data_8RGF
# 
_entry.id   8RGF 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.399 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   8RGF         pdb_00008rgf 10.2210/pdb8rgf/pdb 
WWPDB D_1292135363 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2024-12-04 
2 'Structure model' 1 1 2024-12-25 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.journal_volume'          
2 2 'Structure model' '_citation.page_first'              
3 2 'Structure model' '_citation.page_last'               
4 2 'Structure model' '_citation_author.identifier_ORCID' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8RGF 
_pdbx_database_status.recvd_initial_deposition_date   2023-12-13 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              jens.petersen@astrazeneca.com 
_pdbx_contact_author.name_first         Jens 
_pdbx_contact_author.name_last          Petersen 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-5946-4756 
# 
_audit_author.name               'Petersen, J.' 
_audit_author.pdbx_ordinal       1 
_audit_author.identifier_ORCID   ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            J.Med.Chem. 
_citation.journal_id_ASTM           JMCMAR 
_citation.journal_id_CSD            0151 
_citation.journal_id_ISSN           0022-2623 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            67 
_citation.language                  ? 
_citation.page_first                20827 
_citation.page_last                 20841 
_citation.title                     
;Discovery of (2 R ,4 R )-4-(( S )-2-Amino-3-methylbutanamido)-2-(4-boronobutyl)pyrrolidine-2-carboxylic Acid (AZD0011), an Actively Transported Prodrug of a Potent Arginase Inhibitor to Treat Cancer.
;
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/acs.jmedchem.4c02309 
_citation.pdbx_database_id_PubMed   39572889 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Mlynarski, S.N.' 1  ? 
primary 'Aquila, B.M.'    2  ? 
primary 'Cantin, S.'      3  ? 
primary 'Cook, S.'        4  ? 
primary 'Doshi, A.'       5  ? 
primary 'Finlay, M.R.V.'  6  ? 
primary 'Gangl, E.T.'     7  ? 
primary 'Grebe, T.'       8  ? 
primary 'Gu, C.'          9  ? 
primary 'Kawatkar, S.P.'  10 ? 
primary 'Petersen, J.'    11 ? 
primary 'Pop-Damkov, P.'  12 ? 
primary 'Schuller, A.G.'  13 ? 
primary 'Shao, W.'        14 ? 
primary 'Shields, J.D.'   15 ? 
primary 'Simpson, I.'     16 ? 
primary 'Tavakoli, S.'    17 ? 
primary 'Tentarelli, S.'  18 ? 
primary 'Throner, S.'     19 ? 
primary 'Wang, H.'        20 ? 
primary 'Wang, J.'        21 ? 
primary 'Wu, D.'          22 ? 
primary 'Ye, Q.'          23 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Arginase-2, mitochondrial'                                                         36522.172 3   3.5.3.1 ? ? ? 
2 non-polymer syn 'MANGANESE (II) ION'                                                                54.938    6   ?       ? ? ? 
3 non-polymer syn '4-[(2~{R},4~{R})-4-azanyl-2-carboxy-pyrrolidin-2-yl]butyl-tris(oxidanyl)boranuide' 247.076   2   ?       ? ? ? 
4 water       nat water                                                                               18.015    267 ?       ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Arginase II,Kidney-type arginase,Non-hepatic arginase,Type II arginase' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;HHHHHHGGGENLYFQSVHSVAVIGAPFSQGQKRKGVEHGPAAIREAGLMKRLSSLGCHLKDFGDLSFTPVPKDDLYNNLI
VNPRSVGLANQELAEVVSRAVSDGYSCVTLGGDHSLAIGTISGHARHCPDLCVVWVDAHADINTPLTTSSGNLHGQPVSF
LLRELQDKVPQLPGFSWIKPCISSASIVYIGLRDVDPPEHFILKNYDIQYFSMRDIDRLGIQKVMERTFDLLIGKRQRPI
HLSFDIDAFDPTLAPATGTPVVGGLTYREGMYIAEEIHNTGLLSALDLVEVNPQLATSEEEAKTTANLAVDVIASSFGQT
REGGHIVYDQLPTPS
;
_entity_poly.pdbx_seq_one_letter_code_can   
;HHHHHHGGGENLYFQSVHSVAVIGAPFSQGQKRKGVEHGPAAIREAGLMKRLSSLGCHLKDFGDLSFTPVPKDDLYNNLI
VNPRSVGLANQELAEVVSRAVSDGYSCVTLGGDHSLAIGTISGHARHCPDLCVVWVDAHADINTPLTTSSGNLHGQPVSF
LLRELQDKVPQLPGFSWIKPCISSASIVYIGLRDVDPPEHFILKNYDIQYFSMRDIDRLGIQKVMERTFDLLIGKRQRPI
HLSFDIDAFDPTLAPATGTPVVGGLTYREGMYIAEEIHNTGLLSALDLVEVNPQLATSEEEAKTTANLAVDVIASSFGQT
REGGHIVYDQLPTPS
;
_entity_poly.pdbx_strand_id                 A,B,C 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'MANGANESE (II) ION'                                                                MN    
3 '4-[(2~{R},4~{R})-4-azanyl-2-carboxy-pyrrolidin-2-yl]butyl-tris(oxidanyl)boranuide' A1H0A 
4 water                                                                               HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   HIS n 
1 2   HIS n 
1 3   HIS n 
1 4   HIS n 
1 5   HIS n 
1 6   HIS n 
1 7   GLY n 
1 8   GLY n 
1 9   GLY n 
1 10  GLU n 
1 11  ASN n 
1 12  LEU n 
1 13  TYR n 
1 14  PHE n 
1 15  GLN n 
1 16  SER n 
1 17  VAL n 
1 18  HIS n 
1 19  SER n 
1 20  VAL n 
1 21  ALA n 
1 22  VAL n 
1 23  ILE n 
1 24  GLY n 
1 25  ALA n 
1 26  PRO n 
1 27  PHE n 
1 28  SER n 
1 29  GLN n 
1 30  GLY n 
1 31  GLN n 
1 32  LYS n 
1 33  ARG n 
1 34  LYS n 
1 35  GLY n 
1 36  VAL n 
1 37  GLU n 
1 38  HIS n 
1 39  GLY n 
1 40  PRO n 
1 41  ALA n 
1 42  ALA n 
1 43  ILE n 
1 44  ARG n 
1 45  GLU n 
1 46  ALA n 
1 47  GLY n 
1 48  LEU n 
1 49  MET n 
1 50  LYS n 
1 51  ARG n 
1 52  LEU n 
1 53  SER n 
1 54  SER n 
1 55  LEU n 
1 56  GLY n 
1 57  CYS n 
1 58  HIS n 
1 59  LEU n 
1 60  LYS n 
1 61  ASP n 
1 62  PHE n 
1 63  GLY n 
1 64  ASP n 
1 65  LEU n 
1 66  SER n 
1 67  PHE n 
1 68  THR n 
1 69  PRO n 
1 70  VAL n 
1 71  PRO n 
1 72  LYS n 
1 73  ASP n 
1 74  ASP n 
1 75  LEU n 
1 76  TYR n 
1 77  ASN n 
1 78  ASN n 
1 79  LEU n 
1 80  ILE n 
1 81  VAL n 
1 82  ASN n 
1 83  PRO n 
1 84  ARG n 
1 85  SER n 
1 86  VAL n 
1 87  GLY n 
1 88  LEU n 
1 89  ALA n 
1 90  ASN n 
1 91  GLN n 
1 92  GLU n 
1 93  LEU n 
1 94  ALA n 
1 95  GLU n 
1 96  VAL n 
1 97  VAL n 
1 98  SER n 
1 99  ARG n 
1 100 ALA n 
1 101 VAL n 
1 102 SER n 
1 103 ASP n 
1 104 GLY n 
1 105 TYR n 
1 106 SER n 
1 107 CYS n 
1 108 VAL n 
1 109 THR n 
1 110 LEU n 
1 111 GLY n 
1 112 GLY n 
1 113 ASP n 
1 114 HIS n 
1 115 SER n 
1 116 LEU n 
1 117 ALA n 
1 118 ILE n 
1 119 GLY n 
1 120 THR n 
1 121 ILE n 
1 122 SER n 
1 123 GLY n 
1 124 HIS n 
1 125 ALA n 
1 126 ARG n 
1 127 HIS n 
1 128 CYS n 
1 129 PRO n 
1 130 ASP n 
1 131 LEU n 
1 132 CYS n 
1 133 VAL n 
1 134 VAL n 
1 135 TRP n 
1 136 VAL n 
1 137 ASP n 
1 138 ALA n 
1 139 HIS n 
1 140 ALA n 
1 141 ASP n 
1 142 ILE n 
1 143 ASN n 
1 144 THR n 
1 145 PRO n 
1 146 LEU n 
1 147 THR n 
1 148 THR n 
1 149 SER n 
1 150 SER n 
1 151 GLY n 
1 152 ASN n 
1 153 LEU n 
1 154 HIS n 
1 155 GLY n 
1 156 GLN n 
1 157 PRO n 
1 158 VAL n 
1 159 SER n 
1 160 PHE n 
1 161 LEU n 
1 162 LEU n 
1 163 ARG n 
1 164 GLU n 
1 165 LEU n 
1 166 GLN n 
1 167 ASP n 
1 168 LYS n 
1 169 VAL n 
1 170 PRO n 
1 171 GLN n 
1 172 LEU n 
1 173 PRO n 
1 174 GLY n 
1 175 PHE n 
1 176 SER n 
1 177 TRP n 
1 178 ILE n 
1 179 LYS n 
1 180 PRO n 
1 181 CYS n 
1 182 ILE n 
1 183 SER n 
1 184 SER n 
1 185 ALA n 
1 186 SER n 
1 187 ILE n 
1 188 VAL n 
1 189 TYR n 
1 190 ILE n 
1 191 GLY n 
1 192 LEU n 
1 193 ARG n 
1 194 ASP n 
1 195 VAL n 
1 196 ASP n 
1 197 PRO n 
1 198 PRO n 
1 199 GLU n 
1 200 HIS n 
1 201 PHE n 
1 202 ILE n 
1 203 LEU n 
1 204 LYS n 
1 205 ASN n 
1 206 TYR n 
1 207 ASP n 
1 208 ILE n 
1 209 GLN n 
1 210 TYR n 
1 211 PHE n 
1 212 SER n 
1 213 MET n 
1 214 ARG n 
1 215 ASP n 
1 216 ILE n 
1 217 ASP n 
1 218 ARG n 
1 219 LEU n 
1 220 GLY n 
1 221 ILE n 
1 222 GLN n 
1 223 LYS n 
1 224 VAL n 
1 225 MET n 
1 226 GLU n 
1 227 ARG n 
1 228 THR n 
1 229 PHE n 
1 230 ASP n 
1 231 LEU n 
1 232 LEU n 
1 233 ILE n 
1 234 GLY n 
1 235 LYS n 
1 236 ARG n 
1 237 GLN n 
1 238 ARG n 
1 239 PRO n 
1 240 ILE n 
1 241 HIS n 
1 242 LEU n 
1 243 SER n 
1 244 PHE n 
1 245 ASP n 
1 246 ILE n 
1 247 ASP n 
1 248 ALA n 
1 249 PHE n 
1 250 ASP n 
1 251 PRO n 
1 252 THR n 
1 253 LEU n 
1 254 ALA n 
1 255 PRO n 
1 256 ALA n 
1 257 THR n 
1 258 GLY n 
1 259 THR n 
1 260 PRO n 
1 261 VAL n 
1 262 VAL n 
1 263 GLY n 
1 264 GLY n 
1 265 LEU n 
1 266 THR n 
1 267 TYR n 
1 268 ARG n 
1 269 GLU n 
1 270 GLY n 
1 271 MET n 
1 272 TYR n 
1 273 ILE n 
1 274 ALA n 
1 275 GLU n 
1 276 GLU n 
1 277 ILE n 
1 278 HIS n 
1 279 ASN n 
1 280 THR n 
1 281 GLY n 
1 282 LEU n 
1 283 LEU n 
1 284 SER n 
1 285 ALA n 
1 286 LEU n 
1 287 ASP n 
1 288 LEU n 
1 289 VAL n 
1 290 GLU n 
1 291 VAL n 
1 292 ASN n 
1 293 PRO n 
1 294 GLN n 
1 295 LEU n 
1 296 ALA n 
1 297 THR n 
1 298 SER n 
1 299 GLU n 
1 300 GLU n 
1 301 GLU n 
1 302 ALA n 
1 303 LYS n 
1 304 THR n 
1 305 THR n 
1 306 ALA n 
1 307 ASN n 
1 308 LEU n 
1 309 ALA n 
1 310 VAL n 
1 311 ASP n 
1 312 VAL n 
1 313 ILE n 
1 314 ALA n 
1 315 SER n 
1 316 SER n 
1 317 PHE n 
1 318 GLY n 
1 319 GLN n 
1 320 THR n 
1 321 ARG n 
1 322 GLU n 
1 323 GLY n 
1 324 GLY n 
1 325 HIS n 
1 326 ILE n 
1 327 VAL n 
1 328 TYR n 
1 329 ASP n 
1 330 GLN n 
1 331 LEU n 
1 332 PRO n 
1 333 THR n 
1 334 PRO n 
1 335 SER n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   335 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ARG2 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1H0A non-polymer         . '4-[(2~{R},4~{R})-4-azanyl-2-carboxy-pyrrolidin-2-yl]butyl-tris(oxidanyl)boranuide' ? 
'C9 H20 B N2 O5 -1' 247.076 
ALA   'L-peptide linking' y ALANINE                                                                             ? 'C3 H7 N O2' 
89.093  
ARG   'L-peptide linking' y ARGININE                                                                            ? 'C6 H15 N4 O2 1' 
175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                                          ? 'C4 H8 N2 O3' 
132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                                     ? 'C4 H7 N O4' 
133.103 
CYS   'L-peptide linking' y CYSTEINE                                                                            ? 'C3 H7 N O2 S' 
121.158 
GLN   'L-peptide linking' y GLUTAMINE                                                                           ? 'C5 H10 N2 O3' 
146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                                     ? 'C5 H9 N O4' 
147.129 
GLY   'peptide linking'   y GLYCINE                                                                             ? 'C2 H5 N O2' 
75.067  
HIS   'L-peptide linking' y HISTIDINE                                                                           ? 'C6 H10 N3 O2 1' 
156.162 
HOH   non-polymer         . WATER                                                                               ? 'H2 O' 18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                                          ? 'C6 H13 N O2' 
131.173 
LEU   'L-peptide linking' y LEUCINE                                                                             ? 'C6 H13 N O2' 
131.173 
LYS   'L-peptide linking' y LYSINE                                                                              ? 'C6 H15 N2 O2 1' 
147.195 
MET   'L-peptide linking' y METHIONINE                                                                          ? 'C5 H11 N O2 S' 
149.211 
MN    non-polymer         . 'MANGANESE (II) ION'                                                                ? 'Mn 2' 54.938  
PHE   'L-peptide linking' y PHENYLALANINE                                                                       ? 'C9 H11 N O2' 
165.189 
PRO   'L-peptide linking' y PROLINE                                                                             ? 'C5 H9 N O2' 
115.130 
SER   'L-peptide linking' y SERINE                                                                              ? 'C3 H7 N O3' 
105.093 
THR   'L-peptide linking' y THREONINE                                                                           ? 'C4 H9 N O3' 
119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                                                          ? 'C11 H12 N2 O2' 
204.225 
TYR   'L-peptide linking' y TYROSINE                                                                            ? 'C9 H11 N O3' 
181.189 
VAL   'L-peptide linking' y VALINE                                                                              ? 'C5 H11 N O2' 
117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   HIS 1   7   ?   ?   ?   A . n 
A 1 2   HIS 2   8   ?   ?   ?   A . n 
A 1 3   HIS 3   9   ?   ?   ?   A . n 
A 1 4   HIS 4   10  ?   ?   ?   A . n 
A 1 5   HIS 5   11  ?   ?   ?   A . n 
A 1 6   HIS 6   12  ?   ?   ?   A . n 
A 1 7   GLY 7   13  ?   ?   ?   A . n 
A 1 8   GLY 8   14  ?   ?   ?   A . n 
A 1 9   GLY 9   15  ?   ?   ?   A . n 
A 1 10  GLU 10  16  ?   ?   ?   A . n 
A 1 11  ASN 11  17  ?   ?   ?   A . n 
A 1 12  LEU 12  18  ?   ?   ?   A . n 
A 1 13  TYR 13  19  ?   ?   ?   A . n 
A 1 14  PHE 14  20  ?   ?   ?   A . n 
A 1 15  GLN 15  21  ?   ?   ?   A . n 
A 1 16  SER 16  22  ?   ?   ?   A . n 
A 1 17  VAL 17  23  23  VAL VAL A . n 
A 1 18  HIS 18  24  24  HIS HIS A . n 
A 1 19  SER 19  25  25  SER SER A . n 
A 1 20  VAL 20  26  26  VAL VAL A . n 
A 1 21  ALA 21  27  27  ALA ALA A . n 
A 1 22  VAL 22  28  28  VAL VAL A . n 
A 1 23  ILE 23  29  29  ILE ILE A . n 
A 1 24  GLY 24  30  30  GLY GLY A . n 
A 1 25  ALA 25  31  31  ALA ALA A . n 
A 1 26  PRO 26  32  32  PRO PRO A . n 
A 1 27  PHE 27  33  33  PHE PHE A . n 
A 1 28  SER 28  34  34  SER SER A . n 
A 1 29  GLN 29  35  35  GLN GLN A . n 
A 1 30  GLY 30  36  36  GLY GLY A . n 
A 1 31  GLN 31  37  37  GLN GLN A . n 
A 1 32  LYS 32  38  38  LYS LYS A . n 
A 1 33  ARG 33  39  39  ARG ARG A . n 
A 1 34  LYS 34  40  40  LYS LYS A . n 
A 1 35  GLY 35  41  41  GLY GLY A . n 
A 1 36  VAL 36  42  42  VAL VAL A . n 
A 1 37  GLU 37  43  43  GLU GLU A . n 
A 1 38  HIS 38  44  44  HIS HIS A . n 
A 1 39  GLY 39  45  45  GLY GLY A . n 
A 1 40  PRO 40  46  46  PRO PRO A . n 
A 1 41  ALA 41  47  47  ALA ALA A . n 
A 1 42  ALA 42  48  48  ALA ALA A . n 
A 1 43  ILE 43  49  49  ILE ILE A . n 
A 1 44  ARG 44  50  50  ARG ARG A . n 
A 1 45  GLU 45  51  51  GLU GLU A . n 
A 1 46  ALA 46  52  52  ALA ALA A . n 
A 1 47  GLY 47  53  53  GLY GLY A . n 
A 1 48  LEU 48  54  54  LEU LEU A . n 
A 1 49  MET 49  55  55  MET MET A . n 
A 1 50  LYS 50  56  56  LYS LYS A . n 
A 1 51  ARG 51  57  57  ARG ARG A . n 
A 1 52  LEU 52  58  58  LEU LEU A . n 
A 1 53  SER 53  59  59  SER SER A . n 
A 1 54  SER 54  60  60  SER SER A . n 
A 1 55  LEU 55  61  61  LEU LEU A . n 
A 1 56  GLY 56  62  62  GLY GLY A . n 
A 1 57  CYS 57  63  63  CYS CYS A . n 
A 1 58  HIS 58  64  64  HIS HIS A . n 
A 1 59  LEU 59  65  65  LEU LEU A . n 
A 1 60  LYS 60  66  66  LYS LYS A . n 
A 1 61  ASP 61  67  67  ASP ASP A . n 
A 1 62  PHE 62  68  68  PHE PHE A . n 
A 1 63  GLY 63  69  69  GLY GLY A . n 
A 1 64  ASP 64  70  70  ASP ASP A . n 
A 1 65  LEU 65  71  71  LEU LEU A . n 
A 1 66  SER 66  72  72  SER SER A . n 
A 1 67  PHE 67  73  73  PHE PHE A . n 
A 1 68  THR 68  74  74  THR THR A . n 
A 1 69  PRO 69  75  75  PRO PRO A . n 
A 1 70  VAL 70  76  76  VAL VAL A . n 
A 1 71  PRO 71  77  77  PRO PRO A . n 
A 1 72  LYS 72  78  78  LYS LYS A . n 
A 1 73  ASP 73  79  79  ASP ASP A . n 
A 1 74  ASP 74  80  80  ASP ASP A . n 
A 1 75  LEU 75  81  81  LEU LEU A . n 
A 1 76  TYR 76  82  82  TYR TYR A . n 
A 1 77  ASN 77  83  83  ASN ASN A . n 
A 1 78  ASN 78  84  84  ASN ASN A . n 
A 1 79  LEU 79  85  85  LEU LEU A . n 
A 1 80  ILE 80  86  86  ILE ILE A . n 
A 1 81  VAL 81  87  87  VAL VAL A . n 
A 1 82  ASN 82  88  88  ASN ASN A . n 
A 1 83  PRO 83  89  89  PRO PRO A . n 
A 1 84  ARG 84  90  90  ARG ARG A . n 
A 1 85  SER 85  91  91  SER SER A . n 
A 1 86  VAL 86  92  92  VAL VAL A . n 
A 1 87  GLY 87  93  93  GLY GLY A . n 
A 1 88  LEU 88  94  94  LEU LEU A . n 
A 1 89  ALA 89  95  95  ALA ALA A . n 
A 1 90  ASN 90  96  96  ASN ASN A . n 
A 1 91  GLN 91  97  97  GLN GLN A . n 
A 1 92  GLU 92  98  98  GLU GLU A . n 
A 1 93  LEU 93  99  99  LEU LEU A . n 
A 1 94  ALA 94  100 100 ALA ALA A . n 
A 1 95  GLU 95  101 101 GLU GLU A . n 
A 1 96  VAL 96  102 102 VAL VAL A . n 
A 1 97  VAL 97  103 103 VAL VAL A . n 
A 1 98  SER 98  104 104 SER SER A . n 
A 1 99  ARG 99  105 105 ARG ARG A . n 
A 1 100 ALA 100 106 106 ALA ALA A . n 
A 1 101 VAL 101 107 107 VAL VAL A . n 
A 1 102 SER 102 108 108 SER SER A . n 
A 1 103 ASP 103 109 109 ASP ASP A . n 
A 1 104 GLY 104 110 110 GLY GLY A . n 
A 1 105 TYR 105 111 111 TYR TYR A . n 
A 1 106 SER 106 112 112 SER SER A . n 
A 1 107 CYS 107 113 113 CYS CYS A . n 
A 1 108 VAL 108 114 114 VAL VAL A . n 
A 1 109 THR 109 115 115 THR THR A . n 
A 1 110 LEU 110 116 116 LEU LEU A . n 
A 1 111 GLY 111 117 117 GLY GLY A . n 
A 1 112 GLY 112 118 118 GLY GLY A . n 
A 1 113 ASP 113 119 119 ASP ASP A . n 
A 1 114 HIS 114 120 120 HIS HIS A . n 
A 1 115 SER 115 121 121 SER SER A . n 
A 1 116 LEU 116 122 122 LEU LEU A . n 
A 1 117 ALA 117 123 123 ALA ALA A . n 
A 1 118 ILE 118 124 124 ILE ILE A . n 
A 1 119 GLY 119 125 125 GLY GLY A . n 
A 1 120 THR 120 126 126 THR THR A . n 
A 1 121 ILE 121 127 127 ILE ILE A . n 
A 1 122 SER 122 128 128 SER SER A . n 
A 1 123 GLY 123 129 129 GLY GLY A . n 
A 1 124 HIS 124 130 130 HIS HIS A . n 
A 1 125 ALA 125 131 131 ALA ALA A . n 
A 1 126 ARG 126 132 132 ARG ARG A . n 
A 1 127 HIS 127 133 133 HIS HIS A . n 
A 1 128 CYS 128 134 134 CYS CYS A . n 
A 1 129 PRO 129 135 135 PRO PRO A . n 
A 1 130 ASP 130 136 136 ASP ASP A . n 
A 1 131 LEU 131 137 137 LEU LEU A . n 
A 1 132 CYS 132 138 138 CYS CYS A . n 
A 1 133 VAL 133 139 139 VAL VAL A . n 
A 1 134 VAL 134 140 140 VAL VAL A . n 
A 1 135 TRP 135 141 141 TRP TRP A . n 
A 1 136 VAL 136 142 142 VAL VAL A . n 
A 1 137 ASP 137 143 143 ASP ASP A . n 
A 1 138 ALA 138 144 144 ALA ALA A . n 
A 1 139 HIS 139 145 145 HIS HIS A . n 
A 1 140 ALA 140 146 146 ALA ALA A . n 
A 1 141 ASP 141 147 147 ASP ASP A . n 
A 1 142 ILE 142 148 148 ILE ILE A . n 
A 1 143 ASN 143 149 149 ASN ASN A . n 
A 1 144 THR 144 150 150 THR THR A . n 
A 1 145 PRO 145 151 151 PRO PRO A . n 
A 1 146 LEU 146 152 152 LEU LEU A . n 
A 1 147 THR 147 153 153 THR THR A . n 
A 1 148 THR 148 154 154 THR THR A . n 
A 1 149 SER 149 155 155 SER SER A . n 
A 1 150 SER 150 156 156 SER SER A . n 
A 1 151 GLY 151 157 157 GLY GLY A . n 
A 1 152 ASN 152 158 158 ASN ASN A . n 
A 1 153 LEU 153 159 159 LEU LEU A . n 
A 1 154 HIS 154 160 160 HIS HIS A . n 
A 1 155 GLY 155 161 161 GLY GLY A . n 
A 1 156 GLN 156 162 162 GLN GLN A . n 
A 1 157 PRO 157 163 163 PRO PRO A . n 
A 1 158 VAL 158 164 164 VAL VAL A . n 
A 1 159 SER 159 165 165 SER SER A . n 
A 1 160 PHE 160 166 166 PHE PHE A . n 
A 1 161 LEU 161 167 167 LEU LEU A . n 
A 1 162 LEU 162 168 168 LEU LEU A . n 
A 1 163 ARG 163 169 169 ARG ARG A . n 
A 1 164 GLU 164 170 170 GLU GLU A . n 
A 1 165 LEU 165 171 171 LEU LEU A . n 
A 1 166 GLN 166 172 172 GLN GLN A . n 
A 1 167 ASP 167 173 173 ASP ASP A . n 
A 1 168 LYS 168 174 174 LYS LYS A . n 
A 1 169 VAL 169 175 175 VAL VAL A . n 
A 1 170 PRO 170 176 176 PRO PRO A . n 
A 1 171 GLN 171 177 177 GLN GLN A . n 
A 1 172 LEU 172 178 178 LEU LEU A . n 
A 1 173 PRO 173 179 179 PRO PRO A . n 
A 1 174 GLY 174 180 180 GLY GLY A . n 
A 1 175 PHE 175 181 181 PHE PHE A . n 
A 1 176 SER 176 182 182 SER SER A . n 
A 1 177 TRP 177 183 183 TRP TRP A . n 
A 1 178 ILE 178 184 184 ILE ILE A . n 
A 1 179 LYS 179 185 185 LYS LYS A . n 
A 1 180 PRO 180 186 186 PRO PRO A . n 
A 1 181 CYS 181 187 187 CYS CYS A . n 
A 1 182 ILE 182 188 188 ILE ILE A . n 
A 1 183 SER 183 189 189 SER SER A . n 
A 1 184 SER 184 190 190 SER SER A . n 
A 1 185 ALA 185 191 191 ALA ALA A . n 
A 1 186 SER 186 192 192 SER SER A . n 
A 1 187 ILE 187 193 193 ILE ILE A . n 
A 1 188 VAL 188 194 194 VAL VAL A . n 
A 1 189 TYR 189 195 195 TYR TYR A . n 
A 1 190 ILE 190 196 196 ILE ILE A . n 
A 1 191 GLY 191 197 197 GLY GLY A . n 
A 1 192 LEU 192 198 198 LEU LEU A . n 
A 1 193 ARG 193 199 199 ARG ARG A . n 
A 1 194 ASP 194 200 200 ASP ASP A . n 
A 1 195 VAL 195 201 201 VAL VAL A . n 
A 1 196 ASP 196 202 202 ASP ASP A . n 
A 1 197 PRO 197 203 203 PRO PRO A . n 
A 1 198 PRO 198 204 204 PRO PRO A . n 
A 1 199 GLU 199 205 205 GLU GLU A . n 
A 1 200 HIS 200 206 206 HIS HIS A . n 
A 1 201 PHE 201 207 207 PHE PHE A . n 
A 1 202 ILE 202 208 208 ILE ILE A . n 
A 1 203 LEU 203 209 209 LEU LEU A . n 
A 1 204 LYS 204 210 210 LYS LYS A . n 
A 1 205 ASN 205 211 211 ASN ASN A . n 
A 1 206 TYR 206 212 212 TYR TYR A . n 
A 1 207 ASP 207 213 213 ASP ASP A . n 
A 1 208 ILE 208 214 214 ILE ILE A . n 
A 1 209 GLN 209 215 215 GLN GLN A . n 
A 1 210 TYR 210 216 216 TYR TYR A . n 
A 1 211 PHE 211 217 217 PHE PHE A . n 
A 1 212 SER 212 218 218 SER SER A . n 
A 1 213 MET 213 219 219 MET MET A . n 
A 1 214 ARG 214 220 220 ARG ARG A . n 
A 1 215 ASP 215 221 221 ASP ASP A . n 
A 1 216 ILE 216 222 222 ILE ILE A . n 
A 1 217 ASP 217 223 223 ASP ASP A . n 
A 1 218 ARG 218 224 224 ARG ARG A . n 
A 1 219 LEU 219 225 225 LEU LEU A . n 
A 1 220 GLY 220 226 226 GLY GLY A . n 
A 1 221 ILE 221 227 227 ILE ILE A . n 
A 1 222 GLN 222 228 228 GLN GLN A . n 
A 1 223 LYS 223 229 229 LYS LYS A . n 
A 1 224 VAL 224 230 230 VAL VAL A . n 
A 1 225 MET 225 231 231 MET MET A . n 
A 1 226 GLU 226 232 232 GLU GLU A . n 
A 1 227 ARG 227 233 233 ARG ARG A . n 
A 1 228 THR 228 234 234 THR THR A . n 
A 1 229 PHE 229 235 235 PHE PHE A . n 
A 1 230 ASP 230 236 236 ASP ASP A . n 
A 1 231 LEU 231 237 237 LEU LEU A . n 
A 1 232 LEU 232 238 238 LEU LEU A . n 
A 1 233 ILE 233 239 239 ILE ILE A . n 
A 1 234 GLY 234 240 240 GLY GLY A . n 
A 1 235 LYS 235 241 241 LYS LYS A . n 
A 1 236 ARG 236 242 242 ARG ARG A . n 
A 1 237 GLN 237 243 243 GLN GLN A . n 
A 1 238 ARG 238 244 244 ARG ARG A . n 
A 1 239 PRO 239 245 245 PRO PRO A . n 
A 1 240 ILE 240 246 246 ILE ILE A . n 
A 1 241 HIS 241 247 247 HIS HIS A . n 
A 1 242 LEU 242 248 248 LEU LEU A . n 
A 1 243 SER 243 249 249 SER SER A . n 
A 1 244 PHE 244 250 250 PHE PHE A . n 
A 1 245 ASP 245 251 251 ASP ASP A . n 
A 1 246 ILE 246 252 252 ILE ILE A . n 
A 1 247 ASP 247 253 253 ASP ASP A . n 
A 1 248 ALA 248 254 254 ALA ALA A . n 
A 1 249 PHE 249 255 255 PHE PHE A . n 
A 1 250 ASP 250 256 256 ASP ASP A . n 
A 1 251 PRO 251 257 257 PRO PRO A . n 
A 1 252 THR 252 258 258 THR THR A . n 
A 1 253 LEU 253 259 259 LEU LEU A . n 
A 1 254 ALA 254 260 260 ALA ALA A . n 
A 1 255 PRO 255 261 261 PRO PRO A . n 
A 1 256 ALA 256 262 262 ALA ALA A . n 
A 1 257 THR 257 263 263 THR THR A . n 
A 1 258 GLY 258 264 264 GLY GLY A . n 
A 1 259 THR 259 265 265 THR THR A . n 
A 1 260 PRO 260 266 266 PRO PRO A . n 
A 1 261 VAL 261 267 267 VAL VAL A . n 
A 1 262 VAL 262 268 268 VAL VAL A . n 
A 1 263 GLY 263 269 269 GLY GLY A . n 
A 1 264 GLY 264 270 270 GLY GLY A . n 
A 1 265 LEU 265 271 271 LEU LEU A . n 
A 1 266 THR 266 272 272 THR THR A . n 
A 1 267 TYR 267 273 273 TYR TYR A . n 
A 1 268 ARG 268 274 274 ARG ARG A . n 
A 1 269 GLU 269 275 275 GLU GLU A . n 
A 1 270 GLY 270 276 276 GLY GLY A . n 
A 1 271 MET 271 277 277 MET MET A . n 
A 1 272 TYR 272 278 278 TYR TYR A . n 
A 1 273 ILE 273 279 279 ILE ILE A . n 
A 1 274 ALA 274 280 280 ALA ALA A . n 
A 1 275 GLU 275 281 281 GLU GLU A . n 
A 1 276 GLU 276 282 282 GLU GLU A . n 
A 1 277 ILE 277 283 283 ILE ILE A . n 
A 1 278 HIS 278 284 284 HIS HIS A . n 
A 1 279 ASN 279 285 285 ASN ASN A . n 
A 1 280 THR 280 286 286 THR THR A . n 
A 1 281 GLY 281 287 287 GLY GLY A . n 
A 1 282 LEU 282 288 288 LEU LEU A . n 
A 1 283 LEU 283 289 289 LEU LEU A . n 
A 1 284 SER 284 290 290 SER SER A . n 
A 1 285 ALA 285 291 291 ALA ALA A . n 
A 1 286 LEU 286 292 292 LEU LEU A . n 
A 1 287 ASP 287 293 293 ASP ASP A . n 
A 1 288 LEU 288 294 294 LEU LEU A . n 
A 1 289 VAL 289 295 295 VAL VAL A . n 
A 1 290 GLU 290 296 296 GLU GLU A . n 
A 1 291 VAL 291 297 297 VAL VAL A . n 
A 1 292 ASN 292 298 298 ASN ASN A . n 
A 1 293 PRO 293 299 299 PRO PRO A . n 
A 1 294 GLN 294 300 300 GLN GLN A . n 
A 1 295 LEU 295 301 301 LEU LEU A . n 
A 1 296 ALA 296 302 302 ALA ALA A . n 
A 1 297 THR 297 303 303 THR THR A . n 
A 1 298 SER 298 304 304 SER SER A . n 
A 1 299 GLU 299 305 305 GLU GLU A . n 
A 1 300 GLU 300 306 306 GLU GLU A . n 
A 1 301 GLU 301 307 307 GLU GLU A . n 
A 1 302 ALA 302 308 308 ALA ALA A . n 
A 1 303 LYS 303 309 309 LYS LYS A . n 
A 1 304 THR 304 310 310 THR THR A . n 
A 1 305 THR 305 311 311 THR THR A . n 
A 1 306 ALA 306 312 312 ALA ALA A . n 
A 1 307 ASN 307 313 313 ASN ASN A . n 
A 1 308 LEU 308 314 314 LEU LEU A . n 
A 1 309 ALA 309 315 315 ALA ALA A . n 
A 1 310 VAL 310 316 316 VAL VAL A . n 
A 1 311 ASP 311 317 317 ASP ASP A . n 
A 1 312 VAL 312 318 318 VAL VAL A . n 
A 1 313 ILE 313 319 319 ILE ILE A . n 
A 1 314 ALA 314 320 320 ALA ALA A . n 
A 1 315 SER 315 321 321 SER SER A . n 
A 1 316 SER 316 322 322 SER SER A . n 
A 1 317 PHE 317 323 323 PHE PHE A . n 
A 1 318 GLY 318 324 324 GLY GLY A . n 
A 1 319 GLN 319 325 325 GLN GLN A . n 
A 1 320 THR 320 326 326 THR THR A . n 
A 1 321 ARG 321 327 327 ARG ARG A . n 
A 1 322 GLU 322 328 328 GLU GLU A . n 
A 1 323 GLY 323 329 329 GLY GLY A . n 
A 1 324 GLY 324 330 330 GLY GLY A . n 
A 1 325 HIS 325 331 331 HIS HIS A . n 
A 1 326 ILE 326 332 332 ILE ILE A . n 
A 1 327 VAL 327 333 333 VAL VAL A . n 
A 1 328 TYR 328 334 334 TYR TYR A . n 
A 1 329 ASP 329 335 335 ASP ASP A . n 
A 1 330 GLN 330 336 336 GLN GLN A . n 
A 1 331 LEU 331 337 337 LEU LEU A . n 
A 1 332 PRO 332 338 338 PRO PRO A . n 
A 1 333 THR 333 339 339 THR THR A . n 
A 1 334 PRO 334 340 340 PRO PRO A . n 
A 1 335 SER 335 341 ?   ?   ?   A . n 
B 1 1   HIS 1   7   ?   ?   ?   B . n 
B 1 2   HIS 2   8   ?   ?   ?   B . n 
B 1 3   HIS 3   9   ?   ?   ?   B . n 
B 1 4   HIS 4   10  ?   ?   ?   B . n 
B 1 5   HIS 5   11  ?   ?   ?   B . n 
B 1 6   HIS 6   12  ?   ?   ?   B . n 
B 1 7   GLY 7   13  ?   ?   ?   B . n 
B 1 8   GLY 8   14  ?   ?   ?   B . n 
B 1 9   GLY 9   15  ?   ?   ?   B . n 
B 1 10  GLU 10  16  ?   ?   ?   B . n 
B 1 11  ASN 11  17  17  ASN ASN B . n 
B 1 12  LEU 12  18  18  LEU LEU B . n 
B 1 13  TYR 13  19  19  TYR TYR B . n 
B 1 14  PHE 14  20  20  PHE PHE B . n 
B 1 15  GLN 15  21  21  GLN GLN B . n 
B 1 16  SER 16  22  22  SER SER B . n 
B 1 17  VAL 17  23  23  VAL VAL B . n 
B 1 18  HIS 18  24  24  HIS HIS B . n 
B 1 19  SER 19  25  25  SER SER B . n 
B 1 20  VAL 20  26  26  VAL VAL B . n 
B 1 21  ALA 21  27  27  ALA ALA B . n 
B 1 22  VAL 22  28  28  VAL VAL B . n 
B 1 23  ILE 23  29  29  ILE ILE B . n 
B 1 24  GLY 24  30  30  GLY GLY B . n 
B 1 25  ALA 25  31  31  ALA ALA B . n 
B 1 26  PRO 26  32  32  PRO PRO B . n 
B 1 27  PHE 27  33  33  PHE PHE B . n 
B 1 28  SER 28  34  34  SER SER B . n 
B 1 29  GLN 29  35  35  GLN GLN B . n 
B 1 30  GLY 30  36  36  GLY GLY B . n 
B 1 31  GLN 31  37  37  GLN GLN B . n 
B 1 32  LYS 32  38  38  LYS LYS B . n 
B 1 33  ARG 33  39  39  ARG ARG B . n 
B 1 34  LYS 34  40  40  LYS LYS B . n 
B 1 35  GLY 35  41  41  GLY GLY B . n 
B 1 36  VAL 36  42  42  VAL VAL B . n 
B 1 37  GLU 37  43  43  GLU GLU B . n 
B 1 38  HIS 38  44  44  HIS HIS B . n 
B 1 39  GLY 39  45  45  GLY GLY B . n 
B 1 40  PRO 40  46  46  PRO PRO B . n 
B 1 41  ALA 41  47  47  ALA ALA B . n 
B 1 42  ALA 42  48  48  ALA ALA B . n 
B 1 43  ILE 43  49  49  ILE ILE B . n 
B 1 44  ARG 44  50  50  ARG ARG B . n 
B 1 45  GLU 45  51  51  GLU GLU B . n 
B 1 46  ALA 46  52  52  ALA ALA B . n 
B 1 47  GLY 47  53  53  GLY GLY B . n 
B 1 48  LEU 48  54  54  LEU LEU B . n 
B 1 49  MET 49  55  55  MET MET B . n 
B 1 50  LYS 50  56  56  LYS LYS B . n 
B 1 51  ARG 51  57  57  ARG ARG B . n 
B 1 52  LEU 52  58  58  LEU LEU B . n 
B 1 53  SER 53  59  59  SER SER B . n 
B 1 54  SER 54  60  60  SER SER B . n 
B 1 55  LEU 55  61  61  LEU LEU B . n 
B 1 56  GLY 56  62  62  GLY GLY B . n 
B 1 57  CYS 57  63  63  CYS CYS B . n 
B 1 58  HIS 58  64  64  HIS HIS B . n 
B 1 59  LEU 59  65  65  LEU LEU B . n 
B 1 60  LYS 60  66  66  LYS LYS B . n 
B 1 61  ASP 61  67  67  ASP ASP B . n 
B 1 62  PHE 62  68  68  PHE PHE B . n 
B 1 63  GLY 63  69  69  GLY GLY B . n 
B 1 64  ASP 64  70  70  ASP ASP B . n 
B 1 65  LEU 65  71  71  LEU LEU B . n 
B 1 66  SER 66  72  72  SER SER B . n 
B 1 67  PHE 67  73  73  PHE PHE B . n 
B 1 68  THR 68  74  74  THR THR B . n 
B 1 69  PRO 69  75  75  PRO PRO B . n 
B 1 70  VAL 70  76  76  VAL VAL B . n 
B 1 71  PRO 71  77  77  PRO PRO B . n 
B 1 72  LYS 72  78  78  LYS LYS B . n 
B 1 73  ASP 73  79  79  ASP ASP B . n 
B 1 74  ASP 74  80  80  ASP ASP B . n 
B 1 75  LEU 75  81  81  LEU LEU B . n 
B 1 76  TYR 76  82  82  TYR TYR B . n 
B 1 77  ASN 77  83  83  ASN ASN B . n 
B 1 78  ASN 78  84  84  ASN ASN B . n 
B 1 79  LEU 79  85  85  LEU LEU B . n 
B 1 80  ILE 80  86  86  ILE ILE B . n 
B 1 81  VAL 81  87  87  VAL VAL B . n 
B 1 82  ASN 82  88  88  ASN ASN B . n 
B 1 83  PRO 83  89  89  PRO PRO B . n 
B 1 84  ARG 84  90  90  ARG ARG B . n 
B 1 85  SER 85  91  91  SER SER B . n 
B 1 86  VAL 86  92  92  VAL VAL B . n 
B 1 87  GLY 87  93  93  GLY GLY B . n 
B 1 88  LEU 88  94  94  LEU LEU B . n 
B 1 89  ALA 89  95  95  ALA ALA B . n 
B 1 90  ASN 90  96  96  ASN ASN B . n 
B 1 91  GLN 91  97  97  GLN GLN B . n 
B 1 92  GLU 92  98  98  GLU GLU B . n 
B 1 93  LEU 93  99  99  LEU LEU B . n 
B 1 94  ALA 94  100 100 ALA ALA B . n 
B 1 95  GLU 95  101 101 GLU GLU B . n 
B 1 96  VAL 96  102 102 VAL VAL B . n 
B 1 97  VAL 97  103 103 VAL VAL B . n 
B 1 98  SER 98  104 104 SER SER B . n 
B 1 99  ARG 99  105 105 ARG ARG B . n 
B 1 100 ALA 100 106 106 ALA ALA B . n 
B 1 101 VAL 101 107 107 VAL VAL B . n 
B 1 102 SER 102 108 108 SER SER B . n 
B 1 103 ASP 103 109 109 ASP ASP B . n 
B 1 104 GLY 104 110 110 GLY GLY B . n 
B 1 105 TYR 105 111 111 TYR TYR B . n 
B 1 106 SER 106 112 112 SER SER B . n 
B 1 107 CYS 107 113 113 CYS CYS B . n 
B 1 108 VAL 108 114 114 VAL VAL B . n 
B 1 109 THR 109 115 115 THR THR B . n 
B 1 110 LEU 110 116 116 LEU LEU B . n 
B 1 111 GLY 111 117 117 GLY GLY B . n 
B 1 112 GLY 112 118 118 GLY GLY B . n 
B 1 113 ASP 113 119 119 ASP ASP B . n 
B 1 114 HIS 114 120 120 HIS HIS B . n 
B 1 115 SER 115 121 121 SER SER B . n 
B 1 116 LEU 116 122 122 LEU LEU B . n 
B 1 117 ALA 117 123 123 ALA ALA B . n 
B 1 118 ILE 118 124 124 ILE ILE B . n 
B 1 119 GLY 119 125 125 GLY GLY B . n 
B 1 120 THR 120 126 126 THR THR B . n 
B 1 121 ILE 121 127 127 ILE ILE B . n 
B 1 122 SER 122 128 128 SER SER B . n 
B 1 123 GLY 123 129 129 GLY GLY B . n 
B 1 124 HIS 124 130 130 HIS HIS B . n 
B 1 125 ALA 125 131 131 ALA ALA B . n 
B 1 126 ARG 126 132 132 ARG ARG B . n 
B 1 127 HIS 127 133 133 HIS HIS B . n 
B 1 128 CYS 128 134 134 CYS CYS B . n 
B 1 129 PRO 129 135 135 PRO PRO B . n 
B 1 130 ASP 130 136 136 ASP ASP B . n 
B 1 131 LEU 131 137 137 LEU LEU B . n 
B 1 132 CYS 132 138 138 CYS CYS B . n 
B 1 133 VAL 133 139 139 VAL VAL B . n 
B 1 134 VAL 134 140 140 VAL VAL B . n 
B 1 135 TRP 135 141 141 TRP TRP B . n 
B 1 136 VAL 136 142 142 VAL VAL B . n 
B 1 137 ASP 137 143 143 ASP ASP B . n 
B 1 138 ALA 138 144 144 ALA ALA B . n 
B 1 139 HIS 139 145 145 HIS HIS B . n 
B 1 140 ALA 140 146 146 ALA ALA B . n 
B 1 141 ASP 141 147 147 ASP ASP B . n 
B 1 142 ILE 142 148 148 ILE ILE B . n 
B 1 143 ASN 143 149 149 ASN ASN B . n 
B 1 144 THR 144 150 150 THR THR B . n 
B 1 145 PRO 145 151 151 PRO PRO B . n 
B 1 146 LEU 146 152 152 LEU LEU B . n 
B 1 147 THR 147 153 153 THR THR B . n 
B 1 148 THR 148 154 154 THR THR B . n 
B 1 149 SER 149 155 155 SER SER B . n 
B 1 150 SER 150 156 156 SER SER B . n 
B 1 151 GLY 151 157 157 GLY GLY B . n 
B 1 152 ASN 152 158 158 ASN ASN B . n 
B 1 153 LEU 153 159 159 LEU LEU B . n 
B 1 154 HIS 154 160 160 HIS HIS B . n 
B 1 155 GLY 155 161 161 GLY GLY B . n 
B 1 156 GLN 156 162 162 GLN GLN B . n 
B 1 157 PRO 157 163 163 PRO PRO B . n 
B 1 158 VAL 158 164 164 VAL VAL B . n 
B 1 159 SER 159 165 165 SER SER B . n 
B 1 160 PHE 160 166 166 PHE PHE B . n 
B 1 161 LEU 161 167 167 LEU LEU B . n 
B 1 162 LEU 162 168 168 LEU LEU B . n 
B 1 163 ARG 163 169 169 ARG ARG B . n 
B 1 164 GLU 164 170 170 GLU GLU B . n 
B 1 165 LEU 165 171 171 LEU LEU B . n 
B 1 166 GLN 166 172 172 GLN GLN B . n 
B 1 167 ASP 167 173 173 ASP ASP B . n 
B 1 168 LYS 168 174 174 LYS LYS B . n 
B 1 169 VAL 169 175 175 VAL VAL B . n 
B 1 170 PRO 170 176 176 PRO PRO B . n 
B 1 171 GLN 171 177 177 GLN GLN B . n 
B 1 172 LEU 172 178 178 LEU LEU B . n 
B 1 173 PRO 173 179 179 PRO PRO B . n 
B 1 174 GLY 174 180 180 GLY GLY B . n 
B 1 175 PHE 175 181 181 PHE PHE B . n 
B 1 176 SER 176 182 182 SER SER B . n 
B 1 177 TRP 177 183 183 TRP TRP B . n 
B 1 178 ILE 178 184 184 ILE ILE B . n 
B 1 179 LYS 179 185 185 LYS LYS B . n 
B 1 180 PRO 180 186 186 PRO PRO B . n 
B 1 181 CYS 181 187 187 CYS CYS B . n 
B 1 182 ILE 182 188 188 ILE ILE B . n 
B 1 183 SER 183 189 189 SER SER B . n 
B 1 184 SER 184 190 190 SER SER B . n 
B 1 185 ALA 185 191 191 ALA ALA B . n 
B 1 186 SER 186 192 192 SER SER B . n 
B 1 187 ILE 187 193 193 ILE ILE B . n 
B 1 188 VAL 188 194 194 VAL VAL B . n 
B 1 189 TYR 189 195 195 TYR TYR B . n 
B 1 190 ILE 190 196 196 ILE ILE B . n 
B 1 191 GLY 191 197 197 GLY GLY B . n 
B 1 192 LEU 192 198 198 LEU LEU B . n 
B 1 193 ARG 193 199 199 ARG ARG B . n 
B 1 194 ASP 194 200 200 ASP ASP B . n 
B 1 195 VAL 195 201 201 VAL VAL B . n 
B 1 196 ASP 196 202 202 ASP ASP B . n 
B 1 197 PRO 197 203 203 PRO PRO B . n 
B 1 198 PRO 198 204 204 PRO PRO B . n 
B 1 199 GLU 199 205 205 GLU GLU B . n 
B 1 200 HIS 200 206 206 HIS HIS B . n 
B 1 201 PHE 201 207 207 PHE PHE B . n 
B 1 202 ILE 202 208 208 ILE ILE B . n 
B 1 203 LEU 203 209 209 LEU LEU B . n 
B 1 204 LYS 204 210 210 LYS LYS B . n 
B 1 205 ASN 205 211 211 ASN ASN B . n 
B 1 206 TYR 206 212 212 TYR TYR B . n 
B 1 207 ASP 207 213 213 ASP ASP B . n 
B 1 208 ILE 208 214 214 ILE ILE B . n 
B 1 209 GLN 209 215 215 GLN GLN B . n 
B 1 210 TYR 210 216 216 TYR TYR B . n 
B 1 211 PHE 211 217 217 PHE PHE B . n 
B 1 212 SER 212 218 218 SER SER B . n 
B 1 213 MET 213 219 219 MET MET B . n 
B 1 214 ARG 214 220 220 ARG ARG B . n 
B 1 215 ASP 215 221 221 ASP ASP B . n 
B 1 216 ILE 216 222 222 ILE ILE B . n 
B 1 217 ASP 217 223 223 ASP ASP B . n 
B 1 218 ARG 218 224 224 ARG ARG B . n 
B 1 219 LEU 219 225 225 LEU LEU B . n 
B 1 220 GLY 220 226 226 GLY GLY B . n 
B 1 221 ILE 221 227 227 ILE ILE B . n 
B 1 222 GLN 222 228 228 GLN GLN B . n 
B 1 223 LYS 223 229 229 LYS LYS B . n 
B 1 224 VAL 224 230 230 VAL VAL B . n 
B 1 225 MET 225 231 231 MET MET B . n 
B 1 226 GLU 226 232 232 GLU GLU B . n 
B 1 227 ARG 227 233 233 ARG ARG B . n 
B 1 228 THR 228 234 234 THR THR B . n 
B 1 229 PHE 229 235 235 PHE PHE B . n 
B 1 230 ASP 230 236 236 ASP ASP B . n 
B 1 231 LEU 231 237 237 LEU LEU B . n 
B 1 232 LEU 232 238 238 LEU LEU B . n 
B 1 233 ILE 233 239 239 ILE ILE B . n 
B 1 234 GLY 234 240 240 GLY GLY B . n 
B 1 235 LYS 235 241 241 LYS LYS B . n 
B 1 236 ARG 236 242 242 ARG ARG B . n 
B 1 237 GLN 237 243 243 GLN GLN B . n 
B 1 238 ARG 238 244 244 ARG ARG B . n 
B 1 239 PRO 239 245 245 PRO PRO B . n 
B 1 240 ILE 240 246 246 ILE ILE B . n 
B 1 241 HIS 241 247 247 HIS HIS B . n 
B 1 242 LEU 242 248 248 LEU LEU B . n 
B 1 243 SER 243 249 249 SER SER B . n 
B 1 244 PHE 244 250 250 PHE PHE B . n 
B 1 245 ASP 245 251 251 ASP ASP B . n 
B 1 246 ILE 246 252 252 ILE ILE B . n 
B 1 247 ASP 247 253 253 ASP ASP B . n 
B 1 248 ALA 248 254 254 ALA ALA B . n 
B 1 249 PHE 249 255 255 PHE PHE B . n 
B 1 250 ASP 250 256 256 ASP ASP B . n 
B 1 251 PRO 251 257 257 PRO PRO B . n 
B 1 252 THR 252 258 258 THR THR B . n 
B 1 253 LEU 253 259 259 LEU LEU B . n 
B 1 254 ALA 254 260 260 ALA ALA B . n 
B 1 255 PRO 255 261 261 PRO PRO B . n 
B 1 256 ALA 256 262 262 ALA ALA B . n 
B 1 257 THR 257 263 263 THR THR B . n 
B 1 258 GLY 258 264 264 GLY GLY B . n 
B 1 259 THR 259 265 265 THR THR B . n 
B 1 260 PRO 260 266 266 PRO PRO B . n 
B 1 261 VAL 261 267 267 VAL VAL B . n 
B 1 262 VAL 262 268 268 VAL VAL B . n 
B 1 263 GLY 263 269 269 GLY GLY B . n 
B 1 264 GLY 264 270 270 GLY GLY B . n 
B 1 265 LEU 265 271 271 LEU LEU B . n 
B 1 266 THR 266 272 272 THR THR B . n 
B 1 267 TYR 267 273 273 TYR TYR B . n 
B 1 268 ARG 268 274 274 ARG ARG B . n 
B 1 269 GLU 269 275 275 GLU GLU B . n 
B 1 270 GLY 270 276 276 GLY GLY B . n 
B 1 271 MET 271 277 277 MET MET B . n 
B 1 272 TYR 272 278 278 TYR TYR B . n 
B 1 273 ILE 273 279 279 ILE ILE B . n 
B 1 274 ALA 274 280 280 ALA ALA B . n 
B 1 275 GLU 275 281 281 GLU GLU B . n 
B 1 276 GLU 276 282 282 GLU GLU B . n 
B 1 277 ILE 277 283 283 ILE ILE B . n 
B 1 278 HIS 278 284 284 HIS HIS B . n 
B 1 279 ASN 279 285 285 ASN ASN B . n 
B 1 280 THR 280 286 286 THR THR B . n 
B 1 281 GLY 281 287 287 GLY GLY B . n 
B 1 282 LEU 282 288 288 LEU LEU B . n 
B 1 283 LEU 283 289 289 LEU LEU B . n 
B 1 284 SER 284 290 290 SER SER B . n 
B 1 285 ALA 285 291 291 ALA ALA B . n 
B 1 286 LEU 286 292 292 LEU LEU B . n 
B 1 287 ASP 287 293 293 ASP ASP B . n 
B 1 288 LEU 288 294 294 LEU LEU B . n 
B 1 289 VAL 289 295 295 VAL VAL B . n 
B 1 290 GLU 290 296 296 GLU GLU B . n 
B 1 291 VAL 291 297 297 VAL VAL B . n 
B 1 292 ASN 292 298 298 ASN ASN B . n 
B 1 293 PRO 293 299 299 PRO PRO B . n 
B 1 294 GLN 294 300 300 GLN GLN B . n 
B 1 295 LEU 295 301 301 LEU LEU B . n 
B 1 296 ALA 296 302 302 ALA ALA B . n 
B 1 297 THR 297 303 303 THR THR B . n 
B 1 298 SER 298 304 304 SER SER B . n 
B 1 299 GLU 299 305 305 GLU GLU B . n 
B 1 300 GLU 300 306 306 GLU GLU B . n 
B 1 301 GLU 301 307 307 GLU GLU B . n 
B 1 302 ALA 302 308 308 ALA ALA B . n 
B 1 303 LYS 303 309 309 LYS LYS B . n 
B 1 304 THR 304 310 310 THR THR B . n 
B 1 305 THR 305 311 311 THR THR B . n 
B 1 306 ALA 306 312 312 ALA ALA B . n 
B 1 307 ASN 307 313 313 ASN ASN B . n 
B 1 308 LEU 308 314 314 LEU LEU B . n 
B 1 309 ALA 309 315 315 ALA ALA B . n 
B 1 310 VAL 310 316 316 VAL VAL B . n 
B 1 311 ASP 311 317 317 ASP ASP B . n 
B 1 312 VAL 312 318 318 VAL VAL B . n 
B 1 313 ILE 313 319 319 ILE ILE B . n 
B 1 314 ALA 314 320 320 ALA ALA B . n 
B 1 315 SER 315 321 321 SER SER B . n 
B 1 316 SER 316 322 322 SER SER B . n 
B 1 317 PHE 317 323 323 PHE PHE B . n 
B 1 318 GLY 318 324 324 GLY GLY B . n 
B 1 319 GLN 319 325 325 GLN GLN B . n 
B 1 320 THR 320 326 326 THR THR B . n 
B 1 321 ARG 321 327 327 ARG ARG B . n 
B 1 322 GLU 322 328 328 GLU GLU B . n 
B 1 323 GLY 323 329 329 GLY GLY B . n 
B 1 324 GLY 324 330 330 GLY GLY B . n 
B 1 325 HIS 325 331 331 HIS HIS B . n 
B 1 326 ILE 326 332 332 ILE ILE B . n 
B 1 327 VAL 327 333 333 VAL VAL B . n 
B 1 328 TYR 328 334 334 TYR TYR B . n 
B 1 329 ASP 329 335 335 ASP ASP B . n 
B 1 330 GLN 330 336 336 GLN GLN B . n 
B 1 331 LEU 331 337 337 LEU LEU B . n 
B 1 332 PRO 332 338 338 PRO PRO B . n 
B 1 333 THR 333 339 339 THR THR B . n 
B 1 334 PRO 334 340 340 PRO PRO B . n 
B 1 335 SER 335 341 ?   ?   ?   B . n 
C 1 1   HIS 1   7   ?   ?   ?   C . n 
C 1 2   HIS 2   8   ?   ?   ?   C . n 
C 1 3   HIS 3   9   ?   ?   ?   C . n 
C 1 4   HIS 4   10  ?   ?   ?   C . n 
C 1 5   HIS 5   11  ?   ?   ?   C . n 
C 1 6   HIS 6   12  ?   ?   ?   C . n 
C 1 7   GLY 7   13  ?   ?   ?   C . n 
C 1 8   GLY 8   14  ?   ?   ?   C . n 
C 1 9   GLY 9   15  ?   ?   ?   C . n 
C 1 10  GLU 10  16  ?   ?   ?   C . n 
C 1 11  ASN 11  17  ?   ?   ?   C . n 
C 1 12  LEU 12  18  ?   ?   ?   C . n 
C 1 13  TYR 13  19  ?   ?   ?   C . n 
C 1 14  PHE 14  20  ?   ?   ?   C . n 
C 1 15  GLN 15  21  ?   ?   ?   C . n 
C 1 16  SER 16  22  ?   ?   ?   C . n 
C 1 17  VAL 17  23  23  VAL VAL C . n 
C 1 18  HIS 18  24  24  HIS HIS C . n 
C 1 19  SER 19  25  25  SER SER C . n 
C 1 20  VAL 20  26  26  VAL VAL C . n 
C 1 21  ALA 21  27  27  ALA ALA C . n 
C 1 22  VAL 22  28  28  VAL VAL C . n 
C 1 23  ILE 23  29  29  ILE ILE C . n 
C 1 24  GLY 24  30  30  GLY GLY C . n 
C 1 25  ALA 25  31  31  ALA ALA C . n 
C 1 26  PRO 26  32  32  PRO PRO C . n 
C 1 27  PHE 27  33  33  PHE PHE C . n 
C 1 28  SER 28  34  34  SER SER C . n 
C 1 29  GLN 29  35  35  GLN GLN C . n 
C 1 30  GLY 30  36  36  GLY GLY C . n 
C 1 31  GLN 31  37  37  GLN GLN C . n 
C 1 32  LYS 32  38  38  LYS LYS C . n 
C 1 33  ARG 33  39  39  ARG ARG C . n 
C 1 34  LYS 34  40  40  LYS LYS C . n 
C 1 35  GLY 35  41  41  GLY GLY C . n 
C 1 36  VAL 36  42  42  VAL VAL C . n 
C 1 37  GLU 37  43  43  GLU GLU C . n 
C 1 38  HIS 38  44  44  HIS HIS C . n 
C 1 39  GLY 39  45  45  GLY GLY C . n 
C 1 40  PRO 40  46  46  PRO PRO C . n 
C 1 41  ALA 41  47  47  ALA ALA C . n 
C 1 42  ALA 42  48  48  ALA ALA C . n 
C 1 43  ILE 43  49  49  ILE ILE C . n 
C 1 44  ARG 44  50  50  ARG ARG C . n 
C 1 45  GLU 45  51  51  GLU GLU C . n 
C 1 46  ALA 46  52  52  ALA ALA C . n 
C 1 47  GLY 47  53  53  GLY GLY C . n 
C 1 48  LEU 48  54  54  LEU LEU C . n 
C 1 49  MET 49  55  55  MET MET C . n 
C 1 50  LYS 50  56  56  LYS LYS C . n 
C 1 51  ARG 51  57  57  ARG ARG C . n 
C 1 52  LEU 52  58  58  LEU LEU C . n 
C 1 53  SER 53  59  59  SER SER C . n 
C 1 54  SER 54  60  60  SER SER C . n 
C 1 55  LEU 55  61  61  LEU LEU C . n 
C 1 56  GLY 56  62  62  GLY GLY C . n 
C 1 57  CYS 57  63  63  CYS CYS C . n 
C 1 58  HIS 58  64  64  HIS HIS C . n 
C 1 59  LEU 59  65  65  LEU LEU C . n 
C 1 60  LYS 60  66  66  LYS LYS C . n 
C 1 61  ASP 61  67  67  ASP ASP C . n 
C 1 62  PHE 62  68  68  PHE PHE C . n 
C 1 63  GLY 63  69  69  GLY GLY C . n 
C 1 64  ASP 64  70  70  ASP ASP C . n 
C 1 65  LEU 65  71  71  LEU LEU C . n 
C 1 66  SER 66  72  72  SER SER C . n 
C 1 67  PHE 67  73  73  PHE PHE C . n 
C 1 68  THR 68  74  74  THR THR C . n 
C 1 69  PRO 69  75  75  PRO PRO C . n 
C 1 70  VAL 70  76  76  VAL VAL C . n 
C 1 71  PRO 71  77  77  PRO PRO C . n 
C 1 72  LYS 72  78  78  LYS LYS C . n 
C 1 73  ASP 73  79  79  ASP ASP C . n 
C 1 74  ASP 74  80  80  ASP ASP C . n 
C 1 75  LEU 75  81  81  LEU LEU C . n 
C 1 76  TYR 76  82  82  TYR TYR C . n 
C 1 77  ASN 77  83  83  ASN ASN C . n 
C 1 78  ASN 78  84  84  ASN ASN C . n 
C 1 79  LEU 79  85  85  LEU LEU C . n 
C 1 80  ILE 80  86  86  ILE ILE C . n 
C 1 81  VAL 81  87  87  VAL VAL C . n 
C 1 82  ASN 82  88  88  ASN ASN C . n 
C 1 83  PRO 83  89  89  PRO PRO C . n 
C 1 84  ARG 84  90  90  ARG ARG C . n 
C 1 85  SER 85  91  91  SER SER C . n 
C 1 86  VAL 86  92  92  VAL VAL C . n 
C 1 87  GLY 87  93  93  GLY GLY C . n 
C 1 88  LEU 88  94  94  LEU LEU C . n 
C 1 89  ALA 89  95  95  ALA ALA C . n 
C 1 90  ASN 90  96  96  ASN ASN C . n 
C 1 91  GLN 91  97  97  GLN GLN C . n 
C 1 92  GLU 92  98  98  GLU GLU C . n 
C 1 93  LEU 93  99  99  LEU LEU C . n 
C 1 94  ALA 94  100 100 ALA ALA C . n 
C 1 95  GLU 95  101 101 GLU GLU C . n 
C 1 96  VAL 96  102 102 VAL VAL C . n 
C 1 97  VAL 97  103 103 VAL VAL C . n 
C 1 98  SER 98  104 104 SER SER C . n 
C 1 99  ARG 99  105 105 ARG ARG C . n 
C 1 100 ALA 100 106 106 ALA ALA C . n 
C 1 101 VAL 101 107 107 VAL VAL C . n 
C 1 102 SER 102 108 108 SER SER C . n 
C 1 103 ASP 103 109 109 ASP ASP C . n 
C 1 104 GLY 104 110 110 GLY GLY C . n 
C 1 105 TYR 105 111 111 TYR TYR C . n 
C 1 106 SER 106 112 112 SER SER C . n 
C 1 107 CYS 107 113 113 CYS CYS C . n 
C 1 108 VAL 108 114 114 VAL VAL C . n 
C 1 109 THR 109 115 115 THR THR C . n 
C 1 110 LEU 110 116 116 LEU LEU C . n 
C 1 111 GLY 111 117 117 GLY GLY C . n 
C 1 112 GLY 112 118 118 GLY GLY C . n 
C 1 113 ASP 113 119 119 ASP ASP C . n 
C 1 114 HIS 114 120 120 HIS HIS C . n 
C 1 115 SER 115 121 121 SER SER C . n 
C 1 116 LEU 116 122 122 LEU LEU C . n 
C 1 117 ALA 117 123 123 ALA ALA C . n 
C 1 118 ILE 118 124 124 ILE ILE C . n 
C 1 119 GLY 119 125 125 GLY GLY C . n 
C 1 120 THR 120 126 126 THR THR C . n 
C 1 121 ILE 121 127 127 ILE ILE C . n 
C 1 122 SER 122 128 128 SER SER C . n 
C 1 123 GLY 123 129 129 GLY GLY C . n 
C 1 124 HIS 124 130 130 HIS HIS C . n 
C 1 125 ALA 125 131 131 ALA ALA C . n 
C 1 126 ARG 126 132 132 ARG ARG C . n 
C 1 127 HIS 127 133 133 HIS HIS C . n 
C 1 128 CYS 128 134 134 CYS CYS C . n 
C 1 129 PRO 129 135 135 PRO PRO C . n 
C 1 130 ASP 130 136 136 ASP ASP C . n 
C 1 131 LEU 131 137 137 LEU LEU C . n 
C 1 132 CYS 132 138 138 CYS CYS C . n 
C 1 133 VAL 133 139 139 VAL VAL C . n 
C 1 134 VAL 134 140 140 VAL VAL C . n 
C 1 135 TRP 135 141 141 TRP TRP C . n 
C 1 136 VAL 136 142 142 VAL VAL C . n 
C 1 137 ASP 137 143 143 ASP ASP C . n 
C 1 138 ALA 138 144 144 ALA ALA C . n 
C 1 139 HIS 139 145 145 HIS HIS C . n 
C 1 140 ALA 140 146 146 ALA ALA C . n 
C 1 141 ASP 141 147 147 ASP ASP C . n 
C 1 142 ILE 142 148 148 ILE ILE C . n 
C 1 143 ASN 143 149 149 ASN ASN C . n 
C 1 144 THR 144 150 150 THR THR C . n 
C 1 145 PRO 145 151 151 PRO PRO C . n 
C 1 146 LEU 146 152 152 LEU LEU C . n 
C 1 147 THR 147 153 153 THR THR C . n 
C 1 148 THR 148 154 154 THR THR C . n 
C 1 149 SER 149 155 155 SER SER C . n 
C 1 150 SER 150 156 156 SER SER C . n 
C 1 151 GLY 151 157 157 GLY GLY C . n 
C 1 152 ASN 152 158 158 ASN ASN C . n 
C 1 153 LEU 153 159 159 LEU LEU C . n 
C 1 154 HIS 154 160 160 HIS HIS C . n 
C 1 155 GLY 155 161 161 GLY GLY C . n 
C 1 156 GLN 156 162 162 GLN GLN C . n 
C 1 157 PRO 157 163 163 PRO PRO C . n 
C 1 158 VAL 158 164 164 VAL VAL C . n 
C 1 159 SER 159 165 165 SER SER C . n 
C 1 160 PHE 160 166 166 PHE PHE C . n 
C 1 161 LEU 161 167 167 LEU LEU C . n 
C 1 162 LEU 162 168 168 LEU LEU C . n 
C 1 163 ARG 163 169 169 ARG ARG C . n 
C 1 164 GLU 164 170 170 GLU GLU C . n 
C 1 165 LEU 165 171 171 LEU LEU C . n 
C 1 166 GLN 166 172 172 GLN GLN C . n 
C 1 167 ASP 167 173 173 ASP ASP C . n 
C 1 168 LYS 168 174 174 LYS LYS C . n 
C 1 169 VAL 169 175 175 VAL VAL C . n 
C 1 170 PRO 170 176 176 PRO PRO C . n 
C 1 171 GLN 171 177 177 GLN GLN C . n 
C 1 172 LEU 172 178 178 LEU LEU C . n 
C 1 173 PRO 173 179 179 PRO PRO C . n 
C 1 174 GLY 174 180 180 GLY GLY C . n 
C 1 175 PHE 175 181 181 PHE PHE C . n 
C 1 176 SER 176 182 182 SER SER C . n 
C 1 177 TRP 177 183 183 TRP TRP C . n 
C 1 178 ILE 178 184 184 ILE ILE C . n 
C 1 179 LYS 179 185 185 LYS LYS C . n 
C 1 180 PRO 180 186 186 PRO PRO C . n 
C 1 181 CYS 181 187 187 CYS CYS C . n 
C 1 182 ILE 182 188 188 ILE ILE C . n 
C 1 183 SER 183 189 189 SER SER C . n 
C 1 184 SER 184 190 190 SER SER C . n 
C 1 185 ALA 185 191 191 ALA ALA C . n 
C 1 186 SER 186 192 192 SER SER C . n 
C 1 187 ILE 187 193 193 ILE ILE C . n 
C 1 188 VAL 188 194 194 VAL VAL C . n 
C 1 189 TYR 189 195 195 TYR TYR C . n 
C 1 190 ILE 190 196 196 ILE ILE C . n 
C 1 191 GLY 191 197 197 GLY GLY C . n 
C 1 192 LEU 192 198 198 LEU LEU C . n 
C 1 193 ARG 193 199 199 ARG ARG C . n 
C 1 194 ASP 194 200 200 ASP ASP C . n 
C 1 195 VAL 195 201 201 VAL VAL C . n 
C 1 196 ASP 196 202 202 ASP ASP C . n 
C 1 197 PRO 197 203 203 PRO PRO C . n 
C 1 198 PRO 198 204 204 PRO PRO C . n 
C 1 199 GLU 199 205 205 GLU GLU C . n 
C 1 200 HIS 200 206 206 HIS HIS C . n 
C 1 201 PHE 201 207 207 PHE PHE C . n 
C 1 202 ILE 202 208 208 ILE ILE C . n 
C 1 203 LEU 203 209 209 LEU LEU C . n 
C 1 204 LYS 204 210 210 LYS LYS C . n 
C 1 205 ASN 205 211 211 ASN ASN C . n 
C 1 206 TYR 206 212 212 TYR TYR C . n 
C 1 207 ASP 207 213 213 ASP ASP C . n 
C 1 208 ILE 208 214 214 ILE ILE C . n 
C 1 209 GLN 209 215 215 GLN GLN C . n 
C 1 210 TYR 210 216 216 TYR TYR C . n 
C 1 211 PHE 211 217 217 PHE PHE C . n 
C 1 212 SER 212 218 218 SER SER C . n 
C 1 213 MET 213 219 219 MET MET C . n 
C 1 214 ARG 214 220 220 ARG ARG C . n 
C 1 215 ASP 215 221 221 ASP ASP C . n 
C 1 216 ILE 216 222 222 ILE ILE C . n 
C 1 217 ASP 217 223 223 ASP ASP C . n 
C 1 218 ARG 218 224 224 ARG ARG C . n 
C 1 219 LEU 219 225 225 LEU LEU C . n 
C 1 220 GLY 220 226 226 GLY GLY C . n 
C 1 221 ILE 221 227 227 ILE ILE C . n 
C 1 222 GLN 222 228 228 GLN GLN C . n 
C 1 223 LYS 223 229 229 LYS LYS C . n 
C 1 224 VAL 224 230 230 VAL VAL C . n 
C 1 225 MET 225 231 231 MET MET C . n 
C 1 226 GLU 226 232 232 GLU GLU C . n 
C 1 227 ARG 227 233 233 ARG ARG C . n 
C 1 228 THR 228 234 234 THR THR C . n 
C 1 229 PHE 229 235 235 PHE PHE C . n 
C 1 230 ASP 230 236 236 ASP ASP C . n 
C 1 231 LEU 231 237 237 LEU LEU C . n 
C 1 232 LEU 232 238 238 LEU LEU C . n 
C 1 233 ILE 233 239 239 ILE ILE C . n 
C 1 234 GLY 234 240 240 GLY GLY C . n 
C 1 235 LYS 235 241 241 LYS LYS C . n 
C 1 236 ARG 236 242 242 ARG ARG C . n 
C 1 237 GLN 237 243 243 GLN GLN C . n 
C 1 238 ARG 238 244 244 ARG ARG C . n 
C 1 239 PRO 239 245 245 PRO PRO C . n 
C 1 240 ILE 240 246 246 ILE ILE C . n 
C 1 241 HIS 241 247 247 HIS HIS C . n 
C 1 242 LEU 242 248 248 LEU LEU C . n 
C 1 243 SER 243 249 249 SER SER C . n 
C 1 244 PHE 244 250 250 PHE PHE C . n 
C 1 245 ASP 245 251 251 ASP ASP C . n 
C 1 246 ILE 246 252 252 ILE ILE C . n 
C 1 247 ASP 247 253 253 ASP ASP C . n 
C 1 248 ALA 248 254 254 ALA ALA C . n 
C 1 249 PHE 249 255 255 PHE PHE C . n 
C 1 250 ASP 250 256 256 ASP ASP C . n 
C 1 251 PRO 251 257 257 PRO PRO C . n 
C 1 252 THR 252 258 258 THR THR C . n 
C 1 253 LEU 253 259 259 LEU LEU C . n 
C 1 254 ALA 254 260 260 ALA ALA C . n 
C 1 255 PRO 255 261 261 PRO PRO C . n 
C 1 256 ALA 256 262 262 ALA ALA C . n 
C 1 257 THR 257 263 263 THR THR C . n 
C 1 258 GLY 258 264 264 GLY GLY C . n 
C 1 259 THR 259 265 265 THR THR C . n 
C 1 260 PRO 260 266 266 PRO PRO C . n 
C 1 261 VAL 261 267 267 VAL VAL C . n 
C 1 262 VAL 262 268 268 VAL VAL C . n 
C 1 263 GLY 263 269 269 GLY GLY C . n 
C 1 264 GLY 264 270 270 GLY GLY C . n 
C 1 265 LEU 265 271 271 LEU LEU C . n 
C 1 266 THR 266 272 272 THR THR C . n 
C 1 267 TYR 267 273 273 TYR TYR C . n 
C 1 268 ARG 268 274 274 ARG ARG C . n 
C 1 269 GLU 269 275 275 GLU GLU C . n 
C 1 270 GLY 270 276 276 GLY GLY C . n 
C 1 271 MET 271 277 277 MET MET C . n 
C 1 272 TYR 272 278 278 TYR TYR C . n 
C 1 273 ILE 273 279 279 ILE ILE C . n 
C 1 274 ALA 274 280 280 ALA ALA C . n 
C 1 275 GLU 275 281 281 GLU GLU C . n 
C 1 276 GLU 276 282 282 GLU GLU C . n 
C 1 277 ILE 277 283 283 ILE ILE C . n 
C 1 278 HIS 278 284 284 HIS HIS C . n 
C 1 279 ASN 279 285 285 ASN ASN C . n 
C 1 280 THR 280 286 286 THR THR C . n 
C 1 281 GLY 281 287 287 GLY GLY C . n 
C 1 282 LEU 282 288 288 LEU LEU C . n 
C 1 283 LEU 283 289 289 LEU LEU C . n 
C 1 284 SER 284 290 290 SER SER C . n 
C 1 285 ALA 285 291 291 ALA ALA C . n 
C 1 286 LEU 286 292 292 LEU LEU C . n 
C 1 287 ASP 287 293 293 ASP ASP C . n 
C 1 288 LEU 288 294 294 LEU LEU C . n 
C 1 289 VAL 289 295 295 VAL VAL C . n 
C 1 290 GLU 290 296 296 GLU GLU C . n 
C 1 291 VAL 291 297 297 VAL VAL C . n 
C 1 292 ASN 292 298 298 ASN ASN C . n 
C 1 293 PRO 293 299 299 PRO PRO C . n 
C 1 294 GLN 294 300 300 GLN GLN C . n 
C 1 295 LEU 295 301 301 LEU LEU C . n 
C 1 296 ALA 296 302 302 ALA ALA C . n 
C 1 297 THR 297 303 303 THR THR C . n 
C 1 298 SER 298 304 304 SER SER C . n 
C 1 299 GLU 299 305 305 GLU GLU C . n 
C 1 300 GLU 300 306 306 GLU GLU C . n 
C 1 301 GLU 301 307 307 GLU GLU C . n 
C 1 302 ALA 302 308 308 ALA ALA C . n 
C 1 303 LYS 303 309 309 LYS LYS C . n 
C 1 304 THR 304 310 310 THR THR C . n 
C 1 305 THR 305 311 311 THR THR C . n 
C 1 306 ALA 306 312 312 ALA ALA C . n 
C 1 307 ASN 307 313 313 ASN ASN C . n 
C 1 308 LEU 308 314 314 LEU LEU C . n 
C 1 309 ALA 309 315 315 ALA ALA C . n 
C 1 310 VAL 310 316 316 VAL VAL C . n 
C 1 311 ASP 311 317 317 ASP ASP C . n 
C 1 312 VAL 312 318 318 VAL VAL C . n 
C 1 313 ILE 313 319 319 ILE ILE C . n 
C 1 314 ALA 314 320 320 ALA ALA C . n 
C 1 315 SER 315 321 321 SER SER C . n 
C 1 316 SER 316 322 322 SER SER C . n 
C 1 317 PHE 317 323 323 PHE PHE C . n 
C 1 318 GLY 318 324 324 GLY GLY C . n 
C 1 319 GLN 319 325 325 GLN GLN C . n 
C 1 320 THR 320 326 326 THR THR C . n 
C 1 321 ARG 321 327 327 ARG ARG C . n 
C 1 322 GLU 322 328 328 GLU GLU C . n 
C 1 323 GLY 323 329 329 GLY GLY C . n 
C 1 324 GLY 324 330 330 GLY GLY C . n 
C 1 325 HIS 325 331 331 HIS HIS C . n 
C 1 326 ILE 326 332 332 ILE ILE C . n 
C 1 327 VAL 327 333 333 VAL VAL C . n 
C 1 328 TYR 328 334 334 TYR TYR C . n 
C 1 329 ASP 329 335 335 ASP ASP C . n 
C 1 330 GLN 330 336 336 GLN GLN C . n 
C 1 331 LEU 331 337 337 LEU LEU C . n 
C 1 332 PRO 332 338 338 PRO PRO C . n 
C 1 333 THR 333 339 339 THR THR C . n 
C 1 334 PRO 334 340 340 PRO PRO C . n 
C 1 335 SER 335 341 ?   ?   ?   C . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1H0A 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1H0A 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
D 2 MN    1   401 500 MN    MN  A . 
E 2 MN    1   402 501 MN    MN  A . 
F 3 A1H0A 1   403 1   A1H0A INH A . 
G 2 MN    1   500 500 MN    MN  B . 
H 2 MN    1   501 501 MN    MN  B . 
I 2 MN    1   401 500 MN    MN  C . 
J 2 MN    1   402 501 MN    MN  C . 
K 3 A1H0A 1   403 3   A1H0A INH C . 
L 4 HOH   1   501 27  HOH   HOH A . 
L 4 HOH   2   502 64  HOH   HOH A . 
L 4 HOH   3   503 69  HOH   HOH A . 
L 4 HOH   4   504 46  HOH   HOH A . 
L 4 HOH   5   505 87  HOH   HOH A . 
L 4 HOH   6   506 171 HOH   HOH A . 
L 4 HOH   7   507 60  HOH   HOH A . 
L 4 HOH   8   508 121 HOH   HOH A . 
L 4 HOH   9   509 17  HOH   HOH A . 
L 4 HOH   10  510 111 HOH   HOH A . 
L 4 HOH   11  511 36  HOH   HOH A . 
L 4 HOH   12  512 137 HOH   HOH A . 
L 4 HOH   13  513 227 HOH   HOH A . 
L 4 HOH   14  514 9   HOH   HOH A . 
L 4 HOH   15  515 162 HOH   HOH A . 
L 4 HOH   16  516 114 HOH   HOH A . 
L 4 HOH   17  517 18  HOH   HOH A . 
L 4 HOH   18  518 24  HOH   HOH A . 
L 4 HOH   19  519 189 HOH   HOH A . 
L 4 HOH   20  520 76  HOH   HOH A . 
L 4 HOH   21  521 6   HOH   HOH A . 
L 4 HOH   22  522 32  HOH   HOH A . 
L 4 HOH   23  523 254 HOH   HOH A . 
L 4 HOH   24  524 228 HOH   HOH A . 
L 4 HOH   25  525 91  HOH   HOH A . 
L 4 HOH   26  526 48  HOH   HOH A . 
L 4 HOH   27  527 156 HOH   HOH A . 
L 4 HOH   28  528 255 HOH   HOH A . 
L 4 HOH   29  529 99  HOH   HOH A . 
L 4 HOH   30  530 1   HOH   HOH A . 
L 4 HOH   31  531 12  HOH   HOH A . 
L 4 HOH   32  532 161 HOH   HOH A . 
L 4 HOH   33  533 195 HOH   HOH A . 
L 4 HOH   34  534 63  HOH   HOH A . 
L 4 HOH   35  535 147 HOH   HOH A . 
L 4 HOH   36  536 128 HOH   HOH A . 
L 4 HOH   37  537 224 HOH   HOH A . 
L 4 HOH   38  538 257 HOH   HOH A . 
L 4 HOH   39  539 191 HOH   HOH A . 
L 4 HOH   40  540 266 HOH   HOH A . 
L 4 HOH   41  541 153 HOH   HOH A . 
L 4 HOH   42  542 122 HOH   HOH A . 
L 4 HOH   43  543 220 HOH   HOH A . 
L 4 HOH   44  544 93  HOH   HOH A . 
L 4 HOH   45  545 184 HOH   HOH A . 
L 4 HOH   46  546 13  HOH   HOH A . 
L 4 HOH   47  547 188 HOH   HOH A . 
L 4 HOH   48  548 41  HOH   HOH A . 
L 4 HOH   49  549 132 HOH   HOH A . 
L 4 HOH   50  550 100 HOH   HOH A . 
L 4 HOH   51  551 35  HOH   HOH A . 
L 4 HOH   52  552 49  HOH   HOH A . 
L 4 HOH   53  553 206 HOH   HOH A . 
L 4 HOH   54  554 209 HOH   HOH A . 
L 4 HOH   55  555 226 HOH   HOH A . 
L 4 HOH   56  556 45  HOH   HOH A . 
L 4 HOH   57  557 229 HOH   HOH A . 
L 4 HOH   58  558 109 HOH   HOH A . 
L 4 HOH   59  559 249 HOH   HOH A . 
L 4 HOH   60  560 207 HOH   HOH A . 
L 4 HOH   61  561 11  HOH   HOH A . 
L 4 HOH   62  562 154 HOH   HOH A . 
L 4 HOH   63  563 25  HOH   HOH A . 
L 4 HOH   64  564 123 HOH   HOH A . 
L 4 HOH   65  565 196 HOH   HOH A . 
L 4 HOH   66  566 163 HOH   HOH A . 
L 4 HOH   67  567 108 HOH   HOH A . 
L 4 HOH   68  568 129 HOH   HOH A . 
L 4 HOH   69  569 270 HOH   HOH A . 
L 4 HOH   70  570 126 HOH   HOH A . 
L 4 HOH   71  571 55  HOH   HOH A . 
L 4 HOH   72  572 269 HOH   HOH A . 
L 4 HOH   73  573 261 HOH   HOH A . 
L 4 HOH   74  574 172 HOH   HOH A . 
L 4 HOH   75  575 167 HOH   HOH A . 
L 4 HOH   76  576 74  HOH   HOH A . 
L 4 HOH   77  577 101 HOH   HOH A . 
L 4 HOH   78  578 256 HOH   HOH A . 
L 4 HOH   79  579 40  HOH   HOH A . 
L 4 HOH   80  580 148 HOH   HOH A . 
L 4 HOH   81  581 186 HOH   HOH A . 
L 4 HOH   82  582 246 HOH   HOH A . 
L 4 HOH   83  583 92  HOH   HOH A . 
L 4 HOH   84  584 58  HOH   HOH A . 
L 4 HOH   85  585 213 HOH   HOH A . 
L 4 HOH   86  586 275 HOH   HOH A . 
L 4 HOH   87  587 212 HOH   HOH A . 
L 4 HOH   88  588 222 HOH   HOH A . 
L 4 HOH   89  589 53  HOH   HOH A . 
L 4 HOH   90  590 265 HOH   HOH A . 
L 4 HOH   91  591 80  HOH   HOH A . 
L 4 HOH   92  592 113 HOH   HOH A . 
L 4 HOH   93  593 145 HOH   HOH A . 
L 4 HOH   94  594 244 HOH   HOH A . 
L 4 HOH   95  595 43  HOH   HOH A . 
L 4 HOH   96  596 262 HOH   HOH A . 
L 4 HOH   97  597 221 HOH   HOH A . 
L 4 HOH   98  598 230 HOH   HOH A . 
L 4 HOH   99  599 211 HOH   HOH A . 
L 4 HOH   100 600 217 HOH   HOH A . 
L 4 HOH   101 601 277 HOH   HOH A . 
M 4 HOH   1   601 205 HOH   HOH B . 
M 4 HOH   2   602 152 HOH   HOH B . 
M 4 HOH   3   603 83  HOH   HOH B . 
M 4 HOH   4   604 21  HOH   HOH B . 
M 4 HOH   5   605 248 HOH   HOH B . 
M 4 HOH   6   606 102 HOH   HOH B . 
M 4 HOH   7   607 164 HOH   HOH B . 
M 4 HOH   8   608 98  HOH   HOH B . 
M 4 HOH   9   609 65  HOH   HOH B . 
M 4 HOH   10  610 193 HOH   HOH B . 
M 4 HOH   11  611 199 HOH   HOH B . 
M 4 HOH   12  612 51  HOH   HOH B . 
M 4 HOH   13  613 62  HOH   HOH B . 
M 4 HOH   14  614 263 HOH   HOH B . 
M 4 HOH   15  615 173 HOH   HOH B . 
M 4 HOH   16  616 237 HOH   HOH B . 
M 4 HOH   17  617 2   HOH   HOH B . 
M 4 HOH   18  618 61  HOH   HOH B . 
M 4 HOH   19  619 179 HOH   HOH B . 
M 4 HOH   20  620 150 HOH   HOH B . 
M 4 HOH   21  621 142 HOH   HOH B . 
M 4 HOH   22  622 68  HOH   HOH B . 
M 4 HOH   23  623 112 HOH   HOH B . 
M 4 HOH   24  624 225 HOH   HOH B . 
M 4 HOH   25  625 139 HOH   HOH B . 
M 4 HOH   26  626 242 HOH   HOH B . 
M 4 HOH   27  627 240 HOH   HOH B . 
M 4 HOH   28  628 268 HOH   HOH B . 
M 4 HOH   29  629 176 HOH   HOH B . 
M 4 HOH   30  630 169 HOH   HOH B . 
M 4 HOH   31  631 235 HOH   HOH B . 
M 4 HOH   32  632 198 HOH   HOH B . 
M 4 HOH   33  633 231 HOH   HOH B . 
M 4 HOH   34  634 42  HOH   HOH B . 
M 4 HOH   35  635 90  HOH   HOH B . 
M 4 HOH   36  636 72  HOH   HOH B . 
M 4 HOH   37  637 94  HOH   HOH B . 
M 4 HOH   38  638 238 HOH   HOH B . 
M 4 HOH   39  639 247 HOH   HOH B . 
M 4 HOH   40  640 149 HOH   HOH B . 
M 4 HOH   41  641 210 HOH   HOH B . 
M 4 HOH   42  642 216 HOH   HOH B . 
M 4 HOH   43  643 144 HOH   HOH B . 
M 4 HOH   44  644 197 HOH   HOH B . 
M 4 HOH   45  645 95  HOH   HOH B . 
M 4 HOH   46  646 134 HOH   HOH B . 
M 4 HOH   47  647 103 HOH   HOH B . 
M 4 HOH   48  648 264 HOH   HOH B . 
M 4 HOH   49  649 273 HOH   HOH B . 
M 4 HOH   50  650 201 HOH   HOH B . 
M 4 HOH   51  651 278 HOH   HOH B . 
M 4 HOH   52  652 276 HOH   HOH B . 
N 4 HOH   1   501 56  HOH   HOH C . 
N 4 HOH   2   502 19  HOH   HOH C . 
N 4 HOH   3   503 143 HOH   HOH C . 
N 4 HOH   4   504 31  HOH   HOH C . 
N 4 HOH   5   505 119 HOH   HOH C . 
N 4 HOH   6   506 5   HOH   HOH C . 
N 4 HOH   7   507 125 HOH   HOH C . 
N 4 HOH   8   508 133 HOH   HOH C . 
N 4 HOH   9   509 138 HOH   HOH C . 
N 4 HOH   10  510 3   HOH   HOH C . 
N 4 HOH   11  511 67  HOH   HOH C . 
N 4 HOH   12  512 47  HOH   HOH C . 
N 4 HOH   13  513 151 HOH   HOH C . 
N 4 HOH   14  514 120 HOH   HOH C . 
N 4 HOH   15  515 14  HOH   HOH C . 
N 4 HOH   16  516 75  HOH   HOH C . 
N 4 HOH   17  517 241 HOH   HOH C . 
N 4 HOH   18  518 215 HOH   HOH C . 
N 4 HOH   19  519 8   HOH   HOH C . 
N 4 HOH   20  520 223 HOH   HOH C . 
N 4 HOH   21  521 166 HOH   HOH C . 
N 4 HOH   22  522 84  HOH   HOH C . 
N 4 HOH   23  523 85  HOH   HOH C . 
N 4 HOH   24  524 260 HOH   HOH C . 
N 4 HOH   25  525 236 HOH   HOH C . 
N 4 HOH   26  526 73  HOH   HOH C . 
N 4 HOH   27  527 28  HOH   HOH C . 
N 4 HOH   28  528 26  HOH   HOH C . 
N 4 HOH   29  529 160 HOH   HOH C . 
N 4 HOH   30  530 37  HOH   HOH C . 
N 4 HOH   31  531 10  HOH   HOH C . 
N 4 HOH   32  532 77  HOH   HOH C . 
N 4 HOH   33  533 157 HOH   HOH C . 
N 4 HOH   34  534 33  HOH   HOH C . 
N 4 HOH   35  535 70  HOH   HOH C . 
N 4 HOH   36  536 86  HOH   HOH C . 
N 4 HOH   37  537 245 HOH   HOH C . 
N 4 HOH   38  538 22  HOH   HOH C . 
N 4 HOH   39  539 239 HOH   HOH C . 
N 4 HOH   40  540 105 HOH   HOH C . 
N 4 HOH   41  541 23  HOH   HOH C . 
N 4 HOH   42  542 78  HOH   HOH C . 
N 4 HOH   43  543 146 HOH   HOH C . 
N 4 HOH   44  544 82  HOH   HOH C . 
N 4 HOH   45  545 115 HOH   HOH C . 
N 4 HOH   46  546 117 HOH   HOH C . 
N 4 HOH   47  547 202 HOH   HOH C . 
N 4 HOH   48  548 44  HOH   HOH C . 
N 4 HOH   49  549 20  HOH   HOH C . 
N 4 HOH   50  550 190 HOH   HOH C . 
N 4 HOH   51  551 89  HOH   HOH C . 
N 4 HOH   52  552 71  HOH   HOH C . 
N 4 HOH   53  553 38  HOH   HOH C . 
N 4 HOH   54  554 177 HOH   HOH C . 
N 4 HOH   55  555 118 HOH   HOH C . 
N 4 HOH   56  556 79  HOH   HOH C . 
N 4 HOH   57  557 187 HOH   HOH C . 
N 4 HOH   58  558 59  HOH   HOH C . 
N 4 HOH   59  559 135 HOH   HOH C . 
N 4 HOH   60  560 136 HOH   HOH C . 
N 4 HOH   61  561 168 HOH   HOH C . 
N 4 HOH   62  562 50  HOH   HOH C . 
N 4 HOH   63  563 54  HOH   HOH C . 
N 4 HOH   64  564 116 HOH   HOH C . 
N 4 HOH   65  565 81  HOH   HOH C . 
N 4 HOH   66  566 243 HOH   HOH C . 
N 4 HOH   67  567 218 HOH   HOH C . 
N 4 HOH   68  568 39  HOH   HOH C . 
N 4 HOH   69  569 251 HOH   HOH C . 
N 4 HOH   70  570 107 HOH   HOH C . 
N 4 HOH   71  571 155 HOH   HOH C . 
N 4 HOH   72  572 178 HOH   HOH C . 
N 4 HOH   73  573 97  HOH   HOH C . 
N 4 HOH   74  574 16  HOH   HOH C . 
N 4 HOH   75  575 127 HOH   HOH C . 
N 4 HOH   76  576 29  HOH   HOH C . 
N 4 HOH   77  577 4   HOH   HOH C . 
N 4 HOH   78  578 203 HOH   HOH C . 
N 4 HOH   79  579 250 HOH   HOH C . 
N 4 HOH   80  580 182 HOH   HOH C . 
N 4 HOH   81  581 66  HOH   HOH C . 
N 4 HOH   82  582 130 HOH   HOH C . 
N 4 HOH   83  583 30  HOH   HOH C . 
N 4 HOH   84  584 141 HOH   HOH C . 
N 4 HOH   85  585 159 HOH   HOH C . 
N 4 HOH   86  586 34  HOH   HOH C . 
N 4 HOH   87  587 7   HOH   HOH C . 
N 4 HOH   88  588 170 HOH   HOH C . 
N 4 HOH   89  589 158 HOH   HOH C . 
N 4 HOH   90  590 181 HOH   HOH C . 
N 4 HOH   91  591 57  HOH   HOH C . 
N 4 HOH   92  592 140 HOH   HOH C . 
N 4 HOH   93  593 204 HOH   HOH C . 
N 4 HOH   94  594 15  HOH   HOH C . 
N 4 HOH   95  595 194 HOH   HOH C . 
N 4 HOH   96  596 131 HOH   HOH C . 
N 4 HOH   97  597 88  HOH   HOH C . 
N 4 HOH   98  598 52  HOH   HOH C . 
N 4 HOH   99  599 106 HOH   HOH C . 
N 4 HOH   100 600 175 HOH   HOH C . 
N 4 HOH   101 601 259 HOH   HOH C . 
N 4 HOH   102 602 208 HOH   HOH C . 
N 4 HOH   103 603 274 HOH   HOH C . 
N 4 HOH   104 604 253 HOH   HOH C . 
N 4 HOH   105 605 233 HOH   HOH C . 
N 4 HOH   106 606 232 HOH   HOH C . 
N 4 HOH   107 607 104 HOH   HOH C . 
N 4 HOH   108 608 258 HOH   HOH C . 
N 4 HOH   109 609 110 HOH   HOH C . 
N 4 HOH   110 610 174 HOH   HOH C . 
N 4 HOH   111 611 214 HOH   HOH C . 
N 4 HOH   112 612 185 HOH   HOH C . 
N 4 HOH   113 613 96  HOH   HOH C . 
N 4 HOH   114 614 183 HOH   HOH C . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1 1 Y 1 B HIS 133 ? CA  ? B HIS 127 CA  
2 1 Y 1 B HIS 133 ? CB  ? B HIS 127 CB  
3 1 Y 1 B HIS 133 ? CG  ? B HIS 127 CG  
4 1 Y 1 B HIS 133 ? ND1 ? B HIS 127 ND1 
5 1 Y 1 B HIS 133 ? CD2 ? B HIS 127 CD2 
6 1 Y 1 B HIS 133 ? CE1 ? B HIS 127 CE1 
7 1 Y 1 B HIS 133 ? NE2 ? B HIS 127 NE2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement     ? ? ? ? ? ? ? ? ? ? ? BUSTER  ? ? ? '2.11.7 PACIOREK' 1 
? 'data scaling' ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .                 2 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8RGF 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     46.940 
_cell.length_a_esd                 ? 
_cell.length_b                     135.160 
_cell.length_b_esd                 ? 
_cell.length_c                     145.150 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        12 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         8RGF 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8RGF 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.10 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          41.46 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
;13-18% PEG3350, 
0.2-0.35M Am. Cit. pH7.0
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 12M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2017-10-26 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.976 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'ESRF BEAMLINE ID30B' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.976 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   ID30B 
_diffrn_source.pdbx_synchrotron_site       ESRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8RGF 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.856 
_reflns.d_resolution_low                               98.916 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     78897 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.7 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.3 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          14.2 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.065 
_reflns.pdbx_Rpim_I_all                                0.026 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       498259 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   ? 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.060 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.856 
_reflns_shell.d_res_low                                     1.888 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           24185 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             3869 
_reflns_shell.percent_possible_obs                          99.3 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               6.3 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     2.4 
_reflns_shell.pdbx_Rrim_I_all                               0.673 
_reflns_shell.pdbx_Rpim_I_all                               0.267 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  ? 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.616 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            -17.85500 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            0.00000 
_refine.aniso_B[2][2]                            4.96170 
_refine.aniso_B[2][3]                            0.00000 
_refine.aniso_B[3][3]                            12.89330 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               51.78 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.908 
_refine.correlation_coeff_Fo_to_Fc_free          0.904 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 8RGF 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.86 
_refine.ls_d_res_low                             98.916 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     78399 
_refine.ls_number_reflns_R_free                  3781 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.7 
_refine.ls_percent_reflns_R_free                 4.820 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.240 
_refine.ls_R_factor_R_free                       0.260 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.239 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.000 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.151 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.150 
_refine.pdbx_overall_SU_R_Blow_DPI               0.177 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_R_Cruickshank_DPI             0.177 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_analyze.entry_id                        8RGF 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_coordinate_error_obs    0.30 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_sigma_a_free_details    ? 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_sigma_a_obs_details     ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
_refine_analyze.RG_d_res_high                   ? 
_refine_analyze.RG_d_res_low                    ? 
_refine_analyze.RG_free                         ? 
_refine_analyze.RG_work                         ? 
_refine_analyze.RG_free_work_ratio              ? 
_refine_analyze.pdbx_Luzzati_d_res_high_obs     ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.86 
_refine_hist.d_res_low                        98.916 
_refine_hist.number_atoms_solvent             267 
_refine_hist.number_atoms_total               7644 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        7337 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         40 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.010 ? 7533  ? t_bond_d                  2.00  HARMONIC     
'X-RAY DIFFRACTION' ? 1.08  ? 10258 ? t_angle_deg               2.00  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 2543  ? t_dihedral_angle_d        2.00  SINUSOIDAL   
'X-RAY DIFFRACTION' ? ?     ? ?     ? t_incorr_chiral_ct        ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?     ? t_pseud_angle             ?     ?            
'X-RAY DIFFRACTION' ? ?     ? 179   ? t_trig_c_planes           2.00  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 1102  ? t_gen_planes              5.00  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 7533  ? t_it                      20.00 HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 1     ? t_nbd                     5.00  SEMIHARMONIC 
'X-RAY DIFFRACTION' ? 3.15  ? ?     ? t_omega_torsion           ?     ?            
'X-RAY DIFFRACTION' ? 17.92 ? ?     ? t_other_torsion           ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?     ? t_improper_torsion        ?     ?            
'X-RAY DIFFRACTION' ? ?     ? 996   ? t_chiral_improper_torsion 5.00  SEMIHARMONIC 
'X-RAY DIFFRACTION' ? ?     ? ?     ? t_sum_occupancies         ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?     ? t_utility_distance        ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?     ? t_utility_angle           ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?     ? t_utility_torsion         ?     ?            
'X-RAY DIFFRACTION' ? ?     ? 8874  ? t_ideal_dist_contact      4.00  SEMIHARMONIC 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.86 
_refine_ls_shell.d_res_low                        1.91 
_refine_ls_shell.number_reflns_all                5728 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             289 
_refine_ls_shell.number_reflns_R_work             5439 
_refine_ls_shell.percent_reflns_obs               99.76 
_refine_ls_shell.percent_reflns_R_free            5.05 
_refine_ls_shell.R_factor_all                     0.2735 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.2719 
_refine_ls_shell.redundancy_reflns_all            ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.wR_factor_all                    ? 
_refine_ls_shell.wR_factor_obs                    ? 
_refine_ls_shell.wR_factor_R_free                 ? 
_refine_ls_shell.wR_factor_R_work                 ? 
_refine_ls_shell.pdbx_R_complete                  ? 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
_refine_ls_shell.R_factor_R_free                  0.3052 
# 
_struct.entry_id                     8RGF 
_struct.title                        'Arginase 2 in complex with inhibitor' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        8RGF 
_struct_keywords.text            'arginase, inhibitor, complex, HYDROLASE' 
_struct_keywords.pdbx_keywords   HYDROLASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 1 ? 
D N N 2 ? 
E N N 2 ? 
F N N 3 ? 
G N N 2 ? 
H N N 2 ? 
I N N 2 ? 
J N N 2 ? 
K N N 3 ? 
L N N 4 ? 
M N N 4 ? 
N N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    ARGI2_HUMAN 
_struct_ref.pdbx_db_accession          P78540 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;SVHSVAVIGAPFSQGQKRKGVEHGPAAIREAGLMKRLSSLGCHLKDFGDLSFTPVPKDDLYNNLIVNPRSVGLANQELAE
VVSRAVSDGYSCVTLGGDHSLAIGTISGHARHCPDLCVVWVDAHADINTPLTTSSGNLHGQPVSFLLRELQDKVPQLPGF
SWIKPCISSASIVYIGLRDVDPPEHFILKNYDIQYFSMRDIDRLGIQKVMERTFDLLIGKRQRPIHLSFDIDAFDPTLAP
ATGTPVVGGLTYREGMYIAEEIHNTGLLSALDLVEVNPQLATSEEEAKTTANLAVDVIASSFGQTREGGHIVYDQLPTPS

;
_struct_ref.pdbx_align_begin           22 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 8RGF A 16 ? 335 ? P78540 22 ? 341 ? 22 341 
2 1 8RGF B 16 ? 335 ? P78540 22 ? 341 ? 22 341 
3 1 8RGF C 16 ? 335 ? P78540 22 ? 341 ? 22 341 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 8RGF HIS A 1  ? UNP P78540 ? ? 'expression tag' 7  1  
1 8RGF HIS A 2  ? UNP P78540 ? ? 'expression tag' 8  2  
1 8RGF HIS A 3  ? UNP P78540 ? ? 'expression tag' 9  3  
1 8RGF HIS A 4  ? UNP P78540 ? ? 'expression tag' 10 4  
1 8RGF HIS A 5  ? UNP P78540 ? ? 'expression tag' 11 5  
1 8RGF HIS A 6  ? UNP P78540 ? ? 'expression tag' 12 6  
1 8RGF GLY A 7  ? UNP P78540 ? ? 'expression tag' 13 7  
1 8RGF GLY A 8  ? UNP P78540 ? ? 'expression tag' 14 8  
1 8RGF GLY A 9  ? UNP P78540 ? ? 'expression tag' 15 9  
1 8RGF GLU A 10 ? UNP P78540 ? ? 'expression tag' 16 10 
1 8RGF ASN A 11 ? UNP P78540 ? ? 'expression tag' 17 11 
1 8RGF LEU A 12 ? UNP P78540 ? ? 'expression tag' 18 12 
1 8RGF TYR A 13 ? UNP P78540 ? ? 'expression tag' 19 13 
1 8RGF PHE A 14 ? UNP P78540 ? ? 'expression tag' 20 14 
1 8RGF GLN A 15 ? UNP P78540 ? ? 'expression tag' 21 15 
2 8RGF HIS B 1  ? UNP P78540 ? ? 'expression tag' 7  16 
2 8RGF HIS B 2  ? UNP P78540 ? ? 'expression tag' 8  17 
2 8RGF HIS B 3  ? UNP P78540 ? ? 'expression tag' 9  18 
2 8RGF HIS B 4  ? UNP P78540 ? ? 'expression tag' 10 19 
2 8RGF HIS B 5  ? UNP P78540 ? ? 'expression tag' 11 20 
2 8RGF HIS B 6  ? UNP P78540 ? ? 'expression tag' 12 21 
2 8RGF GLY B 7  ? UNP P78540 ? ? 'expression tag' 13 22 
2 8RGF GLY B 8  ? UNP P78540 ? ? 'expression tag' 14 23 
2 8RGF GLY B 9  ? UNP P78540 ? ? 'expression tag' 15 24 
2 8RGF GLU B 10 ? UNP P78540 ? ? 'expression tag' 16 25 
2 8RGF ASN B 11 ? UNP P78540 ? ? 'expression tag' 17 26 
2 8RGF LEU B 12 ? UNP P78540 ? ? 'expression tag' 18 27 
2 8RGF TYR B 13 ? UNP P78540 ? ? 'expression tag' 19 28 
2 8RGF PHE B 14 ? UNP P78540 ? ? 'expression tag' 20 29 
2 8RGF GLN B 15 ? UNP P78540 ? ? 'expression tag' 21 30 
3 8RGF HIS C 1  ? UNP P78540 ? ? 'expression tag' 7  31 
3 8RGF HIS C 2  ? UNP P78540 ? ? 'expression tag' 8  32 
3 8RGF HIS C 3  ? UNP P78540 ? ? 'expression tag' 9  33 
3 8RGF HIS C 4  ? UNP P78540 ? ? 'expression tag' 10 34 
3 8RGF HIS C 5  ? UNP P78540 ? ? 'expression tag' 11 35 
3 8RGF HIS C 6  ? UNP P78540 ? ? 'expression tag' 12 36 
3 8RGF GLY C 7  ? UNP P78540 ? ? 'expression tag' 13 37 
3 8RGF GLY C 8  ? UNP P78540 ? ? 'expression tag' 14 38 
3 8RGF GLY C 9  ? UNP P78540 ? ? 'expression tag' 15 39 
3 8RGF GLU C 10 ? UNP P78540 ? ? 'expression tag' 16 40 
3 8RGF ASN C 11 ? UNP P78540 ? ? 'expression tag' 17 41 
3 8RGF LEU C 12 ? UNP P78540 ? ? 'expression tag' 18 42 
3 8RGF TYR C 13 ? UNP P78540 ? ? 'expression tag' 19 43 
3 8RGF PHE C 14 ? UNP P78540 ? ? 'expression tag' 20 44 
3 8RGF GLN C 15 ? UNP P78540 ? ? 'expression tag' 21 45 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   trimeric 
_pdbx_struct_assembly.oligomeric_count     3 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 6980  ? 
1 MORE         -44   ? 
1 'SSA (A^2)'  35450 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M,N 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 GLY A 35  ? GLU A 37  ? GLY A 41  GLU A 43  5 ? 3  
HELX_P HELX_P2  AA2 HIS A 38  ? ALA A 46  ? HIS A 44  ALA A 52  1 ? 9  
HELX_P HELX_P3  AA3 GLY A 47  ? SER A 54  ? GLY A 53  SER A 60  1 ? 8  
HELX_P HELX_P4  AA4 ASN A 82  ? ASP A 103 ? ASN A 88  ASP A 109 1 ? 22 
HELX_P HELX_P5  AA5 ASP A 113 ? SER A 115 ? ASP A 119 SER A 121 5 ? 3  
HELX_P HELX_P6  AA6 LEU A 116 ? ARG A 126 ? LEU A 122 ARG A 132 1 ? 11 
HELX_P HELX_P7  AA7 ASN A 152 ? GLY A 155 ? ASN A 158 GLY A 161 5 ? 4  
HELX_P HELX_P8  AA8 GLN A 156 ? LEU A 162 ? GLN A 162 LEU A 168 1 ? 7  
HELX_P HELX_P9  AA9 ARG A 163 ? VAL A 169 ? ARG A 169 VAL A 175 5 ? 7  
HELX_P HELX_P10 AB1 SER A 183 ? ALA A 185 ? SER A 189 ALA A 191 5 ? 3  
HELX_P HELX_P11 AB2 ASP A 196 ? TYR A 206 ? ASP A 202 TYR A 212 1 ? 11 
HELX_P HELX_P12 AB3 MET A 213 ? GLY A 220 ? MET A 219 GLY A 226 1 ? 8  
HELX_P HELX_P13 AB4 GLY A 220 ? GLY A 234 ? GLY A 226 GLY A 240 1 ? 15 
HELX_P HELX_P14 AB5 ASP A 247 ? PHE A 249 ? ASP A 253 PHE A 255 5 ? 3  
HELX_P HELX_P15 AB6 THR A 266 ? GLY A 281 ? THR A 272 GLY A 287 1 ? 16 
HELX_P HELX_P16 AB7 ASN A 292 ? ALA A 296 ? ASN A 298 ALA A 302 5 ? 5  
HELX_P HELX_P17 AB8 SER A 298 ? PHE A 317 ? SER A 304 PHE A 323 1 ? 20 
HELX_P HELX_P18 AB9 GLY B 35  ? GLU B 37  ? GLY B 41  GLU B 43  5 ? 3  
HELX_P HELX_P19 AC1 HIS B 38  ? GLY B 47  ? HIS B 44  GLY B 53  1 ? 10 
HELX_P HELX_P20 AC2 GLY B 47  ? LEU B 55  ? GLY B 53  LEU B 61  1 ? 9  
HELX_P HELX_P21 AC3 LEU B 75  ? LEU B 79  ? LEU B 81  LEU B 85  5 ? 5  
HELX_P HELX_P22 AC4 ASN B 82  ? GLY B 104 ? ASN B 88  GLY B 110 1 ? 23 
HELX_P HELX_P23 AC5 ASP B 113 ? SER B 115 ? ASP B 119 SER B 121 5 ? 3  
HELX_P HELX_P24 AC6 LEU B 116 ? ARG B 126 ? LEU B 122 ARG B 132 1 ? 11 
HELX_P HELX_P25 AC7 ASN B 152 ? GLY B 155 ? ASN B 158 GLY B 161 5 ? 4  
HELX_P HELX_P26 AC8 GLN B 156 ? LEU B 162 ? GLN B 162 LEU B 168 1 ? 7  
HELX_P HELX_P27 AC9 LEU B 165 ? VAL B 169 ? LEU B 171 VAL B 175 5 ? 5  
HELX_P HELX_P28 AD1 SER B 183 ? ALA B 185 ? SER B 189 ALA B 191 5 ? 3  
HELX_P HELX_P29 AD2 ASP B 196 ? TYR B 206 ? ASP B 202 TYR B 212 1 ? 11 
HELX_P HELX_P30 AD3 SER B 212 ? GLY B 220 ? SER B 218 GLY B 226 1 ? 9  
HELX_P HELX_P31 AD4 GLY B 220 ? ILE B 233 ? GLY B 226 ILE B 239 1 ? 14 
HELX_P HELX_P32 AD5 ASP B 247 ? PHE B 249 ? ASP B 253 PHE B 255 5 ? 3  
HELX_P HELX_P33 AD6 THR B 266 ? GLY B 281 ? THR B 272 GLY B 287 1 ? 16 
HELX_P HELX_P34 AD7 ASN B 292 ? ALA B 296 ? ASN B 298 ALA B 302 5 ? 5  
HELX_P HELX_P35 AD8 SER B 298 ? PHE B 317 ? SER B 304 PHE B 323 1 ? 20 
HELX_P HELX_P36 AD9 GLY C 35  ? GLU C 37  ? GLY C 41  GLU C 43  5 ? 3  
HELX_P HELX_P37 AE1 HIS C 38  ? ALA C 46  ? HIS C 44  ALA C 52  1 ? 9  
HELX_P HELX_P38 AE2 GLY C 47  ? LEU C 55  ? GLY C 53  LEU C 61  1 ? 9  
HELX_P HELX_P39 AE3 LEU C 75  ? LEU C 79  ? LEU C 81  LEU C 85  5 ? 5  
HELX_P HELX_P40 AE4 ASN C 82  ? ASP C 103 ? ASN C 88  ASP C 109 1 ? 22 
HELX_P HELX_P41 AE5 ASP C 113 ? SER C 115 ? ASP C 119 SER C 121 5 ? 3  
HELX_P HELX_P42 AE6 LEU C 116 ? CYS C 128 ? LEU C 122 CYS C 134 1 ? 13 
HELX_P HELX_P43 AE7 ASN C 152 ? GLY C 155 ? ASN C 158 GLY C 161 5 ? 4  
HELX_P HELX_P44 AE8 GLN C 156 ? LEU C 162 ? GLN C 162 LEU C 168 1 ? 7  
HELX_P HELX_P45 AE9 ARG C 163 ? VAL C 169 ? ARG C 169 VAL C 175 5 ? 7  
HELX_P HELX_P46 AF1 SER C 183 ? ALA C 185 ? SER C 189 ALA C 191 5 ? 3  
HELX_P HELX_P47 AF2 ASP C 196 ? TYR C 206 ? ASP C 202 TYR C 212 1 ? 11 
HELX_P HELX_P48 AF3 SER C 212 ? GLY C 220 ? SER C 218 GLY C 226 1 ? 9  
HELX_P HELX_P49 AF4 GLY C 220 ? GLY C 234 ? GLY C 226 GLY C 240 1 ? 15 
HELX_P HELX_P50 AF5 ASP C 247 ? PHE C 249 ? ASP C 253 PHE C 255 5 ? 3  
HELX_P HELX_P51 AF6 THR C 266 ? THR C 280 ? THR C 272 THR C 286 1 ? 15 
HELX_P HELX_P52 AF7 ASN C 292 ? ALA C 296 ? ASN C 298 ALA C 302 5 ? 5  
HELX_P HELX_P53 AF8 SER C 298 ? PHE C 317 ? SER C 304 PHE C 323 1 ? 20 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1  metalc ? ? A HIS 114 ND1 ? ? ? 1_555 D MN    . MN  ? ? A HIS 120 A MN    401 1_555 ? ? ? ? ? ? ? 2.104 ? ? 
metalc2  metalc ? ? A ASP 137 OD2 ? ? ? 1_555 D MN    . MN  ? ? A ASP 143 A MN    401 1_555 ? ? ? ? ? ? ? 2.141 ? ? 
metalc3  metalc ? ? A ASP 137 OD1 ? ? ? 1_555 E MN    . MN  ? ? A ASP 143 A MN    402 1_555 ? ? ? ? ? ? ? 2.221 ? ? 
metalc4  metalc ? ? A HIS 139 ND1 ? ? ? 1_555 E MN    . MN  ? ? A HIS 145 A MN    402 1_555 ? ? ? ? ? ? ? 2.272 ? ? 
metalc5  metalc ? ? A ASP 141 OD2 ? ? ? 1_555 D MN    . MN  ? ? A ASP 147 A MN    401 1_555 ? ? ? ? ? ? ? 2.104 ? ? 
metalc6  metalc ? ? A ASP 245 OD2 ? ? ? 1_555 D MN    . MN  ? ? A ASP 251 A MN    401 1_555 ? ? ? ? ? ? ? 2.270 ? ? 
metalc7  metalc ? ? A ASP 245 OD2 ? ? ? 1_555 E MN    . MN  ? ? A ASP 251 A MN    402 1_555 ? ? ? ? ? ? ? 2.460 ? ? 
metalc8  metalc ? ? A ASP 247 OD1 ? ? ? 1_555 E MN    . MN  ? ? A ASP 253 A MN    402 1_555 ? ? ? ? ? ? ? 2.443 ? ? 
metalc9  metalc ? ? A ASP 247 OD2 ? ? ? 1_555 E MN    . MN  ? ? A ASP 253 A MN    402 1_555 ? ? ? ? ? ? ? 2.269 ? ? 
metalc10 metalc ? ? D MN  .   MN  ? ? ? 1_555 F A1H0A . O14 ? ? A MN  401 A A1H0A 403 1_555 ? ? ? ? ? ? ? 2.123 ? ? 
metalc11 metalc ? ? E MN  .   MN  ? ? ? 1_555 F A1H0A . O17 ? ? A MN  402 A A1H0A 403 1_555 ? ? ? ? ? ? ? 2.665 ? ? 
metalc12 metalc ? ? E MN  .   MN  ? ? ? 1_555 F A1H0A . O14 ? ? A MN  402 A A1H0A 403 1_555 ? ? ? ? ? ? ? 2.545 ? ? 
metalc13 metalc ? ? B HIS 114 ND1 ? ? ? 1_555 G MN    . MN  ? ? B HIS 120 B MN    500 1_555 ? ? ? ? ? ? ? 2.291 ? ? 
metalc14 metalc ? ? B ASP 137 OD2 ? ? ? 1_555 G MN    . MN  ? ? B ASP 143 B MN    500 1_555 ? ? ? ? ? ? ? 2.140 ? ? 
metalc15 metalc ? ? B ASP 137 OD1 ? ? ? 1_555 H MN    . MN  ? ? B ASP 143 B MN    501 1_555 ? ? ? ? ? ? ? 2.229 ? ? 
metalc16 metalc ? ? B HIS 139 ND1 ? ? ? 1_555 H MN    . MN  ? ? B HIS 145 B MN    501 1_555 ? ? ? ? ? ? ? 2.368 ? ? 
metalc17 metalc ? ? B ASP 141 OD2 ? ? ? 1_555 G MN    . MN  ? ? B ASP 147 B MN    500 1_555 ? ? ? ? ? ? ? 2.298 ? ? 
metalc18 metalc ? ? B ASP 245 OD2 ? ? ? 1_555 G MN    . MN  ? ? B ASP 251 B MN    500 1_555 ? ? ? ? ? ? ? 2.366 ? ? 
metalc19 metalc ? ? B ASP 245 OD2 ? ? ? 1_555 H MN    . MN  ? ? B ASP 251 B MN    501 1_555 ? ? ? ? ? ? ? 2.547 ? ? 
metalc20 metalc ? ? B ASP 247 OD1 ? ? ? 1_555 H MN    . MN  ? ? B ASP 253 B MN    501 1_555 ? ? ? ? ? ? ? 2.226 ? ? 
metalc21 metalc ? ? B ASP 247 OD2 ? ? ? 1_555 H MN    . MN  ? ? B ASP 253 B MN    501 1_555 ? ? ? ? ? ? ? 2.000 ? ? 
metalc22 metalc ? ? G MN  .   MN  ? ? ? 1_555 M HOH   . O   ? ? B MN  500 B HOH   637 1_555 ? ? ? ? ? ? ? 2.718 ? ? 
metalc23 metalc ? ? H MN  .   MN  ? ? ? 1_555 M HOH   . O   ? ? B MN  501 B HOH   637 1_555 ? ? ? ? ? ? ? 2.561 ? ? 
metalc24 metalc ? ? C HIS 114 ND1 ? ? ? 1_555 I MN    . MN  ? ? C HIS 120 C MN    401 1_555 ? ? ? ? ? ? ? 2.125 ? ? 
metalc25 metalc ? ? C ASP 137 OD2 ? ? ? 1_555 I MN    . MN  ? ? C ASP 143 C MN    401 1_555 ? ? ? ? ? ? ? 2.117 ? ? 
metalc26 metalc ? ? C ASP 137 OD1 ? ? ? 1_555 J MN    . MN  ? ? C ASP 143 C MN    402 1_555 ? ? ? ? ? ? ? 2.193 ? ? 
metalc27 metalc ? ? C HIS 139 ND1 ? ? ? 1_555 J MN    . MN  ? ? C HIS 145 C MN    402 1_555 ? ? ? ? ? ? ? 2.242 ? ? 
metalc28 metalc ? ? C ASP 141 OD2 ? ? ? 1_555 I MN    . MN  ? ? C ASP 147 C MN    401 1_555 ? ? ? ? ? ? ? 2.186 ? ? 
metalc29 metalc ? ? C ASP 245 OD2 ? ? ? 1_555 I MN    . MN  ? ? C ASP 251 C MN    401 1_555 ? ? ? ? ? ? ? 2.258 ? ? 
metalc30 metalc ? ? C ASP 245 OD2 ? ? ? 1_555 J MN    . MN  ? ? C ASP 251 C MN    402 1_555 ? ? ? ? ? ? ? 2.295 ? ? 
metalc31 metalc ? ? C ASP 247 OD1 ? ? ? 1_555 J MN    . MN  ? ? C ASP 253 C MN    402 1_555 ? ? ? ? ? ? ? 2.416 ? ? 
metalc32 metalc ? ? C ASP 247 OD2 ? ? ? 1_555 J MN    . MN  ? ? C ASP 253 C MN    402 1_555 ? ? ? ? ? ? ? 2.201 ? ? 
metalc33 metalc ? ? I MN  .   MN  ? ? ? 1_555 K A1H0A . O14 ? ? C MN  401 C A1H0A 403 1_555 ? ? ? ? ? ? ? 2.319 ? ? 
metalc34 metalc ? ? J MN  .   MN  ? ? ? 1_555 K A1H0A . O17 ? ? C MN  402 C A1H0A 403 1_555 ? ? ? ? ? ? ? 2.669 ? ? 
metalc35 metalc ? ? J MN  .   MN  ? ? ? 1_555 K A1H0A . O14 ? ? C MN  402 C A1H0A 403 1_555 ? ? ? ? ? ? ? 2.375 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  ND1 ? A HIS   114 ? A HIS   120 ? 1_555 MN ? D MN . ? A MN 401 ? 1_555 OD2 ? A ASP   137 ? A ASP   143 ? 1_555 90.5  ? 
2  ND1 ? A HIS   114 ? A HIS   120 ? 1_555 MN ? D MN . ? A MN 401 ? 1_555 OD2 ? A ASP   141 ? A ASP   147 ? 1_555 92.3  ? 
3  OD2 ? A ASP   137 ? A ASP   143 ? 1_555 MN ? D MN . ? A MN 401 ? 1_555 OD2 ? A ASP   141 ? A ASP   147 ? 1_555 86.2  ? 
4  ND1 ? A HIS   114 ? A HIS   120 ? 1_555 MN ? D MN . ? A MN 401 ? 1_555 OD2 ? A ASP   245 ? A ASP   251 ? 1_555 97.8  ? 
5  OD2 ? A ASP   137 ? A ASP   143 ? 1_555 MN ? D MN . ? A MN 401 ? 1_555 OD2 ? A ASP   245 ? A ASP   251 ? 1_555 89.2  ? 
6  OD2 ? A ASP   141 ? A ASP   147 ? 1_555 MN ? D MN . ? A MN 401 ? 1_555 OD2 ? A ASP   245 ? A ASP   251 ? 1_555 169.0 ? 
7  ND1 ? A HIS   114 ? A HIS   120 ? 1_555 MN ? D MN . ? A MN 401 ? 1_555 O14 ? F A1H0A .   ? A A1H0A 403 ? 1_555 163.7 ? 
8  OD2 ? A ASP   137 ? A ASP   143 ? 1_555 MN ? D MN . ? A MN 401 ? 1_555 O14 ? F A1H0A .   ? A A1H0A 403 ? 1_555 105.4 ? 
9  OD2 ? A ASP   141 ? A ASP   147 ? 1_555 MN ? D MN . ? A MN 401 ? 1_555 O14 ? F A1H0A .   ? A A1H0A 403 ? 1_555 85.7  ? 
10 OD2 ? A ASP   245 ? A ASP   251 ? 1_555 MN ? D MN . ? A MN 401 ? 1_555 O14 ? F A1H0A .   ? A A1H0A 403 ? 1_555 85.9  ? 
11 OD1 ? A ASP   137 ? A ASP   143 ? 1_555 MN ? E MN . ? A MN 402 ? 1_555 ND1 ? A HIS   139 ? A HIS   145 ? 1_555 96.1  ? 
12 OD1 ? A ASP   137 ? A ASP   143 ? 1_555 MN ? E MN . ? A MN 402 ? 1_555 OD2 ? A ASP   245 ? A ASP   251 ? 1_555 82.2  ? 
13 ND1 ? A HIS   139 ? A HIS   145 ? 1_555 MN ? E MN . ? A MN 402 ? 1_555 OD2 ? A ASP   245 ? A ASP   251 ? 1_555 166.8 ? 
14 OD1 ? A ASP   137 ? A ASP   143 ? 1_555 MN ? E MN . ? A MN 402 ? 1_555 OD1 ? A ASP   247 ? A ASP   253 ? 1_555 77.0  ? 
15 ND1 ? A HIS   139 ? A HIS   145 ? 1_555 MN ? E MN . ? A MN 402 ? 1_555 OD1 ? A ASP   247 ? A ASP   253 ? 1_555 103.0 ? 
16 OD2 ? A ASP   245 ? A ASP   251 ? 1_555 MN ? E MN . ? A MN 402 ? 1_555 OD1 ? A ASP   247 ? A ASP   253 ? 1_555 89.5  ? 
17 OD1 ? A ASP   137 ? A ASP   143 ? 1_555 MN ? E MN . ? A MN 402 ? 1_555 OD2 ? A ASP   247 ? A ASP   253 ? 1_555 132.4 ? 
18 ND1 ? A HIS   139 ? A HIS   145 ? 1_555 MN ? E MN . ? A MN 402 ? 1_555 OD2 ? A ASP   247 ? A ASP   253 ? 1_555 93.9  ? 
19 OD2 ? A ASP   245 ? A ASP   251 ? 1_555 MN ? E MN . ? A MN 402 ? 1_555 OD2 ? A ASP   247 ? A ASP   253 ? 1_555 96.9  ? 
20 OD1 ? A ASP   247 ? A ASP   253 ? 1_555 MN ? E MN . ? A MN 402 ? 1_555 OD2 ? A ASP   247 ? A ASP   253 ? 1_555 55.4  ? 
21 OD1 ? A ASP   137 ? A ASP   143 ? 1_555 MN ? E MN . ? A MN 402 ? 1_555 O17 ? F A1H0A .   ? A A1H0A 403 ? 1_555 147.3 ? 
22 ND1 ? A HIS   139 ? A HIS   145 ? 1_555 MN ? E MN . ? A MN 402 ? 1_555 O17 ? F A1H0A .   ? A A1H0A 403 ? 1_555 90.7  ? 
23 OD2 ? A ASP   245 ? A ASP   251 ? 1_555 MN ? E MN . ? A MN 402 ? 1_555 O17 ? F A1H0A .   ? A A1H0A 403 ? 1_555 84.0  ? 
24 OD1 ? A ASP   247 ? A ASP   253 ? 1_555 MN ? E MN . ? A MN 402 ? 1_555 O17 ? F A1H0A .   ? A A1H0A 403 ? 1_555 132.4 ? 
25 OD2 ? A ASP   247 ? A ASP   253 ? 1_555 MN ? E MN . ? A MN 402 ? 1_555 O17 ? F A1H0A .   ? A A1H0A 403 ? 1_555 78.6  ? 
26 OD1 ? A ASP   137 ? A ASP   143 ? 1_555 MN ? E MN . ? A MN 402 ? 1_555 O14 ? F A1H0A .   ? A A1H0A 403 ? 1_555 96.6  ? 
27 ND1 ? A HIS   139 ? A HIS   145 ? 1_555 MN ? E MN . ? A MN 402 ? 1_555 O14 ? F A1H0A .   ? A A1H0A 403 ? 1_555 93.8  ? 
28 OD2 ? A ASP   245 ? A ASP   251 ? 1_555 MN ? E MN . ? A MN 402 ? 1_555 O14 ? F A1H0A .   ? A A1H0A 403 ? 1_555 73.5  ? 
29 OD1 ? A ASP   247 ? A ASP   253 ? 1_555 MN ? E MN . ? A MN 402 ? 1_555 O14 ? F A1H0A .   ? A A1H0A 403 ? 1_555 162.5 ? 
30 OD2 ? A ASP   247 ? A ASP   253 ? 1_555 MN ? E MN . ? A MN 402 ? 1_555 O14 ? F A1H0A .   ? A A1H0A 403 ? 1_555 129.0 ? 
31 O17 ? F A1H0A .   ? A A1H0A 403 ? 1_555 MN ? E MN . ? A MN 402 ? 1_555 O14 ? F A1H0A .   ? A A1H0A 403 ? 1_555 51.0  ? 
32 ND1 ? B HIS   114 ? B HIS   120 ? 1_555 MN ? G MN . ? B MN 500 ? 1_555 OD2 ? B ASP   137 ? B ASP   143 ? 1_555 87.5  ? 
33 ND1 ? B HIS   114 ? B HIS   120 ? 1_555 MN ? G MN . ? B MN 500 ? 1_555 OD2 ? B ASP   141 ? B ASP   147 ? 1_555 89.8  ? 
34 OD2 ? B ASP   137 ? B ASP   143 ? 1_555 MN ? G MN . ? B MN 500 ? 1_555 OD2 ? B ASP   141 ? B ASP   147 ? 1_555 75.8  ? 
35 ND1 ? B HIS   114 ? B HIS   120 ? 1_555 MN ? G MN . ? B MN 500 ? 1_555 OD2 ? B ASP   245 ? B ASP   251 ? 1_555 93.6  ? 
36 OD2 ? B ASP   137 ? B ASP   143 ? 1_555 MN ? G MN . ? B MN 500 ? 1_555 OD2 ? B ASP   245 ? B ASP   251 ? 1_555 102.5 ? 
37 OD2 ? B ASP   141 ? B ASP   147 ? 1_555 MN ? G MN . ? B MN 500 ? 1_555 OD2 ? B ASP   245 ? B ASP   251 ? 1_555 176.2 ? 
38 ND1 ? B HIS   114 ? B HIS   120 ? 1_555 MN ? G MN . ? B MN 500 ? 1_555 O   ? M HOH   .   ? B HOH   637 ? 1_555 143.9 ? 
39 OD2 ? B ASP   137 ? B ASP   143 ? 1_555 MN ? G MN . ? B MN 500 ? 1_555 O   ? M HOH   .   ? B HOH   637 ? 1_555 126.3 ? 
40 OD2 ? B ASP   141 ? B ASP   147 ? 1_555 MN ? G MN . ? B MN 500 ? 1_555 O   ? M HOH   .   ? B HOH   637 ? 1_555 108.9 ? 
41 OD2 ? B ASP   245 ? B ASP   251 ? 1_555 MN ? G MN . ? B MN 500 ? 1_555 O   ? M HOH   .   ? B HOH   637 ? 1_555 69.1  ? 
42 OD1 ? B ASP   137 ? B ASP   143 ? 1_555 MN ? H MN . ? B MN 501 ? 1_555 ND1 ? B HIS   139 ? B HIS   145 ? 1_555 96.7  ? 
43 OD1 ? B ASP   137 ? B ASP   143 ? 1_555 MN ? H MN . ? B MN 501 ? 1_555 OD2 ? B ASP   245 ? B ASP   251 ? 1_555 82.3  ? 
44 ND1 ? B HIS   139 ? B HIS   145 ? 1_555 MN ? H MN . ? B MN 501 ? 1_555 OD2 ? B ASP   245 ? B ASP   251 ? 1_555 159.2 ? 
45 OD1 ? B ASP   137 ? B ASP   143 ? 1_555 MN ? H MN . ? B MN 501 ? 1_555 OD1 ? B ASP   247 ? B ASP   253 ? 1_555 87.6  ? 
46 ND1 ? B HIS   139 ? B HIS   145 ? 1_555 MN ? H MN . ? B MN 501 ? 1_555 OD1 ? B ASP   247 ? B ASP   253 ? 1_555 107.7 ? 
47 OD2 ? B ASP   245 ? B ASP   251 ? 1_555 MN ? H MN . ? B MN 501 ? 1_555 OD1 ? B ASP   247 ? B ASP   253 ? 1_555 93.0  ? 
48 OD1 ? B ASP   137 ? B ASP   143 ? 1_555 MN ? H MN . ? B MN 501 ? 1_555 OD2 ? B ASP   247 ? B ASP   253 ? 1_555 150.4 ? 
49 ND1 ? B HIS   139 ? B HIS   145 ? 1_555 MN ? H MN . ? B MN 501 ? 1_555 OD2 ? B ASP   247 ? B ASP   253 ? 1_555 95.1  ? 
50 OD2 ? B ASP   245 ? B ASP   251 ? 1_555 MN ? H MN . ? B MN 501 ? 1_555 OD2 ? B ASP   247 ? B ASP   253 ? 1_555 95.7  ? 
51 OD1 ? B ASP   247 ? B ASP   253 ? 1_555 MN ? H MN . ? B MN 501 ? 1_555 OD2 ? B ASP   247 ? B ASP   253 ? 1_555 62.9  ? 
52 OD1 ? B ASP   137 ? B ASP   143 ? 1_555 MN ? H MN . ? B MN 501 ? 1_555 O   ? M HOH   .   ? B HOH   637 ? 1_555 102.1 ? 
53 ND1 ? B HIS   139 ? B HIS   145 ? 1_555 MN ? H MN . ? B MN 501 ? 1_555 O   ? M HOH   .   ? B HOH   637 ? 1_555 90.9  ? 
54 OD2 ? B ASP   245 ? B ASP   251 ? 1_555 MN ? H MN . ? B MN 501 ? 1_555 O   ? M HOH   .   ? B HOH   637 ? 1_555 69.1  ? 
55 OD1 ? B ASP   247 ? B ASP   253 ? 1_555 MN ? H MN . ? B MN 501 ? 1_555 O   ? M HOH   .   ? B HOH   637 ? 1_555 157.9 ? 
56 OD2 ? B ASP   247 ? B ASP   253 ? 1_555 MN ? H MN . ? B MN 501 ? 1_555 O   ? M HOH   .   ? B HOH   637 ? 1_555 104.8 ? 
57 ND1 ? C HIS   114 ? C HIS   120 ? 1_555 MN ? I MN . ? C MN 401 ? 1_555 OD2 ? C ASP   137 ? C ASP   143 ? 1_555 92.8  ? 
58 ND1 ? C HIS   114 ? C HIS   120 ? 1_555 MN ? I MN . ? C MN 401 ? 1_555 OD2 ? C ASP   141 ? C ASP   147 ? 1_555 86.9  ? 
59 OD2 ? C ASP   137 ? C ASP   143 ? 1_555 MN ? I MN . ? C MN 401 ? 1_555 OD2 ? C ASP   141 ? C ASP   147 ? 1_555 85.4  ? 
60 ND1 ? C HIS   114 ? C HIS   120 ? 1_555 MN ? I MN . ? C MN 401 ? 1_555 OD2 ? C ASP   245 ? C ASP   251 ? 1_555 107.1 ? 
61 OD2 ? C ASP   137 ? C ASP   143 ? 1_555 MN ? I MN . ? C MN 401 ? 1_555 OD2 ? C ASP   245 ? C ASP   251 ? 1_555 90.8  ? 
62 OD2 ? C ASP   141 ? C ASP   147 ? 1_555 MN ? I MN . ? C MN 401 ? 1_555 OD2 ? C ASP   245 ? C ASP   251 ? 1_555 165.7 ? 
63 ND1 ? C HIS   114 ? C HIS   120 ? 1_555 MN ? I MN . ? C MN 401 ? 1_555 O14 ? K A1H0A .   ? C A1H0A 403 ? 1_555 166.6 ? 
64 OD2 ? C ASP   137 ? C ASP   143 ? 1_555 MN ? I MN . ? C MN 401 ? 1_555 O14 ? K A1H0A .   ? C A1H0A 403 ? 1_555 98.7  ? 
65 OD2 ? C ASP   141 ? C ASP   147 ? 1_555 MN ? I MN . ? C MN 401 ? 1_555 O14 ? K A1H0A .   ? C A1H0A 403 ? 1_555 87.2  ? 
66 OD2 ? C ASP   245 ? C ASP   251 ? 1_555 MN ? I MN . ? C MN 401 ? 1_555 O14 ? K A1H0A .   ? C A1H0A 403 ? 1_555 79.7  ? 
67 OD1 ? C ASP   137 ? C ASP   143 ? 1_555 MN ? J MN . ? C MN 402 ? 1_555 ND1 ? C HIS   139 ? C HIS   145 ? 1_555 93.1  ? 
68 OD1 ? C ASP   137 ? C ASP   143 ? 1_555 MN ? J MN . ? C MN 402 ? 1_555 OD2 ? C ASP   245 ? C ASP   251 ? 1_555 90.2  ? 
69 ND1 ? C HIS   139 ? C HIS   145 ? 1_555 MN ? J MN . ? C MN 402 ? 1_555 OD2 ? C ASP   245 ? C ASP   251 ? 1_555 167.3 ? 
70 OD1 ? C ASP   137 ? C ASP   143 ? 1_555 MN ? J MN . ? C MN 402 ? 1_555 OD1 ? C ASP   247 ? C ASP   253 ? 1_555 79.3  ? 
71 ND1 ? C HIS   139 ? C HIS   145 ? 1_555 MN ? J MN . ? C MN 402 ? 1_555 OD1 ? C ASP   247 ? C ASP   253 ? 1_555 101.3 ? 
72 OD2 ? C ASP   245 ? C ASP   251 ? 1_555 MN ? J MN . ? C MN 402 ? 1_555 OD1 ? C ASP   247 ? C ASP   253 ? 1_555 91.4  ? 
73 OD1 ? C ASP   137 ? C ASP   143 ? 1_555 MN ? J MN . ? C MN 402 ? 1_555 OD2 ? C ASP   247 ? C ASP   253 ? 1_555 135.9 ? 
74 ND1 ? C HIS   139 ? C HIS   145 ? 1_555 MN ? J MN . ? C MN 402 ? 1_555 OD2 ? C ASP   247 ? C ASP   253 ? 1_555 93.6  ? 
75 OD2 ? C ASP   245 ? C ASP   251 ? 1_555 MN ? J MN . ? C MN 402 ? 1_555 OD2 ? C ASP   247 ? C ASP   253 ? 1_555 92.5  ? 
76 OD1 ? C ASP   247 ? C ASP   253 ? 1_555 MN ? J MN . ? C MN 402 ? 1_555 OD2 ? C ASP   247 ? C ASP   253 ? 1_555 56.7  ? 
77 OD1 ? C ASP   137 ? C ASP   143 ? 1_555 MN ? J MN . ? C MN 402 ? 1_555 O17 ? K A1H0A .   ? C A1H0A 403 ? 1_555 150.0 ? 
78 ND1 ? C HIS   139 ? C HIS   145 ? 1_555 MN ? J MN . ? C MN 402 ? 1_555 O17 ? K A1H0A .   ? C A1H0A 403 ? 1_555 90.1  ? 
79 OD2 ? C ASP   245 ? C ASP   251 ? 1_555 MN ? J MN . ? C MN 402 ? 1_555 O17 ? K A1H0A .   ? C A1H0A 403 ? 1_555 81.0  ? 
80 OD1 ? C ASP   247 ? C ASP   253 ? 1_555 MN ? J MN . ? C MN 402 ? 1_555 O17 ? K A1H0A .   ? C A1H0A 403 ? 1_555 129.2 ? 
81 OD2 ? C ASP   247 ? C ASP   253 ? 1_555 MN ? J MN . ? C MN 402 ? 1_555 O17 ? K A1H0A .   ? C A1H0A 403 ? 1_555 73.4  ? 
82 OD1 ? C ASP   137 ? C ASP   143 ? 1_555 MN ? J MN . ? C MN 402 ? 1_555 O14 ? K A1H0A .   ? C A1H0A 403 ? 1_555 98.5  ? 
83 ND1 ? C HIS   139 ? C HIS   145 ? 1_555 MN ? J MN . ? C MN 402 ? 1_555 O14 ? K A1H0A .   ? C A1H0A 403 ? 1_555 89.5  ? 
84 OD2 ? C ASP   245 ? C ASP   251 ? 1_555 MN ? J MN . ? C MN 402 ? 1_555 O14 ? K A1H0A .   ? C A1H0A 403 ? 1_555 77.8  ? 
85 OD1 ? C ASP   247 ? C ASP   253 ? 1_555 MN ? J MN . ? C MN 402 ? 1_555 O14 ? K A1H0A .   ? C A1H0A 403 ? 1_555 169.0 ? 
86 OD2 ? C ASP   247 ? C ASP   253 ? 1_555 MN ? J MN . ? C MN 402 ? 1_555 O14 ? K A1H0A .   ? C A1H0A 403 ? 1_555 125.1 ? 
87 O17 ? K A1H0A .   ? C A1H0A 403 ? 1_555 MN ? J MN . ? C MN 402 ? 1_555 O14 ? K A1H0A .   ? C A1H0A 403 ? 1_555 51.7  ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 GLY 111 A . ? GLY 117 A GLY 112 A ? GLY 118 A 1 -0.57 
2 GLY 111 B . ? GLY 117 B GLY 112 B ? GLY 118 B 1 0.58  
3 GLY 111 C . ? GLY 117 C GLY 112 C ? GLY 118 C 1 1.79  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 8 ? 
AA2 ? 8 ? 
AA3 ? 8 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel 
AA1 2 3 ? parallel 
AA1 3 4 ? parallel 
AA1 4 5 ? parallel 
AA1 5 6 ? parallel 
AA1 6 7 ? parallel 
AA1 7 8 ? parallel 
AA2 1 2 ? parallel 
AA2 2 3 ? parallel 
AA2 3 4 ? parallel 
AA2 4 5 ? parallel 
AA2 5 6 ? parallel 
AA2 6 7 ? parallel 
AA2 7 8 ? parallel 
AA3 1 2 ? parallel 
AA3 2 3 ? parallel 
AA3 3 4 ? parallel 
AA3 4 5 ? parallel 
AA3 5 6 ? parallel 
AA3 6 7 ? parallel 
AA3 7 8 ? parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 HIS A 58  ? ASP A 64  ? HIS A 64  ASP A 70  
AA1 2 SER A 19  ? GLY A 24  ? SER A 25  GLY A 30  
AA1 3 SER A 106 ? LEU A 110 ? SER A 112 LEU A 116 
AA1 4 LEU A 283 ? VAL A 289 ? LEU A 289 VAL A 295 
AA1 5 ILE A 240 ? ASP A 245 ? ILE A 246 ASP A 251 
AA1 6 CYS A 132 ? VAL A 136 ? CYS A 138 VAL A 142 
AA1 7 ILE A 187 ? LEU A 192 ? ILE A 193 LEU A 198 
AA1 8 GLN A 209 ? SER A 212 ? GLN A 215 SER A 218 
AA2 1 HIS B 58  ? ASP B 64  ? HIS B 64  ASP B 70  
AA2 2 SER B 19  ? GLY B 24  ? SER B 25  GLY B 30  
AA2 3 SER B 106 ? LEU B 110 ? SER B 112 LEU B 116 
AA2 4 LEU B 283 ? VAL B 289 ? LEU B 289 VAL B 295 
AA2 5 ILE B 240 ? ASP B 245 ? ILE B 246 ASP B 251 
AA2 6 CYS B 132 ? VAL B 136 ? CYS B 138 VAL B 142 
AA2 7 ILE B 187 ? ILE B 190 ? ILE B 193 ILE B 196 
AA2 8 TYR B 210 ? PHE B 211 ? TYR B 216 PHE B 217 
AA3 1 HIS C 58  ? ASP C 64  ? HIS C 64  ASP C 70  
AA3 2 SER C 19  ? GLY C 24  ? SER C 25  GLY C 30  
AA3 3 SER C 106 ? LEU C 110 ? SER C 112 LEU C 116 
AA3 4 LEU C 283 ? VAL C 289 ? LEU C 289 VAL C 295 
AA3 5 ILE C 240 ? ASP C 245 ? ILE C 246 ASP C 251 
AA3 6 CYS C 132 ? VAL C 136 ? CYS C 138 VAL C 142 
AA3 7 ILE C 187 ? ILE C 190 ? ILE C 193 ILE C 196 
AA3 8 GLN C 209 ? PHE C 211 ? GLN C 215 PHE C 217 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O HIS A 58  ? O HIS A 64  N VAL A 20  ? N VAL A 26  
AA1 2 3 N ALA A 21  ? N ALA A 27  O VAL A 108 ? O VAL A 114 
AA1 3 4 N THR A 109 ? N THR A 115 O LEU A 286 ? O LEU A 292 
AA1 4 5 O SER A 284 ? O SER A 290 N ILE A 240 ? N ILE A 246 
AA1 5 6 O ASP A 245 ? O ASP A 251 N VAL A 136 ? N VAL A 142 
AA1 6 7 N TRP A 135 ? N TRP A 141 O VAL A 188 ? O VAL A 194 
AA1 7 8 N GLY A 191 ? N GLY A 197 O PHE A 211 ? O PHE A 217 
AA2 1 2 O PHE B 62  ? O PHE B 68  N VAL B 22  ? N VAL B 28  
AA2 2 3 N ILE B 23  ? N ILE B 29  O LEU B 110 ? O LEU B 116 
AA2 3 4 N THR B 109 ? N THR B 115 O LEU B 288 ? O LEU B 294 
AA2 4 5 O SER B 284 ? O SER B 290 N ILE B 240 ? N ILE B 246 
AA2 5 6 O ASP B 245 ? O ASP B 251 N VAL B 136 ? N VAL B 142 
AA2 6 7 N TRP B 135 ? N TRP B 141 O ILE B 190 ? O ILE B 196 
AA2 7 8 N TYR B 189 ? N TYR B 195 O PHE B 211 ? O PHE B 217 
AA3 1 2 O PHE C 62  ? O PHE C 68  N VAL C 22  ? N VAL C 28  
AA3 2 3 N ALA C 21  ? N ALA C 27  O VAL C 108 ? O VAL C 114 
AA3 3 4 N CYS C 107 ? N CYS C 113 O LEU C 286 ? O LEU C 292 
AA3 4 5 O SER C 284 ? O SER C 290 N ILE C 240 ? N ILE C 246 
AA3 5 6 O ASP C 245 ? O ASP C 251 N VAL C 136 ? N VAL C 142 
AA3 6 7 N TRP C 135 ? N TRP C 141 O ILE C 190 ? O ILE C 196 
AA3 7 8 N TYR C 189 ? N TYR C 195 O PHE C 211 ? O PHE C 217 
# 
_pdbx_entry_details.entry_id                   8RGF 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ASP A 79  ? ? -156.62 78.77  
2  1 LEU A 81  ? ? -29.51  119.86 
3  1 LEU A 85  ? ? -154.66 -57.29 
4  1 ARG A 199 ? ? -155.58 -2.72  
5  1 PRO B 32  ? ? -92.31  55.83  
6  1 SER B 34  ? ? -146.23 -17.05 
7  1 LEU B 85  ? ? -153.02 -62.74 
8  1 ILE B 86  ? ? -60.38  86.65  
9  1 HIS B 120 ? ? -67.90  0.57   
10 1 ASP B 147 ? ? 37.22   39.35  
11 1 ARG B 199 ? ? -149.00 -5.25  
12 1 THR B 265 ? ? -111.46 76.51  
13 1 LEU B 301 ? ? -95.79  34.78  
14 1 LEU C 85  ? ? -158.39 -58.18 
15 1 CYS C 134 ? ? -119.73 66.75  
16 1 ARG C 199 ? ? -152.95 -6.62  
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A HIS 7   ? A HIS 1   
2  1 Y 1 A HIS 8   ? A HIS 2   
3  1 Y 1 A HIS 9   ? A HIS 3   
4  1 Y 1 A HIS 10  ? A HIS 4   
5  1 Y 1 A HIS 11  ? A HIS 5   
6  1 Y 1 A HIS 12  ? A HIS 6   
7  1 Y 1 A GLY 13  ? A GLY 7   
8  1 Y 1 A GLY 14  ? A GLY 8   
9  1 Y 1 A GLY 15  ? A GLY 9   
10 1 Y 1 A GLU 16  ? A GLU 10  
11 1 Y 1 A ASN 17  ? A ASN 11  
12 1 Y 1 A LEU 18  ? A LEU 12  
13 1 Y 1 A TYR 19  ? A TYR 13  
14 1 Y 1 A PHE 20  ? A PHE 14  
15 1 Y 1 A GLN 21  ? A GLN 15  
16 1 Y 1 A SER 22  ? A SER 16  
17 1 Y 1 A SER 341 ? A SER 335 
18 1 Y 1 B HIS 7   ? B HIS 1   
19 1 Y 1 B HIS 8   ? B HIS 2   
20 1 Y 1 B HIS 9   ? B HIS 3   
21 1 Y 1 B HIS 10  ? B HIS 4   
22 1 Y 1 B HIS 11  ? B HIS 5   
23 1 Y 1 B HIS 12  ? B HIS 6   
24 1 Y 1 B GLY 13  ? B GLY 7   
25 1 Y 1 B GLY 14  ? B GLY 8   
26 1 Y 1 B GLY 15  ? B GLY 9   
27 1 Y 1 B GLU 16  ? B GLU 10  
28 1 Y 1 B SER 341 ? B SER 335 
29 1 Y 1 C HIS 7   ? C HIS 1   
30 1 Y 1 C HIS 8   ? C HIS 2   
31 1 Y 1 C HIS 9   ? C HIS 3   
32 1 Y 1 C HIS 10  ? C HIS 4   
33 1 Y 1 C HIS 11  ? C HIS 5   
34 1 Y 1 C HIS 12  ? C HIS 6   
35 1 Y 1 C GLY 13  ? C GLY 7   
36 1 Y 1 C GLY 14  ? C GLY 8   
37 1 Y 1 C GLY 15  ? C GLY 9   
38 1 Y 1 C GLU 16  ? C GLU 10  
39 1 Y 1 C ASN 17  ? C ASN 11  
40 1 Y 1 C LEU 18  ? C LEU 12  
41 1 Y 1 C TYR 19  ? C TYR 13  
42 1 Y 1 C PHE 20  ? C PHE 14  
43 1 Y 1 C GLN 21  ? C GLN 15  
44 1 Y 1 C SER 22  ? C SER 16  
45 1 Y 1 C SER 341 ? C SER 335 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
A1H0A C2   C  N N 1   
A1H0A C3   C  N R 2   
A1H0A C9   C  N N 3   
A1H0A C10  C  N N 4   
A1H0A C11  C  N N 5   
A1H0A C12  C  N N 6   
A1H0A O17  O  N N 7   
A1H0A N1   N  N N 8   
A1H0A C4   C  N N 9   
A1H0A C5   C  N R 10  
A1H0A C6   C  N N 11  
A1H0A O7   O  N N 12  
A1H0A O8   O  N N 13  
A1H0A B13  B  N N 14  
A1H0A O14  O  N N 15  
A1H0A O15  O  N N 16  
A1H0A N16  N  N N 17  
A1H0A H1   H  N N 18  
A1H0A H2   H  N N 19  
A1H0A H3   H  N N 20  
A1H0A H4   H  N N 21  
A1H0A H5   H  N N 22  
A1H0A H6   H  N N 23  
A1H0A H7   H  N N 24  
A1H0A H8   H  N N 25  
A1H0A H9   H  N N 26  
A1H0A H10  H  N N 27  
A1H0A H11  H  N N 28  
A1H0A H12  H  N N 29  
A1H0A H13  H  N N 30  
A1H0A H15  H  N N 31  
A1H0A H16  H  N N 32  
A1H0A H17  H  N N 33  
A1H0A H18  H  N N 34  
A1H0A H20  H  N N 35  
A1H0A H21  H  N N 36  
A1H0A H14  H  N N 37  
ALA   N    N  N N 38  
ALA   CA   C  N S 39  
ALA   C    C  N N 40  
ALA   O    O  N N 41  
ALA   CB   C  N N 42  
ALA   OXT  O  N N 43  
ALA   H    H  N N 44  
ALA   H2   H  N N 45  
ALA   HA   H  N N 46  
ALA   HB1  H  N N 47  
ALA   HB2  H  N N 48  
ALA   HB3  H  N N 49  
ALA   HXT  H  N N 50  
ARG   N    N  N N 51  
ARG   CA   C  N S 52  
ARG   C    C  N N 53  
ARG   O    O  N N 54  
ARG   CB   C  N N 55  
ARG   CG   C  N N 56  
ARG   CD   C  N N 57  
ARG   NE   N  N N 58  
ARG   CZ   C  N N 59  
ARG   NH1  N  N N 60  
ARG   NH2  N  N N 61  
ARG   OXT  O  N N 62  
ARG   H    H  N N 63  
ARG   H2   H  N N 64  
ARG   HA   H  N N 65  
ARG   HB2  H  N N 66  
ARG   HB3  H  N N 67  
ARG   HG2  H  N N 68  
ARG   HG3  H  N N 69  
ARG   HD2  H  N N 70  
ARG   HD3  H  N N 71  
ARG   HE   H  N N 72  
ARG   HH11 H  N N 73  
ARG   HH12 H  N N 74  
ARG   HH21 H  N N 75  
ARG   HH22 H  N N 76  
ARG   HXT  H  N N 77  
ASN   N    N  N N 78  
ASN   CA   C  N S 79  
ASN   C    C  N N 80  
ASN   O    O  N N 81  
ASN   CB   C  N N 82  
ASN   CG   C  N N 83  
ASN   OD1  O  N N 84  
ASN   ND2  N  N N 85  
ASN   OXT  O  N N 86  
ASN   H    H  N N 87  
ASN   H2   H  N N 88  
ASN   HA   H  N N 89  
ASN   HB2  H  N N 90  
ASN   HB3  H  N N 91  
ASN   HD21 H  N N 92  
ASN   HD22 H  N N 93  
ASN   HXT  H  N N 94  
ASP   N    N  N N 95  
ASP   CA   C  N S 96  
ASP   C    C  N N 97  
ASP   O    O  N N 98  
ASP   CB   C  N N 99  
ASP   CG   C  N N 100 
ASP   OD1  O  N N 101 
ASP   OD2  O  N N 102 
ASP   OXT  O  N N 103 
ASP   H    H  N N 104 
ASP   H2   H  N N 105 
ASP   HA   H  N N 106 
ASP   HB2  H  N N 107 
ASP   HB3  H  N N 108 
ASP   HD2  H  N N 109 
ASP   HXT  H  N N 110 
CYS   N    N  N N 111 
CYS   CA   C  N R 112 
CYS   C    C  N N 113 
CYS   O    O  N N 114 
CYS   CB   C  N N 115 
CYS   SG   S  N N 116 
CYS   OXT  O  N N 117 
CYS   H    H  N N 118 
CYS   H2   H  N N 119 
CYS   HA   H  N N 120 
CYS   HB2  H  N N 121 
CYS   HB3  H  N N 122 
CYS   HG   H  N N 123 
CYS   HXT  H  N N 124 
GLN   N    N  N N 125 
GLN   CA   C  N S 126 
GLN   C    C  N N 127 
GLN   O    O  N N 128 
GLN   CB   C  N N 129 
GLN   CG   C  N N 130 
GLN   CD   C  N N 131 
GLN   OE1  O  N N 132 
GLN   NE2  N  N N 133 
GLN   OXT  O  N N 134 
GLN   H    H  N N 135 
GLN   H2   H  N N 136 
GLN   HA   H  N N 137 
GLN   HB2  H  N N 138 
GLN   HB3  H  N N 139 
GLN   HG2  H  N N 140 
GLN   HG3  H  N N 141 
GLN   HE21 H  N N 142 
GLN   HE22 H  N N 143 
GLN   HXT  H  N N 144 
GLU   N    N  N N 145 
GLU   CA   C  N S 146 
GLU   C    C  N N 147 
GLU   O    O  N N 148 
GLU   CB   C  N N 149 
GLU   CG   C  N N 150 
GLU   CD   C  N N 151 
GLU   OE1  O  N N 152 
GLU   OE2  O  N N 153 
GLU   OXT  O  N N 154 
GLU   H    H  N N 155 
GLU   H2   H  N N 156 
GLU   HA   H  N N 157 
GLU   HB2  H  N N 158 
GLU   HB3  H  N N 159 
GLU   HG2  H  N N 160 
GLU   HG3  H  N N 161 
GLU   HE2  H  N N 162 
GLU   HXT  H  N N 163 
GLY   N    N  N N 164 
GLY   CA   C  N N 165 
GLY   C    C  N N 166 
GLY   O    O  N N 167 
GLY   OXT  O  N N 168 
GLY   H    H  N N 169 
GLY   H2   H  N N 170 
GLY   HA2  H  N N 171 
GLY   HA3  H  N N 172 
GLY   HXT  H  N N 173 
HIS   N    N  N N 174 
HIS   CA   C  N S 175 
HIS   C    C  N N 176 
HIS   O    O  N N 177 
HIS   CB   C  N N 178 
HIS   CG   C  Y N 179 
HIS   ND1  N  Y N 180 
HIS   CD2  C  Y N 181 
HIS   CE1  C  Y N 182 
HIS   NE2  N  Y N 183 
HIS   OXT  O  N N 184 
HIS   H    H  N N 185 
HIS   H2   H  N N 186 
HIS   HA   H  N N 187 
HIS   HB2  H  N N 188 
HIS   HB3  H  N N 189 
HIS   HD1  H  N N 190 
HIS   HD2  H  N N 191 
HIS   HE1  H  N N 192 
HIS   HE2  H  N N 193 
HIS   HXT  H  N N 194 
HOH   O    O  N N 195 
HOH   H1   H  N N 196 
HOH   H2   H  N N 197 
ILE   N    N  N N 198 
ILE   CA   C  N S 199 
ILE   C    C  N N 200 
ILE   O    O  N N 201 
ILE   CB   C  N S 202 
ILE   CG1  C  N N 203 
ILE   CG2  C  N N 204 
ILE   CD1  C  N N 205 
ILE   OXT  O  N N 206 
ILE   H    H  N N 207 
ILE   H2   H  N N 208 
ILE   HA   H  N N 209 
ILE   HB   H  N N 210 
ILE   HG12 H  N N 211 
ILE   HG13 H  N N 212 
ILE   HG21 H  N N 213 
ILE   HG22 H  N N 214 
ILE   HG23 H  N N 215 
ILE   HD11 H  N N 216 
ILE   HD12 H  N N 217 
ILE   HD13 H  N N 218 
ILE   HXT  H  N N 219 
LEU   N    N  N N 220 
LEU   CA   C  N S 221 
LEU   C    C  N N 222 
LEU   O    O  N N 223 
LEU   CB   C  N N 224 
LEU   CG   C  N N 225 
LEU   CD1  C  N N 226 
LEU   CD2  C  N N 227 
LEU   OXT  O  N N 228 
LEU   H    H  N N 229 
LEU   H2   H  N N 230 
LEU   HA   H  N N 231 
LEU   HB2  H  N N 232 
LEU   HB3  H  N N 233 
LEU   HG   H  N N 234 
LEU   HD11 H  N N 235 
LEU   HD12 H  N N 236 
LEU   HD13 H  N N 237 
LEU   HD21 H  N N 238 
LEU   HD22 H  N N 239 
LEU   HD23 H  N N 240 
LEU   HXT  H  N N 241 
LYS   N    N  N N 242 
LYS   CA   C  N S 243 
LYS   C    C  N N 244 
LYS   O    O  N N 245 
LYS   CB   C  N N 246 
LYS   CG   C  N N 247 
LYS   CD   C  N N 248 
LYS   CE   C  N N 249 
LYS   NZ   N  N N 250 
LYS   OXT  O  N N 251 
LYS   H    H  N N 252 
LYS   H2   H  N N 253 
LYS   HA   H  N N 254 
LYS   HB2  H  N N 255 
LYS   HB3  H  N N 256 
LYS   HG2  H  N N 257 
LYS   HG3  H  N N 258 
LYS   HD2  H  N N 259 
LYS   HD3  H  N N 260 
LYS   HE2  H  N N 261 
LYS   HE3  H  N N 262 
LYS   HZ1  H  N N 263 
LYS   HZ2  H  N N 264 
LYS   HZ3  H  N N 265 
LYS   HXT  H  N N 266 
MET   N    N  N N 267 
MET   CA   C  N S 268 
MET   C    C  N N 269 
MET   O    O  N N 270 
MET   CB   C  N N 271 
MET   CG   C  N N 272 
MET   SD   S  N N 273 
MET   CE   C  N N 274 
MET   OXT  O  N N 275 
MET   H    H  N N 276 
MET   H2   H  N N 277 
MET   HA   H  N N 278 
MET   HB2  H  N N 279 
MET   HB3  H  N N 280 
MET   HG2  H  N N 281 
MET   HG3  H  N N 282 
MET   HE1  H  N N 283 
MET   HE2  H  N N 284 
MET   HE3  H  N N 285 
MET   HXT  H  N N 286 
MN    MN   MN N N 287 
PHE   N    N  N N 288 
PHE   CA   C  N S 289 
PHE   C    C  N N 290 
PHE   O    O  N N 291 
PHE   CB   C  N N 292 
PHE   CG   C  Y N 293 
PHE   CD1  C  Y N 294 
PHE   CD2  C  Y N 295 
PHE   CE1  C  Y N 296 
PHE   CE2  C  Y N 297 
PHE   CZ   C  Y N 298 
PHE   OXT  O  N N 299 
PHE   H    H  N N 300 
PHE   H2   H  N N 301 
PHE   HA   H  N N 302 
PHE   HB2  H  N N 303 
PHE   HB3  H  N N 304 
PHE   HD1  H  N N 305 
PHE   HD2  H  N N 306 
PHE   HE1  H  N N 307 
PHE   HE2  H  N N 308 
PHE   HZ   H  N N 309 
PHE   HXT  H  N N 310 
PRO   N    N  N N 311 
PRO   CA   C  N S 312 
PRO   C    C  N N 313 
PRO   O    O  N N 314 
PRO   CB   C  N N 315 
PRO   CG   C  N N 316 
PRO   CD   C  N N 317 
PRO   OXT  O  N N 318 
PRO   H    H  N N 319 
PRO   HA   H  N N 320 
PRO   HB2  H  N N 321 
PRO   HB3  H  N N 322 
PRO   HG2  H  N N 323 
PRO   HG3  H  N N 324 
PRO   HD2  H  N N 325 
PRO   HD3  H  N N 326 
PRO   HXT  H  N N 327 
SER   N    N  N N 328 
SER   CA   C  N S 329 
SER   C    C  N N 330 
SER   O    O  N N 331 
SER   CB   C  N N 332 
SER   OG   O  N N 333 
SER   OXT  O  N N 334 
SER   H    H  N N 335 
SER   H2   H  N N 336 
SER   HA   H  N N 337 
SER   HB2  H  N N 338 
SER   HB3  H  N N 339 
SER   HG   H  N N 340 
SER   HXT  H  N N 341 
THR   N    N  N N 342 
THR   CA   C  N S 343 
THR   C    C  N N 344 
THR   O    O  N N 345 
THR   CB   C  N R 346 
THR   OG1  O  N N 347 
THR   CG2  C  N N 348 
THR   OXT  O  N N 349 
THR   H    H  N N 350 
THR   H2   H  N N 351 
THR   HA   H  N N 352 
THR   HB   H  N N 353 
THR   HG1  H  N N 354 
THR   HG21 H  N N 355 
THR   HG22 H  N N 356 
THR   HG23 H  N N 357 
THR   HXT  H  N N 358 
TRP   N    N  N N 359 
TRP   CA   C  N S 360 
TRP   C    C  N N 361 
TRP   O    O  N N 362 
TRP   CB   C  N N 363 
TRP   CG   C  Y N 364 
TRP   CD1  C  Y N 365 
TRP   CD2  C  Y N 366 
TRP   NE1  N  Y N 367 
TRP   CE2  C  Y N 368 
TRP   CE3  C  Y N 369 
TRP   CZ2  C  Y N 370 
TRP   CZ3  C  Y N 371 
TRP   CH2  C  Y N 372 
TRP   OXT  O  N N 373 
TRP   H    H  N N 374 
TRP   H2   H  N N 375 
TRP   HA   H  N N 376 
TRP   HB2  H  N N 377 
TRP   HB3  H  N N 378 
TRP   HD1  H  N N 379 
TRP   HE1  H  N N 380 
TRP   HE3  H  N N 381 
TRP   HZ2  H  N N 382 
TRP   HZ3  H  N N 383 
TRP   HH2  H  N N 384 
TRP   HXT  H  N N 385 
TYR   N    N  N N 386 
TYR   CA   C  N S 387 
TYR   C    C  N N 388 
TYR   O    O  N N 389 
TYR   CB   C  N N 390 
TYR   CG   C  Y N 391 
TYR   CD1  C  Y N 392 
TYR   CD2  C  Y N 393 
TYR   CE1  C  Y N 394 
TYR   CE2  C  Y N 395 
TYR   CZ   C  Y N 396 
TYR   OH   O  N N 397 
TYR   OXT  O  N N 398 
TYR   H    H  N N 399 
TYR   H2   H  N N 400 
TYR   HA   H  N N 401 
TYR   HB2  H  N N 402 
TYR   HB3  H  N N 403 
TYR   HD1  H  N N 404 
TYR   HD2  H  N N 405 
TYR   HE1  H  N N 406 
TYR   HE2  H  N N 407 
TYR   HH   H  N N 408 
TYR   HXT  H  N N 409 
VAL   N    N  N N 410 
VAL   CA   C  N S 411 
VAL   C    C  N N 412 
VAL   O    O  N N 413 
VAL   CB   C  N N 414 
VAL   CG1  C  N N 415 
VAL   CG2  C  N N 416 
VAL   OXT  O  N N 417 
VAL   H    H  N N 418 
VAL   H2   H  N N 419 
VAL   HA   H  N N 420 
VAL   HB   H  N N 421 
VAL   HG11 H  N N 422 
VAL   HG12 H  N N 423 
VAL   HG13 H  N N 424 
VAL   HG21 H  N N 425 
VAL   HG22 H  N N 426 
VAL   HG23 H  N N 427 
VAL   HXT  H  N N 428 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
A1H0A O15 B13  sing N N 1   
A1H0A O8  C6   doub N N 2   
A1H0A B13 C12  sing N N 3   
A1H0A B13 O14  sing N N 4   
A1H0A B13 O17  sing N N 5   
A1H0A C12 C11  sing N N 6   
A1H0A O7  C6   sing N N 7   
A1H0A C6  C5   sing N N 8   
A1H0A C10 C9   sing N N 9   
A1H0A C10 C11  sing N N 10  
A1H0A C9  C5   sing N N 11  
A1H0A C5  N1   sing N N 12  
A1H0A C5  C4   sing N N 13  
A1H0A N1  C2   sing N N 14  
A1H0A C4  C3   sing N N 15  
A1H0A C2  C3   sing N N 16  
A1H0A C3  N16  sing N N 17  
A1H0A C2  H1   sing N N 18  
A1H0A C2  H2   sing N N 19  
A1H0A C3  H3   sing N N 20  
A1H0A C9  H4   sing N N 21  
A1H0A C9  H5   sing N N 22  
A1H0A C10 H6   sing N N 23  
A1H0A C10 H7   sing N N 24  
A1H0A C11 H8   sing N N 25  
A1H0A C11 H9   sing N N 26  
A1H0A C12 H10  sing N N 27  
A1H0A C12 H11  sing N N 28  
A1H0A O17 H12  sing N N 29  
A1H0A N1  H13  sing N N 30  
A1H0A C4  H15  sing N N 31  
A1H0A C4  H16  sing N N 32  
A1H0A O7  H17  sing N N 33  
A1H0A O14 H18  sing N N 34  
A1H0A N16 H20  sing N N 35  
A1H0A N16 H21  sing N N 36  
A1H0A O15 H14  sing N N 37  
ALA   N   CA   sing N N 38  
ALA   N   H    sing N N 39  
ALA   N   H2   sing N N 40  
ALA   CA  C    sing N N 41  
ALA   CA  CB   sing N N 42  
ALA   CA  HA   sing N N 43  
ALA   C   O    doub N N 44  
ALA   C   OXT  sing N N 45  
ALA   CB  HB1  sing N N 46  
ALA   CB  HB2  sing N N 47  
ALA   CB  HB3  sing N N 48  
ALA   OXT HXT  sing N N 49  
ARG   N   CA   sing N N 50  
ARG   N   H    sing N N 51  
ARG   N   H2   sing N N 52  
ARG   CA  C    sing N N 53  
ARG   CA  CB   sing N N 54  
ARG   CA  HA   sing N N 55  
ARG   C   O    doub N N 56  
ARG   C   OXT  sing N N 57  
ARG   CB  CG   sing N N 58  
ARG   CB  HB2  sing N N 59  
ARG   CB  HB3  sing N N 60  
ARG   CG  CD   sing N N 61  
ARG   CG  HG2  sing N N 62  
ARG   CG  HG3  sing N N 63  
ARG   CD  NE   sing N N 64  
ARG   CD  HD2  sing N N 65  
ARG   CD  HD3  sing N N 66  
ARG   NE  CZ   sing N N 67  
ARG   NE  HE   sing N N 68  
ARG   CZ  NH1  sing N N 69  
ARG   CZ  NH2  doub N N 70  
ARG   NH1 HH11 sing N N 71  
ARG   NH1 HH12 sing N N 72  
ARG   NH2 HH21 sing N N 73  
ARG   NH2 HH22 sing N N 74  
ARG   OXT HXT  sing N N 75  
ASN   N   CA   sing N N 76  
ASN   N   H    sing N N 77  
ASN   N   H2   sing N N 78  
ASN   CA  C    sing N N 79  
ASN   CA  CB   sing N N 80  
ASN   CA  HA   sing N N 81  
ASN   C   O    doub N N 82  
ASN   C   OXT  sing N N 83  
ASN   CB  CG   sing N N 84  
ASN   CB  HB2  sing N N 85  
ASN   CB  HB3  sing N N 86  
ASN   CG  OD1  doub N N 87  
ASN   CG  ND2  sing N N 88  
ASN   ND2 HD21 sing N N 89  
ASN   ND2 HD22 sing N N 90  
ASN   OXT HXT  sing N N 91  
ASP   N   CA   sing N N 92  
ASP   N   H    sing N N 93  
ASP   N   H2   sing N N 94  
ASP   CA  C    sing N N 95  
ASP   CA  CB   sing N N 96  
ASP   CA  HA   sing N N 97  
ASP   C   O    doub N N 98  
ASP   C   OXT  sing N N 99  
ASP   CB  CG   sing N N 100 
ASP   CB  HB2  sing N N 101 
ASP   CB  HB3  sing N N 102 
ASP   CG  OD1  doub N N 103 
ASP   CG  OD2  sing N N 104 
ASP   OD2 HD2  sing N N 105 
ASP   OXT HXT  sing N N 106 
CYS   N   CA   sing N N 107 
CYS   N   H    sing N N 108 
CYS   N   H2   sing N N 109 
CYS   CA  C    sing N N 110 
CYS   CA  CB   sing N N 111 
CYS   CA  HA   sing N N 112 
CYS   C   O    doub N N 113 
CYS   C   OXT  sing N N 114 
CYS   CB  SG   sing N N 115 
CYS   CB  HB2  sing N N 116 
CYS   CB  HB3  sing N N 117 
CYS   SG  HG   sing N N 118 
CYS   OXT HXT  sing N N 119 
GLN   N   CA   sing N N 120 
GLN   N   H    sing N N 121 
GLN   N   H2   sing N N 122 
GLN   CA  C    sing N N 123 
GLN   CA  CB   sing N N 124 
GLN   CA  HA   sing N N 125 
GLN   C   O    doub N N 126 
GLN   C   OXT  sing N N 127 
GLN   CB  CG   sing N N 128 
GLN   CB  HB2  sing N N 129 
GLN   CB  HB3  sing N N 130 
GLN   CG  CD   sing N N 131 
GLN   CG  HG2  sing N N 132 
GLN   CG  HG3  sing N N 133 
GLN   CD  OE1  doub N N 134 
GLN   CD  NE2  sing N N 135 
GLN   NE2 HE21 sing N N 136 
GLN   NE2 HE22 sing N N 137 
GLN   OXT HXT  sing N N 138 
GLU   N   CA   sing N N 139 
GLU   N   H    sing N N 140 
GLU   N   H2   sing N N 141 
GLU   CA  C    sing N N 142 
GLU   CA  CB   sing N N 143 
GLU   CA  HA   sing N N 144 
GLU   C   O    doub N N 145 
GLU   C   OXT  sing N N 146 
GLU   CB  CG   sing N N 147 
GLU   CB  HB2  sing N N 148 
GLU   CB  HB3  sing N N 149 
GLU   CG  CD   sing N N 150 
GLU   CG  HG2  sing N N 151 
GLU   CG  HG3  sing N N 152 
GLU   CD  OE1  doub N N 153 
GLU   CD  OE2  sing N N 154 
GLU   OE2 HE2  sing N N 155 
GLU   OXT HXT  sing N N 156 
GLY   N   CA   sing N N 157 
GLY   N   H    sing N N 158 
GLY   N   H2   sing N N 159 
GLY   CA  C    sing N N 160 
GLY   CA  HA2  sing N N 161 
GLY   CA  HA3  sing N N 162 
GLY   C   O    doub N N 163 
GLY   C   OXT  sing N N 164 
GLY   OXT HXT  sing N N 165 
HIS   N   CA   sing N N 166 
HIS   N   H    sing N N 167 
HIS   N   H2   sing N N 168 
HIS   CA  C    sing N N 169 
HIS   CA  CB   sing N N 170 
HIS   CA  HA   sing N N 171 
HIS   C   O    doub N N 172 
HIS   C   OXT  sing N N 173 
HIS   CB  CG   sing N N 174 
HIS   CB  HB2  sing N N 175 
HIS   CB  HB3  sing N N 176 
HIS   CG  ND1  sing Y N 177 
HIS   CG  CD2  doub Y N 178 
HIS   ND1 CE1  doub Y N 179 
HIS   ND1 HD1  sing N N 180 
HIS   CD2 NE2  sing Y N 181 
HIS   CD2 HD2  sing N N 182 
HIS   CE1 NE2  sing Y N 183 
HIS   CE1 HE1  sing N N 184 
HIS   NE2 HE2  sing N N 185 
HIS   OXT HXT  sing N N 186 
HOH   O   H1   sing N N 187 
HOH   O   H2   sing N N 188 
ILE   N   CA   sing N N 189 
ILE   N   H    sing N N 190 
ILE   N   H2   sing N N 191 
ILE   CA  C    sing N N 192 
ILE   CA  CB   sing N N 193 
ILE   CA  HA   sing N N 194 
ILE   C   O    doub N N 195 
ILE   C   OXT  sing N N 196 
ILE   CB  CG1  sing N N 197 
ILE   CB  CG2  sing N N 198 
ILE   CB  HB   sing N N 199 
ILE   CG1 CD1  sing N N 200 
ILE   CG1 HG12 sing N N 201 
ILE   CG1 HG13 sing N N 202 
ILE   CG2 HG21 sing N N 203 
ILE   CG2 HG22 sing N N 204 
ILE   CG2 HG23 sing N N 205 
ILE   CD1 HD11 sing N N 206 
ILE   CD1 HD12 sing N N 207 
ILE   CD1 HD13 sing N N 208 
ILE   OXT HXT  sing N N 209 
LEU   N   CA   sing N N 210 
LEU   N   H    sing N N 211 
LEU   N   H2   sing N N 212 
LEU   CA  C    sing N N 213 
LEU   CA  CB   sing N N 214 
LEU   CA  HA   sing N N 215 
LEU   C   O    doub N N 216 
LEU   C   OXT  sing N N 217 
LEU   CB  CG   sing N N 218 
LEU   CB  HB2  sing N N 219 
LEU   CB  HB3  sing N N 220 
LEU   CG  CD1  sing N N 221 
LEU   CG  CD2  sing N N 222 
LEU   CG  HG   sing N N 223 
LEU   CD1 HD11 sing N N 224 
LEU   CD1 HD12 sing N N 225 
LEU   CD1 HD13 sing N N 226 
LEU   CD2 HD21 sing N N 227 
LEU   CD2 HD22 sing N N 228 
LEU   CD2 HD23 sing N N 229 
LEU   OXT HXT  sing N N 230 
LYS   N   CA   sing N N 231 
LYS   N   H    sing N N 232 
LYS   N   H2   sing N N 233 
LYS   CA  C    sing N N 234 
LYS   CA  CB   sing N N 235 
LYS   CA  HA   sing N N 236 
LYS   C   O    doub N N 237 
LYS   C   OXT  sing N N 238 
LYS   CB  CG   sing N N 239 
LYS   CB  HB2  sing N N 240 
LYS   CB  HB3  sing N N 241 
LYS   CG  CD   sing N N 242 
LYS   CG  HG2  sing N N 243 
LYS   CG  HG3  sing N N 244 
LYS   CD  CE   sing N N 245 
LYS   CD  HD2  sing N N 246 
LYS   CD  HD3  sing N N 247 
LYS   CE  NZ   sing N N 248 
LYS   CE  HE2  sing N N 249 
LYS   CE  HE3  sing N N 250 
LYS   NZ  HZ1  sing N N 251 
LYS   NZ  HZ2  sing N N 252 
LYS   NZ  HZ3  sing N N 253 
LYS   OXT HXT  sing N N 254 
MET   N   CA   sing N N 255 
MET   N   H    sing N N 256 
MET   N   H2   sing N N 257 
MET   CA  C    sing N N 258 
MET   CA  CB   sing N N 259 
MET   CA  HA   sing N N 260 
MET   C   O    doub N N 261 
MET   C   OXT  sing N N 262 
MET   CB  CG   sing N N 263 
MET   CB  HB2  sing N N 264 
MET   CB  HB3  sing N N 265 
MET   CG  SD   sing N N 266 
MET   CG  HG2  sing N N 267 
MET   CG  HG3  sing N N 268 
MET   SD  CE   sing N N 269 
MET   CE  HE1  sing N N 270 
MET   CE  HE2  sing N N 271 
MET   CE  HE3  sing N N 272 
MET   OXT HXT  sing N N 273 
PHE   N   CA   sing N N 274 
PHE   N   H    sing N N 275 
PHE   N   H2   sing N N 276 
PHE   CA  C    sing N N 277 
PHE   CA  CB   sing N N 278 
PHE   CA  HA   sing N N 279 
PHE   C   O    doub N N 280 
PHE   C   OXT  sing N N 281 
PHE   CB  CG   sing N N 282 
PHE   CB  HB2  sing N N 283 
PHE   CB  HB3  sing N N 284 
PHE   CG  CD1  doub Y N 285 
PHE   CG  CD2  sing Y N 286 
PHE   CD1 CE1  sing Y N 287 
PHE   CD1 HD1  sing N N 288 
PHE   CD2 CE2  doub Y N 289 
PHE   CD2 HD2  sing N N 290 
PHE   CE1 CZ   doub Y N 291 
PHE   CE1 HE1  sing N N 292 
PHE   CE2 CZ   sing Y N 293 
PHE   CE2 HE2  sing N N 294 
PHE   CZ  HZ   sing N N 295 
PHE   OXT HXT  sing N N 296 
PRO   N   CA   sing N N 297 
PRO   N   CD   sing N N 298 
PRO   N   H    sing N N 299 
PRO   CA  C    sing N N 300 
PRO   CA  CB   sing N N 301 
PRO   CA  HA   sing N N 302 
PRO   C   O    doub N N 303 
PRO   C   OXT  sing N N 304 
PRO   CB  CG   sing N N 305 
PRO   CB  HB2  sing N N 306 
PRO   CB  HB3  sing N N 307 
PRO   CG  CD   sing N N 308 
PRO   CG  HG2  sing N N 309 
PRO   CG  HG3  sing N N 310 
PRO   CD  HD2  sing N N 311 
PRO   CD  HD3  sing N N 312 
PRO   OXT HXT  sing N N 313 
SER   N   CA   sing N N 314 
SER   N   H    sing N N 315 
SER   N   H2   sing N N 316 
SER   CA  C    sing N N 317 
SER   CA  CB   sing N N 318 
SER   CA  HA   sing N N 319 
SER   C   O    doub N N 320 
SER   C   OXT  sing N N 321 
SER   CB  OG   sing N N 322 
SER   CB  HB2  sing N N 323 
SER   CB  HB3  sing N N 324 
SER   OG  HG   sing N N 325 
SER   OXT HXT  sing N N 326 
THR   N   CA   sing N N 327 
THR   N   H    sing N N 328 
THR   N   H2   sing N N 329 
THR   CA  C    sing N N 330 
THR   CA  CB   sing N N 331 
THR   CA  HA   sing N N 332 
THR   C   O    doub N N 333 
THR   C   OXT  sing N N 334 
THR   CB  OG1  sing N N 335 
THR   CB  CG2  sing N N 336 
THR   CB  HB   sing N N 337 
THR   OG1 HG1  sing N N 338 
THR   CG2 HG21 sing N N 339 
THR   CG2 HG22 sing N N 340 
THR   CG2 HG23 sing N N 341 
THR   OXT HXT  sing N N 342 
TRP   N   CA   sing N N 343 
TRP   N   H    sing N N 344 
TRP   N   H2   sing N N 345 
TRP   CA  C    sing N N 346 
TRP   CA  CB   sing N N 347 
TRP   CA  HA   sing N N 348 
TRP   C   O    doub N N 349 
TRP   C   OXT  sing N N 350 
TRP   CB  CG   sing N N 351 
TRP   CB  HB2  sing N N 352 
TRP   CB  HB3  sing N N 353 
TRP   CG  CD1  doub Y N 354 
TRP   CG  CD2  sing Y N 355 
TRP   CD1 NE1  sing Y N 356 
TRP   CD1 HD1  sing N N 357 
TRP   CD2 CE2  doub Y N 358 
TRP   CD2 CE3  sing Y N 359 
TRP   NE1 CE2  sing Y N 360 
TRP   NE1 HE1  sing N N 361 
TRP   CE2 CZ2  sing Y N 362 
TRP   CE3 CZ3  doub Y N 363 
TRP   CE3 HE3  sing N N 364 
TRP   CZ2 CH2  doub Y N 365 
TRP   CZ2 HZ2  sing N N 366 
TRP   CZ3 CH2  sing Y N 367 
TRP   CZ3 HZ3  sing N N 368 
TRP   CH2 HH2  sing N N 369 
TRP   OXT HXT  sing N N 370 
TYR   N   CA   sing N N 371 
TYR   N   H    sing N N 372 
TYR   N   H2   sing N N 373 
TYR   CA  C    sing N N 374 
TYR   CA  CB   sing N N 375 
TYR   CA  HA   sing N N 376 
TYR   C   O    doub N N 377 
TYR   C   OXT  sing N N 378 
TYR   CB  CG   sing N N 379 
TYR   CB  HB2  sing N N 380 
TYR   CB  HB3  sing N N 381 
TYR   CG  CD1  doub Y N 382 
TYR   CG  CD2  sing Y N 383 
TYR   CD1 CE1  sing Y N 384 
TYR   CD1 HD1  sing N N 385 
TYR   CD2 CE2  doub Y N 386 
TYR   CD2 HD2  sing N N 387 
TYR   CE1 CZ   doub Y N 388 
TYR   CE1 HE1  sing N N 389 
TYR   CE2 CZ   sing Y N 390 
TYR   CE2 HE2  sing N N 391 
TYR   CZ  OH   sing N N 392 
TYR   OH  HH   sing N N 393 
TYR   OXT HXT  sing N N 394 
VAL   N   CA   sing N N 395 
VAL   N   H    sing N N 396 
VAL   N   H2   sing N N 397 
VAL   CA  C    sing N N 398 
VAL   CA  CB   sing N N 399 
VAL   CA  HA   sing N N 400 
VAL   C   O    doub N N 401 
VAL   C   OXT  sing N N 402 
VAL   CB  CG1  sing N N 403 
VAL   CB  CG2  sing N N 404 
VAL   CB  HB   sing N N 405 
VAL   CG1 HG11 sing N N 406 
VAL   CG1 HG12 sing N N 407 
VAL   CG1 HG13 sing N N 408 
VAL   CG2 HG21 sing N N 409 
VAL   CG2 HG22 sing N N 410 
VAL   CG2 HG23 sing N N 411 
VAL   OXT HXT  sing N N 412 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      Other 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          'Inhouse model' 
# 
_atom_sites.entry_id                    8RGF 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.021304 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.007399 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.006889 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
B  
C  
MN 
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . VAL   A 1 17  ? -13.164 13.924  -17.742 1.00 68.52  ? 23  VAL   A N   1 
ATOM   2    C  CA  . VAL   A 1 17  ? -14.109 13.950  -18.862 1.00 68.29  ? 23  VAL   A CA  1 
ATOM   3    C  C   . VAL   A 1 17  ? -14.187 12.554  -19.516 1.00 71.45  ? 23  VAL   A C   1 
ATOM   4    O  O   . VAL   A 1 17  ? -13.161 12.008  -19.941 1.00 71.44  ? 23  VAL   A O   1 
ATOM   5    C  CB  . VAL   A 1 17  ? -13.805 15.061  -19.914 1.00 72.72  ? 23  VAL   A CB  1 
ATOM   6    C  CG1 . VAL   A 1 17  ? -15.053 15.405  -20.728 1.00 72.44  ? 23  VAL   A CG1 1 
ATOM   7    C  CG2 . VAL   A 1 17  ? -13.222 16.321  -19.269 1.00 72.66  ? 23  VAL   A CG2 1 
ATOM   8    N  N   . HIS   A 1 18  ? -15.406 11.986  -19.577 1.00 66.07  ? 24  HIS   A N   1 
ATOM   9    C  CA  . HIS   A 1 18  ? -15.692 10.675  -20.175 1.00 64.86  ? 24  HIS   A CA  1 
ATOM   10   C  C   . HIS   A 1 18  ? -16.881 10.813  -21.120 1.00 64.13  ? 24  HIS   A C   1 
ATOM   11   O  O   . HIS   A 1 18  ? -17.796 11.586  -20.839 1.00 63.85  ? 24  HIS   A O   1 
ATOM   12   C  CB  . HIS   A 1 18  ? -16.080 9.629   -19.101 1.00 66.20  ? 24  HIS   A CB  1 
ATOM   13   C  CG  . HIS   A 1 18  ? -15.206 9.590   -17.884 1.00 70.08  ? 24  HIS   A CG  1 
ATOM   14   N  ND1 . HIS   A 1 18  ? -14.182 8.667   -17.761 1.00 72.05  ? 24  HIS   A ND1 1 
ATOM   15   C  CD2 . HIS   A 1 18  ? -15.265 10.332  -16.753 1.00 71.98  ? 24  HIS   A CD2 1 
ATOM   16   C  CE1 . HIS   A 1 18  ? -13.637 8.894   -16.577 1.00 71.52  ? 24  HIS   A CE1 1 
ATOM   17   N  NE2 . HIS   A 1 18  ? -14.247 9.894   -15.939 1.00 71.85  ? 24  HIS   A NE2 1 
ATOM   18   N  N   . SER   A 1 19  ? -16.896 10.033  -22.211 1.00 56.51  ? 25  SER   A N   1 
ATOM   19   C  CA  . SER   A 1 19  ? -18.024 9.987   -23.139 1.00 53.93  ? 25  SER   A CA  1 
ATOM   20   C  C   . SER   A 1 19  ? -18.854 8.788   -22.667 1.00 51.90  ? 25  SER   A C   1 
ATOM   21   O  O   . SER   A 1 19  ? -18.350 7.667   -22.640 1.00 50.94  ? 25  SER   A O   1 
ATOM   22   C  CB  . SER   A 1 19  ? -17.538 9.800   -24.578 1.00 57.96  ? 25  SER   A CB  1 
ATOM   23   O  OG  . SER   A 1 19  ? -16.815 10.927  -25.047 1.00 65.24  ? 25  SER   A OG  1 
ATOM   24   N  N   . VAL   A 1 20  ? -20.076 9.033   -22.212 1.00 44.80  ? 26  VAL   A N   1 
ATOM   25   C  CA  . VAL   A 1 20  ? -20.923 7.988   -21.636 1.00 44.19  ? 26  VAL   A CA  1 
ATOM   26   C  C   . VAL   A 1 20  ? -22.232 7.851   -22.382 1.00 47.21  ? 26  VAL   A C   1 
ATOM   27   O  O   . VAL   A 1 20  ? -23.008 8.809   -22.453 1.00 47.50  ? 26  VAL   A O   1 
ATOM   28   C  CB  . VAL   A 1 20  ? -21.153 8.231   -20.102 1.00 47.61  ? 26  VAL   A CB  1 
ATOM   29   C  CG1 . VAL   A 1 20  ? -22.148 7.242   -19.500 1.00 47.11  ? 26  VAL   A CG1 1 
ATOM   30   C  CG2 . VAL   A 1 20  ? -19.842 8.223   -19.322 1.00 47.32  ? 26  VAL   A CG2 1 
ATOM   31   N  N   . ALA   A 1 21  ? -22.500 6.643   -22.892 1.00 42.56  ? 27  ALA   A N   1 
ATOM   32   C  CA  . ALA   A 1 21  ? -23.764 6.306   -23.537 1.00 41.93  ? 27  ALA   A CA  1 
ATOM   33   C  C   . ALA   A 1 21  ? -24.638 5.589   -22.524 1.00 45.78  ? 27  ALA   A C   1 
ATOM   34   O  O   . ALA   A 1 21  ? -24.148 4.721   -21.789 1.00 45.49  ? 27  ALA   A O   1 
ATOM   35   C  CB  . ALA   A 1 21  ? -23.528 5.408   -24.731 1.00 42.70  ? 27  ALA   A CB  1 
ATOM   36   N  N   . VAL   A 1 22  ? -25.923 5.945   -22.478 1.00 40.74  ? 28  VAL   A N   1 
ATOM   37   C  CA  . VAL   A 1 22  ? -26.873 5.325   -21.560 1.00 40.21  ? 28  VAL   A CA  1 
ATOM   38   C  C   . VAL   A 1 22  ? -27.965 4.637   -22.373 1.00 42.95  ? 28  VAL   A C   1 
ATOM   39   O  O   . VAL   A 1 22  ? -28.533 5.250   -23.280 1.00 41.90  ? 28  VAL   A O   1 
ATOM   40   C  CB  . VAL   A 1 22  ? -27.424 6.321   -20.491 1.00 43.88  ? 28  VAL   A CB  1 
ATOM   41   C  CG1 . VAL   A 1 22  ? -28.503 5.683   -19.618 1.00 43.38  ? 28  VAL   A CG1 1 
ATOM   42   C  CG2 . VAL   A 1 22  ? -26.296 6.893   -19.628 1.00 43.65  ? 28  VAL   A CG2 1 
ATOM   43   N  N   . ILE   A 1 23  ? -28.217 3.342   -22.068 1.00 38.27  ? 29  ILE   A N   1 
ATOM   44   C  CA  . ILE   A 1 23  ? -29.240 2.521   -22.704 1.00 37.76  ? 29  ILE   A CA  1 
ATOM   45   C  C   . ILE   A 1 23  ? -30.165 1.950   -21.643 1.00 41.65  ? 29  ILE   A C   1 
ATOM   46   O  O   . ILE   A 1 23  ? -29.715 1.227   -20.756 1.00 39.39  ? 29  ILE   A O   1 
ATOM   47   C  CB  . ILE   A 1 23  ? -28.641 1.361   -23.573 1.00 40.39  ? 29  ILE   A CB  1 
ATOM   48   C  CG1 . ILE   A 1 23  ? -27.634 1.859   -24.619 1.00 40.54  ? 29  ILE   A CG1 1 
ATOM   49   C  CG2 . ILE   A 1 23  ? -29.752 0.516   -24.217 1.00 41.46  ? 29  ILE   A CG2 1 
ATOM   50   C  CD1 . ILE   A 1 23  ? -26.782 0.772   -25.214 1.00 45.84  ? 29  ILE   A CD1 1 
ATOM   51   N  N   . GLY   A 1 24  ? -31.458 2.191   -21.807 1.00 39.54  ? 30  GLY   A N   1 
ATOM   52   C  CA  . GLY   A 1 24  ? -32.482 1.589   -20.970 1.00 40.10  ? 30  GLY   A CA  1 
ATOM   53   C  C   . GLY   A 1 24  ? -32.940 0.278   -21.584 1.00 46.09  ? 30  GLY   A C   1 
ATOM   54   O  O   . GLY   A 1 24  ? -33.308 0.238   -22.764 1.00 45.55  ? 30  GLY   A O   1 
ATOM   55   N  N   . ALA   A 1 25  ? -32.890 -0.822  -20.803 1.00 43.65  ? 31  ALA   A N   1 
ATOM   56   C  CA  . ALA   A 1 25  ? -33.313 -2.141  -21.267 1.00 43.36  ? 31  ALA   A CA  1 
ATOM   57   C  C   . ALA   A 1 25  ? -34.431 -2.715  -20.385 1.00 47.49  ? 31  ALA   A C   1 
ATOM   58   O  O   . ALA   A 1 25  ? -34.171 -3.621  -19.578 1.00 47.56  ? 31  ALA   A O   1 
ATOM   59   C  CB  . ALA   A 1 25  ? -32.124 -3.095  -21.363 1.00 44.14  ? 31  ALA   A CB  1 
ATOM   60   N  N   . PRO   A 1 26  ? -35.689 -2.204  -20.545 1.00 43.72  ? 32  PRO   A N   1 
ATOM   61   C  CA  . PRO   A 1 26  ? -36.814 -2.715  -19.740 1.00 43.53  ? 32  PRO   A CA  1 
ATOM   62   C  C   . PRO   A 1 26  ? -37.235 -4.134  -20.138 1.00 48.56  ? 32  PRO   A C   1 
ATOM   63   O  O   . PRO   A 1 26  ? -38.227 -4.334  -20.852 1.00 48.31  ? 32  PRO   A O   1 
ATOM   64   C  CB  . PRO   A 1 26  ? -37.920 -1.678  -19.995 1.00 45.10  ? 32  PRO   A CB  1 
ATOM   65   C  CG  . PRO   A 1 26  ? -37.619 -1.118  -21.314 1.00 49.29  ? 32  PRO   A CG  1 
ATOM   66   C  CD  . PRO   A 1 26  ? -36.133 -1.114  -21.447 1.00 44.81  ? 32  PRO   A CD  1 
ATOM   67   N  N   . PHE   A 1 27  ? -36.475 -5.127  -19.657 1.00 44.52  ? 33  PHE   A N   1 
ATOM   68   C  CA  . PHE   A 1 27  ? -36.681 -6.536  -19.981 1.00 43.64  ? 33  PHE   A CA  1 
ATOM   69   C  C   . PHE   A 1 27  ? -36.745 -7.412  -18.720 1.00 44.88  ? 33  PHE   A C   1 
ATOM   70   O  O   . PHE   A 1 27  ? -35.915 -7.273  -17.826 1.00 43.35  ? 33  PHE   A O   1 
ATOM   71   C  CB  . PHE   A 1 27  ? -35.575 -6.995  -20.952 1.00 45.46  ? 33  PHE   A CB  1 
ATOM   72   C  CG  . PHE   A 1 27  ? -35.730 -8.398  -21.475 1.00 46.92  ? 33  PHE   A CG  1 
ATOM   73   C  CD1 . PHE   A 1 27  ? -36.769 -8.725  -22.338 1.00 50.03  ? 33  PHE   A CD1 1 
ATOM   74   C  CD2 . PHE   A 1 27  ? -34.841 -9.400  -21.097 1.00 49.60  ? 33  PHE   A CD2 1 
ATOM   75   C  CE1 . PHE   A 1 27  ? -36.926 -10.032 -22.806 1.00 51.53  ? 33  PHE   A CE1 1 
ATOM   76   C  CE2 . PHE   A 1 27  ? -34.987 -10.703 -21.577 1.00 52.49  ? 33  PHE   A CE2 1 
ATOM   77   C  CZ  . PHE   A 1 27  ? -36.028 -11.009 -22.432 1.00 50.85  ? 33  PHE   A CZ  1 
ATOM   78   N  N   . SER   A 1 28  ? -37.743 -8.290  -18.645 1.00 39.91  ? 34  SER   A N   1 
ATOM   79   C  CA  . SER   A 1 28  ? -37.958 -9.133  -17.473 1.00 39.35  ? 34  SER   A CA  1 
ATOM   80   C  C   . SER   A 1 28  ? -38.085 -10.621 -17.755 1.00 42.10  ? 34  SER   A C   1 
ATOM   81   O  O   . SER   A 1 28  ? -38.238 -11.400 -16.806 1.00 41.28  ? 34  SER   A O   1 
ATOM   82   C  CB  . SER   A 1 28  ? -39.210 -8.659  -16.738 1.00 43.69  ? 34  SER   A CB  1 
ATOM   83   O  OG  . SER   A 1 28  ? -40.383 -9.075  -17.417 1.00 52.74  ? 34  SER   A OG  1 
ATOM   84   N  N   . GLN   A 1 29  ? -38.072 -11.029 -19.039 1.00 39.25  ? 35  GLN   A N   1 
ATOM   85   C  CA  . GLN   A 1 29  ? -38.308 -12.422 -19.420 1.00 39.13  ? 35  GLN   A CA  1 
ATOM   86   C  C   . GLN   A 1 29  ? -37.182 -13.416 -19.027 1.00 41.69  ? 35  GLN   A C   1 
ATOM   87   O  O   . GLN   A 1 29  ? -37.378 -14.625 -19.172 1.00 41.66  ? 35  GLN   A O   1 
ATOM   88   C  CB  . GLN   A 1 29  ? -38.649 -12.533 -20.917 1.00 40.71  ? 35  GLN   A CB  1 
ATOM   89   C  CG  . GLN   A 1 29  ? -40.149 -12.554 -21.227 1.00 64.78  ? 35  GLN   A CG  1 
ATOM   90   C  CD  . GLN   A 1 29  ? -40.817 -11.218 -21.062 1.00 88.70  ? 35  GLN   A CD  1 
ATOM   91   O  OE1 . GLN   A 1 29  ? -41.312 -10.876 -19.983 1.00 86.63  ? 35  GLN   A OE1 1 
ATOM   92   N  NE2 . GLN   A 1 29  ? -40.861 -10.444 -22.138 1.00 80.46  ? 35  GLN   A NE2 1 
ATOM   93   N  N   . GLY   A 1 30  ? -36.064 -12.917 -18.491 1.00 37.81  ? 36  GLY   A N   1 
ATOM   94   C  CA  . GLY   A 1 30  ? -34.985 -13.769 -17.988 1.00 37.62  ? 36  GLY   A CA  1 
ATOM   95   C  C   . GLY   A 1 30  ? -35.311 -14.392 -16.633 1.00 42.53  ? 36  GLY   A C   1 
ATOM   96   O  O   . GLY   A 1 30  ? -34.603 -15.297 -16.173 1.00 40.94  ? 36  GLY   A O   1 
ATOM   97   N  N   . GLN   A 1 31  ? -36.393 -13.900 -15.975 1.00 39.27  ? 37  GLN   A N   1 
ATOM   98   C  CA  . GLN   A 1 31  ? -36.890 -14.360 -14.679 1.00 40.53  ? 37  GLN   A CA  1 
ATOM   99   C  C   . GLN   A 1 31  ? -38.439 -14.350 -14.620 1.00 49.15  ? 37  GLN   A C   1 
ATOM   100  O  O   . GLN   A 1 31  ? -39.085 -14.032 -15.621 1.00 48.86  ? 37  GLN   A O   1 
ATOM   101  C  CB  . GLN   A 1 31  ? -36.237 -13.604 -13.506 1.00 41.59  ? 37  GLN   A CB  1 
ATOM   102  C  CG  . GLN   A 1 31  ? -36.108 -12.099 -13.684 1.00 44.31  ? 37  GLN   A CG  1 
ATOM   103  C  CD  . GLN   A 1 31  ? -37.309 -11.394 -13.125 1.00 65.90  ? 37  GLN   A CD  1 
ATOM   104  O  OE1 . GLN   A 1 31  ? -37.415 -11.167 -11.917 1.00 63.34  ? 37  GLN   A OE1 1 
ATOM   105  N  NE2 . GLN   A 1 31  ? -38.243 -11.047 -13.994 1.00 57.60  ? 37  GLN   A NE2 1 
ATOM   106  N  N   . LYS   A 1 32  ? -39.024 -14.745 -13.472 1.00 48.36  ? 38  LYS   A N   1 
ATOM   107  C  CA  . LYS   A 1 32  ? -40.480 -14.852 -13.311 1.00 49.27  ? 38  LYS   A CA  1 
ATOM   108  C  C   . LYS   A 1 32  ? -41.128 -13.717 -12.496 1.00 55.61  ? 38  LYS   A C   1 
ATOM   109  O  O   . LYS   A 1 32  ? -42.346 -13.548 -12.582 1.00 56.57  ? 38  LYS   A O   1 
ATOM   110  C  CB  . LYS   A 1 32  ? -40.856 -16.229 -12.717 1.00 51.46  ? 38  LYS   A CB  1 
ATOM   111  C  CG  . LYS   A 1 32  ? -40.684 -17.403 -13.689 1.00 59.55  ? 38  LYS   A CG  1 
ATOM   112  C  CD  . LYS   A 1 32  ? -41.065 -18.732 -13.034 1.00 64.14  ? 38  LYS   A CD  1 
ATOM   113  C  CE  . LYS   A 1 32  ? -40.594 -19.940 -13.811 1.00 67.88  ? 38  LYS   A CE  1 
ATOM   114  N  NZ  . LYS   A 1 32  ? -39.270 -20.436 -13.336 1.00 71.51  ? 38  LYS   A NZ  1 
ATOM   115  N  N   . ARG   A 1 33  ? -40.334 -12.940 -11.729 1.00 52.79  ? 39  ARG   A N   1 
ATOM   116  C  CA  . ARG   A 1 33  ? -40.840 -11.849 -10.878 1.00 52.55  ? 39  ARG   A CA  1 
ATOM   117  C  C   . ARG   A 1 33  ? -41.084 -10.543 -11.651 1.00 56.56  ? 39  ARG   A C   1 
ATOM   118  O  O   . ARG   A 1 33  ? -40.160 -9.990  -12.262 1.00 56.35  ? 39  ARG   A O   1 
ATOM   119  C  CB  . ARG   A 1 33  ? -39.935 -11.620 -9.648  1.00 51.40  ? 39  ARG   A CB  1 
ATOM   120  C  CG  . ARG   A 1 33  ? -39.692 -12.885 -8.821  1.00 59.87  ? 39  ARG   A CG  1 
ATOM   121  C  CD  . ARG   A 1 33  ? -40.362 -12.833 -7.468  1.00 67.62  ? 39  ARG   A CD  1 
ATOM   122  N  NE  . ARG   A 1 33  ? -39.408 -12.465 -6.424  1.00 70.36  ? 39  ARG   A NE  1 
ATOM   123  C  CZ  . ARG   A 1 33  ? -39.741 -11.954 -5.243  1.00 79.92  ? 39  ARG   A CZ  1 
ATOM   124  N  NH1 . ARG   A 1 33  ? -41.016 -11.731 -4.943  1.00 58.42  ? 39  ARG   A NH1 1 
ATOM   125  N  NH2 . ARG   A 1 33  ? -38.801 -11.648 -4.358  1.00 68.65  ? 39  ARG   A NH2 1 
ATOM   126  N  N   . LYS   A 1 34  ? -42.338 -10.044 -11.596 1.00 51.85  ? 40  LYS   A N   1 
ATOM   127  C  CA  . LYS   A 1 34  ? -42.777 -8.819  -12.282 1.00 50.75  ? 40  LYS   A CA  1 
ATOM   128  C  C   . LYS   A 1 34  ? -42.181 -7.549  -11.682 1.00 52.80  ? 40  LYS   A C   1 
ATOM   129  O  O   . LYS   A 1 34  ? -41.998 -7.456  -10.461 1.00 52.02  ? 40  LYS   A O   1 
ATOM   130  C  CB  . LYS   A 1 34  ? -44.321 -8.691  -12.281 1.00 52.63  ? 40  LYS   A CB  1 
ATOM   131  C  CG  . LYS   A 1 34  ? -45.065 -10.016 -12.203 1.00 69.53  ? 40  LYS   A CG  1 
ATOM   132  C  CD  . LYS   A 1 34  ? -46.338 -10.029 -13.015 1.00 78.70  ? 40  LYS   A CD  1 
ATOM   133  C  CE  . LYS   A 1 34  ? -46.852 -11.440 -13.137 1.00 89.48  ? 40  LYS   A CE  1 
ATOM   134  N  NZ  . LYS   A 1 34  ? -48.119 -11.507 -13.906 1.00 98.34  ? 40  LYS   A NZ  1 
ATOM   135  N  N   . GLY   A 1 35  ? -41.917 -6.573  -12.548 1.00 47.76  ? 41  GLY   A N   1 
ATOM   136  C  CA  . GLY   A 1 35  ? -41.464 -5.256  -12.123 1.00 46.65  ? 41  GLY   A CA  1 
ATOM   137  C  C   . GLY   A 1 35  ? -40.049 -4.837  -12.432 1.00 46.58  ? 41  GLY   A C   1 
ATOM   138  O  O   . GLY   A 1 35  ? -39.775 -3.639  -12.388 1.00 44.94  ? 41  GLY   A O   1 
ATOM   139  N  N   . VAL   A 1 36  ? -39.133 -5.803  -12.720 1.00 42.47  ? 42  VAL   A N   1 
ATOM   140  C  CA  . VAL   A 1 36  ? -37.715 -5.505  -13.001 1.00 40.76  ? 42  VAL   A CA  1 
ATOM   141  C  C   . VAL   A 1 36  ? -37.578 -4.678  -14.308 1.00 44.11  ? 42  VAL   A C   1 
ATOM   142  O  O   . VAL   A 1 36  ? -36.597 -3.956  -14.477 1.00 42.68  ? 42  VAL   A O   1 
ATOM   143  C  CB  . VAL   A 1 36  ? -36.796 -6.771  -12.943 1.00 43.72  ? 42  VAL   A CB  1 
ATOM   144  C  CG1 . VAL   A 1 36  ? -37.002 -7.693  -14.139 1.00 44.29  ? 42  VAL   A CG1 1 
ATOM   145  C  CG2 . VAL   A 1 36  ? -35.331 -6.402  -12.799 1.00 42.58  ? 42  VAL   A CG2 1 
ATOM   146  N  N   . GLU   A 1 37  ? -38.596 -4.739  -15.192 1.00 42.41  ? 43  GLU   A N   1 
ATOM   147  C  CA  . GLU   A 1 37  ? -38.657 -3.948  -16.427 1.00 42.82  ? 43  GLU   A CA  1 
ATOM   148  C  C   . GLU   A 1 37  ? -38.790 -2.434  -16.125 1.00 49.27  ? 43  GLU   A C   1 
ATOM   149  O  O   . GLU   A 1 37  ? -38.531 -1.625  -17.007 1.00 51.19  ? 43  GLU   A O   1 
ATOM   150  C  CB  . GLU   A 1 37  ? -39.788 -4.436  -17.374 1.00 43.92  ? 43  GLU   A CB  1 
ATOM   151  C  CG  . GLU   A 1 37  ? -41.196 -4.327  -16.805 1.00 54.91  ? 43  GLU   A CG  1 
ATOM   152  C  CD  . GLU   A 1 37  ? -41.724 -5.585  -16.137 1.00 81.80  ? 43  GLU   A CD  1 
ATOM   153  O  OE1 . GLU   A 1 37  ? -41.047 -6.114  -15.226 1.00 70.31  ? 43  GLU   A OE1 1 
ATOM   154  O  OE2 . GLU   A 1 37  ? -42.823 -6.042  -16.527 1.00 80.73  ? 43  GLU   A OE2 1 
ATOM   155  N  N   . HIS   A 1 38  ? -39.181 -2.063  -14.890 1.00 45.47  ? 44  HIS   A N   1 
ATOM   156  C  CA  . HIS   A 1 38  ? -39.334 -0.672  -14.453 1.00 44.87  ? 44  HIS   A CA  1 
ATOM   157  C  C   . HIS   A 1 38  ? -38.069 -0.113  -13.795 1.00 45.29  ? 44  HIS   A C   1 
ATOM   158  O  O   . HIS   A 1 38  ? -38.027 1.060   -13.422 1.00 42.54  ? 44  HIS   A O   1 
ATOM   159  C  CB  . HIS   A 1 38  ? -40.571 -0.517  -13.559 1.00 46.42  ? 44  HIS   A CB  1 
ATOM   160  C  CG  . HIS   A 1 38  ? -41.840 -0.930  -14.237 1.00 50.65  ? 44  HIS   A CG  1 
ATOM   161  N  ND1 . HIS   A 1 38  ? -42.240 -0.358  -15.433 1.00 52.95  ? 44  HIS   A ND1 1 
ATOM   162  C  CD2 . HIS   A 1 38  ? -42.761 -1.844  -13.861 1.00 53.65  ? 44  HIS   A CD2 1 
ATOM   163  C  CE1 . HIS   A 1 38  ? -43.381 -0.945  -15.751 1.00 52.85  ? 44  HIS   A CE1 1 
ATOM   164  N  NE2 . HIS   A 1 38  ? -43.741 -1.842  -14.834 1.00 53.53  ? 44  HIS   A NE2 1 
ATOM   165  N  N   . GLY   A 1 39  ? -37.032 -0.955  -13.711 1.00 42.18  ? 45  GLY   A N   1 
ATOM   166  C  CA  . GLY   A 1 39  ? -35.720 -0.596  -13.185 1.00 40.87  ? 45  GLY   A CA  1 
ATOM   167  C  C   . GLY   A 1 39  ? -35.063 0.558   -13.923 1.00 43.50  ? 45  GLY   A C   1 
ATOM   168  O  O   . GLY   A 1 39  ? -34.596 1.486   -13.257 1.00 44.14  ? 45  GLY   A O   1 
ATOM   169  N  N   . PRO   A 1 40  ? -35.027 0.592   -15.287 1.00 40.39  ? 46  PRO   A N   1 
ATOM   170  C  CA  . PRO   A 1 40  ? -34.419 1.758   -15.968 1.00 40.02  ? 46  PRO   A CA  1 
ATOM   171  C  C   . PRO   A 1 40  ? -35.153 3.070   -15.658 1.00 41.82  ? 46  PRO   A C   1 
ATOM   172  O  O   . PRO   A 1 40  ? -34.495 4.083   -15.466 1.00 39.56  ? 46  PRO   A O   1 
ATOM   173  C  CB  . PRO   A 1 40  ? -34.506 1.398   -17.457 1.00 41.44  ? 46  PRO   A CB  1 
ATOM   174  C  CG  . PRO   A 1 40  ? -34.686 -0.096  -17.489 1.00 46.62  ? 46  PRO   A CG  1 
ATOM   175  C  CD  . PRO   A 1 40  ? -35.507 -0.397  -16.279 1.00 42.53  ? 46  PRO   A CD  1 
ATOM   176  N  N   . ALA   A 1 41  ? -36.503 3.033   -15.559 1.00 39.28  ? 47  ALA   A N   1 
ATOM   177  C  CA  . ALA   A 1 41  ? -37.325 4.210   -15.244 1.00 39.82  ? 47  ALA   A CA  1 
ATOM   178  C  C   . ALA   A 1 41  ? -37.004 4.724   -13.842 1.00 46.91  ? 47  ALA   A C   1 
ATOM   179  O  O   . ALA   A 1 41  ? -36.764 5.920   -13.672 1.00 48.05  ? 47  ALA   A O   1 
ATOM   180  C  CB  . ALA   A 1 41  ? -38.801 3.867   -15.356 1.00 40.83  ? 47  ALA   A CB  1 
ATOM   181  N  N   . ALA   A 1 42  ? -36.907 3.804   -12.856 1.00 44.13  ? 48  ALA   A N   1 
ATOM   182  C  CA  . ALA   A 1 42  ? -36.592 4.107   -11.458 1.00 42.26  ? 48  ALA   A CA  1 
ATOM   183  C  C   . ALA   A 1 42  ? -35.186 4.682   -11.272 1.00 43.22  ? 48  ALA   A C   1 
ATOM   184  O  O   . ALA   A 1 42  ? -35.029 5.612   -10.481 1.00 43.20  ? 48  ALA   A O   1 
ATOM   185  C  CB  . ALA   A 1 42  ? -36.802 2.872   -10.589 1.00 42.96  ? 48  ALA   A CB  1 
ATOM   186  N  N   . ILE   A 1 43  ? -34.186 4.190   -12.027 1.00 37.85  ? 49  ILE   A N   1 
ATOM   187  C  CA  . ILE   A 1 43  ? -32.794 4.685   -11.952 1.00 37.57  ? 49  ILE   A CA  1 
ATOM   188  C  C   . ILE   A 1 43  ? -32.675 6.088   -12.570 1.00 43.64  ? 49  ILE   A C   1 
ATOM   189  O  O   . ILE   A 1 43  ? -31.901 6.930   -12.090 1.00 42.55  ? 49  ILE   A O   1 
ATOM   190  C  CB  . ILE   A 1 43  ? -31.785 3.685   -12.584 1.00 39.86  ? 49  ILE   A CB  1 
ATOM   191  C  CG1 . ILE   A 1 43  ? -31.762 2.332   -11.808 1.00 39.66  ? 49  ILE   A CG1 1 
ATOM   192  C  CG2 . ILE   A 1 43  ? -30.376 4.296   -12.692 1.00 39.50  ? 49  ILE   A CG2 1 
ATOM   193  C  CD1 . ILE   A 1 43  ? -31.223 1.128   -12.634 1.00 41.95  ? 49  ILE   A CD1 1 
ATOM   194  N  N   . ARG   A 1 44  ? -33.432 6.320   -13.649 1.00 43.26  ? 50  ARG   A N   1 
ATOM   195  C  CA  . ARG   A 1 44  ? -33.475 7.607   -14.349 1.00 44.24  ? 50  ARG   A CA  1 
ATOM   196  C  C   . ARG   A 1 44  ? -34.137 8.636   -13.433 1.00 48.53  ? 50  ARG   A C   1 
ATOM   197  O  O   . ARG   A 1 44  ? -33.607 9.732   -13.268 1.00 47.72  ? 50  ARG   A O   1 
ATOM   198  C  CB  . ARG   A 1 44  ? -34.277 7.476   -15.652 1.00 44.61  ? 50  ARG   A CB  1 
ATOM   199  C  CG  . ARG   A 1 44  ? -33.504 6.894   -16.814 1.00 52.39  ? 50  ARG   A CG  1 
ATOM   200  C  CD  . ARG   A 1 44  ? -34.412 6.823   -18.031 1.00 58.54  ? 50  ARG   A CD  1 
ATOM   201  N  NE  . ARG   A 1 44  ? -33.787 6.146   -19.168 1.00 58.00  ? 50  ARG   A NE  1 
ATOM   202  C  CZ  . ARG   A 1 44  ? -32.881 6.696   -19.969 1.00 63.71  ? 50  ARG   A CZ  1 
ATOM   203  N  NH1 . ARG   A 1 44  ? -32.455 7.934   -19.750 1.00 52.68  ? 50  ARG   A NH1 1 
ATOM   204  N  NH2 . ARG   A 1 44  ? -32.377 6.004   -20.983 1.00 48.26  ? 50  ARG   A NH2 1 
ATOM   205  N  N   . GLU   A 1 45  ? -35.272 8.246   -12.803 1.00 46.63  ? 51  GLU   A N   1 
ATOM   206  C  CA  . GLU   A 1 45  ? -36.053 9.062   -11.870 1.00 47.37  ? 51  GLU   A CA  1 
ATOM   207  C  C   . GLU   A 1 45  ? -35.235 9.456   -10.646 1.00 52.64  ? 51  GLU   A C   1 
ATOM   208  O  O   . GLU   A 1 45  ? -35.448 10.535  -10.094 1.00 52.90  ? 51  GLU   A O   1 
ATOM   209  C  CB  . GLU   A 1 45  ? -37.348 8.345   -11.463 1.00 48.96  ? 51  GLU   A CB  1 
ATOM   210  C  CG  . GLU   A 1 45  ? -38.466 8.536   -12.478 1.00 63.59  ? 51  GLU   A CG  1 
ATOM   211  C  CD  . GLU   A 1 45  ? -39.659 7.602   -12.378 1.00 90.13  ? 51  GLU   A CD  1 
ATOM   212  O  OE1 . GLU   A 1 45  ? -40.057 7.252   -11.242 1.00 87.68  ? 51  GLU   A OE1 1 
ATOM   213  O  OE2 . GLU   A 1 45  ? -40.224 7.256   -13.442 1.00 82.41  ? 51  GLU   A OE2 1 
ATOM   214  N  N   . ALA   A 1 46  ? -34.258 8.602   -10.258 1.00 49.17  ? 52  ALA   A N   1 
ATOM   215  C  CA  . ALA   A 1 46  ? -33.331 8.855   -9.149  1.00 49.00  ? 52  ALA   A CA  1 
ATOM   216  C  C   . ALA   A 1 46  ? -32.240 9.898   -9.493  1.00 51.38  ? 52  ALA   A C   1 
ATOM   217  O  O   . ALA   A 1 46  ? -31.403 10.208  -8.644  1.00 50.94  ? 52  ALA   A O   1 
ATOM   218  C  CB  . ALA   A 1 46  ? -32.716 7.547   -8.663  1.00 49.82  ? 52  ALA   A CB  1 
ATOM   219  N  N   . GLY   A 1 47  ? -32.278 10.432  -10.720 1.00 47.67  ? 53  GLY   A N   1 
ATOM   220  C  CA  . GLY   A 1 47  ? -31.404 11.504  -11.193 1.00 46.85  ? 53  GLY   A CA  1 
ATOM   221  C  C   . GLY   A 1 47  ? -30.070 11.129  -11.796 1.00 49.95  ? 53  GLY   A C   1 
ATOM   222  O  O   . GLY   A 1 47  ? -29.107 11.899  -11.677 1.00 48.86  ? 53  GLY   A O   1 
ATOM   223  N  N   . LEU   A 1 48  ? -30.012 9.964   -12.481 1.00 46.75  ? 54  LEU   A N   1 
ATOM   224  C  CA  . LEU   A 1 48  ? -28.807 9.437   -13.126 1.00 45.90  ? 54  LEU   A CA  1 
ATOM   225  C  C   . LEU   A 1 48  ? -28.129 10.409  -14.092 1.00 48.54  ? 54  LEU   A C   1 
ATOM   226  O  O   . LEU   A 1 48  ? -26.928 10.667  -13.962 1.00 48.13  ? 54  LEU   A O   1 
ATOM   227  C  CB  . LEU   A 1 48  ? -29.108 8.094   -13.849 1.00 45.82  ? 54  LEU   A CB  1 
ATOM   228  C  CG  . LEU   A 1 48  ? -27.928 7.440   -14.605 1.00 50.25  ? 54  LEU   A CG  1 
ATOM   229  C  CD1 . LEU   A 1 48  ? -26.872 6.919   -13.644 1.00 50.87  ? 54  LEU   A CD1 1 
ATOM   230  C  CD2 . LEU   A 1 48  ? -28.401 6.317   -15.486 1.00 51.56  ? 54  LEU   A CD2 1 
ATOM   231  N  N   . MET   A 1 49  ? -28.890 10.933  -15.059 1.00 45.52  ? 55  MET   A N   1 
ATOM   232  C  CA  . MET   A 1 49  ? -28.329 11.791  -16.102 1.00 45.52  ? 55  MET   A CA  1 
ATOM   233  C  C   . MET   A 1 49  ? -27.771 13.087  -15.530 1.00 48.88  ? 55  MET   A C   1 
ATOM   234  O  O   . MET   A 1 49  ? -26.623 13.417  -15.843 1.00 47.58  ? 55  MET   A O   1 
ATOM   235  C  CB  . MET   A 1 49  ? -29.310 12.005  -17.263 1.00 47.86  ? 55  MET   A CB  1 
ATOM   236  C  CG  . MET   A 1 49  ? -29.840 10.695  -17.847 1.00 51.47  ? 55  MET   A CG  1 
ATOM   237  S  SD  . MET   A 1 49  ? -28.564 9.527   -18.435 1.00 55.60  ? 55  MET   A SD  1 
ATOM   238  C  CE  . MET   A 1 49  ? -28.288 10.156  -20.054 1.00 52.48  ? 55  MET   A CE  1 
ATOM   239  N  N   . LYS   A 1 50  ? -28.516 13.740  -14.610 1.00 46.66  ? 56  LYS   A N   1 
ATOM   240  C  CA  . LYS   A 1 50  ? -28.075 14.955  -13.903 1.00 46.73  ? 56  LYS   A CA  1 
ATOM   241  C  C   . LYS   A 1 50  ? -26.780 14.684  -13.103 1.00 48.54  ? 56  LYS   A C   1 
ATOM   242  O  O   . LYS   A 1 50  ? -25.833 15.461  -13.208 1.00 47.73  ? 56  LYS   A O   1 
ATOM   243  C  CB  . LYS   A 1 50  ? -29.196 15.484  -12.990 1.00 50.85  ? 56  LYS   A CB  1 
ATOM   244  C  CG  . LYS   A 1 50  ? -28.997 16.931  -12.536 1.00 74.68  ? 56  LYS   A CG  1 
ATOM   245  C  CD  . LYS   A 1 50  ? -30.077 17.366  -11.549 1.00 87.69  ? 56  LYS   A CD  1 
ATOM   246  C  CE  . LYS   A 1 50  ? -29.852 18.774  -11.053 1.00 102.25 ? 56  LYS   A CE  1 
ATOM   247  N  NZ  . LYS   A 1 50  ? -30.890 19.187  -10.071 1.00 113.53 ? 56  LYS   A NZ  1 
ATOM   248  N  N   . ARG   A 1 51  ? -26.716 13.538  -12.369 1.00 44.35  ? 57  ARG   A N   1 
ATOM   249  C  CA  . ARG   A 1 51  ? -25.528 13.149  -11.603 1.00 43.27  ? 57  ARG   A CA  1 
ATOM   250  C  C   . ARG   A 1 51  ? -24.307 12.928  -12.516 1.00 45.23  ? 57  ARG   A C   1 
ATOM   251  O  O   . ARG   A 1 51  ? -23.208 13.354  -12.162 1.00 44.20  ? 57  ARG   A O   1 
ATOM   252  C  CB  . ARG   A 1 51  ? -25.817 11.910  -10.725 1.00 41.60  ? 57  ARG   A CB  1 
ATOM   253  C  CG  . ARG   A 1 51  ? -24.691 11.553  -9.760  1.00 46.28  ? 57  ARG   A CG  1 
ATOM   254  C  CD  . ARG   A 1 51  ? -24.723 12.315  -8.434  1.00 40.82  ? 57  ARG   A CD  1 
ATOM   255  N  NE  . ARG   A 1 51  ? -25.928 11.987  -7.679  1.00 54.21  ? 57  ARG   A NE  1 
ATOM   256  C  CZ  . ARG   A 1 51  ? -26.055 10.934  -6.875  1.00 63.31  ? 57  ARG   A CZ  1 
ATOM   257  N  NH1 . ARG   A 1 51  ? -27.203 10.699  -6.259  1.00 55.16  ? 57  ARG   A NH1 1 
ATOM   258  N  NH2 . ARG   A 1 51  ? -25.035 10.108  -6.683  1.00 40.03  ? 57  ARG   A NH2 1 
ATOM   259  N  N   . LEU   A 1 52  ? -24.500 12.265  -13.685 1.00 42.17  ? 58  LEU   A N   1 
ATOM   260  C  CA  . LEU   A 1 52  ? -23.403 12.042  -14.636 1.00 42.69  ? 58  LEU   A CA  1 
ATOM   261  C  C   . LEU   A 1 52  ? -22.968 13.358  -15.288 1.00 46.91  ? 58  LEU   A C   1 
ATOM   262  O  O   . LEU   A 1 52  ? -21.764 13.568  -15.492 1.00 45.21  ? 58  LEU   A O   1 
ATOM   263  C  CB  . LEU   A 1 52  ? -23.761 10.988  -15.700 1.00 43.06  ? 58  LEU   A CB  1 
ATOM   264  C  CG  . LEU   A 1 52  ? -24.003 9.556   -15.192 1.00 48.02  ? 58  LEU   A CG  1 
ATOM   265  C  CD1 . LEU   A 1 52  ? -24.656 8.696   -16.269 1.00 47.91  ? 58  LEU   A CD1 1 
ATOM   266  C  CD2 . LEU   A 1 52  ? -22.703 8.906   -14.678 1.00 50.98  ? 58  LEU   A CD2 1 
ATOM   267  N  N   . SER   A 1 53  ? -23.946 14.242  -15.593 1.00 45.69  ? 59  SER   A N   1 
ATOM   268  C  CA  . SER   A 1 53  ? -23.685 15.570  -16.171 1.00 47.23  ? 59  SER   A CA  1 
ATOM   269  C  C   . SER   A 1 53  ? -22.794 16.367  -15.209 1.00 53.27  ? 59  SER   A C   1 
ATOM   270  O  O   . SER   A 1 53  ? -21.746 16.856  -15.639 1.00 53.79  ? 59  SER   A O   1 
ATOM   271  C  CB  . SER   A 1 53  ? -24.988 16.329  -16.409 1.00 53.00  ? 59  SER   A CB  1 
ATOM   272  O  OG  . SER   A 1 53  ? -25.741 15.819  -17.499 1.00 68.41  ? 59  SER   A OG  1 
ATOM   273  N  N   . SER   A 1 54  ? -23.153 16.387  -13.890 1.00 50.16  ? 60  SER   A N   1 
ATOM   274  C  CA  . SER   A 1 54  ? -22.424 17.089  -12.825 1.00 50.66  ? 60  SER   A CA  1 
ATOM   275  C  C   . SER   A 1 54  ? -20.970 16.592  -12.632 1.00 55.05  ? 60  SER   A C   1 
ATOM   276  O  O   . SER   A 1 54  ? -20.156 17.302  -12.040 1.00 55.25  ? 60  SER   A O   1 
ATOM   277  C  CB  . SER   A 1 54  ? -23.211 17.068  -11.515 1.00 56.03  ? 60  SER   A CB  1 
ATOM   278  O  OG  . SER   A 1 54  ? -23.011 15.908  -10.718 1.00 70.35  ? 60  SER   A OG  1 
ATOM   279  N  N   . LEU   A 1 55  ? -20.641 15.400  -13.168 1.00 50.73  ? 61  LEU   A N   1 
ATOM   280  C  CA  . LEU   A 1 55  ? -19.300 14.821  -13.120 1.00 49.77  ? 61  LEU   A CA  1 
ATOM   281  C  C   . LEU   A 1 55  ? -18.484 15.194  -14.362 1.00 54.64  ? 61  LEU   A C   1 
ATOM   282  O  O   . LEU   A 1 55  ? -17.289 14.893  -14.431 1.00 53.59  ? 61  LEU   A O   1 
ATOM   283  C  CB  . LEU   A 1 55  ? -19.375 13.290  -12.945 1.00 49.60  ? 61  LEU   A CB  1 
ATOM   284  C  CG  . LEU   A 1 55  ? -19.778 12.794  -11.554 1.00 53.64  ? 61  LEU   A CG  1 
ATOM   285  C  CD1 . LEU   A 1 55  ? -20.377 11.397  -11.629 1.00 53.58  ? 61  LEU   A CD1 1 
ATOM   286  C  CD2 . LEU   A 1 55  ? -18.593 12.821  -10.594 1.00 55.72  ? 61  LEU   A CD2 1 
ATOM   287  N  N   . GLY   A 1 56  ? -19.128 15.867  -15.317 1.00 52.92  ? 62  GLY   A N   1 
ATOM   288  C  CA  . GLY   A 1 56  ? -18.484 16.313  -16.547 1.00 53.28  ? 62  GLY   A CA  1 
ATOM   289  C  C   . GLY   A 1 56  ? -18.515 15.321  -17.694 1.00 56.73  ? 62  GLY   A C   1 
ATOM   290  O  O   . GLY   A 1 56  ? -17.810 15.507  -18.687 1.00 56.81  ? 62  GLY   A O   1 
ATOM   291  N  N   . CYS   A 1 57  ? -19.348 14.281  -17.585 1.00 52.78  ? 63  CYS   A N   1 
ATOM   292  C  CA  . CYS   A 1 57  ? -19.493 13.260  -18.619 1.00 52.35  ? 63  CYS   A CA  1 
ATOM   293  C  C   . CYS   A 1 57  ? -20.255 13.791  -19.852 1.00 57.48  ? 63  CYS   A C   1 
ATOM   294  O  O   . CYS   A 1 57  ? -21.347 14.351  -19.705 1.00 56.85  ? 63  CYS   A O   1 
ATOM   295  C  CB  . CYS   A 1 57  ? -20.159 12.003  -18.050 1.00 51.93  ? 63  CYS   A CB  1 
ATOM   296  S  SG  . CYS   A 1 57  ? -19.150 11.104  -16.836 1.00 55.04  ? 63  CYS   A SG  1 
ATOM   297  N  N   . HIS   A 1 58  ? -19.677 13.602  -21.062 1.00 55.57  ? 64  HIS   A N   1 
ATOM   298  C  CA  . HIS   A 1 58  ? -20.315 13.933  -22.343 1.00 55.86  ? 64  HIS   A CA  1 
ATOM   299  C  C   . HIS   A 1 58  ? -21.307 12.793  -22.572 1.00 56.68  ? 64  HIS   A C   1 
ATOM   300  O  O   . HIS   A 1 58  ? -20.891 11.654  -22.765 1.00 55.83  ? 64  HIS   A O   1 
ATOM   301  C  CB  . HIS   A 1 58  ? -19.282 14.057  -23.495 1.00 57.65  ? 64  HIS   A CB  1 
ATOM   302  C  CG  . HIS   A 1 58  ? -19.860 13.855  -24.874 1.00 62.36  ? 64  HIS   A CG  1 
ATOM   303  N  ND1 . HIS   A 1 58  ? -21.035 14.488  -25.279 1.00 64.72  ? 64  HIS   A ND1 1 
ATOM   304  C  CD2 . HIS   A 1 58  ? -19.408 13.090  -25.897 1.00 64.81  ? 64  HIS   A CD2 1 
ATOM   305  C  CE1 . HIS   A 1 58  ? -21.258 14.077  -26.518 1.00 64.29  ? 64  HIS   A CE1 1 
ATOM   306  N  NE2 . HIS   A 1 58  ? -20.306 13.241  -26.937 1.00 64.69  ? 64  HIS   A NE2 1 
ATOM   307  N  N   . LEU   A 1 59  ? -22.604 13.086  -22.470 1.00 52.35  ? 65  LEU   A N   1 
ATOM   308  C  CA  . LEU   A 1 59  ? -23.640 12.065  -22.535 1.00 52.25  ? 65  LEU   A CA  1 
ATOM   309  C  C   . LEU   A 1 59  ? -24.396 11.931  -23.846 1.00 55.78  ? 65  LEU   A C   1 
ATOM   310  O  O   . LEU   A 1 59  ? -24.710 12.927  -24.491 1.00 55.19  ? 65  LEU   A O   1 
ATOM   311  C  CB  . LEU   A 1 59  ? -24.654 12.285  -21.400 1.00 52.46  ? 65  LEU   A CB  1 
ATOM   312  C  CG  . LEU   A 1 59  ? -24.151 11.970  -19.991 1.00 57.61  ? 65  LEU   A CG  1 
ATOM   313  C  CD1 . LEU   A 1 59  ? -24.692 12.960  -18.986 1.00 57.65  ? 65  LEU   A CD1 1 
ATOM   314  C  CD2 . LEU   A 1 59  ? -24.480 10.538  -19.593 1.00 59.23  ? 65  LEU   A CD2 1 
ATOM   315  N  N   . LYS   A 1 60  ? -24.733 10.672  -24.196 1.00 51.22  ? 66  LYS   A N   1 
ATOM   316  C  CA  . LYS   A 1 60  ? -25.591 10.297  -25.307 1.00 50.65  ? 66  LYS   A CA  1 
ATOM   317  C  C   . LYS   A 1 60  ? -26.636 9.332   -24.754 1.00 53.42  ? 66  LYS   A C   1 
ATOM   318  O  O   . LYS   A 1 60  ? -26.305 8.203   -24.381 1.00 53.45  ? 66  LYS   A O   1 
ATOM   319  C  CB  . LYS   A 1 60  ? -24.813 9.682   -26.490 1.00 54.01  ? 66  LYS   A CB  1 
ATOM   320  C  CG  . LYS   A 1 60  ? -25.713 9.425   -27.711 1.00 71.57  ? 66  LYS   A CG  1 
ATOM   321  C  CD  . LYS   A 1 60  ? -24.942 8.937   -28.923 1.00 84.10  ? 66  LYS   A CD  1 
ATOM   322  C  CE  . LYS   A 1 60  ? -25.816 8.827   -30.150 1.00 93.78  ? 66  LYS   A CE  1 
ATOM   323  N  NZ  . LYS   A 1 60  ? -25.023 8.476   -31.358 1.00 101.19 ? 66  LYS   A NZ  1 
ATOM   324  N  N   . ASP   A 1 61  ? -27.886 9.782   -24.674 1.00 48.41  ? 67  ASP   A N   1 
ATOM   325  C  CA  . ASP   A 1 61  ? -28.970 8.949   -24.182 1.00 48.20  ? 67  ASP   A CA  1 
ATOM   326  C  C   . ASP   A 1 61  ? -29.664 8.240   -25.352 1.00 51.18  ? 67  ASP   A C   1 
ATOM   327  O  O   . ASP   A 1 61  ? -30.325 8.892   -26.158 1.00 52.65  ? 67  ASP   A O   1 
ATOM   328  C  CB  . ASP   A 1 61  ? -29.959 9.789   -23.353 1.00 50.44  ? 67  ASP   A CB  1 
ATOM   329  C  CG  . ASP   A 1 61  ? -30.998 9.003   -22.564 1.00 60.95  ? 67  ASP   A CG  1 
ATOM   330  O  OD1 . ASP   A 1 61  ? -30.968 7.752   -22.614 1.00 61.35  ? 67  ASP   A OD1 1 
ATOM   331  O  OD2 . ASP   A 1 61  ? -31.837 9.641   -21.890 1.00 66.03  ? 67  ASP   A OD2 1 
ATOM   332  N  N   . PHE   A 1 62  ? -29.520 6.901   -25.436 1.00 45.18  ? 68  PHE   A N   1 
ATOM   333  C  CA  . PHE   A 1 62  ? -30.123 6.077   -26.494 1.00 43.55  ? 68  PHE   A CA  1 
ATOM   334  C  C   . PHE   A 1 62  ? -31.585 5.759   -26.176 1.00 47.77  ? 68  PHE   A C   1 
ATOM   335  O  O   . PHE   A 1 62  ? -32.240 5.051   -26.944 1.00 48.04  ? 68  PHE   A O   1 
ATOM   336  C  CB  . PHE   A 1 62  ? -29.321 4.771   -26.693 1.00 44.61  ? 68  PHE   A CB  1 
ATOM   337  C  CG  . PHE   A 1 62  ? -28.029 4.891   -27.470 1.00 45.03  ? 68  PHE   A CG  1 
ATOM   338  C  CD1 . PHE   A 1 62  ? -26.893 5.434   -26.885 1.00 46.77  ? 68  PHE   A CD1 1 
ATOM   339  C  CD2 . PHE   A 1 62  ? -27.941 4.431   -28.782 1.00 47.18  ? 68  PHE   A CD2 1 
ATOM   340  C  CE1 . PHE   A 1 62  ? -25.698 5.541   -27.605 1.00 47.92  ? 68  PHE   A CE1 1 
ATOM   341  C  CE2 . PHE   A 1 62  ? -26.743 4.533   -29.499 1.00 49.57  ? 68  PHE   A CE2 1 
ATOM   342  C  CZ  . PHE   A 1 62  ? -25.628 5.081   -28.904 1.00 47.50  ? 68  PHE   A CZ  1 
ATOM   343  N  N   . GLY   A 1 63  ? -32.072 6.274   -25.046 1.00 44.59  ? 69  GLY   A N   1 
ATOM   344  C  CA  . GLY   A 1 63  ? -33.422 6.034   -24.548 1.00 45.13  ? 69  GLY   A CA  1 
ATOM   345  C  C   . GLY   A 1 63  ? -33.632 4.623   -24.026 1.00 51.10  ? 69  GLY   A C   1 
ATOM   346  O  O   . GLY   A 1 63  ? -32.669 3.874   -23.820 1.00 49.52  ? 69  GLY   A O   1 
ATOM   347  N  N   . ASP   A 1 64  ? -34.906 4.255   -23.802 1.00 50.42  ? 70  ASP   A N   1 
ATOM   348  C  CA  . ASP   A 1 64  ? -35.308 2.925   -23.326 1.00 51.27  ? 70  ASP   A CA  1 
ATOM   349  C  C   . ASP   A 1 64  ? -35.839 2.088   -24.498 1.00 55.75  ? 70  ASP   A C   1 
ATOM   350  O  O   . ASP   A 1 64  ? -36.918 2.388   -25.020 1.00 56.28  ? 70  ASP   A O   1 
ATOM   351  C  CB  . ASP   A 1 64  ? -36.352 3.026   -22.195 1.00 53.18  ? 70  ASP   A CB  1 
ATOM   352  C  CG  . ASP   A 1 64  ? -35.960 3.961   -21.069 1.00 63.83  ? 70  ASP   A CG  1 
ATOM   353  O  OD1 . ASP   A 1 64  ? -34.892 3.738   -20.455 1.00 63.51  ? 70  ASP   A OD1 1 
ATOM   354  O  OD2 . ASP   A 1 64  ? -36.722 4.916   -20.798 1.00 71.65  ? 70  ASP   A OD2 1 
ATOM   355  N  N   . LEU   A 1 65  ? -35.063 1.059   -24.920 1.00 50.56  ? 71  LEU   A N   1 
ATOM   356  C  CA  . LEU   A 1 65  ? -35.381 0.156   -26.026 1.00 49.58  ? 71  LEU   A CA  1 
ATOM   357  C  C   . LEU   A 1 65  ? -36.682 -0.577  -25.814 1.00 55.57  ? 71  LEU   A C   1 
ATOM   358  O  O   . LEU   A 1 65  ? -37.017 -0.952  -24.687 1.00 55.06  ? 71  LEU   A O   1 
ATOM   359  C  CB  . LEU   A 1 65  ? -34.267 -0.886  -26.258 1.00 49.43  ? 71  LEU   A CB  1 
ATOM   360  C  CG  . LEU   A 1 65  ? -32.815 -0.402  -26.370 1.00 53.82  ? 71  LEU   A CG  1 
ATOM   361  C  CD1 . LEU   A 1 65  ? -31.864 -1.592  -26.443 1.00 53.45  ? 71  LEU   A CD1 1 
ATOM   362  C  CD2 . LEU   A 1 65  ? -32.611 0.538   -27.577 1.00 56.68  ? 71  LEU   A CD2 1 
ATOM   363  N  N   . SER   A 1 66  ? -37.429 -0.762  -26.899 1.00 54.62  ? 72  SER   A N   1 
ATOM   364  C  CA  . SER   A 1 66  ? -38.683 -1.499  -26.868 1.00 55.69  ? 72  SER   A CA  1 
ATOM   365  C  C   . SER   A 1 66  ? -38.346 -2.808  -27.534 1.00 60.46  ? 72  SER   A C   1 
ATOM   366  O  O   . SER   A 1 66  ? -37.939 -2.826  -28.703 1.00 60.73  ? 72  SER   A O   1 
ATOM   367  C  CB  . SER   A 1 66  ? -39.790 -0.756  -27.616 1.00 59.86  ? 72  SER   A CB  1 
ATOM   368  O  OG  . SER   A 1 66  ? -41.010 -1.481  -27.562 1.00 68.14  ? 72  SER   A OG  1 
ATOM   369  N  N   . PHE   A 1 67  ? -38.393 -3.891  -26.759 1.00 57.31  ? 73  PHE   A N   1 
ATOM   370  C  CA  . PHE   A 1 67  ? -38.023 -5.192  -27.283 1.00 57.28  ? 73  PHE   A CA  1 
ATOM   371  C  C   . PHE   A 1 67  ? -39.167 -5.841  -28.019 1.00 64.47  ? 73  PHE   A C   1 
ATOM   372  O  O   . PHE   A 1 67  ? -40.291 -5.877  -27.504 1.00 64.12  ? 73  PHE   A O   1 
ATOM   373  C  CB  . PHE   A 1 67  ? -37.422 -6.114  -26.195 1.00 58.10  ? 73  PHE   A CB  1 
ATOM   374  C  CG  . PHE   A 1 67  ? -36.150 -5.576  -25.582 1.00 58.40  ? 73  PHE   A CG  1 
ATOM   375  C  CD1 . PHE   A 1 67  ? -34.960 -5.572  -26.300 1.00 60.38  ? 73  PHE   A CD1 1 
ATOM   376  C  CD2 . PHE   A 1 67  ? -36.149 -5.041  -24.300 1.00 60.22  ? 73  PHE   A CD2 1 
ATOM   377  C  CE1 . PHE   A 1 67  ? -33.791 -5.049  -25.745 1.00 61.25  ? 73  PHE   A CE1 1 
ATOM   378  C  CE2 . PHE   A 1 67  ? -34.978 -4.522  -23.742 1.00 62.71  ? 73  PHE   A CE2 1 
ATOM   379  C  CZ  . PHE   A 1 67  ? -33.808 -4.523  -24.471 1.00 60.63  ? 73  PHE   A CZ  1 
ATOM   380  N  N   . THR   A 1 68  ? -38.870 -6.324  -29.251 1.00 63.30  ? 74  THR   A N   1 
ATOM   381  C  CA  . THR   A 1 68  ? -39.788 -7.038  -30.141 1.00 64.18  ? 74  THR   A CA  1 
ATOM   382  C  C   . THR   A 1 68  ? -40.237 -8.293  -29.373 1.00 70.23  ? 74  THR   A C   1 
ATOM   383  O  O   . THR   A 1 68  ? -39.391 -9.143  -29.072 1.00 69.97  ? 74  THR   A O   1 
ATOM   384  C  CB  . THR   A 1 68  ? -39.081 -7.383  -31.481 1.00 70.46  ? 74  THR   A CB  1 
ATOM   385  O  OG1 . THR   A 1 68  ? -38.504 -6.205  -32.040 1.00 65.89  ? 74  THR   A OG1 1 
ATOM   386  C  CG2 . THR   A 1 68  ? -40.013 -8.038  -32.506 1.00 70.82  ? 74  THR   A CG2 1 
ATOM   387  N  N   . PRO   A 1 69  ? -41.519 -8.384  -28.946 1.00 68.12  ? 75  PRO   A N   1 
ATOM   388  C  CA  . PRO   A 1 69  ? -41.936 -9.566  -28.183 1.00 68.39  ? 75  PRO   A CA  1 
ATOM   389  C  C   . PRO   A 1 69  ? -42.111 -10.791 -29.067 1.00 73.26  ? 75  PRO   A C   1 
ATOM   390  O  O   . PRO   A 1 69  ? -42.230 -10.667 -30.289 1.00 72.58  ? 75  PRO   A O   1 
ATOM   391  C  CB  . PRO   A 1 69  ? -43.259 -9.134  -27.523 1.00 70.03  ? 75  PRO   A CB  1 
ATOM   392  C  CG  . PRO   A 1 69  ? -43.527 -7.719  -27.989 1.00 74.36  ? 75  PRO   A CG  1 
ATOM   393  C  CD  . PRO   A 1 69  ? -42.658 -7.472  -29.177 1.00 69.87  ? 75  PRO   A CD  1 
ATOM   394  N  N   . VAL   A 1 70  ? -42.077 -11.978 -28.443 1.00 70.93  ? 76  VAL   A N   1 
ATOM   395  C  CA  . VAL   A 1 70  ? -42.295 -13.256 -29.118 1.00 71.17  ? 76  VAL   A CA  1 
ATOM   396  C  C   . VAL   A 1 70  ? -43.620 -13.788 -28.537 1.00 76.70  ? 76  VAL   A C   1 
ATOM   397  O  O   . VAL   A 1 70  ? -43.678 -14.054 -27.330 1.00 77.04  ? 76  VAL   A O   1 
ATOM   398  C  CB  . VAL   A 1 70  ? -41.110 -14.255 -28.980 1.00 74.93  ? 76  VAL   A CB  1 
ATOM   399  C  CG1 . VAL   A 1 70  ? -41.346 -15.500 -29.834 1.00 74.84  ? 76  VAL   A CG1 1 
ATOM   400  C  CG2 . VAL   A 1 70  ? -39.783 -13.598 -29.360 1.00 74.62  ? 76  VAL   A CG2 1 
ATOM   401  N  N   . PRO   A 1 71  ? -44.716 -13.838 -29.344 1.00 73.58  ? 77  PRO   A N   1 
ATOM   402  C  CA  . PRO   A 1 71  ? -46.016 -14.281 -28.798 1.00 73.18  ? 77  PRO   A CA  1 
ATOM   403  C  C   . PRO   A 1 71  ? -46.030 -15.752 -28.395 1.00 75.39  ? 77  PRO   A C   1 
ATOM   404  O  O   . PRO   A 1 71  ? -46.410 -16.066 -27.264 1.00 75.18  ? 77  PRO   A O   1 
ATOM   405  C  CB  . PRO   A 1 71  ? -47.018 -13.967 -29.925 1.00 75.17  ? 77  PRO   A CB  1 
ATOM   406  C  CG  . PRO   A 1 71  ? -46.264 -13.129 -30.922 1.00 80.02  ? 77  PRO   A CG  1 
ATOM   407  C  CD  . PRO   A 1 71  ? -44.826 -13.522 -30.781 1.00 75.49  ? 77  PRO   A CD  1 
ATOM   408  N  N   . LYS   A 1 72  ? -45.601 -16.647 -29.306 1.00 70.39  ? 78  LYS   A N   1 
ATOM   409  C  CA  . LYS   A 1 72  ? -45.524 -18.075 -29.024 1.00 69.38  ? 78  LYS   A CA  1 
ATOM   410  C  C   . LYS   A 1 72  ? -44.088 -18.370 -28.568 1.00 69.63  ? 78  LYS   A C   1 
ATOM   411  O  O   . LYS   A 1 72  ? -43.178 -18.494 -29.397 1.00 68.94  ? 78  LYS   A O   1 
ATOM   412  C  CB  . LYS   A 1 72  ? -45.949 -18.924 -30.242 1.00 72.54  ? 78  LYS   A CB  1 
ATOM   413  C  CG  . LYS   A 1 72  ? -46.149 -20.405 -29.910 1.00 89.89  ? 78  LYS   A CG  1 
ATOM   414  C  CD  . LYS   A 1 72  ? -46.348 -21.267 -31.156 1.00 99.90  ? 78  LYS   A CD  1 
ATOM   415  C  CE  . LYS   A 1 72  ? -46.365 -22.748 -30.845 1.00 108.03 ? 78  LYS   A CE  1 
ATOM   416  N  NZ  . LYS   A 1 72  ? -47.604 -23.167 -30.133 1.00 115.00 ? 78  LYS   A NZ  1 
ATOM   417  N  N   . ASP   A 1 73  ? -43.888 -18.398 -27.233 1.00 63.40  ? 79  ASP   A N   1 
ATOM   418  C  CA  . ASP   A 1 73  ? -42.589 -18.641 -26.598 1.00 61.65  ? 79  ASP   A CA  1 
ATOM   419  C  C   . ASP   A 1 73  ? -42.775 -19.173 -25.176 1.00 64.92  ? 79  ASP   A C   1 
ATOM   420  O  O   . ASP   A 1 73  ? -42.670 -18.423 -24.195 1.00 65.77  ? 79  ASP   A O   1 
ATOM   421  C  CB  . ASP   A 1 73  ? -41.721 -17.364 -26.615 1.00 62.38  ? 79  ASP   A CB  1 
ATOM   422  C  CG  . ASP   A 1 73  ? -40.369 -17.475 -25.938 1.00 60.27  ? 79  ASP   A CG  1 
ATOM   423  O  OD1 . ASP   A 1 73  ? -39.723 -18.550 -26.057 1.00 58.40  ? 79  ASP   A OD1 1 
ATOM   424  O  OD2 . ASP   A 1 73  ? -39.931 -16.479 -25.343 1.00 59.90  ? 79  ASP   A OD2 1 
ATOM   425  N  N   . ASP   A 1 74  ? -43.081 -20.460 -25.062 1.00 59.35  ? 80  ASP   A N   1 
ATOM   426  C  CA  . ASP   A 1 74  ? -43.255 -21.013 -23.732 1.00 58.32  ? 80  ASP   A CA  1 
ATOM   427  C  C   . ASP   A 1 74  ? -42.278 -22.151 -23.457 1.00 55.87  ? 80  ASP   A C   1 
ATOM   428  O  O   . ASP   A 1 74  ? -41.396 -22.428 -24.283 1.00 55.08  ? 80  ASP   A O   1 
ATOM   429  C  CB  . ASP   A 1 74  ? -44.716 -21.384 -23.422 1.00 61.50  ? 80  ASP   A CB  1 
ATOM   430  C  CG  . ASP   A 1 74  ? -45.341 -20.501 -22.346 1.00 78.54  ? 80  ASP   A CG  1 
ATOM   431  O  OD1 . ASP   A 1 74  ? -44.735 -20.372 -21.250 1.00 79.17  ? 80  ASP   A OD1 1 
ATOM   432  O  OD2 . ASP   A 1 74  ? -46.426 -19.931 -22.602 1.00 87.09  ? 80  ASP   A OD2 1 
ATOM   433  N  N   . LEU   A 1 75  ? -42.404 -22.737 -22.245 1.00 47.48  ? 81  LEU   A N   1 
ATOM   434  C  CA  . LEU   A 1 75  ? -41.582 -23.784 -21.654 1.00 45.03  ? 81  LEU   A CA  1 
ATOM   435  C  C   . LEU   A 1 75  ? -40.960 -24.721 -22.679 1.00 42.83  ? 81  LEU   A C   1 
ATOM   436  O  O   . LEU   A 1 75  ? -41.665 -25.349 -23.477 1.00 40.80  ? 81  LEU   A O   1 
ATOM   437  C  CB  . LEU   A 1 75  ? -42.375 -24.545 -20.581 1.00 45.06  ? 81  LEU   A CB  1 
ATOM   438  C  CG  . LEU   A 1 75  ? -41.581 -25.071 -19.387 1.00 48.67  ? 81  LEU   A CG  1 
ATOM   439  C  CD1 . LEU   A 1 75  ? -40.970 -23.935 -18.576 1.00 48.28  ? 81  LEU   A CD1 1 
ATOM   440  C  CD2 . LEU   A 1 75  ? -42.473 -25.914 -18.489 1.00 51.00  ? 81  LEU   A CD2 1 
ATOM   441  N  N   . TYR   A 1 76  ? -39.619 -24.756 -22.679 1.00 35.09  ? 82  TYR   A N   1 
ATOM   442  C  CA  . TYR   A 1 76  ? -38.818 -25.530 -23.610 1.00 33.11  ? 82  TYR   A CA  1 
ATOM   443  C  C   . TYR   A 1 76  ? -38.144 -26.678 -22.870 1.00 35.97  ? 82  TYR   A C   1 
ATOM   444  O  O   . TYR   A 1 76  ? -37.444 -26.446 -21.876 1.00 33.79  ? 82  TYR   A O   1 
ATOM   445  C  CB  . TYR   A 1 76  ? -37.771 -24.608 -24.270 1.00 34.21  ? 82  TYR   A CB  1 
ATOM   446  C  CG  . TYR   A 1 76  ? -36.892 -25.292 -25.291 1.00 35.99  ? 82  TYR   A CG  1 
ATOM   447  C  CD1 . TYR   A 1 76  ? -37.376 -25.608 -26.560 1.00 38.01  ? 82  TYR   A CD1 1 
ATOM   448  C  CD2 . TYR   A 1 76  ? -35.563 -25.606 -25.000 1.00 37.04  ? 82  TYR   A CD2 1 
ATOM   449  C  CE1 . TYR   A 1 76  ? -36.565 -26.235 -27.508 1.00 38.63  ? 82  TYR   A CE1 1 
ATOM   450  C  CE2 . TYR   A 1 76  ? -34.736 -26.205 -25.952 1.00 38.20  ? 82  TYR   A CE2 1 
ATOM   451  C  CZ  . TYR   A 1 76  ? -35.245 -26.530 -27.199 1.00 42.97  ? 82  TYR   A CZ  1 
ATOM   452  O  OH  . TYR   A 1 76  ? -34.432 -27.128 -28.130 1.00 41.25  ? 82  TYR   A OH  1 
ATOM   453  N  N   . ASN   A 1 77  ? -38.383 -27.923 -23.336 1.00 31.88  ? 83  ASN   A N   1 
ATOM   454  C  CA  . ASN   A 1 77  ? -37.842 -29.143 -22.723 1.00 31.82  ? 83  ASN   A CA  1 
ATOM   455  C  C   . ASN   A 1 77  ? -38.240 -29.253 -21.243 1.00 33.33  ? 83  ASN   A C   1 
ATOM   456  O  O   . ASN   A 1 77  ? -37.490 -29.758 -20.409 1.00 29.65  ? 83  ASN   A O   1 
ATOM   457  C  CB  . ASN   A 1 77  ? -36.312 -29.251 -22.963 1.00 29.94  ? 83  ASN   A CB  1 
ATOM   458  C  CG  . ASN   A 1 77  ? -35.980 -29.758 -24.343 1.00 37.98  ? 83  ASN   A CG  1 
ATOM   459  O  OD1 . ASN   A 1 77  ? -36.731 -30.522 -24.950 1.00 29.73  ? 83  ASN   A OD1 1 
ATOM   460  N  ND2 . ASN   A 1 77  ? -34.821 -29.394 -24.856 1.00 30.14  ? 83  ASN   A ND2 1 
ATOM   461  N  N   . ASN   A 1 78  ? -39.452 -28.752 -20.930 1.00 31.84  ? 84  ASN   A N   1 
ATOM   462  C  CA  . ASN   A 1 78  ? -40.062 -28.745 -19.599 1.00 31.63  ? 84  ASN   A CA  1 
ATOM   463  C  C   . ASN   A 1 78  ? -39.162 -28.050 -18.568 1.00 33.67  ? 84  ASN   A C   1 
ATOM   464  O  O   . ASN   A 1 78  ? -39.158 -28.435 -17.405 1.00 33.55  ? 84  ASN   A O   1 
ATOM   465  C  CB  . ASN   A 1 78  ? -40.395 -30.197 -19.161 1.00 34.10  ? 84  ASN   A CB  1 
ATOM   466  C  CG  . ASN   A 1 78  ? -41.319 -30.281 -17.980 1.00 41.85  ? 84  ASN   A CG  1 
ATOM   467  O  OD1 . ASN   A 1 78  ? -42.202 -29.452 -17.811 1.00 40.95  ? 84  ASN   A OD1 1 
ATOM   468  N  ND2 . ASN   A 1 78  ? -41.121 -31.272 -17.123 1.00 38.49  ? 84  ASN   A ND2 1 
ATOM   469  N  N   . LEU   A 1 79  ? -38.404 -27.025 -18.988 1.00 29.97  ? 85  LEU   A N   1 
ATOM   470  C  CA  . LEU   A 1 79  ? -37.434 -26.404 -18.098 1.00 29.14  ? 85  LEU   A CA  1 
ATOM   471  C  C   . LEU   A 1 79  ? -37.090 -24.949 -18.429 1.00 30.98  ? 85  LEU   A C   1 
ATOM   472  O  O   . LEU   A 1 79  ? -37.272 -24.104 -17.560 1.00 31.88  ? 85  LEU   A O   1 
ATOM   473  C  CB  . LEU   A 1 79  ? -36.136 -27.294 -18.048 1.00 28.94  ? 85  LEU   A CB  1 
ATOM   474  C  CG  . LEU   A 1 79  ? -34.989 -26.831 -17.142 1.00 32.57  ? 85  LEU   A CG  1 
ATOM   475  C  CD1 . LEU   A 1 79  ? -35.420 -26.790 -15.673 1.00 33.42  ? 85  LEU   A CD1 1 
ATOM   476  C  CD2 . LEU   A 1 79  ? -33.748 -27.722 -17.321 1.00 33.94  ? 85  LEU   A CD2 1 
ATOM   477  N  N   . ILE   A 1 80  ? -36.610 -24.642 -19.642 1.00 28.17  ? 86  ILE   A N   1 
ATOM   478  C  CA  . ILE   A 1 80  ? -36.174 -23.286 -20.022 1.00 27.80  ? 86  ILE   A CA  1 
ATOM   479  C  C   . ILE   A 1 80  ? -37.374 -22.351 -20.264 1.00 33.12  ? 86  ILE   A C   1 
ATOM   480  O  O   . ILE   A 1 80  ? -38.197 -22.618 -21.130 1.00 32.96  ? 86  ILE   A O   1 
ATOM   481  C  CB  . ILE   A 1 80  ? -35.162 -23.270 -21.201 1.00 30.79  ? 86  ILE   A CB  1 
ATOM   482  C  CG1 . ILE   A 1 80  ? -33.916 -24.217 -20.955 1.00 31.05  ? 86  ILE   A CG1 1 
ATOM   483  C  CG2 . ILE   A 1 80  ? -34.701 -21.830 -21.557 1.00 30.40  ? 86  ILE   A CG2 1 
ATOM   484  C  CD1 . ILE   A 1 80  ? -33.179 -23.993 -19.639 1.00 28.63  ? 86  ILE   A CD1 1 
ATOM   485  N  N   . VAL   A 1 81  ? -37.420 -21.252 -19.514 1.00 31.55  ? 87  VAL   A N   1 
ATOM   486  C  CA  . VAL   A 1 81  ? -38.479 -20.233 -19.566 1.00 32.56  ? 87  VAL   A CA  1 
ATOM   487  C  C   . VAL   A 1 81  ? -38.147 -19.140 -20.576 1.00 35.57  ? 87  VAL   A C   1 
ATOM   488  O  O   . VAL   A 1 81  ? -37.025 -18.615 -20.606 1.00 32.24  ? 87  VAL   A O   1 
ATOM   489  C  CB  . VAL   A 1 81  ? -38.800 -19.673 -18.151 1.00 36.50  ? 87  VAL   A CB  1 
ATOM   490  C  CG1 . VAL   A 1 81  ? -40.058 -18.802 -18.170 1.00 37.01  ? 87  VAL   A CG1 1 
ATOM   491  C  CG2 . VAL   A 1 81  ? -38.969 -20.809 -17.146 1.00 36.38  ? 87  VAL   A CG2 1 
ATOM   492  N  N   . ASN   A 1 82  ? -39.141 -18.811 -21.423 1.00 33.26  ? 88  ASN   A N   1 
ATOM   493  C  CA  . ASN   A 1 82  ? -39.090 -17.778 -22.472 1.00 33.54  ? 88  ASN   A CA  1 
ATOM   494  C  C   . ASN   A 1 82  ? -37.778 -17.738 -23.306 1.00 37.98  ? 88  ASN   A C   1 
ATOM   495  O  O   . ASN   A 1 82  ? -37.218 -16.647 -23.442 1.00 38.43  ? 88  ASN   A O   1 
ATOM   496  C  CB  . ASN   A 1 82  ? -39.377 -16.405 -21.834 1.00 35.81  ? 88  ASN   A CB  1 
ATOM   497  C  CG  . ASN   A 1 82  ? -40.682 -16.349 -21.077 1.00 52.67  ? 88  ASN   A CG  1 
ATOM   498  O  OD1 . ASN   A 1 82  ? -41.667 -16.997 -21.434 1.00 55.51  ? 88  ASN   A OD1 1 
ATOM   499  N  ND2 . ASN   A 1 82  ? -40.713 -15.587 -19.997 1.00 45.49  ? 88  ASN   A ND2 1 
ATOM   500  N  N   . PRO   A 1 83  ? -37.237 -18.860 -23.864 1.00 34.16  ? 89  PRO   A N   1 
ATOM   501  C  CA  . PRO   A 1 83  ? -35.946 -18.757 -24.577 1.00 34.13  ? 89  PRO   A CA  1 
ATOM   502  C  C   . PRO   A 1 83  ? -35.932 -17.844 -25.802 1.00 38.27  ? 89  PRO   A C   1 
ATOM   503  O  O   . PRO   A 1 83  ? -34.966 -17.109 -25.997 1.00 36.19  ? 89  PRO   A O   1 
ATOM   504  C  CB  . PRO   A 1 83  ? -35.602 -20.207 -24.937 1.00 34.99  ? 89  PRO   A CB  1 
ATOM   505  C  CG  . PRO   A 1 83  ? -36.922 -20.926 -24.920 1.00 39.37  ? 89  PRO   A CG  1 
ATOM   506  C  CD  . PRO   A 1 83  ? -37.729 -20.256 -23.854 1.00 35.13  ? 89  PRO   A CD  1 
ATOM   507  N  N   . ARG   A 1 84  ? -37.001 -17.879 -26.618 1.00 36.18  ? 90  ARG   A N   1 
ATOM   508  C  CA  . ARG   A 1 84  ? -37.091 -17.054 -27.835 1.00 35.29  ? 90  ARG   A CA  1 
ATOM   509  C  C   . ARG   A 1 84  ? -37.063 -15.557 -27.548 1.00 36.60  ? 90  ARG   A C   1 
ATOM   510  O  O   . ARG   A 1 84  ? -36.350 -14.847 -28.247 1.00 36.98  ? 90  ARG   A O   1 
ATOM   511  C  CB  . ARG   A 1 84  ? -38.313 -17.445 -28.683 1.00 38.08  ? 90  ARG   A CB  1 
ATOM   512  C  CG  . ARG   A 1 84  ? -38.136 -18.760 -29.418 1.00 51.97  ? 90  ARG   A CG  1 
ATOM   513  C  CD  . ARG   A 1 84  ? -39.469 -19.344 -29.842 1.00 68.25  ? 90  ARG   A CD  1 
ATOM   514  N  NE  . ARG   A 1 84  ? -39.291 -20.506 -30.714 1.00 78.91  ? 90  ARG   A NE  1 
ATOM   515  C  CZ  . ARG   A 1 84  ? -39.348 -21.771 -30.308 1.00 93.87  ? 90  ARG   A CZ  1 
ATOM   516  N  NH1 . ARG   A 1 84  ? -39.588 -22.059 -29.030 1.00 76.59  ? 90  ARG   A NH1 1 
ATOM   517  N  NH2 . ARG   A 1 84  ? -39.163 -22.761 -31.175 1.00 77.38  ? 90  ARG   A NH2 1 
ATOM   518  N  N   . SER   A 1 85  ? -37.799 -15.082 -26.511 1.00 34.46  ? 91  SER   A N   1 
ATOM   519  C  CA  . SER   A 1 85  ? -37.855 -13.675 -26.100 1.00 34.88  ? 91  SER   A CA  1 
ATOM   520  C  C   . SER   A 1 85  ? -36.503 -13.228 -25.560 1.00 38.11  ? 91  SER   A C   1 
ATOM   521  O  O   . SER   A 1 85  ? -36.049 -12.145 -25.909 1.00 35.63  ? 91  SER   A O   1 
ATOM   522  C  CB  . SER   A 1 85  ? -38.921 -13.440 -25.034 1.00 39.90  ? 91  SER   A CB  1 
ATOM   523  O  OG  . SER   A 1 85  ? -40.227 -13.796 -25.455 1.00 52.87  ? 91  SER   A OG  1 
ATOM   524  N  N   . VAL   A 1 86  ? -35.854 -14.075 -24.718 1.00 34.24  ? 92  VAL   A N   1 
ATOM   525  C  CA  . VAL   A 1 86  ? -34.545 -13.758 -24.137 1.00 33.55  ? 92  VAL   A CA  1 
ATOM   526  C  C   . VAL   A 1 86  ? -33.488 -13.653 -25.228 1.00 35.28  ? 92  VAL   A C   1 
ATOM   527  O  O   . VAL   A 1 86  ? -32.750 -12.679 -25.258 1.00 35.13  ? 92  VAL   A O   1 
ATOM   528  C  CB  . VAL   A 1 86  ? -34.160 -14.729 -22.977 1.00 36.44  ? 92  VAL   A CB  1 
ATOM   529  C  CG1 . VAL   A 1 86  ? -32.744 -14.465 -22.461 1.00 36.79  ? 92  VAL   A CG1 1 
ATOM   530  C  CG2 . VAL   A 1 86  ? -35.173 -14.647 -21.837 1.00 35.34  ? 92  VAL   A CG2 1 
ATOM   531  N  N   . GLY   A 1 87  ? -33.460 -14.629 -26.134 1.00 33.25  ? 93  GLY   A N   1 
ATOM   532  C  CA  . GLY   A 1 87  ? -32.524 -14.642 -27.240 1.00 32.40  ? 93  GLY   A CA  1 
ATOM   533  C  C   . GLY   A 1 87  ? -32.684 -13.439 -28.153 1.00 36.26  ? 93  GLY   A C   1 
ATOM   534  O  O   . GLY   A 1 87  ? -31.691 -12.803 -28.511 1.00 34.26  ? 93  GLY   A O   1 
ATOM   535  N  N   . LEU   A 1 88  ? -33.945 -13.108 -28.518 1.00 35.81  ? 94  LEU   A N   1 
ATOM   536  C  CA  . LEU   A 1 88  ? -34.261 -11.986 -29.411 1.00 37.54  ? 94  LEU   A CA  1 
ATOM   537  C  C   . LEU   A 1 88  ? -33.944 -10.616 -28.811 1.00 39.65  ? 94  LEU   A C   1 
ATOM   538  O  O   . LEU   A 1 88  ? -33.298 -9.809  -29.475 1.00 40.08  ? 94  LEU   A O   1 
ATOM   539  C  CB  . LEU   A 1 88  ? -35.719 -12.054 -29.896 1.00 38.51  ? 94  LEU   A CB  1 
ATOM   540  C  CG  . LEU   A 1 88  ? -36.081 -11.184 -31.121 1.00 44.70  ? 94  LEU   A CG  1 
ATOM   541  C  CD1 . LEU   A 1 88  ? -35.425 -11.697 -32.406 1.00 46.01  ? 94  LEU   A CD1 1 
ATOM   542  C  CD2 . LEU   A 1 88  ? -37.595 -11.076 -31.284 1.00 46.68  ? 94  LEU   A CD2 1 
ATOM   543  N  N   . ALA   A 1 89  ? -34.390 -10.363 -27.559 1.00 36.38  ? 95  ALA   A N   1 
ATOM   544  C  CA  . ALA   A 1 89  ? -34.144 -9.131  -26.816 1.00 35.55  ? 95  ALA   A CA  1 
ATOM   545  C  C   . ALA   A 1 89  ? -32.662 -8.854  -26.701 1.00 37.85  ? 95  ALA   A C   1 
ATOM   546  O  O   . ALA   A 1 89  ? -32.240 -7.714  -26.902 1.00 35.54  ? 95  ALA   A O   1 
ATOM   547  C  CB  . ALA   A 1 89  ? -34.756 -9.225  -25.436 1.00 36.48  ? 95  ALA   A CB  1 
ATOM   548  N  N   . ASN   A 1 90  ? -31.857 -9.909  -26.433 1.00 34.60  ? 96  ASN   A N   1 
ATOM   549  C  CA  . ASN   A 1 90  ? -30.408 -9.784  -26.325 1.00 33.62  ? 96  ASN   A CA  1 
ATOM   550  C  C   . ASN   A 1 90  ? -29.742 -9.528  -27.657 1.00 37.52  ? 96  ASN   A C   1 
ATOM   551  O  O   . ASN   A 1 90  ? -28.754 -8.801  -27.691 1.00 35.35  ? 96  ASN   A O   1 
ATOM   552  C  CB  . ASN   A 1 90  ? -29.801 -10.976 -25.604 1.00 32.79  ? 96  ASN   A CB  1 
ATOM   553  C  CG  . ASN   A 1 90  ? -29.878 -10.806 -24.118 1.00 37.15  ? 96  ASN   A CG  1 
ATOM   554  O  OD1 . ASN   A 1 90  ? -29.186 -9.982  -23.539 1.00 34.87  ? 96  ASN   A OD1 1 
ATOM   555  N  ND2 . ASN   A 1 90  ? -30.781 -11.506 -23.482 1.00 36.38  ? 96  ASN   A ND2 1 
ATOM   556  N  N   . GLN   A 1 91  ? -30.280 -10.102 -28.762 1.00 36.40  ? 97  GLN   A N   1 
ATOM   557  C  CA  . GLN   A 1 91  ? -29.729 -9.848  -30.097 1.00 36.76  ? 97  GLN   A CA  1 
ATOM   558  C  C   . GLN   A 1 91  ? -29.862 -8.366  -30.435 1.00 39.97  ? 97  GLN   A C   1 
ATOM   559  O  O   . GLN   A 1 91  ? -28.889 -7.752  -30.873 1.00 40.30  ? 97  GLN   A O   1 
ATOM   560  C  CB  . GLN   A 1 91  ? -30.411 -10.712 -31.166 1.00 37.41  ? 97  GLN   A CB  1 
ATOM   561  C  CG  . GLN   A 1 91  ? -29.585 -10.782 -32.462 1.00 40.36  ? 97  GLN   A CG  1 
ATOM   562  C  CD  . GLN   A 1 91  ? -30.232 -11.592 -33.560 1.00 47.93  ? 97  GLN   A CD  1 
ATOM   563  O  OE1 . GLN   A 1 91  ? -31.393 -11.994 -33.482 1.00 43.47  ? 97  GLN   A OE1 1 
ATOM   564  N  NE2 . GLN   A 1 91  ? -29.474 -11.869 -34.602 1.00 46.03  ? 97  GLN   A NE2 1 
ATOM   565  N  N   . GLU   A 1 92  ? -31.058 -7.793  -30.180 1.00 37.41  ? 98  GLU   A N   1 
ATOM   566  C  CA  . GLU   A 1 92  ? -31.381 -6.374  -30.384 1.00 36.97  ? 98  GLU   A CA  1 
ATOM   567  C  C   . GLU   A 1 92  ? -30.482 -5.486  -29.541 1.00 39.91  ? 98  GLU   A C   1 
ATOM   568  O  O   . GLU   A 1 92  ? -29.866 -4.560  -30.070 1.00 38.69  ? 98  GLU   A O   1 
ATOM   569  C  CB  . GLU   A 1 92  ? -32.855 -6.114  -30.047 1.00 38.54  ? 98  GLU   A CB  1 
ATOM   570  C  CG  . GLU   A 1 92  ? -33.793 -6.726  -31.076 1.00 51.27  ? 98  GLU   A CG  1 
ATOM   571  C  CD  . GLU   A 1 92  ? -35.237 -6.956  -30.678 1.00 75.78  ? 98  GLU   A CD  1 
ATOM   572  O  OE1 . GLU   A 1 92  ? -35.763 -6.225  -29.808 1.00 62.50  ? 98  GLU   A OE1 1 
ATOM   573  O  OE2 . GLU   A 1 92  ? -35.855 -7.868  -31.270 1.00 78.35  ? 98  GLU   A OE2 1 
ATOM   574  N  N   . LEU   A 1 93  ? -30.362 -5.817  -28.227 1.00 37.11  ? 99  LEU   A N   1 
ATOM   575  C  CA  . LEU   A 1 93  ? -29.516 -5.114  -27.272 1.00 35.69  ? 99  LEU   A CA  1 
ATOM   576  C  C   . LEU   A 1 93  ? -28.063 -5.115  -27.720 1.00 37.25  ? 99  LEU   A C   1 
ATOM   577  O  O   . LEU   A 1 93  ? -27.432 -4.067  -27.653 1.00 36.47  ? 99  LEU   A O   1 
ATOM   578  C  CB  . LEU   A 1 93  ? -29.666 -5.696  -25.842 1.00 35.68  ? 99  LEU   A CB  1 
ATOM   579  C  CG  . LEU   A 1 93  ? -28.844 -5.001  -24.715 1.00 40.34  ? 99  LEU   A CG  1 
ATOM   580  C  CD1 . LEU   A 1 93  ? -29.197 -3.505  -24.579 1.00 40.44  ? 99  LEU   A CD1 1 
ATOM   581  C  CD2 . LEU   A 1 93  ? -29.044 -5.696  -23.382 1.00 41.26  ? 99  LEU   A CD2 1 
ATOM   582  N  N   . ALA   A 1 94  ? -27.539 -6.260  -28.217 1.00 34.81  ? 100 ALA   A N   1 
ATOM   583  C  CA  . ALA   A 1 94  ? -26.149 -6.344  -28.703 1.00 34.79  ? 100 ALA   A CA  1 
ATOM   584  C  C   . ALA   A 1 94  ? -25.849 -5.315  -29.826 1.00 38.28  ? 100 ALA   A C   1 
ATOM   585  O  O   . ALA   A 1 94  ? -24.757 -4.738  -29.850 1.00 35.66  ? 100 ALA   A O   1 
ATOM   586  C  CB  . ALA   A 1 94  ? -25.842 -7.749  -29.189 1.00 35.99  ? 100 ALA   A CB  1 
ATOM   587  N  N   . GLU   A 1 95  ? -26.812 -5.084  -30.739 1.00 36.93  ? 101 GLU   A N   1 
ATOM   588  C  CA  . GLU   A 1 95  ? -26.622 -4.113  -31.829 1.00 37.95  ? 101 GLU   A CA  1 
ATOM   589  C  C   . GLU   A 1 95  ? -26.447 -2.679  -31.324 1.00 41.81  ? 101 GLU   A C   1 
ATOM   590  O  O   . GLU   A 1 95  ? -25.572 -1.972  -31.819 1.00 42.07  ? 101 GLU   A O   1 
ATOM   591  C  CB  . GLU   A 1 95  ? -27.748 -4.200  -32.871 1.00 39.70  ? 101 GLU   A CB  1 
ATOM   592  C  CG  . GLU   A 1 95  ? -27.701 -5.451  -33.740 1.00 51.53  ? 101 GLU   A CG  1 
ATOM   593  C  CD  . GLU   A 1 95  ? -26.486 -5.621  -34.638 1.00 77.15  ? 101 GLU   A CD  1 
ATOM   594  O  OE1 . GLU   A 1 95  ? -26.078 -6.784  -34.852 1.00 71.18  ? 101 GLU   A OE1 1 
ATOM   595  O  OE2 . GLU   A 1 95  ? -25.943 -4.602  -35.129 1.00 73.41  ? 101 GLU   A OE2 1 
ATOM   596  N  N   . VAL   A 1 96  ? -27.256 -2.269  -30.323 1.00 39.42  ? 102 VAL   A N   1 
ATOM   597  C  CA  . VAL   A 1 96  ? -27.226 -0.933  -29.705 1.00 39.24  ? 102 VAL   A CA  1 
ATOM   598  C  C   . VAL   A 1 96  ? -25.914 -0.722  -28.938 1.00 41.57  ? 102 VAL   A C   1 
ATOM   599  O  O   . VAL   A 1 96  ? -25.287 0.329   -29.057 1.00 40.37  ? 102 VAL   A O   1 
ATOM   600  C  CB  . VAL   A 1 96  ? -28.481 -0.659  -28.839 1.00 43.69  ? 102 VAL   A CB  1 
ATOM   601  C  CG1 . VAL   A 1 96  ? -28.534 0.799   -28.380 1.00 43.92  ? 102 VAL   A CG1 1 
ATOM   602  C  CG2 . VAL   A 1 96  ? -29.767 -1.014  -29.589 1.00 43.69  ? 102 VAL   A CG2 1 
ATOM   603  N  N   . VAL   A 1 97  ? -25.471 -1.751  -28.187 1.00 37.65  ? 103 VAL   A N   1 
ATOM   604  C  CA  . VAL   A 1 97  ? -24.223 -1.671  -27.426 1.00 36.26  ? 103 VAL   A CA  1 
ATOM   605  C  C   . VAL   A 1 97  ? -23.046 -1.543  -28.390 1.00 39.35  ? 103 VAL   A C   1 
ATOM   606  O  O   . VAL   A 1 97  ? -22.151 -0.727  -28.153 1.00 38.48  ? 103 VAL   A O   1 
ATOM   607  C  CB  . VAL   A 1 97  ? -24.094 -2.861  -26.417 1.00 37.68  ? 103 VAL   A CB  1 
ATOM   608  C  CG1 . VAL   A 1 97  ? -22.677 -2.974  -25.841 1.00 37.24  ? 103 VAL   A CG1 1 
ATOM   609  C  CG2 . VAL   A 1 97  ? -25.110 -2.712  -25.294 1.00 36.65  ? 103 VAL   A CG2 1 
ATOM   610  N  N   . SER   A 1 98  ? -23.065 -2.337  -29.487 1.00 36.27  ? 104 SER   A N   1 
ATOM   611  C  CA  . SER   A 1 98  ? -22.047 -2.335  -30.537 1.00 36.76  ? 104 SER   A CA  1 
ATOM   612  C  C   . SER   A 1 98  ? -21.888 -0.899  -31.119 1.00 41.41  ? 104 SER   A C   1 
ATOM   613  O  O   . SER   A 1 98  ? -20.773 -0.388  -31.210 1.00 39.16  ? 104 SER   A O   1 
ATOM   614  C  CB  . SER   A 1 98  ? -22.453 -3.316  -31.638 1.00 40.23  ? 104 SER   A CB  1 
ATOM   615  O  OG  . SER   A 1 98  ? -21.557 -3.322  -32.732 1.00 47.42  ? 104 SER   A OG  1 
ATOM   616  N  N   . ARG   A 1 99  ? -23.017 -0.261  -31.460 1.00 40.57  ? 105 ARG   A N   1 
ATOM   617  C  CA  . ARG   A 1 99  ? -23.106 1.108   -31.984 1.00 42.26  ? 105 ARG   A CA  1 
ATOM   618  C  C   . ARG   A 1 99  ? -22.482 2.110   -31.000 1.00 47.50  ? 105 ARG   A C   1 
ATOM   619  O  O   . ARG   A 1 99  ? -21.591 2.870   -31.401 1.00 48.10  ? 105 ARG   A O   1 
ATOM   620  C  CB  . ARG   A 1 99  ? -24.579 1.484   -32.253 1.00 44.73  ? 105 ARG   A CB  1 
ATOM   621  C  CG  . ARG   A 1 99  ? -25.127 0.900   -33.551 1.00 67.51  ? 105 ARG   A CG  1 
ATOM   622  C  CD  . ARG   A 1 99  ? -26.626 1.114   -33.701 1.00 86.25  ? 105 ARG   A CD  1 
ATOM   623  N  NE  . ARG   A 1 99  ? -27.127 0.532   -34.951 1.00 101.32 ? 105 ARG   A NE  1 
ATOM   624  C  CZ  . ARG   A 1 99  ? -28.056 -0.418  -35.027 1.00 117.69 ? 105 ARG   A CZ  1 
ATOM   625  N  NH1 . ARG   A 1 99  ? -28.619 -0.898  -33.924 1.00 105.52 ? 105 ARG   A NH1 1 
ATOM   626  N  NH2 . ARG   A 1 99  ? -28.440 -0.885  -36.209 1.00 102.19 ? 105 ARG   A NH2 1 
ATOM   627  N  N   . ALA   A 1 100 ? -22.908 2.063   -29.703 1.00 42.57  ? 106 ALA   A N   1 
ATOM   628  C  CA  . ALA   A 1 100 ? -22.406 2.935   -28.642 1.00 42.08  ? 106 ALA   A CA  1 
ATOM   629  C  C   . ALA   A 1 100 ? -20.896 2.814   -28.474 1.00 44.40  ? 106 ALA   A C   1 
ATOM   630  O  O   . ALA   A 1 100 ? -20.203 3.833   -28.480 1.00 43.02  ? 106 ALA   A O   1 
ATOM   631  C  CB  . ALA   A 1 100 ? -23.111 2.626   -27.336 1.00 42.98  ? 106 ALA   A CB  1 
ATOM   632  N  N   . VAL   A 1 101 ? -20.382 1.565   -28.393 1.00 40.40  ? 107 VAL   A N   1 
ATOM   633  C  CA  . VAL   A 1 101 ? -18.950 1.275   -28.261 1.00 39.65  ? 107 VAL   A CA  1 
ATOM   634  C  C   . VAL   A 1 101 ? -18.169 1.734   -29.507 1.00 45.15  ? 107 VAL   A C   1 
ATOM   635  O  O   . VAL   A 1 101 ? -17.168 2.439   -29.360 1.00 43.18  ? 107 VAL   A O   1 
ATOM   636  C  CB  . VAL   A 1 101 ? -18.683 -0.216  -27.881 1.00 42.60  ? 107 VAL   A CB  1 
ATOM   637  C  CG1 . VAL   A 1 101 ? -17.183 -0.526  -27.824 1.00 41.87  ? 107 VAL   A CG1 1 
ATOM   638  C  CG2 . VAL   A 1 101 ? -19.345 -0.566  -26.544 1.00 42.48  ? 107 VAL   A CG2 1 
ATOM   639  N  N   . SER   A 1 102 ? -18.631 1.357   -30.736 1.00 44.07  ? 108 SER   A N   1 
ATOM   640  C  CA  . SER   A 1 102 ? -17.957 1.774   -31.981 1.00 45.01  ? 108 SER   A CA  1 
ATOM   641  C  C   . SER   A 1 102 ? -17.958 3.304   -32.168 1.00 50.67  ? 108 SER   A C   1 
ATOM   642  O  O   . SER   A 1 102 ? -16.988 3.824   -32.713 1.00 51.40  ? 108 SER   A O   1 
ATOM   643  C  CB  . SER   A 1 102 ? -18.498 1.045   -33.208 1.00 47.38  ? 108 SER   A CB  1 
ATOM   644  O  OG  . SER   A 1 102 ? -19.910 1.119   -33.307 1.00 58.98  ? 108 SER   A OG  1 
ATOM   645  N  N   . ASP   A 1 103 ? -18.977 4.018   -31.621 1.00 47.80  ? 109 ASP   A N   1 
ATOM   646  C  CA  . ASP   A 1 103 ? -19.064 5.492   -31.597 1.00 47.96  ? 109 ASP   A CA  1 
ATOM   647  C  C   . ASP   A 1 103 ? -18.161 6.114   -30.499 1.00 51.15  ? 109 ASP   A C   1 
ATOM   648  O  O   . ASP   A 1 103 ? -18.181 7.334   -30.325 1.00 51.10  ? 109 ASP   A O   1 
ATOM   649  C  CB  . ASP   A 1 103 ? -20.522 5.972   -31.386 1.00 50.55  ? 109 ASP   A CB  1 
ATOM   650  C  CG  . ASP   A 1 103 ? -21.491 5.805   -32.551 1.00 66.82  ? 109 ASP   A CG  1 
ATOM   651  O  OD1 . ASP   A 1 103 ? -21.062 5.320   -33.625 1.00 69.00  ? 109 ASP   A OD1 1 
ATOM   652  O  OD2 . ASP   A 1 103 ? -22.687 6.127   -32.378 1.00 74.84  ? 109 ASP   A OD2 1 
ATOM   653  N  N   . GLY   A 1 104 ? -17.430 5.280   -29.750 1.00 46.90  ? 110 GLY   A N   1 
ATOM   654  C  CA  . GLY   A 1 104 ? -16.475 5.696   -28.720 1.00 46.80  ? 110 GLY   A CA  1 
ATOM   655  C  C   . GLY   A 1 104 ? -17.001 6.044   -27.336 1.00 49.35  ? 110 GLY   A C   1 
ATOM   656  O  O   . GLY   A 1 104 ? -16.318 6.735   -26.574 1.00 48.48  ? 110 GLY   A O   1 
ATOM   657  N  N   . TYR   A 1 105 ? -18.185 5.546   -26.975 1.00 45.37  ? 111 TYR   A N   1 
ATOM   658  C  CA  . TYR   A 1 105 ? -18.748 5.795   -25.651 1.00 45.06  ? 111 TYR   A CA  1 
ATOM   659  C  C   . TYR   A 1 105 ? -18.527 4.620   -24.707 1.00 46.04  ? 111 TYR   A C   1 
ATOM   660  O  O   . TYR   A 1 105 ? -18.463 3.461   -25.144 1.00 43.83  ? 111 TYR   A O   1 
ATOM   661  C  CB  . TYR   A 1 105 ? -20.262 6.044   -25.733 1.00 47.40  ? 111 TYR   A CB  1 
ATOM   662  C  CG  . TYR   A 1 105 ? -20.650 7.308   -26.462 1.00 52.29  ? 111 TYR   A CG  1 
ATOM   663  C  CD1 . TYR   A 1 105 ? -20.722 8.526   -25.795 1.00 54.41  ? 111 TYR   A CD1 1 
ATOM   664  C  CD2 . TYR   A 1 105 ? -20.993 7.279   -27.812 1.00 53.93  ? 111 TYR   A CD2 1 
ATOM   665  C  CE1 . TYR   A 1 105 ? -21.087 9.694   -26.460 1.00 56.77  ? 111 TYR   A CE1 1 
ATOM   666  C  CE2 . TYR   A 1 105 ? -21.356 8.441   -28.490 1.00 55.45  ? 111 TYR   A CE2 1 
ATOM   667  C  CZ  . TYR   A 1 105 ? -21.408 9.646   -27.808 1.00 63.72  ? 111 TYR   A CZ  1 
ATOM   668  O  OH  . TYR   A 1 105 ? -21.772 10.794  -28.470 1.00 64.73  ? 111 TYR   A OH  1 
ATOM   669  N  N   . SER   A 1 106 ? -18.463 4.931   -23.393 1.00 41.65  ? 112 SER   A N   1 
ATOM   670  C  CA  . SER   A 1 106 ? -18.424 3.946   -22.312 1.00 39.88  ? 112 SER   A CA  1 
ATOM   671  C  C   . SER   A 1 106 ? -19.906 3.617   -22.184 1.00 42.55  ? 112 SER   A C   1 
ATOM   672  O  O   . SER   A 1 106 ? -20.735 4.530   -22.051 1.00 40.52  ? 112 SER   A O   1 
ATOM   673  C  CB  . SER   A 1 106 ? -17.867 4.578   -21.043 1.00 41.83  ? 112 SER   A CB  1 
ATOM   674  O  OG  . SER   A 1 106 ? -16.481 4.822   -21.221 1.00 49.22  ? 112 SER   A OG  1 
ATOM   675  N  N   . CYS   A 1 107 ? -20.260 2.347   -22.377 1.00 39.65  ? 113 CYS   A N   1 
ATOM   676  C  CA  . CYS   A 1 107 ? -21.660 1.987   -22.480 1.00 39.96  ? 113 CYS   A CA  1 
ATOM   677  C  C   . CYS   A 1 107 ? -22.328 1.509   -21.177 1.00 43.74  ? 113 CYS   A C   1 
ATOM   678  O  O   . CYS   A 1 107 ? -22.029 0.420   -20.685 1.00 43.45  ? 113 CYS   A O   1 
ATOM   679  C  CB  . CYS   A 1 107 ? -21.833 0.973   -23.601 1.00 41.05  ? 113 CYS   A CB  1 
ATOM   680  S  SG  . CYS   A 1 107 ? -23.543 0.749   -24.104 1.00 45.63  ? 113 CYS   A SG  1 
ATOM   681  N  N   . VAL   A 1 108 ? -23.295 2.312   -20.669 1.00 38.06  ? 114 VAL   A N   1 
ATOM   682  C  CA  . VAL   A 1 108 ? -24.069 2.049   -19.457 1.00 36.60  ? 114 VAL   A CA  1 
ATOM   683  C  C   . VAL   A 1 108 ? -25.436 1.471   -19.825 1.00 42.41  ? 114 VAL   A C   1 
ATOM   684  O  O   . VAL   A 1 108 ? -26.264 2.177   -20.411 1.00 42.76  ? 114 VAL   A O   1 
ATOM   685  C  CB  . VAL   A 1 108 ? -24.220 3.306   -18.539 1.00 39.02  ? 114 VAL   A CB  1 
ATOM   686  C  CG1 . VAL   A 1 108 ? -25.019 2.983   -17.276 1.00 38.34  ? 114 VAL   A CG1 1 
ATOM   687  C  CG2 . VAL   A 1 108 ? -22.871 3.888   -18.158 1.00 38.34  ? 114 VAL   A CG2 1 
ATOM   688  N  N   . THR   A 1 109 ? -25.694 0.208   -19.452 1.00 37.61  ? 115 THR   A N   1 
ATOM   689  C  CA  . THR   A 1 109 ? -26.999 -0.407  -19.715 1.00 37.75  ? 115 THR   A CA  1 
ATOM   690  C  C   . THR   A 1 109 ? -27.764 -0.586  -18.414 1.00 41.71  ? 115 THR   A C   1 
ATOM   691  O  O   . THR   A 1 109 ? -27.241 -1.156  -17.451 1.00 40.64  ? 115 THR   A O   1 
ATOM   692  C  CB  . THR   A 1 109 ? -26.898 -1.701  -20.559 1.00 45.09  ? 115 THR   A CB  1 
ATOM   693  O  OG1 . THR   A 1 109 ? -26.020 -1.502  -21.661 1.00 44.81  ? 115 THR   A OG1 1 
ATOM   694  C  CG2 . THR   A 1 109 ? -28.250 -2.166  -21.083 1.00 44.46  ? 115 THR   A CG2 1 
ATOM   695  N  N   . LEU   A 1 110 ? -29.006 -0.100  -18.394 1.00 37.49  ? 116 LEU   A N   1 
ATOM   696  C  CA  . LEU   A 1 110 ? -29.882 -0.182  -17.243 1.00 37.23  ? 116 LEU   A CA  1 
ATOM   697  C  C   . LEU   A 1 110 ? -30.842 -1.328  -17.439 1.00 39.19  ? 116 LEU   A C   1 
ATOM   698  O  O   . LEU   A 1 110 ? -31.530 -1.373  -18.451 1.00 38.37  ? 116 LEU   A O   1 
ATOM   699  C  CB  . LEU   A 1 110 ? -30.663 1.147   -17.042 1.00 37.62  ? 116 LEU   A CB  1 
ATOM   700  C  CG  . LEU   A 1 110 ? -29.857 2.457   -17.027 1.00 40.72  ? 116 LEU   A CG  1 
ATOM   701  C  CD1 . LEU   A 1 110 ? -30.776 3.643   -16.754 1.00 41.06  ? 116 LEU   A CD1 1 
ATOM   702  C  CD2 . LEU   A 1 110 ? -28.758 2.425   -15.985 1.00 42.51  ? 116 LEU   A CD2 1 
ATOM   703  N  N   . GLY   A 1 111 ? -30.844 -2.260  -16.490 1.00 33.24  ? 117 GLY   A N   1 
ATOM   704  C  CA  . GLY   A 1 111 ? -31.732 -3.405  -16.498 1.00 32.79  ? 117 GLY   A CA  1 
ATOM   705  C  C   . GLY   A 1 111 ? -32.958 -3.142  -15.652 1.00 36.70  ? 117 GLY   A C   1 
ATOM   706  O  O   . GLY   A 1 111 ? -33.024 -2.116  -14.972 1.00 38.20  ? 117 GLY   A O   1 
ATOM   707  N  N   . GLY   A 1 112 ? -33.928 -4.057  -15.649 1.00 33.41  ? 118 GLY   A N   1 
ATOM   708  C  CA  . GLY   A 1 112 ? -33.907 -5.299  -16.413 1.00 32.90  ? 118 GLY   A CA  1 
ATOM   709  C  C   . GLY   A 1 112 ? -33.131 -6.404  -15.713 1.00 35.68  ? 118 GLY   A C   1 
ATOM   710  O  O   . GLY   A 1 112 ? -32.226 -6.114  -14.934 1.00 35.34  ? 118 GLY   A O   1 
ATOM   711  N  N   . ASP   A 1 113 ? -33.489 -7.668  -15.976 1.00 31.08  ? 119 ASP   A N   1 
ATOM   712  C  CA  . ASP   A 1 113 ? -32.845 -8.806  -15.321 1.00 30.08  ? 119 ASP   A CA  1 
ATOM   713  C  C   . ASP   A 1 113 ? -31.449 -9.076  -15.863 1.00 33.33  ? 119 ASP   A C   1 
ATOM   714  O  O   . ASP   A 1 113 ? -31.086 -8.540  -16.908 1.00 33.79  ? 119 ASP   A O   1 
ATOM   715  C  CB  . ASP   A 1 113 ? -33.733 -10.040 -15.361 1.00 31.55  ? 119 ASP   A CB  1 
ATOM   716  C  CG  . ASP   A 1 113 ? -33.894 -10.610 -16.732 1.00 37.45  ? 119 ASP   A CG  1 
ATOM   717  O  OD1 . ASP   A 1 113 ? -32.912 -11.141 -17.265 1.00 38.02  ? 119 ASP   A OD1 1 
ATOM   718  O  OD2 . ASP   A 1 113 ? -35.010 -10.570 -17.253 1.00 42.09  ? 119 ASP   A OD2 1 
ATOM   719  N  N   . HIS   A 1 114 ? -30.664 -9.906  -15.158 1.00 29.97  ? 120 HIS   A N   1 
ATOM   720  C  CA  . HIS   A 1 114 ? -29.281 -10.167 -15.546 1.00 28.74  ? 120 HIS   A CA  1 
ATOM   721  C  C   . HIS   A 1 114 ? -29.095 -10.999 -16.857 1.00 31.73  ? 120 HIS   A C   1 
ATOM   722  O  O   . HIS   A 1 114 ? -27.960 -11.086 -17.348 1.00 30.40  ? 120 HIS   A O   1 
ATOM   723  C  CB  . HIS   A 1 114 ? -28.464 -10.767 -14.380 1.00 27.99  ? 120 HIS   A CB  1 
ATOM   724  C  CG  . HIS   A 1 114 ? -27.088 -10.150 -14.321 1.00 30.13  ? 120 HIS   A CG  1 
ATOM   725  N  ND1 . HIS   A 1 114 ? -26.343 -10.156 -13.159 1.00 30.49  ? 120 HIS   A ND1 1 
ATOM   726  C  CD2 . HIS   A 1 114 ? -26.407 -9.461  -15.273 1.00 30.72  ? 120 HIS   A CD2 1 
ATOM   727  C  CE1 . HIS   A 1 114 ? -25.230 -9.498  -13.449 1.00 29.31  ? 120 HIS   A CE1 1 
ATOM   728  N  NE2 . HIS   A 1 114 ? -25.219 -9.073  -14.713 1.00 29.50  ? 120 HIS   A NE2 1 
ATOM   729  N  N   . SER   A 1 115 ? -30.175 -11.547 -17.479 1.00 29.36  ? 121 SER   A N   1 
ATOM   730  C  CA  . SER   A 1 115 ? -29.986 -12.241 -18.777 1.00 29.27  ? 121 SER   A CA  1 
ATOM   731  C  C   . SER   A 1 115 ? -29.498 -11.246 -19.860 1.00 31.80  ? 121 SER   A C   1 
ATOM   732  O  O   . SER   A 1 115 ? -28.904 -11.643 -20.863 1.00 30.48  ? 121 SER   A O   1 
ATOM   733  C  CB  . SER   A 1 115 ? -31.266 -12.930 -19.245 1.00 31.98  ? 121 SER   A CB  1 
ATOM   734  O  OG  . SER   A 1 115 ? -32.188 -11.999 -19.796 1.00 38.61  ? 121 SER   A OG  1 
ATOM   735  N  N   . LEU   A 1 116 ? -29.727 -9.945  -19.626 1.00 30.85  ? 122 LEU   A N   1 
ATOM   736  C  CA  . LEU   A 1 116 ? -29.297 -8.860  -20.506 1.00 30.53  ? 122 LEU   A CA  1 
ATOM   737  C  C   . LEU   A 1 116 ? -27.774 -8.746  -20.690 1.00 34.54  ? 122 LEU   A C   1 
ATOM   738  O  O   . LEU   A 1 116 ? -27.331 -8.146  -21.667 1.00 32.89  ? 122 LEU   A O   1 
ATOM   739  C  CB  . LEU   A 1 116 ? -29.890 -7.532  -20.044 1.00 30.97  ? 122 LEU   A CB  1 
ATOM   740  C  CG  . LEU   A 1 116 ? -31.409 -7.447  -20.102 1.00 36.51  ? 122 LEU   A CG  1 
ATOM   741  C  CD1 . LEU   A 1 116 ? -31.895 -6.301  -19.265 1.00 37.60  ? 122 LEU   A CD1 1 
ATOM   742  C  CD2 . LEU   A 1 116 ? -31.909 -7.299  -21.556 1.00 41.12  ? 122 LEU   A CD2 1 
ATOM   743  N  N   . ALA   A 1 117 ? -26.971 -9.360  -19.799 1.00 30.40  ? 123 ALA   A N   1 
ATOM   744  C  CA  . ALA   A 1 117 ? -25.514 -9.361  -19.985 1.00 29.24  ? 123 ALA   A CA  1 
ATOM   745  C  C   . ALA   A 1 117 ? -25.103 -10.165 -21.242 1.00 31.51  ? 123 ALA   A C   1 
ATOM   746  O  O   . ALA   A 1 117 ? -24.041 -9.901  -21.790 1.00 31.62  ? 123 ALA   A O   1 
ATOM   747  C  CB  . ALA   A 1 117 ? -24.821 -9.906  -18.752 1.00 29.72  ? 123 ALA   A CB  1 
ATOM   748  N  N   . ILE   A 1 118 ? -25.938 -11.142 -21.712 1.00 28.37  ? 124 ILE   A N   1 
ATOM   749  C  CA  . ILE   A 1 118 ? -25.662 -11.877 -22.965 1.00 27.56  ? 124 ILE   A CA  1 
ATOM   750  C  C   . ILE   A 1 118 ? -25.526 -10.810 -24.081 1.00 32.39  ? 124 ILE   A C   1 
ATOM   751  O  O   . ILE   A 1 118 ? -24.516 -10.763 -24.760 1.00 32.66  ? 124 ILE   A O   1 
ATOM   752  C  CB  . ILE   A 1 118 ? -26.745 -12.937 -23.344 1.00 30.16  ? 124 ILE   A CB  1 
ATOM   753  C  CG1 . ILE   A 1 118 ? -26.840 -14.080 -22.315 1.00 29.60  ? 124 ILE   A CG1 1 
ATOM   754  C  CG2 . ILE   A 1 118 ? -26.451 -13.526 -24.725 1.00 31.84  ? 124 ILE   A CG2 1 
ATOM   755  C  CD1 . ILE   A 1 118 ? -28.293 -14.745 -22.215 1.00 31.77  ? 124 ILE   A CD1 1 
ATOM   756  N  N   . GLY   A 1 119 ? -26.496 -9.910  -24.169 1.00 29.65  ? 125 GLY   A N   1 
ATOM   757  C  CA  . GLY   A 1 119 ? -26.479 -8.849  -25.168 1.00 30.71  ? 125 GLY   A CA  1 
ATOM   758  C  C   . GLY   A 1 119 ? -25.382 -7.822  -25.006 1.00 34.05  ? 125 GLY   A C   1 
ATOM   759  O  O   . GLY   A 1 119 ? -24.706 -7.500  -25.980 1.00 34.81  ? 125 GLY   A O   1 
ATOM   760  N  N   . THR   A 1 120 ? -25.175 -7.308  -23.779 1.00 29.89  ? 126 THR   A N   1 
ATOM   761  C  CA  . THR   A 1 120 ? -24.183 -6.252  -23.553 1.00 28.05  ? 126 THR   A CA  1 
ATOM   762  C  C   . THR   A 1 120 ? -22.770 -6.731  -23.760 1.00 31.36  ? 126 THR   A C   1 
ATOM   763  O  O   . THR   A 1 120 ? -21.981 -6.014  -24.356 1.00 30.53  ? 126 THR   A O   1 
ATOM   764  C  CB  . THR   A 1 120 ? -24.354 -5.553  -22.189 1.00 32.70  ? 126 THR   A CB  1 
ATOM   765  O  OG1 . THR   A 1 120 ? -24.024 -6.453  -21.146 1.00 27.81  ? 126 THR   A OG1 1 
ATOM   766  C  CG2 . THR   A 1 120 ? -25.760 -4.997  -21.968 1.00 28.73  ? 126 THR   A CG2 1 
ATOM   767  N  N   . ILE   A 1 121 ? -22.421 -7.912  -23.219 1.00 28.25  ? 127 ILE   A N   1 
ATOM   768  C  CA  . ILE   A 1 121 ? -21.061 -8.444  -23.383 1.00 28.08  ? 127 ILE   A CA  1 
ATOM   769  C  C   . ILE   A 1 121 ? -20.805 -8.837  -24.866 1.00 31.53  ? 127 ILE   A C   1 
ATOM   770  O  O   . ILE   A 1 121 ? -19.720 -8.547  -25.392 1.00 29.30  ? 127 ILE   A O   1 
ATOM   771  C  CB  . ILE   A 1 121 ? -20.746 -9.580  -22.357 1.00 30.29  ? 127 ILE   A CB  1 
ATOM   772  C  CG1 . ILE   A 1 121 ? -20.748 -9.011  -20.908 1.00 30.02  ? 127 ILE   A CG1 1 
ATOM   773  C  CG2 . ILE   A 1 121 ? -19.404 -10.256 -22.684 1.00 30.04  ? 127 ILE   A CG2 1 
ATOM   774  C  CD1 . ILE   A 1 121 ? -20.832 -10.078 -19.751 1.00 28.11  ? 127 ILE   A CD1 1 
ATOM   775  N  N   . SER   A 1 122 ? -21.803 -9.486  -25.519 1.00 27.91  ? 128 SER   A N   1 
ATOM   776  C  CA  . SER   A 1 122 ? -21.705 -9.868  -26.958 1.00 28.62  ? 128 SER   A CA  1 
ATOM   777  C  C   . SER   A 1 122 ? -21.466 -8.628  -27.843 1.00 33.38  ? 128 SER   A C   1 
ATOM   778  O  O   . SER   A 1 122 ? -20.578 -8.651  -28.687 1.00 34.35  ? 128 SER   A O   1 
ATOM   779  C  CB  . SER   A 1 122 ? -22.974 -10.582 -27.427 1.00 30.91  ? 128 SER   A CB  1 
ATOM   780  O  OG  . SER   A 1 122 ? -23.134 -11.852 -26.810 1.00 32.47  ? 128 SER   A OG  1 
ATOM   781  N  N   . GLY   A 1 123 ? -22.223 -7.557  -27.605 1.00 32.49  ? 129 GLY   A N   1 
ATOM   782  C  CA  . GLY   A 1 123 ? -22.100 -6.305  -28.350 1.00 32.89  ? 129 GLY   A CA  1 
ATOM   783  C  C   . GLY   A 1 123 ? -20.781 -5.598  -28.118 1.00 35.89  ? 129 GLY   A C   1 
ATOM   784  O  O   . GLY   A 1 123 ? -20.209 -5.017  -29.042 1.00 34.97  ? 129 GLY   A O   1 
ATOM   785  N  N   . HIS   A 1 124 ? -20.286 -5.641  -26.871 1.00 31.78  ? 130 HIS   A N   1 
ATOM   786  C  CA  . HIS   A 1 124 ? -19.011 -5.040  -26.463 1.00 30.81  ? 130 HIS   A CA  1 
ATOM   787  C  C   . HIS   A 1 124 ? -17.814 -5.801  -27.069 1.00 34.38  ? 130 HIS   A C   1 
ATOM   788  O  O   . HIS   A 1 124 ? -16.854 -5.170  -27.520 1.00 33.78  ? 130 HIS   A O   1 
ATOM   789  C  CB  . HIS   A 1 124 ? -18.921 -5.075  -24.908 1.00 31.86  ? 130 HIS   A CB  1 
ATOM   790  C  CG  . HIS   A 1 124 ? -17.822 -4.239  -24.311 1.00 35.00  ? 130 HIS   A CG  1 
ATOM   791  N  ND1 . HIS   A 1 124 ? -17.637 -4.183  -22.937 1.00 36.29  ? 130 HIS   A ND1 1 
ATOM   792  C  CD2 . HIS   A 1 124 ? -16.898 -3.445  -24.906 1.00 36.02  ? 130 HIS   A CD2 1 
ATOM   793  C  CE1 . HIS   A 1 124 ? -16.590 -3.391  -22.746 1.00 35.60  ? 130 HIS   A CE1 1 
ATOM   794  N  NE2 . HIS   A 1 124 ? -16.118 -2.918  -23.904 1.00 35.91  ? 130 HIS   A NE2 1 
ATOM   795  N  N   . ALA   A 1 125 ? -17.853 -7.153  -27.061 1.00 32.11  ? 131 ALA   A N   1 
ATOM   796  C  CA  . ALA   A 1 125 ? -16.766 -7.970  -27.616 1.00 32.62  ? 131 ALA   A CA  1 
ATOM   797  C  C   . ALA   A 1 125 ? -16.662 -7.851  -29.153 1.00 34.16  ? 131 ALA   A C   1 
ATOM   798  O  O   . ALA   A 1 125 ? -15.620 -8.169  -29.711 1.00 33.90  ? 131 ALA   A O   1 
ATOM   799  C  CB  . ALA   A 1 125 ? -16.928 -9.424  -27.210 1.00 33.54  ? 131 ALA   A CB  1 
ATOM   800  N  N   . ARG   A 1 126 ? -17.706 -7.338  -29.817 1.00 32.24  ? 132 ARG   A N   1 
ATOM   801  C  CA  . ARG   A 1 126 ? -17.671 -7.091  -31.268 1.00 33.51  ? 132 ARG   A CA  1 
ATOM   802  C  C   . ARG   A 1 126 ? -16.664 -6.016  -31.631 1.00 38.52  ? 132 ARG   A C   1 
ATOM   803  O  O   . ARG   A 1 126 ? -16.347 -5.869  -32.809 1.00 38.55  ? 132 ARG   A O   1 
ATOM   804  C  CB  . ARG   A 1 126 ? -19.044 -6.691  -31.802 1.00 34.58  ? 132 ARG   A CB  1 
ATOM   805  C  CG  . ARG   A 1 126 ? -19.888 -7.895  -32.142 1.00 40.13  ? 132 ARG   A CG  1 
ATOM   806  C  CD  . ARG   A 1 126 ? -21.298 -7.489  -32.458 1.00 33.80  ? 132 ARG   A CD  1 
ATOM   807  N  NE  . ARG   A 1 126 ? -22.185 -8.640  -32.349 1.00 37.51  ? 132 ARG   A NE  1 
ATOM   808  C  CZ  . ARG   A 1 126 ? -23.505 -8.566  -32.372 1.00 44.89  ? 132 ARG   A CZ  1 
ATOM   809  N  NH1 . ARG   A 1 126 ? -24.105 -7.397  -32.539 1.00 38.60  ? 132 ARG   A NH1 1 
ATOM   810  N  NH2 . ARG   A 1 126 ? -24.236 -9.658  -32.250 1.00 39.84  ? 132 ARG   A NH2 1 
ATOM   811  N  N   . HIS   A 1 127 ? -16.143 -5.279  -30.618 1.00 35.39  ? 133 HIS   A N   1 
ATOM   812  C  CA  . HIS   A 1 127 ? -15.176 -4.190  -30.814 1.00 35.02  ? 133 HIS   A CA  1 
ATOM   813  C  C   . HIS   A 1 127 ? -13.925 -4.304  -29.983 1.00 39.32  ? 133 HIS   A C   1 
ATOM   814  O  O   . HIS   A 1 127 ? -12.887 -3.739  -30.339 1.00 37.71  ? 133 HIS   A O   1 
ATOM   815  C  CB  . HIS   A 1 127 ? -15.867 -2.848  -30.570 1.00 35.28  ? 133 HIS   A CB  1 
ATOM   816  C  CG  . HIS   A 1 127 ? -17.047 -2.662  -31.469 1.00 38.38  ? 133 HIS   A CG  1 
ATOM   817  N  ND1 . HIS   A 1 127 ? -16.888 -2.416  -32.825 1.00 39.67  ? 133 HIS   A ND1 1 
ATOM   818  C  CD2 . HIS   A 1 127 ? -18.365 -2.804  -31.199 1.00 39.46  ? 133 HIS   A CD2 1 
ATOM   819  C  CE1 . HIS   A 1 127 ? -18.113 -2.379  -33.320 1.00 38.94  ? 133 HIS   A CE1 1 
ATOM   820  N  NE2 . HIS   A 1 127 ? -19.031 -2.603  -32.380 1.00 39.01  ? 133 HIS   A NE2 1 
ATOM   821  N  N   . CYS   A 1 128 ? -14.009 -5.082  -28.894 1.00 37.17  ? 134 CYS   A N   1 
ATOM   822  C  CA  . CYS   A 1 128 ? -12.918 -5.282  -27.950 1.00 36.54  ? 134 CYS   A CA  1 
ATOM   823  C  C   . CYS   A 1 128 ? -12.546 -6.763  -27.873 1.00 42.16  ? 134 CYS   A C   1 
ATOM   824  O  O   . CYS   A 1 128 ? -13.172 -7.488  -27.092 1.00 42.12  ? 134 CYS   A O   1 
ATOM   825  C  CB  . CYS   A 1 128 ? -13.318 -4.733  -26.584 1.00 35.18  ? 134 CYS   A CB  1 
ATOM   826  S  SG  . CYS   A 1 128 ? -13.828 -2.997  -26.610 1.00 37.96  ? 134 CYS   A SG  1 
ATOM   827  N  N   . PRO   A 1 129 ? -11.543 -7.232  -28.661 1.00 39.17  ? 135 PRO   A N   1 
ATOM   828  C  CA  . PRO   A 1 129 ? -11.188 -8.658  -28.626 1.00 39.18  ? 135 PRO   A CA  1 
ATOM   829  C  C   . PRO   A 1 129 ? -10.526 -9.094  -27.314 1.00 42.85  ? 135 PRO   A C   1 
ATOM   830  O  O   . PRO   A 1 129 ? -10.515 -10.281 -27.005 1.00 43.89  ? 135 PRO   A O   1 
ATOM   831  C  CB  . PRO   A 1 129 ? -10.232 -8.802  -29.803 1.00 40.40  ? 135 PRO   A CB  1 
ATOM   832  C  CG  . PRO   A 1 129 ? -9.584  -7.454  -29.923 1.00 44.30  ? 135 PRO   A CG  1 
ATOM   833  C  CD  . PRO   A 1 129 ? -10.696 -6.503  -29.633 1.00 40.26  ? 135 PRO   A CD  1 
ATOM   834  N  N   . ASP   A 1 130 ? -9.958  -8.149  -26.565 1.00 37.63  ? 136 ASP   A N   1 
ATOM   835  C  CA  . ASP   A 1 130 ? -9.288  -8.472  -25.307 1.00 36.05  ? 136 ASP   A CA  1 
ATOM   836  C  C   . ASP   A 1 130 ? -10.082 -7.936  -24.121 1.00 36.23  ? 136 ASP   A C   1 
ATOM   837  O  O   . ASP   A 1 130 ? -9.479  -7.632  -23.108 1.00 35.57  ? 136 ASP   A O   1 
ATOM   838  C  CB  . ASP   A 1 130 ? -7.846  -7.920  -25.327 1.00 37.12  ? 136 ASP   A CB  1 
ATOM   839  C  CG  . ASP   A 1 130 ? -6.849  -8.588  -24.403 1.00 42.91  ? 136 ASP   A CG  1 
ATOM   840  O  OD1 . ASP   A 1 130 ? -7.127  -9.716  -23.934 1.00 42.82  ? 136 ASP   A OD1 1 
ATOM   841  O  OD2 . ASP   A 1 130 ? -5.763  -8.016  -24.198 1.00 44.11  ? 136 ASP   A OD2 1 
ATOM   842  N  N   . LEU   A 1 131 ? -11.424 -7.847  -24.214 1.00 33.22  ? 137 LEU   A N   1 
ATOM   843  C  CA  . LEU   A 1 131 ? -12.197 -7.375  -23.069 1.00 32.96  ? 137 LEU   A CA  1 
ATOM   844  C  C   . LEU   A 1 131 ? -12.123 -8.368  -21.879 1.00 34.87  ? 137 LEU   A C   1 
ATOM   845  O  O   . LEU   A 1 131 ? -11.925 -9.574  -22.059 1.00 33.95  ? 137 LEU   A O   1 
ATOM   846  C  CB  . LEU   A 1 131 ? -13.673 -6.963  -23.407 1.00 33.94  ? 137 LEU   A CB  1 
ATOM   847  C  CG  . LEU   A 1 131 ? -14.824 -8.001  -23.521 1.00 41.16  ? 137 LEU   A CG  1 
ATOM   848  C  CD1 . LEU   A 1 131 ? -15.204 -8.578  -22.182 1.00 44.28  ? 137 LEU   A CD1 1 
ATOM   849  C  CD2 . LEU   A 1 131 ? -16.124 -7.330  -23.901 1.00 43.32  ? 137 LEU   A CD2 1 
ATOM   850  N  N   . CYS   A 1 132 ? -12.215 -7.831  -20.675 1.00 32.20  ? 138 CYS   A N   1 
ATOM   851  C  CA  . CYS   A 1 132 ? -12.279 -8.633  -19.451 1.00 31.73  ? 138 CYS   A CA  1 
ATOM   852  C  C   . CYS   A 1 132 ? -13.524 -8.185  -18.697 1.00 33.40  ? 138 CYS   A C   1 
ATOM   853  O  O   . CYS   A 1 132 ? -14.045 -7.092  -18.953 1.00 32.91  ? 138 CYS   A O   1 
ATOM   854  C  CB  . CYS   A 1 132 ? -11.009 -8.515  -18.614 1.00 31.91  ? 138 CYS   A CB  1 
ATOM   855  S  SG  . CYS   A 1 132 ? -10.703 -6.854  -17.993 1.00 35.83  ? 138 CYS   A SG  1 
ATOM   856  N  N   . VAL   A 1 133 ? -14.058 -9.062  -17.840 1.00 27.08  ? 139 VAL   A N   1 
ATOM   857  C  CA  . VAL   A 1 133 ? -15.308 -8.816  -17.140 1.00 24.45  ? 139 VAL   A CA  1 
ATOM   858  C  C   . VAL   A 1 133 ? -15.115 -8.876  -15.619 1.00 28.03  ? 139 VAL   A C   1 
ATOM   859  O  O   . VAL   A 1 133 ? -14.485 -9.788  -15.101 1.00 26.79  ? 139 VAL   A O   1 
ATOM   860  C  CB  . VAL   A 1 133 ? -16.411 -9.848  -17.580 1.00 26.40  ? 139 VAL   A CB  1 
ATOM   861  C  CG1 . VAL   A 1 133 ? -17.725 -9.598  -16.847 1.00 26.59  ? 139 VAL   A CG1 1 
ATOM   862  C  CG2 . VAL   A 1 133 ? -16.634 -9.831  -19.102 1.00 25.93  ? 139 VAL   A CG2 1 
ATOM   863  N  N   . VAL   A 1 134 ? -15.686 -7.919  -14.916 1.00 25.79  ? 140 VAL   A N   1 
ATOM   864  C  CA  . VAL   A 1 134 ? -15.738 -7.944  -13.448 1.00 25.43  ? 140 VAL   A CA  1 
ATOM   865  C  C   . VAL   A 1 134 ? -17.236 -8.107  -13.183 1.00 29.07  ? 140 VAL   A C   1 
ATOM   866  O  O   . VAL   A 1 134 ? -18.011 -7.244  -13.561 1.00 28.41  ? 140 VAL   A O   1 
ATOM   867  C  CB  . VAL   A 1 134 ? -15.142 -6.695  -12.761 1.00 30.09  ? 140 VAL   A CB  1 
ATOM   868  C  CG1 . VAL   A 1 134 ? -15.273 -6.813  -11.241 1.00 30.32  ? 140 VAL   A CG1 1 
ATOM   869  C  CG2 . VAL   A 1 134 ? -13.687 -6.510  -13.142 1.00 30.19  ? 140 VAL   A CG2 1 
ATOM   870  N  N   . TRP   A 1 135 ? -17.641 -9.267  -12.651 1.00 27.49  ? 141 TRP   A N   1 
ATOM   871  C  CA  . TRP   A 1 135 ? -19.040 -9.579  -12.406 1.00 26.56  ? 141 TRP   A CA  1 
ATOM   872  C  C   . TRP   A 1 135 ? -19.321 -9.464  -10.900 1.00 28.68  ? 141 TRP   A C   1 
ATOM   873  O  O   . TRP   A 1 135 ? -18.849 -10.286 -10.113 1.00 26.44  ? 141 TRP   A O   1 
ATOM   874  C  CB  . TRP   A 1 135 ? -19.327 -10.989 -12.936 1.00 25.45  ? 141 TRP   A CB  1 
ATOM   875  C  CG  . TRP   A 1 135 ? -20.790 -11.330 -13.062 1.00 26.71  ? 141 TRP   A CG  1 
ATOM   876  C  CD1 . TRP   A 1 135 ? -21.633 -11.693 -12.059 1.00 29.10  ? 141 TRP   A CD1 1 
ATOM   877  C  CD2 . TRP   A 1 135 ? -21.526 -11.489 -14.284 1.00 26.81  ? 141 TRP   A CD2 1 
ATOM   878  N  NE1 . TRP   A 1 135 ? -22.856 -12.044 -12.573 1.00 28.93  ? 141 TRP   A NE1 1 
ATOM   879  C  CE2 . TRP   A 1 135 ? -22.826 -11.906 -13.937 1.00 30.44  ? 141 TRP   A CE2 1 
ATOM   880  C  CE3 . TRP   A 1 135 ? -21.218 -11.293 -15.644 1.00 28.78  ? 141 TRP   A CE3 1 
ATOM   881  C  CZ2 . TRP   A 1 135 ? -23.815 -12.163 -14.901 1.00 29.26  ? 141 TRP   A CZ2 1 
ATOM   882  C  CZ3 . TRP   A 1 135 ? -22.217 -11.490 -16.591 1.00 29.88  ? 141 TRP   A CZ3 1 
ATOM   883  C  CH2 . TRP   A 1 135 ? -23.499 -11.924 -16.213 1.00 29.87  ? 141 TRP   A CH2 1 
ATOM   884  N  N   . VAL   A 1 136 ? -20.076 -8.436  -10.507 1.00 26.89  ? 142 VAL   A N   1 
ATOM   885  C  CA  . VAL   A 1 136 ? -20.380 -8.132  -9.097  1.00 26.19  ? 142 VAL   A CA  1 
ATOM   886  C  C   . VAL   A 1 136 ? -21.805 -8.546  -8.846  1.00 29.36  ? 142 VAL   A C   1 
ATOM   887  O  O   . VAL   A 1 136 ? -22.722 -7.981  -9.444  1.00 29.02  ? 142 VAL   A O   1 
ATOM   888  C  CB  . VAL   A 1 136 ? -20.068 -6.667  -8.700  1.00 29.26  ? 142 VAL   A CB  1 
ATOM   889  C  CG1 . VAL   A 1 136 ? -20.286 -6.458  -7.203  1.00 28.34  ? 142 VAL   A CG1 1 
ATOM   890  C  CG2 . VAL   A 1 136 ? -18.637 -6.285  -9.075  1.00 28.92  ? 142 VAL   A CG2 1 
ATOM   891  N  N   . ASP   A 1 137 ? -21.983 -9.598  -8.027  1.00 25.41  ? 143 ASP   A N   1 
ATOM   892  C  CA  . ASP   A 1 137 ? -23.302 -10.211 -7.846  1.00 25.46  ? 143 ASP   A CA  1 
ATOM   893  C  C   . ASP   A 1 137 ? -23.286 -11.191 -6.674  1.00 30.02  ? 143 ASP   A C   1 
ATOM   894  O  O   . ASP   A 1 137 ? -22.223 -11.729 -6.366  1.00 29.33  ? 143 ASP   A O   1 
ATOM   895  C  CB  . ASP   A 1 137 ? -23.535 -11.006 -9.150  1.00 25.56  ? 143 ASP   A CB  1 
ATOM   896  C  CG  . ASP   A 1 137 ? -24.934 -11.413 -9.537  1.00 28.20  ? 143 ASP   A CG  1 
ATOM   897  O  OD1 . ASP   A 1 137 ? -25.747 -11.659 -8.635  1.00 24.41  ? 143 ASP   A OD1 1 
ATOM   898  O  OD2 . ASP   A 1 137 ? -25.186 -11.560 -10.754 1.00 31.64  ? 143 ASP   A OD2 1 
ATOM   899  N  N   . ALA   A 1 138 ? -24.468 -11.496 -6.086  1.00 27.29  ? 144 ALA   A N   1 
ATOM   900  C  CA  . ALA   A 1 138 ? -24.593 -12.539 -5.061  1.00 28.08  ? 144 ALA   A CA  1 
ATOM   901  C  C   . ALA   A 1 138 ? -24.522 -13.896 -5.765  1.00 30.48  ? 144 ALA   A C   1 
ATOM   902  O  O   . ALA   A 1 138 ? -24.248 -14.915 -5.126  1.00 29.75  ? 144 ALA   A O   1 
ATOM   903  C  CB  . ALA   A 1 138 ? -25.936 -12.423 -4.326  1.00 28.35  ? 144 ALA   A CB  1 
ATOM   904  N  N   . HIS   A 1 139 ? -24.777 -13.903 -7.090  1.00 27.73  ? 145 HIS   A N   1 
ATOM   905  C  CA  . HIS   A 1 139 ? -24.841 -15.102 -7.918  1.00 26.93  ? 145 HIS   A CA  1 
ATOM   906  C  C   . HIS   A 1 139 ? -23.798 -15.175 -9.025  1.00 30.26  ? 145 HIS   A C   1 
ATOM   907  O  O   . HIS   A 1 139 ? -23.314 -14.138 -9.499  1.00 29.86  ? 145 HIS   A O   1 
ATOM   908  C  CB  . HIS   A 1 139 ? -26.255 -15.246 -8.529  1.00 27.84  ? 145 HIS   A CB  1 
ATOM   909  C  CG  . HIS   A 1 139 ? -27.353 -15.053 -7.534  1.00 30.59  ? 145 HIS   A CG  1 
ATOM   910  N  ND1 . HIS   A 1 139 ? -27.956 -13.821 -7.362  1.00 31.76  ? 145 HIS   A ND1 1 
ATOM   911  C  CD2 . HIS   A 1 139 ? -27.899 -15.938 -6.663  1.00 31.97  ? 145 HIS   A CD2 1 
ATOM   912  C  CE1 . HIS   A 1 139 ? -28.867 -13.998 -6.423  1.00 31.32  ? 145 HIS   A CE1 1 
ATOM   913  N  NE2 . HIS   A 1 139 ? -28.871 -15.258 -5.972  1.00 31.86  ? 145 HIS   A NE2 1 
ATOM   914  N  N   . ALA   A 1 140 ? -23.456 -16.417 -9.452  1.00 25.77  ? 146 ALA   A N   1 
ATOM   915  C  CA  . ALA   A 1 140 ? -22.503 -16.612 -10.538 1.00 26.31  ? 146 ALA   A CA  1 
ATOM   916  C  C   . ALA   A 1 140 ? -23.156 -16.562 -11.931 1.00 27.89  ? 146 ALA   A C   1 
ATOM   917  O  O   . ALA   A 1 140 ? -22.474 -16.289 -12.903 1.00 26.49  ? 146 ALA   A O   1 
ATOM   918  C  CB  . ALA   A 1 140 ? -21.711 -17.902 -10.341 1.00 26.53  ? 146 ALA   A CB  1 
ATOM   919  N  N   . ASP   A 1 141 ? -24.493 -16.775 -12.024 1.00 26.04  ? 147 ASP   A N   1 
ATOM   920  C  CA  . ASP   A 1 141 ? -25.236 -16.715 -13.294 1.00 25.36  ? 147 ASP   A CA  1 
ATOM   921  C  C   . ASP   A 1 141 ? -24.565 -17.551 -14.403 1.00 29.40  ? 147 ASP   A C   1 
ATOM   922  O  O   . ASP   A 1 141 ? -24.491 -17.137 -15.564 1.00 28.11  ? 147 ASP   A O   1 
ATOM   923  C  CB  . ASP   A 1 141 ? -25.433 -15.235 -13.717 1.00 26.06  ? 147 ASP   A CB  1 
ATOM   924  C  CG  . ASP   A 1 141 ? -26.230 -14.406 -12.716 1.00 30.06  ? 147 ASP   A CG  1 
ATOM   925  O  OD1 . ASP   A 1 141 ? -26.823 -14.995 -11.792 1.00 29.38  ? 147 ASP   A OD1 1 
ATOM   926  O  OD2 . ASP   A 1 141 ? -26.298 -13.179 -12.888 1.00 31.44  ? 147 ASP   A OD2 1 
ATOM   927  N  N   . ILE   A 1 142 ? -24.016 -18.703 -14.017 1.00 27.21  ? 148 ILE   A N   1 
ATOM   928  C  CA  . ILE   A 1 142 ? -23.218 -19.542 -14.899 1.00 25.88  ? 148 ILE   A CA  1 
ATOM   929  C  C   . ILE   A 1 142 ? -23.807 -20.953 -15.063 1.00 31.04  ? 148 ILE   A C   1 
ATOM   930  O  O   . ILE   A 1 142 ? -23.154 -21.847 -15.623 1.00 30.04  ? 148 ILE   A O   1 
ATOM   931  C  CB  . ILE   A 1 142 ? -21.729 -19.529 -14.422 1.00 27.75  ? 148 ILE   A CB  1 
ATOM   932  C  CG1 . ILE   A 1 142 ? -20.772 -20.008 -15.529 1.00 28.67  ? 148 ILE   A CG1 1 
ATOM   933  C  CG2 . ILE   A 1 142 ? -21.543 -20.314 -13.098 1.00 24.59  ? 148 ILE   A CG2 1 
ATOM   934  C  CD1 . ILE   A 1 142 ? -19.324 -19.535 -15.366 1.00 32.33  ? 148 ILE   A CD1 1 
ATOM   935  N  N   . ASN   A 1 143 ? -25.065 -21.158 -14.615 1.00 28.22  ? 149 ASN   A N   1 
ATOM   936  C  CA  . ASN   A 1 143 ? -25.696 -22.438 -14.910 1.00 26.63  ? 149 ASN   A CA  1 
ATOM   937  C  C   . ASN   A 1 143 ? -25.783 -22.547 -16.434 1.00 28.93  ? 149 ASN   A C   1 
ATOM   938  O  O   . ASN   A 1 143 ? -25.966 -21.534 -17.123 1.00 29.24  ? 149 ASN   A O   1 
ATOM   939  C  CB  . ASN   A 1 143 ? -27.153 -22.508 -14.360 1.00 24.47  ? 149 ASN   A CB  1 
ATOM   940  C  CG  . ASN   A 1 143 ? -27.231 -22.983 -12.930 1.00 25.36  ? 149 ASN   A CG  1 
ATOM   941  O  OD1 . ASN   A 1 143 ? -26.753 -24.060 -12.590 1.00 29.40  ? 149 ASN   A OD1 1 
ATOM   942  N  ND2 . ASN   A 1 143 ? -27.777 -22.159 -12.051 1.00 27.51  ? 149 ASN   A ND2 1 
ATOM   943  N  N   . THR   A 1 144 ? -25.697 -23.764 -16.960 1.00 25.64  ? 150 THR   A N   1 
ATOM   944  C  CA  . THR   A 1 144 ? -25.909 -23.952 -18.395 1.00 25.32  ? 150 THR   A CA  1 
ATOM   945  C  C   . THR   A 1 144 ? -27.427 -24.278 -18.525 1.00 29.23  ? 150 THR   A C   1 
ATOM   946  O  O   . THR   A 1 144 ? -28.044 -24.578 -17.505 1.00 28.08  ? 150 THR   A O   1 
ATOM   947  C  CB  . THR   A 1 144 ? -25.098 -25.124 -18.968 1.00 27.81  ? 150 THR   A CB  1 
ATOM   948  O  OG1 . THR   A 1 144 ? -25.708 -26.358 -18.596 1.00 27.50  ? 150 THR   A OG1 1 
ATOM   949  C  CG2 . THR   A 1 144 ? -23.587 -25.083 -18.618 1.00 28.23  ? 150 THR   A CG2 1 
ATOM   950  N  N   . PRO   A 1 145 ? -28.031 -24.335 -19.736 1.00 28.22  ? 151 PRO   A N   1 
ATOM   951  C  CA  . PRO   A 1 145 ? -29.455 -24.765 -19.830 1.00 28.02  ? 151 PRO   A CA  1 
ATOM   952  C  C   . PRO   A 1 145 ? -29.719 -26.210 -19.380 1.00 29.90  ? 151 PRO   A C   1 
ATOM   953  O  O   . PRO   A 1 145 ? -30.876 -26.602 -19.215 1.00 29.09  ? 151 PRO   A O   1 
ATOM   954  C  CB  . PRO   A 1 145 ? -29.786 -24.543 -21.318 1.00 29.36  ? 151 PRO   A CB  1 
ATOM   955  C  CG  . PRO   A 1 145 ? -28.774 -23.507 -21.779 1.00 32.77  ? 151 PRO   A CG  1 
ATOM   956  C  CD  . PRO   A 1 145 ? -27.520 -23.930 -21.064 1.00 28.97  ? 151 PRO   A CD  1 
ATOM   957  N  N   . LEU   A 1 146 ? -28.644 -27.006 -19.143 1.00 26.09  ? 152 LEU   A N   1 
ATOM   958  C  CA  . LEU   A 1 146 ? -28.784 -28.386 -18.684 1.00 26.15  ? 152 LEU   A CA  1 
ATOM   959  C  C   . LEU   A 1 146 ? -28.596 -28.531 -17.166 1.00 28.29  ? 152 LEU   A C   1 
ATOM   960  O  O   . LEU   A 1 146 ? -29.050 -29.514 -16.592 1.00 28.37  ? 152 LEU   A O   1 
ATOM   961  C  CB  . LEU   A 1 146 ? -27.849 -29.337 -19.479 1.00 26.22  ? 152 LEU   A CB  1 
ATOM   962  C  CG  . LEU   A 1 146 ? -28.101 -29.451 -20.983 1.00 30.73  ? 152 LEU   A CG  1 
ATOM   963  C  CD1 . LEU   A 1 146 ? -26.982 -30.240 -21.655 1.00 30.50  ? 152 LEU   A CD1 1 
ATOM   964  C  CD2 . LEU   A 1 146 ? -29.459 -30.106 -21.254 1.00 32.50  ? 152 LEU   A CD2 1 
ATOM   965  N  N   . THR   A 1 147 ? -27.968 -27.546 -16.504 1.00 24.25  ? 153 THR   A N   1 
ATOM   966  C  CA  . THR   A 1 147 ? -27.743 -27.607 -15.059 1.00 24.24  ? 153 THR   A CA  1 
ATOM   967  C  C   . THR   A 1 147 ? -28.740 -26.770 -14.268 1.00 28.47  ? 153 THR   A C   1 
ATOM   968  O  O   . THR   A 1 147 ? -28.942 -27.029 -13.088 1.00 30.22  ? 153 THR   A O   1 
ATOM   969  C  CB  . THR   A 1 147 ? -26.312 -27.196 -14.670 1.00 31.70  ? 153 THR   A CB  1 
ATOM   970  O  OG1 . THR   A 1 147 ? -26.154 -25.815 -14.903 1.00 28.04  ? 153 THR   A OG1 1 
ATOM   971  C  CG2 . THR   A 1 147 ? -25.246 -27.972 -15.401 1.00 28.21  ? 153 THR   A CG2 1 
ATOM   972  N  N   . THR   A 1 148 ? -29.331 -25.756 -14.888 1.00 26.04  ? 154 THR   A N   1 
ATOM   973  C  CA  . THR   A 1 148 ? -30.340 -24.944 -14.216 1.00 26.42  ? 154 THR   A CA  1 
ATOM   974  C  C   . THR   A 1 148 ? -31.450 -25.815 -13.587 1.00 30.02  ? 154 THR   A C   1 
ATOM   975  O  O   . THR   A 1 148 ? -31.854 -26.805 -14.193 1.00 29.46  ? 154 THR   A O   1 
ATOM   976  C  CB  . THR   A 1 148 ? -30.937 -23.904 -15.181 1.00 29.57  ? 154 THR   A CB  1 
ATOM   977  O  OG1 . THR   A 1 148 ? -31.863 -23.107 -14.449 1.00 29.72  ? 154 THR   A OG1 1 
ATOM   978  C  CG2 . THR   A 1 148 ? -31.628 -24.550 -16.411 1.00 29.38  ? 154 THR   A CG2 1 
ATOM   979  N  N   . SER   A 1 149 ? -31.889 -25.459 -12.361 1.00 30.10  ? 155 SER   A N   1 
ATOM   980  C  CA  . SER   A 1 149 ? -32.994 -26.094 -11.637 1.00 30.88  ? 155 SER   A CA  1 
ATOM   981  C  C   . SER   A 1 149 ? -34.226 -25.235 -11.905 1.00 36.33  ? 155 SER   A C   1 
ATOM   982  O  O   . SER   A 1 149 ? -35.315 -25.764 -12.105 1.00 35.89  ? 155 SER   A O   1 
ATOM   983  C  CB  . SER   A 1 149 ? -32.728 -26.105 -10.130 1.00 35.96  ? 155 SER   A CB  1 
ATOM   984  O  OG  . SER   A 1 149 ? -31.850 -27.159 -9.769  1.00 52.45  ? 155 SER   A OG  1 
ATOM   985  N  N   . SER   A 1 150 ? -34.044 -23.901 -11.924 1.00 33.00  ? 156 SER   A N   1 
ATOM   986  C  CA  . SER   A 1 150 ? -35.169 -22.982 -12.145 1.00 32.38  ? 156 SER   A CA  1 
ATOM   987  C  C   . SER   A 1 150 ? -35.608 -22.828 -13.602 1.00 36.00  ? 156 SER   A C   1 
ATOM   988  O  O   . SER   A 1 150 ? -36.804 -22.613 -13.861 1.00 36.96  ? 156 SER   A O   1 
ATOM   989  C  CB  . SER   A 1 150 ? -34.870 -21.616 -11.550 1.00 32.61  ? 156 SER   A CB  1 
ATOM   990  O  OG  . SER   A 1 150 ? -33.883 -21.004 -12.354 1.00 34.87  ? 156 SER   A OG  1 
ATOM   991  N  N   . GLY   A 1 151 ? -34.655 -22.899 -14.531 1.00 29.78  ? 157 GLY   A N   1 
ATOM   992  C  CA  . GLY   A 1 151 ? -34.925 -22.686 -15.951 1.00 29.64  ? 157 GLY   A CA  1 
ATOM   993  C  C   . GLY   A 1 151 ? -34.960 -21.218 -16.352 1.00 33.17  ? 157 GLY   A C   1 
ATOM   994  O  O   . GLY   A 1 151 ? -35.132 -20.905 -17.535 1.00 33.10  ? 157 GLY   A O   1 
ATOM   995  N  N   . ASN   A 1 152 ? -34.739 -20.303 -15.371 1.00 30.26  ? 158 ASN   A N   1 
ATOM   996  C  CA  . ASN   A 1 152 ? -34.726 -18.850 -15.547 1.00 30.12  ? 158 ASN   A CA  1 
ATOM   997  C  C   . ASN   A 1 152 ? -33.411 -18.437 -16.164 1.00 33.86  ? 158 ASN   A C   1 
ATOM   998  O  O   . ASN   A 1 152 ? -32.338 -18.800 -15.647 1.00 32.24  ? 158 ASN   A O   1 
ATOM   999  C  CB  . ASN   A 1 152 ? -34.977 -18.137 -14.204 1.00 32.67  ? 158 ASN   A CB  1 
ATOM   1000 C  CG  . ASN   A 1 152 ? -36.359 -18.406 -13.660 1.00 42.53  ? 158 ASN   A CG  1 
ATOM   1001 O  OD1 . ASN   A 1 152 ? -37.272 -18.780 -14.384 1.00 39.49  ? 158 ASN   A OD1 1 
ATOM   1002 N  ND2 . ASN   A 1 152 ? -36.522 -18.323 -12.371 1.00 34.08  ? 158 ASN   A ND2 1 
ATOM   1003 N  N   . LEU   A 1 153 ? -33.479 -17.760 -17.327 1.00 30.03  ? 159 LEU   A N   1 
ATOM   1004 C  CA  . LEU   A 1 153 ? -32.259 -17.455 -18.075 1.00 29.46  ? 159 LEU   A CA  1 
ATOM   1005 C  C   . LEU   A 1 153 ? -31.363 -16.389 -17.433 1.00 32.25  ? 159 LEU   A C   1 
ATOM   1006 O  O   . LEU   A 1 153 ? -30.176 -16.313 -17.802 1.00 30.85  ? 159 LEU   A O   1 
ATOM   1007 C  CB  . LEU   A 1 153 ? -32.545 -17.145 -19.544 1.00 29.40  ? 159 LEU   A CB  1 
ATOM   1008 C  CG  . LEU   A 1 153 ? -32.909 -18.411 -20.361 1.00 34.17  ? 159 LEU   A CG  1 
ATOM   1009 C  CD1 . LEU   A 1 153 ? -33.857 -18.088 -21.479 1.00 34.77  ? 159 LEU   A CD1 1 
ATOM   1010 C  CD2 . LEU   A 1 153 ? -31.654 -19.141 -20.890 1.00 34.20  ? 159 LEU   A CD2 1 
ATOM   1011 N  N   . HIS   A 1 154 ? -31.862 -15.641 -16.425 1.00 29.76  ? 160 HIS   A N   1 
ATOM   1012 C  CA  . HIS   A 1 154 ? -30.998 -14.669 -15.726 1.00 30.48  ? 160 HIS   A CA  1 
ATOM   1013 C  C   . HIS   A 1 154 ? -29.938 -15.356 -14.819 1.00 32.26  ? 160 HIS   A C   1 
ATOM   1014 O  O   . HIS   A 1 154 ? -28.986 -14.701 -14.398 1.00 29.13  ? 160 HIS   A O   1 
ATOM   1015 C  CB  . HIS   A 1 154 ? -31.810 -13.594 -14.962 1.00 31.23  ? 160 HIS   A CB  1 
ATOM   1016 C  CG  . HIS   A 1 154 ? -32.475 -14.065 -13.700 1.00 34.76  ? 160 HIS   A CG  1 
ATOM   1017 N  ND1 . HIS   A 1 154 ? -32.708 -13.198 -12.656 1.00 36.39  ? 160 HIS   A ND1 1 
ATOM   1018 C  CD2 . HIS   A 1 154 ? -32.926 -15.297 -13.351 1.00 36.70  ? 160 HIS   A CD2 1 
ATOM   1019 C  CE1 . HIS   A 1 154 ? -33.277 -13.923 -11.708 1.00 36.17  ? 160 HIS   A CE1 1 
ATOM   1020 N  NE2 . HIS   A 1 154 ? -33.442 -15.189 -12.091 1.00 36.50  ? 160 HIS   A NE2 1 
ATOM   1021 N  N   . GLY   A 1 155 ? -30.105 -16.656 -14.554 1.00 29.52  ? 161 GLY   A N   1 
ATOM   1022 C  CA  . GLY   A 1 155 ? -29.153 -17.430 -13.758 1.00 28.65  ? 161 GLY   A CA  1 
ATOM   1023 C  C   . GLY   A 1 155 ? -28.217 -18.255 -14.622 1.00 29.48  ? 161 GLY   A C   1 
ATOM   1024 O  O   . GLY   A 1 155 ? -27.506 -19.127 -14.106 1.00 28.99  ? 161 GLY   A O   1 
ATOM   1025 N  N   . GLN   A 1 156 ? -28.211 -17.991 -15.945 1.00 25.95  ? 162 GLN   A N   1 
ATOM   1026 C  CA  . GLN   A 1 156 ? -27.430 -18.701 -16.982 1.00 26.04  ? 162 GLN   A CA  1 
ATOM   1027 C  C   . GLN   A 1 156 ? -26.572 -17.831 -17.973 1.00 31.06  ? 162 GLN   A C   1 
ATOM   1028 O  O   . GLN   A 1 156 ? -25.918 -18.436 -18.832 1.00 30.59  ? 162 GLN   A O   1 
ATOM   1029 C  CB  . GLN   A 1 156 ? -28.406 -19.545 -17.851 1.00 27.95  ? 162 GLN   A CB  1 
ATOM   1030 C  CG  . GLN   A 1 156 ? -29.157 -20.685 -17.130 1.00 25.38  ? 162 GLN   A CG  1 
ATOM   1031 C  CD  . GLN   A 1 156 ? -30.201 -21.250 -18.049 1.00 32.62  ? 162 GLN   A CD  1 
ATOM   1032 O  OE1 . GLN   A 1 156 ? -29.892 -21.765 -19.118 1.00 27.24  ? 162 GLN   A OE1 1 
ATOM   1033 N  NE2 . GLN   A 1 156 ? -31.473 -21.124 -17.685 1.00 29.57  ? 162 GLN   A NE2 1 
ATOM   1034 N  N   . PRO   A 1 157 ? -26.585 -16.464 -17.971 1.00 29.23  ? 163 PRO   A N   1 
ATOM   1035 C  CA  . PRO   A 1 157 ? -25.914 -15.710 -19.053 1.00 28.20  ? 163 PRO   A CA  1 
ATOM   1036 C  C   . PRO   A 1 157 ? -24.461 -16.033 -19.338 1.00 30.47  ? 163 PRO   A C   1 
ATOM   1037 O  O   . PRO   A 1 157 ? -24.106 -16.159 -20.509 1.00 30.47  ? 163 PRO   A O   1 
ATOM   1038 C  CB  . PRO   A 1 157 ? -26.071 -14.241 -18.627 1.00 29.44  ? 163 PRO   A CB  1 
ATOM   1039 C  CG  . PRO   A 1 157 ? -26.369 -14.290 -17.168 1.00 33.12  ? 163 PRO   A CG  1 
ATOM   1040 C  CD  . PRO   A 1 157 ? -27.253 -15.521 -17.062 1.00 29.82  ? 163 PRO   A CD  1 
ATOM   1041 N  N   . VAL   A 1 158 ? -23.645 -16.219 -18.291 1.00 27.23  ? 164 VAL   A N   1 
ATOM   1042 C  CA  . VAL   A 1 158 ? -22.214 -16.493 -18.473 1.00 26.10  ? 164 VAL   A CA  1 
ATOM   1043 C  C   . VAL   A 1 158 ? -21.972 -17.806 -19.253 1.00 27.98  ? 164 VAL   A C   1 
ATOM   1044 O  O   . VAL   A 1 158 ? -20.976 -17.890 -19.955 1.00 27.44  ? 164 VAL   A O   1 
ATOM   1045 C  CB  . VAL   A 1 158 ? -21.436 -16.415 -17.133 1.00 29.02  ? 164 VAL   A CB  1 
ATOM   1046 C  CG1 . VAL   A 1 158 ? -19.924 -16.571 -17.366 1.00 28.29  ? 164 VAL   A CG1 1 
ATOM   1047 C  CG2 . VAL   A 1 158 ? -21.731 -15.076 -16.438 1.00 28.84  ? 164 VAL   A CG2 1 
ATOM   1048 N  N   . SER   A 1 159 ? -22.865 -18.823 -19.146 1.00 26.54  ? 165 SER   A N   1 
ATOM   1049 C  CA  . SER   A 1 159 ? -22.661 -20.091 -19.863 1.00 25.55  ? 165 SER   A CA  1 
ATOM   1050 C  C   . SER   A 1 159 ? -22.608 -19.930 -21.391 1.00 29.09  ? 165 SER   A C   1 
ATOM   1051 O  O   . SER   A 1 159 ? -21.872 -20.652 -22.054 1.00 27.43  ? 165 SER   A O   1 
ATOM   1052 C  CB  . SER   A 1 159 ? -23.686 -21.150 -19.459 1.00 26.04  ? 165 SER   A CB  1 
ATOM   1053 O  OG  . SER   A 1 159 ? -25.000 -20.865 -19.931 1.00 26.54  ? 165 SER   A OG  1 
ATOM   1054 N  N   . PHE   A 1 160 ? -23.376 -18.979 -21.940 1.00 28.09  ? 166 PHE   A N   1 
ATOM   1055 C  CA  . PHE   A 1 160 ? -23.424 -18.722 -23.382 1.00 27.90  ? 166 PHE   A CA  1 
ATOM   1056 C  C   . PHE   A 1 160 ? -22.211 -17.952 -23.881 1.00 31.57  ? 166 PHE   A C   1 
ATOM   1057 O  O   . PHE   A 1 160 ? -21.887 -18.038 -25.064 1.00 32.48  ? 166 PHE   A O   1 
ATOM   1058 C  CB  . PHE   A 1 160 ? -24.699 -17.937 -23.749 1.00 29.66  ? 166 PHE   A CB  1 
ATOM   1059 C  CG  . PHE   A 1 160 ? -25.950 -18.621 -23.273 1.00 30.77  ? 166 PHE   A CG  1 
ATOM   1060 C  CD1 . PHE   A 1 160 ? -26.497 -19.679 -23.985 1.00 33.45  ? 166 PHE   A CD1 1 
ATOM   1061 C  CD2 . PHE   A 1 160 ? -26.574 -18.219 -22.100 1.00 32.22  ? 166 PHE   A CD2 1 
ATOM   1062 C  CE1 . PHE   A 1 160 ? -27.639 -20.336 -23.518 1.00 34.63  ? 166 PHE   A CE1 1 
ATOM   1063 C  CE2 . PHE   A 1 160 ? -27.719 -18.866 -21.641 1.00 34.60  ? 166 PHE   A CE2 1 
ATOM   1064 C  CZ  . PHE   A 1 160 ? -28.236 -19.927 -22.345 1.00 33.60  ? 166 PHE   A CZ  1 
ATOM   1065 N  N   . LEU   A 1 161 ? -21.566 -17.182 -22.986 1.00 27.30  ? 167 LEU   A N   1 
ATOM   1066 C  CA  . LEU   A 1 161 ? -20.444 -16.305 -23.315 1.00 26.34  ? 167 LEU   A CA  1 
ATOM   1067 C  C   . LEU   A 1 161 ? -19.085 -16.937 -23.170 1.00 31.21  ? 167 LEU   A C   1 
ATOM   1068 O  O   . LEU   A 1 161 ? -18.134 -16.476 -23.802 1.00 32.44  ? 167 LEU   A O   1 
ATOM   1069 C  CB  . LEU   A 1 161 ? -20.500 -15.063 -22.436 1.00 26.26  ? 167 LEU   A CB  1 
ATOM   1070 C  CG  . LEU   A 1 161 ? -21.749 -14.214 -22.584 1.00 30.49  ? 167 LEU   A CG  1 
ATOM   1071 C  CD1 . LEU   A 1 161 ? -21.889 -13.291 -21.420 1.00 29.14  ? 167 LEU   A CD1 1 
ATOM   1072 C  CD2 . LEU   A 1 161 ? -21.739 -13.450 -23.916 1.00 33.17  ? 167 LEU   A CD2 1 
ATOM   1073 N  N   . LEU   A 1 162 ? -18.970 -17.932 -22.294 1.00 28.94  ? 168 LEU   A N   1 
ATOM   1074 C  CA  . LEU   A 1 162 ? -17.696 -18.558 -21.985 1.00 29.63  ? 168 LEU   A CA  1 
ATOM   1075 C  C   . LEU   A 1 162 ? -17.254 -19.589 -23.012 1.00 31.88  ? 168 LEU   A C   1 
ATOM   1076 O  O   . LEU   A 1 162 ? -17.950 -20.575 -23.251 1.00 31.14  ? 168 LEU   A O   1 
ATOM   1077 C  CB  . LEU   A 1 162 ? -17.744 -19.144 -20.565 1.00 30.97  ? 168 LEU   A CB  1 
ATOM   1078 C  CG  . LEU   A 1 162 ? -16.434 -19.111 -19.793 1.00 37.84  ? 168 LEU   A CG  1 
ATOM   1079 C  CD1 . LEU   A 1 162 ? -16.096 -17.694 -19.302 1.00 37.86  ? 168 LEU   A CD1 1 
ATOM   1080 C  CD2 . LEU   A 1 162 ? -16.474 -20.123 -18.638 1.00 43.02  ? 168 LEU   A CD2 1 
ATOM   1081 N  N   . ARG   A 1 163 ? -16.062 -19.378 -23.607 1.00 28.45  ? 169 ARG   A N   1 
ATOM   1082 C  CA  . ARG   A 1 163 ? -15.509 -20.280 -24.631 1.00 29.07  ? 169 ARG   A CA  1 
ATOM   1083 C  C   . ARG   A 1 163 ? -15.385 -21.739 -24.181 1.00 32.08  ? 169 ARG   A C   1 
ATOM   1084 O  O   . ARG   A 1 163 ? -15.721 -22.650 -24.943 1.00 30.25  ? 169 ARG   A O   1 
ATOM   1085 C  CB  . ARG   A 1 163 ? -14.153 -19.776 -25.144 1.00 30.44  ? 169 ARG   A CB  1 
ATOM   1086 C  CG  . ARG   A 1 163 ? -14.261 -18.518 -26.010 1.00 35.91  ? 169 ARG   A CG  1 
ATOM   1087 C  CD  . ARG   A 1 163 ? -12.909 -18.156 -26.575 1.00 45.22  ? 169 ARG   A CD  1 
ATOM   1088 N  NE  . ARG   A 1 163 ? -12.709 -16.710 -26.647 1.00 59.62  ? 169 ARG   A NE  1 
ATOM   1089 C  CZ  . ARG   A 1 163 ? -12.919 -15.972 -27.731 1.00 77.59  ? 169 ARG   A CZ  1 
ATOM   1090 N  NH1 . ARG   A 1 163 ? -13.363 -16.534 -28.852 1.00 72.46  ? 169 ARG   A NH1 1 
ATOM   1091 N  NH2 . ARG   A 1 163 ? -12.695 -14.666 -27.704 1.00 54.81  ? 169 ARG   A NH2 1 
ATOM   1092 N  N   . GLU   A 1 164 ? -14.926 -21.953 -22.931 1.00 30.89  ? 170 GLU   A N   1 
ATOM   1093 C  CA  . GLU   A 1 164 ? -14.671 -23.286 -22.361 1.00 29.36  ? 170 GLU   A CA  1 
ATOM   1094 C  C   . GLU   A 1 164 ? -15.938 -24.106 -22.171 1.00 33.75  ? 170 GLU   A C   1 
ATOM   1095 O  O   . GLU   A 1 164 ? -15.853 -25.329 -22.067 1.00 34.45  ? 170 GLU   A O   1 
ATOM   1096 C  CB  . GLU   A 1 164 ? -13.865 -23.191 -21.053 1.00 30.98  ? 170 GLU   A CB  1 
ATOM   1097 C  CG  . GLU   A 1 164 ? -12.449 -22.643 -21.239 1.00 38.89  ? 170 GLU   A CG  1 
ATOM   1098 C  CD  . GLU   A 1 164 ? -12.258 -21.138 -21.384 1.00 51.78  ? 170 GLU   A CD  1 
ATOM   1099 O  OE1 . GLU   A 1 164 ? -13.256 -20.377 -21.433 1.00 39.40  ? 170 GLU   A OE1 1 
ATOM   1100 O  OE2 . GLU   A 1 164 ? -11.081 -20.720 -21.455 1.00 47.24  ? 170 GLU   A OE2 1 
ATOM   1101 N  N   . LEU   A 1 165 ? -17.109 -23.445 -22.160 1.00 29.37  ? 171 LEU   A N   1 
ATOM   1102 C  CA  . LEU   A 1 165 ? -18.404 -24.105 -21.979 1.00 29.43  ? 171 LEU   A CA  1 
ATOM   1103 C  C   . LEU   A 1 165 ? -19.163 -24.396 -23.256 1.00 35.09  ? 171 LEU   A C   1 
ATOM   1104 O  O   . LEU   A 1 165 ? -20.258 -24.971 -23.177 1.00 35.51  ? 171 LEU   A O   1 
ATOM   1105 C  CB  . LEU   A 1 165 ? -19.292 -23.286 -21.022 1.00 29.41  ? 171 LEU   A CB  1 
ATOM   1106 C  CG  . LEU   A 1 165 ? -18.911 -23.288 -19.524 1.00 33.22  ? 171 LEU   A CG  1 
ATOM   1107 C  CD1 . LEU   A 1 165 ? -19.738 -22.281 -18.751 1.00 31.11  ? 171 LEU   A CD1 1 
ATOM   1108 C  CD2 . LEU   A 1 165 ? -19.008 -24.711 -18.893 1.00 36.66  ? 171 LEU   A CD2 1 
ATOM   1109 N  N   . GLN   A 1 166 ? -18.617 -24.010 -24.434 1.00 32.22  ? 172 GLN   A N   1 
ATOM   1110 C  CA  . GLN   A 1 166 ? -19.305 -24.224 -25.717 1.00 32.46  ? 172 GLN   A CA  1 
ATOM   1111 C  C   . GLN   A 1 166 ? -19.826 -25.671 -25.902 1.00 36.28  ? 172 GLN   A C   1 
ATOM   1112 O  O   . GLN   A 1 166 ? -20.975 -25.840 -26.284 1.00 36.23  ? 172 GLN   A O   1 
ATOM   1113 C  CB  . GLN   A 1 166 ? -18.439 -23.773 -26.905 1.00 33.60  ? 172 GLN   A CB  1 
ATOM   1114 C  CG  . GLN   A 1 166 ? -19.171 -23.779 -28.266 1.00 56.99  ? 172 GLN   A CG  1 
ATOM   1115 C  CD  . GLN   A 1 166 ? -18.678 -22.755 -29.279 1.00 74.72  ? 172 GLN   A CD  1 
ATOM   1116 O  OE1 . GLN   A 1 166 ? -17.479 -22.489 -29.426 1.00 65.12  ? 172 GLN   A OE1 1 
ATOM   1117 N  NE2 . GLN   A 1 166 ? -19.606 -22.182 -30.033 1.00 71.38  ? 172 GLN   A NE2 1 
ATOM   1118 N  N   . ASP   A 1 167 ? -19.032 -26.691 -25.546 1.00 33.06  ? 173 ASP   A N   1 
ATOM   1119 C  CA  . ASP   A 1 167 ? -19.437 -28.090 -25.708 1.00 33.88  ? 173 ASP   A CA  1 
ATOM   1120 C  C   . ASP   A 1 167 ? -20.428 -28.603 -24.636 1.00 35.77  ? 173 ASP   A C   1 
ATOM   1121 O  O   . ASP   A 1 167 ? -20.898 -29.727 -24.739 1.00 35.60  ? 173 ASP   A O   1 
ATOM   1122 C  CB  . ASP   A 1 167 ? -18.202 -28.999 -25.803 1.00 37.46  ? 173 ASP   A CB  1 
ATOM   1123 C  CG  . ASP   A 1 167 ? -17.404 -29.146 -24.519 1.00 59.24  ? 173 ASP   A CG  1 
ATOM   1124 O  OD1 . ASP   A 1 167 ? -17.183 -28.111 -23.825 1.00 62.05  ? 173 ASP   A OD1 1 
ATOM   1125 O  OD2 . ASP   A 1 167 ? -16.958 -30.277 -24.230 1.00 66.11  ? 173 ASP   A OD2 1 
ATOM   1126 N  N   . LYS   A 1 168 ? -20.741 -27.784 -23.626 1.00 31.25  ? 174 LYS   A N   1 
ATOM   1127 C  CA  . LYS   A 1 168 ? -21.662 -28.129 -22.556 1.00 30.17  ? 174 LYS   A CA  1 
ATOM   1128 C  C   . LYS   A 1 168 ? -23.030 -27.422 -22.711 1.00 33.37  ? 174 LYS   A C   1 
ATOM   1129 O  O   . LYS   A 1 168 ? -23.943 -27.678 -21.923 1.00 34.87  ? 174 LYS   A O   1 
ATOM   1130 C  CB  . LYS   A 1 168 ? -21.025 -27.771 -21.193 1.00 30.49  ? 174 LYS   A CB  1 
ATOM   1131 C  CG  . LYS   A 1 168 ? -19.594 -28.309 -20.981 1.00 32.36  ? 174 LYS   A CG  1 
ATOM   1132 C  CD  . LYS   A 1 168 ? -19.471 -29.846 -21.066 1.00 29.94  ? 174 LYS   A CD  1 
ATOM   1133 C  CE  . LYS   A 1 168 ? -18.073 -30.289 -20.665 1.00 36.91  ? 174 LYS   A CE  1 
ATOM   1134 N  NZ  . LYS   A 1 168 ? -17.897 -31.761 -20.788 1.00 34.34  ? 174 LYS   A NZ  1 
ATOM   1135 N  N   . VAL   A 1 169 ? -23.153 -26.514 -23.684 1.00 29.67  ? 175 VAL   A N   1 
ATOM   1136 C  CA  . VAL   A 1 169 ? -24.352 -25.678 -23.871 1.00 28.86  ? 175 VAL   A CA  1 
ATOM   1137 C  C   . VAL   A 1 169 ? -25.169 -26.132 -25.089 1.00 34.03  ? 175 VAL   A C   1 
ATOM   1138 O  O   . VAL   A 1 169 ? -24.661 -26.046 -26.206 1.00 32.30  ? 175 VAL   A O   1 
ATOM   1139 C  CB  . VAL   A 1 169 ? -23.963 -24.161 -23.957 1.00 31.63  ? 175 VAL   A CB  1 
ATOM   1140 C  CG1 . VAL   A 1 169 ? -25.192 -23.272 -24.214 1.00 31.11  ? 175 VAL   A CG1 1 
ATOM   1141 C  CG2 . VAL   A 1 169 ? -23.221 -23.702 -22.695 1.00 31.10  ? 175 VAL   A CG2 1 
ATOM   1142 N  N   . PRO   A 1 170 ? -26.439 -26.577 -24.911 1.00 31.59  ? 176 PRO   A N   1 
ATOM   1143 C  CA  . PRO   A 1 170 ? -27.254 -26.942 -26.086 1.00 31.81  ? 176 PRO   A CA  1 
ATOM   1144 C  C   . PRO   A 1 170 ? -27.725 -25.710 -26.860 1.00 36.86  ? 176 PRO   A C   1 
ATOM   1145 O  O   . PRO   A 1 170 ? -27.697 -24.608 -26.328 1.00 35.57  ? 176 PRO   A O   1 
ATOM   1146 C  CB  . PRO   A 1 170 ? -28.448 -27.671 -25.466 1.00 33.62  ? 176 PRO   A CB  1 
ATOM   1147 C  CG  . PRO   A 1 170 ? -28.608 -27.051 -24.145 1.00 36.81  ? 176 PRO   A CG  1 
ATOM   1148 C  CD  . PRO   A 1 170 ? -27.209 -26.734 -23.663 1.00 32.71  ? 176 PRO   A CD  1 
ATOM   1149 N  N   . GLN   A 1 171 ? -28.182 -25.907 -28.112 1.00 37.33  ? 177 GLN   A N   1 
ATOM   1150 C  CA  . GLN   A 1 171 ? -28.683 -24.813 -28.934 1.00 37.53  ? 177 GLN   A CA  1 
ATOM   1151 C  C   . GLN   A 1 171 ? -30.128 -24.529 -28.549 1.00 40.03  ? 177 GLN   A C   1 
ATOM   1152 O  O   . GLN   A 1 171 ? -30.995 -25.394 -28.683 1.00 42.10  ? 177 GLN   A O   1 
ATOM   1153 C  CB  . GLN   A 1 171 ? -28.538 -25.114 -30.443 1.00 39.40  ? 177 GLN   A CB  1 
ATOM   1154 C  CG  . GLN   A 1 171 ? -27.767 -24.009 -31.166 1.00 65.10  ? 177 GLN   A CG  1 
ATOM   1155 C  CD  . GLN   A 1 171 ? -28.011 -23.991 -32.658 1.00 92.69  ? 177 GLN   A CD  1 
ATOM   1156 O  OE1 . GLN   A 1 171 ? -27.244 -24.560 -33.445 1.00 91.49  ? 177 GLN   A OE1 1 
ATOM   1157 N  NE2 . GLN   A 1 171 ? -29.064 -23.303 -33.085 1.00 82.04  ? 177 GLN   A NE2 1 
ATOM   1158 N  N   . LEU   A 1 172 ? -30.367 -23.344 -27.995 1.00 33.70  ? 178 LEU   A N   1 
ATOM   1159 C  CA  . LEU   A 1 172 ? -31.692 -22.928 -27.559 1.00 32.79  ? 178 LEU   A CA  1 
ATOM   1160 C  C   . LEU   A 1 172 ? -32.349 -22.132 -28.687 1.00 36.93  ? 178 LEU   A C   1 
ATOM   1161 O  O   . LEU   A 1 172 ? -31.642 -21.434 -29.426 1.00 35.22  ? 178 LEU   A O   1 
ATOM   1162 C  CB  . LEU   A 1 172 ? -31.539 -22.008 -26.328 1.00 33.09  ? 178 LEU   A CB  1 
ATOM   1163 C  CG  . LEU   A 1 172 ? -31.927 -22.470 -24.914 1.00 37.17  ? 178 LEU   A CG  1 
ATOM   1164 C  CD1 . LEU   A 1 172 ? -31.736 -23.966 -24.657 1.00 36.24  ? 178 LEU   A CD1 1 
ATOM   1165 C  CD2 . LEU   A 1 172 ? -31.310 -21.563 -23.866 1.00 37.06  ? 178 LEU   A CD2 1 
ATOM   1166 N  N   . PRO   A 1 173 ? -33.696 -22.183 -28.827 1.00 34.78  ? 179 PRO   A N   1 
ATOM   1167 C  CA  . PRO   A 1 173 ? -34.345 -21.351 -29.855 1.00 34.56  ? 179 PRO   A CA  1 
ATOM   1168 C  C   . PRO   A 1 173 ? -34.123 -19.865 -29.585 1.00 37.91  ? 179 PRO   A C   1 
ATOM   1169 O  O   . PRO   A 1 173 ? -34.286 -19.429 -28.448 1.00 38.06  ? 179 PRO   A O   1 
ATOM   1170 C  CB  . PRO   A 1 173 ? -35.826 -21.731 -29.750 1.00 36.59  ? 179 PRO   A CB  1 
ATOM   1171 C  CG  . PRO   A 1 173 ? -35.994 -22.377 -28.475 1.00 40.64  ? 179 PRO   A CG  1 
ATOM   1172 C  CD  . PRO   A 1 173 ? -34.685 -22.947 -28.039 1.00 36.30  ? 179 PRO   A CD  1 
ATOM   1173 N  N   . GLY   A 1 174 ? -33.708 -19.126 -30.621 1.00 34.50  ? 180 GLY   A N   1 
ATOM   1174 C  CA  . GLY   A 1 174 ? -33.426 -17.695 -30.555 1.00 33.71  ? 180 GLY   A CA  1 
ATOM   1175 C  C   . GLY   A 1 174 ? -32.015 -17.334 -30.133 1.00 37.00  ? 180 GLY   A C   1 
ATOM   1176 O  O   . GLY   A 1 174 ? -31.690 -16.153 -30.054 1.00 36.36  ? 180 GLY   A O   1 
ATOM   1177 N  N   . PHE   A 1 175 ? -31.162 -18.344 -29.875 1.00 34.39  ? 181 PHE   A N   1 
ATOM   1178 C  CA  . PHE   A 1 175 ? -29.797 -18.179 -29.375 1.00 33.86  ? 181 PHE   A CA  1 
ATOM   1179 C  C   . PHE   A 1 175 ? -28.691 -18.519 -30.368 1.00 38.72  ? 181 PHE   A C   1 
ATOM   1180 O  O   . PHE   A 1 175 ? -27.514 -18.475 -29.987 1.00 36.56  ? 181 PHE   A O   1 
ATOM   1181 C  CB  . PHE   A 1 175 ? -29.613 -19.041 -28.100 1.00 35.17  ? 181 PHE   A CB  1 
ATOM   1182 C  CG  . PHE   A 1 175 ? -30.107 -18.451 -26.797 1.00 35.87  ? 181 PHE   A CG  1 
ATOM   1183 C  CD1 . PHE   A 1 175 ? -31.470 -18.316 -26.545 1.00 38.15  ? 181 PHE   A CD1 1 
ATOM   1184 C  CD2 . PHE   A 1 175 ? -29.216 -18.126 -25.782 1.00 36.83  ? 181 PHE   A CD2 1 
ATOM   1185 C  CE1 . PHE   A 1 175 ? -31.922 -17.790 -25.327 1.00 39.58  ? 181 PHE   A CE1 1 
ATOM   1186 C  CE2 . PHE   A 1 175 ? -29.667 -17.586 -24.574 1.00 39.03  ? 181 PHE   A CE2 1 
ATOM   1187 C  CZ  . PHE   A 1 175 ? -31.017 -17.423 -24.352 1.00 37.42  ? 181 PHE   A CZ  1 
ATOM   1188 N  N   . SER   A 1 176 ? -29.040 -18.869 -31.631 1.00 37.29  ? 182 SER   A N   1 
ATOM   1189 C  CA  . SER   A 1 176 ? -28.026 -19.257 -32.624 1.00 37.75  ? 182 SER   A CA  1 
ATOM   1190 C  C   . SER   A 1 176 ? -27.051 -18.122 -32.998 1.00 40.86  ? 182 SER   A C   1 
ATOM   1191 O  O   . SER   A 1 176 ? -25.934 -18.418 -33.415 1.00 40.89  ? 182 SER   A O   1 
ATOM   1192 C  CB  . SER   A 1 176 ? -28.664 -19.867 -33.869 1.00 41.40  ? 182 SER   A CB  1 
ATOM   1193 O  OG  . SER   A 1 176 ? -29.501 -18.943 -34.546 1.00 53.70  ? 182 SER   A OG  1 
ATOM   1194 N  N   . TRP   A 1 177 ? -27.438 -16.851 -32.779 1.00 36.64  ? 183 TRP   A N   1 
ATOM   1195 C  CA  . TRP   A 1 177 ? -26.615 -15.664 -33.079 1.00 36.21  ? 183 TRP   A CA  1 
ATOM   1196 C  C   . TRP   A 1 177 ? -25.419 -15.457 -32.107 1.00 41.99  ? 183 TRP   A C   1 
ATOM   1197 O  O   . TRP   A 1 177 ? -24.482 -14.719 -32.436 1.00 39.38  ? 183 TRP   A O   1 
ATOM   1198 C  CB  . TRP   A 1 177 ? -27.503 -14.394 -33.129 1.00 34.81  ? 183 TRP   A CB  1 
ATOM   1199 C  CG  . TRP   A 1 177 ? -28.085 -14.020 -31.801 1.00 35.45  ? 183 TRP   A CG  1 
ATOM   1200 C  CD1 . TRP   A 1 177 ? -29.210 -14.534 -31.232 1.00 38.21  ? 183 TRP   A CD1 1 
ATOM   1201 C  CD2 . TRP   A 1 177 ? -27.479 -13.180 -30.804 1.00 35.10  ? 183 TRP   A CD2 1 
ATOM   1202 N  NE1 . TRP   A 1 177 ? -29.364 -14.042 -29.959 1.00 37.15  ? 183 TRP   A NE1 1 
ATOM   1203 C  CE2 . TRP   A 1 177 ? -28.312 -13.215 -29.666 1.00 38.02  ? 183 TRP   A CE2 1 
ATOM   1204 C  CE3 . TRP   A 1 177 ? -26.328 -12.370 -30.777 1.00 36.34  ? 183 TRP   A CE3 1 
ATOM   1205 C  CZ2 . TRP   A 1 177 ? -28.020 -12.498 -28.497 1.00 36.87  ? 183 TRP   A CZ2 1 
ATOM   1206 C  CZ3 . TRP   A 1 177 ? -26.044 -11.650 -29.620 1.00 37.66  ? 183 TRP   A CZ3 1 
ATOM   1207 C  CH2 . TRP   A 1 177 ? -26.895 -11.704 -28.505 1.00 37.95  ? 183 TRP   A CH2 1 
ATOM   1208 N  N   . ILE   A 1 178 ? -25.468 -16.073 -30.902 1.00 40.16  ? 184 ILE   A N   1 
ATOM   1209 C  CA  . ILE   A 1 178 ? -24.410 -15.889 -29.894 1.00 39.53  ? 184 ILE   A CA  1 
ATOM   1210 C  C   . ILE   A 1 178 ? -23.168 -16.682 -30.241 1.00 43.65  ? 184 ILE   A C   1 
ATOM   1211 O  O   . ILE   A 1 178 ? -23.248 -17.847 -30.601 1.00 45.40  ? 184 ILE   A O   1 
ATOM   1212 C  CB  . ILE   A 1 178 ? -24.913 -16.195 -28.436 1.00 42.93  ? 184 ILE   A CB  1 
ATOM   1213 C  CG1 . ILE   A 1 178 ? -26.115 -15.332 -28.082 1.00 42.83  ? 184 ILE   A CG1 1 
ATOM   1214 C  CG2 . ILE   A 1 178 ? -23.803 -16.014 -27.367 1.00 43.63  ? 184 ILE   A CG2 1 
ATOM   1215 C  CD1 . ILE   A 1 178 ? -27.136 -16.000 -27.377 1.00 47.96  ? 184 ILE   A CD1 1 
ATOM   1216 N  N   . LYS   A 1 179 ? -22.021 -16.043 -30.106 1.00 40.17  ? 185 LYS   A N   1 
ATOM   1217 C  CA  . LYS   A 1 179 ? -20.710 -16.649 -30.279 1.00 40.00  ? 185 LYS   A CA  1 
ATOM   1218 C  C   . LYS   A 1 179 ? -20.002 -16.477 -28.919 1.00 41.39  ? 185 LYS   A C   1 
ATOM   1219 O  O   . LYS   A 1 179 ? -19.913 -15.335 -28.464 1.00 39.54  ? 185 LYS   A O   1 
ATOM   1220 C  CB  . LYS   A 1 179 ? -19.914 -15.910 -31.371 1.00 44.16  ? 185 LYS   A CB  1 
ATOM   1221 C  CG  . LYS   A 1 179 ? -20.399 -16.207 -32.794 1.00 74.83  ? 185 LYS   A CG  1 
ATOM   1222 C  CD  . LYS   A 1 179 ? -20.067 -15.063 -33.761 1.00 91.21  ? 185 LYS   A CD  1 
ATOM   1223 C  CE  . LYS   A 1 179 ? -20.516 -15.328 -35.184 1.00 105.97 ? 185 LYS   A CE  1 
ATOM   1224 N  NZ  . LYS   A 1 179 ? -21.988 -15.164 -35.357 1.00 117.56 ? 185 LYS   A NZ  1 
ATOM   1225 N  N   . PRO   A 1 180 ? -19.501 -17.554 -28.254 1.00 37.57  ? 186 PRO   A N   1 
ATOM   1226 C  CA  . PRO   A 1 180 ? -18.740 -17.358 -26.999 1.00 37.04  ? 186 PRO   A CA  1 
ATOM   1227 C  C   . PRO   A 1 180 ? -17.592 -16.389 -27.266 1.00 39.35  ? 186 PRO   A C   1 
ATOM   1228 O  O   . PRO   A 1 180 ? -16.929 -16.503 -28.295 1.00 38.78  ? 186 PRO   A O   1 
ATOM   1229 C  CB  . PRO   A 1 180 ? -18.227 -18.767 -26.667 1.00 38.86  ? 186 PRO   A CB  1 
ATOM   1230 C  CG  . PRO   A 1 180 ? -19.182 -19.685 -27.355 1.00 43.87  ? 186 PRO   A CG  1 
ATOM   1231 C  CD  . PRO   A 1 180 ? -19.499 -18.978 -28.650 1.00 39.78  ? 186 PRO   A CD  1 
ATOM   1232 N  N   . CYS   A 1 181 ? -17.401 -15.404 -26.387 1.00 36.26  ? 187 CYS   A N   1 
ATOM   1233 C  CA  . CYS   A 1 181 ? -16.439 -14.329 -26.632 1.00 36.65  ? 187 CYS   A CA  1 
ATOM   1234 C  C   . CYS   A 1 181 ? -15.476 -14.026 -25.471 1.00 43.02  ? 187 CYS   A C   1 
ATOM   1235 O  O   . CYS   A 1 181 ? -14.669 -13.092 -25.592 1.00 43.93  ? 187 CYS   A O   1 
ATOM   1236 C  CB  . CYS   A 1 181 ? -17.200 -13.075 -27.051 1.00 36.46  ? 187 CYS   A CB  1 
ATOM   1237 S  SG  . CYS   A 1 181 ? -18.468 -12.544 -25.865 1.00 40.19  ? 187 CYS   A SG  1 
ATOM   1238 N  N   . ILE   A 1 182 ? -15.574 -14.776 -24.355 1.00 37.73  ? 188 ILE   A N   1 
ATOM   1239 C  CA  . ILE   A 1 182 ? -14.731 -14.590 -23.175 1.00 37.78  ? 188 ILE   A CA  1 
ATOM   1240 C  C   . ILE   A 1 182 ? -14.167 -15.907 -22.704 1.00 38.49  ? 188 ILE   A C   1 
ATOM   1241 O  O   . ILE   A 1 182 ? -14.830 -16.935 -22.823 1.00 36.25  ? 188 ILE   A O   1 
ATOM   1242 C  CB  . ILE   A 1 182 ? -15.398 -13.779 -22.015 1.00 42.34  ? 188 ILE   A CB  1 
ATOM   1243 C  CG1 . ILE   A 1 182 ? -16.751 -14.370 -21.568 1.00 43.33  ? 188 ILE   A CG1 1 
ATOM   1244 C  CG2 . ILE   A 1 182 ? -15.536 -12.287 -22.398 1.00 44.45  ? 188 ILE   A CG2 1 
ATOM   1245 C  CD1 . ILE   A 1 182 ? -17.151 -14.053 -20.133 1.00 52.61  ? 188 ILE   A CD1 1 
ATOM   1246 N  N   . SER   A 1 183 ? -12.908 -15.889 -22.239 1.00 34.57  ? 189 SER   A N   1 
ATOM   1247 C  CA  . SER   A 1 183 ? -12.266 -17.090 -21.725 1.00 34.20  ? 189 SER   A CA  1 
ATOM   1248 C  C   . SER   A 1 183 ? -12.414 -17.096 -20.202 1.00 34.12  ? 189 SER   A C   1 
ATOM   1249 O  O   . SER   A 1 183 ? -12.632 -16.052 -19.587 1.00 31.68  ? 189 SER   A O   1 
ATOM   1250 C  CB  . SER   A 1 183 ? -10.797 -17.153 -22.146 1.00 39.88  ? 189 SER   A CB  1 
ATOM   1251 O  OG  . SER   A 1 183 ? -9.993  -16.262 -21.384 1.00 55.43  ? 189 SER   A OG  1 
ATOM   1252 N  N   . SER   A 1 184 ? -12.262 -18.268 -19.599 1.00 31.99  ? 190 SER   A N   1 
ATOM   1253 C  CA  . SER   A 1 184 ? -12.366 -18.476 -18.159 1.00 30.77  ? 190 SER   A CA  1 
ATOM   1254 C  C   . SER   A 1 184 ? -11.422 -17.567 -17.339 1.00 34.59  ? 190 SER   A C   1 
ATOM   1255 O  O   . SER   A 1 184 ? -11.833 -17.096 -16.283 1.00 33.85  ? 190 SER   A O   1 
ATOM   1256 C  CB  . SER   A 1 184 ? -12.181 -19.956 -17.839 1.00 35.21  ? 190 SER   A CB  1 
ATOM   1257 O  OG  . SER   A 1 184 ? -10.879 -20.397 -18.191 1.00 50.18  ? 190 SER   A OG  1 
ATOM   1258 N  N   . ALA   A 1 185 ? -10.196 -17.248 -17.855 1.00 30.09  ? 191 ALA   A N   1 
ATOM   1259 C  CA  . ALA   A 1 185 ? -9.249  -16.361 -17.172 1.00 30.59  ? 191 ALA   A CA  1 
ATOM   1260 C  C   . ALA   A 1 185 ? -9.570  -14.864 -17.363 1.00 33.35  ? 191 ALA   A C   1 
ATOM   1261 O  O   . ALA   A 1 185 ? -8.897  -14.017 -16.773 1.00 32.54  ? 191 ALA   A O   1 
ATOM   1262 C  CB  . ALA   A 1 185 ? -7.824  -16.665 -17.651 1.00 31.95  ? 191 ALA   A CB  1 
ATOM   1263 N  N   . SER   A 1 186 ? -10.636 -14.531 -18.116 1.00 28.82  ? 192 SER   A N   1 
ATOM   1264 C  CA  . SER   A 1 186 ? -10.994 -13.133 -18.409 1.00 28.52  ? 192 SER   A CA  1 
ATOM   1265 C  C   . SER   A 1 186 ? -12.215 -12.610 -17.634 1.00 31.58  ? 192 SER   A C   1 
ATOM   1266 O  O   . SER   A 1 186 ? -12.643 -11.476 -17.856 1.00 30.14  ? 192 SER   A O   1 
ATOM   1267 C  CB  . SER   A 1 186 ? -11.172 -12.936 -19.916 1.00 31.48  ? 192 SER   A CB  1 
ATOM   1268 O  OG  . SER   A 1 186 ? -9.938  -13.219 -20.559 1.00 37.14  ? 192 SER   A OG  1 
ATOM   1269 N  N   . ILE   A 1 187 ? -12.763 -13.426 -16.718 1.00 27.64  ? 193 ILE   A N   1 
ATOM   1270 C  CA  . ILE   A 1 187 ? -13.881 -12.990 -15.876 1.00 26.82  ? 193 ILE   A CA  1 
ATOM   1271 C  C   . ILE   A 1 187 ? -13.561 -13.238 -14.408 1.00 28.87  ? 193 ILE   A C   1 
ATOM   1272 O  O   . ILE   A 1 187 ? -13.063 -14.316 -14.053 1.00 30.19  ? 193 ILE   A O   1 
ATOM   1273 C  CB  . ILE   A 1 187 ? -15.268 -13.572 -16.310 1.00 29.55  ? 193 ILE   A CB  1 
ATOM   1274 C  CG1 . ILE   A 1 187 ? -16.412 -13.047 -15.391 1.00 29.35  ? 193 ILE   A CG1 1 
ATOM   1275 C  CG2 . ILE   A 1 187 ? -15.234 -15.122 -16.420 1.00 28.94  ? 193 ILE   A CG2 1 
ATOM   1276 C  CD1 . ILE   A 1 187 ? -17.908 -13.524 -15.736 1.00 30.46  ? 193 ILE   A CD1 1 
ATOM   1277 N  N   . VAL   A 1 188 ? -13.787 -12.209 -13.569 1.00 25.06  ? 194 VAL   A N   1 
ATOM   1278 C  CA  . VAL   A 1 188 ? -13.602 -12.290 -12.111 1.00 23.95  ? 194 VAL   A CA  1 
ATOM   1279 C  C   . VAL   A 1 188 ? -14.921 -11.933 -11.443 1.00 28.29  ? 194 VAL   A C   1 
ATOM   1280 O  O   . VAL   A 1 188 ? -15.536 -10.919 -11.776 1.00 27.33  ? 194 VAL   A O   1 
ATOM   1281 C  CB  . VAL   A 1 188 ? -12.409 -11.460 -11.555 1.00 28.35  ? 194 VAL   A CB  1 
ATOM   1282 C  CG1 . VAL   A 1 188 ? -12.345 -11.549 -10.015 1.00 28.39  ? 194 VAL   A CG1 1 
ATOM   1283 C  CG2 . VAL   A 1 188 ? -11.090 -11.924 -12.168 1.00 27.58  ? 194 VAL   A CG2 1 
ATOM   1284 N  N   . TYR   A 1 189 ? -15.382 -12.812 -10.539 1.00 25.51  ? 195 TYR   A N   1 
ATOM   1285 C  CA  . TYR   A 1 189 ? -16.585 -12.584 -9.763  1.00 25.83  ? 195 TYR   A CA  1 
ATOM   1286 C  C   . TYR   A 1 189 ? -16.253 -11.963 -8.404  1.00 28.48  ? 195 TYR   A C   1 
ATOM   1287 O  O   . TYR   A 1 189 ? -15.265 -12.334 -7.779  1.00 26.96  ? 195 TYR   A O   1 
ATOM   1288 C  CB  . TYR   A 1 189 ? -17.295 -13.911 -9.485  1.00 25.05  ? 195 TYR   A CB  1 
ATOM   1289 C  CG  . TYR   A 1 189 ? -17.977 -14.497 -10.692 1.00 25.96  ? 195 TYR   A CG  1 
ATOM   1290 C  CD1 . TYR   A 1 189 ? -19.281 -14.144 -11.014 1.00 26.50  ? 195 TYR   A CD1 1 
ATOM   1291 C  CD2 . TYR   A 1 189 ? -17.346 -15.468 -11.474 1.00 25.92  ? 195 TYR   A CD2 1 
ATOM   1292 C  CE1 . TYR   A 1 189 ? -19.936 -14.721 -12.091 1.00 28.23  ? 195 TYR   A CE1 1 
ATOM   1293 C  CE2 . TYR   A 1 189 ? -17.999 -16.058 -12.559 1.00 26.25  ? 195 TYR   A CE2 1 
ATOM   1294 C  CZ  . TYR   A 1 189 ? -19.315 -15.716 -12.825 1.00 31.73  ? 195 TYR   A CZ  1 
ATOM   1295 O  OH  . TYR   A 1 189 ? -19.997 -16.267 -13.868 1.00 27.96  ? 195 TYR   A OH  1 
ATOM   1296 N  N   . ILE   A 1 190 ? -17.112 -11.055 -7.922  1.00 25.48  ? 196 ILE   A N   1 
ATOM   1297 C  CA  . ILE   A 1 190 ? -16.972 -10.453 -6.597  1.00 24.56  ? 196 ILE   A CA  1 
ATOM   1298 C  C   . ILE   A 1 190 ? -18.324 -10.456 -5.943  1.00 30.01  ? 196 ILE   A C   1 
ATOM   1299 O  O   . ILE   A 1 190 ? -19.277 -10.001 -6.564  1.00 30.21  ? 196 ILE   A O   1 
ATOM   1300 C  CB  . ILE   A 1 190 ? -16.371 -9.003  -6.617  1.00 27.66  ? 196 ILE   A CB  1 
ATOM   1301 C  CG1 . ILE   A 1 190 ? -14.954 -8.966  -7.225  1.00 27.58  ? 196 ILE   A CG1 1 
ATOM   1302 C  CG2 . ILE   A 1 190 ? -16.371 -8.367  -5.190  1.00 26.76  ? 196 ILE   A CG2 1 
ATOM   1303 C  CD1 . ILE   A 1 190 ? -14.506 -7.583  -7.689  1.00 29.02  ? 196 ILE   A CD1 1 
ATOM   1304 N  N   . GLY   A 1 191 ? -18.398 -10.935 -4.691  1.00 27.98  ? 197 GLY   A N   1 
ATOM   1305 C  CA  . GLY   A 1 191 ? -19.618 -10.891 -3.888  1.00 26.93  ? 197 GLY   A CA  1 
ATOM   1306 C  C   . GLY   A 1 191 ? -20.462 -12.139 -3.807  1.00 29.69  ? 197 GLY   A C   1 
ATOM   1307 O  O   . GLY   A 1 191 ? -21.556 -12.089 -3.242  1.00 28.96  ? 197 GLY   A O   1 
ATOM   1308 N  N   . LEU   A 1 192 ? -19.987 -13.260 -4.373  1.00 24.70  ? 198 LEU   A N   1 
ATOM   1309 C  CA  . LEU   A 1 192 ? -20.757 -14.507 -4.420  1.00 24.37  ? 198 LEU   A CA  1 
ATOM   1310 C  C   . LEU   A 1 192 ? -21.152 -15.018 -3.042  1.00 27.81  ? 198 LEU   A C   1 
ATOM   1311 O  O   . LEU   A 1 192 ? -20.330 -15.012 -2.141  1.00 27.64  ? 198 LEU   A O   1 
ATOM   1312 C  CB  . LEU   A 1 192 ? -20.003 -15.609 -5.193  1.00 24.08  ? 198 LEU   A CB  1 
ATOM   1313 C  CG  . LEU   A 1 192 ? -19.577 -15.281 -6.641  1.00 27.64  ? 198 LEU   A CG  1 
ATOM   1314 C  CD1 . LEU   A 1 192 ? -18.946 -16.509 -7.288  1.00 27.43  ? 198 LEU   A CD1 1 
ATOM   1315 C  CD2 . LEU   A 1 192 ? -20.761 -14.837 -7.461  1.00 26.00  ? 198 LEU   A CD2 1 
ATOM   1316 N  N   . ARG   A 1 193 ? -22.403 -15.485 -2.899  1.00 23.96  ? 199 ARG   A N   1 
ATOM   1317 C  CA  . ARG   A 1 193 ? -22.922 -16.047 -1.658  1.00 24.84  ? 199 ARG   A CA  1 
ATOM   1318 C  C   . ARG   A 1 193 ? -24.102 -17.024 -1.879  1.00 29.17  ? 199 ARG   A C   1 
ATOM   1319 O  O   . ARG   A 1 193 ? -24.534 -17.639 -0.924  1.00 30.66  ? 199 ARG   A O   1 
ATOM   1320 C  CB  . ARG   A 1 193 ? -23.258 -14.965 -0.606  1.00 25.77  ? 199 ARG   A CB  1 
ATOM   1321 C  CG  . ARG   A 1 193 ? -24.274 -13.932 -1.068  1.00 30.95  ? 199 ARG   A CG  1 
ATOM   1322 C  CD  . ARG   A 1 193 ? -24.271 -12.792 -0.073  1.00 32.19  ? 199 ARG   A CD  1 
ATOM   1323 N  NE  . ARG   A 1 193 ? -25.321 -11.813 -0.335  1.00 27.88  ? 199 ARG   A NE  1 
ATOM   1324 C  CZ  . ARG   A 1 193 ? -25.238 -10.802 -1.196  1.00 36.95  ? 199 ARG   A CZ  1 
ATOM   1325 N  NH1 . ARG   A 1 193 ? -24.131 -10.616 -1.916  1.00 26.21  ? 199 ARG   A NH1 1 
ATOM   1326 N  NH2 . ARG   A 1 193 ? -26.245 -9.943  -1.316  1.00 27.46  ? 199 ARG   A NH2 1 
ATOM   1327 N  N   . ASP   A 1 194 ? -24.561 -17.217 -3.119  1.00 26.34  ? 200 ASP   A N   1 
ATOM   1328 C  CA  . ASP   A 1 194 ? -25.666 -18.155 -3.421  1.00 27.33  ? 200 ASP   A CA  1 
ATOM   1329 C  C   . ASP   A 1 194 ? -25.376 -18.831 -4.766  1.00 32.24  ? 200 ASP   A C   1 
ATOM   1330 O  O   . ASP   A 1 194 ? -25.785 -18.364 -5.828  1.00 32.23  ? 200 ASP   A O   1 
ATOM   1331 C  CB  . ASP   A 1 194 ? -27.015 -17.396 -3.404  1.00 27.92  ? 200 ASP   A CB  1 
ATOM   1332 C  CG  . ASP   A 1 194 ? -28.229 -18.210 -3.782  1.00 36.02  ? 200 ASP   A CG  1 
ATOM   1333 O  OD1 . ASP   A 1 194 ? -28.124 -19.448 -3.813  1.00 38.50  ? 200 ASP   A OD1 1 
ATOM   1334 O  OD2 . ASP   A 1 194 ? -29.268 -17.602 -4.101  1.00 41.26  ? 200 ASP   A OD2 1 
ATOM   1335 N  N   . VAL   A 1 195 ? -24.604 -19.906 -4.692  1.00 28.96  ? 201 VAL   A N   1 
ATOM   1336 C  CA  . VAL   A 1 195 ? -24.063 -20.643 -5.824  1.00 27.86  ? 201 VAL   A CA  1 
ATOM   1337 C  C   . VAL   A 1 195 ? -24.631 -22.069 -5.832  1.00 30.15  ? 201 VAL   A C   1 
ATOM   1338 O  O   . VAL   A 1 195 ? -24.527 -22.789 -4.826  1.00 29.89  ? 201 VAL   A O   1 
ATOM   1339 C  CB  . VAL   A 1 195 ? -22.503 -20.641 -5.728  1.00 30.91  ? 201 VAL   A CB  1 
ATOM   1340 C  CG1 . VAL   A 1 195 ? -21.863 -21.338 -6.918  1.00 30.18  ? 201 VAL   A CG1 1 
ATOM   1341 C  CG2 . VAL   A 1 195 ? -21.946 -19.224 -5.579  1.00 31.00  ? 201 VAL   A CG2 1 
ATOM   1342 N  N   . ASP   A 1 196 ? -25.201 -22.484 -6.976  1.00 27.62  ? 202 ASP   A N   1 
ATOM   1343 C  CA  . ASP   A 1 196 ? -25.728 -23.848 -7.134  1.00 26.39  ? 202 ASP   A CA  1 
ATOM   1344 C  C   . ASP   A 1 196 ? -24.568 -24.846 -7.227  1.00 28.92  ? 202 ASP   A C   1 
ATOM   1345 O  O   . ASP   A 1 196 ? -23.477 -24.453 -7.659  1.00 28.21  ? 202 ASP   A O   1 
ATOM   1346 C  CB  . ASP   A 1 196 ? -26.625 -23.934 -8.382  1.00 28.15  ? 202 ASP   A CB  1 
ATOM   1347 C  CG  . ASP   A 1 196 ? -27.893 -23.107 -8.227  1.00 32.09  ? 202 ASP   A CG  1 
ATOM   1348 O  OD1 . ASP   A 1 196 ? -28.375 -22.975 -7.090  1.00 32.63  ? 202 ASP   A OD1 1 
ATOM   1349 O  OD2 . ASP   A 1 196 ? -28.379 -22.581 -9.232  1.00 31.59  ? 202 ASP   A OD2 1 
ATOM   1350 N  N   . PRO   A 1 197 ? -24.773 -26.119 -6.811  1.00 27.14  ? 203 PRO   A N   1 
ATOM   1351 C  CA  . PRO   A 1 197 ? -23.694 -27.124 -6.916  1.00 27.26  ? 203 PRO   A CA  1 
ATOM   1352 C  C   . PRO   A 1 197 ? -23.062 -27.224 -8.332  1.00 29.28  ? 203 PRO   A C   1 
ATOM   1353 O  O   . PRO   A 1 197 ? -21.834 -27.202 -8.401  1.00 27.82  ? 203 PRO   A O   1 
ATOM   1354 C  CB  . PRO   A 1 197 ? -24.388 -28.426 -6.471  1.00 28.38  ? 203 PRO   A CB  1 
ATOM   1355 C  CG  . PRO   A 1 197 ? -25.473 -27.976 -5.570  1.00 32.27  ? 203 PRO   A CG  1 
ATOM   1356 C  CD  . PRO   A 1 197 ? -26.001 -26.727 -6.240  1.00 27.45  ? 203 PRO   A CD  1 
ATOM   1357 N  N   . PRO   A 1 198 ? -23.803 -27.243 -9.472  1.00 27.91  ? 204 PRO   A N   1 
ATOM   1358 C  CA  . PRO   A 1 198 ? -23.110 -27.275 -10.777 1.00 27.41  ? 204 PRO   A CA  1 
ATOM   1359 C  C   . PRO   A 1 198 ? -22.273 -26.030 -11.046 1.00 29.76  ? 204 PRO   A C   1 
ATOM   1360 O  O   . PRO   A 1 198 ? -21.200 -26.139 -11.664 1.00 27.53  ? 204 PRO   A O   1 
ATOM   1361 C  CB  . PRO   A 1 198 ? -24.245 -27.388 -11.794 1.00 29.79  ? 204 PRO   A CB  1 
ATOM   1362 C  CG  . PRO   A 1 198 ? -25.468 -26.992 -11.085 1.00 35.16  ? 204 PRO   A CG  1 
ATOM   1363 C  CD  . PRO   A 1 198 ? -25.273 -27.309 -9.651  1.00 30.62  ? 204 PRO   A CD  1 
ATOM   1364 N  N   . GLU   A 1 199 ? -22.753 -24.853 -10.572 1.00 27.44  ? 205 GLU   A N   1 
ATOM   1365 C  CA  . GLU   A 1 199 ? -22.028 -23.578 -10.715 1.00 26.18  ? 205 GLU   A CA  1 
ATOM   1366 C  C   . GLU   A 1 199 ? -20.708 -23.622 -9.958  1.00 29.41  ? 205 GLU   A C   1 
ATOM   1367 O  O   . GLU   A 1 199 ? -19.692 -23.206 -10.511 1.00 28.21  ? 205 GLU   A O   1 
ATOM   1368 C  CB  . GLU   A 1 199 ? -22.864 -22.404 -10.238 1.00 27.69  ? 205 GLU   A CB  1 
ATOM   1369 C  CG  . GLU   A 1 199 ? -24.131 -22.184 -11.046 1.00 32.58  ? 205 GLU   A CG  1 
ATOM   1370 C  CD  . GLU   A 1 199 ? -24.831 -20.928 -10.581 1.00 36.94  ? 205 GLU   A CD  1 
ATOM   1371 O  OE1 . GLU   A 1 199 ? -25.337 -20.930 -9.438  1.00 30.22  ? 205 GLU   A OE1 1 
ATOM   1372 O  OE2 . GLU   A 1 199 ? -24.754 -19.908 -11.301 1.00 28.74  ? 205 GLU   A OE2 1 
ATOM   1373 N  N   . HIS   A 1 200 ? -20.706 -24.182 -8.735  1.00 26.46  ? 206 HIS   A N   1 
ATOM   1374 C  CA  . HIS   A 1 200 ? -19.492 -24.318 -7.932  1.00 27.03  ? 206 HIS   A CA  1 
ATOM   1375 C  C   . HIS   A 1 200 ? -18.508 -25.204 -8.687  1.00 28.34  ? 206 HIS   A C   1 
ATOM   1376 O  O   . HIS   A 1 200 ? -17.336 -24.849 -8.786  1.00 27.50  ? 206 HIS   A O   1 
ATOM   1377 C  CB  . HIS   A 1 200 ? -19.778 -24.860 -6.527  1.00 28.13  ? 206 HIS   A CB  1 
ATOM   1378 C  CG  . HIS   A 1 200 ? -18.524 -25.057 -5.726  1.00 32.35  ? 206 HIS   A CG  1 
ATOM   1379 N  ND1 . HIS   A 1 200 ? -17.915 -26.305 -5.631  1.00 34.42  ? 206 HIS   A ND1 1 
ATOM   1380 C  CD2 . HIS   A 1 200 ? -17.754 -24.147 -5.086  1.00 34.11  ? 206 HIS   A CD2 1 
ATOM   1381 C  CE1 . HIS   A 1 200 ? -16.818 -26.115 -4.905  1.00 33.69  ? 206 HIS   A CE1 1 
ATOM   1382 N  NE2 . HIS   A 1 200 ? -16.678 -24.845 -4.550  1.00 34.14  ? 206 HIS   A NE2 1 
ATOM   1383 N  N   . PHE   A 1 201 ? -18.996 -26.317 -9.267  1.00 25.17  ? 207 PHE   A N   1 
ATOM   1384 C  CA  . PHE   A 1 201 ? -18.168 -27.184 -10.108 1.00 24.97  ? 207 PHE   A CA  1 
ATOM   1385 C  C   . PHE   A 1 201 ? -17.561 -26.430 -11.285 1.00 27.35  ? 207 PHE   A C   1 
ATOM   1386 O  O   . PHE   A 1 201 ? -16.346 -26.518 -11.500 1.00 26.50  ? 207 PHE   A O   1 
ATOM   1387 C  CB  . PHE   A 1 201 ? -18.906 -28.436 -10.588 1.00 27.43  ? 207 PHE   A CB  1 
ATOM   1388 C  CG  . PHE   A 1 201 ? -18.065 -29.306 -11.500 1.00 28.18  ? 207 PHE   A CG  1 
ATOM   1389 C  CD1 . PHE   A 1 201 ? -17.092 -30.151 -10.978 1.00 31.36  ? 207 PHE   A CD1 1 
ATOM   1390 C  CD2 . PHE   A 1 201 ? -18.206 -29.235 -12.886 1.00 29.58  ? 207 PHE   A CD2 1 
ATOM   1391 C  CE1 . PHE   A 1 201 ? -16.332 -30.970 -11.822 1.00 30.86  ? 207 PHE   A CE1 1 
ATOM   1392 C  CE2 . PHE   A 1 201 ? -17.451 -30.053 -13.722 1.00 30.75  ? 207 PHE   A CE2 1 
ATOM   1393 C  CZ  . PHE   A 1 201 ? -16.511 -30.908 -13.185 1.00 28.89  ? 207 PHE   A CZ  1 
ATOM   1394 N  N   . ILE   A 1 202 ? -18.378 -25.668 -12.021 1.00 23.16  ? 208 ILE   A N   1 
ATOM   1395 C  CA  . ILE   A 1 202 ? -17.927 -24.869 -13.161 1.00 22.93  ? 208 ILE   A CA  1 
ATOM   1396 C  C   . ILE   A 1 202 ? -16.812 -23.884 -12.743 1.00 28.15  ? 208 ILE   A C   1 
ATOM   1397 O  O   . ILE   A 1 202 ? -15.746 -23.864 -13.376 1.00 27.07  ? 208 ILE   A O   1 
ATOM   1398 C  CB  . ILE   A 1 202 ? -19.086 -24.169 -13.921 1.00 24.71  ? 208 ILE   A CB  1 
ATOM   1399 C  CG1 . ILE   A 1 202 ? -19.919 -25.201 -14.713 1.00 24.97  ? 208 ILE   A CG1 1 
ATOM   1400 C  CG2 . ILE   A 1 202 ? -18.542 -23.095 -14.918 1.00 22.56  ? 208 ILE   A CG2 1 
ATOM   1401 C  CD1 . ILE   A 1 202 ? -21.404 -24.648 -14.974 1.00 29.01  ? 208 ILE   A CD1 1 
ATOM   1402 N  N   . LEU   A 1 203 ? -17.028 -23.131 -11.651 1.00 24.43  ? 209 LEU   A N   1 
ATOM   1403 C  CA  . LEU   A 1 203 ? -16.013 -22.168 -11.183 1.00 23.13  ? 209 LEU   A CA  1 
ATOM   1404 C  C   . LEU   A 1 203 ? -14.681 -22.855 -10.859 1.00 26.32  ? 209 LEU   A C   1 
ATOM   1405 O  O   . LEU   A 1 203 ? -13.642 -22.426 -11.366 1.00 27.12  ? 209 LEU   A O   1 
ATOM   1406 C  CB  . LEU   A 1 203 ? -16.503 -21.367 -9.980  1.00 23.12  ? 209 LEU   A CB  1 
ATOM   1407 C  CG  . LEU   A 1 203 ? -17.734 -20.477 -10.189 1.00 28.44  ? 209 LEU   A CG  1 
ATOM   1408 C  CD1 . LEU   A 1 203 ? -18.223 -19.914 -8.831  1.00 29.51  ? 209 LEU   A CD1 1 
ATOM   1409 C  CD2 . LEU   A 1 203 ? -17.447 -19.355 -11.186 1.00 28.93  ? 209 LEU   A CD2 1 
ATOM   1410 N  N   . LYS   A 1 204 ? -14.726 -23.930 -10.070 1.00 25.09  ? 210 LYS   A N   1 
ATOM   1411 C  CA  . LYS   A 1 204 ? -13.527 -24.670 -9.649  1.00 25.98  ? 210 LYS   A CA  1 
ATOM   1412 C  C   . LYS   A 1 204 ? -12.853 -25.403 -10.798 1.00 29.12  ? 210 LYS   A C   1 
ATOM   1413 O  O   . LYS   A 1 204 ? -11.631 -25.325 -10.970 1.00 27.22  ? 210 LYS   A O   1 
ATOM   1414 C  CB  . LYS   A 1 204 ? -13.852 -25.660 -8.490  1.00 27.86  ? 210 LYS   A CB  1 
ATOM   1415 C  CG  . LYS   A 1 204 ? -14.166 -24.982 -7.156  1.00 42.03  ? 210 LYS   A CG  1 
ATOM   1416 C  CD  . LYS   A 1 204 ? -12.914 -24.393 -6.470  1.00 53.62  ? 210 LYS   A CD  1 
ATOM   1417 C  CE  . LYS   A 1 204 ? -13.205 -23.887 -5.079  1.00 60.36  ? 210 LYS   A CE  1 
ATOM   1418 N  NZ  . LYS   A 1 204 ? -11.961 -23.567 -4.333  1.00 71.98  ? 210 LYS   A NZ  1 
ATOM   1419 N  N   . ASN   A 1 205 ? -13.645 -26.159 -11.552 1.00 27.14  ? 211 ASN   A N   1 
ATOM   1420 C  CA  . ASN   A 1 205 ? -13.137 -26.993 -12.625 1.00 27.53  ? 211 ASN   A CA  1 
ATOM   1421 C  C   . ASN   A 1 205 ? -12.458 -26.217 -13.740 1.00 30.30  ? 211 ASN   A C   1 
ATOM   1422 O  O   . ASN   A 1 205 ? -11.441 -26.667 -14.262 1.00 29.89  ? 211 ASN   A O   1 
ATOM   1423 C  CB  . ASN   A 1 205 ? -14.246 -27.864 -13.172 1.00 28.45  ? 211 ASN   A CB  1 
ATOM   1424 C  CG  . ASN   A 1 205 ? -13.757 -28.860 -14.164 1.00 29.54  ? 211 ASN   A CG  1 
ATOM   1425 O  OD1 . ASN   A 1 205 ? -13.077 -29.833 -13.810 1.00 27.59  ? 211 ASN   A OD1 1 
ATOM   1426 N  ND2 . ASN   A 1 205 ? -14.083 -28.617 -15.422 1.00 24.62  ? 211 ASN   A ND2 1 
ATOM   1427 N  N   . TYR   A 1 206 ? -12.991 -25.039 -14.069 1.00 27.16  ? 212 TYR   A N   1 
ATOM   1428 C  CA  . TYR   A 1 206 ? -12.463 -24.237 -15.164 1.00 27.44  ? 212 TYR   A CA  1 
ATOM   1429 C  C   . TYR   A 1 206 ? -11.545 -23.114 -14.698 1.00 31.84  ? 212 TYR   A C   1 
ATOM   1430 O  O   . TYR   A 1 206 ? -11.144 -22.272 -15.496 1.00 32.00  ? 212 TYR   A O   1 
ATOM   1431 C  CB  . TYR   A 1 206 ? -13.609 -23.741 -16.049 1.00 27.72  ? 212 TYR   A CB  1 
ATOM   1432 C  CG  . TYR   A 1 206 ? -14.257 -24.877 -16.811 1.00 27.02  ? 212 TYR   A CG  1 
ATOM   1433 C  CD1 . TYR   A 1 206 ? -13.652 -25.416 -17.944 1.00 28.83  ? 212 TYR   A CD1 1 
ATOM   1434 C  CD2 . TYR   A 1 206 ? -15.448 -25.453 -16.368 1.00 26.64  ? 212 TYR   A CD2 1 
ATOM   1435 C  CE1 . TYR   A 1 206 ? -14.232 -26.469 -18.642 1.00 29.59  ? 212 TYR   A CE1 1 
ATOM   1436 C  CE2 . TYR   A 1 206 ? -16.037 -26.512 -17.059 1.00 26.92  ? 212 TYR   A CE2 1 
ATOM   1437 C  CZ  . TYR   A 1 206 ? -15.428 -27.012 -18.197 1.00 28.61  ? 212 TYR   A CZ  1 
ATOM   1438 O  OH  . TYR   A 1 206 ? -15.972 -28.066 -18.875 1.00 30.09  ? 212 TYR   A OH  1 
ATOM   1439 N  N   . ASP   A 1 207 ? -11.195 -23.123 -13.414 1.00 30.99  ? 213 ASP   A N   1 
ATOM   1440 C  CA  . ASP   A 1 207 ? -10.298 -22.138 -12.800 1.00 32.02  ? 213 ASP   A CA  1 
ATOM   1441 C  C   . ASP   A 1 207 ? -10.775 -20.701 -12.933 1.00 33.36  ? 213 ASP   A C   1 
ATOM   1442 O  O   . ASP   A 1 207 ? -9.957  -19.813 -13.172 1.00 32.29  ? 213 ASP   A O   1 
ATOM   1443 C  CB  . ASP   A 1 207 ? -8.886  -22.265 -13.391 1.00 34.74  ? 213 ASP   A CB  1 
ATOM   1444 C  CG  . ASP   A 1 207 ? -8.356  -23.660 -13.321 1.00 48.59  ? 213 ASP   A CG  1 
ATOM   1445 O  OD1 . ASP   A 1 207 ? -8.247  -24.186 -12.205 1.00 47.87  ? 213 ASP   A OD1 1 
ATOM   1446 O  OD2 . ASP   A 1 207 ? -8.089  -24.244 -14.395 1.00 60.99  ? 213 ASP   A OD2 1 
ATOM   1447 N  N   . ILE   A 1 208 ? -12.086 -20.468 -12.817 1.00 28.16  ? 214 ILE   A N   1 
ATOM   1448 C  CA  . ILE   A 1 208 ? -12.634 -19.118 -12.891 1.00 26.62  ? 214 ILE   A CA  1 
ATOM   1449 C  C   . ILE   A 1 208 ? -12.441 -18.501 -11.514 1.00 30.52  ? 214 ILE   A C   1 
ATOM   1450 O  O   . ILE   A 1 208 ? -12.894 -19.054 -10.514 1.00 29.33  ? 214 ILE   A O   1 
ATOM   1451 C  CB  . ILE   A 1 208 ? -14.111 -19.071 -13.354 1.00 29.44  ? 214 ILE   A CB  1 
ATOM   1452 C  CG1 . ILE   A 1 208 ? -14.291 -19.793 -14.711 1.00 30.58  ? 214 ILE   A CG1 1 
ATOM   1453 C  CG2 . ILE   A 1 208 ? -14.591 -17.612 -13.413 1.00 27.03  ? 214 ILE   A CG2 1 
ATOM   1454 C  CD1 . ILE   A 1 208 ? -15.722 -20.152 -15.068 1.00 32.99  ? 214 ILE   A CD1 1 
ATOM   1455 N  N   . GLN   A 1 209 ? -11.729 -17.368 -11.467 1.00 26.40  ? 215 GLN   A N   1 
ATOM   1456 C  CA  . GLN   A 1 209 ? -11.437 -16.722 -10.215 1.00 27.17  ? 215 GLN   A CA  1 
ATOM   1457 C  C   . GLN   A 1 209 ? -12.620 -15.967 -9.645  1.00 28.97  ? 215 GLN   A C   1 
ATOM   1458 O  O   . GLN   A 1 209 ? -13.351 -15.295 -10.361 1.00 27.47  ? 215 GLN   A O   1 
ATOM   1459 C  CB  . GLN   A 1 209 ? -10.191 -15.845 -10.329 1.00 28.31  ? 215 GLN   A CB  1 
ATOM   1460 C  CG  . GLN   A 1 209 ? -8.982  -16.632 -10.878 1.00 33.46  ? 215 GLN   A CG  1 
ATOM   1461 C  CD  . GLN   A 1 209 ? -8.541  -17.757 -9.968  1.00 48.58  ? 215 GLN   A CD  1 
ATOM   1462 O  OE1 . GLN   A 1 209 ? -8.289  -17.562 -8.778  1.00 49.45  ? 215 GLN   A OE1 1 
ATOM   1463 N  NE2 . GLN   A 1 209 ? -8.440  -18.957 -10.512 1.00 36.28  ? 215 GLN   A NE2 1 
ATOM   1464 N  N   . TYR   A 1 210 ? -12.824 -16.125 -8.339  1.00 26.43  ? 216 TYR   A N   1 
ATOM   1465 C  CA  . TYR   A 1 210 ? -13.920 -15.447 -7.687  1.00 26.07  ? 216 TYR   A CA  1 
ATOM   1466 C  C   . TYR   A 1 210 ? -13.522 -15.019 -6.298  1.00 29.26  ? 216 TYR   A C   1 
ATOM   1467 O  O   . TYR   A 1 210 ? -12.630 -15.613 -5.689  1.00 29.20  ? 216 TYR   A O   1 
ATOM   1468 C  CB  . TYR   A 1 210 ? -15.218 -16.308 -7.696  1.00 25.94  ? 216 TYR   A CB  1 
ATOM   1469 C  CG  . TYR   A 1 210 ? -15.148 -17.608 -6.921  1.00 25.66  ? 216 TYR   A CG  1 
ATOM   1470 C  CD1 . TYR   A 1 210 ? -15.464 -17.651 -5.563  1.00 27.07  ? 216 TYR   A CD1 1 
ATOM   1471 C  CD2 . TYR   A 1 210 ? -14.761 -18.795 -7.543  1.00 26.98  ? 216 TYR   A CD2 1 
ATOM   1472 C  CE1 . TYR   A 1 210 ? -15.374 -18.838 -4.837  1.00 29.61  ? 216 TYR   A CE1 1 
ATOM   1473 C  CE2 . TYR   A 1 210 ? -14.730 -20.005 -6.840  1.00 29.25  ? 216 TYR   A CE2 1 
ATOM   1474 C  CZ  . TYR   A 1 210 ? -15.018 -20.015 -5.480  1.00 35.61  ? 216 TYR   A CZ  1 
ATOM   1475 O  OH  . TYR   A 1 210 ? -14.981 -21.187 -4.769  1.00 34.91  ? 216 TYR   A OH  1 
ATOM   1476 N  N   . PHE   A 1 211 ? -14.167 -13.971 -5.819  1.00 24.70  ? 217 PHE   A N   1 
ATOM   1477 C  CA  . PHE   A 1 211 ? -13.999 -13.457 -4.468  1.00 24.11  ? 217 PHE   A CA  1 
ATOM   1478 C  C   . PHE   A 1 211 ? -15.382 -13.455 -3.886  1.00 29.14  ? 217 PHE   A C   1 
ATOM   1479 O  O   . PHE   A 1 211 ? -16.173 -12.548 -4.149  1.00 29.21  ? 217 PHE   A O   1 
ATOM   1480 C  CB  . PHE   A 1 211 ? -13.332 -12.073 -4.469  1.00 26.21  ? 217 PHE   A CB  1 
ATOM   1481 C  CG  . PHE   A 1 211 ? -11.928 -12.161 -5.019  1.00 28.24  ? 217 PHE   A CG  1 
ATOM   1482 C  CD1 . PHE   A 1 211 ? -10.880 -12.611 -4.222  1.00 31.61  ? 217 PHE   A CD1 1 
ATOM   1483 C  CD2 . PHE   A 1 211 ? -11.669 -11.887 -6.365  1.00 29.64  ? 217 PHE   A CD2 1 
ATOM   1484 C  CE1 . PHE   A 1 211 ? -9.589  -12.744 -4.745  1.00 32.02  ? 217 PHE   A CE1 1 
ATOM   1485 C  CE2 . PHE   A 1 211 ? -10.382 -12.042 -6.891  1.00 32.54  ? 217 PHE   A CE2 1 
ATOM   1486 C  CZ  . PHE   A 1 211 ? -9.351  -12.474 -6.079  1.00 31.43  ? 217 PHE   A CZ  1 
ATOM   1487 N  N   . SER   A 1 212 ? -15.720 -14.561 -3.182  1.00 26.23  ? 218 SER   A N   1 
ATOM   1488 C  CA  . SER   A 1 212 ? -17.028 -14.690 -2.539  1.00 26.11  ? 218 SER   A CA  1 
ATOM   1489 C  C   . SER   A 1 212 ? -17.082 -13.753 -1.312  1.00 29.69  ? 218 SER   A C   1 
ATOM   1490 O  O   . SER   A 1 212 ? -16.052 -13.193 -0.918  1.00 28.19  ? 218 SER   A O   1 
ATOM   1491 C  CB  . SER   A 1 212 ? -17.236 -16.133 -2.087  1.00 29.20  ? 218 SER   A CB  1 
ATOM   1492 O  OG  . SER   A 1 212 ? -16.477 -16.436 -0.923  1.00 30.53  ? 218 SER   A OG  1 
ATOM   1493 N  N   . MET   A 1 213 ? -18.262 -13.620 -0.679  1.00 26.95  ? 219 MET   A N   1 
ATOM   1494 C  CA  . MET   A 1 213 ? -18.369 -12.859 0.572   1.00 26.76  ? 219 MET   A CA  1 
ATOM   1495 C  C   . MET   A 1 213 ? -17.386 -13.383 1.624   1.00 31.57  ? 219 MET   A C   1 
ATOM   1496 O  O   . MET   A 1 213 ? -16.828 -12.581 2.355   1.00 31.60  ? 219 MET   A O   1 
ATOM   1497 C  CB  . MET   A 1 213 ? -19.801 -12.877 1.133   1.00 28.11  ? 219 MET   A CB  1 
ATOM   1498 C  CG  . MET   A 1 213 ? -20.799 -12.157 0.250   1.00 29.17  ? 219 MET   A CG  1 
ATOM   1499 S  SD  . MET   A 1 213 ? -20.366 -10.505 -0.331  1.00 31.31  ? 219 MET   A SD  1 
ATOM   1500 C  CE  . MET   A 1 213 ? -20.018 -9.656  1.208   1.00 28.82  ? 219 MET   A CE  1 
ATOM   1501 N  N   . ARG   A 1 214 ? -17.136 -14.713 1.658   1.00 29.10  ? 220 ARG   A N   1 
ATOM   1502 C  CA  . ARG   A 1 214 ? -16.156 -15.318 2.561   1.00 28.05  ? 220 ARG   A CA  1 
ATOM   1503 C  C   . ARG   A 1 214 ? -14.746 -14.785 2.239   1.00 29.35  ? 220 ARG   A C   1 
ATOM   1504 O  O   . ARG   A 1 214 ? -14.049 -14.371 3.152   1.00 28.92  ? 220 ARG   A O   1 
ATOM   1505 C  CB  . ARG   A 1 214 ? -16.209 -16.842 2.475   1.00 30.62  ? 220 ARG   A CB  1 
ATOM   1506 C  CG  . ARG   A 1 214 ? -15.200 -17.514 3.381   1.00 27.24  ? 220 ARG   A CG  1 
ATOM   1507 C  CD  . ARG   A 1 214 ? -15.233 -18.997 3.232   1.00 31.36  ? 220 ARG   A CD  1 
ATOM   1508 N  NE  . ARG   A 1 214 ? -13.954 -19.524 3.683   1.00 31.95  ? 220 ARG   A NE  1 
ATOM   1509 C  CZ  . ARG   A 1 214 ? -13.690 -19.948 4.907   1.00 42.07  ? 220 ARG   A CZ  1 
ATOM   1510 N  NH1 . ARG   A 1 214 ? -14.645 -19.964 5.832   1.00 36.86  ? 220 ARG   A NH1 1 
ATOM   1511 N  NH2 . ARG   A 1 214 ? -12.471 -20.378 5.217   1.00 34.13  ? 220 ARG   A NH2 1 
ATOM   1512 N  N   . ASP   A 1 215 ? -14.347 -14.749 0.948   1.00 25.31  ? 221 ASP   A N   1 
ATOM   1513 C  CA  . ASP   A 1 215 ? -13.036 -14.179 0.544   1.00 23.98  ? 221 ASP   A CA  1 
ATOM   1514 C  C   . ASP   A 1 215 ? -12.907 -12.715 0.959   1.00 28.40  ? 221 ASP   A C   1 
ATOM   1515 O  O   . ASP   A 1 215 ? -11.839 -12.298 1.375   1.00 28.92  ? 221 ASP   A O   1 
ATOM   1516 C  CB  . ASP   A 1 215 ? -12.811 -14.344 -0.985  1.00 24.71  ? 221 ASP   A CB  1 
ATOM   1517 C  CG  . ASP   A 1 215 ? -12.737 -15.817 -1.400  1.00 35.98  ? 221 ASP   A CG  1 
ATOM   1518 O  OD1 . ASP   A 1 215 ? -11.988 -16.577 -0.757  1.00 37.11  ? 221 ASP   A OD1 1 
ATOM   1519 O  OD2 . ASP   A 1 215 ? -13.423 -16.200 -2.365  1.00 34.00  ? 221 ASP   A OD2 1 
ATOM   1520 N  N   . ILE   A 1 216 ? -13.992 -11.923 0.845   1.00 26.06  ? 222 ILE   A N   1 
ATOM   1521 C  CA  . ILE   A 1 216 ? -13.989 -10.506 1.223   1.00 26.54  ? 222 ILE   A CA  1 
ATOM   1522 C  C   . ILE   A 1 216 ? -13.807 -10.394 2.745   1.00 29.40  ? 222 ILE   A C   1 
ATOM   1523 O  O   . ILE   A 1 216 ? -13.072 -9.517  3.210   1.00 29.93  ? 222 ILE   A O   1 
ATOM   1524 C  CB  . ILE   A 1 216 ? -15.276 -9.773  0.733   1.00 28.87  ? 222 ILE   A CB  1 
ATOM   1525 C  CG1 . ILE   A 1 216 ? -15.352 -9.775  -0.825  1.00 28.76  ? 222 ILE   A CG1 1 
ATOM   1526 C  CG2 . ILE   A 1 216 ? -15.328 -8.323  1.309   1.00 29.77  ? 222 ILE   A CG2 1 
ATOM   1527 C  CD1 . ILE   A 1 216 ? -16.705 -9.282  -1.431  1.00 31.44  ? 222 ILE   A CD1 1 
ATOM   1528 N  N   . ASP   A 1 217 ? -14.488 -11.276 3.510   1.00 26.30  ? 223 ASP   A N   1 
ATOM   1529 C  CA  . ASP   A 1 217 ? -14.411 -11.323 4.986   1.00 25.78  ? 223 ASP   A CA  1 
ATOM   1530 C  C   . ASP   A 1 217 ? -12.974 -11.554 5.431   1.00 31.62  ? 223 ASP   A C   1 
ATOM   1531 O  O   . ASP   A 1 217 ? -12.544 -10.927 6.393   1.00 33.45  ? 223 ASP   A O   1 
ATOM   1532 C  CB  . ASP   A 1 217 ? -15.289 -12.447 5.557   1.00 26.36  ? 223 ASP   A CB  1 
ATOM   1533 C  CG  . ASP   A 1 217 ? -16.779 -12.263 5.379   1.00 33.83  ? 223 ASP   A CG  1 
ATOM   1534 O  OD1 . ASP   A 1 217 ? -17.221 -11.102 5.235   1.00 34.23  ? 223 ASP   A OD1 1 
ATOM   1535 O  OD2 . ASP   A 1 217 ? -17.507 -13.286 5.366   1.00 33.67  ? 223 ASP   A OD2 1 
ATOM   1536 N  N   . ARG   A 1 218 ? -12.244 -12.441 4.732   1.00 27.42  ? 224 ARG   A N   1 
ATOM   1537 C  CA  . ARG   A 1 218 ? -10.851 -12.790 5.020   1.00 26.93  ? 224 ARG   A CA  1 
ATOM   1538 C  C   . ARG   A 1 218 ? -9.834  -11.749 4.565   1.00 32.35  ? 224 ARG   A C   1 
ATOM   1539 O  O   . ARG   A 1 218 ? -9.006  -11.296 5.364   1.00 31.68  ? 224 ARG   A O   1 
ATOM   1540 C  CB  . ARG   A 1 218 ? -10.498 -14.131 4.381   1.00 27.41  ? 224 ARG   A CB  1 
ATOM   1541 C  CG  . ARG   A 1 218 ? -11.254 -15.325 4.951   1.00 35.34  ? 224 ARG   A CG  1 
ATOM   1542 C  CD  . ARG   A 1 218 ? -11.041 -16.596 4.135   1.00 41.96  ? 224 ARG   A CD  1 
ATOM   1543 N  NE  . ARG   A 1 218 ? -9.619  -16.884 3.907   1.00 39.16  ? 224 ARG   A NE  1 
ATOM   1544 C  CZ  . ARG   A 1 218 ? -8.846  -17.599 4.719   1.00 52.59  ? 224 ARG   A CZ  1 
ATOM   1545 N  NH1 . ARG   A 1 218 ? -9.341  -18.114 5.839   1.00 40.87  ? 224 ARG   A NH1 1 
ATOM   1546 N  NH2 . ARG   A 1 218 ? -7.568  -17.796 4.422   1.00 42.93  ? 224 ARG   A NH2 1 
ATOM   1547 N  N   . LEU   A 1 219 ? -9.877  -11.389 3.271   1.00 28.97  ? 225 LEU   A N   1 
ATOM   1548 C  CA  . LEU   A 1 219 ? -8.914  -10.480 2.628   1.00 28.35  ? 225 LEU   A CA  1 
ATOM   1549 C  C   . LEU   A 1 219 ? -9.194  -9.025  2.810   1.00 31.79  ? 225 LEU   A C   1 
ATOM   1550 O  O   . LEU   A 1 219 ? -8.263  -8.226  2.903   1.00 31.13  ? 225 LEU   A O   1 
ATOM   1551 C  CB  . LEU   A 1 219 ? -8.857  -10.792 1.109   1.00 28.32  ? 225 LEU   A CB  1 
ATOM   1552 C  CG  . LEU   A 1 219 ? -8.294  -12.165 0.705   1.00 33.94  ? 225 LEU   A CG  1 
ATOM   1553 C  CD1 . LEU   A 1 219 ? -8.526  -12.439 -0.780  1.00 33.93  ? 225 LEU   A CD1 1 
ATOM   1554 C  CD2 . LEU   A 1 219 ? -6.788  -12.267 1.006   1.00 37.48  ? 225 LEU   A CD2 1 
ATOM   1555 N  N   . GLY   A 1 220 ? -10.464 -8.665  2.772   1.00 28.88  ? 226 GLY   A N   1 
ATOM   1556 C  CA  . GLY   A 1 220 ? -10.867 -7.270  2.784   1.00 29.83  ? 226 GLY   A CA  1 
ATOM   1557 C  C   . GLY   A 1 220 ? -11.003 -6.806  1.344   1.00 31.37  ? 226 GLY   A C   1 
ATOM   1558 O  O   . GLY   A 1 220 ? -10.333 -7.331  0.456   1.00 29.01  ? 226 GLY   A O   1 
ATOM   1559 N  N   . ILE   A 1 221 ? -11.852 -5.813  1.099   1.00 29.28  ? 227 ILE   A N   1 
ATOM   1560 C  CA  . ILE   A 1 221 ? -12.142 -5.341  -0.267  1.00 28.90  ? 227 ILE   A CA  1 
ATOM   1561 C  C   . ILE   A 1 221 ? -10.906 -4.717  -0.977  1.00 31.71  ? 227 ILE   A C   1 
ATOM   1562 O  O   . ILE   A 1 221 ? -10.824 -4.808  -2.204  1.00 30.37  ? 227 ILE   A O   1 
ATOM   1563 C  CB  . ILE   A 1 221 ? -13.401 -4.415  -0.299  1.00 32.08  ? 227 ILE   A CB  1 
ATOM   1564 C  CG1 . ILE   A 1 221 ? -14.016 -4.347  -1.723  1.00 32.50  ? 227 ILE   A CG1 1 
ATOM   1565 C  CG2 . ILE   A 1 221 ? -13.168 -3.005  0.303   1.00 32.40  ? 227 ILE   A CG2 1 
ATOM   1566 C  CD1 . ILE   A 1 221 ? -14.750 -5.678  -2.186  1.00 37.68  ? 227 ILE   A CD1 1 
ATOM   1567 N  N   . GLN   A 1 222 ? -9.923  -4.161  -0.220  1.00 30.17  ? 228 GLN   A N   1 
ATOM   1568 C  CA  . GLN   A 1 222 ? -8.744  -3.566  -0.861  1.00 30.13  ? 228 GLN   A CA  1 
ATOM   1569 C  C   . GLN   A 1 222 ? -7.952  -4.634  -1.572  1.00 33.34  ? 228 GLN   A C   1 
ATOM   1570 O  O   . GLN   A 1 222 ? -7.731  -4.497  -2.775  1.00 31.64  ? 228 GLN   A O   1 
ATOM   1571 C  CB  . GLN   A 1 222 ? -7.855  -2.758  0.111   1.00 31.97  ? 228 GLN   A CB  1 
ATOM   1572 C  CG  . GLN   A 1 222 ? -6.581  -2.186  -0.567  1.00 31.95  ? 228 GLN   A CG  1 
ATOM   1573 C  CD  . GLN   A 1 222 ? -5.452  -1.780  0.354   1.00 51.73  ? 228 GLN   A CD  1 
ATOM   1574 O  OE1 . GLN   A 1 222 ? -4.293  -1.663  -0.063  1.00 48.80  ? 228 GLN   A OE1 1 
ATOM   1575 N  NE2 . GLN   A 1 222 ? -5.738  -1.554  1.622   1.00 42.61  ? 228 GLN   A NE2 1 
ATOM   1576 N  N   . LYS   A 1 223 ? -7.587  -5.723  -0.861  1.00 29.48  ? 229 LYS   A N   1 
ATOM   1577 C  CA  . LYS   A 1 223 ? -6.850  -6.846  -1.436  1.00 28.73  ? 229 LYS   A CA  1 
ATOM   1578 C  C   . LYS   A 1 223 ? -7.655  -7.540  -2.524  1.00 31.66  ? 229 LYS   A C   1 
ATOM   1579 O  O   . LYS   A 1 223 ? -7.072  -7.958  -3.515  1.00 32.77  ? 229 LYS   A O   1 
ATOM   1580 C  CB  . LYS   A 1 223 ? -6.393  -7.840  -0.350  1.00 31.36  ? 229 LYS   A CB  1 
ATOM   1581 C  CG  . LYS   A 1 223 ? -5.095  -7.416  0.330   1.00 51.80  ? 229 LYS   A CG  1 
ATOM   1582 C  CD  . LYS   A 1 223 ? -4.662  -8.408  1.413   1.00 67.58  ? 229 LYS   A CD  1 
ATOM   1583 C  CE  . LYS   A 1 223 ? -4.080  -7.731  2.637   1.00 77.49  ? 229 LYS   A CE  1 
ATOM   1584 N  NZ  . LYS   A 1 223 ? -2.713  -7.203  2.391   1.00 90.92  ? 229 LYS   A NZ  1 
ATOM   1585 N  N   . VAL   A 1 224 ? -8.993  -7.605  -2.376  1.00 27.80  ? 230 VAL   A N   1 
ATOM   1586 C  CA  . VAL   A 1 224 ? -9.867  -8.197  -3.388  1.00 27.24  ? 230 VAL   A CA  1 
ATOM   1587 C  C   . VAL   A 1 224 ? -9.750  -7.415  -4.706  1.00 30.53  ? 230 VAL   A C   1 
ATOM   1588 O  O   . VAL   A 1 224 ? -9.632  -8.038  -5.749  1.00 30.50  ? 230 VAL   A O   1 
ATOM   1589 C  CB  . VAL   A 1 224 ? -11.342 -8.332  -2.902  1.00 30.64  ? 230 VAL   A CB  1 
ATOM   1590 C  CG1 . VAL   A 1 224 ? -12.299 -8.516  -4.077  1.00 30.81  ? 230 VAL   A CG1 1 
ATOM   1591 C  CG2 . VAL   A 1 224 ? -11.490 -9.488  -1.896  1.00 30.11  ? 230 VAL   A CG2 1 
ATOM   1592 N  N   . MET   A 1 225 ? -9.746  -6.065  -4.652  1.00 29.13  ? 231 MET   A N   1 
ATOM   1593 C  CA  . MET   A 1 225 ? -9.650  -5.238  -5.866  1.00 28.51  ? 231 MET   A CA  1 
ATOM   1594 C  C   . MET   A 1 225 ? -8.281  -5.319  -6.500  1.00 34.26  ? 231 MET   A C   1 
ATOM   1595 O  O   . MET   A 1 225 ? -8.204  -5.387  -7.729  1.00 34.16  ? 231 MET   A O   1 
ATOM   1596 C  CB  . MET   A 1 225 ? -10.095 -3.778  -5.641  1.00 29.48  ? 231 MET   A CB  1 
ATOM   1597 C  CG  . MET   A 1 225 ? -11.572 -3.612  -5.345  1.00 31.19  ? 231 MET   A CG  1 
ATOM   1598 S  SD  . MET   A 1 225 ? -12.726 -4.706  -6.238  1.00 33.85  ? 231 MET   A SD  1 
ATOM   1599 C  CE  . MET   A 1 225 ? -12.454 -4.205  -7.943  1.00 30.92  ? 231 MET   A CE  1 
ATOM   1600 N  N   . GLU   A 1 226 ? -7.207  -5.368  -5.674  1.00 31.94  ? 232 GLU   A N   1 
ATOM   1601 C  CA  . GLU   A 1 226 ? -5.814  -5.526  -6.137  1.00 31.74  ? 232 GLU   A CA  1 
ATOM   1602 C  C   . GLU   A 1 226 ? -5.598  -6.845  -6.886  1.00 35.58  ? 232 GLU   A C   1 
ATOM   1603 O  O   . GLU   A 1 226 ? -4.968  -6.873  -7.956  1.00 33.62  ? 232 GLU   A O   1 
ATOM   1604 C  CB  . GLU   A 1 226 ? -4.845  -5.478  -4.946  1.00 33.62  ? 232 GLU   A CB  1 
ATOM   1605 C  CG  . GLU   A 1 226 ? -4.392  -4.085  -4.560  1.00 42.14  ? 232 GLU   A CG  1 
ATOM   1606 C  CD  . GLU   A 1 226 ? -3.662  -3.994  -3.231  1.00 55.68  ? 232 GLU   A CD  1 
ATOM   1607 O  OE1 . GLU   A 1 226 ? -3.079  -5.006  -2.776  1.00 50.79  ? 232 GLU   A OE1 1 
ATOM   1608 O  OE2 . GLU   A 1 226 ? -3.662  -2.888  -2.649  1.00 46.48  ? 232 GLU   A OE2 1 
ATOM   1609 N  N   . ARG   A 1 227 ? -6.080  -7.955  -6.292  1.00 31.65  ? 233 ARG   A N   1 
ATOM   1610 C  CA  . ARG   A 1 227 ? -5.946  -9.284  -6.883  1.00 29.98  ? 233 ARG   A CA  1 
ATOM   1611 C  C   . ARG   A 1 227 ? -6.787  -9.393  -8.147  1.00 31.92  ? 233 ARG   A C   1 
ATOM   1612 O  O   . ARG   A 1 227 ? -6.311  -9.985  -9.109  1.00 30.59  ? 233 ARG   A O   1 
ATOM   1613 C  CB  . ARG   A 1 227 ? -6.286  -10.387 -5.878  1.00 28.19  ? 233 ARG   A CB  1 
ATOM   1614 C  CG  . ARG   A 1 227 ? -5.227  -10.500 -4.780  1.00 37.25  ? 233 ARG   A CG  1 
ATOM   1615 C  CD  . ARG   A 1 227 ? -5.610  -11.485 -3.693  1.00 42.83  ? 233 ARG   A CD  1 
ATOM   1616 N  NE  . ARG   A 1 227 ? -4.609  -11.482 -2.625  1.00 54.48  ? 233 ARG   A NE  1 
ATOM   1617 C  CZ  . ARG   A 1 227 ? -4.437  -12.460 -1.743  1.00 68.73  ? 233 ARG   A CZ  1 
ATOM   1618 N  NH1 . ARG   A 1 227 ? -5.193  -13.549 -1.791  1.00 55.38  ? 233 ARG   A NH1 1 
ATOM   1619 N  NH2 . ARG   A 1 227 ? -3.504  -12.358 -0.807  1.00 59.52  ? 233 ARG   A NH2 1 
ATOM   1620 N  N   . THR   A 1 228 ? -7.998  -8.775  -8.168  1.00 29.21  ? 234 THR   A N   1 
ATOM   1621 C  CA  . THR   A 1 228 ? -8.858  -8.758  -9.361  1.00 29.69  ? 234 THR   A CA  1 
ATOM   1622 C  C   . THR   A 1 228 ? -8.120  -8.107  -10.554 1.00 34.37  ? 234 THR   A C   1 
ATOM   1623 O  O   . THR   A 1 228 ? -8.132  -8.661  -11.667 1.00 33.35  ? 234 THR   A O   1 
ATOM   1624 C  CB  . THR   A 1 228 ? -10.182 -8.042  -9.058  1.00 31.28  ? 234 THR   A CB  1 
ATOM   1625 O  OG1 . THR   A 1 228 ? -10.932 -8.851  -8.152  1.00 26.49  ? 234 THR   A OG1 1 
ATOM   1626 C  CG2 . THR   A 1 228 ? -11.009 -7.751  -10.322 1.00 30.37  ? 234 THR   A CG2 1 
ATOM   1627 N  N   . PHE   A 1 229 ? -7.470  -6.942  -10.306 1.00 30.96  ? 235 PHE   A N   1 
ATOM   1628 C  CA  . PHE   A 1 229 ? -6.746  -6.221  -11.350 1.00 31.58  ? 235 PHE   A CA  1 
ATOM   1629 C  C   . PHE   A 1 229 ? -5.470  -6.936  -11.725 1.00 34.78  ? 235 PHE   A C   1 
ATOM   1630 O  O   . PHE   A 1 229 ? -5.153  -6.992  -12.905 1.00 33.92  ? 235 PHE   A O   1 
ATOM   1631 C  CB  . PHE   A 1 229 ? -6.534  -4.732  -11.013 1.00 33.47  ? 235 PHE   A CB  1 
ATOM   1632 C  CG  . PHE   A 1 229 ? -7.830  -3.970  -10.828 1.00 35.53  ? 235 PHE   A CG  1 
ATOM   1633 C  CD1 . PHE   A 1 229 ? -8.932  -4.230  -11.631 1.00 38.67  ? 235 PHE   A CD1 1 
ATOM   1634 C  CD2 . PHE   A 1 229 ? -7.956  -3.011  -9.829  1.00 38.36  ? 235 PHE   A CD2 1 
ATOM   1635 C  CE1 . PHE   A 1 229 ? -10.149 -3.578  -11.412 1.00 39.76  ? 235 PHE   A CE1 1 
ATOM   1636 C  CE2 . PHE   A 1 229 ? -9.168  -2.348  -9.627  1.00 40.87  ? 235 PHE   A CE2 1 
ATOM   1637 C  CZ  . PHE   A 1 229 ? -10.254 -2.634  -10.423 1.00 38.67  ? 235 PHE   A CZ  1 
ATOM   1638 N  N   . ASP   A 1 230 ? -4.801  -7.581  -10.767 1.00 31.53  ? 236 ASP   A N   1 
ATOM   1639 C  CA  . ASP   A 1 230 ? -3.598  -8.378  -11.065 1.00 32.52  ? 236 ASP   A CA  1 
ATOM   1640 C  C   . ASP   A 1 230 ? -3.926  -9.554  -12.000 1.00 35.10  ? 236 ASP   A C   1 
ATOM   1641 O  O   . ASP   A 1 230 ? -3.195  -9.804  -12.959 1.00 34.36  ? 236 ASP   A O   1 
ATOM   1642 C  CB  . ASP   A 1 230 ? -2.929  -8.876  -9.775  1.00 35.61  ? 236 ASP   A CB  1 
ATOM   1643 C  CG  . ASP   A 1 230 ? -1.460  -9.168  -9.967  1.00 57.51  ? 236 ASP   A CG  1 
ATOM   1644 O  OD1 . ASP   A 1 230 ? -0.665  -8.201  -10.020 1.00 61.80  ? 236 ASP   A OD1 1 
ATOM   1645 O  OD2 . ASP   A 1 230 ? -1.102  -10.359 -10.071 1.00 65.52  ? 236 ASP   A OD2 1 
ATOM   1646 N  N   . LEU   A 1 231 ? -5.070  -10.228 -11.763 1.00 31.55  ? 237 LEU   A N   1 
ATOM   1647 C  CA  . LEU   A 1 231 ? -5.504  -11.345 -12.610 1.00 31.16  ? 237 LEU   A CA  1 
ATOM   1648 C  C   . LEU   A 1 231 ? -5.937  -10.869 -14.005 1.00 33.25  ? 237 LEU   A C   1 
ATOM   1649 O  O   . LEU   A 1 231 ? -5.656  -11.534 -14.999 1.00 33.64  ? 237 LEU   A O   1 
ATOM   1650 C  CB  . LEU   A 1 231 ? -6.672  -12.127 -11.944 1.00 31.17  ? 237 LEU   A CB  1 
ATOM   1651 C  CG  . LEU   A 1 231 ? -6.407  -12.873 -10.610 1.00 34.90  ? 237 LEU   A CG  1 
ATOM   1652 C  CD1 . LEU   A 1 231 ? -7.712  -13.183 -9.896  1.00 34.97  ? 237 LEU   A CD1 1 
ATOM   1653 C  CD2 . LEU   A 1 231 ? -5.621  -14.140 -10.811 1.00 37.31  ? 237 LEU   A CD2 1 
ATOM   1654 N  N   . LEU   A 1 232 ? -6.643  -9.747  -14.085 1.00 28.03  ? 238 LEU   A N   1 
ATOM   1655 C  CA  . LEU   A 1 232 ? -7.155  -9.306  -15.371 1.00 27.46  ? 238 LEU   A CA  1 
ATOM   1656 C  C   . LEU   A 1 232 ? -6.241  -8.400  -16.185 1.00 32.16  ? 238 LEU   A C   1 
ATOM   1657 O  O   . LEU   A 1 232 ? -6.044  -8.663  -17.364 1.00 31.88  ? 238 LEU   A O   1 
ATOM   1658 C  CB  . LEU   A 1 232 ? -8.518  -8.639  -15.202 1.00 26.94  ? 238 LEU   A CB  1 
ATOM   1659 C  CG  . LEU   A 1 232 ? -9.626  -9.540  -14.652 1.00 29.51  ? 238 LEU   A CG  1 
ATOM   1660 C  CD1 . LEU   A 1 232 ? -10.877 -8.727  -14.394 1.00 28.13  ? 238 LEU   A CD1 1 
ATOM   1661 C  CD2 . LEU   A 1 232 ? -9.910  -10.692 -15.601 1.00 29.02  ? 238 LEU   A CD2 1 
ATOM   1662 N  N   . ILE   A 1 233 ? -5.712  -7.333  -15.578 1.00 31.73  ? 239 ILE   A N   1 
ATOM   1663 C  CA  . ILE   A 1 233 ? -4.922  -6.319  -16.300 1.00 31.50  ? 239 ILE   A CA  1 
ATOM   1664 C  C   . ILE   A 1 233 ? -3.485  -6.207  -15.784 1.00 38.26  ? 239 ILE   A C   1 
ATOM   1665 O  O   . ILE   A 1 233 ? -2.837  -5.181  -15.978 1.00 37.06  ? 239 ILE   A O   1 
ATOM   1666 C  CB  . ILE   A 1 233 ? -5.682  -4.952  -16.313 1.00 33.10  ? 239 ILE   A CB  1 
ATOM   1667 C  CG1 . ILE   A 1 233 ? -5.997  -4.435  -14.865 1.00 33.34  ? 239 ILE   A CG1 1 
ATOM   1668 C  CG2 . ILE   A 1 233 ? -6.968  -5.071  -17.156 1.00 32.38  ? 239 ILE   A CG2 1 
ATOM   1669 C  CD1 . ILE   A 1 233 ? -6.223  -2.906  -14.746 1.00 34.60  ? 239 ILE   A CD1 1 
ATOM   1670 N  N   . GLY   A 1 234 ? -2.992  -7.287  -15.183 1.00 36.98  ? 240 GLY   A N   1 
ATOM   1671 C  CA  . GLY   A 1 234 ? -1.647  -7.350  -14.629 1.00 37.70  ? 240 GLY   A CA  1 
ATOM   1672 C  C   . GLY   A 1 234 ? -0.554  -7.378  -15.674 1.00 43.25  ? 240 GLY   A C   1 
ATOM   1673 O  O   . GLY   A 1 234 ? 0.522   -6.802  -15.463 1.00 43.77  ? 240 GLY   A O   1 
ATOM   1674 N  N   . LYS   A 1 235 ? -0.840  -8.020  -16.818 1.00 40.18  ? 241 LYS   A N   1 
ATOM   1675 C  CA  . LYS   A 1 235 ? 0.079   -8.178  -17.952 1.00 39.93  ? 241 LYS   A CA  1 
ATOM   1676 C  C   . LYS   A 1 235 ? -0.091  -7.114  -19.043 1.00 43.68  ? 241 LYS   A C   1 
ATOM   1677 O  O   . LYS   A 1 235 ? 0.889   -6.743  -19.688 1.00 44.19  ? 241 LYS   A O   1 
ATOM   1678 C  CB  . LYS   A 1 235 ? -0.047  -9.587  -18.550 1.00 42.58  ? 241 LYS   A CB  1 
ATOM   1679 C  CG  . LYS   A 1 235 ? 0.539   -10.683 -17.667 1.00 58.47  ? 241 LYS   A CG  1 
ATOM   1680 C  CD  . LYS   A 1 235 ? 0.277   -12.075 -18.241 1.00 70.57  ? 241 LYS   A CD  1 
ATOM   1681 C  CE  . LYS   A 1 235 ? 0.910   -13.175 -17.422 1.00 86.72  ? 241 LYS   A CE  1 
ATOM   1682 N  NZ  . LYS   A 1 235 ? 2.393   -13.210 -17.572 1.00 99.02  ? 241 LYS   A NZ  1 
ATOM   1683 N  N   . ARG   A 1 236 ? -1.321  -6.631  -19.259 1.00 38.31  ? 242 ARG   A N   1 
ATOM   1684 C  CA  . ARG   A 1 236 ? -1.600  -5.643  -20.301 1.00 37.53  ? 242 ARG   A CA  1 
ATOM   1685 C  C   . ARG   A 1 236 ? -2.894  -4.906  -20.007 1.00 39.98  ? 242 ARG   A C   1 
ATOM   1686 O  O   . ARG   A 1 236 ? -3.780  -5.454  -19.340 1.00 39.50  ? 242 ARG   A O   1 
ATOM   1687 C  CB  . ARG   A 1 236 ? -1.646  -6.330  -21.706 1.00 38.57  ? 242 ARG   A CB  1 
ATOM   1688 C  CG  . ARG   A 1 236 ? -2.907  -7.163  -21.994 1.00 49.43  ? 242 ARG   A CG  1 
ATOM   1689 C  CD  . ARG   A 1 236 ? -2.606  -8.459  -22.725 1.00 63.21  ? 242 ARG   A CD  1 
ATOM   1690 N  NE  . ARG   A 1 236 ? -3.792  -9.319  -22.794 1.00 61.37  ? 242 ARG   A NE  1 
ATOM   1691 C  CZ  . ARG   A 1 236 ? -4.086  -10.278 -21.922 1.00 63.14  ? 242 ARG   A CZ  1 
ATOM   1692 N  NH1 . ARG   A 1 236 ? -3.265  -10.544 -20.914 1.00 54.71  ? 242 ARG   A NH1 1 
ATOM   1693 N  NH2 . ARG   A 1 236 ? -5.194  -10.992 -22.063 1.00 40.81  ? 242 ARG   A NH2 1 
ATOM   1694 N  N   . GLN   A 1 237 ? -3.019  -3.688  -20.546 1.00 35.74  ? 243 GLN   A N   1 
ATOM   1695 C  CA  . GLN   A 1 237 ? -4.223  -2.862  -20.441 1.00 35.49  ? 243 GLN   A CA  1 
ATOM   1696 C  C   . GLN   A 1 237 ? -5.308  -3.547  -21.261 1.00 38.50  ? 243 GLN   A C   1 
ATOM   1697 O  O   . GLN   A 1 237 ? -5.019  -4.125  -22.308 1.00 39.96  ? 243 GLN   A O   1 
ATOM   1698 C  CB  . GLN   A 1 237 ? -3.980  -1.456  -21.014 1.00 37.18  ? 243 GLN   A CB  1 
ATOM   1699 C  CG  . GLN   A 1 237 ? -3.164  -0.555  -20.092 1.00 59.64  ? 243 GLN   A CG  1 
ATOM   1700 C  CD  . GLN   A 1 237 ? -3.299  0.889   -20.493 1.00 92.13  ? 243 GLN   A CD  1 
ATOM   1701 O  OE1 . GLN   A 1 237 ? -4.240  1.582   -20.092 1.00 91.46  ? 243 GLN   A OE1 1 
ATOM   1702 N  NE2 . GLN   A 1 237 ? -2.365  1.373   -21.299 1.00 88.26  ? 243 GLN   A NE2 1 
ATOM   1703 N  N   . ARG   A 1 238 ? -6.541  -3.512  -20.773 1.00 33.27  ? 244 ARG   A N   1 
ATOM   1704 C  CA  . ARG   A 1 238 ? -7.669  -4.139  -21.450 1.00 31.41  ? 244 ARG   A CA  1 
ATOM   1705 C  C   . ARG   A 1 238 ? -8.922  -3.368  -21.133 1.00 33.42  ? 244 ARG   A C   1 
ATOM   1706 O  O   . ARG   A 1 238 ? -9.056  -2.884  -20.006 1.00 34.22  ? 244 ARG   A O   1 
ATOM   1707 C  CB  . ARG   A 1 238 ? -7.876  -5.586  -20.967 1.00 28.89  ? 244 ARG   A CB  1 
ATOM   1708 C  CG  . ARG   A 1 238 ? -6.657  -6.502  -21.039 1.00 31.49  ? 244 ARG   A CG  1 
ATOM   1709 C  CD  . ARG   A 1 238 ? -6.873  -7.764  -20.265 1.00 32.91  ? 244 ARG   A CD  1 
ATOM   1710 N  NE  . ARG   A 1 238 ? -7.708  -8.721  -20.988 1.00 33.77  ? 244 ARG   A NE  1 
ATOM   1711 C  CZ  . ARG   A 1 238 ? -8.026  -9.930  -20.541 1.00 38.70  ? 244 ARG   A CZ  1 
ATOM   1712 N  NH1 . ARG   A 1 238 ? -7.599  -10.340 -19.355 1.00 31.64  ? 244 ARG   A NH1 1 
ATOM   1713 N  NH2 . ARG   A 1 238 ? -8.780  -10.735 -21.274 1.00 33.20  ? 244 ARG   A NH2 1 
ATOM   1714 N  N   . PRO   A 1 239 ? -9.891  -3.297  -22.071 1.00 30.99  ? 245 PRO   A N   1 
ATOM   1715 C  CA  . PRO   A 1 239 ? -11.168 -2.642  -21.747 1.00 30.41  ? 245 PRO   A CA  1 
ATOM   1716 C  C   . PRO   A 1 239 ? -11.927 -3.493  -20.716 1.00 36.28  ? 245 PRO   A C   1 
ATOM   1717 O  O   . PRO   A 1 239 ? -11.916 -4.729  -20.804 1.00 36.03  ? 245 PRO   A O   1 
ATOM   1718 C  CB  . PRO   A 1 239 ? -11.891 -2.589  -23.103 1.00 31.56  ? 245 PRO   A CB  1 
ATOM   1719 C  CG  . PRO   A 1 239 ? -11.278 -3.636  -23.906 1.00 35.23  ? 245 PRO   A CG  1 
ATOM   1720 C  CD  . PRO   A 1 239 ? -9.887  -3.840  -23.452 1.00 30.44  ? 245 PRO   A CD  1 
ATOM   1721 N  N   . ILE   A 1 240 ? -12.554 -2.840  -19.726 1.00 31.82  ? 246 ILE   A N   1 
ATOM   1722 C  CA  . ILE   A 1 240 ? -13.247 -3.551  -18.659 1.00 30.56  ? 246 ILE   A CA  1 
ATOM   1723 C  C   . ILE   A 1 240 ? -14.747 -3.412  -18.822 1.00 33.50  ? 246 ILE   A C   1 
ATOM   1724 O  O   . ILE   A 1 240 ? -15.262 -2.309  -19.025 1.00 34.85  ? 246 ILE   A O   1 
ATOM   1725 C  CB  . ILE   A 1 240 ? -12.753 -3.086  -17.241 1.00 33.42  ? 246 ILE   A CB  1 
ATOM   1726 C  CG1 . ILE   A 1 240 ? -11.222 -3.341  -17.028 1.00 33.88  ? 246 ILE   A CG1 1 
ATOM   1727 C  CG2 . ILE   A 1 240 ? -13.581 -3.738  -16.107 1.00 33.27  ? 246 ILE   A CG2 1 
ATOM   1728 C  CD1 . ILE   A 1 240 ? -10.602 -2.582  -15.776 1.00 37.62  ? 246 ILE   A CD1 1 
ATOM   1729 N  N   . HIS   A 1 241 ? -15.437 -4.542  -18.724 1.00 29.74  ? 247 HIS   A N   1 
ATOM   1730 C  CA  . HIS   A 1 241 ? -16.882 -4.607  -18.724 1.00 29.00  ? 247 HIS   A CA  1 
ATOM   1731 C  C   . HIS   A 1 241 ? -17.296 -4.914  -17.271 1.00 32.28  ? 247 HIS   A C   1 
ATOM   1732 O  O   . HIS   A 1 241 ? -17.019 -6.007  -16.774 1.00 30.06  ? 247 HIS   A O   1 
ATOM   1733 C  CB  . HIS   A 1 241 ? -17.378 -5.716  -19.660 1.00 30.58  ? 247 HIS   A CB  1 
ATOM   1734 C  CG  . HIS   A 1 241 ? -18.860 -5.704  -19.816 1.00 34.08  ? 247 HIS   A CG  1 
ATOM   1735 N  ND1 . HIS   A 1 241 ? -19.453 -5.242  -20.969 1.00 36.25  ? 247 HIS   A ND1 1 
ATOM   1736 C  CD2 . HIS   A 1 241 ? -19.823 -6.053  -18.935 1.00 35.37  ? 247 HIS   A CD2 1 
ATOM   1737 C  CE1 . HIS   A 1 241 ? -20.753 -5.346  -20.769 1.00 35.68  ? 247 HIS   A CE1 1 
ATOM   1738 N  NE2 . HIS   A 1 241 ? -21.019 -5.810  -19.549 1.00 36.14  ? 247 HIS   A NE2 1 
ATOM   1739 N  N   . LEU   A 1 242 ? -17.939 -3.946  -16.593 1.00 29.63  ? 248 LEU   A N   1 
ATOM   1740 C  CA  . LEU   A 1 242 ? -18.411 -4.117  -15.220 1.00 28.96  ? 248 LEU   A CA  1 
ATOM   1741 C  C   . LEU   A 1 242 ? -19.877 -4.519  -15.250 1.00 32.26  ? 248 LEU   A C   1 
ATOM   1742 O  O   . LEU   A 1 242 ? -20.729 -3.725  -15.618 1.00 33.42  ? 248 LEU   A O   1 
ATOM   1743 C  CB  . LEU   A 1 242 ? -18.186 -2.825  -14.370 1.00 29.05  ? 248 LEU   A CB  1 
ATOM   1744 C  CG  . LEU   A 1 242 ? -18.671 -2.832  -12.888 1.00 31.98  ? 248 LEU   A CG  1 
ATOM   1745 C  CD1 . LEU   A 1 242 ? -18.026 -3.982  -12.067 1.00 30.17  ? 248 LEU   A CD1 1 
ATOM   1746 C  CD2 . LEU   A 1 242 ? -18.377 -1.491  -12.231 1.00 34.16  ? 248 LEU   A CD2 1 
ATOM   1747 N  N   . SER   A 1 243 ? -20.170 -5.770  -14.912 1.00 28.45  ? 249 SER   A N   1 
ATOM   1748 C  CA  . SER   A 1 243 ? -21.557 -6.244  -14.889 1.00 27.28  ? 249 SER   A CA  1 
ATOM   1749 C  C   . SER   A 1 243 ? -21.982 -6.283  -13.424 1.00 29.70  ? 249 SER   A C   1 
ATOM   1750 O  O   . SER   A 1 243 ? -21.582 -7.171  -12.660 1.00 26.76  ? 249 SER   A O   1 
ATOM   1751 C  CB  . SER   A 1 243 ? -21.689 -7.588  -15.594 1.00 28.74  ? 249 SER   A CB  1 
ATOM   1752 O  OG  . SER   A 1 243 ? -23.060 -7.767  -15.902 1.00 33.33  ? 249 SER   A OG  1 
ATOM   1753 N  N   . PHE   A 1 244 ? -22.749 -5.253  -13.011 1.00 28.10  ? 250 PHE   A N   1 
ATOM   1754 C  CA  . PHE   A 1 244 ? -23.117 -5.059  -11.611 1.00 27.38  ? 250 PHE   A CA  1 
ATOM   1755 C  C   . PHE   A 1 244 ? -24.567 -5.359  -11.298 1.00 31.30  ? 250 PHE   A C   1 
ATOM   1756 O  O   . PHE   A 1 244 ? -25.459 -4.564  -11.623 1.00 30.77  ? 250 PHE   A O   1 
ATOM   1757 C  CB  . PHE   A 1 244 ? -22.743 -3.641  -11.159 1.00 29.20  ? 250 PHE   A CB  1 
ATOM   1758 C  CG  . PHE   A 1 244 ? -22.447 -3.456  -9.685  1.00 30.05  ? 250 PHE   A CG  1 
ATOM   1759 C  CD1 . PHE   A 1 244 ? -23.430 -3.684  -8.723  1.00 32.51  ? 250 PHE   A CD1 1 
ATOM   1760 C  CD2 . PHE   A 1 244 ? -21.204 -2.994  -9.262  1.00 31.50  ? 250 PHE   A CD2 1 
ATOM   1761 C  CE1 . PHE   A 1 244 ? -23.148 -3.528  -7.362  1.00 32.68  ? 250 PHE   A CE1 1 
ATOM   1762 C  CE2 . PHE   A 1 244 ? -20.930 -2.827  -7.902  1.00 33.32  ? 250 PHE   A CE2 1 
ATOM   1763 C  CZ  . PHE   A 1 244 ? -21.904 -3.091  -6.968  1.00 31.82  ? 250 PHE   A CZ  1 
ATOM   1764 N  N   . ASP   A 1 245 ? -24.797 -6.473  -10.604 1.00 26.18  ? 251 ASP   A N   1 
ATOM   1765 C  CA  . ASP   A 1 245 ? -26.141 -6.847  -10.163 1.00 26.73  ? 251 ASP   A CA  1 
ATOM   1766 C  C   . ASP   A 1 245 ? -26.345 -6.159  -8.791  1.00 33.30  ? 251 ASP   A C   1 
ATOM   1767 O  O   . ASP   A 1 245 ? -25.492 -6.277  -7.914  1.00 33.15  ? 251 ASP   A O   1 
ATOM   1768 C  CB  . ASP   A 1 245 ? -26.244 -8.377  -10.084 1.00 27.34  ? 251 ASP   A CB  1 
ATOM   1769 C  CG  . ASP   A 1 245 ? -27.626 -8.952  -9.831  1.00 31.44  ? 251 ASP   A CG  1 
ATOM   1770 O  OD1 . ASP   A 1 245 ? -28.426 -8.298  -9.140  1.00 32.51  ? 251 ASP   A OD1 1 
ATOM   1771 O  OD2 . ASP   A 1 245 ? -27.872 -10.104 -10.239 1.00 34.78  ? 251 ASP   A OD2 1 
ATOM   1772 N  N   . ILE   A 1 246 ? -27.410 -5.341  -8.650  1.00 30.72  ? 252 ILE   A N   1 
ATOM   1773 C  CA  . ILE   A 1 246 ? -27.707 -4.617  -7.410  1.00 30.32  ? 252 ILE   A CA  1 
ATOM   1774 C  C   . ILE   A 1 246 ? -27.863 -5.581  -6.206  1.00 32.71  ? 252 ILE   A C   1 
ATOM   1775 O  O   . ILE   A 1 246 ? -27.609 -5.172  -5.071  1.00 32.81  ? 252 ILE   A O   1 
ATOM   1776 C  CB  . ILE   A 1 246 ? -28.930 -3.646  -7.584  1.00 32.30  ? 252 ILE   A CB  1 
ATOM   1777 C  CG1 . ILE   A 1 246 ? -28.871 -2.427  -6.624  1.00 32.87  ? 252 ILE   A CG1 1 
ATOM   1778 C  CG2 . ILE   A 1 246 ? -30.264 -4.376  -7.476  1.00 31.53  ? 252 ILE   A CG2 1 
ATOM   1779 C  CD1 . ILE   A 1 246 ? -27.715 -1.433  -6.816  1.00 34.33  ? 252 ILE   A CD1 1 
ATOM   1780 N  N   . ASP   A 1 247 ? -28.234 -6.860  -6.458  1.00 27.60  ? 253 ASP   A N   1 
ATOM   1781 C  CA  . ASP   A 1 247 ? -28.382 -7.840  -5.376  1.00 26.46  ? 253 ASP   A CA  1 
ATOM   1782 C  C   . ASP   A 1 247 ? -27.022 -8.272  -4.781  1.00 28.90  ? 253 ASP   A C   1 
ATOM   1783 O  O   . ASP   A 1 247 ? -27.016 -9.016  -3.808  1.00 28.70  ? 253 ASP   A O   1 
ATOM   1784 C  CB  . ASP   A 1 247 ? -29.285 -9.046  -5.750  1.00 27.39  ? 253 ASP   A CB  1 
ATOM   1785 C  CG  . ASP   A 1 247 ? -28.724 -10.138 -6.645  1.00 30.94  ? 253 ASP   A CG  1 
ATOM   1786 O  OD1 . ASP   A 1 247 ? -27.481 -10.201 -6.812  1.00 31.13  ? 253 ASP   A OD1 1 
ATOM   1787 O  OD2 . ASP   A 1 247 ? -29.525 -10.900 -7.211  1.00 32.69  ? 253 ASP   A OD2 1 
ATOM   1788 N  N   . ALA   A 1 248 ? -25.896 -7.754  -5.299  1.00 26.92  ? 254 ALA   A N   1 
ATOM   1789 C  CA  . ALA   A 1 248 ? -24.562 -7.975  -4.709  1.00 27.53  ? 254 ALA   A CA  1 
ATOM   1790 C  C   . ALA   A 1 248 ? -24.534 -7.301  -3.310  1.00 31.72  ? 254 ALA   A C   1 
ATOM   1791 O  O   . ALA   A 1 248 ? -23.885 -7.798  -2.393  1.00 31.95  ? 254 ALA   A O   1 
ATOM   1792 C  CB  . ALA   A 1 248 ? -23.493 -7.355  -5.584  1.00 28.11  ? 254 ALA   A CB  1 
ATOM   1793 N  N   . PHE   A 1 249 ? -25.258 -6.174  -3.163  1.00 28.88  ? 255 PHE   A N   1 
ATOM   1794 C  CA  . PHE   A 1 249 ? -25.434 -5.447  -1.903  1.00 28.26  ? 255 PHE   A CA  1 
ATOM   1795 C  C   . PHE   A 1 249 ? -26.321 -6.198  -0.943  1.00 30.58  ? 255 PHE   A C   1 
ATOM   1796 O  O   . PHE   A 1 249 ? -27.212 -6.936  -1.355  1.00 29.41  ? 255 PHE   A O   1 
ATOM   1797 C  CB  . PHE   A 1 249 ? -26.093 -4.078  -2.157  1.00 29.94  ? 255 PHE   A CB  1 
ATOM   1798 C  CG  . PHE   A 1 249 ? -25.156 -3.045  -2.708  1.00 30.62  ? 255 PHE   A CG  1 
ATOM   1799 C  CD1 . PHE   A 1 249 ? -24.152 -2.500  -1.914  1.00 33.33  ? 255 PHE   A CD1 1 
ATOM   1800 C  CD2 . PHE   A 1 249 ? -25.281 -2.601  -4.018  1.00 31.30  ? 255 PHE   A CD2 1 
ATOM   1801 C  CE1 . PHE   A 1 249 ? -23.276 -1.545  -2.430  1.00 33.98  ? 255 PHE   A CE1 1 
ATOM   1802 C  CE2 . PHE   A 1 249 ? -24.412 -1.636  -4.531  1.00 34.59  ? 255 PHE   A CE2 1 
ATOM   1803 C  CZ  . PHE   A 1 249 ? -23.408 -1.121  -3.740  1.00 33.33  ? 255 PHE   A CZ  1 
ATOM   1804 N  N   . ASP   A 1 250 ? -26.134 -5.945  0.357   1.00 28.68  ? 256 ASP   A N   1 
ATOM   1805 C  CA  . ASP   A 1 250 ? -26.992 -6.547  1.354   1.00 28.73  ? 256 ASP   A CA  1 
ATOM   1806 C  C   . ASP   A 1 250 ? -28.467 -6.125  1.112   1.00 31.77  ? 256 ASP   A C   1 
ATOM   1807 O  O   . ASP   A 1 250 ? -28.682 -4.985  0.700   1.00 32.16  ? 256 ASP   A O   1 
ATOM   1808 C  CB  . ASP   A 1 250 ? -26.530 -6.126  2.764   1.00 30.81  ? 256 ASP   A CB  1 
ATOM   1809 C  CG  . ASP   A 1 250 ? -27.182 -6.986  3.818   1.00 38.32  ? 256 ASP   A CG  1 
ATOM   1810 O  OD1 . ASP   A 1 250 ? -26.697 -8.116  4.040   1.00 36.86  ? 256 ASP   A OD1 1 
ATOM   1811 O  OD2 . ASP   A 1 250 ? -28.264 -6.596  4.312   1.00 41.51  ? 256 ASP   A OD2 1 
ATOM   1812 N  N   . PRO   A 1 251 ? -29.459 -7.040  1.260   1.00 29.73  ? 257 PRO   A N   1 
ATOM   1813 C  CA  . PRO   A 1 251 ? -30.875 -6.656  1.060   1.00 31.33  ? 257 PRO   A CA  1 
ATOM   1814 C  C   . PRO   A 1 251 ? -31.371 -5.487  1.922   1.00 38.85  ? 257 PRO   A C   1 
ATOM   1815 O  O   . PRO   A 1 251 ? -32.406 -4.898  1.585   1.00 38.72  ? 257 PRO   A O   1 
ATOM   1816 C  CB  . PRO   A 1 251 ? -31.650 -7.940  1.380   1.00 32.96  ? 257 PRO   A CB  1 
ATOM   1817 C  CG  . PRO   A 1 251 ? -30.675 -9.037  1.213   1.00 36.90  ? 257 PRO   A CG  1 
ATOM   1818 C  CD  . PRO   A 1 251 ? -29.351 -8.458  1.645   1.00 31.01  ? 257 PRO   A CD  1 
ATOM   1819 N  N   . THR   A 1 252 ? -30.666 -5.153  3.032   1.00 36.80  ? 258 THR   A N   1 
ATOM   1820 C  CA  . THR   A 1 252 ? -31.018 -3.985  3.869   1.00 37.29  ? 258 THR   A CA  1 
ATOM   1821 C  C   . THR   A 1 252 ? -30.721 -2.679  3.082   1.00 41.93  ? 258 THR   A C   1 
ATOM   1822 O  O   . THR   A 1 252 ? -31.395 -1.668  3.284   1.00 42.95  ? 258 THR   A O   1 
ATOM   1823 C  CB  . THR   A 1 252 ? -30.259 -4.002  5.212   1.00 42.99  ? 258 THR   A CB  1 
ATOM   1824 O  OG1 . THR   A 1 252 ? -28.851 -3.952  4.952   1.00 44.62  ? 258 THR   A OG1 1 
ATOM   1825 C  CG2 . THR   A 1 252 ? -30.620 -5.205  6.086   1.00 37.50  ? 258 THR   A CG2 1 
ATOM   1826 N  N   . LEU   A 1 253 ? -29.716 -2.714  2.184   1.00 37.51  ? 259 LEU   A N   1 
ATOM   1827 C  CA  . LEU   A 1 253 ? -29.334 -1.583  1.341   1.00 37.50  ? 259 LEU   A CA  1 
ATOM   1828 C  C   . LEU   A 1 253 ? -30.013 -1.605  -0.025  1.00 42.54  ? 259 LEU   A C   1 
ATOM   1829 O  O   . LEU   A 1 253 ? -30.314 -0.539  -0.572  1.00 43.24  ? 259 LEU   A O   1 
ATOM   1830 C  CB  . LEU   A 1 253 ? -27.821 -1.500  1.161   1.00 37.73  ? 259 LEU   A CB  1 
ATOM   1831 C  CG  . LEU   A 1 253 ? -26.978 -1.561  2.430   1.00 42.83  ? 259 LEU   A CG  1 
ATOM   1832 C  CD1 . LEU   A 1 253 ? -25.562 -1.951  2.098   1.00 42.28  ? 259 LEU   A CD1 1 
ATOM   1833 C  CD2 . LEU   A 1 253 ? -27.050 -0.236  3.224   1.00 44.86  ? 259 LEU   A CD2 1 
ATOM   1834 N  N   . ALA   A 1 254 ? -30.259 -2.804  -0.577  1.00 38.65  ? 260 ALA   A N   1 
ATOM   1835 C  CA  . ALA   A 1 254 ? -30.905 -2.967  -1.882  1.00 37.89  ? 260 ALA   A CA  1 
ATOM   1836 C  C   . ALA   A 1 254 ? -32.130 -3.917  -1.788  1.00 40.57  ? 260 ALA   A C   1 
ATOM   1837 O  O   . ALA   A 1 254 ? -32.085 -5.035  -2.317  1.00 39.63  ? 260 ALA   A O   1 
ATOM   1838 C  CB  . ALA   A 1 254 ? -29.885 -3.460  -2.909  1.00 38.51  ? 260 ALA   A CB  1 
ATOM   1839 N  N   . PRO   A 1 255 ? -33.228 -3.513  -1.093  1.00 37.57  ? 261 PRO   A N   1 
ATOM   1840 C  CA  . PRO   A 1 255 ? -34.371 -4.430  -0.936  1.00 37.46  ? 261 PRO   A CA  1 
ATOM   1841 C  C   . PRO   A 1 255 ? -35.173 -4.720  -2.196  1.00 41.69  ? 261 PRO   A C   1 
ATOM   1842 O  O   . PRO   A 1 255 ? -35.713 -5.821  -2.331  1.00 41.07  ? 261 PRO   A O   1 
ATOM   1843 C  CB  . PRO   A 1 255 ? -35.231 -3.741  0.132   1.00 39.21  ? 261 PRO   A CB  1 
ATOM   1844 C  CG  . PRO   A 1 255 ? -34.904 -2.300  0.006   1.00 43.46  ? 261 PRO   A CG  1 
ATOM   1845 C  CD  . PRO   A 1 255 ? -33.453 -2.257  -0.334  1.00 39.62  ? 261 PRO   A CD  1 
ATOM   1846 N  N   . ALA   A 1 256 ? -35.273 -3.731  -3.101  1.00 39.57  ? 262 ALA   A N   1 
ATOM   1847 C  CA  . ALA   A 1 256 ? -36.063 -3.833  -4.334  1.00 38.65  ? 262 ALA   A CA  1 
ATOM   1848 C  C   . ALA   A 1 256 ? -35.327 -4.625  -5.443  1.00 38.79  ? 262 ALA   A C   1 
ATOM   1849 O  O   . ALA   A 1 256 ? -34.880 -4.053  -6.431  1.00 37.30  ? 262 ALA   A O   1 
ATOM   1850 C  CB  . ALA   A 1 256 ? -36.470 -2.440  -4.809  1.00 39.38  ? 262 ALA   A CB  1 
ATOM   1851 N  N   . THR   A 1 257 ? -35.194 -5.950  -5.233  1.00 35.61  ? 263 THR   A N   1 
ATOM   1852 C  CA  . THR   A 1 257 ? -34.549 -6.916  -6.135  1.00 34.60  ? 263 THR   A CA  1 
ATOM   1853 C  C   . THR   A 1 257 ? -35.265 -8.267  -5.988  1.00 37.30  ? 263 THR   A C   1 
ATOM   1854 O  O   . THR   A 1 257 ? -35.824 -8.545  -4.931  1.00 37.61  ? 263 THR   A O   1 
ATOM   1855 C  CB  . THR   A 1 257 ? -33.000 -6.932  -5.950  1.00 40.40  ? 263 THR   A CB  1 
ATOM   1856 O  OG1 . THR   A 1 257 ? -32.391 -7.531  -7.101  1.00 38.50  ? 263 THR   A OG1 1 
ATOM   1857 C  CG2 . THR   A 1 257 ? -32.539 -7.639  -4.660  1.00 40.42  ? 263 THR   A CG2 1 
ATOM   1858 N  N   . GLY   A 1 258 ? -35.261 -9.075  -7.043  1.00 31.79  ? 264 GLY   A N   1 
ATOM   1859 C  CA  . GLY   A 1 258 ? -35.988 -10.341 -7.081  1.00 32.19  ? 264 GLY   A CA  1 
ATOM   1860 C  C   . GLY   A 1 258 ? -35.417 -11.511 -6.313  1.00 35.88  ? 264 GLY   A C   1 
ATOM   1861 O  O   . GLY   A 1 258 ? -36.167 -12.385 -5.868  1.00 35.68  ? 264 GLY   A O   1 
ATOM   1862 N  N   . THR   A 1 259 ? -34.089 -11.574 -6.190  1.00 33.84  ? 265 THR   A N   1 
ATOM   1863 C  CA  . THR   A 1 259 ? -33.457 -12.695 -5.488  1.00 34.18  ? 265 THR   A CA  1 
ATOM   1864 C  C   . THR   A 1 259 ? -32.510 -12.147 -4.404  1.00 36.37  ? 265 THR   A C   1 
ATOM   1865 O  O   . THR   A 1 259 ? -31.290 -12.229 -4.569  1.00 34.90  ? 265 THR   A O   1 
ATOM   1866 C  CB  . THR   A 1 259 ? -32.777 -13.660 -6.506  1.00 44.05  ? 265 THR   A CB  1 
ATOM   1867 O  OG1 . THR   A 1 259 ? -33.671 -13.931 -7.574  1.00 45.04  ? 265 THR   A OG1 1 
ATOM   1868 C  CG2 . THR   A 1 259 ? -32.362 -14.990 -5.873  1.00 45.19  ? 265 THR   A CG2 1 
ATOM   1869 N  N   . PRO   A 1 260 ? -33.043 -11.533 -3.317  1.00 33.45  ? 266 PRO   A N   1 
ATOM   1870 C  CA  . PRO   A 1 260 ? -32.141 -11.024 -2.276  1.00 32.76  ? 266 PRO   A CA  1 
ATOM   1871 C  C   . PRO   A 1 260 ? -31.526 -12.163 -1.458  1.00 33.77  ? 266 PRO   A C   1 
ATOM   1872 O  O   . PRO   A 1 260 ? -32.149 -13.213 -1.229  1.00 32.63  ? 266 PRO   A O   1 
ATOM   1873 C  CB  . PRO   A 1 260 ? -33.044 -10.111 -1.449  1.00 35.08  ? 266 PRO   A CB  1 
ATOM   1874 C  CG  . PRO   A 1 260 ? -34.412 -10.722 -1.583  1.00 38.47  ? 266 PRO   A CG  1 
ATOM   1875 C  CD  . PRO   A 1 260 ? -34.468 -11.320 -2.955  1.00 33.36  ? 266 PRO   A CD  1 
ATOM   1876 N  N   . VAL   A 1 261 ? -30.259 -11.990 -1.114  1.00 29.29  ? 267 VAL   A N   1 
ATOM   1877 C  CA  . VAL   A 1 261 ? -29.506 -12.954 -0.310  1.00 28.91  ? 267 VAL   A CA  1 
ATOM   1878 C  C   . VAL   A 1 261 ? -28.830 -12.150 0.801   1.00 31.00  ? 267 VAL   A C   1 
ATOM   1879 O  O   . VAL   A 1 261 ? -28.005 -11.276 0.520   1.00 30.56  ? 267 VAL   A O   1 
ATOM   1880 C  CB  . VAL   A 1 261 ? -28.473 -13.818 -1.121  1.00 32.00  ? 267 VAL   A CB  1 
ATOM   1881 C  CG1 . VAL   A 1 261 ? -27.804 -14.852 -0.212  1.00 30.98  ? 267 VAL   A CG1 1 
ATOM   1882 C  CG2 . VAL   A 1 261 ? -29.132 -14.519 -2.311  1.00 32.12  ? 267 VAL   A CG2 1 
ATOM   1883 N  N   . VAL   A 1 262 ? -29.143 -12.483 2.061   1.00 29.64  ? 268 VAL   A N   1 
ATOM   1884 C  CA  . VAL   A 1 262 ? -28.566 -11.815 3.241   1.00 30.66  ? 268 VAL   A CA  1 
ATOM   1885 C  C   . VAL   A 1 262 ? -27.028 -11.959 3.272   1.00 33.82  ? 268 VAL   A C   1 
ATOM   1886 O  O   . VAL   A 1 262 ? -26.484 -12.943 2.752   1.00 32.91  ? 268 VAL   A O   1 
ATOM   1887 C  CB  . VAL   A 1 262 ? -29.213 -12.335 4.553   1.00 37.51  ? 268 VAL   A CB  1 
ATOM   1888 C  CG1 . VAL   A 1 262 ? -30.722 -12.062 4.575   1.00 38.24  ? 268 VAL   A CG1 1 
ATOM   1889 C  CG2 . VAL   A 1 262 ? -28.945 -13.826 4.745   1.00 37.91  ? 268 VAL   A CG2 1 
ATOM   1890 N  N   . GLY   A 1 263 ? -26.361 -10.979 3.862   1.00 29.84  ? 269 GLY   A N   1 
ATOM   1891 C  CA  . GLY   A 1 263 ? -24.912 -10.993 4.047   1.00 30.57  ? 269 GLY   A CA  1 
ATOM   1892 C  C   . GLY   A 1 263 ? -24.141 -10.507 2.839   1.00 32.82  ? 269 GLY   A C   1 
ATOM   1893 O  O   . GLY   A 1 263 ? -23.073 -11.033 2.526   1.00 31.16  ? 269 GLY   A O   1 
ATOM   1894 N  N   . GLY   A 1 264 ? -24.657 -9.453  2.218   1.00 29.18  ? 270 GLY   A N   1 
ATOM   1895 C  CA  . GLY   A 1 264 ? -24.080 -8.838  1.031   1.00 27.17  ? 270 GLY   A CA  1 
ATOM   1896 C  C   . GLY   A 1 264 ? -23.057 -7.764  1.300   1.00 29.38  ? 270 GLY   A C   1 
ATOM   1897 O  O   . GLY   A 1 264 ? -22.639 -7.561  2.442   1.00 27.96  ? 270 GLY   A O   1 
ATOM   1898 N  N   . LEU   A 1 265 ? -22.634 -7.088  0.233   1.00 25.03  ? 271 LEU   A N   1 
ATOM   1899 C  CA  . LEU   A 1 265 ? -21.685 -5.974  0.302   1.00 24.77  ? 271 LEU   A CA  1 
ATOM   1900 C  C   . LEU   A 1 265 ? -22.273 -4.816  1.094   1.00 29.25  ? 271 LEU   A C   1 
ATOM   1901 O  O   . LEU   A 1 265 ? -23.490 -4.587  1.072   1.00 27.03  ? 271 LEU   A O   1 
ATOM   1902 C  CB  . LEU   A 1 265 ? -21.348 -5.433  -1.117  1.00 25.01  ? 271 LEU   A CB  1 
ATOM   1903 C  CG  . LEU   A 1 265 ? -20.708 -6.376  -2.117  1.00 29.03  ? 271 LEU   A CG  1 
ATOM   1904 C  CD1 . LEU   A 1 265 ? -20.718 -5.769  -3.493  1.00 28.81  ? 271 LEU   A CD1 1 
ATOM   1905 C  CD2 . LEU   A 1 265 ? -19.287 -6.712  -1.718  1.00 30.98  ? 271 LEU   A CD2 1 
ATOM   1906 N  N   . THR   A 1 266 ? -21.399 -4.065  1.760   1.00 26.53  ? 272 THR   A N   1 
ATOM   1907 C  CA  . THR   A 1 266 ? -21.858 -2.858  2.438   1.00 28.75  ? 272 THR   A CA  1 
ATOM   1908 C  C   . THR   A 1 266 ? -21.848 -1.740  1.391   1.00 34.38  ? 272 THR   A C   1 
ATOM   1909 O  O   . THR   A 1 266 ? -21.309 -1.929  0.290   1.00 33.68  ? 272 THR   A O   1 
ATOM   1910 C  CB  . THR   A 1 266 ? -20.988 -2.535  3.643   1.00 30.10  ? 272 THR   A CB  1 
ATOM   1911 O  OG1 . THR   A 1 266 ? -19.663 -2.254  3.189   1.00 30.14  ? 272 THR   A OG1 1 
ATOM   1912 C  CG2 . THR   A 1 266 ? -21.016 -3.656  4.719   1.00 29.20  ? 272 THR   A CG2 1 
ATOM   1913 N  N   . TYR   A 1 267 ? -22.446 -0.588  1.729   1.00 31.35  ? 273 TYR   A N   1 
ATOM   1914 C  CA  . TYR   A 1 267 ? -22.456 0.566   0.862   1.00 31.58  ? 273 TYR   A CA  1 
ATOM   1915 C  C   . TYR   A 1 267 ? -21.011 0.957   0.564   1.00 34.67  ? 273 TYR   A C   1 
ATOM   1916 O  O   . TYR   A 1 267 ? -20.657 1.177   -0.595  1.00 33.15  ? 273 TYR   A O   1 
ATOM   1917 C  CB  . TYR   A 1 267 ? -23.226 1.722   1.517   1.00 33.33  ? 273 TYR   A CB  1 
ATOM   1918 C  CG  . TYR   A 1 267 ? -23.175 2.996   0.705   1.00 35.98  ? 273 TYR   A CG  1 
ATOM   1919 C  CD1 . TYR   A 1 267 ? -22.118 3.895   0.847   1.00 37.18  ? 273 TYR   A CD1 1 
ATOM   1920 C  CD2 . TYR   A 1 267 ? -24.167 3.296   -0.217  1.00 37.41  ? 273 TYR   A CD2 1 
ATOM   1921 C  CE1 . TYR   A 1 267 ? -22.055 5.061   0.090   1.00 38.35  ? 273 TYR   A CE1 1 
ATOM   1922 C  CE2 . TYR   A 1 267 ? -24.113 4.461   -0.983  1.00 38.89  ? 273 TYR   A CE2 1 
ATOM   1923 C  CZ  . TYR   A 1 267 ? -23.054 5.341   -0.822  1.00 45.12  ? 273 TYR   A CZ  1 
ATOM   1924 O  OH  . TYR   A 1 267 ? -22.990 6.505   -1.549  1.00 48.24  ? 273 TYR   A OH  1 
ATOM   1925 N  N   . ARG   A 1 268 ? -20.169 0.949   1.606   1.00 30.84  ? 274 ARG   A N   1 
ATOM   1926 C  CA  . ARG   A 1 268 ? -18.752 1.287   1.528   1.00 29.84  ? 274 ARG   A CA  1 
ATOM   1927 C  C   . ARG   A 1 268 ? -17.963 0.349   0.599   1.00 33.21  ? 274 ARG   A C   1 
ATOM   1928 O  O   . ARG   A 1 268 ? -17.121 0.817   -0.159  1.00 32.89  ? 274 ARG   A O   1 
ATOM   1929 C  CB  . ARG   A 1 268 ? -18.150 1.323   2.940   1.00 29.58  ? 274 ARG   A CB  1 
ATOM   1930 C  CG  . ARG   A 1 268 ? -18.600 2.544   3.771   1.00 34.11  ? 274 ARG   A CG  1 
ATOM   1931 C  CD  . ARG   A 1 268 ? -18.428 2.360   5.269   1.00 29.10  ? 274 ARG   A CD  1 
ATOM   1932 N  NE  . ARG   A 1 268 ? -17.056 1.979   5.618   1.00 34.22  ? 274 ARG   A NE  1 
ATOM   1933 C  CZ  . ARG   A 1 268 ? -16.621 1.826   6.865   1.00 42.63  ? 274 ARG   A CZ  1 
ATOM   1934 N  NH1 . ARG   A 1 268 ? -17.425 2.074   7.891   1.00 32.62  ? 274 ARG   A NH1 1 
ATOM   1935 N  NH2 . ARG   A 1 268 ? -15.364 1.484   7.096   1.00 29.22  ? 274 ARG   A NH2 1 
ATOM   1936 N  N   . GLU   A 1 269 ? -18.195 -0.969  0.690   1.00 29.46  ? 275 GLU   A N   1 
ATOM   1937 C  CA  . GLU   A 1 269 ? -17.508 -1.953  -0.179  1.00 28.37  ? 275 GLU   A CA  1 
ATOM   1938 C  C   . GLU   A 1 269 ? -17.938 -1.771  -1.634  1.00 30.77  ? 275 GLU   A C   1 
ATOM   1939 O  O   . GLU   A 1 269 ? -17.094 -1.795  -2.511  1.00 31.24  ? 275 GLU   A O   1 
ATOM   1940 C  CB  . GLU   A 1 269 ? -17.777 -3.384  0.278   1.00 28.82  ? 275 GLU   A CB  1 
ATOM   1941 C  CG  . GLU   A 1 269 ? -17.098 -3.731  1.586   1.00 30.38  ? 275 GLU   A CG  1 
ATOM   1942 C  CD  . GLU   A 1 269 ? -17.591 -5.012  2.223   1.00 37.65  ? 275 GLU   A CD  1 
ATOM   1943 O  OE1 . GLU   A 1 269 ? -18.780 -5.352  2.040   1.00 28.69  ? 275 GLU   A OE1 1 
ATOM   1944 O  OE2 . GLU   A 1 269 ? -16.788 -5.674  2.916   1.00 31.20  ? 275 GLU   A OE2 1 
ATOM   1945 N  N   . GLY   A 1 270 ? -19.223 -1.520  -1.851  1.00 28.48  ? 276 GLY   A N   1 
ATOM   1946 C  CA  . GLY   A 1 270 ? -19.811 -1.286  -3.165  1.00 29.43  ? 276 GLY   A CA  1 
ATOM   1947 C  C   . GLY   A 1 270 ? -19.221 -0.077  -3.851  1.00 35.43  ? 276 GLY   A C   1 
ATOM   1948 O  O   . GLY   A 1 270 ? -18.845 -0.149  -5.025  1.00 34.96  ? 276 GLY   A O   1 
ATOM   1949 N  N   . MET   A 1 271 ? -19.087 1.028   -3.099  1.00 33.29  ? 277 MET   A N   1 
ATOM   1950 C  CA  . MET   A 1 271 ? -18.476 2.261   -3.607  1.00 32.70  ? 277 MET   A CA  1 
ATOM   1951 C  C   . MET   A 1 271 ? -17.010 2.044   -3.854  1.00 35.79  ? 277 MET   A C   1 
ATOM   1952 O  O   . MET   A 1 271 ? -16.471 2.585   -4.821  1.00 36.29  ? 277 MET   A O   1 
ATOM   1953 C  CB  . MET   A 1 271 ? -18.687 3.440   -2.642  1.00 35.20  ? 277 MET   A CB  1 
ATOM   1954 C  CG  . MET   A 1 271 ? -20.153 3.810   -2.465  1.00 39.17  ? 277 MET   A CG  1 
ATOM   1955 S  SD  . MET   A 1 271 ? -21.021 4.230   -4.001  1.00 43.18  ? 277 MET   A SD  1 
ATOM   1956 C  CE  . MET   A 1 271 ? -22.288 2.939   -4.047  1.00 39.39  ? 277 MET   A CE  1 
ATOM   1957 N  N   . TYR   A 1 272 ? -16.361 1.237   -3.005  1.00 30.29  ? 278 TYR   A N   1 
ATOM   1958 C  CA  . TYR   A 1 272 ? -14.939 0.945   -3.163  1.00 29.03  ? 278 TYR   A CA  1 
ATOM   1959 C  C   . TYR   A 1 272 ? -14.662 0.204   -4.477  1.00 31.43  ? 278 TYR   A C   1 
ATOM   1960 O  O   . TYR   A 1 272 ? -13.671 0.516   -5.158  1.00 28.88  ? 278 TYR   A O   1 
ATOM   1961 C  CB  . TYR   A 1 272 ? -14.379 0.171   -1.973  1.00 29.17  ? 278 TYR   A CB  1 
ATOM   1962 C  CG  . TYR   A 1 272 ? -12.871 0.082   -2.033  1.00 28.81  ? 278 TYR   A CG  1 
ATOM   1963 C  CD1 . TYR   A 1 272 ? -12.074 1.136   -1.593  1.00 31.89  ? 278 TYR   A CD1 1 
ATOM   1964 C  CD2 . TYR   A 1 272 ? -12.241 -1.015  -2.607  1.00 28.40  ? 278 TYR   A CD2 1 
ATOM   1965 C  CE1 . TYR   A 1 272 ? -10.685 1.094   -1.715  1.00 31.39  ? 278 TYR   A CE1 1 
ATOM   1966 C  CE2 . TYR   A 1 272 ? -10.850 -1.077  -2.709  1.00 28.23  ? 278 TYR   A CE2 1 
ATOM   1967 C  CZ  . TYR   A 1 272 ? -10.080 -0.020  -2.264  1.00 28.86  ? 278 TYR   A CZ  1 
ATOM   1968 O  OH  . TYR   A 1 272 ? -8.707  -0.074  -2.361  1.00 34.77  ? 278 TYR   A OH  1 
ATOM   1969 N  N   . ILE   A 1 273 ? -15.495 -0.812  -4.794  1.00 27.65  ? 279 ILE   A N   1 
ATOM   1970 C  CA  . ILE   A 1 273 ? -15.379 -1.587  -6.043  1.00 26.74  ? 279 ILE   A CA  1 
ATOM   1971 C  C   . ILE   A 1 273 ? -15.482 -0.596  -7.232  1.00 32.92  ? 279 ILE   A C   1 
ATOM   1972 O  O   . ILE   A 1 273 ? -14.600 -0.566  -8.097  1.00 33.23  ? 279 ILE   A O   1 
ATOM   1973 C  CB  . ILE   A 1 273 ? -16.489 -2.687  -6.125  1.00 28.82  ? 279 ILE   A CB  1 
ATOM   1974 C  CG1 . ILE   A 1 273 ? -16.199 -3.829  -5.117  1.00 27.18  ? 279 ILE   A CG1 1 
ATOM   1975 C  CG2 . ILE   A 1 273 ? -16.578 -3.259  -7.569  1.00 27.25  ? 279 ILE   A CG2 1 
ATOM   1976 C  CD1 . ILE   A 1 273 ? -17.392 -4.747  -4.882  1.00 28.07  ? 279 ILE   A CD1 1 
ATOM   1977 N  N   . ALA   A 1 274 ? -16.569 0.213   -7.240  1.00 29.71  ? 280 ALA   A N   1 
ATOM   1978 C  CA  . ALA   A 1 274 ? -16.846 1.205   -8.272  1.00 29.79  ? 280 ALA   A CA  1 
ATOM   1979 C  C   . ALA   A 1 274 ? -15.713 2.236   -8.447  1.00 34.80  ? 280 ALA   A C   1 
ATOM   1980 O  O   . ALA   A 1 274 ? -15.317 2.498   -9.585  1.00 33.54  ? 280 ALA   A O   1 
ATOM   1981 C  CB  . ALA   A 1 274 ? -18.184 1.869   -8.003  1.00 30.21  ? 280 ALA   A CB  1 
ATOM   1982 N  N   . GLU   A 1 275 ? -15.122 2.731   -7.330  1.00 32.36  ? 281 GLU   A N   1 
ATOM   1983 C  CA  . GLU   A 1 275 ? -13.999 3.683   -7.325  1.00 31.77  ? 281 GLU   A CA  1 
ATOM   1984 C  C   . GLU   A 1 275 ? -12.730 3.073   -7.914  1.00 35.05  ? 281 GLU   A C   1 
ATOM   1985 O  O   . GLU   A 1 275 ? -12.010 3.744   -8.671  1.00 34.09  ? 281 GLU   A O   1 
ATOM   1986 C  CB  . GLU   A 1 275 ? -13.696 4.185   -5.894  1.00 32.86  ? 281 GLU   A CB  1 
ATOM   1987 C  CG  . GLU   A 1 275 ? -14.670 5.209   -5.362  1.00 43.45  ? 281 GLU   A CG  1 
ATOM   1988 C  CD  . GLU   A 1 275 ? -14.659 5.388   -3.850  1.00 55.67  ? 281 GLU   A CD  1 
ATOM   1989 O  OE1 . GLU   A 1 275 ? -13.785 4.804   -3.166  1.00 47.03  ? 281 GLU   A OE1 1 
ATOM   1990 O  OE2 . GLU   A 1 275 ? -15.540 6.120   -3.350  1.00 40.48  ? 281 GLU   A OE2 1 
ATOM   1991 N  N   . GLU   A 1 276 ? -12.427 1.820   -7.541  1.00 30.91  ? 282 GLU   A N   1 
ATOM   1992 C  CA  . GLU   A 1 276 ? -11.244 1.137   -8.053  1.00 31.21  ? 282 GLU   A CA  1 
ATOM   1993 C  C   . GLU   A 1 276 ? -11.325 0.873   -9.550  1.00 34.26  ? 282 GLU   A C   1 
ATOM   1994 O  O   . GLU   A 1 276 ? -10.302 0.967   -10.229 1.00 34.06  ? 282 GLU   A O   1 
ATOM   1995 C  CB  . GLU   A 1 276 ? -10.905 -0.131  -7.273  1.00 32.47  ? 282 GLU   A CB  1 
ATOM   1996 C  CG  . GLU   A 1 276 ? -10.283 0.146   -5.914  1.00 37.44  ? 282 GLU   A CG  1 
ATOM   1997 C  CD  . GLU   A 1 276 ? -9.132  1.130   -5.926  1.00 42.82  ? 282 GLU   A CD  1 
ATOM   1998 O  OE1 . GLU   A 1 276 ? -8.053  0.786   -6.457  1.00 41.69  ? 282 GLU   A OE1 1 
ATOM   1999 O  OE2 . GLU   A 1 276 ? -9.333  2.270   -5.452  1.00 40.41  ? 282 GLU   A OE2 1 
ATOM   2000 N  N   . ILE   A 1 277 ? -12.537 0.592   -10.056 1.00 31.05  ? 283 ILE   A N   1 
ATOM   2001 C  CA  . ILE   A 1 277 ? -12.789 0.373   -11.487 1.00 31.40  ? 283 ILE   A CA  1 
ATOM   2002 C  C   . ILE   A 1 277 ? -12.531 1.709   -12.220 1.00 36.10  ? 283 ILE   A C   1 
ATOM   2003 O  O   . ILE   A 1 277 ? -11.840 1.712   -13.247 1.00 35.86  ? 283 ILE   A O   1 
ATOM   2004 C  CB  . ILE   A 1 277 ? -14.218 -0.211  -11.730 1.00 34.82  ? 283 ILE   A CB  1 
ATOM   2005 C  CG1 . ILE   A 1 277 ? -14.331 -1.710  -11.253 1.00 35.23  ? 283 ILE   A CG1 1 
ATOM   2006 C  CG2 . ILE   A 1 277 ? -14.708 -0.016  -13.201 1.00 36.49  ? 283 ILE   A CG2 1 
ATOM   2007 C  CD1 . ILE   A 1 277 ? -13.671 -2.762  -12.048 1.00 44.59  ? 283 ILE   A CD1 1 
ATOM   2008 N  N   . HIS   A 1 278 ? -13.047 2.833   -11.670 1.00 34.79  ? 284 HIS   A N   1 
ATOM   2009 C  CA  . HIS   A 1 278 ? -12.793 4.171   -12.237 1.00 35.71  ? 284 HIS   A CA  1 
ATOM   2010 C  C   . HIS   A 1 278 ? -11.285 4.464   -12.305 1.00 39.47  ? 284 HIS   A C   1 
ATOM   2011 O  O   . HIS   A 1 278 ? -10.799 4.914   -13.352 1.00 38.14  ? 284 HIS   A O   1 
ATOM   2012 C  CB  . HIS   A 1 278 ? -13.522 5.298   -11.478 1.00 37.24  ? 284 HIS   A CB  1 
ATOM   2013 C  CG  . HIS   A 1 278 ? -13.068 6.662   -11.927 1.00 41.68  ? 284 HIS   A CG  1 
ATOM   2014 N  ND1 . HIS   A 1 278 ? -13.565 7.243   -13.088 1.00 43.85  ? 284 HIS   A ND1 1 
ATOM   2015 C  CD2 . HIS   A 1 278 ? -12.095 7.461   -11.423 1.00 43.62  ? 284 HIS   A CD2 1 
ATOM   2016 C  CE1 . HIS   A 1 278 ? -12.923 8.394   -13.219 1.00 43.17  ? 284 HIS   A CE1 1 
ATOM   2017 N  NE2 . HIS   A 1 278 ? -12.012 8.561   -12.254 1.00 43.45  ? 284 HIS   A NE2 1 
ATOM   2018 N  N   . ASN   A 1 279 ? -10.546 4.183   -11.209 1.00 36.80  ? 285 ASN   A N   1 
ATOM   2019 C  CA  . ASN   A 1 279 ? -9.098  4.432   -11.097 1.00 36.47  ? 285 ASN   A CA  1 
ATOM   2020 C  C   . ASN   A 1 279 ? -8.238  3.701   -12.132 1.00 39.66  ? 285 ASN   A C   1 
ATOM   2021 O  O   . ASN   A 1 279 ? -7.107  4.139   -12.377 1.00 40.00  ? 285 ASN   A O   1 
ATOM   2022 C  CB  . ASN   A 1 279 ? -8.583  4.149   -9.668  1.00 39.76  ? 285 ASN   A CB  1 
ATOM   2023 C  CG  . ASN   A 1 279 ? -9.062  5.124   -8.615  1.00 63.43  ? 285 ASN   A CG  1 
ATOM   2024 O  OD1 . ASN   A 1 279 ? -9.490  6.243   -8.906  1.00 60.08  ? 285 ASN   A OD1 1 
ATOM   2025 N  ND2 . ASN   A 1 279 ? -8.981  4.728   -7.350  1.00 53.92  ? 285 ASN   A ND2 1 
ATOM   2026 N  N   . THR   A 1 280 ? -8.733  2.590   -12.727 1.00 34.83  ? 286 THR   A N   1 
ATOM   2027 C  CA  . THR   A 1 280 ? -7.967  1.889   -13.781 1.00 34.46  ? 286 THR   A CA  1 
ATOM   2028 C  C   . THR   A 1 280 ? -7.951  2.769   -15.048 1.00 39.45  ? 286 THR   A C   1 
ATOM   2029 O  O   . THR   A 1 280 ? -6.965  2.772   -15.778 1.00 40.05  ? 286 THR   A O   1 
ATOM   2030 C  CB  . THR   A 1 280 ? -8.550  0.505   -14.128 1.00 37.81  ? 286 THR   A CB  1 
ATOM   2031 O  OG1 . THR   A 1 280 ? -9.859  0.663   -14.675 1.00 35.88  ? 286 THR   A OG1 1 
ATOM   2032 C  CG2 . THR   A 1 280 ? -8.567  -0.460  -12.938 1.00 38.33  ? 286 THR   A CG2 1 
ATOM   2033 N  N   . GLY   A 1 281 ? -9.053  3.492   -15.267 1.00 36.38  ? 287 GLY   A N   1 
ATOM   2034 C  CA  . GLY   A 1 281 ? -9.284  4.345   -16.424 1.00 36.90  ? 287 GLY   A CA  1 
ATOM   2035 C  C   . GLY   A 1 281 ? -9.570  3.502   -17.651 1.00 41.72  ? 287 GLY   A C   1 
ATOM   2036 O  O   . GLY   A 1 281 ? -9.512  4.000   -18.774 1.00 41.90  ? 287 GLY   A O   1 
ATOM   2037 N  N   . LEU   A 1 282 ? -9.889  2.208   -17.426 1.00 36.93  ? 288 LEU   A N   1 
ATOM   2038 C  CA  . LEU   A 1 282 ? -10.123 1.190   -18.445 1.00 35.18  ? 288 LEU   A CA  1 
ATOM   2039 C  C   . LEU   A 1 282 ? -11.568 0.755   -18.555 1.00 38.03  ? 288 LEU   A C   1 
ATOM   2040 O  O   . LEU   A 1 282 ? -11.880 -0.123  -19.373 1.00 36.35  ? 288 LEU   A O   1 
ATOM   2041 C  CB  . LEU   A 1 282 ? -9.193  -0.011  -18.207 1.00 34.51  ? 288 LEU   A CB  1 
ATOM   2042 C  CG  . LEU   A 1 282 ? -7.710  0.203   -18.543 1.00 39.53  ? 288 LEU   A CG  1 
ATOM   2043 C  CD1 . LEU   A 1 282 ? -6.870  -0.943  -18.033 1.00 39.40  ? 288 LEU   A CD1 1 
ATOM   2044 C  CD2 . LEU   A 1 282 ? -7.487  0.369   -20.055 1.00 41.60  ? 288 LEU   A CD2 1 
ATOM   2045 N  N   . LEU   A 1 283 ? -12.463 1.401   -17.791 1.00 35.13  ? 289 LEU   A N   1 
ATOM   2046 C  CA  . LEU   A 1 283 ? -13.887 1.080   -17.865 1.00 35.05  ? 289 LEU   A CA  1 
ATOM   2047 C  C   . LEU   A 1 283 ? -14.442 1.400   -19.248 1.00 40.43  ? 289 LEU   A C   1 
ATOM   2048 O  O   . LEU   A 1 283 ? -14.311 2.525   -19.731 1.00 39.66  ? 289 LEU   A O   1 
ATOM   2049 C  CB  . LEU   A 1 283 ? -14.727 1.713   -16.748 1.00 34.16  ? 289 LEU   A CB  1 
ATOM   2050 C  CG  . LEU   A 1 283 ? -16.222 1.345   -16.766 1.00 37.66  ? 289 LEU   A CG  1 
ATOM   2051 C  CD1 . LEU   A 1 283 ? -16.440 -0.151  -16.522 1.00 37.23  ? 289 LEU   A CD1 1 
ATOM   2052 C  CD2 . LEU   A 1 283 ? -16.983 2.161   -15.798 1.00 38.90  ? 289 LEU   A CD2 1 
ATOM   2053 N  N   . SER   A 1 284 ? -15.059 0.393   -19.877 1.00 36.81  ? 290 SER   A N   1 
ATOM   2054 C  CA  . SER   A 1 284 ? -15.557 0.491   -21.238 1.00 35.89  ? 290 SER   A CA  1 
ATOM   2055 C  C   . SER   A 1 284 ? -17.058 0.286   -21.346 1.00 40.17  ? 290 SER   A C   1 
ATOM   2056 O  O   . SER   A 1 284 ? -17.677 0.765   -22.301 1.00 40.73  ? 290 SER   A O   1 
ATOM   2057 C  CB  . SER   A 1 284 ? -14.804 -0.504  -22.104 1.00 38.52  ? 290 SER   A CB  1 
ATOM   2058 O  OG  . SER   A 1 284 ? -15.095 -0.338  -23.480 1.00 40.60  ? 290 SER   A OG  1 
ATOM   2059 N  N   . ALA   A 1 285 ? -17.643 -0.455  -20.389 1.00 34.77  ? 291 ALA   A N   1 
ATOM   2060 C  CA  . ALA   A 1 285 ? -19.079 -0.728  -20.317 1.00 32.83  ? 291 ALA   A CA  1 
ATOM   2061 C  C   . ALA   A 1 285 ? -19.489 -1.137  -18.912 1.00 35.38  ? 291 ALA   A C   1 
ATOM   2062 O  O   . ALA   A 1 285 ? -18.712 -1.744  -18.183 1.00 34.27  ? 291 ALA   A O   1 
ATOM   2063 C  CB  . ALA   A 1 285 ? -19.496 -1.790  -21.326 1.00 33.19  ? 291 ALA   A CB  1 
ATOM   2064 N  N   . LEU   A 1 286 ? -20.718 -0.799  -18.544 1.00 31.57  ? 292 LEU   A N   1 
ATOM   2065 C  CA  . LEU   A 1 286 ? -21.276 -1.073  -17.241 1.00 31.70  ? 292 LEU   A CA  1 
ATOM   2066 C  C   . LEU   A 1 286 ? -22.702 -1.504  -17.382 1.00 34.37  ? 292 LEU   A C   1 
ATOM   2067 O  O   . LEU   A 1 286 ? -23.480 -0.823  -18.032 1.00 35.33  ? 292 LEU   A O   1 
ATOM   2068 C  CB  . LEU   A 1 286 ? -21.197 0.213   -16.379 1.00 32.31  ? 292 LEU   A CB  1 
ATOM   2069 C  CG  . LEU   A 1 286 ? -21.571 0.146   -14.891 1.00 37.52  ? 292 LEU   A CG  1 
ATOM   2070 C  CD1 . LEU   A 1 286 ? -20.931 1.274   -14.163 1.00 39.09  ? 292 LEU   A CD1 1 
ATOM   2071 C  CD2 . LEU   A 1 286 ? -23.067 0.272   -14.667 1.00 38.48  ? 292 LEU   A CD2 1 
ATOM   2072 N  N   . ASP   A 1 287 ? -23.061 -2.608  -16.731 1.00 30.21  ? 293 ASP   A N   1 
ATOM   2073 C  CA  . ASP   A 1 287 ? -24.443 -3.077  -16.631 1.00 28.88  ? 293 ASP   A CA  1 
ATOM   2074 C  C   . ASP   A 1 287 ? -24.846 -2.841  -15.176 1.00 33.80  ? 293 ASP   A C   1 
ATOM   2075 O  O   . ASP   A 1 287 ? -24.038 -3.106  -14.284 1.00 32.03  ? 293 ASP   A O   1 
ATOM   2076 C  CB  . ASP   A 1 287 ? -24.540 -4.581  -16.908 1.00 29.84  ? 293 ASP   A CB  1 
ATOM   2077 C  CG  . ASP   A 1 287 ? -23.945 -5.047  -18.207 1.00 37.24  ? 293 ASP   A CG  1 
ATOM   2078 O  OD1 . ASP   A 1 287 ? -24.091 -4.326  -19.216 1.00 35.18  ? 293 ASP   A OD1 1 
ATOM   2079 O  OD2 . ASP   A 1 287 ? -23.362 -6.158  -18.226 1.00 38.77  ? 293 ASP   A OD2 1 
ATOM   2080 N  N   . LEU   A 1 288 ? -26.064 -2.301  -14.934 1.00 30.76  ? 294 LEU   A N   1 
ATOM   2081 C  CA  . LEU   A 1 288 ? -26.614 -2.114  -13.596 1.00 30.78  ? 294 LEU   A CA  1 
ATOM   2082 C  C   . LEU   A 1 288 ? -27.969 -2.734  -13.676 1.00 34.94  ? 294 LEU   A C   1 
ATOM   2083 O  O   . LEU   A 1 288 ? -28.913 -2.124  -14.179 1.00 34.65  ? 294 LEU   A O   1 
ATOM   2084 C  CB  . LEU   A 1 288 ? -26.706 -0.628  -13.139 1.00 31.26  ? 294 LEU   A CB  1 
ATOM   2085 C  CG  . LEU   A 1 288 ? -26.809 -0.360  -11.595 1.00 35.34  ? 294 LEU   A CG  1 
ATOM   2086 C  CD1 . LEU   A 1 288 ? -27.979 -1.083  -10.953 1.00 34.25  ? 294 LEU   A CD1 1 
ATOM   2087 C  CD2 . LEU   A 1 288 ? -25.505 -0.702  -10.858 1.00 38.33  ? 294 LEU   A CD2 1 
ATOM   2088 N  N   . VAL   A 1 289 ? -28.065 -3.965  -13.189 1.00 30.22  ? 295 VAL   A N   1 
ATOM   2089 C  CA  . VAL   A 1 289 ? -29.276 -4.760  -13.331 1.00 29.96  ? 295 VAL   A CA  1 
ATOM   2090 C  C   . VAL   A 1 289 ? -29.964 -5.149  -12.027 1.00 34.25  ? 295 VAL   A C   1 
ATOM   2091 O  O   . VAL   A 1 289 ? -29.440 -4.961  -10.921 1.00 33.55  ? 295 VAL   A O   1 
ATOM   2092 C  CB  . VAL   A 1 289 ? -28.945 -6.036  -14.173 1.00 33.37  ? 295 VAL   A CB  1 
ATOM   2093 C  CG1 . VAL   A 1 289 ? -28.299 -5.686  -15.529 1.00 32.81  ? 295 VAL   A CG1 1 
ATOM   2094 C  CG2 . VAL   A 1 289 ? -28.070 -7.008  -13.386 1.00 32.45  ? 295 VAL   A CG2 1 
ATOM   2095 N  N   . GLU   A 1 290 ? -31.150 -5.749  -12.197 1.00 31.64  ? 296 GLU   A N   1 
ATOM   2096 C  CA  . GLU   A 1 290 ? -31.993 -6.384  -11.199 1.00 31.27  ? 296 GLU   A CA  1 
ATOM   2097 C  C   . GLU   A 1 290 ? -32.669 -5.410  -10.199 1.00 37.62  ? 296 GLU   A C   1 
ATOM   2098 O  O   . GLU   A 1 290 ? -33.222 -5.858  -9.194  1.00 38.12  ? 296 GLU   A O   1 
ATOM   2099 C  CB  . GLU   A 1 290 ? -31.220 -7.528  -10.487 1.00 32.44  ? 296 GLU   A CB  1 
ATOM   2100 C  CG  . GLU   A 1 290 ? -30.840 -8.685  -11.426 1.00 33.18  ? 296 GLU   A CG  1 
ATOM   2101 C  CD  . GLU   A 1 290 ? -31.954 -9.652  -11.814 1.00 48.38  ? 296 GLU   A CD  1 
ATOM   2102 O  OE1 . GLU   A 1 290 ? -33.062 -9.568  -11.234 1.00 47.21  ? 296 GLU   A OE1 1 
ATOM   2103 O  OE2 . GLU   A 1 290 ? -31.704 -10.528 -12.673 1.00 35.31  ? 296 GLU   A OE2 1 
ATOM   2104 N  N   . VAL   A 1 291 ? -32.713 -4.105  -10.508 1.00 34.81  ? 297 VAL   A N   1 
ATOM   2105 C  CA  . VAL   A 1 291 ? -33.482 -3.165  -9.687  1.00 34.29  ? 297 VAL   A CA  1 
ATOM   2106 C  C   . VAL   A 1 291 ? -34.965 -3.402  -10.067 1.00 39.15  ? 297 VAL   A C   1 
ATOM   2107 O  O   . VAL   A 1 291 ? -35.344 -3.193  -11.221 1.00 38.36  ? 297 VAL   A O   1 
ATOM   2108 C  CB  . VAL   A 1 291 ? -33.056 -1.674  -9.852  1.00 36.69  ? 297 VAL   A CB  1 
ATOM   2109 C  CG1 . VAL   A 1 291 ? -33.966 -0.744  -9.040  1.00 36.54  ? 297 VAL   A CG1 1 
ATOM   2110 C  CG2 . VAL   A 1 291 ? -31.593 -1.470  -9.451  1.00 35.35  ? 297 VAL   A CG2 1 
ATOM   2111 N  N   . ASN   A 1 292 ? -35.750 -3.933  -9.119  1.00 37.43  ? 298 ASN   A N   1 
ATOM   2112 C  CA  . ASN   A 1 292 ? -37.176 -4.200  -9.284  1.00 38.31  ? 298 ASN   A CA  1 
ATOM   2113 C  C   . ASN   A 1 292 ? -37.954 -3.342  -8.248  1.00 46.75  ? 298 ASN   A C   1 
ATOM   2114 O  O   . ASN   A 1 292 ? -38.208 -3.799  -7.123  1.00 45.33  ? 298 ASN   A O   1 
ATOM   2115 C  CB  . ASN   A 1 292 ? -37.491 -5.701  -9.171  1.00 36.12  ? 298 ASN   A CB  1 
ATOM   2116 C  CG  . ASN   A 1 292 ? -38.941 -6.048  -9.438  1.00 50.57  ? 298 ASN   A CG  1 
ATOM   2117 O  OD1 . ASN   A 1 292 ? -39.863 -5.239  -9.252  1.00 43.35  ? 298 ASN   A OD1 1 
ATOM   2118 N  ND2 . ASN   A 1 292 ? -39.183 -7.252  -9.915  1.00 44.84  ? 298 ASN   A ND2 1 
ATOM   2119 N  N   . PRO   A 1 293 ? -38.355 -2.102  -8.628  1.00 47.58  ? 299 PRO   A N   1 
ATOM   2120 C  CA  . PRO   A 1 293 ? -39.052 -1.221  -7.665  1.00 48.55  ? 299 PRO   A CA  1 
ATOM   2121 C  C   . PRO   A 1 293 ? -40.390 -1.731  -7.122  1.00 53.29  ? 299 PRO   A C   1 
ATOM   2122 O  O   . PRO   A 1 293 ? -40.747 -1.369  -6.004  1.00 53.65  ? 299 PRO   A O   1 
ATOM   2123 C  CB  . PRO   A 1 293 ? -39.208 0.103   -8.424  1.00 50.54  ? 299 PRO   A CB  1 
ATOM   2124 C  CG  . PRO   A 1 293 ? -39.016 -0.224  -9.840  1.00 54.67  ? 299 PRO   A CG  1 
ATOM   2125 C  CD  . PRO   A 1 293 ? -38.113 -1.412  -9.913  1.00 49.71  ? 299 PRO   A CD  1 
ATOM   2126 N  N   . GLN   A 1 294 ? -41.096 -2.596  -7.862  1.00 51.05  ? 300 GLN   A N   1 
ATOM   2127 C  CA  . GLN   A 1 294 ? -42.386 -3.159  -7.437  1.00 51.81  ? 300 GLN   A CA  1 
ATOM   2128 C  C   . GLN   A 1 294 ? -42.285 -4.142  -6.255  1.00 56.69  ? 300 GLN   A C   1 
ATOM   2129 O  O   . GLN   A 1 294 ? -43.301 -4.407  -5.600  1.00 56.22  ? 300 GLN   A O   1 
ATOM   2130 C  CB  . GLN   A 1 294 ? -43.101 -3.833  -8.621  1.00 53.79  ? 300 GLN   A CB  1 
ATOM   2131 C  CG  . GLN   A 1 294 ? -43.610 -2.859  -9.686  1.00 75.47  ? 300 GLN   A CG  1 
ATOM   2132 C  CD  . GLN   A 1 294 ? -44.578 -3.494  -10.661 1.00 99.61  ? 300 GLN   A CD  1 
ATOM   2133 O  OE1 . GLN   A 1 294 ? -44.665 -4.722  -10.801 1.00 96.30  ? 300 GLN   A OE1 1 
ATOM   2134 N  NE2 . GLN   A 1 294 ? -45.334 -2.659  -11.364 1.00 91.69  ? 300 GLN   A NE2 1 
ATOM   2135 N  N   . LEU   A 1 295 ? -41.073 -4.677  -5.982  1.00 53.12  ? 301 LEU   A N   1 
ATOM   2136 C  CA  . LEU   A 1 295 ? -40.843 -5.652  -4.913  1.00 52.93  ? 301 LEU   A CA  1 
ATOM   2137 C  C   . LEU   A 1 295 ? -40.497 -5.034  -3.552  1.00 60.50  ? 301 LEU   A C   1 
ATOM   2138 O  O   . LEU   A 1 295 ? -40.497 -5.743  -2.535  1.00 60.21  ? 301 LEU   A O   1 
ATOM   2139 C  CB  . LEU   A 1 295 ? -39.795 -6.689  -5.330  1.00 52.16  ? 301 LEU   A CB  1 
ATOM   2140 C  CG  . LEU   A 1 295 ? -40.257 -7.689  -6.381  1.00 55.91  ? 301 LEU   A CG  1 
ATOM   2141 C  CD1 . LEU   A 1 295 ? -39.143 -8.635  -6.734  1.00 55.99  ? 301 LEU   A CD1 1 
ATOM   2142 C  CD2 . LEU   A 1 295 ? -41.491 -8.457  -5.924  1.00 56.55  ? 301 LEU   A CD2 1 
ATOM   2143 N  N   . ALA   A 1 296 ? -40.230 -3.718  -3.526  1.00 59.53  ? 302 ALA   A N   1 
ATOM   2144 C  CA  . ALA   A 1 296 ? -39.959 -2.987  -2.288  1.00 60.46  ? 302 ALA   A CA  1 
ATOM   2145 C  C   . ALA   A 1 296 ? -41.270 -2.905  -1.484  1.00 66.32  ? 302 ALA   A C   1 
ATOM   2146 O  O   . ALA   A 1 296 ? -42.350 -2.845  -2.082  1.00 65.68  ? 302 ALA   A O   1 
ATOM   2147 C  CB  . ALA   A 1 296 ? -39.458 -1.594  -2.617  1.00 61.26  ? 302 ALA   A CB  1 
ATOM   2148 N  N   . THR   A 1 297 ? -41.181 -2.949  -0.145  1.00 65.08  ? 303 THR   A N   1 
ATOM   2149 C  CA  . THR   A 1 297 ? -42.367 -2.906  0.726   1.00 65.74  ? 303 THR   A CA  1 
ATOM   2150 C  C   . THR   A 1 297 ? -42.980 -1.502  0.816   1.00 70.63  ? 303 THR   A C   1 
ATOM   2151 O  O   . THR   A 1 297 ? -44.136 -1.362  1.228   1.00 70.33  ? 303 THR   A O   1 
ATOM   2152 C  CB  . THR   A 1 297 ? -42.068 -3.500  2.107   1.00 74.53  ? 303 THR   A CB  1 
ATOM   2153 O  OG1 . THR   A 1 297 ? -41.012 -2.761  2.718   1.00 72.94  ? 303 THR   A OG1 1 
ATOM   2154 C  CG2 . THR   A 1 297 ? -41.724 -4.986  2.049   1.00 74.49  ? 303 THR   A CG2 1 
ATOM   2155 N  N   . SER   A 1 298 ? -42.202 -0.473  0.421   1.00 67.26  ? 304 SER   A N   1 
ATOM   2156 C  CA  . SER   A 1 298 ? -42.586 0.936   0.438   1.00 67.15  ? 304 SER   A CA  1 
ATOM   2157 C  C   . SER   A 1 298 ? -41.922 1.705   -0.720  1.00 71.47  ? 304 SER   A C   1 
ATOM   2158 O  O   . SER   A 1 298 ? -41.045 1.157   -1.393  1.00 70.90  ? 304 SER   A O   1 
ATOM   2159 C  CB  . SER   A 1 298 ? -42.185 1.561   1.771   1.00 70.61  ? 304 SER   A CB  1 
ATOM   2160 O  OG  . SER   A 1 298 ? -40.789 1.429   1.988   1.00 78.36  ? 304 SER   A OG  1 
ATOM   2161 N  N   . GLU   A 1 299 ? -42.331 2.980   -0.934  1.00 68.06  ? 305 GLU   A N   1 
ATOM   2162 C  CA  . GLU   A 1 299 ? -41.770 3.861   -1.964  1.00 68.07  ? 305 GLU   A CA  1 
ATOM   2163 C  C   . GLU   A 1 299 ? -40.334 4.262   -1.595  1.00 71.49  ? 305 GLU   A C   1 
ATOM   2164 O  O   . GLU   A 1 299 ? -39.501 4.447   -2.487  1.00 71.27  ? 305 GLU   A O   1 
ATOM   2165 C  CB  . GLU   A 1 299 ? -42.644 5.116   -2.141  1.00 69.66  ? 305 GLU   A CB  1 
ATOM   2166 C  CG  . GLU   A 1 299 ? -42.447 5.811   -3.479  1.00 82.69  ? 305 GLU   A CG  1 
ATOM   2167 C  CD  . GLU   A 1 299 ? -43.179 7.128   -3.658  1.00 106.57 ? 305 GLU   A CD  1 
ATOM   2168 O  OE1 . GLU   A 1 299 ? -44.431 7.131   -3.610  1.00 98.22  ? 305 GLU   A OE1 1 
ATOM   2169 O  OE2 . GLU   A 1 299 ? -42.498 8.152   -3.893  1.00 102.74 ? 305 GLU   A OE2 1 
ATOM   2170 N  N   . GLU   A 1 300 ? -40.047 4.379   -0.283  1.00 67.00  ? 306 GLU   A N   1 
ATOM   2171 C  CA  . GLU   A 1 300 ? -38.724 4.754   0.201   1.00 66.77  ? 306 GLU   A CA  1 
ATOM   2172 C  C   . GLU   A 1 300 ? -37.692 3.649   -0.025  1.00 68.19  ? 306 GLU   A C   1 
ATOM   2173 O  O   . GLU   A 1 300 ? -36.534 3.969   -0.265  1.00 68.10  ? 306 GLU   A O   1 
ATOM   2174 C  CB  . GLU   A 1 300 ? -38.746 5.254   1.664   1.00 68.72  ? 306 GLU   A CB  1 
ATOM   2175 C  CG  . GLU   A 1 300 ? -39.251 4.274   2.713   1.00 82.51  ? 306 GLU   A CG  1 
ATOM   2176 C  CD  . GLU   A 1 300 ? -39.340 4.866   4.108   1.00 111.32 ? 306 GLU   A CD  1 
ATOM   2177 O  OE1 . GLU   A 1 300 ? -38.285 4.985   4.773   1.00 111.41 ? 306 GLU   A OE1 1 
ATOM   2178 O  OE2 . GLU   A 1 300 ? -40.463 5.222   4.532   1.00 106.45 ? 306 GLU   A OE2 1 
ATOM   2179 N  N   . GLU   A 1 301 ? -38.112 2.368   0.020   1.00 62.68  ? 307 GLU   A N   1 
ATOM   2180 C  CA  . GLU   A 1 301 ? -37.245 1.203   -0.227  1.00 61.29  ? 307 GLU   A CA  1 
ATOM   2181 C  C   . GLU   A 1 301 ? -36.921 1.092   -1.726  1.00 61.71  ? 307 GLU   A C   1 
ATOM   2182 O  O   . GLU   A 1 301 ? -35.801 0.722   -2.088  1.00 60.76  ? 307 GLU   A O   1 
ATOM   2183 C  CB  . GLU   A 1 301 ? -37.890 -0.090  0.298   1.00 62.73  ? 307 GLU   A CB  1 
ATOM   2184 C  CG  . GLU   A 1 301 ? -37.813 -0.263  1.808   1.00 73.18  ? 307 GLU   A CG  1 
ATOM   2185 C  CD  . GLU   A 1 301 ? -37.876 -1.694  2.314   1.00 97.05  ? 307 GLU   A CD  1 
ATOM   2186 O  OE1 . GLU   A 1 301 ? -38.444 -2.564  1.611   1.00 82.15  ? 307 GLU   A OE1 1 
ATOM   2187 O  OE2 . GLU   A 1 301 ? -37.352 -1.945  3.423   1.00 98.30  ? 307 GLU   A OE2 1 
ATOM   2188 N  N   . ALA   A 1 302 ? -37.901 1.446   -2.590  1.00 56.32  ? 308 ALA   A N   1 
ATOM   2189 C  CA  . ALA   A 1 302 ? -37.766 1.502   -4.049  1.00 55.10  ? 308 ALA   A CA  1 
ATOM   2190 C  C   . ALA   A 1 302 ? -36.785 2.617   -4.404  1.00 54.86  ? 308 ALA   A C   1 
ATOM   2191 O  O   . ALA   A 1 302 ? -35.891 2.406   -5.232  1.00 53.02  ? 308 ALA   A O   1 
ATOM   2192 C  CB  . ALA   A 1 302 ? -39.119 1.782   -4.689  1.00 55.93  ? 308 ALA   A CB  1 
ATOM   2193 N  N   . LYS   A 1 303 ? -36.939 3.799   -3.745  1.00 49.49  ? 309 LYS   A N   1 
ATOM   2194 C  CA  . LYS   A 1 303 ? -36.074 4.966   -3.916  1.00 47.92  ? 309 LYS   A CA  1 
ATOM   2195 C  C   . LYS   A 1 303 ? -34.671 4.696   -3.405  1.00 49.86  ? 309 LYS   A C   1 
ATOM   2196 O  O   . LYS   A 1 303 ? -33.722 5.083   -4.076  1.00 49.60  ? 309 LYS   A O   1 
ATOM   2197 C  CB  . LYS   A 1 303 ? -36.656 6.214   -3.233  1.00 51.08  ? 309 LYS   A CB  1 
ATOM   2198 C  CG  . LYS   A 1 303 ? -37.746 6.906   -4.048  1.00 70.80  ? 309 LYS   A CG  1 
ATOM   2199 C  CD  . LYS   A 1 303 ? -38.130 8.247   -3.435  1.00 84.87  ? 309 LYS   A CD  1 
ATOM   2200 C  CE  . LYS   A 1 303 ? -39.133 9.001   -4.278  1.00 99.42  ? 309 LYS   A CE  1 
ATOM   2201 N  NZ  . LYS   A 1 303 ? -39.370 10.375  -3.755  1.00 108.73 ? 309 LYS   A NZ  1 
ATOM   2202 N  N   . THR   A 1 304 ? -34.531 4.039   -2.225  1.00 45.52  ? 310 THR   A N   1 
ATOM   2203 C  CA  . THR   A 1 304 ? -33.221 3.697   -1.639  1.00 44.63  ? 310 THR   A CA  1 
ATOM   2204 C  C   . THR   A 1 304 ? -32.420 2.840   -2.625  1.00 44.11  ? 310 THR   A C   1 
ATOM   2205 O  O   . THR   A 1 304 ? -31.265 3.164   -2.898  1.00 42.51  ? 310 THR   A O   1 
ATOM   2206 C  CB  . THR   A 1 304 ? -33.374 3.035   -0.242  1.00 54.26  ? 310 THR   A CB  1 
ATOM   2207 O  OG1 . THR   A 1 304 ? -33.990 3.959   0.648   1.00 57.71  ? 310 THR   A OG1 1 
ATOM   2208 C  CG2 . THR   A 1 304 ? -32.045 2.609   0.359   1.00 52.78  ? 310 THR   A CG2 1 
ATOM   2209 N  N   . THR   A 1 305 ? -33.056 1.774   -3.170  1.00 39.97  ? 311 THR   A N   1 
ATOM   2210 C  CA  . THR   A 1 305 ? -32.457 0.856   -4.153  1.00 39.08  ? 311 THR   A CA  1 
ATOM   2211 C  C   . THR   A 1 305 ? -32.013 1.622   -5.400  1.00 42.29  ? 311 THR   A C   1 
ATOM   2212 O  O   . THR   A 1 305 ? -30.859 1.480   -5.829  1.00 40.19  ? 311 THR   A O   1 
ATOM   2213 C  CB  . THR   A 1 305 ? -33.418 -0.310  -4.469  1.00 45.62  ? 311 THR   A CB  1 
ATOM   2214 O  OG1 . THR   A 1 305 ? -33.848 -0.931  -3.252  1.00 42.68  ? 311 THR   A OG1 1 
ATOM   2215 C  CG2 . THR   A 1 305 ? -32.789 -1.365  -5.382  1.00 44.00  ? 311 THR   A CG2 1 
ATOM   2216 N  N   . ALA   A 1 306 ? -32.927 2.450   -5.969  1.00 39.68  ? 312 ALA   A N   1 
ATOM   2217 C  CA  . ALA   A 1 306 ? -32.678 3.280   -7.146  1.00 39.77  ? 312 ALA   A CA  1 
ATOM   2218 C  C   . ALA   A 1 306 ? -31.522 4.262   -6.924  1.00 42.47  ? 312 ALA   A C   1 
ATOM   2219 O  O   . ALA   A 1 306 ? -30.663 4.382   -7.797  1.00 42.05  ? 312 ALA   A O   1 
ATOM   2220 C  CB  . ALA   A 1 306 ? -33.949 4.027   -7.539  1.00 41.03  ? 312 ALA   A CB  1 
ATOM   2221 N  N   . ASN   A 1 307 ? -31.469 4.927   -5.739  1.00 39.46  ? 313 ASN   A N   1 
ATOM   2222 C  CA  . ASN   A 1 307 ? -30.397 5.873   -5.387  1.00 38.44  ? 313 ASN   A CA  1 
ATOM   2223 C  C   . ASN   A 1 307 ? -29.053 5.173   -5.261  1.00 40.04  ? 313 ASN   A C   1 
ATOM   2224 O  O   . ASN   A 1 307 ? -28.017 5.745   -5.610  1.00 39.69  ? 313 ASN   A O   1 
ATOM   2225 C  CB  . ASN   A 1 307 ? -30.720 6.612   -4.087  1.00 41.44  ? 313 ASN   A CB  1 
ATOM   2226 C  CG  . ASN   A 1 307 ? -31.851 7.619   -4.178  1.00 66.39  ? 313 ASN   A CG  1 
ATOM   2227 O  OD1 . ASN   A 1 307 ? -32.298 8.028   -5.259  1.00 59.79  ? 313 ASN   A OD1 1 
ATOM   2228 N  ND2 . ASN   A 1 307 ? -32.333 8.051   -3.028  1.00 59.34  ? 313 ASN   A ND2 1 
ATOM   2229 N  N   . LEU   A 1 308 ? -29.069 3.938   -4.747  1.00 36.75  ? 314 LEU   A N   1 
ATOM   2230 C  CA  . LEU   A 1 308 ? -27.853 3.130   -4.612  1.00 36.16  ? 314 LEU   A CA  1 
ATOM   2231 C  C   . LEU   A 1 308 ? -27.329 2.780   -6.019  1.00 37.69  ? 314 LEU   A C   1 
ATOM   2232 O  O   . LEU   A 1 308 ? -26.128 2.916   -6.271  1.00 35.95  ? 314 LEU   A O   1 
ATOM   2233 C  CB  . LEU   A 1 308 ? -28.173 1.875   -3.774  1.00 36.11  ? 314 LEU   A CB  1 
ATOM   2234 C  CG  . LEU   A 1 308 ? -27.060 0.868   -3.490  1.00 40.13  ? 314 LEU   A CG  1 
ATOM   2235 C  CD1 . LEU   A 1 308 ? -25.894 1.505   -2.754  1.00 40.30  ? 314 LEU   A CD1 1 
ATOM   2236 C  CD2 . LEU   A 1 308 ? -27.603 -0.315  -2.727  1.00 41.17  ? 314 LEU   A CD2 1 
ATOM   2237 N  N   . ALA   A 1 309 ? -28.244 2.417   -6.954  1.00 33.49  ? 315 ALA   A N   1 
ATOM   2238 C  CA  . ALA   A 1 309 ? -27.886 2.123   -8.357  1.00 33.44  ? 315 ALA   A CA  1 
ATOM   2239 C  C   . ALA   A 1 309 ? -27.180 3.348   -8.996  1.00 37.05  ? 315 ALA   A C   1 
ATOM   2240 O  O   . ALA   A 1 309 ? -26.140 3.188   -9.631  1.00 35.65  ? 315 ALA   A O   1 
ATOM   2241 C  CB  . ALA   A 1 309 ? -29.138 1.752   -9.149  1.00 34.13  ? 315 ALA   A CB  1 
ATOM   2242 N  N   . VAL   A 1 310 ? -27.704 4.579   -8.739  1.00 35.37  ? 316 VAL   A N   1 
ATOM   2243 C  CA  . VAL   A 1 310 ? -27.129 5.852   -9.219  1.00 34.40  ? 316 VAL   A CA  1 
ATOM   2244 C  C   . VAL   A 1 310 ? -25.736 6.075   -8.620  1.00 37.47  ? 316 VAL   A C   1 
ATOM   2245 O  O   . VAL   A 1 310 ? -24.821 6.494   -9.331  1.00 37.15  ? 316 VAL   A O   1 
ATOM   2246 C  CB  . VAL   A 1 310 ? -28.088 7.059   -8.972  1.00 38.29  ? 316 VAL   A CB  1 
ATOM   2247 C  CG1 . VAL   A 1 310 ? -27.465 8.383   -9.415  1.00 38.33  ? 316 VAL   A CG1 1 
ATOM   2248 C  CG2 . VAL   A 1 310 ? -29.416 6.849   -9.669  1.00 38.07  ? 316 VAL   A CG2 1 
ATOM   2249 N  N   . ASP   A 1 311 ? -25.557 5.758   -7.320  1.00 34.26  ? 317 ASP   A N   1 
ATOM   2250 C  CA  . ASP   A 1 311 ? -24.262 5.928   -6.660  1.00 33.18  ? 317 ASP   A CA  1 
ATOM   2251 C  C   . ASP   A 1 311 ? -23.191 4.998   -7.248  1.00 35.95  ? 317 ASP   A C   1 
ATOM   2252 O  O   . ASP   A 1 311 ? -22.036 5.401   -7.360  1.00 35.36  ? 317 ASP   A O   1 
ATOM   2253 C  CB  . ASP   A 1 311 ? -24.401 5.722   -5.137  1.00 35.12  ? 317 ASP   A CB  1 
ATOM   2254 C  CG  . ASP   A 1 311 ? -25.120 6.828   -4.372  1.00 43.96  ? 317 ASP   A CG  1 
ATOM   2255 O  OD1 . ASP   A 1 311 ? -25.342 7.908   -4.955  1.00 45.39  ? 317 ASP   A OD1 1 
ATOM   2256 O  OD2 . ASP   A 1 311 ? -25.411 6.626   -3.171  1.00 46.33  ? 317 ASP   A OD2 1 
ATOM   2257 N  N   . VAL   A 1 312 ? -23.565 3.761   -7.630  1.00 33.54  ? 318 VAL   A N   1 
ATOM   2258 C  CA  . VAL   A 1 312 ? -22.605 2.810   -8.236  1.00 32.89  ? 318 VAL   A CA  1 
ATOM   2259 C  C   . VAL   A 1 312 ? -22.119 3.362   -9.592  1.00 36.20  ? 318 VAL   A C   1 
ATOM   2260 O  O   . VAL   A 1 312 ? -20.910 3.431   -9.859  1.00 35.75  ? 318 VAL   A O   1 
ATOM   2261 C  CB  . VAL   A 1 312 ? -23.210 1.376   -8.364  1.00 36.05  ? 318 VAL   A CB  1 
ATOM   2262 C  CG1 . VAL   A 1 312 ? -22.388 0.491   -9.314  1.00 35.42  ? 318 VAL   A CG1 1 
ATOM   2263 C  CG2 . VAL   A 1 312 ? -23.330 0.717   -6.991  1.00 36.05  ? 318 VAL   A CG2 1 
ATOM   2264 N  N   . ILE   A 1 313 ? -23.072 3.750   -10.433 1.00 34.41  ? 319 ILE   A N   1 
ATOM   2265 C  CA  . ILE   A 1 313 ? -22.779 4.274   -11.774 1.00 34.20  ? 319 ILE   A CA  1 
ATOM   2266 C  C   . ILE   A 1 313 ? -21.924 5.550   -11.669 1.00 38.18  ? 319 ILE   A C   1 
ATOM   2267 O  O   . ILE   A 1 313 ? -20.846 5.610   -12.270 1.00 36.48  ? 319 ILE   A O   1 
ATOM   2268 C  CB  . ILE   A 1 313 ? -24.063 4.426   -12.634 1.00 36.47  ? 319 ILE   A CB  1 
ATOM   2269 C  CG1 . ILE   A 1 313 ? -24.844 3.076   -12.689 1.00 35.36  ? 319 ILE   A CG1 1 
ATOM   2270 C  CG2 . ILE   A 1 313 ? -23.674 4.899   -14.053 1.00 37.70  ? 319 ILE   A CG2 1 
ATOM   2271 C  CD1 . ILE   A 1 313 ? -26.332 3.158   -13.089 1.00 36.20  ? 319 ILE   A CD1 1 
ATOM   2272 N  N   . ALA   A 1 314 ? -22.362 6.511   -10.833 1.00 37.65  ? 320 ALA   A N   1 
ATOM   2273 C  CA  . ALA   A 1 314 ? -21.641 7.756   -10.582 1.00 37.33  ? 320 ALA   A CA  1 
ATOM   2274 C  C   . ALA   A 1 314 ? -20.227 7.490   -10.088 1.00 38.18  ? 320 ALA   A C   1 
ATOM   2275 O  O   . ALA   A 1 314 ? -19.310 8.086   -10.620 1.00 36.75  ? 320 ALA   A O   1 
ATOM   2276 C  CB  . ALA   A 1 314 ? -22.403 8.617   -9.587  1.00 38.92  ? 320 ALA   A CB  1 
ATOM   2277 N  N   . SER   A 1 315 ? -20.027 6.540   -9.127  1.00 35.71  ? 321 SER   A N   1 
ATOM   2278 C  CA  . SER   A 1 315 ? -18.688 6.198   -8.641  1.00 34.73  ? 321 SER   A CA  1 
ATOM   2279 C  C   . SER   A 1 315 ? -17.842 5.523   -9.700  1.00 36.69  ? 321 SER   A C   1 
ATOM   2280 O  O   . SER   A 1 315 ? -16.626 5.716   -9.709  1.00 36.06  ? 321 SER   A O   1 
ATOM   2281 C  CB  . SER   A 1 315 ? -18.749 5.345   -7.375  1.00 37.94  ? 321 SER   A CB  1 
ATOM   2282 O  OG  . SER   A 1 315 ? -19.548 5.987   -6.397  1.00 43.80  ? 321 SER   A OG  1 
ATOM   2283 N  N   . SER   A 1 316 ? -18.473 4.770   -10.622 1.00 33.16  ? 322 SER   A N   1 
ATOM   2284 C  CA  . SER   A 1 316 ? -17.737 4.115   -11.705 1.00 33.76  ? 322 SER   A CA  1 
ATOM   2285 C  C   . SER   A 1 316 ? -17.202 5.154   -12.716 1.00 39.21  ? 322 SER   A C   1 
ATOM   2286 O  O   . SER   A 1 316 ? -16.241 4.868   -13.422 1.00 38.19  ? 322 SER   A O   1 
ATOM   2287 C  CB  . SER   A 1 316 ? -18.613 3.085   -12.411 1.00 37.32  ? 322 SER   A CB  1 
ATOM   2288 O  OG  . SER   A 1 316 ? -19.117 2.096   -11.527 1.00 39.14  ? 322 SER   A OG  1 
ATOM   2289 N  N   . PHE   A 1 317 ? -17.786 6.376   -12.720 1.00 38.65  ? 323 PHE   A N   1 
ATOM   2290 C  CA  . PHE   A 1 317 ? -17.373 7.463   -13.610 1.00 39.70  ? 323 PHE   A CA  1 
ATOM   2291 C  C   . PHE   A 1 317 ? -16.746 8.679   -12.878 1.00 45.54  ? 323 PHE   A C   1 
ATOM   2292 O  O   . PHE   A 1 317 ? -16.699 9.790   -13.430 1.00 45.08  ? 323 PHE   A O   1 
ATOM   2293 C  CB  . PHE   A 1 317 ? -18.532 7.864   -14.540 1.00 40.85  ? 323 PHE   A CB  1 
ATOM   2294 C  CG  . PHE   A 1 317 ? -18.826 6.763   -15.543 1.00 41.64  ? 323 PHE   A CG  1 
ATOM   2295 C  CD1 . PHE   A 1 317 ? -17.942 6.493   -16.585 1.00 43.80  ? 323 PHE   A CD1 1 
ATOM   2296 C  CD2 . PHE   A 1 317 ? -19.973 5.987   -15.434 1.00 42.69  ? 323 PHE   A CD2 1 
ATOM   2297 C  CE1 . PHE   A 1 317 ? -18.194 5.453   -17.485 1.00 44.37  ? 323 PHE   A CE1 1 
ATOM   2298 C  CE2 . PHE   A 1 317 ? -20.218 4.942   -16.331 1.00 44.87  ? 323 PHE   A CE2 1 
ATOM   2299 C  CZ  . PHE   A 1 317 ? -19.338 4.693   -17.361 1.00 42.68  ? 323 PHE   A CZ  1 
ATOM   2300 N  N   . GLY   A 1 318 ? -16.214 8.448   -11.672 1.00 41.93  ? 324 GLY   A N   1 
ATOM   2301 C  CA  . GLY   A 1 318 ? -15.486 9.484   -10.957 1.00 41.50  ? 324 GLY   A CA  1 
ATOM   2302 C  C   . GLY   A 1 318 ? -16.023 10.048  -9.662  1.00 45.59  ? 324 GLY   A C   1 
ATOM   2303 O  O   . GLY   A 1 318 ? -15.307 10.827  -9.027  1.00 45.36  ? 324 GLY   A O   1 
ATOM   2304 N  N   . GLN   A 1 319 ? -17.267 9.714   -9.254  1.00 42.37  ? 325 GLN   A N   1 
ATOM   2305 C  CA  . GLN   A 1 319 ? -17.759 10.229  -7.966  1.00 43.72  ? 325 GLN   A CA  1 
ATOM   2306 C  C   . GLN   A 1 319 ? -16.944 9.588   -6.838  1.00 49.95  ? 325 GLN   A C   1 
ATOM   2307 O  O   . GLN   A 1 319 ? -16.683 8.387   -6.872  1.00 49.30  ? 325 GLN   A O   1 
ATOM   2308 C  CB  . GLN   A 1 319 ? -19.261 9.992   -7.785  1.00 45.57  ? 325 GLN   A CB  1 
ATOM   2309 C  CG  . GLN   A 1 319 ? -19.834 10.626  -6.519  1.00 59.30  ? 325 GLN   A CG  1 
ATOM   2310 C  CD  . GLN   A 1 319 ? -21.196 10.079  -6.218  1.00 68.77  ? 325 GLN   A CD  1 
ATOM   2311 O  OE1 . GLN   A 1 319 ? -21.359 9.004   -5.618  1.00 62.15  ? 325 GLN   A OE1 1 
ATOM   2312 N  NE2 . GLN   A 1 319 ? -22.200 10.781  -6.685  1.00 54.53  ? 325 GLN   A NE2 1 
ATOM   2313 N  N   . THR   A 1 320 ? -16.444 10.401  -5.908  1.00 49.29  ? 326 THR   A N   1 
ATOM   2314 C  CA  . THR   A 1 320 ? -15.591 9.869   -4.855  1.00 50.49  ? 326 THR   A CA  1 
ATOM   2315 C  C   . THR   A 1 320 ? -16.082 10.308  -3.464  1.00 55.69  ? 326 THR   A C   1 
ATOM   2316 O  O   . THR   A 1 320 ? -16.948 11.185  -3.342  1.00 54.37  ? 326 THR   A O   1 
ATOM   2317 C  CB  . THR   A 1 320 ? -14.100 10.175  -5.157  1.00 62.10  ? 326 THR   A CB  1 
ATOM   2318 O  OG1 . THR   A 1 320 ? -13.268 9.255   -4.448  1.00 68.63  ? 326 THR   A OG1 1 
ATOM   2319 C  CG2 . THR   A 1 320 ? -13.697 11.608  -4.847  1.00 60.34  ? 326 THR   A CG2 1 
ATOM   2320 N  N   . ARG   A 1 321 ? -15.580 9.616   -2.431  1.00 54.05  ? 327 ARG   A N   1 
ATOM   2321 C  CA  . ARG   A 1 321 ? -15.898 9.885   -1.032  1.00 54.55  ? 327 ARG   A CA  1 
ATOM   2322 C  C   . ARG   A 1 321 ? -15.087 11.104  -0.556  1.00 61.71  ? 327 ARG   A C   1 
ATOM   2323 O  O   . ARG   A 1 321 ? -15.590 11.874  0.248   1.00 62.06  ? 327 ARG   A O   1 
ATOM   2324 C  CB  . ARG   A 1 321 ? -15.587 8.652   -0.167  1.00 51.63  ? 327 ARG   A CB  1 
ATOM   2325 C  CG  . ARG   A 1 321 ? -16.814 7.974   0.446   1.00 53.83  ? 327 ARG   A CG  1 
ATOM   2326 C  CD  . ARG   A 1 321 ? -17.337 6.755   -0.319  1.00 40.89  ? 327 ARG   A CD  1 
ATOM   2327 N  NE  . ARG   A 1 321 ? -16.278 5.820   -0.701  1.00 38.83  ? 327 ARG   A NE  1 
ATOM   2328 C  CZ  . ARG   A 1 321 ? -15.881 4.761   0.001   1.00 44.98  ? 327 ARG   A CZ  1 
ATOM   2329 N  NH1 . ARG   A 1 321 ? -16.431 4.489   1.178   1.00 38.10  ? 327 ARG   A NH1 1 
ATOM   2330 N  NH2 . ARG   A 1 321 ? -14.913 3.979   -0.461  1.00 34.11  ? 327 ARG   A NH2 1 
ATOM   2331 N  N   . GLU   A 1 322 ? -13.859 11.296  -1.090  1.00 60.79  ? 328 GLU   A N   1 
ATOM   2332 C  CA  . GLU   A 1 322 ? -12.951 12.406  -0.750  1.00 61.85  ? 328 GLU   A CA  1 
ATOM   2333 C  C   . GLU   A 1 322 ? -13.279 13.763  -1.443  1.00 69.88  ? 328 GLU   A C   1 
ATOM   2334 O  O   . GLU   A 1 322 ? -12.613 14.763  -1.158  1.00 69.06  ? 328 GLU   A O   1 
ATOM   2335 C  CB  . GLU   A 1 322 ? -11.487 12.005  -1.015  1.00 63.26  ? 328 GLU   A CB  1 
ATOM   2336 C  CG  . GLU   A 1 322 ? -11.031 10.781  -0.231  1.00 75.16  ? 328 GLU   A CG  1 
ATOM   2337 C  CD  . GLU   A 1 322 ? -9.626  10.273  -0.497  1.00 96.58  ? 328 GLU   A CD  1 
ATOM   2338 O  OE1 . GLU   A 1 322 ? -8.845  10.979  -1.176  1.00 95.13  ? 328 GLU   A OE1 1 
ATOM   2339 O  OE2 . GLU   A 1 322 ? -9.299  9.172   0.005   1.00 86.70  ? 328 GLU   A OE2 1 
ATOM   2340 N  N   . GLY   A 1 323 ? -14.286 13.773  -2.326  1.00 69.90  ? 329 GLY   A N   1 
ATOM   2341 C  CA  . GLY   A 1 323 ? -14.767 14.945  -3.062  1.00 71.22  ? 329 GLY   A CA  1 
ATOM   2342 C  C   . GLY   A 1 323 ? -13.763 15.682  -3.933  1.00 79.07  ? 329 GLY   A C   1 
ATOM   2343 O  O   . GLY   A 1 323 ? -13.744 16.918  -3.940  1.00 78.67  ? 329 GLY   A O   1 
ATOM   2344 N  N   . GLY   A 1 324 ? -12.950 14.927  -4.677  1.00 78.72  ? 330 GLY   A N   1 
ATOM   2345 C  CA  . GLY   A 1 324 ? -11.921 15.457  -5.571  1.00 79.64  ? 330 GLY   A CA  1 
ATOM   2346 C  C   . GLY   A 1 324 ? -12.237 15.402  -7.057  1.00 86.16  ? 330 GLY   A C   1 
ATOM   2347 O  O   . GLY   A 1 324 ? -11.321 15.493  -7.881  1.00 85.64  ? 330 GLY   A O   1 
ATOM   2348 N  N   . HIS   A 1 325 ? -13.532 15.265  -7.418  1.00 85.02  ? 331 HIS   A N   1 
ATOM   2349 C  CA  . HIS   A 1 325 ? -13.979 15.211  -8.814  1.00 86.08  ? 331 HIS   A CA  1 
ATOM   2350 C  C   . HIS   A 1 325 ? -13.920 16.582  -9.490  1.00 92.35  ? 331 HIS   A C   1 
ATOM   2351 O  O   . HIS   A 1 325 ? -13.230 16.724  -10.502 1.00 92.04  ? 331 HIS   A O   1 
ATOM   2352 C  CB  . HIS   A 1 325 ? -15.362 14.542  -8.974  1.00 87.14  ? 331 HIS   A CB  1 
ATOM   2353 C  CG  . HIS   A 1 325 ? -16.262 14.634  -7.777  1.00 90.80  ? 331 HIS   A CG  1 
ATOM   2354 N  ND1 . HIS   A 1 325 ? -16.112 13.781  -6.694  1.00 92.67  ? 331 HIS   A ND1 1 
ATOM   2355 C  CD2 . HIS   A 1 325 ? -17.323 15.444  -7.551  1.00 92.70  ? 331 HIS   A CD2 1 
ATOM   2356 C  CE1 . HIS   A 1 325 ? -17.070 14.110  -5.842  1.00 92.17  ? 331 HIS   A CE1 1 
ATOM   2357 N  NE2 . HIS   A 1 325 ? -17.823 15.107  -6.313  1.00 92.52  ? 331 HIS   A NE2 1 
ATOM   2358 N  N   . ILE   A 1 326 ? -14.615 17.592  -8.920  1.00 90.72  ? 332 ILE   A N   1 
ATOM   2359 C  CA  . ILE   A 1 326 ? -14.622 18.967  -9.435  1.00 91.21  ? 332 ILE   A CA  1 
ATOM   2360 C  C   . ILE   A 1 326 ? -13.300 19.628  -9.015  1.00 97.21  ? 332 ILE   A C   1 
ATOM   2361 O  O   . ILE   A 1 326 ? -13.095 19.900  -7.831  1.00 96.95  ? 332 ILE   A O   1 
ATOM   2362 C  CB  . ILE   A 1 326 ? -15.897 19.751  -8.992  1.00 94.13  ? 332 ILE   A CB  1 
ATOM   2363 C  CG1 . ILE   A 1 326 ? -17.175 19.079  -9.539  1.00 94.65  ? 332 ILE   A CG1 1 
ATOM   2364 C  CG2 . ILE   A 1 326 ? -15.838 21.222  -9.427  1.00 94.60  ? 332 ILE   A CG2 1 
ATOM   2365 C  CD1 . ILE   A 1 326 ? -18.309 18.961  -8.545  1.00 103.26 ? 332 ILE   A CD1 1 
ATOM   2366 N  N   . VAL   A 1 327 ? -12.388 19.827  -9.988  1.00 95.58  ? 333 VAL   A N   1 
ATOM   2367 C  CA  . VAL   A 1 327 ? -11.053 20.395  -9.766  1.00 96.37  ? 333 VAL   A CA  1 
ATOM   2368 C  C   . VAL   A 1 327 ? -11.117 21.901  -9.461  1.00 101.89 ? 333 VAL   A C   1 
ATOM   2369 O  O   . VAL   A 1 327 ? -11.659 22.683  -10.249 1.00 101.37 ? 333 VAL   A O   1 
ATOM   2370 C  CB  . VAL   A 1 327 ? -10.054 20.056  -10.917 1.00 100.55 ? 333 VAL   A CB  1 
ATOM   2371 C  CG1 . VAL   A 1 327 ? -8.688  20.706  -10.694 1.00 100.35 ? 333 VAL   A CG1 1 
ATOM   2372 C  CG2 . VAL   A 1 327 ? -9.897  18.547  -11.087 1.00 100.47 ? 333 VAL   A CG2 1 
ATOM   2373 N  N   . TYR   A 1 328 ? -10.556 22.283  -8.300  1.00 99.72  ? 334 TYR   A N   1 
ATOM   2374 C  CA  . TYR   A 1 328 ? -10.446 23.657  -7.815  1.00 100.01 ? 334 TYR   A CA  1 
ATOM   2375 C  C   . TYR   A 1 328 ? -9.017  24.119  -8.104  1.00 106.38 ? 334 TYR   A C   1 
ATOM   2376 O  O   . TYR   A 1 328 ? -8.072  23.350  -7.893  1.00 105.76 ? 334 TYR   A O   1 
ATOM   2377 C  CB  . TYR   A 1 328 ? -10.738 23.707  -6.304  1.00 100.58 ? 334 TYR   A CB  1 
ATOM   2378 C  CG  . TYR   A 1 328 ? -11.566 24.893  -5.860  1.00 101.14 ? 334 TYR   A CG  1 
ATOM   2379 C  CD1 . TYR   A 1 328 ? -12.941 24.932  -6.080  1.00 102.87 ? 334 TYR   A CD1 1 
ATOM   2380 C  CD2 . TYR   A 1 328 ? -10.989 25.945  -5.154  1.00 101.53 ? 334 TYR   A CD2 1 
ATOM   2381 C  CE1 . TYR   A 1 328 ? -13.713 26.010  -5.650  1.00 103.50 ? 334 TYR   A CE1 1 
ATOM   2382 C  CE2 . TYR   A 1 328 ? -11.752 27.025  -4.712  1.00 102.30 ? 334 TYR   A CE2 1 
ATOM   2383 C  CZ  . TYR   A 1 328 ? -13.114 27.056  -4.965  1.00 109.68 ? 334 TYR   A CZ  1 
ATOM   2384 O  OH  . TYR   A 1 328 ? -13.872 28.120  -4.534  1.00 110.08 ? 334 TYR   A OH  1 
ATOM   2385 N  N   . ASP   A 1 329 ? -8.858  25.349  -8.624  1.00 105.03 ? 335 ASP   A N   1 
ATOM   2386 C  CA  . ASP   A 1 329 ? -7.538  25.877  -8.976  1.00 105.69 ? 335 ASP   A CA  1 
ATOM   2387 C  C   . ASP   A 1 329 ? -7.051  27.002  -8.060  1.00 110.30 ? 335 ASP   A C   1 
ATOM   2388 O  O   . ASP   A 1 329 ? -5.861  27.029  -7.734  1.00 109.94 ? 335 ASP   A O   1 
ATOM   2389 C  CB  . ASP   A 1 329 ? -7.490  26.303  -10.454 1.00 107.91 ? 335 ASP   A CB  1 
ATOM   2390 C  CG  . ASP   A 1 329 ? -7.550  25.136  -11.429 1.00 120.69 ? 335 ASP   A CG  1 
ATOM   2391 O  OD1 . ASP   A 1 329 ? -6.563  24.366  -11.499 1.00 121.66 ? 335 ASP   A OD1 1 
ATOM   2392 O  OD2 . ASP   A 1 329 ? -8.576  25.003  -12.134 1.00 127.01 ? 335 ASP   A OD2 1 
ATOM   2393 N  N   . GLN   A 1 330 ? -7.951  27.924  -7.647  1.00 107.27 ? 336 GLN   A N   1 
ATOM   2394 C  CA  . GLN   A 1 330 ? -7.591  29.059  -6.788  1.00 107.37 ? 336 GLN   A CA  1 
ATOM   2395 C  C   . GLN   A 1 330 ? -8.626  29.383  -5.706  1.00 111.40 ? 336 GLN   A C   1 
ATOM   2396 O  O   . GLN   A 1 330 ? -9.830  29.393  -5.982  1.00 110.75 ? 336 GLN   A O   1 
ATOM   2397 C  CB  . GLN   A 1 330 ? -7.316  30.314  -7.638  1.00 108.85 ? 336 GLN   A CB  1 
ATOM   2398 C  CG  . GLN   A 1 330 ? -5.915  30.371  -8.247  1.00 127.43 ? 336 GLN   A CG  1 
ATOM   2399 C  CD  . GLN   A 1 330 ? -5.912  30.764  -9.707  1.00 148.24 ? 336 GLN   A CD  1 
ATOM   2400 O  OE1 . GLN   A 1 330 ? -6.688  31.615  -10.163 1.00 144.65 ? 336 GLN   A OE1 1 
ATOM   2401 N  NE2 . GLN   A 1 330 ? -4.998  30.181  -10.468 1.00 139.59 ? 336 GLN   A NE2 1 
ATOM   2402 N  N   . LEU   A 1 331 ? -8.141  29.685  -4.480  1.00 108.19 ? 337 LEU   A N   1 
ATOM   2403 C  CA  . LEU   A 1 331 ? -8.975  30.080  -3.339  1.00 108.00 ? 337 LEU   A CA  1 
ATOM   2404 C  C   . LEU   A 1 331 ? -9.038  31.619  -3.292  1.00 111.84 ? 337 LEU   A C   1 
ATOM   2405 O  O   . LEU   A 1 331 ? -7.979  32.258  -3.353  1.00 110.83 ? 337 LEU   A O   1 
ATOM   2406 C  CB  . LEU   A 1 331 ? -8.413  29.557  -1.994  1.00 108.04 ? 337 LEU   A CB  1 
ATOM   2407 C  CG  . LEU   A 1 331 ? -8.156  28.058  -1.822  1.00 112.63 ? 337 LEU   A CG  1 
ATOM   2408 C  CD1 . LEU   A 1 331 ? -7.144  27.816  -0.725  1.00 112.79 ? 337 LEU   A CD1 1 
ATOM   2409 C  CD2 . LEU   A 1 331 ? -9.436  27.292  -1.521  1.00 114.81 ? 337 LEU   A CD2 1 
ATOM   2410 N  N   . PRO   A 1 332 ? -10.243 32.235  -3.167  1.00 108.97 ? 338 PRO   A N   1 
ATOM   2411 C  CA  . PRO   A 1 332 ? -10.312 33.710  -3.120  1.00 109.06 ? 338 PRO   A CA  1 
ATOM   2412 C  C   . PRO   A 1 332 ? -9.662  34.339  -1.880  1.00 113.44 ? 338 PRO   A C   1 
ATOM   2413 O  O   . PRO   A 1 332 ? -9.862  33.862  -0.759  1.00 112.74 ? 338 PRO   A O   1 
ATOM   2414 C  CB  . PRO   A 1 332 ? -11.814 34.006  -3.207  1.00 110.79 ? 338 PRO   A CB  1 
ATOM   2415 C  CG  . PRO   A 1 332 ? -12.478 32.772  -2.723  1.00 115.05 ? 338 PRO   A CG  1 
ATOM   2416 C  CD  . PRO   A 1 332 ? -11.589 31.627  -3.099  1.00 110.49 ? 338 PRO   A CD  1 
ATOM   2417 N  N   . THR   A 1 333 ? -8.865  35.402  -2.099  1.00 110.62 ? 339 THR   A N   1 
ATOM   2418 C  CA  . THR   A 1 333 ? -8.143  36.137  -1.052  1.00 110.79 ? 339 THR   A CA  1 
ATOM   2419 C  C   . THR   A 1 333 ? -8.936  37.379  -0.591  1.00 115.30 ? 339 THR   A C   1 
ATOM   2420 O  O   . THR   A 1 333 ? -9.669  37.950  -1.405  1.00 115.00 ? 339 THR   A O   1 
ATOM   2421 C  CB  . THR   A 1 333 ? -6.729  36.530  -1.532  1.00 119.48 ? 339 THR   A CB  1 
ATOM   2422 O  OG1 . THR   A 1 333 ? -6.830  37.416  -2.647  1.00 120.05 ? 339 THR   A OG1 1 
ATOM   2423 C  CG2 . THR   A 1 333 ? -5.857  35.326  -1.876  1.00 117.78 ? 339 THR   A CG2 1 
ATOM   2424 N  N   . PRO   A 1 334 ? -8.795  37.835  0.684   1.00 112.15 ? 340 PRO   A N   1 
ATOM   2425 C  CA  . PRO   A 1 334 ? -9.546  39.027  1.121   1.00 115.24 ? 340 PRO   A CA  1 
ATOM   2426 C  C   . PRO   A 1 334 ? -8.966  40.332  0.575   1.00 130.12 ? 340 PRO   A C   1 
ATOM   2427 O  O   . PRO   A 1 334 ? -7.750  40.496  0.495   1.00 85.84  ? 340 PRO   A O   1 
ATOM   2428 C  CB  . PRO   A 1 334 ? -9.455  38.971  2.655   1.00 116.53 ? 340 PRO   A CB  1 
ATOM   2429 C  CG  . PRO   A 1 334 ? -8.792  37.655  2.991   1.00 119.93 ? 340 PRO   A CG  1 
ATOM   2430 C  CD  . PRO   A 1 334 ? -7.986  37.291  1.792   1.00 114.74 ? 340 PRO   A CD  1 
ATOM   2431 N  N   . ASN   B 1 11  ? -19.746 0.853   43.694  1.00 46.29  ? 17  ASN   B N   1 
ATOM   2432 C  CA  . ASN   B 1 11  ? -18.383 0.511   43.293  1.00 45.25  ? 17  ASN   B CA  1 
ATOM   2433 C  C   . ASN   B 1 11  ? -17.384 1.522   43.847  1.00 46.00  ? 17  ASN   B C   1 
ATOM   2434 O  O   . ASN   B 1 11  ? -17.624 2.727   43.772  1.00 45.27  ? 17  ASN   B O   1 
ATOM   2435 C  CB  . ASN   B 1 11  ? -18.288 0.416   41.774  1.00 46.52  ? 17  ASN   B CB  1 
ATOM   2436 C  CG  . ASN   B 1 11  ? -19.078 -0.735  41.204  1.00 64.86  ? 17  ASN   B CG  1 
ATOM   2437 O  OD1 . ASN   B 1 11  ? -18.936 -1.889  41.627  1.00 58.67  ? 17  ASN   B OD1 1 
ATOM   2438 N  ND2 . ASN   B 1 11  ? -19.904 -0.449  40.208  1.00 55.59  ? 17  ASN   B ND2 1 
ATOM   2439 N  N   . LEU   B 1 12  ? -16.275 1.034   44.412  1.00 41.80  ? 18  LEU   B N   1 
ATOM   2440 C  CA  . LEU   B 1 12  ? -15.281 1.905   45.057  1.00 40.32  ? 18  LEU   B CA  1 
ATOM   2441 C  C   . LEU   B 1 12  ? -13.927 1.918   44.377  1.00 41.38  ? 18  LEU   B C   1 
ATOM   2442 O  O   . LEU   B 1 12  ? -13.100 2.763   44.717  1.00 39.98  ? 18  LEU   B O   1 
ATOM   2443 C  CB  . LEU   B 1 12  ? -15.097 1.504   46.542  1.00 40.60  ? 18  LEU   B CB  1 
ATOM   2444 C  CG  . LEU   B 1 12  ? -16.339 1.282   47.401  1.00 45.33  ? 18  LEU   B CG  1 
ATOM   2445 C  CD1 . LEU   B 1 12  ? -15.949 0.775   48.778  1.00 45.34  ? 18  LEU   B CD1 1 
ATOM   2446 C  CD2 . LEU   B 1 12  ? -17.168 2.555   47.523  1.00 47.90  ? 18  LEU   B CD2 1 
ATOM   2447 N  N   . TYR   B 1 13  ? -13.689 0.986   43.421  1.00 37.16  ? 19  TYR   B N   1 
ATOM   2448 C  CA  . TYR   B 1 13  ? -12.407 0.838   42.736  1.00 37.31  ? 19  TYR   B CA  1 
ATOM   2449 C  C   . TYR   B 1 13  ? -12.577 0.932   41.232  1.00 40.71  ? 19  TYR   B C   1 
ATOM   2450 O  O   . TYR   B 1 13  ? -13.516 0.366   40.673  1.00 39.46  ? 19  TYR   B O   1 
ATOM   2451 C  CB  . TYR   B 1 13  ? -11.748 -0.495  43.102  1.00 39.76  ? 19  TYR   B CB  1 
ATOM   2452 C  CG  . TYR   B 1 13  ? -11.446 -0.645  44.573  1.00 42.92  ? 19  TYR   B CG  1 
ATOM   2453 C  CD1 . TYR   B 1 13  ? -12.425 -1.068  45.465  1.00 45.38  ? 19  TYR   B CD1 1 
ATOM   2454 C  CD2 . TYR   B 1 13  ? -10.170 -0.408  45.069  1.00 44.63  ? 19  TYR   B CD2 1 
ATOM   2455 C  CE1 . TYR   B 1 13  ? -12.156 -1.199  46.825  1.00 47.22  ? 19  TYR   B CE1 1 
ATOM   2456 C  CE2 . TYR   B 1 13  ? -9.883  -0.552  46.424  1.00 46.15  ? 19  TYR   B CE2 1 
ATOM   2457 C  CZ  . TYR   B 1 13  ? -10.883 -0.941  47.298  1.00 53.64  ? 19  TYR   B CZ  1 
ATOM   2458 O  OH  . TYR   B 1 13  ? -10.610 -1.111  48.628  1.00 53.81  ? 19  TYR   B OH  1 
ATOM   2459 N  N   . PHE   B 1 14  ? -11.677 1.685   40.589  1.00 35.93  ? 20  PHE   B N   1 
ATOM   2460 C  CA  . PHE   B 1 14  ? -11.713 1.959   39.150  1.00 35.10  ? 20  PHE   B CA  1 
ATOM   2461 C  C   . PHE   B 1 14  ? -10.310 1.893   38.580  1.00 39.81  ? 20  PHE   B C   1 
ATOM   2462 O  O   . PHE   B 1 14  ? -9.358  2.168   39.304  1.00 38.97  ? 20  PHE   B O   1 
ATOM   2463 C  CB  . PHE   B 1 14  ? -12.342 3.342   38.906  1.00 36.05  ? 20  PHE   B CB  1 
ATOM   2464 C  CG  . PHE   B 1 14  ? -13.725 3.509   39.502  1.00 36.34  ? 20  PHE   B CG  1 
ATOM   2465 C  CD1 . PHE   B 1 14  ? -14.856 3.147   38.787  1.00 37.29  ? 20  PHE   B CD1 1 
ATOM   2466 C  CD2 . PHE   B 1 14  ? -13.892 3.996   40.799  1.00 37.77  ? 20  PHE   B CD2 1 
ATOM   2467 C  CE1 . PHE   B 1 14  ? -16.128 3.297   39.338  1.00 37.71  ? 20  PHE   B CE1 1 
ATOM   2468 C  CE2 . PHE   B 1 14  ? -15.162 4.110   41.362  1.00 40.00  ? 20  PHE   B CE2 1 
ATOM   2469 C  CZ  . PHE   B 1 14  ? -16.273 3.768   40.628  1.00 38.27  ? 20  PHE   B CZ  1 
ATOM   2470 N  N   . GLN   B 1 15  ? -10.171 1.528   37.277  1.00 37.49  ? 21  GLN   B N   1 
ATOM   2471 C  CA  . GLN   B 1 15  ? -8.862  1.438   36.632  1.00 37.98  ? 21  GLN   B CA  1 
ATOM   2472 C  C   . GLN   B 1 15  ? -8.200  2.815   36.545  1.00 39.66  ? 21  GLN   B C   1 
ATOM   2473 O  O   . GLN   B 1 15  ? -6.981  2.927   36.635  1.00 37.88  ? 21  GLN   B O   1 
ATOM   2474 C  CB  . GLN   B 1 15  ? -8.964  0.769   35.238  1.00 39.93  ? 21  GLN   B CB  1 
ATOM   2475 C  CG  . GLN   B 1 15  ? -8.578  -0.717  35.231  1.00 63.55  ? 21  GLN   B CG  1 
ATOM   2476 C  CD  . GLN   B 1 15  ? -7.174  -1.003  35.731  1.00 88.61  ? 21  GLN   B CD  1 
ATOM   2477 O  OE1 . GLN   B 1 15  ? -6.207  -0.290  35.426  1.00 86.90  ? 21  GLN   B OE1 1 
ATOM   2478 N  NE2 . GLN   B 1 15  ? -7.029  -2.071  36.501  1.00 80.68  ? 21  GLN   B NE2 1 
ATOM   2479 N  N   . SER   B 1 16  ? -9.018  3.851   36.400  1.00 38.16  ? 22  SER   B N   1 
ATOM   2480 C  CA  . SER   B 1 16  ? -8.569  5.241   36.367  1.00 39.69  ? 22  SER   B CA  1 
ATOM   2481 C  C   . SER   B 1 16  ? -9.671  6.186   36.827  1.00 43.77  ? 22  SER   B C   1 
ATOM   2482 O  O   . SER   B 1 16  ? -10.861 5.882   36.727  1.00 43.64  ? 22  SER   B O   1 
ATOM   2483 C  CB  . SER   B 1 16  ? -8.014  5.632   34.989  1.00 43.69  ? 22  SER   B CB  1 
ATOM   2484 O  OG  . SER   B 1 16  ? -8.976  5.475   33.960  1.00 52.72  ? 22  SER   B OG  1 
ATOM   2485 N  N   . VAL   B 1 17  ? -9.256  7.306   37.400  1.00 41.19  ? 23  VAL   B N   1 
ATOM   2486 C  CA  . VAL   B 1 17  ? -10.152 8.329   37.899  1.00 41.50  ? 23  VAL   B CA  1 
ATOM   2487 C  C   . VAL   B 1 17  ? -9.850  9.587   37.088  1.00 48.47  ? 23  VAL   B C   1 
ATOM   2488 O  O   . VAL   B 1 17  ? -8.690  9.996   37.005  1.00 48.41  ? 23  VAL   B O   1 
ATOM   2489 C  CB  . VAL   B 1 17  ? -9.957  8.524   39.431  1.00 44.99  ? 23  VAL   B CB  1 
ATOM   2490 C  CG1 . VAL   B 1 17  ? -10.702 9.748   39.942  1.00 44.37  ? 23  VAL   B CG1 1 
ATOM   2491 C  CG2 . VAL   B 1 17  ? -10.385 7.268   40.196  1.00 45.03  ? 23  VAL   B CG2 1 
ATOM   2492 N  N   . HIS   B 1 18  ? -10.886 10.159  36.462  1.00 47.50  ? 24  HIS   B N   1 
ATOM   2493 C  CA  . HIS   B 1 18  ? -10.772 11.364  35.646  1.00 48.99  ? 24  HIS   B CA  1 
ATOM   2494 C  C   . HIS   B 1 18  ? -11.608 12.501  36.222  1.00 54.66  ? 24  HIS   B C   1 
ATOM   2495 O  O   . HIS   B 1 18  ? -12.710 12.269  36.720  1.00 54.14  ? 24  HIS   B O   1 
ATOM   2496 C  CB  . HIS   B 1 18  ? -11.233 11.097  34.190  1.00 49.82  ? 24  HIS   B CB  1 
ATOM   2497 C  CG  . HIS   B 1 18  ? -10.543 9.956   33.502  1.00 53.41  ? 24  HIS   B CG  1 
ATOM   2498 N  ND1 . HIS   B 1 18  ? -9.218  10.043  33.096  1.00 55.13  ? 24  HIS   B ND1 1 
ATOM   2499 C  CD2 . HIS   B 1 18  ? -11.032 8.748   33.134  1.00 55.32  ? 24  HIS   B CD2 1 
ATOM   2500 C  CE1 . HIS   B 1 18  ? -8.942  8.886   32.519  1.00 54.42  ? 24  HIS   B CE1 1 
ATOM   2501 N  NE2 . HIS   B 1 18  ? -10.001 8.074   32.522  1.00 55.00  ? 24  HIS   B NE2 1 
ATOM   2502 N  N   . SER   B 1 19  ? -11.095 13.736  36.120  1.00 52.89  ? 25  SER   B N   1 
ATOM   2503 C  CA  . SER   B 1 19  ? -11.820 14.950  36.518  1.00 52.93  ? 25  SER   B CA  1 
ATOM   2504 C  C   . SER   B 1 19  ? -12.462 15.445  35.204  1.00 56.57  ? 25  SER   B C   1 
ATOM   2505 O  O   . SER   B 1 19  ? -11.738 15.746  34.254  1.00 55.99  ? 25  SER   B O   1 
ATOM   2506 C  CB  . SER   B 1 19  ? -10.856 15.990  37.091  1.00 56.11  ? 25  SER   B CB  1 
ATOM   2507 O  OG  . SER   B 1 19  ? -9.990  15.439  38.072  1.00 63.61  ? 25  SER   B OG  1 
ATOM   2508 N  N   . VAL   B 1 20  ? -13.806 15.419  35.116  1.00 54.03  ? 26  VAL   B N   1 
ATOM   2509 C  CA  . VAL   B 1 20  ? -14.545 15.757  33.892  1.00 54.58  ? 26  VAL   B CA  1 
ATOM   2510 C  C   . VAL   B 1 20  ? -15.640 16.820  34.130  1.00 62.34  ? 26  VAL   B C   1 
ATOM   2511 O  O   . VAL   B 1 20  ? -16.426 16.697  35.072  1.00 61.84  ? 26  VAL   B O   1 
ATOM   2512 C  CB  . VAL   B 1 20  ? -15.124 14.475  33.198  1.00 57.75  ? 26  VAL   B CB  1 
ATOM   2513 C  CG1 . VAL   B 1 20  ? -15.811 14.807  31.876  1.00 57.49  ? 26  VAL   B CG1 1 
ATOM   2514 C  CG2 . VAL   B 1 20  ? -14.051 13.407  32.981  1.00 57.15  ? 26  VAL   B CG2 1 
ATOM   2515 N  N   . ALA   B 1 21  ? -15.709 17.832  33.228  1.00 60.88  ? 27  ALA   B N   1 
ATOM   2516 C  CA  . ALA   B 1 21  ? -16.692 18.923  33.246  1.00 61.00  ? 27  ALA   B CA  1 
ATOM   2517 C  C   . ALA   B 1 21  ? -17.681 18.821  32.065  1.00 65.61  ? 27  ALA   B C   1 
ATOM   2518 O  O   . ALA   B 1 21  ? -17.262 18.573  30.938  1.00 65.59  ? 27  ALA   B O   1 
ATOM   2519 C  CB  . ALA   B 1 21  ? -15.973 20.264  33.221  1.00 61.66  ? 27  ALA   B CB  1 
ATOM   2520 N  N   . VAL   B 1 22  ? -18.984 18.985  32.329  1.00 62.47  ? 28  VAL   B N   1 
ATOM   2521 C  CA  . VAL   B 1 22  ? -20.034 18.887  31.308  1.00 63.07  ? 28  VAL   B CA  1 
ATOM   2522 C  C   . VAL   B 1 22  ? -20.712 20.257  31.065  1.00 70.59  ? 28  VAL   B C   1 
ATOM   2523 O  O   . VAL   B 1 22  ? -21.228 20.869  32.008  1.00 70.30  ? 28  VAL   B O   1 
ATOM   2524 C  CB  . VAL   B 1 22  ? -21.047 17.746  31.618  1.00 66.52  ? 28  VAL   B CB  1 
ATOM   2525 C  CG1 . VAL   B 1 22  ? -22.156 17.665  30.570  1.00 66.26  ? 28  VAL   B CG1 1 
ATOM   2526 C  CG2 . VAL   B 1 22  ? -20.338 16.402  31.752  1.00 66.25  ? 28  VAL   B CG2 1 
ATOM   2527 N  N   . ILE   B 1 23  ? -20.690 20.728  29.793  1.00 69.33  ? 29  ILE   B N   1 
ATOM   2528 C  CA  . ILE   B 1 23  ? -21.278 22.002  29.347  1.00 69.62  ? 29  ILE   B CA  1 
ATOM   2529 C  C   . ILE   B 1 23  ? -22.396 21.746  28.328  1.00 76.80  ? 29  ILE   B C   1 
ATOM   2530 O  O   . ILE   B 1 23  ? -22.185 21.035  27.352  1.00 75.62  ? 29  ILE   B O   1 
ATOM   2531 C  CB  . ILE   B 1 23  ? -20.206 22.976  28.768  1.00 72.23  ? 29  ILE   B CB  1 
ATOM   2532 C  CG1 . ILE   B 1 23  ? -19.011 23.171  29.730  1.00 72.29  ? 29  ILE   B CG1 1 
ATOM   2533 C  CG2 . ILE   B 1 23  ? -20.837 24.324  28.369  1.00 73.20  ? 29  ILE   B CG2 1 
ATOM   2534 C  CD1 . ILE   B 1 23  ? -17.897 24.081  29.215  1.00 76.20  ? 29  ILE   B CD1 1 
ATOM   2535 N  N   . GLY   B 1 24  ? -23.555 22.353  28.552  1.00 77.39  ? 30  GLY   B N   1 
ATOM   2536 C  CA  . GLY   B 1 24  ? -24.688 22.262  27.639  1.00 79.10  ? 30  GLY   B CA  1 
ATOM   2537 C  C   . GLY   B 1 24  ? -24.798 23.499  26.764  1.00 87.69  ? 30  GLY   B C   1 
ATOM   2538 O  O   . GLY   B 1 24  ? -25.501 24.442  27.131  1.00 87.04  ? 30  GLY   B O   1 
ATOM   2539 N  N   . ALA   B 1 25  ? -24.077 23.520  25.616  1.00 87.74  ? 31  ALA   B N   1 
ATOM   2540 C  CA  . ALA   B 1 25  ? -24.081 24.637  24.659  1.00 89.05  ? 31  ALA   B CA  1 
ATOM   2541 C  C   . ALA   B 1 25  ? -25.129 24.380  23.550  1.00 96.86  ? 31  ALA   B C   1 
ATOM   2542 O  O   . ALA   B 1 25  ? -24.853 23.608  22.627  1.00 96.57  ? 31  ALA   B O   1 
ATOM   2543 C  CB  . ALA   B 1 25  ? -22.691 24.828  24.060  1.00 89.67  ? 31  ALA   B CB  1 
ATOM   2544 N  N   . PRO   B 1 26  ? -26.348 24.979  23.626  1.00 96.51  ? 32  PRO   B N   1 
ATOM   2545 C  CA  . PRO   B 1 26  ? -27.373 24.682  22.616  1.00 97.57  ? 32  PRO   B CA  1 
ATOM   2546 C  C   . PRO   B 1 26  ? -27.394 25.635  21.414  1.00 105.35 ? 32  PRO   B C   1 
ATOM   2547 O  O   . PRO   B 1 26  ? -28.441 26.207  21.099  1.00 104.82 ? 32  PRO   B O   1 
ATOM   2548 C  CB  . PRO   B 1 26  ? -28.673 24.711  23.431  1.00 99.00  ? 32  PRO   B CB  1 
ATOM   2549 C  CG  . PRO   B 1 26  ? -28.362 25.561  24.652  1.00 103.05 ? 32  PRO   B CG  1 
ATOM   2550 C  CD  . PRO   B 1 26  ? -26.890 25.891  24.651  1.00 98.39  ? 32  PRO   B CD  1 
ATOM   2551 N  N   . PHE   B 1 27  ? -26.239 25.770  20.721  1.00 105.10 ? 33  PHE   B N   1 
ATOM   2552 C  CA  . PHE   B 1 27  ? -26.066 26.591  19.512  1.00 106.56 ? 33  PHE   B CA  1 
ATOM   2553 C  C   . PHE   B 1 27  ? -27.071 26.177  18.428  1.00 113.31 ? 33  PHE   B C   1 
ATOM   2554 O  O   . PHE   B 1 27  ? -27.356 24.987  18.276  1.00 112.85 ? 33  PHE   B O   1 
ATOM   2555 C  CB  . PHE   B 1 27  ? -24.647 26.411  18.945  1.00 108.71 ? 33  PHE   B CB  1 
ATOM   2556 C  CG  . PHE   B 1 27  ? -23.564 27.305  19.497  1.00 110.75 ? 33  PHE   B CG  1 
ATOM   2557 C  CD1 . PHE   B 1 27  ? -22.987 27.043  20.734  1.00 114.25 ? 33  PHE   B CD1 1 
ATOM   2558 C  CD2 . PHE   B 1 27  ? -23.053 28.352  18.739  1.00 113.36 ? 33  PHE   B CD2 1 
ATOM   2559 C  CE1 . PHE   B 1 27  ? -21.958 27.851  21.230  1.00 115.34 ? 33  PHE   B CE1 1 
ATOM   2560 C  CE2 . PHE   B 1 27  ? -22.016 29.153  19.231  1.00 116.38 ? 33  PHE   B CE2 1 
ATOM   2561 C  CZ  . PHE   B 1 27  ? -21.472 28.892  20.470  1.00 114.49 ? 33  PHE   B CZ  1 
ATOM   2562 N  N   . SER   B 1 28  ? -27.603 27.158  17.685  1.00 111.99 ? 34  SER   B N   1 
ATOM   2563 C  CA  . SER   B 1 28  ? -28.564 26.935  16.599  1.00 112.83 ? 34  SER   B CA  1 
ATOM   2564 C  C   . SER   B 1 28  ? -28.374 27.953  15.469  1.00 118.78 ? 34  SER   B C   1 
ATOM   2565 O  O   . SER   B 1 28  ? -28.840 27.723  14.351  1.00 118.69 ? 34  SER   B O   1 
ATOM   2566 C  CB  . SER   B 1 28  ? -29.998 26.964  17.124  1.00 116.85 ? 34  SER   B CB  1 
ATOM   2567 O  OG  . SER   B 1 28  ? -30.316 28.204  17.735  1.00 127.14 ? 34  SER   B OG  1 
ATOM   2568 N  N   . GLN   B 1 29  ? -27.662 29.062  15.761  1.00 116.55 ? 35  GLN   B N   1 
ATOM   2569 C  CA  . GLN   B 1 29  ? -27.375 30.143  14.812  1.00 116.86 ? 35  GLN   B CA  1 
ATOM   2570 C  C   . GLN   B 1 29  ? -26.192 29.831  13.868  1.00 121.00 ? 35  GLN   B C   1 
ATOM   2571 O  O   . GLN   B 1 29  ? -25.923 30.607  12.947  1.00 120.65 ? 35  GLN   B O   1 
ATOM   2572 C  CB  . GLN   B 1 29  ? -27.185 31.483  15.549  1.00 118.35 ? 35  GLN   B CB  1 
ATOM   2573 C  CG  . GLN   B 1 29  ? -28.503 32.098  16.027  1.00 138.11 ? 35  GLN   B CG  1 
ATOM   2574 C  CD  . GLN   B 1 29  ? -28.306 33.381  16.795  1.00 161.19 ? 35  GLN   B CD  1 
ATOM   2575 O  OE1 . GLN   B 1 29  ? -27.914 33.382  17.968  1.00 158.00 ? 35  GLN   B OE1 1 
ATOM   2576 N  NE2 . GLN   B 1 29  ? -28.609 34.505  16.162  1.00 153.33 ? 35  GLN   B NE2 1 
ATOM   2577 N  N   . GLY   B 1 30  ? -25.528 28.693  14.091  1.00 117.46 ? 36  GLY   B N   1 
ATOM   2578 C  CA  . GLY   B 1 30  ? -24.415 28.216  13.273  1.00 117.18 ? 36  GLY   B CA  1 
ATOM   2579 C  C   . GLY   B 1 30  ? -24.869 27.608  11.958  1.00 120.66 ? 36  GLY   B C   1 
ATOM   2580 O  O   . GLY   B 1 30  ? -24.074 27.479  11.022  1.00 120.09 ? 36  GLY   B O   1 
ATOM   2581 N  N   . GLN   B 1 31  ? -26.160 27.226  11.893  1.00 117.09 ? 37  GLN   B N   1 
ATOM   2582 C  CA  . GLN   B 1 31  ? -26.845 26.650  10.730  1.00 116.88 ? 37  GLN   B CA  1 
ATOM   2583 C  C   . GLN   B 1 31  ? -28.300 27.173  10.632  1.00 120.89 ? 37  GLN   B C   1 
ATOM   2584 O  O   . GLN   B 1 31  ? -28.638 28.132  11.333  1.00 120.70 ? 37  GLN   B O   1 
ATOM   2585 C  CB  . GLN   B 1 31  ? -26.733 25.110  10.689  1.00 118.15 ? 37  GLN   B CB  1 
ATOM   2586 C  CG  . GLN   B 1 31  ? -26.934 24.401  12.020  1.00 130.93 ? 37  GLN   B CG  1 
ATOM   2587 C  CD  . GLN   B 1 31  ? -28.366 24.012  12.237  1.00 150.51 ? 37  GLN   B CD  1 
ATOM   2588 O  OE1 . GLN   B 1 31  ? -28.836 22.986  11.735  1.00 146.49 ? 37  GLN   B OE1 1 
ATOM   2589 N  NE2 . GLN   B 1 31  ? -29.085 24.817  13.005  1.00 142.59 ? 37  GLN   B NE2 1 
ATOM   2590 N  N   . LYS   B 1 32  ? -29.143 26.587  9.751   1.00 117.07 ? 38  LYS   B N   1 
ATOM   2591 C  CA  . LYS   B 1 32  ? -30.522 27.057  9.547   1.00 116.70 ? 38  LYS   B CA  1 
ATOM   2592 C  C   . LYS   B 1 32  ? -31.622 26.076  9.991   1.00 119.97 ? 38  LYS   B C   1 
ATOM   2593 O  O   . LYS   B 1 32  ? -32.766 26.502  10.176  1.00 119.55 ? 38  LYS   B O   1 
ATOM   2594 C  CB  . LYS   B 1 32  ? -30.741 27.477  8.083   1.00 119.34 ? 38  LYS   B CB  1 
ATOM   2595 C  CG  . LYS   B 1 32  ? -29.951 28.715  7.676   1.00 132.66 ? 38  LYS   B CG  1 
ATOM   2596 C  CD  . LYS   B 1 32  ? -30.300 29.167  6.272   1.00 142.06 ? 38  LYS   B CD  1 
ATOM   2597 C  CE  . LYS   B 1 32  ? -29.414 30.296  5.810   1.00 153.21 ? 38  LYS   B CE  1 
ATOM   2598 N  NZ  . LYS   B 1 32  ? -28.095 29.805  5.328   1.00 162.98 ? 38  LYS   B NZ  1 
ATOM   2599 N  N   . ARG   B 1 33  ? -31.288 24.782  10.156  1.00 116.03 ? 39  ARG   B N   1 
ATOM   2600 C  CA  . ARG   B 1 33  ? -32.245 23.748  10.568  1.00 115.48 ? 39  ARG   B CA  1 
ATOM   2601 C  C   . ARG   B 1 33  ? -32.479 23.765  12.087  1.00 117.91 ? 39  ARG   B C   1 
ATOM   2602 O  O   . ARG   B 1 33  ? -31.553 23.506  12.860  1.00 117.67 ? 39  ARG   B O   1 
ATOM   2603 C  CB  . ARG   B 1 33  ? -31.802 22.355  10.080  1.00 116.52 ? 39  ARG   B CB  1 
ATOM   2604 C  CG  . ARG   B 1 33  ? -31.797 22.205  8.561   1.00 128.74 ? 39  ARG   B CG  1 
ATOM   2605 C  CD  . ARG   B 1 33  ? -32.714 21.095  8.090   1.00 139.63 ? 39  ARG   B CD  1 
ATOM   2606 N  NE  . ARG   B 1 33  ? -32.045 19.793  8.082   1.00 149.01 ? 39  ARG   B NE  1 
ATOM   2607 C  CZ  . ARG   B 1 33  ? -32.601 18.666  7.648   1.00 164.78 ? 39  ARG   B CZ  1 
ATOM   2608 N  NH1 . ARG   B 1 33  ? -33.845 18.665  7.184   1.00 152.55 ? 39  ARG   B NH1 1 
ATOM   2609 N  NH2 . ARG   B 1 33  ? -31.917 17.530  7.675   1.00 152.04 ? 39  ARG   B NH2 1 
ATOM   2610 N  N   . LYS   B 1 34  ? -33.716 24.086  12.509  1.00 112.90 ? 40  LYS   B N   1 
ATOM   2611 C  CA  . LYS   B 1 34  ? -34.095 24.150  13.926  1.00 111.94 ? 40  LYS   B CA  1 
ATOM   2612 C  C   . LYS   B 1 34  ? -34.321 22.760  14.541  1.00 113.60 ? 40  LYS   B C   1 
ATOM   2613 O  O   . LYS   B 1 34  ? -34.724 21.829  13.838  1.00 113.25 ? 40  LYS   B O   1 
ATOM   2614 C  CB  . LYS   B 1 34  ? -35.308 25.082  14.150  1.00 114.58 ? 40  LYS   B CB  1 
ATOM   2615 C  CG  . LYS   B 1 34  ? -36.603 24.646  13.450  1.00 130.31 ? 40  LYS   B CG  1 
ATOM   2616 C  CD  . LYS   B 1 34  ? -37.740 25.644  13.643  1.00 139.47 ? 40  LYS   B CD  1 
ATOM   2617 C  CE  . LYS   B 1 34  ? -37.932 26.537  12.440  1.00 149.06 ? 40  LYS   B CE  1 
ATOM   2618 N  NZ  . LYS   B 1 34  ? -39.101 27.441  12.606  1.00 156.98 ? 40  LYS   B NZ  1 
ATOM   2619 N  N   . GLY   B 1 35  ? -34.060 22.647  15.844  1.00 108.08 ? 41  GLY   B N   1 
ATOM   2620 C  CA  . GLY   B 1 35  ? -34.220 21.408  16.602  1.00 106.59 ? 41  GLY   B CA  1 
ATOM   2621 C  C   . GLY   B 1 35  ? -32.945 20.872  17.223  1.00 106.94 ? 41  GLY   B C   1 
ATOM   2622 O  O   . GLY   B 1 35  ? -33.003 19.979  18.071  1.00 105.76 ? 41  GLY   B O   1 
ATOM   2623 N  N   . VAL   B 1 36  ? -31.783 21.421  16.805  1.00 101.79 ? 42  VAL   B N   1 
ATOM   2624 C  CA  . VAL   B 1 36  ? -30.447 21.039  17.273  1.00 100.76 ? 42  VAL   B CA  1 
ATOM   2625 C  C   . VAL   B 1 36  ? -30.158 21.605  18.690  1.00 103.29 ? 42  VAL   B C   1 
ATOM   2626 O  O   . VAL   B 1 36  ? -29.216 21.159  19.350  1.00 102.57 ? 42  VAL   B O   1 
ATOM   2627 C  CB  . VAL   B 1 36  ? -29.360 21.394  16.217  1.00 104.39 ? 42  VAL   B CB  1 
ATOM   2628 C  CG1 . VAL   B 1 36  ? -28.973 22.871  16.257  1.00 104.11 ? 42  VAL   B CG1 1 
ATOM   2629 C  CG2 . VAL   B 1 36  ? -28.134 20.495  16.341  1.00 104.20 ? 42  VAL   B CG2 1 
ATOM   2630 N  N   . GLU   B 1 37  ? -30.988 22.568  19.151  1.00 99.14  ? 43  GLU   B N   1 
ATOM   2631 C  CA  . GLU   B 1 37  ? -30.891 23.185  20.481  1.00 98.41  ? 43  GLU   B CA  1 
ATOM   2632 C  C   . GLU   B 1 37  ? -31.337 22.216  21.590  1.00 99.82  ? 43  GLU   B C   1 
ATOM   2633 O  O   . GLU   B 1 37  ? -30.886 22.337  22.729  1.00 99.25  ? 43  GLU   B O   1 
ATOM   2634 C  CB  . GLU   B 1 37  ? -31.662 24.525  20.552  1.00 99.90  ? 43  GLU   B CB  1 
ATOM   2635 C  CG  . GLU   B 1 37  ? -33.150 24.449  20.227  1.00 111.54 ? 43  GLU   B CG  1 
ATOM   2636 C  CD  . GLU   B 1 37  ? -33.553 24.646  18.776  1.00 134.83 ? 43  GLU   B CD  1 
ATOM   2637 O  OE1 . GLU   B 1 37  ? -32.672 24.595  17.886  1.00 134.34 ? 43  GLU   B OE1 1 
ATOM   2638 O  OE2 . GLU   B 1 37  ? -34.765 24.841  18.528  1.00 126.75 ? 43  GLU   B OE2 1 
ATOM   2639 N  N   . HIS   B 1 38  ? -32.205 21.244  21.239  1.00 94.54  ? 44  HIS   B N   1 
ATOM   2640 C  CA  . HIS   B 1 38  ? -32.721 20.206  22.135  1.00 93.64  ? 44  HIS   B CA  1 
ATOM   2641 C  C   . HIS   B 1 38  ? -31.729 19.021  22.279  1.00 94.81  ? 44  HIS   B C   1 
ATOM   2642 O  O   . HIS   B 1 38  ? -32.073 17.989  22.866  1.00 94.25  ? 44  HIS   B O   1 
ATOM   2643 C  CB  . HIS   B 1 38  ? -34.100 19.715  21.646  1.00 94.68  ? 44  HIS   B CB  1 
ATOM   2644 C  CG  . HIS   B 1 38  ? -35.148 20.785  21.597  1.00 98.34  ? 44  HIS   B CG  1 
ATOM   2645 N  ND1 . HIS   B 1 38  ? -35.758 21.251  22.749  1.00 100.19 ? 44  HIS   B ND1 1 
ATOM   2646 C  CD2 . HIS   B 1 38  ? -35.671 21.435  20.531  1.00 100.22 ? 44  HIS   B CD2 1 
ATOM   2647 C  CE1 . HIS   B 1 38  ? -36.621 22.171  22.349  1.00 99.67  ? 44  HIS   B CE1 1 
ATOM   2648 N  NE2 . HIS   B 1 38  ? -36.604 22.316  21.023  1.00 99.98  ? 44  HIS   B NE2 1 
ATOM   2649 N  N   . GLY   B 1 39  ? -30.516 19.202  21.749  1.00 89.13  ? 45  GLY   B N   1 
ATOM   2650 C  CA  . GLY   B 1 39  ? -29.427 18.230  21.771  1.00 87.85  ? 45  GLY   B CA  1 
ATOM   2651 C  C   . GLY   B 1 39  ? -28.857 17.928  23.148  1.00 88.55  ? 45  GLY   B C   1 
ATOM   2652 O  O   . GLY   B 1 39  ? -28.856 16.755  23.542  1.00 87.58  ? 45  GLY   B O   1 
ATOM   2653 N  N   . PRO   B 1 40  ? -28.360 18.942  23.925  1.00 82.58  ? 46  PRO   B N   1 
ATOM   2654 C  CA  . PRO   B 1 40  ? -27.830 18.641  25.274  1.00 81.24  ? 46  PRO   B CA  1 
ATOM   2655 C  C   . PRO   B 1 40  ? -28.894 18.075  26.218  1.00 81.30  ? 46  PRO   B C   1 
ATOM   2656 O  O   . PRO   B 1 40  ? -28.573 17.246  27.062  1.00 80.34  ? 46  PRO   B O   1 
ATOM   2657 C  CB  . PRO   B 1 40  ? -27.288 19.990  25.760  1.00 83.09  ? 46  PRO   B CB  1 
ATOM   2658 C  CG  . PRO   B 1 40  ? -27.189 20.843  24.539  1.00 87.64  ? 46  PRO   B CG  1 
ATOM   2659 C  CD  . PRO   B 1 40  ? -28.282 20.390  23.644  1.00 83.40  ? 46  PRO   B CD  1 
ATOM   2660 N  N   . ALA   B 1 41  ? -30.161 18.483  26.032  1.00 75.56  ? 47  ALA   B N   1 
ATOM   2661 C  CA  . ALA   B 1 41  ? -31.309 17.998  26.795  1.00 74.49  ? 47  ALA   B CA  1 
ATOM   2662 C  C   . ALA   B 1 41  ? -31.550 16.495  26.542  1.00 75.36  ? 47  ALA   B C   1 
ATOM   2663 O  O   . ALA   B 1 41  ? -31.684 15.735  27.502  1.00 75.03  ? 47  ALA   B O   1 
ATOM   2664 C  CB  . ALA   B 1 41  ? -32.555 18.801  26.436  1.00 75.25  ? 47  ALA   B CB  1 
ATOM   2665 N  N   . ALA   B 1 42  ? -31.568 16.069  25.256  1.00 68.80  ? 48  ALA   B N   1 
ATOM   2666 C  CA  . ALA   B 1 42  ? -31.788 14.677  24.848  1.00 66.74  ? 48  ALA   B CA  1 
ATOM   2667 C  C   . ALA   B 1 42  ? -30.682 13.724  25.313  1.00 65.54  ? 48  ALA   B C   1 
ATOM   2668 O  O   . ALA   B 1 42  ? -30.982 12.567  25.623  1.00 63.85  ? 48  ALA   B O   1 
ATOM   2669 C  CB  . ALA   B 1 42  ? -31.948 14.590  23.345  1.00 67.38  ? 48  ALA   B CB  1 
ATOM   2670 N  N   . ILE   B 1 43  ? -29.411 14.211  25.324  1.00 59.38  ? 49  ILE   B N   1 
ATOM   2671 C  CA  . ILE   B 1 43  ? -28.216 13.492  25.768  1.00 58.52  ? 49  ILE   B CA  1 
ATOM   2672 C  C   . ILE   B 1 43  ? -28.325 13.229  27.294  1.00 63.24  ? 49  ILE   B C   1 
ATOM   2673 O  O   . ILE   B 1 43  ? -28.128 12.091  27.731  1.00 63.07  ? 49  ILE   B O   1 
ATOM   2674 C  CB  . ILE   B 1 43  ? -26.906 14.237  25.332  1.00 60.99  ? 49  ILE   B CB  1 
ATOM   2675 C  CG1 . ILE   B 1 43  ? -26.677 14.095  23.797  1.00 61.41  ? 49  ILE   B CG1 1 
ATOM   2676 C  CG2 . ILE   B 1 43  ? -25.670 13.751  26.107  1.00 61.32  ? 49  ILE   B CG2 1 
ATOM   2677 C  CD1 . ILE   B 1 43  ? -25.569 15.005  23.152  1.00 64.89  ? 49  ILE   B CD1 1 
ATOM   2678 N  N   . ARG   B 1 44  ? -28.686 14.273  28.081  1.00 59.25  ? 50  ARG   B N   1 
ATOM   2679 C  CA  . ARG   B 1 44  ? -28.874 14.201  29.534  1.00 58.90  ? 50  ARG   B CA  1 
ATOM   2680 C  C   . ARG   B 1 44  ? -30.015 13.234  29.878  1.00 65.00  ? 50  ARG   B C   1 
ATOM   2681 O  O   . ARG   B 1 44  ? -29.830 12.366  30.735  1.00 64.62  ? 50  ARG   B O   1 
ATOM   2682 C  CB  . ARG   B 1 44  ? -29.146 15.597  30.122  1.00 57.64  ? 50  ARG   B CB  1 
ATOM   2683 C  CG  . ARG   B 1 44  ? -27.931 16.521  30.163  1.00 58.87  ? 50  ARG   B CG  1 
ATOM   2684 C  CD  . ARG   B 1 44  ? -28.291 17.898  30.710  1.00 58.80  ? 50  ARG   B CD  1 
ATOM   2685 N  NE  . ARG   B 1 44  ? -27.151 18.814  30.663  1.00 59.86  ? 50  ARG   B NE  1 
ATOM   2686 C  CZ  . ARG   B 1 44  ? -26.203 18.893  31.593  1.00 73.84  ? 50  ARG   B CZ  1 
ATOM   2687 N  NH1 . ARG   B 1 44  ? -26.256 18.122  32.675  1.00 64.44  ? 50  ARG   B NH1 1 
ATOM   2688 N  NH2 . ARG   B 1 44  ? -25.188 19.734  31.444  1.00 56.74  ? 50  ARG   B NH2 1 
ATOM   2689 N  N   . GLU   B 1 45  ? -31.172 13.349  29.173  1.00 63.35  ? 51  GLU   B N   1 
ATOM   2690 C  CA  . GLU   B 1 45  ? -32.356 12.492  29.347  1.00 64.38  ? 51  GLU   B CA  1 
ATOM   2691 C  C   . GLU   B 1 45  ? -32.057 11.002  29.079  1.00 69.30  ? 51  GLU   B C   1 
ATOM   2692 O  O   . GLU   B 1 45  ? -32.761 10.129  29.600  1.00 69.15  ? 51  GLU   B O   1 
ATOM   2693 C  CB  . GLU   B 1 45  ? -33.525 12.976  28.474  1.00 66.23  ? 51  GLU   B CB  1 
ATOM   2694 C  CG  . GLU   B 1 45  ? -34.215 14.224  29.010  1.00 82.28  ? 51  GLU   B CG  1 
ATOM   2695 C  CD  . GLU   B 1 45  ? -34.853 15.127  27.967  1.00 112.88 ? 51  GLU   B CD  1 
ATOM   2696 O  OE1 . GLU   B 1 45  ? -35.704 14.640  27.187  1.00 111.92 ? 51  GLU   B OE1 1 
ATOM   2697 O  OE2 . GLU   B 1 45  ? -34.531 16.338  27.960  1.00 108.16 ? 51  GLU   B OE2 1 
ATOM   2698 N  N   . ALA   B 1 46  ? -31.012 10.722  28.270  1.00 65.65  ? 52  ALA   B N   1 
ATOM   2699 C  CA  . ALA   B 1 46  ? -30.553 9.368   27.962  1.00 65.30  ? 52  ALA   B CA  1 
ATOM   2700 C  C   . ALA   B 1 46  ? -29.817 8.773   29.182  1.00 68.72  ? 52  ALA   B C   1 
ATOM   2701 O  O   . ALA   B 1 46  ? -29.874 7.562   29.392  1.00 69.03  ? 52  ALA   B O   1 
ATOM   2702 C  CB  . ALA   B 1 46  ? -29.651 9.382   26.736  1.00 65.99  ? 52  ALA   B CB  1 
ATOM   2703 N  N   . GLY   B 1 47  ? -29.167 9.638   29.973  1.00 63.93  ? 53  GLY   B N   1 
ATOM   2704 C  CA  . GLY   B 1 47  ? -28.473 9.279   31.207  1.00 62.31  ? 53  GLY   B CA  1 
ATOM   2705 C  C   . GLY   B 1 47  ? -26.969 9.472   31.237  1.00 62.17  ? 53  GLY   B C   1 
ATOM   2706 O  O   . GLY   B 1 47  ? -26.269 8.640   31.822  1.00 62.02  ? 53  GLY   B O   1 
ATOM   2707 N  N   . LEU   B 1 48  ? -26.455 10.579  30.653  1.00 55.35  ? 54  LEU   B N   1 
ATOM   2708 C  CA  . LEU   B 1 48  ? -25.011 10.859  30.603  1.00 53.53  ? 54  LEU   B CA  1 
ATOM   2709 C  C   . LEU   B 1 48  ? -24.343 10.993  31.969  1.00 57.16  ? 54  LEU   B C   1 
ATOM   2710 O  O   . LEU   B 1 48  ? -23.307 10.363  32.183  1.00 56.42  ? 54  LEU   B O   1 
ATOM   2711 C  CB  . LEU   B 1 48  ? -24.682 12.089  29.733  1.00 53.12  ? 54  LEU   B CB  1 
ATOM   2712 C  CG  . LEU   B 1 48  ? -23.201 12.549  29.719  1.00 57.11  ? 54  LEU   B CG  1 
ATOM   2713 C  CD1 . LEU   B 1 48  ? -22.311 11.596  28.917  1.00 56.70  ? 54  LEU   B CD1 1 
ATOM   2714 C  CD2 . LEU   B 1 48  ? -23.068 13.974  29.223  1.00 59.20  ? 54  LEU   B CD2 1 
ATOM   2715 N  N   . MET   B 1 49  ? -24.881 11.868  32.856  1.00 53.91  ? 55  MET   B N   1 
ATOM   2716 C  CA  . MET   B 1 49  ? -24.302 12.141  34.181  1.00 53.61  ? 55  MET   B CA  1 
ATOM   2717 C  C   . MET   B 1 49  ? -24.127 10.873  35.029  1.00 52.53  ? 55  MET   B C   1 
ATOM   2718 O  O   . MET   B 1 49  ? -23.037 10.647  35.548  1.00 50.46  ? 55  MET   B O   1 
ATOM   2719 C  CB  . MET   B 1 49  ? -25.079 13.238  34.933  1.00 56.48  ? 55  MET   B CB  1 
ATOM   2720 C  CG  . MET   B 1 49  ? -25.041 14.624  34.247  1.00 60.86  ? 55  MET   B CG  1 
ATOM   2721 S  SD  . MET   B 1 49  ? -23.492 15.127  33.425  1.00 65.48  ? 55  MET   B SD  1 
ATOM   2722 C  CE  . MET   B 1 49  ? -22.427 15.406  34.835  1.00 62.48  ? 55  MET   B CE  1 
ATOM   2723 N  N   . LYS   B 1 50  ? -25.173 10.026  35.086  1.00 48.43  ? 56  LYS   B N   1 
ATOM   2724 C  CA  . LYS   B 1 50  ? -25.213 8.731   35.776  1.00 47.67  ? 56  LYS   B CA  1 
ATOM   2725 C  C   . LYS   B 1 50  ? -24.098 7.817   35.238  1.00 51.39  ? 56  LYS   B C   1 
ATOM   2726 O  O   . LYS   B 1 50  ? -23.423 7.147   36.023  1.00 51.03  ? 56  LYS   B O   1 
ATOM   2727 C  CB  . LYS   B 1 50  ? -26.591 8.078   35.551  1.00 50.60  ? 56  LYS   B CB  1 
ATOM   2728 C  CG  . LYS   B 1 50  ? -26.893 6.867   36.427  1.00 70.22  ? 56  LYS   B CG  1 
ATOM   2729 C  CD  . LYS   B 1 50  ? -28.324 6.378   36.200  1.00 83.51  ? 56  LYS   B CD  1 
ATOM   2730 C  CE  . LYS   B 1 50  ? -28.843 5.548   37.350  1.00 97.02  ? 56  LYS   B CE  1 
ATOM   2731 N  NZ  . LYS   B 1 50  ? -30.328 5.437   37.325  1.00 106.68 ? 56  LYS   B NZ  1 
ATOM   2732 N  N   . ARG   B 1 51  ? -23.899 7.812   33.896  1.00 46.86  ? 57  ARG   B N   1 
ATOM   2733 C  CA  . ARG   B 1 51  ? -22.877 7.012   33.223  1.00 45.48  ? 57  ARG   B CA  1 
ATOM   2734 C  C   . ARG   B 1 51  ? -21.460 7.454   33.571  1.00 47.17  ? 57  ARG   B C   1 
ATOM   2735 O  O   . ARG   B 1 51  ? -20.622 6.602   33.866  1.00 46.69  ? 57  ARG   B O   1 
ATOM   2736 C  CB  . ARG   B 1 51  ? -23.095 6.998   31.693  1.00 46.05  ? 57  ARG   B CB  1 
ATOM   2737 C  CG  . ARG   B 1 51  ? -22.157 6.044   30.951  1.00 53.92  ? 57  ARG   B CG  1 
ATOM   2738 C  CD  . ARG   B 1 51  ? -22.650 4.601   30.953  1.00 55.66  ? 57  ARG   B CD  1 
ATOM   2739 N  NE  . ARG   B 1 51  ? -23.860 4.460   30.146  1.00 59.64  ? 57  ARG   B NE  1 
ATOM   2740 C  CZ  . ARG   B 1 51  ? -23.864 4.280   28.829  1.00 62.15  ? 57  ARG   B CZ  1 
ATOM   2741 N  NH1 . ARG   B 1 51  ? -25.007 4.191   28.173  1.00 48.34  ? 57  ARG   B NH1 1 
ATOM   2742 N  NH2 . ARG   B 1 51  ? -22.720 4.187   28.160  1.00 39.37  ? 57  ARG   B NH2 1 
ATOM   2743 N  N   . LEU   B 1 52  ? -21.166 8.765   33.529  1.00 43.06  ? 58  LEU   B N   1 
ATOM   2744 C  CA  . LEU   B 1 52  ? -19.819 9.219   33.882  1.00 42.64  ? 58  LEU   B CA  1 
ATOM   2745 C  C   . LEU   B 1 52  ? -19.492 8.950   35.370  1.00 47.65  ? 58  LEU   B C   1 
ATOM   2746 O  O   . LEU   B 1 52  ? -18.344 8.626   35.676  1.00 46.34  ? 58  LEU   B O   1 
ATOM   2747 C  CB  . LEU   B 1 52  ? -19.564 10.684  33.484  1.00 43.04  ? 58  LEU   B CB  1 
ATOM   2748 C  CG  . LEU   B 1 52  ? -19.568 10.982  31.963  1.00 47.81  ? 58  LEU   B CG  1 
ATOM   2749 C  CD1 . LEU   B 1 52  ? -19.571 12.491  31.695  1.00 48.37  ? 58  LEU   B CD1 1 
ATOM   2750 C  CD2 . LEU   B 1 52  ? -18.381 10.333  31.261  1.00 48.84  ? 58  LEU   B CD2 1 
ATOM   2751 N  N   . SER   B 1 53  ? -20.523 9.002   36.267  1.00 46.15  ? 59  SER   B N   1 
ATOM   2752 C  CA  . SER   B 1 53  ? -20.388 8.712   37.705  1.00 46.43  ? 59  SER   B CA  1 
ATOM   2753 C  C   . SER   B 1 53  ? -19.968 7.247   37.868  1.00 50.34  ? 59  SER   B C   1 
ATOM   2754 O  O   . SER   B 1 53  ? -18.965 6.979   38.535  1.00 49.41  ? 59  SER   B O   1 
ATOM   2755 C  CB  . SER   B 1 53  ? -21.705 8.950   38.442  1.00 51.14  ? 59  SER   B CB  1 
ATOM   2756 O  OG  . SER   B 1 53  ? -22.238 10.243  38.220  1.00 62.23  ? 59  SER   B OG  1 
ATOM   2757 N  N   . SER   B 1 54  ? -20.666 6.311   37.155  1.00 46.64  ? 60  SER   B N   1 
ATOM   2758 C  CA  . SER   B 1 54  ? -20.358 4.871   37.180  1.00 45.68  ? 60  SER   B CA  1 
ATOM   2759 C  C   . SER   B 1 54  ? -18.923 4.549   36.732  1.00 46.27  ? 60  SER   B C   1 
ATOM   2760 O  O   . SER   B 1 54  ? -18.404 3.497   37.090  1.00 46.35  ? 60  SER   B O   1 
ATOM   2761 C  CB  . SER   B 1 54  ? -21.389 4.066   36.395  1.00 50.93  ? 60  SER   B CB  1 
ATOM   2762 O  OG  . SER   B 1 54  ? -21.297 4.278   34.996  1.00 61.20  ? 60  SER   B OG  1 
ATOM   2763 N  N   . LEU   B 1 55  ? -18.253 5.482   36.028  1.00 41.60  ? 61  LEU   B N   1 
ATOM   2764 C  CA  . LEU   B 1 55  ? -16.864 5.302   35.602  1.00 41.16  ? 61  LEU   B CA  1 
ATOM   2765 C  C   . LEU   B 1 55  ? -15.846 5.879   36.603  1.00 45.22  ? 61  LEU   B C   1 
ATOM   2766 O  O   . LEU   B 1 55  ? -14.646 5.863   36.343  1.00 42.18  ? 61  LEU   B O   1 
ATOM   2767 C  CB  . LEU   B 1 55  ? -16.630 5.846   34.172  1.00 41.57  ? 61  LEU   B CB  1 
ATOM   2768 C  CG  . LEU   B 1 55  ? -17.545 5.313   33.058  1.00 47.09  ? 61  LEU   B CG  1 
ATOM   2769 C  CD1 . LEU   B 1 55  ? -17.396 6.149   31.778  1.00 46.95  ? 61  LEU   B CD1 1 
ATOM   2770 C  CD2 . LEU   B 1 55  ? -17.310 3.810   32.788  1.00 50.32  ? 61  LEU   B CD2 1 
ATOM   2771 N  N   . GLY   B 1 56  ? -16.338 6.362   37.746  1.00 45.96  ? 62  GLY   B N   1 
ATOM   2772 C  CA  . GLY   B 1 56  ? -15.510 6.913   38.815  1.00 46.81  ? 62  GLY   B CA  1 
ATOM   2773 C  C   . GLY   B 1 56  ? -14.968 8.295   38.531  1.00 53.18  ? 62  GLY   B C   1 
ATOM   2774 O  O   . GLY   B 1 56  ? -13.911 8.660   39.058  1.00 54.10  ? 62  GLY   B O   1 
ATOM   2775 N  N   . CYS   B 1 57  ? -15.698 9.077   37.700  1.00 49.60  ? 63  CYS   B N   1 
ATOM   2776 C  CA  . CYS   B 1 57  ? -15.315 10.437  37.320  1.00 49.17  ? 63  CYS   B CA  1 
ATOM   2777 C  C   . CYS   B 1 57  ? -15.676 11.453  38.399  1.00 50.77  ? 63  CYS   B C   1 
ATOM   2778 O  O   . CYS   B 1 57  ? -16.816 11.474  38.856  1.00 49.10  ? 63  CYS   B O   1 
ATOM   2779 C  CB  . CYS   B 1 57  ? -15.937 10.840  35.982  1.00 49.73  ? 63  CYS   B CB  1 
ATOM   2780 S  SG  . CYS   B 1 57  ? -15.382 9.866   34.556  1.00 53.92  ? 63  CYS   B SG  1 
ATOM   2781 N  N   . HIS   B 1 58  ? -14.732 12.355  38.722  1.00 48.01  ? 64  HIS   B N   1 
ATOM   2782 C  CA  . HIS   B 1 58  ? -14.971 13.507  39.594  1.00 48.07  ? 64  HIS   B CA  1 
ATOM   2783 C  C   . HIS   B 1 58  ? -15.721 14.498  38.680  1.00 53.79  ? 64  HIS   B C   1 
ATOM   2784 O  O   . HIS   B 1 58  ? -15.093 15.098  37.810  1.00 54.54  ? 64  HIS   B O   1 
ATOM   2785 C  CB  . HIS   B 1 58  ? -13.634 14.133  40.043  1.00 48.47  ? 64  HIS   B CB  1 
ATOM   2786 C  CG  . HIS   B 1 58  ? -12.837 13.334  41.029  1.00 51.23  ? 64  HIS   B CG  1 
ATOM   2787 N  ND1 . HIS   B 1 58  ? -13.386 12.901  42.227  1.00 52.63  ? 64  HIS   B ND1 1 
ATOM   2788 C  CD2 . HIS   B 1 58  ? -11.522 13.016  41.011  1.00 52.38  ? 64  HIS   B CD2 1 
ATOM   2789 C  CE1 . HIS   B 1 58  ? -12.400 12.299  42.873  1.00 51.63  ? 64  HIS   B CE1 1 
ATOM   2790 N  NE2 . HIS   B 1 58  ? -11.261 12.336  42.177  1.00 51.99  ? 64  HIS   B NE2 1 
ATOM   2791 N  N   . LEU   B 1 59  ? -17.051 14.588  38.796  1.00 52.06  ? 65  LEU   B N   1 
ATOM   2792 C  CA  . LEU   B 1 59  ? -17.880 15.435  37.935  1.00 53.98  ? 65  LEU   B CA  1 
ATOM   2793 C  C   . LEU   B 1 59  ? -18.079 16.875  38.404  1.00 61.79  ? 65  LEU   B C   1 
ATOM   2794 O  O   . LEU   B 1 59  ? -18.348 17.117  39.585  1.00 61.67  ? 65  LEU   B O   1 
ATOM   2795 C  CB  . LEU   B 1 59  ? -19.271 14.800  37.680  1.00 54.44  ? 65  LEU   B CB  1 
ATOM   2796 C  CG  . LEU   B 1 59  ? -19.453 13.766  36.548  1.00 59.51  ? 65  LEU   B CG  1 
ATOM   2797 C  CD1 . LEU   B 1 59  ? -18.406 13.903  35.424  1.00 59.43  ? 65  LEU   B CD1 1 
ATOM   2798 C  CD2 . LEU   B 1 59  ? -19.511 12.366  37.096  1.00 62.80  ? 65  LEU   B CD2 1 
ATOM   2799 N  N   . LYS   B 1 60  ? -18.029 17.818  37.438  1.00 60.73  ? 66  LYS   B N   1 
ATOM   2800 C  CA  . LYS   B 1 60  ? -18.252 19.255  37.620  1.00 61.31  ? 66  LYS   B CA  1 
ATOM   2801 C  C   . LYS   B 1 60  ? -19.203 19.764  36.515  1.00 67.33  ? 66  LYS   B C   1 
ATOM   2802 O  O   . LYS   B 1 60  ? -18.750 20.196  35.454  1.00 67.25  ? 66  LYS   B O   1 
ATOM   2803 C  CB  . LYS   B 1 60  ? -16.916 20.026  37.635  1.00 63.63  ? 66  LYS   B CB  1 
ATOM   2804 C  CG  . LYS   B 1 60  ? -17.039 21.459  38.149  1.00 81.07  ? 66  LYS   B CG  1 
ATOM   2805 C  CD  . LYS   B 1 60  ? -15.727 22.223  38.037  1.00 92.85  ? 66  LYS   B CD  1 
ATOM   2806 C  CE  . LYS   B 1 60  ? -15.904 23.679  38.400  1.00 106.37 ? 66  LYS   B CE  1 
ATOM   2807 N  NZ  . LYS   B 1 60  ? -14.654 24.459  38.197  1.00 116.20 ? 66  LYS   B NZ  1 
ATOM   2808 N  N   . ASP   B 1 61  ? -20.520 19.684  36.760  1.00 65.01  ? 67  ASP   B N   1 
ATOM   2809 C  CA  . ASP   B 1 61  ? -21.533 20.120  35.799  1.00 65.52  ? 67  ASP   B CA  1 
ATOM   2810 C  C   . ASP   B 1 61  ? -21.658 21.654  35.762  1.00 72.57  ? 67  ASP   B C   1 
ATOM   2811 O  O   . ASP   B 1 61  ? -21.963 22.274  36.783  1.00 72.32  ? 67  ASP   B O   1 
ATOM   2812 C  CB  . ASP   B 1 61  ? -22.889 19.468  36.121  1.00 66.96  ? 67  ASP   B CB  1 
ATOM   2813 C  CG  . ASP   B 1 61  ? -23.893 19.414  34.984  1.00 75.01  ? 67  ASP   B CG  1 
ATOM   2814 O  OD1 . ASP   B 1 61  ? -23.699 20.129  33.978  1.00 75.04  ? 67  ASP   B OD1 1 
ATOM   2815 O  OD2 . ASP   B 1 61  ? -24.883 18.665  35.107  1.00 81.89  ? 67  ASP   B OD2 1 
ATOM   2816 N  N   . PHE   B 1 62  ? -21.422 22.255  34.577  1.00 71.04  ? 68  PHE   B N   1 
ATOM   2817 C  CA  . PHE   B 1 62  ? -21.531 23.700  34.339  1.00 71.65  ? 68  PHE   B CA  1 
ATOM   2818 C  C   . PHE   B 1 62  ? -22.946 24.080  33.868  1.00 80.09  ? 68  PHE   B C   1 
ATOM   2819 O  O   . PHE   B 1 62  ? -23.247 25.266  33.720  1.00 80.42  ? 68  PHE   B O   1 
ATOM   2820 C  CB  . PHE   B 1 62  ? -20.482 24.164  33.320  1.00 73.06  ? 68  PHE   B CB  1 
ATOM   2821 C  CG  . PHE   B 1 62  ? -19.097 24.396  33.868  1.00 74.32  ? 68  PHE   B CG  1 
ATOM   2822 C  CD1 . PHE   B 1 62  ? -18.199 23.344  34.006  1.00 77.38  ? 68  PHE   B CD1 1 
ATOM   2823 C  CD2 . PHE   B 1 62  ? -18.665 25.676  34.188  1.00 76.51  ? 68  PHE   B CD2 1 
ATOM   2824 C  CE1 . PHE   B 1 62  ? -16.903 23.566  34.484  1.00 78.38  ? 68  PHE   B CE1 1 
ATOM   2825 C  CE2 . PHE   B 1 62  ? -17.369 25.899  34.661  1.00 79.35  ? 68  PHE   B CE2 1 
ATOM   2826 C  CZ  . PHE   B 1 62  ? -16.496 24.842  34.807  1.00 77.58  ? 68  PHE   B CZ  1 
ATOM   2827 N  N   . GLY   B 1 63  ? -23.788 23.069  33.638  1.00 79.76  ? 69  GLY   B N   1 
ATOM   2828 C  CA  . GLY   B 1 63  ? -25.178 23.221  33.212  1.00 81.21  ? 69  GLY   B CA  1 
ATOM   2829 C  C   . GLY   B 1 63  ? -25.384 23.734  31.799  1.00 88.96  ? 69  GLY   B C   1 
ATOM   2830 O  O   . GLY   B 1 63  ? -24.419 24.068  31.101  1.00 88.85  ? 69  GLY   B O   1 
ATOM   2831 N  N   . ASP   B 1 64  ? -26.662 23.807  31.373  1.00 87.93  ? 70  ASP   B N   1 
ATOM   2832 C  CA  . ASP   B 1 64  ? -27.041 24.301  30.048  1.00 89.19  ? 70  ASP   B CA  1 
ATOM   2833 C  C   . ASP   B 1 64  ? -26.874 25.831  29.949  1.00 96.58  ? 70  ASP   B C   1 
ATOM   2834 O  O   . ASP   B 1 64  ? -27.682 26.577  30.515  1.00 96.19  ? 70  ASP   B O   1 
ATOM   2835 C  CB  . ASP   B 1 64  ? -28.471 23.850  29.667  1.00 90.97  ? 70  ASP   B CB  1 
ATOM   2836 C  CG  . ASP   B 1 64  ? -28.667 22.346  29.521  1.00 99.11  ? 70  ASP   B CG  1 
ATOM   2837 O  OD1 . ASP   B 1 64  ? -27.686 21.644  29.186  1.00 98.88  ? 70  ASP   B OD1 1 
ATOM   2838 O  OD2 . ASP   B 1 64  ? -29.810 21.876  29.702  1.00 104.17 ? 70  ASP   B OD2 1 
ATOM   2839 N  N   . LEU   B 1 65  ? -25.799 26.287  29.251  1.00 95.47  ? 71  LEU   B N   1 
ATOM   2840 C  CA  . LEU   B 1 65  ? -25.461 27.704  29.059  1.00 96.41  ? 71  LEU   B CA  1 
ATOM   2841 C  C   . LEU   B 1 65  ? -26.544 28.498  28.336  1.00 104.21 ? 71  LEU   B C   1 
ATOM   2842 O  O   . LEU   B 1 65  ? -27.155 27.997  27.391  1.00 103.57 ? 71  LEU   B O   1 
ATOM   2843 C  CB  . LEU   B 1 65  ? -24.116 27.881  28.330  1.00 96.24  ? 71  LEU   B CB  1 
ATOM   2844 C  CG  . LEU   B 1 65  ? -22.831 27.798  29.162  1.00 100.84 ? 71  LEU   B CG  1 
ATOM   2845 C  CD1 . LEU   B 1 65  ? -21.613 27.971  28.278  1.00 100.82 ? 71  LEU   B CD1 1 
ATOM   2846 C  CD2 . LEU   B 1 65  ? -22.790 28.863  30.257  1.00 103.54 ? 71  LEU   B CD2 1 
ATOM   2847 N  N   . SER   B 1 66  ? -26.773 29.743  28.789  1.00 104.27 ? 72  SER   B N   1 
ATOM   2848 C  CA  . SER   B 1 66  ? -27.763 30.652  28.212  1.00 105.68 ? 72  SER   B CA  1 
ATOM   2849 C  C   . SER   B 1 66  ? -27.127 31.539  27.148  1.00 112.67 ? 72  SER   B C   1 
ATOM   2850 O  O   . SER   B 1 66  ? -26.095 32.172  27.401  1.00 112.07 ? 72  SER   B O   1 
ATOM   2851 C  CB  . SER   B 1 66  ? -28.417 31.504  29.298  1.00 109.49 ? 72  SER   B CB  1 
ATOM   2852 O  OG  . SER   B 1 66  ? -29.315 30.743  30.089  1.00 118.66 ? 72  SER   B OG  1 
ATOM   2853 N  N   . PHE   B 1 67  ? -27.738 31.563  25.951  1.00 111.94 ? 73  PHE   B N   1 
ATOM   2854 C  CA  . PHE   B 1 67  ? -27.281 32.373  24.823  1.00 113.14 ? 73  PHE   B CA  1 
ATOM   2855 C  C   . PHE   B 1 67  ? -28.361 33.354  24.379  1.00 120.01 ? 73  PHE   B C   1 
ATOM   2856 O  O   . PHE   B 1 67  ? -29.508 32.957  24.154  1.00 119.41 ? 73  PHE   B O   1 
ATOM   2857 C  CB  . PHE   B 1 67  ? -26.813 31.495  23.648  1.00 114.97 ? 73  PHE   B CB  1 
ATOM   2858 C  CG  . PHE   B 1 67  ? -25.556 30.696  23.901  1.00 116.53 ? 73  PHE   B CG  1 
ATOM   2859 C  CD1 . PHE   B 1 67  ? -24.324 31.328  24.039  1.00 119.68 ? 73  PHE   B CD1 1 
ATOM   2860 C  CD2 . PHE   B 1 67  ? -25.593 29.308  23.950  1.00 118.74 ? 73  PHE   B CD2 1 
ATOM   2861 C  CE1 . PHE   B 1 67  ? -23.161 30.588  24.267  1.00 120.65 ? 73  PHE   B CE1 1 
ATOM   2862 C  CE2 . PHE   B 1 67  ? -24.427 28.568  24.167  1.00 121.67 ? 73  PHE   B CE2 1 
ATOM   2863 C  CZ  . PHE   B 1 67  ? -23.220 29.213  24.324  1.00 119.83 ? 73  PHE   B CZ  1 
ATOM   2864 N  N   . THR   B 1 68  ? -27.989 34.640  24.276  1.00 119.13 ? 74  THR   B N   1 
ATOM   2865 C  CA  . THR   B 1 68  ? -28.885 35.725  23.865  1.00 120.14 ? 74  THR   B CA  1 
ATOM   2866 C  C   . THR   B 1 68  ? -28.549 36.207  22.446  1.00 126.54 ? 74  THR   B C   1 
ATOM   2867 O  O   . THR   B 1 68  ? -27.379 36.499  22.171  1.00 126.25 ? 74  THR   B O   1 
ATOM   2868 C  CB  . THR   B 1 68  ? -28.897 36.865  24.899  1.00 128.55 ? 74  THR   B CB  1 
ATOM   2869 O  OG1 . THR   B 1 68  ? -27.553 37.225  25.233  1.00 128.34 ? 74  THR   B OG1 1 
ATOM   2870 C  CG2 . THR   B 1 68  ? -29.684 36.508  26.158  1.00 126.70 ? 74  THR   B CG2 1 
ATOM   2871 N  N   . PRO   B 1 69  ? -29.542 36.278  21.523  1.00 124.79 ? 75  PRO   B N   1 
ATOM   2872 C  CA  . PRO   B 1 69  ? -29.234 36.722  20.154  1.00 125.29 ? 75  PRO   B CA  1 
ATOM   2873 C  C   . PRO   B 1 69  ? -29.081 38.236  20.033  1.00 131.07 ? 75  PRO   B C   1 
ATOM   2874 O  O   . PRO   B 1 69  ? -29.818 38.986  20.680  1.00 130.71 ? 75  PRO   B O   1 
ATOM   2875 C  CB  . PRO   B 1 69  ? -30.418 36.199  19.323  1.00 126.92 ? 75  PRO   B CB  1 
ATOM   2876 C  CG  . PRO   B 1 69  ? -31.347 35.503  20.296  1.00 131.09 ? 75  PRO   B CG  1 
ATOM   2877 C  CD  . PRO   B 1 69  ? -30.975 35.959  21.666  1.00 126.48 ? 75  PRO   B CD  1 
ATOM   2878 N  N   . VAL   B 1 70  ? -28.117 38.680  19.200  1.00 128.94 ? 76  VAL   B N   1 
ATOM   2879 C  CA  . VAL   B 1 70  ? -27.843 40.099  18.934  1.00 129.35 ? 76  VAL   B CA  1 
ATOM   2880 C  C   . VAL   B 1 70  ? -29.002 40.651  18.061  1.00 134.53 ? 76  VAL   B C   1 
ATOM   2881 O  O   . VAL   B 1 70  ? -29.326 40.022  17.047  1.00 134.01 ? 76  VAL   B O   1 
ATOM   2882 C  CB  . VAL   B 1 70  ? -26.441 40.310  18.280  1.00 133.23 ? 76  VAL   B CB  1 
ATOM   2883 C  CG1 . VAL   B 1 70  ? -26.154 41.789  18.022  1.00 133.02 ? 76  VAL   B CG1 1 
ATOM   2884 C  CG2 . VAL   B 1 70  ? -25.331 39.693  19.130  1.00 133.03 ? 76  VAL   B CG2 1 
ATOM   2885 N  N   . PRO   B 1 71  ? -29.666 41.776  18.448  1.00 132.13 ? 77  PRO   B N   1 
ATOM   2886 C  CA  . PRO   B 1 71  ? -30.791 42.286  17.635  1.00 132.27 ? 77  PRO   B CA  1 
ATOM   2887 C  C   . PRO   B 1 71  ? -30.385 42.771  16.240  1.00 136.83 ? 77  PRO   B C   1 
ATOM   2888 O  O   . PRO   B 1 71  ? -31.053 42.423  15.263  1.00 136.33 ? 77  PRO   B O   1 
ATOM   2889 C  CB  . PRO   B 1 71  ? -31.387 43.411  18.497  1.00 133.98 ? 77  PRO   B CB  1 
ATOM   2890 C  CG  . PRO   B 1 71  ? -30.791 43.233  19.859  1.00 138.29 ? 77  PRO   B CG  1 
ATOM   2891 C  CD  . PRO   B 1 71  ? -29.445 42.630  19.632  1.00 133.77 ? 77  PRO   B CD  1 
ATOM   2892 N  N   . LYS   B 1 72  ? -29.285 43.549  16.144  1.00 133.84 ? 78  LYS   B N   1 
ATOM   2893 C  CA  . LYS   B 1 72  ? -28.764 44.058  14.876  1.00 133.78 ? 78  LYS   B CA  1 
ATOM   2894 C  C   . LYS   B 1 72  ? -27.576 43.190  14.442  1.00 137.49 ? 78  LYS   B C   1 
ATOM   2895 O  O   . LYS   B 1 72  ? -26.425 43.464  14.801  1.00 137.02 ? 78  LYS   B O   1 
ATOM   2896 C  CB  . LYS   B 1 72  ? -28.392 45.550  14.986  1.00 136.52 ? 78  LYS   B CB  1 
ATOM   2897 C  CG  . LYS   B 1 72  ? -28.460 46.295  13.657  1.00 152.49 ? 78  LYS   B CG  1 
ATOM   2898 C  CD  . LYS   B 1 72  ? -28.104 47.770  13.819  1.00 162.77 ? 78  LYS   B CD  1 
ATOM   2899 C  CE  . LYS   B 1 72  ? -28.295 48.563  12.547  1.00 173.23 ? 78  LYS   B CE  1 
ATOM   2900 N  NZ  . LYS   B 1 72  ? -29.728 48.863  12.284  1.00 181.57 ? 78  LYS   B NZ  1 
ATOM   2901 N  N   . ASP   B 1 73  ? -27.880 42.107  13.707  1.00 133.99 ? 79  ASP   B N   1 
ATOM   2902 C  CA  . ASP   B 1 73  ? -26.900 41.139  13.218  1.00 133.72 ? 79  ASP   B CA  1 
ATOM   2903 C  C   . ASP   B 1 73  ? -27.051 40.929  11.703  1.00 137.08 ? 79  ASP   B C   1 
ATOM   2904 O  O   . ASP   B 1 73  ? -27.705 39.981  11.258  1.00 136.59 ? 79  ASP   B O   1 
ATOM   2905 C  CB  . ASP   B 1 73  ? -27.017 39.813  14.007  1.00 135.56 ? 79  ASP   B CB  1 
ATOM   2906 C  CG  . ASP   B 1 73  ? -25.852 38.845  13.866  1.00 145.10 ? 79  ASP   B CG  1 
ATOM   2907 O  OD1 . ASP   B 1 73  ? -24.863 39.195  13.187  1.00 145.57 ? 79  ASP   B OD1 1 
ATOM   2908 O  OD2 . ASP   B 1 73  ? -25.924 37.743  14.450  1.00 150.78 ? 79  ASP   B OD2 1 
ATOM   2909 N  N   . ASP   B 1 74  ? -26.457 41.845  10.917  1.00 133.26 ? 80  ASP   B N   1 
ATOM   2910 C  CA  . ASP   B 1 74  ? -26.480 41.810  9.452   1.00 132.79 ? 80  ASP   B CA  1 
ATOM   2911 C  C   . ASP   B 1 74  ? -25.392 40.863  8.940   1.00 135.35 ? 80  ASP   B C   1 
ATOM   2912 O  O   . ASP   B 1 74  ? -24.254 40.918  9.420   1.00 134.86 ? 80  ASP   B O   1 
ATOM   2913 C  CB  . ASP   B 1 74  ? -26.322 43.224  8.865   1.00 134.69 ? 80  ASP   B CB  1 
ATOM   2914 C  CG  . ASP   B 1 74  ? -27.426 44.176  9.286   1.00 144.75 ? 80  ASP   B CG  1 
ATOM   2915 O  OD1 . ASP   B 1 74  ? -27.262 44.850  10.326  1.00 145.35 ? 80  ASP   B OD1 1 
ATOM   2916 O  OD2 . ASP   B 1 74  ? -28.460 44.233  8.587   1.00 150.15 ? 80  ASP   B OD2 1 
ATOM   2917 N  N   . LEU   B 1 75  ? -25.752 39.979  7.987   1.00 130.72 ? 81  LEU   B N   1 
ATOM   2918 C  CA  . LEU   B 1 75  ? -24.854 38.964  7.432   1.00 129.91 ? 81  LEU   B CA  1 
ATOM   2919 C  C   . LEU   B 1 75  ? -23.715 39.564  6.578   1.00 132.39 ? 81  LEU   B C   1 
ATOM   2920 O  O   . LEU   B 1 75  ? -23.940 40.487  5.794   1.00 131.89 ? 81  LEU   B O   1 
ATOM   2921 C  CB  . LEU   B 1 75  ? -25.632 37.849  6.687   1.00 129.92 ? 81  LEU   B CB  1 
ATOM   2922 C  CG  . LEU   B 1 75  ? -26.232 38.088  5.294   1.00 134.57 ? 81  LEU   B CG  1 
ATOM   2923 C  CD1 . LEU   B 1 75  ? -26.514 36.770  4.612   1.00 134.75 ? 81  LEU   B CD1 1 
ATOM   2924 C  CD2 . LEU   B 1 75  ? -27.530 38.855  5.368   1.00 136.93 ? 81  LEU   B CD2 1 
ATOM   2925 N  N   . TYR   B 1 76  ? -22.486 39.050  6.792   1.00 128.00 ? 82  TYR   B N   1 
ATOM   2926 C  CA  . TYR   B 1 76  ? -21.236 39.466  6.146   1.00 127.38 ? 82  TYR   B CA  1 
ATOM   2927 C  C   . TYR   B 1 76  ? -21.132 38.959  4.704   1.00 130.30 ? 82  TYR   B C   1 
ATOM   2928 O  O   . TYR   B 1 76  ? -21.347 37.772  4.453   1.00 129.80 ? 82  TYR   B O   1 
ATOM   2929 C  CB  . TYR   B 1 76  ? -20.035 38.987  6.986   1.00 128.62 ? 82  TYR   B CB  1 
ATOM   2930 C  CG  . TYR   B 1 76  ? -18.676 39.438  6.491   1.00 130.67 ? 82  TYR   B CG  1 
ATOM   2931 C  CD1 . TYR   B 1 76  ? -18.153 40.674  6.859   1.00 132.71 ? 82  TYR   B CD1 1 
ATOM   2932 C  CD2 . TYR   B 1 76  ? -17.879 38.596  5.720   1.00 131.55 ? 82  TYR   B CD2 1 
ATOM   2933 C  CE1 . TYR   B 1 76  ? -16.890 41.083  6.429   1.00 133.60 ? 82  TYR   B CE1 1 
ATOM   2934 C  CE2 . TYR   B 1 76  ? -16.617 38.995  5.281   1.00 132.55 ? 82  TYR   B CE2 1 
ATOM   2935 C  CZ  . TYR   B 1 76  ? -16.125 40.239  5.641   1.00 140.35 ? 82  TYR   B CZ  1 
ATOM   2936 O  OH  . TYR   B 1 76  ? -14.879 40.636  5.217   1.00 141.73 ? 82  TYR   B OH  1 
ATOM   2937 N  N   . ASN   B 1 77  ? -20.784 39.874  3.766   1.00 126.25 ? 83  ASN   B N   1 
ATOM   2938 C  CA  . ASN   B 1 77  ? -20.606 39.645  2.320   1.00 125.71 ? 83  ASN   B CA  1 
ATOM   2939 C  C   . ASN   B 1 77  ? -21.812 38.953  1.643   1.00 128.34 ? 83  ASN   B C   1 
ATOM   2940 O  O   . ASN   B 1 77  ? -21.645 38.273  0.624   1.00 127.77 ? 83  ASN   B O   1 
ATOM   2941 C  CB  . ASN   B 1 77  ? -19.289 38.898  2.031   1.00 126.93 ? 83  ASN   B CB  1 
ATOM   2942 C  CG  . ASN   B 1 77  ? -18.134 39.806  1.685   1.00 149.88 ? 83  ASN   B CG  1 
ATOM   2943 O  OD1 . ASN   B 1 77  ? -17.621 40.557  2.525   1.00 144.20 ? 83  ASN   B OD1 1 
ATOM   2944 N  ND2 . ASN   B 1 77  ? -17.684 39.741  0.440   1.00 141.27 ? 83  ASN   B ND2 1 
ATOM   2945 N  N   . ASN   B 1 78  ? -23.028 39.176  2.198   1.00 124.10 ? 84  ASN   B N   1 
ATOM   2946 C  CA  . ASN   B 1 78  ? -24.316 38.633  1.746   1.00 123.57 ? 84  ASN   B CA  1 
ATOM   2947 C  C   . ASN   B 1 78  ? -24.307 37.094  1.621   1.00 126.57 ? 84  ASN   B C   1 
ATOM   2948 O  O   . ASN   B 1 78  ? -24.775 36.543  0.621   1.00 126.13 ? 84  ASN   B O   1 
ATOM   2949 C  CB  . ASN   B 1 78  ? -24.792 39.323  0.460   1.00 124.32 ? 84  ASN   B CB  1 
ATOM   2950 C  CG  . ASN   B 1 78  ? -25.210 40.752  0.682   1.00 147.18 ? 84  ASN   B CG  1 
ATOM   2951 O  OD1 . ASN   B 1 78  ? -24.386 41.674  0.685   1.00 140.32 ? 84  ASN   B OD1 1 
ATOM   2952 N  ND2 . ASN   B 1 78  ? -26.501 40.960  0.893   1.00 139.38 ? 84  ASN   B ND2 1 
ATOM   2953 N  N   . LEU   B 1 79  ? -23.761 36.409  2.650   1.00 122.45 ? 85  LEU   B N   1 
ATOM   2954 C  CA  . LEU   B 1 79  ? -23.676 34.946  2.712   1.00 121.78 ? 85  LEU   B CA  1 
ATOM   2955 C  C   . LEU   B 1 79  ? -23.649 34.430  4.163   1.00 124.10 ? 85  LEU   B C   1 
ATOM   2956 O  O   . LEU   B 1 79  ? -24.580 33.730  4.567   1.00 123.33 ? 85  LEU   B O   1 
ATOM   2957 C  CB  . LEU   B 1 79  ? -22.464 34.429  1.900   1.00 121.82 ? 85  LEU   B CB  1 
ATOM   2958 C  CG  . LEU   B 1 79  ? -22.440 32.939  1.535   1.00 126.41 ? 85  LEU   B CG  1 
ATOM   2959 C  CD1 . LEU   B 1 79  ? -23.374 32.631  0.366   1.00 126.47 ? 85  LEU   B CD1 1 
ATOM   2960 C  CD2 . LEU   B 1 79  ? -21.037 32.504  1.181   1.00 128.88 ? 85  LEU   B CD2 1 
ATOM   2961 N  N   . ILE   B 1 80  ? -22.600 34.801  4.940   1.00 119.73 ? 86  ILE   B N   1 
ATOM   2962 C  CA  . ILE   B 1 80  ? -22.364 34.395  6.337   1.00 119.11 ? 86  ILE   B CA  1 
ATOM   2963 C  C   . ILE   B 1 80  ? -23.508 34.842  7.266   1.00 122.40 ? 86  ILE   B C   1 
ATOM   2964 O  O   . ILE   B 1 80  ? -23.431 35.908  7.876   1.00 121.79 ? 86  ILE   B O   1 
ATOM   2965 C  CB  . ILE   B 1 80  ? -20.956 34.855  6.853   1.00 122.10 ? 86  ILE   B CB  1 
ATOM   2966 C  CG1 . ILE   B 1 80  ? -19.831 34.696  5.787   1.00 122.46 ? 86  ILE   B CG1 1 
ATOM   2967 C  CG2 . ILE   B 1 80  ? -20.578 34.173  8.175   1.00 122.81 ? 86  ILE   B CG2 1 
ATOM   2968 C  CD1 . ILE   B 1 80  ? -19.499 33.266  5.324   1.00 130.37 ? 86  ILE   B CD1 1 
ATOM   2969 N  N   . VAL   B 1 81  ? -24.561 34.007  7.369   1.00 118.81 ? 87  VAL   B N   1 
ATOM   2970 C  CA  . VAL   B 1 81  ? -25.758 34.247  8.187   1.00 118.56 ? 87  VAL   B CA  1 
ATOM   2971 C  C   . VAL   B 1 81  ? -25.427 34.173  9.701   1.00 122.00 ? 87  VAL   B C   1 
ATOM   2972 O  O   . VAL   B 1 81  ? -24.796 33.212  10.151  1.00 121.69 ? 87  VAL   B O   1 
ATOM   2973 C  CB  . VAL   B 1 81  ? -26.950 33.337  7.751   1.00 122.57 ? 87  VAL   B CB  1 
ATOM   2974 C  CG1 . VAL   B 1 81  ? -26.564 31.860  7.698   1.00 122.40 ? 87  VAL   B CG1 1 
ATOM   2975 C  CG2 . VAL   B 1 81  ? -28.197 33.558  8.607   1.00 122.40 ? 87  VAL   B CG2 1 
ATOM   2976 N  N   . ASN   B 1 82  ? -25.843 35.223  10.460  1.00 117.86 ? 88  ASN   B N   1 
ATOM   2977 C  CA  . ASN   B 1 82  ? -25.632 35.428  11.905  1.00 117.19 ? 88  ASN   B CA  1 
ATOM   2978 C  C   . ASN   B 1 82  ? -24.132 35.366  12.313  1.00 120.34 ? 88  ASN   B C   1 
ATOM   2979 O  O   . ASN   B 1 82  ? -23.766 34.496  13.107  1.00 119.67 ? 88  ASN   B O   1 
ATOM   2980 C  CB  . ASN   B 1 82  ? -26.500 34.469  12.751  1.00 117.21 ? 88  ASN   B CB  1 
ATOM   2981 C  CG  . ASN   B 1 82  ? -27.990 34.591  12.533  1.00 137.84 ? 88  ASN   B CG  1 
ATOM   2982 O  OD1 . ASN   B 1 82  ? -28.604 35.631  12.796  1.00 132.48 ? 88  ASN   B OD1 1 
ATOM   2983 N  ND2 . ASN   B 1 82  ? -28.616 33.503  12.109  1.00 128.22 ? 88  ASN   B ND2 1 
ATOM   2984 N  N   . PRO   B 1 83  ? -23.239 36.255  11.795  1.00 116.83 ? 89  PRO   B N   1 
ATOM   2985 C  CA  . PRO   B 1 83  ? -21.816 36.153  12.172  1.00 116.62 ? 89  PRO   B CA  1 
ATOM   2986 C  C   . PRO   B 1 83  ? -21.455 36.698  13.554  1.00 120.60 ? 89  PRO   B C   1 
ATOM   2987 O  O   . PRO   B 1 83  ? -20.557 36.148  14.189  1.00 120.05 ? 89  PRO   B O   1 
ATOM   2988 C  CB  . PRO   B 1 83  ? -21.092 36.900  11.051  1.00 118.37 ? 89  PRO   B CB  1 
ATOM   2989 C  CG  . PRO   B 1 83  ? -22.078 37.887  10.555  1.00 122.85 ? 89  PRO   B CG  1 
ATOM   2990 C  CD  . PRO   B 1 83  ? -23.461 37.357  10.833  1.00 118.40 ? 89  PRO   B CD  1 
ATOM   2991 N  N   . ARG   B 1 84  ? -22.137 37.769  14.017  1.00 117.34 ? 90  ARG   B N   1 
ATOM   2992 C  CA  . ARG   B 1 84  ? -21.880 38.392  15.323  1.00 117.15 ? 90  ARG   B CA  1 
ATOM   2993 C  C   . ARG   B 1 84  ? -22.243 37.483  16.500  1.00 119.93 ? 90  ARG   B C   1 
ATOM   2994 O  O   . ARG   B 1 84  ? -21.449 37.371  17.430  1.00 119.37 ? 90  ARG   B O   1 
ATOM   2995 C  CB  . ARG   B 1 84  ? -22.570 39.762  15.448  1.00 118.20 ? 90  ARG   B CB  1 
ATOM   2996 C  CG  . ARG   B 1 84  ? -21.910 40.857  14.621  1.00 130.57 ? 90  ARG   B CG  1 
ATOM   2997 C  CD  . ARG   B 1 84  ? -22.773 42.102  14.545  1.00 143.40 ? 90  ARG   B CD  1 
ATOM   2998 N  NE  . ARG   B 1 84  ? -22.250 43.076  13.583  1.00 154.65 ? 90  ARG   B NE  1 
ATOM   2999 C  CZ  . ARG   B 1 84  ? -22.586 43.122  12.297  1.00 170.38 ? 90  ARG   B CZ  1 
ATOM   3000 N  NH1 . ARG   B 1 84  ? -23.444 42.242  11.795  1.00 158.47 ? 90  ARG   B NH1 1 
ATOM   3001 N  NH2 . ARG   B 1 84  ? -22.063 44.045  11.501  1.00 157.50 ? 90  ARG   B NH2 1 
ATOM   3002 N  N   . SER   B 1 85  ? -23.423 36.825  16.443  1.00 115.70 ? 91  SER   B N   1 
ATOM   3003 C  CA  . SER   B 1 85  ? -23.933 35.912  17.473  1.00 115.23 ? 91  SER   B CA  1 
ATOM   3004 C  C   . SER   B 1 85  ? -23.051 34.677  17.696  1.00 118.49 ? 91  SER   B C   1 
ATOM   3005 O  O   . SER   B 1 85  ? -22.916 34.229  18.835  1.00 118.08 ? 91  SER   B O   1 
ATOM   3006 C  CB  . SER   B 1 85  ? -25.359 35.479  17.146  1.00 118.78 ? 91  SER   B CB  1 
ATOM   3007 O  OG  . SER   B 1 85  ? -26.269 36.561  17.255  1.00 127.74 ? 91  SER   B OG  1 
ATOM   3008 N  N   . VAL   B 1 86  ? -22.462 34.132  16.616  1.00 114.54 ? 92  VAL   B N   1 
ATOM   3009 C  CA  . VAL   B 1 86  ? -21.597 32.948  16.657  1.00 114.15 ? 92  VAL   B CA  1 
ATOM   3010 C  C   . VAL   B 1 86  ? -20.223 33.290  17.267  1.00 117.94 ? 92  VAL   B C   1 
ATOM   3011 O  O   . VAL   B 1 86  ? -19.792 32.610  18.201  1.00 117.74 ? 92  VAL   B O   1 
ATOM   3012 C  CB  . VAL   B 1 86  ? -21.505 32.237  15.270  1.00 117.87 ? 92  VAL   B CB  1 
ATOM   3013 C  CG1 . VAL   B 1 86  ? -20.462 31.120  15.268  1.00 117.65 ? 92  VAL   B CG1 1 
ATOM   3014 C  CG2 . VAL   B 1 86  ? -22.865 31.691  14.840  1.00 117.66 ? 92  VAL   B CG2 1 
ATOM   3015 N  N   . GLY   B 1 87  ? -19.574 34.334  16.744  1.00 114.16 ? 93  GLY   B N   1 
ATOM   3016 C  CA  . GLY   B 1 87  ? -18.257 34.794  17.186  1.00 113.83 ? 93  GLY   B CA  1 
ATOM   3017 C  C   . GLY   B 1 87  ? -18.188 35.324  18.608  1.00 117.13 ? 93  GLY   B C   1 
ATOM   3018 O  O   . GLY   B 1 87  ? -17.151 35.197  19.268  1.00 116.09 ? 93  GLY   B O   1 
ATOM   3019 N  N   . LEU   B 1 88  ? -19.293 35.934  19.085  1.00 113.77 ? 94  LEU   B N   1 
ATOM   3020 C  CA  . LEU   B 1 88  ? -19.421 36.486  20.437  1.00 113.39 ? 94  LEU   B CA  1 
ATOM   3021 C  C   . LEU   B 1 88  ? -19.530 35.334  21.446  1.00 115.34 ? 94  LEU   B C   1 
ATOM   3022 O  O   . LEU   B 1 88  ? -18.790 35.319  22.431  1.00 114.77 ? 94  LEU   B O   1 
ATOM   3023 C  CB  . LEU   B 1 88  ? -20.660 37.405  20.512  1.00 113.69 ? 94  LEU   B CB  1 
ATOM   3024 C  CG  . LEU   B 1 88  ? -20.821 38.316  21.733  1.00 118.77 ? 94  LEU   B CG  1 
ATOM   3025 C  CD1 . LEU   B 1 88  ? -19.969 39.577  21.604  1.00 119.00 ? 94  LEU   B CD1 1 
ATOM   3026 C  CD2 . LEU   B 1 88  ? -22.278 38.712  21.908  1.00 121.55 ? 94  LEU   B CD2 1 
ATOM   3027 N  N   . ALA   B 1 89  ? -20.422 34.356  21.167  1.00 110.20 ? 95  ALA   B N   1 
ATOM   3028 C  CA  . ALA   B 1 89  ? -20.665 33.170  21.991  1.00 109.16 ? 95  ALA   B CA  1 
ATOM   3029 C  C   . ALA   B 1 89  ? -19.433 32.266  22.129  1.00 110.77 ? 95  ALA   B C   1 
ATOM   3030 O  O   . ALA   B 1 89  ? -19.245 31.663  23.185  1.00 110.26 ? 95  ALA   B O   1 
ATOM   3031 C  CB  . ALA   B 1 89  ? -21.835 32.379  21.430  1.00 109.86 ? 95  ALA   B CB  1 
ATOM   3032 N  N   . ASN   B 1 90  ? -18.597 32.184  21.078  1.00 105.80 ? 96  ASN   B N   1 
ATOM   3033 C  CA  . ASN   B 1 90  ? -17.380 31.369  21.070  1.00 104.95 ? 96  ASN   B CA  1 
ATOM   3034 C  C   . ASN   B 1 90  ? -16.222 31.982  21.875  1.00 107.84 ? 96  ASN   B C   1 
ATOM   3035 O  O   . ASN   B 1 90  ? -15.388 31.228  22.370  1.00 107.58 ? 96  ASN   B O   1 
ATOM   3036 C  CB  . ASN   B 1 90  ? -16.946 31.023  19.642  1.00 104.40 ? 96  ASN   B CB  1 
ATOM   3037 C  CG  . ASN   B 1 90  ? -17.525 29.725  19.131  1.00 117.80 ? 96  ASN   B CG  1 
ATOM   3038 O  OD1 . ASN   B 1 90  ? -17.139 28.633  19.560  1.00 108.43 ? 96  ASN   B OD1 1 
ATOM   3039 N  ND2 . ASN   B 1 90  ? -18.457 29.812  18.195  1.00 107.01 ? 96  ASN   B ND2 1 
ATOM   3040 N  N   . GLN   B 1 91  ? -16.168 33.332  22.016  1.00 103.10 ? 97  GLN   B N   1 
ATOM   3041 C  CA  . GLN   B 1 91  ? -15.130 34.046  22.787  1.00 102.10 ? 97  GLN   B CA  1 
ATOM   3042 C  C   . GLN   B 1 91  ? -15.272 33.727  24.277  1.00 103.20 ? 97  GLN   B C   1 
ATOM   3043 O  O   . GLN   B 1 91  ? -14.278 33.633  25.004  1.00 102.20 ? 97  GLN   B O   1 
ATOM   3044 C  CB  . GLN   B 1 91  ? -15.253 35.570  22.566  1.00 103.60 ? 97  GLN   B CB  1 
ATOM   3045 C  CG  . GLN   B 1 91  ? -14.116 36.406  23.178  1.00 119.62 ? 97  GLN   B CG  1 
ATOM   3046 C  CD  . GLN   B 1 91  ? -14.408 37.891  23.228  1.00 139.95 ? 97  GLN   B CD  1 
ATOM   3047 O  OE1 . GLN   B 1 91  ? -15.551 38.334  23.400  1.00 135.52 ? 97  GLN   B OE1 1 
ATOM   3048 N  NE2 . GLN   B 1 91  ? -13.362 38.698  23.127  1.00 132.48 ? 97  GLN   B NE2 1 
ATOM   3049 N  N   . GLU   B 1 92  ? -16.526 33.559  24.702  1.00 98.30  ? 98  GLU   B N   1 
ATOM   3050 C  CA  . GLU   B 1 92  ? -16.959 33.290  26.064  1.00 97.58  ? 98  GLU   B CA  1 
ATOM   3051 C  C   . GLU   B 1 92  ? -16.882 31.811  26.398  1.00 99.75  ? 98  GLU   B C   1 
ATOM   3052 O  O   . GLU   B 1 92  ? -16.410 31.461  27.481  1.00 98.81  ? 98  GLU   B O   1 
ATOM   3053 C  CB  . GLU   B 1 92  ? -18.376 33.838  26.259  1.00 99.06  ? 98  GLU   B CB  1 
ATOM   3054 C  CG  . GLU   B 1 92  ? -18.570 35.243  25.687  1.00 110.82 ? 98  GLU   B CG  1 
ATOM   3055 C  CD  . GLU   B 1 92  ? -17.702 36.378  26.215  1.00 129.51 ? 98  GLU   B CD  1 
ATOM   3056 O  OE1 . GLU   B 1 92  ? -17.298 36.340  27.401  1.00 112.49 ? 98  GLU   B OE1 1 
ATOM   3057 O  OE2 . GLU   B 1 92  ? -17.470 37.337  25.444  1.00 126.23 ? 98  GLU   B OE2 1 
ATOM   3058 N  N   . LEU   B 1 93  ? -17.310 30.942  25.451  1.00 95.50  ? 99  LEU   B N   1 
ATOM   3059 C  CA  . LEU   B 1 93  ? -17.259 29.483  25.567  1.00 94.56  ? 99  LEU   B CA  1 
ATOM   3060 C  C   . LEU   B 1 93  ? -15.797 29.057  25.702  1.00 95.80  ? 99  LEU   B C   1 
ATOM   3061 O  O   . LEU   B 1 93  ? -15.513 28.103  26.422  1.00 95.36  ? 99  LEU   B O   1 
ATOM   3062 C  CB  . LEU   B 1 93  ? -17.907 28.827  24.333  1.00 94.84  ? 99  LEU   B CB  1 
ATOM   3063 C  CG  . LEU   B 1 93  ? -18.368 27.372  24.475  1.00 99.94  ? 99  LEU   B CG  1 
ATOM   3064 C  CD1 . LEU   B 1 93  ? -19.827 27.294  24.892  1.00 100.10 ? 99  LEU   B CD1 1 
ATOM   3065 C  CD2 . LEU   B 1 93  ? -18.204 26.633  23.172  1.00 102.82 ? 99  LEU   B CD2 1 
ATOM   3066 N  N   . ALA   B 1 94  ? -14.873 29.808  25.052  1.00 90.57  ? 100 ALA   B N   1 
ATOM   3067 C  CA  . ALA   B 1 94  ? -13.423 29.599  25.103  1.00 89.80  ? 100 ALA   B CA  1 
ATOM   3068 C  C   . ALA   B 1 94  ? -12.887 29.844  26.510  1.00 92.53  ? 100 ALA   B C   1 
ATOM   3069 O  O   . ALA   B 1 94  ? -12.009 29.110  26.963  1.00 92.57  ? 100 ALA   B O   1 
ATOM   3070 C  CB  . ALA   B 1 94  ? -12.722 30.525  24.120  1.00 90.52  ? 100 ALA   B CB  1 
ATOM   3071 N  N   . GLU   B 1 95  ? -13.415 30.875  27.199  1.00 87.48  ? 101 GLU   B N   1 
ATOM   3072 C  CA  . GLU   B 1 95  ? -13.019 31.235  28.561  1.00 86.29  ? 101 GLU   B CA  1 
ATOM   3073 C  C   . GLU   B 1 95  ? -13.396 30.143  29.571  1.00 86.55  ? 101 GLU   B C   1 
ATOM   3074 O  O   . GLU   B 1 95  ? -12.533 29.716  30.344  1.00 85.70  ? 101 GLU   B O   1 
ATOM   3075 C  CB  . GLU   B 1 95  ? -13.581 32.615  28.957  1.00 87.72  ? 101 GLU   B CB  1 
ATOM   3076 C  CG  . GLU   B 1 95  ? -12.718 33.787  28.508  1.00 97.93  ? 101 GLU   B CG  1 
ATOM   3077 C  CD  . GLU   B 1 95  ? -11.374 33.989  29.190  1.00 118.81 ? 101 GLU   B CD  1 
ATOM   3078 O  OE1 . GLU   B 1 95  ? -10.572 34.795  28.667  1.00 117.79 ? 101 GLU   B OE1 1 
ATOM   3079 O  OE2 . GLU   B 1 95  ? -11.121 33.362  30.246  1.00 110.68 ? 101 GLU   B OE2 1 
ATOM   3080 N  N   . VAL   B 1 96  ? -14.661 29.653  29.510  1.00 80.70  ? 102 VAL   B N   1 
ATOM   3081 C  CA  . VAL   B 1 96  ? -15.212 28.570  30.342  1.00 79.48  ? 102 VAL   B CA  1 
ATOM   3082 C  C   . VAL   B 1 96  ? -14.384 27.280  30.145  1.00 81.18  ? 102 VAL   B C   1 
ATOM   3083 O  O   . VAL   B 1 96  ? -14.097 26.585  31.120  1.00 81.36  ? 102 VAL   B O   1 
ATOM   3084 C  CB  . VAL   B 1 96  ? -16.727 28.331  30.065  1.00 83.22  ? 102 VAL   B CB  1 
ATOM   3085 C  CG1 . VAL   B 1 96  ? -17.320 27.322  31.044  1.00 83.13  ? 102 VAL   B CG1 1 
ATOM   3086 C  CG2 . VAL   B 1 96  ? -17.518 29.635  30.110  1.00 82.85  ? 102 VAL   B CG2 1 
ATOM   3087 N  N   . VAL   B 1 97  ? -13.982 26.987  28.893  1.00 75.30  ? 103 VAL   B N   1 
ATOM   3088 C  CA  . VAL   B 1 97  ? -13.155 25.824  28.547  1.00 74.23  ? 103 VAL   B CA  1 
ATOM   3089 C  C   . VAL   B 1 97  ? -11.704 26.027  29.049  1.00 78.37  ? 103 VAL   B C   1 
ATOM   3090 O  O   . VAL   B 1 97  ? -11.098 25.074  29.548  1.00 78.06  ? 103 VAL   B O   1 
ATOM   3091 C  CB  . VAL   B 1 97  ? -13.262 25.456  27.033  1.00 76.93  ? 103 VAL   B CB  1 
ATOM   3092 C  CG1 . VAL   B 1 97  ? -12.195 24.454  26.604  1.00 76.57  ? 103 VAL   B CG1 1 
ATOM   3093 C  CG2 . VAL   B 1 97  ? -14.650 24.927  26.696  1.00 76.36  ? 103 VAL   B CG2 1 
ATOM   3094 N  N   . SER   B 1 98  ? -11.173 27.273  28.964  1.00 74.93  ? 104 SER   B N   1 
ATOM   3095 C  CA  . SER   B 1 98  ? -9.822  27.609  29.446  1.00 74.80  ? 104 SER   B CA  1 
ATOM   3096 C  C   . SER   B 1 98  ? -9.753  27.545  30.976  1.00 77.78  ? 104 SER   B C   1 
ATOM   3097 O  O   . SER   B 1 98  ? -8.683  27.259  31.524  1.00 76.87  ? 104 SER   B O   1 
ATOM   3098 C  CB  . SER   B 1 98  ? -9.398  28.998  28.974  1.00 79.24  ? 104 SER   B CB  1 
ATOM   3099 O  OG  . SER   B 1 98  ? -8.025  29.244  29.242  1.00 87.74  ? 104 SER   B OG  1 
ATOM   3100 N  N   . ARG   B 1 99  ? -10.896 27.819  31.653  1.00 74.41  ? 105 ARG   B N   1 
ATOM   3101 C  CA  . ARG   B 1 99  ? -11.045 27.795  33.115  1.00 74.68  ? 105 ARG   B CA  1 
ATOM   3102 C  C   . ARG   B 1 99  ? -10.792 26.368  33.613  1.00 78.94  ? 105 ARG   B C   1 
ATOM   3103 O  O   . ARG   B 1 99  ? -9.866  26.141  34.403  1.00 78.41  ? 105 ARG   B O   1 
ATOM   3104 C  CB  . ARG   B 1 99  ? -12.465 28.259  33.511  1.00 74.69  ? 105 ARG   B CB  1 
ATOM   3105 C  CG  . ARG   B 1 99  ? -12.589 28.852  34.922  1.00 86.68  ? 105 ARG   B CG  1 
ATOM   3106 C  CD  . ARG   B 1 99  ? -12.221 30.332  35.020  1.00 93.54  ? 105 ARG   B CD  1 
ATOM   3107 N  NE  . ARG   B 1 99  ? -12.997 31.171  34.101  1.00 98.91  ? 105 ARG   B NE  1 
ATOM   3108 C  CZ  . ARG   B 1 99  ? -12.526 31.674  32.963  1.00 110.31 ? 105 ARG   B CZ  1 
ATOM   3109 N  NH1 . ARG   B 1 99  ? -11.268 31.452  32.599  1.00 94.50  ? 105 ARG   B NH1 1 
ATOM   3110 N  NH2 . ARG   B 1 99  ? -13.302 32.422  32.191  1.00 95.15  ? 105 ARG   B NH2 1 
ATOM   3111 N  N   . ALA   B 1 100 ? -11.581 25.407  33.074  1.00 75.25  ? 106 ALA   B N   1 
ATOM   3112 C  CA  . ALA   B 1 100 ? -11.530 23.974  33.359  1.00 74.35  ? 106 ALA   B CA  1 
ATOM   3113 C  C   . ALA   B 1 100 ? -10.143 23.361  33.099  1.00 77.67  ? 106 ALA   B C   1 
ATOM   3114 O  O   . ALA   B 1 100 ? -9.661  22.603  33.940  1.00 76.95  ? 106 ALA   B O   1 
ATOM   3115 C  CB  . ALA   B 1 100 ? -12.595 23.254  32.555  1.00 74.99  ? 106 ALA   B CB  1 
ATOM   3116 N  N   . VAL   B 1 101 ? -9.491  23.716  31.971  1.00 74.40  ? 107 VAL   B N   1 
ATOM   3117 C  CA  . VAL   B 1 101 ? -8.154  23.210  31.612  1.00 74.57  ? 107 VAL   B CA  1 
ATOM   3118 C  C   . VAL   B 1 101 ? -7.105  23.621  32.659  1.00 79.19  ? 107 VAL   B C   1 
ATOM   3119 O  O   . VAL   B 1 101 ? -6.352  22.764  33.130  1.00 78.58  ? 107 VAL   B O   1 
ATOM   3120 C  CB  . VAL   B 1 101 ? -7.744  23.574  30.158  1.00 78.23  ? 107 VAL   B CB  1 
ATOM   3121 C  CG1 . VAL   B 1 101 ? -6.262  23.312  29.912  1.00 77.95  ? 107 VAL   B CG1 1 
ATOM   3122 C  CG2 . VAL   B 1 101 ? -8.593  22.813  29.146  1.00 77.91  ? 107 VAL   B CG2 1 
ATOM   3123 N  N   . SER   B 1 102 ? -7.092  24.916  33.042  1.00 77.05  ? 108 SER   B N   1 
ATOM   3124 C  CA  . SER   B 1 102 ? -6.196  25.479  34.060  1.00 77.37  ? 108 SER   B CA  1 
ATOM   3125 C  C   . SER   B 1 102 ? -6.453  24.828  35.430  1.00 80.97  ? 108 SER   B C   1 
ATOM   3126 O  O   . SER   B 1 102 ? -5.500  24.584  36.176  1.00 80.08  ? 108 SER   B O   1 
ATOM   3127 C  CB  . SER   B 1 102 ? -6.367  26.994  34.147  1.00 81.34  ? 108 SER   B CB  1 
ATOM   3128 O  OG  . SER   B 1 102 ? -5.358  27.576  34.957  1.00 91.96  ? 108 SER   B OG  1 
ATOM   3129 N  N   . ASP   B 1 103 ? -7.739  24.515  35.730  1.00 77.66  ? 109 ASP   B N   1 
ATOM   3130 C  CA  . ASP   B 1 103 ? -8.175  23.830  36.952  1.00 77.79  ? 109 ASP   B CA  1 
ATOM   3131 C  C   . ASP   B 1 103 ? -7.635  22.386  37.020  1.00 81.48  ? 109 ASP   B C   1 
ATOM   3132 O  O   . ASP   B 1 103 ? -7.420  21.866  38.118  1.00 81.48  ? 109 ASP   B O   1 
ATOM   3133 C  CB  . ASP   B 1 103 ? -9.716  23.828  37.059  1.00 79.84  ? 109 ASP   B CB  1 
ATOM   3134 C  CG  . ASP   B 1 103 ? -10.361 25.110  37.579  1.00 93.17  ? 109 ASP   B CG  1 
ATOM   3135 O  OD1 . ASP   B 1 103 ? -9.620  26.014  38.037  1.00 94.35  ? 109 ASP   B OD1 1 
ATOM   3136 O  OD2 . ASP   B 1 103 ? -11.610 25.194  37.564  1.00 99.21  ? 109 ASP   B OD2 1 
ATOM   3137 N  N   . GLY   B 1 104 ? -7.416  21.776  35.850  1.00 77.00  ? 110 GLY   B N   1 
ATOM   3138 C  CA  . GLY   B 1 104 ? -6.907  20.414  35.696  1.00 76.18  ? 110 GLY   B CA  1 
ATOM   3139 C  C   . GLY   B 1 104 ? -7.960  19.413  35.250  1.00 78.54  ? 110 GLY   B C   1 
ATOM   3140 O  O   . GLY   B 1 104 ? -7.744  18.203  35.355  1.00 77.81  ? 110 GLY   B O   1 
ATOM   3141 N  N   . TYR   B 1 105 ? -9.107  19.921  34.742  1.00 74.07  ? 111 TYR   B N   1 
ATOM   3142 C  CA  . TYR   B 1 105 ? -10.269 19.157  34.275  1.00 73.54  ? 111 TYR   B CA  1 
ATOM   3143 C  C   . TYR   B 1 105 ? -10.277 18.870  32.750  1.00 75.71  ? 111 TYR   B C   1 
ATOM   3144 O  O   . TYR   B 1 105 ? -9.580  19.540  31.975  1.00 74.96  ? 111 TYR   B O   1 
ATOM   3145 C  CB  . TYR   B 1 105 ? -11.565 19.895  34.663  1.00 75.11  ? 111 TYR   B CB  1 
ATOM   3146 C  CG  . TYR   B 1 105 ? -11.982 19.723  36.107  1.00 78.34  ? 111 TYR   B CG  1 
ATOM   3147 C  CD1 . TYR   B 1 105 ? -11.359 20.443  37.126  1.00 80.56  ? 111 TYR   B CD1 1 
ATOM   3148 C  CD2 . TYR   B 1 105 ? -13.053 18.902  36.450  1.00 79.45  ? 111 TYR   B CD2 1 
ATOM   3149 C  CE1 . TYR   B 1 105 ? -11.754 20.303  38.456  1.00 81.62  ? 111 TYR   B CE1 1 
ATOM   3150 C  CE2 . TYR   B 1 105 ? -13.459 18.755  37.777  1.00 80.54  ? 111 TYR   B CE2 1 
ATOM   3151 C  CZ  . TYR   B 1 105 ? -12.807 19.461  38.777  1.00 89.57  ? 111 TYR   B CZ  1 
ATOM   3152 O  OH  . TYR   B 1 105 ? -13.202 19.320  40.087  1.00 91.84  ? 111 TYR   B OH  1 
ATOM   3153 N  N   . SER   B 1 106 ? -11.095 17.866  32.339  1.00 70.06  ? 112 SER   B N   1 
ATOM   3154 C  CA  . SER   B 1 106 ? -11.321 17.450  30.952  1.00 68.20  ? 112 SER   B CA  1 
ATOM   3155 C  C   . SER   B 1 106 ? -12.711 17.930  30.570  1.00 69.61  ? 112 SER   B C   1 
ATOM   3156 O  O   . SER   B 1 106 ? -13.703 17.469  31.134  1.00 68.44  ? 112 SER   B O   1 
ATOM   3157 C  CB  . SER   B 1 106 ? -11.200 15.934  30.804  1.00 71.13  ? 112 SER   B CB  1 
ATOM   3158 O  OG  . SER   B 1 106 ? -9.853  15.500  30.916  1.00 78.54  ? 112 SER   B OG  1 
ATOM   3159 N  N   . CYS   B 1 107 ? -12.784 18.909  29.656  1.00 65.81  ? 113 CYS   B N   1 
ATOM   3160 C  CA  . CYS   B 1 107 ? -14.052 19.513  29.265  1.00 65.29  ? 113 CYS   B CA  1 
ATOM   3161 C  C   . CYS   B 1 107 ? -14.817 18.708  28.219  1.00 66.52  ? 113 CYS   B C   1 
ATOM   3162 O  O   . CYS   B 1 107 ? -14.212 18.209  27.280  1.00 66.72  ? 113 CYS   B O   1 
ATOM   3163 C  CB  . CYS   B 1 107 ? -13.847 20.960  28.827  1.00 66.27  ? 113 CYS   B CB  1 
ATOM   3164 S  SG  . CYS   B 1 107 ? -15.329 21.983  28.986  1.00 70.64  ? 113 CYS   B SG  1 
ATOM   3165 N  N   . VAL   B 1 108 ? -16.151 18.598  28.392  1.00 60.30  ? 114 VAL   B N   1 
ATOM   3166 C  CA  . VAL   B 1 108 ? -17.095 17.879  27.533  1.00 59.32  ? 114 VAL   B CA  1 
ATOM   3167 C  C   . VAL   B 1 108 ? -18.280 18.806  27.206  1.00 62.08  ? 114 VAL   B C   1 
ATOM   3168 O  O   . VAL   B 1 108 ? -19.069 19.149  28.092  1.00 61.44  ? 114 VAL   B O   1 
ATOM   3169 C  CB  . VAL   B 1 108 ? -17.535 16.509  28.139  1.00 62.99  ? 114 VAL   B CB  1 
ATOM   3170 C  CG1 . VAL   B 1 108 ? -18.686 15.878  27.357  1.00 62.87  ? 114 VAL   B CG1 1 
ATOM   3171 C  CG2 . VAL   B 1 108 ? -16.361 15.545  28.221  1.00 62.64  ? 114 VAL   B CG2 1 
ATOM   3172 N  N   . THR   B 1 109 ? -18.397 19.203  25.926  1.00 57.65  ? 115 THR   B N   1 
ATOM   3173 C  CA  . THR   B 1 109 ? -19.428 20.125  25.445  1.00 56.83  ? 115 THR   B CA  1 
ATOM   3174 C  C   . THR   B 1 109 ? -20.516 19.421  24.625  1.00 59.73  ? 115 THR   B C   1 
ATOM   3175 O  O   . THR   B 1 109 ? -20.211 18.804  23.601  1.00 60.18  ? 115 THR   B O   1 
ATOM   3176 C  CB  . THR   B 1 109 ? -18.762 21.285  24.669  1.00 68.08  ? 115 THR   B CB  1 
ATOM   3177 O  OG1 . THR   B 1 109 ? -17.415 21.494  25.127  1.00 65.86  ? 115 THR   B OG1 1 
ATOM   3178 C  CG2 . THR   B 1 109 ? -19.559 22.571  24.750  1.00 68.21  ? 115 THR   B CG2 1 
ATOM   3179 N  N   . LEU   B 1 110 ? -21.780 19.522  25.065  1.00 54.77  ? 116 LEU   B N   1 
ATOM   3180 C  CA  . LEU   B 1 110 ? -22.914 18.918  24.367  1.00 55.07  ? 116 LEU   B CA  1 
ATOM   3181 C  C   . LEU   B 1 110 ? -23.616 19.928  23.445  1.00 59.29  ? 116 LEU   B C   1 
ATOM   3182 O  O   . LEU   B 1 110 ? -24.069 20.979  23.913  1.00 58.20  ? 116 LEU   B O   1 
ATOM   3183 C  CB  . LEU   B 1 110 ? -23.931 18.297  25.348  1.00 55.31  ? 116 LEU   B CB  1 
ATOM   3184 C  CG  . LEU   B 1 110 ? -23.408 17.479  26.541  1.00 60.43  ? 116 LEU   B CG  1 
ATOM   3185 C  CD1 . LEU   B 1 110 ? -24.544 17.156  27.498  1.00 60.59  ? 116 LEU   B CD1 1 
ATOM   3186 C  CD2 . LEU   B 1 110 ? -22.698 16.197  26.086  1.00 62.61  ? 116 LEU   B CD2 1 
ATOM   3187 N  N   . GLY   B 1 111 ? -23.694 19.594  22.151  1.00 55.77  ? 117 GLY   B N   1 
ATOM   3188 C  CA  . GLY   B 1 111 ? -24.323 20.434  21.141  1.00 55.90  ? 117 GLY   B CA  1 
ATOM   3189 C  C   . GLY   B 1 111 ? -25.799 20.141  20.904  1.00 62.90  ? 117 GLY   B C   1 
ATOM   3190 O  O   . GLY   B 1 111 ? -26.333 19.178  21.464  1.00 62.09  ? 117 GLY   B O   1 
ATOM   3191 N  N   . GLY   B 1 112 ? -26.476 20.942  20.063  1.00 61.96  ? 118 GLY   B N   1 
ATOM   3192 C  CA  . GLY   B 1 112 ? -25.917 22.080  19.333  1.00 62.34  ? 118 GLY   B CA  1 
ATOM   3193 C  C   . GLY   B 1 112 ? -25.181 21.694  18.061  1.00 67.27  ? 118 GLY   B C   1 
ATOM   3194 O  O   . GLY   B 1 112 ? -24.888 20.513  17.852  1.00 67.30  ? 118 GLY   B O   1 
ATOM   3195 N  N   . ASP   B 1 113 ? -24.869 22.687  17.201  1.00 63.49  ? 119 ASP   B N   1 
ATOM   3196 C  CA  . ASP   B 1 113 ? -24.142 22.438  15.955  1.00 63.08  ? 119 ASP   B CA  1 
ATOM   3197 C  C   . ASP   B 1 113 ? -22.628 22.624  16.129  1.00 66.62  ? 119 ASP   B C   1 
ATOM   3198 O  O   . ASP   B 1 113 ? -22.201 23.159  17.150  1.00 65.99  ? 119 ASP   B O   1 
ATOM   3199 C  CB  . ASP   B 1 113 ? -24.713 23.250  14.783  1.00 64.97  ? 119 ASP   B CB  1 
ATOM   3200 C  CG  . ASP   B 1 113 ? -24.551 24.743  14.913  1.00 73.53  ? 119 ASP   B CG  1 
ATOM   3201 O  OD1 . ASP   B 1 113 ? -23.440 25.238  14.651  1.00 72.80  ? 119 ASP   B OD1 1 
ATOM   3202 O  OD2 . ASP   B 1 113 ? -25.547 25.419  15.241  1.00 81.23  ? 119 ASP   B OD2 1 
ATOM   3203 N  N   . HIS   B 1 114 ? -21.824 22.183  15.136  1.00 63.61  ? 120 HIS   B N   1 
ATOM   3204 C  CA  . HIS   B 1 114 ? -20.357 22.183  15.172  1.00 64.04  ? 120 HIS   B CA  1 
ATOM   3205 C  C   . HIS   B 1 114 ? -19.672 23.566  15.154  1.00 67.58  ? 120 HIS   B C   1 
ATOM   3206 O  O   . HIS   B 1 114 ? -18.439 23.613  15.211  1.00 65.75  ? 120 HIS   B O   1 
ATOM   3207 C  CB  . HIS   B 1 114 ? -19.777 21.290  14.054  1.00 65.27  ? 120 HIS   B CB  1 
ATOM   3208 C  CG  . HIS   B 1 114 ? -18.635 20.425  14.504  1.00 69.04  ? 120 HIS   B CG  1 
ATOM   3209 N  ND1 . HIS   B 1 114 ? -18.479 19.137  14.028  1.00 71.07  ? 120 HIS   B ND1 1 
ATOM   3210 C  CD2 . HIS   B 1 114 ? -17.648 20.677  15.398  1.00 71.17  ? 120 HIS   B CD2 1 
ATOM   3211 C  CE1 . HIS   B 1 114 ? -17.400 18.658  14.625  1.00 70.61  ? 120 HIS   B CE1 1 
ATOM   3212 N  NE2 . HIS   B 1 114 ? -16.871 19.547  15.462  1.00 71.05  ? 120 HIS   B NE2 1 
ATOM   3213 N  N   . SER   B 1 115 ? -20.436 24.681  15.119  1.00 66.58  ? 121 SER   B N   1 
ATOM   3214 C  CA  . SER   B 1 115 ? -19.842 26.032  15.162  1.00 67.41  ? 121 SER   B CA  1 
ATOM   3215 C  C   . SER   B 1 115 ? -19.111 26.314  16.490  1.00 72.10  ? 121 SER   B C   1 
ATOM   3216 O  O   . SER   B 1 115 ? -18.112 27.038  16.479  1.00 72.31  ? 121 SER   B O   1 
ATOM   3217 C  CB  . SER   B 1 115 ? -20.889 27.110  14.898  1.00 71.71  ? 121 SER   B CB  1 
ATOM   3218 O  OG  . SER   B 1 115 ? -21.932 27.101  15.859  1.00 80.44  ? 121 SER   B OG  1 
ATOM   3219 N  N   . LEU   B 1 116 ? -19.563 25.676  17.610  1.00 68.07  ? 122 LEU   B N   1 
ATOM   3220 C  CA  . LEU   B 1 116 ? -18.999 25.816  18.964  1.00 67.43  ? 122 LEU   B CA  1 
ATOM   3221 C  C   . LEU   B 1 116 ? -17.524 25.373  19.107  1.00 70.91  ? 122 LEU   B C   1 
ATOM   3222 O  O   . LEU   B 1 116 ? -16.916 25.631  20.147  1.00 70.89  ? 122 LEU   B O   1 
ATOM   3223 C  CB  . LEU   B 1 116 ? -19.881 25.117  20.025  1.00 67.49  ? 122 LEU   B CB  1 
ATOM   3224 C  CG  . LEU   B 1 116 ? -20.183 23.609  19.888  1.00 72.74  ? 122 LEU   B CG  1 
ATOM   3225 C  CD1 . LEU   B 1 116 ? -19.223 22.767  20.732  1.00 72.79  ? 122 LEU   B CD1 1 
ATOM   3226 C  CD2 . LEU   B 1 116 ? -21.605 23.304  20.338  1.00 76.00  ? 122 LEU   B CD2 1 
ATOM   3227 N  N   . ALA   B 1 117 ? -16.959 24.721  18.080  1.00 66.96  ? 123 ALA   B N   1 
ATOM   3228 C  CA  . ALA   B 1 117 ? -15.586 24.212  18.077  1.00 66.31  ? 123 ALA   B CA  1 
ATOM   3229 C  C   . ALA   B 1 117 ? -14.494 25.284  18.031  1.00 68.60  ? 123 ALA   B C   1 
ATOM   3230 O  O   . ALA   B 1 117 ? -13.360 25.008  18.422  1.00 66.83  ? 123 ALA   B O   1 
ATOM   3231 C  CB  . ALA   B 1 117 ? -15.404 23.225  16.938  1.00 67.18  ? 123 ALA   B CB  1 
ATOM   3232 N  N   . ILE   B 1 118 ? -14.819 26.491  17.536  1.00 66.47  ? 124 ILE   B N   1 
ATOM   3233 C  CA  . ILE   B 1 118 ? -13.866 27.613  17.453  1.00 66.34  ? 124 ILE   B CA  1 
ATOM   3234 C  C   . ILE   B 1 118 ? -13.421 28.005  18.876  1.00 68.19  ? 124 ILE   B C   1 
ATOM   3235 O  O   . ILE   B 1 118 ? -12.226 28.153  19.124  1.00 66.87  ? 124 ILE   B O   1 
ATOM   3236 C  CB  . ILE   B 1 118 ? -14.432 28.831  16.654  1.00 69.93  ? 124 ILE   B CB  1 
ATOM   3237 C  CG1 . ILE   B 1 118 ? -15.146 28.391  15.351  1.00 70.67  ? 124 ILE   B CG1 1 
ATOM   3238 C  CG2 . ILE   B 1 118 ? -13.322 29.860  16.363  1.00 71.12  ? 124 ILE   B CG2 1 
ATOM   3239 C  CD1 . ILE   B 1 118 ? -16.272 29.326  14.854  1.00 79.62  ? 124 ILE   B CD1 1 
ATOM   3240 N  N   . GLY   B 1 119 ? -14.391 28.118  19.784  1.00 64.79  ? 125 GLY   B N   1 
ATOM   3241 C  CA  . GLY   B 1 119 ? -14.167 28.444  21.188  1.00 65.07  ? 125 GLY   B CA  1 
ATOM   3242 C  C   . GLY   B 1 119 ? -13.383 27.390  21.945  1.00 68.58  ? 125 GLY   B C   1 
ATOM   3243 O  O   . GLY   B 1 119 ? -12.298 27.688  22.457  1.00 67.94  ? 125 GLY   B O   1 
ATOM   3244 N  N   . THR   B 1 120 ? -13.913 26.137  21.979  1.00 64.69  ? 126 THR   B N   1 
ATOM   3245 C  CA  . THR   B 1 120 ? -13.329 24.983  22.687  1.00 64.12  ? 126 THR   B CA  1 
ATOM   3246 C  C   . THR   B 1 120 ? -11.850 24.740  22.336  1.00 67.94  ? 126 THR   B C   1 
ATOM   3247 O  O   . THR   B 1 120 ? -11.050 24.489  23.236  1.00 67.41  ? 126 THR   B O   1 
ATOM   3248 C  CB  . THR   B 1 120 ? -14.173 23.703  22.499  1.00 74.35  ? 126 THR   B CB  1 
ATOM   3249 O  OG1 . THR   B 1 120 ? -14.020 23.205  21.170  1.00 75.00  ? 126 THR   B OG1 1 
ATOM   3250 C  CG2 . THR   B 1 120 ? -15.649 23.894  22.836  1.00 72.63  ? 126 THR   B CG2 1 
ATOM   3251 N  N   . ILE   B 1 121 ? -11.482 24.847  21.045  1.00 64.10  ? 127 ILE   B N   1 
ATOM   3252 C  CA  . ILE   B 1 121 ? -10.096 24.633  20.614  1.00 63.55  ? 127 ILE   B CA  1 
ATOM   3253 C  C   . ILE   B 1 121 ? -9.216  25.856  20.987  1.00 69.55  ? 127 ILE   B C   1 
ATOM   3254 O  O   . ILE   B 1 121 ? -8.056  25.674  21.375  1.00 68.17  ? 127 ILE   B O   1 
ATOM   3255 C  CB  . ILE   B 1 121 ? -10.009 24.198  19.114  1.00 65.76  ? 127 ILE   B CB  1 
ATOM   3256 C  CG1 . ILE   B 1 121 ? -10.776 22.855  18.904  1.00 65.60  ? 127 ILE   B CG1 1 
ATOM   3257 C  CG2 . ILE   B 1 121 ? -8.544  24.053  18.646  1.00 65.71  ? 127 ILE   B CG2 1 
ATOM   3258 C  CD1 . ILE   B 1 121 ? -11.295 22.571  17.525  1.00 68.96  ? 127 ILE   B CD1 1 
ATOM   3259 N  N   . SER   B 1 122 ? -9.771  27.084  20.909  1.00 69.38  ? 128 SER   B N   1 
ATOM   3260 C  CA  . SER   B 1 122 ? -9.024  28.302  21.257  1.00 70.55  ? 128 SER   B CA  1 
ATOM   3261 C  C   . SER   B 1 122 ? -8.738  28.393  22.763  1.00 76.41  ? 128 SER   B C   1 
ATOM   3262 O  O   . SER   B 1 122 ? -7.590  28.641  23.151  1.00 75.87  ? 128 SER   B O   1 
ATOM   3263 C  CB  . SER   B 1 122 ? -9.732  29.550  20.743  1.00 74.95  ? 128 SER   B CB  1 
ATOM   3264 O  OG  . SER   B 1 122 ? -9.524  29.695  19.347  1.00 85.93  ? 128 SER   B OG  1 
ATOM   3265 N  N   . GLY   B 1 123 ? -9.768  28.142  23.580  1.00 74.10  ? 129 GLY   B N   1 
ATOM   3266 C  CA  . GLY   B 1 123 ? -9.677  28.127  25.037  1.00 74.24  ? 129 GLY   B CA  1 
ATOM   3267 C  C   . GLY   B 1 123 ? -8.711  27.082  25.559  1.00 79.23  ? 129 GLY   B C   1 
ATOM   3268 O  O   . GLY   B 1 123 ? -7.946  27.350  26.489  1.00 79.56  ? 129 GLY   B O   1 
ATOM   3269 N  N   . HIS   B 1 124 ? -8.727  25.893  24.938  1.00 75.57  ? 130 HIS   B N   1 
ATOM   3270 C  CA  . HIS   B 1 124 ? -7.867  24.748  25.233  1.00 75.78  ? 130 HIS   B CA  1 
ATOM   3271 C  C   . HIS   B 1 124 ? -6.386  25.109  24.980  1.00 78.70  ? 130 HIS   B C   1 
ATOM   3272 O  O   . HIS   B 1 124 ? -5.526  24.802  25.813  1.00 77.44  ? 130 HIS   B O   1 
ATOM   3273 C  CB  . HIS   B 1 124 ? -8.308  23.572  24.332  1.00 77.17  ? 130 HIS   B CB  1 
ATOM   3274 C  CG  . HIS   B 1 124 ? -7.771  22.224  24.692  1.00 80.99  ? 130 HIS   B CG  1 
ATOM   3275 N  ND1 . HIS   B 1 124 ? -8.170  21.095  24.004  1.00 82.94  ? 130 HIS   B ND1 1 
ATOM   3276 C  CD2 . HIS   B 1 124 ? -6.865  21.864  25.631  1.00 83.06  ? 130 HIS   B CD2 1 
ATOM   3277 C  CE1 . HIS   B 1 124 ? -7.500  20.091  24.544  1.00 82.55  ? 130 HIS   B CE1 1 
ATOM   3278 N  NE2 . HIS   B 1 124 ? -6.698  20.508  25.522  1.00 82.88  ? 130 HIS   B NE2 1 
ATOM   3279 N  N   . ALA   B 1 125 ? -6.109  25.791  23.844  1.00 75.72  ? 131 ALA   B N   1 
ATOM   3280 C  CA  . ALA   B 1 125 ? -4.778  26.242  23.418  1.00 75.52  ? 131 ALA   B CA  1 
ATOM   3281 C  C   . ALA   B 1 125 ? -4.183  27.314  24.348  1.00 79.13  ? 131 ALA   B C   1 
ATOM   3282 O  O   . ALA   B 1 125 ? -2.952  27.436  24.414  1.00 78.30  ? 131 ALA   B O   1 
ATOM   3283 C  CB  . ALA   B 1 125 ? -4.839  26.763  21.994  1.00 76.27  ? 131 ALA   B CB  1 
ATOM   3284 N  N   . ARG   B 1 126 ? -5.055  28.088  25.056  1.00 75.43  ? 132 ARG   B N   1 
ATOM   3285 C  CA  . ARG   B 1 126 ? -4.658  29.115  26.030  1.00 75.34  ? 132 ARG   B CA  1 
ATOM   3286 C  C   . ARG   B 1 126 ? -3.933  28.440  27.202  1.00 79.90  ? 132 ARG   B C   1 
ATOM   3287 O  O   . ARG   B 1 126 ? -2.705  28.509  27.270  1.00 79.17  ? 132 ARG   B O   1 
ATOM   3288 C  CB  . ARG   B 1 126 ? -5.884  29.887  26.565  1.00 74.71  ? 132 ARG   B CB  1 
ATOM   3289 C  CG  . ARG   B 1 126 ? -6.364  31.037  25.696  1.00 81.97  ? 132 ARG   B CG  1 
ATOM   3290 C  CD  . ARG   B 1 126 ? -7.578  31.701  26.322  1.00 83.48  ? 132 ARG   B CD  1 
ATOM   3291 N  NE  . ARG   B 1 126 ? -8.293  32.553  25.370  1.00 86.88  ? 132 ARG   B NE  1 
ATOM   3292 C  CZ  . ARG   B 1 126 ? -9.602  32.789  25.409  1.00 98.89  ? 132 ARG   B CZ  1 
ATOM   3293 N  NH1 . ARG   B 1 126 ? -10.357 32.234  26.348  1.00 84.17  ? 132 ARG   B NH1 1 
ATOM   3294 N  NH2 . ARG   B 1 126 ? -10.168 33.573  24.501  1.00 85.53  ? 132 ARG   B NH2 1 
ATOM   3295 N  N   . HIS   B 1 127 ? -4.642  27.530  27.898  1.00 77.05  ? 133 HIS   B N   1 
ATOM   3296 C  C   . HIS   B 1 127 ? -2.230  25.437  28.211  1.00 89.47  ? 133 HIS   B C   1 
ATOM   3297 O  O   . HIS   B 1 127 ? -3.062  25.601  29.103  1.00 89.22  ? 133 HIS   B O   1 
ATOM   3298 N  N   . CYS   B 1 128 ? -2.452  24.661  27.141  1.00 85.40  ? 134 CYS   B N   1 
ATOM   3299 C  CA  . CYS   B 1 128 ? -1.341  24.004  26.452  1.00 84.63  ? 134 CYS   B CA  1 
ATOM   3300 C  C   . CYS   B 1 128 ? -1.249  24.427  24.975  1.00 86.83  ? 134 CYS   B C   1 
ATOM   3301 O  O   . CYS   B 1 128 ? -2.156  24.120  24.193  1.00 86.67  ? 134 CYS   B O   1 
ATOM   3302 C  CB  . CYS   B 1 128 ? -1.409  22.484  26.596  1.00 84.96  ? 134 CYS   B CB  1 
ATOM   3303 S  SG  . CYS   B 1 128 ? -1.677  21.895  28.292  1.00 88.84  ? 134 CYS   B SG  1 
ATOM   3304 N  N   . PRO   B 1 129 ? -0.158  25.119  24.563  1.00 81.33  ? 135 PRO   B N   1 
ATOM   3305 C  CA  . PRO   B 1 129 ? -0.040  25.506  23.144  1.00 80.00  ? 135 PRO   B CA  1 
ATOM   3306 C  C   . PRO   B 1 129 ? 0.415   24.364  22.218  1.00 79.35  ? 135 PRO   B C   1 
ATOM   3307 O  O   . PRO   B 1 129 ? 0.306   24.498  20.994  1.00 79.17  ? 135 PRO   B O   1 
ATOM   3308 C  CB  . PRO   B 1 129 ? 0.968   26.659  23.177  1.00 81.95  ? 135 PRO   B CB  1 
ATOM   3309 C  CG  . PRO   B 1 129 ? 1.822   26.381  24.370  1.00 86.63  ? 135 PRO   B CG  1 
ATOM   3310 C  CD  . PRO   B 1 129 ? 1.015   25.565  25.348  1.00 82.40  ? 135 PRO   B CD  1 
ATOM   3311 N  N   . ASP   B 1 130 ? 0.930   23.251  22.796  1.00 71.19  ? 136 ASP   B N   1 
ATOM   3312 C  CA  . ASP   B 1 130 ? 1.421   22.091  22.051  1.00 68.82  ? 136 ASP   B CA  1 
ATOM   3313 C  C   . ASP   B 1 130 ? 0.360   20.982  21.923  1.00 69.41  ? 136 ASP   B C   1 
ATOM   3314 O  O   . ASP   B 1 130 ? 0.702   19.809  21.790  1.00 69.10  ? 136 ASP   B O   1 
ATOM   3315 C  CB  . ASP   B 1 130 ? 2.734   21.570  22.672  1.00 70.28  ? 136 ASP   B CB  1 
ATOM   3316 C  CG  . ASP   B 1 130 ? 3.564   20.650  21.786  1.00 76.97  ? 136 ASP   B CG  1 
ATOM   3317 O  OD1 . ASP   B 1 130 ? 3.434   20.740  20.542  1.00 76.66  ? 136 ASP   B OD1 1 
ATOM   3318 O  OD2 . ASP   B 1 130 ? 4.342   19.840  22.338  1.00 81.72  ? 136 ASP   B OD2 1 
ATOM   3319 N  N   . LEU   B 1 131 ? -0.928  21.358  21.916  1.00 62.70  ? 137 LEU   B N   1 
ATOM   3320 C  CA  . LEU   B 1 131 ? -2.027  20.409  21.777  1.00 61.40  ? 137 LEU   B CA  1 
ATOM   3321 C  C   . LEU   B 1 131 ? -2.148  19.867  20.329  1.00 63.16  ? 137 LEU   B C   1 
ATOM   3322 O  O   . LEU   B 1 131 ? -1.483  20.375  19.421  1.00 62.27  ? 137 LEU   B O   1 
ATOM   3323 C  CB  . LEU   B 1 131 ? -3.355  21.043  22.277  1.00 61.33  ? 137 LEU   B CB  1 
ATOM   3324 C  CG  . LEU   B 1 131 ? -4.184  21.893  21.305  1.00 65.62  ? 137 LEU   B CG  1 
ATOM   3325 C  CD1 . LEU   B 1 131 ? -5.601  22.052  21.806  1.00 65.41  ? 137 LEU   B CD1 1 
ATOM   3326 C  CD2 . LEU   B 1 131 ? -3.564  23.252  21.074  1.00 68.49  ? 137 LEU   B CD2 1 
ATOM   3327 N  N   . CYS   B 1 132 ? -2.994  18.830  20.133  1.00 57.76  ? 138 CYS   B N   1 
ATOM   3328 C  CA  . CYS   B 1 132 ? -3.283  18.222  18.831  1.00 55.88  ? 138 CYS   B CA  1 
ATOM   3329 C  C   . CYS   B 1 132 ? -4.756  17.823  18.774  1.00 58.04  ? 138 CYS   B C   1 
ATOM   3330 O  O   . CYS   B 1 132 ? -5.298  17.358  19.781  1.00 57.77  ? 138 CYS   B O   1 
ATOM   3331 C  CB  . CYS   B 1 132 ? -2.353  17.048  18.545  1.00 55.70  ? 138 CYS   B CB  1 
ATOM   3332 S  SG  . CYS   B 1 132 ? -2.514  15.670  19.710  1.00 59.13  ? 138 CYS   B SG  1 
ATOM   3333 N  N   . VAL   B 1 133 ? -5.413  18.045  17.609  1.00 53.19  ? 139 VAL   B N   1 
ATOM   3334 C  CA  . VAL   B 1 133 ? -6.855  17.817  17.394  1.00 52.12  ? 139 VAL   B CA  1 
ATOM   3335 C  C   . VAL   B 1 133 ? -7.146  16.535  16.569  1.00 53.87  ? 139 VAL   B C   1 
ATOM   3336 O  O   . VAL   B 1 133 ? -6.394  16.205  15.645  1.00 52.26  ? 139 VAL   B O   1 
ATOM   3337 C  CB  . VAL   B 1 133 ? -7.559  19.068  16.761  1.00 55.93  ? 139 VAL   B CB  1 
ATOM   3338 C  CG1 . VAL   B 1 133 ? -9.083  18.923  16.743  1.00 55.40  ? 139 VAL   B CG1 1 
ATOM   3339 C  CG2 . VAL   B 1 133 ? -7.167  20.365  17.471  1.00 55.95  ? 139 VAL   B CG2 1 
ATOM   3340 N  N   . VAL   B 1 134 ? -8.266  15.848  16.911  1.00 48.82  ? 140 VAL   B N   1 
ATOM   3341 C  CA  . VAL   B 1 134 ? -8.821  14.680  16.215  1.00 47.48  ? 140 VAL   B CA  1 
ATOM   3342 C  C   . VAL   B 1 134 ? -10.257 15.070  15.862  1.00 48.89  ? 140 VAL   B C   1 
ATOM   3343 O  O   . VAL   B 1 134 ? -11.105 15.220  16.745  1.00 46.95  ? 140 VAL   B O   1 
ATOM   3344 C  CB  . VAL   B 1 134 ? -8.732  13.345  17.013  1.00 51.02  ? 140 VAL   B CB  1 
ATOM   3345 C  CG1 . VAL   B 1 134 ? -9.427  12.209  16.258  1.00 50.60  ? 140 VAL   B CG1 1 
ATOM   3346 C  CG2 . VAL   B 1 134 ? -7.280  12.976  17.314  1.00 50.59  ? 140 VAL   B CG2 1 
ATOM   3347 N  N   . TRP   B 1 135 ? -10.508 15.289  14.561  1.00 46.20  ? 141 TRP   B N   1 
ATOM   3348 C  CA  . TRP   B 1 135 ? -11.797 15.734  14.044  1.00 46.28  ? 141 TRP   B CA  1 
ATOM   3349 C  C   . TRP   B 1 135 ? -12.561 14.565  13.399  1.00 50.08  ? 141 TRP   B C   1 
ATOM   3350 O  O   . TRP   B 1 135 ? -12.235 14.151  12.287  1.00 50.56  ? 141 TRP   B O   1 
ATOM   3351 C  CB  . TRP   B 1 135 ? -11.566 16.895  13.049  1.00 45.54  ? 141 TRP   B CB  1 
ATOM   3352 C  CG  . TRP   B 1 135 ? -12.780 17.726  12.793  1.00 46.92  ? 141 TRP   B CG  1 
ATOM   3353 C  CD1 . TRP   B 1 135 ? -13.850 17.399  12.016  1.00 49.84  ? 141 TRP   B CD1 1 
ATOM   3354 C  CD2 . TRP   B 1 135 ? -13.038 19.038  13.301  1.00 47.36  ? 141 TRP   B CD2 1 
ATOM   3355 N  NE1 . TRP   B 1 135 ? -14.788 18.399  12.058  1.00 49.46  ? 141 TRP   B NE1 1 
ATOM   3356 C  CE2 . TRP   B 1 135 ? -14.309 19.427  12.827  1.00 51.24  ? 141 TRP   B CE2 1 
ATOM   3357 C  CE3 . TRP   B 1 135 ? -12.341 19.904  14.165  1.00 48.86  ? 141 TRP   B CE3 1 
ATOM   3358 C  CZ2 . TRP   B 1 135 ? -14.880 20.664  13.150  1.00 50.87  ? 141 TRP   B CZ2 1 
ATOM   3359 C  CZ3 . TRP   B 1 135 ? -12.910 21.127  14.486  1.00 50.43  ? 141 TRP   B CZ3 1 
ATOM   3360 C  CH2 . TRP   B 1 135 ? -14.171 21.488  13.996  1.00 50.94  ? 141 TRP   B CH2 1 
ATOM   3361 N  N   . VAL   B 1 136 ? -13.569 14.033  14.109  1.00 45.10  ? 142 VAL   B N   1 
ATOM   3362 C  CA  . VAL   B 1 136 ? -14.371 12.896  13.663  1.00 43.29  ? 142 VAL   B CA  1 
ATOM   3363 C  C   . VAL   B 1 136 ? -15.676 13.432  13.122  1.00 45.84  ? 142 VAL   B C   1 
ATOM   3364 O  O   . VAL   B 1 136 ? -16.502 13.944  13.878  1.00 45.47  ? 142 VAL   B O   1 
ATOM   3365 C  CB  . VAL   B 1 136 ? -14.538 11.820  14.776  1.00 45.66  ? 142 VAL   B CB  1 
ATOM   3366 C  CG1 . VAL   B 1 136 ? -15.300 10.609  14.258  1.00 45.10  ? 142 VAL   B CG1 1 
ATOM   3367 C  CG2 . VAL   B 1 136 ? -13.184 11.394  15.339  1.00 44.82  ? 142 VAL   B CG2 1 
ATOM   3368 N  N   . ASP   B 1 137 ? -15.843 13.356  11.785  1.00 42.27  ? 143 ASP   B N   1 
ATOM   3369 C  CA  . ASP   B 1 137 ? -16.973 13.954  11.062  1.00 41.42  ? 143 ASP   B CA  1 
ATOM   3370 C  C   . ASP   B 1 137 ? -17.084 13.366  9.655   1.00 42.87  ? 143 ASP   B C   1 
ATOM   3371 O  O   . ASP   B 1 137 ? -16.073 12.986  9.059   1.00 42.13  ? 143 ASP   B O   1 
ATOM   3372 C  CB  . ASP   B 1 137 ? -16.648 15.460  10.872  1.00 42.74  ? 143 ASP   B CB  1 
ATOM   3373 C  CG  . ASP   B 1 137 ? -17.744 16.507  10.960  1.00 47.74  ? 143 ASP   B CG  1 
ATOM   3374 O  OD1 . ASP   B 1 137 ? -18.820 16.330  10.302  1.00 41.10  ? 143 ASP   B OD1 1 
ATOM   3375 O  OD2 . ASP   B 1 137 ? -17.491 17.568  11.586  1.00 60.41  ? 143 ASP   B OD2 1 
ATOM   3376 N  N   . ALA   B 1 138 ? -18.297 13.393  9.101   1.00 39.98  ? 144 ALA   B N   1 
ATOM   3377 C  CA  . ALA   B 1 138 ? -18.592 13.058  7.705   1.00 40.38  ? 144 ALA   B CA  1 
ATOM   3378 C  C   . ALA   B 1 138 ? -18.106 14.244  6.865   1.00 47.19  ? 144 ALA   B C   1 
ATOM   3379 O  O   . ALA   B 1 138 ? -17.806 14.080  5.679   1.00 47.68  ? 144 ALA   B O   1 
ATOM   3380 C  CB  . ALA   B 1 138 ? -20.091 12.903  7.520   1.00 41.01  ? 144 ALA   B CB  1 
ATOM   3381 N  N   . HIS   B 1 139 ? -18.001 15.438  7.509   1.00 44.44  ? 145 HIS   B N   1 
ATOM   3382 C  CA  . HIS   B 1 139 ? -17.623 16.722  6.906   1.00 43.94  ? 145 HIS   B CA  1 
ATOM   3383 C  C   . HIS   B 1 139 ? -16.255 17.263  7.379   1.00 51.67  ? 145 HIS   B C   1 
ATOM   3384 O  O   . HIS   B 1 139 ? -15.804 16.932  8.472   1.00 51.64  ? 145 HIS   B O   1 
ATOM   3385 C  CB  . HIS   B 1 139 ? -18.753 17.718  7.148   1.00 42.85  ? 145 HIS   B CB  1 
ATOM   3386 C  CG  . HIS   B 1 139 ? -20.090 17.180  6.735   1.00 44.79  ? 145 HIS   B CG  1 
ATOM   3387 N  ND1 . HIS   B 1 139 ? -20.990 16.690  7.662   1.00 45.67  ? 145 HIS   B ND1 1 
ATOM   3388 C  CD2 . HIS   B 1 139 ? -20.613 17.026  5.499   1.00 45.52  ? 145 HIS   B CD2 1 
ATOM   3389 C  CE1 . HIS   B 1 139 ? -22.032 16.259  6.972   1.00 44.70  ? 145 HIS   B CE1 1 
ATOM   3390 N  NE2 . HIS   B 1 139 ? -21.857 16.444  5.664   1.00 45.29  ? 145 HIS   B NE2 1 
ATOM   3391 N  N   . ALA   B 1 140 ? -15.558 18.042  6.532   1.00 50.25  ? 146 ALA   B N   1 
ATOM   3392 C  CA  . ALA   B 1 140 ? -14.233 18.571  6.894   1.00 50.49  ? 146 ALA   B CA  1 
ATOM   3393 C  C   . ALA   B 1 140 ? -14.293 19.931  7.606   1.00 55.18  ? 146 ALA   B C   1 
ATOM   3394 O  O   . ALA   B 1 140 ? -13.273 20.396  8.121   1.00 53.29  ? 146 ALA   B O   1 
ATOM   3395 C  CB  . ALA   B 1 140 ? -13.333 18.650  5.677   1.00 51.60  ? 146 ALA   B CB  1 
ATOM   3396 N  N   . ASP   B 1 141 ? -15.483 20.569  7.619   1.00 54.07  ? 147 ASP   B N   1 
ATOM   3397 C  CA  . ASP   B 1 141 ? -15.751 21.867  8.259   1.00 55.22  ? 147 ASP   B CA  1 
ATOM   3398 C  C   . ASP   B 1 141 ? -14.561 22.877  8.131   1.00 59.23  ? 147 ASP   B C   1 
ATOM   3399 O  O   . ASP   B 1 141 ? -14.250 23.592  9.091   1.00 60.19  ? 147 ASP   B O   1 
ATOM   3400 C  CB  . ASP   B 1 141 ? -16.152 21.639  9.740   1.00 57.46  ? 147 ASP   B CB  1 
ATOM   3401 C  CG  . ASP   B 1 141 ? -17.335 20.711  9.995   1.00 70.15  ? 147 ASP   B CG  1 
ATOM   3402 O  OD1 . ASP   B 1 141 ? -18.104 20.442  9.042   1.00 72.04  ? 147 ASP   B OD1 1 
ATOM   3403 O  OD2 . ASP   B 1 141 ? -17.498 20.263  11.154  1.00 74.47  ? 147 ASP   B OD2 1 
ATOM   3404 N  N   . ILE   B 1 142 ? -13.890 22.906  6.950   1.00 53.36  ? 148 ILE   B N   1 
ATOM   3405 C  CA  . ILE   B 1 142 ? -12.689 23.713  6.702   1.00 52.74  ? 148 ILE   B CA  1 
ATOM   3406 C  C   . ILE   B 1 142 ? -12.889 24.759  5.549   1.00 58.46  ? 148 ILE   B C   1 
ATOM   3407 O  O   . ILE   B 1 142 ? -11.917 25.235  4.957   1.00 57.76  ? 148 ILE   B O   1 
ATOM   3408 C  CB  . ILE   B 1 142 ? -11.454 22.779  6.503   1.00 54.93  ? 148 ILE   B CB  1 
ATOM   3409 C  CG1 . ILE   B 1 142 ? -10.125 23.537  6.695   1.00 54.92  ? 148 ILE   B CG1 1 
ATOM   3410 C  CG2 . ILE   B 1 142 ? -11.497 21.999  5.168   1.00 55.05  ? 148 ILE   B CG2 1 
ATOM   3411 C  CD1 . ILE   B 1 142 ? -8.903  22.674  6.867   1.00 62.80  ? 148 ILE   B CD1 1 
ATOM   3412 N  N   . ASN   B 1 143 ? -14.141 25.145  5.279   1.00 56.16  ? 149 ASN   B N   1 
ATOM   3413 C  CA  . ASN   B 1 143 ? -14.424 26.173  4.282   1.00 56.95  ? 149 ASN   B CA  1 
ATOM   3414 C  C   . ASN   B 1 143 ? -14.014 27.520  4.872   1.00 64.69  ? 149 ASN   B C   1 
ATOM   3415 O  O   . ASN   B 1 143 ? -14.129 27.710  6.084   1.00 64.80  ? 149 ASN   B O   1 
ATOM   3416 C  CB  . ASN   B 1 143 ? -15.919 26.204  3.951   1.00 56.52  ? 149 ASN   B CB  1 
ATOM   3417 C  CG  . ASN   B 1 143 ? -16.330 25.360  2.768   1.00 79.83  ? 149 ASN   B CG  1 
ATOM   3418 O  OD1 . ASN   B 1 143 ? -15.676 25.351  1.717   1.00 74.43  ? 149 ASN   B OD1 1 
ATOM   3419 N  ND2 . ASN   B 1 143 ? -17.472 24.688  2.890   1.00 70.61  ? 149 ASN   B ND2 1 
ATOM   3420 N  N   . THR   B 1 144 ? -13.500 28.436  4.040   1.00 63.09  ? 150 THR   B N   1 
ATOM   3421 C  CA  . THR   B 1 144 ? -13.153 29.780  4.509   1.00 63.54  ? 150 THR   B CA  1 
ATOM   3422 C  C   . THR   B 1 144 ? -14.433 30.623  4.334   1.00 69.89  ? 150 THR   B C   1 
ATOM   3423 O  O   . THR   B 1 144 ? -15.328 30.167  3.612   1.00 68.67  ? 150 THR   B O   1 
ATOM   3424 C  CB  . THR   B 1 144 ? -11.902 30.356  3.795   1.00 70.31  ? 150 THR   B CB  1 
ATOM   3425 O  OG1 . THR   B 1 144 ? -12.228 30.772  2.469   1.00 73.92  ? 150 THR   B OG1 1 
ATOM   3426 C  CG2 . THR   B 1 144 ? -10.696 29.414  3.816   1.00 65.95  ? 150 THR   B CG2 1 
ATOM   3427 N  N   . PRO   B 1 145 ? -14.584 31.824  4.958   1.00 69.45  ? 151 PRO   B N   1 
ATOM   3428 C  CA  . PRO   B 1 145 ? -15.824 32.605  4.744   1.00 70.10  ? 151 PRO   B CA  1 
ATOM   3429 C  C   . PRO   B 1 145 ? -16.112 32.983  3.280   1.00 75.11  ? 151 PRO   B C   1 
ATOM   3430 O  O   . PRO   B 1 145 ? -17.248 33.331  2.945   1.00 74.67  ? 151 PRO   B O   1 
ATOM   3431 C  CB  . PRO   B 1 145 ? -15.628 33.840  5.632   1.00 71.89  ? 151 PRO   B CB  1 
ATOM   3432 C  CG  . PRO   B 1 145 ? -14.580 33.438  6.629   1.00 76.16  ? 151 PRO   B CG  1 
ATOM   3433 C  CD  . PRO   B 1 145 ? -13.666 32.531  5.876   1.00 71.56  ? 151 PRO   B CD  1 
ATOM   3434 N  N   . LEU   B 1 146 ? -15.095 32.865  2.406   1.00 72.80  ? 152 LEU   B N   1 
ATOM   3435 C  CA  . LEU   B 1 146 ? -15.205 33.171  0.979   1.00 73.40  ? 152 LEU   B CA  1 
ATOM   3436 C  C   . LEU   B 1 146 ? -15.379 31.926  0.085   1.00 78.49  ? 152 LEU   B C   1 
ATOM   3437 O  O   . LEU   B 1 146 ? -15.972 32.042  -0.991  1.00 78.40  ? 152 LEU   B O   1 
ATOM   3438 C  CB  . LEU   B 1 146 ? -14.019 34.033  0.512   1.00 73.45  ? 152 LEU   B CB  1 
ATOM   3439 C  CG  . LEU   B 1 146 ? -13.850 35.389  1.215   1.00 78.07  ? 152 LEU   B CG  1 
ATOM   3440 C  CD1 . LEU   B 1 146 ? -12.431 35.907  1.074   1.00 77.99  ? 152 LEU   B CD1 1 
ATOM   3441 C  CD2 . LEU   B 1 146 ? -14.871 36.411  0.722   1.00 80.77  ? 152 LEU   B CD2 1 
ATOM   3442 N  N   . THR   B 1 147 ? -14.884 30.742  0.528   1.00 74.87  ? 153 THR   B N   1 
ATOM   3443 C  CA  . THR   B 1 147 ? -15.014 29.492  -0.241  1.00 74.12  ? 153 THR   B CA  1 
ATOM   3444 C  C   . THR   B 1 147 ? -16.355 28.787  -0.008  1.00 77.57  ? 153 THR   B C   1 
ATOM   3445 O  O   . THR   B 1 147 ? -16.779 28.008  -0.860  1.00 77.00  ? 153 THR   B O   1 
ATOM   3446 C  CB  . THR   B 1 147 ? -13.830 28.532  -0.022  1.00 78.08  ? 153 THR   B CB  1 
ATOM   3447 O  OG1 . THR   B 1 147 ? -13.823 28.038  1.313   1.00 76.51  ? 153 THR   B OG1 1 
ATOM   3448 C  CG2 . THR   B 1 147 ? -12.482 29.122  -0.412  1.00 74.35  ? 153 THR   B CG2 1 
ATOM   3449 N  N   . THR   B 1 148 ? -17.017 29.060  1.134   1.00 74.38  ? 154 THR   B N   1 
ATOM   3450 C  CA  . THR   B 1 148 ? -18.310 28.468  1.511   1.00 74.49  ? 154 THR   B CA  1 
ATOM   3451 C  C   . THR   B 1 148 ? -19.440 28.853  0.530   1.00 78.64  ? 154 THR   B C   1 
ATOM   3452 O  O   . THR   B 1 148 ? -19.336 29.867  -0.159  1.00 79.08  ? 154 THR   B O   1 
ATOM   3453 C  CB  . THR   B 1 148 ? -18.653 28.775  2.988   1.00 83.04  ? 154 THR   B CB  1 
ATOM   3454 O  OG1 . THR   B 1 148 ? -19.887 28.143  3.334   1.00 84.15  ? 154 THR   B OG1 1 
ATOM   3455 C  CG2 . THR   B 1 148 ? -18.732 30.268  3.290   1.00 81.42  ? 154 THR   B CG2 1 
ATOM   3456 N  N   . SER   B 1 149 ? -20.505 28.031  0.468   1.00 74.78  ? 155 SER   B N   1 
ATOM   3457 C  CA  . SER   B 1 149 ? -21.646 28.238  -0.427  1.00 74.72  ? 155 SER   B CA  1 
ATOM   3458 C  C   . SER   B 1 149 ? -22.992 28.300  0.292   1.00 78.71  ? 155 SER   B C   1 
ATOM   3459 O  O   . SER   B 1 149 ? -23.930 28.900  -0.233  1.00 78.07  ? 155 SER   B O   1 
ATOM   3460 C  CB  . SER   B 1 149 ? -21.684 27.150  -1.497  1.00 78.53  ? 155 SER   B CB  1 
ATOM   3461 O  OG  . SER   B 1 149 ? -20.541 27.206  -2.335  1.00 88.18  ? 155 SER   B OG  1 
ATOM   3462 N  N   . SER   B 1 150 ? -23.097 27.662  1.473   1.00 75.87  ? 156 SER   B N   1 
ATOM   3463 C  CA  . SER   B 1 150 ? -24.336 27.596  2.261   1.00 75.80  ? 156 SER   B CA  1 
ATOM   3464 C  C   . SER   B 1 150 ? -24.597 28.836  3.117   1.00 78.87  ? 156 SER   B C   1 
ATOM   3465 O  O   . SER   B 1 150 ? -25.760 29.197  3.330   1.00 78.33  ? 156 SER   B O   1 
ATOM   3466 C  CB  . SER   B 1 150 ? -24.336 26.353  3.150   1.00 79.87  ? 156 SER   B CB  1 
ATOM   3467 O  OG  . SER   B 1 150 ? -23.226 26.351  4.034   1.00 88.24  ? 156 SER   B OG  1 
ATOM   3468 N  N   . GLY   B 1 151 ? -23.522 29.436  3.627   1.00 74.79  ? 157 GLY   B N   1 
ATOM   3469 C  CA  . GLY   B 1 151 ? -23.579 30.587  4.521   1.00 74.67  ? 157 GLY   B CA  1 
ATOM   3470 C  C   . GLY   B 1 151 ? -23.535 30.208  5.994   1.00 78.53  ? 157 GLY   B C   1 
ATOM   3471 O  O   . GLY   B 1 151 ? -23.330 31.073  6.851   1.00 78.34  ? 157 GLY   B O   1 
ATOM   3472 N  N   . ASN   B 1 152 ? -23.720 28.905  6.294   1.00 74.37  ? 158 ASN   B N   1 
ATOM   3473 C  CA  . ASN   B 1 152 ? -23.706 28.336  7.642   1.00 73.96  ? 158 ASN   B CA  1 
ATOM   3474 C  C   . ASN   B 1 152 ? -22.271 28.214  8.152   1.00 76.75  ? 158 ASN   B C   1 
ATOM   3475 O  O   . ASN   B 1 152 ? -21.414 27.694  7.437   1.00 76.04  ? 158 ASN   B O   1 
ATOM   3476 C  CB  . ASN   B 1 152 ? -24.415 26.977  7.652   1.00 74.40  ? 158 ASN   B CB  1 
ATOM   3477 C  CG  . ASN   B 1 152 ? -25.746 26.960  6.928   1.00 96.46  ? 158 ASN   B CG  1 
ATOM   3478 O  OD1 . ASN   B 1 152 ? -26.526 27.921  6.964   1.00 87.81  ? 158 ASN   B OD1 1 
ATOM   3479 N  ND2 . ASN   B 1 152 ? -26.032 25.861  6.245   1.00 90.23  ? 158 ASN   B ND2 1 
ATOM   3480 N  N   . LEU   B 1 153 ? -22.008 28.722  9.378   1.00 72.79  ? 159 LEU   B N   1 
ATOM   3481 C  CA  . LEU   B 1 153 ? -20.675 28.733  10.002  1.00 71.99  ? 159 LEU   B CA  1 
ATOM   3482 C  C   . LEU   B 1 153 ? -20.205 27.376  10.565  1.00 73.57  ? 159 LEU   B C   1 
ATOM   3483 O  O   . LEU   B 1 153 ? -19.012 27.230  10.852  1.00 71.45  ? 159 LEU   B O   1 
ATOM   3484 C  CB  . LEU   B 1 153 ? -20.585 29.822  11.088  1.00 72.15  ? 159 LEU   B CB  1 
ATOM   3485 C  CG  . LEU   B 1 153 ? -20.135 31.206  10.618  1.00 76.90  ? 159 LEU   B CG  1 
ATOM   3486 C  CD1 . LEU   B 1 153 ? -20.816 32.294  11.419  1.00 77.39  ? 159 LEU   B CD1 1 
ATOM   3487 C  CD2 . LEU   B 1 153 ? -18.617 31.356  10.691  1.00 77.64  ? 159 LEU   B CD2 1 
ATOM   3488 N  N   . HIS   B 1 154 ? -21.119 26.390  10.701  1.00 70.84  ? 160 HIS   B N   1 
ATOM   3489 C  CA  . HIS   B 1 154 ? -20.774 25.052  11.209  1.00 71.20  ? 160 HIS   B CA  1 
ATOM   3490 C  C   . HIS   B 1 154 ? -19.856 24.264  10.248  1.00 75.20  ? 160 HIS   B C   1 
ATOM   3491 O  O   . HIS   B 1 154 ? -19.203 23.311  10.677  1.00 75.10  ? 160 HIS   B O   1 
ATOM   3492 C  CB  . HIS   B 1 154 ? -22.021 24.243  11.622  1.00 72.17  ? 160 HIS   B CB  1 
ATOM   3493 C  CG  . HIS   B 1 154 ? -22.902 23.756  10.510  1.00 76.07  ? 160 HIS   B CG  1 
ATOM   3494 N  ND1 . HIS   B 1 154 ? -23.868 22.787  10.739  1.00 78.10  ? 160 HIS   B ND1 1 
ATOM   3495 C  CD2 . HIS   B 1 154 ? -22.964 24.129  9.209   1.00 78.07  ? 160 HIS   B CD2 1 
ATOM   3496 C  CE1 . HIS   B 1 154 ? -24.474 22.598  9.579   1.00 77.56  ? 160 HIS   B CE1 1 
ATOM   3497 N  NE2 . HIS   B 1 154 ? -23.965 23.383  8.628   1.00 77.93  ? 160 HIS   B NE2 1 
ATOM   3498 N  N   . GLY   B 1 155 ? -19.785 24.706  8.987   1.00 70.89  ? 161 GLY   B N   1 
ATOM   3499 C  CA  . GLY   B 1 155 ? -18.927 24.116  7.965   1.00 70.20  ? 161 GLY   B CA  1 
ATOM   3500 C  C   . GLY   B 1 155 ? -17.638 24.883  7.739   1.00 72.70  ? 161 GLY   B C   1 
ATOM   3501 O  O   . GLY   B 1 155 ? -16.932 24.625  6.760   1.00 72.20  ? 161 GLY   B O   1 
ATOM   3502 N  N   . GLN   B 1 156 ? -17.311 25.825  8.654   1.00 68.33  ? 162 GLN   B N   1 
ATOM   3503 C  CA  . GLN   B 1 156 ? -16.125 26.693  8.577   1.00 68.07  ? 162 GLN   B CA  1 
ATOM   3504 C  C   . GLN   B 1 156 ? -15.205 26.786  9.842   1.00 73.07  ? 162 GLN   B C   1 
ATOM   3505 O  O   . GLN   B 1 156 ? -14.240 27.555  9.762   1.00 73.13  ? 162 GLN   B O   1 
ATOM   3506 C  CB  . GLN   B 1 156 ? -16.567 28.126  8.202   1.00 69.19  ? 162 GLN   B CB  1 
ATOM   3507 C  CG  . GLN   B 1 156 ? -17.315 28.267  6.876   1.00 71.84  ? 162 GLN   B CG  1 
ATOM   3508 C  CD  . GLN   B 1 156 ? -18.069 29.568  6.812   1.00 76.67  ? 162 GLN   B CD  1 
ATOM   3509 O  OE1 . GLN   B 1 156 ? -17.484 30.658  6.881   1.00 66.08  ? 162 GLN   B OE1 1 
ATOM   3510 N  NE2 . GLN   B 1 156 ? -19.385 29.478  6.678   1.00 64.29  ? 162 GLN   B NE2 1 
ATOM   3511 N  N   . PRO   B 1 157 ? -15.420 26.074  10.990  1.00 68.96  ? 163 PRO   B N   1 
ATOM   3512 C  CA  . PRO   B 1 157 ? -14.574 26.315  12.175  1.00 68.44  ? 163 PRO   B CA  1 
ATOM   3513 C  C   . PRO   B 1 157 ? -13.057 26.170  12.041  1.00 70.64  ? 163 PRO   B C   1 
ATOM   3514 O  O   . PRO   B 1 157 ? -12.336 26.945  12.673  1.00 71.01  ? 163 PRO   B O   1 
ATOM   3515 C  CB  . PRO   B 1 157 ? -15.109 25.310  13.207  1.00 70.59  ? 163 PRO   B CB  1 
ATOM   3516 C  CG  . PRO   B 1 157 ? -15.914 24.335  12.434  1.00 75.26  ? 163 PRO   B CG  1 
ATOM   3517 C  CD  . PRO   B 1 157 ? -16.505 25.134  11.329  1.00 70.80  ? 163 PRO   B CD  1 
ATOM   3518 N  N   . VAL   B 1 158 ? -12.571 25.192  11.265  1.00 65.08  ? 164 VAL   B N   1 
ATOM   3519 C  CA  . VAL   B 1 158 ? -11.132 24.893  11.136  1.00 64.03  ? 164 VAL   B CA  1 
ATOM   3520 C  C   . VAL   B 1 158 ? -10.341 26.010  10.393  1.00 68.20  ? 164 VAL   B C   1 
ATOM   3521 O  O   . VAL   B 1 158 ? -9.135  26.153  10.625  1.00 66.64  ? 164 VAL   B O   1 
ATOM   3522 C  CB  . VAL   B 1 158 ? -10.908 23.479  10.517  1.00 66.92  ? 164 VAL   B CB  1 
ATOM   3523 C  CG1 . VAL   B 1 158 ? -9.449  23.036  10.625  1.00 66.35  ? 164 VAL   B CG1 1 
ATOM   3524 C  CG2 . VAL   B 1 158 ? -11.818 22.447  11.180  1.00 66.57  ? 164 VAL   B CG2 1 
ATOM   3525 N  N   . SER   B 1 159 ? -11.017 26.802  9.528   1.00 66.63  ? 165 SER   B N   1 
ATOM   3526 C  CA  . SER   B 1 159 ? -10.381 27.894  8.766   1.00 67.55  ? 165 SER   B CA  1 
ATOM   3527 C  C   . SER   B 1 159 ? -9.783  28.980  9.678   1.00 73.91  ? 165 SER   B C   1 
ATOM   3528 O  O   . SER   B 1 159 ? -8.640  29.402  9.468   1.00 74.00  ? 165 SER   B O   1 
ATOM   3529 C  CB  . SER   B 1 159 ? -11.358 28.505  7.765   1.00 69.81  ? 165 SER   B CB  1 
ATOM   3530 O  OG  . SER   B 1 159 ? -12.481 29.082  8.409   1.00 76.38  ? 165 SER   B OG  1 
ATOM   3531 N  N   . PHE   B 1 160 ? -10.537 29.373  10.719  1.00 71.68  ? 166 PHE   B N   1 
ATOM   3532 C  CA  . PHE   B 1 160 ? -10.140 30.376  11.712  1.00 72.12  ? 166 PHE   B CA  1 
ATOM   3533 C  C   . PHE   B 1 160 ? -8.984  29.912  12.615  1.00 78.73  ? 166 PHE   B C   1 
ATOM   3534 O  O   . PHE   B 1 160 ? -8.152  30.735  13.005  1.00 79.07  ? 166 PHE   B O   1 
ATOM   3535 C  CB  . PHE   B 1 160 ? -11.353 30.791  12.570  1.00 73.50  ? 166 PHE   B CB  1 
ATOM   3536 C  CG  . PHE   B 1 160 ? -12.621 31.069  11.793  1.00 75.09  ? 166 PHE   B CG  1 
ATOM   3537 C  CD1 . PHE   B 1 160 ? -12.748 32.220  11.022  1.00 78.44  ? 166 PHE   B CD1 1 
ATOM   3538 C  CD2 . PHE   B 1 160 ? -13.695 30.189  11.845  1.00 77.31  ? 166 PHE   B CD2 1 
ATOM   3539 C  CE1 . PHE   B 1 160 ? -13.924 32.477  10.306  1.00 79.36  ? 166 PHE   B CE1 1 
ATOM   3540 C  CE2 . PHE   B 1 160 ? -14.876 30.453  11.136  1.00 80.07  ? 166 PHE   B CE2 1 
ATOM   3541 C  CZ  . PHE   B 1 160 ? -14.980 31.593  10.368  1.00 78.19  ? 166 PHE   B CZ  1 
ATOM   3542 N  N   . LEU   B 1 161 ? -8.925  28.602  12.933  1.00 76.19  ? 167 LEU   B N   1 
ATOM   3543 C  CA  . LEU   B 1 161 ? -7.930  28.018  13.840  1.00 76.74  ? 167 LEU   B CA  1 
ATOM   3544 C  C   . LEU   B 1 161 ? -6.559  27.695  13.220  1.00 82.85  ? 167 LEU   B C   1 
ATOM   3545 O  O   . LEU   B 1 161 ? -5.577  27.611  13.963  1.00 81.47  ? 167 LEU   B O   1 
ATOM   3546 C  CB  . LEU   B 1 161 ? -8.501  26.763  14.522  1.00 76.76  ? 167 LEU   B CB  1 
ATOM   3547 C  CG  . LEU   B 1 161 ? -9.707  26.984  15.434  1.00 81.48  ? 167 LEU   B CG  1 
ATOM   3548 C  CD1 . LEU   B 1 161 ? -10.632 25.785  15.415  1.00 81.53  ? 167 LEU   B CD1 1 
ATOM   3549 C  CD2 . LEU   B 1 161 ? -9.274  27.332  16.852  1.00 84.25  ? 167 LEU   B CD2 1 
ATOM   3550 N  N   . LEU   B 1 162 ? -6.482  27.506  11.889  1.00 82.47  ? 168 LEU   B N   1 
ATOM   3551 C  CA  . LEU   B 1 162 ? -5.215  27.168  11.233  1.00 83.83  ? 168 LEU   B CA  1 
ATOM   3552 C  C   . LEU   B 1 162 ? -4.312  28.376  10.944  1.00 90.67  ? 168 LEU   B C   1 
ATOM   3553 O  O   . LEU   B 1 162 ? -4.779  29.400  10.439  1.00 90.22  ? 168 LEU   B O   1 
ATOM   3554 C  CB  . LEU   B 1 162 ? -5.441  26.339  9.961   1.00 84.08  ? 168 LEU   B CB  1 
ATOM   3555 C  CG  . LEU   B 1 162 ? -5.579  24.827  10.156  1.00 89.09  ? 168 LEU   B CG  1 
ATOM   3556 C  CD1 . LEU   B 1 162 ? -6.174  24.181  8.929   1.00 89.52  ? 168 LEU   B CD1 1 
ATOM   3557 C  CD2 . LEU   B 1 162 ? -4.235  24.174  10.468  1.00 90.79  ? 168 LEU   B CD2 1 
ATOM   3558 N  N   . ARG   B 1 163 ? -3.007  28.227  11.263  1.00 89.40  ? 169 ARG   B N   1 
ATOM   3559 C  CA  . ARG   B 1 163 ? -1.954  29.234  11.083  1.00 90.21  ? 169 ARG   B CA  1 
ATOM   3560 C  C   . ARG   B 1 163 ? -1.644  29.525  9.612   1.00 96.01  ? 169 ARG   B C   1 
ATOM   3561 O  O   . ARG   B 1 163 ? -1.316  30.663  9.265   1.00 95.52  ? 169 ARG   B O   1 
ATOM   3562 C  CB  . ARG   B 1 163 ? -0.665  28.812  11.813  1.00 90.60  ? 169 ARG   B CB  1 
ATOM   3563 C  CG  . ARG   B 1 163 ? -0.667  29.134  13.301  1.00 102.51 ? 169 ARG   B CG  1 
ATOM   3564 C  CD  . ARG   B 1 163 ? 0.740   29.235  13.857  1.00 114.58 ? 169 ARG   B CD  1 
ATOM   3565 N  NE  . ARG   B 1 163 ? 1.269   27.933  14.267  1.00 124.83 ? 169 ARG   B NE  1 
ATOM   3566 C  CZ  . ARG   B 1 163 ? 1.233   27.466  15.512  1.00 140.51 ? 169 ARG   B CZ  1 
ATOM   3567 N  NH1 . ARG   B 1 163 ? 0.692   28.191  16.485  1.00 129.24 ? 169 ARG   B NH1 1 
ATOM   3568 N  NH2 . ARG   B 1 163 ? 1.738   26.274  15.793  1.00 127.19 ? 169 ARG   B NH2 1 
ATOM   3569 N  N   . GLU   B 1 164 ? -1.722  28.484  8.761   1.00 93.58  ? 170 GLU   B N   1 
ATOM   3570 C  CA  . GLU   B 1 164 ? -1.443  28.559  7.327   1.00 93.48  ? 170 GLU   B CA  1 
ATOM   3571 C  C   . GLU   B 1 164 ? -2.602  29.168  6.530   1.00 98.20  ? 170 GLU   B C   1 
ATOM   3572 O  O   . GLU   B 1 164 ? -2.384  29.625  5.408   1.00 97.90  ? 170 GLU   B O   1 
ATOM   3573 C  CB  . GLU   B 1 164 ? -1.057  27.172  6.784   1.00 94.75  ? 170 GLU   B CB  1 
ATOM   3574 C  CG  . GLU   B 1 164 ? 0.361   26.731  7.136   1.00 103.44 ? 170 GLU   B CG  1 
ATOM   3575 C  CD  . GLU   B 1 164 ? 0.626   26.175  8.527   1.00 117.16 ? 170 GLU   B CD  1 
ATOM   3576 O  OE1 . GLU   B 1 164 ? -0.316  26.107  9.350   1.00 102.46 ? 170 GLU   B OE1 1 
ATOM   3577 O  OE2 . GLU   B 1 164 ? 1.791   25.799  8.790   1.00 110.01 ? 170 GLU   B OE2 1 
ATOM   3578 N  N   . LEU   B 1 165 ? -3.819  29.192  7.115   1.00 95.74  ? 171 LEU   B N   1 
ATOM   3579 C  CA  . LEU   B 1 165 ? -5.028  29.732  6.483   1.00 96.35  ? 171 LEU   B CA  1 
ATOM   3580 C  C   . LEU   B 1 165 ? -5.404  31.164  6.914   1.00 102.16 ? 171 LEU   B C   1 
ATOM   3581 O  O   . LEU   B 1 165 ? -6.490  31.627  6.556   1.00 101.48 ? 171 LEU   B O   1 
ATOM   3582 C  CB  . LEU   B 1 165 ? -6.224  28.787  6.709   1.00 96.42  ? 171 LEU   B CB  1 
ATOM   3583 C  CG  . LEU   B 1 165 ? -6.424  27.638  5.723   1.00 101.12 ? 171 LEU   B CG  1 
ATOM   3584 C  CD1 . LEU   B 1 165 ? -7.434  26.652  6.267   1.00 101.21 ? 171 LEU   B CD1 1 
ATOM   3585 C  CD2 . LEU   B 1 165 ? -6.892  28.140  4.354   1.00 103.60 ? 171 LEU   B CD2 1 
ATOM   3586 N  N   . GLN   B 1 166 ? -4.523  31.864  7.665   1.00 100.54 ? 172 GLN   B N   1 
ATOM   3587 C  CA  . GLN   B 1 166 ? -4.774  33.236  8.138   1.00 101.11 ? 172 GLN   B CA  1 
ATOM   3588 C  C   . GLN   B 1 166 ? -4.860  34.248  6.979   1.00 105.62 ? 172 GLN   B C   1 
ATOM   3589 O  O   . GLN   B 1 166 ? -5.736  35.119  6.990   1.00 104.95 ? 172 GLN   B O   1 
ATOM   3590 C  CB  . GLN   B 1 166 ? -3.720  33.669  9.177   1.00 102.68 ? 172 GLN   B CB  1 
ATOM   3591 C  CG  . GLN   B 1 166 ? -4.160  34.864  10.033  1.00 122.15 ? 172 GLN   B CG  1 
ATOM   3592 C  CD  . GLN   B 1 166 ? -3.080  35.435  10.929  1.00 144.09 ? 172 GLN   B CD  1 
ATOM   3593 O  OE1 . GLN   B 1 166 ? -1.878  35.403  10.626  1.00 140.06 ? 172 GLN   B OE1 1 
ATOM   3594 N  NE2 . GLN   B 1 166 ? -3.499  36.027  12.038  1.00 136.48 ? 172 GLN   B NE2 1 
ATOM   3595 N  N   . ASP   B 1 167 ? -3.970  34.102  5.975   1.00 103.01 ? 173 ASP   B N   1 
ATOM   3596 C  CA  . ASP   B 1 167 ? -3.897  34.955  4.781   1.00 103.17 ? 173 ASP   B CA  1 
ATOM   3597 C  C   . ASP   B 1 167 ? -5.066  34.753  3.797   1.00 107.20 ? 173 ASP   B C   1 
ATOM   3598 O  O   . ASP   B 1 167 ? -5.267  35.594  2.917   1.00 106.70 ? 173 ASP   B O   1 
ATOM   3599 C  CB  . ASP   B 1 167 ? -2.537  34.801  4.071   1.00 105.11 ? 173 ASP   B CB  1 
ATOM   3600 C  CG  . ASP   B 1 167 ? -2.072  33.370  3.894   1.00 115.96 ? 173 ASP   B CG  1 
ATOM   3601 O  OD1 . ASP   B 1 167 ? -1.577  32.780  4.882   1.00 116.55 ? 173 ASP   B OD1 1 
ATOM   3602 O  OD2 . ASP   B 1 167 ? -2.179  32.847  2.764   1.00 122.31 ? 173 ASP   B OD2 1 
ATOM   3603 N  N   . LYS   B 1 168 ? -5.839  33.659  3.959   1.00 103.91 ? 174 LYS   B N   1 
ATOM   3604 C  CA  . LYS   B 1 168 ? -6.993  33.329  3.113   1.00 103.82 ? 174 LYS   B CA  1 
ATOM   3605 C  C   . LYS   B 1 168 ? -8.334  33.567  3.829   1.00 108.09 ? 174 LYS   B C   1 
ATOM   3606 O  O   . LYS   B 1 168 ? -9.391  33.449  3.201   1.00 107.42 ? 174 LYS   B O   1 
ATOM   3607 C  CB  . LYS   B 1 168 ? -6.902  31.875  2.598   1.00 106.43 ? 174 LYS   B CB  1 
ATOM   3608 C  CG  . LYS   B 1 168 ? -5.602  31.528  1.869   1.00 121.98 ? 174 LYS   B CG  1 
ATOM   3609 C  CD  . LYS   B 1 168 ? -5.605  31.953  0.405   1.00 132.29 ? 174 LYS   B CD  1 
ATOM   3610 C  CE  . LYS   B 1 168 ? -4.230  32.396  -0.019  1.00 142.71 ? 174 LYS   B CE  1 
ATOM   3611 N  NZ  . LYS   B 1 168 ? -4.065  32.352  -1.494  1.00 152.11 ? 174 LYS   B NZ  1 
ATOM   3612 N  N   . VAL   B 1 169 ? -8.291  33.903  5.136   1.00 105.69 ? 175 VAL   B N   1 
ATOM   3613 C  CA  . VAL   B 1 169 ? -9.484  34.150  5.954   1.00 106.10 ? 175 VAL   B CA  1 
ATOM   3614 C  C   . VAL   B 1 169 ? -9.597  35.647  6.336   1.00 111.19 ? 175 VAL   B C   1 
ATOM   3615 O  O   . VAL   B 1 169 ? -8.668  36.192  6.943   1.00 110.68 ? 175 VAL   B O   1 
ATOM   3616 C  CB  . VAL   B 1 169 ? -9.580  33.190  7.180   1.00 109.94 ? 175 VAL   B CB  1 
ATOM   3617 C  CG1 . VAL   B 1 169 ? -10.716 33.582  8.126   1.00 109.72 ? 175 VAL   B CG1 1 
ATOM   3618 C  CG2 . VAL   B 1 169 ? -9.753  31.744  6.728   1.00 109.73 ? 175 VAL   B CG2 1 
ATOM   3619 N  N   . PRO   B 1 170 ? -10.726 36.318  5.988   1.00 108.58 ? 176 PRO   B N   1 
ATOM   3620 C  CA  . PRO   B 1 170 ? -10.871 37.739  6.348   1.00 108.70 ? 176 PRO   B CA  1 
ATOM   3621 C  C   . PRO   B 1 170 ? -11.314 37.949  7.798   1.00 112.99 ? 176 PRO   B C   1 
ATOM   3622 O  O   . PRO   B 1 170 ? -11.787 37.008  8.441   1.00 112.56 ? 176 PRO   B O   1 
ATOM   3623 C  CB  . PRO   B 1 170 ? -11.939 38.234  5.367   1.00 110.46 ? 176 PRO   B CB  1 
ATOM   3624 C  CG  . PRO   B 1 170 ? -12.790 37.040  5.104   1.00 114.71 ? 176 PRO   B CG  1 
ATOM   3625 C  CD  . PRO   B 1 170 ? -11.917 35.820  5.264   1.00 110.21 ? 176 PRO   B CD  1 
ATOM   3626 N  N   . GLN   B 1 171 ? -11.184 39.192  8.303   1.00 109.72 ? 177 GLN   B N   1 
ATOM   3627 C  CA  . GLN   B 1 171 ? -11.617 39.559  9.650   1.00 109.57 ? 177 GLN   B CA  1 
ATOM   3628 C  C   . GLN   B 1 171 ? -13.137 39.770  9.611   1.00 113.41 ? 177 GLN   B C   1 
ATOM   3629 O  O   . GLN   B 1 171 ? -13.626 40.626  8.870   1.00 113.01 ? 177 GLN   B O   1 
ATOM   3630 C  CB  . GLN   B 1 171 ? -10.879 40.818  10.142  1.00 111.02 ? 177 GLN   B CB  1 
ATOM   3631 C  CG  . GLN   B 1 171 ? -10.913 40.994  11.659  1.00 128.72 ? 177 GLN   B CG  1 
ATOM   3632 C  CD  . GLN   B 1 171 ? -10.335 42.319  12.091  1.00 147.69 ? 177 GLN   B CD  1 
ATOM   3633 O  OE1 . GLN   B 1 171 ? -9.115  42.514  12.125  1.00 142.54 ? 177 GLN   B OE1 1 
ATOM   3634 N  NE2 . GLN   B 1 171 ? -11.202 43.253  12.455  1.00 139.72 ? 177 GLN   B NE2 1 
ATOM   3635 N  N   . LEU   B 1 172 ? -13.875 38.953  10.370  1.00 110.21 ? 178 LEU   B N   1 
ATOM   3636 C  CA  . LEU   B 1 172 ? -15.338 38.977  10.427  1.00 110.33 ? 178 LEU   B CA  1 
ATOM   3637 C  C   . LEU   B 1 172 ? -15.881 39.738  11.656  1.00 114.58 ? 178 LEU   B C   1 
ATOM   3638 O  O   . LEU   B 1 172 ? -15.128 39.906  12.621  1.00 114.17 ? 178 LEU   B O   1 
ATOM   3639 C  CB  . LEU   B 1 172 ? -15.859 37.525  10.409  1.00 110.46 ? 178 LEU   B CB  1 
ATOM   3640 C  CG  . LEU   B 1 172 ? -16.483 37.043  9.099   1.00 115.17 ? 178 LEU   B CG  1 
ATOM   3641 C  CD1 . LEU   B 1 172 ? -15.421 36.782  8.040   1.00 115.35 ? 178 LEU   B CD1 1 
ATOM   3642 C  CD2 . LEU   B 1 172 ? -17.312 35.797  9.324   1.00 117.37 ? 178 LEU   B CD2 1 
ATOM   3643 N  N   . PRO   B 1 173 ? -17.169 40.197  11.666  1.00 111.37 ? 179 PRO   B N   1 
ATOM   3644 C  CA  . PRO   B 1 173 ? -17.678 40.916  12.851  1.00 111.25 ? 179 PRO   B CA  1 
ATOM   3645 C  C   . PRO   B 1 173 ? -17.852 40.025  14.090  1.00 114.70 ? 179 PRO   B C   1 
ATOM   3646 O  O   . PRO   B 1 173 ? -18.721 39.147  14.128  1.00 114.12 ? 179 PRO   B O   1 
ATOM   3647 C  CB  . PRO   B 1 173 ? -18.991 41.535  12.360  1.00 113.09 ? 179 PRO   B CB  1 
ATOM   3648 C  CG  . PRO   B 1 173 ? -19.445 40.643  11.267  1.00 117.46 ? 179 PRO   B CG  1 
ATOM   3649 C  CD  . PRO   B 1 173 ? -18.202 40.110  10.609  1.00 112.96 ? 179 PRO   B CD  1 
ATOM   3650 N  N   . GLY   B 1 174 ? -16.990 40.258  15.081  1.00 110.94 ? 180 GLY   B N   1 
ATOM   3651 C  CA  . GLY   B 1 174 ? -16.956 39.514  16.336  1.00 110.42 ? 180 GLY   B CA  1 
ATOM   3652 C  C   . GLY   B 1 174 ? -16.034 38.310  16.305  1.00 113.27 ? 180 GLY   B C   1 
ATOM   3653 O  O   . GLY   B 1 174 ? -16.172 37.408  17.132  1.00 113.06 ? 180 GLY   B O   1 
ATOM   3654 N  N   . PHE   B 1 175 ? -15.081 38.294  15.355  1.00 108.82 ? 181 PHE   B N   1 
ATOM   3655 C  CA  . PHE   B 1 175 ? -14.106 37.216  15.152  1.00 108.21 ? 181 PHE   B CA  1 
ATOM   3656 C  C   . PHE   B 1 175 ? -12.656 37.718  15.305  1.00 112.08 ? 181 PHE   B C   1 
ATOM   3657 O  O   . PHE   B 1 175 ? -11.713 36.983  14.996  1.00 111.52 ? 181 PHE   B O   1 
ATOM   3658 C  CB  . PHE   B 1 175 ? -14.315 36.569  13.762  1.00 109.78 ? 181 PHE   B CB  1 
ATOM   3659 C  CG  . PHE   B 1 175 ? -15.427 35.549  13.651  1.00 111.00 ? 181 PHE   B CG  1 
ATOM   3660 C  CD1 . PHE   B 1 175 ? -16.759 35.945  13.633  1.00 113.85 ? 181 PHE   B CD1 1 
ATOM   3661 C  CD2 . PHE   B 1 175 ? -15.140 34.199  13.495  1.00 113.03 ? 181 PHE   B CD2 1 
ATOM   3662 C  CE1 . PHE   B 1 175 ? -17.784 35.002  13.512  1.00 114.74 ? 181 PHE   B CE1 1 
ATOM   3663 C  CE2 . PHE   B 1 175 ? -16.166 33.256  13.384  1.00 115.84 ? 181 PHE   B CE2 1 
ATOM   3664 C  CZ  . PHE   B 1 175 ? -17.481 33.664  13.393  1.00 113.88 ? 181 PHE   B CZ  1 
ATOM   3665 N  N   . SER   B 1 176 ? -12.488 38.968  15.790  1.00 108.80 ? 182 SER   B N   1 
ATOM   3666 C  CA  . SER   B 1 176 ? -11.195 39.637  15.996  1.00 108.53 ? 182 SER   B CA  1 
ATOM   3667 C  C   . SER   B 1 176 ? -10.330 38.996  17.087  1.00 111.74 ? 182 SER   B C   1 
ATOM   3668 O  O   . SER   B 1 176 ? -9.100  39.028  16.989  1.00 110.93 ? 182 SER   B O   1 
ATOM   3669 C  CB  . SER   B 1 176 ? -11.407 41.118  16.297  1.00 112.22 ? 182 SER   B CB  1 
ATOM   3670 O  OG  . SER   B 1 176 ? -12.309 41.311  17.374  1.00 121.10 ? 182 SER   B OG  1 
ATOM   3671 N  N   . TRP   B 1 177 ? -10.978 38.430  18.123  1.00 108.27 ? 183 TRP   B N   1 
ATOM   3672 C  CA  . TRP   B 1 177 ? -10.345 37.776  19.273  1.00 107.96 ? 183 TRP   B CA  1 
ATOM   3673 C  C   . TRP   B 1 177 ? -9.570  36.493  18.930  1.00 111.13 ? 183 TRP   B C   1 
ATOM   3674 O  O   . TRP   B 1 177 ? -8.589  36.189  19.613  1.00 110.64 ? 183 TRP   B O   1 
ATOM   3675 C  CB  . TRP   B 1 177 ? -11.384 37.500  20.373  1.00 106.75 ? 183 TRP   B CB  1 
ATOM   3676 C  CG  . TRP   B 1 177 ? -12.501 36.601  19.936  1.00 107.82 ? 183 TRP   B CG  1 
ATOM   3677 C  CD1 . TRP   B 1 177 ? -13.665 36.974  19.330  1.00 110.77 ? 183 TRP   B CD1 1 
ATOM   3678 C  CD2 . TRP   B 1 177 ? -12.552 35.173  20.061  1.00 107.75 ? 183 TRP   B CD2 1 
ATOM   3679 N  NE1 . TRP   B 1 177 ? -14.442 35.868  19.074  1.00 110.33 ? 183 TRP   B NE1 1 
ATOM   3680 C  CE2 . TRP   B 1 177 ? -13.779 34.747  19.505  1.00 111.81 ? 183 TRP   B CE2 1 
ATOM   3681 C  CE3 . TRP   B 1 177 ? -11.677 34.206  20.592  1.00 108.99 ? 183 TRP   B CE3 1 
ATOM   3682 C  CZ2 . TRP   B 1 177 ? -14.153 33.397  19.459  1.00 111.16 ? 183 TRP   B CZ2 1 
ATOM   3683 C  CZ3 . TRP   B 1 177 ? -12.051 32.871  20.555  1.00 110.48 ? 183 TRP   B CZ3 1 
ATOM   3684 C  CH2 . TRP   B 1 177 ? -13.279 32.478  20.002  1.00 111.18 ? 183 TRP   B CH2 1 
ATOM   3685 N  N   . ILE   B 1 178 ? -10.019 35.737  17.894  1.00 106.98 ? 184 ILE   B N   1 
ATOM   3686 C  CA  . ILE   B 1 178 ? -9.405  34.474  17.447  1.00 106.42 ? 184 ILE   B CA  1 
ATOM   3687 C  C   . ILE   B 1 178 ? -7.970  34.666  16.958  1.00 110.28 ? 184 ILE   B C   1 
ATOM   3688 O  O   . ILE   B 1 178 ? -7.718  35.470  16.056  1.00 109.86 ? 184 ILE   B O   1 
ATOM   3689 C  CB  . ILE   B 1 178 ? -10.272 33.709  16.397  1.00 109.31 ? 184 ILE   B CB  1 
ATOM   3690 C  CG1 . ILE   B 1 178 ? -11.672 33.415  16.936  1.00 109.50 ? 184 ILE   B CG1 1 
ATOM   3691 C  CG2 . ILE   B 1 178 ? -9.599  32.399  15.937  1.00 109.86 ? 184 ILE   B CG2 1 
ATOM   3692 C  CD1 . ILE   B 1 178 ? -12.768 33.738  16.028  1.00 114.58 ? 184 ILE   B CD1 1 
ATOM   3693 N  N   . LYS   B 1 179 ? -7.043  33.900  17.553  1.00 106.81 ? 185 LYS   B N   1 
ATOM   3694 C  CA  . LYS   B 1 179 ? -5.625  33.873  17.205  1.00 106.55 ? 185 LYS   B CA  1 
ATOM   3695 C  C   . LYS   B 1 179 ? -5.308  32.485  16.607  1.00 109.74 ? 185 LYS   B C   1 
ATOM   3696 O  O   . LYS   B 1 179 ? -5.791  31.483  17.146  1.00 109.29 ? 185 LYS   B O   1 
ATOM   3697 C  CB  . LYS   B 1 179 ? -4.744  34.140  18.442  1.00 109.23 ? 185 LYS   B CB  1 
ATOM   3698 C  CG  . LYS   B 1 179 ? -4.872  35.550  19.015  1.00 124.81 ? 185 LYS   B CG  1 
ATOM   3699 C  CD  . LYS   B 1 179 ? -3.949  35.755  20.211  1.00 134.47 ? 185 LYS   B CD  1 
ATOM   3700 C  CE  . LYS   B 1 179 ? -4.178  37.074  20.911  1.00 144.06 ? 185 LYS   B CE  1 
ATOM   3701 N  NZ  . LYS   B 1 179 ? -5.358  37.026  21.815  1.00 151.37 ? 185 LYS   B NZ  1 
ATOM   3702 N  N   . PRO   B 1 180 ? -4.532  32.388  15.496  1.00 105.45 ? 186 PRO   B N   1 
ATOM   3703 C  CA  . PRO   B 1 180 ? -4.225  31.061  14.931  1.00 104.75 ? 186 PRO   B CA  1 
ATOM   3704 C  C   . PRO   B 1 180 ? -3.291  30.275  15.853  1.00 106.40 ? 186 PRO   B C   1 
ATOM   3705 O  O   . PRO   B 1 180 ? -2.121  30.629  16.027  1.00 106.21 ? 186 PRO   B O   1 
ATOM   3706 C  CB  . PRO   B 1 180 ? -3.609  31.382  13.561  1.00 106.63 ? 186 PRO   B CB  1 
ATOM   3707 C  CG  . PRO   B 1 180 ? -3.811  32.853  13.352  1.00 111.23 ? 186 PRO   B CG  1 
ATOM   3708 C  CD  . PRO   B 1 180 ? -3.881  33.454  14.713  1.00 106.85 ? 186 PRO   B CD  1 
ATOM   3709 N  N   . CYS   B 1 181 ? -3.847  29.228  16.486  1.00 100.74 ? 187 CYS   B N   1 
ATOM   3710 C  CA  . CYS   B 1 181 ? -3.184  28.397  17.491  1.00 99.22  ? 187 CYS   B CA  1 
ATOM   3711 C  C   . CYS   B 1 181 ? -2.632  27.064  16.972  1.00 100.23 ? 187 CYS   B C   1 
ATOM   3712 O  O   . CYS   B 1 181 ? -1.525  26.690  17.363  1.00 99.90  ? 187 CYS   B O   1 
ATOM   3713 C  CB  . CYS   B 1 181 ? -4.116  28.178  18.679  1.00 99.22  ? 187 CYS   B CB  1 
ATOM   3714 S  SG  . CYS   B 1 181 ? -5.744  27.510  18.236  1.00 102.87 ? 187 CYS   B SG  1 
ATOM   3715 N  N   . ILE   B 1 182 ? -3.406  26.329  16.148  1.00 94.37  ? 188 ILE   B N   1 
ATOM   3716 C  CA  . ILE   B 1 182 ? -2.997  25.008  15.648  1.00 93.00  ? 188 ILE   B CA  1 
ATOM   3717 C  C   . ILE   B 1 182 ? -2.425  25.046  14.226  1.00 93.32  ? 188 ILE   B C   1 
ATOM   3718 O  O   . ILE   B 1 182 ? -3.015  25.660  13.336  1.00 92.86  ? 188 ILE   B O   1 
ATOM   3719 C  CB  . ILE   B 1 182 ? -4.122  23.936  15.782  1.00 96.18  ? 188 ILE   B CB  1 
ATOM   3720 C  CG1 . ILE   B 1 182 ? -5.480  24.427  15.215  1.00 96.42  ? 188 ILE   B CG1 1 
ATOM   3721 C  CG2 . ILE   B 1 182 ? -4.247  23.459  17.237  1.00 97.12  ? 188 ILE   B CG2 1 
ATOM   3722 C  CD1 . ILE   B 1 182 ? -6.364  23.338  14.647  1.00 103.89 ? 188 ILE   B CD1 1 
ATOM   3723 N  N   . SER   B 1 183 ? -1.275  24.368  14.025  1.00 87.10  ? 189 SER   B N   1 
ATOM   3724 C  CA  . SER   B 1 183 ? -0.597  24.254  12.731  1.00 85.68  ? 189 SER   B CA  1 
ATOM   3725 C  C   . SER   B 1 183 ? -1.160  23.069  11.920  1.00 86.73  ? 189 SER   B C   1 
ATOM   3726 O  O   . SER   B 1 183 ? -1.953  22.285  12.452  1.00 86.51  ? 189 SER   B O   1 
ATOM   3727 C  CB  . SER   B 1 183 ? 0.915   24.138  12.916  1.00 89.41  ? 189 SER   B CB  1 
ATOM   3728 O  OG  . SER   B 1 183 ? 1.287   22.963  13.619  1.00 99.31  ? 189 SER   B OG  1 
ATOM   3729 N  N   . SER   B 1 184 ? -0.778  22.968  10.627  1.00 80.47  ? 190 SER   B N   1 
ATOM   3730 C  CA  . SER   B 1 184 ? -1.240  21.939  9.684   1.00 78.87  ? 190 SER   B CA  1 
ATOM   3731 C  C   . SER   B 1 184 ? -1.018  20.497  10.155  1.00 78.88  ? 190 SER   B C   1 
ATOM   3732 O  O   . SER   B 1 184 ? -1.923  19.674  10.013  1.00 78.37  ? 190 SER   B O   1 
ATOM   3733 C  CB  . SER   B 1 184 ? -0.624  22.155  8.301   1.00 82.05  ? 190 SER   B CB  1 
ATOM   3734 O  OG  . SER   B 1 184 ? 0.791   22.059  8.328   1.00 89.58  ? 190 SER   B OG  1 
ATOM   3735 N  N   . ALA   B 1 185 ? 0.164   20.209  10.739  1.00 72.54  ? 191 ALA   B N   1 
ATOM   3736 C  CA  . ALA   B 1 185 ? 0.560   18.887  11.243  1.00 71.04  ? 191 ALA   B CA  1 
ATOM   3737 C  C   . ALA   B 1 185 ? 0.003   18.545  12.650  1.00 71.25  ? 191 ALA   B C   1 
ATOM   3738 O  O   . ALA   B 1 185 ? 0.391   17.525  13.227  1.00 71.01  ? 191 ALA   B O   1 
ATOM   3739 C  CB  . ALA   B 1 185 ? 2.082   18.759  11.222  1.00 71.76  ? 191 ALA   B CB  1 
ATOM   3740 N  N   . SER   B 1 186 ? -0.914  19.380  13.180  1.00 64.82  ? 192 SER   B N   1 
ATOM   3741 C  CA  . SER   B 1 186 ? -1.514  19.207  14.510  1.00 63.10  ? 192 SER   B CA  1 
ATOM   3742 C  C   . SER   B 1 186 ? -3.017  18.863  14.479  1.00 63.74  ? 192 SER   B C   1 
ATOM   3743 O  O   . SER   B 1 186 ? -3.627  18.681  15.538  1.00 63.12  ? 192 SER   B O   1 
ATOM   3744 C  CB  . SER   B 1 186 ? -1.235  20.425  15.388  1.00 65.00  ? 192 SER   B CB  1 
ATOM   3745 O  OG  . SER   B 1 186 ? 0.159   20.537  15.626  1.00 70.65  ? 192 SER   B OG  1 
ATOM   3746 N  N   . ILE   B 1 187 ? -3.599  18.724  13.273  1.00 57.24  ? 193 ILE   B N   1 
ATOM   3747 C  CA  . ILE   B 1 187 ? -4.990  18.300  13.094  1.00 55.43  ? 193 ILE   B CA  1 
ATOM   3748 C  C   . ILE   B 1 187 ? -5.028  17.051  12.183  1.00 57.21  ? 193 ILE   B C   1 
ATOM   3749 O  O   . ILE   B 1 187 ? -4.290  17.004  11.192  1.00 56.20  ? 193 ILE   B O   1 
ATOM   3750 C  CB  . ILE   B 1 187 ? -5.962  19.438  12.662  1.00 58.24  ? 193 ILE   B CB  1 
ATOM   3751 C  CG1 . ILE   B 1 187 ? -7.440  18.982  12.758  1.00 58.06  ? 193 ILE   B CG1 1 
ATOM   3752 C  CG2 . ILE   B 1 187 ? -5.619  20.014  11.267  1.00 60.15  ? 193 ILE   B CG2 1 
ATOM   3753 C  CD1 . ILE   B 1 187 ? -8.485  20.078  12.891  1.00 62.70  ? 193 ILE   B CD1 1 
ATOM   3754 N  N   . VAL   B 1 188 ? -5.813  16.012  12.581  1.00 51.53  ? 194 VAL   B N   1 
ATOM   3755 C  CA  . VAL   B 1 188 ? -6.014  14.765  11.816  1.00 48.64  ? 194 VAL   B CA  1 
ATOM   3756 C  C   . VAL   B 1 188 ? -7.514  14.480  11.775  1.00 48.65  ? 194 VAL   B C   1 
ATOM   3757 O  O   . VAL   B 1 188 ? -8.173  14.476  12.816  1.00 47.36  ? 194 VAL   B O   1 
ATOM   3758 C  CB  . VAL   B 1 188 ? -5.147  13.546  12.261  1.00 52.05  ? 194 VAL   B CB  1 
ATOM   3759 C  CG1 . VAL   B 1 188 ? -5.499  12.284  11.460  1.00 51.83  ? 194 VAL   B CG1 1 
ATOM   3760 C  CG2 . VAL   B 1 188 ? -3.655  13.837  12.118  1.00 51.52  ? 194 VAL   B CG2 1 
ATOM   3761 N  N   . TYR   B 1 189 ? -8.064  14.312  10.561  1.00 43.70  ? 195 TYR   B N   1 
ATOM   3762 C  CA  . TYR   B 1 189 ? -9.488  14.053  10.368  1.00 43.09  ? 195 TYR   B CA  1 
ATOM   3763 C  C   . TYR   B 1 189 ? -9.740  12.539  10.277  1.00 43.78  ? 195 TYR   B C   1 
ATOM   3764 O  O   . TYR   B 1 189 ? -8.854  11.799  9.851   1.00 43.35  ? 195 TYR   B O   1 
ATOM   3765 C  CB  . TYR   B 1 189 ? -9.967  14.693  9.064   1.00 45.03  ? 195 TYR   B CB  1 
ATOM   3766 C  CG  . TYR   B 1 189 ? -10.164 16.188  9.113   1.00 47.65  ? 195 TYR   B CG  1 
ATOM   3767 C  CD1 . TYR   B 1 189 ? -9.117  17.057  8.824   1.00 49.94  ? 195 TYR   B CD1 1 
ATOM   3768 C  CD2 . TYR   B 1 189 ? -11.422 16.735  9.332   1.00 48.35  ? 195 TYR   B CD2 1 
ATOM   3769 C  CE1 . TYR   B 1 189 ? -9.301  18.438  8.835   1.00 51.87  ? 195 TYR   B CE1 1 
ATOM   3770 C  CE2 . TYR   B 1 189 ? -11.618 18.113  9.351   1.00 49.40  ? 195 TYR   B CE2 1 
ATOM   3771 C  CZ  . TYR   B 1 189 ? -10.559 18.961  9.084   1.00 56.64  ? 195 TYR   B CZ  1 
ATOM   3772 O  OH  . TYR   B 1 189 ? -10.768 20.317  9.043   1.00 55.58  ? 195 TYR   B OH  1 
ATOM   3773 N  N   . ILE   B 1 190 ? -10.960 12.096  10.626  1.00 39.79  ? 196 ILE   B N   1 
ATOM   3774 C  CA  . ILE   B 1 190 ? -11.375 10.688  10.545  1.00 39.02  ? 196 ILE   B CA  1 
ATOM   3775 C  C   . ILE   B 1 190 ? -12.860 10.616  10.163  1.00 44.50  ? 196 ILE   B C   1 
ATOM   3776 O  O   . ILE   B 1 190 ? -13.689 11.221  10.835  1.00 45.17  ? 196 ILE   B O   1 
ATOM   3777 C  CB  . ILE   B 1 190 ? -11.061 9.863   11.846  1.00 41.26  ? 196 ILE   B CB  1 
ATOM   3778 C  CG1 . ILE   B 1 190 ? -9.549  9.857   12.196  1.00 41.03  ? 196 ILE   B CG1 1 
ATOM   3779 C  CG2 . ILE   B 1 190 ? -11.588 8.413   11.714  1.00 40.46  ? 196 ILE   B CG2 1 
ATOM   3780 C  CD1 . ILE   B 1 190 ? -9.170  9.387   13.635  1.00 47.30  ? 196 ILE   B CD1 1 
ATOM   3781 N  N   . GLY   B 1 191 ? -13.178 9.877   9.096   1.00 40.57  ? 197 GLY   B N   1 
ATOM   3782 C  CA  . GLY   B 1 191 ? -14.557 9.646   8.678   1.00 39.73  ? 197 GLY   B CA  1 
ATOM   3783 C  C   . GLY   B 1 191 ? -15.101 10.436  7.502   1.00 41.46  ? 197 GLY   B C   1 
ATOM   3784 O  O   . GLY   B 1 191 ? -16.287 10.305  7.177   1.00 38.64  ? 197 GLY   B O   1 
ATOM   3785 N  N   . LEU   B 1 192 ? -14.255 11.278  6.888   1.00 40.31  ? 198 LEU   B N   1 
ATOM   3786 C  CA  . LEU   B 1 192 ? -14.592 12.160  5.742   1.00 41.77  ? 198 LEU   B CA  1 
ATOM   3787 C  C   . LEU   B 1 192 ? -15.243 11.432  4.565   1.00 46.77  ? 198 LEU   B C   1 
ATOM   3788 O  O   . LEU   B 1 192 ? -14.697 10.440  4.078   1.00 45.18  ? 198 LEU   B O   1 
ATOM   3789 C  CB  . LEU   B 1 192 ? -13.346 12.932  5.246   1.00 41.99  ? 198 LEU   B CB  1 
ATOM   3790 C  CG  . LEU   B 1 192 ? -12.606 13.866  6.234   1.00 47.39  ? 198 LEU   B CG  1 
ATOM   3791 C  CD1 . LEU   B 1 192 ? -11.498 14.628  5.526   1.00 47.79  ? 198 LEU   B CD1 1 
ATOM   3792 C  CD2 . LEU   B 1 192 ? -13.553 14.856  6.900   1.00 48.18  ? 198 LEU   B CD2 1 
ATOM   3793 N  N   . ARG   B 1 193 ? -16.430 11.909  4.138   1.00 45.63  ? 199 ARG   B N   1 
ATOM   3794 C  CA  . ARG   B 1 193 ? -17.173 11.340  3.010   1.00 46.62  ? 199 ARG   B CA  1 
ATOM   3795 C  C   . ARG   B 1 193 ? -18.029 12.377  2.217   1.00 52.92  ? 199 ARG   B C   1 
ATOM   3796 O  O   . ARG   B 1 193 ? -18.607 12.027  1.185   1.00 52.11  ? 199 ARG   B O   1 
ATOM   3797 C  CB  . ARG   B 1 193 ? -18.012 10.136  3.437   1.00 46.15  ? 199 ARG   B CB  1 
ATOM   3798 C  CG  . ARG   B 1 193 ? -19.127 10.410  4.436   1.00 49.60  ? 199 ARG   B CG  1 
ATOM   3799 C  CD  . ARG   B 1 193 ? -19.680 9.074   4.865   1.00 44.16  ? 199 ARG   B CD  1 
ATOM   3800 N  NE  . ARG   B 1 193 ? -20.787 9.162   5.809   1.00 44.62  ? 199 ARG   B NE  1 
ATOM   3801 C  CZ  . ARG   B 1 193 ? -20.649 9.345   7.120   1.00 51.19  ? 199 ARG   B CZ  1 
ATOM   3802 N  NH1 . ARG   B 1 193 ? -19.442 9.509   7.654   1.00 33.06  ? 199 ARG   B NH1 1 
ATOM   3803 N  NH2 . ARG   B 1 193 ? -21.715 9.360   7.907   1.00 34.25  ? 199 ARG   B NH2 1 
ATOM   3804 N  N   . ASP   B 1 194 ? -18.091 13.636  2.695   1.00 51.72  ? 200 ASP   B N   1 
ATOM   3805 C  CA  . ASP   B 1 194 ? -18.827 14.733  2.054   1.00 51.92  ? 200 ASP   B CA  1 
ATOM   3806 C  C   . ASP   B 1 194 ? -17.962 15.987  2.131   1.00 57.43  ? 200 ASP   B C   1 
ATOM   3807 O  O   . ASP   B 1 194 ? -18.125 16.821  3.025   1.00 58.07  ? 200 ASP   B O   1 
ATOM   3808 C  CB  . ASP   B 1 194 ? -20.212 14.927  2.701   1.00 53.96  ? 200 ASP   B CB  1 
ATOM   3809 C  CG  . ASP   B 1 194 ? -21.123 15.973  2.070   1.00 67.09  ? 200 ASP   B CG  1 
ATOM   3810 O  OD1 . ASP   B 1 194 ? -20.738 16.554  1.031   1.00 68.83  ? 200 ASP   B OD1 1 
ATOM   3811 O  OD2 . ASP   B 1 194 ? -22.241 16.179  2.594   1.00 71.32  ? 200 ASP   B OD2 1 
ATOM   3812 N  N   . VAL   B 1 195 ? -16.994 16.071  1.209   1.00 53.94  ? 201 VAL   B N   1 
ATOM   3813 C  CA  . VAL   B 1 195 ? -16.018 17.148  1.091   1.00 53.45  ? 201 VAL   B CA  1 
ATOM   3814 C  C   . VAL   B 1 195 ? -16.346 18.014  -0.164  1.00 58.74  ? 201 VAL   B C   1 
ATOM   3815 O  O   . VAL   B 1 195 ? -16.363 17.502  -1.288  1.00 57.84  ? 201 VAL   B O   1 
ATOM   3816 C  CB  . VAL   B 1 195 ? -14.570 16.562  1.066   1.00 56.73  ? 201 VAL   B CB  1 
ATOM   3817 C  CG1 . VAL   B 1 195 ? -13.512 17.652  0.934   1.00 56.05  ? 201 VAL   B CG1 1 
ATOM   3818 C  CG2 . VAL   B 1 195 ? -14.295 15.690  2.297   1.00 56.55  ? 201 VAL   B CG2 1 
ATOM   3819 N  N   . ASP   B 1 196 ? -16.617 19.318  0.051   1.00 55.75  ? 202 ASP   B N   1 
ATOM   3820 C  CA  . ASP   B 1 196 ? -16.886 20.292  -1.014  1.00 55.43  ? 202 ASP   B CA  1 
ATOM   3821 C  C   . ASP   B 1 196 ? -15.570 20.586  -1.774  1.00 57.45  ? 202 ASP   B C   1 
ATOM   3822 O  O   . ASP   B 1 196 ? -14.497 20.491  -1.164  1.00 55.54  ? 202 ASP   B O   1 
ATOM   3823 C  CB  . ASP   B 1 196 ? -17.488 21.585  -0.428  1.00 57.45  ? 202 ASP   B CB  1 
ATOM   3824 C  CG  . ASP   B 1 196 ? -18.909 21.447  0.105   1.00 69.67  ? 202 ASP   B CG  1 
ATOM   3825 O  OD1 . ASP   B 1 196 ? -19.619 20.499  -0.315  1.00 69.69  ? 202 ASP   B OD1 1 
ATOM   3826 O  OD2 . ASP   B 1 196 ? -19.327 22.312  0.903   1.00 77.64  ? 202 ASP   B OD2 1 
ATOM   3827 N  N   . PRO   B 1 197 ? -15.607 20.914  -3.097  1.00 54.48  ? 203 PRO   B N   1 
ATOM   3828 C  CA  . PRO   B 1 197 ? -14.342 21.151  -3.828  1.00 54.53  ? 203 PRO   B CA  1 
ATOM   3829 C  C   . PRO   B 1 197 ? -13.361 22.141  -3.162  1.00 58.75  ? 203 PRO   B C   1 
ATOM   3830 O  O   . PRO   B 1 197 ? -12.178 21.776  -3.093  1.00 58.02  ? 203 PRO   B O   1 
ATOM   3831 C  CB  . PRO   B 1 197 ? -14.801 21.604  -5.218  1.00 56.45  ? 203 PRO   B CB  1 
ATOM   3832 C  CG  . PRO   B 1 197 ? -16.176 21.029  -5.362  1.00 60.51  ? 203 PRO   B CG  1 
ATOM   3833 C  CD  . PRO   B 1 197 ? -16.778 21.047  -3.991  1.00 55.86  ? 203 PRO   B CD  1 
ATOM   3834 N  N   . PRO   B 1 198 ? -13.753 23.324  -2.603  1.00 56.07  ? 204 PRO   B N   1 
ATOM   3835 C  CA  . PRO   B 1 198 ? -12.731 24.176  -1.958  1.00 56.48  ? 204 PRO   B CA  1 
ATOM   3836 C  C   . PRO   B 1 198 ? -12.058 23.540  -0.726  1.00 60.64  ? 204 PRO   B C   1 
ATOM   3837 O  O   . PRO   B 1 198 ? -10.849 23.728  -0.535  1.00 60.72  ? 204 PRO   B O   1 
ATOM   3838 C  CB  . PRO   B 1 198 ? -13.483 25.469  -1.639  1.00 58.22  ? 204 PRO   B CB  1 
ATOM   3839 C  CG  . PRO   B 1 198 ? -14.914 25.107  -1.608  1.00 62.50  ? 204 PRO   B CG  1 
ATOM   3840 C  CD  . PRO   B 1 198 ? -15.087 23.970  -2.565  1.00 57.93  ? 204 PRO   B CD  1 
ATOM   3841 N  N   . GLU   B 1 199 ? -12.814 22.731  0.061   1.00 56.73  ? 205 GLU   B N   1 
ATOM   3842 C  CA  . GLU   B 1 199 ? -12.299 21.989  1.232   1.00 55.98  ? 205 GLU   B CA  1 
ATOM   3843 C  C   . GLU   B 1 199 ? -11.187 21.008  0.797   1.00 60.41  ? 205 GLU   B C   1 
ATOM   3844 O  O   . GLU   B 1 199 ? -10.113 21.003  1.407   1.00 58.71  ? 205 GLU   B O   1 
ATOM   3845 C  CB  . GLU   B 1 199 ? -13.434 21.244  1.972   1.00 56.90  ? 205 GLU   B CB  1 
ATOM   3846 C  CG  . GLU   B 1 199 ? -14.358 22.136  2.785   1.00 61.63  ? 205 GLU   B CG  1 
ATOM   3847 C  CD  . GLU   B 1 199 ? -15.578 21.477  3.409   1.00 69.87  ? 205 GLU   B CD  1 
ATOM   3848 O  OE1 . GLU   B 1 199 ? -16.296 20.746  2.688   1.00 52.08  ? 205 GLU   B OE1 1 
ATOM   3849 O  OE2 . GLU   B 1 199 ? -15.868 21.769  4.594   1.00 54.47  ? 205 GLU   B OE2 1 
ATOM   3850 N  N   . HIS   B 1 200 ? -11.423 20.237  -0.301  1.00 59.30  ? 206 HIS   B N   1 
ATOM   3851 C  CA  . HIS   B 1 200 ? -10.472 19.267  -0.872  1.00 60.35  ? 206 HIS   B CA  1 
ATOM   3852 C  C   . HIS   B 1 200 ? -9.143  19.917  -1.281  1.00 65.66  ? 206 HIS   B C   1 
ATOM   3853 O  O   . HIS   B 1 200 ? -8.079  19.330  -1.058  1.00 64.32  ? 206 HIS   B O   1 
ATOM   3854 C  CB  . HIS   B 1 200 ? -11.102 18.501  -2.055  1.00 61.78  ? 206 HIS   B CB  1 
ATOM   3855 C  CG  . HIS   B 1 200 ? -10.200 17.467  -2.662  1.00 65.84  ? 206 HIS   B CG  1 
ATOM   3856 N  ND1 . HIS   B 1 200 ? -10.061 16.208  -2.099  1.00 68.14  ? 206 HIS   B ND1 1 
ATOM   3857 C  CD2 . HIS   B 1 200 ? -9.404  17.545  -3.756  1.00 67.88  ? 206 HIS   B CD2 1 
ATOM   3858 C  CE1 . HIS   B 1 200 ? -9.186  15.567  -2.860  1.00 67.46  ? 206 HIS   B CE1 1 
ATOM   3859 N  NE2 . HIS   B 1 200 ? -8.765  16.329  -3.870  1.00 67.75  ? 206 HIS   B NE2 1 
ATOM   3860 N  N   . PHE   B 1 201 ? -9.209  21.133  -1.876  1.00 64.11  ? 207 PHE   B N   1 
ATOM   3861 C  CA  . PHE   B 1 201 ? -8.030  21.892  -2.297  1.00 64.10  ? 207 PHE   B CA  1 
ATOM   3862 C  C   . PHE   B 1 201 ? -7.186  22.267  -1.070  1.00 65.43  ? 207 PHE   B C   1 
ATOM   3863 O  O   . PHE   B 1 201 ? -5.960  22.115  -1.091  1.00 63.16  ? 207 PHE   B O   1 
ATOM   3864 C  CB  . PHE   B 1 201 ? -8.445  23.147  -3.096  1.00 66.68  ? 207 PHE   B CB  1 
ATOM   3865 C  CG  . PHE   B 1 201 ? -7.284  23.915  -3.686  1.00 69.42  ? 207 PHE   B CG  1 
ATOM   3866 C  CD1 . PHE   B 1 201 ? -6.783  23.594  -4.940  1.00 73.96  ? 207 PHE   B CD1 1 
ATOM   3867 C  CD2 . PHE   B 1 201 ? -6.687  24.954  -2.983  1.00 72.50  ? 207 PHE   B CD2 1 
ATOM   3868 C  CE1 . PHE   B 1 201 ? -5.717  24.312  -5.489  1.00 75.53  ? 207 PHE   B CE1 1 
ATOM   3869 C  CE2 . PHE   B 1 201 ? -5.613  25.661  -3.526  1.00 75.68  ? 207 PHE   B CE2 1 
ATOM   3870 C  CZ  . PHE   B 1 201 ? -5.131  25.331  -4.772  1.00 74.19  ? 207 PHE   B CZ  1 
ATOM   3871 N  N   . ILE   B 1 202 ? -7.855  22.731  0.000   1.00 62.50  ? 208 ILE   B N   1 
ATOM   3872 C  CA  . ILE   B 1 202 ? -7.214  23.116  1.264   1.00 62.58  ? 208 ILE   B CA  1 
ATOM   3873 C  C   . ILE   B 1 202 ? -6.443  21.934  1.872   1.00 65.04  ? 208 ILE   B C   1 
ATOM   3874 O  O   . ILE   B 1 202 ? -5.237  22.061  2.099   1.00 63.70  ? 208 ILE   B O   1 
ATOM   3875 C  CB  . ILE   B 1 202 ? -8.231  23.773  2.249   1.00 66.07  ? 208 ILE   B CB  1 
ATOM   3876 C  CG1 . ILE   B 1 202 ? -8.703  25.145  1.712   1.00 66.92  ? 208 ILE   B CG1 1 
ATOM   3877 C  CG2 . ILE   B 1 202 ? -7.619  23.933  3.637   1.00 67.05  ? 208 ILE   B CG2 1 
ATOM   3878 C  CD1 . ILE   B 1 202 ? -10.069 25.637  2.221   1.00 75.52  ? 208 ILE   B CD1 1 
ATOM   3879 N  N   . LEU   B 1 203 ? -7.127  20.782  2.081   1.00 62.18  ? 209 LEU   B N   1 
ATOM   3880 C  CA  . LEU   B 1 203 ? -6.534  19.565  2.652   1.00 62.55  ? 209 LEU   B CA  1 
ATOM   3881 C  C   . LEU   B 1 203 ? -5.307  19.116  1.878   1.00 67.95  ? 209 LEU   B C   1 
ATOM   3882 O  O   . LEU   B 1 203 ? -4.254  18.905  2.483   1.00 67.83  ? 209 LEU   B O   1 
ATOM   3883 C  CB  . LEU   B 1 203 ? -7.556  18.409  2.738   1.00 62.88  ? 209 LEU   B CB  1 
ATOM   3884 C  CG  . LEU   B 1 203 ? -8.867  18.649  3.507   1.00 67.60  ? 209 LEU   B CG  1 
ATOM   3885 C  CD1 . LEU   B 1 203 ? -9.899  17.605  3.147   1.00 67.55  ? 209 LEU   B CD1 1 
ATOM   3886 C  CD2 . LEU   B 1 203 ? -8.642  18.684  5.023   1.00 70.60  ? 209 LEU   B CD2 1 
ATOM   3887 N  N   . LYS   B 1 204 ? -5.426  19.034  0.533   1.00 65.40  ? 210 LYS   B N   1 
ATOM   3888 C  CA  . LYS   B 1 204 ? -4.348  18.601  -0.360  1.00 65.68  ? 210 LYS   B CA  1 
ATOM   3889 C  C   . LYS   B 1 204 ? -3.159  19.568  -0.424  1.00 69.46  ? 210 LYS   B C   1 
ATOM   3890 O  O   . LYS   B 1 204 ? -2.015  19.120  -0.301  1.00 68.40  ? 210 LYS   B O   1 
ATOM   3891 C  CB  . LYS   B 1 204 ? -4.890  18.299  -1.774  1.00 69.02  ? 210 LYS   B CB  1 
ATOM   3892 C  CG  . LYS   B 1 204 ? -5.744  17.028  -1.871  1.00 88.76  ? 210 LYS   B CG  1 
ATOM   3893 C  CD  . LYS   B 1 204 ? -4.907  15.746  -1.930  1.00 100.44 ? 210 LYS   B CD  1 
ATOM   3894 C  CE  . LYS   B 1 204 ? -5.756  14.506  -1.817  1.00 112.50 ? 210 LYS   B CE  1 
ATOM   3895 N  NZ  . LYS   B 1 204 ? -4.925  13.275  -1.789  1.00 122.25 ? 210 LYS   B NZ  1 
ATOM   3896 N  N   . ASN   B 1 205 ? -3.423  20.882  -0.606  1.00 66.53  ? 211 ASN   B N   1 
ATOM   3897 C  CA  . ASN   B 1 205 ? -2.371  21.899  -0.734  1.00 66.90  ? 211 ASN   B CA  1 
ATOM   3898 C  C   . ASN   B 1 205 ? -1.622  22.224  0.559   1.00 72.34  ? 211 ASN   B C   1 
ATOM   3899 O  O   . ASN   B 1 205 ? -0.408  22.454  0.498   1.00 72.22  ? 211 ASN   B O   1 
ATOM   3900 C  CB  . ASN   B 1 205 ? -2.911  23.176  -1.366  1.00 67.61  ? 211 ASN   B CB  1 
ATOM   3901 C  CG  . ASN   B 1 205 ? -3.000  23.092  -2.869  1.00 87.65  ? 211 ASN   B CG  1 
ATOM   3902 O  OD1 . ASN   B 1 205 ? -3.960  22.552  -3.434  1.00 74.38  ? 211 ASN   B OD1 1 
ATOM   3903 N  ND2 . ASN   B 1 205 ? -1.979  23.604  -3.548  1.00 81.12  ? 211 ASN   B ND2 1 
ATOM   3904 N  N   . TYR   B 1 206 ? -2.326  22.256  1.716   1.00 69.55  ? 212 TYR   B N   1 
ATOM   3905 C  CA  . TYR   B 1 206 ? -1.701  22.574  3.006   1.00 69.46  ? 212 TYR   B CA  1 
ATOM   3906 C  C   . TYR   B 1 206 ? -1.148  21.336  3.750   1.00 70.93  ? 212 TYR   B C   1 
ATOM   3907 O  O   . TYR   B 1 206 ? -0.667  21.472  4.880   1.00 70.40  ? 212 TYR   B O   1 
ATOM   3908 C  CB  . TYR   B 1 206 ? -2.646  23.401  3.897   1.00 71.45  ? 212 TYR   B CB  1 
ATOM   3909 C  CG  . TYR   B 1 206 ? -2.959  24.774  3.341   1.00 74.36  ? 212 TYR   B CG  1 
ATOM   3910 C  CD1 . TYR   B 1 206 ? -2.057  25.827  3.478   1.00 76.61  ? 212 TYR   B CD1 1 
ATOM   3911 C  CD2 . TYR   B 1 206 ? -4.166  25.029  2.697   1.00 75.64  ? 212 TYR   B CD2 1 
ATOM   3912 C  CE1 . TYR   B 1 206 ? -2.343  27.097  2.974   1.00 78.00  ? 212 TYR   B CE1 1 
ATOM   3913 C  CE2 . TYR   B 1 206 ? -4.463  26.292  2.185   1.00 77.01  ? 212 TYR   B CE2 1 
ATOM   3914 C  CZ  . TYR   B 1 206 ? -3.550  27.326  2.331   1.00 85.92  ? 212 TYR   B CZ  1 
ATOM   3915 O  OH  . TYR   B 1 206 ? -3.840  28.572  1.824   1.00 87.53  ? 212 TYR   B OH  1 
ATOM   3916 N  N   . ASP   B 1 207 ? -1.164  20.152  3.085   1.00 65.20  ? 213 ASP   B N   1 
ATOM   3917 C  CA  . ASP   B 1 207 ? -0.666  18.859  3.581   1.00 64.11  ? 213 ASP   B CA  1 
ATOM   3918 C  C   . ASP   B 1 207 ? -1.346  18.422  4.909   1.00 63.07  ? 213 ASP   B C   1 
ATOM   3919 O  O   . ASP   B 1 207 ? -0.703  17.867  5.806   1.00 61.85  ? 213 ASP   B O   1 
ATOM   3920 C  CB  . ASP   B 1 207 ? 0.879   18.849  3.669   1.00 66.89  ? 213 ASP   B CB  1 
ATOM   3921 C  CG  . ASP   B 1 207 ? 1.537   17.476  3.656   1.00 84.39  ? 213 ASP   B CG  1 
ATOM   3922 O  OD1 . ASP   B 1 207 ? 0.928   16.524  3.106   1.00 86.49  ? 213 ASP   B OD1 1 
ATOM   3923 O  OD2 . ASP   B 1 207 ? 2.675   17.359  4.164   1.00 91.72  ? 213 ASP   B OD2 1 
ATOM   3924 N  N   . ILE   B 1 208 ? -2.661  18.676  5.007   1.00 57.14  ? 214 ILE   B N   1 
ATOM   3925 C  CA  . ILE   B 1 208 ? -3.484  18.302  6.154   1.00 56.55  ? 214 ILE   B CA  1 
ATOM   3926 C  C   . ILE   B 1 208 ? -3.784  16.796  6.032   1.00 58.88  ? 214 ILE   B C   1 
ATOM   3927 O  O   . ILE   B 1 208 ? -4.536  16.388  5.141   1.00 57.83  ? 214 ILE   B O   1 
ATOM   3928 C  CB  . ILE   B 1 208 ? -4.772  19.178  6.263   1.00 59.47  ? 214 ILE   B CB  1 
ATOM   3929 C  CG1 . ILE   B 1 208 ? -4.418  20.694  6.330   1.00 60.06  ? 214 ILE   B CG1 1 
ATOM   3930 C  CG2 . ILE   B 1 208 ? -5.632  18.753  7.468   1.00 59.48  ? 214 ILE   B CG2 1 
ATOM   3931 C  CD1 . ILE   B 1 208 ? -5.462  21.628  5.752   1.00 63.35  ? 214 ILE   B CD1 1 
ATOM   3932 N  N   . GLN   B 1 209 ? -3.154  15.983  6.914   1.00 53.85  ? 215 GLN   B N   1 
ATOM   3933 C  CA  . GLN   B 1 209 ? -3.303  14.524  6.963   1.00 52.65  ? 215 GLN   B CA  1 
ATOM   3934 C  C   . GLN   B 1 209 ? -4.729  14.112  7.363   1.00 53.16  ? 215 GLN   B C   1 
ATOM   3935 O  O   . GLN   B 1 209 ? -5.273  14.636  8.333   1.00 53.69  ? 215 GLN   B O   1 
ATOM   3936 C  CB  . GLN   B 1 209 ? -2.261  13.902  7.909   1.00 53.92  ? 215 GLN   B CB  1 
ATOM   3937 C  CG  . GLN   B 1 209 ? -0.803  14.075  7.459   1.00 73.61  ? 215 GLN   B CG  1 
ATOM   3938 C  CD  . GLN   B 1 209 ? -0.441  13.281  6.221   1.00 98.01  ? 215 GLN   B CD  1 
ATOM   3939 O  OE1 . GLN   B 1 209 ? -0.657  12.066  6.137   1.00 96.10  ? 215 GLN   B OE1 1 
ATOM   3940 N  NE2 . GLN   B 1 209 ? 0.159   13.948  5.249   1.00 91.40  ? 215 GLN   B NE2 1 
ATOM   3941 N  N   . TYR   B 1 210 ? -5.348  13.203  6.597   1.00 46.60  ? 216 TYR   B N   1 
ATOM   3942 C  CA  . TYR   B 1 210 ? -6.706  12.746  6.895   1.00 45.42  ? 216 TYR   B CA  1 
ATOM   3943 C  C   . TYR   B 1 210 ? -6.944  11.278  6.558   1.00 46.23  ? 216 TYR   B C   1 
ATOM   3944 O  O   . TYR   B 1 210 ? -6.197  10.676  5.780   1.00 45.41  ? 216 TYR   B O   1 
ATOM   3945 C  CB  . TYR   B 1 210 ? -7.782  13.643  6.248   1.00 47.23  ? 216 TYR   B CB  1 
ATOM   3946 C  CG  . TYR   B 1 210 ? -7.860  13.591  4.734   1.00 50.75  ? 216 TYR   B CG  1 
ATOM   3947 C  CD1 . TYR   B 1 210 ? -7.106  14.460  3.948   1.00 53.02  ? 216 TYR   B CD1 1 
ATOM   3948 C  CD2 . TYR   B 1 210 ? -8.745  12.727  4.089   1.00 51.28  ? 216 TYR   B CD2 1 
ATOM   3949 C  CE1 . TYR   B 1 210 ? -7.209  14.451  2.556   1.00 54.50  ? 216 TYR   B CE1 1 
ATOM   3950 C  CE2 . TYR   B 1 210 ? -8.850  12.703  2.699   1.00 52.35  ? 216 TYR   B CE2 1 
ATOM   3951 C  CZ  . TYR   B 1 210 ? -8.081  13.569  1.934   1.00 60.25  ? 216 TYR   B CZ  1 
ATOM   3952 O  OH  . TYR   B 1 210 ? -8.193  13.562  0.561   1.00 58.88  ? 216 TYR   B OH  1 
ATOM   3953 N  N   . PHE   B 1 211 ? -8.007  10.719  7.157   1.00 41.44  ? 217 PHE   B N   1 
ATOM   3954 C  CA  . PHE   B 1 211 ? -8.447  9.343   6.956   1.00 39.35  ? 217 PHE   B CA  1 
ATOM   3955 C  C   . PHE   B 1 211 ? -9.927  9.334   6.630   1.00 41.73  ? 217 PHE   B C   1 
ATOM   3956 O  O   . PHE   B 1 211 ? -10.764 9.335   7.534   1.00 41.52  ? 217 PHE   B O   1 
ATOM   3957 C  CB  . PHE   B 1 211 ? -8.085  8.454   8.159   1.00 39.99  ? 217 PHE   B CB  1 
ATOM   3958 C  CG  . PHE   B 1 211 ? -6.596  8.333   8.391   1.00 39.91  ? 217 PHE   B CG  1 
ATOM   3959 C  CD1 . PHE   B 1 211 ? -5.839  7.401   7.691   1.00 41.28  ? 217 PHE   B CD1 1 
ATOM   3960 C  CD2 . PHE   B 1 211 ? -5.955  9.133   9.333   1.00 41.32  ? 217 PHE   B CD2 1 
ATOM   3961 C  CE1 . PHE   B 1 211 ? -4.457  7.309   7.888   1.00 41.68  ? 217 PHE   B CE1 1 
ATOM   3962 C  CE2 . PHE   B 1 211 ? -4.576  9.027   9.542   1.00 43.65  ? 217 PHE   B CE2 1 
ATOM   3963 C  CZ  . PHE   B 1 211 ? -3.838  8.113   8.823   1.00 41.66  ? 217 PHE   B CZ  1 
ATOM   3964 N  N   . SER   B 1 212 ? -10.264 9.365   5.310   1.00 36.23  ? 218 SER   B N   1 
ATOM   3965 C  CA  . SER   B 1 212 ? -11.667 9.360   4.851   1.00 34.99  ? 218 SER   B CA  1 
ATOM   3966 C  C   . SER   B 1 212 ? -12.252 7.942   5.016   1.00 36.17  ? 218 SER   B C   1 
ATOM   3967 O  O   . SER   B 1 212 ? -11.512 7.035   5.354   1.00 36.61  ? 218 SER   B O   1 
ATOM   3968 C  CB  . SER   B 1 212 ? -11.740 9.772   3.377   1.00 39.52  ? 218 SER   B CB  1 
ATOM   3969 O  OG  . SER   B 1 212 ? -11.208 8.782   2.504   1.00 45.73  ? 218 SER   B OG  1 
ATOM   3970 N  N   . MET   B 1 213 ? -13.541 7.746   4.714   1.00 32.91  ? 219 MET   B N   1 
ATOM   3971 C  CA  . MET   B 1 213 ? -14.196 6.432   4.744   1.00 32.84  ? 219 MET   B CA  1 
ATOM   3972 C  C   . MET   B 1 213 ? -13.464 5.441   3.859   1.00 39.08  ? 219 MET   B C   1 
ATOM   3973 O  O   . MET   B 1 213 ? -13.274 4.299   4.267   1.00 38.71  ? 219 MET   B O   1 
ATOM   3974 C  CB  . MET   B 1 213 ? -15.665 6.530   4.331   1.00 34.32  ? 219 MET   B CB  1 
ATOM   3975 C  CG  . MET   B 1 213 ? -16.556 7.231   5.340   1.00 37.20  ? 219 MET   B CG  1 
ATOM   3976 S  SD  . MET   B 1 213 ? -16.335 6.838   7.113   1.00 39.27  ? 219 MET   B SD  1 
ATOM   3977 C  CE  . MET   B 1 213 ? -16.340 5.037   7.099   1.00 35.82  ? 219 MET   B CE  1 
ATOM   3978 N  N   . ARG   B 1 214 ? -12.958 5.914   2.687   1.00 36.70  ? 220 ARG   B N   1 
ATOM   3979 C  CA  . ARG   B 1 214 ? -12.183 5.114   1.751   1.00 35.82  ? 220 ARG   B CA  1 
ATOM   3980 C  C   . ARG   B 1 214 ? -10.882 4.631   2.405   1.00 38.33  ? 220 ARG   B C   1 
ATOM   3981 O  O   . ARG   B 1 214 ? -10.540 3.469   2.263   1.00 36.98  ? 220 ARG   B O   1 
ATOM   3982 C  CB  . ARG   B 1 214 ? -11.928 5.898   0.452   1.00 36.08  ? 220 ARG   B CB  1 
ATOM   3983 C  CG  . ARG   B 1 214 ? -11.282 5.056   -0.614  1.00 41.34  ? 220 ARG   B CG  1 
ATOM   3984 C  CD  . ARG   B 1 214 ? -10.619 5.915   -1.647  1.00 44.20  ? 220 ARG   B CD  1 
ATOM   3985 N  NE  . ARG   B 1 214 ? -9.405  5.275   -2.131  1.00 46.37  ? 220 ARG   B NE  1 
ATOM   3986 C  CZ  . ARG   B 1 214 ? -9.367  4.424   -3.147  1.00 62.87  ? 220 ARG   B CZ  1 
ATOM   3987 N  NH1 . ARG   B 1 214 ? -10.486 4.095   -3.793  1.00 51.13  ? 220 ARG   B NH1 1 
ATOM   3988 N  NH2 . ARG   B 1 214 ? -8.215  3.885   -3.521  1.00 50.04  ? 220 ARG   B NH2 1 
ATOM   3989 N  N   . ASP   B 1 215 ? -10.180 5.506   3.141   1.00 36.66  ? 221 ASP   B N   1 
ATOM   3990 C  CA  . ASP   B 1 215 ? -8.955  5.158   3.877   1.00 37.09  ? 221 ASP   B CA  1 
ATOM   3991 C  C   . ASP   B 1 215 ? -9.225  4.103   4.987   1.00 39.61  ? 221 ASP   B C   1 
ATOM   3992 O  O   . ASP   B 1 215 ? -8.410  3.200   5.186   1.00 40.07  ? 221 ASP   B O   1 
ATOM   3993 C  CB  . ASP   B 1 215 ? -8.341  6.417   4.498   1.00 39.84  ? 221 ASP   B CB  1 
ATOM   3994 C  CG  . ASP   B 1 215 ? -7.682  7.336   3.488   1.00 48.17  ? 221 ASP   B CG  1 
ATOM   3995 O  OD1 . ASP   B 1 215 ? -6.637  6.948   2.932   1.00 49.84  ? 221 ASP   B OD1 1 
ATOM   3996 O  OD2 . ASP   B 1 215 ? -8.197  8.451   3.282   1.00 52.20  ? 221 ASP   B OD2 1 
ATOM   3997 N  N   . ILE   B 1 216 ? -10.354 4.238   5.705   1.00 35.38  ? 222 ILE   B N   1 
ATOM   3998 C  CA  . ILE   B 1 216 ? -10.787 3.310   6.760   1.00 35.05  ? 222 ILE   B CA  1 
ATOM   3999 C  C   . ILE   B 1 216 ? -11.089 1.954   6.076   1.00 37.78  ? 222 ILE   B C   1 
ATOM   4000 O  O   . ILE   B 1 216 ? -10.684 0.920   6.598   1.00 36.28  ? 222 ILE   B O   1 
ATOM   4001 C  CB  . ILE   B 1 216 ? -12.006 3.876   7.563   1.00 37.96  ? 222 ILE   B CB  1 
ATOM   4002 C  CG1 . ILE   B 1 216 ? -11.636 5.201   8.307   1.00 37.21  ? 222 ILE   B CG1 1 
ATOM   4003 C  CG2 . ILE   B 1 216 ? -12.574 2.846   8.576   1.00 37.96  ? 222 ILE   B CG2 1 
ATOM   4004 C  CD1 . ILE   B 1 216 ? -12.865 6.020   8.701   1.00 34.88  ? 222 ILE   B CD1 1 
ATOM   4005 N  N   . ASP   B 1 217 ? -11.733 1.982   4.876   1.00 34.77  ? 223 ASP   B N   1 
ATOM   4006 C  CA  . ASP   B 1 217 ? -12.047 0.777   4.074   1.00 34.03  ? 223 ASP   B CA  1 
ATOM   4007 C  C   . ASP   B 1 217 ? -10.797 -0.043  3.736   1.00 38.13  ? 223 ASP   B C   1 
ATOM   4008 O  O   . ASP   B 1 217 ? -10.830 -1.266  3.834   1.00 37.02  ? 223 ASP   B O   1 
ATOM   4009 C  CB  . ASP   B 1 217 ? -12.788 1.153   2.787   1.00 34.61  ? 223 ASP   B CB  1 
ATOM   4010 C  CG  . ASP   B 1 217 ? -14.195 1.673   2.975   1.00 36.26  ? 223 ASP   B CG  1 
ATOM   4011 O  OD1 . ASP   B 1 217 ? -14.816 1.345   4.004   1.00 36.25  ? 223 ASP   B OD1 1 
ATOM   4012 O  OD2 . ASP   B 1 217 ? -14.697 2.368   2.062   1.00 38.19  ? 223 ASP   B OD2 1 
ATOM   4013 N  N   . ARG   B 1 218 ? -9.685  0.644   3.414   1.00 35.99  ? 224 ARG   B N   1 
ATOM   4014 C  CA  . ARG   B 1 218 ? -8.388  0.073   3.038   1.00 35.38  ? 224 ARG   B CA  1 
ATOM   4015 C  C   . ARG   B 1 218 ? -7.541  -0.363  4.215   1.00 40.71  ? 224 ARG   B C   1 
ATOM   4016 O  O   . ARG   B 1 218 ? -7.016  -1.483  4.229   1.00 40.35  ? 224 ARG   B O   1 
ATOM   4017 C  CB  . ARG   B 1 218 ? -7.586  1.101   2.209   1.00 35.83  ? 224 ARG   B CB  1 
ATOM   4018 C  CG  . ARG   B 1 218 ? -8.145  1.407   0.813   1.00 43.52  ? 224 ARG   B CG  1 
ATOM   4019 C  CD  . ARG   B 1 218 ? -7.452  2.579   0.103   1.00 39.08  ? 224 ARG   B CD  1 
ATOM   4020 N  NE  . ARG   B 1 218 ? -5.991  2.429   0.043   1.00 45.37  ? 224 ARG   B NE  1 
ATOM   4021 C  CZ  . ARG   B 1 218 ? -5.327  1.782   -0.910  1.00 60.98  ? 224 ARG   B CZ  1 
ATOM   4022 N  NH1 . ARG   B 1 218 ? -5.981  1.201   -1.910  1.00 52.16  ? 224 ARG   B NH1 1 
ATOM   4023 N  NH2 . ARG   B 1 218 ? -4.005  1.703   -0.867  1.00 47.09  ? 224 ARG   B NH2 1 
ATOM   4024 N  N   . LEU   B 1 219 ? -7.331  0.553   5.181   1.00 38.42  ? 225 LEU   B N   1 
ATOM   4025 C  CA  . LEU   B 1 219 ? -6.448  0.302   6.317   1.00 38.39  ? 225 LEU   B CA  1 
ATOM   4026 C  C   . LEU   B 1 219 ? -7.091  -0.425  7.497   1.00 40.06  ? 225 LEU   B C   1 
ATOM   4027 O  O   . LEU   B 1 219 ? -6.415  -1.176  8.186   1.00 40.24  ? 225 LEU   B O   1 
ATOM   4028 C  CB  . LEU   B 1 219 ? -5.833  1.640   6.812   1.00 38.69  ? 225 LEU   B CB  1 
ATOM   4029 C  CG  . LEU   B 1 219 ? -4.940  2.432   5.840   1.00 43.57  ? 225 LEU   B CG  1 
ATOM   4030 C  CD1 . LEU   B 1 219 ? -4.880  3.894   6.235   1.00 44.29  ? 225 LEU   B CD1 1 
ATOM   4031 C  CD2 . LEU   B 1 219 ? -3.538  1.865   5.780   1.00 44.91  ? 225 LEU   B CD2 1 
ATOM   4032 N  N   . GLY   B 1 220 ? -8.357  -0.149  7.757   1.00 37.14  ? 226 GLY   B N   1 
ATOM   4033 C  CA  . GLY   B 1 220 ? -9.042  -0.658  8.935   1.00 37.06  ? 226 GLY   B CA  1 
ATOM   4034 C  C   . GLY   B 1 220 ? -8.882  0.348   10.073  1.00 40.33  ? 226 GLY   B C   1 
ATOM   4035 O  O   . GLY   B 1 220 ? -7.852  1.033   10.164  1.00 38.68  ? 226 GLY   B O   1 
ATOM   4036 N  N   . ILE   B 1 221 ? -9.884  0.427   10.959  1.00 36.46  ? 227 ILE   B N   1 
ATOM   4037 C  CA  . ILE   B 1 221 ? -9.908  1.377   12.077  1.00 35.85  ? 227 ILE   B CA  1 
ATOM   4038 C  C   . ILE   B 1 221 ? -8.670  1.255   13.021  1.00 40.41  ? 227 ILE   B C   1 
ATOM   4039 O  O   . ILE   B 1 221 ? -8.216  2.297   13.492  1.00 40.73  ? 227 ILE   B O   1 
ATOM   4040 C  CB  . ILE   B 1 221 ? -11.263 1.373   12.846  1.00 37.88  ? 227 ILE   B CB  1 
ATOM   4041 C  CG1 . ILE   B 1 221 ? -11.506 2.711   13.600  1.00 37.70  ? 227 ILE   B CG1 1 
ATOM   4042 C  CG2 . ILE   B 1 221 ? -11.457 0.149   13.766  1.00 37.64  ? 227 ILE   B CG2 1 
ATOM   4043 C  CD1 . ILE   B 1 221 ? -11.807 3.980   12.664  1.00 41.39  ? 227 ILE   B CD1 1 
ATOM   4044 N  N   . GLN   B 1 222 ? -8.092  0.038   13.230  1.00 35.99  ? 228 GLN   B N   1 
ATOM   4045 C  CA  . GLN   B 1 222 ? -6.912  -0.144  14.088  1.00 36.22  ? 228 GLN   B CA  1 
ATOM   4046 C  C   . GLN   B 1 222 ? -5.689  0.618   13.538  1.00 41.11  ? 228 GLN   B C   1 
ATOM   4047 O  O   . GLN   B 1 222 ? -5.048  1.357   14.290  1.00 40.91  ? 228 GLN   B O   1 
ATOM   4048 C  CB  . GLN   B 1 222 ? -6.581  -1.632  14.322  1.00 36.84  ? 228 GLN   B CB  1 
ATOM   4049 C  CG  . GLN   B 1 222 ? -5.421  -1.841  15.309  1.00 43.23  ? 228 GLN   B CG  1 
ATOM   4050 C  CD  . GLN   B 1 222 ? -4.696  -3.156  15.234  1.00 58.12  ? 228 GLN   B CD  1 
ATOM   4051 O  OE1 . GLN   B 1 222 ? -3.508  -3.230  15.541  1.00 53.68  ? 228 GLN   B OE1 1 
ATOM   4052 N  NE2 . GLN   B 1 222 ? -5.384  -4.237  14.890  1.00 49.22  ? 228 GLN   B NE2 1 
ATOM   4053 N  N   . LYS   B 1 223 ? -5.379  0.431   12.240  1.00 37.48  ? 229 LYS   B N   1 
ATOM   4054 C  CA  . LYS   B 1 223 ? -4.269  1.083   11.535  1.00 38.28  ? 229 LYS   B CA  1 
ATOM   4055 C  C   . LYS   B 1 223 ? -4.439  2.596   11.457  1.00 41.24  ? 229 LYS   B C   1 
ATOM   4056 O  O   . LYS   B 1 223 ? -3.455  3.326   11.543  1.00 41.40  ? 229 LYS   B O   1 
ATOM   4057 C  CB  . LYS   B 1 223 ? -4.099  0.505   10.118  1.00 41.01  ? 229 LYS   B CB  1 
ATOM   4058 C  CG  . LYS   B 1 223 ? -2.876  -0.399  9.994   1.00 59.12  ? 229 LYS   B CG  1 
ATOM   4059 C  CD  . LYS   B 1 223 ? -2.772  -1.023  8.615   1.00 73.56  ? 229 LYS   B CD  1 
ATOM   4060 C  CE  . LYS   B 1 223 ? -1.797  -2.176  8.575   1.00 89.96  ? 229 LYS   B CE  1 
ATOM   4061 N  NZ  . LYS   B 1 223 ? -2.392  -3.430  9.112   1.00 99.27  ? 229 LYS   B NZ  1 
ATOM   4062 N  N   . VAL   B 1 224 ? -5.677  3.052   11.280  1.00 37.08  ? 230 VAL   B N   1 
ATOM   4063 C  CA  . VAL   B 1 224 ? -6.057  4.457   11.216  1.00 36.50  ? 230 VAL   B CA  1 
ATOM   4064 C  C   . VAL   B 1 224 ? -5.728  5.125   12.558  1.00 43.23  ? 230 VAL   B C   1 
ATOM   4065 O  O   . VAL   B 1 224 ? -5.091  6.172   12.567  1.00 44.32  ? 230 VAL   B O   1 
ATOM   4066 C  CB  . VAL   B 1 224 ? -7.536  4.608   10.798  1.00 37.85  ? 230 VAL   B CB  1 
ATOM   4067 C  CG1 . VAL   B 1 224 ? -8.099  5.983   11.147  1.00 37.04  ? 230 VAL   B CG1 1 
ATOM   4068 C  CG2 . VAL   B 1 224 ? -7.724  4.295   9.316   1.00 36.94  ? 230 VAL   B CG2 1 
ATOM   4069 N  N   . MET   B 1 225 ? -6.102  4.488   13.684  1.00 39.66  ? 231 MET   B N   1 
ATOM   4070 C  CA  . MET   B 1 225 ? -5.787  5.001   15.015  1.00 37.84  ? 231 MET   B CA  1 
ATOM   4071 C  C   . MET   B 1 225 ? -4.288  4.973   15.290  1.00 43.63  ? 231 MET   B C   1 
ATOM   4072 O  O   . MET   B 1 225 ? -3.778  5.956   15.822  1.00 44.19  ? 231 MET   B O   1 
ATOM   4073 C  CB  . MET   B 1 225 ? -6.605  4.310   16.124  1.00 38.95  ? 231 MET   B CB  1 
ATOM   4074 C  CG  . MET   B 1 225 ? -8.111  4.601   16.079  1.00 40.93  ? 231 MET   B CG  1 
ATOM   4075 S  SD  . MET   B 1 225 ? -8.615  6.303   15.676  1.00 44.28  ? 231 MET   B SD  1 
ATOM   4076 C  CE  . MET   B 1 225 ? -8.024  7.214   17.144  1.00 40.07  ? 231 MET   B CE  1 
ATOM   4077 N  N   . GLU   B 1 226 ? -3.572  3.891   14.884  1.00 41.62  ? 232 GLU   B N   1 
ATOM   4078 C  CA  . GLU   B 1 226 ? -2.118  3.755   15.047  1.00 42.35  ? 232 GLU   B CA  1 
ATOM   4079 C  C   . GLU   B 1 226 ? -1.381  4.873   14.300  1.00 48.50  ? 232 GLU   B C   1 
ATOM   4080 O  O   . GLU   B 1 226 ? -0.482  5.501   14.873  1.00 47.70  ? 232 GLU   B O   1 
ATOM   4081 C  CB  . GLU   B 1 226 ? -1.623  2.400   14.533  1.00 44.46  ? 232 GLU   B CB  1 
ATOM   4082 C  CG  . GLU   B 1 226 ? -1.866  1.222   15.468  1.00 58.58  ? 232 GLU   B CG  1 
ATOM   4083 C  CD  . GLU   B 1 226 ? -1.341  -0.120  14.985  1.00 81.05  ? 232 GLU   B CD  1 
ATOM   4084 O  OE1 . GLU   B 1 226 ? -1.030  -0.248  13.778  1.00 70.55  ? 232 GLU   B OE1 1 
ATOM   4085 O  OE2 . GLU   B 1 226 ? -1.246  -1.051  15.818  1.00 78.50  ? 232 GLU   B OE2 1 
ATOM   4086 N  N   . ARG   B 1 227 ? -1.786  5.129   13.031  1.00 46.03  ? 233 ARG   B N   1 
ATOM   4087 C  CA  . ARG   B 1 227 ? -1.198  6.149   12.151  1.00 45.93  ? 233 ARG   B CA  1 
ATOM   4088 C  C   . ARG   B 1 227 ? -1.469  7.570   12.628  1.00 48.69  ? 233 ARG   B C   1 
ATOM   4089 O  O   . ARG   B 1 227 ? -0.561  8.399   12.553  1.00 49.13  ? 233 ARG   B O   1 
ATOM   4090 C  CB  . ARG   B 1 227 ? -1.644  5.957   10.690  1.00 45.80  ? 233 ARG   B CB  1 
ATOM   4091 C  CG  . ARG   B 1 227 ? -0.870  4.885   9.944   1.00 56.36  ? 233 ARG   B CG  1 
ATOM   4092 C  CD  . ARG   B 1 227 ? -1.689  4.351   8.794   1.00 70.99  ? 233 ARG   B CD  1 
ATOM   4093 N  NE  . ARG   B 1 227 ? -0.898  3.493   7.912   1.00 87.14  ? 233 ARG   B NE  1 
ATOM   4094 C  CZ  . ARG   B 1 227 ? -0.423  3.868   6.728   1.00 101.16 ? 233 ARG   B CZ  1 
ATOM   4095 N  NH1 . ARG   B 1 227 ? -0.656  5.092   6.267   1.00 81.26  ? 233 ARG   B NH1 1 
ATOM   4096 N  NH2 . ARG   B 1 227 ? 0.283   3.020   5.992   1.00 94.54  ? 233 ARG   B NH2 1 
ATOM   4097 N  N   . THR   B 1 228 ? -2.701  7.843   13.105  1.00 44.79  ? 234 THR   B N   1 
ATOM   4098 C  CA  . THR   B 1 228 ? -3.177  9.118   13.668  1.00 44.94  ? 234 THR   B CA  1 
ATOM   4099 C  C   . THR   B 1 228 ? -2.320  9.548   14.867  1.00 52.16  ? 234 THR   B C   1 
ATOM   4100 O  O   . THR   B 1 228 ? -2.020  10.738  15.000  1.00 51.87  ? 234 THR   B O   1 
ATOM   4101 C  CB  . THR   B 1 228 ? -4.665  9.007   14.085  1.00 52.10  ? 234 THR   B CB  1 
ATOM   4102 O  OG1 . THR   B 1 228 ? -5.468  8.808   12.928  1.00 49.41  ? 234 THR   B OG1 1 
ATOM   4103 C  CG2 . THR   B 1 228 ? -5.186  10.243  14.845  1.00 52.83  ? 234 THR   B CG2 1 
ATOM   4104 N  N   . PHE   B 1 229 ? -1.969  8.590   15.757  1.00 49.94  ? 235 PHE   B N   1 
ATOM   4105 C  CA  . PHE   B 1 229 ? -1.154  8.861   16.941  1.00 49.98  ? 235 PHE   B CA  1 
ATOM   4106 C  C   . PHE   B 1 229 ? 0.314   8.959   16.584  1.00 56.13  ? 235 PHE   B C   1 
ATOM   4107 O  O   . PHE   B 1 229 ? 1.025   9.734   17.215  1.00 56.35  ? 235 PHE   B O   1 
ATOM   4108 C  CB  . PHE   B 1 229 ? -1.404  7.840   18.073  1.00 51.11  ? 235 PHE   B CB  1 
ATOM   4109 C  CG  . PHE   B 1 229 ? -2.821  7.801   18.611  1.00 52.09  ? 235 PHE   B CG  1 
ATOM   4110 C  CD1 . PHE   B 1 229 ? -3.548  8.974   18.798  1.00 53.97  ? 235 PHE   B CD1 1 
ATOM   4111 C  CD2 . PHE   B 1 229 ? -3.409  6.595   18.983  1.00 53.38  ? 235 PHE   B CD2 1 
ATOM   4112 C  CE1 . PHE   B 1 229 ? -4.854  8.936   19.290  1.00 54.51  ? 235 PHE   B CE1 1 
ATOM   4113 C  CE2 . PHE   B 1 229 ? -4.716  6.560   19.481  1.00 55.52  ? 235 PHE   B CE2 1 
ATOM   4114 C  CZ  . PHE   B 1 229 ? -5.427  7.729   19.634  1.00 53.54  ? 235 PHE   B CZ  1 
ATOM   4115 N  N   . ASP   B 1 230 ? 0.766   8.207   15.549  1.00 53.86  ? 236 ASP   B N   1 
ATOM   4116 C  CA  . ASP   B 1 230 ? 2.141   8.254   15.046  1.00 54.65  ? 236 ASP   B CA  1 
ATOM   4117 C  C   . ASP   B 1 230 ? 2.410   9.663   14.516  1.00 59.58  ? 236 ASP   B C   1 
ATOM   4118 O  O   . ASP   B 1 230 ? 3.518   10.182  14.685  1.00 59.29  ? 236 ASP   B O   1 
ATOM   4119 C  CB  . ASP   B 1 230 ? 2.354   7.235   13.908  1.00 57.11  ? 236 ASP   B CB  1 
ATOM   4120 C  CG  . ASP   B 1 230 ? 2.699   5.818   14.335  1.00 71.70  ? 236 ASP   B CG  1 
ATOM   4121 O  OD1 . ASP   B 1 230 ? 3.526   5.657   15.260  1.00 71.37  ? 236 ASP   B OD1 1 
ATOM   4122 O  OD2 . ASP   B 1 230 ? 2.208   4.869   13.686  1.00 83.24  ? 236 ASP   B OD2 1 
ATOM   4123 N  N   . LEU   B 1 231 ? 1.375   10.286  13.908  1.00 56.86  ? 237 LEU   B N   1 
ATOM   4124 C  CA  . LEU   B 1 231 ? 1.437   11.636  13.357  1.00 57.14  ? 237 LEU   B CA  1 
ATOM   4125 C  C   . LEU   B 1 231 ? 1.395   12.710  14.443  1.00 63.62  ? 237 LEU   B C   1 
ATOM   4126 O  O   . LEU   B 1 231 ? 2.303   13.543  14.504  1.00 64.01  ? 237 LEU   B O   1 
ATOM   4127 C  CB  . LEU   B 1 231 ? 0.307   11.884  12.327  1.00 56.69  ? 237 LEU   B CB  1 
ATOM   4128 C  CG  . LEU   B 1 231 ? 0.380   11.146  10.981  1.00 60.67  ? 237 LEU   B CG  1 
ATOM   4129 C  CD1 . LEU   B 1 231 ? -0.950  11.215  10.254  1.00 60.05  ? 237 LEU   B CD1 1 
ATOM   4130 C  CD2 . LEU   B 1 231 ? 1.530   11.660  10.097  1.00 62.65  ? 237 LEU   B CD2 1 
ATOM   4131 N  N   . LEU   B 1 232 ? 0.334   12.704  15.280  1.00 60.69  ? 238 LEU   B N   1 
ATOM   4132 C  CA  . LEU   B 1 232 ? 0.090   13.709  16.313  1.00 60.44  ? 238 LEU   B CA  1 
ATOM   4133 C  C   . LEU   B 1 232 ? 0.987   13.616  17.553  1.00 67.30  ? 238 LEU   B C   1 
ATOM   4134 O  O   . LEU   B 1 232 ? 1.598   14.622  17.917  1.00 68.10  ? 238 LEU   B O   1 
ATOM   4135 C  CB  . LEU   B 1 232 ? -1.387  13.725  16.744  1.00 60.03  ? 238 LEU   B CB  1 
ATOM   4136 C  CG  . LEU   B 1 232 ? -2.444  14.129  15.709  1.00 64.27  ? 238 LEU   B CG  1 
ATOM   4137 C  CD1 . LEU   B 1 232 ? -3.836  14.091  16.307  1.00 63.99  ? 238 LEU   B CD1 1 
ATOM   4138 C  CD2 . LEU   B 1 232 ? -2.186  15.512  15.141  1.00 66.35  ? 238 LEU   B CD2 1 
ATOM   4139 N  N   . ILE   B 1 233 ? 1.055   12.442  18.210  1.00 63.90  ? 239 ILE   B N   1 
ATOM   4140 C  CA  . ILE   B 1 233 ? 1.802   12.281  19.465  1.00 63.34  ? 239 ILE   B CA  1 
ATOM   4141 C  C   . ILE   B 1 233 ? 3.040   11.366  19.339  1.00 67.46  ? 239 ILE   B C   1 
ATOM   4142 O  O   . ILE   B 1 233 ? 3.573   10.892  20.348  1.00 67.33  ? 239 ILE   B O   1 
ATOM   4143 C  CB  . ILE   B 1 233 ? 0.859   11.849  20.632  1.00 66.09  ? 239 ILE   B CB  1 
ATOM   4144 C  CG1 . ILE   B 1 233 ? 0.038   10.573  20.285  1.00 66.54  ? 239 ILE   B CG1 1 
ATOM   4145 C  CG2 . ILE   B 1 233 ? -0.053  13.012  21.046  1.00 65.74  ? 239 ILE   B CG2 1 
ATOM   4146 C  CD1 . ILE   B 1 233 ? -0.290  9.674   21.457  1.00 75.67  ? 239 ILE   B CD1 1 
ATOM   4147 N  N   . GLY   B 1 234 ? 3.523   11.184  18.117  1.00 64.49  ? 240 GLY   B N   1 
ATOM   4148 C  CA  . GLY   B 1 234 ? 4.729   10.404  17.859  1.00 64.86  ? 240 GLY   B CA  1 
ATOM   4149 C  C   . GLY   B 1 234 ? 5.992   11.168  18.217  1.00 70.76  ? 240 GLY   B C   1 
ATOM   4150 O  O   . GLY   B 1 234 ? 6.969   10.573  18.682  1.00 70.69  ? 240 GLY   B O   1 
ATOM   4151 N  N   . LYS   B 1 235 ? 5.985   12.498  18.009  1.00 68.45  ? 241 LYS   B N   1 
ATOM   4152 C  CA  . LYS   B 1 235 ? 7.128   13.369  18.314  1.00 68.77  ? 241 LYS   B CA  1 
ATOM   4153 C  C   . LYS   B 1 235 ? 7.328   13.529  19.835  1.00 74.06  ? 241 LYS   B C   1 
ATOM   4154 O  O   . LYS   B 1 235 ? 8.462   13.428  20.320  1.00 73.79  ? 241 LYS   B O   1 
ATOM   4155 C  CB  . LYS   B 1 235 ? 6.982   14.734  17.615  1.00 71.01  ? 241 LYS   B CB  1 
ATOM   4156 C  CG  . LYS   B 1 235 ? 7.196   14.666  16.107  1.00 89.13  ? 241 LYS   B CG  1 
ATOM   4157 C  CD  . LYS   B 1 235 ? 6.328   15.664  15.354  1.00 102.13 ? 241 LYS   B CD  1 
ATOM   4158 C  CE  . LYS   B 1 235 ? 6.205   15.297  13.893  1.00 116.04 ? 241 LYS   B CE  1 
ATOM   4159 N  NZ  . LYS   B 1 235 ? 5.568   16.380  13.099  1.00 127.37 ? 241 LYS   B NZ  1 
ATOM   4160 N  N   . ARG   B 1 236 ? 6.219   13.753  20.577  1.00 71.29  ? 242 ARG   B N   1 
ATOM   4161 C  CA  . ARG   B 1 236 ? 6.182   13.923  22.040  1.00 71.28  ? 242 ARG   B CA  1 
ATOM   4162 C  C   . ARG   B 1 236 ? 4.753   13.764  22.588  1.00 73.89  ? 242 ARG   B C   1 
ATOM   4163 O  O   . ARG   B 1 236 ? 3.793   13.832  21.814  1.00 73.37  ? 242 ARG   B O   1 
ATOM   4164 C  CB  . ARG   B 1 236 ? 6.791   15.291  22.464  1.00 72.92  ? 242 ARG   B CB  1 
ATOM   4165 C  CG  . ARG   B 1 236 ? 6.119   16.527  21.852  1.00 86.56  ? 242 ARG   B CG  1 
ATOM   4166 C  CD  . ARG   B 1 236 ? 7.134   17.600  21.500  1.00 100.83 ? 242 ARG   B CD  1 
ATOM   4167 N  NE  . ARG   B 1 236 ? 6.503   18.775  20.892  1.00 113.91 ? 242 ARG   B NE  1 
ATOM   4168 C  CZ  . ARG   B 1 236 ? 6.340   18.953  19.584  1.00 129.80 ? 242 ARG   B CZ  1 
ATOM   4169 N  NH1 . ARG   B 1 236 ? 6.761   18.034  18.724  1.00 118.14 ? 242 ARG   B NH1 1 
ATOM   4170 N  NH2 . ARG   B 1 236 ? 5.756   20.052  19.126  1.00 116.63 ? 242 ARG   B NH2 1 
ATOM   4171 N  N   . GLN   B 1 237 ? 4.614   13.571  23.923  1.00 69.27  ? 243 GLN   B N   1 
ATOM   4172 C  CA  . GLN   B 1 237 ? 3.305   13.475  24.591  1.00 68.01  ? 243 GLN   B CA  1 
ATOM   4173 C  C   . GLN   B 1 237 ? 2.636   14.844  24.501  1.00 68.35  ? 243 GLN   B C   1 
ATOM   4174 O  O   . GLN   B 1 237 ? 3.283   15.856  24.780  1.00 68.27  ? 243 GLN   B O   1 
ATOM   4175 C  CB  . GLN   B 1 237 ? 3.451   13.034  26.060  1.00 69.44  ? 243 GLN   B CB  1 
ATOM   4176 C  CG  . GLN   B 1 237 ? 3.847   11.568  26.245  1.00 88.25  ? 243 GLN   B CG  1 
ATOM   4177 C  CD  . GLN   B 1 237 ? 2.692   10.626  26.015  1.00 109.39 ? 243 GLN   B CD  1 
ATOM   4178 O  OE1 . GLN   B 1 237 ? 2.483   10.123  24.906  1.00 103.59 ? 243 GLN   B OE1 1 
ATOM   4179 N  NE2 . GLN   B 1 237 ? 1.910   10.376  27.058  1.00 103.64 ? 243 GLN   B NE2 1 
ATOM   4180 N  N   . ARG   B 1 238 ? 1.381   14.884  24.026  1.00 62.15  ? 244 ARG   B N   1 
ATOM   4181 C  CA  . ARG   B 1 238 ? 0.644   16.131  23.813  1.00 60.73  ? 244 ARG   B CA  1 
ATOM   4182 C  C   . ARG   B 1 238 ? -0.827  15.988  24.197  1.00 63.33  ? 244 ARG   B C   1 
ATOM   4183 O  O   . ARG   B 1 238 ? -1.383  14.910  23.978  1.00 63.72  ? 244 ARG   B O   1 
ATOM   4184 C  CB  . ARG   B 1 238 ? 0.720   16.548  22.326  1.00 60.94  ? 244 ARG   B CB  1 
ATOM   4185 C  CG  . ARG   B 1 238 ? 2.127   16.807  21.779  1.00 69.09  ? 244 ARG   B CG  1 
ATOM   4186 C  CD  . ARG   B 1 238 ? 2.135   16.876  20.269  1.00 72.94  ? 244 ARG   B CD  1 
ATOM   4187 N  NE  . ARG   B 1 238 ? 1.647   18.167  19.783  1.00 73.52  ? 244 ARG   B NE  1 
ATOM   4188 C  CZ  . ARG   B 1 238 ? 1.335   18.428  18.519  1.00 79.62  ? 244 ARG   B CZ  1 
ATOM   4189 N  NH1 . ARG   B 1 238 ? 1.446   17.483  17.592  1.00 56.17  ? 244 ARG   B NH1 1 
ATOM   4190 N  NH2 . ARG   B 1 238 ? 0.906   19.633  18.172  1.00 64.51  ? 244 ARG   B NH2 1 
ATOM   4191 N  N   . PRO   B 1 239 ? -1.500  17.064  24.700  1.00 57.72  ? 245 PRO   B N   1 
ATOM   4192 C  CA  . PRO   B 1 239 ? -2.937  16.956  25.022  1.00 56.71  ? 245 PRO   B CA  1 
ATOM   4193 C  C   . PRO   B 1 239 ? -3.769  16.755  23.760  1.00 59.25  ? 245 PRO   B C   1 
ATOM   4194 O  O   . PRO   B 1 239 ? -3.359  17.229  22.697  1.00 59.87  ? 245 PRO   B O   1 
ATOM   4195 C  CB  . PRO   B 1 239 ? -3.267  18.309  25.671  1.00 58.56  ? 245 PRO   B CB  1 
ATOM   4196 C  CG  . PRO   B 1 239 ? -1.964  18.902  26.031  1.00 63.25  ? 245 PRO   B CG  1 
ATOM   4197 C  CD  . PRO   B 1 239 ? -0.987  18.411  25.021  1.00 59.17  ? 245 PRO   B CD  1 
ATOM   4198 N  N   . ILE   B 1 240 ? -4.939  16.083  23.876  1.00 52.67  ? 246 ILE   B N   1 
ATOM   4199 C  CA  . ILE   B 1 240 ? -5.802  15.771  22.736  1.00 50.79  ? 246 ILE   B CA  1 
ATOM   4200 C  C   . ILE   B 1 240 ? -7.182  16.412  22.859  1.00 53.66  ? 246 ILE   B C   1 
ATOM   4201 O  O   . ILE   B 1 240 ? -7.833  16.295  23.896  1.00 54.40  ? 246 ILE   B O   1 
ATOM   4202 C  CB  . ILE   B 1 240 ? -5.873  14.213  22.488  1.00 52.67  ? 246 ILE   B CB  1 
ATOM   4203 C  CG1 . ILE   B 1 240 ? -4.467  13.623  22.183  1.00 52.76  ? 246 ILE   B CG1 1 
ATOM   4204 C  CG2 . ILE   B 1 240 ? -6.879  13.840  21.386  1.00 52.20  ? 246 ILE   B CG2 1 
ATOM   4205 C  CD1 . ILE   B 1 240 ? -4.279  12.071  22.349  1.00 54.33  ? 246 ILE   B CD1 1 
ATOM   4206 N  N   . HIS   B 1 241 ? -7.641  17.053  21.768  1.00 49.30  ? 247 HIS   B N   1 
ATOM   4207 C  CA  . HIS   B 1 241 ? -8.973  17.643  21.672  1.00 48.79  ? 247 HIS   B CA  1 
ATOM   4208 C  C   . HIS   B 1 241 ? -9.800  16.798  20.688  1.00 55.75  ? 247 HIS   B C   1 
ATOM   4209 O  O   . HIS   B 1 241 ? -9.597  16.874  19.469  1.00 56.04  ? 247 HIS   B O   1 
ATOM   4210 C  CB  . HIS   B 1 241 ? -8.922  19.117  21.200  1.00 48.71  ? 247 HIS   B CB  1 
ATOM   4211 C  CG  . HIS   B 1 241 ? -10.239 19.821  21.326  1.00 51.43  ? 247 HIS   B CG  1 
ATOM   4212 N  ND1 . HIS   B 1 241 ? -10.388 20.906  22.156  1.00 52.67  ? 247 HIS   B ND1 1 
ATOM   4213 C  CD2 . HIS   B 1 241 ? -11.435 19.543  20.755  1.00 53.19  ? 247 HIS   B CD2 1 
ATOM   4214 C  CE1 . HIS   B 1 241 ? -11.661 21.251  22.072  1.00 52.16  ? 247 HIS   B CE1 1 
ATOM   4215 N  NE2 . HIS   B 1 241 ? -12.333 20.454  21.250  1.00 52.65  ? 247 HIS   B NE2 1 
ATOM   4216 N  N   . LEU   B 1 242 ? -10.755 16.028  21.214  1.00 52.02  ? 248 LEU   B N   1 
ATOM   4217 C  CA  . LEU   B 1 242 ? -11.584 15.198  20.368  1.00 51.38  ? 248 LEU   B CA  1 
ATOM   4218 C  C   . LEU   B 1 242 ? -12.856 15.911  19.982  1.00 53.54  ? 248 LEU   B C   1 
ATOM   4219 O  O   . LEU   B 1 242 ? -13.785 16.000  20.779  1.00 52.91  ? 248 LEU   B O   1 
ATOM   4220 C  CB  . LEU   B 1 242 ? -11.837 13.800  21.008  1.00 51.29  ? 248 LEU   B CB  1 
ATOM   4221 C  CG  . LEU   B 1 242 ? -12.705 12.769  20.234  1.00 55.40  ? 248 LEU   B CG  1 
ATOM   4222 C  CD1 . LEU   B 1 242 ? -12.018 12.296  18.942  1.00 55.32  ? 248 LEU   B CD1 1 
ATOM   4223 C  CD2 . LEU   B 1 242 ? -12.995 11.558  21.097  1.00 55.98  ? 248 LEU   B CD2 1 
ATOM   4224 N  N   . SER   B 1 243 ? -12.902 16.433  18.744  1.00 49.98  ? 249 SER   B N   1 
ATOM   4225 C  CA  . SER   B 1 243 ? -14.114 17.074  18.258  1.00 49.29  ? 249 SER   B CA  1 
ATOM   4226 C  C   . SER   B 1 243 ? -14.886 15.986  17.509  1.00 52.72  ? 249 SER   B C   1 
ATOM   4227 O  O   . SER   B 1 243 ? -14.351 15.394  16.557  1.00 53.31  ? 249 SER   B O   1 
ATOM   4228 C  CB  . SER   B 1 243 ? -13.793 18.284  17.385  1.00 53.09  ? 249 SER   B CB  1 
ATOM   4229 O  OG  . SER   B 1 243 ? -14.919 19.142  17.388  1.00 59.84  ? 249 SER   B OG  1 
ATOM   4230 N  N   . PHE   B 1 244 ? -16.107 15.671  17.984  1.00 46.55  ? 250 PHE   B N   1 
ATOM   4231 C  CA  . PHE   B 1 244 ? -16.891 14.557  17.461  1.00 44.80  ? 250 PHE   B CA  1 
ATOM   4232 C  C   . PHE   B 1 244 ? -18.301 14.923  17.039  1.00 47.40  ? 250 PHE   B C   1 
ATOM   4233 O  O   . PHE   B 1 244 ? -19.173 15.194  17.872  1.00 46.23  ? 250 PHE   B O   1 
ATOM   4234 C  CB  . PHE   B 1 244 ? -16.912 13.391  18.489  1.00 45.26  ? 250 PHE   B CB  1 
ATOM   4235 C  CG  . PHE   B 1 244 ? -17.085 11.988  17.948  1.00 45.11  ? 250 PHE   B CG  1 
ATOM   4236 C  CD1 . PHE   B 1 244 ? -18.291 11.583  17.384  1.00 46.87  ? 250 PHE   B CD1 1 
ATOM   4237 C  CD2 . PHE   B 1 244 ? -16.076 11.042  18.093  1.00 46.36  ? 250 PHE   B CD2 1 
ATOM   4238 C  CE1 . PHE   B 1 244 ? -18.446 10.289  16.882  1.00 46.92  ? 250 PHE   B CE1 1 
ATOM   4239 C  CE2 . PHE   B 1 244 ? -16.249 9.733   17.628  1.00 48.00  ? 250 PHE   B CE2 1 
ATOM   4240 C  CZ  . PHE   B 1 244 ? -17.429 9.371   17.019  1.00 45.61  ? 250 PHE   B CZ  1 
ATOM   4241 N  N   . ASP   B 1 245 ? -18.533 14.877  15.720  1.00 43.38  ? 251 ASP   B N   1 
ATOM   4242 C  CA  . ASP   B 1 245 ? -19.844 15.116  15.137  1.00 42.68  ? 251 ASP   B CA  1 
ATOM   4243 C  C   . ASP   B 1 245 ? -20.520 13.758  15.022  1.00 48.19  ? 251 ASP   B C   1 
ATOM   4244 O  O   . ASP   B 1 245 ? -19.931 12.829  14.467  1.00 48.39  ? 251 ASP   B O   1 
ATOM   4245 C  CB  . ASP   B 1 245 ? -19.682 15.779  13.753  1.00 43.47  ? 251 ASP   B CB  1 
ATOM   4246 C  CG  . ASP   B 1 245 ? -20.951 16.295  13.127  1.00 44.65  ? 251 ASP   B CG  1 
ATOM   4247 O  OD1 . ASP   B 1 245 ? -22.001 15.628  13.265  1.00 43.64  ? 251 ASP   B OD1 1 
ATOM   4248 O  OD2 . ASP   B 1 245 ? -20.893 17.345  12.451  1.00 54.96  ? 251 ASP   B OD2 1 
ATOM   4249 N  N   . ILE   B 1 246 ? -21.763 13.653  15.509  1.00 45.63  ? 252 ILE   B N   1 
ATOM   4250 C  CA  . ILE   B 1 246 ? -22.541 12.420  15.490  1.00 46.41  ? 252 ILE   B CA  1 
ATOM   4251 C  C   . ILE   B 1 246 ? -22.814 11.901  14.051  1.00 51.83  ? 252 ILE   B C   1 
ATOM   4252 O  O   . ILE   B 1 246 ? -23.054 10.699  13.870  1.00 51.22  ? 252 ILE   B O   1 
ATOM   4253 C  CB  . ILE   B 1 246 ? -23.832 12.573  16.341  1.00 49.52  ? 252 ILE   B CB  1 
ATOM   4254 C  CG1 . ILE   B 1 246 ? -24.274 11.220  16.980  1.00 49.83  ? 252 ILE   B CG1 1 
ATOM   4255 C  CG2 . ILE   B 1 246 ? -24.979 13.258  15.582  1.00 49.73  ? 252 ILE   B CG2 1 
ATOM   4256 C  CD1 . ILE   B 1 246 ? -23.311 10.662  18.080  1.00 50.11  ? 252 ILE   B CD1 1 
ATOM   4257 N  N   . ASP   B 1 247 ? -22.753 12.803  13.036  1.00 48.17  ? 253 ASP   B N   1 
ATOM   4258 C  CA  . ASP   B 1 247 ? -22.994 12.421  11.645  1.00 46.70  ? 253 ASP   B CA  1 
ATOM   4259 C  C   . ASP   B 1 247 ? -21.800 11.677  11.010  1.00 49.25  ? 253 ASP   B C   1 
ATOM   4260 O  O   . ASP   B 1 247 ? -21.926 11.251  9.872   1.00 49.74  ? 253 ASP   B O   1 
ATOM   4261 C  CB  . ASP   B 1 247 ? -23.469 13.618  10.782  1.00 47.43  ? 253 ASP   B CB  1 
ATOM   4262 C  CG  . ASP   B 1 247 ? -22.452 14.701  10.477  1.00 41.80  ? 253 ASP   B CG  1 
ATOM   4263 O  OD1 . ASP   B 1 247 ? -21.233 14.432  10.598  1.00 38.19  ? 253 ASP   B OD1 1 
ATOM   4264 O  OD2 . ASP   B 1 247 ? -22.878 15.844  10.146  1.00 46.26  ? 253 ASP   B OD2 1 
ATOM   4265 N  N   . ALA   B 1 248 ? -20.657 11.523  11.718  1.00 44.92  ? 254 ALA   B N   1 
ATOM   4266 C  CA  . ALA   B 1 248 ? -19.519 10.723  11.229  1.00 44.62  ? 254 ALA   B CA  1 
ATOM   4267 C  C   . ALA   B 1 248 ? -19.955 9.240   11.180  1.00 45.77  ? 254 ALA   B C   1 
ATOM   4268 O  O   . ALA   B 1 248 ? -19.431 8.477   10.368  1.00 44.02  ? 254 ALA   B O   1 
ATOM   4269 C  CB  . ALA   B 1 248 ? -18.315 10.873  12.137  1.00 45.53  ? 254 ALA   B CB  1 
ATOM   4270 N  N   . PHE   B 1 249 ? -20.945 8.868   12.029  1.00 42.00  ? 255 PHE   B N   1 
ATOM   4271 C  CA  . PHE   B 1 249 ? -21.581 7.550   12.091  1.00 41.81  ? 255 PHE   B CA  1 
ATOM   4272 C  C   . PHE   B 1 249 ? -22.591 7.443   10.961  1.00 46.23  ? 255 PHE   B C   1 
ATOM   4273 O  O   . PHE   B 1 249 ? -23.136 8.458   10.529  1.00 47.44  ? 255 PHE   B O   1 
ATOM   4274 C  CB  . PHE   B 1 249 ? -22.352 7.374   13.411  1.00 42.79  ? 255 PHE   B CB  1 
ATOM   4275 C  CG  . PHE   B 1 249 ? -21.515 7.052   14.621  1.00 43.70  ? 255 PHE   B CG  1 
ATOM   4276 C  CD1 . PHE   B 1 249 ? -20.938 5.793   14.776  1.00 45.49  ? 255 PHE   B CD1 1 
ATOM   4277 C  CD2 . PHE   B 1 249 ? -21.376 7.974   15.653  1.00 45.45  ? 255 PHE   B CD2 1 
ATOM   4278 C  CE1 . PHE   B 1 249 ? -20.178 5.485   15.909  1.00 45.93  ? 255 PHE   B CE1 1 
ATOM   4279 C  CE2 . PHE   B 1 249 ? -20.615 7.666   16.784  1.00 48.19  ? 255 PHE   B CE2 1 
ATOM   4280 C  CZ  . PHE   B 1 249 ? -20.026 6.419   16.910  1.00 46.00  ? 255 PHE   B CZ  1 
ATOM   4281 N  N   . ASP   B 1 250 ? -22.881 6.220   10.520  1.00 40.68  ? 256 ASP   B N   1 
ATOM   4282 C  CA  . ASP   B 1 250 ? -23.858 5.959   9.480   1.00 40.32  ? 256 ASP   B CA  1 
ATOM   4283 C  C   . ASP   B 1 250 ? -25.256 6.417   9.933   1.00 47.01  ? 256 ASP   B C   1 
ATOM   4284 O  O   . ASP   B 1 250 ? -25.606 6.218   11.104  1.00 46.90  ? 256 ASP   B O   1 
ATOM   4285 C  CB  . ASP   B 1 250 ? -23.877 4.460   9.142   1.00 41.55  ? 256 ASP   B CB  1 
ATOM   4286 C  CG  . ASP   B 1 250 ? -24.627 4.134   7.865   1.00 46.40  ? 256 ASP   B CG  1 
ATOM   4287 O  OD1 . ASP   B 1 250 ? -25.856 3.937   7.931   1.00 44.82  ? 256 ASP   B OD1 1 
ATOM   4288 O  OD2 . ASP   B 1 250 ? -23.997 4.128   6.799   1.00 51.65  ? 256 ASP   B OD2 1 
ATOM   4289 N  N   . PRO   B 1 251 ? -26.071 7.016   9.023   1.00 45.07  ? 257 PRO   B N   1 
ATOM   4290 C  CA  . PRO   B 1 251 ? -27.427 7.452   9.405   1.00 44.90  ? 257 PRO   B CA  1 
ATOM   4291 C  C   . PRO   B 1 251 ? -28.354 6.376   9.974   1.00 49.46  ? 257 PRO   B C   1 
ATOM   4292 O  O   . PRO   B 1 251 ? -29.377 6.733   10.544  1.00 49.32  ? 257 PRO   B O   1 
ATOM   4293 C  CB  . PRO   B 1 251 ? -27.983 8.040   8.103   1.00 46.82  ? 257 PRO   B CB  1 
ATOM   4294 C  CG  . PRO   B 1 251 ? -26.769 8.455   7.326   1.00 51.12  ? 257 PRO   B CG  1 
ATOM   4295 C  CD  . PRO   B 1 251 ? -25.787 7.365   7.614   1.00 46.95  ? 257 PRO   B CD  1 
ATOM   4296 N  N   . THR   B 1 252 ? -28.026 5.072   9.817   1.00 46.50  ? 258 THR   B N   1 
ATOM   4297 C  CA  . THR   B 1 252 ? -28.841 4.002   10.401  1.00 47.42  ? 258 THR   B CA  1 
ATOM   4298 C  C   . THR   B 1 252 ? -28.667 4.015   11.931  1.00 52.05  ? 258 THR   B C   1 
ATOM   4299 O  O   . THR   B 1 252 ? -29.608 3.707   12.663  1.00 52.63  ? 258 THR   B O   1 
ATOM   4300 C  CB  . THR   B 1 252 ? -28.507 2.615   9.799   1.00 57.07  ? 258 THR   B CB  1 
ATOM   4301 O  OG1 . THR   B 1 252 ? -27.113 2.339   9.934   1.00 58.47  ? 258 THR   B OG1 1 
ATOM   4302 C  CG2 . THR   B 1 252 ? -28.939 2.476   8.346   1.00 56.23  ? 258 THR   B CG2 1 
ATOM   4303 N  N   . LEU   B 1 253 ? -27.468 4.417   12.394  1.00 48.22  ? 259 LEU   B N   1 
ATOM   4304 C  CA  . LEU   B 1 253 ? -27.050 4.468   13.799  1.00 48.03  ? 259 LEU   B CA  1 
ATOM   4305 C  C   . LEU   B 1 253 ? -27.306 5.805   14.492  1.00 52.03  ? 259 LEU   B C   1 
ATOM   4306 O  O   . LEU   B 1 253 ? -27.633 5.816   15.682  1.00 51.07  ? 259 LEU   B O   1 
ATOM   4307 C  CB  . LEU   B 1 253 ? -25.572 4.101   13.911  1.00 48.06  ? 259 LEU   B CB  1 
ATOM   4308 C  CG  . LEU   B 1 253 ? -25.183 2.773   13.290  1.00 52.35  ? 259 LEU   B CG  1 
ATOM   4309 C  CD1 . LEU   B 1 253 ? -23.728 2.749   12.989  1.00 52.17  ? 259 LEU   B CD1 1 
ATOM   4310 C  CD2 . LEU   B 1 253 ? -25.607 1.609   14.166  1.00 55.24  ? 259 LEU   B CD2 1 
ATOM   4311 N  N   . ALA   B 1 254 ? -27.128 6.925   13.761  1.00 47.92  ? 260 ALA   B N   1 
ATOM   4312 C  CA  . ALA   B 1 254 ? -27.377 8.278   14.262  1.00 47.25  ? 260 ALA   B CA  1 
ATOM   4313 C  C   . ALA   B 1 254 ? -28.402 8.971   13.320  1.00 51.39  ? 260 ALA   B C   1 
ATOM   4314 O  O   . ALA   B 1 254 ? -28.014 9.888   12.588  1.00 49.24  ? 260 ALA   B O   1 
ATOM   4315 C  CB  . ALA   B 1 254 ? -26.068 9.057   14.329  1.00 47.57  ? 260 ALA   B CB  1 
ATOM   4316 N  N   . PRO   B 1 255 ? -29.685 8.500   13.269  1.00 50.69  ? 261 PRO   B N   1 
ATOM   4317 C  CA  . PRO   B 1 255 ? -30.651 9.079   12.308  1.00 52.02  ? 261 PRO   B CA  1 
ATOM   4318 C  C   . PRO   B 1 255 ? -31.104 10.500  12.581  1.00 59.32  ? 261 PRO   B C   1 
ATOM   4319 O  O   . PRO   B 1 255 ? -31.471 11.210  11.642  1.00 60.65  ? 261 PRO   B O   1 
ATOM   4320 C  CB  . PRO   B 1 255 ? -31.837 8.106   12.346  1.00 53.78  ? 261 PRO   B CB  1 
ATOM   4321 C  CG  . PRO   B 1 255 ? -31.746 7.439   13.656  1.00 57.57  ? 261 PRO   B CG  1 
ATOM   4322 C  CD  . PRO   B 1 255 ? -30.295 7.388   14.029  1.00 52.80  ? 261 PRO   B CD  1 
ATOM   4323 N  N   . ALA   B 1 256 ? -31.095 10.909  13.854  1.00 56.96  ? 262 ALA   B N   1 
ATOM   4324 C  CA  . ALA   B 1 256 ? -31.493 12.252  14.263  1.00 56.73  ? 262 ALA   B CA  1 
ATOM   4325 C  C   . ALA   B 1 256 ? -30.286 13.213  14.240  1.00 59.83  ? 262 ALA   B C   1 
ATOM   4326 O  O   . ALA   B 1 256 ? -29.712 13.524  15.285  1.00 58.78  ? 262 ALA   B O   1 
ATOM   4327 C  CB  . ALA   B 1 256 ? -32.152 12.203  15.641  1.00 57.42  ? 262 ALA   B CB  1 
ATOM   4328 N  N   . THR   B 1 257 ? -29.884 13.648  13.023  1.00 57.31  ? 263 THR   B N   1 
ATOM   4329 C  CA  . THR   B 1 257 ? -28.768 14.589  12.792  1.00 57.06  ? 263 THR   B CA  1 
ATOM   4330 C  C   . THR   B 1 257 ? -29.074 15.508  11.590  1.00 63.37  ? 263 THR   B C   1 
ATOM   4331 O  O   . THR   B 1 257 ? -29.931 15.170  10.771  1.00 63.62  ? 263 THR   B O   1 
ATOM   4332 C  CB  . THR   B 1 257 ? -27.404 13.867  12.711  1.00 62.10  ? 263 THR   B CB  1 
ATOM   4333 O  OG1 . THR   B 1 257 ? -26.354 14.828  12.829  1.00 62.75  ? 263 THR   B OG1 1 
ATOM   4334 C  CG2 . THR   B 1 257 ? -27.222 13.032  11.438  1.00 58.26  ? 263 THR   B CG2 1 
ATOM   4335 N  N   . GLY   B 1 258 ? -28.373 16.644  11.511  1.00 61.33  ? 264 GLY   B N   1 
ATOM   4336 C  CA  . GLY   B 1 258 ? -28.570 17.680  10.494  1.00 61.50  ? 264 GLY   B CA  1 
ATOM   4337 C  C   . GLY   B 1 258 ? -28.267 17.320  9.053   1.00 64.51  ? 264 GLY   B C   1 
ATOM   4338 O  O   . GLY   B 1 258 ? -29.165 17.353  8.205   1.00 64.39  ? 264 GLY   B O   1 
ATOM   4339 N  N   . THR   B 1 259 ? -26.991 17.020  8.760   1.00 59.67  ? 265 THR   B N   1 
ATOM   4340 C  CA  . THR   B 1 259 ? -26.516 16.655  7.421   1.00 58.38  ? 265 THR   B CA  1 
ATOM   4341 C  C   . THR   B 1 259 ? -26.091 15.155  7.391   1.00 57.48  ? 265 THR   B C   1 
ATOM   4342 O  O   . THR   B 1 259 ? -24.890 14.870  7.429   1.00 55.81  ? 265 THR   B O   1 
ATOM   4343 C  CB  . THR   B 1 259 ? -25.379 17.609  6.991   1.00 70.94  ? 265 THR   B CB  1 
ATOM   4344 O  OG1 . THR   B 1 259 ? -25.611 18.922  7.507   1.00 72.74  ? 265 THR   B OG1 1 
ATOM   4345 C  CG2 . THR   B 1 259 ? -25.187 17.653  5.478   1.00 70.73  ? 265 THR   B CG2 1 
ATOM   4346 N  N   . PRO   B 1 260 ? -27.039 14.187  7.346   1.00 53.04  ? 266 PRO   B N   1 
ATOM   4347 C  CA  . PRO   B 1 260 ? -26.635 12.774  7.335   1.00 52.77  ? 266 PRO   B CA  1 
ATOM   4348 C  C   . PRO   B 1 260 ? -26.140 12.304  5.967   1.00 55.92  ? 266 PRO   B C   1 
ATOM   4349 O  O   . PRO   B 1 260 ? -26.831 12.491  4.957   1.00 54.79  ? 266 PRO   B O   1 
ATOM   4350 C  CB  . PRO   B 1 260 ? -27.910 12.030  7.769   1.00 54.74  ? 266 PRO   B CB  1 
ATOM   4351 C  CG  . PRO   B 1 260 ? -28.947 13.108  8.064   1.00 59.16  ? 266 PRO   B CG  1 
ATOM   4352 C  CD  . PRO   B 1 260 ? -28.508 14.300  7.302   1.00 54.61  ? 266 PRO   B CD  1 
ATOM   4353 N  N   . VAL   B 1 261 ? -24.925 11.704  5.938   1.00 51.31  ? 267 VAL   B N   1 
ATOM   4354 C  CA  . VAL   B 1 261 ? -24.305 11.171  4.720   1.00 50.00  ? 267 VAL   B CA  1 
ATOM   4355 C  C   . VAL   B 1 261 ? -24.181 9.646   4.855   1.00 52.91  ? 267 VAL   B C   1 
ATOM   4356 O  O   . VAL   B 1 261 ? -23.564 9.154   5.807   1.00 51.79  ? 267 VAL   B O   1 
ATOM   4357 C  CB  . VAL   B 1 261 ? -22.938 11.839  4.391   1.00 53.56  ? 267 VAL   B CB  1 
ATOM   4358 C  CG1 . VAL   B 1 261 ? -22.430 11.424  3.007   1.00 52.78  ? 267 VAL   B CG1 1 
ATOM   4359 C  CG2 . VAL   B 1 261 ? -23.019 13.362  4.497   1.00 53.50  ? 267 VAL   B CG2 1 
ATOM   4360 N  N   . VAL   B 1 262 ? -24.762 8.911   3.889   1.00 48.57  ? 268 VAL   B N   1 
ATOM   4361 C  CA  . VAL   B 1 262 ? -24.762 7.448   3.799   1.00 47.48  ? 268 VAL   B CA  1 
ATOM   4362 C  C   . VAL   B 1 262 ? -23.319 6.893   3.759   1.00 46.85  ? 268 VAL   B C   1 
ATOM   4363 O  O   . VAL   B 1 262 ? -22.409 7.586   3.291   1.00 45.10  ? 268 VAL   B O   1 
ATOM   4364 C  CB  . VAL   B 1 262 ? -25.661 6.992   2.605   1.00 52.47  ? 268 VAL   B CB  1 
ATOM   4365 C  CG1 . VAL   B 1 262 ? -25.087 7.422   1.258   1.00 52.58  ? 268 VAL   B CG1 1 
ATOM   4366 C  CG2 . VAL   B 1 262 ? -25.956 5.495   2.630   1.00 52.51  ? 268 VAL   B CG2 1 
ATOM   4367 N  N   . GLY   B 1 263 ? -23.120 5.690   4.317   1.00 41.94  ? 269 GLY   B N   1 
ATOM   4368 C  CA  . GLY   B 1 263 ? -21.820 5.015   4.337   1.00 39.79  ? 269 GLY   B CA  1 
ATOM   4369 C  C   . GLY   B 1 263 ? -20.814 5.519   5.356   1.00 40.22  ? 269 GLY   B C   1 
ATOM   4370 O  O   . GLY   B 1 263 ? -19.631 5.699   5.045   1.00 38.98  ? 269 GLY   B O   1 
ATOM   4371 N  N   . GLY   B 1 264 ? -21.268 5.681   6.592   1.00 36.01  ? 270 GLY   B N   1 
ATOM   4372 C  CA  . GLY   B 1 264 ? -20.423 6.156   7.673   1.00 35.71  ? 270 GLY   B CA  1 
ATOM   4373 C  C   . GLY   B 1 264 ? -19.830 5.088   8.568   1.00 39.38  ? 270 GLY   B C   1 
ATOM   4374 O  O   . GLY   B 1 264 ? -19.817 3.893   8.232   1.00 38.13  ? 270 GLY   B O   1 
ATOM   4375 N  N   . LEU   B 1 265 ? -19.327 5.540   9.727   1.00 35.72  ? 271 LEU   B N   1 
ATOM   4376 C  CA  . LEU   B 1 265 ? -18.724 4.681   10.749  1.00 34.01  ? 271 LEU   B CA  1 
ATOM   4377 C  C   . LEU   B 1 265 ? -19.752 3.776   11.334  1.00 34.93  ? 271 LEU   B C   1 
ATOM   4378 O  O   . LEU   B 1 265 ? -20.917 4.163   11.489  1.00 32.65  ? 271 LEU   B O   1 
ATOM   4379 C  CB  . LEU   B 1 265 ? -18.090 5.503   11.886  1.00 33.62  ? 271 LEU   B CB  1 
ATOM   4380 C  CG  . LEU   B 1 265 ? -16.958 6.446   11.548  1.00 37.32  ? 271 LEU   B CG  1 
ATOM   4381 C  CD1 . LEU   B 1 265 ? -16.730 7.394   12.706  1.00 38.32  ? 271 LEU   B CD1 1 
ATOM   4382 C  CD2 . LEU   B 1 265 ? -15.675 5.698   11.210  1.00 39.63  ? 271 LEU   B CD2 1 
ATOM   4383 N  N   . THR   B 1 266 ? -19.333 2.534   11.636  1.00 32.73  ? 272 THR   B N   1 
ATOM   4384 C  CA  . THR   B 1 266 ? -20.215 1.585   12.302  1.00 31.88  ? 272 THR   B CA  1 
ATOM   4385 C  C   . THR   B 1 266 ? -20.139 1.917   13.808  1.00 35.00  ? 272 THR   B C   1 
ATOM   4386 O  O   . THR   B 1 266 ? -19.232 2.642   14.221  1.00 33.76  ? 272 THR   B O   1 
ATOM   4387 C  CB  . THR   B 1 266 ? -19.726 0.134   12.085  1.00 36.77  ? 272 THR   B CB  1 
ATOM   4388 O  OG1 . THR   B 1 266 ? -18.425 -0.004  12.664  1.00 33.73  ? 272 THR   B OG1 1 
ATOM   4389 C  CG2 . THR   B 1 266 ? -19.709 -0.277  10.603  1.00 37.11  ? 272 THR   B CG2 1 
ATOM   4390 N  N   . TYR   B 1 267 ? -21.058 1.357   14.617  1.00 32.72  ? 273 TYR   B N   1 
ATOM   4391 C  CA  . TYR   B 1 267 ? -21.034 1.530   16.080  1.00 32.93  ? 273 TYR   B CA  1 
ATOM   4392 C  C   . TYR   B 1 267 ? -19.648 1.147   16.597  1.00 35.10  ? 273 TYR   B C   1 
ATOM   4393 O  O   . TYR   B 1 267 ? -19.034 1.914   17.332  1.00 33.16  ? 273 TYR   B O   1 
ATOM   4394 C  CB  . TYR   B 1 267 ? -22.119 0.662   16.738  1.00 34.55  ? 273 TYR   B CB  1 
ATOM   4395 C  CG  . TYR   B 1 267 ? -22.166 0.775   18.248  1.00 37.62  ? 273 TYR   B CG  1 
ATOM   4396 C  CD1 . TYR   B 1 267 ? -22.853 1.815   18.870  1.00 40.19  ? 273 TYR   B CD1 1 
ATOM   4397 C  CD2 . TYR   B 1 267 ? -21.483 -0.130  19.057  1.00 37.39  ? 273 TYR   B CD2 1 
ATOM   4398 C  CE1 . TYR   B 1 267 ? -22.895 1.927   20.261  1.00 39.84  ? 273 TYR   B CE1 1 
ATOM   4399 C  CE2 . TYR   B 1 267 ? -21.520 -0.031  20.446  1.00 38.18  ? 273 TYR   B CE2 1 
ATOM   4400 C  CZ  . TYR   B 1 267 ? -22.227 1.003   21.044  1.00 45.38  ? 273 TYR   B CZ  1 
ATOM   4401 O  OH  . TYR   B 1 267 ? -22.265 1.111   22.410  1.00 42.43  ? 273 TYR   B OH  1 
ATOM   4402 N  N   . ARG   B 1 268 ? -19.148 -0.042  16.177  1.00 30.81  ? 274 ARG   B N   1 
ATOM   4403 C  CA  . ARG   B 1 268 ? -17.849 -0.606  16.562  1.00 29.75  ? 274 ARG   B CA  1 
ATOM   4404 C  C   . ARG   B 1 268 ? -16.677 0.265   16.220  1.00 32.40  ? 274 ARG   B C   1 
ATOM   4405 O  O   . ARG   B 1 268 ? -15.788 0.413   17.056  1.00 32.01  ? 274 ARG   B O   1 
ATOM   4406 C  CB  . ARG   B 1 268 ? -17.672 -2.010  15.971  1.00 27.65  ? 274 ARG   B CB  1 
ATOM   4407 C  CG  . ARG   B 1 268 ? -18.598 -3.040  16.609  1.00 33.22  ? 274 ARG   B CG  1 
ATOM   4408 C  CD  . ARG   B 1 268 ? -18.861 -4.222  15.678  1.00 31.99  ? 274 ARG   B CD  1 
ATOM   4409 N  NE  . ARG   B 1 268 ? -17.623 -4.940  15.360  1.00 27.65  ? 274 ARG   B NE  1 
ATOM   4410 C  CZ  . ARG   B 1 268 ? -17.562 -6.006  14.579  1.00 28.51  ? 274 ARG   B CZ  1 
ATOM   4411 N  NH1 . ARG   B 1 268 ? -18.672 -6.534  14.081  1.00 28.65  ? 274 ARG   B NH1 1 
ATOM   4412 N  NH2 . ARG   B 1 268 ? -16.398 -6.597  14.344  1.00 25.99  ? 274 ARG   B NH2 1 
ATOM   4413 N  N   . GLU   B 1 269 ? -16.691 0.907   15.034  1.00 29.43  ? 275 GLU   B N   1 
ATOM   4414 C  CA  . GLU   B 1 269 ? -15.590 1.799   14.637  1.00 28.65  ? 275 GLU   B CA  1 
ATOM   4415 C  C   . GLU   B 1 269 ? -15.519 3.063   15.521  1.00 31.49  ? 275 GLU   B C   1 
ATOM   4416 O  O   . GLU   B 1 269 ? -14.437 3.451   15.931  1.00 30.02  ? 275 GLU   B O   1 
ATOM   4417 C  CB  . GLU   B 1 269 ? -15.690 2.186   13.164  1.00 29.42  ? 275 GLU   B CB  1 
ATOM   4418 C  CG  . GLU   B 1 269 ? -15.198 1.074   12.256  1.00 35.85  ? 275 GLU   B CG  1 
ATOM   4419 C  CD  . GLU   B 1 269 ? -15.605 1.228   10.807  1.00 43.44  ? 275 GLU   B CD  1 
ATOM   4420 O  OE1 . GLU   B 1 269 ? -16.536 2.013   10.523  1.00 34.02  ? 275 GLU   B OE1 1 
ATOM   4421 O  OE2 . GLU   B 1 269 ? -14.995 0.548   9.952   1.00 37.38  ? 275 GLU   B OE2 1 
ATOM   4422 N  N   . GLY   B 1 270 ? -16.666 3.655   15.811  1.00 30.86  ? 276 GLY   B N   1 
ATOM   4423 C  CA  . GLY   B 1 270 ? -16.753 4.844   16.651  1.00 31.64  ? 276 GLY   B CA  1 
ATOM   4424 C  C   . GLY   B 1 270 ? -16.337 4.559   18.081  1.00 35.13  ? 276 GLY   B C   1 
ATOM   4425 O  O   . GLY   B 1 270 ? -15.622 5.358   18.683  1.00 35.24  ? 276 GLY   B O   1 
ATOM   4426 N  N   . MET   B 1 271 ? -16.750 3.396   18.633  1.00 33.06  ? 277 MET   B N   1 
ATOM   4427 C  CA  . MET   B 1 271 ? -16.334 3.007   19.998  1.00 32.13  ? 277 MET   B CA  1 
ATOM   4428 C  C   . MET   B 1 271 ? -14.851 2.783   20.006  1.00 35.06  ? 277 MET   B C   1 
ATOM   4429 O  O   . MET   B 1 271 ? -14.182 3.208   20.940  1.00 34.88  ? 277 MET   B O   1 
ATOM   4430 C  CB  . MET   B 1 271 ? -17.048 1.751   20.492  1.00 34.27  ? 277 MET   B CB  1 
ATOM   4431 C  CG  . MET   B 1 271 ? -18.547 1.916   20.675  1.00 38.20  ? 277 MET   B CG  1 
ATOM   4432 S  SD  . MET   B 1 271 ? -19.067 3.282   21.760  1.00 43.02  ? 277 MET   B SD  1 
ATOM   4433 C  CE  . MET   B 1 271 ? -19.835 4.333   20.576  1.00 38.99  ? 277 MET   B CE  1 
ATOM   4434 N  N   . TYR   B 1 272 ? -14.317 2.177   18.929  1.00 30.34  ? 278 TYR   B N   1 
ATOM   4435 C  CA  . TYR   B 1 272 ? -12.898 1.927   18.811  1.00 29.69  ? 278 TYR   B CA  1 
ATOM   4436 C  C   . TYR   B 1 272 ? -12.070 3.236   18.855  1.00 35.11  ? 278 TYR   B C   1 
ATOM   4437 O  O   . TYR   B 1 272 ? -11.063 3.301   19.571  1.00 34.21  ? 278 TYR   B O   1 
ATOM   4438 C  CB  . TYR   B 1 272 ? -12.577 1.077   17.567  1.00 30.33  ? 278 TYR   B CB  1 
ATOM   4439 C  CG  . TYR   B 1 272 ? -11.150 0.593   17.605  1.00 30.29  ? 278 TYR   B CG  1 
ATOM   4440 C  CD1 . TYR   B 1 272 ? -10.801 -0.549  18.321  1.00 32.39  ? 278 TYR   B CD1 1 
ATOM   4441 C  CD2 . TYR   B 1 272 ? -10.127 1.336   17.027  1.00 30.97  ? 278 TYR   B CD2 1 
ATOM   4442 C  CE1 . TYR   B 1 272 ? -9.472  -0.954  18.434  1.00 32.19  ? 278 TYR   B CE1 1 
ATOM   4443 C  CE2 . TYR   B 1 272 ? -8.798  0.929   17.119  1.00 31.09  ? 278 TYR   B CE2 1 
ATOM   4444 C  CZ  . TYR   B 1 272 ? -8.475  -0.213  17.824  1.00 36.30  ? 278 TYR   B CZ  1 
ATOM   4445 O  OH  . TYR   B 1 272 ? -7.160  -0.603  17.920  1.00 37.04  ? 278 TYR   B OH  1 
ATOM   4446 N  N   . ILE   B 1 273 ? -12.491 4.256   18.089  1.00 33.80  ? 279 ILE   B N   1 
ATOM   4447 C  CA  . ILE   B 1 273 ? -11.833 5.576   18.064  1.00 33.72  ? 279 ILE   B CA  1 
ATOM   4448 C  C   . ILE   B 1 273 ? -11.759 6.129   19.511  1.00 38.46  ? 279 ILE   B C   1 
ATOM   4449 O  O   . ILE   B 1 273 ? -10.673 6.452   19.991  1.00 37.41  ? 279 ILE   B O   1 
ATOM   4450 C  CB  . ILE   B 1 273 ? -12.597 6.576   17.140  1.00 35.62  ? 279 ILE   B CB  1 
ATOM   4451 C  CG1 . ILE   B 1 273 ? -12.527 6.149   15.650  1.00 35.44  ? 279 ILE   B CG1 1 
ATOM   4452 C  CG2 . ILE   B 1 273 ? -12.079 8.023   17.329  1.00 34.85  ? 279 ILE   B CG2 1 
ATOM   4453 C  CD1 . ILE   B 1 273 ? -13.680 6.688   14.811  1.00 41.06  ? 279 ILE   B CD1 1 
ATOM   4454 N  N   . ALA   B 1 274 ? -12.919 6.223   20.171  1.00 37.16  ? 280 ALA   B N   1 
ATOM   4455 C  CA  . ALA   B 1 274 ? -13.097 6.726   21.548  1.00 37.77  ? 280 ALA   B CA  1 
ATOM   4456 C  C   . ALA   B 1 274 ? -12.260 5.944   22.584  1.00 42.49  ? 280 ALA   B C   1 
ATOM   4457 O  O   . ALA   B 1 274 ? -11.691 6.559   23.490  1.00 41.72  ? 280 ALA   B O   1 
ATOM   4458 C  CB  . ALA   B 1 274 ? -14.576 6.693   21.911  1.00 38.58  ? 280 ALA   B CB  1 
ATOM   4459 N  N   . GLU   B 1 275 ? -12.156 4.595   22.430  1.00 38.15  ? 281 GLU   B N   1 
ATOM   4460 C  CA  . GLU   B 1 275 ? -11.379 3.724   23.321  1.00 36.16  ? 281 GLU   B CA  1 
ATOM   4461 C  C   . GLU   B 1 275 ? -9.887  3.965   23.178  1.00 40.12  ? 281 GLU   B C   1 
ATOM   4462 O  O   . GLU   B 1 275 ? -9.180  3.983   24.187  1.00 40.37  ? 281 GLU   B O   1 
ATOM   4463 C  CB  . GLU   B 1 275 ? -11.651 2.240   23.032  1.00 36.50  ? 281 GLU   B CB  1 
ATOM   4464 C  CG  . GLU   B 1 275 ? -13.009 1.742   23.487  1.00 37.55  ? 281 GLU   B CG  1 
ATOM   4465 C  CD  . GLU   B 1 275 ? -13.330 0.356   22.956  1.00 43.57  ? 281 GLU   B CD  1 
ATOM   4466 O  OE1 . GLU   B 1 275 ? -12.570 -0.157  22.102  1.00 36.08  ? 281 GLU   B OE1 1 
ATOM   4467 O  OE2 . GLU   B 1 275 ? -14.366 -0.204  23.377  1.00 38.70  ? 281 GLU   B OE2 1 
ATOM   4468 N  N   . GLU   B 1 276 ? -9.402  4.104   21.937  1.00 34.61  ? 282 GLU   B N   1 
ATOM   4469 C  CA  . GLU   B 1 276 ? -7.992  4.349   21.660  1.00 34.91  ? 282 GLU   B CA  1 
ATOM   4470 C  C   . GLU   B 1 276 ? -7.583  5.714   22.181  1.00 39.68  ? 282 GLU   B C   1 
ATOM   4471 O  O   . GLU   B 1 276 ? -6.477  5.849   22.700  1.00 40.38  ? 282 GLU   B O   1 
ATOM   4472 C  CB  . GLU   B 1 276 ? -7.676  4.221   20.157  1.00 36.59  ? 282 GLU   B CB  1 
ATOM   4473 C  CG  . GLU   B 1 276 ? -7.468  2.784   19.698  1.00 43.81  ? 282 GLU   B CG  1 
ATOM   4474 C  CD  . GLU   B 1 276 ? -6.656  1.897   20.625  1.00 56.45  ? 282 GLU   B CD  1 
ATOM   4475 O  OE1 . GLU   B 1 276 ? -5.419  2.075   20.708  1.00 53.26  ? 282 GLU   B OE1 1 
ATOM   4476 O  OE2 . GLU   B 1 276 ? -7.275  1.075   21.334  1.00 47.84  ? 282 GLU   B OE2 1 
ATOM   4477 N  N   . ILE   B 1 277 ? -8.489  6.709   22.060  1.00 35.92  ? 283 ILE   B N   1 
ATOM   4478 C  CA  . ILE   B 1 277 ? -8.298  8.069   22.566  1.00 37.00  ? 283 ILE   B CA  1 
ATOM   4479 C  C   . ILE   B 1 277 ? -8.112  7.959   24.101  1.00 42.71  ? 283 ILE   B C   1 
ATOM   4480 O  O   . ILE   B 1 277 ? -7.122  8.476   24.623  1.00 42.96  ? 283 ILE   B O   1 
ATOM   4481 C  CB  . ILE   B 1 277 ? -9.491  8.992   22.146  1.00 40.47  ? 283 ILE   B CB  1 
ATOM   4482 C  CG1 . ILE   B 1 277 ? -9.428  9.409   20.629  1.00 40.82  ? 283 ILE   B CG1 1 
ATOM   4483 C  CG2 . ILE   B 1 277 ? -9.635  10.214  23.070  1.00 41.91  ? 283 ILE   B CG2 1 
ATOM   4484 C  CD1 . ILE   B 1 277 ? -8.205  10.264  20.154  1.00 50.33  ? 283 ILE   B CD1 1 
ATOM   4485 N  N   . HIS   B 1 278 ? -9.001  7.215   24.789  1.00 39.64  ? 284 HIS   B N   1 
ATOM   4486 C  CA  . HIS   B 1 278 ? -8.875  6.994   26.241  1.00 40.86  ? 284 HIS   B CA  1 
ATOM   4487 C  C   . HIS   B 1 278 ? -7.533  6.347   26.581  1.00 44.87  ? 284 HIS   B C   1 
ATOM   4488 O  O   . HIS   B 1 278 ? -6.857  6.831   27.481  1.00 45.67  ? 284 HIS   B O   1 
ATOM   4489 C  CB  . HIS   B 1 278 ? -10.039 6.159   26.821  1.00 42.38  ? 284 HIS   B CB  1 
ATOM   4490 C  CG  . HIS   B 1 278 ? -9.777  5.719   28.235  1.00 46.45  ? 284 HIS   B CG  1 
ATOM   4491 N  ND1 . HIS   B 1 278 ? -10.054 6.545   29.311  1.00 48.38  ? 284 HIS   B ND1 1 
ATOM   4492 C  CD2 . HIS   B 1 278 ? -9.178  4.594   28.694  1.00 48.72  ? 284 HIS   B CD2 1 
ATOM   4493 C  CE1 . HIS   B 1 278 ? -9.635  5.891   30.382  1.00 47.98  ? 284 HIS   B CE1 1 
ATOM   4494 N  NE2 . HIS   B 1 278 ? -9.103  4.712   30.062  1.00 48.39  ? 284 HIS   B NE2 1 
ATOM   4495 N  N   . ASN   B 1 279 ? -7.137  5.278   25.853  1.00 40.85  ? 285 ASN   B N   1 
ATOM   4496 C  CA  . ASN   B 1 279 ? -5.895  4.522   26.084  1.00 41.50  ? 285 ASN   B CA  1 
ATOM   4497 C  C   . ASN   B 1 279 ? -4.585  5.333   25.975  1.00 48.51  ? 285 ASN   B C   1 
ATOM   4498 O  O   . ASN   B 1 279 ? -3.553  4.856   26.460  1.00 49.65  ? 285 ASN   B O   1 
ATOM   4499 C  CB  . ASN   B 1 279 ? -5.830  3.282   25.174  1.00 43.50  ? 285 ASN   B CB  1 
ATOM   4500 C  CG  . ASN   B 1 279 ? -6.913  2.252   25.453  1.00 63.83  ? 285 ASN   B CG  1 
ATOM   4501 O  OD1 . ASN   B 1 279 ? -7.590  2.280   26.490  1.00 52.06  ? 285 ASN   B OD1 1 
ATOM   4502 N  ND2 . ASN   B 1 279 ? -7.116  1.324   24.519  1.00 54.03  ? 285 ASN   B ND2 1 
ATOM   4503 N  N   . THR   B 1 280 ? -4.595  6.515   25.332  1.00 47.42  ? 286 THR   B N   1 
ATOM   4504 C  CA  . THR   B 1 280 ? -3.373  7.349   25.257  1.00 47.93  ? 286 THR   B CA  1 
ATOM   4505 C  C   . THR   B 1 280 ? -3.143  8.031   26.620  1.00 53.92  ? 286 THR   B C   1 
ATOM   4506 O  O   . THR   B 1 280 ? -2.002  8.352   26.967  1.00 53.83  ? 286 THR   B O   1 
ATOM   4507 C  CB  . THR   B 1 280 ? -3.475  8.430   24.166  1.00 50.08  ? 286 THR   B CB  1 
ATOM   4508 O  OG1 . THR   B 1 280 ? -4.552  9.319   24.465  1.00 46.91  ? 286 THR   B OG1 1 
ATOM   4509 C  CG2 . THR   B 1 280 ? -3.638  7.850   22.768  1.00 48.22  ? 286 THR   B CG2 1 
ATOM   4510 N  N   . GLY   B 1 281 ? -4.245  8.267   27.342  1.00 51.50  ? 287 GLY   B N   1 
ATOM   4511 C  CA  . GLY   B 1 281 ? -4.270  8.951   28.631  1.00 52.34  ? 287 GLY   B CA  1 
ATOM   4512 C  C   . GLY   B 1 281 ? -4.048  10.446  28.496  1.00 58.17  ? 287 GLY   B C   1 
ATOM   4513 O  O   . GLY   B 1 281 ? -3.900  11.148  29.503  1.00 58.25  ? 287 GLY   B O   1 
ATOM   4514 N  N   . LEU   B 1 282 ? -4.048  10.949  27.235  1.00 53.74  ? 288 LEU   B N   1 
ATOM   4515 C  CA  . LEU   B 1 282 ? -3.788  12.350  26.904  1.00 51.98  ? 288 LEU   B CA  1 
ATOM   4516 C  C   . LEU   B 1 282 ? -5.021  13.162  26.536  1.00 52.85  ? 288 LEU   B C   1 
ATOM   4517 O  O   . LEU   B 1 282 ? -4.857  14.336  26.218  1.00 52.76  ? 288 LEU   B O   1 
ATOM   4518 C  CB  . LEU   B 1 282 ? -2.725  12.459  25.803  1.00 51.62  ? 288 LEU   B CB  1 
ATOM   4519 C  CG  . LEU   B 1 282 ? -1.344  11.892  26.106  1.00 56.31  ? 288 LEU   B CG  1 
ATOM   4520 C  CD1 . LEU   B 1 282 ? -0.638  11.511  24.832  1.00 56.56  ? 288 LEU   B CD1 1 
ATOM   4521 C  CD2 . LEU   B 1 282 ? -0.492  12.877  26.921  1.00 59.12  ? 288 LEU   B CD2 1 
ATOM   4522 N  N   . LEU   B 1 283 ? -6.251  12.585  26.612  1.00 48.46  ? 289 LEU   B N   1 
ATOM   4523 C  CA  . LEU   B 1 283 ? -7.475  13.333  26.297  1.00 48.97  ? 289 LEU   B CA  1 
ATOM   4524 C  C   . LEU   B 1 283 ? -7.646  14.516  27.253  1.00 57.70  ? 289 LEU   B C   1 
ATOM   4525 O  O   . LEU   B 1 283 ? -7.679  14.318  28.471  1.00 59.17  ? 289 LEU   B O   1 
ATOM   4526 C  CB  . LEU   B 1 283 ? -8.740  12.454  26.297  1.00 48.57  ? 289 LEU   B CB  1 
ATOM   4527 C  CG  . LEU   B 1 283 ? -10.077 13.170  25.999  1.00 52.99  ? 289 LEU   B CG  1 
ATOM   4528 C  CD1 . LEU   B 1 283 ? -10.175 13.625  24.535  1.00 53.81  ? 289 LEU   B CD1 1 
ATOM   4529 C  CD2 . LEU   B 1 283 ? -11.252 12.301  26.323  1.00 53.60  ? 289 LEU   B CD2 1 
ATOM   4530 N  N   . SER   B 1 284 ? -7.771  15.734  26.699  1.00 54.63  ? 290 SER   B N   1 
ATOM   4531 C  CA  . SER   B 1 284 ? -7.906  16.955  27.496  1.00 54.43  ? 290 SER   B CA  1 
ATOM   4532 C  C   . SER   B 1 284 ? -9.223  17.705  27.265  1.00 57.29  ? 290 SER   B C   1 
ATOM   4533 O  O   . SER   B 1 284 ? -9.657  18.419  28.168  1.00 57.89  ? 290 SER   B O   1 
ATOM   4534 C  CB  . SER   B 1 284 ? -6.694  17.857  27.289  1.00 58.78  ? 290 SER   B CB  1 
ATOM   4535 O  OG  . SER   B 1 284 ? -6.717  19.006  28.121  1.00 69.14  ? 290 SER   B OG  1 
ATOM   4536 N  N   . ALA   B 1 285 ? -9.880  17.525  26.092  1.00 52.10  ? 291 ALA   B N   1 
ATOM   4537 C  CA  . ALA   B 1 285 ? -11.164 18.172  25.764  1.00 51.20  ? 291 ALA   B CA  1 
ATOM   4538 C  C   . ALA   B 1 285 ? -11.989 17.386  24.732  1.00 54.10  ? 291 ALA   B C   1 
ATOM   4539 O  O   . ALA   B 1 285 ? -11.416 16.718  23.883  1.00 54.33  ? 291 ALA   B O   1 
ATOM   4540 C  CB  . ALA   B 1 285 ? -10.928 19.589  25.276  1.00 52.06  ? 291 ALA   B CB  1 
ATOM   4541 N  N   . LEU   B 1 286 ? -13.326 17.485  24.788  1.00 50.93  ? 292 LEU   B N   1 
ATOM   4542 C  CA  . LEU   B 1 286 ? -14.215 16.747  23.896  1.00 51.63  ? 292 LEU   B CA  1 
ATOM   4543 C  C   . LEU   B 1 286 ? -15.504 17.486  23.530  1.00 54.21  ? 292 LEU   B C   1 
ATOM   4544 O  O   . LEU   B 1 286 ? -16.166 18.022  24.410  1.00 53.13  ? 292 LEU   B O   1 
ATOM   4545 C  CB  . LEU   B 1 286 ? -14.555 15.390  24.557  1.00 52.04  ? 292 LEU   B CB  1 
ATOM   4546 C  CG  . LEU   B 1 286 ? -15.303 14.360  23.734  1.00 57.23  ? 292 LEU   B CG  1 
ATOM   4547 C  CD1 . LEU   B 1 286 ? -14.833 12.993  24.085  1.00 58.40  ? 292 LEU   B CD1 1 
ATOM   4548 C  CD2 . LEU   B 1 286 ? -16.804 14.443  23.965  1.00 58.98  ? 292 LEU   B CD2 1 
ATOM   4549 N  N   . ASP   B 1 287 ? -15.913 17.400  22.242  1.00 50.06  ? 293 ASP   B N   1 
ATOM   4550 C  CA  . ASP   B 1 287 ? -17.158 17.980  21.741  1.00 49.36  ? 293 ASP   B CA  1 
ATOM   4551 C  C   . ASP   B 1 287 ? -18.083 16.898  21.191  1.00 51.35  ? 293 ASP   B C   1 
ATOM   4552 O  O   . ASP   B 1 287 ? -17.621 16.027  20.466  1.00 49.51  ? 293 ASP   B O   1 
ATOM   4553 C  CB  . ASP   B 1 287 ? -16.873 19.049  20.652  1.00 52.21  ? 293 ASP   B CB  1 
ATOM   4554 C  CG  . ASP   B 1 287 ? -15.682 19.958  20.930  1.00 66.18  ? 293 ASP   B CG  1 
ATOM   4555 O  OD1 . ASP   B 1 287 ? -15.623 20.543  22.032  1.00 68.03  ? 293 ASP   B OD1 1 
ATOM   4556 O  OD2 . ASP   B 1 287 ? -14.813 20.081  20.047  1.00 73.09  ? 293 ASP   B OD2 1 
ATOM   4557 N  N   . LEU   B 1 288 ? -19.386 16.960  21.517  1.00 48.96  ? 294 LEU   B N   1 
ATOM   4558 C  CA  . LEU   B 1 288 ? -20.381 16.020  21.010  1.00 50.48  ? 294 LEU   B CA  1 
ATOM   4559 C  C   . LEU   B 1 288 ? -21.546 16.810  20.428  1.00 58.48  ? 294 LEU   B C   1 
ATOM   4560 O  O   . LEU   B 1 288 ? -22.444 17.265  21.144  1.00 58.07  ? 294 LEU   B O   1 
ATOM   4561 C  CB  . LEU   B 1 288 ? -20.829 14.979  22.061  1.00 50.25  ? 294 LEU   B CB  1 
ATOM   4562 C  CG  . LEU   B 1 288 ? -21.120 13.551  21.557  1.00 54.01  ? 294 LEU   B CG  1 
ATOM   4563 C  CD1 . LEU   B 1 288 ? -22.313 13.505  20.614  1.00 53.63  ? 294 LEU   B CD1 1 
ATOM   4564 C  CD2 . LEU   B 1 288 ? -19.863 12.882  20.957  1.00 55.37  ? 294 LEU   B CD2 1 
ATOM   4565 N  N   . VAL   B 1 289 ? -21.508 16.977  19.097  1.00 57.11  ? 295 VAL   B N   1 
ATOM   4566 C  CA  . VAL   B 1 289 ? -22.443 17.827  18.371  1.00 56.98  ? 295 VAL   B CA  1 
ATOM   4567 C  C   . VAL   B 1 289 ? -23.343 17.112  17.354  1.00 61.23  ? 295 VAL   B C   1 
ATOM   4568 O  O   . VAL   B 1 289 ? -23.185 15.926  17.053  1.00 60.37  ? 295 VAL   B O   1 
ATOM   4569 C  CB  . VAL   B 1 289 ? -21.665 18.987  17.688  1.00 60.31  ? 295 VAL   B CB  1 
ATOM   4570 C  CG1 . VAL   B 1 289 ? -20.932 19.848  18.714  1.00 59.78  ? 295 VAL   B CG1 1 
ATOM   4571 C  CG2 . VAL   B 1 289 ? -20.692 18.465  16.633  1.00 60.06  ? 295 VAL   B CG2 1 
ATOM   4572 N  N   . GLU   B 1 290 ? -24.284 17.906  16.829  1.00 57.34  ? 296 GLU   B N   1 
ATOM   4573 C  CA  . GLU   B 1 290 ? -25.258 17.673  15.772  1.00 57.19  ? 296 GLU   B CA  1 
ATOM   4574 C  C   . GLU   B 1 290 ? -26.335 16.652  16.127  1.00 62.76  ? 296 GLU   B C   1 
ATOM   4575 O  O   . GLU   B 1 290 ? -26.975 16.109  15.223  1.00 63.03  ? 296 GLU   B O   1 
ATOM   4576 C  CB  . GLU   B 1 290 ? -24.581 17.357  14.427  1.00 58.31  ? 296 GLU   B CB  1 
ATOM   4577 C  CG  . GLU   B 1 290 ? -23.558 18.409  13.998  1.00 64.05  ? 296 GLU   B CG  1 
ATOM   4578 C  CD  . GLU   B 1 290 ? -24.021 19.791  13.563  1.00 69.82  ? 296 GLU   B CD  1 
ATOM   4579 O  OE1 . GLU   B 1 290 ? -25.247 20.039  13.534  1.00 49.81  ? 296 GLU   B OE1 1 
ATOM   4580 O  OE2 . GLU   B 1 290 ? -23.145 20.636  13.267  1.00 50.72  ? 296 GLU   B OE2 1 
ATOM   4581 N  N   . VAL   B 1 291 ? -26.626 16.475  17.432  1.00 59.28  ? 297 VAL   B N   1 
ATOM   4582 C  CA  . VAL   B 1 291 ? -27.738 15.612  17.839  1.00 59.69  ? 297 VAL   B CA  1 
ATOM   4583 C  C   . VAL   B 1 291 ? -29.017 16.475  17.672  1.00 66.82  ? 297 VAL   B C   1 
ATOM   4584 O  O   . VAL   B 1 291 ? -29.108 17.551  18.265  1.00 67.04  ? 297 VAL   B O   1 
ATOM   4585 C  CB  . VAL   B 1 291 ? -27.578 15.020  19.271  1.00 62.54  ? 297 VAL   B CB  1 
ATOM   4586 C  CG1 . VAL   B 1 291 ? -28.810 14.214  19.681  1.00 61.96  ? 297 VAL   B CG1 1 
ATOM   4587 C  CG2 . VAL   B 1 291 ? -26.322 14.157  19.372  1.00 62.31  ? 297 VAL   B CG2 1 
ATOM   4588 N  N   . ASN   B 1 292 ? -29.953 16.036  16.811  1.00 64.68  ? 298 ASN   B N   1 
ATOM   4589 C  CA  . ASN   B 1 292 ? -31.186 16.773  16.540  1.00 64.98  ? 298 ASN   B CA  1 
ATOM   4590 C  C   . ASN   B 1 292 ? -32.428 15.910  16.807  1.00 70.82  ? 298 ASN   B C   1 
ATOM   4591 O  O   . ASN   B 1 292 ? -32.940 15.265  15.887  1.00 70.65  ? 298 ASN   B O   1 
ATOM   4592 C  CB  . ASN   B 1 292 ? -31.181 17.339  15.118  1.00 66.76  ? 298 ASN   B CB  1 
ATOM   4593 C  CG  . ASN   B 1 292 ? -32.182 18.449  14.892  1.00 90.37  ? 298 ASN   B CG  1 
ATOM   4594 O  OD1 . ASN   B 1 292 ? -33.386 18.327  15.172  1.00 80.72  ? 298 ASN   B OD1 1 
ATOM   4595 N  ND2 . ASN   B 1 292 ? -31.711 19.542  14.315  1.00 83.52  ? 298 ASN   B ND2 1 
ATOM   4596 N  N   . PRO   B 1 293 ? -32.956 15.924  18.052  1.00 68.58  ? 299 PRO   B N   1 
ATOM   4597 C  CA  . PRO   B 1 293 ? -34.144 15.100  18.366  1.00 69.25  ? 299 PRO   B CA  1 
ATOM   4598 C  C   . PRO   B 1 293 ? -35.420 15.424  17.578  1.00 76.19  ? 299 PRO   B C   1 
ATOM   4599 O  O   . PRO   B 1 293 ? -36.351 14.612  17.576  1.00 75.88  ? 299 PRO   B O   1 
ATOM   4600 C  CB  . PRO   B 1 293 ? -34.346 15.309  19.870  1.00 70.86  ? 299 PRO   B CB  1 
ATOM   4601 C  CG  . PRO   B 1 293 ? -33.094 15.909  20.355  1.00 74.88  ? 299 PRO   B CG  1 
ATOM   4602 C  CD  . PRO   B 1 293 ? -32.466 16.644  19.242  1.00 70.15  ? 299 PRO   B CD  1 
ATOM   4603 N  N   . GLN   B 1 294 ? -35.465 16.602  16.918  1.00 74.69  ? 300 GLN   B N   1 
ATOM   4604 C  CA  . GLN   B 1 294 ? -36.598 17.035  16.095  1.00 75.22  ? 300 GLN   B CA  1 
ATOM   4605 C  C   . GLN   B 1 294 ? -36.564 16.404  14.691  1.00 79.47  ? 300 GLN   B C   1 
ATOM   4606 O  O   . GLN   B 1 294 ? -37.591 16.384  14.012  1.00 79.37  ? 300 GLN   B O   1 
ATOM   4607 C  CB  . GLN   B 1 294 ? -36.680 18.571  16.014  1.00 76.76  ? 300 GLN   B CB  1 
ATOM   4608 C  CG  . GLN   B 1 294 ? -37.239 19.217  17.280  1.00 97.65  ? 300 GLN   B CG  1 
ATOM   4609 C  CD  . GLN   B 1 294 ? -38.079 20.439  16.990  1.00 121.85 ? 300 GLN   B CD  1 
ATOM   4610 O  OE1 . GLN   B 1 294 ? -39.179 20.356  16.426  1.00 115.20 ? 300 GLN   B OE1 1 
ATOM   4611 N  NE2 . GLN   B 1 294 ? -37.603 21.600  17.420  1.00 118.89 ? 300 GLN   B NE2 1 
ATOM   4612 N  N   . LEU   B 1 295 ? -35.399 15.868  14.273  1.00 75.91  ? 301 LEU   B N   1 
ATOM   4613 C  CA  . LEU   B 1 295 ? -35.228 15.226  12.966  1.00 75.81  ? 301 LEU   B CA  1 
ATOM   4614 C  C   . LEU   B 1 295 ? -35.389 13.686  13.010  1.00 79.85  ? 301 LEU   B C   1 
ATOM   4615 O  O   . LEU   B 1 295 ? -34.726 12.978  12.247  1.00 80.45  ? 301 LEU   B O   1 
ATOM   4616 C  CB  . LEU   B 1 295 ? -33.880 15.644  12.326  1.00 75.86  ? 301 LEU   B CB  1 
ATOM   4617 C  CG  . LEU   B 1 295 ? -33.754 17.103  11.854  1.00 80.54  ? 301 LEU   B CG  1 
ATOM   4618 C  CD1 . LEU   B 1 295 ? -32.327 17.431  11.486  1.00 80.66  ? 301 LEU   B CD1 1 
ATOM   4619 C  CD2 . LEU   B 1 295 ? -34.663 17.392  10.662  1.00 83.75  ? 301 LEU   B CD2 1 
ATOM   4620 N  N   . ALA   B 1 296 ? -36.295 13.177  13.878  1.00 75.24  ? 302 ALA   B N   1 
ATOM   4621 C  CA  . ALA   B 1 296 ? -36.552 11.739  14.041  1.00 74.70  ? 302 ALA   B CA  1 
ATOM   4622 C  C   . ALA   B 1 296 ? -37.970 11.342  13.629  1.00 77.20  ? 302 ALA   B C   1 
ATOM   4623 O  O   . ALA   B 1 296 ? -38.936 11.974  14.058  1.00 76.16  ? 302 ALA   B O   1 
ATOM   4624 C  CB  . ALA   B 1 296 ? -36.280 11.315  15.476  1.00 75.48  ? 302 ALA   B CB  1 
ATOM   4625 N  N   . THR   B 1 297 ? -38.086 10.288  12.802  1.00 74.22  ? 303 THR   B N   1 
ATOM   4626 C  CA  . THR   B 1 297 ? -39.364 9.781   12.277  1.00 74.52  ? 303 THR   B CA  1 
ATOM   4627 C  C   . THR   B 1 297 ? -40.118 8.875   13.282  1.00 78.77  ? 303 THR   B C   1 
ATOM   4628 O  O   . THR   B 1 297 ? -41.315 8.619   13.098  1.00 77.45  ? 303 THR   B O   1 
ATOM   4629 C  CB  . THR   B 1 297 ? -39.168 9.095   10.902  1.00 84.08  ? 303 THR   B CB  1 
ATOM   4630 O  OG1 . THR   B 1 297 ? -38.354 7.928   11.045  1.00 83.98  ? 303 THR   B OG1 1 
ATOM   4631 C  CG2 . THR   B 1 297 ? -38.574 10.031  9.843   1.00 82.81  ? 303 THR   B CG2 1 
ATOM   4632 N  N   . SER   B 1 298 ? -39.414 8.394   14.332  1.00 76.23  ? 304 SER   B N   1 
ATOM   4633 C  CA  . SER   B 1 298 ? -39.962 7.526   15.387  1.00 76.61  ? 304 SER   B CA  1 
ATOM   4634 C  C   . SER   B 1 298 ? -39.257 7.796   16.722  1.00 81.93  ? 304 SER   B C   1 
ATOM   4635 O  O   . SER   B 1 298 ? -38.199 8.431   16.721  1.00 80.90  ? 304 SER   B O   1 
ATOM   4636 C  CB  . SER   B 1 298 ? -39.838 6.052   14.999  1.00 79.28  ? 304 SER   B CB  1 
ATOM   4637 O  OG  . SER   B 1 298 ? -38.488 5.670   14.794  1.00 85.42  ? 304 SER   B OG  1 
ATOM   4638 N  N   . GLU   B 1 299 ? -39.841 7.331   17.859  1.00 80.42  ? 305 GLU   B N   1 
ATOM   4639 C  CA  . GLU   B 1 299 ? -39.241 7.561   19.180  1.00 81.14  ? 305 GLU   B CA  1 
ATOM   4640 C  C   . GLU   B 1 299 ? -37.938 6.791   19.376  1.00 85.32  ? 305 GLU   B C   1 
ATOM   4641 O  O   . GLU   B 1 299 ? -37.000 7.335   19.969  1.00 84.78  ? 305 GLU   B O   1 
ATOM   4642 C  CB  . GLU   B 1 299 ? -40.220 7.329   20.341  1.00 82.75  ? 305 GLU   B CB  1 
ATOM   4643 C  CG  . GLU   B 1 299 ? -39.926 8.269   21.503  1.00 97.03  ? 305 GLU   B CG  1 
ATOM   4644 C  CD  . GLU   B 1 299 ? -40.773 8.120   22.750  1.00 125.18 ? 305 GLU   B CD  1 
ATOM   4645 O  OE1 . GLU   B 1 299 ? -41.501 9.082   23.089  1.00 119.69 ? 305 GLU   B OE1 1 
ATOM   4646 O  OE2 . GLU   B 1 299 ? -40.673 7.063   23.416  1.00 123.72 ? 305 GLU   B OE2 1 
ATOM   4647 N  N   . GLU   B 1 300 ? -37.864 5.559   18.832  1.00 82.06  ? 306 GLU   B N   1 
ATOM   4648 C  CA  . GLU   B 1 300 ? -36.669 4.720   18.899  1.00 82.10  ? 306 GLU   B CA  1 
ATOM   4649 C  C   . GLU   B 1 300 ? -35.496 5.331   18.127  1.00 85.20  ? 306 GLU   B C   1 
ATOM   4650 O  O   . GLU   B 1 300 ? -34.359 5.184   18.568  1.00 85.35  ? 306 GLU   B O   1 
ATOM   4651 C  CB  . GLU   B 1 300 ? -36.949 3.260   18.487  1.00 83.68  ? 306 GLU   B CB  1 
ATOM   4652 C  CG  . GLU   B 1 300 ? -37.528 3.061   17.095  1.00 95.25  ? 306 GLU   B CG  1 
ATOM   4653 C  CD  . GLU   B 1 300 ? -37.884 1.621   16.781  1.00 122.31 ? 306 GLU   B CD  1 
ATOM   4654 O  OE1 . GLU   B 1 300 ? -36.977 0.758   16.820  1.00 118.60 ? 306 GLU   B OE1 1 
ATOM   4655 O  OE2 . GLU   B 1 300 ? -39.073 1.357   16.488  1.00 120.45 ? 306 GLU   B OE2 1 
ATOM   4656 N  N   . GLU   B 1 301 ? -35.777 6.059   17.018  1.00 80.18  ? 307 GLU   B N   1 
ATOM   4657 C  CA  . GLU   B 1 301 ? -34.767 6.758   16.211  1.00 78.98  ? 307 GLU   B CA  1 
ATOM   4658 C  C   . GLU   B 1 301 ? -34.157 7.926   16.988  1.00 80.19  ? 307 GLU   B C   1 
ATOM   4659 O  O   . GLU   B 1 301 ? -32.970 8.201   16.839  1.00 79.34  ? 307 GLU   B O   1 
ATOM   4660 C  CB  . GLU   B 1 301 ? -35.358 7.247   14.880  1.00 80.24  ? 307 GLU   B CB  1 
ATOM   4661 C  CG  . GLU   B 1 301 ? -35.331 6.186   13.790  1.00 90.07  ? 307 GLU   B CG  1 
ATOM   4662 C  CD  . GLU   B 1 301 ? -35.758 6.627   12.403  1.00 107.31 ? 307 GLU   B CD  1 
ATOM   4663 O  OE1 . GLU   B 1 301 ? -35.330 7.717   11.957  1.00 103.82 ? 307 GLU   B OE1 1 
ATOM   4664 O  OE2 . GLU   B 1 301 ? -36.480 5.851   11.736  1.00 97.80  ? 307 GLU   B OE2 1 
ATOM   4665 N  N   . ALA   B 1 302 ? -34.969 8.602   17.819  1.00 75.71  ? 308 ALA   B N   1 
ATOM   4666 C  CA  . ALA   B 1 302 ? -34.525 9.722   18.655  1.00 75.22  ? 308 ALA   B CA  1 
ATOM   4667 C  C   . ALA   B 1 302 ? -33.719 9.187   19.840  1.00 76.57  ? 308 ALA   B C   1 
ATOM   4668 O  O   . ALA   B 1 302 ? -32.698 9.774   20.213  1.00 75.41  ? 308 ALA   B O   1 
ATOM   4669 C  CB  . ALA   B 1 302 ? -35.730 10.513  19.154  1.00 76.09  ? 308 ALA   B CB  1 
ATOM   4670 N  N   . LYS   B 1 303 ? -34.179 8.056   20.412  1.00 71.79  ? 309 LYS   B N   1 
ATOM   4671 C  CA  . LYS   B 1 303 ? -33.544 7.396   21.550  1.00 70.88  ? 309 LYS   B CA  1 
ATOM   4672 C  C   . LYS   B 1 303 ? -32.214 6.750   21.186  1.00 71.56  ? 309 LYS   B C   1 
ATOM   4673 O  O   . LYS   B 1 303 ? -31.283 6.845   21.982  1.00 71.46  ? 309 LYS   B O   1 
ATOM   4674 C  CB  . LYS   B 1 303 ? -34.498 6.403   22.236  1.00 73.51  ? 309 LYS   B CB  1 
ATOM   4675 C  CG  . LYS   B 1 303 ? -35.499 7.091   23.154  1.00 86.28  ? 309 LYS   B CG  1 
ATOM   4676 C  CD  . LYS   B 1 303 ? -36.194 6.119   24.088  1.00 96.24  ? 309 LYS   B CD  1 
ATOM   4677 C  CE  . LYS   B 1 303 ? -37.093 6.845   25.058  1.00 107.80 ? 309 LYS   B CE  1 
ATOM   4678 N  NZ  . LYS   B 1 303 ? -37.686 5.923   26.062  1.00 116.45 ? 309 LYS   B NZ  1 
ATOM   4679 N  N   . THR   B 1 304 ? -32.111 6.127   19.980  1.00 64.93  ? 310 THR   B N   1 
ATOM   4680 C  CA  . THR   B 1 304 ? -30.885 5.483   19.485  1.00 63.38  ? 310 THR   B CA  1 
ATOM   4681 C  C   . THR   B 1 304 ? -29.730 6.487   19.361  1.00 64.05  ? 310 THR   B C   1 
ATOM   4682 O  O   . THR   B 1 304 ? -28.622 6.185   19.800  1.00 63.82  ? 310 THR   B O   1 
ATOM   4683 C  CB  . THR   B 1 304 ? -31.163 4.699   18.186  1.00 72.31  ? 310 THR   B CB  1 
ATOM   4684 O  OG1 . THR   B 1 304 ? -32.114 3.672   18.469  1.00 72.85  ? 310 THR   B OG1 1 
ATOM   4685 C  CG2 . THR   B 1 304 ? -29.906 4.064   17.581  1.00 71.40  ? 310 THR   B CG2 1 
ATOM   4686 N  N   . THR   B 1 305 ? -29.999 7.679   18.795  1.00 58.81  ? 311 THR   B N   1 
ATOM   4687 C  CA  . THR   B 1 305 ? -29.011 8.750   18.583  1.00 57.26  ? 311 THR   B CA  1 
ATOM   4688 C  C   . THR   B 1 305 ? -28.510 9.341   19.904  1.00 59.33  ? 311 THR   B C   1 
ATOM   4689 O  O   . THR   B 1 305 ? -27.336 9.734   20.002  1.00 58.47  ? 311 THR   B O   1 
ATOM   4690 C  CB  . THR   B 1 305 ? -29.597 9.853   17.673  1.00 62.41  ? 311 THR   B CB  1 
ATOM   4691 O  OG1 . THR   B 1 305 ? -30.494 9.282   16.709  1.00 57.77  ? 311 THR   B OG1 1 
ATOM   4692 C  CG2 . THR   B 1 305 ? -28.517 10.697  16.996  1.00 56.13  ? 311 THR   B CG2 1 
ATOM   4693 N  N   . ALA   B 1 306 ? -29.418 9.451   20.900  1.00 54.61  ? 312 ALA   B N   1 
ATOM   4694 C  CA  . ALA   B 1 306 ? -29.081 9.972   22.228  1.00 53.43  ? 312 ALA   B CA  1 
ATOM   4695 C  C   . ALA   B 1 306 ? -28.229 8.924   22.954  1.00 52.00  ? 312 ALA   B C   1 
ATOM   4696 O  O   . ALA   B 1 306 ? -27.142 9.253   23.422  1.00 48.80  ? 312 ALA   B O   1 
ATOM   4697 C  CB  . ALA   B 1 306 ? -30.345 10.286  23.019  1.00 54.39  ? 312 ALA   B CB  1 
ATOM   4698 N  N   . ASN   B 1 307 ? -28.685 7.644   22.953  1.00 48.60  ? 313 ASN   B N   1 
ATOM   4699 C  CA  . ASN   B 1 307 ? -27.968 6.522   23.568  1.00 48.04  ? 313 ASN   B CA  1 
ATOM   4700 C  C   . ASN   B 1 307 ? -26.573 6.356   22.959  1.00 49.95  ? 313 ASN   B C   1 
ATOM   4701 O  O   . ASN   B 1 307 ? -25.621 6.108   23.700  1.00 50.05  ? 313 ASN   B O   1 
ATOM   4702 C  CB  . ASN   B 1 307 ? -28.778 5.220   23.485  1.00 51.19  ? 313 ASN   B CB  1 
ATOM   4703 C  CG  . ASN   B 1 307 ? -30.007 5.187   24.364  1.00 81.37  ? 313 ASN   B CG  1 
ATOM   4704 O  OD1 . ASN   B 1 307 ? -30.039 5.750   25.462  1.00 81.59  ? 313 ASN   B OD1 1 
ATOM   4705 N  ND2 . ASN   B 1 307 ? -31.044 4.491   23.909  1.00 72.76  ? 313 ASN   B ND2 1 
ATOM   4706 N  N   . LEU   B 1 308 ? -26.443 6.589   21.628  1.00 44.07  ? 314 LEU   B N   1 
ATOM   4707 C  CA  . LEU   B 1 308 ? -25.175 6.526   20.898  1.00 42.98  ? 314 LEU   B CA  1 
ATOM   4708 C  C   . LEU   B 1 308 ? -24.202 7.595   21.355  1.00 44.80  ? 314 LEU   B C   1 
ATOM   4709 O  O   . LEU   B 1 308 ? -23.012 7.309   21.509  1.00 43.46  ? 314 LEU   B O   1 
ATOM   4710 C  CB  . LEU   B 1 308 ? -25.392 6.606   19.361  1.00 42.96  ? 314 LEU   B CB  1 
ATOM   4711 C  CG  . LEU   B 1 308 ? -24.141 6.626   18.460  1.00 46.48  ? 314 LEU   B CG  1 
ATOM   4712 C  CD1 . LEU   B 1 308 ? -23.300 5.352   18.617  1.00 46.21  ? 314 LEU   B CD1 1 
ATOM   4713 C  CD2 . LEU   B 1 308 ? -24.514 6.825   17.015  1.00 46.75  ? 314 LEU   B CD2 1 
ATOM   4714 N  N   . ALA   B 1 309 ? -24.695 8.835   21.518  1.00 42.37  ? 315 ALA   B N   1 
ATOM   4715 C  CA  . ALA   B 1 309 ? -23.897 9.999   21.938  1.00 42.45  ? 315 ALA   B CA  1 
ATOM   4716 C  C   . ALA   B 1 309 ? -23.308 9.779   23.358  1.00 46.59  ? 315 ALA   B C   1 
ATOM   4717 O  O   . ALA   B 1 309 ? -22.134 10.086  23.597  1.00 45.19  ? 315 ALA   B O   1 
ATOM   4718 C  CB  . ALA   B 1 309 ? -24.767 11.253  21.903  1.00 43.38  ? 315 ALA   B CB  1 
ATOM   4719 N  N   . VAL   B 1 310 ? -24.109 9.192   24.266  1.00 44.36  ? 316 VAL   B N   1 
ATOM   4720 C  CA  . VAL   B 1 310 ? -23.656 8.851   25.630  1.00 45.12  ? 316 VAL   B CA  1 
ATOM   4721 C  C   . VAL   B 1 310 ? -22.515 7.809   25.524  1.00 45.96  ? 316 VAL   B C   1 
ATOM   4722 O  O   . VAL   B 1 310 ? -21.458 7.997   26.127  1.00 44.31  ? 316 VAL   B O   1 
ATOM   4723 C  CB  . VAL   B 1 310 ? -24.832 8.392   26.540  1.00 49.46  ? 316 VAL   B CB  1 
ATOM   4724 C  CG1 . VAL   B 1 310 ? -24.334 7.823   27.871  1.00 49.37  ? 316 VAL   B CG1 1 
ATOM   4725 C  CG2 . VAL   B 1 310 ? -25.812 9.539   26.779  1.00 49.42  ? 316 VAL   B CG2 1 
ATOM   4726 N  N   . ASP   B 1 311 ? -22.700 6.776   24.668  1.00 42.39  ? 317 ASP   B N   1 
ATOM   4727 C  CA  . ASP   B 1 311 ? -21.674 5.744   24.456  1.00 41.35  ? 317 ASP   B CA  1 
ATOM   4728 C  C   . ASP   B 1 311 ? -20.329 6.289   24.032  1.00 42.72  ? 317 ASP   B C   1 
ATOM   4729 O  O   . ASP   B 1 311 ? -19.313 5.814   24.539  1.00 42.55  ? 317 ASP   B O   1 
ATOM   4730 C  CB  . ASP   B 1 311 ? -22.150 4.666   23.476  1.00 42.66  ? 317 ASP   B CB  1 
ATOM   4731 C  CG  . ASP   B 1 311 ? -23.178 3.731   24.050  1.00 51.65  ? 317 ASP   B CG  1 
ATOM   4732 O  OD1 . ASP   B 1 311 ? -23.211 3.575   25.289  1.00 52.22  ? 317 ASP   B OD1 1 
ATOM   4733 O  OD2 . ASP   B 1 311 ? -23.934 3.126   23.261  1.00 59.92  ? 317 ASP   B OD2 1 
ATOM   4734 N  N   . VAL   B 1 312 ? -20.306 7.294   23.117  1.00 38.43  ? 318 VAL   B N   1 
ATOM   4735 C  CA  . VAL   B 1 312 ? -19.053 7.899   22.621  1.00 37.54  ? 318 VAL   B CA  1 
ATOM   4736 C  C   . VAL   B 1 312 ? -18.279 8.585   23.758  1.00 40.68  ? 318 VAL   B C   1 
ATOM   4737 O  O   . VAL   B 1 312 ? -17.057 8.417   23.854  1.00 39.02  ? 318 VAL   B O   1 
ATOM   4738 C  CB  . VAL   B 1 312 ? -19.297 8.867   21.406  1.00 41.68  ? 318 VAL   B CB  1 
ATOM   4739 C  CG1 . VAL   B 1 312 ? -18.015 9.577   20.976  1.00 41.49  ? 318 VAL   B CG1 1 
ATOM   4740 C  CG2 . VAL   B 1 312 ? -19.920 8.134   20.223  1.00 41.31  ? 318 VAL   B CG2 1 
ATOM   4741 N  N   . ILE   B 1 313 ? -18.981 9.401   24.579  1.00 38.57  ? 319 ILE   B N   1 
ATOM   4742 C  CA  . ILE   B 1 313 ? -18.355 10.126  25.698  1.00 38.77  ? 319 ILE   B CA  1 
ATOM   4743 C  C   . ILE   B 1 313 ? -17.883 9.133   26.770  1.00 40.00  ? 319 ILE   B C   1 
ATOM   4744 O  O   . ILE   B 1 313 ? -16.735 9.215   27.206  1.00 38.15  ? 319 ILE   B O   1 
ATOM   4745 C  CB  . ILE   B 1 313 ? -19.242 11.269  26.296  1.00 42.77  ? 319 ILE   B CB  1 
ATOM   4746 C  CG1 . ILE   B 1 313 ? -19.769 12.242  25.201  1.00 43.12  ? 319 ILE   B CG1 1 
ATOM   4747 C  CG2 . ILE   B 1 313 ? -18.458 12.035  27.387  1.00 43.36  ? 319 ILE   B CG2 1 
ATOM   4748 C  CD1 . ILE   B 1 313 ? -21.194 12.740  25.422  1.00 47.19  ? 319 ILE   B CD1 1 
ATOM   4749 N  N   . ALA   B 1 314 ? -18.746 8.164   27.135  1.00 38.33  ? 320 ALA   B N   1 
ATOM   4750 C  CA  . ALA   B 1 314 ? -18.397 7.120   28.118  1.00 37.00  ? 320 ALA   B CA  1 
ATOM   4751 C  C   . ALA   B 1 314 ? -17.152 6.355   27.692  1.00 40.57  ? 320 ALA   B C   1 
ATOM   4752 O  O   . ALA   B 1 314 ? -16.255 6.176   28.507  1.00 39.57  ? 320 ALA   B O   1 
ATOM   4753 C  CB  . ALA   B 1 314 ? -19.564 6.172   28.313  1.00 37.79  ? 320 ALA   B CB  1 
ATOM   4754 N  N   . SER   B 1 315 ? -17.053 5.955   26.391  1.00 37.06  ? 321 SER   B N   1 
ATOM   4755 C  CA  . SER   B 1 315 ? -15.866 5.251   25.890  1.00 35.80  ? 321 SER   B CA  1 
ATOM   4756 C  C   . SER   B 1 315 ? -14.635 6.125   25.884  1.00 40.08  ? 321 SER   B C   1 
ATOM   4757 O  O   . SER   B 1 315 ? -13.524 5.612   26.003  1.00 40.04  ? 321 SER   B O   1 
ATOM   4758 C  CB  . SER   B 1 315 ? -16.116 4.639   24.511  1.00 37.49  ? 321 SER   B CB  1 
ATOM   4759 O  OG  . SER   B 1 315 ? -17.287 3.840   24.517  1.00 44.87  ? 321 SER   B OG  1 
ATOM   4760 N  N   . SER   B 1 316 ? -14.816 7.458   25.818  1.00 39.54  ? 322 SER   B N   1 
ATOM   4761 C  CA  . SER   B 1 316 ? -13.675 8.381   25.831  1.00 39.80  ? 322 SER   B CA  1 
ATOM   4762 C  C   . SER   B 1 316 ? -13.027 8.504   27.220  1.00 44.17  ? 322 SER   B C   1 
ATOM   4763 O  O   . SER   B 1 316 ? -11.866 8.888   27.308  1.00 43.24  ? 322 SER   B O   1 
ATOM   4764 C  CB  . SER   B 1 316 ? -14.075 9.746   25.279  1.00 44.56  ? 322 SER   B CB  1 
ATOM   4765 O  OG  . SER   B 1 316 ? -14.635 9.642   23.978  1.00 48.53  ? 322 SER   B OG  1 
ATOM   4766 N  N   . PHE   B 1 317 ? -13.755 8.093   28.281  1.00 42.20  ? 323 PHE   B N   1 
ATOM   4767 C  CA  . PHE   B 1 317 ? -13.308 8.114   29.681  1.00 42.00  ? 323 PHE   B CA  1 
ATOM   4768 C  C   . PHE   B 1 317 ? -13.323 6.730   30.387  1.00 47.75  ? 323 PHE   B C   1 
ATOM   4769 O  O   . PHE   B 1 317 ? -13.622 6.654   31.582  1.00 47.23  ? 323 PHE   B O   1 
ATOM   4770 C  CB  . PHE   B 1 317 ? -14.106 9.153   30.492  1.00 43.12  ? 323 PHE   B CB  1 
ATOM   4771 C  CG  . PHE   B 1 317 ? -13.916 10.565  29.995  1.00 44.20  ? 323 PHE   B CG  1 
ATOM   4772 C  CD1 . PHE   B 1 317 ? -12.738 11.259  30.254  1.00 46.82  ? 323 PHE   B CD1 1 
ATOM   4773 C  CD2 . PHE   B 1 317 ? -14.904 11.191  29.242  1.00 46.07  ? 323 PHE   B CD2 1 
ATOM   4774 C  CE1 . PHE   B 1 317 ? -12.549 12.553  29.759  1.00 47.04  ? 323 PHE   B CE1 1 
ATOM   4775 C  CE2 . PHE   B 1 317 ? -14.718 12.487  28.760  1.00 48.20  ? 323 PHE   B CE2 1 
ATOM   4776 C  CZ  . PHE   B 1 317 ? -13.547 13.160  29.027  1.00 45.88  ? 323 PHE   B CZ  1 
ATOM   4777 N  N   . GLY   B 1 318 ? -12.984 5.665   29.659  1.00 44.97  ? 324 GLY   B N   1 
ATOM   4778 C  CA  . GLY   B 1 318 ? -12.859 4.342   30.262  1.00 43.72  ? 324 GLY   B CA  1 
ATOM   4779 C  C   . GLY   B 1 318 ? -13.827 3.233   29.905  1.00 44.87  ? 324 GLY   B C   1 
ATOM   4780 O  O   . GLY   B 1 318 ? -13.433 2.073   30.020  1.00 44.35  ? 324 GLY   B O   1 
ATOM   4781 N  N   . GLN   B 1 319 ? -15.090 3.539   29.521  1.00 39.53  ? 325 GLN   B N   1 
ATOM   4782 C  CA  . GLN   B 1 319 ? -16.038 2.480   29.152  1.00 39.94  ? 325 GLN   B CA  1 
ATOM   4783 C  C   . GLN   B 1 319 ? -15.497 1.639   27.970  1.00 43.65  ? 325 GLN   B C   1 
ATOM   4784 O  O   . GLN   B 1 319 ? -14.989 2.193   27.007  1.00 41.52  ? 325 GLN   B O   1 
ATOM   4785 C  CB  . GLN   B 1 319 ? -17.434 3.039   28.833  1.00 41.33  ? 325 GLN   B CB  1 
ATOM   4786 C  CG  . GLN   B 1 319 ? -18.461 1.958   28.540  1.00 57.39  ? 325 GLN   B CG  1 
ATOM   4787 C  CD  . GLN   B 1 319 ? -19.839 2.508   28.332  1.00 82.08  ? 325 GLN   B CD  1 
ATOM   4788 O  OE1 . GLN   B 1 319 ? -20.188 2.997   27.251  1.00 78.44  ? 325 GLN   B OE1 1 
ATOM   4789 N  NE2 . GLN   B 1 319 ? -20.670 2.358   29.345  1.00 76.11  ? 325 GLN   B NE2 1 
ATOM   4790 N  N   . THR   B 1 320 ? -15.542 0.311   28.081  1.00 41.95  ? 326 THR   B N   1 
ATOM   4791 C  CA  . THR   B 1 320 ? -15.046 -0.544  26.996  1.00 42.20  ? 326 THR   B CA  1 
ATOM   4792 C  C   . THR   B 1 320 ? -15.988 -1.743  26.763  1.00 45.76  ? 326 THR   B C   1 
ATOM   4793 O  O   . THR   B 1 320 ? -16.908 -1.962  27.551  1.00 45.29  ? 326 THR   B O   1 
ATOM   4794 C  CB  . THR   B 1 320 ? -13.569 -0.913  27.230  1.00 52.67  ? 326 THR   B CB  1 
ATOM   4795 O  OG1 . THR   B 1 320 ? -12.978 -1.268  25.981  1.00 62.26  ? 326 THR   B OG1 1 
ATOM   4796 C  CG2 . THR   B 1 320 ? -13.382 -2.015  28.243  1.00 47.38  ? 326 THR   B CG2 1 
ATOM   4797 N  N   . ARG   B 1 321 ? -15.765 -2.488  25.668  1.00 43.15  ? 327 ARG   B N   1 
ATOM   4798 C  CA  . ARG   B 1 321 ? -16.576 -3.654  25.306  1.00 42.56  ? 327 ARG   B CA  1 
ATOM   4799 C  C   . ARG   B 1 321 ? -16.347 -4.814  26.280  1.00 44.83  ? 327 ARG   B C   1 
ATOM   4800 O  O   . ARG   B 1 321 ? -17.284 -5.528  26.589  1.00 43.42  ? 327 ARG   B O   1 
ATOM   4801 C  CB  . ARG   B 1 321 ? -16.285 -4.092  23.858  1.00 40.96  ? 327 ARG   B CB  1 
ATOM   4802 C  CG  . ARG   B 1 321 ? -17.308 -3.622  22.822  1.00 43.78  ? 327 ARG   B CG  1 
ATOM   4803 C  CD  . ARG   B 1 321 ? -17.146 -2.171  22.385  1.00 34.86  ? 327 ARG   B CD  1 
ATOM   4804 N  NE  . ARG   B 1 321 ? -15.839 -1.899  21.776  1.00 38.83  ? 327 ARG   B NE  1 
ATOM   4805 C  CZ  . ARG   B 1 321 ? -15.560 -2.045  20.485  1.00 42.64  ? 327 ARG   B CZ  1 
ATOM   4806 N  NH1 . ARG   B 1 321 ? -16.479 -2.516  19.650  1.00 28.82  ? 327 ARG   B NH1 1 
ATOM   4807 N  NH2 . ARG   B 1 321 ? -14.350 -1.755  20.026  1.00 25.68  ? 327 ARG   B NH2 1 
ATOM   4808 N  N   . GLU   B 1 322 ? -15.120 -4.970  26.784  1.00 42.68  ? 328 GLU   B N   1 
ATOM   4809 C  CA  . GLU   B 1 322 ? -14.737 -6.036  27.720  1.00 43.54  ? 328 GLU   B CA  1 
ATOM   4810 C  C   . GLU   B 1 322 ? -15.083 -5.740  29.185  1.00 49.31  ? 328 GLU   B C   1 
ATOM   4811 O  O   . GLU   B 1 322 ? -15.032 -6.645  30.017  1.00 48.61  ? 328 GLU   B O   1 
ATOM   4812 C  CB  . GLU   B 1 322 ? -13.221 -6.308  27.608  1.00 44.99  ? 328 GLU   B CB  1 
ATOM   4813 C  CG  . GLU   B 1 322 ? -12.740 -6.262  26.169  1.00 56.93  ? 328 GLU   B CG  1 
ATOM   4814 C  CD  . GLU   B 1 322 ? -11.306 -6.614  25.832  1.00 74.15  ? 328 GLU   B CD  1 
ATOM   4815 O  OE1 . GLU   B 1 322 ? -10.479 -6.773  26.760  1.00 78.81  ? 328 GLU   B OE1 1 
ATOM   4816 O  OE2 . GLU   B 1 322 ? -11.015 -6.731  24.618  1.00 46.91  ? 328 GLU   B OE2 1 
ATOM   4817 N  N   . GLY   B 1 323 ? -15.409 -4.488  29.494  1.00 48.18  ? 329 GLY   B N   1 
ATOM   4818 C  CA  . GLY   B 1 323 ? -15.614 -4.064  30.872  1.00 48.84  ? 329 GLY   B CA  1 
ATOM   4819 C  C   . GLY   B 1 323 ? -14.233 -3.831  31.467  1.00 54.28  ? 329 GLY   B C   1 
ATOM   4820 O  O   . GLY   B 1 323 ? -13.291 -3.482  30.749  1.00 56.21  ? 329 GLY   B O   1 
ATOM   4821 N  N   . GLY   B 1 324 ? -14.061 -4.075  32.742  1.00 49.70  ? 330 GLY   B N   1 
ATOM   4822 C  CA  . GLY   B 1 324 ? -12.732 -3.885  33.310  1.00 49.18  ? 330 GLY   B CA  1 
ATOM   4823 C  C   . GLY   B 1 324 ? -12.428 -2.467  33.754  1.00 51.96  ? 330 GLY   B C   1 
ATOM   4824 O  O   . GLY   B 1 324 ? -11.400 -2.255  34.392  1.00 50.98  ? 330 GLY   B O   1 
ATOM   4825 N  N   . HIS   B 1 325 ? -13.310 -1.489  33.420  1.00 48.87  ? 331 HIS   B N   1 
ATOM   4826 C  CA  . HIS   B 1 325 ? -13.202 -0.090  33.854  1.00 49.74  ? 331 HIS   B CA  1 
ATOM   4827 C  C   . HIS   B 1 325 ? -13.420 -0.054  35.381  1.00 53.37  ? 331 HIS   B C   1 
ATOM   4828 O  O   . HIS   B 1 325 ? -12.624 0.539   36.116  1.00 51.61  ? 331 HIS   B O   1 
ATOM   4829 C  CB  . HIS   B 1 325 ? -14.194 0.831   33.108  1.00 51.28  ? 331 HIS   B CB  1 
ATOM   4830 C  CG  . HIS   B 1 325 ? -15.497 0.196   32.699  1.00 55.34  ? 331 HIS   B CG  1 
ATOM   4831 N  ND1 . HIS   B 1 325 ? -15.650 -0.412  31.453  1.00 57.47  ? 331 HIS   B ND1 1 
ATOM   4832 C  CD2 . HIS   B 1 325 ? -16.686 0.159   33.349  1.00 57.61  ? 331 HIS   B CD2 1 
ATOM   4833 C  CE1 . HIS   B 1 325 ? -16.916 -0.806  31.398  1.00 56.97  ? 331 HIS   B CE1 1 
ATOM   4834 N  NE2 . HIS   B 1 325 ? -17.578 -0.494  32.519  1.00 57.39  ? 331 HIS   B NE2 1 
ATOM   4835 N  N   . ILE   B 1 326 ? -14.453 -0.772  35.848  1.00 50.72  ? 332 ILE   B N   1 
ATOM   4836 C  CA  . ILE   B 1 326 ? -14.730 -0.961  37.269  1.00 51.17  ? 332 ILE   B CA  1 
ATOM   4837 C  C   . ILE   B 1 326 ? -13.847 -2.139  37.736  1.00 55.76  ? 332 ILE   B C   1 
ATOM   4838 O  O   . ILE   B 1 326 ? -13.889 -3.211  37.129  1.00 56.68  ? 332 ILE   B O   1 
ATOM   4839 C  CB  . ILE   B 1 326 ? -16.246 -1.181  37.537  1.00 54.35  ? 332 ILE   B CB  1 
ATOM   4840 C  CG1 . ILE   B 1 326 ? -17.024 0.142   37.336  1.00 55.17  ? 332 ILE   B CG1 1 
ATOM   4841 C  CG2 . ILE   B 1 326 ? -16.481 -1.745  38.949  1.00 55.38  ? 332 ILE   B CG2 1 
ATOM   4842 C  CD1 . ILE   B 1 326 ? -18.481 0.002   36.842  1.00 62.84  ? 332 ILE   B CD1 1 
ATOM   4843 N  N   . VAL   B 1 327 ? -13.026 -1.917  38.775  1.00 51.45  ? 333 VAL   B N   1 
ATOM   4844 C  CA  . VAL   B 1 327 ? -12.122 -2.917  39.342  1.00 51.32  ? 333 VAL   B CA  1 
ATOM   4845 C  C   . VAL   B 1 327 ? -12.784 -3.694  40.499  1.00 56.09  ? 333 VAL   B C   1 
ATOM   4846 O  O   . VAL   B 1 327 ? -13.169 -3.107  41.511  1.00 55.44  ? 333 VAL   B O   1 
ATOM   4847 C  CB  . VAL   B 1 327 ? -10.744 -2.319  39.736  1.00 55.50  ? 333 VAL   B CB  1 
ATOM   4848 C  CG1 . VAL   B 1 327 ? -9.847  -3.358  40.403  1.00 55.19  ? 333 VAL   B CG1 1 
ATOM   4849 C  CG2 . VAL   B 1 327 ? -10.040 -1.706  38.529  1.00 55.26  ? 333 VAL   B CG2 1 
ATOM   4850 N  N   . TYR   B 1 328 ? -12.910 -5.021  40.317  1.00 52.67  ? 334 TYR   B N   1 
ATOM   4851 C  CA  . TYR   B 1 328 ? -13.453 -5.982  41.278  1.00 51.68  ? 334 TYR   B CA  1 
ATOM   4852 C  C   . TYR   B 1 328 ? -12.272 -6.540  42.083  1.00 59.59  ? 334 TYR   B C   1 
ATOM   4853 O  O   . TYR   B 1 328 ? -11.307 -7.052  41.501  1.00 58.15  ? 334 TYR   B O   1 
ATOM   4854 C  CB  . TYR   B 1 328 ? -14.177 -7.111  40.525  1.00 50.60  ? 334 TYR   B CB  1 
ATOM   4855 C  CG  . TYR   B 1 328 ? -15.251 -7.815  41.320  1.00 48.83  ? 334 TYR   B CG  1 
ATOM   4856 C  CD1 . TYR   B 1 328 ? -16.511 -7.246  41.482  1.00 49.46  ? 334 TYR   B CD1 1 
ATOM   4857 C  CD2 . TYR   B 1 328 ? -15.038 -9.088  41.842  1.00 48.84  ? 334 TYR   B CD2 1 
ATOM   4858 C  CE1 . TYR   B 1 328 ? -17.516 -7.902  42.192  1.00 49.71  ? 334 TYR   B CE1 1 
ATOM   4859 C  CE2 . TYR   B 1 328 ? -16.044 -9.767  42.529  1.00 49.07  ? 334 TYR   B CE2 1 
ATOM   4860 C  CZ  . TYR   B 1 328 ? -17.277 -9.165  42.713  1.00 54.08  ? 334 TYR   B CZ  1 
ATOM   4861 O  OH  . TYR   B 1 328 ? -18.261 -9.826  43.410  1.00 53.15  ? 334 TYR   B OH  1 
ATOM   4862 N  N   . ASP   B 1 329 ? -12.342 -6.403  43.423  1.00 60.43  ? 335 ASP   B N   1 
ATOM   4863 C  CA  . ASP   B 1 329 ? -11.305 -6.827  44.377  1.00 61.58  ? 335 ASP   B CA  1 
ATOM   4864 C  C   . ASP   B 1 329 ? -11.102 -8.356  44.476  1.00 65.02  ? 335 ASP   B C   1 
ATOM   4865 O  O   . ASP   B 1 329 ? -10.003 -8.846  44.185  1.00 65.32  ? 335 ASP   B O   1 
ATOM   4866 C  CB  . ASP   B 1 329 ? -11.572 -6.220  45.779  1.00 64.58  ? 335 ASP   B CB  1 
ATOM   4867 C  CG  . ASP   B 1 329 ? -13.039 -6.158  46.189  1.00 79.36  ? 335 ASP   B CG  1 
ATOM   4868 O  OD1 . ASP   B 1 329 ? -13.666 -7.234  46.331  1.00 80.90  ? 335 ASP   B OD1 1 
ATOM   4869 O  OD2 . ASP   B 1 329 ? -13.552 -5.035  46.389  1.00 85.67  ? 335 ASP   B OD2 1 
ATOM   4870 N  N   . GLN   B 1 330 ? -12.158 -9.092  44.913  1.00 59.59  ? 336 GLN   B N   1 
ATOM   4871 C  CA  . GLN   B 1 330 ? -12.192 -10.541 45.140  1.00 58.14  ? 336 GLN   B CA  1 
ATOM   4872 C  C   . GLN   B 1 330 ? -13.621 -11.071 45.008  1.00 55.96  ? 336 GLN   B C   1 
ATOM   4873 O  O   . GLN   B 1 330 ? -14.582 -10.346 45.287  1.00 55.07  ? 336 GLN   B O   1 
ATOM   4874 C  CB  . GLN   B 1 330 ? -11.713 -10.862 46.575  1.00 60.49  ? 336 GLN   B CB  1 
ATOM   4875 C  CG  . GLN   B 1 330 ? -10.197 -10.872 46.788  1.00 86.12  ? 336 GLN   B CG  1 
ATOM   4876 C  CD  . GLN   B 1 330 ? -9.826  -11.160 48.228  1.00 111.14 ? 336 GLN   B CD  1 
ATOM   4877 O  OE1 . GLN   B 1 330 ? -9.193  -12.176 48.538  1.00 106.91 ? 336 GLN   B OE1 1 
ATOM   4878 N  NE2 . GLN   B 1 330 ? -10.202 -10.269 49.141  1.00 105.14 ? 336 GLN   B NE2 1 
ATOM   4879 N  N   . LEU   B 1 331 ? -13.756 -12.358 44.647  1.00 48.37  ? 337 LEU   B N   1 
ATOM   4880 C  CA  . LEU   B 1 331 ? -15.051 -13.029 44.542  1.00 46.56  ? 337 LEU   B CA  1 
ATOM   4881 C  C   . LEU   B 1 331 ? -15.573 -13.410 45.935  1.00 49.47  ? 337 LEU   B C   1 
ATOM   4882 O  O   . LEU   B 1 331 ? -14.802 -13.949 46.733  1.00 47.41  ? 337 LEU   B O   1 
ATOM   4883 C  CB  . LEU   B 1 331 ? -14.926 -14.339 43.731  1.00 45.87  ? 337 LEU   B CB  1 
ATOM   4884 C  CG  . LEU   B 1 331 ? -14.681 -14.240 42.234  1.00 49.52  ? 337 LEU   B CG  1 
ATOM   4885 C  CD1 . LEU   B 1 331 ? -14.295 -15.579 41.680  1.00 49.32  ? 337 LEU   B CD1 1 
ATOM   4886 C  CD2 . LEU   B 1 331 ? -15.899 -13.692 41.505  1.00 50.25  ? 337 LEU   B CD2 1 
ATOM   4887 N  N   . PRO   B 1 332 ? -16.884 -13.252 46.221  1.00 47.89  ? 338 PRO   B N   1 
ATOM   4888 C  CA  . PRO   B 1 332 ? -17.406 -13.735 47.514  1.00 48.33  ? 338 PRO   B CA  1 
ATOM   4889 C  C   . PRO   B 1 332 ? -17.312 -15.262 47.590  1.00 54.41  ? 338 PRO   B C   1 
ATOM   4890 O  O   . PRO   B 1 332 ? -17.441 -15.942 46.569  1.00 52.17  ? 338 PRO   B O   1 
ATOM   4891 C  CB  . PRO   B 1 332 ? -18.862 -13.257 47.518  1.00 49.59  ? 338 PRO   B CB  1 
ATOM   4892 C  CG  . PRO   B 1 332 ? -18.959 -12.245 46.416  1.00 53.76  ? 338 PRO   B CG  1 
ATOM   4893 C  CD  . PRO   B 1 332 ? -17.963 -12.677 45.395  1.00 49.24  ? 338 PRO   B CD  1 
ATOM   4894 N  N   . THR   B 1 333 ? -16.995 -15.791 48.782  1.00 54.08  ? 339 THR   B N   1 
ATOM   4895 C  CA  . THR   B 1 333 ? -16.859 -17.234 49.018  1.00 54.97  ? 339 THR   B CA  1 
ATOM   4896 C  C   . THR   B 1 333 ? -18.140 -17.772 49.681  1.00 59.11  ? 339 THR   B C   1 
ATOM   4897 O  O   . THR   B 1 333 ? -18.751 -17.037 50.460  1.00 58.52  ? 339 THR   B O   1 
ATOM   4898 C  CB  . THR   B 1 333 ? -15.588 -17.554 49.824  1.00 67.08  ? 339 THR   B CB  1 
ATOM   4899 O  OG1 . THR   B 1 333 ? -15.598 -16.808 51.042  1.00 70.93  ? 339 THR   B OG1 1 
ATOM   4900 C  CG2 . THR   B 1 333 ? -14.310 -17.270 49.046  1.00 65.51  ? 339 THR   B CG2 1 
ATOM   4901 N  N   . PRO   B 1 334 ? -18.589 -19.016 49.365  1.00 56.33  ? 340 PRO   B N   1 
ATOM   4902 C  CA  . PRO   B 1 334 ? -19.830 -19.535 49.977  1.00 60.38  ? 340 PRO   B CA  1 
ATOM   4903 C  C   . PRO   B 1 334 ? -19.693 -19.813 51.474  1.00 86.92  ? 340 PRO   B C   1 
ATOM   4904 O  O   . PRO   B 1 334 ? -18.599 -20.116 51.944  1.00 54.48  ? 340 PRO   B O   1 
ATOM   4905 C  CB  . PRO   B 1 334 ? -20.096 -20.834 49.197  1.00 61.68  ? 340 PRO   B CB  1 
ATOM   4906 C  CG  . PRO   B 1 334 ? -19.208 -20.768 47.982  1.00 64.64  ? 340 PRO   B CG  1 
ATOM   4907 C  CD  . PRO   B 1 334 ? -18.012 -20.003 48.432  1.00 59.17  ? 340 PRO   B CD  1 
ATOM   4908 N  N   . VAL   C 1 17  ? -21.133 -37.163 5.266   1.00 51.54  ? 23  VAL   C N   1 
ATOM   4909 C  CA  . VAL   C 1 17  ? -22.438 -37.386 5.901   1.00 51.32  ? 23  VAL   C CA  1 
ATOM   4910 C  C   . VAL   C 1 17  ? -22.344 -37.191 7.429   1.00 53.67  ? 23  VAL   C C   1 
ATOM   4911 O  O   . VAL   C 1 17  ? -21.642 -37.951 8.107   1.00 53.38  ? 23  VAL   C O   1 
ATOM   4912 C  CB  . VAL   C 1 17  ? -23.069 -38.763 5.524   1.00 55.88  ? 23  VAL   C CB  1 
ATOM   4913 C  CG1 . VAL   C 1 17  ? -24.405 -38.985 6.242   1.00 55.35  ? 23  VAL   C CG1 1 
ATOM   4914 C  CG2 . VAL   C 1 17  ? -23.251 -38.893 4.009   1.00 56.11  ? 23  VAL   C CG2 1 
ATOM   4915 N  N   . HIS   C 1 18  ? -23.072 -36.191 7.962   1.00 48.22  ? 24  HIS   C N   1 
ATOM   4916 C  CA  . HIS   C 1 18  ? -23.118 -35.912 9.405   1.00 47.12  ? 24  HIS   C CA  1 
ATOM   4917 C  C   . HIS   C 1 18  ? -24.393 -36.511 10.007  1.00 45.46  ? 24  HIS   C C   1 
ATOM   4918 O  O   . HIS   C 1 18  ? -25.468 -36.298 9.454   1.00 44.42  ? 24  HIS   C O   1 
ATOM   4919 C  CB  . HIS   C 1 18  ? -23.148 -34.395 9.677   1.00 49.02  ? 24  HIS   C CB  1 
ATOM   4920 C  CG  . HIS   C 1 18  ? -22.088 -33.603 8.984   1.00 53.48  ? 24  HIS   C CG  1 
ATOM   4921 N  ND1 . HIS   C 1 18  ? -20.783 -33.587 9.442   1.00 56.10  ? 24  HIS   C ND1 1 
ATOM   4922 C  CD2 . HIS   C 1 18  ? -22.192 -32.763 7.930   1.00 55.59  ? 24  HIS   C CD2 1 
ATOM   4923 C  CE1 . HIS   C 1 18  ? -20.128 -32.777 8.626   1.00 55.44  ? 24  HIS   C CE1 1 
ATOM   4924 N  NE2 . HIS   C 1 18  ? -20.934 -32.265 7.697   1.00 55.67  ? 24  HIS   C NE2 1 
ATOM   4925 N  N   . SER   C 1 19  ? -24.280 -37.227 11.138  1.00 39.17  ? 25  SER   C N   1 
ATOM   4926 C  CA  . SER   C 1 19  ? -25.434 -37.758 11.884  1.00 38.02  ? 25  SER   C CA  1 
ATOM   4927 C  C   . SER   C 1 19  ? -25.750 -36.692 12.937  1.00 38.45  ? 25  SER   C C   1 
ATOM   4928 O  O   . SER   C 1 19  ? -24.886 -36.354 13.748  1.00 36.24  ? 25  SER   C O   1 
ATOM   4929 C  CB  . SER   C 1 19  ? -25.121 -39.111 12.518  1.00 41.19  ? 25  SER   C CB  1 
ATOM   4930 O  OG  . SER   C 1 19  ? -25.354 -40.148 11.578  1.00 50.29  ? 25  SER   C OG  1 
ATOM   4931 N  N   . VAL   C 1 20  ? -26.941 -36.067 12.821  1.00 34.28  ? 26  VAL   C N   1 
ATOM   4932 C  CA  . VAL   C 1 20  ? -27.344 -34.918 13.633  1.00 32.72  ? 26  VAL   C CA  1 
ATOM   4933 C  C   . VAL   C 1 20  ? -28.641 -35.190 14.387  1.00 35.08  ? 26  VAL   C C   1 
ATOM   4934 O  O   . VAL   C 1 20  ? -29.620 -35.616 13.790  1.00 35.11  ? 26  VAL   C O   1 
ATOM   4935 C  CB  . VAL   C 1 20  ? -27.462 -33.649 12.745  1.00 36.51  ? 26  VAL   C CB  1 
ATOM   4936 C  CG1 . VAL   C 1 20  ? -27.929 -32.432 13.546  1.00 36.07  ? 26  VAL   C CG1 1 
ATOM   4937 C  CG2 . VAL   C 1 20  ? -26.161 -33.354 11.986  1.00 36.30  ? 26  VAL   C CG2 1 
ATOM   4938 N  N   . ALA   C 1 21  ? -28.627 -34.963 15.694  1.00 30.37  ? 27  ALA   C N   1 
ATOM   4939 C  CA  . ALA   C 1 21  ? -29.795 -35.102 16.557  1.00 30.97  ? 27  ALA   C CA  1 
ATOM   4940 C  C   . ALA   C 1 21  ? -30.244 -33.691 16.929  1.00 33.99  ? 27  ALA   C C   1 
ATOM   4941 O  O   . ALA   C 1 21  ? -29.411 -32.817 17.168  1.00 31.85  ? 27  ALA   C O   1 
ATOM   4942 C  CB  . ALA   C 1 21  ? -29.444 -35.882 17.808  1.00 31.77  ? 27  ALA   C CB  1 
ATOM   4943 N  N   . VAL   C 1 22  ? -31.545 -33.448 16.893  1.00 29.99  ? 28  VAL   C N   1 
ATOM   4944 C  CA  . VAL   C 1 22  ? -32.096 -32.138 17.223  1.00 29.18  ? 28  VAL   C CA  1 
ATOM   4945 C  C   . VAL   C 1 22  ? -32.941 -32.312 18.463  1.00 33.91  ? 28  VAL   C C   1 
ATOM   4946 O  O   . VAL   C 1 22  ? -33.775 -33.213 18.506  1.00 32.44  ? 28  VAL   C O   1 
ATOM   4947 C  CB  . VAL   C 1 22  ? -32.884 -31.506 16.046  1.00 32.78  ? 28  VAL   C CB  1 
ATOM   4948 C  CG1 . VAL   C 1 22  ? -33.609 -30.236 16.474  1.00 31.79  ? 28  VAL   C CG1 1 
ATOM   4949 C  CG2 . VAL   C 1 22  ? -31.974 -31.233 14.845  1.00 33.03  ? 28  VAL   C CG2 1 
ATOM   4950 N  N   . ILE   C 1 23  ? -32.680 -31.499 19.496  1.00 31.45  ? 29  ILE   C N   1 
ATOM   4951 C  CA  . ILE   C 1 23  ? -33.422 -31.555 20.768  1.00 30.79  ? 29  ILE   C CA  1 
ATOM   4952 C  C   . ILE   C 1 23  ? -34.025 -30.194 21.015  1.00 32.63  ? 29  ILE   C C   1 
ATOM   4953 O  O   . ILE   C 1 23  ? -33.290 -29.204 21.027  1.00 30.19  ? 29  ILE   C O   1 
ATOM   4954 C  CB  . ILE   C 1 23  ? -32.504 -31.977 21.953  1.00 34.18  ? 29  ILE   C CB  1 
ATOM   4955 C  CG1 . ILE   C 1 23  ? -31.918 -33.381 21.758  1.00 34.41  ? 29  ILE   C CG1 1 
ATOM   4956 C  CG2 . ILE   C 1 23  ? -33.257 -31.890 23.315  1.00 37.41  ? 29  ILE   C CG2 1 
ATOM   4957 C  CD1 . ILE   C 1 23  ? -30.822 -33.695 22.696  1.00 43.59  ? 29  ILE   C CD1 1 
ATOM   4958 N  N   . GLY   C 1 24  ? -35.348 -30.135 21.208  1.00 28.79  ? 30  GLY   C N   1 
ATOM   4959 C  CA  . GLY   C 1 24  ? -35.987 -28.880 21.571  1.00 28.90  ? 30  GLY   C CA  1 
ATOM   4960 C  C   . GLY   C 1 24  ? -36.012 -28.771 23.088  1.00 34.66  ? 30  GLY   C C   1 
ATOM   4961 O  O   . GLY   C 1 24  ? -36.476 -29.695 23.776  1.00 35.91  ? 30  GLY   C O   1 
ATOM   4962 N  N   . ALA   C 1 25  ? -35.456 -27.689 23.632  1.00 32.62  ? 31  ALA   C N   1 
ATOM   4963 C  CA  . ALA   C 1 25  ? -35.434 -27.466 25.089  1.00 33.09  ? 31  ALA   C CA  1 
ATOM   4964 C  C   . ALA   C 1 25  ? -36.222 -26.167 25.369  1.00 38.83  ? 31  ALA   C C   1 
ATOM   4965 O  O   . ALA   C 1 25  ? -35.615 -25.092 25.446  1.00 36.86  ? 31  ALA   C O   1 
ATOM   4966 C  CB  . ALA   C 1 25  ? -34.001 -27.365 25.594  1.00 34.02  ? 31  ALA   C CB  1 
ATOM   4967 N  N   . PRO   C 1 26  ? -37.585 -26.239 25.402  1.00 38.94  ? 32  PRO   C N   1 
ATOM   4968 C  CA  . PRO   C 1 26  ? -38.396 -25.016 25.607  1.00 40.54  ? 32  PRO   C CA  1 
ATOM   4969 C  C   . PRO   C 1 26  ? -38.352 -24.543 27.068  1.00 50.10  ? 32  PRO   C C   1 
ATOM   4970 O  O   . PRO   C 1 26  ? -39.315 -24.669 27.828  1.00 50.16  ? 32  PRO   C O   1 
ATOM   4971 C  CB  . PRO   C 1 26  ? -39.789 -25.443 25.130  1.00 42.13  ? 32  PRO   C CB  1 
ATOM   4972 C  CG  . PRO   C 1 26  ? -39.840 -26.900 25.370  1.00 45.68  ? 32  PRO   C CG  1 
ATOM   4973 C  CD  . PRO   C 1 26  ? -38.442 -27.439 25.297  1.00 40.52  ? 32  PRO   C CD  1 
ATOM   4974 N  N   . PHE   C 1 27  ? -37.182 -24.003 27.432  1.00 50.28  ? 33  PHE   C N   1 
ATOM   4975 C  CA  . PHE   C 1 27  ? -36.677 -23.577 28.733  1.00 52.73  ? 33  PHE   C CA  1 
ATOM   4976 C  C   . PHE   C 1 27  ? -36.768 -22.065 28.902  1.00 53.35  ? 33  PHE   C C   1 
ATOM   4977 O  O   . PHE   C 1 27  ? -36.115 -21.350 28.146  1.00 51.26  ? 33  PHE   C O   1 
ATOM   4978 C  CB  . PHE   C 1 27  ? -35.172 -23.908 28.721  1.00 57.00  ? 33  PHE   C CB  1 
ATOM   4979 C  CG  . PHE   C 1 27  ? -34.546 -24.708 29.831  1.00 60.95  ? 33  PHE   C CG  1 
ATOM   4980 C  CD1 . PHE   C 1 27  ? -34.604 -24.264 31.150  1.00 66.05  ? 33  PHE   C CD1 1 
ATOM   4981 C  CD2 . PHE   C 1 27  ? -33.752 -25.815 29.542  1.00 64.22  ? 33  PHE   C CD2 1 
ATOM   4982 C  CE1 . PHE   C 1 27  ? -33.957 -24.972 32.170  1.00 67.78  ? 33  PHE   C CE1 1 
ATOM   4983 C  CE2 . PHE   C 1 27  ? -33.100 -26.518 30.557  1.00 68.01  ? 33  PHE   C CE2 1 
ATOM   4984 C  CZ  . PHE   C 1 27  ? -33.192 -26.082 31.862  1.00 66.63  ? 33  PHE   C CZ  1 
ATOM   4985 N  N   . SER   C 1 28  ? -37.478 -21.571 29.934  1.00 49.76  ? 34  SER   C N   1 
ATOM   4986 C  CA  . SER   C 1 28  ? -37.558 -20.125 30.180  1.00 49.65  ? 34  SER   C CA  1 
ATOM   4987 C  C   . SER   C 1 28  ? -37.181 -19.700 31.606  1.00 52.58  ? 34  SER   C C   1 
ATOM   4988 O  O   . SER   C 1 28  ? -36.835 -18.538 31.809  1.00 52.20  ? 34  SER   C O   1 
ATOM   4989 C  CB  . SER   C 1 28  ? -38.934 -19.574 29.805  1.00 54.07  ? 34  SER   C CB  1 
ATOM   4990 O  OG  . SER   C 1 28  ? -39.972 -20.162 30.571  1.00 66.04  ? 34  SER   C OG  1 
ATOM   4991 N  N   . GLN   C 1 29  ? -37.212 -20.634 32.575  1.00 49.39  ? 35  GLN   C N   1 
ATOM   4992 C  CA  . GLN   C 1 29  ? -36.939 -20.367 33.997  1.00 49.79  ? 35  GLN   C CA  1 
ATOM   4993 C  C   . GLN   C 1 29  ? -35.512 -19.832 34.318  1.00 51.78  ? 35  GLN   C C   1 
ATOM   4994 O  O   . GLN   C 1 29  ? -35.285 -19.386 35.445  1.00 50.90  ? 35  GLN   C O   1 
ATOM   4995 C  CB  . GLN   C 1 29  ? -37.267 -21.595 34.865  1.00 51.59  ? 35  GLN   C CB  1 
ATOM   4996 C  CG  . GLN   C 1 29  ? -38.750 -21.728 35.241  1.00 71.57  ? 35  GLN   C CG  1 
ATOM   4997 C  CD  . GLN   C 1 29  ? -39.658 -22.156 34.107  1.00 95.94  ? 35  GLN   C CD  1 
ATOM   4998 O  OE1 . GLN   C 1 29  ? -39.341 -23.048 33.303  1.00 93.04  ? 35  GLN   C OE1 1 
ATOM   4999 N  NE2 . GLN   C 1 29  ? -40.831 -21.541 34.040  1.00 88.62  ? 35  GLN   C NE2 1 
ATOM   5000 N  N   . GLY   C 1 30  ? -34.595 -19.841 33.337  1.00 47.20  ? 36  GLY   C N   1 
ATOM   5001 C  CA  . GLY   C 1 30  ? -33.252 -19.278 33.497  1.00 45.83  ? 36  GLY   C CA  1 
ATOM   5002 C  C   . GLY   C 1 30  ? -33.245 -17.754 33.458  1.00 48.51  ? 36  GLY   C C   1 
ATOM   5003 O  O   . GLY   C 1 30  ? -32.215 -17.128 33.711  1.00 46.85  ? 36  GLY   C O   1 
ATOM   5004 N  N   . GLN   C 1 31  ? -34.397 -17.145 33.120  1.00 46.65  ? 37  GLN   C N   1 
ATOM   5005 C  CA  . GLN   C 1 31  ? -34.623 -15.693 33.056  1.00 47.55  ? 37  GLN   C CA  1 
ATOM   5006 C  C   . GLN   C 1 31  ? -36.110 -15.344 33.308  1.00 54.57  ? 37  GLN   C C   1 
ATOM   5007 O  O   . GLN   C 1 31  ? -36.896 -16.232 33.639  1.00 53.25  ? 37  GLN   C O   1 
ATOM   5008 C  CB  . GLN   C 1 31  ? -34.058 -15.049 31.764  1.00 48.64  ? 37  GLN   C CB  1 
ATOM   5009 C  CG  . GLN   C 1 31  ? -34.337 -15.808 30.468  1.00 53.06  ? 37  GLN   C CG  1 
ATOM   5010 C  CD  . GLN   C 1 31  ? -35.670 -15.451 29.886  1.00 75.84  ? 37  GLN   C CD  1 
ATOM   5011 O  OE1 . GLN   C 1 31  ? -35.818 -14.427 29.220  1.00 72.60  ? 37  GLN   C OE1 1 
ATOM   5012 N  NE2 . GLN   C 1 31  ? -36.669 -16.288 30.132  1.00 70.06  ? 37  GLN   C NE2 1 
ATOM   5013 N  N   . LYS   C 1 32  ? -36.478 -14.055 33.191  1.00 54.38  ? 38  LYS   C N   1 
ATOM   5014 C  CA  . LYS   C 1 32  ? -37.822 -13.569 33.508  1.00 55.35  ? 38  LYS   C CA  1 
ATOM   5015 C  C   . LYS   C 1 32  ? -38.679 -13.200 32.298  1.00 63.17  ? 38  LYS   C C   1 
ATOM   5016 O  O   . LYS   C 1 32  ? -39.896 -13.036 32.451  1.00 64.28  ? 38  LYS   C O   1 
ATOM   5017 C  CB  . LYS   C 1 32  ? -37.736 -12.389 34.497  1.00 57.67  ? 38  LYS   C CB  1 
ATOM   5018 C  CG  . LYS   C 1 32  ? -37.234 -12.803 35.885  1.00 70.87  ? 38  LYS   C CG  1 
ATOM   5019 C  CD  . LYS   C 1 32  ? -37.237 -11.642 36.872  1.00 79.36  ? 38  LYS   C CD  1 
ATOM   5020 C  CE  . LYS   C 1 32  ? -36.642 -12.021 38.206  1.00 84.59  ? 38  LYS   C CE  1 
ATOM   5021 N  NZ  . LYS   C 1 32  ? -35.155 -12.039 38.165  1.00 88.14  ? 38  LYS   C NZ  1 
ATOM   5022 N  N   . ARG   C 1 33  ? -38.070 -13.078 31.104  1.00 61.11  ? 39  ARG   C N   1 
ATOM   5023 C  CA  . ARG   C 1 33  ? -38.794 -12.730 29.876  1.00 61.33  ? 39  ARG   C CA  1 
ATOM   5024 C  C   . ARG   C 1 33  ? -39.434 -13.978 29.245  1.00 65.04  ? 39  ARG   C C   1 
ATOM   5025 O  O   . ARG   C 1 33  ? -38.726 -14.911 28.849  1.00 64.87  ? 39  ARG   C O   1 
ATOM   5026 C  CB  . ARG   C 1 33  ? -37.880 -11.988 28.870  1.00 62.42  ? 39  ARG   C CB  1 
ATOM   5027 C  CG  . ARG   C 1 33  ? -37.344 -10.644 29.366  1.00 75.89  ? 39  ARG   C CG  1 
ATOM   5028 C  CD  . ARG   C 1 33  ? -37.963 -9.473  28.624  1.00 89.84  ? 39  ARG   C CD  1 
ATOM   5029 N  NE  . ARG   C 1 33  ? -37.006 -8.831  27.719  1.00 100.04 ? 39  ARG   C NE  1 
ATOM   5030 C  CZ  . ARG   C 1 33  ? -37.272 -7.764  26.969  1.00 113.60 ? 39  ARG   C CZ  1 
ATOM   5031 N  NH1 . ARG   C 1 33  ? -38.476 -7.202  27.004  1.00 101.25 ? 39  ARG   C NH1 1 
ATOM   5032 N  NH2 . ARG   C 1 33  ? -36.338 -7.251  26.179  1.00 96.24  ? 39  ARG   C NH2 1 
ATOM   5033 N  N   . LYS   C 1 34  ? -40.774 -13.999 29.163  1.00 60.11  ? 40  LYS   C N   1 
ATOM   5034 C  CA  . LYS   C 1 34  ? -41.483 -15.126 28.558  1.00 59.01  ? 40  LYS   C CA  1 
ATOM   5035 C  C   . LYS   C 1 34  ? -41.468 -15.056 27.004  1.00 57.79  ? 40  LYS   C C   1 
ATOM   5036 O  O   . LYS   C 1 34  ? -41.409 -13.958 26.433  1.00 56.90  ? 40  LYS   C O   1 
ATOM   5037 C  CB  . LYS   C 1 34  ? -42.907 -15.286 29.140  1.00 62.80  ? 40  LYS   C CB  1 
ATOM   5038 C  CG  . LYS   C 1 34  ? -43.836 -14.081 28.950  1.00 84.47  ? 40  LYS   C CG  1 
ATOM   5039 C  CD  . LYS   C 1 34  ? -45.143 -14.217 29.737  1.00 95.71  ? 40  LYS   C CD  1 
ATOM   5040 C  CE  . LYS   C 1 34  ? -45.079 -13.589 31.114  1.00 103.85 ? 40  LYS   C CE  1 
ATOM   5041 N  NZ  . LYS   C 1 34  ? -46.425 -13.502 31.740  1.00 109.81 ? 40  LYS   C NZ  1 
ATOM   5042 N  N   . GLY   C 1 35  ? -41.503 -16.229 26.360  1.00 49.12  ? 41  GLY   C N   1 
ATOM   5043 C  CA  . GLY   C 1 35  ? -41.488 -16.365 24.906  1.00 46.91  ? 41  GLY   C CA  1 
ATOM   5044 C  C   . GLY   C 1 35  ? -40.341 -17.202 24.362  1.00 46.58  ? 41  GLY   C C   1 
ATOM   5045 O  O   . GLY   C 1 35  ? -40.484 -17.834 23.315  1.00 45.57  ? 41  GLY   C O   1 
ATOM   5046 N  N   . VAL   C 1 36  ? -39.204 -17.234 25.084  1.00 40.50  ? 42  VAL   C N   1 
ATOM   5047 C  CA  . VAL   C 1 36  ? -37.994 -17.988 24.713  1.00 38.86  ? 42  VAL   C CA  1 
ATOM   5048 C  C   . VAL   C 1 36  ? -38.287 -19.507 24.624  1.00 42.50  ? 42  VAL   C C   1 
ATOM   5049 O  O   . VAL   C 1 36  ? -37.621 -20.210 23.861  1.00 42.12  ? 42  VAL   C O   1 
ATOM   5050 C  CB  . VAL   C 1 36  ? -36.799 -17.618 25.630  1.00 41.32  ? 42  VAL   C CB  1 
ATOM   5051 C  CG1 . VAL   C 1 36  ? -36.878 -18.297 26.998  1.00 40.81  ? 42  VAL   C CG1 1 
ATOM   5052 C  CG2 . VAL   C 1 36  ? -35.460 -17.879 24.948  1.00 40.63  ? 42  VAL   C CG2 1 
ATOM   5053 N  N   . GLU   C 1 37  ? -39.349 -19.986 25.325  1.00 39.06  ? 43  GLU   C N   1 
ATOM   5054 C  CA  . GLU   C 1 37  ? -39.810 -21.371 25.270  1.00 39.21  ? 43  GLU   C CA  1 
ATOM   5055 C  C   . GLU   C 1 37  ? -40.347 -21.728 23.861  1.00 44.08  ? 43  GLU   C C   1 
ATOM   5056 O  O   . GLU   C 1 37  ? -40.466 -22.907 23.540  1.00 43.53  ? 43  GLU   C O   1 
ATOM   5057 C  CB  . GLU   C 1 37  ? -40.854 -21.671 26.374  1.00 40.45  ? 43  GLU   C CB  1 
ATOM   5058 C  CG  . GLU   C 1 37  ? -42.173 -20.913 26.248  1.00 49.56  ? 43  GLU   C CG  1 
ATOM   5059 C  CD  . GLU   C 1 37  ? -42.262 -19.586 26.987  1.00 73.36  ? 43  GLU   C CD  1 
ATOM   5060 O  OE1 . GLU   C 1 37  ? -41.233 -18.878 27.090  1.00 58.53  ? 43  GLU   C OE1 1 
ATOM   5061 O  OE2 . GLU   C 1 37  ? -43.375 -19.249 27.455  1.00 66.65  ? 43  GLU   C OE2 1 
ATOM   5062 N  N   . HIS   C 1 38  ? -40.674 -20.705 23.035  1.00 42.10  ? 44  HIS   C N   1 
ATOM   5063 C  CA  . HIS   C 1 38  ? -41.142 -20.866 21.654  1.00 42.26  ? 44  HIS   C CA  1 
ATOM   5064 C  C   . HIS   C 1 38  ? -39.998 -20.796 20.631  1.00 41.12  ? 44  HIS   C C   1 
ATOM   5065 O  O   . HIS   C 1 38  ? -40.219 -20.997 19.436  1.00 38.54  ? 44  HIS   C O   1 
ATOM   5066 C  CB  . HIS   C 1 38  ? -42.276 -19.880 21.328  1.00 44.75  ? 44  HIS   C CB  1 
ATOM   5067 C  CG  . HIS   C 1 38  ? -43.458 -20.049 22.232  1.00 49.79  ? 44  HIS   C CG  1 
ATOM   5068 N  ND1 . HIS   C 1 38  ? -44.308 -21.138 22.112  1.00 52.50  ? 44  HIS   C ND1 1 
ATOM   5069 C  CD2 . HIS   C 1 38  ? -43.873 -19.282 23.267  1.00 52.61  ? 44  HIS   C CD2 1 
ATOM   5070 C  CE1 . HIS   C 1 38  ? -45.218 -20.988 23.062  1.00 52.20  ? 44  HIS   C CE1 1 
ATOM   5071 N  NE2 . HIS   C 1 38  ? -44.999 -19.887 23.780  1.00 52.51  ? 44  HIS   C NE2 1 
ATOM   5072 N  N   . GLY   C 1 39  ? -38.775 -20.577 21.119  1.00 36.98  ? 45  GLY   C N   1 
ATOM   5073 C  CA  . GLY   C 1 39  ? -37.570 -20.602 20.289  1.00 35.12  ? 45  GLY   C CA  1 
ATOM   5074 C  C   . GLY   C 1 39  ? -37.413 -21.876 19.464  1.00 34.14  ? 45  GLY   C C   1 
ATOM   5075 O  O   . GLY   C 1 39  ? -37.243 -21.757 18.257  1.00 34.79  ? 45  GLY   C O   1 
ATOM   5076 N  N   . PRO   C 1 40  ? -37.539 -23.115 20.027  1.00 30.68  ? 46  PRO   C N   1 
ATOM   5077 C  CA  . PRO   C 1 40  ? -37.359 -24.322 19.193  1.00 30.42  ? 46  PRO   C CA  1 
ATOM   5078 C  C   . PRO   C 1 40  ? -38.352 -24.445 18.041  1.00 35.15  ? 46  PRO   C C   1 
ATOM   5079 O  O   . PRO   C 1 40  ? -37.914 -24.672 16.924  1.00 32.23  ? 46  PRO   C O   1 
ATOM   5080 C  CB  . PRO   C 1 40  ? -37.441 -25.482 20.200  1.00 31.55  ? 46  PRO   C CB  1 
ATOM   5081 C  CG  . PRO   C 1 40  ? -37.133 -24.884 21.497  1.00 34.39  ? 46  PRO   C CG  1 
ATOM   5082 C  CD  . PRO   C 1 40  ? -37.706 -23.491 21.447  1.00 30.61  ? 46  PRO   C CD  1 
ATOM   5083 N  N   . ALA   C 1 41  ? -39.669 -24.186 18.288  1.00 34.96  ? 47  ALA   C N   1 
ATOM   5084 C  CA  . ALA   C 1 41  ? -40.718 -24.204 17.249  1.00 35.15  ? 47  ALA   C CA  1 
ATOM   5085 C  C   . ALA   C 1 41  ? -40.437 -23.172 16.149  1.00 37.97  ? 47  ALA   C C   1 
ATOM   5086 O  O   . ALA   C 1 41  ? -40.542 -23.497 14.971  1.00 39.48  ? 47  ALA   C O   1 
ATOM   5087 C  CB  . ALA   C 1 41  ? -42.085 -23.931 17.876  1.00 36.16  ? 47  ALA   C CB  1 
ATOM   5088 N  N   . ALA   C 1 42  ? -40.062 -21.939 16.534  1.00 33.00  ? 48  ALA   C N   1 
ATOM   5089 C  CA  . ALA   C 1 42  ? -39.721 -20.851 15.617  1.00 32.59  ? 48  ALA   C CA  1 
ATOM   5090 C  C   . ALA   C 1 42  ? -38.583 -21.241 14.677  1.00 36.12  ? 48  ALA   C C   1 
ATOM   5091 O  O   . ALA   C 1 42  ? -38.639 -20.934 13.485  1.00 35.40  ? 48  ALA   C O   1 
ATOM   5092 C  CB  . ALA   C 1 42  ? -39.336 -19.616 16.402  1.00 33.47  ? 48  ALA   C CB  1 
ATOM   5093 N  N   . ILE   C 1 43  ? -37.551 -21.914 15.221  1.00 32.37  ? 49  ILE   C N   1 
ATOM   5094 C  CA  . ILE   C 1 43  ? -36.403 -22.362 14.434  1.00 31.05  ? 49  ILE   C CA  1 
ATOM   5095 C  C   . ILE   C 1 43  ? -36.828 -23.460 13.452  1.00 34.63  ? 49  ILE   C C   1 
ATOM   5096 O  O   . ILE   C 1 43  ? -36.445 -23.400 12.280  1.00 33.73  ? 49  ILE   C O   1 
ATOM   5097 C  CB  . ILE   C 1 43  ? -35.205 -22.739 15.346  1.00 32.49  ? 49  ILE   C CB  1 
ATOM   5098 C  CG1 . ILE   C 1 43  ? -34.635 -21.459 16.029  1.00 31.82  ? 49  ILE   C CG1 1 
ATOM   5099 C  CG2 . ILE   C 1 43  ? -34.108 -23.475 14.549  1.00 30.14  ? 49  ILE   C CG2 1 
ATOM   5100 C  CD1 . ILE   C 1 43  ? -33.902 -21.723 17.393  1.00 33.14  ? 49  ILE   C CD1 1 
ATOM   5101 N  N   . ARG   C 1 44  ? -37.643 -24.419 13.915  1.00 31.37  ? 50  ARG   C N   1 
ATOM   5102 C  CA  . ARG   C 1 44  ? -38.164 -25.516 13.077  1.00 32.73  ? 50  ARG   C CA  1 
ATOM   5103 C  C   . ARG   C 1 44  ? -39.089 -24.989 11.948  1.00 38.38  ? 50  ARG   C C   1 
ATOM   5104 O  O   . ARG   C 1 44  ? -39.009 -25.480 10.822  1.00 36.68  ? 50  ARG   C O   1 
ATOM   5105 C  CB  . ARG   C 1 44  ? -38.887 -26.562 13.933  1.00 31.94  ? 50  ARG   C CB  1 
ATOM   5106 C  CG  . ARG   C 1 44  ? -37.946 -27.443 14.739  1.00 31.90  ? 50  ARG   C CG  1 
ATOM   5107 C  CD  . ARG   C 1 44  ? -38.679 -28.689 15.181  1.00 36.77  ? 50  ARG   C CD  1 
ATOM   5108 N  NE  . ARG   C 1 44  ? -37.931 -29.492 16.149  1.00 34.33  ? 50  ARG   C NE  1 
ATOM   5109 C  CZ  . ARG   C 1 44  ? -37.952 -29.295 17.463  1.00 43.95  ? 50  ARG   C CZ  1 
ATOM   5110 N  NH1 . ARG   C 1 44  ? -38.598 -28.253 17.974  1.00 37.48  ? 50  ARG   C NH1 1 
ATOM   5111 N  NH2 . ARG   C 1 44  ? -37.291 -30.110 18.273  1.00 36.33  ? 50  ARG   C NH2 1 
ATOM   5112 N  N   . GLU   C 1 45  ? -39.913 -23.953 12.248  1.00 37.65  ? 51  GLU   C N   1 
ATOM   5113 C  CA  . GLU   C 1 45  ? -40.814 -23.309 11.281  1.00 37.56  ? 51  GLU   C CA  1 
ATOM   5114 C  C   . GLU   C 1 45  ? -40.049 -22.496 10.217  1.00 41.22  ? 51  GLU   C C   1 
ATOM   5115 O  O   . GLU   C 1 45  ? -40.563 -22.274 9.119   1.00 41.04  ? 51  GLU   C O   1 
ATOM   5116 C  CB  . GLU   C 1 45  ? -41.853 -22.440 12.005  1.00 39.33  ? 51  GLU   C CB  1 
ATOM   5117 C  CG  . GLU   C 1 45  ? -43.118 -23.208 12.341  1.00 57.89  ? 51  GLU   C CG  1 
ATOM   5118 C  CD  . GLU   C 1 45  ? -43.541 -23.187 13.798  1.00 92.32  ? 51  GLU   C CD  1 
ATOM   5119 O  OE1 . GLU   C 1 45  ? -43.961 -22.110 14.281  1.00 90.97  ? 51  GLU   C OE1 1 
ATOM   5120 O  OE2 . GLU   C 1 45  ? -43.488 -24.258 14.446  1.00 91.14  ? 51  GLU   C OE2 1 
ATOM   5121 N  N   . ALA   C 1 46  ? -38.807 -22.074 10.535  1.00 36.92  ? 52  ALA   C N   1 
ATOM   5122 C  CA  . ALA   C 1 46  ? -37.960 -21.333 9.607   1.00 35.81  ? 52  ALA   C CA  1 
ATOM   5123 C  C   . ALA   C 1 46  ? -37.249 -22.297 8.640   1.00 38.26  ? 52  ALA   C C   1 
ATOM   5124 O  O   . ALA   C 1 46  ? -36.460 -21.860 7.812   1.00 39.19  ? 52  ALA   C O   1 
ATOM   5125 C  CB  . ALA   C 1 46  ? -36.961 -20.473 10.372  1.00 36.46  ? 52  ALA   C CB  1 
ATOM   5126 N  N   . GLY   C 1 47  ? -37.555 -23.588 8.734   1.00 33.54  ? 53  GLY   C N   1 
ATOM   5127 C  CA  . GLY   C 1 47  ? -37.052 -24.612 7.825   1.00 32.68  ? 53  GLY   C CA  1 
ATOM   5128 C  C   . GLY   C 1 47  ? -35.769 -25.330 8.189   1.00 33.21  ? 53  GLY   C C   1 
ATOM   5129 O  O   . GLY   C 1 47  ? -35.108 -25.871 7.293   1.00 32.04  ? 53  GLY   C O   1 
ATOM   5130 N  N   . LEU   C 1 48  ? -35.455 -25.421 9.499   1.00 30.38  ? 54  LEU   C N   1 
ATOM   5131 C  CA  . LEU   C 1 48  ? -34.241 -26.089 9.997   1.00 29.78  ? 54  LEU   C CA  1 
ATOM   5132 C  C   . LEU   C 1 48  ? -34.014 -27.500 9.451   1.00 34.11  ? 54  LEU   C C   1 
ATOM   5133 O  O   . LEU   C 1 48  ? -32.924 -27.782 8.942   1.00 33.89  ? 54  LEU   C O   1 
ATOM   5134 C  CB  . LEU   C 1 48  ? -34.160 -26.112 11.553  1.00 29.11  ? 54  LEU   C CB  1 
ATOM   5135 C  CG  . LEU   C 1 48  ? -32.890 -26.823 12.108  1.00 32.55  ? 54  LEU   C CG  1 
ATOM   5136 C  CD1 . LEU   C 1 48  ? -31.599 -26.042 11.755  1.00 32.86  ? 54  LEU   C CD1 1 
ATOM   5137 C  CD2 . LEU   C 1 48  ? -33.010 -27.150 13.619  1.00 30.92  ? 54  LEU   C CD2 1 
ATOM   5138 N  N   . MET   C 1 49  ? -35.014 -28.391 9.596   1.00 31.67  ? 55  MET   C N   1 
ATOM   5139 C  CA  . MET   C 1 49  ? -34.879 -29.790 9.198   1.00 31.68  ? 55  MET   C CA  1 
ATOM   5140 C  C   . MET   C 1 49  ? -34.662 -29.960 7.701   1.00 34.70  ? 55  MET   C C   1 
ATOM   5141 O  O   . MET   C 1 49  ? -33.764 -30.715 7.318   1.00 33.75  ? 55  MET   C O   1 
ATOM   5142 C  CB  . MET   C 1 49  ? -36.044 -30.659 9.725   1.00 33.79  ? 55  MET   C CB  1 
ATOM   5143 C  CG  . MET   C 1 49  ? -36.205 -30.612 11.251  1.00 37.30  ? 55  MET   C CG  1 
ATOM   5144 S  SD  . MET   C 1 49  ? -34.657 -30.815 12.195  1.00 40.41  ? 55  MET   C SD  1 
ATOM   5145 C  CE  . MET   C 1 49  ? -34.454 -32.524 12.121  1.00 37.82  ? 55  MET   C CE  1 
ATOM   5146 N  N   . LYS   C 1 50  ? -35.439 -29.253 6.870   1.00 32.94  ? 56  LYS   C N   1 
ATOM   5147 C  CA  . LYS   C 1 50  ? -35.329 -29.264 5.395   1.00 34.31  ? 56  LYS   C CA  1 
ATOM   5148 C  C   . LYS   C 1 50  ? -33.936 -28.805 4.973   1.00 36.82  ? 56  LYS   C C   1 
ATOM   5149 O  O   . LYS   C 1 50  ? -33.331 -29.406 4.093   1.00 36.68  ? 56  LYS   C O   1 
ATOM   5150 C  CB  . LYS   C 1 50  ? -36.407 -28.358 4.762   1.00 38.68  ? 56  LYS   C CB  1 
ATOM   5151 C  CG  . LYS   C 1 50  ? -36.453 -28.342 3.233   1.00 63.85  ? 56  LYS   C CG  1 
ATOM   5152 C  CD  . LYS   C 1 50  ? -37.349 -27.209 2.726   1.00 79.60  ? 56  LYS   C CD  1 
ATOM   5153 C  CE  . LYS   C 1 50  ? -37.360 -27.079 1.218   1.00 94.98  ? 56  LYS   C CE  1 
ATOM   5154 N  NZ  . LYS   C 1 50  ? -38.270 -28.068 0.579   1.00 108.31 ? 56  LYS   C NZ  1 
ATOM   5155 N  N   . ARG   C 1 51  ? -33.415 -27.778 5.643   1.00 32.77  ? 57  ARG   C N   1 
ATOM   5156 C  CA  . ARG   C 1 51  ? -32.082 -27.250 5.365   1.00 32.09  ? 57  ARG   C CA  1 
ATOM   5157 C  C   . ARG   C 1 51  ? -30.985 -28.260 5.722   1.00 33.68  ? 57  ARG   C C   1 
ATOM   5158 O  O   . ARG   C 1 51  ? -30.088 -28.472 4.905   1.00 33.06  ? 57  ARG   C O   1 
ATOM   5159 C  CB  . ARG   C 1 51  ? -31.878 -25.906 6.066   1.00 33.26  ? 57  ARG   C CB  1 
ATOM   5160 C  CG  . ARG   C 1 51  ? -30.625 -25.190 5.596   1.00 48.56  ? 57  ARG   C CG  1 
ATOM   5161 C  CD  . ARG   C 1 51  ? -30.860 -24.392 4.323   1.00 45.74  ? 57  ARG   C CD  1 
ATOM   5162 N  NE  . ARG   C 1 51  ? -31.778 -23.291 4.544   1.00 54.69  ? 57  ARG   C NE  1 
ATOM   5163 C  CZ  . ARG   C 1 51  ? -31.456 -22.165 5.165   1.00 55.06  ? 57  ARG   C CZ  1 
ATOM   5164 N  NH1 . ARG   C 1 51  ? -32.360 -21.217 5.331   1.00 48.72  ? 57  ARG   C NH1 1 
ATOM   5165 N  NH2 . ARG   C 1 51  ? -30.225 -21.980 5.625   1.00 37.17  ? 57  ARG   C NH2 1 
ATOM   5166 N  N   . LEU   C 1 52  ? -31.079 -28.925 6.901   1.00 30.09  ? 58  LEU   C N   1 
ATOM   5167 C  CA  . LEU   C 1 52  ? -30.101 -29.962 7.287   1.00 29.67  ? 58  LEU   C CA  1 
ATOM   5168 C  C   . LEU   C 1 52  ? -30.177 -31.186 6.372   1.00 33.84  ? 58  LEU   C C   1 
ATOM   5169 O  O   . LEU   C 1 52  ? -29.133 -31.733 6.019   1.00 33.44  ? 58  LEU   C O   1 
ATOM   5170 C  CB  . LEU   C 1 52  ? -30.241 -30.358 8.759   1.00 29.12  ? 58  LEU   C CB  1 
ATOM   5171 C  CG  . LEU   C 1 52  ? -29.923 -29.254 9.775   1.00 33.40  ? 58  LEU   C CG  1 
ATOM   5172 C  CD1 . LEU   C 1 52  ? -30.248 -29.696 11.173  1.00 34.03  ? 58  LEU   C CD1 1 
ATOM   5173 C  CD2 . LEU   C 1 52  ? -28.453 -28.784 9.678   1.00 34.04  ? 58  LEU   C CD2 1 
ATOM   5174 N  N   . SER   C 1 53  ? -31.401 -31.608 5.977   1.00 32.12  ? 59  SER   C N   1 
ATOM   5175 C  CA  . SER   C 1 53  ? -31.621 -32.746 5.064   1.00 34.44  ? 59  SER   C CA  1 
ATOM   5176 C  C   . SER   C 1 53  ? -30.900 -32.518 3.724   1.00 39.90  ? 59  SER   C C   1 
ATOM   5177 O  O   . SER   C 1 53  ? -30.187 -33.411 3.265   1.00 40.35  ? 59  SER   C O   1 
ATOM   5178 C  CB  . SER   C 1 53  ? -33.110 -32.964 4.807   1.00 40.30  ? 59  SER   C CB  1 
ATOM   5179 O  OG  . SER   C 1 53  ? -33.823 -33.078 6.026   1.00 55.98  ? 59  SER   C OG  1 
ATOM   5180 N  N   . SER   C 1 54  ? -31.020 -31.299 3.160   1.00 37.73  ? 60  SER   C N   1 
ATOM   5181 C  CA  . SER   C 1 54  ? -30.382 -30.887 1.906   1.00 38.13  ? 60  SER   C CA  1 
ATOM   5182 C  C   . SER   C 1 54  ? -28.837 -30.883 1.974   1.00 42.72  ? 60  SER   C C   1 
ATOM   5183 O  O   . SER   C 1 54  ? -28.173 -30.955 0.937   1.00 42.04  ? 60  SER   C O   1 
ATOM   5184 C  CB  . SER   C 1 54  ? -30.926 -29.541 1.442   1.00 42.25  ? 60  SER   C CB  1 
ATOM   5185 O  OG  . SER   C 1 54  ? -30.291 -28.458 2.102   1.00 56.75  ? 60  SER   C OG  1 
ATOM   5186 N  N   . LEU   C 1 55  ? -28.271 -30.852 3.196   1.00 38.83  ? 61  LEU   C N   1 
ATOM   5187 C  CA  . LEU   C 1 55  ? -26.819 -30.876 3.419   1.00 38.51  ? 61  LEU   C CA  1 
ATOM   5188 C  C   . LEU   C 1 55  ? -26.312 -32.322 3.418   1.00 42.83  ? 61  LEU   C C   1 
ATOM   5189 O  O   . LEU   C 1 55  ? -25.103 -32.554 3.497   1.00 42.56  ? 61  LEU   C O   1 
ATOM   5190 C  CB  . LEU   C 1 55  ? -26.512 -30.200 4.778   1.00 38.43  ? 61  LEU   C CB  1 
ATOM   5191 C  CG  . LEU   C 1 55  ? -25.916 -28.774 4.843   1.00 43.84  ? 61  LEU   C CG  1 
ATOM   5192 C  CD1 . LEU   C 1 55  ? -26.101 -27.955 3.558   1.00 43.27  ? 61  LEU   C CD1 1 
ATOM   5193 C  CD2 . LEU   C 1 55  ? -26.414 -28.023 6.079   1.00 44.02  ? 61  LEU   C CD2 1 
ATOM   5194 N  N   . GLY   C 1 56  ? -27.245 -33.278 3.373   1.00 39.41  ? 62  GLY   C N   1 
ATOM   5195 C  CA  . GLY   C 1 56  ? -26.934 -34.698 3.398   1.00 38.61  ? 62  GLY   C CA  1 
ATOM   5196 C  C   . GLY   C 1 56  ? -26.898 -35.310 4.784   1.00 41.88  ? 62  GLY   C C   1 
ATOM   5197 O  O   . GLY   C 1 56  ? -26.491 -36.465 4.925   1.00 41.79  ? 62  GLY   C O   1 
ATOM   5198 N  N   . CYS   C 1 57  ? -27.344 -34.555 5.816   1.00 36.60  ? 63  CYS   C N   1 
ATOM   5199 C  CA  . CYS   C 1 57  ? -27.390 -35.004 7.216   1.00 35.73  ? 63  CYS   C CA  1 
ATOM   5200 C  C   . CYS   C 1 57  ? -28.385 -36.114 7.424   1.00 37.70  ? 63  CYS   C C   1 
ATOM   5201 O  O   . CYS   C 1 57  ? -29.507 -36.043 6.903   1.00 38.36  ? 63  CYS   C O   1 
ATOM   5202 C  CB  . CYS   C 1 57  ? -27.728 -33.843 8.149   1.00 36.24  ? 63  CYS   C CB  1 
ATOM   5203 S  SG  . CYS   C 1 57  ? -26.509 -32.523 8.172   1.00 40.44  ? 63  CYS   C SG  1 
ATOM   5204 N  N   . HIS   C 1 58  ? -28.017 -37.062 8.271   1.00 34.12  ? 64  HIS   C N   1 
ATOM   5205 C  CA  . HIS   C 1 58  ? -28.877 -38.147 8.735   1.00 34.41  ? 64  HIS   C CA  1 
ATOM   5206 C  C   . HIS   C 1 58  ? -29.473 -37.614 10.041  1.00 37.20  ? 64  HIS   C C   1 
ATOM   5207 O  O   . HIS   C 1 58  ? -28.746 -37.414 11.017  1.00 37.29  ? 64  HIS   C O   1 
ATOM   5208 C  CB  . HIS   C 1 58  ? -28.081 -39.430 8.951   1.00 35.66  ? 64  HIS   C CB  1 
ATOM   5209 C  CG  . HIS   C 1 58  ? -28.894 -40.508 9.577   1.00 40.18  ? 64  HIS   C CG  1 
ATOM   5210 N  ND1 . HIS   C 1 58  ? -29.961 -41.079 8.913   1.00 43.06  ? 64  HIS   C ND1 1 
ATOM   5211 C  CD2 . HIS   C 1 58  ? -28.804 -41.052 10.810  1.00 43.01  ? 64  HIS   C CD2 1 
ATOM   5212 C  CE1 . HIS   C 1 58  ? -30.458 -41.978 9.745   1.00 42.53  ? 64  HIS   C CE1 1 
ATOM   5213 N  NE2 . HIS   C 1 58  ? -29.792 -41.997 10.895  1.00 42.91  ? 64  HIS   C NE2 1 
ATOM   5214 N  N   . LEU   C 1 59  ? -30.781 -37.266 10.018  1.00 33.44  ? 65  LEU   C N   1 
ATOM   5215 C  CA  . LEU   C 1 59  ? -31.433 -36.584 11.131  1.00 32.75  ? 65  LEU   C CA  1 
ATOM   5216 C  C   . LEU   C 1 59  ? -32.254 -37.416 12.072  1.00 34.63  ? 65  LEU   C C   1 
ATOM   5217 O  O   . LEU   C 1 59  ? -32.935 -38.359 11.670  1.00 33.15  ? 65  LEU   C O   1 
ATOM   5218 C  CB  . LEU   C 1 59  ? -32.366 -35.477 10.598  1.00 33.96  ? 65  LEU   C CB  1 
ATOM   5219 C  CG  . LEU   C 1 59  ? -31.817 -34.130 10.100  1.00 39.88  ? 65  LEU   C CG  1 
ATOM   5220 C  CD1 . LEU   C 1 59  ? -30.497 -33.734 10.744  1.00 40.07  ? 65  LEU   C CD1 1 
ATOM   5221 C  CD2 . LEU   C 1 59  ? -31.861 -34.031 8.633   1.00 43.08  ? 65  LEU   C CD2 1 
ATOM   5222 N  N   . LYS   C 1 60  ? -32.233 -37.008 13.338  1.00 30.54  ? 66  LYS   C N   1 
ATOM   5223 C  CA  . LYS   C 1 60  ? -33.091 -37.551 14.377  1.00 30.70  ? 66  LYS   C CA  1 
ATOM   5224 C  C   . LYS   C 1 60  ? -33.572 -36.341 15.148  1.00 34.48  ? 66  LYS   C C   1 
ATOM   5225 O  O   . LYS   C 1 60  ? -32.747 -35.582 15.636  1.00 34.59  ? 66  LYS   C O   1 
ATOM   5226 C  CB  . LYS   C 1 60  ? -32.381 -38.544 15.293  1.00 31.82  ? 66  LYS   C CB  1 
ATOM   5227 C  CG  . LYS   C 1 60  ? -33.283 -39.057 16.433  1.00 35.33  ? 66  LYS   C CG  1 
ATOM   5228 C  CD  . LYS   C 1 60  ? -32.574 -40.051 17.338  1.00 43.17  ? 66  LYS   C CD  1 
ATOM   5229 C  CE  . LYS   C 1 60  ? -33.499 -40.835 18.221  1.00 43.83  ? 66  LYS   C CE  1 
ATOM   5230 N  NZ  . LYS   C 1 60  ? -34.596 -39.997 18.744  1.00 56.19  ? 66  LYS   C NZ  1 
ATOM   5231 N  N   . ASP   C 1 61  ? -34.892 -36.118 15.186  1.00 28.88  ? 67  ASP   C N   1 
ATOM   5232 C  CA  . ASP   C 1 61  ? -35.493 -35.035 15.938  1.00 28.40  ? 67  ASP   C CA  1 
ATOM   5233 C  C   . ASP   C 1 61  ? -36.172 -35.648 17.165  1.00 31.41  ? 67  ASP   C C   1 
ATOM   5234 O  O   . ASP   C 1 61  ? -37.026 -36.541 17.052  1.00 28.70  ? 67  ASP   C O   1 
ATOM   5235 C  CB  . ASP   C 1 61  ? -36.495 -34.222 15.097  1.00 30.70  ? 67  ASP   C CB  1 
ATOM   5236 C  CG  . ASP   C 1 61  ? -36.904 -32.877 15.708  1.00 34.70  ? 67  ASP   C CG  1 
ATOM   5237 O  OD1 . ASP   C 1 61  ? -36.491 -32.584 16.869  1.00 36.08  ? 67  ASP   C OD1 1 
ATOM   5238 O  OD2 . ASP   C 1 61  ? -37.579 -32.094 15.013  1.00 37.14  ? 67  ASP   C OD2 1 
ATOM   5239 N  N   . PHE   C 1 62  ? -35.757 -35.204 18.343  1.00 29.81  ? 68  PHE   C N   1 
ATOM   5240 C  CA  . PHE   C 1 62  ? -36.350 -35.729 19.580  1.00 30.63  ? 68  PHE   C CA  1 
ATOM   5241 C  C   . PHE   C 1 62  ? -37.650 -34.968 19.900  1.00 33.74  ? 68  PHE   C C   1 
ATOM   5242 O  O   . PHE   C 1 62  ? -38.416 -35.368 20.775  1.00 33.98  ? 68  PHE   C O   1 
ATOM   5243 C  CB  . PHE   C 1 62  ? -35.346 -35.593 20.724  1.00 31.54  ? 68  PHE   C CB  1 
ATOM   5244 C  CG  . PHE   C 1 62  ? -34.241 -36.624 20.708  1.00 32.06  ? 68  PHE   C CG  1 
ATOM   5245 C  CD1 . PHE   C 1 62  ? -33.118 -36.457 19.896  1.00 35.26  ? 68  PHE   C CD1 1 
ATOM   5246 C  CD2 . PHE   C 1 62  ? -34.285 -37.724 21.554  1.00 33.18  ? 68  PHE   C CD2 1 
ATOM   5247 C  CE1 . PHE   C 1 62  ? -32.068 -37.383 19.926  1.00 34.90  ? 68  PHE   C CE1 1 
ATOM   5248 C  CE2 . PHE   C 1 62  ? -33.237 -38.658 21.573  1.00 36.44  ? 68  PHE   C CE2 1 
ATOM   5249 C  CZ  . PHE   C 1 62  ? -32.137 -38.478 20.759  1.00 34.45  ? 68  PHE   C CZ  1 
ATOM   5250 N  N   . GLY   C 1 63  ? -37.903 -33.919 19.137  1.00 29.78  ? 69  GLY   C N   1 
ATOM   5251 C  CA  . GLY   C 1 63  ? -39.030 -33.024 19.355  1.00 30.43  ? 69  GLY   C CA  1 
ATOM   5252 C  C   . GLY   C 1 63  ? -38.658 -32.143 20.530  1.00 35.17  ? 69  GLY   C C   1 
ATOM   5253 O  O   . GLY   C 1 63  ? -37.464 -32.005 20.843  1.00 32.82  ? 69  GLY   C O   1 
ATOM   5254 N  N   . ASP   C 1 64  ? -39.658 -31.533 21.179  1.00 31.65  ? 70  ASP   C N   1 
ATOM   5255 C  CA  . ASP   C 1 64  ? -39.421 -30.679 22.343  1.00 32.98  ? 70  ASP   C CA  1 
ATOM   5256 C  C   . ASP   C 1 64  ? -39.581 -31.481 23.605  1.00 39.65  ? 70  ASP   C C   1 
ATOM   5257 O  O   . ASP   C 1 64  ? -40.572 -32.195 23.767  1.00 40.81  ? 70  ASP   C O   1 
ATOM   5258 C  CB  . ASP   C 1 64  ? -40.365 -29.460 22.353  1.00 34.60  ? 70  ASP   C CB  1 
ATOM   5259 C  CG  . ASP   C 1 64  ? -40.121 -28.462 21.237  1.00 42.71  ? 70  ASP   C CG  1 
ATOM   5260 O  OD1 . ASP   C 1 64  ? -39.016 -28.477 20.655  1.00 39.71  ? 70  ASP   C OD1 1 
ATOM   5261 O  OD2 . ASP   C 1 64  ? -41.043 -27.665 20.936  1.00 50.23  ? 70  ASP   C OD2 1 
ATOM   5262 N  N   . LEU   C 1 65  ? -38.607 -31.404 24.488  1.00 36.82  ? 71  LEU   C N   1 
ATOM   5263 C  CA  . LEU   C 1 65  ? -38.680 -32.135 25.751  1.00 37.39  ? 71  LEU   C CA  1 
ATOM   5264 C  C   . LEU   C 1 65  ? -39.686 -31.480 26.696  1.00 43.85  ? 71  LEU   C C   1 
ATOM   5265 O  O   . LEU   C 1 65  ? -39.827 -30.251 26.727  1.00 42.05  ? 71  LEU   C O   1 
ATOM   5266 C  CB  . LEU   C 1 65  ? -37.319 -32.247 26.457  1.00 37.39  ? 71  LEU   C CB  1 
ATOM   5267 C  CG  . LEU   C 1 65  ? -36.138 -32.869 25.709  1.00 41.28  ? 71  LEU   C CG  1 
ATOM   5268 C  CD1 . LEU   C 1 65  ? -34.903 -32.811 26.563  1.00 40.73  ? 71  LEU   C CD1 1 
ATOM   5269 C  CD2 . LEU   C 1 65  ? -36.419 -34.313 25.253  1.00 42.17  ? 71  LEU   C CD2 1 
ATOM   5270 N  N   . SER   C 1 66  ? -40.404 -32.331 27.430  1.00 44.82  ? 72  SER   C N   1 
ATOM   5271 C  CA  . SER   C 1 66  ? -41.382 -31.959 28.443  1.00 46.71  ? 72  SER   C CA  1 
ATOM   5272 C  C   . SER   C 1 66  ? -40.646 -32.110 29.780  1.00 52.37  ? 72  SER   C C   1 
ATOM   5273 O  O   . SER   C 1 66  ? -40.398 -33.236 30.239  1.00 51.56  ? 72  SER   C O   1 
ATOM   5274 C  CB  . SER   C 1 66  ? -42.603 -32.875 28.374  1.00 50.89  ? 72  SER   C CB  1 
ATOM   5275 O  OG  . SER   C 1 66  ? -43.590 -32.451 29.300  1.00 64.46  ? 72  SER   C OG  1 
ATOM   5276 N  N   . PHE   C 1 67  ? -40.190 -30.977 30.329  1.00 50.71  ? 73  PHE   C N   1 
ATOM   5277 C  CA  . PHE   C 1 67  ? -39.432 -30.965 31.573  1.00 52.41  ? 73  PHE   C CA  1 
ATOM   5278 C  C   . PHE   C 1 67  ? -40.360 -31.063 32.772  1.00 60.81  ? 73  PHE   C C   1 
ATOM   5279 O  O   . PHE   C 1 67  ? -41.414 -30.423 32.776  1.00 60.28  ? 73  PHE   C O   1 
ATOM   5280 C  CB  . PHE   C 1 67  ? -38.525 -29.719 31.661  1.00 54.06  ? 73  PHE   C CB  1 
ATOM   5281 C  CG  . PHE   C 1 67  ? -37.469 -29.615 30.579  1.00 55.08  ? 73  PHE   C CG  1 
ATOM   5282 C  CD1 . PHE   C 1 67  ? -36.517 -30.619 30.411  1.00 57.35  ? 73  PHE   C CD1 1 
ATOM   5283 C  CD2 . PHE   C 1 67  ? -37.395 -28.492 29.762  1.00 56.48  ? 73  PHE   C CD2 1 
ATOM   5284 C  CE1 . PHE   C 1 67  ? -35.521 -30.506 29.431  1.00 57.84  ? 73  PHE   C CE1 1 
ATOM   5285 C  CE2 . PHE   C 1 67  ? -36.397 -28.379 28.786  1.00 58.80  ? 73  PHE   C CE2 1 
ATOM   5286 C  CZ  . PHE   C 1 67  ? -35.467 -29.386 28.628  1.00 56.36  ? 73  PHE   C CZ  1 
ATOM   5287 N  N   . THR   C 1 68  ? -39.981 -31.888 33.772  1.00 60.95  ? 74  THR   C N   1 
ATOM   5288 C  CA  . THR   C 1 68  ? -40.760 -32.097 34.995  1.00 62.19  ? 74  THR   C CA  1 
ATOM   5289 C  C   . THR   C 1 68  ? -40.916 -30.769 35.758  1.00 70.05  ? 74  THR   C C   1 
ATOM   5290 O  O   . THR   C 1 68  ? -39.906 -30.148 36.111  1.00 69.16  ? 74  THR   C O   1 
ATOM   5291 C  CB  . THR   C 1 68  ? -40.185 -33.246 35.843  1.00 69.31  ? 74  THR   C CB  1 
ATOM   5292 O  OG1 . THR   C 1 68  ? -40.042 -34.411 35.029  1.00 68.02  ? 74  THR   C OG1 1 
ATOM   5293 C  CG2 . THR   C 1 68  ? -41.063 -33.580 37.049  1.00 68.06  ? 74  THR   C CG2 1 
ATOM   5294 N  N   . PRO   C 1 69  ? -42.169 -30.286 35.958  1.00 69.88  ? 75  PRO   C N   1 
ATOM   5295 C  CA  . PRO   C 1 69  ? -42.352 -29.004 36.656  1.00 70.88  ? 75  PRO   C CA  1 
ATOM   5296 C  C   . PRO   C 1 69  ? -42.117 -29.107 38.159  1.00 77.57  ? 75  PRO   C C   1 
ATOM   5297 O  O   . PRO   C 1 69  ? -42.401 -30.144 38.764  1.00 77.25  ? 75  PRO   C O   1 
ATOM   5298 C  CB  . PRO   C 1 69  ? -43.799 -28.603 36.321  1.00 72.51  ? 75  PRO   C CB  1 
ATOM   5299 C  CG  . PRO   C 1 69  ? -44.337 -29.683 35.400  1.00 76.33  ? 75  PRO   C CG  1 
ATOM   5300 C  CD  . PRO   C 1 69  ? -43.471 -30.880 35.589  1.00 71.63  ? 75  PRO   C CD  1 
ATOM   5301 N  N   . VAL   C 1 70  ? -41.562 -28.030 38.748  1.00 76.36  ? 76  VAL   C N   1 
ATOM   5302 C  CA  . VAL   C 1 70  ? -41.288 -27.919 40.186  1.00 76.77  ? 76  VAL   C CA  1 
ATOM   5303 C  C   . VAL   C 1 70  ? -42.226 -26.815 40.722  1.00 82.21  ? 76  VAL   C C   1 
ATOM   5304 O  O   . VAL   C 1 70  ? -41.870 -25.633 40.653  1.00 81.30  ? 76  VAL   C O   1 
ATOM   5305 C  CB  . VAL   C 1 70  ? -39.786 -27.647 40.513  1.00 80.39  ? 76  VAL   C CB  1 
ATOM   5306 C  CG1 . VAL   C 1 70  ? -39.526 -27.713 42.014  1.00 80.22  ? 76  VAL   C CG1 1 
ATOM   5307 C  CG2 . VAL   C 1 70  ? -38.869 -28.615 39.778  1.00 80.04  ? 76  VAL   C CG2 1 
ATOM   5308 N  N   . PRO   C 1 71  ? -43.455 -27.172 41.187  1.00 80.63  ? 77  PRO   C N   1 
ATOM   5309 C  CA  . PRO   C 1 71  ? -44.389 -26.136 41.673  1.00 81.02  ? 77  PRO   C CA  1 
ATOM   5310 C  C   . PRO   C 1 71  ? -43.882 -25.383 42.906  1.00 85.76  ? 77  PRO   C C   1 
ATOM   5311 O  O   . PRO   C 1 71  ? -44.043 -24.162 42.979  1.00 85.22  ? 77  PRO   C O   1 
ATOM   5312 C  CB  . PRO   C 1 71  ? -45.689 -26.913 41.944  1.00 82.79  ? 77  PRO   C CB  1 
ATOM   5313 C  CG  . PRO   C 1 71  ? -45.518 -28.236 41.254  1.00 87.15  ? 77  PRO   C CG  1 
ATOM   5314 C  CD  . PRO   C 1 71  ? -44.049 -28.518 41.307  1.00 82.54  ? 77  PRO   C CD  1 
ATOM   5315 N  N   . LYS   C 1 72  ? -43.242 -26.101 43.854  1.00 82.88  ? 78  LYS   C N   1 
ATOM   5316 C  CA  . LYS   C 1 72  ? -42.669 -25.486 45.050  1.00 82.97  ? 78  LYS   C CA  1 
ATOM   5317 C  C   . LYS   C 1 72  ? -41.178 -25.218 44.797  1.00 86.38  ? 78  LYS   C C   1 
ATOM   5318 O  O   . LYS   C 1 72  ? -40.341 -26.114 44.951  1.00 85.40  ? 78  LYS   C O   1 
ATOM   5319 C  CB  . LYS   C 1 72  ? -42.924 -26.337 46.315  1.00 85.81  ? 78  LYS   C CB  1 
ATOM   5320 C  CG  . LYS   C 1 72  ? -42.486 -25.648 47.608  1.00 104.07 ? 78  LYS   C CG  1 
ATOM   5321 C  CD  . LYS   C 1 72  ? -42.881 -26.427 48.858  1.00 116.01 ? 78  LYS   C CD  1 
ATOM   5322 C  CE  . LYS   C 1 72  ? -42.349 -25.796 50.129  1.00 127.34 ? 78  LYS   C CE  1 
ATOM   5323 N  NZ  . LYS   C 1 72  ? -43.003 -24.494 50.442  1.00 135.01 ? 78  LYS   C NZ  1 
ATOM   5324 N  N   . ASP   C 1 73  ? -40.869 -23.986 44.354  1.00 83.01  ? 79  ASP   C N   1 
ATOM   5325 C  CA  . ASP   C 1 73  ? -39.509 -23.559 44.033  1.00 83.02  ? 79  ASP   C CA  1 
ATOM   5326 C  C   . ASP   C 1 73  ? -39.294 -22.080 44.385  1.00 87.36  ? 79  ASP   C C   1 
ATOM   5327 O  O   . ASP   C 1 73  ? -39.543 -21.193 43.558  1.00 87.02  ? 79  ASP   C O   1 
ATOM   5328 C  CB  . ASP   C 1 73  ? -39.189 -23.855 42.550  1.00 84.67  ? 79  ASP   C CB  1 
ATOM   5329 C  CG  . ASP   C 1 73  ? -37.745 -23.661 42.111  1.00 90.23  ? 79  ASP   C CG  1 
ATOM   5330 O  OD1 . ASP   C 1 73  ? -36.868 -23.483 42.989  1.00 89.43  ? 79  ASP   C OD1 1 
ATOM   5331 O  OD2 . ASP   C 1 73  ? -37.484 -23.751 40.895  1.00 94.43  ? 79  ASP   C OD2 1 
ATOM   5332 N  N   . ASP   C 1 74  ? -38.837 -21.829 45.628  1.00 83.78  ? 80  ASP   C N   1 
ATOM   5333 C  CA  . ASP   C 1 74  ? -38.564 -20.487 46.141  1.00 83.61  ? 80  ASP   C CA  1 
ATOM   5334 C  C   . ASP   C 1 74  ? -37.143 -20.032 45.841  1.00 86.13  ? 80  ASP   C C   1 
ATOM   5335 O  O   . ASP   C 1 74  ? -36.239 -20.864 45.710  1.00 85.48  ? 80  ASP   C O   1 
ATOM   5336 C  CB  . ASP   C 1 74  ? -38.877 -20.391 47.643  1.00 86.01  ? 80  ASP   C CB  1 
ATOM   5337 C  CG  . ASP   C 1 74  ? -40.249 -19.811 47.924  1.00 99.13  ? 80  ASP   C CG  1 
ATOM   5338 O  OD1 . ASP   C 1 74  ? -40.412 -18.576 47.784  1.00 100.09 ? 80  ASP   C OD1 1 
ATOM   5339 O  OD2 . ASP   C 1 74  ? -41.164 -20.592 48.271  1.00 105.34 ? 80  ASP   C OD2 1 
ATOM   5340 N  N   . LEU   C 1 75  ? -36.955 -18.702 45.735  1.00 81.87  ? 81  LEU   C N   1 
ATOM   5341 C  CA  . LEU   C 1 75  ? -35.679 -18.056 45.421  1.00 81.38  ? 81  LEU   C CA  1 
ATOM   5342 C  C   . LEU   C 1 75  ? -34.603 -18.287 46.490  1.00 83.87  ? 81  LEU   C C   1 
ATOM   5343 O  O   . LEU   C 1 75  ? -34.879 -18.173 47.686  1.00 84.04  ? 81  LEU   C O   1 
ATOM   5344 C  CB  . LEU   C 1 75  ? -35.831 -16.555 45.076  1.00 81.61  ? 81  LEU   C CB  1 
ATOM   5345 C  CG  . LEU   C 1 75  ? -36.642 -15.626 45.991  1.00 86.49  ? 81  LEU   C CG  1 
ATOM   5346 C  CD1 . LEU   C 1 75  ? -36.163 -14.201 45.841  1.00 86.88  ? 81  LEU   C CD1 1 
ATOM   5347 C  CD2 . LEU   C 1 75  ? -38.140 -15.657 45.651  1.00 88.85  ? 81  LEU   C CD2 1 
ATOM   5348 N  N   . TYR   C 1 76  ? -33.392 -18.678 46.035  1.00 78.35  ? 82  TYR   C N   1 
ATOM   5349 C  CA  . TYR   C 1 76  ? -32.214 -18.984 46.856  1.00 77.31  ? 82  TYR   C CA  1 
ATOM   5350 C  C   . TYR   C 1 76  ? -31.487 -17.696 47.259  1.00 80.19  ? 82  TYR   C C   1 
ATOM   5351 O  O   . TYR   C 1 76  ? -31.240 -16.846 46.398  1.00 79.81  ? 82  TYR   C O   1 
ATOM   5352 C  CB  . TYR   C 1 76  ? -31.277 -19.935 46.081  1.00 78.03  ? 82  TYR   C CB  1 
ATOM   5353 C  CG  . TYR   C 1 76  ? -29.981 -20.280 46.782  1.00 79.41  ? 82  TYR   C CG  1 
ATOM   5354 C  CD1 . TYR   C 1 76  ? -29.904 -21.363 47.654  1.00 81.14  ? 82  TYR   C CD1 1 
ATOM   5355 C  CD2 . TYR   C 1 76  ? -28.810 -19.574 46.514  1.00 80.15  ? 82  TYR   C CD2 1 
ATOM   5356 C  CE1 . TYR   C 1 76  ? -28.705 -21.705 48.280  1.00 81.49  ? 82  TYR   C CE1 1 
ATOM   5357 C  CE2 . TYR   C 1 76  ? -27.609 -19.896 47.146  1.00 80.96  ? 82  TYR   C CE2 1 
ATOM   5358 C  CZ  . TYR   C 1 76  ? -27.559 -20.971 48.019  1.00 88.02  ? 82  TYR   C CZ  1 
ATOM   5359 O  OH  . TYR   C 1 76  ? -26.372 -21.305 48.625  1.00 89.21  ? 82  TYR   C OH  1 
ATOM   5360 N  N   . ASN   C 1 77  ? -31.141 -17.562 48.571  1.00 75.64  ? 83  ASN   C N   1 
ATOM   5361 C  CA  . ASN   C 1 77  ? -30.464 -16.399 49.179  1.00 74.98  ? 83  ASN   C CA  1 
ATOM   5362 C  C   . ASN   C 1 77  ? -31.109 -15.056 48.776  1.00 77.25  ? 83  ASN   C C   1 
ATOM   5363 O  O   . ASN   C 1 77  ? -30.410 -14.052 48.587  1.00 76.29  ? 83  ASN   C O   1 
ATOM   5364 C  CB  . ASN   C 1 77  ? -28.939 -16.412 48.909  1.00 77.10  ? 83  ASN   C CB  1 
ATOM   5365 C  CG  . ASN   C 1 77  ? -28.106 -17.229 49.879  1.00 108.68 ? 83  ASN   C CG  1 
ATOM   5366 O  OD1 . ASN   C 1 77  ? -28.543 -17.611 50.976  1.00 108.43 ? 83  ASN   C OD1 1 
ATOM   5367 N  ND2 . ASN   C 1 77  ? -26.862 -17.490 49.505  1.00 99.29  ? 83  ASN   C ND2 1 
ATOM   5368 N  N   . ASN   C 1 78  ? -32.458 -15.064 48.645  1.00 73.29  ? 84  ASN   C N   1 
ATOM   5369 C  CA  . ASN   C 1 78  ? -33.319 -13.944 48.258  1.00 73.09  ? 84  ASN   C CA  1 
ATOM   5370 C  C   . ASN   C 1 78  ? -32.836 -13.219 46.975  1.00 76.00  ? 84  ASN   C C   1 
ATOM   5371 O  O   . ASN   C 1 78  ? -32.784 -11.983 46.945  1.00 76.20  ? 84  ASN   C O   1 
ATOM   5372 C  CB  . ASN   C 1 78  ? -33.525 -12.974 49.433  1.00 76.66  ? 84  ASN   C CB  1 
ATOM   5373 C  CG  . ASN   C 1 78  ? -34.956 -12.533 49.589  1.00 107.85 ? 84  ASN   C CG  1 
ATOM   5374 O  OD1 . ASN   C 1 78  ? -35.770 -13.202 50.237  1.00 104.32 ? 84  ASN   C OD1 1 
ATOM   5375 N  ND2 . ASN   C 1 78  ? -35.299 -11.404 48.986  1.00 102.34 ? 84  ASN   C ND2 1 
ATOM   5376 N  N   . LEU   C 1 79  ? -32.488 -14.003 45.914  1.00 70.57  ? 85  LEU   C N   1 
ATOM   5377 C  CA  . LEU   C 1 79  ? -32.009 -13.478 44.625  1.00 69.27  ? 85  LEU   C CA  1 
ATOM   5378 C  C   . LEU   C 1 79  ? -32.181 -14.463 43.453  1.00 70.48  ? 85  LEU   C C   1 
ATOM   5379 O  O   . LEU   C 1 79  ? -32.832 -14.104 42.467  1.00 69.35  ? 85  LEU   C O   1 
ATOM   5380 C  CB  . LEU   C 1 79  ? -30.546 -12.985 44.731  1.00 69.21  ? 85  LEU   C CB  1 
ATOM   5381 C  CG  . LEU   C 1 79  ? -29.943 -12.218 43.538  1.00 73.47  ? 85  LEU   C CG  1 
ATOM   5382 C  CD1 . LEU   C 1 79  ? -30.656 -10.889 43.284  1.00 73.40  ? 85  LEU   C CD1 1 
ATOM   5383 C  CD2 . LEU   C 1 79  ? -28.478 -11.958 43.767  1.00 75.21  ? 85  LEU   C CD2 1 
ATOM   5384 N  N   . ILE   C 1 80  ? -31.580 -15.681 43.552  1.00 65.57  ? 86  ILE   C N   1 
ATOM   5385 C  CA  . ILE   C 1 80  ? -31.612 -16.733 42.514  1.00 64.36  ? 86  ILE   C CA  1 
ATOM   5386 C  C   . ILE   C 1 80  ? -33.041 -17.232 42.244  1.00 66.89  ? 86  ILE   C C   1 
ATOM   5387 O  O   . ILE   C 1 80  ? -33.574 -18.039 43.009  1.00 65.87  ? 86  ILE   C O   1 
ATOM   5388 C  CB  . ILE   C 1 80  ? -30.632 -17.919 42.811  1.00 67.64  ? 86  ILE   C CB  1 
ATOM   5389 C  CG1 . ILE   C 1 80  ? -29.242 -17.449 43.350  1.00 68.27  ? 86  ILE   C CG1 1 
ATOM   5390 C  CG2 . ILE   C 1 80  ? -30.487 -18.861 41.603  1.00 67.59  ? 86  ILE   C CG2 1 
ATOM   5391 C  CD1 . ILE   C 1 80  ? -28.426 -16.547 42.471  1.00 75.32  ? 86  ILE   C CD1 1 
ATOM   5392 N  N   . VAL   C 1 81  ? -33.635 -16.761 41.139  1.00 62.79  ? 87  VAL   C N   1 
ATOM   5393 C  CA  . VAL   C 1 81  ? -34.997 -17.096 40.718  1.00 62.77  ? 87  VAL   C CA  1 
ATOM   5394 C  C   . VAL   C 1 81  ? -35.058 -18.521 40.103  1.00 65.06  ? 87  VAL   C C   1 
ATOM   5395 O  O   . VAL   C 1 81  ? -34.149 -18.921 39.367  1.00 64.02  ? 87  VAL   C O   1 
ATOM   5396 C  CB  . VAL   C 1 81  ? -35.600 -15.973 39.812  1.00 67.55  ? 87  VAL   C CB  1 
ATOM   5397 C  CG1 . VAL   C 1 81  ? -34.799 -15.760 38.526  1.00 67.64  ? 87  VAL   C CG1 1 
ATOM   5398 C  CG2 . VAL   C 1 81  ? -37.081 -16.197 39.517  1.00 67.47  ? 87  VAL   C CG2 1 
ATOM   5399 N  N   . ASN   C 1 82  ? -36.113 -19.287 40.478  1.00 60.84  ? 88  ASN   C N   1 
ATOM   5400 C  CA  . ASN   C 1 82  ? -36.439 -20.664 40.069  1.00 60.28  ? 88  ASN   C CA  1 
ATOM   5401 C  C   . ASN   C 1 82  ? -35.228 -21.638 40.031  1.00 62.50  ? 88  ASN   C C   1 
ATOM   5402 O  O   . ASN   C 1 82  ? -35.011 -22.242 38.983  1.00 63.28  ? 88  ASN   C O   1 
ATOM   5403 C  CB  . ASN   C 1 82  ? -37.175 -20.668 38.709  1.00 62.89  ? 88  ASN   C CB  1 
ATOM   5404 C  CG  . ASN   C 1 82  ? -38.311 -19.687 38.574  1.00 85.98  ? 88  ASN   C CG  1 
ATOM   5405 O  OD1 . ASN   C 1 82  ? -39.303 -19.732 39.314  1.00 84.39  ? 88  ASN   C OD1 1 
ATOM   5406 N  ND2 . ASN   C 1 82  ? -38.215 -18.819 37.574  1.00 74.90  ? 88  ASN   C ND2 1 
ATOM   5407 N  N   . PRO   C 1 83  ? -34.433 -21.842 41.111  1.00 56.65  ? 89  PRO   C N   1 
ATOM   5408 C  CA  . PRO   C 1 83  ? -33.271 -22.738 40.988  1.00 55.76  ? 89  PRO   C CA  1 
ATOM   5409 C  C   . PRO   C 1 83  ? -33.596 -24.203 40.713  1.00 56.05  ? 89  PRO   C C   1 
ATOM   5410 O  O   . PRO   C 1 83  ? -33.031 -24.759 39.781  1.00 54.21  ? 89  PRO   C O   1 
ATOM   5411 C  CB  . PRO   C 1 83  ? -32.512 -22.557 42.311  1.00 57.78  ? 89  PRO   C CB  1 
ATOM   5412 C  CG  . PRO   C 1 83  ? -33.091 -21.368 42.945  1.00 62.95  ? 89  PRO   C CG  1 
ATOM   5413 C  CD  . PRO   C 1 83  ? -34.495 -21.246 42.460  1.00 58.62  ? 89  PRO   C CD  1 
ATOM   5414 N  N   . ARG   C 1 84  ? -34.495 -24.819 41.513  1.00 50.68  ? 90  ARG   C N   1 
ATOM   5415 C  CA  . ARG   C 1 84  ? -34.865 -26.237 41.388  1.00 49.21  ? 90  ARG   C CA  1 
ATOM   5416 C  C   . ARG   C 1 84  ? -35.343 -26.606 39.996  1.00 48.54  ? 90  ARG   C C   1 
ATOM   5417 O  O   . ARG   C 1 84  ? -34.905 -27.628 39.476  1.00 46.75  ? 90  ARG   C O   1 
ATOM   5418 C  CB  . ARG   C 1 84  ? -35.882 -26.668 42.458  1.00 49.77  ? 90  ARG   C CB  1 
ATOM   5419 C  CG  . ARG   C 1 84  ? -35.292 -26.816 43.851  1.00 64.88  ? 90  ARG   C CG  1 
ATOM   5420 C  CD  . ARG   C 1 84  ? -36.373 -26.745 44.926  1.00 75.03  ? 90  ARG   C CD  1 
ATOM   5421 N  NE  . ARG   C 1 84  ? -35.846 -26.256 46.204  1.00 77.10  ? 90  ARG   C NE  1 
ATOM   5422 C  CZ  . ARG   C 1 84  ? -35.796 -24.974 46.555  1.00 88.38  ? 90  ARG   C CZ  1 
ATOM   5423 N  NH1 . ARG   C 1 84  ? -36.247 -24.034 45.732  1.00 74.70  ? 90  ARG   C NH1 1 
ATOM   5424 N  NH2 . ARG   C 1 84  ? -35.292 -24.621 47.730  1.00 72.34  ? 90  ARG   C NH2 1 
ATOM   5425 N  N   . SER   C 1 85  ? -36.208 -25.765 39.391  1.00 44.85  ? 91  SER   C N   1 
ATOM   5426 C  CA  . SER   C 1 85  ? -36.751 -25.933 38.034  1.00 45.05  ? 91  SER   C CA  1 
ATOM   5427 C  C   . SER   C 1 85  ? -35.623 -25.996 36.993  1.00 45.95  ? 91  SER   C C   1 
ATOM   5428 O  O   . SER   C 1 85  ? -35.587 -26.935 36.206  1.00 45.05  ? 91  SER   C O   1 
ATOM   5429 C  CB  . SER   C 1 85  ? -37.697 -24.785 37.682  1.00 49.73  ? 91  SER   C CB  1 
ATOM   5430 O  OG  . SER   C 1 85  ? -38.732 -24.630 38.638  1.00 62.46  ? 91  SER   C OG  1 
ATOM   5431 N  N   . VAL   C 1 86  ? -34.694 -25.021 37.031  1.00 41.60  ? 92  VAL   C N   1 
ATOM   5432 C  CA  . VAL   C 1 86  ? -33.538 -24.891 36.131  1.00 41.17  ? 92  VAL   C CA  1 
ATOM   5433 C  C   . VAL   C 1 86  ? -32.619 -26.120 36.282  1.00 43.66  ? 92  VAL   C C   1 
ATOM   5434 O  O   . VAL   C 1 86  ? -32.269 -26.747 35.282  1.00 42.86  ? 92  VAL   C O   1 
ATOM   5435 C  CB  . VAL   C 1 86  ? -32.791 -23.532 36.351  1.00 44.88  ? 92  VAL   C CB  1 
ATOM   5436 C  CG1 . VAL   C 1 86  ? -31.474 -23.454 35.564  1.00 45.18  ? 92  VAL   C CG1 1 
ATOM   5437 C  CG2 . VAL   C 1 86  ? -33.681 -22.349 35.999  1.00 44.02  ? 92  VAL   C CG2 1 
ATOM   5438 N  N   . GLY   C 1 87  ? -32.294 -26.476 37.526  1.00 38.86  ? 93  GLY   C N   1 
ATOM   5439 C  CA  . GLY   C 1 87  ? -31.417 -27.599 37.822  1.00 37.60  ? 93  GLY   C CA  1 
ATOM   5440 C  C   . GLY   C 1 87  ? -31.937 -28.945 37.367  1.00 40.65  ? 93  GLY   C C   1 
ATOM   5441 O  O   . GLY   C 1 87  ? -31.176 -29.730 36.792  1.00 40.45  ? 93  GLY   C O   1 
ATOM   5442 N  N   . LEU   C 1 88  ? -33.225 -29.233 37.647  1.00 36.91  ? 94  LEU   C N   1 
ATOM   5443 C  CA  . LEU   C 1 88  ? -33.886 -30.493 37.307  1.00 37.75  ? 94  LEU   C CA  1 
ATOM   5444 C  C   . LEU   C 1 88  ? -34.022 -30.672 35.783  1.00 39.57  ? 94  LEU   C C   1 
ATOM   5445 O  O   . LEU   C 1 88  ? -33.739 -31.757 35.271  1.00 38.51  ? 94  LEU   C O   1 
ATOM   5446 C  CB  . LEU   C 1 88  ? -35.283 -30.585 37.995  1.00 39.20  ? 94  LEU   C CB  1 
ATOM   5447 C  CG  . LEU   C 1 88  ? -36.207 -31.751 37.570  1.00 46.18  ? 94  LEU   C CG  1 
ATOM   5448 C  CD1 . LEU   C 1 88  ? -35.630 -33.089 37.967  1.00 47.46  ? 94  LEU   C CD1 1 
ATOM   5449 C  CD2 . LEU   C 1 88  ? -37.598 -31.612 38.169  1.00 50.79  ? 94  LEU   C CD2 1 
ATOM   5450 N  N   . ALA   C 1 89  ? -34.502 -29.624 35.086  1.00 35.10  ? 95  ALA   C N   1 
ATOM   5451 C  CA  . ALA   C 1 89  ? -34.679 -29.601 33.638  1.00 35.39  ? 95  ALA   C CA  1 
ATOM   5452 C  C   . ALA   C 1 89  ? -33.332 -29.824 32.928  1.00 37.55  ? 95  ALA   C C   1 
ATOM   5453 O  O   . ALA   C 1 89  ? -33.300 -30.550 31.937  1.00 34.51  ? 95  ALA   C O   1 
ATOM   5454 C  CB  . ALA   C 1 89  ? -35.299 -28.288 33.203  1.00 36.13  ? 95  ALA   C CB  1 
ATOM   5455 N  N   . ASN   C 1 90  ? -32.229 -29.242 33.469  1.00 33.60  ? 96  ASN   C N   1 
ATOM   5456 C  CA  . ASN   C 1 90  ? -30.877 -29.451 32.940  1.00 32.20  ? 96  ASN   C CA  1 
ATOM   5457 C  C   . ASN   C 1 90  ? -30.410 -30.886 33.175  1.00 36.14  ? 96  ASN   C C   1 
ATOM   5458 O  O   . ASN   C 1 90  ? -29.779 -31.467 32.299  1.00 34.23  ? 96  ASN   C O   1 
ATOM   5459 C  CB  . ASN   C 1 90  ? -29.888 -28.413 33.506  1.00 28.17  ? 96  ASN   C CB  1 
ATOM   5460 C  CG  . ASN   C 1 90  ? -29.825 -27.177 32.655  1.00 45.28  ? 96  ASN   C CG  1 
ATOM   5461 O  OD1 . ASN   C 1 90  ? -29.520 -27.250 31.456  1.00 36.95  ? 96  ASN   C OD1 1 
ATOM   5462 N  ND2 . ASN   C 1 90  ? -30.169 -26.026 33.232  1.00 35.05  ? 96  ASN   C ND2 1 
ATOM   5463 N  N   . GLN   C 1 91  ? -30.759 -31.480 34.345  1.00 34.89  ? 97  GLN   C N   1 
ATOM   5464 C  CA  . GLN   C 1 91  ? -30.422 -32.866 34.678  1.00 34.89  ? 97  GLN   C CA  1 
ATOM   5465 C  C   . GLN   C 1 91  ? -31.065 -33.833 33.684  1.00 38.03  ? 97  GLN   C C   1 
ATOM   5466 O  O   . GLN   C 1 91  ? -30.403 -34.770 33.232  1.00 37.32  ? 97  GLN   C O   1 
ATOM   5467 C  CB  . GLN   C 1 91  ? -30.823 -33.212 36.127  1.00 35.94  ? 97  GLN   C CB  1 
ATOM   5468 C  CG  . GLN   C 1 91  ? -30.232 -34.548 36.600  1.00 48.15  ? 97  GLN   C CG  1 
ATOM   5469 C  CD  . GLN   C 1 91  ? -30.660 -34.932 37.990  1.00 63.88  ? 97  GLN   C CD  1 
ATOM   5470 O  OE1 . GLN   C 1 91  ? -31.709 -34.511 38.491  1.00 56.93  ? 97  GLN   C OE1 1 
ATOM   5471 N  NE2 . GLN   C 1 91  ? -29.874 -35.782 38.629  1.00 57.32  ? 97  GLN   C NE2 1 
ATOM   5472 N  N   . GLU   C 1 92  ? -32.330 -33.559 33.304  1.00 34.49  ? 98  GLU   C N   1 
ATOM   5473 C  CA  . GLU   C 1 92  ? -33.095 -34.348 32.328  1.00 34.86  ? 98  GLU   C CA  1 
ATOM   5474 C  C   . GLU   C 1 92  ? -32.489 -34.167 30.919  1.00 37.25  ? 98  GLU   C C   1 
ATOM   5475 O  O   . GLU   C 1 92  ? -32.253 -35.154 30.219  1.00 36.31  ? 98  GLU   C O   1 
ATOM   5476 C  CB  . GLU   C 1 92  ? -34.578 -33.913 32.335  1.00 36.08  ? 98  GLU   C CB  1 
ATOM   5477 C  CG  . GLU   C 1 92  ? -35.294 -34.277 33.626  1.00 44.34  ? 98  GLU   C CG  1 
ATOM   5478 C  CD  . GLU   C 1 92  ? -36.781 -33.975 33.684  1.00 63.41  ? 98  GLU   C CD  1 
ATOM   5479 O  OE1 . GLU   C 1 92  ? -37.531 -34.841 34.187  1.00 64.30  ? 98  GLU   C OE1 1 
ATOM   5480 O  OE2 . GLU   C 1 92  ? -37.195 -32.874 33.255  1.00 52.12  ? 98  GLU   C OE2 1 
ATOM   5481 N  N   . LEU   C 1 93  ? -32.230 -32.902 30.528  1.00 32.74  ? 99  LEU   C N   1 
ATOM   5482 C  CA  . LEU   C 1 93  ? -31.617 -32.541 29.249  1.00 31.32  ? 99  LEU   C CA  1 
ATOM   5483 C  C   . LEU   C 1 93  ? -30.259 -33.244 29.058  1.00 35.56  ? 99  LEU   C C   1 
ATOM   5484 O  O   . LEU   C 1 93  ? -30.002 -33.746 27.960  1.00 35.47  ? 99  LEU   C O   1 
ATOM   5485 C  CB  . LEU   C 1 93  ? -31.495 -31.008 29.107  1.00 30.58  ? 99  LEU   C CB  1 
ATOM   5486 C  CG  . LEU   C 1 93  ? -30.830 -30.451 27.831  1.00 32.59  ? 99  LEU   C CG  1 
ATOM   5487 C  CD1 . LEU   C 1 93  ? -31.532 -30.932 26.559  1.00 32.71  ? 99  LEU   C CD1 1 
ATOM   5488 C  CD2 . LEU   C 1 93  ? -30.797 -28.953 27.866  1.00 29.93  ? 99  LEU   C CD2 1 
ATOM   5489 N  N   . ALA   C 1 94  ? -29.424 -33.299 30.115  1.00 32.51  ? 100 ALA   C N   1 
ATOM   5490 C  CA  . ALA   C 1 94  ? -28.108 -33.958 30.087  1.00 32.16  ? 100 ALA   C CA  1 
ATOM   5491 C  C   . ALA   C 1 94  ? -28.202 -35.460 29.764  1.00 36.77  ? 100 ALA   C C   1 
ATOM   5492 O  O   . ALA   C 1 94  ? -27.359 -35.967 29.021  1.00 32.71  ? 100 ALA   C O   1 
ATOM   5493 C  CB  . ALA   C 1 94  ? -27.369 -33.736 31.395  1.00 32.07  ? 100 ALA   C CB  1 
ATOM   5494 N  N   . GLU   C 1 95  ? -29.253 -36.160 30.275  1.00 35.83  ? 101 GLU   C N   1 
ATOM   5495 C  CA  . GLU   C 1 95  ? -29.488 -37.596 29.999  1.00 35.40  ? 101 GLU   C CA  1 
ATOM   5496 C  C   . GLU   C 1 95  ? -29.753 -37.833 28.487  1.00 35.93  ? 101 GLU   C C   1 
ATOM   5497 O  O   . GLU   C 1 95  ? -29.223 -38.779 27.896  1.00 36.29  ? 101 GLU   C O   1 
ATOM   5498 C  CB  . GLU   C 1 95  ? -30.671 -38.122 30.842  1.00 37.16  ? 101 GLU   C CB  1 
ATOM   5499 C  CG  . GLU   C 1 95  ? -30.380 -38.291 32.331  1.00 54.59  ? 101 GLU   C CG  1 
ATOM   5500 C  CD  . GLU   C 1 95  ? -29.380 -39.364 32.729  1.00 92.42  ? 101 GLU   C CD  1 
ATOM   5501 O  OE1 . GLU   C 1 95  ? -28.468 -39.057 33.531  1.00 88.43  ? 101 GLU   C OE1 1 
ATOM   5502 O  OE2 . GLU   C 1 95  ? -29.517 -40.517 32.256  1.00 98.51  ? 101 GLU   C OE2 1 
ATOM   5503 N  N   . VAL   C 1 96  ? -30.557 -36.965 27.874  1.00 31.06  ? 102 VAL   C N   1 
ATOM   5504 C  CA  . VAL   C 1 96  ? -30.911 -37.011 26.454  1.00 31.97  ? 102 VAL   C CA  1 
ATOM   5505 C  C   . VAL   C 1 96  ? -29.677 -36.735 25.580  1.00 36.32  ? 102 VAL   C C   1 
ATOM   5506 O  O   . VAL   C 1 96  ? -29.395 -37.498 24.657  1.00 35.33  ? 102 VAL   C O   1 
ATOM   5507 C  CB  . VAL   C 1 96  ? -32.105 -36.068 26.093  1.00 34.89  ? 102 VAL   C CB  1 
ATOM   5508 C  CG1 . VAL   C 1 96  ? -32.585 -36.308 24.657  1.00 34.80  ? 102 VAL   C CG1 1 
ATOM   5509 C  CG2 . VAL   C 1 96  ? -33.273 -36.256 27.059  1.00 34.44  ? 102 VAL   C CG2 1 
ATOM   5510 N  N   . VAL   C 1 97  ? -28.938 -35.654 25.892  1.00 33.74  ? 103 VAL   C N   1 
ATOM   5511 C  CA  . VAL   C 1 97  ? -27.726 -35.270 25.155  1.00 32.12  ? 103 VAL   C CA  1 
ATOM   5512 C  C   . VAL   C 1 97  ? -26.713 -36.414 25.264  1.00 35.23  ? 103 VAL   C C   1 
ATOM   5513 O  O   . VAL   C 1 97  ? -26.205 -36.860 24.244  1.00 34.35  ? 103 VAL   C O   1 
ATOM   5514 C  CB  . VAL   C 1 97  ? -27.166 -33.908 25.645  1.00 34.70  ? 103 VAL   C CB  1 
ATOM   5515 C  CG1 . VAL   C 1 97  ? -25.797 -33.603 25.028  1.00 34.65  ? 103 VAL   C CG1 1 
ATOM   5516 C  CG2 . VAL   C 1 97  ? -28.148 -32.776 25.349  1.00 34.07  ? 103 VAL   C CG2 1 
ATOM   5517 N  N   . SER   C 1 98  ? -26.488 -36.937 26.486  1.00 34.65  ? 104 SER   C N   1 
ATOM   5518 C  CA  . SER   C 1 98  ? -25.546 -38.034 26.733  1.00 35.74  ? 104 SER   C CA  1 
ATOM   5519 C  C   . SER   C 1 98  ? -25.865 -39.262 25.843  1.00 40.04  ? 104 SER   C C   1 
ATOM   5520 O  O   . SER   C 1 98  ? -24.954 -39.833 25.237  1.00 37.02  ? 104 SER   C O   1 
ATOM   5521 C  CB  . SER   C 1 98  ? -25.533 -38.405 28.215  1.00 39.53  ? 104 SER   C CB  1 
ATOM   5522 O  OG  . SER   C 1 98  ? -24.549 -39.386 28.494  1.00 53.71  ? 104 SER   C OG  1 
ATOM   5523 N  N   . ARG   C 1 99  ? -27.163 -39.607 25.721  1.00 37.20  ? 105 ARG   C N   1 
ATOM   5524 C  CA  . ARG   C 1 99  ? -27.644 -40.722 24.903  1.00 37.72  ? 105 ARG   C CA  1 
ATOM   5525 C  C   . ARG   C 1 99  ? -27.408 -40.440 23.401  1.00 40.54  ? 105 ARG   C C   1 
ATOM   5526 O  O   . ARG   C 1 99  ? -26.810 -41.279 22.728  1.00 40.29  ? 105 ARG   C O   1 
ATOM   5527 C  CB  . ARG   C 1 99  ? -29.135 -41.015 25.201  1.00 39.56  ? 105 ARG   C CB  1 
ATOM   5528 C  CG  . ARG   C 1 99  ? -29.643 -42.358 24.658  1.00 63.12  ? 105 ARG   C CG  1 
ATOM   5529 C  CD  . ARG   C 1 99  ? -29.714 -43.438 25.729  1.00 86.78  ? 105 ARG   C CD  1 
ATOM   5530 N  NE  . ARG   C 1 99  ? -31.067 -43.617 26.271  1.00 102.28 ? 105 ARG   C NE  1 
ATOM   5531 C  CZ  . ARG   C 1 99  ? -31.527 -43.034 27.378  1.00 118.61 ? 105 ARG   C CZ  1 
ATOM   5532 N  NH1 . ARG   C 1 99  ? -30.752 -42.210 28.075  1.00 106.55 ? 105 ARG   C NH1 1 
ATOM   5533 N  NH2 . ARG   C 1 99  ? -32.764 -43.269 27.794  1.00 103.74 ? 105 ARG   C NH2 1 
ATOM   5534 N  N   . ALA   C 1 100 ? -27.834 -39.256 22.888  1.00 35.94  ? 106 ALA   C N   1 
ATOM   5535 C  CA  . ALA   C 1 100 ? -27.620 -38.897 21.486  1.00 35.49  ? 106 ALA   C CA  1 
ATOM   5536 C  C   . ALA   C 1 100 ? -26.120 -38.959 21.101  1.00 39.78  ? 106 ALA   C C   1 
ATOM   5537 O  O   . ALA   C 1 100 ? -25.777 -39.534 20.068  1.00 38.79  ? 106 ALA   C O   1 
ATOM   5538 C  CB  . ALA   C 1 100 ? -28.211 -37.532 21.183  1.00 36.50  ? 106 ALA   C CB  1 
ATOM   5539 N  N   . VAL   C 1 101 ? -25.243 -38.426 21.972  1.00 36.39  ? 107 VAL   C N   1 
ATOM   5540 C  CA  . VAL   C 1 101 ? -23.790 -38.407 21.786  1.00 34.95  ? 107 VAL   C CA  1 
ATOM   5541 C  C   . VAL   C 1 101 ? -23.262 -39.856 21.800  1.00 41.46  ? 107 VAL   C C   1 
ATOM   5542 O  O   . VAL   C 1 101 ? -22.448 -40.201 20.944  1.00 40.93  ? 107 VAL   C O   1 
ATOM   5543 C  CB  . VAL   C 1 101 ? -23.103 -37.467 22.815  1.00 37.33  ? 107 VAL   C CB  1 
ATOM   5544 C  CG1 . VAL   C 1 101 ? -21.594 -37.699 22.889  1.00 37.18  ? 107 VAL   C CG1 1 
ATOM   5545 C  CG2 . VAL   C 1 101 ? -23.407 -35.994 22.501  1.00 36.92  ? 107 VAL   C CG2 1 
ATOM   5546 N  N   . SER   C 1 102 ? -23.794 -40.721 22.699  1.00 41.10  ? 108 SER   C N   1 
ATOM   5547 C  CA  . SER   C 1 102 ? -23.407 -42.143 22.778  1.00 42.55  ? 108 SER   C CA  1 
ATOM   5548 C  C   . SER   C 1 102 ? -23.753 -42.883 21.482  1.00 45.50  ? 108 SER   C C   1 
ATOM   5549 O  O   . SER   C 1 102 ? -22.952 -43.690 21.001  1.00 46.05  ? 108 SER   C O   1 
ATOM   5550 C  CB  . SER   C 1 102 ? -24.110 -42.830 23.947  1.00 48.70  ? 108 SER   C CB  1 
ATOM   5551 O  OG  . SER   C 1 102 ? -23.353 -43.952 24.366  1.00 62.53  ? 108 SER   C OG  1 
ATOM   5552 N  N   . ASP   C 1 103 ? -24.929 -42.568 20.897  1.00 41.68  ? 109 ASP   C N   1 
ATOM   5553 C  CA  . ASP   C 1 103 ? -25.428 -43.147 19.647  1.00 41.95  ? 109 ASP   C CA  1 
ATOM   5554 C  C   . ASP   C 1 103 ? -24.783 -42.571 18.363  1.00 44.49  ? 109 ASP   C C   1 
ATOM   5555 O  O   . ASP   C 1 103 ? -25.260 -42.856 17.265  1.00 45.87  ? 109 ASP   C O   1 
ATOM   5556 C  CB  . ASP   C 1 103 ? -26.964 -43.049 19.586  1.00 44.81  ? 109 ASP   C CB  1 
ATOM   5557 C  CG  . ASP   C 1 103 ? -27.675 -43.839 20.676  1.00 58.57  ? 109 ASP   C CG  1 
ATOM   5558 O  OD1 . ASP   C 1 103 ? -26.985 -44.572 21.433  1.00 59.13  ? 109 ASP   C OD1 1 
ATOM   5559 O  OD2 . ASP   C 1 103 ? -28.914 -43.707 20.791  1.00 66.47  ? 109 ASP   C OD2 1 
ATOM   5560 N  N   . GLY   C 1 104 ? -23.704 -41.801 18.511  1.00 39.53  ? 110 GLY   C N   1 
ATOM   5561 C  CA  . GLY   C 1 104 ? -22.941 -41.234 17.401  1.00 38.69  ? 110 GLY   C CA  1 
ATOM   5562 C  C   . GLY   C 1 104 ? -23.489 -39.982 16.744  1.00 40.71  ? 110 GLY   C C   1 
ATOM   5563 O  O   . GLY   C 1 104 ? -22.999 -39.587 15.686  1.00 40.74  ? 110 GLY   C O   1 
ATOM   5564 N  N   . TYR   C 1 105 ? -24.505 -39.343 17.343  1.00 35.68  ? 111 TYR   C N   1 
ATOM   5565 C  CA  . TYR   C 1 105 ? -25.097 -38.121 16.784  1.00 34.01  ? 111 TYR   C CA  1 
ATOM   5566 C  C   . TYR   C 1 105 ? -24.384 -36.840 17.277  1.00 35.86  ? 111 TYR   C C   1 
ATOM   5567 O  O   . TYR   C 1 105 ? -24.019 -36.745 18.450  1.00 34.41  ? 111 TYR   C O   1 
ATOM   5568 C  CB  . TYR   C 1 105 ? -26.585 -38.016 17.181  1.00 34.80  ? 111 TYR   C CB  1 
ATOM   5569 C  CG  . TYR   C 1 105 ? -27.539 -38.844 16.347  1.00 36.86  ? 111 TYR   C CG  1 
ATOM   5570 C  CD1 . TYR   C 1 105 ? -27.974 -38.399 15.102  1.00 38.30  ? 111 TYR   C CD1 1 
ATOM   5571 C  CD2 . TYR   C 1 105 ? -28.031 -40.058 16.813  1.00 38.43  ? 111 TYR   C CD2 1 
ATOM   5572 C  CE1 . TYR   C 1 105 ? -28.836 -39.161 14.319  1.00 39.59  ? 111 TYR   C CE1 1 
ATOM   5573 C  CE2 . TYR   C 1 105 ? -28.897 -40.835 16.036  1.00 39.77  ? 111 TYR   C CE2 1 
ATOM   5574 C  CZ  . TYR   C 1 105 ? -29.311 -40.371 14.798  1.00 46.97  ? 111 TYR   C CZ  1 
ATOM   5575 O  OH  . TYR   C 1 105 ? -30.171 -41.110 14.022  1.00 50.89  ? 111 TYR   C OH  1 
ATOM   5576 N  N   . SER   C 1 106 ? -24.250 -35.835 16.386  1.00 32.71  ? 112 SER   C N   1 
ATOM   5577 C  CA  . SER   C 1 106 ? -23.782 -34.492 16.745  1.00 31.46  ? 112 SER   C CA  1 
ATOM   5578 C  C   . SER   C 1 106 ? -25.082 -33.889 17.275  1.00 34.77  ? 112 SER   C C   1 
ATOM   5579 O  O   . SER   C 1 106 ? -26.095 -33.890 16.586  1.00 33.71  ? 112 SER   C O   1 
ATOM   5580 C  CB  . SER   C 1 106 ? -23.288 -33.715 15.524  1.00 34.13  ? 112 SER   C CB  1 
ATOM   5581 O  OG  . SER   C 1 106 ? -22.151 -34.352 14.963  1.00 43.16  ? 112 SER   C OG  1 
ATOM   5582 N  N   . CYS   C 1 107 ? -25.068 -33.454 18.518  1.00 33.22  ? 113 CYS   C N   1 
ATOM   5583 C  CA  . CYS   C 1 107 ? -26.271 -33.034 19.195  1.00 33.47  ? 113 CYS   C CA  1 
ATOM   5584 C  C   . CYS   C 1 107 ? -26.546 -31.517 19.127  1.00 31.98  ? 113 CYS   C C   1 
ATOM   5585 O  O   . CYS   C 1 107 ? -25.777 -30.726 19.660  1.00 29.13  ? 113 CYS   C O   1 
ATOM   5586 C  CB  . CYS   C 1 107 ? -26.215 -33.547 20.628  1.00 36.57  ? 113 CYS   C CB  1 
ATOM   5587 S  SG  . CYS   C 1 107 ? -27.776 -33.420 21.501  1.00 41.70  ? 113 CYS   C SG  1 
ATOM   5588 N  N   . VAL   C 1 108 ? -27.629 -31.130 18.437  1.00 27.04  ? 114 VAL   C N   1 
ATOM   5589 C  CA  . VAL   C 1 108 ? -28.072 -29.743 18.273  1.00 27.05  ? 114 VAL   C CA  1 
ATOM   5590 C  C   . VAL   C 1 108 ? -29.187 -29.520 19.296  1.00 33.67  ? 114 VAL   C C   1 
ATOM   5591 O  O   . VAL   C 1 108 ? -30.200 -30.236 19.255  1.00 31.95  ? 114 VAL   C O   1 
ATOM   5592 C  CB  . VAL   C 1 108 ? -28.571 -29.409 16.834  1.00 29.29  ? 114 VAL   C CB  1 
ATOM   5593 C  CG1 . VAL   C 1 108 ? -29.176 -27.996 16.751  1.00 28.16  ? 114 VAL   C CG1 1 
ATOM   5594 C  CG2 . VAL   C 1 108 ? -27.458 -29.571 15.801  1.00 29.15  ? 114 VAL   C CG2 1 
ATOM   5595 N  N   . THR   C 1 109 ? -28.980 -28.579 20.236  1.00 29.98  ? 115 THR   C N   1 
ATOM   5596 C  CA  . THR   C 1 109 ? -30.025 -28.278 21.220  1.00 28.64  ? 115 THR   C CA  1 
ATOM   5597 C  C   . THR   C 1 109 ? -30.543 -26.899 20.919  1.00 30.83  ? 115 THR   C C   1 
ATOM   5598 O  O   . THR   C 1 109 ? -29.777 -25.936 20.857  1.00 27.94  ? 115 THR   C O   1 
ATOM   5599 C  CB  . THR   C 1 109 ? -29.586 -28.473 22.680  1.00 30.94  ? 115 THR   C CB  1 
ATOM   5600 O  OG1 . THR   C 1 109 ? -29.095 -29.809 22.859  1.00 31.80  ? 115 THR   C OG1 1 
ATOM   5601 C  CG2 . THR   C 1 109 ? -30.750 -28.224 23.676  1.00 29.86  ? 115 THR   C CG2 1 
ATOM   5602 N  N   . LEU   C 1 110 ? -31.860 -26.808 20.732  1.00 28.30  ? 116 LEU   C N   1 
ATOM   5603 C  CA  . LEU   C 1 110 ? -32.535 -25.554 20.452  1.00 27.87  ? 116 LEU   C CA  1 
ATOM   5604 C  C   . LEU   C 1 110 ? -33.138 -24.997 21.749  1.00 31.51  ? 116 LEU   C C   1 
ATOM   5605 O  O   . LEU   C 1 110 ? -33.938 -25.665 22.398  1.00 32.21  ? 116 LEU   C O   1 
ATOM   5606 C  CB  . LEU   C 1 110 ? -33.648 -25.771 19.399  1.00 28.21  ? 116 LEU   C CB  1 
ATOM   5607 C  CG  . LEU   C 1 110 ? -33.219 -26.456 18.070  1.00 31.25  ? 116 LEU   C CG  1 
ATOM   5608 C  CD1 . LEU   C 1 110 ? -34.379 -26.641 17.138  1.00 31.05  ? 116 LEU   C CD1 1 
ATOM   5609 C  CD2 . LEU   C 1 110 ? -32.107 -25.661 17.379  1.00 28.19  ? 116 LEU   C CD2 1 
ATOM   5610 N  N   . GLY   C 1 111 ? -32.757 -23.776 22.088  1.00 29.38  ? 117 GLY   C N   1 
ATOM   5611 C  CA  . GLY   C 1 111 ? -33.258 -23.077 23.270  1.00 29.52  ? 117 GLY   C CA  1 
ATOM   5612 C  C   . GLY   C 1 111 ? -34.435 -22.167 22.963  1.00 33.00  ? 117 GLY   C C   1 
ATOM   5613 O  O   . GLY   C 1 111 ? -34.769 -21.980 21.796  1.00 33.95  ? 117 GLY   C O   1 
ATOM   5614 N  N   . GLY   C 1 112 ? -35.073 -21.594 23.984  1.00 29.22  ? 118 GLY   C N   1 
ATOM   5615 C  CA  . GLY   C 1 112 ? -34.707 -21.741 25.394  1.00 28.97  ? 118 GLY   C CA  1 
ATOM   5616 C  C   . GLY   C 1 112 ? -33.613 -20.770 25.791  1.00 32.75  ? 118 GLY   C C   1 
ATOM   5617 O  O   . GLY   C 1 112 ? -32.890 -20.273 24.918  1.00 33.74  ? 118 GLY   C O   1 
ATOM   5618 N  N   . ASP   C 1 113 ? -33.468 -20.483 27.101  1.00 27.78  ? 119 ASP   C N   1 
ATOM   5619 C  CA  . ASP   C 1 113 ? -32.435 -19.547 27.519  1.00 27.36  ? 119 ASP   C CA  1 
ATOM   5620 C  C   . ASP   C 1 113 ? -31.093 -20.268 27.651  1.00 27.34  ? 119 ASP   C C   1 
ATOM   5621 O  O   . ASP   C 1 113 ? -31.061 -21.491 27.625  1.00 28.36  ? 119 ASP   C O   1 
ATOM   5622 C  CB  . ASP   C 1 113 ? -32.829 -18.793 28.799  1.00 30.07  ? 119 ASP   C CB  1 
ATOM   5623 C  CG  . ASP   C 1 113 ? -33.052 -19.698 29.984  1.00 39.68  ? 119 ASP   C CG  1 
ATOM   5624 O  OD1 . ASP   C 1 113 ? -32.082 -20.350 30.422  1.00 37.75  ? 119 ASP   C OD1 1 
ATOM   5625 O  OD2 . ASP   C 1 113 ? -34.208 -19.808 30.431  1.00 46.41  ? 119 ASP   C OD2 1 
ATOM   5626 N  N   . HIS   C 1 114 ? -29.997 -19.513 27.796  1.00 25.19  ? 120 HIS   C N   1 
ATOM   5627 C  CA  . HIS   C 1 114 ? -28.646 -20.070 27.876  1.00 26.39  ? 120 HIS   C CA  1 
ATOM   5628 C  C   . HIS   C 1 114 ? -28.351 -20.869 29.164  1.00 33.31  ? 120 HIS   C C   1 
ATOM   5629 O  O   . HIS   C 1 114 ? -27.289 -21.494 29.226  1.00 32.69  ? 120 HIS   C O   1 
ATOM   5630 C  CB  . HIS   C 1 114 ? -27.557 -18.975 27.625  1.00 26.00  ? 120 HIS   C CB  1 
ATOM   5631 C  CG  . HIS   C 1 114 ? -26.425 -19.480 26.767  1.00 27.98  ? 120 HIS   C CG  1 
ATOM   5632 N  ND1 . HIS   C 1 114 ? -25.586 -18.610 26.093  1.00 29.01  ? 120 HIS   C ND1 1 
ATOM   5633 C  CD2 . HIS   C 1 114 ? -26.049 -20.751 26.472  1.00 29.11  ? 120 HIS   C CD2 1 
ATOM   5634 C  CE1 . HIS   C 1 114 ? -24.768 -19.374 25.383  1.00 27.61  ? 120 HIS   C CE1 1 
ATOM   5635 N  NE2 . HIS   C 1 114 ? -24.989 -20.665 25.609  1.00 27.86  ? 120 HIS   C NE2 1 
ATOM   5636 N  N   . SER   C 1 115 ? -29.302 -20.970 30.144  1.00 31.29  ? 121 SER   C N   1 
ATOM   5637 C  CA  . SER   C 1 115 ? -29.050 -21.849 31.289  1.00 30.81  ? 121 SER   C CA  1 
ATOM   5638 C  C   . SER   C 1 115 ? -29.005 -23.320 30.863  1.00 34.27  ? 121 SER   C C   1 
ATOM   5639 O  O   . SER   C 1 115 ? -28.386 -24.127 31.549  1.00 33.06  ? 121 SER   C O   1 
ATOM   5640 C  CB  . SER   C 1 115 ? -30.063 -21.641 32.422  1.00 33.62  ? 121 SER   C CB  1 
ATOM   5641 O  OG  . SER   C 1 115 ? -31.300 -22.268 32.119  1.00 36.88  ? 121 SER   C OG  1 
ATOM   5642 N  N   . LEU   C 1 116 ? -29.602 -23.655 29.689  1.00 32.28  ? 122 LEU   C N   1 
ATOM   5643 C  CA  . LEU   C 1 116 ? -29.614 -25.008 29.152  1.00 31.46  ? 122 LEU   C CA  1 
ATOM   5644 C  C   . LEU   C 1 116 ? -28.209 -25.532 28.807  1.00 32.34  ? 122 LEU   C C   1 
ATOM   5645 O  O   . LEU   C 1 116 ? -28.049 -26.743 28.668  1.00 31.34  ? 122 LEU   C O   1 
ATOM   5646 C  CB  . LEU   C 1 116 ? -30.592 -25.172 27.979  1.00 32.29  ? 122 LEU   C CB  1 
ATOM   5647 C  CG  . LEU   C 1 116 ? -30.272 -24.536 26.607  1.00 38.32  ? 122 LEU   C CG  1 
ATOM   5648 C  CD1 . LEU   C 1 116 ? -29.298 -25.402 25.774  1.00 38.42  ? 122 LEU   C CD1 1 
ATOM   5649 C  CD2 . LEU   C 1 116 ? -31.533 -24.395 25.827  1.00 41.60  ? 122 LEU   C CD2 1 
ATOM   5650 N  N   . ALA   C 1 117 ? -27.197 -24.648 28.706  1.00 28.79  ? 123 ALA   C N   1 
ATOM   5651 C  CA  . ALA   C 1 117 ? -25.817 -25.104 28.452  1.00 29.07  ? 123 ALA   C CA  1 
ATOM   5652 C  C   . ALA   C 1 117 ? -25.275 -25.914 29.622  1.00 31.74  ? 123 ALA   C C   1 
ATOM   5653 O  O   . ALA   C 1 117 ? -24.330 -26.680 29.438  1.00 31.59  ? 123 ALA   C O   1 
ATOM   5654 C  CB  . ALA   C 1 117 ? -24.900 -23.924 28.147  1.00 29.55  ? 123 ALA   C CB  1 
ATOM   5655 N  N   . ILE   C 1 118 ? -25.874 -25.774 30.834  1.00 28.72  ? 124 ILE   C N   1 
ATOM   5656 C  CA  . ILE   C 1 118 ? -25.478 -26.591 31.991  1.00 27.70  ? 124 ILE   C CA  1 
ATOM   5657 C  C   . ILE   C 1 118 ? -25.728 -28.057 31.604  1.00 30.45  ? 124 ILE   C C   1 
ATOM   5658 O  O   . ILE   C 1 118 ? -24.813 -28.876 31.682  1.00 30.69  ? 124 ILE   C O   1 
ATOM   5659 C  CB  . ILE   C 1 118 ? -26.223 -26.216 33.312  1.00 30.48  ? 124 ILE   C CB  1 
ATOM   5660 C  CG1 . ILE   C 1 118 ? -25.906 -24.763 33.760  1.00 30.96  ? 124 ILE   C CG1 1 
ATOM   5661 C  CG2 . ILE   C 1 118 ? -25.906 -27.229 34.461  1.00 30.93  ? 124 ILE   C CG2 1 
ATOM   5662 C  CD1 . ILE   C 1 118 ? -26.932 -24.173 34.863  1.00 28.72  ? 124 ILE   C CD1 1 
ATOM   5663 N  N   . GLY   C 1 119 ? -26.948 -28.353 31.163  1.00 25.82  ? 125 GLY   C N   1 
ATOM   5664 C  CA  . GLY   C 1 119 ? -27.335 -29.693 30.750  1.00 26.13  ? 125 GLY   C CA  1 
ATOM   5665 C  C   . GLY   C 1 119 ? -26.653 -30.206 29.496  1.00 29.31  ? 125 GLY   C C   1 
ATOM   5666 O  O   . GLY   C 1 119 ? -26.127 -31.325 29.518  1.00 28.58  ? 125 GLY   C O   1 
ATOM   5667 N  N   . THR   C 1 120 ? -26.579 -29.390 28.417  1.00 27.54  ? 126 THR   C N   1 
ATOM   5668 C  CA  . THR   C 1 120 ? -25.949 -29.858 27.155  1.00 26.99  ? 126 THR   C CA  1 
ATOM   5669 C  C   . THR   C 1 120 ? -24.439 -30.140 27.315  1.00 29.02  ? 126 THR   C C   1 
ATOM   5670 O  O   . THR   C 1 120 ? -23.953 -31.164 26.817  1.00 27.57  ? 126 THR   C O   1 
ATOM   5671 C  CB  . THR   C 1 120 ? -26.234 -28.923 25.969  1.00 28.69  ? 126 THR   C CB  1 
ATOM   5672 O  OG1 . THR   C 1 120 ? -25.507 -27.726 26.143  1.00 25.00  ? 126 THR   C OG1 1 
ATOM   5673 C  CG2 . THR   C 1 120 ? -27.716 -28.604 25.794  1.00 25.14  ? 126 THR   C CG2 1 
ATOM   5674 N  N   . ILE   C 1 121 ? -23.704 -29.235 27.995  1.00 25.48  ? 127 ILE   C N   1 
ATOM   5675 C  CA  . ILE   C 1 121 ? -22.262 -29.434 28.211  1.00 25.21  ? 127 ILE   C CA  1 
ATOM   5676 C  C   . ILE   C 1 121 ? -22.033 -30.591 29.194  1.00 29.70  ? 127 ILE   C C   1 
ATOM   5677 O  O   . ILE   C 1 121 ? -21.159 -31.426 28.953  1.00 28.74  ? 127 ILE   C O   1 
ATOM   5678 C  CB  . ILE   C 1 121 ? -21.516 -28.116 28.591  1.00 27.52  ? 127 ILE   C CB  1 
ATOM   5679 C  CG1 . ILE   C 1 121 ? -21.612 -27.069 27.438  1.00 28.14  ? 127 ILE   C CG1 1 
ATOM   5680 C  CG2 . ILE   C 1 121 ? -20.045 -28.374 28.983  1.00 27.74  ? 127 ILE   C CG2 1 
ATOM   5681 C  CD1 . ILE   C 1 121 ? -21.147 -25.588 27.790  1.00 28.32  ? 127 ILE   C CD1 1 
ATOM   5682 N  N   . SER   C 1 122 ? -22.846 -30.676 30.265  1.00 28.54  ? 128 SER   C N   1 
ATOM   5683 C  CA  . SER   C 1 122 ? -22.760 -31.787 31.240  1.00 28.91  ? 128 SER   C CA  1 
ATOM   5684 C  C   . SER   C 1 122 ? -22.965 -33.145 30.574  1.00 31.82  ? 128 SER   C C   1 
ATOM   5685 O  O   . SER   C 1 122 ? -22.151 -34.051 30.770  1.00 30.34  ? 128 SER   C O   1 
ATOM   5686 C  CB  . SER   C 1 122 ? -23.759 -31.606 32.379  1.00 31.44  ? 128 SER   C CB  1 
ATOM   5687 O  OG  . SER   C 1 122 ? -23.360 -30.526 33.206  1.00 37.22  ? 128 SER   C OG  1 
ATOM   5688 N  N   . GLY   C 1 123 ? -24.024 -33.253 29.774  1.00 30.17  ? 129 GLY   C N   1 
ATOM   5689 C  CA  . GLY   C 1 123 ? -24.370 -34.464 29.040  1.00 29.60  ? 129 GLY   C CA  1 
ATOM   5690 C  C   . GLY   C 1 123 ? -23.324 -34.857 28.020  1.00 33.49  ? 129 GLY   C C   1 
ATOM   5691 O  O   . GLY   C 1 123 ? -22.938 -36.021 27.936  1.00 33.58  ? 129 GLY   C O   1 
ATOM   5692 N  N   . HIS   C 1 124 ? -22.839 -33.874 27.248  1.00 28.69  ? 130 HIS   C N   1 
ATOM   5693 C  CA  . HIS   C 1 124 ? -21.795 -34.061 26.240  1.00 27.00  ? 130 HIS   C CA  1 
ATOM   5694 C  C   . HIS   C 1 124 ? -20.470 -34.544 26.879  1.00 28.11  ? 130 HIS   C C   1 
ATOM   5695 O  O   . HIS   C 1 124 ? -19.872 -35.497 26.389  1.00 28.85  ? 130 HIS   C O   1 
ATOM   5696 C  CB  . HIS   C 1 124 ? -21.590 -32.715 25.497  1.00 26.39  ? 130 HIS   C CB  1 
ATOM   5697 C  CG  . HIS   C 1 124 ? -20.708 -32.765 24.280  1.00 28.63  ? 130 HIS   C CG  1 
ATOM   5698 N  ND1 . HIS   C 1 124 ? -20.269 -31.598 23.670  1.00 29.56  ? 130 HIS   C ND1 1 
ATOM   5699 C  CD2 . HIS   C 1 124 ? -20.219 -33.824 23.590  1.00 29.39  ? 130 HIS   C CD2 1 
ATOM   5700 C  CE1 . HIS   C 1 124 ? -19.546 -31.984 22.624  1.00 28.89  ? 130 HIS   C CE1 1 
ATOM   5701 N  NE2 . HIS   C 1 124 ? -19.481 -33.312 22.543  1.00 29.39  ? 130 HIS   C NE2 1 
ATOM   5702 N  N   . ALA   C 1 125 ? -20.048 -33.927 28.006  1.00 27.64  ? 131 ALA   C N   1 
ATOM   5703 C  CA  . ALA   C 1 125 ? -18.785 -34.258 28.684  1.00 26.73  ? 131 ALA   C CA  1 
ATOM   5704 C  C   . ALA   C 1 125 ? -18.731 -35.675 29.291  1.00 32.02  ? 131 ALA   C C   1 
ATOM   5705 O  O   . ALA   C 1 125 ? -17.641 -36.198 29.524  1.00 32.39  ? 131 ALA   C O   1 
ATOM   5706 C  CB  . ALA   C 1 125 ? -18.463 -33.209 29.729  1.00 28.07  ? 131 ALA   C CB  1 
ATOM   5707 N  N   . ARG   C 1 126 ? -19.882 -36.309 29.503  1.00 30.03  ? 132 ARG   C N   1 
ATOM   5708 C  CA  . ARG   C 1 126 ? -19.936 -37.668 30.038  1.00 31.64  ? 132 ARG   C CA  1 
ATOM   5709 C  C   . ARG   C 1 126 ? -19.243 -38.661 29.115  1.00 35.00  ? 132 ARG   C C   1 
ATOM   5710 O  O   . ARG   C 1 126 ? -18.447 -39.468 29.590  1.00 35.27  ? 132 ARG   C O   1 
ATOM   5711 C  CB  . ARG   C 1 126 ? -21.376 -38.093 30.309  1.00 35.60  ? 132 ARG   C CB  1 
ATOM   5712 C  CG  . ARG   C 1 126 ? -21.909 -37.428 31.557  1.00 45.12  ? 132 ARG   C CG  1 
ATOM   5713 C  CD  . ARG   C 1 126 ? -23.379 -37.678 31.718  1.00 49.70  ? 132 ARG   C CD  1 
ATOM   5714 N  NE  . ARG   C 1 126 ? -23.890 -36.872 32.818  1.00 54.71  ? 132 ARG   C NE  1 
ATOM   5715 C  CZ  . ARG   C 1 126 ? -25.175 -36.717 33.093  1.00 61.78  ? 132 ARG   C CZ  1 
ATOM   5716 N  NH1 . ARG   C 1 126 ? -26.098 -37.309 32.341  1.00 39.44  ? 132 ARG   C NH1 1 
ATOM   5717 N  NH2 . ARG   C 1 126 ? -25.551 -35.972 34.121  1.00 47.67  ? 132 ARG   C NH2 1 
ATOM   5718 N  N   . HIS   C 1 127 ? -19.483 -38.544 27.795  1.00 32.47  ? 133 HIS   C N   1 
ATOM   5719 C  CA  . HIS   C 1 127 ? -18.864 -39.413 26.794  1.00 33.76  ? 133 HIS   C CA  1 
ATOM   5720 C  C   . HIS   C 1 127 ? -17.692 -38.747 26.087  1.00 34.12  ? 133 HIS   C C   1 
ATOM   5721 O  O   . HIS   C 1 127 ? -16.836 -39.462 25.556  1.00 31.75  ? 133 HIS   C O   1 
ATOM   5722 C  CB  . HIS   C 1 127 ? -19.889 -39.966 25.809  1.00 35.34  ? 133 HIS   C CB  1 
ATOM   5723 C  CG  . HIS   C 1 127 ? -21.005 -40.689 26.498  1.00 39.64  ? 133 HIS   C CG  1 
ATOM   5724 N  ND1 . HIS   C 1 127 ? -20.758 -41.729 27.377  1.00 42.03  ? 133 HIS   C ND1 1 
ATOM   5725 C  CD2 . HIS   C 1 127 ? -22.334 -40.445 26.469  1.00 42.10  ? 133 HIS   C CD2 1 
ATOM   5726 C  CE1 . HIS   C 1 127 ? -21.943 -42.091 27.845  1.00 41.55  ? 133 HIS   C CE1 1 
ATOM   5727 N  NE2 . HIS   C 1 127 ? -22.922 -41.357 27.313  1.00 41.95  ? 133 HIS   C NE2 1 
ATOM   5728 N  N   . CYS   C 1 128 ? -17.612 -37.390 26.162  1.00 29.60  ? 134 CYS   C N   1 
ATOM   5729 C  CA  . CYS   C 1 128 ? -16.516 -36.595 25.563  1.00 28.89  ? 134 CYS   C CA  1 
ATOM   5730 C  C   . CYS   C 1 128 ? -15.775 -35.808 26.646  1.00 30.56  ? 134 CYS   C C   1 
ATOM   5731 O  O   . CYS   C 1 128 ? -15.854 -34.583 26.633  1.00 29.59  ? 134 CYS   C O   1 
ATOM   5732 C  CB  . CYS   C 1 128 ? -17.050 -35.674 24.464  1.00 28.70  ? 134 CYS   C CB  1 
ATOM   5733 S  SG  . CYS   C 1 128 ? -17.691 -36.540 23.016  1.00 32.31  ? 134 CYS   C SG  1 
ATOM   5734 N  N   . PRO   C 1 129 ? -15.045 -36.451 27.598  1.00 29.06  ? 135 PRO   C N   1 
ATOM   5735 C  CA  . PRO   C 1 129 ? -14.380 -35.673 28.651  1.00 29.50  ? 135 PRO   C CA  1 
ATOM   5736 C  C   . PRO   C 1 129 ? -13.315 -34.687 28.153  1.00 32.64  ? 135 PRO   C C   1 
ATOM   5737 O  O   . PRO   C 1 129 ? -13.034 -33.724 28.850  1.00 32.20  ? 135 PRO   C O   1 
ATOM   5738 C  CB  . PRO   C 1 129 ? -13.810 -36.758 29.586  1.00 31.57  ? 135 PRO   C CB  1 
ATOM   5739 C  CG  . PRO   C 1 129 ? -13.671 -37.950 28.744  1.00 34.55  ? 135 PRO   C CG  1 
ATOM   5740 C  CD  . PRO   C 1 129 ? -14.838 -37.899 27.812  1.00 29.68  ? 135 PRO   C CD  1 
ATOM   5741 N  N   . ASP   C 1 130 ? -12.782 -34.886 26.934  1.00 28.78  ? 136 ASP   C N   1 
ATOM   5742 C  CA  . ASP   C 1 130 ? -11.761 -33.993 26.357  1.00 27.71  ? 136 ASP   C CA  1 
ATOM   5743 C  C   . ASP   C 1 130 ? -12.385 -32.908 25.468  1.00 30.80  ? 136 ASP   C C   1 
ATOM   5744 O  O   . ASP   C 1 130 ? -11.698 -32.300 24.644  1.00 28.70  ? 136 ASP   C O   1 
ATOM   5745 C  CB  . ASP   C 1 130 ? -10.719 -34.811 25.587  1.00 29.03  ? 136 ASP   C CB  1 
ATOM   5746 C  CG  . ASP   C 1 130 ? -9.422  -34.086 25.292  1.00 30.68  ? 136 ASP   C CG  1 
ATOM   5747 O  OD1 . ASP   C 1 130 ? -9.048  -33.183 26.080  1.00 27.31  ? 136 ASP   C OD1 1 
ATOM   5748 O  OD2 . ASP   C 1 130 ? -8.753  -34.458 24.310  1.00 38.47  ? 136 ASP   C OD2 1 
ATOM   5749 N  N   . LEU   C 1 131 ? -13.696 -32.648 25.640  1.00 28.04  ? 137 LEU   C N   1 
ATOM   5750 C  CA  . LEU   C 1 131 ? -14.336 -31.631 24.808  1.00 28.74  ? 137 LEU   C CA  1 
ATOM   5751 C  C   . LEU   C 1 131 ? -13.777 -30.215 25.065  1.00 30.23  ? 137 LEU   C C   1 
ATOM   5752 O  O   . LEU   C 1 131 ? -13.278 -29.917 26.164  1.00 29.48  ? 137 LEU   C O   1 
ATOM   5753 C  CB  . LEU   C 1 131 ? -15.897 -31.650 24.949  1.00 29.01  ? 137 LEU   C CB  1 
ATOM   5754 C  CG  . LEU   C 1 131 ? -16.559 -31.147 26.270  1.00 35.99  ? 137 LEU   C CG  1 
ATOM   5755 C  CD1 . LEU   C 1 131 ? -16.523 -29.672 26.388  1.00 38.21  ? 137 LEU   C CD1 1 
ATOM   5756 C  CD2 . LEU   C 1 131 ? -18.040 -31.384 26.250  1.00 37.53  ? 137 LEU   C CD2 1 
ATOM   5757 N  N   . CYS   C 1 132 ? -13.922 -29.337 24.071  1.00 25.96  ? 138 CYS   C N   1 
ATOM   5758 C  CA  . CYS   C 1 132 ? -13.602 -27.939 24.236  1.00 25.68  ? 138 CYS   C CA  1 
ATOM   5759 C  C   . CYS   C 1 132 ? -14.859 -27.149 23.852  1.00 28.49  ? 138 CYS   C C   1 
ATOM   5760 O  O   . CYS   C 1 132 ? -15.725 -27.680 23.168  1.00 29.01  ? 138 CYS   C O   1 
ATOM   5761 C  CB  . CYS   C 1 132 ? -12.375 -27.510 23.440  1.00 26.04  ? 138 CYS   C CB  1 
ATOM   5762 S  SG  . CYS   C 1 132 ? -12.516 -27.766 21.678  1.00 29.67  ? 138 CYS   C SG  1 
ATOM   5763 N  N   . VAL   C 1 133 ? -14.994 -25.951 24.381  1.00 25.68  ? 139 VAL   C N   1 
ATOM   5764 C  CA  . VAL   C 1 133 ? -16.198 -25.132 24.156  1.00 25.42  ? 139 VAL   C CA  1 
ATOM   5765 C  C   . VAL   C 1 133 ? -15.823 -23.843 23.458  1.00 28.82  ? 139 VAL   C C   1 
ATOM   5766 O  O   . VAL   C 1 133 ? -14.864 -23.195 23.858  1.00 27.45  ? 139 VAL   C O   1 
ATOM   5767 C  CB  . VAL   C 1 133 ? -16.952 -24.856 25.496  1.00 28.61  ? 139 VAL   C CB  1 
ATOM   5768 C  CG1 . VAL   C 1 133 ? -18.229 -24.006 25.274  1.00 28.82  ? 139 VAL   C CG1 1 
ATOM   5769 C  CG2 . VAL   C 1 133 ? -17.299 -26.156 26.230  1.00 27.74  ? 139 VAL   C CG2 1 
ATOM   5770 N  N   . VAL   C 1 134 ? -16.578 -23.481 22.410  1.00 24.36  ? 140 VAL   C N   1 
ATOM   5771 C  CA  . VAL   C 1 134 ? -16.469 -22.182 21.744  1.00 22.32  ? 140 VAL   C CA  1 
ATOM   5772 C  C   . VAL   C 1 134 ? -17.821 -21.537 22.119  1.00 26.14  ? 140 VAL   C C   1 
ATOM   5773 O  O   . VAL   C 1 134 ? -18.868 -22.073 21.756  1.00 25.07  ? 140 VAL   C O   1 
ATOM   5774 C  CB  . VAL   C 1 134 ? -16.254 -22.246 20.223  1.00 25.12  ? 140 VAL   C CB  1 
ATOM   5775 C  CG1 . VAL   C 1 134 ? -16.219 -20.833 19.628  1.00 24.79  ? 140 VAL   C CG1 1 
ATOM   5776 C  CG2 . VAL   C 1 134 ? -14.967 -23.019 19.885  1.00 24.93  ? 140 VAL   C CG2 1 
ATOM   5777 N  N   . TRP   C 1 135 ? -17.764 -20.499 22.947  1.00 25.46  ? 141 TRP   C N   1 
ATOM   5778 C  CA  . TRP   C 1 135 ? -18.930 -19.794 23.498  1.00 25.95  ? 141 TRP   C CA  1 
ATOM   5779 C  C   . TRP   C 1 135 ? -19.094 -18.469 22.766  1.00 27.38  ? 141 TRP   C C   1 
ATOM   5780 O  O   . TRP   C 1 135 ? -18.327 -17.510 22.966  1.00 24.70  ? 141 TRP   C O   1 
ATOM   5781 C  CB  . TRP   C 1 135 ? -18.763 -19.617 25.018  1.00 24.84  ? 141 TRP   C CB  1 
ATOM   5782 C  CG  . TRP   C 1 135 ? -20.010 -19.220 25.759  1.00 25.30  ? 141 TRP   C CG  1 
ATOM   5783 C  CD1 . TRP   C 1 135 ? -20.615 -17.996 25.755  1.00 28.22  ? 141 TRP   C CD1 1 
ATOM   5784 C  CD2 . TRP   C 1 135 ? -20.814 -20.064 26.592  1.00 25.31  ? 141 TRP   C CD2 1 
ATOM   5785 N  NE1 . TRP   C 1 135 ? -21.732 -18.015 26.557  1.00 27.49  ? 141 TRP   C NE1 1 
ATOM   5786 C  CE2 . TRP   C 1 135 ? -21.867 -19.267 27.103  1.00 28.72  ? 141 TRP   C CE2 1 
ATOM   5787 C  CE3 . TRP   C 1 135 ? -20.715 -21.408 27.010  1.00 26.20  ? 141 TRP   C CE3 1 
ATOM   5788 C  CZ2 . TRP   C 1 135 ? -22.823 -19.770 28.000  1.00 27.43  ? 141 TRP   C CZ2 1 
ATOM   5789 C  CZ3 . TRP   C 1 135 ? -21.677 -21.915 27.880  1.00 27.27  ? 141 TRP   C CZ3 1 
ATOM   5790 C  CH2 . TRP   C 1 135 ? -22.727 -21.109 28.349  1.00 27.72  ? 141 TRP   C CH2 1 
ATOM   5791 N  N   . VAL   C 1 136 ? -20.124 -18.411 21.907  1.00 25.42  ? 142 VAL   C N   1 
ATOM   5792 C  CA  . VAL   C 1 136 ? -20.382 -17.256 21.039  1.00 23.63  ? 142 VAL   C CA  1 
ATOM   5793 C  C   . VAL   C 1 136 ? -21.542 -16.492 21.602  1.00 26.78  ? 142 VAL   C C   1 
ATOM   5794 O  O   . VAL   C 1 136 ? -22.663 -16.996 21.626  1.00 25.58  ? 142 VAL   C O   1 
ATOM   5795 C  CB  . VAL   C 1 136 ? -20.581 -17.651 19.554  1.00 25.37  ? 142 VAL   C CB  1 
ATOM   5796 C  CG1 . VAL   C 1 136 ? -20.712 -16.394 18.675  1.00 24.42  ? 142 VAL   C CG1 1 
ATOM   5797 C  CG2 . VAL   C 1 136 ? -19.431 -18.552 19.060  1.00 24.64  ? 142 VAL   C CG2 1 
ATOM   5798 N  N   . ASP   C 1 137 ? -21.265 -15.288 22.090  1.00 25.39  ? 143 ASP   C N   1 
ATOM   5799 C  CA  . ASP   C 1 137 ? -22.254 -14.552 22.873  1.00 24.46  ? 143 ASP   C CA  1 
ATOM   5800 C  C   . ASP   C 1 137 ? -21.839 -13.109 23.118  1.00 28.46  ? 143 ASP   C C   1 
ATOM   5801 O  O   . ASP   C 1 137 ? -20.644 -12.797 23.178  1.00 27.09  ? 143 ASP   C O   1 
ATOM   5802 C  CB  . ASP   C 1 137 ? -22.331 -15.284 24.249  1.00 25.16  ? 143 ASP   C CB  1 
ATOM   5803 C  CG  . ASP   C 1 137 ? -23.594 -15.103 25.082  1.00 26.79  ? 143 ASP   C CG  1 
ATOM   5804 O  OD1 . ASP   C 1 137 ? -24.111 -13.960 25.137  1.00 26.77  ? 143 ASP   C OD1 1 
ATOM   5805 O  OD2 . ASP   C 1 137 ? -23.928 -16.035 25.858  1.00 29.74  ? 143 ASP   C OD2 1 
ATOM   5806 N  N   . ALA   C 1 138 ? -22.821 -12.224 23.338  1.00 27.33  ? 144 ALA   C N   1 
ATOM   5807 C  CA  . ALA   C 1 138 ? -22.508 -10.850 23.768  1.00 27.23  ? 144 ALA   C CA  1 
ATOM   5808 C  C   . ALA   C 1 138 ? -22.053 -10.883 25.260  1.00 31.22  ? 144 ALA   C C   1 
ATOM   5809 O  O   . ALA   C 1 138 ? -21.296 -10.016 25.710  1.00 32.37  ? 144 ALA   C O   1 
ATOM   5810 C  CB  . ALA   C 1 138 ? -23.743 -9.955  23.624  1.00 28.27  ? 144 ALA   C CB  1 
ATOM   5811 N  N   . HIS   C 1 139 ? -22.460 -11.931 25.992  1.00 27.35  ? 145 HIS   C N   1 
ATOM   5812 C  CA  . HIS   C 1 139 ? -22.217 -12.102 27.428  1.00 27.49  ? 145 HIS   C CA  1 
ATOM   5813 C  C   . HIS   C 1 139 ? -21.296 -13.276 27.771  1.00 31.71  ? 145 HIS   C C   1 
ATOM   5814 O  O   . HIS   C 1 139 ? -21.247 -14.263 27.034  1.00 31.18  ? 145 HIS   C O   1 
ATOM   5815 C  CB  . HIS   C 1 139 ? -23.570 -12.285 28.126  1.00 28.29  ? 145 HIS   C CB  1 
ATOM   5816 C  CG  . HIS   C 1 139 ? -24.587 -11.268 27.690  1.00 31.41  ? 145 HIS   C CG  1 
ATOM   5817 N  ND1 . HIS   C 1 139 ? -25.551 -11.574 26.749  1.00 32.79  ? 145 HIS   C ND1 1 
ATOM   5818 C  CD2 . HIS   C 1 139 ? -24.722 -9.966  28.049  1.00 32.56  ? 145 HIS   C CD2 1 
ATOM   5819 C  CE1 . HIS   C 1 139 ? -26.269 -10.464 26.592  1.00 31.85  ? 145 HIS   C CE1 1 
ATOM   5820 N  NE2 . HIS   C 1 139 ? -25.802 -9.466  27.349  1.00 32.06  ? 145 HIS   C NE2 1 
ATOM   5821 N  N   . ALA   C 1 140 ? -20.612 -13.195 28.917  1.00 28.38  ? 146 ALA   C N   1 
ATOM   5822 C  CA  . ALA   C 1 140 ? -19.749 -14.285 29.382  1.00 29.98  ? 146 ALA   C CA  1 
ATOM   5823 C  C   . ALA   C 1 140 ? -20.503 -15.363 30.169  1.00 31.36  ? 146 ALA   C C   1 
ATOM   5824 O  O   . ALA   C 1 140 ? -19.996 -16.479 30.310  1.00 29.74  ? 146 ALA   C O   1 
ATOM   5825 C  CB  . ALA   C 1 140 ? -18.566 -13.747 30.180  1.00 31.28  ? 146 ALA   C CB  1 
ATOM   5826 N  N   . ASP   C 1 141 ? -21.741 -15.054 30.654  1.00 29.68  ? 147 ASP   C N   1 
ATOM   5827 C  CA  . ASP   C 1 141 ? -22.606 -16.002 31.371  1.00 29.25  ? 147 ASP   C CA  1 
ATOM   5828 C  C   . ASP   C 1 141 ? -21.810 -16.760 32.459  1.00 32.39  ? 147 ASP   C C   1 
ATOM   5829 O  O   . ASP   C 1 141 ? -21.951 -17.973 32.604  1.00 30.12  ? 147 ASP   C O   1 
ATOM   5830 C  CB  . ASP   C 1 141 ? -23.203 -16.992 30.343  1.00 30.64  ? 147 ASP   C CB  1 
ATOM   5831 C  CG  . ASP   C 1 141 ? -24.145 -16.364 29.336  1.00 33.57  ? 147 ASP   C CG  1 
ATOM   5832 O  OD1 . ASP   C 1 141 ? -24.472 -15.153 29.492  1.00 31.32  ? 147 ASP   C OD1 1 
ATOM   5833 O  OD2 . ASP   C 1 141 ? -24.660 -17.103 28.472  1.00 33.31  ? 147 ASP   C OD2 1 
ATOM   5834 N  N   . ILE   C 1 142 ? -20.904 -16.045 33.161  1.00 28.95  ? 148 ILE   C N   1 
ATOM   5835 C  CA  . ILE   C 1 142 ? -20.007 -16.676 34.109  1.00 28.49  ? 148 ILE   C CA  1 
ATOM   5836 C  C   . ILE   C 1 142 ? -20.128 -16.063 35.535  1.00 34.74  ? 148 ILE   C C   1 
ATOM   5837 O  O   . ILE   C 1 142 ? -19.258 -16.275 36.381  1.00 33.20  ? 148 ILE   C O   1 
ATOM   5838 C  CB  . ILE   C 1 142 ? -18.572 -16.690 33.523  1.00 30.58  ? 148 ILE   C CB  1 
ATOM   5839 C  CG1 . ILE   C 1 142 ? -17.693 -17.781 34.199  1.00 29.88  ? 148 ILE   C CG1 1 
ATOM   5840 C  CG2 . ILE   C 1 142 ? -17.916 -15.306 33.508  1.00 30.70  ? 148 ILE   C CG2 1 
ATOM   5841 C  CD1 . ILE   C 1 142 ? -16.366 -18.071 33.452  1.00 32.91  ? 148 ILE   C CD1 1 
ATOM   5842 N  N   . ASN   C 1 143 ? -21.264 -15.388 35.821  1.00 32.53  ? 149 ASN   C N   1 
ATOM   5843 C  CA  . ASN   C 1 143 ? -21.511 -14.892 37.176  1.00 34.00  ? 149 ASN   C CA  1 
ATOM   5844 C  C   . ASN   C 1 143 ? -21.700 -16.130 38.045  1.00 39.76  ? 149 ASN   C C   1 
ATOM   5845 O  O   . ASN   C 1 143 ? -22.094 -17.180 37.535  1.00 37.88  ? 149 ASN   C O   1 
ATOM   5846 C  CB  . ASN   C 1 143 ? -22.800 -14.073 37.239  1.00 34.83  ? 149 ASN   C CB  1 
ATOM   5847 C  CG  . ASN   C 1 143 ? -22.604 -12.613 36.987  1.00 42.17  ? 149 ASN   C CG  1 
ATOM   5848 O  OD1 . ASN   C 1 143 ? -21.843 -11.929 37.687  1.00 34.29  ? 149 ASN   C OD1 1 
ATOM   5849 N  ND2 . ASN   C 1 143 ? -23.302 -12.105 35.985  1.00 40.15  ? 149 ASN   C ND2 1 
ATOM   5850 N  N   . THR   C 1 144 ? -21.346 -16.040 39.322  1.00 37.66  ? 150 THR   C N   1 
ATOM   5851 C  CA  . THR   C 1 144 ? -21.575 -17.167 40.215  1.00 37.53  ? 150 THR   C CA  1 
ATOM   5852 C  C   . THR   C 1 144 ? -22.905 -16.837 40.890  1.00 41.72  ? 150 THR   C C   1 
ATOM   5853 O  O   . THR   C 1 144 ? -23.332 -15.671 40.823  1.00 40.94  ? 150 THR   C O   1 
ATOM   5854 C  CB  . THR   C 1 144 ? -20.433 -17.314 41.260  1.00 39.87  ? 150 THR   C CB  1 
ATOM   5855 O  OG1 . THR   C 1 144 ? -20.499 -16.233 42.182  1.00 41.20  ? 150 THR   C OG1 1 
ATOM   5856 C  CG2 . THR   C 1 144 ? -19.043 -17.420 40.639  1.00 33.00  ? 150 THR   C CG2 1 
ATOM   5857 N  N   . PRO   C 1 145 ? -23.577 -17.771 41.602  1.00 39.46  ? 151 PRO   C N   1 
ATOM   5858 C  CA  . PRO   C 1 145 ? -24.796 -17.368 42.327  1.00 39.28  ? 151 PRO   C CA  1 
ATOM   5859 C  C   . PRO   C 1 145 ? -24.536 -16.274 43.383  1.00 42.27  ? 151 PRO   C C   1 
ATOM   5860 O  O   . PRO   C 1 145 ? -25.482 -15.643 43.845  1.00 40.90  ? 151 PRO   C O   1 
ATOM   5861 C  CB  . PRO   C 1 145 ? -25.291 -18.683 42.936  1.00 41.04  ? 151 PRO   C CB  1 
ATOM   5862 C  CG  . PRO   C 1 145 ? -24.661 -19.757 42.079  1.00 44.82  ? 151 PRO   C CG  1 
ATOM   5863 C  CD  . PRO   C 1 145 ? -23.299 -19.206 41.802  1.00 40.61  ? 151 PRO   C CD  1 
ATOM   5864 N  N   . LEU   C 1 146 ? -23.257 -16.011 43.713  1.00 39.91  ? 152 LEU   C N   1 
ATOM   5865 C  CA  . LEU   C 1 146 ? -22.858 -14.988 44.694  1.00 40.60  ? 152 LEU   C CA  1 
ATOM   5866 C  C   . LEU   C 1 146 ? -22.441 -13.627 44.086  1.00 45.87  ? 152 LEU   C C   1 
ATOM   5867 O  O   . LEU   C 1 146 ? -22.288 -12.660 44.843  1.00 44.89  ? 152 LEU   C O   1 
ATOM   5868 C  CB  . LEU   C 1 146 ? -21.754 -15.501 45.635  1.00 40.56  ? 152 LEU   C CB  1 
ATOM   5869 C  CG  . LEU   C 1 146 ? -22.032 -16.729 46.488  1.00 44.44  ? 152 LEU   C CG  1 
ATOM   5870 C  CD1 . LEU   C 1 146 ? -20.782 -17.133 47.211  1.00 44.54  ? 152 LEU   C CD1 1 
ATOM   5871 C  CD2 . LEU   C 1 146 ? -23.151 -16.486 47.483  1.00 46.70  ? 152 LEU   C CD2 1 
ATOM   5872 N  N   . THR   C 1 147 ? -22.259 -13.538 42.741  1.00 41.41  ? 153 THR   C N   1 
ATOM   5873 C  CA  . THR   C 1 147 ? -21.882 -12.275 42.080  1.00 40.33  ? 153 THR   C CA  1 
ATOM   5874 C  C   . THR   C 1 147 ? -23.012 -11.686 41.244  1.00 44.09  ? 153 THR   C C   1 
ATOM   5875 O  O   . THR   C 1 147 ? -22.987 -10.490 40.952  1.00 43.16  ? 153 THR   C O   1 
ATOM   5876 C  CB  . THR   C 1 147 ? -20.637 -12.415 41.211  1.00 43.61  ? 153 THR   C CB  1 
ATOM   5877 O  OG1 . THR   C 1 147 ? -20.939 -13.213 40.069  1.00 41.61  ? 153 THR   C OG1 1 
ATOM   5878 C  CG2 . THR   C 1 147 ? -19.442 -12.934 41.957  1.00 42.07  ? 153 THR   C CG2 1 
ATOM   5879 N  N   . THR   C 1 148 ? -23.967 -12.533 40.808  1.00 41.30  ? 154 THR   C N   1 
ATOM   5880 C  CA  . THR   C 1 148 ? -25.118 -12.124 40.002  1.00 41.67  ? 154 THR   C CA  1 
ATOM   5881 C  C   . THR   C 1 148 ? -25.869 -10.956 40.637  1.00 48.64  ? 154 THR   C C   1 
ATOM   5882 O  O   . THR   C 1 148 ? -26.017 -10.921 41.863  1.00 49.86  ? 154 THR   C O   1 
ATOM   5883 C  CB  . THR   C 1 148 ? -26.047 -13.318 39.697  1.00 43.97  ? 154 THR   C CB  1 
ATOM   5884 O  OG1 . THR   C 1 148 ? -27.178 -12.862 38.959  1.00 37.46  ? 154 THR   C OG1 1 
ATOM   5885 C  CG2 . THR   C 1 148 ? -26.524 -14.041 40.947  1.00 44.43  ? 154 THR   C CG2 1 
ATOM   5886 N  N   . SER   C 1 149 ? -26.307 -9.999  39.810  1.00 44.98  ? 155 SER   C N   1 
ATOM   5887 C  CA  . SER   C 1 149 ? -27.075 -8.840  40.266  1.00 45.19  ? 155 SER   C CA  1 
ATOM   5888 C  C   . SER   C 1 149 ? -28.523 -9.027  39.893  1.00 49.23  ? 155 SER   C C   1 
ATOM   5889 O  O   . SER   C 1 149 ? -29.394 -8.485  40.563  1.00 50.00  ? 155 SER   C O   1 
ATOM   5890 C  CB  . SER   C 1 149 ? -26.555 -7.550  39.638  1.00 48.20  ? 155 SER   C CB  1 
ATOM   5891 O  OG  . SER   C 1 149 ? -25.187 -7.338  39.945  1.00 59.79  ? 155 SER   C OG  1 
ATOM   5892 N  N   . SER   C 1 150 ? -28.785 -9.762  38.798  1.00 44.34  ? 156 SER   C N   1 
ATOM   5893 C  CA  . SER   C 1 150 ? -30.138 -10.012 38.302  1.00 43.09  ? 156 SER   C CA  1 
ATOM   5894 C  C   . SER   C 1 150 ? -30.785 -11.192 39.005  1.00 46.44  ? 156 SER   C C   1 
ATOM   5895 O  O   . SER   C 1 150 ? -32.009 -11.213 39.161  1.00 47.11  ? 156 SER   C O   1 
ATOM   5896 C  CB  . SER   C 1 150 ? -30.093 -10.311 36.804  1.00 44.69  ? 156 SER   C CB  1 
ATOM   5897 O  OG  . SER   C 1 150 ? -29.386 -11.524 36.569  1.00 42.20  ? 156 SER   C OG  1 
ATOM   5898 N  N   . GLY   C 1 151 ? -29.972 -12.201 39.323  1.00 40.92  ? 157 GLY   C N   1 
ATOM   5899 C  CA  . GLY   C 1 151 ? -30.430 -13.469 39.872  1.00 40.60  ? 157 GLY   C CA  1 
ATOM   5900 C  C   . GLY   C 1 151 ? -30.889 -14.425 38.778  1.00 45.02  ? 157 GLY   C C   1 
ATOM   5901 O  O   . GLY   C 1 151 ? -31.449 -15.482 39.076  1.00 45.47  ? 157 GLY   C O   1 
ATOM   5902 N  N   . ASN   C 1 152 ? -30.658 -14.061 37.492  1.00 39.60  ? 158 ASN   C N   1 
ATOM   5903 C  CA  . ASN   C 1 152 ? -31.046 -14.870 36.337  1.00 37.22  ? 158 ASN   C CA  1 
ATOM   5904 C  C   . ASN   C 1 152 ? -29.992 -15.922 36.029  1.00 39.52  ? 158 ASN   C C   1 
ATOM   5905 O  O   . ASN   C 1 152 ? -28.824 -15.588 35.788  1.00 38.55  ? 158 ASN   C O   1 
ATOM   5906 C  CB  . ASN   C 1 152 ? -31.383 -13.986 35.152  1.00 36.76  ? 158 ASN   C CB  1 
ATOM   5907 C  CG  . ASN   C 1 152 ? -32.626 -13.149 35.381  1.00 54.12  ? 158 ASN   C CG  1 
ATOM   5908 O  OD1 . ASN   C 1 152 ? -33.549 -13.512 36.128  1.00 47.60  ? 158 ASN   C OD1 1 
ATOM   5909 N  ND2 . ASN   C 1 152 ? -32.686 -12.017 34.731  1.00 42.93  ? 158 ASN   C ND2 1 
ATOM   5910 N  N   . LEU   C 1 153 ? -30.384 -17.207 36.145  1.00 35.86  ? 159 LEU   C N   1 
ATOM   5911 C  CA  . LEU   C 1 153 ? -29.463 -18.325 35.959  1.00 34.93  ? 159 LEU   C CA  1 
ATOM   5912 C  C   . LEU   C 1 153 ? -28.859 -18.414 34.538  1.00 35.78  ? 159 LEU   C C   1 
ATOM   5913 O  O   . LEU   C 1 153 ? -27.783 -18.972 34.409  1.00 34.75  ? 159 LEU   C O   1 
ATOM   5914 C  CB  . LEU   C 1 153 ? -30.088 -19.658 36.395  1.00 35.13  ? 159 LEU   C CB  1 
ATOM   5915 C  CG  . LEU   C 1 153 ? -30.025 -19.904 37.919  1.00 40.22  ? 159 LEU   C CG  1 
ATOM   5916 C  CD1 . LEU   C 1 153 ? -31.121 -20.828 38.382  1.00 40.29  ? 159 LEU   C CD1 1 
ATOM   5917 C  CD2 . LEU   C 1 153 ? -28.658 -20.419 38.356  1.00 41.20  ? 159 LEU   C CD2 1 
ATOM   5918 N  N   . HIS   C 1 154 ? -29.490 -17.806 33.513  1.00 33.69  ? 160 HIS   C N   1 
ATOM   5919 C  CA  . HIS   C 1 154 ? -28.957 -17.773 32.136  1.00 33.53  ? 160 HIS   C CA  1 
ATOM   5920 C  C   . HIS   C 1 154 ? -27.694 -16.888 32.040  1.00 35.74  ? 160 HIS   C C   1 
ATOM   5921 O  O   . HIS   C 1 154 ? -26.949 -16.984 31.070  1.00 35.04  ? 160 HIS   C O   1 
ATOM   5922 C  CB  . HIS   C 1 154 ? -30.050 -17.393 31.101  1.00 34.61  ? 160 HIS   C CB  1 
ATOM   5923 C  CG  . HIS   C 1 154 ? -30.421 -15.938 31.047  1.00 38.63  ? 160 HIS   C CG  1 
ATOM   5924 N  ND1 . HIS   C 1 154 ? -30.909 -15.366 29.885  1.00 41.17  ? 160 HIS   C ND1 1 
ATOM   5925 C  CD2 . HIS   C 1 154 ? -30.337 -14.977 32.000  1.00 41.10  ? 160 HIS   C CD2 1 
ATOM   5926 C  CE1 . HIS   C 1 154 ? -31.109 -14.086 30.170  1.00 40.74  ? 160 HIS   C CE1 1 
ATOM   5927 N  NE2 . HIS   C 1 154 ? -30.770 -13.805 31.428  1.00 40.86  ? 160 HIS   C NE2 1 
ATOM   5928 N  N   . GLY   C 1 155 ? -27.441 -16.088 33.082  1.00 31.84  ? 161 GLY   C N   1 
ATOM   5929 C  CA  . GLY   C 1 155 ? -26.256 -15.246 33.174  1.00 31.09  ? 161 GLY   C CA  1 
ATOM   5930 C  C   . GLY   C 1 155 ? -25.168 -15.876 34.025  1.00 32.31  ? 161 GLY   C C   1 
ATOM   5931 O  O   . GLY   C 1 155 ? -24.137 -15.244 34.283  1.00 30.61  ? 161 GLY   C O   1 
ATOM   5932 N  N   . GLN   C 1 156 ? -25.373 -17.137 34.457  1.00 29.37  ? 162 GLN   C N   1 
ATOM   5933 C  CA  . GLN   C 1 156 ? -24.431 -17.878 35.313  1.00 28.70  ? 162 GLN   C CA  1 
ATOM   5934 C  C   . GLN   C 1 156 ? -24.012 -19.322 34.842  1.00 32.95  ? 162 GLN   C C   1 
ATOM   5935 O  O   . GLN   C 1 156 ? -23.340 -19.993 35.625  1.00 31.97  ? 162 GLN   C O   1 
ATOM   5936 C  CB  . GLN   C 1 156 ? -25.074 -18.047 36.717  1.00 29.82  ? 162 GLN   C CB  1 
ATOM   5937 C  CG  . GLN   C 1 156 ? -25.473 -16.776 37.471  1.00 37.43  ? 162 GLN   C CG  1 
ATOM   5938 C  CD  . GLN   C 1 156 ? -26.419 -17.108 38.614  1.00 44.80  ? 162 GLN   C CD  1 
ATOM   5939 O  OE1 . GLN   C 1 156 ? -26.125 -17.928 39.478  1.00 41.68  ? 162 GLN   C OE1 1 
ATOM   5940 N  NE2 . GLN   C 1 156 ? -27.590 -16.515 38.627  1.00 35.35  ? 162 GLN   C NE2 1 
ATOM   5941 N  N   . PRO   C 1 157 ? -24.390 -19.887 33.663  1.00 31.55  ? 163 PRO   C N   1 
ATOM   5942 C  CA  . PRO   C 1 157 ? -24.124 -21.325 33.423  1.00 30.90  ? 163 PRO   C CA  1 
ATOM   5943 C  C   . PRO   C 1 157 ? -22.679 -21.805 33.524  1.00 32.84  ? 163 PRO   C C   1 
ATOM   5944 O  O   . PRO   C 1 157 ? -22.438 -22.906 34.033  1.00 31.79  ? 163 PRO   C O   1 
ATOM   5945 C  CB  . PRO   C 1 157 ? -24.685 -21.555 32.018  1.00 32.32  ? 163 PRO   C CB  1 
ATOM   5946 C  CG  . PRO   C 1 157 ? -24.770 -20.172 31.402  1.00 35.74  ? 163 PRO   C CG  1 
ATOM   5947 C  CD  . PRO   C 1 157 ? -25.182 -19.329 32.556  1.00 32.44  ? 163 PRO   C CD  1 
ATOM   5948 N  N   . VAL   C 1 158 ? -21.732 -20.999 33.017  1.00 29.28  ? 164 VAL   C N   1 
ATOM   5949 C  CA  . VAL   C 1 158 ? -20.311 -21.343 32.985  1.00 28.52  ? 164 VAL   C CA  1 
ATOM   5950 C  C   . VAL   C 1 158 ? -19.731 -21.528 34.406  1.00 31.96  ? 164 VAL   C C   1 
ATOM   5951 O  O   . VAL   C 1 158 ? -18.839 -22.360 34.566  1.00 31.56  ? 164 VAL   C O   1 
ATOM   5952 C  CB  . VAL   C 1 158 ? -19.465 -20.378 32.110  1.00 31.92  ? 164 VAL   C CB  1 
ATOM   5953 C  CG1 . VAL   C 1 158 ? -18.030 -20.885 31.956  1.00 31.75  ? 164 VAL   C CG1 1 
ATOM   5954 C  CG2 . VAL   C 1 158 ? -20.097 -20.195 30.720  1.00 32.09  ? 164 VAL   C CG2 1 
ATOM   5955 N  N   . SER   C 1 159 ? -20.234 -20.774 35.425  1.00 31.96  ? 165 SER   C N   1 
ATOM   5956 C  CA  . SER   C 1 159 ? -19.736 -20.903 36.808  1.00 31.16  ? 165 SER   C CA  1 
ATOM   5957 C  C   . SER   C 1 159 ? -19.940 -22.306 37.364  1.00 35.28  ? 165 SER   C C   1 
ATOM   5958 O  O   . SER   C 1 159 ? -19.042 -22.807 38.026  1.00 34.59  ? 165 SER   C O   1 
ATOM   5959 C  CB  . SER   C 1 159 ? -20.329 -19.848 37.737  1.00 31.57  ? 165 SER   C CB  1 
ATOM   5960 O  OG  . SER   C 1 159 ? -21.693 -20.107 38.025  1.00 38.18  ? 165 SER   C OG  1 
ATOM   5961 N  N   . PHE   C 1 160 ? -21.066 -22.962 37.019  1.00 32.14  ? 166 PHE   C N   1 
ATOM   5962 C  CA  . PHE   C 1 160 ? -21.364 -24.340 37.429  1.00 32.56  ? 166 PHE   C CA  1 
ATOM   5963 C  C   . PHE   C 1 160 ? -20.501 -25.405 36.716  1.00 36.00  ? 166 PHE   C C   1 
ATOM   5964 O  O   . PHE   C 1 160 ? -20.292 -26.470 37.283  1.00 36.25  ? 166 PHE   C O   1 
ATOM   5965 C  CB  . PHE   C 1 160 ? -22.857 -24.663 37.212  1.00 34.49  ? 166 PHE   C CB  1 
ATOM   5966 C  CG  . PHE   C 1 160 ? -23.792 -23.733 37.932  1.00 35.88  ? 166 PHE   C CG  1 
ATOM   5967 C  CD1 . PHE   C 1 160 ? -24.042 -23.885 39.294  1.00 39.38  ? 166 PHE   C CD1 1 
ATOM   5968 C  CD2 . PHE   C 1 160 ? -24.374 -22.658 37.269  1.00 38.46  ? 166 PHE   C CD2 1 
ATOM   5969 C  CE1 . PHE   C 1 160 ? -24.865 -22.982 39.973  1.00 40.64  ? 166 PHE   C CE1 1 
ATOM   5970 C  CE2 . PHE   C 1 160 ? -25.202 -21.761 37.947  1.00 41.47  ? 166 PHE   C CE2 1 
ATOM   5971 C  CZ  . PHE   C 1 160 ? -25.451 -21.937 39.291  1.00 39.88  ? 166 PHE   C CZ  1 
ATOM   5972 N  N   . LEU   C 1 161 ? -20.000 -25.132 35.487  1.00 32.38  ? 167 LEU   C N   1 
ATOM   5973 C  CA  . LEU   C 1 161 ? -19.218 -26.104 34.707  1.00 32.18  ? 167 LEU   C CA  1 
ATOM   5974 C  C   . LEU   C 1 161 ? -17.699 -26.001 34.848  1.00 37.95  ? 167 LEU   C C   1 
ATOM   5975 O  O   . LEU   C 1 161 ? -16.986 -26.975 34.586  1.00 38.23  ? 167 LEU   C O   1 
ATOM   5976 C  CB  . LEU   C 1 161 ? -19.605 -25.992 33.214  1.00 32.05  ? 167 LEU   C CB  1 
ATOM   5977 C  CG  . LEU   C 1 161 ? -21.122 -26.094 32.917  1.00 34.93  ? 167 LEU   C CG  1 
ATOM   5978 C  CD1 . LEU   C 1 161 ? -21.455 -25.493 31.564  1.00 35.01  ? 167 LEU   C CD1 1 
ATOM   5979 C  CD2 . LEU   C 1 161 ? -21.608 -27.524 33.026  1.00 35.18  ? 167 LEU   C CD2 1 
ATOM   5980 N  N   . LEU   C 1 162 ? -17.207 -24.816 35.199  1.00 35.64  ? 168 LEU   C N   1 
ATOM   5981 C  CA  . LEU   C 1 162 ? -15.781 -24.505 35.284  1.00 35.77  ? 168 LEU   C CA  1 
ATOM   5982 C  C   . LEU   C 1 162 ? -15.133 -25.109 36.519  1.00 38.86  ? 168 LEU   C C   1 
ATOM   5983 O  O   . LEU   C 1 162 ? -15.518 -24.766 37.636  1.00 37.36  ? 168 LEU   C O   1 
ATOM   5984 C  CB  . LEU   C 1 162 ? -15.605 -22.970 35.239  1.00 36.41  ? 168 LEU   C CB  1 
ATOM   5985 C  CG  . LEU   C 1 162 ? -14.383 -22.366 34.527  1.00 43.42  ? 168 LEU   C CG  1 
ATOM   5986 C  CD1 . LEU   C 1 162 ? -13.166 -22.311 35.427  1.00 45.57  ? 168 LEU   C CD1 1 
ATOM   5987 C  CD2 . LEU   C 1 162 ? -14.122 -22.978 33.156  1.00 44.87  ? 168 LEU   C CD2 1 
ATOM   5988 N  N   . ARG   C 1 163 ? -14.145 -26.011 36.311  1.00 36.68  ? 169 ARG   C N   1 
ATOM   5989 C  CA  . ARG   C 1 163 ? -13.421 -26.706 37.390  1.00 37.56  ? 169 ARG   C CA  1 
ATOM   5990 C  C   . ARG   C 1 163 ? -12.768 -25.767 38.395  1.00 42.49  ? 169 ARG   C C   1 
ATOM   5991 O  O   . ARG   C 1 163 ? -12.940 -25.943 39.603  1.00 41.19  ? 169 ARG   C O   1 
ATOM   5992 C  CB  . ARG   C 1 163 ? -12.347 -27.645 36.821  1.00 39.34  ? 169 ARG   C CB  1 
ATOM   5993 C  CG  . ARG   C 1 163 ? -12.896 -28.927 36.221  1.00 45.47  ? 169 ARG   C CG  1 
ATOM   5994 C  CD  . ARG   C 1 163 ? -11.768 -29.801 35.696  1.00 51.91  ? 169 ARG   C CD  1 
ATOM   5995 N  NE  . ARG   C 1 163 ? -12.180 -30.558 34.510  1.00 65.03  ? 169 ARG   C NE  1 
ATOM   5996 C  CZ  . ARG   C 1 163 ? -12.760 -31.752 34.552  1.00 79.88  ? 169 ARG   C CZ  1 
ATOM   5997 N  NH1 . ARG   C 1 163 ? -12.995 -32.343 35.717  1.00 73.62  ? 169 ARG   C NH1 1 
ATOM   5998 N  NH2 . ARG   C 1 163 ? -13.112 -32.363 33.429  1.00 63.76  ? 169 ARG   C NH2 1 
ATOM   5999 N  N   . GLU   C 1 164 ? -12.020 -24.774 37.895  1.00 41.97  ? 170 GLU   C N   1 
ATOM   6000 C  CA  . GLU   C 1 164 ? -11.271 -23.801 38.705  1.00 41.64  ? 170 GLU   C CA  1 
ATOM   6001 C  C   . GLU   C 1 164 ? -12.152 -22.890 39.561  1.00 47.46  ? 170 GLU   C C   1 
ATOM   6002 O  O   . GLU   C 1 164 ? -11.638 -22.263 40.491  1.00 49.25  ? 170 GLU   C O   1 
ATOM   6003 C  CB  . GLU   C 1 164 ? -10.321 -22.977 37.819  1.00 42.78  ? 170 GLU   C CB  1 
ATOM   6004 C  CG  . GLU   C 1 164 ? -9.191  -23.784 37.183  1.00 50.27  ? 170 GLU   C CG  1 
ATOM   6005 C  CD  . GLU   C 1 164 ? -9.457  -24.439 35.835  1.00 58.96  ? 170 GLU   C CD  1 
ATOM   6006 O  OE1 . GLU   C 1 164 ? -10.638 -24.565 35.436  1.00 43.56  ? 170 GLU   C OE1 1 
ATOM   6007 O  OE2 . GLU   C 1 164 ? -8.470  -24.869 35.195  1.00 50.17  ? 170 GLU   C OE2 1 
ATOM   6008 N  N   . LEU   C 1 165 ? -13.464 -22.820 39.275  1.00 42.07  ? 171 LEU   C N   1 
ATOM   6009 C  CA  . LEU   C 1 165 ? -14.386 -21.978 40.041  1.00 41.13  ? 171 LEU   C CA  1 
ATOM   6010 C  C   . LEU   C 1 165 ? -15.213 -22.732 41.096  1.00 43.21  ? 171 LEU   C C   1 
ATOM   6011 O  O   . LEU   C 1 165 ? -16.034 -22.087 41.745  1.00 41.77  ? 171 LEU   C O   1 
ATOM   6012 C  CB  . LEU   C 1 165 ? -15.356 -21.237 39.096  1.00 41.30  ? 171 LEU   C CB  1 
ATOM   6013 C  CG  . LEU   C 1 165 ? -14.905 -19.910 38.512  1.00 45.81  ? 171 LEU   C CG  1 
ATOM   6014 C  CD1 . LEU   C 1 165 ? -15.723 -19.576 37.267  1.00 46.48  ? 171 LEU   C CD1 1 
ATOM   6015 C  CD2 . LEU   C 1 165 ? -15.044 -18.780 39.538  1.00 46.98  ? 171 LEU   C CD2 1 
ATOM   6016 N  N   . GLN   C 1 166 ? -15.050 -24.076 41.236  1.00 39.91  ? 172 GLN   C N   1 
ATOM   6017 C  CA  . GLN   C 1 166 ? -15.853 -24.907 42.161  1.00 40.94  ? 172 GLN   C CA  1 
ATOM   6018 C  C   . GLN   C 1 166 ? -15.912 -24.362 43.618  1.00 46.56  ? 172 GLN   C C   1 
ATOM   6019 O  O   . GLN   C 1 166 ? -16.996 -24.328 44.222  1.00 45.65  ? 172 GLN   C O   1 
ATOM   6020 C  CB  . GLN   C 1 166 ? -15.399 -26.380 42.133  1.00 42.73  ? 172 GLN   C CB  1 
ATOM   6021 C  CG  . GLN   C 1 166 ? -16.347 -27.342 42.872  1.00 60.55  ? 172 GLN   C CG  1 
ATOM   6022 C  CD  . GLN   C 1 166 ? -16.021 -28.816 42.715  1.00 77.39  ? 172 GLN   C CD  1 
ATOM   6023 O  OE1 . GLN   C 1 166 ? -14.863 -29.226 42.563  1.00 70.57  ? 172 GLN   C OE1 1 
ATOM   6024 N  NE2 . GLN   C 1 166 ? -17.044 -29.656 42.819  1.00 68.36  ? 172 GLN   C NE2 1 
ATOM   6025 N  N   . ASP   C 1 167 ? -14.775 -23.880 44.143  1.00 45.50  ? 173 ASP   C N   1 
ATOM   6026 C  CA  . ASP   C 1 167 ? -14.692 -23.340 45.511  1.00 46.57  ? 173 ASP   C CA  1 
ATOM   6027 C  C   . ASP   C 1 167 ? -15.435 -21.996 45.696  1.00 48.24  ? 173 ASP   C C   1 
ATOM   6028 O  O   . ASP   C 1 167 ? -15.679 -21.598 46.839  1.00 48.10  ? 173 ASP   C O   1 
ATOM   6029 C  CB  . ASP   C 1 167 ? -13.227 -23.250 45.981  1.00 49.52  ? 173 ASP   C CB  1 
ATOM   6030 C  CG  . ASP   C 1 167 ? -12.332 -22.330 45.167  1.00 69.91  ? 173 ASP   C CG  1 
ATOM   6031 O  OD1 . ASP   C 1 167 ? -12.667 -22.055 43.989  1.00 72.06  ? 173 ASP   C OD1 1 
ATOM   6032 O  OD2 . ASP   C 1 167 ? -11.268 -21.925 45.689  1.00 78.34  ? 173 ASP   C OD2 1 
ATOM   6033 N  N   . LYS   C 1 168 ? -15.842 -21.331 44.582  1.00 42.61  ? 174 LYS   C N   1 
ATOM   6034 C  CA  . LYS   C 1 168 ? -16.579 -20.062 44.599  1.00 41.48  ? 174 LYS   C CA  1 
ATOM   6035 C  C   . LYS   C 1 168 ? -18.068 -20.228 44.321  1.00 45.16  ? 174 LYS   C C   1 
ATOM   6036 O  O   . LYS   C 1 168 ? -18.812 -19.252 44.401  1.00 45.72  ? 174 LYS   C O   1 
ATOM   6037 C  CB  . LYS   C 1 168 ? -15.954 -19.030 43.623  1.00 43.77  ? 174 LYS   C CB  1 
ATOM   6038 C  CG  . LYS   C 1 168 ? -14.433 -18.868 43.734  1.00 43.47  ? 174 LYS   C CG  1 
ATOM   6039 C  CD  . LYS   C 1 168 ? -13.984 -18.170 45.030  1.00 52.50  ? 174 LYS   C CD  1 
ATOM   6040 C  CE  . LYS   C 1 168 ? -12.474 -18.157 45.111  1.00 64.60  ? 174 LYS   C CE  1 
ATOM   6041 N  NZ  . LYS   C 1 168 ? -11.988 -17.892 46.488  1.00 77.34  ? 174 LYS   C NZ  1 
ATOM   6042 N  N   . VAL   C 1 169 ? -18.506 -21.450 43.984  1.00 42.35  ? 175 VAL   C N   1 
ATOM   6043 C  CA  . VAL   C 1 169 ? -19.905 -21.742 43.663  1.00 42.22  ? 175 VAL   C CA  1 
ATOM   6044 C  C   . VAL   C 1 169 ? -20.585 -22.515 44.805  1.00 47.25  ? 175 VAL   C C   1 
ATOM   6045 O  O   . VAL   C 1 169 ? -20.174 -23.645 45.098  1.00 45.47  ? 175 VAL   C O   1 
ATOM   6046 C  CB  . VAL   C 1 169 ? -20.071 -22.442 42.277  1.00 45.45  ? 175 VAL   C CB  1 
ATOM   6047 C  CG1 . VAL   C 1 169 ? -21.505 -22.929 42.061  1.00 45.10  ? 175 VAL   C CG1 1 
ATOM   6048 C  CG2 . VAL   C 1 169 ? -19.653 -21.513 41.144  1.00 45.16  ? 175 VAL   C CG2 1 
ATOM   6049 N  N   . PRO   C 1 170 ? -21.623 -21.928 45.452  1.00 45.98  ? 176 PRO   C N   1 
ATOM   6050 C  CA  . PRO   C 1 170 ? -22.309 -22.656 46.529  1.00 47.08  ? 176 PRO   C CA  1 
ATOM   6051 C  C   . PRO   C 1 170 ? -23.192 -23.753 45.948  1.00 53.67  ? 176 PRO   C C   1 
ATOM   6052 O  O   . PRO   C 1 170 ? -23.523 -23.706 44.760  1.00 53.18  ? 176 PRO   C O   1 
ATOM   6053 C  CB  . PRO   C 1 170 ? -23.150 -21.570 47.213  1.00 48.38  ? 176 PRO   C CB  1 
ATOM   6054 C  CG  . PRO   C 1 170 ? -23.403 -20.566 46.164  1.00 51.70  ? 176 PRO   C CG  1 
ATOM   6055 C  CD  . PRO   C 1 170 ? -22.241 -20.605 45.216  1.00 47.00  ? 176 PRO   C CD  1 
ATOM   6056 N  N   . GLN   C 1 171 ? -23.573 -24.736 46.778  1.00 51.37  ? 177 GLN   C N   1 
ATOM   6057 C  CA  . GLN   C 1 171 ? -24.441 -25.820 46.338  1.00 51.46  ? 177 GLN   C CA  1 
ATOM   6058 C  C   . GLN   C 1 171 ? -25.885 -25.322 46.339  1.00 55.15  ? 177 GLN   C C   1 
ATOM   6059 O  O   . GLN   C 1 171 ? -26.415 -24.985 47.396  1.00 55.81  ? 177 GLN   C O   1 
ATOM   6060 C  CB  . GLN   C 1 171 ? -24.250 -27.062 47.227  1.00 53.18  ? 177 GLN   C CB  1 
ATOM   6061 C  CG  . GLN   C 1 171 ? -24.306 -28.364 46.441  1.00 77.96  ? 177 GLN   C CG  1 
ATOM   6062 C  CD  . GLN   C 1 171 ? -25.490 -29.211 46.833  1.00 104.59 ? 177 GLN   C CD  1 
ATOM   6063 O  OE1 . GLN   C 1 171 ? -25.363 -30.180 47.593  1.00 100.24 ? 177 GLN   C OE1 1 
ATOM   6064 N  NE2 . GLN   C 1 171 ? -26.667 -28.870 46.318  1.00 98.65  ? 177 GLN   C NE2 1 
ATOM   6065 N  N   . LEU   C 1 172 ? -26.489 -25.195 45.144  1.00 50.58  ? 178 LEU   C N   1 
ATOM   6066 C  CA  . LEU   C 1 172 ? -27.868 -24.725 44.952  1.00 49.92  ? 178 LEU   C CA  1 
ATOM   6067 C  C   . LEU   C 1 172 ? -28.819 -25.918 44.944  1.00 52.34  ? 178 LEU   C C   1 
ATOM   6068 O  O   . LEU   C 1 172 ? -28.406 -26.995 44.501  1.00 51.42  ? 178 LEU   C O   1 
ATOM   6069 C  CB  . LEU   C 1 172 ? -27.987 -23.995 43.602  1.00 49.98  ? 178 LEU   C CB  1 
ATOM   6070 C  CG  . LEU   C 1 172 ? -28.077 -22.482 43.604  1.00 55.28  ? 178 LEU   C CG  1 
ATOM   6071 C  CD1 . LEU   C 1 172 ? -26.822 -21.847 44.190  1.00 55.58  ? 178 LEU   C CD1 1 
ATOM   6072 C  CD2 . LEU   C 1 172 ? -28.286 -21.967 42.192  1.00 58.15  ? 178 LEU   C CD2 1 
ATOM   6073 N  N   . PRO   C 1 173 ? -30.093 -25.769 45.395  1.00 48.81  ? 179 PRO   C N   1 
ATOM   6074 C  CA  . PRO   C 1 173 ? -31.015 -26.920 45.350  1.00 48.08  ? 179 PRO   C CA  1 
ATOM   6075 C  C   . PRO   C 1 173 ? -31.323 -27.320 43.901  1.00 50.14  ? 179 PRO   C C   1 
ATOM   6076 O  O   . PRO   C 1 173 ? -31.590 -26.458 43.054  1.00 50.28  ? 179 PRO   C O   1 
ATOM   6077 C  CB  . PRO   C 1 173 ? -32.258 -26.412 46.091  1.00 49.76  ? 179 PRO   C CB  1 
ATOM   6078 C  CG  . PRO   C 1 173 ? -32.208 -24.925 45.954  1.00 53.99  ? 179 PRO   C CG  1 
ATOM   6079 C  CD  . PRO   C 1 173 ? -30.752 -24.571 45.963  1.00 49.89  ? 179 PRO   C CD  1 
ATOM   6080 N  N   . GLY   C 1 174 ? -31.221 -28.615 43.624  1.00 44.25  ? 180 GLY   C N   1 
ATOM   6081 C  CA  . GLY   C 1 174 ? -31.435 -29.165 42.290  1.00 42.80  ? 180 GLY   C CA  1 
ATOM   6082 C  C   . GLY   C 1 174 ? -30.216 -29.088 41.390  1.00 42.77  ? 180 GLY   C C   1 
ATOM   6083 O  O   . GLY   C 1 174 ? -30.290 -29.503 40.232  1.00 41.82  ? 180 GLY   C O   1 
ATOM   6084 N  N   . PHE   C 1 175 ? -29.075 -28.598 41.924  1.00 37.19  ? 181 PHE   C N   1 
ATOM   6085 C  CA  . PHE   C 1 175 ? -27.826 -28.415 41.187  1.00 36.69  ? 181 PHE   C CA  1 
ATOM   6086 C  C   . PHE   C 1 175 ? -26.699 -29.332 41.628  1.00 42.11  ? 181 PHE   C C   1 
ATOM   6087 O  O   . PHE   C 1 175 ? -25.606 -29.253 41.065  1.00 40.89  ? 181 PHE   C O   1 
ATOM   6088 C  CB  . PHE   C 1 175 ? -27.373 -26.933 41.237  1.00 37.99  ? 181 PHE   C CB  1 
ATOM   6089 C  CG  . PHE   C 1 175 ? -28.111 -25.985 40.318  1.00 38.55  ? 181 PHE   C CG  1 
ATOM   6090 C  CD1 . PHE   C 1 175 ? -29.434 -25.645 40.557  1.00 40.34  ? 181 PHE   C CD1 1 
ATOM   6091 C  CD2 . PHE   C 1 175 ? -27.457 -25.375 39.253  1.00 41.97  ? 181 PHE   C CD2 1 
ATOM   6092 C  CE1 . PHE   C 1 175 ? -30.112 -24.769 39.710  1.00 41.54  ? 181 PHE   C CE1 1 
ATOM   6093 C  CE2 . PHE   C 1 175 ? -28.139 -24.506 38.397  1.00 44.06  ? 181 PHE   C CE2 1 
ATOM   6094 C  CZ  . PHE   C 1 175 ? -29.465 -24.217 38.625  1.00 41.65  ? 181 PHE   C CZ  1 
ATOM   6095 N  N   . SER   C 1 176 ? -26.946 -30.215 42.617  1.00 41.10  ? 182 SER   C N   1 
ATOM   6096 C  CA  . SER   C 1 176 ? -25.905 -31.118 43.136  1.00 41.63  ? 182 SER   C CA  1 
ATOM   6097 C  C   . SER   C 1 176 ? -25.376 -32.152 42.147  1.00 45.45  ? 182 SER   C C   1 
ATOM   6098 O  O   . SER   C 1 176 ? -24.186 -32.489 42.204  1.00 46.62  ? 182 SER   C O   1 
ATOM   6099 C  CB  . SER   C 1 176 ? -26.379 -31.818 44.398  1.00 47.01  ? 182 SER   C CB  1 
ATOM   6100 O  OG  . SER   C 1 176 ? -25.285 -32.324 45.143  1.00 62.84  ? 182 SER   C OG  1 
ATOM   6101 N  N   . TRP   C 1 177 ? -26.242 -32.649 41.249  1.00 40.76  ? 183 TRP   C N   1 
ATOM   6102 C  CA  . TRP   C 1 177 ? -25.884 -33.620 40.198  1.00 40.53  ? 183 TRP   C CA  1 
ATOM   6103 C  C   . TRP   C 1 177 ? -24.740 -33.128 39.296  1.00 43.95  ? 183 TRP   C C   1 
ATOM   6104 O  O   . TRP   C 1 177 ? -24.027 -33.954 38.730  1.00 42.44  ? 183 TRP   C O   1 
ATOM   6105 C  CB  . TRP   C 1 177 ? -27.116 -33.966 39.332  1.00 38.92  ? 183 TRP   C CB  1 
ATOM   6106 C  CG  . TRP   C 1 177 ? -27.650 -32.806 38.539  1.00 39.52  ? 183 TRP   C CG  1 
ATOM   6107 C  CD1 . TRP   C 1 177 ? -28.582 -31.895 38.943  1.00 42.27  ? 183 TRP   C CD1 1 
ATOM   6108 C  CD2 . TRP   C 1 177 ? -27.263 -32.424 37.208  1.00 38.86  ? 183 TRP   C CD2 1 
ATOM   6109 N  NE1 . TRP   C 1 177 ? -28.810 -30.975 37.942  1.00 41.64  ? 183 TRP   C NE1 1 
ATOM   6110 C  CE2 . TRP   C 1 177 ? -27.994 -31.261 36.877  1.00 42.47  ? 183 TRP   C CE2 1 
ATOM   6111 C  CE3 . TRP   C 1 177 ? -26.353 -32.943 36.268  1.00 39.68  ? 183 TRP   C CE3 1 
ATOM   6112 C  CZ2 . TRP   C 1 177 ? -27.839 -30.603 35.647  1.00 41.15  ? 183 TRP   C CZ2 1 
ATOM   6113 C  CZ3 . TRP   C 1 177 ? -26.199 -32.289 35.050  1.00 40.24  ? 183 TRP   C CZ3 1 
ATOM   6114 C  CH2 . TRP   C 1 177 ? -26.948 -31.149 34.742  1.00 40.71  ? 183 TRP   C CH2 1 
ATOM   6115 N  N   . ILE   C 1 178 ? -24.586 -31.782 39.151  1.00 41.08  ? 184 ILE   C N   1 
ATOM   6116 C  CA  . ILE   C 1 178 ? -23.577 -31.143 38.301  1.00 40.73  ? 184 ILE   C CA  1 
ATOM   6117 C  C   . ILE   C 1 178 ? -22.182 -31.390 38.797  1.00 47.52  ? 184 ILE   C C   1 
ATOM   6118 O  O   . ILE   C 1 178 ? -21.841 -30.977 39.905  1.00 50.52  ? 184 ILE   C O   1 
ATOM   6119 C  CB  . ILE   C 1 178 ? -23.813 -29.618 38.103  1.00 43.29  ? 184 ILE   C CB  1 
ATOM   6120 C  CG1 . ILE   C 1 178 ? -25.200 -29.330 37.549  1.00 42.88  ? 184 ILE   C CG1 1 
ATOM   6121 C  CG2 . ILE   C 1 178 ? -22.703 -28.985 37.219  1.00 43.50  ? 184 ILE   C CG2 1 
ATOM   6122 C  CD1 . ILE   C 1 178 ? -25.714 -28.018 37.880  1.00 44.47  ? 184 ILE   C CD1 1 
ATOM   6123 N  N   . LYS   C 1 179 ? -21.360 -31.987 37.938  1.00 42.92  ? 185 LYS   C N   1 
ATOM   6124 C  CA  . LYS   C 1 179 ? -19.954 -32.241 38.181  1.00 42.55  ? 185 LYS   C CA  1 
ATOM   6125 C  C   . LYS   C 1 179 ? -19.175 -31.275 37.254  1.00 46.76  ? 185 LYS   C C   1 
ATOM   6126 O  O   . LYS   C 1 179 ? -19.297 -31.416 36.024  1.00 46.16  ? 185 LYS   C O   1 
ATOM   6127 C  CB  . LYS   C 1 179 ? -19.612 -33.699 37.840  1.00 45.72  ? 185 LYS   C CB  1 
ATOM   6128 C  CG  . LYS   C 1 179 ? -20.270 -34.733 38.745  1.00 69.16  ? 185 LYS   C CG  1 
ATOM   6129 C  CD  . LYS   C 1 179 ? -20.021 -36.156 38.235  1.00 82.17  ? 185 LYS   C CD  1 
ATOM   6130 C  CE  . LYS   C 1 179 ? -20.518 -37.224 39.185  1.00 97.13  ? 185 LYS   C CE  1 
ATOM   6131 N  NZ  . LYS   C 1 179 ? -22.004 -37.333 39.193  1.00 107.81 ? 185 LYS   C NZ  1 
ATOM   6132 N  N   . PRO   C 1 180 ? -18.407 -30.276 37.787  1.00 42.74  ? 186 PRO   C N   1 
ATOM   6133 C  CA  . PRO   C 1 180 ? -17.639 -29.377 36.889  1.00 42.65  ? 186 PRO   C CA  1 
ATOM   6134 C  C   . PRO   C 1 180 ? -16.846 -30.183 35.862  1.00 44.16  ? 186 PRO   C C   1 
ATOM   6135 O  O   . PRO   C 1 180 ? -16.139 -31.117 36.231  1.00 43.04  ? 186 PRO   C O   1 
ATOM   6136 C  CB  . PRO   C 1 180 ? -16.751 -28.577 37.854  1.00 44.41  ? 186 PRO   C CB  1 
ATOM   6137 C  CG  . PRO   C 1 180 ? -17.517 -28.583 39.132  1.00 48.80  ? 186 PRO   C CG  1 
ATOM   6138 C  CD  . PRO   C 1 180 ? -18.164 -29.938 39.204  1.00 44.11  ? 186 PRO   C CD  1 
ATOM   6139 N  N   . CYS   C 1 181 ? -17.045 -29.888 34.568  1.00 39.74  ? 187 CYS   C N   1 
ATOM   6140 C  CA  . CYS   C 1 181 ? -16.483 -30.703 33.483  1.00 39.22  ? 187 CYS   C CA  1 
ATOM   6141 C  C   . CYS   C 1 181 ? -15.575 -29.960 32.489  1.00 43.28  ? 187 CYS   C C   1 
ATOM   6142 O  O   . CYS   C 1 181 ? -15.046 -30.591 31.576  1.00 44.02  ? 187 CYS   C O   1 
ATOM   6143 C  CB  . CYS   C 1 181 ? -17.608 -31.437 32.759  1.00 39.08  ? 187 CYS   C CB  1 
ATOM   6144 S  SG  . CYS   C 1 181 ? -19.001 -30.378 32.278  1.00 42.54  ? 187 CYS   C SG  1 
ATOM   6145 N  N   . ILE   C 1 182 ? -15.363 -28.659 32.655  1.00 40.04  ? 188 ILE   C N   1 
ATOM   6146 C  CA  . ILE   C 1 182 ? -14.473 -27.927 31.746  1.00 40.15  ? 188 ILE   C CA  1 
ATOM   6147 C  C   . ILE   C 1 182 ? -13.420 -27.149 32.500  1.00 39.95  ? 188 ILE   C C   1 
ATOM   6148 O  O   . ILE   C 1 182 ? -13.729 -26.570 33.526  1.00 37.69  ? 188 ILE   C O   1 
ATOM   6149 C  CB  . ILE   C 1 182 ? -15.201 -27.034 30.699  1.00 44.03  ? 188 ILE   C CB  1 
ATOM   6150 C  CG1 . ILE   C 1 182 ? -16.260 -26.110 31.349  1.00 45.29  ? 188 ILE   C CG1 1 
ATOM   6151 C  CG2 . ILE   C 1 182 ? -15.779 -27.896 29.575  1.00 46.69  ? 188 ILE   C CG2 1 
ATOM   6152 C  CD1 . ILE   C 1 182 ? -16.884 -24.991 30.411  1.00 60.75  ? 188 ILE   C CD1 1 
ATOM   6153 N  N   . SER   C 1 183 ? -12.184 -27.127 31.988  1.00 36.40  ? 189 SER   C N   1 
ATOM   6154 C  CA  . SER   C 1 183 ? -11.130 -26.329 32.605  1.00 36.72  ? 189 SER   C CA  1 
ATOM   6155 C  C   . SER   C 1 183 ? -11.060 -24.978 31.875  1.00 38.47  ? 189 SER   C C   1 
ATOM   6156 O  O   . SER   C 1 183 ? -11.441 -24.889 30.704  1.00 34.86  ? 189 SER   C O   1 
ATOM   6157 C  CB  . SER   C 1 183 ? -9.788  -27.054 32.558  1.00 41.84  ? 189 SER   C CB  1 
ATOM   6158 O  OG  . SER   C 1 183 ? -9.228  -27.038 31.254  1.00 58.48  ? 189 SER   C OG  1 
ATOM   6159 N  N   . SER   C 1 184 ? -10.566 -23.934 32.560  1.00 36.04  ? 190 SER   C N   1 
ATOM   6160 C  CA  . SER   C 1 184 ? -10.469 -22.587 32.002  1.00 35.35  ? 190 SER   C CA  1 
ATOM   6161 C  C   . SER   C 1 184 ? -9.713  -22.513 30.653  1.00 37.26  ? 190 SER   C C   1 
ATOM   6162 O  O   . SER   C 1 184 ? -10.049 -21.661 29.840  1.00 36.66  ? 190 SER   C O   1 
ATOM   6163 C  CB  . SER   C 1 184 ? -9.887  -21.619 33.028  1.00 40.68  ? 190 SER   C CB  1 
ATOM   6164 O  OG  . SER   C 1 184 ? -8.543  -21.929 33.345  1.00 55.68  ? 190 SER   C OG  1 
ATOM   6165 N  N   . ALA   C 1 185 ? -8.756  -23.434 30.390  1.00 34.28  ? 191 ALA   C N   1 
ATOM   6166 C  CA  . ALA   C 1 185 ? -7.999  -23.499 29.127  1.00 34.11  ? 191 ALA   C CA  1 
ATOM   6167 C  C   . ALA   C 1 185 ? -8.784  -24.153 27.958  1.00 34.07  ? 191 ALA   C C   1 
ATOM   6168 O  O   . ALA   C 1 185 ? -8.347  -24.076 26.807  1.00 32.98  ? 191 ALA   C O   1 
ATOM   6169 C  CB  . ALA   C 1 185 ? -6.678  -24.239 29.347  1.00 35.07  ? 191 ALA   C CB  1 
ATOM   6170 N  N   . SER   C 1 186 ? -9.920  -24.801 28.254  1.00 30.61  ? 192 SER   C N   1 
ATOM   6171 C  CA  . SER   C 1 186 ? -10.746 -25.524 27.263  1.00 30.40  ? 192 SER   C CA  1 
ATOM   6172 C  C   . SER   C 1 186 ? -12.000 -24.784 26.799  1.00 31.42  ? 192 SER   C C   1 
ATOM   6173 O  O   . SER   C 1 186 ? -12.819 -25.367 26.101  1.00 30.18  ? 192 SER   C O   1 
ATOM   6174 C  CB  . SER   C 1 186 ? -11.124 -26.896 27.805  1.00 33.53  ? 192 SER   C CB  1 
ATOM   6175 O  OG  . SER   C 1 186 ? -9.936  -27.653 27.946  1.00 38.83  ? 192 SER   C OG  1 
ATOM   6176 N  N   . ILE   C 1 187 ? -12.176 -23.540 27.235  1.00 26.88  ? 193 ILE   C N   1 
ATOM   6177 C  CA  . ILE   C 1 187 ? -13.269 -22.664 26.801  1.00 26.45  ? 193 ILE   C CA  1 
ATOM   6178 C  C   . ILE   C 1 187 ? -12.716 -21.352 26.220  1.00 32.07  ? 193 ILE   C C   1 
ATOM   6179 O  O   . ILE   C 1 187 ? -11.873 -20.699 26.849  1.00 32.13  ? 193 ILE   C O   1 
ATOM   6180 C  CB  . ILE   C 1 187 ? -14.371 -22.435 27.889  1.00 29.50  ? 193 ILE   C CB  1 
ATOM   6181 C  CG1 . ILE   C 1 187 ? -15.508 -21.475 27.366  1.00 28.91  ? 193 ILE   C CG1 1 
ATOM   6182 C  CG2 . ILE   C 1 187 ? -13.768 -21.951 29.245  1.00 30.17  ? 193 ILE   C CG2 1 
ATOM   6183 C  CD1 . ILE   C 1 187 ? -16.787 -21.365 28.241  1.00 31.20  ? 193 ILE   C CD1 1 
ATOM   6184 N  N   . VAL   C 1 188 ? -13.225 -20.946 25.045  1.00 27.60  ? 194 VAL   C N   1 
ATOM   6185 C  CA  . VAL   C 1 188 ? -12.863 -19.671 24.418  1.00 26.13  ? 194 VAL   C CA  1 
ATOM   6186 C  C   . VAL   C 1 188 ? -14.177 -18.936 24.120  1.00 29.44  ? 194 VAL   C C   1 
ATOM   6187 O  O   . VAL   C 1 188 ? -15.085 -19.532 23.545  1.00 28.14  ? 194 VAL   C O   1 
ATOM   6188 C  CB  . VAL   C 1 188 ? -12.017 -19.871 23.139  1.00 28.32  ? 194 VAL   C CB  1 
ATOM   6189 C  CG1 . VAL   C 1 188 ? -11.864 -18.569 22.342  1.00 27.66  ? 194 VAL   C CG1 1 
ATOM   6190 C  CG2 . VAL   C 1 188 ? -10.644 -20.483 23.471  1.00 28.04  ? 194 VAL   C CG2 1 
ATOM   6191 N  N   . TYR   C 1 189 ? -14.265 -17.663 24.531  1.00 26.54  ? 195 TYR   C N   1 
ATOM   6192 C  CA  . TYR   C 1 189 ? -15.396 -16.795 24.220  1.00 26.98  ? 195 TYR   C CA  1 
ATOM   6193 C  C   . TYR   C 1 189 ? -15.160 -15.995 22.960  1.00 28.77  ? 195 TYR   C C   1 
ATOM   6194 O  O   . TYR   C 1 189 ? -14.034 -15.514 22.733  1.00 27.01  ? 195 TYR   C O   1 
ATOM   6195 C  CB  . TYR   C 1 189 ? -15.653 -15.799 25.352  1.00 28.12  ? 195 TYR   C CB  1 
ATOM   6196 C  CG  . TYR   C 1 189 ? -16.211 -16.420 26.602  1.00 28.78  ? 195 TYR   C CG  1 
ATOM   6197 C  CD1 . TYR   C 1 189 ? -17.578 -16.573 26.772  1.00 29.26  ? 195 TYR   C CD1 1 
ATOM   6198 C  CD2 . TYR   C 1 189 ? -15.371 -16.830 27.634  1.00 29.18  ? 195 TYR   C CD2 1 
ATOM   6199 C  CE1 . TYR   C 1 189 ? -18.101 -17.130 27.937  1.00 30.63  ? 195 TYR   C CE1 1 
ATOM   6200 C  CE2 . TYR   C 1 189 ? -15.883 -17.369 28.809  1.00 29.55  ? 195 TYR   C CE2 1 
ATOM   6201 C  CZ  . TYR   C 1 189 ? -17.251 -17.511 28.958  1.00 34.55  ? 195 TYR   C CZ  1 
ATOM   6202 O  OH  . TYR   C 1 189 ? -17.755 -17.998 30.129  1.00 31.01  ? 195 TYR   C OH  1 
ATOM   6203 N  N   . ILE   C 1 190 ? -16.242 -15.763 22.178  1.00 23.58  ? 196 ILE   C N   1 
ATOM   6204 C  CA  . ILE   C 1 190 ? -16.219 -14.886 20.990  1.00 22.74  ? 196 ILE   C CA  1 
ATOM   6205 C  C   . ILE   C 1 190 ? -17.454 -13.977 20.999  1.00 27.26  ? 196 ILE   C C   1 
ATOM   6206 O  O   . ILE   C 1 190 ? -18.573 -14.487 21.074  1.00 26.48  ? 196 ILE   C O   1 
ATOM   6207 C  CB  . ILE   C 1 190 ? -16.132 -15.679 19.632  1.00 24.69  ? 196 ILE   C CB  1 
ATOM   6208 C  CG1 . ILE   C 1 190 ? -14.897 -16.643 19.574  1.00 24.07  ? 196 ILE   C CG1 1 
ATOM   6209 C  CG2 . ILE   C 1 190 ? -16.124 -14.714 18.432  1.00 26.53  ? 196 ILE   C CG2 1 
ATOM   6210 C  CD1 . ILE   C 1 190 ? -14.904 -17.612 18.352  1.00 22.24  ? 196 ILE   C CD1 1 
ATOM   6211 N  N   . GLY   C 1 191 ? -17.249 -12.661 20.854  1.00 25.45  ? 197 GLY   C N   1 
ATOM   6212 C  CA  . GLY   C 1 191 ? -18.346 -11.693 20.722  1.00 24.87  ? 197 GLY   C CA  1 
ATOM   6213 C  C   . GLY   C 1 191 ? -18.661 -10.794 21.901  1.00 28.62  ? 197 GLY   C C   1 
ATOM   6214 O  O   . GLY   C 1 191 ? -19.551 -9.950  21.795  1.00 28.49  ? 197 GLY   C O   1 
ATOM   6215 N  N   . LEU   C 1 192 ? -17.971 -10.992 23.044  1.00 26.29  ? 198 LEU   C N   1 
ATOM   6216 C  CA  . LEU   C 1 192 ? -18.200 -10.288 24.307  1.00 26.27  ? 198 LEU   C CA  1 
ATOM   6217 C  C   . LEU   C 1 192 ? -18.279 -8.787  24.169  1.00 31.45  ? 198 LEU   C C   1 
ATOM   6218 O  O   . LEU   C 1 192 ? -17.422 -8.178  23.544  1.00 29.55  ? 198 LEU   C O   1 
ATOM   6219 C  CB  . LEU   C 1 192 ? -17.160 -10.664 25.386  1.00 25.62  ? 198 LEU   C CB  1 
ATOM   6220 C  CG  . LEU   C 1 192 ? -16.971 -12.140 25.754  1.00 29.10  ? 198 LEU   C CG  1 
ATOM   6221 C  CD1 . LEU   C 1 192 ? -15.971 -12.278 26.910  1.00 28.17  ? 198 LEU   C CD1 1 
ATOM   6222 C  CD2 . LEU   C 1 192 ? -18.308 -12.816 26.094  1.00 28.89  ? 198 LEU   C CD2 1 
ATOM   6223 N  N   . ARG   C 1 193 ? -19.326 -8.197  24.734  1.00 31.64  ? 199 ARG   C N   1 
ATOM   6224 C  CA  . ARG   C 1 193 ? -19.502 -6.740  24.727  1.00 32.36  ? 199 ARG   C CA  1 
ATOM   6225 C  C   . ARG   C 1 193 ? -20.332 -6.243  25.922  1.00 37.09  ? 199 ARG   C C   1 
ATOM   6226 O  O   . ARG   C 1 193 ? -20.453 -5.043  26.099  1.00 36.27  ? 199 ARG   C O   1 
ATOM   6227 C  CB  . ARG   C 1 193 ? -20.045 -6.213  23.381  1.00 29.40  ? 199 ARG   C CB  1 
ATOM   6228 C  CG  . ARG   C 1 193 ? -21.417 -6.747  22.980  1.00 30.11  ? 199 ARG   C CG  1 
ATOM   6229 C  CD  . ARG   C 1 193 ? -21.673 -6.319  21.543  1.00 27.47  ? 199 ARG   C CD  1 
ATOM   6230 N  NE  . ARG   C 1 193 ? -22.986 -6.751  21.074  1.00 31.17  ? 199 ARG   C NE  1 
ATOM   6231 C  CZ  . ARG   C 1 193 ? -23.278 -7.973  20.640  1.00 38.40  ? 199 ARG   C CZ  1 
ATOM   6232 N  NH1 . ARG   C 1 193 ? -22.340 -8.926  20.615  1.00 28.63  ? 199 ARG   C NH1 1 
ATOM   6233 N  NH2 . ARG   C 1 193 ? -24.501 -8.255  20.220  1.00 27.96  ? 199 ARG   C NH2 1 
ATOM   6234 N  N   . ASP   C 1 194 ? -20.905 -7.157  26.735  1.00 33.55  ? 200 ASP   C N   1 
ATOM   6235 C  CA  . ASP   C 1 194 ? -21.688 -6.767  27.914  1.00 32.91  ? 200 ASP   C CA  1 
ATOM   6236 C  C   . ASP   C 1 194 ? -21.284 -7.672  29.083  1.00 35.90  ? 200 ASP   C C   1 
ATOM   6237 O  O   . ASP   C 1 194 ? -21.972 -8.648  29.401  1.00 34.68  ? 200 ASP   C O   1 
ATOM   6238 C  CB  . ASP   C 1 194 ? -23.195 -6.782  27.600  1.00 33.81  ? 200 ASP   C CB  1 
ATOM   6239 C  CG  . ASP   C 1 194 ? -24.149 -6.526  28.765  1.00 44.07  ? 200 ASP   C CG  1 
ATOM   6240 O  OD1 . ASP   C 1 194 ? -23.690 -6.019  29.816  1.00 43.74  ? 200 ASP   C OD1 1 
ATOM   6241 O  OD2 . ASP   C 1 194 ? -25.359 -6.834  28.622  1.00 46.88  ? 200 ASP   C OD2 1 
ATOM   6242 N  N   . VAL   C 1 195 ? -20.119 -7.330  29.693  1.00 31.41  ? 201 VAL   C N   1 
ATOM   6243 C  CA  . VAL   C 1 195 ? -19.438 -8.074  30.740  1.00 31.25  ? 201 VAL   C CA  1 
ATOM   6244 C  C   . VAL   C 1 195 ? -19.514 -7.355  32.103  1.00 37.92  ? 201 VAL   C C   1 
ATOM   6245 O  O   . VAL   C 1 195 ? -19.084 -6.206  32.214  1.00 37.15  ? 201 VAL   C O   1 
ATOM   6246 C  CB  . VAL   C 1 195 ? -17.971 -8.392  30.307  1.00 33.66  ? 201 VAL   C CB  1 
ATOM   6247 C  CG1 . VAL   C 1 195 ? -17.261 -9.278  31.336  1.00 33.08  ? 201 VAL   C CG1 1 
ATOM   6248 C  CG2 . VAL   C 1 195 ? -17.927 -9.056  28.917  1.00 33.10  ? 201 VAL   C CG2 1 
ATOM   6249 N  N   . ASP   C 1 196 ? -20.068 -8.046  33.130  1.00 35.17  ? 202 ASP   C N   1 
ATOM   6250 C  CA  . ASP   C 1 196 ? -20.163 -7.513  34.496  1.00 33.75  ? 202 ASP   C CA  1 
ATOM   6251 C  C   . ASP   C 1 196 ? -18.783 -7.444  35.147  1.00 38.49  ? 202 ASP   C C   1 
ATOM   6252 O  O   . ASP   C 1 196 ? -17.943 -8.307  34.865  1.00 36.33  ? 202 ASP   C O   1 
ATOM   6253 C  CB  . ASP   C 1 196 ? -21.112 -8.358  35.354  1.00 34.39  ? 202 ASP   C CB  1 
ATOM   6254 C  CG  . ASP   C 1 196 ? -22.561 -8.304  34.930  1.00 41.50  ? 202 ASP   C CG  1 
ATOM   6255 O  OD1 . ASP   C 1 196 ? -22.992 -7.244  34.403  1.00 40.74  ? 202 ASP   C OD1 1 
ATOM   6256 O  OD2 . ASP   C 1 196 ? -23.275 -9.307  35.137  1.00 45.64  ? 202 ASP   C OD2 1 
ATOM   6257 N  N   . PRO   C 1 197 ? -18.536 -6.465  36.064  1.00 37.48  ? 203 PRO   C N   1 
ATOM   6258 C  CA  . PRO   C 1 197 ? -17.220 -6.402  36.745  1.00 36.86  ? 203 PRO   C CA  1 
ATOM   6259 C  C   . PRO   C 1 197 ? -16.765 -7.722  37.405  1.00 39.82  ? 203 PRO   C C   1 
ATOM   6260 O  O   . PRO   C 1 197 ? -15.589 -8.046  37.211  1.00 39.49  ? 203 PRO   C O   1 
ATOM   6261 C  CB  . PRO   C 1 197 ? -17.385 -5.253  37.746  1.00 38.29  ? 203 PRO   C CB  1 
ATOM   6262 C  CG  . PRO   C 1 197 ? -18.479 -4.408  37.164  1.00 42.57  ? 203 PRO   C CG  1 
ATOM   6263 C  CD  . PRO   C 1 197 ? -19.430 -5.376  36.524  1.00 38.48  ? 203 PRO   C CD  1 
ATOM   6264 N  N   . PRO   C 1 198 ? -17.612 -8.540  38.108  1.00 37.03  ? 204 PRO   C N   1 
ATOM   6265 C  CA  . PRO   C 1 198 ? -17.110 -9.827  38.617  1.00 36.77  ? 204 PRO   C CA  1 
ATOM   6266 C  C   . PRO   C 1 198 ? -16.771 -10.823 37.494  1.00 39.54  ? 204 PRO   C C   1 
ATOM   6267 O  O   . PRO   C 1 198 ? -15.875 -11.637 37.659  1.00 38.30  ? 204 PRO   C O   1 
ATOM   6268 C  CB  . PRO   C 1 198 ? -18.266 -10.348 39.460  1.00 38.34  ? 204 PRO   C CB  1 
ATOM   6269 C  CG  . PRO   C 1 198 ? -19.458 -9.694  38.948  1.00 42.58  ? 204 PRO   C CG  1 
ATOM   6270 C  CD  . PRO   C 1 198 ? -19.038 -8.363  38.463  1.00 38.92  ? 204 PRO   C CD  1 
ATOM   6271 N  N   . GLU   C 1 199 ? -17.471 -10.732 36.343  1.00 36.09  ? 205 GLU   C N   1 
ATOM   6272 C  CA  . GLU   C 1 199 ? -17.203 -11.599 35.187  1.00 34.62  ? 205 GLU   C CA  1 
ATOM   6273 C  C   . GLU   C 1 199 ? -15.877 -11.232 34.574  1.00 36.34  ? 205 GLU   C C   1 
ATOM   6274 O  O   . GLU   C 1 199 ? -15.092 -12.138 34.301  1.00 34.17  ? 205 GLU   C O   1 
ATOM   6275 C  CB  . GLU   C 1 199 ? -18.318 -11.534 34.158  1.00 34.98  ? 205 GLU   C CB  1 
ATOM   6276 C  CG  . GLU   C 1 199 ? -19.614 -12.141 34.646  1.00 37.80  ? 205 GLU   C CG  1 
ATOM   6277 C  CD  . GLU   C 1 199 ? -20.662 -12.058 33.565  1.00 42.85  ? 205 GLU   C CD  1 
ATOM   6278 O  OE1 . GLU   C 1 199 ? -21.034 -10.922 33.196  1.00 36.46  ? 205 GLU   C OE1 1 
ATOM   6279 O  OE2 . GLU   C 1 199 ? -21.043 -13.121 33.024  1.00 34.31  ? 205 GLU   C OE2 1 
ATOM   6280 N  N   . HIS   C 1 200 ? -15.584 -9.906  34.419  1.00 34.19  ? 206 HIS   C N   1 
ATOM   6281 C  CA  . HIS   C 1 200 ? -14.291 -9.478  33.888  1.00 33.51  ? 206 HIS   C CA  1 
ATOM   6282 C  C   . HIS   C 1 200 ? -13.174 -9.980  34.806  1.00 37.16  ? 206 HIS   C C   1 
ATOM   6283 O  O   . HIS   C 1 200 ? -12.118 -10.393 34.317  1.00 36.10  ? 206 HIS   C O   1 
ATOM   6284 C  CB  . HIS   C 1 200 ? -14.216 -7.950  33.706  1.00 34.42  ? 206 HIS   C CB  1 
ATOM   6285 C  CG  . HIS   C 1 200 ? -12.922 -7.503  33.105  1.00 37.52  ? 206 HIS   C CG  1 
ATOM   6286 N  ND1 . HIS   C 1 200 ? -11.818 -7.233  33.890  1.00 39.14  ? 206 HIS   C ND1 1 
ATOM   6287 C  CD2 . HIS   C 1 200 ? -12.585 -7.338  31.805  1.00 39.09  ? 206 HIS   C CD2 1 
ATOM   6288 C  CE1 . HIS   C 1 200 ? -10.843 -6.930  33.047  1.00 38.28  ? 206 HIS   C CE1 1 
ATOM   6289 N  NE2 . HIS   C 1 200 ? -11.260 -6.967  31.785  1.00 38.72  ? 206 HIS   C NE2 1 
ATOM   6290 N  N   . PHE   C 1 201 ? -13.414 -9.946  36.140  1.00 35.18  ? 207 PHE   C N   1 
ATOM   6291 C  CA  . PHE   C 1 201 ? -12.457 -10.433 37.136  1.00 36.21  ? 207 PHE   C CA  1 
ATOM   6292 C  C   . PHE   C 1 201 ? -12.183 -11.919 36.941  1.00 37.20  ? 207 PHE   C C   1 
ATOM   6293 O  O   . PHE   C 1 201 ? -11.024 -12.319 36.874  1.00 36.61  ? 207 PHE   C O   1 
ATOM   6294 C  CB  . PHE   C 1 201 ? -12.942 -10.117 38.566  1.00 39.01  ? 207 PHE   C CB  1 
ATOM   6295 C  CG  . PHE   C 1 201 ? -12.114 -10.762 39.651  1.00 42.14  ? 207 PHE   C CG  1 
ATOM   6296 C  CD1 . PHE   C 1 201 ? -10.963 -10.147 40.129  1.00 46.51  ? 207 PHE   C CD1 1 
ATOM   6297 C  CD2 . PHE   C 1 201 ? -12.487 -11.985 40.199  1.00 44.95  ? 207 PHE   C CD2 1 
ATOM   6298 C  CE1 . PHE   C 1 201 ? -10.210 -10.737 41.145  1.00 47.55  ? 207 PHE   C CE1 1 
ATOM   6299 C  CE2 . PHE   C 1 201 ? -11.710 -12.590 41.189  1.00 48.36  ? 207 PHE   C CE2 1 
ATOM   6300 C  CZ  . PHE   C 1 201 ? -10.581 -11.960 41.658  1.00 46.69  ? 207 PHE   C CZ  1 
ATOM   6301 N  N   . ILE   C 1 202 ? -13.245 -12.737 36.797  1.00 33.98  ? 208 ILE   C N   1 
ATOM   6302 C  CA  . ILE   C 1 202 ? -13.101 -14.181 36.575  1.00 33.00  ? 208 ILE   C CA  1 
ATOM   6303 C  C   . ILE   C 1 202 ? -12.271 -14.457 35.312  1.00 36.70  ? 208 ILE   C C   1 
ATOM   6304 O  O   . ILE   C 1 202 ? -11.312 -15.235 35.361  1.00 36.77  ? 208 ILE   C O   1 
ATOM   6305 C  CB  . ILE   C 1 202 ? -14.489 -14.899 36.548  1.00 35.42  ? 208 ILE   C CB  1 
ATOM   6306 C  CG1 . ILE   C 1 202 ? -15.113 -14.938 37.956  1.00 35.95  ? 208 ILE   C CG1 1 
ATOM   6307 C  CG2 . ILE   C 1 202 ? -14.350 -16.321 35.996  1.00 34.91  ? 208 ILE   C CG2 1 
ATOM   6308 C  CD1 . ILE   C 1 202 ? -16.684 -15.071 37.994  1.00 39.92  ? 208 ILE   C CD1 1 
ATOM   6309 N  N   . LEU   C 1 203 ? -12.632 -13.805 34.188  1.00 34.40  ? 209 LEU   C N   1 
ATOM   6310 C  CA  . LEU   C 1 203 ? -11.961 -13.992 32.899  1.00 33.95  ? 209 LEU   C CA  1 
ATOM   6311 C  C   . LEU   C 1 203 ? -10.466 -13.748 33.012  1.00 37.98  ? 209 LEU   C C   1 
ATOM   6312 O  O   . LEU   C 1 203 ? -9.687  -14.610 32.619  1.00 38.17  ? 209 LEU   C O   1 
ATOM   6313 C  CB  . LEU   C 1 203 ? -12.603 -13.112 31.800  1.00 33.83  ? 209 LEU   C CB  1 
ATOM   6314 C  CG  . LEU   C 1 203 ? -14.050 -13.486 31.425  1.00 39.46  ? 209 LEU   C CG  1 
ATOM   6315 C  CD1 . LEU   C 1 203 ? -14.702 -12.394 30.581  1.00 40.08  ? 209 LEU   C CD1 1 
ATOM   6316 C  CD2 . LEU   C 1 203 ? -14.119 -14.839 30.710  1.00 41.20  ? 209 LEU   C CD2 1 
ATOM   6317 N  N   . LYS   C 1 204 ? -10.069 -12.628 33.649  1.00 35.87  ? 210 LYS   C N   1 
ATOM   6318 C  CA  . LYS   C 1 204 ? -8.650  -12.299 33.819  1.00 36.29  ? 210 LYS   C CA  1 
ATOM   6319 C  C   . LYS   C 1 204 ? -7.956  -13.169 34.864  1.00 41.17  ? 210 LYS   C C   1 
ATOM   6320 O  O   . LYS   C 1 204 ? -6.909  -13.740 34.573  1.00 41.15  ? 210 LYS   C O   1 
ATOM   6321 C  CB  . LYS   C 1 204 ? -8.448  -10.807 34.100  1.00 40.02  ? 210 LYS   C CB  1 
ATOM   6322 C  CG  . LYS   C 1 204 ? -8.821  -9.895  32.926  1.00 61.58  ? 210 LYS   C CG  1 
ATOM   6323 C  CD  . LYS   C 1 204 ? -7.853  -9.976  31.739  1.00 73.54  ? 210 LYS   C CD  1 
ATOM   6324 C  CE  . LYS   C 1 204 ? -8.135  -8.900  30.722  1.00 86.65  ? 210 LYS   C CE  1 
ATOM   6325 N  NZ  . LYS   C 1 204 ? -7.100  -8.860  29.654  1.00 100.77 ? 210 LYS   C NZ  1 
ATOM   6326 N  N   . ASN   C 1 205 ? -8.569  -13.324 36.039  1.00 38.40  ? 211 ASN   C N   1 
ATOM   6327 C  CA  . ASN   C 1 205 ? -7.995  -14.092 37.147  1.00 38.72  ? 211 ASN   C CA  1 
ATOM   6328 C  C   . ASN   C 1 205 ? -7.828  -15.582 36.869  1.00 42.46  ? 211 ASN   C C   1 
ATOM   6329 O  O   . ASN   C 1 205 ? -6.820  -16.151 37.291  1.00 41.45  ? 211 ASN   C O   1 
ATOM   6330 C  CB  . ASN   C 1 205 ? -8.769  -13.853 38.438  1.00 41.21  ? 211 ASN   C CB  1 
ATOM   6331 C  CG  . ASN   C 1 205 ? -8.176  -12.709 39.230  1.00 86.27  ? 211 ASN   C CG  1 
ATOM   6332 O  OD1 . ASN   C 1 205 ? -8.170  -11.541 38.797  1.00 84.27  ? 211 ASN   C OD1 1 
ATOM   6333 N  ND2 . ASN   C 1 205 ? -7.625  -13.023 40.397  1.00 82.08  ? 211 ASN   C ND2 1 
ATOM   6334 N  N   . TYR   C 1 206 ? -8.762  -16.202 36.127  1.00 39.94  ? 212 TYR   C N   1 
ATOM   6335 C  CA  . TYR   C 1 206 ? -8.673  -17.635 35.793  1.00 39.57  ? 212 TYR   C CA  1 
ATOM   6336 C  C   . TYR   C 1 206 ? -8.111  -17.905 34.385  1.00 41.78  ? 212 TYR   C C   1 
ATOM   6337 O  O   . TYR   C 1 206 ? -8.133  -19.053 33.922  1.00 40.13  ? 212 TYR   C O   1 
ATOM   6338 C  CB  . TYR   C 1 206 ? -10.021 -18.339 36.011  1.00 41.87  ? 212 TYR   C CB  1 
ATOM   6339 C  CG  . TYR   C 1 206 ? -10.476 -18.302 37.452  1.00 44.55  ? 212 TYR   C CG  1 
ATOM   6340 C  CD1 . TYR   C 1 206 ? -10.083 -19.288 38.354  1.00 46.41  ? 212 TYR   C CD1 1 
ATOM   6341 C  CD2 . TYR   C 1 206 ? -11.253 -17.250 37.931  1.00 45.73  ? 212 TYR   C CD2 1 
ATOM   6342 C  CE1 . TYR   C 1 206 ? -10.473 -19.239 39.692  1.00 46.61  ? 212 TYR   C CE1 1 
ATOM   6343 C  CE2 . TYR   C 1 206 ? -11.628 -17.178 39.270  1.00 46.95  ? 212 TYR   C CE2 1 
ATOM   6344 C  CZ  . TYR   C 1 206 ? -11.250 -18.184 40.144  1.00 52.82  ? 212 TYR   C CZ  1 
ATOM   6345 O  OH  . TYR   C 1 206 ? -11.665 -18.124 41.454  1.00 49.97  ? 212 TYR   C OH  1 
ATOM   6346 N  N   . ASP   C 1 207 ? -7.545  -16.852 33.737  1.00 38.30  ? 213 ASP   C N   1 
ATOM   6347 C  CA  . ASP   C 1 207 ? -6.912  -16.890 32.414  1.00 38.22  ? 213 ASP   C CA  1 
ATOM   6348 C  C   . ASP   C 1 207 ? -7.793  -17.537 31.326  1.00 38.95  ? 213 ASP   C C   1 
ATOM   6349 O  O   . ASP   C 1 207 ? -7.334  -18.385 30.563  1.00 38.98  ? 213 ASP   C O   1 
ATOM   6350 C  CB  . ASP   C 1 207 ? -5.518  -17.550 32.474  1.00 40.53  ? 213 ASP   C CB  1 
ATOM   6351 C  CG  . ASP   C 1 207 ? -4.426  -16.674 31.895  1.00 62.31  ? 213 ASP   C CG  1 
ATOM   6352 O  OD1 . ASP   C 1 207 ? -4.519  -16.319 30.692  1.00 63.20  ? 213 ASP   C OD1 1 
ATOM   6353 O  OD2 . ASP   C 1 207 ? -3.486  -16.328 32.645  1.00 74.07  ? 213 ASP   C OD2 1 
ATOM   6354 N  N   . ILE   C 1 208 ? -9.067  -17.170 31.308  1.00 34.54  ? 214 ILE   C N   1 
ATOM   6355 C  CA  . ILE   C 1 208 ? -10.005 -17.668 30.304  1.00 33.02  ? 214 ILE   C CA  1 
ATOM   6356 C  C   . ILE   C 1 208 ? -9.829  -16.782 29.072  1.00 35.40  ? 214 ILE   C C   1 
ATOM   6357 O  O   . ILE   C 1 208 ? -10.018 -15.569 29.153  1.00 35.69  ? 214 ILE   C O   1 
ATOM   6358 C  CB  . ILE   C 1 208 ? -11.473 -17.692 30.806  1.00 35.50  ? 214 ILE   C CB  1 
ATOM   6359 C  CG1 . ILE   C 1 208 ? -11.606 -18.602 32.052  1.00 35.44  ? 214 ILE   C CG1 1 
ATOM   6360 C  CG2 . ILE   C 1 208 ? -12.409 -18.168 29.667  1.00 34.96  ? 214 ILE   C CG2 1 
ATOM   6361 C  CD1 . ILE   C 1 208 ? -12.691 -18.247 33.021  1.00 39.82  ? 214 ILE   C CD1 1 
ATOM   6362 N  N   . GLN   C 1 209 ? -9.446  -17.387 27.944  1.00 30.93  ? 215 GLN   C N   1 
ATOM   6363 C  CA  . GLN   C 1 209 ? -9.225  -16.654 26.706  1.00 30.51  ? 215 GLN   C CA  1 
ATOM   6364 C  C   . GLN   C 1 209 ? -10.531 -16.215 26.067  1.00 33.87  ? 215 GLN   C C   1 
ATOM   6365 O  O   . GLN   C 1 209 ? -11.489 -16.991 26.016  1.00 32.82  ? 215 GLN   C O   1 
ATOM   6366 C  CB  . GLN   C 1 209 ? -8.370  -17.469 25.733  1.00 31.65  ? 215 GLN   C CB  1 
ATOM   6367 C  CG  . GLN   C 1 209 ? -7.032  -17.956 26.336  1.00 44.20  ? 215 GLN   C CG  1 
ATOM   6368 C  CD  . GLN   C 1 209 ? -6.221  -16.845 26.964  1.00 58.89  ? 215 GLN   C CD  1 
ATOM   6369 O  OE1 . GLN   C 1 209 ? -5.900  -15.835 26.322  1.00 54.57  ? 215 GLN   C OE1 1 
ATOM   6370 N  NE2 . GLN   C 1 209 ? -5.931  -16.977 28.253  1.00 47.26  ? 215 GLN   C NE2 1 
ATOM   6371 N  N   . TYR   C 1 210 ? -10.577 -14.957 25.626  1.00 29.96  ? 216 TYR   C N   1 
ATOM   6372 C  CA  . TYR   C 1 210 ? -11.757 -14.409 24.963  1.00 29.56  ? 216 TYR   C CA  1 
ATOM   6373 C  C   . TYR   C 1 210 ? -11.418 -13.468 23.800  1.00 32.10  ? 216 TYR   C C   1 
ATOM   6374 O  O   . TYR   C 1 210 ? -10.325 -12.881 23.758  1.00 31.03  ? 216 TYR   C O   1 
ATOM   6375 C  CB  . TYR   C 1 210 ? -12.712 -13.748 25.966  1.00 31.17  ? 216 TYR   C CB  1 
ATOM   6376 C  CG  . TYR   C 1 210 ? -12.145 -12.519 26.646  1.00 34.63  ? 216 TYR   C CG  1 
ATOM   6377 C  CD1 . TYR   C 1 210 ? -12.304 -11.253 26.086  1.00 36.95  ? 216 TYR   C CD1 1 
ATOM   6378 C  CD2 . TYR   C 1 210 ? -11.482 -12.617 27.864  1.00 36.40  ? 216 TYR   C CD2 1 
ATOM   6379 C  CE1 . TYR   C 1 210 ? -11.781 -10.120 26.702  1.00 40.26  ? 216 TYR   C CE1 1 
ATOM   6380 C  CE2 . TYR   C 1 210 ? -10.951 -11.488 28.492  1.00 37.69  ? 216 TYR   C CE2 1 
ATOM   6381 C  CZ  . TYR   C 1 210 ? -11.105 -10.242 27.906  1.00 47.22  ? 216 TYR   C CZ  1 
ATOM   6382 O  OH  . TYR   C 1 210 ? -10.620 -9.121  28.532  1.00 48.92  ? 216 TYR   C OH  1 
ATOM   6383 N  N   . PHE   C 1 211 ? -12.367 -13.313 22.867  1.00 26.46  ? 217 PHE   C N   1 
ATOM   6384 C  CA  . PHE   C 1 211 ? -12.230 -12.388 21.741  1.00 26.53  ? 217 PHE   C CA  1 
ATOM   6385 C  C   . PHE   C 1 211 ? -13.445 -11.509 21.775  1.00 30.06  ? 217 PHE   C C   1 
ATOM   6386 O  O   . PHE   C 1 211 ? -14.522 -11.913 21.324  1.00 29.33  ? 217 PHE   C O   1 
ATOM   6387 C  CB  . PHE   C 1 211 ? -12.061 -13.120 20.386  1.00 28.38  ? 217 PHE   C CB  1 
ATOM   6388 C  CG  . PHE   C 1 211 ? -10.773 -13.901 20.308  1.00 29.32  ? 217 PHE   C CG  1 
ATOM   6389 C  CD1 . PHE   C 1 211 ? -9.569  -13.261 20.023  1.00 32.19  ? 217 PHE   C CD1 1 
ATOM   6390 C  CD2 . PHE   C 1 211 ? -10.743 -15.251 20.629  1.00 31.88  ? 217 PHE   C CD2 1 
ATOM   6391 C  CE1 . PHE   C 1 211 ? -8.374  -13.976 19.986  1.00 34.05  ? 217 PHE   C CE1 1 
ATOM   6392 C  CE2 . PHE   C 1 211 ? -9.545  -15.963 20.601  1.00 35.67  ? 217 PHE   C CE2 1 
ATOM   6393 C  CZ  . PHE   C 1 211 ? -8.369  -15.321 20.281  1.00 34.49  ? 217 PHE   C CZ  1 
ATOM   6394 N  N   . SER   C 1 212 ? -13.316 -10.352 22.436  1.00 26.15  ? 218 SER   C N   1 
ATOM   6395 C  CA  . SER   C 1 212 ? -14.450 -9.417  22.541  1.00 25.90  ? 218 SER   C CA  1 
ATOM   6396 C  C   . SER   C 1 212 ? -14.692 -8.783  21.171  1.00 29.21  ? 218 SER   C C   1 
ATOM   6397 O  O   . SER   C 1 212 ? -13.924 -9.027  20.249  1.00 28.61  ? 218 SER   C O   1 
ATOM   6398 C  CB  . SER   C 1 212 ? -14.126 -8.321  23.550  1.00 29.00  ? 218 SER   C CB  1 
ATOM   6399 O  OG  . SER   C 1 212 ? -13.064 -7.524  23.045  1.00 31.43  ? 218 SER   C OG  1 
ATOM   6400 N  N   . MET   C 1 213 ? -15.709 -7.903  21.056  1.00 26.11  ? 219 MET   C N   1 
ATOM   6401 C  CA  . MET   C 1 213 ? -15.963 -7.198  19.813  1.00 26.07  ? 219 MET   C CA  1 
ATOM   6402 C  C   . MET   C 1 213 ? -14.772 -6.317  19.433  1.00 31.48  ? 219 MET   C C   1 
ATOM   6403 O  O   . MET   C 1 213 ? -14.480 -6.173  18.239  1.00 31.69  ? 219 MET   C O   1 
ATOM   6404 C  CB  . MET   C 1 213 ? -17.251 -6.363  19.930  1.00 27.28  ? 219 MET   C CB  1 
ATOM   6405 C  CG  . MET   C 1 213 ? -18.537 -7.218  19.956  1.00 29.44  ? 219 MET   C CG  1 
ATOM   6406 S  SD  . MET   C 1 213 ? -18.720 -8.610  18.778  1.00 31.11  ? 219 MET   C SD  1 
ATOM   6407 C  CE  . MET   C 1 213 ? -18.461 -7.798  17.208  1.00 27.46  ? 219 MET   C CE  1 
ATOM   6408 N  N   . ARG   C 1 214 ? -14.035 -5.810  20.445  1.00 29.92  ? 220 ARG   C N   1 
ATOM   6409 C  CA  . ARG   C 1 214 ? -12.834 -4.992  20.242  1.00 29.73  ? 220 ARG   C CA  1 
ATOM   6410 C  C   . ARG   C 1 214 ? -11.701 -5.851  19.671  1.00 32.38  ? 220 ARG   C C   1 
ATOM   6411 O  O   . ARG   C 1 214 ? -11.006 -5.397  18.771  1.00 30.76  ? 220 ARG   C O   1 
ATOM   6412 C  CB  . ARG   C 1 214 ? -12.412 -4.292  21.552  1.00 29.96  ? 220 ARG   C CB  1 
ATOM   6413 C  CG  . ARG   C 1 214 ? -11.116 -3.499  21.405  1.00 32.60  ? 220 ARG   C CG  1 
ATOM   6414 C  CD  . ARG   C 1 214 ? -10.548 -3.042  22.722  1.00 41.10  ? 220 ARG   C CD  1 
ATOM   6415 N  NE  . ARG   C 1 214 ? -9.105  -2.838  22.604  1.00 42.94  ? 220 ARG   C NE  1 
ATOM   6416 C  CZ  . ARG   C 1 214 ? -8.541  -1.712  22.187  1.00 57.10  ? 220 ARG   C CZ  1 
ATOM   6417 N  NH1 . ARG   C 1 214 ? -9.293  -0.662  21.868  1.00 45.41  ? 220 ARG   C NH1 1 
ATOM   6418 N  NH2 . ARG   C 1 214 ? -7.220  -1.624  22.089  1.00 45.36  ? 220 ARG   C NH2 1 
ATOM   6419 N  N   . ASP   C 1 215 ? -11.526 -7.093  20.165  1.00 30.72  ? 221 ASP   C N   1 
ATOM   6420 C  CA  . ASP   C 1 215 ? -10.532 -8.022  19.588  1.00 31.61  ? 221 ASP   C CA  1 
ATOM   6421 C  C   . ASP   C 1 215 ? -10.864 -8.338  18.107  1.00 32.42  ? 221 ASP   C C   1 
ATOM   6422 O  O   . ASP   C 1 215 ? -9.957  -8.393  17.280  1.00 31.76  ? 221 ASP   C O   1 
ATOM   6423 C  CB  . ASP   C 1 215 ? -10.443 -9.321  20.392  1.00 33.51  ? 221 ASP   C CB  1 
ATOM   6424 C  CG  . ASP   C 1 215 ? -9.894  -9.136  21.785  1.00 39.74  ? 221 ASP   C CG  1 
ATOM   6425 O  OD1 . ASP   C 1 215 ? -8.792  -8.538  21.917  1.00 41.18  ? 221 ASP   C OD1 1 
ATOM   6426 O  OD2 . ASP   C 1 215 ? -10.550 -9.599  22.744  1.00 34.78  ? 221 ASP   C OD2 1 
ATOM   6427 N  N   . ILE   C 1 216 ? -12.164 -8.485  17.778  1.00 27.92  ? 222 ILE   C N   1 
ATOM   6428 C  CA  . ILE   C 1 216 ? -12.634 -8.741  16.407  1.00 27.21  ? 222 ILE   C CA  1 
ATOM   6429 C  C   . ILE   C 1 216 ? -12.365 -7.515  15.524  1.00 32.94  ? 222 ILE   C C   1 
ATOM   6430 O  O   . ILE   C 1 216 ? -11.920 -7.681  14.389  1.00 31.74  ? 222 ILE   C O   1 
ATOM   6431 C  CB  . ILE   C 1 216 ? -14.127 -9.233  16.336  1.00 29.72  ? 222 ILE   C CB  1 
ATOM   6432 C  CG1 . ILE   C 1 216 ? -14.332 -10.532 17.164  1.00 27.93  ? 222 ILE   C CG1 1 
ATOM   6433 C  CG2 . ILE   C 1 216 ? -14.549 -9.455  14.845  1.00 30.45  ? 222 ILE   C CG2 1 
ATOM   6434 C  CD1 . ILE   C 1 216 ? -15.862 -10.849 17.484  1.00 28.81  ? 222 ILE   C CD1 1 
ATOM   6435 N  N   . ASP   C 1 217 ? -12.642 -6.276  16.042  1.00 30.81  ? 223 ASP   C N   1 
ATOM   6436 C  CA  . ASP   C 1 217 ? -12.383 -5.021  15.312  1.00 29.77  ? 223 ASP   C CA  1 
ATOM   6437 C  C   . ASP   C 1 217 ? -10.903 -4.907  14.916  1.00 35.56  ? 223 ASP   C C   1 
ATOM   6438 O  O   . ASP   C 1 217 ? -10.580 -4.430  13.825  1.00 36.04  ? 223 ASP   C O   1 
ATOM   6439 C  CB  . ASP   C 1 217 ? -12.752 -3.813  16.180  1.00 30.49  ? 223 ASP   C CB  1 
ATOM   6440 C  CG  . ASP   C 1 217 ? -14.227 -3.671  16.445  1.00 36.52  ? 223 ASP   C CG  1 
ATOM   6441 O  OD1 . ASP   C 1 217 ? -15.026 -4.267  15.682  1.00 34.99  ? 223 ASP   C OD1 1 
ATOM   6442 O  OD2 . ASP   C 1 217 ? -14.591 -2.997  17.444  1.00 35.40  ? 223 ASP   C OD2 1 
ATOM   6443 N  N   . ARG   C 1 218 ? -10.019 -5.361  15.798  1.00 34.08  ? 224 ARG   C N   1 
ATOM   6444 C  CA  . ARG   C 1 218 ? -8.562  -5.315  15.614  1.00 34.46  ? 224 ARG   C CA  1 
ATOM   6445 C  C   . ARG   C 1 218 ? -8.006  -6.454  14.732  1.00 37.58  ? 224 ARG   C C   1 
ATOM   6446 O  O   . ARG   C 1 218 ? -7.355  -6.205  13.711  1.00 37.06  ? 224 ARG   C O   1 
ATOM   6447 C  CB  . ARG   C 1 218 ? -7.884  -5.355  16.990  1.00 35.66  ? 224 ARG   C CB  1 
ATOM   6448 C  CG  . ARG   C 1 218 ? -7.945  -4.037  17.737  1.00 40.28  ? 224 ARG   C CG  1 
ATOM   6449 C  CD  . ARG   C 1 218 ? -7.319  -4.129  19.125  1.00 37.29  ? 224 ARG   C CD  1 
ATOM   6450 N  NE  . ARG   C 1 218 ? -5.934  -4.605  19.070  1.00 38.03  ? 224 ARG   C NE  1 
ATOM   6451 C  CZ  . ARG   C 1 218 ? -4.865  -3.812  19.065  1.00 50.99  ? 224 ARG   C CZ  1 
ATOM   6452 N  NH1 . ARG   C 1 218 ? -5.006  -2.496  19.125  1.00 40.32  ? 224 ARG   C NH1 1 
ATOM   6453 N  NH2 . ARG   C 1 218 ? -3.645  -4.331  19.020  1.00 38.68  ? 224 ARG   C NH2 1 
ATOM   6454 N  N   . LEU   C 1 219 ? -8.248  -7.707  15.140  1.00 31.93  ? 225 LEU   C N   1 
ATOM   6455 C  CA  . LEU   C 1 219 ? -7.694  -8.871  14.445  1.00 32.30  ? 225 LEU   C CA  1 
ATOM   6456 C  C   . LEU   C 1 219 ? -8.436  -9.252  13.185  1.00 33.86  ? 225 LEU   C C   1 
ATOM   6457 O  O   . LEU   C 1 219 ? -7.823  -9.750  12.240  1.00 32.86  ? 225 LEU   C O   1 
ATOM   6458 C  CB  . LEU   C 1 219 ? -7.681  -10.097 15.403  1.00 32.51  ? 225 LEU   C CB  1 
ATOM   6459 C  CG  . LEU   C 1 219 ? -6.713  -10.038 16.571  1.00 38.61  ? 225 LEU   C CG  1 
ATOM   6460 C  CD1 . LEU   C 1 219 ? -7.096  -11.067 17.642  1.00 38.60  ? 225 LEU   C CD1 1 
ATOM   6461 C  CD2 . LEU   C 1 219 ? -5.267  -10.262 16.105  1.00 42.40  ? 225 LEU   C CD2 1 
ATOM   6462 N  N   . GLY   C 1 220 ? -9.761  -9.118  13.224  1.00 29.81  ? 226 GLY   C N   1 
ATOM   6463 C  CA  . GLY   C 1 220 ? -10.620 -9.600  12.155  1.00 28.47  ? 226 GLY   C CA  1 
ATOM   6464 C  C   . GLY   C 1 220 ? -11.058 -11.011 12.506  1.00 31.26  ? 226 GLY   C C   1 
ATOM   6465 O  O   . GLY   C 1 220 ? -10.327 -11.741 13.186  1.00 29.15  ? 226 GLY   C O   1 
ATOM   6466 N  N   . ILE   C 1 221 ? -12.246 -11.418 12.029  1.00 27.02  ? 227 ILE   C N   1 
ATOM   6467 C  CA  . ILE   C 1 221 ? -12.782 -12.750 12.348  1.00 25.85  ? 227 ILE   C CA  1 
ATOM   6468 C  C   . ILE   C 1 221 ? -11.892 -13.944 11.849  1.00 30.58  ? 227 ILE   C C   1 
ATOM   6469 O  O   . ILE   C 1 221 ? -11.902 -14.986 12.506  1.00 29.45  ? 227 ILE   C O   1 
ATOM   6470 C  CB  . ILE   C 1 221 ? -14.276 -12.873 11.907  1.00 27.02  ? 227 ILE   C CB  1 
ATOM   6471 C  CG1 . ILE   C 1 221 ? -14.977 -14.000 12.676  1.00 26.58  ? 227 ILE   C CG1 1 
ATOM   6472 C  CG2 . ILE   C 1 221 ? -14.467 -12.973 10.396  1.00 25.98  ? 227 ILE   C CG2 1 
ATOM   6473 C  CD1 . ILE   C 1 221 ? -15.163 -13.732 14.238  1.00 26.19  ? 227 ILE   C CD1 1 
ATOM   6474 N  N   . GLN   C 1 222 ? -11.117 -13.797 10.744  1.00 29.74  ? 228 GLN   C N   1 
ATOM   6475 C  CA  . GLN   C 1 222 ? -10.263 -14.902 10.279  1.00 29.83  ? 228 GLN   C CA  1 
ATOM   6476 C  C   . GLN   C 1 222 ? -9.222  -15.216 11.331  1.00 32.45  ? 228 GLN   C C   1 
ATOM   6477 O  O   . GLN   C 1 222 ? -9.112  -16.369 11.716  1.00 32.00  ? 228 GLN   C O   1 
ATOM   6478 C  CB  . GLN   C 1 222 ? -9.608  -14.617 8.903   1.00 31.04  ? 228 GLN   C CB  1 
ATOM   6479 C  CG  . GLN   C 1 222 ? -8.561  -15.667 8.490   1.00 34.15  ? 228 GLN   C CG  1 
ATOM   6480 C  CD  . GLN   C 1 222 ? -7.685  -15.256 7.333   1.00 50.22  ? 228 GLN   C CD  1 
ATOM   6481 O  OE1 . GLN   C 1 222 ? -6.608  -15.809 7.119   1.00 49.59  ? 228 GLN   C OE1 1 
ATOM   6482 N  NE2 . GLN   C 1 222 ? -8.118  -14.298 6.542   1.00 38.85  ? 228 GLN   C NE2 1 
ATOM   6483 N  N   . LYS   C 1 223 ? -8.489  -14.194 11.812  1.00 27.56  ? 229 LYS   C N   1 
ATOM   6484 C  CA  . LYS   C 1 223 ? -7.453  -14.357 12.843  1.00 28.45  ? 229 LYS   C CA  1 
ATOM   6485 C  C   . LYS   C 1 223 ? -8.029  -14.827 14.178  1.00 30.39  ? 229 LYS   C C   1 
ATOM   6486 O  O   . LYS   C 1 223 ? -7.440  -15.687 14.837  1.00 28.76  ? 229 LYS   C O   1 
ATOM   6487 C  CB  . LYS   C 1 223 ? -6.632  -13.067 12.992  1.00 30.22  ? 229 LYS   C CB  1 
ATOM   6488 C  CG  . LYS   C 1 223 ? -5.534  -12.974 11.938  1.00 45.37  ? 229 LYS   C CG  1 
ATOM   6489 C  CD  . LYS   C 1 223 ? -4.646  -11.743 12.143  1.00 56.98  ? 229 LYS   C CD  1 
ATOM   6490 C  CE  . LYS   C 1 223 ? -3.797  -11.455 10.925  1.00 67.30  ? 229 LYS   C CE  1 
ATOM   6491 N  NZ  . LYS   C 1 223 ? -2.972  -10.233 11.105  1.00 77.80  ? 229 LYS   C NZ  1 
ATOM   6492 N  N   . VAL   C 1 224 ? -9.214  -14.315 14.540  1.00 27.04  ? 230 VAL   C N   1 
ATOM   6493 C  CA  . VAL   C 1 224 ? -9.939  -14.748 15.747  1.00 26.95  ? 230 VAL   C CA  1 
ATOM   6494 C  C   . VAL   C 1 224 ? -10.148 -16.288 15.720  1.00 30.19  ? 230 VAL   C C   1 
ATOM   6495 O  O   . VAL   C 1 224 ? -9.820  -16.949 16.713  1.00 30.39  ? 230 VAL   C O   1 
ATOM   6496 C  CB  . VAL   C 1 224 ? -11.276 -13.954 15.971  1.00 29.78  ? 230 VAL   C CB  1 
ATOM   6497 C  CG1 . VAL   C 1 224 ? -12.175 -14.646 16.997  1.00 29.02  ? 230 VAL   C CG1 1 
ATOM   6498 C  CG2 . VAL   C 1 224 ? -10.995 -12.503 16.397  1.00 29.49  ? 230 VAL   C CG2 1 
ATOM   6499 N  N   . MET   C 1 225 ? -10.646 -16.842 14.592  1.00 27.34  ? 231 MET   C N   1 
ATOM   6500 C  CA  . MET   C 1 225 ? -10.916 -18.291 14.433  1.00 25.82  ? 231 MET   C CA  1 
ATOM   6501 C  C   . MET   C 1 225 ? -9.619  -19.101 14.472  1.00 29.88  ? 231 MET   C C   1 
ATOM   6502 O  O   . MET   C 1 225 ? -9.565  -20.114 15.185  1.00 28.94  ? 231 MET   C O   1 
ATOM   6503 C  CB  . MET   C 1 225 ? -11.750 -18.597 13.170  1.00 26.87  ? 231 MET   C CB  1 
ATOM   6504 C  CG  . MET   C 1 225 ? -13.222 -18.135 13.264  1.00 27.85  ? 231 MET   C CG  1 
ATOM   6505 S  SD  . MET   C 1 225 ? -13.961 -18.286 14.921  1.00 29.06  ? 231 MET   C SD  1 
ATOM   6506 C  CE  . MET   C 1 225 ? -14.181 -20.090 15.046  1.00 27.20  ? 231 MET   C CE  1 
ATOM   6507 N  N   . GLU   C 1 226 ? -8.557  -18.598 13.794  1.00 28.36  ? 232 GLU   C N   1 
ATOM   6508 C  CA  . GLU   C 1 226 ? -7.217  -19.223 13.813  1.00 29.05  ? 232 GLU   C CA  1 
ATOM   6509 C  C   . GLU   C 1 226 ? -6.681  -19.287 15.226  1.00 31.40  ? 232 GLU   C C   1 
ATOM   6510 O  O   . GLU   C 1 226 ? -6.235  -20.353 15.634  1.00 31.57  ? 232 GLU   C O   1 
ATOM   6511 C  CB  . GLU   C 1 226 ? -6.199  -18.490 12.912  1.00 30.72  ? 232 GLU   C CB  1 
ATOM   6512 C  CG  . GLU   C 1 226 ? -6.507  -18.516 11.422  1.00 38.61  ? 232 GLU   C CG  1 
ATOM   6513 C  CD  . GLU   C 1 226 ? -5.676  -17.629 10.506  1.00 56.90  ? 232 GLU   C CD  1 
ATOM   6514 O  OE1 . GLU   C 1 226 ? -5.024  -16.674 10.993  1.00 40.63  ? 232 GLU   C OE1 1 
ATOM   6515 O  OE2 . GLU   C 1 226 ? -5.730  -17.862 9.277   1.00 53.00  ? 232 GLU   C OE2 1 
ATOM   6516 N  N   . ARG   C 1 227 ? -6.738  -18.159 15.986  1.00 27.94  ? 233 ARG   C N   1 
ATOM   6517 C  CA  . ARG   C 1 227 ? -6.263  -18.095 17.360  1.00 27.31  ? 233 ARG   C CA  1 
ATOM   6518 C  C   . ARG   C 1 227 ? -7.066  -18.994 18.270  1.00 31.60  ? 233 ARG   C C   1 
ATOM   6519 O  O   . ARG   C 1 227 ? -6.478  -19.698 19.087  1.00 30.71  ? 233 ARG   C O   1 
ATOM   6520 C  CB  . ARG   C 1 227 ? -6.194  -16.655 17.872  1.00 28.62  ? 233 ARG   C CB  1 
ATOM   6521 C  CG  . ARG   C 1 227 ? -4.955  -15.936 17.349  1.00 36.86  ? 233 ARG   C CG  1 
ATOM   6522 C  CD  . ARG   C 1 227 ? -5.109  -14.431 17.350  1.00 52.19  ? 233 ARG   C CD  1 
ATOM   6523 N  NE  . ARG   C 1 227 ? -3.974  -13.794 16.682  1.00 58.50  ? 233 ARG   C NE  1 
ATOM   6524 C  CZ  . ARG   C 1 227 ? -3.172  -12.901 17.248  1.00 71.60  ? 233 ARG   C CZ  1 
ATOM   6525 N  NH1 . ARG   C 1 227 ? -3.397  -12.491 18.491  1.00 60.25  ? 233 ARG   C NH1 1 
ATOM   6526 N  NH2 . ARG   C 1 227 ? -2.165  -12.379 16.564  1.00 58.91  ? 233 ARG   C NH2 1 
ATOM   6527 N  N   . THR   C 1 228 ? -8.416  -19.010 18.098  1.00 27.92  ? 234 THR   C N   1 
ATOM   6528 C  CA  . THR   C 1 228 ? -9.294  -19.903 18.860  1.00 26.90  ? 234 THR   C CA  1 
ATOM   6529 C  C   . THR   C 1 228 ? -8.877  -21.380 18.713  1.00 28.52  ? 234 THR   C C   1 
ATOM   6530 O  O   . THR   C 1 228 ? -8.757  -22.070 19.727  1.00 26.91  ? 234 THR   C O   1 
ATOM   6531 C  CB  . THR   C 1 228 ? -10.755 -19.693 18.435  1.00 28.64  ? 234 THR   C CB  1 
ATOM   6532 O  OG1 . THR   C 1 228 ? -11.108 -18.335 18.743  1.00 29.23  ? 234 THR   C OG1 1 
ATOM   6533 C  CG2 . THR   C 1 228 ? -11.698 -20.648 19.166  1.00 27.39  ? 234 THR   C CG2 1 
ATOM   6534 N  N   . PHE   C 1 229 ? -8.699  -21.862 17.468  1.00 28.99  ? 235 PHE   C N   1 
ATOM   6535 C  CA  . PHE   C 1 229 ? -8.301  -23.252 17.218  1.00 30.33  ? 235 PHE   C CA  1 
ATOM   6536 C  C   . PHE   C 1 229 ? -6.885  -23.528 17.695  1.00 34.37  ? 235 PHE   C C   1 
ATOM   6537 O  O   . PHE   C 1 229 ? -6.641  -24.614 18.207  1.00 34.84  ? 235 PHE   C O   1 
ATOM   6538 C  CB  . PHE   C 1 229 ? -8.506  -23.669 15.766  1.00 32.68  ? 235 PHE   C CB  1 
ATOM   6539 C  CG  . PHE   C 1 229 ? -9.922  -23.533 15.265  1.00 34.74  ? 235 PHE   C CG  1 
ATOM   6540 C  CD1 . PHE   C 1 229 ? -11.006 -23.837 16.091  1.00 37.35  ? 235 PHE   C CD1 1 
ATOM   6541 C  CD2 . PHE   C 1 229 ? -10.177 -23.127 13.958  1.00 36.10  ? 235 PHE   C CD2 1 
ATOM   6542 C  CE1 . PHE   C 1 229 ? -12.317 -23.697 15.628  1.00 37.93  ? 235 PHE   C CE1 1 
ATOM   6543 C  CE2 . PHE   C 1 229 ? -11.489 -23.011 13.490  1.00 38.48  ? 235 PHE   C CE2 1 
ATOM   6544 C  CZ  . PHE   C 1 229 ? -12.548 -23.289 14.331  1.00 36.56  ? 235 PHE   C CZ  1 
ATOM   6545 N  N   . ASP   C 1 230 ? -5.975  -22.536 17.614  1.00 31.60  ? 236 ASP   C N   1 
ATOM   6546 C  CA  . ASP   C 1 230 ? -4.614  -22.689 18.164  1.00 31.79  ? 236 ASP   C CA  1 
ATOM   6547 C  C   . ASP   C 1 230 ? -4.693  -22.976 19.660  1.00 33.93  ? 236 ASP   C C   1 
ATOM   6548 O  O   . ASP   C 1 230 ? -3.978  -23.839 20.147  1.00 33.24  ? 236 ASP   C O   1 
ATOM   6549 C  CB  . ASP   C 1 230 ? -3.752  -21.416 17.954  1.00 34.17  ? 236 ASP   C CB  1 
ATOM   6550 C  CG  . ASP   C 1 230 ? -3.355  -21.114 16.522  1.00 49.59  ? 236 ASP   C CG  1 
ATOM   6551 O  OD1 . ASP   C 1 230 ? -3.568  -21.988 15.646  1.00 51.14  ? 236 ASP   C OD1 1 
ATOM   6552 O  OD2 . ASP   C 1 230 ? -2.842  -19.994 16.272  1.00 56.42  ? 236 ASP   C OD2 1 
ATOM   6553 N  N   . LEU   C 1 231 ? -5.568  -22.270 20.390  1.00 30.59  ? 237 LEU   C N   1 
ATOM   6554 C  CA  . LEU   C 1 231 ? -5.717  -22.477 21.836  1.00 29.92  ? 237 LEU   C CA  1 
ATOM   6555 C  C   . LEU   C 1 231 ? -6.374  -23.819 22.208  1.00 32.08  ? 237 LEU   C C   1 
ATOM   6556 O  O   . LEU   C 1 231 ? -6.000  -24.447 23.203  1.00 32.15  ? 237 LEU   C O   1 
ATOM   6557 C  CB  . LEU   C 1 231 ? -6.520  -21.332 22.475  1.00 30.39  ? 237 LEU   C CB  1 
ATOM   6558 C  CG  . LEU   C 1 231 ? -5.906  -19.922 22.432  1.00 34.44  ? 237 LEU   C CG  1 
ATOM   6559 C  CD1 . LEU   C 1 231 ? -6.998  -18.878 22.605  1.00 33.55  ? 237 LEU   C CD1 1 
ATOM   6560 C  CD2 . LEU   C 1 231 ? -4.802  -19.744 23.483  1.00 37.81  ? 237 LEU   C CD2 1 
ATOM   6561 N  N   . LEU   C 1 232 ? -7.389  -24.217 21.448  1.00 27.24  ? 238 LEU   C N   1 
ATOM   6562 C  CA  . LEU   C 1 232 ? -8.193  -25.399 21.763  1.00 27.05  ? 238 LEU   C CA  1 
ATOM   6563 C  C   . LEU   C 1 232 ? -7.720  -26.698 21.136  1.00 29.14  ? 238 LEU   C C   1 
ATOM   6564 O  O   . LEU   C 1 232 ? -7.629  -27.698 21.846  1.00 28.61  ? 238 LEU   C O   1 
ATOM   6565 C  CB  . LEU   C 1 232 ? -9.658  -25.127 21.397  1.00 26.43  ? 238 LEU   C CB  1 
ATOM   6566 C  CG  . LEU   C 1 232 ? -10.340 -23.962 22.144  1.00 26.50  ? 238 LEU   C CG  1 
ATOM   6567 C  CD1 . LEU   C 1 232 ? -11.820 -23.871 21.723  1.00 26.05  ? 238 LEU   C CD1 1 
ATOM   6568 C  CD2 . LEU   C 1 232 ? -10.283 -24.181 23.689  1.00 26.09  ? 238 LEU   C CD2 1 
ATOM   6569 N  N   . ILE   C 1 233 ? -7.409  -26.689 19.835  1.00 26.41  ? 239 ILE   C N   1 
ATOM   6570 C  CA  . ILE   C 1 233 ? -7.012  -27.879 19.084  1.00 26.00  ? 239 ILE   C CA  1 
ATOM   6571 C  C   . ILE   C 1 233 ? -5.584  -27.786 18.480  1.00 31.45  ? 239 ILE   C C   1 
ATOM   6572 O  O   . ILE   C 1 233 ? -5.245  -28.543 17.560  1.00 31.87  ? 239 ILE   C O   1 
ATOM   6573 C  CB  . ILE   C 1 233 ? -8.077  -28.277 18.033  1.00 29.03  ? 239 ILE   C CB  1 
ATOM   6574 C  CG1 . ILE   C 1 233 ? -8.376  -27.114 17.038  1.00 29.45  ? 239 ILE   C CG1 1 
ATOM   6575 C  CG2 . ILE   C 1 233 ? -9.360  -28.805 18.739  1.00 27.65  ? 239 ILE   C CG2 1 
ATOM   6576 C  CD1 . ILE   C 1 233 ? -9.279  -27.459 15.836  1.00 31.69  ? 239 ILE   C CD1 1 
ATOM   6577 N  N   . GLY   C 1 234 ? -4.746  -26.935 19.067  1.00 29.78  ? 240 GLY   C N   1 
ATOM   6578 C  CA  . GLY   C 1 234 ? -3.358  -26.773 18.646  1.00 30.46  ? 240 GLY   C CA  1 
ATOM   6579 C  C   . GLY   C 1 234 ? -2.501  -27.989 18.957  1.00 36.34  ? 240 GLY   C C   1 
ATOM   6580 O  O   . GLY   C 1 234 ? -1.536  -28.270 18.241  1.00 38.16  ? 240 GLY   C O   1 
ATOM   6581 N  N   . LYS   C 1 235 ? -2.850  -28.728 20.018  1.00 31.55  ? 241 LYS   C N   1 
ATOM   6582 C  CA  . LYS   C 1 235 ? -2.104  -29.932 20.434  1.00 30.98  ? 241 LYS   C CA  1 
ATOM   6583 C  C   . LYS   C 1 235 ? -2.701  -31.244 19.933  1.00 32.87  ? 241 LYS   C C   1 
ATOM   6584 O  O   . LYS   C 1 235 ? -1.955  -32.192 19.690  1.00 31.35  ? 241 LYS   C O   1 
ATOM   6585 C  CB  . LYS   C 1 235 ? -1.937  -29.972 21.958  1.00 34.68  ? 241 LYS   C CB  1 
ATOM   6586 C  CG  . LYS   C 1 235 ? -0.942  -28.930 22.478  1.00 52.45  ? 241 LYS   C CG  1 
ATOM   6587 C  CD  . LYS   C 1 235 ? -0.973  -28.830 23.996  1.00 68.89  ? 241 LYS   C CD  1 
ATOM   6588 C  CE  . LYS   C 1 235 ? -0.005  -27.803 24.542  1.00 85.67  ? 241 LYS   C CE  1 
ATOM   6589 N  NZ  . LYS   C 1 235 ? 1.406   -28.275 24.482  1.00 100.81 ? 241 LYS   C NZ  1 
ATOM   6590 N  N   . ARG   C 1 236 ? -4.036  -31.328 19.826  1.00 27.26  ? 242 ARG   C N   1 
ATOM   6591 C  CA  . ARG   C 1 236 ? -4.717  -32.547 19.385  1.00 27.66  ? 242 ARG   C CA  1 
ATOM   6592 C  C   . ARG   C 1 236 ? -6.127  -32.226 18.952  1.00 31.94  ? 242 ARG   C C   1 
ATOM   6593 O  O   . ARG   C 1 236 ? -6.666  -31.206 19.370  1.00 29.29  ? 242 ARG   C O   1 
ATOM   6594 C  CB  . ARG   C 1 236 ? -4.776  -33.606 20.532  1.00 27.92  ? 242 ARG   C CB  1 
ATOM   6595 C  CG  . ARG   C 1 236 ? -5.605  -33.174 21.722  1.00 27.03  ? 242 ARG   C CG  1 
ATOM   6596 C  CD  . ARG   C 1 236 ? -5.537  -34.100 22.899  1.00 29.62  ? 242 ARG   C CD  1 
ATOM   6597 N  NE  . ARG   C 1 236 ? -6.189  -33.484 24.056  1.00 30.48  ? 242 ARG   C NE  1 
ATOM   6598 C  CZ  . ARG   C 1 236 ? -5.611  -32.602 24.863  1.00 42.03  ? 242 ARG   C CZ  1 
ATOM   6599 N  NH1 . ARG   C 1 236 ? -4.348  -32.241 24.668  1.00 38.40  ? 242 ARG   C NH1 1 
ATOM   6600 N  NH2 . ARG   C 1 236 ? -6.283  -32.087 25.878  1.00 30.70  ? 242 ARG   C NH2 1 
ATOM   6601 N  N   . GLN   C 1 237 ? -6.734  -33.132 18.170  1.00 31.43  ? 243 GLN   C N   1 
ATOM   6602 C  CA  . GLN   C 1 237 ? -8.133  -33.021 17.749  1.00 32.51  ? 243 GLN   C CA  1 
ATOM   6603 C  C   . GLN   C 1 237 ? -8.963  -33.335 18.980  1.00 33.85  ? 243 GLN   C C   1 
ATOM   6604 O  O   . GLN   C 1 237 ? -8.578  -34.194 19.785  1.00 32.13  ? 243 GLN   C O   1 
ATOM   6605 C  CB  . GLN   C 1 237 ? -8.456  -34.010 16.624  1.00 34.78  ? 243 GLN   C CB  1 
ATOM   6606 C  CG  . GLN   C 1 237 ? -7.862  -33.600 15.269  1.00 58.40  ? 243 GLN   C CG  1 
ATOM   6607 C  CD  . GLN   C 1 237 ? -8.504  -34.256 14.059  1.00 90.48  ? 243 GLN   C CD  1 
ATOM   6608 O  OE1 . GLN   C 1 237 ? -8.527  -33.682 12.961  1.00 86.72  ? 243 GLN   C OE1 1 
ATOM   6609 N  NE2 . GLN   C 1 237 ? -9.026  -35.473 14.215  1.00 87.77  ? 243 GLN   C NE2 1 
ATOM   6610 N  N   . ARG   C 1 238 ? -10.049 -32.574 19.186  1.00 29.15  ? 244 ARG   C N   1 
ATOM   6611 C  CA  . ARG   C 1 238 ? -10.909 -32.731 20.348  1.00 27.74  ? 244 ARG   C CA  1 
ATOM   6612 C  C   . ARG   C 1 238 ? -12.355 -32.518 19.895  1.00 29.09  ? 244 ARG   C C   1 
ATOM   6613 O  O   . ARG   C 1 238 ? -12.551 -31.737 18.974  1.00 27.13  ? 244 ARG   C O   1 
ATOM   6614 C  CB  . ARG   C 1 238 ? -10.588 -31.641 21.382  1.00 27.87  ? 244 ARG   C CB  1 
ATOM   6615 C  CG  . ARG   C 1 238 ? -9.176  -31.710 21.959  1.00 37.16  ? 244 ARG   C CG  1 
ATOM   6616 C  CD  . ARG   C 1 238 ? -8.894  -30.463 22.739  1.00 34.57  ? 244 ARG   C CD  1 
ATOM   6617 N  NE  . ARG   C 1 238 ? -9.472  -30.540 24.074  1.00 28.59  ? 244 ARG   C NE  1 
ATOM   6618 C  CZ  . ARG   C 1 238 ? -9.306  -29.628 25.010  1.00 31.50  ? 244 ARG   C CZ  1 
ATOM   6619 N  NH1 . ARG   C 1 238 ? -8.641  -28.509 24.744  1.00 30.16  ? 244 ARG   C NH1 1 
ATOM   6620 N  NH2 . ARG   C 1 238 ? -9.823  -29.806 26.213  1.00 30.92  ? 244 ARG   C NH2 1 
ATOM   6621 N  N   . PRO   C 1 239 ? -13.361 -33.134 20.562  1.00 26.35  ? 245 PRO   C N   1 
ATOM   6622 C  CA  . PRO   C 1 239 ? -14.772 -32.825 20.215  1.00 26.39  ? 245 PRO   C CA  1 
ATOM   6623 C  C   . PRO   C 1 239 ? -15.077 -31.359 20.547  1.00 26.90  ? 245 PRO   C C   1 
ATOM   6624 O  O   . PRO   C 1 239 ? -14.757 -30.890 21.633  1.00 27.09  ? 245 PRO   C O   1 
ATOM   6625 C  CB  . PRO   C 1 239 ? -15.595 -33.758 21.125  1.00 28.13  ? 245 PRO   C CB  1 
ATOM   6626 C  CG  . PRO   C 1 239 ? -14.629 -34.650 21.801  1.00 31.78  ? 245 PRO   C CG  1 
ATOM   6627 C  CD  . PRO   C 1 239 ? -13.269 -34.069 21.708  1.00 27.92  ? 245 PRO   C CD  1 
ATOM   6628 N  N   . ILE   C 1 240 ? -15.686 -30.639 19.621  1.00 24.63  ? 246 ILE   C N   1 
ATOM   6629 C  CA  . ILE   C 1 240 ? -15.993 -29.235 19.855  1.00 24.12  ? 246 ILE   C CA  1 
ATOM   6630 C  C   . ILE   C 1 240 ? -17.444 -29.117 20.241  1.00 27.35  ? 246 ILE   C C   1 
ATOM   6631 O  O   . ILE   C 1 240 ? -18.297 -29.701 19.574  1.00 25.69  ? 246 ILE   C O   1 
ATOM   6632 C  CB  . ILE   C 1 240 ? -15.675 -28.340 18.620  1.00 26.83  ? 246 ILE   C CB  1 
ATOM   6633 C  CG1 . ILE   C 1 240 ? -14.145 -28.224 18.397  1.00 28.62  ? 246 ILE   C CG1 1 
ATOM   6634 C  CG2 . ILE   C 1 240 ? -16.318 -26.908 18.748  1.00 24.84  ? 246 ILE   C CG2 1 
ATOM   6635 C  CD1 . ILE   C 1 240 ? -13.741 -27.677 16.907  1.00 34.31  ? 246 ILE   C CD1 1 
ATOM   6636 N  N   . HIS   C 1 241 ? -17.703 -28.315 21.276  1.00 25.15  ? 247 HIS   C N   1 
ATOM   6637 C  CA  . HIS   C 1 241 ? -19.032 -27.924 21.724  1.00 23.53  ? 247 HIS   C CA  1 
ATOM   6638 C  C   . HIS   C 1 241 ? -19.234 -26.425 21.373  1.00 27.97  ? 247 HIS   C C   1 
ATOM   6639 O  O   . HIS   C 1 241 ? -18.634 -25.540 22.003  1.00 26.55  ? 247 HIS   C O   1 
ATOM   6640 C  CB  . HIS   C 1 241 ? -19.219 -28.171 23.241  1.00 24.43  ? 247 HIS   C CB  1 
ATOM   6641 C  CG  . HIS   C 1 241 ? -20.643 -27.970 23.674  1.00 26.68  ? 247 HIS   C CG  1 
ATOM   6642 N  ND1 . HIS   C 1 241 ? -21.428 -29.036 24.080  1.00 27.94  ? 247 HIS   C ND1 1 
ATOM   6643 C  CD2 . HIS   C 1 241 ? -21.400 -26.844 23.679  1.00 28.01  ? 247 HIS   C CD2 1 
ATOM   6644 C  CE1 . HIS   C 1 241 ? -22.621 -28.524 24.345  1.00 27.10  ? 247 HIS   C CE1 1 
ATOM   6645 N  NE2 . HIS   C 1 241 ? -22.665 -27.218 24.095  1.00 27.46  ? 247 HIS   C NE2 1 
ATOM   6646 N  N   . LEU   C 1 242 ? -20.094 -26.133 20.401  1.00 24.02  ? 248 LEU   C N   1 
ATOM   6647 C  CA  . LEU   C 1 242 ? -20.342 -24.743 20.023  1.00 23.49  ? 248 LEU   C CA  1 
ATOM   6648 C  C   . LEU   C 1 242 ? -21.590 -24.248 20.732  1.00 27.21  ? 248 LEU   C C   1 
ATOM   6649 O  O   . LEU   C 1 242 ? -22.671 -24.735 20.433  1.00 24.88  ? 248 LEU   C O   1 
ATOM   6650 C  CB  . LEU   C 1 242 ? -20.481 -24.599 18.475  1.00 23.19  ? 248 LEU   C CB  1 
ATOM   6651 C  CG  . LEU   C 1 242 ? -20.772 -23.162 17.936  1.00 26.77  ? 248 LEU   C CG  1 
ATOM   6652 C  CD1 . LEU   C 1 242 ? -19.675 -22.163 18.320  1.00 26.57  ? 248 LEU   C CD1 1 
ATOM   6653 C  CD2 . LEU   C 1 242 ? -20.949 -23.143 16.406  1.00 24.89  ? 248 LEU   C CD2 1 
ATOM   6654 N  N   . SER   C 1 243 ? -21.433 -23.339 21.702  1.00 26.19  ? 249 SER   C N   1 
ATOM   6655 C  CA  . SER   C 1 243 ? -22.570 -22.782 22.460  1.00 25.82  ? 249 SER   C CA  1 
ATOM   6656 C  C   . SER   C 1 243 ? -22.865 -21.390 21.953  1.00 26.46  ? 249 SER   C C   1 
ATOM   6657 O  O   . SER   C 1 243 ? -22.178 -20.423 22.281  1.00 25.36  ? 249 SER   C O   1 
ATOM   6658 C  CB  . SER   C 1 243 ? -22.325 -22.839 23.959  1.00 26.75  ? 249 SER   C CB  1 
ATOM   6659 O  OG  . SER   C 1 243 ? -23.598 -22.828 24.580  1.00 29.47  ? 249 SER   C OG  1 
ATOM   6660 N  N   . PHE   C 1 244 ? -23.857 -21.299 21.051  1.00 25.45  ? 250 PHE   C N   1 
ATOM   6661 C  CA  . PHE   C 1 244 ? -24.118 -20.063 20.320  1.00 23.59  ? 250 PHE   C CA  1 
ATOM   6662 C  C   . PHE   C 1 244 ? -25.364 -19.344 20.791  1.00 28.15  ? 250 PHE   C C   1 
ATOM   6663 O  O   . PHE   C 1 244 ? -26.481 -19.808 20.551  1.00 26.45  ? 250 PHE   C O   1 
ATOM   6664 C  CB  . PHE   C 1 244 ? -24.216 -20.389 18.798  1.00 24.51  ? 250 PHE   C CB  1 
ATOM   6665 C  CG  . PHE   C 1 244 ? -23.898 -19.267 17.848  1.00 25.29  ? 250 PHE   C CG  1 
ATOM   6666 C  CD1 . PHE   C 1 244 ? -24.672 -18.111 17.823  1.00 29.92  ? 250 PHE   C CD1 1 
ATOM   6667 C  CD2 . PHE   C 1 244 ? -22.834 -19.368 16.956  1.00 28.23  ? 250 PHE   C CD2 1 
ATOM   6668 C  CE1 . PHE   C 1 244 ? -24.345 -17.052 16.965  1.00 30.38  ? 250 PHE   C CE1 1 
ATOM   6669 C  CE2 . PHE   C 1 244 ? -22.524 -18.318 16.089  1.00 29.80  ? 250 PHE   C CE2 1 
ATOM   6670 C  CZ  . PHE   C 1 244 ? -23.288 -17.173 16.091  1.00 28.86  ? 250 PHE   C CZ  1 
ATOM   6671 N  N   . ASP   C 1 245 ? -25.165 -18.182 21.401  1.00 25.08  ? 251 ASP   C N   1 
ATOM   6672 C  CA  . ASP   C 1 245 ? -26.264 -17.343 21.839  1.00 24.46  ? 251 ASP   C CA  1 
ATOM   6673 C  C   . ASP   C 1 245 ? -26.565 -16.396 20.695  1.00 28.80  ? 251 ASP   C C   1 
ATOM   6674 O  O   . ASP   C 1 245 ? -25.667 -15.687 20.224  1.00 27.90  ? 251 ASP   C O   1 
ATOM   6675 C  CB  . ASP   C 1 245 ? -25.874 -16.616 23.143  1.00 24.84  ? 251 ASP   C CB  1 
ATOM   6676 C  CG  . ASP   C 1 245 ? -26.948 -15.739 23.778  1.00 28.53  ? 251 ASP   C CG  1 
ATOM   6677 O  OD1 . ASP   C 1 245 ? -27.827 -15.257 23.046  1.00 27.83  ? 251 ASP   C OD1 1 
ATOM   6678 O  OD2 . ASP   C 1 245 ? -26.883 -15.516 25.011  1.00 33.13  ? 251 ASP   C OD2 1 
ATOM   6679 N  N   . ILE   C 1 246 ? -27.824 -16.400 20.202  1.00 26.12  ? 252 ILE   C N   1 
ATOM   6680 C  CA  . ILE   C 1 246 ? -28.187 -15.554 19.064  1.00 26.44  ? 252 ILE   C CA  1 
ATOM   6681 C  C   . ILE   C 1 246 ? -27.871 -14.050 19.301  1.00 29.81  ? 252 ILE   C C   1 
ATOM   6682 O  O   . ILE   C 1 246 ? -27.523 -13.358 18.341  1.00 29.78  ? 252 ILE   C O   1 
ATOM   6683 C  CB  . ILE   C 1 246 ? -29.669 -15.812 18.614  1.00 29.02  ? 252 ILE   C CB  1 
ATOM   6684 C  CG1 . ILE   C 1 246 ? -29.884 -15.443 17.116  1.00 28.98  ? 252 ILE   C CG1 1 
ATOM   6685 C  CG2 . ILE   C 1 246 ? -30.685 -15.140 19.542  1.00 29.81  ? 252 ILE   C CG2 1 
ATOM   6686 C  CD1 . ILE   C 1 246 ? -29.336 -16.424 16.107  1.00 30.35  ? 252 ILE   C CD1 1 
ATOM   6687 N  N   . ASP   C 1 247 ? -27.880 -13.577 20.577  1.00 27.16  ? 253 ASP   C N   1 
ATOM   6688 C  CA  . ASP   C 1 247 ? -27.579 -12.182 20.917  1.00 26.29  ? 253 ASP   C CA  1 
ATOM   6689 C  C   . ASP   C 1 247 ? -26.093 -11.809 20.675  1.00 30.04  ? 253 ASP   C C   1 
ATOM   6690 O  O   . ASP   C 1 247 ? -25.740 -10.651 20.840  1.00 30.67  ? 253 ASP   C O   1 
ATOM   6691 C  CB  . ASP   C 1 247 ? -28.062 -11.807 22.350  1.00 28.50  ? 253 ASP   C CB  1 
ATOM   6692 C  CG  . ASP   C 1 247 ? -27.275 -12.343 23.537  1.00 33.14  ? 253 ASP   C CG  1 
ATOM   6693 O  OD1 . ASP   C 1 247 ? -26.085 -12.686 23.362  1.00 31.45  ? 253 ASP   C OD1 1 
ATOM   6694 O  OD2 . ASP   C 1 247 ? -27.857 -12.438 24.643  1.00 36.68  ? 253 ASP   C OD2 1 
ATOM   6695 N  N   . ALA   C 1 248 ? -25.237 -12.769 20.245  1.00 27.87  ? 254 ALA   C N   1 
ATOM   6696 C  CA  . ALA   C 1 248 ? -23.857 -12.466 19.839  1.00 26.93  ? 254 ALA   C CA  1 
ATOM   6697 C  C   . ALA   C 1 248 ? -23.946 -11.554 18.585  1.00 30.31  ? 254 ALA   C C   1 
ATOM   6698 O  O   . ALA   C 1 248 ? -23.095 -10.692 18.388  1.00 29.54  ? 254 ALA   C O   1 
ATOM   6699 C  CB  . ALA   C 1 248 ? -23.126 -13.758 19.479  1.00 27.02  ? 254 ALA   C CB  1 
ATOM   6700 N  N   . PHE   C 1 249 ? -25.001 -11.739 17.758  1.00 28.01  ? 255 PHE   C N   1 
ATOM   6701 C  CA  . PHE   C 1 249 ? -25.235 -10.919 16.567  1.00 28.53  ? 255 PHE   C CA  1 
ATOM   6702 C  C   . PHE   C 1 249 ? -25.790 -9.576  16.957  1.00 29.94  ? 255 PHE   C C   1 
ATOM   6703 O  O   . PHE   C 1 249 ? -26.527 -9.476  17.942  1.00 28.55  ? 255 PHE   C O   1 
ATOM   6704 C  CB  . PHE   C 1 249 ? -26.269 -11.568 15.628  1.00 29.78  ? 255 PHE   C CB  1 
ATOM   6705 C  CG  . PHE   C 1 249 ? -25.770 -12.754 14.849  1.00 29.55  ? 255 PHE   C CG  1 
ATOM   6706 C  CD1 . PHE   C 1 249 ? -25.017 -12.578 13.695  1.00 31.30  ? 255 PHE   C CD1 1 
ATOM   6707 C  CD2 . PHE   C 1 249 ? -26.072 -14.048 15.256  1.00 31.21  ? 255 PHE   C CD2 1 
ATOM   6708 C  CE1 . PHE   C 1 249 ? -24.569 -13.668 12.961  1.00 31.91  ? 255 PHE   C CE1 1 
ATOM   6709 C  CE2 . PHE   C 1 249 ? -25.627 -15.144 14.516  1.00 34.15  ? 255 PHE   C CE2 1 
ATOM   6710 C  CZ  . PHE   C 1 249 ? -24.876 -14.944 13.371  1.00 31.61  ? 255 PHE   C CZ  1 
ATOM   6711 N  N   . ASP   C 1 250 ? -25.536 -8.572  16.112  1.00 28.41  ? 256 ASP   C N   1 
ATOM   6712 C  CA  . ASP   C 1 250 ? -26.070 -7.222  16.299  1.00 28.48  ? 256 ASP   C CA  1 
ATOM   6713 C  C   . ASP   C 1 250 ? -27.602 -7.266  16.361  1.00 34.44  ? 256 ASP   C C   1 
ATOM   6714 O  O   . ASP   C 1 250 ? -28.197 -7.971  15.552  1.00 33.63  ? 256 ASP   C O   1 
ATOM   6715 C  CB  . ASP   C 1 250 ? -25.653 -6.300  15.142  1.00 30.07  ? 256 ASP   C CB  1 
ATOM   6716 C  CG  . ASP   C 1 250 ? -25.913 -4.830  15.471  1.00 38.31  ? 256 ASP   C CG  1 
ATOM   6717 O  OD1 . ASP   C 1 250 ? -25.026 -4.192  16.071  1.00 38.16  ? 256 ASP   C OD1 1 
ATOM   6718 O  OD2 . ASP   C 1 250 ? -27.037 -4.356  15.213  1.00 38.90  ? 256 ASP   C OD2 1 
ATOM   6719 N  N   . PRO   C 1 251 ? -28.243 -6.499  17.284  1.00 33.18  ? 257 PRO   C N   1 
ATOM   6720 C  CA  . PRO   C 1 251 ? -29.727 -6.502  17.370  1.00 33.47  ? 257 PRO   C CA  1 
ATOM   6721 C  C   . PRO   C 1 251 ? -30.501 -6.248  16.070  1.00 37.42  ? 257 PRO   C C   1 
ATOM   6722 O  O   . PRO   C 1 251 ? -31.614 -6.761  15.946  1.00 38.65  ? 257 PRO   C O   1 
ATOM   6723 C  CB  . PRO   C 1 251 ? -30.018 -5.427  18.411  1.00 35.36  ? 257 PRO   C CB  1 
ATOM   6724 C  CG  . PRO   C 1 251 ? -28.789 -5.402  19.271  1.00 39.17  ? 257 PRO   C CG  1 
ATOM   6725 C  CD  . PRO   C 1 251 ? -27.648 -5.642  18.332  1.00 34.20  ? 257 PRO   C CD  1 
ATOM   6726 N  N   . THR   C 1 252 ? -29.936 -5.500  15.102  1.00 33.30  ? 258 THR   C N   1 
ATOM   6727 C  CA  . THR   C 1 252 ? -30.567 -5.261  13.792  1.00 33.09  ? 258 THR   C CA  1 
ATOM   6728 C  C   . THR   C 1 252 ? -30.759 -6.577  13.000  1.00 37.32  ? 258 THR   C C   1 
ATOM   6729 O  O   . THR   C 1 252 ? -31.691 -6.680  12.217  1.00 37.14  ? 258 THR   C O   1 
ATOM   6730 C  CB  . THR   C 1 252 ? -29.788 -4.229  12.960  1.00 43.83  ? 258 THR   C CB  1 
ATOM   6731 O  OG1 . THR   C 1 252 ? -28.455 -4.699  12.731  1.00 48.33  ? 258 THR   C OG1 1 
ATOM   6732 C  CG2 . THR   C 1 252 ? -29.758 -2.849  13.605  1.00 43.97  ? 258 THR   C CG2 1 
ATOM   6733 N  N   . LEU   C 1 253 ? -29.891 -7.587  13.236  1.00 34.02  ? 259 LEU   C N   1 
ATOM   6734 C  CA  . LEU   C 1 253 ? -29.911 -8.911  12.584  1.00 33.11  ? 259 LEU   C CA  1 
ATOM   6735 C  C   . LEU   C 1 253 ? -30.683 -9.949  13.396  1.00 35.21  ? 259 LEU   C C   1 
ATOM   6736 O  O   . LEU   C 1 253 ? -31.381 -10.792 12.823  1.00 34.99  ? 259 LEU   C O   1 
ATOM   6737 C  CB  . LEU   C 1 253 ? -28.452 -9.390  12.373  1.00 32.94  ? 259 LEU   C CB  1 
ATOM   6738 C  CG  . LEU   C 1 253 ? -27.539 -8.441  11.630  1.00 37.82  ? 259 LEU   C CG  1 
ATOM   6739 C  CD1 . LEU   C 1 253 ? -26.097 -8.790  11.868  1.00 37.33  ? 259 LEU   C CD1 1 
ATOM   6740 C  CD2 . LEU   C 1 253 ? -27.869 -8.409  10.127  1.00 40.86  ? 259 LEU   C CD2 1 
ATOM   6741 N  N   . ALA   C 1 254 ? -30.552 -9.889  14.737  1.00 32.34  ? 260 ALA   C N   1 
ATOM   6742 C  CA  . ALA   C 1 254 ? -31.216 -10.793 15.675  1.00 32.00  ? 260 ALA   C CA  1 
ATOM   6743 C  C   . ALA   C 1 254 ? -32.038 -9.997  16.708  1.00 37.35  ? 260 ALA   C C   1 
ATOM   6744 O  O   . ALA   C 1 254 ? -31.665 -9.917  17.894  1.00 36.85  ? 260 ALA   C O   1 
ATOM   6745 C  CB  . ALA   C 1 254 ? -30.181 -11.695 16.359  1.00 32.32  ? 260 ALA   C CB  1 
ATOM   6746 N  N   . PRO   C 1 255 ? -33.151 -9.351  16.266  1.00 34.05  ? 261 PRO   C N   1 
ATOM   6747 C  CA  . PRO   C 1 255 ? -33.936 -8.544  17.211  1.00 33.88  ? 261 PRO   C CA  1 
ATOM   6748 C  C   . PRO   C 1 255 ? -34.715 -9.316  18.269  1.00 39.17  ? 261 PRO   C C   1 
ATOM   6749 O  O   . PRO   C 1 255 ? -34.863 -8.818  19.381  1.00 39.09  ? 261 PRO   C O   1 
ATOM   6750 C  CB  . PRO   C 1 255 ? -34.870 -7.743  16.293  1.00 34.90  ? 261 PRO   C CB  1 
ATOM   6751 C  CG  . PRO   C 1 255 ? -35.036 -8.610  15.078  1.00 39.12  ? 261 PRO   C CG  1 
ATOM   6752 C  CD  . PRO   C 1 255 ? -33.712 -9.282  14.896  1.00 34.49  ? 261 PRO   C CD  1 
ATOM   6753 N  N   . ALA   C 1 256 ? -35.239 -10.499 17.926  1.00 36.76  ? 262 ALA   C N   1 
ATOM   6754 C  CA  . ALA   C 1 256 ? -36.097 -11.273 18.817  1.00 36.19  ? 262 ALA   C CA  1 
ATOM   6755 C  C   . ALA   C 1 256 ? -35.312 -12.076 19.874  1.00 39.66  ? 262 ALA   C C   1 
ATOM   6756 O  O   . ALA   C 1 256 ? -35.245 -13.303 19.809  1.00 39.51  ? 262 ALA   C O   1 
ATOM   6757 C  CB  . ALA   C 1 256 ? -37.034 -12.155 17.997  1.00 36.79  ? 262 ALA   C CB  1 
ATOM   6758 N  N   . THR   C 1 257 ? -34.704 -11.339 20.843  1.00 35.92  ? 263 THR   C N   1 
ATOM   6759 C  CA  . THR   C 1 257 ? -33.865 -11.837 21.943  1.00 34.55  ? 263 THR   C CA  1 
ATOM   6760 C  C   . THR   C 1 257 ? -34.041 -10.942 23.208  1.00 37.09  ? 263 THR   C C   1 
ATOM   6761 O  O   . THR   C 1 257 ? -34.315 -9.750  23.082  1.00 35.14  ? 263 THR   C O   1 
ATOM   6762 C  CB  . THR   C 1 257 ? -32.398 -12.018 21.453  1.00 33.36  ? 263 THR   C CB  1 
ATOM   6763 O  OG1 . THR   C 1 257 ? -31.744 -12.957 22.306  1.00 32.76  ? 263 THR   C OG1 1 
ATOM   6764 C  CG2 . THR   C 1 257 ? -31.599 -10.702 21.368  1.00 30.92  ? 263 THR   C CG2 1 
ATOM   6765 N  N   . GLY   C 1 258 ? -33.857 -11.530 24.384  1.00 34.32  ? 264 GLY   C N   1 
ATOM   6766 C  CA  . GLY   C 1 258 ? -34.067 -10.889 25.687  1.00 34.29  ? 264 GLY   C CA  1 
ATOM   6767 C  C   . GLY   C 1 258 ? -33.120 -9.787  26.097  1.00 39.09  ? 264 GLY   C C   1 
ATOM   6768 O  O   . GLY   C 1 258 ? -33.546 -8.764  26.649  1.00 39.04  ? 264 GLY   C O   1 
ATOM   6769 N  N   . THR   C 1 259 ? -31.822 -9.997  25.868  1.00 34.54  ? 265 THR   C N   1 
ATOM   6770 C  CA  . THR   C 1 259 ? -30.812 -9.020  26.262  1.00 34.36  ? 265 THR   C CA  1 
ATOM   6771 C  C   . THR   C 1 259 ? -30.018 -8.522  25.029  1.00 38.20  ? 265 THR   C C   1 
ATOM   6772 O  O   . THR   C 1 259 ? -28.819 -8.836  24.913  1.00 35.80  ? 265 THR   C O   1 
ATOM   6773 C  CB  . THR   C 1 259 ? -29.932 -9.582  27.409  1.00 47.27  ? 265 THR   C CB  1 
ATOM   6774 O  OG1 . THR   C 1 259 ? -29.269 -10.750 26.936  1.00 59.53  ? 265 THR   C OG1 1 
ATOM   6775 C  CG2 . THR   C 1 259 ? -30.726 -9.948  28.649  1.00 46.00  ? 265 THR   C CG2 1 
ATOM   6776 N  N   . PRO   C 1 260 ? -30.653 -7.749  24.091  1.00 35.92  ? 266 PRO   C N   1 
ATOM   6777 C  CA  . PRO   C 1 260 ? -29.894 -7.261  22.925  1.00 35.89  ? 266 PRO   C CA  1 
ATOM   6778 C  C   . PRO   C 1 260 ? -28.843 -6.252  23.351  1.00 39.55  ? 266 PRO   C C   1 
ATOM   6779 O  O   . PRO   C 1 260 ? -29.069 -5.497  24.302  1.00 40.25  ? 266 PRO   C O   1 
ATOM   6780 C  CB  . PRO   C 1 260 ? -30.966 -6.596  22.053  1.00 37.90  ? 266 PRO   C CB  1 
ATOM   6781 C  CG  . PRO   C 1 260 ? -32.055 -6.214  23.001  1.00 41.88  ? 266 PRO   C CG  1 
ATOM   6782 C  CD  . PRO   C 1 260 ? -32.055 -7.268  24.055  1.00 36.88  ? 266 PRO   C CD  1 
ATOM   6783 N  N   . VAL   C 1 261 ? -27.676 -6.283  22.701  1.00 34.45  ? 267 VAL   C N   1 
ATOM   6784 C  CA  . VAL   C 1 261 ? -26.580 -5.353  22.975  1.00 34.06  ? 267 VAL   C CA  1 
ATOM   6785 C  C   . VAL   C 1 261 ? -26.037 -4.879  21.616  1.00 37.79  ? 267 VAL   C C   1 
ATOM   6786 O  O   . VAL   C 1 261 ? -25.560 -5.699  20.832  1.00 36.71  ? 267 VAL   C O   1 
ATOM   6787 C  CB  . VAL   C 1 261 ? -25.442 -5.933  23.879  1.00 36.95  ? 267 VAL   C CB  1 
ATOM   6788 C  CG1 . VAL   C 1 261 ? -24.423 -4.852  24.222  1.00 36.36  ? 267 VAL   C CG1 1 
ATOM   6789 C  CG2 . VAL   C 1 261 ? -25.991 -6.571  25.163  1.00 36.90  ? 267 VAL   C CG2 1 
ATOM   6790 N  N   . VAL   C 1 262 ? -26.071 -3.556  21.372  1.00 34.80  ? 268 VAL   C N   1 
ATOM   6791 C  CA  . VAL   C 1 262 ? -25.595 -2.903  20.142  1.00 34.51  ? 268 VAL   C CA  1 
ATOM   6792 C  C   . VAL   C 1 262 ? -24.088 -3.177  19.906  1.00 34.32  ? 268 VAL   C C   1 
ATOM   6793 O  O   . VAL   C 1 262 ? -23.341 -3.364  20.867  1.00 31.70  ? 268 VAL   C O   1 
ATOM   6794 C  CB  . VAL   C 1 262 ? -25.934 -1.371  20.169  1.00 40.24  ? 268 VAL   C CB  1 
ATOM   6795 C  CG1 . VAL   C 1 262 ? -25.433 -0.649  18.923  1.00 41.05  ? 268 VAL   C CG1 1 
ATOM   6796 C  CG2 . VAL   C 1 262 ? -27.436 -1.152  20.296  1.00 40.27  ? 268 VAL   C CG2 1 
ATOM   6797 N  N   . GLY   C 1 263 ? -23.700 -3.199  18.628  1.00 29.98  ? 269 GLY   C N   1 
ATOM   6798 C  CA  . GLY   C 1 263 ? -22.336 -3.380  18.144  1.00 29.50  ? 269 GLY   C CA  1 
ATOM   6799 C  C   . GLY   C 1 263 ? -21.873 -4.813  18.126  1.00 31.37  ? 269 GLY   C C   1 
ATOM   6800 O  O   . GLY   C 1 263 ? -20.727 -5.078  18.455  1.00 30.01  ? 269 GLY   C O   1 
ATOM   6801 N  N   . GLY   C 1 264 ? -22.767 -5.725  17.756  1.00 28.60  ? 270 GLY   C N   1 
ATOM   6802 C  CA  . GLY   C 1 264 ? -22.467 -7.155  17.704  1.00 27.61  ? 270 GLY   C CA  1 
ATOM   6803 C  C   . GLY   C 1 264 ? -21.890 -7.648  16.401  1.00 29.36  ? 270 GLY   C C   1 
ATOM   6804 O  O   . GLY   C 1 264 ? -21.469 -6.852  15.551  1.00 27.66  ? 270 GLY   C O   1 
ATOM   6805 N  N   . LEU   C 1 265 ? -21.877 -8.980  16.241  1.00 27.48  ? 271 LEU   C N   1 
ATOM   6806 C  CA  . LEU   C 1 265 ? -21.394 -9.653  15.031  1.00 26.17  ? 271 LEU   C CA  1 
ATOM   6807 C  C   . LEU   C 1 265 ? -22.259 -9.302  13.859  1.00 29.71  ? 271 LEU   C C   1 
ATOM   6808 O  O   . LEU   C 1 265 ? -23.490 -9.231  13.973  1.00 28.73  ? 271 LEU   C O   1 
ATOM   6809 C  CB  . LEU   C 1 265 ? -21.460 -11.193 15.183  1.00 25.24  ? 271 LEU   C CB  1 
ATOM   6810 C  CG  . LEU   C 1 265 ? -20.617 -11.836 16.279  1.00 29.16  ? 271 LEU   C CG  1 
ATOM   6811 C  CD1 . LEU   C 1 265 ? -20.912 -13.315 16.374  1.00 28.97  ? 271 LEU   C CD1 1 
ATOM   6812 C  CD2 . LEU   C 1 265 ? -19.124 -11.624 16.029  1.00 30.66  ? 271 LEU   C CD2 1 
ATOM   6813 N  N   . THR   C 1 266 ? -21.630 -9.178  12.701  1.00 26.90  ? 272 THR   C N   1 
ATOM   6814 C  CA  . THR   C 1 266 ? -22.373 -9.019  11.459  1.00 27.11  ? 272 THR   C CA  1 
ATOM   6815 C  C   . THR   C 1 266 ? -22.769 -10.445 11.048  1.00 30.56  ? 272 THR   C C   1 
ATOM   6816 O  O   . THR   C 1 266 ? -22.176 -11.419 11.540  1.00 27.69  ? 272 THR   C O   1 
ATOM   6817 C  CB  . THR   C 1 266 ? -21.499 -8.399  10.377  1.00 31.02  ? 272 THR   C CB  1 
ATOM   6818 O  OG1 . THR   C 1 266 ? -20.456 -9.331  10.022  1.00 28.08  ? 272 THR   C OG1 1 
ATOM   6819 C  CG2 . THR   C 1 266 ? -20.960 -7.012  10.772  1.00 31.43  ? 272 THR   C CG2 1 
ATOM   6820 N  N   . TYR   C 1 267 ? -23.748 -10.566 10.137  1.00 27.69  ? 273 TYR   C N   1 
ATOM   6821 C  CA  . TYR   C 1 267 ? -24.174 -11.844 9.563   1.00 27.26  ? 273 TYR   C CA  1 
ATOM   6822 C  C   . TYR   C 1 267 ? -22.950 -12.594 9.011   1.00 29.03  ? 273 TYR   C C   1 
ATOM   6823 O  O   . TYR   C 1 267 ? -22.776 -13.776 9.276   1.00 27.97  ? 273 TYR   C O   1 
ATOM   6824 C  CB  . TYR   C 1 267 ? -25.173 -11.568 8.427   1.00 28.88  ? 273 TYR   C CB  1 
ATOM   6825 C  CG  . TYR   C 1 267 ? -25.652 -12.816 7.742   1.00 31.22  ? 273 TYR   C CG  1 
ATOM   6826 C  CD1 . TYR   C 1 267 ? -26.761 -13.512 8.217   1.00 32.81  ? 273 TYR   C CD1 1 
ATOM   6827 C  CD2 . TYR   C 1 267 ? -24.988 -13.321 6.624   1.00 31.47  ? 273 TYR   C CD2 1 
ATOM   6828 C  CE1 . TYR   C 1 267 ? -27.176 -14.696 7.616   1.00 33.27  ? 273 TYR   C CE1 1 
ATOM   6829 C  CE2 . TYR   C 1 267 ? -25.401 -14.500 6.012   1.00 32.25  ? 273 TYR   C CE2 1 
ATOM   6830 C  CZ  . TYR   C 1 267 ? -26.489 -15.187 6.515   1.00 35.67  ? 273 TYR   C CZ  1 
ATOM   6831 O  OH  . TYR   C 1 267 ? -26.915 -16.322 5.873   1.00 35.68  ? 273 TYR   C OH  1 
ATOM   6832 N  N   . ARG   C 1 268 ? -22.082 -11.878 8.275   1.00 26.59  ? 274 ARG   C N   1 
ATOM   6833 C  CA  . ARG   C 1 268 ? -20.890 -12.447 7.651   1.00 26.07  ? 274 ARG   C CA  1 
ATOM   6834 C  C   . ARG   C 1 268 ? -19.924 -13.046 8.657   1.00 28.83  ? 274 ARG   C C   1 
ATOM   6835 O  O   . ARG   C 1 268 ? -19.408 -14.139 8.413   1.00 27.09  ? 274 ARG   C O   1 
ATOM   6836 C  CB  . ARG   C 1 268 ? -20.226 -11.405 6.751   1.00 26.93  ? 274 ARG   C CB  1 
ATOM   6837 C  CG  . ARG   C 1 268 ? -21.061 -11.123 5.482   1.00 27.18  ? 274 ARG   C CG  1 
ATOM   6838 C  CD  . ARG   C 1 268 ? -20.813 -9.755  4.899   1.00 28.91  ? 274 ARG   C CD  1 
ATOM   6839 N  NE  . ARG   C 1 268 ? -19.392 -9.573  4.594   1.00 27.34  ? 274 ARG   C NE  1 
ATOM   6840 C  CZ  . ARG   C 1 268 ? -18.879 -8.467  4.077   1.00 38.17  ? 274 ARG   C CZ  1 
ATOM   6841 N  NH1 . ARG   C 1 268 ? -19.671 -7.467  3.721   1.00 30.05  ? 274 ARG   C NH1 1 
ATOM   6842 N  NH2 . ARG   C 1 268 ? -17.579 -8.378  3.849   1.00 25.86  ? 274 ARG   C NH2 1 
ATOM   6843 N  N   . GLU   C 1 269 ? -19.678 -12.348 9.783   1.00 25.71  ? 275 GLU   C N   1 
ATOM   6844 C  CA  . GLU   C 1 269 ? -18.786 -12.820 10.865  1.00 25.64  ? 275 GLU   C CA  1 
ATOM   6845 C  C   . GLU   C 1 269 ? -19.334 -14.077 11.535  1.00 27.93  ? 275 GLU   C C   1 
ATOM   6846 O  O   . GLU   C 1 269 ? -18.587 -15.014 11.783  1.00 25.99  ? 275 GLU   C O   1 
ATOM   6847 C  CB  . GLU   C 1 269 ? -18.575 -11.717 11.915  1.00 26.38  ? 275 GLU   C CB  1 
ATOM   6848 C  CG  . GLU   C 1 269 ? -17.636 -10.632 11.422  1.00 31.43  ? 275 GLU   C CG  1 
ATOM   6849 C  CD  . GLU   C 1 269 ? -17.573 -9.399  12.294  1.00 36.73  ? 275 GLU   C CD  1 
ATOM   6850 O  OE1 . GLU   C 1 269 ? -18.581 -9.110  12.974  1.00 33.38  ? 275 GLU   C OE1 1 
ATOM   6851 O  OE2 . GLU   C 1 269 ? -16.577 -8.649  12.188  1.00 30.80  ? 275 GLU   C OE2 1 
ATOM   6852 N  N   . GLY   C 1 270 ? -20.643 -14.097 11.773  1.00 25.66  ? 276 GLY   C N   1 
ATOM   6853 C  CA  . GLY   C 1 270 ? -21.340 -15.237 12.375  1.00 24.38  ? 276 GLY   C CA  1 
ATOM   6854 C  C   . GLY   C 1 270 ? -21.253 -16.463 11.502  1.00 26.86  ? 276 GLY   C C   1 
ATOM   6855 O  O   . GLY   C 1 270 ? -20.965 -17.556 11.992  1.00 27.50  ? 276 GLY   C O   1 
ATOM   6856 N  N   . MET   C 1 271 ? -21.457 -16.290 10.185  1.00 25.11  ? 277 MET   C N   1 
ATOM   6857 C  CA  . MET   C 1 271 ? -21.354 -17.400 9.220   1.00 24.41  ? 277 MET   C CA  1 
ATOM   6858 C  C   . MET   C 1 271 ? -19.913 -17.876 9.157   1.00 28.18  ? 277 MET   C C   1 
ATOM   6859 O  O   . MET   C 1 271 ? -19.662 -19.077 9.107   1.00 25.27  ? 277 MET   C O   1 
ATOM   6860 C  CB  . MET   C 1 271 ? -21.847 -16.991 7.810   1.00 26.62  ? 277 MET   C CB  1 
ATOM   6861 C  CG  . MET   C 1 271 ? -23.327 -16.688 7.730   1.00 29.90  ? 277 MET   C CG  1 
ATOM   6862 S  SD  . MET   C 1 271 ? -24.427 -18.013 8.310   1.00 34.30  ? 277 MET   C SD  1 
ATOM   6863 C  CE  . MET   C 1 271 ? -24.952 -17.341 9.841   1.00 30.67  ? 277 MET   C CE  1 
ATOM   6864 N  N   . TYR   C 1 272 ? -18.968 -16.938 9.221   1.00 26.44  ? 278 TYR   C N   1 
ATOM   6865 C  CA  . TYR   C 1 272 ? -17.553 -17.262 9.202   1.00 25.91  ? 278 TYR   C CA  1 
ATOM   6866 C  C   . TYR   C 1 272 ? -17.154 -18.180 10.383  1.00 27.14  ? 278 TYR   C C   1 
ATOM   6867 O  O   . TYR   C 1 272 ? -16.425 -19.160 10.178  1.00 26.43  ? 278 TYR   C O   1 
ATOM   6868 C  CB  . TYR   C 1 272 ? -16.691 -15.974 9.141   1.00 26.65  ? 278 TYR   C CB  1 
ATOM   6869 C  CG  . TYR   C 1 272 ? -15.253 -16.332 8.829   1.00 30.47  ? 278 TYR   C CG  1 
ATOM   6870 C  CD1 . TYR   C 1 272 ? -14.822 -16.478 7.516   1.00 33.40  ? 278 TYR   C CD1 1 
ATOM   6871 C  CD2 . TYR   C 1 272 ? -14.350 -16.622 9.847   1.00 31.75  ? 278 TYR   C CD2 1 
ATOM   6872 C  CE1 . TYR   C 1 272 ? -13.530 -16.911 7.223   1.00 35.91  ? 278 TYR   C CE1 1 
ATOM   6873 C  CE2 . TYR   C 1 272 ? -13.057 -17.051 9.566   1.00 32.90  ? 278 TYR   C CE2 1 
ATOM   6874 C  CZ  . TYR   C 1 272 ? -12.652 -17.197 8.253   1.00 39.88  ? 278 TYR   C CZ  1 
ATOM   6875 O  OH  . TYR   C 1 272 ? -11.372 -17.611 7.980   1.00 42.71  ? 278 TYR   C OH  1 
ATOM   6876 N  N   . ILE   C 1 273 ? -17.619 -17.848 11.620  1.00 23.53  ? 279 ILE   C N   1 
ATOM   6877 C  CA  . ILE   C 1 273 ? -17.395 -18.650 12.831  1.00 21.81  ? 279 ILE   C CA  1 
ATOM   6878 C  C   . ILE   C 1 273 ? -17.901 -20.079 12.575  1.00 26.85  ? 279 ILE   C C   1 
ATOM   6879 O  O   . ILE   C 1 273 ? -17.142 -21.032 12.728  1.00 25.06  ? 279 ILE   C O   1 
ATOM   6880 C  CB  . ILE   C 1 273 ? -18.102 -18.039 14.076  1.00 23.70  ? 279 ILE   C CB  1 
ATOM   6881 C  CG1 . ILE   C 1 273 ? -17.495 -16.681 14.446  1.00 24.04  ? 279 ILE   C CG1 1 
ATOM   6882 C  CG2 . ILE   C 1 273 ? -18.081 -19.036 15.296  1.00 23.15  ? 279 ILE   C CG2 1 
ATOM   6883 C  CD1 . ILE   C 1 273 ? -18.302 -15.891 15.448  1.00 24.39  ? 279 ILE   C CD1 1 
ATOM   6884 N  N   . ALA   C 1 274 ? -19.185 -20.214 12.187  1.00 24.27  ? 280 ALA   C N   1 
ATOM   6885 C  CA  . ALA   C 1 274 ? -19.829 -21.503 11.921  1.00 24.73  ? 280 ALA   C CA  1 
ATOM   6886 C  C   . ALA   C 1 274 ? -19.110 -22.310 10.820  1.00 25.73  ? 280 ALA   C C   1 
ATOM   6887 O  O   . ALA   C 1 274 ? -18.842 -23.501 11.010  1.00 22.72  ? 280 ALA   C O   1 
ATOM   6888 C  CB  . ALA   C 1 274 ? -21.294 -21.285 11.550  1.00 25.09  ? 280 ALA   C CB  1 
ATOM   6889 N  N   . GLU   C 1 275 ? -18.785 -21.663 9.678   1.00 24.53  ? 281 GLU   C N   1 
ATOM   6890 C  CA  . GLU   C 1 275 ? -18.068 -22.302 8.557   1.00 25.22  ? 281 GLU   C CA  1 
ATOM   6891 C  C   . GLU   C 1 275 ? -16.711 -22.831 9.049   1.00 27.91  ? 281 GLU   C C   1 
ATOM   6892 O  O   . GLU   C 1 275 ? -16.343 -23.937 8.685   1.00 27.32  ? 281 GLU   C O   1 
ATOM   6893 C  CB  . GLU   C 1 275 ? -17.820 -21.296 7.421   1.00 26.45  ? 281 GLU   C CB  1 
ATOM   6894 C  CG  . GLU   C 1 275 ? -19.065 -20.924 6.637   1.00 30.05  ? 281 GLU   C CG  1 
ATOM   6895 C  CD  . GLU   C 1 275 ? -18.919 -19.752 5.683   1.00 41.77  ? 281 GLU   C CD  1 
ATOM   6896 O  OE1 . GLU   C 1 275 ? -17.879 -19.056 5.706   1.00 29.60  ? 281 GLU   C OE1 1 
ATOM   6897 O  OE2 . GLU   C 1 275 ? -19.879 -19.511 4.923   1.00 33.62  ? 281 GLU   C OE2 1 
ATOM   6898 N  N   . GLU   C 1 276 ? -15.971 -22.039 9.857   1.00 26.91  ? 282 GLU   C N   1 
ATOM   6899 C  CA  . GLU   C 1 276 ? -14.670 -22.490 10.393  1.00 26.67  ? 282 GLU   C CA  1 
ATOM   6900 C  C   . GLU   C 1 276 ? -14.799 -23.700 11.318  1.00 31.11  ? 282 GLU   C C   1 
ATOM   6901 O  O   . GLU   C 1 276 ? -13.954 -24.611 11.252  1.00 29.03  ? 282 GLU   C O   1 
ATOM   6902 C  CB  . GLU   C 1 276 ? -13.890 -21.354 11.053  1.00 27.24  ? 282 GLU   C CB  1 
ATOM   6903 C  CG  . GLU   C 1 276 ? -13.250 -20.427 10.035  1.00 33.47  ? 282 GLU   C CG  1 
ATOM   6904 C  CD  . GLU   C 1 276 ? -12.470 -21.105 8.921   1.00 40.01  ? 282 GLU   C CD  1 
ATOM   6905 O  OE1 . GLU   C 1 276 ? -11.437 -21.751 9.201   1.00 40.02  ? 282 GLU   C OE1 1 
ATOM   6906 O  OE2 . GLU   C 1 276 ? -12.944 -21.047 7.769   1.00 36.11  ? 282 GLU   C OE2 1 
ATOM   6907 N  N   . ILE   C 1 277 ? -15.870 -23.723 12.152  1.00 28.60  ? 283 ILE   C N   1 
ATOM   6908 C  CA  . ILE   C 1 277 ? -16.188 -24.829 13.072  1.00 27.83  ? 283 ILE   C CA  1 
ATOM   6909 C  C   . ILE   C 1 277 ? -16.435 -26.100 12.206  1.00 29.29  ? 283 ILE   C C   1 
ATOM   6910 O  O   . ILE   C 1 277 ? -15.882 -27.173 12.485  1.00 26.10  ? 283 ILE   C O   1 
ATOM   6911 C  CB  . ILE   C 1 277 ? -17.424 -24.495 13.960  1.00 31.44  ? 283 ILE   C CB  1 
ATOM   6912 C  CG1 . ILE   C 1 277 ? -17.156 -23.324 14.989  1.00 33.06  ? 283 ILE   C CG1 1 
ATOM   6913 C  CG2 . ILE   C 1 277 ? -17.971 -25.750 14.653  1.00 31.87  ? 283 ILE   C CG2 1 
ATOM   6914 C  CD1 . ILE   C 1 277 ? -16.231 -23.569 16.204  1.00 43.65  ? 283 ILE   C CD1 1 
ATOM   6915 N  N   . HIS   C 1 278 ? -17.252 -25.945 11.146  1.00 26.38  ? 284 HIS   C N   1 
ATOM   6916 C  CA  . HIS   C 1 278 ? -17.542 -27.036 10.217  1.00 26.28  ? 284 HIS   C CA  1 
ATOM   6917 C  C   . HIS   C 1 278 ? -16.259 -27.568 9.599   1.00 30.95  ? 284 HIS   C C   1 
ATOM   6918 O  O   . HIS   C 1 278 ? -16.064 -28.776 9.602   1.00 29.42  ? 284 HIS   C O   1 
ATOM   6919 C  CB  . HIS   C 1 278 ? -18.524 -26.643 9.112   1.00 27.28  ? 284 HIS   C CB  1 
ATOM   6920 C  CG  . HIS   C 1 278 ? -18.639 -27.735 8.078   1.00 31.79  ? 284 HIS   C CG  1 
ATOM   6921 N  ND1 . HIS   C 1 278 ? -19.296 -28.926 8.357   1.00 33.96  ? 284 HIS   C ND1 1 
ATOM   6922 C  CD2 . HIS   C 1 278 ? -18.083 -27.826 6.848   1.00 33.55  ? 284 HIS   C CD2 1 
ATOM   6923 C  CE1 . HIS   C 1 278 ? -19.141 -29.684 7.286   1.00 33.18  ? 284 HIS   C CE1 1 
ATOM   6924 N  NE2 . HIS   C 1 278 ? -18.444 -29.058 6.342   1.00 33.47  ? 284 HIS   C NE2 1 
ATOM   6925 N  N   . ASN   C 1 279 ? -15.370 -26.670 9.117   1.00 28.37  ? 285 ASN   C N   1 
ATOM   6926 C  CA  . ASN   C 1 279 ? -14.105 -27.049 8.471   1.00 28.24  ? 285 ASN   C CA  1 
ATOM   6927 C  C   . ASN   C 1 279 ? -13.185 -27.921 9.313   1.00 31.82  ? 285 ASN   C C   1 
ATOM   6928 O  O   . ASN   C 1 279 ? -12.372 -28.643 8.733   1.00 32.03  ? 285 ASN   C O   1 
ATOM   6929 C  CB  . ASN   C 1 279 ? -13.355 -25.804 7.987   1.00 30.42  ? 285 ASN   C CB  1 
ATOM   6930 C  CG  . ASN   C 1 279 ? -14.000 -25.108 6.804   1.00 52.29  ? 285 ASN   C CG  1 
ATOM   6931 O  OD1 . ASN   C 1 279 ? -14.848 -25.673 6.101   1.00 45.32  ? 285 ASN   C OD1 1 
ATOM   6932 N  ND2 . ASN   C 1 279 ? -13.601 -23.852 6.553   1.00 41.21  ? 285 ASN   C ND2 1 
ATOM   6933 N  N   . THR   C 1 280 ? -13.270 -27.844 10.668  1.00 28.58  ? 286 THR   C N   1 
ATOM   6934 C  CA  . THR   C 1 280 ? -12.441 -28.685 11.551  1.00 28.58  ? 286 THR   C CA  1 
ATOM   6935 C  C   . THR   C 1 280 ? -12.842 -30.153 11.441  1.00 32.22  ? 286 THR   C C   1 
ATOM   6936 O  O   . THR   C 1 280 ? -12.030 -31.044 11.708  1.00 31.44  ? 286 THR   C O   1 
ATOM   6937 C  CB  . THR   C 1 280 ? -12.542 -28.277 13.044  1.00 33.39  ? 286 THR   C CB  1 
ATOM   6938 O  OG1 . THR   C 1 280 ? -13.852 -28.557 13.560  1.00 27.19  ? 286 THR   C OG1 1 
ATOM   6939 C  CG2 . THR   C 1 280 ? -12.128 -26.836 13.311  1.00 30.38  ? 286 THR   C CG2 1 
ATOM   6940 N  N   . GLY   C 1 281 ? -14.119 -30.382 11.146  1.00 29.45  ? 287 GLY   C N   1 
ATOM   6941 C  CA  . GLY   C 1 281 ? -14.724 -31.708 11.137  1.00 29.38  ? 287 GLY   C CA  1 
ATOM   6942 C  C   . GLY   C 1 281 ? -14.882 -32.276 12.543  1.00 30.91  ? 287 GLY   C C   1 
ATOM   6943 O  O   . GLY   C 1 281 ? -15.146 -33.466 12.683  1.00 30.45  ? 287 GLY   C O   1 
ATOM   6944 N  N   . LEU   C 1 282 ? -14.747 -31.436 13.601  1.00 25.15  ? 288 LEU   C N   1 
ATOM   6945 C  CA  . LEU   C 1 282 ? -14.781 -31.885 15.002  1.00 24.13  ? 288 LEU   C CA  1 
ATOM   6946 C  C   . LEU   C 1 282 ? -16.023 -31.528 15.792  1.00 26.32  ? 288 LEU   C C   1 
ATOM   6947 O  O   . LEU   C 1 282 ? -16.102 -31.864 16.986  1.00 26.72  ? 288 LEU   C O   1 
ATOM   6948 C  CB  . LEU   C 1 282 ? -13.542 -31.348 15.743  1.00 24.40  ? 288 LEU   C CB  1 
ATOM   6949 C  CG  . LEU   C 1 282 ? -12.184 -31.833 15.215  1.00 29.16  ? 288 LEU   C CG  1 
ATOM   6950 C  CD1 . LEU   C 1 282 ? -11.045 -31.021 15.809  1.00 29.01  ? 288 LEU   C CD1 1 
ATOM   6951 C  CD2 . LEU   C 1 282 ? -11.997 -33.324 15.423  1.00 32.59  ? 288 LEU   C CD2 1 
ATOM   6952 N  N   . LEU   C 1 283 ? -16.979 -30.813 15.158  1.00 24.71  ? 289 LEU   C N   1 
ATOM   6953 C  CA  . LEU   C 1 283 ? -18.182 -30.382 15.858  1.00 24.57  ? 289 LEU   C CA  1 
ATOM   6954 C  C   . LEU   C 1 283 ? -18.924 -31.597 16.363  1.00 27.53  ? 289 LEU   C C   1 
ATOM   6955 O  O   . LEU   C 1 283 ? -19.202 -32.507 15.580  1.00 29.36  ? 289 LEU   C O   1 
ATOM   6956 C  CB  . LEU   C 1 283 ? -19.068 -29.493 14.985  1.00 23.90  ? 289 LEU   C CB  1 
ATOM   6957 C  CG  . LEU   C 1 283 ? -20.382 -28.973 15.642  1.00 27.64  ? 289 LEU   C CG  1 
ATOM   6958 C  CD1 . LEU   C 1 283 ? -20.100 -28.018 16.814  1.00 27.91  ? 289 LEU   C CD1 1 
ATOM   6959 C  CD2 . LEU   C 1 283 ? -21.248 -28.270 14.612  1.00 24.71  ? 289 LEU   C CD2 1 
ATOM   6960 N  N   . SER   C 1 284 ? -19.149 -31.641 17.684  1.00 23.62  ? 290 SER   C N   1 
ATOM   6961 C  CA  . SER   C 1 284 ? -19.774 -32.768 18.368  1.00 24.77  ? 290 SER   C CA  1 
ATOM   6962 C  C   . SER   C 1 284 ? -21.134 -32.403 19.007  1.00 30.32  ? 290 SER   C C   1 
ATOM   6963 O  O   . SER   C 1 284 ? -21.978 -33.274 19.177  1.00 29.79  ? 290 SER   C O   1 
ATOM   6964 C  CB  . SER   C 1 284 ? -18.808 -33.342 19.392  1.00 25.03  ? 290 SER   C CB  1 
ATOM   6965 O  OG  . SER   C 1 284 ? -19.332 -34.490 20.032  1.00 29.64  ? 290 SER   C OG  1 
ATOM   6966 N  N   . ALA   C 1 285 ? -21.310 -31.140 19.392  1.00 26.84  ? 291 ALA   C N   1 
ATOM   6967 C  CA  . ALA   C 1 285 ? -22.578 -30.619 19.946  1.00 25.34  ? 291 ALA   C CA  1 
ATOM   6968 C  C   . ALA   C 1 285 ? -22.682 -29.143 19.679  1.00 26.37  ? 291 ALA   C C   1 
ATOM   6969 O  O   . ALA   C 1 285 ? -21.674 -28.434 19.648  1.00 25.71  ? 291 ALA   C O   1 
ATOM   6970 C  CB  . ALA   C 1 285 ? -22.710 -30.922 21.447  1.00 25.78  ? 291 ALA   C CB  1 
ATOM   6971 N  N   . LEU   C 1 286 ? -23.901 -28.650 19.510  1.00 22.25  ? 292 LEU   C N   1 
ATOM   6972 C  CA  . LEU   C 1 286 ? -24.129 -27.257 19.221  1.00 22.21  ? 292 LEU   C CA  1 
ATOM   6973 C  C   . LEU   C 1 286 ? -25.384 -26.816 19.960  1.00 28.24  ? 292 LEU   C C   1 
ATOM   6974 O  O   . LEU   C 1 286 ? -26.389 -27.541 19.934  1.00 26.91  ? 292 LEU   C O   1 
ATOM   6975 C  CB  . LEU   C 1 286 ? -24.328 -27.089 17.690  1.00 22.95  ? 292 LEU   C CB  1 
ATOM   6976 C  CG  . LEU   C 1 286 ? -24.571 -25.681 17.133  1.00 28.54  ? 292 LEU   C CG  1 
ATOM   6977 C  CD1 . LEU   C 1 286 ? -24.244 -25.642 15.683  1.00 30.46  ? 292 LEU   C CD1 1 
ATOM   6978 C  CD2 . LEU   C 1 286 ? -26.042 -25.293 17.215  1.00 29.81  ? 292 LEU   C CD2 1 
ATOM   6979 N  N   . ASP   C 1 287 ? -25.312 -25.649 20.624  1.00 25.05  ? 293 ASP   C N   1 
ATOM   6980 C  CA  . ASP   C 1 287 ? -26.482 -25.038 21.258  1.00 24.21  ? 293 ASP   C CA  1 
ATOM   6981 C  C   . ASP   C 1 287 ? -26.824 -23.802 20.481  1.00 27.27  ? 293 ASP   C C   1 
ATOM   6982 O  O   . ASP   C 1 287 ? -25.934 -23.003 20.163  1.00 26.64  ? 293 ASP   C O   1 
ATOM   6983 C  CB  . ASP   C 1 287 ? -26.201 -24.600 22.709  1.00 24.63  ? 293 ASP   C CB  1 
ATOM   6984 C  CG  . ASP   C 1 287 ? -25.575 -25.645 23.579  1.00 29.71  ? 293 ASP   C CG  1 
ATOM   6985 O  OD1 . ASP   C 1 287 ? -26.013 -26.795 23.513  1.00 29.22  ? 293 ASP   C OD1 1 
ATOM   6986 O  OD2 . ASP   C 1 287 ? -24.653 -25.300 24.340  1.00 36.26  ? 293 ASP   C OD2 1 
ATOM   6987 N  N   . LEU   C 1 288 ? -28.116 -23.588 20.225  1.00 24.65  ? 294 LEU   C N   1 
ATOM   6988 C  CA  . LEU   C 1 288 ? -28.553 -22.364 19.563  1.00 24.69  ? 294 LEU   C CA  1 
ATOM   6989 C  C   . LEU   C 1 288 ? -29.654 -21.844 20.478  1.00 29.28  ? 294 LEU   C C   1 
ATOM   6990 O  O   . LEU   C 1 288 ? -30.739 -22.428 20.545  1.00 28.22  ? 294 LEU   C O   1 
ATOM   6991 C  CB  . LEU   C 1 288 ? -29.057 -22.602 18.114  1.00 24.20  ? 294 LEU   C CB  1 
ATOM   6992 C  CG  . LEU   C 1 288 ? -29.116 -21.329 17.218  1.00 27.95  ? 294 LEU   C CG  1 
ATOM   6993 C  CD1 . LEU   C 1 288 ? -30.019 -20.222 17.813  1.00 28.62  ? 294 LEU   C CD1 1 
ATOM   6994 C  CD2 . LEU   C 1 288 ? -27.717 -20.736 16.990  1.00 29.42  ? 294 LEU   C CD2 1 
ATOM   6995 N  N   . VAL   C 1 289 ? -29.330 -20.784 21.230  1.00 27.62  ? 295 VAL   C N   1 
ATOM   6996 C  CA  . VAL   C 1 289 ? -30.176 -20.309 22.317  1.00 27.42  ? 295 VAL   C CA  1 
ATOM   6997 C  C   . VAL   C 1 289 ? -30.578 -18.856 22.204  1.00 31.24  ? 295 VAL   C C   1 
ATOM   6998 O  O   . VAL   C 1 289 ? -30.030 -18.112 21.387  1.00 28.80  ? 295 VAL   C O   1 
ATOM   6999 C  CB  . VAL   C 1 289 ? -29.520 -20.592 23.724  1.00 29.16  ? 295 VAL   C CB  1 
ATOM   7000 C  CG1 . VAL   C 1 289 ? -29.192 -22.073 23.915  1.00 28.56  ? 295 VAL   C CG1 1 
ATOM   7001 C  CG2 . VAL   C 1 289 ? -28.267 -19.743 23.935  1.00 28.66  ? 295 VAL   C CG2 1 
ATOM   7002 N  N   . GLU   C 1 290 ? -31.549 -18.463 23.074  1.00 31.65  ? 296 GLU   C N   1 
ATOM   7003 C  CA  . GLU   C 1 290 ? -32.039 -17.104 23.319  1.00 31.69  ? 296 GLU   C CA  1 
ATOM   7004 C  C   . GLU   C 1 290 ? -32.871 -16.489 22.169  1.00 36.70  ? 296 GLU   C C   1 
ATOM   7005 O  O   . GLU   C 1 290 ? -33.089 -15.275 22.159  1.00 36.63  ? 296 GLU   C O   1 
ATOM   7006 C  CB  . GLU   C 1 290 ? -30.878 -16.166 23.747  1.00 33.01  ? 296 GLU   C CB  1 
ATOM   7007 C  CG  . GLU   C 1 290 ? -30.209 -16.562 25.070  1.00 34.45  ? 296 GLU   C CG  1 
ATOM   7008 C  CD  . GLU   C 1 290 ? -31.033 -16.377 26.342  1.00 42.96  ? 296 GLU   C CD  1 
ATOM   7009 O  OE1 . GLU   C 1 290 ? -32.156 -15.829 26.261  1.00 40.00  ? 296 GLU   C OE1 1 
ATOM   7010 O  OE2 . GLU   C 1 290 ? -30.548 -16.757 27.429  1.00 31.42  ? 296 GLU   C OE2 1 
ATOM   7011 N  N   . VAL   C 1 291 ? -33.394 -17.327 21.252  1.00 32.45  ? 297 VAL   C N   1 
ATOM   7012 C  CA  . VAL   C 1 291 ? -34.334 -16.883 20.218  1.00 31.95  ? 297 VAL   C CA  1 
ATOM   7013 C  C   . VAL   C 1 291 ? -35.686 -16.805 20.965  1.00 37.54  ? 297 VAL   C C   1 
ATOM   7014 O  O   . VAL   C 1 291 ? -36.186 -17.822 21.440  1.00 36.08  ? 297 VAL   C O   1 
ATOM   7015 C  CB  . VAL   C 1 291 ? -34.435 -17.822 18.983  1.00 34.72  ? 297 VAL   C CB  1 
ATOM   7016 C  CG1 . VAL   C 1 291 ? -35.625 -17.437 18.081  1.00 33.87  ? 297 VAL   C CG1 1 
ATOM   7017 C  CG2 . VAL   C 1 291 ? -33.127 -17.856 18.193  1.00 33.59  ? 297 VAL   C CG2 1 
ATOM   7018 N  N   . ASN   C 1 292 ? -36.239 -15.594 21.076  1.00 36.56  ? 298 ASN   C N   1 
ATOM   7019 C  CA  . ASN   C 1 292 ? -37.505 -15.332 21.759  1.00 36.32  ? 298 ASN   C CA  1 
ATOM   7020 C  C   . ASN   C 1 292 ? -38.451 -14.640 20.758  1.00 39.71  ? 298 ASN   C C   1 
ATOM   7021 O  O   . ASN   C 1 292 ? -38.375 -13.425 20.588  1.00 37.46  ? 298 ASN   C O   1 
ATOM   7022 C  CB  . ASN   C 1 292 ? -37.263 -14.484 23.030  1.00 37.15  ? 298 ASN   C CB  1 
ATOM   7023 C  CG  . ASN   C 1 292 ? -38.495 -14.243 23.889  1.00 52.70  ? 298 ASN   C CG  1 
ATOM   7024 O  OD1 . ASN   C 1 292 ? -39.635 -14.252 23.421  1.00 43.30  ? 298 ASN   C OD1 1 
ATOM   7025 N  ND2 . ASN   C 1 292 ? -38.289 -13.979 25.164  1.00 46.99  ? 298 ASN   C ND2 1 
ATOM   7026 N  N   . PRO   C 1 293 ? -39.315 -15.422 20.057  1.00 38.44  ? 299 PRO   C N   1 
ATOM   7027 C  CA  . PRO   C 1 293 ? -40.199 -14.816 19.039  1.00 39.79  ? 299 PRO   C CA  1 
ATOM   7028 C  C   . PRO   C 1 293 ? -41.200 -13.783 19.564  1.00 47.38  ? 299 PRO   C C   1 
ATOM   7029 O  O   . PRO   C 1 293 ? -41.602 -12.909 18.794  1.00 47.56  ? 299 PRO   C O   1 
ATOM   7030 C  CB  . PRO   C 1 293 ? -40.883 -16.012 18.376  1.00 40.96  ? 299 PRO   C CB  1 
ATOM   7031 C  CG  . PRO   C 1 293 ? -40.688 -17.142 19.288  1.00 44.81  ? 299 PRO   C CG  1 
ATOM   7032 C  CD  . PRO   C 1 293 ? -39.481 -16.887 20.125  1.00 39.75  ? 299 PRO   C CD  1 
ATOM   7033 N  N   . GLN   C 1 294 ? -41.557 -13.845 20.861  1.00 46.98  ? 300 GLN   C N   1 
ATOM   7034 C  CA  . GLN   C 1 294 ? -42.476 -12.893 21.519  1.00 48.32  ? 300 GLN   C CA  1 
ATOM   7035 C  C   . GLN   C 1 294 ? -41.919 -11.467 21.630  1.00 53.48  ? 300 GLN   C C   1 
ATOM   7036 O  O   . GLN   C 1 294 ? -42.698 -10.510 21.661  1.00 53.14  ? 300 GLN   C O   1 
ATOM   7037 C  CB  . GLN   C 1 294 ? -42.840 -13.379 22.927  1.00 50.05  ? 300 GLN   C CB  1 
ATOM   7038 C  CG  . GLN   C 1 294 ? -44.052 -14.300 22.975  1.00 70.33  ? 300 GLN   C CG  1 
ATOM   7039 C  CD  . GLN   C 1 294 ? -44.532 -14.536 24.390  1.00 86.87  ? 300 GLN   C CD  1 
ATOM   7040 O  OE1 . GLN   C 1 294 ? -44.647 -13.608 25.207  1.00 81.52  ? 300 GLN   C OE1 1 
ATOM   7041 N  NE2 . GLN   C 1 294 ? -44.853 -15.788 24.700  1.00 76.47  ? 300 GLN   C NE2 1 
ATOM   7042 N  N   . LEU   C 1 295 ? -40.586 -11.324 21.718  1.00 50.93  ? 301 LEU   C N   1 
ATOM   7043 C  CA  . LEU   C 1 295 ? -39.943 -10.017 21.892  1.00 51.24  ? 301 LEU   C CA  1 
ATOM   7044 C  C   . LEU   C 1 295 ? -39.752 -9.226  20.599  1.00 57.00  ? 301 LEU   C C   1 
ATOM   7045 O  O   . LEU   C 1 295 ? -39.320 -8.069  20.647  1.00 57.68  ? 301 LEU   C O   1 
ATOM   7046 C  CB  . LEU   C 1 295 ? -38.620 -10.151 22.647  1.00 51.02  ? 301 LEU   C CB  1 
ATOM   7047 C  CG  . LEU   C 1 295 ? -38.688 -10.675 24.075  1.00 54.96  ? 301 LEU   C CG  1 
ATOM   7048 C  CD1 . LEU   C 1 295 ? -37.321 -10.718 24.667  1.00 54.96  ? 301 LEU   C CD1 1 
ATOM   7049 C  CD2 . LEU   C 1 295 ? -39.590 -9.820  24.965  1.00 56.02  ? 301 LEU   C CD2 1 
ATOM   7050 N  N   . ALA   C 1 296 ? -40.097 -9.829  19.456  1.00 53.85  ? 302 ALA   C N   1 
ATOM   7051 C  CA  . ALA   C 1 296 ? -40.017 -9.175  18.159  1.00 54.11  ? 302 ALA   C CA  1 
ATOM   7052 C  C   . ALA   C 1 296 ? -41.177 -8.168  18.037  1.00 60.47  ? 302 ALA   C C   1 
ATOM   7053 O  O   . ALA   C 1 296 ? -42.329 -8.517  18.320  1.00 60.02  ? 302 ALA   C O   1 
ATOM   7054 C  CB  . ALA   C 1 296 ? -40.121 -10.212 17.066  1.00 54.64  ? 302 ALA   C CB  1 
ATOM   7055 N  N   . THR   C 1 297 ? -40.869 -6.933  17.616  1.00 58.92  ? 303 THR   C N   1 
ATOM   7056 C  CA  . THR   C 1 297 ? -41.863 -5.859  17.449  1.00 59.75  ? 303 THR   C CA  1 
ATOM   7057 C  C   . THR   C 1 297 ? -42.864 -6.157  16.317  1.00 65.67  ? 303 THR   C C   1 
ATOM   7058 O  O   . THR   C 1 297 ? -43.980 -5.627  16.332  1.00 66.14  ? 303 THR   C O   1 
ATOM   7059 C  CB  . THR   C 1 297 ? -41.190 -4.480  17.289  1.00 66.35  ? 303 THR   C CB  1 
ATOM   7060 O  OG1 . THR   C 1 297 ? -40.395 -4.457  16.104  1.00 66.39  ? 303 THR   C OG1 1 
ATOM   7061 C  CG2 . THR   C 1 297 ? -40.361 -4.070  18.505  1.00 64.37  ? 303 THR   C CG2 1 
ATOM   7062 N  N   . SER   C 1 298 ? -42.459 -7.003  15.348  1.00 62.69  ? 304 SER   C N   1 
ATOM   7063 C  CA  . SER   C 1 298 ? -43.258 -7.424  14.198  1.00 63.00  ? 304 SER   C CA  1 
ATOM   7064 C  C   . SER   C 1 298 ? -43.002 -8.899  13.860  1.00 69.03  ? 304 SER   C C   1 
ATOM   7065 O  O   . SER   C 1 298 ? -41.990 -9.458  14.297  1.00 69.16  ? 304 SER   C O   1 
ATOM   7066 C  CB  . SER   C 1 298 ? -42.956 -6.544  12.990  1.00 65.99  ? 304 SER   C CB  1 
ATOM   7067 O  OG  . SER   C 1 298 ? -41.595 -6.636  12.604  1.00 75.15  ? 304 SER   C OG  1 
ATOM   7068 N  N   . GLU   C 1 299 ? -43.913 -9.527  13.072  1.00 66.02  ? 305 GLU   C N   1 
ATOM   7069 C  CA  . GLU   C 1 299 ? -43.809 -10.929 12.639  1.00 65.65  ? 305 GLU   C CA  1 
ATOM   7070 C  C   . GLU   C 1 299 ? -42.543 -11.168 11.803  1.00 67.84  ? 305 GLU   C C   1 
ATOM   7071 O  O   . GLU   C 1 299 ? -41.938 -12.240 11.907  1.00 67.56  ? 305 GLU   C O   1 
ATOM   7072 C  CB  . GLU   C 1 299 ? -45.063 -11.355 11.854  1.00 67.33  ? 305 GLU   C CB  1 
ATOM   7073 C  CG  . GLU   C 1 299 ? -45.336 -12.851 11.906  1.00 80.49  ? 305 GLU   C CG  1 
ATOM   7074 C  CD  . GLU   C 1 299 ? -46.551 -13.317 11.124  1.00 106.16 ? 305 GLU   C CD  1 
ATOM   7075 O  OE1 . GLU   C 1 299 ? -47.584 -13.625 11.762  1.00 96.68  ? 305 GLU   C OE1 1 
ATOM   7076 O  OE2 . GLU   C 1 299 ? -46.464 -13.396 9.877   1.00 103.18 ? 305 GLU   C OE2 1 
ATOM   7077 N  N   . GLU   C 1 300 ? -42.137 -10.159 11.001  1.00 62.60  ? 306 GLU   C N   1 
ATOM   7078 C  CA  . GLU   C 1 300 ? -40.936 -10.226 10.172  1.00 61.80  ? 306 GLU   C CA  1 
ATOM   7079 C  C   . GLU   C 1 300 ? -39.642 -10.198 11.014  1.00 61.11  ? 306 GLU   C C   1 
ATOM   7080 O  O   . GLU   C 1 300 ? -38.665 -10.832 10.617  1.00 60.70  ? 306 GLU   C O   1 
ATOM   7081 C  CB  . GLU   C 1 300 ? -40.936 -9.167  9.046   1.00 63.64  ? 306 GLU   C CB  1 
ATOM   7082 C  CG  . GLU   C 1 300 ? -40.805 -7.711  9.473   1.00 77.78  ? 306 GLU   C CG  1 
ATOM   7083 C  CD  . GLU   C 1 300 ? -39.753 -6.912  8.722   1.00 107.14 ? 306 GLU   C CD  1 
ATOM   7084 O  OE1 . GLU   C 1 300 ? -39.623 -7.095  7.490   1.00 102.31 ? 306 GLU   C OE1 1 
ATOM   7085 O  OE2 . GLU   C 1 300 ? -39.073 -6.082  9.367   1.00 108.02 ? 306 GLU   C OE2 1 
ATOM   7086 N  N   . GLU   C 1 301 ? -39.649 -9.499  12.172  1.00 53.58  ? 307 GLU   C N   1 
ATOM   7087 C  CA  . GLU   C 1 301 ? -38.516 -9.432  13.103  1.00 51.80  ? 307 GLU   C CA  1 
ATOM   7088 C  C   . GLU   C 1 301 ? -38.275 -10.821 13.743  1.00 52.54  ? 307 GLU   C C   1 
ATOM   7089 O  O   . GLU   C 1 301 ? -37.121 -11.221 13.925  1.00 51.05  ? 307 GLU   C O   1 
ATOM   7090 C  CB  . GLU   C 1 301 ? -38.759 -8.377  14.201  1.00 53.34  ? 307 GLU   C CB  1 
ATOM   7091 C  CG  . GLU   C 1 301 ? -38.224 -6.983  13.891  1.00 64.82  ? 307 GLU   C CG  1 
ATOM   7092 C  CD  . GLU   C 1 301 ? -37.874 -6.092  15.078  1.00 86.41  ? 307 GLU   C CD  1 
ATOM   7093 O  OE1 . GLU   C 1 301 ? -38.149 -6.475  16.240  1.00 69.35  ? 307 GLU   C OE1 1 
ATOM   7094 O  OE2 . GLU   C 1 301 ? -37.316 -4.996  14.841  1.00 87.84  ? 307 GLU   C OE2 1 
ATOM   7095 N  N   . ALA   C 1 302 ? -39.362 -11.556 14.071  1.00 48.05  ? 308 ALA   C N   1 
ATOM   7096 C  CA  . ALA   C 1 302 ? -39.280 -12.897 14.660  1.00 47.56  ? 308 ALA   C CA  1 
ATOM   7097 C  C   . ALA   C 1 302 ? -38.745 -13.886 13.625  1.00 50.01  ? 308 ALA   C C   1 
ATOM   7098 O  O   . ALA   C 1 302 ? -37.908 -14.733 13.964  1.00 49.36  ? 308 ALA   C O   1 
ATOM   7099 C  CB  . ALA   C 1 302 ? -40.648 -13.346 15.157  1.00 48.40  ? 308 ALA   C CB  1 
ATOM   7100 N  N   . LYS   C 1 303 ? -39.212 -13.751 12.358  1.00 45.55  ? 309 LYS   C N   1 
ATOM   7101 C  CA  . LYS   C 1 303 ? -38.801 -14.592 11.232  1.00 44.53  ? 309 LYS   C CA  1 
ATOM   7102 C  C   . LYS   C 1 303 ? -37.350 -14.341 10.854  1.00 45.08  ? 309 LYS   C C   1 
ATOM   7103 O  O   . LYS   C 1 303 ? -36.625 -15.309 10.676  1.00 44.37  ? 309 LYS   C O   1 
ATOM   7104 C  CB  . LYS   C 1 303 ? -39.761 -14.478 10.035  1.00 46.93  ? 309 LYS   C CB  1 
ATOM   7105 C  CG  . LYS   C 1 303 ? -41.089 -15.198 10.284  1.00 67.72  ? 309 LYS   C CG  1 
ATOM   7106 C  CD  . LYS   C 1 303 ? -42.086 -15.060 9.131   1.00 79.07  ? 309 LYS   C CD  1 
ATOM   7107 C  CE  . LYS   C 1 303 ? -43.401 -15.744 9.439   1.00 86.44  ? 309 LYS   C CE  1 
ATOM   7108 N  NZ  . LYS   C 1 303 ? -44.175 -16.044 8.202   1.00 94.47  ? 309 LYS   C NZ  1 
ATOM   7109 N  N   . THR   C 1 304 ? -36.907 -13.064 10.827  1.00 39.72  ? 310 THR   C N   1 
ATOM   7110 C  CA  . THR   C 1 304 ? -35.517 -12.681 10.553  1.00 39.02  ? 310 THR   C CA  1 
ATOM   7111 C  C   . THR   C 1 304 ? -34.570 -13.414 11.539  1.00 39.27  ? 310 THR   C C   1 
ATOM   7112 O  O   . THR   C 1 304 ? -33.593 -14.015 11.095  1.00 37.43  ? 310 THR   C O   1 
ATOM   7113 C  CB  . THR   C 1 304 ? -35.353 -11.148 10.616  1.00 48.90  ? 310 THR   C CB  1 
ATOM   7114 O  OG1 . THR   C 1 304 ? -36.155 -10.556 9.598   1.00 54.89  ? 310 THR   C OG1 1 
ATOM   7115 C  CG2 . THR   C 1 304 ? -33.905 -10.693 10.431  1.00 46.60  ? 310 THR   C CG2 1 
ATOM   7116 N  N   . THR   C 1 305 ? -34.868 -13.344 12.858  1.00 34.48  ? 311 THR   C N   1 
ATOM   7117 C  CA  . THR   C 1 305 ? -34.088 -13.999 13.927  1.00 33.48  ? 311 THR   C CA  1 
ATOM   7118 C  C   . THR   C 1 305 ? -34.092 -15.510 13.747  1.00 35.44  ? 311 THR   C C   1 
ATOM   7119 O  O   . THR   C 1 305 ? -33.021 -16.117 13.795  1.00 34.35  ? 311 THR   C O   1 
ATOM   7120 C  CB  . THR   C 1 305 ? -34.592 -13.612 15.331  1.00 39.33  ? 311 THR   C CB  1 
ATOM   7121 O  OG1 . THR   C 1 305 ? -34.961 -12.233 15.361  1.00 40.05  ? 311 THR   C OG1 1 
ATOM   7122 C  CG2 . THR   C 1 305 ? -33.563 -13.915 16.430  1.00 34.14  ? 311 THR   C CG2 1 
ATOM   7123 N  N   . ALA   C 1 306 ? -35.289 -16.128 13.546  1.00 31.38  ? 312 ALA   C N   1 
ATOM   7124 C  CA  . ALA   C 1 306 ? -35.389 -17.566 13.327  1.00 31.61  ? 312 ALA   C CA  1 
ATOM   7125 C  C   . ALA   C 1 306 ? -34.640 -18.008 12.063  1.00 33.94  ? 312 ALA   C C   1 
ATOM   7126 O  O   . ALA   C 1 306 ? -33.974 -19.034 12.105  1.00 32.48  ? 312 ALA   C O   1 
ATOM   7127 C  CB  . ALA   C 1 306 ? -36.847 -18.012 13.290  1.00 32.75  ? 312 ALA   C CB  1 
ATOM   7128 N  N   . ASN   C 1 307 ? -34.662 -17.199 10.978  1.00 33.09  ? 313 ASN   C N   1 
ATOM   7129 C  CA  . ASN   C 1 307 ? -33.930 -17.517 9.738   1.00 33.26  ? 313 ASN   C CA  1 
ATOM   7130 C  C   . ASN   C 1 307 ? -32.430 -17.474 9.979   1.00 35.06  ? 313 ASN   C C   1 
ATOM   7131 O  O   . ASN   C 1 307 ? -31.704 -18.314 9.456   1.00 33.26  ? 313 ASN   C O   1 
ATOM   7132 C  CB  . ASN   C 1 307 ? -34.302 -16.581 8.592   1.00 36.59  ? 313 ASN   C CB  1 
ATOM   7133 C  CG  . ASN   C 1 307 ? -35.665 -16.863 8.011   1.00 52.82  ? 313 ASN   C CG  1 
ATOM   7134 O  OD1 . ASN   C 1 307 ? -36.140 -18.006 7.973   1.00 50.20  ? 313 ASN   C OD1 1 
ATOM   7135 N  ND2 . ASN   C 1 307 ? -36.306 -15.825 7.520   1.00 47.85  ? 313 ASN   C ND2 1 
ATOM   7136 N  N   . LEU   C 1 308 ? -31.991 -16.502 10.794  1.00 32.21  ? 314 LEU   C N   1 
ATOM   7137 C  CA  . LEU   C 1 308 ? -30.594 -16.333 11.192  1.00 30.86  ? 314 LEU   C CA  1 
ATOM   7138 C  C   . LEU   C 1 308 ? -30.104 -17.556 11.991  1.00 31.34  ? 314 LEU   C C   1 
ATOM   7139 O  O   . LEU   C 1 308 ? -29.015 -18.063 11.709  1.00 30.16  ? 314 LEU   C O   1 
ATOM   7140 C  CB  . LEU   C 1 308 ? -30.414 -15.026 11.984  1.00 30.15  ? 314 LEU   C CB  1 
ATOM   7141 C  CG  . LEU   C 1 308 ? -29.008 -14.716 12.452  1.00 34.41  ? 314 LEU   C CG  1 
ATOM   7142 C  CD1 . LEU   C 1 308 ? -28.034 -14.615 11.265  1.00 35.45  ? 314 LEU   C CD1 1 
ATOM   7143 C  CD2 . LEU   C 1 308 ? -28.987 -13.446 13.263  1.00 35.82  ? 314 LEU   C CD2 1 
ATOM   7144 N  N   . ALA   C 1 309 ? -30.923 -18.042 12.945  1.00 28.00  ? 315 ALA   C N   1 
ATOM   7145 C  CA  . ALA   C 1 309 ? -30.645 -19.233 13.775  1.00 28.02  ? 315 ALA   C CA  1 
ATOM   7146 C  C   . ALA   C 1 309 ? -30.451 -20.468 12.879  1.00 32.35  ? 315 ALA   C C   1 
ATOM   7147 O  O   . ALA   C 1 309 ? -29.511 -21.226 13.099  1.00 32.40  ? 315 ALA   C O   1 
ATOM   7148 C  CB  . ALA   C 1 309 ? -31.783 -19.473 14.745  1.00 28.41  ? 315 ALA   C CB  1 
ATOM   7149 N  N   . VAL   C 1 310 ? -31.297 -20.632 11.838  1.00 28.74  ? 316 VAL   C N   1 
ATOM   7150 C  CA  . VAL   C 1 310 ? -31.188 -21.738 10.862  1.00 27.83  ? 316 VAL   C CA  1 
ATOM   7151 C  C   . VAL   C 1 310 ? -29.866 -21.639 10.071  1.00 29.90  ? 316 VAL   C C   1 
ATOM   7152 O  O   . VAL   C 1 310 ? -29.182 -22.655 9.908   1.00 29.78  ? 316 VAL   C O   1 
ATOM   7153 C  CB  . VAL   C 1 310 ? -32.426 -21.837 9.927   1.00 31.28  ? 316 VAL   C CB  1 
ATOM   7154 C  CG1 . VAL   C 1 310 ? -32.178 -22.825 8.780   1.00 30.50  ? 316 VAL   C CG1 1 
ATOM   7155 C  CG2 . VAL   C 1 310 ? -33.655 -22.254 10.724  1.00 31.20  ? 316 VAL   C CG2 1 
ATOM   7156 N  N   . ASP   C 1 311 ? -29.504 -20.430 9.622   1.00 26.51  ? 317 ASP   C N   1 
ATOM   7157 C  CA  . ASP   C 1 311 ? -28.258 -20.199 8.886   1.00 26.93  ? 317 ASP   C CA  1 
ATOM   7158 C  C   . ASP   C 1 311 ? -27.020 -20.568 9.704   1.00 29.95  ? 317 ASP   C C   1 
ATOM   7159 O  O   . ASP   C 1 311 ? -26.094 -21.177 9.158   1.00 28.03  ? 317 ASP   C O   1 
ATOM   7160 C  CB  . ASP   C 1 311 ? -28.162 -18.768 8.365   1.00 28.95  ? 317 ASP   C CB  1 
ATOM   7161 C  CG  . ASP   C 1 311 ? -29.118 -18.412 7.239   1.00 39.14  ? 317 ASP   C CG  1 
ATOM   7162 O  OD1 . ASP   C 1 311 ? -29.763 -19.332 6.685   1.00 37.67  ? 317 ASP   C OD1 1 
ATOM   7163 O  OD2 . ASP   C 1 311 ? -29.228 -17.219 6.920   1.00 48.85  ? 317 ASP   C OD2 1 
ATOM   7164 N  N   . VAL   C 1 312 ? -26.999 -20.204 11.002  1.00 27.83  ? 318 VAL   C N   1 
ATOM   7165 C  CA  . VAL   C 1 312 ? -25.887 -20.576 11.906  1.00 26.22  ? 318 VAL   C CA  1 
ATOM   7166 C  C   . VAL   C 1 312 ? -25.801 -22.090 11.973  1.00 27.32  ? 318 VAL   C C   1 
ATOM   7167 O  O   . VAL   C 1 312 ? -24.707 -22.633 11.856  1.00 26.03  ? 318 VAL   C O   1 
ATOM   7168 C  CB  . VAL   C 1 312 ? -26.040 -19.977 13.349  1.00 28.94  ? 318 VAL   C CB  1 
ATOM   7169 C  CG1 . VAL   C 1 312 ? -25.029 -20.582 14.328  1.00 27.07  ? 318 VAL   C CG1 1 
ATOM   7170 C  CG2 . VAL   C 1 312 ? -25.915 -18.476 13.334  1.00 29.67  ? 318 VAL   C CG2 1 
ATOM   7171 N  N   . ILE   C 1 313 ? -26.936 -22.785 12.240  1.00 23.95  ? 319 ILE   C N   1 
ATOM   7172 C  CA  . ILE   C 1 313 ? -26.932 -24.245 12.402  1.00 24.50  ? 319 ILE   C CA  1 
ATOM   7173 C  C   . ILE   C 1 313 ? -26.513 -24.941 11.096  1.00 27.14  ? 319 ILE   C C   1 
ATOM   7174 O  O   . ILE   C 1 313 ? -25.614 -25.790 11.142  1.00 24.87  ? 319 ILE   C O   1 
ATOM   7175 C  CB  . ILE   C 1 313 ? -28.256 -24.826 13.002  1.00 27.47  ? 319 ILE   C CB  1 
ATOM   7176 C  CG1 . ILE   C 1 313 ? -28.587 -24.191 14.396  1.00 27.99  ? 319 ILE   C CG1 1 
ATOM   7177 C  CG2 . ILE   C 1 313 ? -28.155 -26.340 13.144  1.00 28.62  ? 319 ILE   C CG2 1 
ATOM   7178 C  CD1 . ILE   C 1 313 ? -30.080 -24.192 14.770  1.00 30.20  ? 319 ILE   C CD1 1 
ATOM   7179 N  N   . ALA   C 1 314 ? -27.104 -24.543 9.951   1.00 25.42  ? 320 ALA   C N   1 
ATOM   7180 C  CA  . ALA   C 1 314 ? -26.766 -25.097 8.619   1.00 26.38  ? 320 ALA   C CA  1 
ATOM   7181 C  C   . ALA   C 1 314 ? -25.282 -24.886 8.289   1.00 29.09  ? 320 ALA   C C   1 
ATOM   7182 O  O   . ALA   C 1 314 ? -24.623 -25.814 7.816   1.00 27.11  ? 320 ALA   C O   1 
ATOM   7183 C  CB  . ALA   C 1 314 ? -27.611 -24.441 7.547   1.00 27.75  ? 320 ALA   C CB  1 
ATOM   7184 N  N   . SER   C 1 315 ? -24.765 -23.669 8.531   1.00 25.83  ? 321 SER   C N   1 
ATOM   7185 C  CA  . SER   C 1 315 ? -23.352 -23.355 8.277   1.00 24.49  ? 321 SER   C CA  1 
ATOM   7186 C  C   . SER   C 1 315 ? -22.432 -24.193 9.149   1.00 27.82  ? 321 SER   C C   1 
ATOM   7187 O  O   . SER   C 1 315 ? -21.343 -24.549 8.708   1.00 29.33  ? 321 SER   C O   1 
ATOM   7188 C  CB  . SER   C 1 315 ? -23.076 -21.873 8.508   1.00 28.62  ? 321 SER   C CB  1 
ATOM   7189 O  OG  . SER   C 1 315 ? -23.769 -21.099 7.542   1.00 40.09  ? 321 SER   C OG  1 
ATOM   7190 N  N   . SER   C 1 316 ? -22.875 -24.556 10.369  1.00 25.23  ? 322 SER   C N   1 
ATOM   7191 C  CA  . SER   C 1 316 ? -22.079 -25.376 11.261  1.00 25.33  ? 322 SER   C CA  1 
ATOM   7192 C  C   . SER   C 1 316 ? -21.956 -26.820 10.774  1.00 29.74  ? 322 SER   C C   1 
ATOM   7193 O  O   . SER   C 1 316 ? -21.050 -27.532 11.212  1.00 30.27  ? 322 SER   C O   1 
ATOM   7194 C  CB  . SER   C 1 316 ? -22.641 -25.326 12.681  1.00 26.55  ? 322 SER   C CB  1 
ATOM   7195 O  OG  . SER   C 1 316 ? -22.511 -24.031 13.237  1.00 28.92  ? 322 SER   C OG  1 
ATOM   7196 N  N   . PHE   C 1 317 ? -22.872 -27.248 9.876   1.00 26.75  ? 323 PHE   C N   1 
ATOM   7197 C  CA  . PHE   C 1 317 ? -22.928 -28.585 9.299   1.00 26.78  ? 323 PHE   C CA  1 
ATOM   7198 C  C   . PHE   C 1 317 ? -22.623 -28.635 7.797   1.00 32.01  ? 323 PHE   C C   1 
ATOM   7199 O  O   . PHE   C 1 317 ? -22.883 -29.640 7.137   1.00 32.21  ? 323 PHE   C O   1 
ATOM   7200 C  CB  . PHE   C 1 317 ? -24.258 -29.282 9.637   1.00 28.18  ? 323 PHE   C CB  1 
ATOM   7201 C  CG  . PHE   C 1 317 ? -24.283 -29.680 11.093  1.00 29.21  ? 323 PHE   C CG  1 
ATOM   7202 C  CD1 . PHE   C 1 317 ? -23.564 -30.786 11.542  1.00 31.57  ? 323 PHE   C CD1 1 
ATOM   7203 C  CD2 . PHE   C 1 317 ? -24.954 -28.901 12.032  1.00 30.98  ? 323 PHE   C CD2 1 
ATOM   7204 C  CE1 . PHE   C 1 317 ? -23.515 -31.105 12.905  1.00 32.97  ? 323 PHE   C CE1 1 
ATOM   7205 C  CE2 . PHE   C 1 317 ? -24.914 -29.228 13.397  1.00 32.92  ? 323 PHE   C CE2 1 
ATOM   7206 C  CZ  . PHE   C 1 317 ? -24.210 -30.335 13.823  1.00 31.93  ? 323 PHE   C CZ  1 
ATOM   7207 N  N   . GLY   C 1 318 ? -22.026 -27.582 7.264   1.00 29.81  ? 324 GLY   C N   1 
ATOM   7208 C  CA  . GLY   C 1 318 ? -21.618 -27.658 5.874   1.00 29.95  ? 324 GLY   C CA  1 
ATOM   7209 C  C   . GLY   C 1 318 ? -22.071 -26.612 4.913   1.00 34.81  ? 324 GLY   C C   1 
ATOM   7210 O  O   . GLY   C 1 318 ? -21.454 -26.497 3.854   1.00 35.68  ? 324 GLY   C O   1 
ATOM   7211 N  N   . GLN   C 1 319 ? -23.162 -25.881 5.226   1.00 30.06  ? 325 GLN   C N   1 
ATOM   7212 C  CA  . GLN   C 1 319 ? -23.639 -24.845 4.329   1.00 29.44  ? 325 GLN   C CA  1 
ATOM   7213 C  C   . GLN   C 1 319 ? -22.549 -23.784 4.152   1.00 34.11  ? 325 GLN   C C   1 
ATOM   7214 O  O   . GLN   C 1 319 ? -21.955 -23.319 5.127   1.00 32.94  ? 325 GLN   C O   1 
ATOM   7215 C  CB  . GLN   C 1 319 ? -24.942 -24.214 4.845   1.00 30.93  ? 325 GLN   C CB  1 
ATOM   7216 C  CG  . GLN   C 1 319 ? -25.524 -23.170 3.911   1.00 52.87  ? 325 GLN   C CG  1 
ATOM   7217 C  CD  . GLN   C 1 319 ? -26.991 -22.957 4.156   1.00 70.09  ? 325 GLN   C CD  1 
ATOM   7218 O  OE1 . GLN   C 1 319 ? -27.401 -22.096 4.939   1.00 69.28  ? 325 GLN   C OE1 1 
ATOM   7219 N  NE2 . GLN   C 1 319 ? -27.809 -23.726 3.471   1.00 61.81  ? 325 GLN   C NE2 1 
ATOM   7220 N  N   . THR   C 1 320 ? -22.253 -23.467 2.889   1.00 33.74  ? 326 THR   C N   1 
ATOM   7221 C  CA  . THR   C 1 320 ? -21.233 -22.488 2.535   1.00 35.08  ? 326 THR   C CA  1 
ATOM   7222 C  C   . THR   C 1 320 ? -21.866 -21.410 1.695   1.00 38.56  ? 326 THR   C C   1 
ATOM   7223 O  O   . THR   C 1 320 ? -22.979 -21.556 1.198   1.00 39.05  ? 326 THR   C O   1 
ATOM   7224 C  CB  . THR   C 1 320 ? -20.062 -23.133 1.758   1.00 45.83  ? 326 THR   C CB  1 
ATOM   7225 O  OG1 . THR   C 1 320 ? -20.568 -23.776 0.589   1.00 48.64  ? 326 THR   C OG1 1 
ATOM   7226 C  CG2 . THR   C 1 320 ? -19.232 -24.086 2.598   1.00 46.31  ? 326 THR   C CG2 1 
ATOM   7227 N  N   . ARG   C 1 321 ? -21.153 -20.333 1.541   1.00 36.25  ? 327 ARG   C N   1 
ATOM   7228 C  CA  . ARG   C 1 321 ? -21.595 -19.216 0.729   1.00 35.93  ? 327 ARG   C CA  1 
ATOM   7229 C  C   . ARG   C 1 321 ? -21.035 -19.420 -0.683  1.00 42.52  ? 327 ARG   C C   1 
ATOM   7230 O  O   . ARG   C 1 321 ? -21.515 -18.813 -1.618  1.00 44.27  ? 327 ARG   C O   1 
ATOM   7231 C  CB  . ARG   C 1 321 ? -21.157 -17.918 1.389   1.00 33.87  ? 327 ARG   C CB  1 
ATOM   7232 C  CG  . ARG   C 1 321 ? -21.945 -17.715 2.696   1.00 43.22  ? 327 ARG   C CG  1 
ATOM   7233 C  CD  . ARG   C 1 321 ? -21.476 -16.547 3.513   1.00 31.41  ? 327 ARG   C CD  1 
ATOM   7234 N  NE  . ARG   C 1 321 ? -20.211 -16.798 4.195   1.00 27.43  ? 327 ARG   C NE  1 
ATOM   7235 C  CZ  . ARG   C 1 321 ? -19.434 -15.823 4.663   1.00 34.85  ? 327 ARG   C CZ  1 
ATOM   7236 N  NH1 . ARG   C 1 321 ? -19.794 -14.555 4.523   1.00 28.66  ? 327 ARG   C NH1 1 
ATOM   7237 N  NH2 . ARG   C 1 321 ? -18.302 -16.109 5.282   1.00 28.46  ? 327 ARG   C NH2 1 
ATOM   7238 N  N   . GLU   C 1 322 ? -20.107 -20.371 -0.841  1.00 39.59  ? 328 GLU   C N   1 
ATOM   7239 C  CA  . GLU   C 1 322 ? -19.493 -20.734 -2.114  1.00 39.89  ? 328 GLU   C CA  1 
ATOM   7240 C  C   . GLU   C 1 322 ? -20.178 -21.885 -2.855  1.00 44.89  ? 328 GLU   C C   1 
ATOM   7241 O  O   . GLU   C 1 322 ? -19.939 -22.061 -4.047  1.00 44.46  ? 328 GLU   C O   1 
ATOM   7242 C  CB  . GLU   C 1 322 ? -18.016 -21.035 -1.909  1.00 41.02  ? 328 GLU   C CB  1 
ATOM   7243 C  CG  . GLU   C 1 322 ? -17.226 -19.763 -2.007  1.00 51.38  ? 328 GLU   C CG  1 
ATOM   7244 C  CD  . GLU   C 1 322 ? -15.818 -19.834 -1.471  1.00 61.52  ? 328 GLU   C CD  1 
ATOM   7245 O  OE1 . GLU   C 1 322 ? -15.101 -20.809 -1.802  1.00 53.79  ? 328 GLU   C OE1 1 
ATOM   7246 O  OE2 . GLU   C 1 322 ? -15.413 -18.873 -0.776  1.00 37.77  ? 328 GLU   C OE2 1 
ATOM   7247 N  N   . GLY   C 1 323 ? -20.985 -22.657 -2.141  1.00 44.02  ? 329 GLY   C N   1 
ATOM   7248 C  CA  . GLY   C 1 323 ? -21.772 -23.762 -2.684  1.00 44.73  ? 329 GLY   C CA  1 
ATOM   7249 C  C   . GLY   C 1 323 ? -21.102 -25.108 -2.916  1.00 50.55  ? 329 GLY   C C   1 
ATOM   7250 O  O   . GLY   C 1 323 ? -21.636 -25.927 -3.678  1.00 51.20  ? 329 GLY   C O   1 
ATOM   7251 N  N   . GLY   C 1 324 ? -19.975 -25.364 -2.248  1.00 45.60  ? 330 GLY   C N   1 
ATOM   7252 C  CA  . GLY   C 1 324 ? -19.246 -26.619 -2.404  1.00 44.72  ? 330 GLY   C CA  1 
ATOM   7253 C  C   . GLY   C 1 324 ? -19.597 -27.777 -1.483  1.00 49.61  ? 330 GLY   C C   1 
ATOM   7254 O  O   . GLY   C 1 324 ? -18.895 -28.792 -1.503  1.00 50.72  ? 330 GLY   C O   1 
ATOM   7255 N  N   . HIS   C 1 325 ? -20.686 -27.665 -0.700  1.00 45.02  ? 331 HIS   C N   1 
ATOM   7256 C  CA  . HIS   C 1 325 ? -21.119 -28.700 0.255   1.00 45.63  ? 331 HIS   C CA  1 
ATOM   7257 C  C   . HIS   C 1 325 ? -21.700 -29.976 -0.369  1.00 47.81  ? 331 HIS   C C   1 
ATOM   7258 O  O   . HIS   C 1 325 ? -21.623 -31.041 0.240   1.00 47.91  ? 331 HIS   C O   1 
ATOM   7259 C  CB  . HIS   C 1 325 ? -22.111 -28.135 1.287   1.00 46.89  ? 331 HIS   C CB  1 
ATOM   7260 C  CG  . HIS   C 1 325 ? -23.095 -27.134 0.757   1.00 50.88  ? 331 HIS   C CG  1 
ATOM   7261 N  ND1 . HIS   C 1 325 ? -22.725 -25.814 0.506   1.00 52.99  ? 331 HIS   C ND1 1 
ATOM   7262 C  CD2 . HIS   C 1 325 ? -24.422 -27.268 0.521   1.00 53.17  ? 331 HIS   C CD2 1 
ATOM   7263 C  CE1 . HIS   C 1 325 ? -23.829 -25.201 0.104   1.00 52.70  ? 331 HIS   C CE1 1 
ATOM   7264 N  NE2 . HIS   C 1 325 ? -24.875 -26.040 0.084   1.00 53.18  ? 331 HIS   C NE2 1 
ATOM   7265 N  N   . ILE   C 1 326 ? -22.319 -29.858 -1.542  1.00 42.89  ? 332 ILE   C N   1 
ATOM   7266 C  CA  . ILE   C 1 326 ? -22.944 -30.967 -2.262  1.00 42.00  ? 332 ILE   C CA  1 
ATOM   7267 C  C   . ILE   C 1 326 ? -21.979 -31.480 -3.337  1.00 42.90  ? 332 ILE   C C   1 
ATOM   7268 O  O   . ILE   C 1 326 ? -21.361 -30.677 -4.042  1.00 42.66  ? 332 ILE   C O   1 
ATOM   7269 C  CB  . ILE   C 1 326 ? -24.322 -30.498 -2.820  1.00 45.25  ? 332 ILE   C CB  1 
ATOM   7270 C  CG1 . ILE   C 1 326 ? -25.330 -30.279 -1.655  1.00 46.59  ? 332 ILE   C CG1 1 
ATOM   7271 C  CG2 . ILE   C 1 326 ? -24.891 -31.454 -3.876  1.00 45.50  ? 332 ILE   C CG2 1 
ATOM   7272 C  CD1 . ILE   C 1 326 ? -26.321 -29.130 -1.870  1.00 58.24  ? 332 ILE   C CD1 1 
ATOM   7273 N  N   . VAL   C 1 327 ? -21.833 -32.808 -3.436  1.00 38.18  ? 333 VAL   C N   1 
ATOM   7274 C  CA  . VAL   C 1 327 ? -20.957 -33.440 -4.420  1.00 37.65  ? 333 VAL   C CA  1 
ATOM   7275 C  C   . VAL   C 1 327 ? -21.538 -33.205 -5.821  1.00 40.45  ? 333 VAL   C C   1 
ATOM   7276 O  O   . VAL   C 1 327 ? -22.728 -33.462 -6.072  1.00 40.80  ? 333 VAL   C O   1 
ATOM   7277 C  CB  . VAL   C 1 327 ? -20.709 -34.949 -4.121  1.00 42.09  ? 333 VAL   C CB  1 
ATOM   7278 C  CG1 . VAL   C 1 327 ? -19.932 -35.632 -5.250  1.00 41.95  ? 333 VAL   C CG1 1 
ATOM   7279 C  CG2 . VAL   C 1 327 ? -19.993 -35.142 -2.786  1.00 41.80  ? 333 VAL   C CG2 1 
ATOM   7280 N  N   . TYR   C 1 328 ? -20.707 -32.650 -6.704  1.00 33.98  ? 334 TYR   C N   1 
ATOM   7281 C  CA  . TYR   C 1 328 ? -21.048 -32.405 -8.096  1.00 33.56  ? 334 TYR   C CA  1 
ATOM   7282 C  C   . TYR   C 1 328 ? -19.748 -32.488 -8.856  1.00 37.66  ? 334 TYR   C C   1 
ATOM   7283 O  O   . TYR   C 1 328 ? -18.832 -31.717 -8.580  1.00 39.14  ? 334 TYR   C O   1 
ATOM   7284 C  CB  . TYR   C 1 328 ? -21.779 -31.072 -8.276  1.00 34.57  ? 334 TYR   C CB  1 
ATOM   7285 C  CG  . TYR   C 1 328 ? -22.405 -30.946 -9.640  1.00 35.11  ? 334 TYR   C CG  1 
ATOM   7286 C  CD1 . TYR   C 1 328 ? -21.622 -30.726 -10.771 1.00 36.34  ? 334 TYR   C CD1 1 
ATOM   7287 C  CD2 . TYR   C 1 328 ? -23.775 -31.102 -9.813  1.00 35.04  ? 334 TYR   C CD2 1 
ATOM   7288 C  CE1 . TYR   C 1 328 ? -22.187 -30.653 -12.035 1.00 36.42  ? 334 TYR   C CE1 1 
ATOM   7289 C  CE2 . TYR   C 1 328 ? -24.352 -31.031 -11.074 1.00 35.39  ? 334 TYR   C CE2 1 
ATOM   7290 C  CZ  . TYR   C 1 328 ? -23.556 -30.793 -12.178 1.00 39.40  ? 334 TYR   C CZ  1 
ATOM   7291 O  OH  . TYR   C 1 328 ? -24.123 -30.712 -13.416 1.00 36.62  ? 334 TYR   C OH  1 
ATOM   7292 N  N   . ASP   C 1 329 ? -19.619 -33.498 -9.717  1.00 33.79  ? 335 ASP   C N   1 
ATOM   7293 C  CA  . ASP   C 1 329 ? -18.360 -33.770 -10.400 1.00 35.04  ? 335 ASP   C CA  1 
ATOM   7294 C  C   . ASP   C 1 329 ? -18.451 -34.029 -11.889 1.00 36.88  ? 335 ASP   C C   1 
ATOM   7295 O  O   . ASP   C 1 329 ? -17.452 -34.459 -12.480 1.00 34.22  ? 335 ASP   C O   1 
ATOM   7296 C  CB  . ASP   C 1 329 ? -17.630 -34.959 -9.724  1.00 37.60  ? 335 ASP   C CB  1 
ATOM   7297 C  CG  . ASP   C 1 329 ? -18.441 -36.247 -9.601  1.00 48.42  ? 335 ASP   C CG  1 
ATOM   7298 O  OD1 . ASP   C 1 329 ? -19.453 -36.397 -10.336 1.00 48.60  ? 335 ASP   C OD1 1 
ATOM   7299 O  OD2 . ASP   C 1 329 ? -18.070 -37.101 -8.772  1.00 53.95  ? 335 ASP   C OD2 1 
ATOM   7300 N  N   . GLN   C 1 330 ? -19.626 -33.842 -12.502 1.00 32.93  ? 336 GLN   C N   1 
ATOM   7301 C  CA  . GLN   C 1 330 ? -19.691 -34.023 -13.947 1.00 32.87  ? 336 GLN   C CA  1 
ATOM   7302 C  C   . GLN   C 1 330 ? -20.842 -33.258 -14.541 1.00 35.11  ? 336 GLN   C C   1 
ATOM   7303 O  O   . GLN   C 1 330 ? -21.983 -33.338 -14.068 1.00 35.81  ? 336 GLN   C O   1 
ATOM   7304 C  CB  . GLN   C 1 330 ? -19.636 -35.497 -14.410 1.00 35.05  ? 336 GLN   C CB  1 
ATOM   7305 C  CG  . GLN   C 1 330 ? -20.913 -36.322 -14.469 1.00 53.87  ? 336 GLN   C CG  1 
ATOM   7306 C  CD  . GLN   C 1 330 ? -20.631 -37.600 -15.234 1.00 71.70  ? 336 GLN   C CD  1 
ATOM   7307 O  OE1 . GLN   C 1 330 ? -19.934 -38.505 -14.753 1.00 69.81  ? 336 GLN   C OE1 1 
ATOM   7308 N  NE2 . GLN   C 1 330 ? -21.121 -37.682 -16.465 1.00 57.01  ? 336 GLN   C NE2 1 
ATOM   7309 N  N   . LEU   C 1 331 ? -20.520 -32.464 -15.550 1.00 28.87  ? 337 LEU   C N   1 
ATOM   7310 C  CA  . LEU   C 1 331 ? -21.512 -31.651 -16.221 1.00 27.98  ? 337 LEU   C CA  1 
ATOM   7311 C  C   . LEU   C 1 331 ? -22.336 -32.452 -17.223 1.00 30.53  ? 337 LEU   C C   1 
ATOM   7312 O  O   . LEU   C 1 331 ? -21.770 -33.253 -17.975 1.00 29.93  ? 337 LEU   C O   1 
ATOM   7313 C  CB  . LEU   C 1 331 ? -20.834 -30.457 -16.944 1.00 27.57  ? 337 LEU   C CB  1 
ATOM   7314 C  CG  . LEU   C 1 331 ? -20.403 -29.331 -16.021 1.00 31.36  ? 337 LEU   C CG  1 
ATOM   7315 C  CD1 . LEU   C 1 331 ? -19.375 -28.450 -16.696 1.00 31.28  ? 337 LEU   C CD1 1 
ATOM   7316 C  CD2 . LEU   C 1 331 ? -21.608 -28.486 -15.571 1.00 31.97  ? 337 LEU   C CD2 1 
ATOM   7317 N  N   . PRO   C 1 332 ? -23.667 -32.183 -17.325 1.00 26.45  ? 338 PRO   C N   1 
ATOM   7318 C  CA  . PRO   C 1 332 ? -24.453 -32.808 -18.391 1.00 26.06  ? 338 PRO   C CA  1 
ATOM   7319 C  C   . PRO   C 1 332 ? -24.015 -32.240 -19.742 1.00 30.01  ? 338 PRO   C C   1 
ATOM   7320 O  O   . PRO   C 1 332 ? -23.521 -31.110 -19.812 1.00 30.61  ? 338 PRO   C O   1 
ATOM   7321 C  CB  . PRO   C 1 332 ? -25.899 -32.389 -18.075 1.00 27.51  ? 338 PRO   C CB  1 
ATOM   7322 C  CG  . PRO   C 1 332 ? -25.786 -31.209 -17.227 1.00 29.86  ? 338 PRO   C CG  1 
ATOM   7323 C  CD  . PRO   C 1 332 ? -24.486 -31.249 -16.522 1.00 27.19  ? 338 PRO   C CD  1 
ATOM   7324 N  N   . THR   C 1 333 ? -24.150 -33.029 -20.797 1.00 27.17  ? 339 THR   C N   1 
ATOM   7325 C  CA  . THR   C 1 333 ? -23.726 -32.632 -22.144 1.00 28.10  ? 339 THR   C CA  1 
ATOM   7326 C  C   . THR   C 1 333 ? -24.885 -32.703 -23.123 1.00 31.38  ? 339 THR   C C   1 
ATOM   7327 O  O   . THR   C 1 333 ? -25.710 -33.618 -22.991 1.00 30.45  ? 339 THR   C O   1 
ATOM   7328 C  CB  . THR   C 1 333 ? -22.552 -33.526 -22.642 1.00 34.15  ? 339 THR   C CB  1 
ATOM   7329 O  OG1 . THR   C 1 333 ? -22.922 -34.896 -22.534 1.00 34.66  ? 339 THR   C OG1 1 
ATOM   7330 C  CG2 . THR   C 1 333 ? -21.265 -33.293 -21.880 1.00 32.09  ? 339 THR   C CG2 1 
ATOM   7331 N  N   . PRO   C 1 334 ? -24.941 -31.767 -24.113 1.00 28.53  ? 340 PRO   C N   1 
ATOM   7332 C  CA  . PRO   C 1 334 ? -26.065 -31.763 -25.084 1.00 34.54  ? 340 PRO   C CA  1 
ATOM   7333 C  C   . PRO   C 1 334 ? -26.086 -32.888 -26.126 1.00 40.25  ? 340 PRO   C C   1 
ATOM   7334 O  O   . PRO   C 1 334 ? -25.097 -33.594 -26.311 1.00 38.96  ? 340 PRO   C O   1 
ATOM   7335 C  CB  . PRO   C 1 334 ? -25.943 -30.400 -25.765 1.00 35.30  ? 340 PRO   C CB  1 
ATOM   7336 C  CG  . PRO   C 1 334 ? -24.509 -30.038 -25.646 1.00 37.62  ? 340 PRO   C CG  1 
ATOM   7337 C  CD  . PRO   C 1 334 ? -24.030 -30.625 -24.343 1.00 30.80  ? 340 PRO   C CD  1 
HETATM 7338 MN MN  . MN    D 2 .   ? -27.067 -11.567 -11.776 1.00 31.50  ? 401 MN    A MN  1 
HETATM 7339 MN MN  . MN    E 2 .   ? -27.955 -11.872 -8.530  1.00 35.89  ? 402 MN    A MN  1 
HETATM 7340 C  C2  . A1H0A F 3 .   ? -28.341 -19.490 -7.743  1.00 33.23  ? 403 A1H0A A C2  1 
HETATM 7341 C  C3  . A1H0A F 3 .   ? -29.671 -19.503 -6.928  1.00 37.37  ? 403 A1H0A A C3  1 
HETATM 7342 C  C9  . A1H0A F 3 .   ? -29.917 -17.705 -9.661  1.00 37.39  ? 403 A1H0A A C9  1 
HETATM 7343 C  C10 . A1H0A F 3 .   ? -31.156 -16.801 -9.760  1.00 37.23  ? 403 A1H0A A C10 1 
HETATM 7344 C  C11 . A1H0A F 3 .   ? -30.672 -15.350 -9.573  1.00 35.76  ? 403 A1H0A A C11 1 
HETATM 7345 C  C12 . A1H0A F 3 .   ? -29.864 -14.857 -10.788 1.00 35.59  ? 403 A1H0A A C12 1 
HETATM 7346 O  O17 . A1H0A F 3 .   ? -30.202 -12.580 -9.775  1.00 37.71  ? 403 A1H0A A O17 1 
HETATM 7347 N  N1  . A1H0A F 3 .   ? -28.736 -19.769 -9.156  1.00 34.37  ? 403 A1H0A A N1  1 
HETATM 7348 C  C4  . A1H0A F 3 .   ? -30.792 -19.544 -8.012  1.00 38.24  ? 403 A1H0A A C4  1 
HETATM 7349 C  C5  . A1H0A F 3 .   ? -30.097 -19.208 -9.362  1.00 37.86  ? 403 A1H0A A C5  1 
HETATM 7350 C  C6  . A1H0A F 3 .   ? -30.770 -19.863 -10.564 1.00 36.17  ? 403 A1H0A A C6  1 
HETATM 7351 O  O7  . A1H0A F 3 .   ? -32.107 -19.853 -10.689 1.00 36.13  ? 403 A1H0A A O7  1 
HETATM 7352 O  O8  . A1H0A F 3 .   ? -30.118 -20.354 -11.463 1.00 33.61  ? 403 A1H0A A O8  1 
HETATM 7353 B  B13 . A1H0A F 3 .   ? -29.590 -13.274 -10.800 1.00 40.11  ? 403 A1H0A A B13 1 
HETATM 7354 O  O14 . A1H0A F 3 .   ? -28.246 -13.025 -10.780 1.00 36.35  ? 403 A1H0A A O14 1 
HETATM 7355 O  O15 . A1H0A F 3 .   ? -30.042 -12.786 -11.987 1.00 48.23  ? 403 A1H0A A O15 1 
HETATM 7356 N  N16 . A1H0A F 3 .   ? -29.736 -20.641 -5.996  1.00 36.34  ? 403 A1H0A A N16 1 
HETATM 7357 MN MN  . MN    G 2 .   ? -19.174 18.860  11.863  1.00 59.74  ? 500 MN    B MN  1 
HETATM 7358 MN MN  . MN    H 2 .   ? -21.019 16.573  10.027  1.00 48.51  ? 501 MN    B MN  1 
HETATM 7359 MN MN  . MN    I 2 .   ? -25.800 -16.580 26.682  1.00 29.69  ? 401 MN    C MN  1 
HETATM 7360 MN MN  . MN    J 2 .   ? -26.175 -13.431 25.658  1.00 31.08  ? 402 MN    C MN  1 
HETATM 7361 C  C2  . A1H0A K 3 .   ? -24.122 -9.311  31.888  1.00 39.51  ? 403 A1H0A C C2  1 
HETATM 7362 C  C3  . A1H0A K 3 .   ? -25.306 -8.315  31.733  1.00 41.05  ? 403 A1H0A C C3  1 
HETATM 7363 C  C9  . A1H0A K 3 .   ? -26.363 -11.441 31.478  1.00 43.09  ? 403 A1H0A C C9  1 
HETATM 7364 C  C10 . A1H0A K 3 .   ? -27.817 -11.749 31.104  1.00 41.75  ? 403 A1H0A C C10 1 
HETATM 7365 C  C11 . A1H0A K 3 .   ? -27.804 -12.288 29.672  1.00 39.30  ? 403 A1H0A C C11 1 
HETATM 7366 C  C12 . A1H0A K 3 .   ? -27.572 -13.805 29.657  1.00 38.83  ? 403 A1H0A C C12 1 
HETATM 7367 O  O17 . A1H0A K 3 .   ? -28.288 -13.674 27.271  1.00 34.62  ? 403 A1H0A C O17 1 
HETATM 7368 N  N1  . A1H0A K 3 .   ? -24.619 -10.381 32.801  1.00 38.15  ? 403 A1H0A C N1  1 
HETATM 7369 C  C4  . A1H0A K 3 .   ? -26.541 -9.020  32.358  1.00 40.27  ? 403 A1H0A C C4  1 
HETATM 7370 C  C5  . A1H0A K 3 .   ? -26.094 -10.470 32.648  1.00 40.48  ? 403 A1H0A C C5  1 
HETATM 7371 C  C6  . A1H0A K 3 .   ? -26.695 -11.022 33.930  1.00 38.66  ? 403 A1H0A C C6  1 
HETATM 7372 O  O7  . A1H0A K 3 .   ? -26.014 -11.654 34.703  1.00 37.70  ? 403 A1H0A C O7  1 
HETATM 7373 O  O8  . A1H0A K 3 .   ? -27.997 -10.880 34.205  1.00 38.94  ? 403 A1H0A C O8  1 
HETATM 7374 B  B13 . A1H0A K 3 .   ? -27.603 -14.438 28.180  1.00 37.80  ? 403 A1H0A C B13 1 
HETATM 7375 O  O14 . A1H0A K 3 .   ? -26.317 -14.578 27.733  1.00 32.75  ? 403 A1H0A C O14 1 
HETATM 7376 O  O15 . A1H0A K 3 .   ? -28.203 -15.666 28.246  1.00 43.32  ? 403 A1H0A C O15 1 
HETATM 7377 N  N16 . A1H0A K 3 .   ? -24.981 -7.035  32.375  1.00 41.78  ? 403 A1H0A C N16 1 
HETATM 7378 O  O   . HOH   L 4 .   ? -9.204  -26.636 -12.153 1.00 41.69  ? 501 HOH   A O   1 
HETATM 7379 O  O   . HOH   L 4 .   ? -27.135 -18.754 -11.291 1.00 30.34  ? 502 HOH   A O   1 
HETATM 7380 O  O   . HOH   L 4 .   ? -37.888 -17.010 -16.260 1.00 46.48  ? 503 HOH   A O   1 
HETATM 7381 O  O   . HOH   L 4 .   ? -20.334 -21.330 -24.148 1.00 28.17  ? 504 HOH   A O   1 
HETATM 7382 O  O   . HOH   L 4 .   ? -14.168 -5.258  3.070   1.00 30.71  ? 505 HOH   A O   1 
HETATM 7383 O  O   . HOH   L 4 .   ? -17.820 7.143   -4.254  1.00 53.77  ? 506 HOH   A O   1 
HETATM 7384 O  O   . HOH   L 4 .   ? -17.780 -2.196  5.080   1.00 33.50  ? 507 HOH   A O   1 
HETATM 7385 O  O   . HOH   L 4 .   ? -6.832  -12.500 -17.531 1.00 43.60  ? 508 HOH   A O   1 
HETATM 7386 O  O   . HOH   L 4 .   ? -24.178 -28.437 -19.288 1.00 27.82  ? 509 HOH   A O   1 
HETATM 7387 O  O   . HOH   L 4 .   ? -14.773 -28.545 -21.221 1.00 45.96  ? 510 HOH   A O   1 
HETATM 7388 O  O   . HOH   L 4 .   ? -25.135 -18.419 -8.429  1.00 29.36  ? 511 HOH   A O   1 
HETATM 7389 O  O   . HOH   L 4 .   ? -34.632 -8.120  -9.609  1.00 37.17  ? 512 HOH   A O   1 
HETATM 7390 O  O   . HOH   L 4 .   ? -12.646 11.077  -9.288  1.00 55.52  ? 513 HOH   A O   1 
HETATM 7391 O  O   . HOH   L 4 .   ? -29.082 -9.601  -2.193  1.00 33.48  ? 514 HOH   A O   1 
HETATM 7392 O  O   . HOH   L 4 .   ? -31.973 10.703  -15.171 1.00 53.51  ? 515 HOH   A O   1 
HETATM 7393 O  O   . HOH   L 4 .   ? -28.028 8.425   -5.076  1.00 50.95  ? 516 HOH   A O   1 
HETATM 7394 O  O   . HOH   L 4 .   ? -23.524 -2.186  -20.915 1.00 35.91  ? 517 HOH   A O   1 
HETATM 7395 O  O   . HOH   L 4 .   ? -38.903 -24.138 -15.415 1.00 38.16  ? 518 HOH   A O   1 
HETATM 7396 O  O   . HOH   L 4 .   ? -15.443 -22.362 -27.610 1.00 48.65  ? 519 HOH   A O   1 
HETATM 7397 O  O   . HOH   L 4 .   ? -38.444 1.058   -17.270 1.00 44.72  ? 520 HOH   A O   1 
HETATM 7398 O  O   . HOH   L 4 .   ? -22.461 -13.535 3.332   1.00 31.56  ? 521 HOH   A O   1 
HETATM 7399 O  O   . HOH   L 4 .   ? -7.459  -2.044  -3.871  1.00 31.39  ? 522 HOH   A O   1 
HETATM 7400 O  O   . HOH   L 4 .   ? -8.157  -18.857 -14.947 1.00 47.19  ? 523 HOH   A O   1 
HETATM 7401 O  O   . HOH   L 4 .   ? -3.604  -4.627  -8.589  1.00 44.20  ? 524 HOH   A O   1 
HETATM 7402 O  O   . HOH   L 4 .   ? -14.739 7.227   -8.494  1.00 41.70  ? 525 HOH   A O   1 
HETATM 7403 O  O   . HOH   L 4 .   ? -32.116 -10.200 -7.582  1.00 38.32  ? 526 HOH   A O   1 
HETATM 7404 O  O   . HOH   L 4 .   ? -4.846  -5.586  -24.977 1.00 50.54  ? 527 HOH   A O   1 
HETATM 7405 O  O   . HOH   L 4 .   ? -14.579 -30.655 -22.983 1.00 53.39  ? 528 HOH   A O   1 
HETATM 7406 O  O   . HOH   L 4 .   ? -16.818 -9.715  7.532   1.00 35.20  ? 529 HOH   A O   1 
HETATM 7407 O  O   . HOH   L 4 .   ? -30.882 -20.605 -14.064 1.00 27.99  ? 530 HOH   A O   1 
HETATM 7408 O  O   . HOH   L 4 .   ? -31.486 -2.313  -12.743 1.00 35.46  ? 531 HOH   A O   1 
HETATM 7409 O  O   . HOH   L 4 .   ? -11.234 -11.284 -24.058 1.00 41.65  ? 532 HOH   A O   1 
HETATM 7410 O  O   . HOH   L 4 .   ? -38.018 -25.717 -12.423 1.00 48.07  ? 533 HOH   A O   1 
HETATM 7411 O  O   . HOH   L 4 .   ? -41.926 -27.798 -22.317 1.00 32.09  ? 534 HOH   A O   1 
HETATM 7412 O  O   . HOH   L 4 .   ? -16.369 1.785   -24.673 1.00 50.33  ? 535 HOH   A O   1 
HETATM 7413 O  O   . HOH   L 4 .   ? -43.334 -8.615  -15.780 1.00 62.62  ? 536 HOH   A O   1 
HETATM 7414 O  O   . HOH   L 4 .   ? -27.022 -8.387  6.735   1.00 47.76  ? 537 HOH   A O   1 
HETATM 7415 O  O   . HOH   L 4 .   ? -11.472 -19.615 2.551   1.00 56.92  ? 538 HOH   A O   1 
HETATM 7416 O  O   . HOH   L 4 .   ? -10.605 -23.306 -17.964 1.00 38.87  ? 539 HOH   A O   1 
HETATM 7417 O  O   . HOH   L 4 .   ? -45.371 -5.063  -13.420 1.00 62.69  ? 540 HOH   A O   1 
HETATM 7418 O  O   . HOH   L 4 .   ? -17.444 -4.992  5.484   1.00 31.18  ? 541 HOH   A O   1 
HETATM 7419 O  O   . HOH   L 4 .   ? -36.338 -12.302 -9.659  1.00 41.18  ? 542 HOH   A O   1 
HETATM 7420 O  O   . HOH   L 4 .   ? -13.446 -11.169 -27.131 1.00 61.99  ? 543 HOH   A O   1 
HETATM 7421 O  O   . HOH   L 4 .   ? -28.578 -25.536 -10.805 1.00 37.79  ? 544 HOH   A O   1 
HETATM 7422 O  O   . HOH   L 4 .   ? -19.782 -11.031 -29.822 1.00 39.54  ? 545 HOH   A O   1 
HETATM 7423 O  O   . HOH   L 4 .   ? -10.870 -16.027 -13.934 1.00 28.95  ? 546 HOH   A O   1 
HETATM 7424 O  O   . HOH   L 4 .   ? -41.497 -20.229 -21.209 1.00 53.23  ? 547 HOH   A O   1 
HETATM 7425 O  O   . HOH   L 4 .   ? -7.889  -5.608  2.080   1.00 33.95  ? 548 HOH   A O   1 
HETATM 7426 O  O   . HOH   L 4 .   ? -32.999 -14.220 -31.546 1.00 40.73  ? 549 HOH   A O   1 
HETATM 7427 O  O   . HOH   L 4 .   ? -26.708 -8.431  -32.537 1.00 40.64  ? 550 HOH   A O   1 
HETATM 7428 O  O   . HOH   L 4 .   ? -36.176 -17.048 -18.470 1.00 37.18  ? 551 HOH   A O   1 
HETATM 7429 O  O   . HOH   L 4 .   ? -12.051 -21.145 -8.876  1.00 32.24  ? 552 HOH   A O   1 
HETATM 7430 O  O   . HOH   L 4 .   ? -29.185 12.192  -7.529  1.00 65.00  ? 553 HOH   A O   1 
HETATM 7431 O  O   . HOH   L 4 .   ? -33.479 -11.785 -9.343  1.00 48.50  ? 554 HOH   A O   1 
HETATM 7432 O  O   . HOH   L 4 .   ? -3.373  -9.047  -18.074 1.00 46.58  ? 555 HOH   A O   1 
HETATM 7433 O  O   . HOH   L 4 .   ? -28.033 -21.883 -26.836 1.00 34.91  ? 556 HOH   A O   1 
HETATM 7434 O  O   . HOH   L 4 .   ? -30.146 -8.491  5.141   1.00 54.83  ? 557 HOH   A O   1 
HETATM 7435 O  O   . HOH   L 4 .   ? -31.104 -23.129 -11.022 1.00 34.23  ? 558 HOH   A O   1 
HETATM 7436 O  O   . HOH   L 4 .   ? -31.714 12.295  -20.971 1.00 71.32  ? 559 HOH   A O   1 
HETATM 7437 O  O   . HOH   L 4 .   ? -26.159 -17.470 1.368   1.00 50.89  ? 560 HOH   A O   1 
HETATM 7438 O  O   . HOH   L 4 .   ? -29.994 -6.940  -2.180  1.00 30.87  ? 561 HOH   A O   1 
HETATM 7439 O  O   . HOH   L 4 .   ? -9.636  -16.188 1.161   1.00 44.86  ? 562 HOH   A O   1 
HETATM 7440 O  O   . HOH   L 4 .   ? -37.901 -10.163 -26.885 1.00 47.02  ? 563 HOH   A O   1 
HETATM 7441 O  O   . HOH   L 4 .   ? -14.204 -9.587  8.269   1.00 44.17  ? 564 HOH   A O   1 
HETATM 7442 O  O   . HOH   L 4 .   ? -14.412 5.276   -15.558 1.00 44.31  ? 565 HOH   A O   1 
HETATM 7443 O  O   . HOH   L 4 .   ? -23.993 -27.728 -28.400 1.00 49.24  ? 566 HOH   A O   1 
HETATM 7444 O  O   . HOH   L 4 .   ? -2.410  -5.100  0.000   1.00 44.14  ? 567 HOH   A O   1 
HETATM 7445 O  O   . HOH   L 4 .   ? -12.130 6.885   -7.993  1.00 49.81  ? 568 HOH   A O   1 
HETATM 7446 O  O   . HOH   L 4 .   ? -33.505 -29.794 -27.371 1.00 46.61  ? 569 HOH   A O   1 
HETATM 7447 O  O   . HOH   L 4 .   ? -9.329  -5.359  -26.797 1.00 36.54  ? 570 HOH   A O   1 
HETATM 7448 O  O   . HOH   L 4 .   ? -12.851 -31.813 -11.740 1.00 51.39  ? 571 HOH   A O   1 
HETATM 7449 O  O   . HOH   L 4 .   ? -30.504 -16.384 -33.684 1.00 52.58  ? 572 HOH   A O   1 
HETATM 7450 O  O   . HOH   L 4 .   ? -8.949  -19.164 -19.940 1.00 48.08  ? 573 HOH   A O   1 
HETATM 7451 O  O   . HOH   L 4 .   ? -10.003 -23.458 -9.497  1.00 43.89  ? 574 HOH   A O   1 
HETATM 7452 O  O   . HOH   L 4 .   ? -13.617 -7.411  5.104   1.00 39.50  ? 575 HOH   A O   1 
HETATM 7453 O  O   . HOH   L 4 .   ? -24.618 -15.144 2.861   1.00 35.19  ? 576 HOH   A O   1 
HETATM 7454 O  O   . HOH   L 4 .   ? -39.795 -8.083  -20.670 1.00 46.32  ? 577 HOH   A O   1 
HETATM 7455 O  O   . HOH   L 4 .   ? -32.784 -27.690 -21.103 1.00 40.13  ? 578 HOH   A O   1 
HETATM 7456 O  O   . HOH   L 4 .   ? -11.180 -11.424 8.907   1.00 31.75  ? 579 HOH   A O   1 
HETATM 7457 O  O   . HOH   L 4 .   ? -31.039 -14.656 2.437   1.00 42.01  ? 580 HOH   A O   1 
HETATM 7458 O  O   . HOH   L 4 .   ? -7.935  -21.793 -10.109 1.00 50.46  ? 581 HOH   A O   1 
HETATM 7459 O  O   . HOH   L 4 .   ? -35.110 -7.703  -34.084 1.00 55.64  ? 582 HOH   A O   1 
HETATM 7460 O  O   . HOH   L 4 .   ? -11.038 -13.834 -23.207 1.00 40.03  ? 583 HOH   A O   1 
HETATM 7461 O  O   . HOH   L 4 .   ? -12.009 -18.179 -4.056  1.00 40.01  ? 584 HOH   A O   1 
HETATM 7462 O  O   . HOH   L 4 .   ? -34.692 -5.779  3.254   1.00 60.78  ? 585 HOH   A O   1 
HETATM 7463 O  O   . HOH   L 4 .   ? -9.676  -15.938 -5.525  1.00 51.16  ? 586 HOH   A O   1 
HETATM 7464 O  O   . HOH   L 4 .   ? -14.286 5.336   -18.722 1.00 52.97  ? 587 HOH   A O   1 
HETATM 7465 O  O   . HOH   L 4 .   ? -23.846 -0.075  4.319   1.00 40.90  ? 588 HOH   A O   1 
HETATM 7466 O  O   . HOH   L 4 .   ? -23.968 -20.873 -1.935  1.00 35.66  ? 589 HOH   A O   1 
HETATM 7467 O  O   . HOH   L 4 .   ? -36.579 -31.644 -18.255 1.00 48.03  ? 590 HOH   A O   1 
HETATM 7468 O  O   . HOH   L 4 .   ? -12.308 3.550   -15.686 1.00 38.21  ? 591 HOH   A O   1 
HETATM 7469 O  O   . HOH   L 4 .   ? -11.127 -18.293 -7.009  1.00 39.53  ? 592 HOH   A O   1 
HETATM 7470 O  O   . HOH   L 4 .   ? -8.470  -14.730 -13.814 1.00 40.69  ? 593 HOH   A O   1 
HETATM 7471 O  O   . HOH   L 4 .   ? -28.766 2.032   0.179   1.00 42.80  ? 594 HOH   A O   1 
HETATM 7472 O  O   . HOH   L 4 .   ? -21.396 0.945   4.497   1.00 28.15  ? 595 HOH   A O   1 
HETATM 7473 O  O   . HOH   L 4 .   ? -6.783  -13.704 -20.459 1.00 64.19  ? 596 HOH   A O   1 
HETATM 7474 O  O   . HOH   L 4 .   ? -28.801 -27.161 -8.648  1.00 55.45  ? 597 HOH   A O   1 
HETATM 7475 O  O   . HOH   L 4 .   ? -10.106 9.017   -3.504  1.00 60.71  ? 598 HOH   A O   1 
HETATM 7476 O  O   . HOH   L 4 .   ? -31.657 -23.158 -8.352  1.00 54.26  ? 599 HOH   A O   1 
HETATM 7477 O  O   . HOH   L 4 .   ? -33.000 10.888  -17.700 1.00 62.61  ? 600 HOH   A O   1 
HETATM 7478 O  O   . HOH   L 4 .   ? -18.581 -1.463  7.578   1.00 37.01  ? 601 HOH   A O   1 
HETATM 7479 O  O   . HOH   M 4 .   ? -13.257 -3.513  24.633  1.00 66.49  ? 601 HOH   B O   1 
HETATM 7480 O  O   . HOH   M 4 .   ? -24.231 10.917  8.641   1.00 54.64  ? 602 HOH   B O   1 
HETATM 7481 O  O   . HOH   M 4 .   ? -10.241 2.181   26.433  1.00 42.33  ? 603 HOH   B O   1 
HETATM 7482 O  O   . HOH   M 4 .   ? -4.432  4.268   22.034  1.00 45.26  ? 604 HOH   B O   1 
HETATM 7483 O  O   . HOH   M 4 .   ? -8.513  -6.493  23.715  1.00 56.43  ? 605 HOH   B O   1 
HETATM 7484 O  O   . HOH   M 4 .   ? -12.556 3.290   26.902  1.00 41.74  ? 606 HOH   B O   1 
HETATM 7485 O  O   . HOH   M 4 .   ? -12.396 -15.134 46.791  1.00 51.35  ? 607 HOH   B O   1 
HETATM 7486 O  O   . HOH   M 4 .   ? -5.418  1.214   16.978  1.00 39.54  ? 608 HOH   B O   1 
HETATM 7487 O  O   . HOH   M 4 .   ? -12.568 -0.589  10.209  1.00 31.63  ? 609 HOH   B O   1 
HETATM 7488 O  O   . HOH   M 4 .   ? -20.852 -9.200  43.855  1.00 68.20  ? 610 HOH   B O   1 
HETATM 7489 O  O   . HOH   M 4 .   ? -12.385 -1.029  7.391   1.00 40.22  ? 611 HOH   B O   1 
HETATM 7490 O  O   . HOH   M 4 .   ? -18.809 5.879   2.473   1.00 36.87  ? 612 HOH   B O   1 
HETATM 7491 O  O   . HOH   M 4 .   ? -1.899  16.552  9.999   1.00 52.10  ? 613 HOH   B O   1 
HETATM 7492 O  O   . HOH   M 4 .   ? -27.586 18.670  13.497  1.00 56.22  ? 614 HOH   B O   1 
HETATM 7493 O  O   . HOH   M 4 .   ? -26.446 29.952  10.369  1.00 80.22  ? 615 HOH   B O   1 
HETATM 7494 O  O   . HOH   M 4 .   ? -4.131  3.038   18.525  1.00 43.29  ? 616 HOH   B O   1 
HETATM 7495 O  O   . HOH   M 4 .   ? -17.233 -2.278  11.785  1.00 31.01  ? 617 HOH   B O   1 
HETATM 7496 O  O   . HOH   M 4 .   ? -16.640 1.218   24.206  1.00 40.44  ? 618 HOH   B O   1 
HETATM 7497 O  O   . HOH   M 4 .   ? -21.733 2.006   7.834   1.00 55.41  ? 619 HOH   B O   1 
HETATM 7498 O  O   . HOH   M 4 .   ? -12.965 7.887   35.651  1.00 51.84  ? 620 HOH   B O   1 
HETATM 7499 O  O   . HOH   M 4 .   ? -20.330 7.931   1.567   1.00 40.76  ? 621 HOH   B O   1 
HETATM 7500 O  O   . HOH   M 4 .   ? -6.430  -1.885  10.822  1.00 37.22  ? 622 HOH   B O   1 
HETATM 7501 O  O   . HOH   M 4 .   ? -15.446 -1.312  4.266   1.00 40.45  ? 623 HOH   B O   1 
HETATM 7502 O  O   . HOH   M 4 .   ? -5.374  4.565   2.392   1.00 53.05  ? 624 HOH   B O   1 
HETATM 7503 O  O   . HOH   M 4 .   ? -26.401 4.465   25.770  1.00 53.52  ? 625 HOH   B O   1 
HETATM 7504 O  O   . HOH   M 4 .   ? -5.877  -3.825  3.311   1.00 49.33  ? 626 HOH   B O   1 
HETATM 7505 O  O   . HOH   M 4 .   ? -2.763  -0.890  18.131  1.00 54.48  ? 627 HOH   B O   1 
HETATM 7506 O  O   . HOH   M 4 .   ? -29.637 20.285  12.593  1.00 64.01  ? 628 HOH   B O   1 
HETATM 7507 O  O   . HOH   M 4 .   ? -25.527 9.914   10.817  1.00 50.86  ? 629 HOH   B O   1 
HETATM 7508 O  O   . HOH   M 4 .   ? -20.191 2.144   39.146  1.00 54.26  ? 630 HOH   B O   1 
HETATM 7509 O  O   . HOH   M 4 .   ? -20.174 1.097   46.473  1.00 74.92  ? 631 HOH   B O   1 
HETATM 7510 O  O   . HOH   M 4 .   ? -22.996 -0.430  13.590  1.00 45.17  ? 632 HOH   B O   1 
HETATM 7511 O  O   . HOH   M 4 .   ? -13.207 -2.776  4.193   1.00 44.71  ? 633 HOH   B O   1 
HETATM 7512 O  O   . HOH   M 4 .   ? -9.880  -3.713  2.742   1.00 31.67  ? 634 HOH   B O   1 
HETATM 7513 O  O   . HOH   M 4 .   ? -15.288 -1.165  42.291  1.00 40.20  ? 635 HOH   B O   1 
HETATM 7514 O  O   . HOH   M 4 .   ? -16.258 -1.705  45.314  1.00 42.23  ? 636 HOH   B O   1 
HETATM 7515 O  O   . HOH   M 4 .   ? -21.302 19.113  10.191  1.00 35.03  ? 637 HOH   B O   1 
HETATM 7516 O  O   . HOH   M 4 .   ? 8.913   11.020  22.004  1.00 67.38  ? 638 HOH   B O   1 
HETATM 7517 O  O   . HOH   M 4 .   ? -8.735  -7.842  50.210  1.00 56.91  ? 639 HOH   B O   1 
HETATM 7518 O  O   . HOH   M 4 .   ? -16.806 5.277   45.192  1.00 44.48  ? 640 HOH   B O   1 
HETATM 7519 O  O   . HOH   M 4 .   ? -26.647 2.660   21.975  1.00 53.56  ? 641 HOH   B O   1 
HETATM 7520 O  O   . HOH   M 4 .   ? -27.961 11.044  34.431  1.00 63.59  ? 642 HOH   B O   1 
HETATM 7521 O  O   . HOH   M 4 .   ? -8.337  -7.081  40.743  1.00 58.68  ? 643 HOH   B O   1 
HETATM 7522 O  O   . HOH   M 4 .   ? 1.653   7.627   10.570  1.00 56.01  ? 644 HOH   B O   1 
HETATM 7523 O  O   . HOH   M 4 .   ? -21.079 -1.934  14.688  1.00 31.49  ? 645 HOH   B O   1 
HETATM 7524 O  O   . HOH   M 4 .   ? -4.573  22.440  27.558  1.00 55.46  ? 646 HOH   B O   1 
HETATM 7525 O  O   . HOH   M 4 .   ? -12.604 3.862   34.537  1.00 59.90  ? 647 HOH   B O   1 
HETATM 7526 O  O   . HOH   M 4 .   ? -13.750 21.079  24.893  1.00 54.12  ? 648 HOH   B O   1 
HETATM 7527 O  O   . HOH   M 4 .   ? -10.826 -6.197  37.717  1.00 52.14  ? 649 HOH   B O   1 
HETATM 7528 O  O   . HOH   M 4 .   ? -19.068 0.434   25.065  1.00 58.59  ? 650 HOH   B O   1 
HETATM 7529 O  O   . HOH   M 4 .   ? -18.782 -4.352  11.277  1.00 36.95  ? 651 HOH   B O   1 
HETATM 7530 O  O   . HOH   M 4 .   ? -19.778 -3.813  8.689   1.00 29.80  ? 652 HOH   B O   1 
HETATM 7531 O  O   . HOH   N 4 .   ? -22.319 -20.212 5.458   1.00 36.02  ? 501 HOH   C O   1 
HETATM 7532 O  O   . HOH   N 4 .   ? -14.858 -34.393 -12.433 1.00 33.37  ? 502 HOH   C O   1 
HETATM 7533 O  O   . HOH   N 4 .   ? -26.711 -30.786 -13.639 1.00 34.47  ? 503 HOH   C O   1 
HETATM 7534 O  O   . HOH   N 4 .   ? -19.318 -33.299 -18.937 1.00 30.74  ? 504 HOH   C O   1 
HETATM 7535 O  O   . HOH   N 4 .   ? -23.619 -12.968 32.463  1.00 37.75  ? 505 HOH   C O   1 
HETATM 7536 O  O   . HOH   N 4 .   ? -9.386  -20.272 27.636  1.00 26.42  ? 506 HOH   C O   1 
HETATM 7537 O  O   . HOH   N 4 .   ? -10.997 -20.245 42.895  1.00 53.90  ? 507 HOH   C O   1 
HETATM 7538 O  O   . HOH   N 4 .   ? -17.666 -24.695 39.278  1.00 41.91  ? 508 HOH   C O   1 
HETATM 7539 O  O   . HOH   N 4 .   ? -8.121  -13.856 29.890  1.00 42.68  ? 509 HOH   C O   1 
HETATM 7540 O  O   . HOH   N 4 .   ? -33.060 -20.323 20.596  1.00 29.05  ? 510 HOH   C O   1 
HETATM 7541 O  O   . HOH   N 4 .   ? -18.571 -8.066  8.614   1.00 30.55  ? 511 HOH   C O   1 
HETATM 7542 O  O   . HOH   N 4 .   ? -30.521 -12.208 24.639  1.00 34.12  ? 512 HOH   C O   1 
HETATM 7543 O  O   . HOH   N 4 .   ? -25.357 -17.846 4.320   1.00 56.39  ? 513 HOH   C O   1 
HETATM 7544 O  O   . HOH   N 4 .   ? -32.556 -19.141 7.009   1.00 35.16  ? 514 HOH   C O   1 
HETATM 7545 O  O   . HOH   N 4 .   ? -19.884 -24.561 6.456   1.00 29.06  ? 515 HOH   C O   1 
HETATM 7546 O  O   . HOH   N 4 .   ? -30.866 -12.927 27.283  1.00 35.59  ? 516 HOH   C O   1 
HETATM 7547 O  O   . HOH   N 4 .   ? -28.258 -36.088 34.164  1.00 46.48  ? 517 HOH   C O   1 
HETATM 7548 O  O   . HOH   N 4 .   ? -22.700 -5.019  14.014  1.00 46.99  ? 518 HOH   C O   1 
HETATM 7549 O  O   . HOH   N 4 .   ? -19.699 -29.859 11.206  1.00 33.87  ? 519 HOH   C O   1 
HETATM 7550 O  O   . HOH   N 4 .   ? -13.339 -28.851 40.376  1.00 61.27  ? 520 HOH   C O   1 
HETATM 7551 O  O   . HOH   N 4 .   ? -21.115 -27.148 39.757  1.00 47.44  ? 521 HOH   C O   1 
HETATM 7552 O  O   . HOH   N 4 .   ? -14.578 -33.211 31.151  1.00 35.38  ? 522 HOH   C O   1 
HETATM 7553 O  O   . HOH   N 4 .   ? -20.255 -38.920 20.025  1.00 37.02  ? 523 HOH   C O   1 
HETATM 7554 O  O   . HOH   N 4 .   ? -16.183 -37.532 -6.883  1.00 41.72  ? 524 HOH   C O   1 
HETATM 7555 O  O   . HOH   N 4 .   ? -22.250 -45.043 18.766  1.00 55.06  ? 525 HOH   C O   1 
HETATM 7556 O  O   . HOH   N 4 .   ? -18.629 -16.543 44.113  1.00 44.16  ? 526 HOH   C O   1 
HETATM 7557 O  O   . HOH   N 4 .   ? -37.878 -27.906 10.423  1.00 38.04  ? 527 HOH   C O   1 
HETATM 7558 O  O   . HOH   N 4 .   ? -33.808 -14.350 24.708  1.00 32.01  ? 528 HOH   C O   1 
HETATM 7559 O  O   . HOH   N 4 .   ? -28.829 -26.338 2.954   1.00 59.23  ? 529 HOH   C O   1 
HETATM 7560 O  O   . HOH   N 4 .   ? -12.033 -31.089 28.270  1.00 31.90  ? 530 HOH   C O   1 
HETATM 7561 O  O   . HOH   N 4 .   ? -39.636 -37.051 17.592  1.00 33.65  ? 531 HOH   C O   1 
HETATM 7562 O  O   . HOH   N 4 .   ? -40.054 -18.892 12.393  1.00 35.48  ? 532 HOH   C O   1 
HETATM 7563 O  O   . HOH   N 4 .   ? -24.278 -25.313 -3.784  1.00 45.95  ? 533 HOH   C O   1 
HETATM 7564 O  O   . HOH   N 4 .   ? -21.453 -11.077 30.518  1.00 30.22  ? 534 HOH   C O   1 
HETATM 7565 O  O   . HOH   N 4 .   ? -9.952  -18.434 10.164  1.00 32.35  ? 535 HOH   C O   1 
HETATM 7566 O  O   . HOH   N 4 .   ? -15.102 -2.801  13.395  1.00 37.80  ? 536 HOH   C O   1 
HETATM 7567 O  O   . HOH   N 4 .   ? -35.451 -16.441 49.707  1.00 72.81  ? 537 HOH   C O   1 
HETATM 7568 O  O   . HOH   N 4 .   ? -29.067 -9.534  18.925  1.00 33.03  ? 538 HOH   C O   1 
HETATM 7569 O  O   . HOH   N 4 .   ? -21.725 -32.014 34.936  1.00 45.22  ? 539 HOH   C O   1 
HETATM 7570 O  O   . HOH   N 4 .   ? -13.195 -6.957  12.089  1.00 40.68  ? 540 HOH   C O   1 
HETATM 7571 O  O   . HOH   N 4 .   ? -27.419 -8.503  20.946  1.00 30.38  ? 541 HOH   C O   1 
HETATM 7572 O  O   . HOH   N 4 .   ? -26.884 -13.761 36.399  1.00 38.33  ? 542 HOH   C O   1 
HETATM 7573 O  O   . HOH   N 4 .   ? -23.937 -27.093 41.187  1.00 44.87  ? 543 HOH   C O   1 
HETATM 7574 O  O   . HOH   N 4 .   ? -14.179 -9.295  11.047  1.00 29.69  ? 544 HOH   C O   1 
HETATM 7575 O  O   . HOH   N 4 .   ? -17.336 -24.585 5.783   1.00 34.20  ? 545 HOH   C O   1 
HETATM 7576 O  O   . HOH   N 4 .   ? -15.501 -34.510 17.336  1.00 40.67  ? 546 HOH   C O   1 
HETATM 7577 O  O   . HOH   N 4 .   ? -20.500 -34.334 32.934  1.00 41.60  ? 547 HOH   C O   1 
HETATM 7578 O  O   . HOH   N 4 .   ? -17.333 -6.528  10.632  1.00 30.45  ? 548 HOH   C O   1 
HETATM 7579 O  O   . HOH   N 4 .   ? -40.089 -32.537 16.018  1.00 36.29  ? 549 HOH   C O   1 
HETATM 7580 O  O   . HOH   N 4 .   ? -34.133 -5.491  12.578  1.00 58.06  ? 550 HOH   C O   1 
HETATM 7581 O  O   . HOH   N 4 .   ? -20.979 -2.834  22.156  1.00 31.97  ? 551 HOH   C O   1 
HETATM 7582 O  O   . HOH   N 4 .   ? -21.074 -36.275 18.887  1.00 37.86  ? 552 HOH   C O   1 
HETATM 7583 O  O   . HOH   N 4 .   ? -9.271  -2.585  12.268  1.00 33.20  ? 553 HOH   C O   1 
HETATM 7584 O  O   . HOH   N 4 .   ? -34.451 -39.077 9.486   1.00 59.85  ? 554 HOH   C O   1 
HETATM 7585 O  O   . HOH   N 4 .   ? -29.990 -41.237 21.366  1.00 57.89  ? 555 HOH   C O   1 
HETATM 7586 O  O   . HOH   N 4 .   ? -42.155 -31.950 20.090  1.00 36.68  ? 556 HOH   C O   1 
HETATM 7587 O  O   . HOH   N 4 .   ? -22.515 -35.866 -18.440 1.00 43.98  ? 557 HOH   C O   1 
HETATM 7588 O  O   . HOH   N 4 .   ? -8.367  -11.687 10.352  1.00 33.56  ? 558 HOH   C O   1 
HETATM 7589 O  O   . HOH   N 4 .   ? -31.992 -13.446 8.917   1.00 37.67  ? 559 HOH   C O   1 
HETATM 7590 O  O   . HOH   N 4 .   ? -41.539 -34.759 23.353  1.00 42.36  ? 560 HOH   C O   1 
HETATM 7591 O  O   . HOH   N 4 .   ? -30.533 -11.243 33.147  1.00 45.97  ? 561 HOH   C O   1 
HETATM 7592 O  O   . HOH   N 4 .   ? -9.619  -35.626 21.949  1.00 34.24  ? 562 HOH   C O   1 
HETATM 7593 O  O   . HOH   N 4 .   ? -23.719 -35.723 -25.187 1.00 43.61  ? 563 HOH   C O   1 
HETATM 7594 O  O   . HOH   N 4 .   ? -9.743  -20.923 11.238  1.00 37.49  ? 564 HOH   C O   1 
HETATM 7595 O  O   . HOH   N 4 .   ? -5.423  -35.269 16.965  1.00 33.78  ? 565 HOH   C O   1 
HETATM 7596 O  O   . HOH   N 4 .   ? -30.157 -36.113 4.195   1.00 45.73  ? 566 HOH   C O   1 
HETATM 7597 O  O   . HOH   N 4 .   ? -37.905 -28.245 35.385  1.00 56.23  ? 567 HOH   C O   1 
HETATM 7598 O  O   . HOH   N 4 .   ? -5.126  -28.923 21.884  1.00 31.98  ? 568 HOH   C O   1 
HETATM 7599 O  O   . HOH   N 4 .   ? -27.204 -5.509  33.088  1.00 50.62  ? 569 HOH   C O   1 
HETATM 7600 O  O   . HOH   N 4 .   ? -20.722 -36.410 16.191  1.00 44.22  ? 570 HOH   C O   1 
HETATM 7601 O  O   . HOH   N 4 .   ? -7.153  -26.089 25.276  1.00 38.44  ? 571 HOH   C O   1 
HETATM 7602 O  O   . HOH   N 4 .   ? -7.364  -11.826 7.613   1.00 47.43  ? 572 HOH   C O   1 
HETATM 7603 O  O   . HOH   N 4 .   ? -25.034 -25.149 42.751  1.00 41.19  ? 573 HOH   C O   1 
HETATM 7604 O  O   . HOH   N 4 .   ? -19.103 -3.442  20.050  1.00 33.11  ? 574 HOH   C O   1 
HETATM 7605 O  O   . HOH   N 4 .   ? -26.093 -9.983  37.015  1.00 37.80  ? 575 HOH   C O   1 
HETATM 7606 O  O   . HOH   N 4 .   ? -11.316 -24.443 10.318  1.00 37.53  ? 576 HOH   C O   1 
HETATM 7607 O  O   . HOH   N 4 .   ? -26.318 -29.587 22.541  1.00 27.57  ? 577 HOH   C O   1 
HETATM 7608 O  O   . HOH   N 4 .   ? -7.480  -21.500 26.098  1.00 46.34  ? 578 HOH   C O   1 
HETATM 7609 O  O   . HOH   N 4 .   ? -35.628 -8.926  50.280  1.00 57.29  ? 579 HOH   C O   1 
HETATM 7610 O  O   . HOH   N 4 .   ? -28.291 -2.429  16.841  1.00 45.93  ? 580 HOH   C O   1 
HETATM 7611 O  O   . HOH   N 4 .   ? -18.864 -4.926  28.930  1.00 38.24  ? 581 HOH   C O   1 
HETATM 7612 O  O   . HOH   N 4 .   ? -25.106 -1.595  14.980  1.00 43.76  ? 582 HOH   C O   1 
HETATM 7613 O  O   . HOH   N 4 .   ? -33.114 -18.070 36.672  1.00 46.48  ? 583 HOH   C O   1 
HETATM 7614 O  O   . HOH   N 4 .   ? -22.029 -34.884 -10.247 1.00 57.10  ? 584 HOH   C O   1 
HETATM 7615 O  O   . HOH   N 4 .   ? -8.792  -10.622 24.719  1.00 45.56  ? 585 HOH   C O   1 
HETATM 7616 O  O   . HOH   N 4 .   ? -37.916 -28.141 7.697   1.00 38.02  ? 586 HOH   C O   1 
HETATM 7617 O  O   . HOH   N 4 .   ? -13.502 -6.114  37.165  1.00 45.26  ? 587 HOH   C O   1 
HETATM 7618 O  O   . HOH   N 4 .   ? -31.061 -6.583  9.440   1.00 44.94  ? 588 HOH   C O   1 
HETATM 7619 O  O   . HOH   N 4 .   ? -18.444 -20.328 2.562   1.00 48.54  ? 589 HOH   C O   1 
HETATM 7620 O  O   . HOH   N 4 .   ? -11.291 -29.327 30.349  1.00 36.90  ? 590 HOH   C O   1 
HETATM 7621 O  O   . HOH   N 4 .   ? -32.376 -38.024 7.712   1.00 39.07  ? 591 HOH   C O   1 
HETATM 7622 O  O   . HOH   N 4 .   ? -22.294 -45.283 26.740  1.00 56.86  ? 592 HOH   C O   1 
HETATM 7623 O  O   . HOH   N 4 .   ? -23.861 -34.287 5.849   1.00 47.18  ? 593 HOH   C O   1 
HETATM 7624 O  O   . HOH   N 4 .   ? -17.161 -29.833 12.243  1.00 29.88  ? 594 HOH   C O   1 
HETATM 7625 O  O   . HOH   N 4 .   ? -34.938 -41.702 21.177  1.00 50.91  ? 595 HOH   C O   1 
HETATM 7626 O  O   . HOH   N 4 .   ? -30.586 -11.380 9.994   1.00 37.68  ? 596 HOH   C O   1 
HETATM 7627 O  O   . HOH   N 4 .   ? -41.053 -24.647 21.145  1.00 39.33  ? 597 HOH   C O   1 
HETATM 7628 O  O   . HOH   N 4 .   ? -17.717 -32.575 -16.692 1.00 30.86  ? 598 HOH   C O   1 
HETATM 7629 O  O   . HOH   N 4 .   ? -20.774 -32.846 12.721  1.00 66.13  ? 599 HOH   C O   1 
HETATM 7630 O  O   . HOH   N 4 .   ? -7.031  -25.013 32.529  1.00 49.20  ? 600 HOH   C O   1 
HETATM 7631 O  O   . HOH   N 4 .   ? -25.755 -42.449 27.406  1.00 53.64  ? 601 HOH   C O   1 
HETATM 7632 O  O   . HOH   N 4 .   ? -9.014  -30.684 11.490  1.00 63.54  ? 602 HOH   C O   1 
HETATM 7633 O  O   . HOH   N 4 .   ? -12.178 -20.470 -2.593  1.00 58.01  ? 603 HOH   C O   1 
HETATM 7634 O  O   . HOH   N 4 .   ? -27.226 -1.733  23.530  1.00 39.07  ? 604 HOH   C O   1 
HETATM 7635 O  O   . HOH   N 4 .   ? -23.113 -9.153  7.309   1.00 33.46  ? 605 HOH   C O   1 
HETATM 7636 O  O   . HOH   N 4 .   ? -40.271 -16.708 14.017  1.00 51.31  ? 606 HOH   C O   1 
HETATM 7637 O  O   . HOH   N 4 .   ? -12.737 -3.035  12.074  1.00 57.85  ? 607 HOH   C O   1 
HETATM 7638 O  O   . HOH   N 4 .   ? -5.309  -30.522 15.130  1.00 62.80  ? 608 HOH   C O   1 
HETATM 7639 O  O   . HOH   N 4 .   ? -8.178  -13.080 26.456  1.00 44.84  ? 609 HOH   C O   1 
HETATM 7640 O  O   . HOH   N 4 .   ? -42.648 -19.990 17.609  1.00 51.26  ? 610 HOH   C O   1 
HETATM 7641 O  O   . HOH   N 4 .   ? -17.766 -33.085 -5.479  1.00 48.14  ? 611 HOH   C O   1 
HETATM 7642 O  O   . HOH   N 4 .   ? -5.296  -24.684 14.635  1.00 47.88  ? 612 HOH   C O   1 
HETATM 7643 O  O   . HOH   N 4 .   ? -41.122 -30.553 17.759  1.00 38.90  ? 613 HOH   C O   1 
HETATM 7644 O  O   . HOH   N 4 .   ? -19.536 -6.141  6.924   1.00 35.23  ? 614 HOH   C O   1 
# 
