 4293 HG2 GLN C2428 55.891 31.555 22.081 ATOM 4294 HE22 GLN C2428 56.488 35.090 21.640 ATOM 4295 HE21 GLN C2428 55.316 33.833 21.651 ATOM 4296 H GLN C2428 54.649 30.693 23.999 ATOM 4297 N LEU C2429 56.234 30.368 26.806 ATOM 4298 CA LEU C2429 56.584 30.172 28.216 ATOM 4299 C LEU C2429 56.621 28.692 28.515 ATOM 4300 O LEU C2429 57.541 28.205 29.152 ATOM 4301 CB LEU C2429 55.609 30.906 29.182 ATOM 4302 CG LEU C2429 56.057 30.870 30.676 ATOM 4303 CDl LEU C2429 57.349 31.676 30.973 ATOM 4304 CD2 LEU C2429 54.941 31.438 31.593 ATOM 4305 HA LEU C2429 57.587 30.582 28.368 ATOM 4306 HBl LEU C2429 55.499 31.957 28.879 ATOM 4307 HB2 LEU C2429 54.623 30.424 29.084 ATOM 4308 HG LEU C2429 56.263 29.828 30.955 ATOM 4309 HD21 LEU C2429 53.959 30.996 31.373 ATOM 4310 HD22 LEU C2429 55.194 31.249 32.646 ATOM 4311 HD23 LEU C2429 54.869 32.525 31.459 ATOM 4312 HDIl LEU C2429 57.176 32.737 30.756 ATOM 4313 HD12 LEU C2429 57.588 31.576 32.041 ATOM 4314 HD13 LEU C2429 58.221 31.329 30.406 ATOM 4315 H LEU C2429 55.385 30.845 26.576 ATOM 4316 N LYS C2430 55.601 27.954 28.033 ATOM 4317 CA LYS C2430 55.551 26.510 28.245 ATOM 4318 C LYS C2430 56.811 25.838 27.733 ATOM 4319 O LYS C2430 57.315 24.963 28.420 ATOM 4320 CB LYS C2430 54.296 25.940 27.528 ATOM 4321 CG LYS C2430 54.170 24.407 27.694 ATOM 4322 CD LYS C2430 52.976 23.852 26.873

ATOM 4323 CE LYS C2430 53.000 22.302 26.903

ATOM 4324 NZ LYS C2430 51.824 21.720 26.224

ATOM 4325 HA LYS C2430 55.473 26.308 29.326

ATOM 4326 HBl LYS C2430 53.390 26.420 27.935

ATOM 4327 HB2 LYS C2430 54.364 26.180 26.455

ATOM 4328 HGl LYS C2430 55.092 23.922 27.338

ATOM 4329 HG2 LYS C2430 54.037 24.164 28.762

ATOM 4330 HDl LYS C2430 52.030 24.230 27.293

ATOM 4331 HD2 LYS C2430 53.045 24.184 25.823

ATOM 4332 HEl LYS C2430 53.917 21.939 26.410

ATOM 4333 HE2 LYS C2430 53.036 21.972 27.952

ATOM 4334 HZl LYS C2430 51.799 21.975 25.173

ATOM 4335 HZ2 LYS C2430 51.837 20.643 26.319

ATOM 4336 HZ3 LYS C2430 50.900 22.066 26.654

ATOM 4337 H LYS C2430 54.853 28.395 27.536

ATOM 4338 N GLU C2431 57.352 26.212 26.548

ATOM 4339 CA GLU C2431 58.555 25.534 26.043

ATOM 4340 C GLU C2431 59.789 25.854 26.871

ATOM 4341 O GLU C2431 60.751 25.106 26.794

ATOM 4342 CB GLU C2431 58.757 25.596 24.501

ATOM 4343 CG GLU C2431 59.165 26.986 23.959

ATOM 4344 CD GLU C2431 60.594 27.359 24.252

ATOM 4345 OEl GLU C2431 61.502 26.678 23.704

ATOM 4346 OE2 GLU C2431 60.822 28.338 25.015

ATOM 4347 HA GLU C2431 58.384 24.455 26.211

ATOM 4348 HBl GLU C2431 59.521 24.867 24.184

ATOM 4349 HB2 GLU C2431 57.800 25.307 24.033

ATOM 4350 HGl GLU C2431 59.016 27.020 22.867

ATOM 4351 HG2 GLU C2431 58.499 27.720 24.407

ATOM 4352 H GLU C2431 56.938 26.947 26.008

ATOM 4353 N ARG C2432 59.782 26.925 27.704

ATOM 4354 CA ARG C2432 60.867 27.125 28.676

ATOM 4355 C ARG C2432 60.876 26.052 29.755

ATOM 4356 O ARG C2432 61.890 25.893 30.417

ATOM 4357 CB ARG C2432 60.774 28.496 29.415

ATOM 4358 CG ARG C2432 60.727 29.742 28.483

ATOM 4359 CD ARG C2432 62.066 30.021 27.749

ATOM 4360 NE ARG C2432 61.855 30.924 26.614

ATOM 4361 CZ ARG C2432 61.797 32.236 26.706

ATOM 4362 NHl ARG C2432 61.861 32.881 27.848

ATOM 4363 NH2 ARG C2432 61.667 32.933 25.598

ATOM 4364 HA ARG C2432 61.832 27.066 28.152

ATOM 4365 HBl ARG C2432 59.863 28.488 30.034

ATOM 4366 HB2 ARG C2432 61.632 28.610 30.099

ATOM 4367 HGl ARG C2432 59.946 29.628 27.723

ATOM 4368 HG2 ARG C2432 60.452 30.619 29.088

ATOM 4369 HDl ARG C2432 62.848 30.365 28.442

ATOM 4370 HD2 ARG C2432 62.447 29.082 27.324

ATOM 4371 HE ARG C2432 61.781 30.486 25.679

ATOM 4372 HH12 ARG C2432 61.808 33.907 27.875

ATOM 4373 HHIl ARG C2432 61.950 32.395 28.746

ATOM 4374 HH22 ARG C2432 61.635 33.963 25.615

ATOM 4375 HH21 ARG C2432 61.600 32.469 24.679

ATOM 4376 H ARG C2432 59.003 27.553 27.720

ATOM 4377 N CYS C2433 59.753 25.327 29.978

ATOM 4378 CA CYS C2433 59.617 24.485 31.168

ATOM 4379 C CYS C2433 60.198 23.095 31.047

ATOM 4380 O CYS C2433 60.468 22.665 29.937

ATOM 4381 CB CYS C2433 58.111 24.403 31.545

ATOM 4382 SG CYS C2433 57.528 26.110 31.834

ATOM 4383 HA CYS C2433 60.140 24.980 32.000

ATOM 4384 HBl CYS C2433 57.532 23.947 30.729

ATOM 4385 HB2 CYS C2433 57.941 23.792 32.440

ATOM 4386 HG CYS C2433 56.785 25.915 32.485

ATOM 4387 LPGl CYS C2433 57.297 26.400 31.265

ATOM 4388 LPG2 CYS C2433 58.010 26.501 32.108

ATOM 4389 H CYS C2433 58.961 25.404 29.378 ATOM 4390 N ILE C2434 60.382 22.410 32.208

ATOM 4391 CA ILE C2434 61.022 21.094 32.254

ATOM 4392 C ILE C2434 60.001 20.033 32.618

ATOM 4393 O ILE C2434 59.165 20.282 33.472

ATOM 4394 CB ILE C2434 62.277 21.063 33.191

ATOM 4395 CGl ILE C2434 63.007 19.686 33.091

ATOM 4396 CG2 ILE C2434 61.944 21.400 34.675

ATOM 4397 CDl ILE C2434 64.458 19.690 33.648

ATOM 4398 HA ILE C2434 61.394 20.855 31.243

ATOM 4399 HB ILE C2434 62.963 21.844 32.819

ATOM 4400 HGIl ILE C2434 62.419 18.915 33.616

ATOM 4401 HG12 ILE C2434 63.088 19.391 32.032

ATOM 4402 HDIl ILE C2434 64.488 19.871 34.731

ATOM 4403 HD12 ILE C2434 64.930 18.712 33.462

ATOM 4404 HD13 ILE C2434 65.057 20.463 33.142

ATOM 4405 HG21 ILE C2434 61.231 20.671 35.089

ATOM 4406 HG22 ILE C2434 62.848 21.388 35.299

ATOM 4407 HG23 ILE C2434 61.520 22.405 34.785

ATOM 4408 H ILE C2434 60.081 22.799 33.077

ATOM 4409 N LYS C2435 60.048 18.847 31.957

ATOM 4410 CA LYS C2435 59.009 17.833 o o 199

ATOM 4411 C LYS C2435 59.414 16.872 33.220

ATOM 4412 O LYS C2435 60.410 16.186 33.050

ATOM 4413 CB LYS C2435 58.819 17.062 30.784

ATOM 4414 CG LYS C2435 57.513 16.217 30.792

ATOM 4415 CD LYS C2435 57.571 14.981 29.847

ATOM 4416 CE LYS C2435 58.439 13.828 30.431

ATOM 4417 NZ LYS C2435 58.263 12.558 29.691

ATOM 4418 HA LYS C2435 58.056 18.327 32.351

ATOM 4419 HBl LYS C2435 58.771 17.784 29.951

ATOM 4420 HB2 LYS C2435 59.704 16.434 30.611

ATOM 4421 HGl LYS C2435 57.293 15.868 31.812

ATOM 4422 HG2 LYS C2435 56.680 16.875 30.487

ATOM 4423 HDl LYS C2435 56.545 14.598 29.719

ATOM 4424 HD2 LYS C2435 57.950 15.279 28.856

ATOM 4425 HEl LYS C2435 59.506 14.105 30.425

ATOM 4426 HE2 LYS C2435 58.143 13.645 31.474

ATOM 4427 HZl LYS C2435 58.540 12.657 28.651

ATOM 4428 HZ2 LYS C2435 58.875 11.772 30.115

ATOM 4429 HZ3 LYS C2435 57.240 12.209 29.733

ATOM 4430 H LYS C2435 60.785 18.644 31.311

ATOM 4431 N ASP C2436 58.673 16.791 34.351

ATOM 4432 CA ASP C2436 59.006 15.811 35.389

ATOM 4433 C ASP C2436 58.808 14.410 34.861

ATOM 4434 O ASP C2436 58.145 14.264 33.849

ATOM 4435 CB ASP C2436 58.111 16.060 36.628

ATOM 4436 CG ASP C2436 58.365 15.167 37.815

ATOM 4437 ODl ASP C2436 58.046 13.953 37.723

ATOM 4438 OD2 ASP C2436 58.877 15.666 38.853

ATOM 4439 HA ASP C2436 60.058 15.940 35.690

ATOM 4440 HBl ASP C2436 58.240 17.105 36.933

ATOM 4441 HB2 ASP C2436 57.077 15.934 36.298

ATOM 4442 H ASP C2436 57.869 17.373 34.482

ATOM 4443 N GLU C2437 59.389 13.390 35.534

ATOM 4444 CA GLU C2437 59.347 12.012 35.045

ATOM 4445 C GLU C2437 58.287 11.200 35.762

ATOM 4446 O GLU C2437 57.520 10.523 35.096

ATOM 4447 CB GLU C2437 60.753 11.330 35.062

ATOM 4448 CG GLU C2437 61.588 11.415 36.374

ATOM 4449 CD GLU C2437 62.200 12.778 36.594

ATOM 4450 OEl GLU C2437 61.555 13.619 37.278

ATOM 4451 OE2 GLU C2437 63.329 13.024 36.087

ATOM 4452 HA GLU C2437 59.057 12.013 33.980

ATOM 4453 HBl GLU C2437 60.605 10.265 34.816

ATOM 4454 HB2 GLU C2437 61.372 11.774 34.264

ATOM 4455 HGl GLU C2437 60.993 11.110 37.246

ATOM 4456 HG2 GLU C2437 62.425 10.701 36.298

ATOM 4457 H GLU C2437 59.851 13.578 36.397 ATOM 4458 N GLU C2438 58.221 11.246 37.112 ATOM 4459 CA GLU C2438 57.235 10.453 37.842 ATOM 4460 C GLU C2438 55.858 11.025 37.612 ATOM 4461 O GLU C2438 54.929 10.260 37.404 ATOM 4462 CB GLU C2438 57.536 10.277 39.363 ATOM 4463 CG GLU C2438 57.941 11.571 40.119 ATOM 4464 CD GLU C2438 57.741 11.393 41.601 ATOM 4465 OEl GLU C2438 56.735 11.934 42.139 ATOM 4466 OE2 GLU C2438 58.589 10.716 42.242 ATOM 4467 HA GLU C2438 57.247 9.428 37.427 ATOM 4468 HBl GLU C2438 56.630 9.857 39.832 ATOM 4469 HB2 GLU C2438 58.354 9.549 39.499 ATOM 4470 HGl GLU C2438 58.999 11.827 39.945 ATOM 4471 HG2 GLU C2438 57.332 12.410 39.772 ATOM 4472 H GLU C2438 58.825 11.848 37.623 ATOM 4473 N THR C2439 55.661 12.363 37.673 ATOM 4474 CA THR C2439 54.348 12.962 37.465 ATOM 4475 C THR C2439 54.143 13.172 35.984 ATOM 4476 O THR C2439 53.016 13.091 35.523 ATOM 4477 CB THR C2439 54.253 14.328 38.196 ATOM 4478 OGl THR C2439 55.224 15.206 37.613 ATOM 4479 CG2 THR C2439 54.486 14.205 39.724 ATOM 4480 HA THR C2439 53.556 12.299 37.859 ATOM 4481 HB THR C2439 53.244 14.740 38.032 ATOM 4482 HGl THR C2439 55.201 16.085 37.977 ATOM 4483 HG23 THR C2439 53.581 13.841 40.224 ATOM 4484 HG21 THR C2439 55.299 13.508 39.953 ATOM 4485 HG22 THR C2439 54.740 15.187 40.147 ATOM 4486 H THR C2439 56.467 12.949 37.583 ATOM 4487 N GLY C2440 55.218 13.448 35.159 ATOM 4488 CA GLY C2440 55.040 13.748 33.743 ATOM 4489 C GLY C2440 54.799 15.220 33.469 ATOM 4490 O GLY C2440 54.700 15.578 32.305 ATOM 4491 HA2 GLY C2440 54.176 13.193 33.345 ATOM 4492 HAl GLY C2440 55.915 13.399 33.179 ATOM 4493 H GLY C2440 56.147 13.484 35.531 ATOM 4494 N LEU C2441 54.663 16.085 34.505 ATOM 4495 CA LEU C2441 54.100 17.420 34.291 ATOM 4496 C LEU C2441 55.133 18.458 33.904 ATOM 4497 O LEU C2441 56.305 18.225 34.141 ATOM 4498 CB LEU C2441 53.361 17.883 35.578 ATOM 4499 CG LEU C2441 52.226 16.928 36.071 ATOM 4500 CDl LEU C2441 51.887 17.238 37.555 ATOM 4501 CD2 LEU C2441 50.930 17.020 35.220 ATOM 4502 HA LEU C2441 53.382 17.349 33.468 ATOM 4503 HBl LEU C2441 54.128 17.984 36.362 ATOM 4504 HB2 LEU C2441 52.936 18.876 35.405 ATOM 4505 HG LEU C2441 52.573 15.884 36.018 ATOM 4506 HD21 LEU C2441 51.120 16.709 34.182 ATOM 4507 HD22 LEU C2441 50.153 16.355 35.630 ATOM 4508 HD23 LEU C2441 50.535 18.048 35.227 ATOM 4509 HDIl LEU C2441 51.506 18.263 37.657 ATOM 4510 HD12 LEU C2441 51.128 16.542 37.942 ATOM 4511 HD13 LEU C2441 52.790 17.137 38.174 ATOM 4512 H LEU C2441 54.875 15.812 35.442 ATOM 4513 N CYS C2442 54.695 19.598 33.306 ATOM 4514 CA CYS C2442 55.621 20.635 32.853 ATOM 4515 C CYS C2442 55.805 21.630 33.975 ATOM 4516 O CYS C2442 54.816 22.183 34.430 ATOM 4517 CB CYS C2442 55.142 21.340 31.558 ATOM 4518 SG CYS C2442 55.086 20.103 30.217 ATOM 4519 HA CYS C2442 56.587 20.175 32.603 ATOM 4520 HBl CYS C2442 54.145 21..782 31.694 ATOM 4521 HB2 CYS C2442 55.846 22..140 31.284 ATOM 4522 HG CYS C2442 54.851 20.718 29.453 ATOM 4523 LPGl CYS C2442 54.608 19.633 30.323 ATOM 4524 LPG2 CYS C2442 55.686 19.799 30.125 ATOM 4525 H CYS C2442 53.724 19.777 33.180 ATOM 4526 N LEU C2443 57.061 21.841 34.441 ATOM 4527 CA LEU C2443 57.315 22.651 35.627 ATOM 4528 C LEU C2443 58.247 23.782 35.275 ATOM 4529 O LEU C2443 59.157 23.563 34.495 ATOM 4530 CB LEU C2443 58.018 21.821 36.734 ATOM 4531 CG LEU C2443 57.230 20.549 37.161 ATOM 4532 CDl LEU C2443 58.118 19.683 38.096 ATOM 4533 CD2 LEU C2443 55.911 20.895 37.903 ATOM 4534 HA LEU C2443 56.378 23.063 36.022 ATOM 4535 HBl LEU C2443 58.998 21.505 36.341 ATOM 4536 HB2 LEU C2443 58.194 22.461 37.615 ATOM 4537 HG LEU C2443 56.985 19.957 36.262 ATOM 4538 HD21 LEU C2443 55.246 21.527 37.301 ATOM 4539 HD22 LEU C2443 55.373 19.962 38.122 ATOM 4540 HD23 LEU C2443 56.130 21.412 38.850 ATOM 4541 HDIl LEU C2443 58.440 20.275 38.964 ATOM 4542 HD12 LEU C2443 57.560 18.809 38.464 ATOM 4543 HD13 LEU C2443 59.017 19.335 37.562 ATOM 4544 H LEU C2443 57.857 21.422 34.007 ATOM 4545 N LEU C2444 58.033 24.981 35.853 ATOM 4546 CA LEU C2444 58.792 26.165 35.445 ATOM 4547 C LEU C2444 60.016 26.350 36.324 ATOM 4548 O LEU C2444 59.806 26.633 37.492 ATOM 4549 CB LEU C2444 57.819 27.369 35.605 ATOM 4550 CG LEU C2444 58.353 28.777 35.220 ATOM 4551 CDl LEU C2444 58.526 28.940 33.684 ATOM 4552 CD2 LEU C2444 57.326 29.820 35.749 ATOM 4553 HA LEU C2444 59.055 26.086 34.382 ATOM 4554 HBl LEU C2444 56.926 27.173 34.997 ATOM 4555 HB2 LEU C2444 57.501 27.407 36.658 ATOM 4556 HG LEU C2444 59.329 28.950 35.707 ATOM 4557 HD21 LEU C2444 57.332 29.837 36.851 ATOM 4558 HD22 LEU C2444 57.556 30.827 35.392 ATOM 4559 HD23 LEU C2444 56.309 29.578 35.406 ATOM 4560 HDIl LEU C2444 57.558 28.826 33.175 ATOM 4561 HD12 LEU C2444 58. .923 29.940 33.453 ATOM 4562 HD13 LEU C2444 59. >29 28.199 33.279 ATOM 4563 H LEU C2444 57.321 25.079 36.549 ATOM 4564 N PRO C2445 61.294 26.209 35.872 ATOM 4565 CA PRO C2445 62.403 26.304 36.806 ATOM 4566 C PRO C2445 62.616 27.672 37.414 ATOM 4567 O PRO C2445 62.419 28.650 36.713 ATOM 4568 CB PRO C2445 63.613 25.825 35.962 ATOM 4569 CG PRO C2445 63.169 25.969 34.485 ATOM 4570 CD PRO C2445 61.623 25.873 34.494 ATOM 4571 HA PRO C2445 62.232 25.558 37.589 ATOM 4572 HD2 PRO C2445 61.203 26.574 33.756 ATOM 4573 HDl PRO C2445 61.303 24.845 34.276 ATOM 4574 HG2 PRO C2445 63.476 26.961 34.115 ATOM 4575 HGl PRO C2445 63.626 25.200 33.838 ATOM 4576 HBl PRO C2445 64.528 26.402 36.180 ATOM 4577 HB2 PRO C2445 63.825 24.761 36.166 ATOM 4578 N LEU C2446 63.048 27.714 38.701 ATOM 4579 CA LEU C2446 63.223 28.967 39.444 ATOM 4580 C LEU C2446 64.466 28.876 40.317 ATOM 4581 O LEU C2446 64.979 27.784 40.508 ATOM 4582 CB LEU C2446 62.025 29.172 40.423 ATOM 4583 CG LEU C2446 60.985 30.278 40.074 ATOM 4584 CDl LEU C2446 61.583 31.707 40.202 ATOM 4585 CD2 LEU C2446 60.315 30.075 38.691 ATOM 4586 HA LEU C2446 63.332 29.825 38.765 ATOM 4587 HBl LEU C2446 61.516 28.207 40.537 ATOM 4588 HB2 LEU C2446 62.392 29.433 41.426 ATOM 4589 HG LEU C2446 60.185 30.205 40.833 ATOM 4590 HD21 LEU C2446 59.942 29.049 38.576 ATOM 4591 HD22 LEU C2446 59.463 30.761 38.600 ATOM 4592 HD23 LEU C2446 61.019 30.285 37.877 ATOM 4593 HDIl LEU C2446 62.290 31.917 39.386 ATOM 4594 HD12 LEU C2446 60.774 32.451 40.170

ATOM 4595 HD13 LEU C2446 62.108 31.829 41.162

ATOM 4596 H LEU C2446 63.222 26.866 39.205

ATOM 4597 N LYS C2447 64.934 30.026 40.869

ATOM 4598 CA LYS C2447 66.033 30.033 41.839

ATOM 4599 C LYS C2447 65.634 30.824 43.076

ATOM 4600 O LYS C2447 64.543 31.373 43.126

ATOM 4601 CB LYS C2447 67.290 30.589 41.108

ATOM 4602 CG LYS C2447 67.842 29.518 40.128

ATOM 4603 CD LYS C2447 69.062 29.956 39.274

ATOM 4604 CE LYS C2447 68.796 31.191 38.371

ATOM 4605 NZ LYS C2447 67.578 31.062 37.537

ATOM 4606 HA LYS C2447 66.218 29.014 42.218

ATOM 4607 HBl LYS C2447 67.001 31.506 40.575

ATOM 4608 HB2 LYS C2447 68.092 30.854 41.813

ATOM 4609 HGl LYS C2447 68.179 28.680 40.749

ATOM 4610 HG2 LYS C2447 67.046 29.150 39.463

ATOM 4611 HDl LYS C2447 69.917 30.171 39.937

ATOM 4612 HD2 LYS C2447 69.344 29.104 38.630

ATOM 4613 HEl LYS C2447 68.725 32.096 38.996

ATOM 4614 HE2 LYS C2447 69.671 31.317 37.710

ATOM 4615 HZl LYS C2447 66.664 31.087 38.113

ATOM 4616 HZ2 LYS C2447 67.508 31.886 36.839

ATOM 4617 HZ3 LYS C2447 67.583 30.149 36.959

ATOM 4618 H LYS C2447 64.531 30.910 40.623

ATOM 4619 N GLU C2448 66.519 30.852 44.102

ATOM 4620 CA GLU C2448 66.191 31.455 45.396

ATOM 4621 C GLU C2448 64.876 30.969 45.963

ATOM 4622 O GLU C2448 63.887 31.672 45.971

ATOM 4623 CB GLU C2448 66.278 33.002 45.289

ATOM 4624 CG GLU C2448 67.717 33.464 44.936

ATOM 4625 CD GLU C2448 67.763 34.960 44.761

ATOM 4626 OEl GLU C2448 67.555 35.433 43.611

ATOM 4627 OE2 GLU C2448 68.008 35.676 45.770

ATOM 4628 HA GLU C2448 66.956 31.137 46.125

ATOM 4629 OT GLU C2448 64.797 29.840 46.422

ATOM 4630 HBl GLU C2448 65.580 33.356 44.514

ATOM 4631 HB2 GLU C2448 65.985 33.456 46.250

ATOM 4632 HGl GLU C2448 68.412 33.170 45.740

ATOM 4633 HG2 GLU C2448 68.055 32.985 44.003

ATOM 4634 H GLU C2448 67.438 30.466 43.995

TER 4635 GLU C2448

CONECT 1 19 20

CONECT 19 1

CONECT 745 744 746 750

CONECT 750 745

CONECT 756 757 765 766

CONECT 765 756

CONECT 1482 1481 1483 1488

CONECT 1488 1482

CONECT 1496 1497 1514 1515

CONECT 1514 1496

CONECT 4621 4620 4622 4629

CONECT 4629 4621

MASTER 0 0 0 0 4632 12 24

END

Claims

1. An isolated keratin-binding polypeptide which comprises an amino acid sequence derived by at least one amino acid substitution from the native sequence of the desmoplakin keratin-binding domain B (KBD-B) as represented by amino acids no. 2250 to 2448 of SEQ ID NO:1 and wherein said at least one amino acid substitution conveys to the polypeptide at least one improved functional and/or structural property in comparison to native isolated KBD-B, or a homologue, functional variant, derivative or fragment of said keratin-binding polypeptide which comprises said at least one amino acid substitution and possesses the keratin-binding properties of said keratin-binding polypeptide.

2. The keratin-binding polypeptide according to claim 1 , which comprises an amino acid sequence derived by at least one amino acid substitution from the native sequence of the desmoplakin keratin-binding domain B (KBD-B) as represented by amino acids no. 2209 to 2448, preferably 2193 to 2481 of SEQ ID NO:1.

3. The keratin-binding polypeptide according to claim 1 or 2, wherein the at least one improved functional and/or structural property is selected from the group consisting of

- increased stability, - improved keratin-binding properties,

- increased load density,

- increased solubility,

- decreased dimer formation,

- increased specifity for hair keratin in comparison to skin keratin, and - increased specifity for skin keratin in comparison to hair keratin.

4. The keratin-binding polypeptide according to any one of claims 1 to 3, wherein at least one position of the at least one amino acid substitution is within one of the following regions: - in the keratin binding interface of KBD-B,

- in a region stabilizing the secondary or tertiary structure of isolated KBD-B,

- at the surface of isolated KBD-B, or

- in a region responsible for the formation of KBD-B dimers in a solvent or during crystallisation.

5. The keratin-binding polypeptide according to any one of claims 1 to 4, which possesses (a) improved keratin-binding properties in comparison to native isolated KBD-B; and/or

(b) increased specifity for hair keratin in comparison to skin keratin.

6. The keratin-binding polypeptide according to any one of claims 1 to 4, which

(a) is able to bind as a monomer to keratin, and/or

(b) is present as a monomer in solution and/or crystalline form.

7. The keratin-binding polypeptide according to claim 5 or 6, wherein the at least one amino acid substitution is located in the keratin-binding interface of KBD-B.

8. The keratin-binding polypeptide according to any one of claims 1 to 7, wherein the maximum number of said amino acid substitions is ten, preferably two.

9. The keratin-binding polypeptide according to any one of claims 1 to 8, wherein said at least one amino acid substitution is selected from the group consisting of

(a) D2407X_a, wherein X_a = any amino acid except D;

(b) E2293X_b, wherein X_b = I, L, V, M, A or F;

(c) E2422X_C, wherein X_c = I, L, V, M, A, F or Y; (d) G2362X_d, wherein X_d =M, I, Q, V, L, F, A or N;

(e) H2363X_e, wherein X_e = any small hydrophobic amino acid, F, K, M, or S;

(f) E2421X_f, wherein X_f = I, M, V, L, F or A;

(g) F2416X_g, wherein X₉ = any hydrophobic acid smaller than F;

(h) L2358X_h, wherein X_h = any aliphatic hydrophobic amino acid except L; (i) Y2339X,, wherein X, = any hydrophobic aromatic amino acid except Y;

C) K2328X_j, wherein X_j = R, S, T or Y; (k) S2331X_k, wherein X_k = R, S, T or Y; (I) R2334X,, wherein X, = R, S, T or Y; (m) R2284X_m, wherein X_m = any basic amino acid except R; and (n) G2286X_n, wherein X_n = any basic amino acid; or a homologue, functional variant, derivative or fragment thereof which comprises said at least one amino acid substitution and possesses the keratin- binding properties of said keratin-binding polypeptide.

10. The keratin-binding polypeptide of claim 9, wherein said said at least one amino acid substitution is selected from the group consisting of

(a) D2407X_a, wherein X_a = any hydophobic amino acid, preferably any hydrophobic aliphatic amino acid, or K or R;

(b) E2293X_b, wherein X_b = any hydrophobic aliphatic amino acid; (c) E2422X_C, wherein X_c = I or F;

(d) G2362X_d, wherein X_d = M, I or Q;

(e) H2363X_e, wherein X₆ = F, A, K, M, V or S; (f) E2421X_f, wherein X_f = I or M;

(g) F2416X_g, wherein X₉ = W; (h) L2358X_h, wherein X_h = I or V; (i) Y2339X,, wherein X, = W; G + k) double substitution K2328X, and S2331X_k, wherein \ _k = R, S, T or Y;

(k + I) double substitution S2331X_k and R2334X,, wherein X _{k J} = R, S, T or Y; and (m + n) double substitution R2284X_m and G2286X_n, wherein X_m, _n = K.

1 1. The keratin-binding polypeptide of claim 9 or 10, wherein said at least one amino acid substitution is selected from the group consisting of

(a) D2407X_a, wherein X_a = A;

(b) E2293X_b, wherein X_b = I; (C) E2422Xc, wherein Xc = I; (d) G2362X_d, wherein X_d = M;

(e) H2363X_e, wherein X₆ = F; and (f) E2421X_f, wherein X_f = I.

12. The keratin-binding polypeptide according to any one of claims 8 to 1 1 , comprising an amino acid sequence selected from the group consisting of SEQ

ID NO:7, SEQ ID NO:10, SEQ ID NO:13, SEQ ID NO:16, SEQ ID NO:19, SEQ ID NO:22, SEQ ID NO:25, SEQ ID NO:28, SEQ ID NO:31 and SEQ ID NO:34.

13. The keratin-binding polypeptide according to any one of claims 1 to 12 which consists of the amino acid sequence as defined in any one of claims 1 to 12.

14. An isolated nucleic acid sequence encoding the keratin-binding polypeptide as defined in any one of claims 1 to 13, or a nucleic acid complementary thereto.

15. The isolated nucleic acid sequence of claim 14 which comprises a sequence selected from the group consisting of the coding regions comprised in the vectors having SEQ ID NO:8, SEQ ID NO:11 , SEQ ID NO:14, SEQ ID NO:17, SEQ ID NO:20, SEQ ID NO:23, SEQ ID NO:26, SEQ ID NO:29, SEQ ID NO:32 and SEQ ID NO:35, its RNA homologue or a nucleic acid sequence complementary thereto.

16. A vector comprising the nucleic acid sequence of claim 15.

17. A cell being transformed or transfected with the vector of claim 16 and/or comprising the nucleic acid of claim 16 and/or being capable of expressing an keratin-binding polypeptide as defined in any one of claims 1 to 13.

18. The polypeptide according to any one of claim 1 to 13 for use as a medicament.

19. The polypeptide according to claim 18 for use in the treatment of hair and/or skin diseases or clinical conditions, preferably for use in the treatment of one or more of the following: hair loss, hair damage, acne, age marks, rash / allergy, atopic dermatitis, basalioma, candidosis, condylomata acuminata, dekubitus, molluscum contagiosum, perioral dermatitis, dermatophyte infections, erysipelas, pediculosis, furuncles, herpes zoster, human papilloma-virus infection, hyperhidrosis, ichthyosis, actinic keratosis, pityriasis versicolor, lichen ruber planus, scabies, herpes labialis, mycosis (especially madura mycosis), rosacea, seborreic rash, sun burn, thrush, vitiligo, diaper dermatitis, infestation with crab lice or hair lice, skin cancer, psoriasis, and wounds.

20. A composition comprising a keratin-binding polypeptide according to any one of claims 1 to 13 or a pharmaceutically or cosmetically acceptable functional variant thereof.

21. The composition of claim 20, which is suitable for the treatment of keratin or keratin-comprising material.

22. The composition according to claim 20 or 21 , wherein the keratin-binding polypeptide acts as

(i) a carrier or shuttle for a further compound; or (ii) as an active ingredient of the composition.

23. The composition according to any one of claims 20 to 22, wherein the keratin- binding polypeptide

(a) is able to bind as a monomer to keratin, and/or

(b) is present as a monomer in solution and/or crystalline form.

24. The composition according to any one of claims 20 to 23, which

(i) is suitable for the treatment of hair and preferably comprises a polypeptide according to any one of claims 1 to 13 with an increased specifity for hair keratin in comparison to skin keratin; or (ii) is suitable for the treatment of skin and preferably comprises a polypeptide according to any one of claims 1 to 13 with an increased specifity for skin keratin in comparison to hair keratin.

25. The composition according to any one of claims 20 to 24, which is a cosmetic or pharmaceutical composition.

26. The composition of claim 25, which is a pharmaceutical composition.

27. The pharmaceutical composition of claim 26, further comprising a pharmaceutically active ingredient.

28. The pharmaceutical composition of claim 26 or 27 for use in the prevention and/or treatment of hair and/or skin diseases or clinical conditions, preferably in the treatment of one or more of the following: hair loss, hair damage, acne, age marks, rash / allergy, atopic dermatitis, basalioma, candidosis, condylomata acuminata, dekubitus, molluscum contagiosum, perioral dermatitis, dermatophyte infections, erysipelas, pediculosis, furuncles, herpes zoster, human papilloma-virus infection, hyperhidrosis, ichthyosis, actinic keratosis, pityriasis versicolor, lichen ruber planus, scabies, herpes labialis, mycosis (especially madura mycosis), rosacea, seborreic rash, sun burn, thrush, vitiligo, diaper dermatitis, infestation with crab lice or hair lice, skin cancer, psoriasis, wound healing and wound treatment.

29. The composition of claim 25, which is a cosmetic composition.

30. The cosmetic composition of claim 29, further comprising a cosmetically active ingredient.

31. The cosmetic composition of claim 29 or 30, which is a hair tonic, hair conditioner, hair dye, skin cleansing lotion, shampoo, body mist, skin tanning lotion, skin whitening lotion or sun cream.

32. Use of the isolated keratin-binding polypeptide as defined in any one of claims 1 to 13 for the treatment of keratin or a keratin-comprising material.

33. The use of claim 32 wherein the keratin-binding polypeptide is linked to a second functional domain.

34. The use according to any one of claims 31 to 32 for

(a) prevention or treatment of diseases or clinical conditions, preferably of the diseases or clinical conditions as defined in claim 28; (b) cosmetic applications, preferably for hair and/or skin application; or

(c) the treatment of inanimate material in vitro, preferably of leather, wool, human hair, animal hair, or horn.

35. A three-dimensional structure model of the rod domain of a keratin coiled coil formed by two keratin monomers (keratin model), comprising an amino acid sequence per monomer strand of at least 30, preferably at least 35, more preferably at least 39 consecutive amino acids of the native rod segment 1 B of said keratin.

36. The keratin model of claim 35, whose backbone heavy atoms lie within a rmsd range of 0 to 3 A, preferably of 0 to 2.5 A, on the corresponding heavy atom coordinates as indicated in table 2 for the 1 B segment of the rod domain of CK8/18.

37. The keratin model of claim 35 or 36, wherein said amino acid sequences start with any of the amino acids of the sixth heptad repeat forming rod segment 1 B and ends with any of the amino acids of the tenth heptad repeat forming rod segment 1 B.

38. The keratin model according to any one of claims 35 to 37, which is a model of the complete rod domain of a hair or skin keratin, preferably a keratin selected from the group consisting of CK8/18, K32/82, K35/82, K39/82, K40/82, K32/85, K35/85, K39/85, K40/85, K5/14 and K1/10.

39. The keratin model according to any one of claims 35 to 38, which comprises the model of the CK8/18 rod domain segment bound by KBD-B, and whose atom coordinates are preferably the coordinates as indicated in table 2 or coordinates deviating therefrom by not more than an rmsd value in the range from 0 to 3 A, preferably from 0 to 2.5 A.

40. The keratin model according to any one of claims 35 to 39, which is a partial or complete model of the CK8/18 rod domain and whose atom coordinates are preferably the coordinates as indicated in table 1 or coordinates deviating therefrom by not more than an rmsd value in the range from 0 to 3 A, preferably from 0 to 2.5 A.

41. The keratin model according to any one of claims 35 to 40, wherein the side chain geometry of the amino acids is adjusted using the internal rotamer library of program SCWRL.

42. Use of the keratin structure model according to any one of claims 35 to 41 for analysing the interaction between said keratin structure and a candidate molecule.

43. A method for evaluating the interaction of a candidate molecule, preferably a candidate keratin-binding polypeptide, with keratin comprising the following steps: (a) selecting a candidate molecule and a keratin; (b) determining the interaction of the candidate molecule with the keratin structure model of embodiment (9) for said keratin by conducting a computer simulation of the interaction between said keratin structure model and a threedimensional model of the candidate molecule, wherein the steric and electrostatic interaction between the candidate molecule and the keratin structure are determined.

44. The method of claim 43, additionally comprising the following step:

(c) analyzing the interaction of the candidate molecule with keratin in vitro or in vivo, preferably in vitro.

45. The method according to any one of claims 43 to 44, wherein the interaction comprises a binding of the candidate molecule to the keratin surface, and/or an intercalation of the candidate molecule into the keratin structure, and/or a disturbance of the keratin structure by the candidate molecule.

46. The method according to any one of claims 43 to 45, which is suitable for identification of keratin-binding polypetides with improved properties in comparison to KBD-B, and wherein the candidate molecule is a putative keratin-binding polypeptide, comprising the following steps:

(a) selecting a putative keratin-binding polypeptide and a keratin;

(b) determining the shape complementarity in a complex of said putative keratin-binding polypeptide with the rod domain of said keratin by conducting a computer simulation of the threedimensional arrangement of (i) the candidate keratin-binding polypeptide and (ii) the rod domain of said keratin;

(c) comparing the result to the result of the corresponding computer simulation of (i) native KBD-B and (ii) said keratin;

(d) determining whether the differences between the putative keratin-binding polypeptide and KBD-B established in the comparison step (c) may lead to to the desired improvement.

47. The method of claim 46, additionally comprising the following steps:

(e) synthesis of the keratin-binding polypeptide amino acid sequence of the putative keratin-binding polypeptide; and/or (f) in vitro testing the structural and functional properties of the keratin-binding polypeptide amino acid sequence of the keratin-binding polypeptide selected in step (d), preferably in comparison to native KBD-B.

48. The method of claim 46 or 47, wherein the putative keratin-binding polypeptide is derived by at least one amino acid exchange from a native keratin-binding domain and preferably comprises an amino acid sequence as defined in any one of claims 1 to 13.

49. The method of claim 48, wherein an initial complex between KBD-B and CK8/18 is modified by introduction of one or more amino acids into the amino acid sequence of KBD-B and wherein steps (a) to (d) are modified as follows: (a) changing at least one amino acid in the native amino acid sequence of KBD-

B as represented by amino acids 2250 to 2448 of SEQ ID NO:1 and selecting the resulting polypeptide as putative keratin-binding polypeptide;

(b) fitting the changed amino acid(s) into the existing threedimensional structure of KBD-B as defined by the interaction model with the KBD-B coordinates provided in table 4, subsequently establishing its interaction with the CK8/18 keratin rod domain with the coordinates provided in table 4, and finally adjusting the orientation of the changed amino acid residues;

(c) comparing the result to the initial complex formed by KBD-B and CK8/18;

(d) determining the steric, lipophilic and/or electrostatic effects the amino acid exchange has onto the complex geometry and the interaction between polypeptide and keratin and determining whether the differences between the keratin-binding polypeptide derived from KBD-B and the native KBD-B may lead to to the desired improvement.

50. A method for preparing the polypeptide according to any one of claims 1 to 13 or the polypeptide resulting from the method of any one of claims 46 to 49.

51. The preparation method of claim 50 which comprises using the vector of claim 16 and/or the cell of claim 17.

52. The preparation method of any one of claims 50 to 51 comprising as additional steps the steps defined in any one of claims 46 to 49.