data_9EIA
# 
_entry.id   9EIA 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.401 
_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   9EIA         pdb_00009eia 10.2210/pdb9eia/pdb 
WWPDB D_1000290534 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-01-29 
# 
_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_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9EIA 
_pdbx_database_status.recvd_initial_deposition_date   2024-11-25 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_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           Y 
# 
loop_
_pdbx_contact_author.id 
_pdbx_contact_author.email 
_pdbx_contact_author.name_first 
_pdbx_contact_author.name_last 
_pdbx_contact_author.name_mi 
_pdbx_contact_author.role 
_pdbx_contact_author.identifier_ORCID 
2 hausinge@msu.edu Robert Hausinger P 'principal investigator/group leader' 0000-0002-3643-2054 
3 hujian1@msu.edu  Jian   Hu        ? 'principal investigator/group leader' 0000-0001-6657-9826 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Gatreddi, S.'    1 ? 
'Hausinger, R.P.' 2 ? 
'Hu, J.'          3 ? 
# 
_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            Biorxiv 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2692-8205 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
'Structural Basis for Catalysis and Substrate Specificity of a LarA Racemase with a Broad Substrate Spectrum.' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1101/2024.11.28.625916 
_citation.pdbx_database_id_PubMed   39651260 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Gatreddi, S.'        1 ? 
primary 'Urdiain-Arraiza, J.' 2 ? 
primary 'Desguin, B.'         3 ? 
primary 'Hausinger, R.P.'     4 ? 
primary 'Hu, J.'              5 ? 
# 
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 'A broad-substrate spectrum lactate racemase A'                                            45898.801 2   ? ? ? ? 
2 non-polymer syn 1,2-ETHANEDIOL                                                                             62.068    3   ? ? ? ? 
3 non-polymer syn '3-methanethioyl-1-(5-O-phosphono-beta-D-ribofuranosyl)-5-(sulfanylcarbonyl)pyridin-1-ium' 396.353   2   ? ? ? ? 
4 non-polymer syn 'DI(HYDROXYETHYL)ETHER'                                                                    106.120   3   ? ? ? ? 
5 non-polymer syn 'LACTIC ACID'                                                                              90.078    2   ? ? ? ? 
6 non-polymer syn 'NICKEL (II) ION'                                                                          58.693    2   ? ? ? ? 
7 water       nat water                                                                                      18.015    516 ? ? ? ? 
# 
_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       
;RVTLDYGKTGLNVDLPDDRTLPPLTIRPAPPLDDPEAEVVRCLAEPIGSPPLLDLARGKRSACILVCDITRPVPNPVLLR
PILRTLHAAGLATQDILILVATGLHRPSTPAEKVEMLSEEIARTYRVEDHYGTRLEEHTYLGTTPNGVPAWIDSRYVQAD
LKIATGLIEPHLMAGYSGGRKLICPGIAAFETVKLWHGPRFLEHPLADCGFLEGNPVHEENTRIARMAGCDFIVNVTLDG
ARRITSVVAGDMEQAFLKGVAFVETVVKAAVPAPVDVVVTSSAGHPLDLTFYQAVKGLTGALPIVKPGGTIVIAAALAEG
LGSPEFQSLFEEHPTLEGFMEAILKEESFTVDQWQLEELAKVRRKARVKFVSDGVPAAVLSRCHVEPVATVELAVAQALE
QYGPEARVAVIPKGPYVLPVVDPTL
;
_entity_poly.pdbx_seq_one_letter_code_can   
;RVTLDYGKTGLNVDLPDDRTLPPLTIRPAPPLDDPEAEVVRCLAEPIGSPPLLDLARGKRSACILVCDITRPVPNPVLLR
PILRTLHAAGLATQDILILVATGLHRPSTPAEKVEMLSEEIARTYRVEDHYGTRLEEHTYLGTTPNGVPAWIDSRYVQAD
LKIATGLIEPHLMAGYSGGRKLICPGIAAFETVKLWHGPRFLEHPLADCGFLEGNPVHEENTRIARMAGCDFIVNVTLDG
ARRITSVVAGDMEQAFLKGVAFVETVVKAAVPAPVDVVVTSSAGHPLDLTFYQAVKGLTGALPIVKPGGTIVIAAALAEG
LGSPEFQSLFEEHPTLEGFMEAILKEESFTVDQWQLEELAKVRRKARVKFVSDGVPAAVLSRCHVEPVATVELAVAQALE
QYGPEARVAVIPKGPYVLPVVDPTL
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 1,2-ETHANEDIOL                                                                             EDO 
3 '3-methanethioyl-1-(5-O-phosphono-beta-D-ribofuranosyl)-5-(sulfanylcarbonyl)pyridin-1-ium' 4EY 
4 'DI(HYDROXYETHYL)ETHER'                                                                    PEG 
5 'LACTIC ACID'                                                                              LAC 
6 'NICKEL (II) ION'                                                                          NI  
7 water                                                                                      HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   ARG n 
1 2   VAL n 
1 3   THR n 
1 4   LEU n 
1 5   ASP n 
1 6   TYR n 
1 7   GLY n 
1 8   LYS n 
1 9   THR n 
1 10  GLY n 
1 11  LEU n 
1 12  ASN n 
1 13  VAL n 
1 14  ASP n 
1 15  LEU n 
1 16  PRO n 
1 17  ASP n 
1 18  ASP n 
1 19  ARG n 
1 20  THR n 
1 21  LEU n 
1 22  PRO n 
1 23  PRO n 
1 24  LEU n 
1 25  THR n 
1 26  ILE n 
1 27  ARG n 
1 28  PRO n 
1 29  ALA n 
1 30  PRO n 
1 31  PRO n 
1 32  LEU n 
1 33  ASP n 
1 34  ASP n 
1 35  PRO n 
1 36  GLU n 
1 37  ALA n 
1 38  GLU n 
1 39  VAL n 
1 40  VAL n 
1 41  ARG n 
1 42  CYS n 
1 43  LEU n 
1 44  ALA n 
1 45  GLU n 
1 46  PRO n 
1 47  ILE n 
1 48  GLY n 
1 49  SER n 
1 50  PRO n 
1 51  PRO n 
1 52  LEU n 
1 53  LEU n 
1 54  ASP n 
1 55  LEU n 
1 56  ALA n 
1 57  ARG n 
1 58  GLY n 
1 59  LYS n 
1 60  ARG n 
1 61  SER n 
1 62  ALA n 
1 63  CYS n 
1 64  ILE n 
1 65  LEU n 
1 66  VAL n 
1 67  CYS n 
1 68  ASP n 
1 69  ILE n 
1 70  THR n 
1 71  ARG n 
1 72  PRO n 
1 73  VAL n 
1 74  PRO n 
1 75  ASN n 
1 76  PRO n 
1 77  VAL n 
1 78  LEU n 
1 79  LEU n 
1 80  ARG n 
1 81  PRO n 
1 82  ILE n 
1 83  LEU n 
1 84  ARG n 
1 85  THR n 
1 86  LEU n 
1 87  HIS n 
1 88  ALA n 
1 89  ALA n 
1 90  GLY n 
1 91  LEU n 
1 92  ALA n 
1 93  THR n 
1 94  GLN n 
1 95  ASP n 
1 96  ILE n 
1 97  LEU n 
1 98  ILE n 
1 99  LEU n 
1 100 VAL n 
1 101 ALA n 
1 102 THR n 
1 103 GLY n 
1 104 LEU n 
1 105 HIS n 
1 106 ARG n 
1 107 PRO n 
1 108 SER n 
1 109 THR n 
1 110 PRO n 
1 111 ALA n 
1 112 GLU n 
1 113 LYS n 
1 114 VAL n 
1 115 GLU n 
1 116 MET n 
1 117 LEU n 
1 118 SER n 
1 119 GLU n 
1 120 GLU n 
1 121 ILE n 
1 122 ALA n 
1 123 ARG n 
1 124 THR n 
1 125 TYR n 
1 126 ARG n 
1 127 VAL n 
1 128 GLU n 
1 129 ASP n 
1 130 HIS n 
1 131 TYR n 
1 132 GLY n 
1 133 THR n 
1 134 ARG n 
1 135 LEU n 
1 136 GLU n 
1 137 GLU n 
1 138 HIS n 
1 139 THR n 
1 140 TYR n 
1 141 LEU n 
1 142 GLY n 
1 143 THR n 
1 144 THR n 
1 145 PRO n 
1 146 ASN n 
1 147 GLY n 
1 148 VAL n 
1 149 PRO n 
1 150 ALA n 
1 151 TRP n 
1 152 ILE n 
1 153 ASP n 
1 154 SER n 
1 155 ARG n 
1 156 TYR n 
1 157 VAL n 
1 158 GLN n 
1 159 ALA n 
1 160 ASP n 
1 161 LEU n 
1 162 LYS n 
1 163 ILE n 
1 164 ALA n 
1 165 THR n 
1 166 GLY n 
1 167 LEU n 
1 168 ILE n 
1 169 GLU n 
1 170 PRO n 
1 171 HIS n 
1 172 LEU n 
1 173 MET n 
1 174 ALA n 
1 175 GLY n 
1 176 TYR n 
1 177 SER n 
1 178 GLY n 
1 179 GLY n 
1 180 ARG n 
1 181 LYS n 
1 182 LEU n 
1 183 ILE n 
1 184 CYS n 
1 185 PRO n 
1 186 GLY n 
1 187 ILE n 
1 188 ALA n 
1 189 ALA n 
1 190 PHE n 
1 191 GLU n 
1 192 THR n 
1 193 VAL n 
1 194 LYS n 
1 195 LEU n 
1 196 TRP n 
1 197 HIS n 
1 198 GLY n 
1 199 PRO n 
1 200 ARG n 
1 201 PHE n 
1 202 LEU n 
1 203 GLU n 
1 204 HIS n 
1 205 PRO n 
1 206 LEU n 
1 207 ALA n 
1 208 ASP n 
1 209 CYS n 
1 210 GLY n 
1 211 PHE n 
1 212 LEU n 
1 213 GLU n 
1 214 GLY n 
1 215 ASN n 
1 216 PRO n 
1 217 VAL n 
1 218 HIS n 
1 219 GLU n 
1 220 GLU n 
1 221 ASN n 
1 222 THR n 
1 223 ARG n 
1 224 ILE n 
1 225 ALA n 
1 226 ARG n 
1 227 MET n 
1 228 ALA n 
1 229 GLY n 
1 230 CYS n 
1 231 ASP n 
1 232 PHE n 
1 233 ILE n 
1 234 VAL n 
1 235 ASN n 
1 236 VAL n 
1 237 THR n 
1 238 LEU n 
1 239 ASP n 
1 240 GLY n 
1 241 ALA n 
1 242 ARG n 
1 243 ARG n 
1 244 ILE n 
1 245 THR n 
1 246 SER n 
1 247 VAL n 
1 248 VAL n 
1 249 ALA n 
1 250 GLY n 
1 251 ASP n 
1 252 MET n 
1 253 GLU n 
1 254 GLN n 
1 255 ALA n 
1 256 PHE n 
1 257 LEU n 
1 258 LYS n 
1 259 GLY n 
1 260 VAL n 
1 261 ALA n 
1 262 PHE n 
1 263 VAL n 
1 264 GLU n 
1 265 THR n 
1 266 VAL n 
1 267 VAL n 
1 268 LYS n 
1 269 ALA n 
1 270 ALA n 
1 271 VAL n 
1 272 PRO n 
1 273 ALA n 
1 274 PRO n 
1 275 VAL n 
1 276 ASP n 
1 277 VAL n 
1 278 VAL n 
1 279 VAL n 
1 280 THR n 
1 281 SER n 
1 282 SER n 
1 283 ALA n 
1 284 GLY n 
1 285 HIS n 
1 286 PRO n 
1 287 LEU n 
1 288 ASP n 
1 289 LEU n 
1 290 THR n 
1 291 PHE n 
1 292 TYR n 
1 293 GLN n 
1 294 ALA n 
1 295 VAL n 
1 296 LYS n 
1 297 GLY n 
1 298 LEU n 
1 299 THR n 
1 300 GLY n 
1 301 ALA n 
1 302 LEU n 
1 303 PRO n 
1 304 ILE n 
1 305 VAL n 
1 306 LYS n 
1 307 PRO n 
1 308 GLY n 
1 309 GLY n 
1 310 THR n 
1 311 ILE n 
1 312 VAL n 
1 313 ILE n 
1 314 ALA n 
1 315 ALA n 
1 316 ALA n 
1 317 LEU n 
1 318 ALA n 
1 319 GLU n 
1 320 GLY n 
1 321 LEU n 
1 322 GLY n 
1 323 SER n 
1 324 PRO n 
1 325 GLU n 
1 326 PHE n 
1 327 GLN n 
1 328 SER n 
1 329 LEU n 
1 330 PHE n 
1 331 GLU n 
1 332 GLU n 
1 333 HIS n 
1 334 PRO n 
1 335 THR n 
1 336 LEU n 
1 337 GLU n 
1 338 GLY n 
1 339 PHE n 
1 340 MET n 
1 341 GLU n 
1 342 ALA n 
1 343 ILE n 
1 344 LEU n 
1 345 LYS n 
1 346 GLU n 
1 347 GLU n 
1 348 SER n 
1 349 PHE n 
1 350 THR n 
1 351 VAL n 
1 352 ASP n 
1 353 GLN n 
1 354 TRP n 
1 355 GLN n 
1 356 LEU n 
1 357 GLU n 
1 358 GLU n 
1 359 LEU n 
1 360 ALA n 
1 361 LYS n 
1 362 VAL n 
1 363 ARG n 
1 364 ARG n 
1 365 LYS n 
1 366 ALA n 
1 367 ARG n 
1 368 VAL n 
1 369 LYS n 
1 370 PHE n 
1 371 VAL n 
1 372 SER n 
1 373 ASP n 
1 374 GLY n 
1 375 VAL n 
1 376 PRO n 
1 377 ALA n 
1 378 ALA n 
1 379 VAL n 
1 380 LEU n 
1 381 SER n 
1 382 ARG n 
1 383 CYS n 
1 384 HIS n 
1 385 VAL n 
1 386 GLU n 
1 387 PRO n 
1 388 VAL n 
1 389 ALA n 
1 390 THR n 
1 391 VAL n 
1 392 GLU n 
1 393 LEU n 
1 394 ALA n 
1 395 VAL n 
1 396 ALA n 
1 397 GLN n 
1 398 ALA n 
1 399 LEU n 
1 400 GLU n 
1 401 GLN n 
1 402 TYR n 
1 403 GLY n 
1 404 PRO n 
1 405 GLU n 
1 406 ALA n 
1 407 ARG n 
1 408 VAL n 
1 409 ALA n 
1 410 VAL n 
1 411 ILE n 
1 412 PRO n 
1 413 LYS n 
1 414 GLY n 
1 415 PRO n 
1 416 TYR n 
1 417 VAL n 
1 418 LEU n 
1 419 PRO n 
1 420 VAL n 
1 421 VAL n 
1 422 ASP n 
1 423 PRO n 
1 424 THR n 
1 425 LEU 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                   425 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 Isop_3476 
_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      'Isosphaera pallida' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     128 
_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      'Lactococcus lactis' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     1358 
_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               NZ3900 
_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 
4EY non-polymer         . '3-methanethioyl-1-(5-O-phosphono-beta-D-ribofuranosyl)-5-(sulfanylcarbonyl)pyridin-1-ium' 
'Dithiodinicotinic acid mononucleotide' 'C12 H15 N O8 P S2 1' 396.353 
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 
EDO non-polymer         . 1,2-ETHANEDIOL                                                                             
'ETHYLENE GLYCOL'                       'C2 H6 O2'            62.068  
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 
LAC non-polymer         . 'LACTIC ACID'                                                                              ? 'C3 H6 O3' 
90.078  
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 
NI  non-polymer         . 'NICKEL (II) ION'                                                                          ? 'Ni 2' 
58.693  
PEG non-polymer         . 'DI(HYDROXYETHYL)ETHER'                                                                    ? 'C4 H10 O3' 
106.120 
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   ARG 1   3   3   ARG ARG A . n 
A 1 2   VAL 2   4   4   VAL VAL A . n 
A 1 3   THR 3   5   5   THR THR A . n 
A 1 4   LEU 4   6   6   LEU LEU A . n 
A 1 5   ASP 5   7   7   ASP ASP A . n 
A 1 6   TYR 6   8   8   TYR TYR A . n 
A 1 7   GLY 7   9   9   GLY GLY A . n 
A 1 8   LYS 8   10  10  LYS LYS A . n 
A 1 9   THR 9   11  11  THR THR A . n 
A 1 10  GLY 10  12  12  GLY GLY A . n 
A 1 11  LEU 11  13  13  LEU LEU A . n 
A 1 12  ASN 12  14  14  ASN ASN A . n 
A 1 13  VAL 13  15  15  VAL VAL A . n 
A 1 14  ASP 14  16  16  ASP ASP A . n 
A 1 15  LEU 15  17  17  LEU LEU A . n 
A 1 16  PRO 16  18  18  PRO PRO A . n 
A 1 17  ASP 17  19  19  ASP ASP A . n 
A 1 18  ASP 18  20  20  ASP ASP A . n 
A 1 19  ARG 19  21  21  ARG ARG A . n 
A 1 20  THR 20  22  22  THR THR A . n 
A 1 21  LEU 21  23  23  LEU LEU A . n 
A 1 22  PRO 22  24  24  PRO PRO A . n 
A 1 23  PRO 23  25  25  PRO PRO A . n 
A 1 24  LEU 24  26  26  LEU LEU A . n 
A 1 25  THR 25  27  27  THR THR A . n 
A 1 26  ILE 26  28  28  ILE ILE A . n 
A 1 27  ARG 27  29  29  ARG ARG A . n 
A 1 28  PRO 28  30  30  PRO PRO A . n 
A 1 29  ALA 29  31  31  ALA ALA A . n 
A 1 30  PRO 30  32  32  PRO PRO A . n 
A 1 31  PRO 31  33  33  PRO PRO A . n 
A 1 32  LEU 32  34  34  LEU LEU A . n 
A 1 33  ASP 33  35  35  ASP ASP A . n 
A 1 34  ASP 34  36  36  ASP ASP A . n 
A 1 35  PRO 35  37  37  PRO PRO A . n 
A 1 36  GLU 36  38  38  GLU GLU A . n 
A 1 37  ALA 37  39  39  ALA ALA A . n 
A 1 38  GLU 38  40  40  GLU GLU A . n 
A 1 39  VAL 39  41  41  VAL VAL A . n 
A 1 40  VAL 40  42  42  VAL VAL A . n 
A 1 41  ARG 41  43  43  ARG ARG A . n 
A 1 42  CYS 42  44  44  CYS CYS A . n 
A 1 43  LEU 43  45  45  LEU LEU A . n 
A 1 44  ALA 44  46  46  ALA ALA A . n 
A 1 45  GLU 45  47  47  GLU GLU A . n 
A 1 46  PRO 46  48  48  PRO PRO A . n 
A 1 47  ILE 47  49  49  ILE ILE A . n 
A 1 48  GLY 48  50  50  GLY GLY A . n 
A 1 49  SER 49  51  51  SER SER A . n 
A 1 50  PRO 50  52  52  PRO PRO A . n 
A 1 51  PRO 51  53  53  PRO PRO A . n 
A 1 52  LEU 52  54  54  LEU LEU A . n 
A 1 53  LEU 53  55  55  LEU LEU A . n 
A 1 54  ASP 54  56  56  ASP ASP A . n 
A 1 55  LEU 55  57  57  LEU LEU A . n 
A 1 56  ALA 56  58  58  ALA ALA A . n 
A 1 57  ARG 57  59  59  ARG ARG A . n 
A 1 58  GLY 58  60  60  GLY GLY A . n 
A 1 59  LYS 59  61  61  LYS LYS A . n 
A 1 60  ARG 60  62  62  ARG ARG A . n 
A 1 61  SER 61  63  63  SER SER A . n 
A 1 62  ALA 62  64  64  ALA ALA A . n 
A 1 63  CYS 63  65  65  CYS CYS A . n 
A 1 64  ILE 64  66  66  ILE ILE A . n 
A 1 65  LEU 65  67  67  LEU LEU A . n 
A 1 66  VAL 66  68  68  VAL VAL A . n 
A 1 67  CYS 67  69  69  CYS CYS A . n 
A 1 68  ASP 68  70  70  ASP ASP A . n 
A 1 69  ILE 69  71  71  ILE ILE A . n 
A 1 70  THR 70  72  72  THR THR A . n 
A 1 71  ARG 71  73  73  ARG ARG A . n 
A 1 72  PRO 72  74  74  PRO PRO A . n 
A 1 73  VAL 73  75  75  VAL VAL A . n 
A 1 74  PRO 74  76  76  PRO PRO A . n 
A 1 75  ASN 75  77  77  ASN ASN A . n 
A 1 76  PRO 76  78  78  PRO PRO A . n 
A 1 77  VAL 77  79  79  VAL VAL A . n 
A 1 78  LEU 78  80  80  LEU LEU A . n 
A 1 79  LEU 79  81  81  LEU LEU A . n 
A 1 80  ARG 80  82  82  ARG ARG A . n 
A 1 81  PRO 81  83  83  PRO PRO A . n 
A 1 82  ILE 82  84  84  ILE ILE A . n 
A 1 83  LEU 83  85  85  LEU LEU A . n 
A 1 84  ARG 84  86  86  ARG ARG A . n 
A 1 85  THR 85  87  87  THR THR A . n 
A 1 86  LEU 86  88  88  LEU LEU A . n 
A 1 87  HIS 87  89  89  HIS HIS A . n 
A 1 88  ALA 88  90  90  ALA ALA A . n 
A 1 89  ALA 89  91  91  ALA ALA A . n 
A 1 90  GLY 90  92  92  GLY GLY A . n 
A 1 91  LEU 91  93  93  LEU LEU A . n 
A 1 92  ALA 92  94  94  ALA ALA A . n 
A 1 93  THR 93  95  95  THR THR A . n 
A 1 94  GLN 94  96  96  GLN GLN A . n 
A 1 95  ASP 95  97  97  ASP ASP A . n 
A 1 96  ILE 96  98  98  ILE ILE A . n 
A 1 97  LEU 97  99  99  LEU LEU A . n 
A 1 98  ILE 98  100 100 ILE ILE A . n 
A 1 99  LEU 99  101 101 LEU LEU A . n 
A 1 100 VAL 100 102 102 VAL VAL A . n 
A 1 101 ALA 101 103 103 ALA ALA A . n 
A 1 102 THR 102 104 104 THR THR A . n 
A 1 103 GLY 103 105 105 GLY GLY A . n 
A 1 104 LEU 104 106 106 LEU LEU A . n 
A 1 105 HIS 105 107 107 HIS HIS A . n 
A 1 106 ARG 106 108 108 ARG ARG A . n 
A 1 107 PRO 107 109 109 PRO PRO A . n 
A 1 108 SER 108 110 110 SER SER A . n 
A 1 109 THR 109 111 111 THR THR A . n 
A 1 110 PRO 110 112 112 PRO PRO A . n 
A 1 111 ALA 111 113 113 ALA ALA A . n 
A 1 112 GLU 112 114 114 GLU GLU A . n 
A 1 113 LYS 113 115 115 LYS LYS A . n 
A 1 114 VAL 114 116 116 VAL VAL A . n 
A 1 115 GLU 115 117 117 GLU GLU A . n 
A 1 116 MET 116 118 118 MET MET A . n 
A 1 117 LEU 117 119 119 LEU LEU A . n 
A 1 118 SER 118 120 120 SER SER A . n 
A 1 119 GLU 119 121 121 GLU GLU A . n 
A 1 120 GLU 120 122 122 GLU GLU A . n 
A 1 121 ILE 121 123 123 ILE ILE A . n 
A 1 122 ALA 122 124 124 ALA ALA A . n 
A 1 123 ARG 123 125 125 ARG ARG A . n 
A 1 124 THR 124 126 126 THR THR A . n 
A 1 125 TYR 125 127 127 TYR TYR A . n 
A 1 126 ARG 126 128 128 ARG ARG A . n 
A 1 127 VAL 127 129 129 VAL VAL A . n 
A 1 128 GLU 128 130 130 GLU GLU A . n 
A 1 129 ASP 129 131 131 ASP ASP A . n 
A 1 130 HIS 130 132 132 HIS HIS A . n 
A 1 131 TYR 131 133 133 TYR TYR A . n 
A 1 132 GLY 132 134 134 GLY GLY A . n 
A 1 133 THR 133 135 135 THR THR A . n 
A 1 134 ARG 134 136 136 ARG ARG A . n 
A 1 135 LEU 135 137 137 LEU LEU A . n 
A 1 136 GLU 136 138 138 GLU GLU A . n 
A 1 137 GLU 137 139 139 GLU GLU A . n 
A 1 138 HIS 138 140 140 HIS HIS A . n 
A 1 139 THR 139 141 141 THR THR A . n 
A 1 140 TYR 140 142 142 TYR TYR A . n 
A 1 141 LEU 141 143 143 LEU LEU A . n 
A 1 142 GLY 142 144 144 GLY GLY A . n 
A 1 143 THR 143 145 145 THR THR A . n 
A 1 144 THR 144 146 146 THR THR A . n 
A 1 145 PRO 145 147 147 PRO PRO A . n 
A 1 146 ASN 146 148 148 ASN ASN A . n 
A 1 147 GLY 147 149 149 GLY GLY A . n 
A 1 148 VAL 148 150 150 VAL VAL A . n 
A 1 149 PRO 149 151 151 PRO PRO A . n 
A 1 150 ALA 150 152 152 ALA ALA A . n 
A 1 151 TRP 151 153 153 TRP TRP A . n 
A 1 152 ILE 152 154 154 ILE ILE A . n 
A 1 153 ASP 153 155 155 ASP ASP A . n 
A 1 154 SER 154 156 156 SER SER A . n 
A 1 155 ARG 155 157 157 ARG ARG A . n 
A 1 156 TYR 156 158 158 TYR TYR A . n 
A 1 157 VAL 157 159 159 VAL VAL A . n 
A 1 158 GLN 158 160 160 GLN GLN A . n 
A 1 159 ALA 159 161 161 ALA ALA A . n 
A 1 160 ASP 160 162 162 ASP ASP A . n 
A 1 161 LEU 161 163 163 LEU LEU A . n 
A 1 162 LYS 162 164 164 LYS LYS A . n 
A 1 163 ILE 163 165 165 ILE ILE A . n 
A 1 164 ALA 164 166 166 ALA ALA A . n 
A 1 165 THR 165 167 167 THR THR A . n 
A 1 166 GLY 166 168 168 GLY GLY A . n 
A 1 167 LEU 167 169 169 LEU LEU A . n 
A 1 168 ILE 168 170 170 ILE ILE A . n 
A 1 169 GLU 169 171 171 GLU GLU A . n 
A 1 170 PRO 170 172 172 PRO PRO A . n 
A 1 171 HIS 171 173 173 HIS HIS A . n 
A 1 172 LEU 172 174 174 LEU LEU A . n 
A 1 173 MET 173 175 175 MET MET A . n 
A 1 174 ALA 174 176 176 ALA ALA A . n 
A 1 175 GLY 175 177 177 GLY GLY A . n 
A 1 176 TYR 176 178 178 TYR TYR A . n 
A 1 177 SER 177 179 179 SER SER A . n 
A 1 178 GLY 178 180 180 GLY GLY A . n 
A 1 179 GLY 179 181 181 GLY GLY A . n 
A 1 180 ARG 180 182 182 ARG ARG A . n 
A 1 181 LYS 181 183 183 LYS LYS A . n 
A 1 182 LEU 182 184 184 LEU LEU A . n 
A 1 183 ILE 183 185 185 ILE ILE A . n 
A 1 184 CYS 184 186 186 CYS CYS A . n 
A 1 185 PRO 185 187 187 PRO PRO A . n 
A 1 186 GLY 186 188 188 GLY GLY A . n 
A 1 187 ILE 187 189 189 ILE ILE A . n 
A 1 188 ALA 188 190 190 ALA ALA A . n 
A 1 189 ALA 189 191 191 ALA ALA A . n 
A 1 190 PHE 190 192 192 PHE PHE A . n 
A 1 191 GLU 191 193 193 GLU GLU A . n 
A 1 192 THR 192 194 194 THR THR A . n 
A 1 193 VAL 193 195 195 VAL VAL A . n 
A 1 194 LYS 194 196 196 LYS LYS A . n 
A 1 195 LEU 195 197 197 LEU LEU A . n 
A 1 196 TRP 196 198 198 TRP TRP A . n 
A 1 197 HIS 197 199 199 HIS HIS A . n 
A 1 198 GLY 198 200 200 GLY GLY A . n 
A 1 199 PRO 199 201 201 PRO PRO A . n 
A 1 200 ARG 200 202 202 ARG ARG A . n 
A 1 201 PHE 201 203 203 PHE PHE A . n 
A 1 202 LEU 202 204 204 LEU LEU A . n 
A 1 203 GLU 203 205 205 GLU GLU A . n 
A 1 204 HIS 204 206 206 HIS HIS A . n 
A 1 205 PRO 205 207 207 PRO PRO A . n 
A 1 206 LEU 206 208 208 LEU LEU A . n 
A 1 207 ALA 207 209 209 ALA ALA A . n 
A 1 208 ASP 208 210 210 ASP ASP A . n 
A 1 209 CYS 209 211 211 CYS CYS A . n 
A 1 210 GLY 210 212 212 GLY GLY A . n 
A 1 211 PHE 211 213 213 PHE PHE A . n 
A 1 212 LEU 212 214 214 LEU LEU A . n 
A 1 213 GLU 213 215 215 GLU GLU A . n 
A 1 214 GLY 214 216 216 GLY GLY A . n 
A 1 215 ASN 215 217 217 ASN ASN A . n 
A 1 216 PRO 216 218 218 PRO PRO A . n 
A 1 217 VAL 217 219 219 VAL VAL A . n 
A 1 218 HIS 218 220 220 HIS HIS A . n 
A 1 219 GLU 219 221 221 GLU GLU A . n 
A 1 220 GLU 220 222 222 GLU GLU A . n 
A 1 221 ASN 221 223 223 ASN ASN A . n 
A 1 222 THR 222 224 224 THR THR A . n 
A 1 223 ARG 223 225 225 ARG ARG A . n 
A 1 224 ILE 224 226 226 ILE ILE A . n 
A 1 225 ALA 225 227 227 ALA ALA A . n 
A 1 226 ARG 226 228 228 ARG ARG A . n 
A 1 227 MET 227 229 229 MET MET A . n 
A 1 228 ALA 228 230 230 ALA ALA A . n 
A 1 229 GLY 229 231 231 GLY GLY A . n 
A 1 230 CYS 230 232 232 CYS CYS A . n 
A 1 231 ASP 231 233 233 ASP ASP A . n 
A 1 232 PHE 232 234 234 PHE PHE A . n 
A 1 233 ILE 233 235 235 ILE ILE A . n 
A 1 234 VAL 234 236 236 VAL VAL A . n 
A 1 235 ASN 235 237 237 ASN ASN A . n 
A 1 236 VAL 236 238 238 VAL VAL A . n 
A 1 237 THR 237 239 239 THR THR A . n 
A 1 238 LEU 238 240 240 LEU LEU A . n 
A 1 239 ASP 239 241 241 ASP ASP A . n 
A 1 240 GLY 240 242 242 GLY GLY A . n 
A 1 241 ALA 241 243 243 ALA ALA A . n 
A 1 242 ARG 242 244 244 ARG ARG A . n 
A 1 243 ARG 243 245 245 ARG ARG A . n 
A 1 244 ILE 244 246 246 ILE ILE A . n 
A 1 245 THR 245 247 247 THR THR A . n 
A 1 246 SER 246 248 248 SER SER A . n 
A 1 247 VAL 247 249 249 VAL VAL A . n 
A 1 248 VAL 248 250 250 VAL VAL A . n 
A 1 249 ALA 249 251 251 ALA ALA A . n 
A 1 250 GLY 250 252 252 GLY GLY A . n 
A 1 251 ASP 251 253 253 ASP ASP A . n 
A 1 252 MET 252 254 254 MET MET A . n 
A 1 253 GLU 253 255 255 GLU GLU A . n 
A 1 254 GLN 254 256 256 GLN GLN A . n 
A 1 255 ALA 255 257 257 ALA ALA A . n 
A 1 256 PHE 256 258 258 PHE PHE A . n 
A 1 257 LEU 257 259 259 LEU LEU A . n 
A 1 258 LYS 258 260 260 LYS LYS A . n 
A 1 259 GLY 259 261 261 GLY GLY A . n 
A 1 260 VAL 260 262 262 VAL VAL A . n 
A 1 261 ALA 261 263 263 ALA ALA A . n 
A 1 262 PHE 262 264 264 PHE PHE A . n 
A 1 263 VAL 263 265 265 VAL VAL A . n 
A 1 264 GLU 264 266 266 GLU GLU A . n 
A 1 265 THR 265 267 267 THR THR A . n 
A 1 266 VAL 266 268 268 VAL VAL A . n 
A 1 267 VAL 267 269 269 VAL VAL A . n 
A 1 268 LYS 268 270 270 LYS LYS A . n 
A 1 269 ALA 269 271 271 ALA ALA A . n 
A 1 270 ALA 270 272 272 ALA ALA A . n 
A 1 271 VAL 271 273 273 VAL VAL A . n 
A 1 272 PRO 272 274 274 PRO PRO A . n 
A 1 273 ALA 273 275 275 ALA ALA A . n 
A 1 274 PRO 274 276 276 PRO PRO A . n 
A 1 275 VAL 275 277 277 VAL VAL A . n 
A 1 276 ASP 276 278 278 ASP ASP A . n 
A 1 277 VAL 277 279 279 VAL VAL A . n 
A 1 278 VAL 278 280 280 VAL VAL A . n 
A 1 279 VAL 279 281 281 VAL VAL A . n 
A 1 280 THR 280 282 282 THR THR A . n 
A 1 281 SER 281 283 283 SER SER A . n 
A 1 282 SER 282 284 284 SER SER A . n 
A 1 283 ALA 283 285 285 ALA ALA A . n 
A 1 284 GLY 284 286 286 GLY GLY A . n 
A 1 285 HIS 285 287 287 HIS HIS A . n 
A 1 286 PRO 286 288 288 PRO PRO A . n 
A 1 287 LEU 287 289 289 LEU LEU A . n 
A 1 288 ASP 288 290 290 ASP ASP A . n 
A 1 289 LEU 289 291 291 LEU LEU A . n 
A 1 290 THR 290 292 292 THR THR A . n 
A 1 291 PHE 291 293 293 PHE PHE A . n 
A 1 292 TYR 292 294 294 TYR TYR A . n 
A 1 293 GLN 293 295 295 GLN GLN A . n 
A 1 294 ALA 294 296 296 ALA ALA A . n 
A 1 295 VAL 295 297 297 VAL VAL A . n 
A 1 296 LYS 296 298 298 LYS LYS A . n 
A 1 297 GLY 297 299 299 GLY GLY A . n 
A 1 298 LEU 298 300 300 LEU LEU A . n 
A 1 299 THR 299 301 301 THR THR A . n 
A 1 300 GLY 300 302 302 GLY GLY A . n 
A 1 301 ALA 301 303 303 ALA ALA A . n 
A 1 302 LEU 302 304 304 LEU LEU A . n 
A 1 303 PRO 303 305 305 PRO PRO A . n 
A 1 304 ILE 304 306 306 ILE ILE A . n 
A 1 305 VAL 305 307 307 VAL VAL A . n 
A 1 306 LYS 306 308 308 LYS LYS A . n 
A 1 307 PRO 307 309 309 PRO PRO A . n 
A 1 308 GLY 308 310 310 GLY GLY A . n 
A 1 309 GLY 309 311 311 GLY GLY A . n 
A 1 310 THR 310 312 312 THR THR A . n 
A 1 311 ILE 311 313 313 ILE ILE A . n 
A 1 312 VAL 312 314 314 VAL VAL A . n 
A 1 313 ILE 313 315 315 ILE ILE A . n 
A 1 314 ALA 314 316 316 ALA ALA A . n 
A 1 315 ALA 315 317 317 ALA ALA A . n 
A 1 316 ALA 316 318 318 ALA ALA A . n 
A 1 317 LEU 317 319 319 LEU LEU A . n 
A 1 318 ALA 318 320 320 ALA ALA A . n 
A 1 319 GLU 319 321 321 GLU GLU A . n 
A 1 320 GLY 320 322 322 GLY GLY A . n 
A 1 321 LEU 321 323 323 LEU LEU A . n 
A 1 322 GLY 322 324 324 GLY GLY A . n 
A 1 323 SER 323 325 325 SER SER A . n 
A 1 324 PRO 324 326 326 PRO PRO A . n 
A 1 325 GLU 325 327 327 GLU GLU A . n 
A 1 326 PHE 326 328 328 PHE PHE A . n 
A 1 327 GLN 327 329 329 GLN GLN A . n 
A 1 328 SER 328 330 330 SER SER A . n 
A 1 329 LEU 329 331 331 LEU LEU A . n 
A 1 330 PHE 330 332 332 PHE PHE A . n 
A 1 331 GLU 331 333 333 GLU GLU A . n 
A 1 332 GLU 332 334 334 GLU GLU A . n 
A 1 333 HIS 333 335 335 HIS HIS A . n 
A 1 334 PRO 334 336 336 PRO PRO A . n 
A 1 335 THR 335 337 337 THR THR A . n 
A 1 336 LEU 336 338 338 LEU LEU A . n 
A 1 337 GLU 337 339 339 GLU GLU A . n 
A 1 338 GLY 338 340 340 GLY GLY A . n 
A 1 339 PHE 339 341 341 PHE PHE A . n 
A 1 340 MET 340 342 342 MET MET A . n 
A 1 341 GLU 341 343 343 GLU GLU A . n 
A 1 342 ALA 342 344 344 ALA ALA A . n 
A 1 343 ILE 343 345 345 ILE ILE A . n 
A 1 344 LEU 344 346 346 LEU LEU A . n 
A 1 345 LYS 345 347 347 LYS LYS A . n 
A 1 346 GLU 346 348 348 GLU GLU A . n 
A 1 347 GLU 347 349 349 GLU GLU A . n 
A 1 348 SER 348 350 350 SER SER A . n 
A 1 349 PHE 349 351 351 PHE PHE A . n 
A 1 350 THR 350 352 352 THR THR A . n 
A 1 351 VAL 351 353 353 VAL VAL A . n 
A 1 352 ASP 352 354 354 ASP ASP A . n 
A 1 353 GLN 353 355 355 GLN GLN A . n 
A 1 354 TRP 354 356 356 TRP TRP A . n 
A 1 355 GLN 355 357 357 GLN GLN A . n 
A 1 356 LEU 356 358 358 LEU LEU A . n 
A 1 357 GLU 357 359 359 GLU GLU A . n 
A 1 358 GLU 358 360 360 GLU GLU A . n 
A 1 359 LEU 359 361 361 LEU LEU A . n 
A 1 360 ALA 360 362 362 ALA ALA A . n 
A 1 361 LYS 361 363 363 LYS LYS A . n 
A 1 362 VAL 362 364 364 VAL VAL A . n 
A 1 363 ARG 363 365 365 ARG ARG A . n 
A 1 364 ARG 364 366 366 ARG ARG A . n 
A 1 365 LYS 365 367 367 LYS LYS A . n 
A 1 366 ALA 366 368 368 ALA ALA A . n 
A 1 367 ARG 367 369 369 ARG ARG A . n 
A 1 368 VAL 368 370 370 VAL VAL A . n 
A 1 369 LYS 369 371 371 LYS LYS A . n 
A 1 370 PHE 370 372 372 PHE PHE A . n 
A 1 371 VAL 371 373 373 VAL VAL A . n 
A 1 372 SER 372 374 374 SER SER A . n 
A 1 373 ASP 373 375 375 ASP ASP A . n 
A 1 374 GLY 374 376 376 GLY GLY A . n 
A 1 375 VAL 375 377 377 VAL VAL A . n 
A 1 376 PRO 376 378 378 PRO PRO A . n 
A 1 377 ALA 377 379 379 ALA ALA A . n 
A 1 378 ALA 378 380 380 ALA ALA A . n 
A 1 379 VAL 379 381 381 VAL VAL A . n 
A 1 380 LEU 380 382 382 LEU LEU A . n 
A 1 381 SER 381 383 383 SER SER A . n 
A 1 382 ARG 382 384 384 ARG ARG A . n 
A 1 383 CYS 383 385 385 CYS CYS A . n 
A 1 384 HIS 384 386 386 HIS HIS A . n 
A 1 385 VAL 385 387 387 VAL VAL A . n 
A 1 386 GLU 386 388 388 GLU GLU A . n 
A 1 387 PRO 387 389 389 PRO PRO A . n 
A 1 388 VAL 388 390 390 VAL VAL A . n 
A 1 389 ALA 389 391 391 ALA ALA A . n 
A 1 390 THR 390 392 392 THR THR A . n 
A 1 391 VAL 391 393 393 VAL VAL A . n 
A 1 392 GLU 392 394 394 GLU GLU A . n 
A 1 393 LEU 393 395 395 LEU LEU A . n 
A 1 394 ALA 394 396 396 ALA ALA A . n 
A 1 395 VAL 395 397 397 VAL VAL A . n 
A 1 396 ALA 396 398 398 ALA ALA A . n 
A 1 397 GLN 397 399 399 GLN GLN A . n 
A 1 398 ALA 398 400 400 ALA ALA A . n 
A 1 399 LEU 399 401 401 LEU LEU A . n 
A 1 400 GLU 400 402 402 GLU GLU A . n 
A 1 401 GLN 401 403 403 GLN GLN A . n 
A 1 402 TYR 402 404 404 TYR TYR A . n 
A 1 403 GLY 403 405 405 GLY GLY A . n 
A 1 404 PRO 404 406 406 PRO PRO A . n 
A 1 405 GLU 405 407 407 GLU GLU A . n 
A 1 406 ALA 406 408 408 ALA ALA A . n 
A 1 407 ARG 407 409 409 ARG ARG A . n 
A 1 408 VAL 408 410 410 VAL VAL A . n 
A 1 409 ALA 409 411 411 ALA ALA A . n 
A 1 410 VAL 410 412 412 VAL VAL A . n 
A 1 411 ILE 411 413 413 ILE ILE A . n 
A 1 412 PRO 412 414 414 PRO PRO A . n 
A 1 413 LYS 413 415 415 LYS LYS A . n 
A 1 414 GLY 414 416 416 GLY GLY A . n 
A 1 415 PRO 415 417 417 PRO PRO A . n 
A 1 416 TYR 416 418 418 TYR TYR A . n 
A 1 417 VAL 417 419 419 VAL VAL A . n 
A 1 418 LEU 418 420 420 LEU LEU A . n 
A 1 419 PRO 419 421 421 PRO PRO A . n 
A 1 420 VAL 420 422 422 VAL VAL A . n 
A 1 421 VAL 421 423 423 VAL VAL A . n 
A 1 422 ASP 422 424 424 ASP ASP A . n 
A 1 423 PRO 423 425 425 PRO PRO A . n 
A 1 424 THR 424 426 426 THR THR A . n 
A 1 425 LEU 425 427 427 LEU LEU A . n 
B 1 1   ARG 1   3   3   ARG ARG B . n 
B 1 2   VAL 2   4   4   VAL VAL B . n 
B 1 3   THR 3   5   5   THR THR B . n 
B 1 4   LEU 4   6   6   LEU LEU B . n 
B 1 5   ASP 5   7   7   ASP ASP B . n 
B 1 6   TYR 6   8   8   TYR TYR B . n 
B 1 7   GLY 7   9   9   GLY GLY B . n 
B 1 8   LYS 8   10  10  LYS LYS B . n 
B 1 9   THR 9   11  11  THR THR B . n 
B 1 10  GLY 10  12  12  GLY GLY B . n 
B 1 11  LEU 11  13  13  LEU LEU B . n 
B 1 12  ASN 12  14  14  ASN ASN B . n 
B 1 13  VAL 13  15  15  VAL VAL B . n 
B 1 14  ASP 14  16  16  ASP ASP B . n 
B 1 15  LEU 15  17  17  LEU LEU B . n 
B 1 16  PRO 16  18  18  PRO PRO B . n 
B 1 17  ASP 17  19  19  ASP ASP B . n 
B 1 18  ASP 18  20  20  ASP ASP B . n 
B 1 19  ARG 19  21  21  ARG ARG B . n 
B 1 20  THR 20  22  22  THR THR B . n 
B 1 21  LEU 21  23  23  LEU LEU B . n 
B 1 22  PRO 22  24  24  PRO PRO B . n 
B 1 23  PRO 23  25  25  PRO PRO B . n 
B 1 24  LEU 24  26  26  LEU LEU B . n 
B 1 25  THR 25  27  27  THR THR B . n 
B 1 26  ILE 26  28  28  ILE ILE B . n 
B 1 27  ARG 27  29  29  ARG ARG B . n 
B 1 28  PRO 28  30  30  PRO PRO B . n 
B 1 29  ALA 29  31  31  ALA ALA B . n 
B 1 30  PRO 30  32  32  PRO PRO B . n 
B 1 31  PRO 31  33  33  PRO PRO B . n 
B 1 32  LEU 32  34  34  LEU LEU B . n 
B 1 33  ASP 33  35  35  ASP ASP B . n 
B 1 34  ASP 34  36  36  ASP ASP B . n 
B 1 35  PRO 35  37  37  PRO PRO B . n 
B 1 36  GLU 36  38  38  GLU GLU B . n 
B 1 37  ALA 37  39  39  ALA ALA B . n 
B 1 38  GLU 38  40  40  GLU GLU B . n 
B 1 39  VAL 39  41  41  VAL VAL B . n 
B 1 40  VAL 40  42  42  VAL VAL B . n 
B 1 41  ARG 41  43  43  ARG ARG B . n 
B 1 42  CYS 42  44  44  CYS CYS B . n 
B 1 43  LEU 43  45  45  LEU LEU B . n 
B 1 44  ALA 44  46  46  ALA ALA B . n 
B 1 45  GLU 45  47  47  GLU GLU B . n 
B 1 46  PRO 46  48  48  PRO PRO B . n 
B 1 47  ILE 47  49  49  ILE ILE B . n 
B 1 48  GLY 48  50  50  GLY GLY B . n 
B 1 49  SER 49  51  51  SER SER B . n 
B 1 50  PRO 50  52  52  PRO PRO B . n 
B 1 51  PRO 51  53  53  PRO PRO B . n 
B 1 52  LEU 52  54  54  LEU LEU B . n 
B 1 53  LEU 53  55  55  LEU LEU B . n 
B 1 54  ASP 54  56  56  ASP ASP B . n 
B 1 55  LEU 55  57  57  LEU LEU B . n 
B 1 56  ALA 56  58  58  ALA ALA B . n 
B 1 57  ARG 57  59  59  ARG ARG B . n 
B 1 58  GLY 58  60  60  GLY GLY B . n 
B 1 59  LYS 59  61  61  LYS LYS B . n 
B 1 60  ARG 60  62  62  ARG ARG B . n 
B 1 61  SER 61  63  63  SER SER B . n 
B 1 62  ALA 62  64  64  ALA ALA B . n 
B 1 63  CYS 63  65  65  CYS CYS B . n 
B 1 64  ILE 64  66  66  ILE ILE B . n 
B 1 65  LEU 65  67  67  LEU LEU B . n 
B 1 66  VAL 66  68  68  VAL VAL B . n 
B 1 67  CYS 67  69  69  CYS CYS B . n 
B 1 68  ASP 68  70  70  ASP ASP B . n 
B 1 69  ILE 69  71  71  ILE ILE B . n 
B 1 70  THR 70  72  72  THR THR B . n 
B 1 71  ARG 71  73  73  ARG ARG B . n 
B 1 72  PRO 72  74  74  PRO PRO B . n 
B 1 73  VAL 73  75  75  VAL VAL B . n 
B 1 74  PRO 74  76  76  PRO PRO B . n 
B 1 75  ASN 75  77  77  ASN ASN B . n 
B 1 76  PRO 76  78  78  PRO PRO B . n 
B 1 77  VAL 77  79  79  VAL VAL B . n 
B 1 78  LEU 78  80  80  LEU LEU B . n 
B 1 79  LEU 79  81  81  LEU LEU B . n 
B 1 80  ARG 80  82  82  ARG ARG B . n 
B 1 81  PRO 81  83  83  PRO PRO B . n 
B 1 82  ILE 82  84  84  ILE ILE B . n 
B 1 83  LEU 83  85  85  LEU LEU B . n 
B 1 84  ARG 84  86  86  ARG ARG B . n 
B 1 85  THR 85  87  87  THR THR B . n 
B 1 86  LEU 86  88  88  LEU LEU B . n 
B 1 87  HIS 87  89  89  HIS HIS B . n 
B 1 88  ALA 88  90  90  ALA ALA B . n 
B 1 89  ALA 89  91  91  ALA ALA B . n 
B 1 90  GLY 90  92  92  GLY GLY B . n 
B 1 91  LEU 91  93  93  LEU LEU B . n 
B 1 92  ALA 92  94  94  ALA ALA B . n 
B 1 93  THR 93  95  95  THR THR B . n 
B 1 94  GLN 94  96  96  GLN GLN B . n 
B 1 95  ASP 95  97  97  ASP ASP B . n 
B 1 96  ILE 96  98  98  ILE ILE B . n 
B 1 97  LEU 97  99  99  LEU LEU B . n 
B 1 98  ILE 98  100 100 ILE ILE B . n 
B 1 99  LEU 99  101 101 LEU LEU B . n 
B 1 100 VAL 100 102 102 VAL VAL B . n 
B 1 101 ALA 101 103 103 ALA ALA B . n 
B 1 102 THR 102 104 104 THR THR B . n 
B 1 103 GLY 103 105 105 GLY GLY B . n 
B 1 104 LEU 104 106 106 LEU LEU B . n 
B 1 105 HIS 105 107 107 HIS HIS B . n 
B 1 106 ARG 106 108 108 ARG ARG B . n 
B 1 107 PRO 107 109 109 PRO PRO B . n 
B 1 108 SER 108 110 110 SER SER B . n 
B 1 109 THR 109 111 111 THR THR B . n 
B 1 110 PRO 110 112 112 PRO PRO B . n 
B 1 111 ALA 111 113 113 ALA ALA B . n 
B 1 112 GLU 112 114 114 GLU GLU B . n 
B 1 113 LYS 113 115 115 LYS LYS B . n 
B 1 114 VAL 114 116 116 VAL VAL B . n 
B 1 115 GLU 115 117 117 GLU GLU B . n 
B 1 116 MET 116 118 118 MET MET B . n 
B 1 117 LEU 117 119 119 LEU LEU B . n 
B 1 118 SER 118 120 120 SER SER B . n 
B 1 119 GLU 119 121 121 GLU GLU B . n 
B 1 120 GLU 120 122 122 GLU GLU B . n 
B 1 121 ILE 121 123 123 ILE ILE B . n 
B 1 122 ALA 122 124 124 ALA ALA B . n 
B 1 123 ARG 123 125 125 ARG ARG B . n 
B 1 124 THR 124 126 126 THR THR B . n 
B 1 125 TYR 125 127 127 TYR TYR B . n 
B 1 126 ARG 126 128 128 ARG ARG B . n 
B 1 127 VAL 127 129 129 VAL VAL B . n 
B 1 128 GLU 128 130 130 GLU GLU B . n 
B 1 129 ASP 129 131 131 ASP ASP B . n 
B 1 130 HIS 130 132 132 HIS HIS B . n 
B 1 131 TYR 131 133 133 TYR TYR B . n 
B 1 132 GLY 132 134 134 GLY GLY B . n 
B 1 133 THR 133 135 135 THR THR B . n 
B 1 134 ARG 134 136 136 ARG ARG B . n 
B 1 135 LEU 135 137 137 LEU LEU B . n 
B 1 136 GLU 136 138 138 GLU GLU B . n 
B 1 137 GLU 137 139 139 GLU GLU B . n 
B 1 138 HIS 138 140 140 HIS HIS B . n 
B 1 139 THR 139 141 141 THR THR B . n 
B 1 140 TYR 140 142 142 TYR TYR B . n 
B 1 141 LEU 141 143 143 LEU LEU B . n 
B 1 142 GLY 142 144 144 GLY GLY B . n 
B 1 143 THR 143 145 145 THR THR B . n 
B 1 144 THR 144 146 146 THR THR B . n 
B 1 145 PRO 145 147 147 PRO PRO B . n 
B 1 146 ASN 146 148 148 ASN ASN B . n 
B 1 147 GLY 147 149 149 GLY GLY B . n 
B 1 148 VAL 148 150 150 VAL VAL B . n 
B 1 149 PRO 149 151 151 PRO PRO B . n 
B 1 150 ALA 150 152 152 ALA ALA B . n 
B 1 151 TRP 151 153 153 TRP TRP B . n 
B 1 152 ILE 152 154 154 ILE ILE B . n 
B 1 153 ASP 153 155 155 ASP ASP B . n 
B 1 154 SER 154 156 156 SER SER B . n 
B 1 155 ARG 155 157 157 ARG ARG B . n 
B 1 156 TYR 156 158 158 TYR TYR B . n 
B 1 157 VAL 157 159 159 VAL VAL B . n 
B 1 158 GLN 158 160 160 GLN GLN B . n 
B 1 159 ALA 159 161 161 ALA ALA B . n 
B 1 160 ASP 160 162 162 ASP ASP B . n 
B 1 161 LEU 161 163 163 LEU LEU B . n 
B 1 162 LYS 162 164 164 LYS LYS B . n 
B 1 163 ILE 163 165 165 ILE ILE B . n 
B 1 164 ALA 164 166 166 ALA ALA B . n 
B 1 165 THR 165 167 167 THR THR B . n 
B 1 166 GLY 166 168 168 GLY GLY B . n 
B 1 167 LEU 167 169 169 LEU LEU B . n 
B 1 168 ILE 168 170 170 ILE ILE B . n 
B 1 169 GLU 169 171 171 GLU GLU B . n 
B 1 170 PRO 170 172 172 PRO PRO B . n 
B 1 171 HIS 171 173 173 HIS HIS B . n 
B 1 172 LEU 172 174 174 LEU LEU B . n 
B 1 173 MET 173 175 175 MET MET B . n 
B 1 174 ALA 174 176 176 ALA ALA B . n 
B 1 175 GLY 175 177 177 GLY GLY B . n 
B 1 176 TYR 176 178 178 TYR TYR B . n 
B 1 177 SER 177 179 179 SER SER B . n 
B 1 178 GLY 178 180 180 GLY GLY B . n 
B 1 179 GLY 179 181 181 GLY GLY B . n 
B 1 180 ARG 180 182 182 ARG ARG B . n 
B 1 181 LYS 181 183 183 LYS LYS B . n 
B 1 182 LEU 182 184 184 LEU LEU B . n 
B 1 183 ILE 183 185 185 ILE ILE B . n 
B 1 184 CYS 184 186 186 CYS CYS B . n 
B 1 185 PRO 185 187 187 PRO PRO B . n 
B 1 186 GLY 186 188 188 GLY GLY B . n 
B 1 187 ILE 187 189 189 ILE ILE B . n 
B 1 188 ALA 188 190 190 ALA ALA B . n 
B 1 189 ALA 189 191 191 ALA ALA B . n 
B 1 190 PHE 190 192 192 PHE PHE B . n 
B 1 191 GLU 191 193 193 GLU GLU B . n 
B 1 192 THR 192 194 194 THR THR B . n 
B 1 193 VAL 193 195 195 VAL VAL B . n 
B 1 194 LYS 194 196 196 LYS LYS B . n 
B 1 195 LEU 195 197 197 LEU LEU B . n 
B 1 196 TRP 196 198 198 TRP TRP B . n 
B 1 197 HIS 197 199 199 HIS HIS B . n 
B 1 198 GLY 198 200 200 GLY GLY B . n 
B 1 199 PRO 199 201 201 PRO PRO B . n 
B 1 200 ARG 200 202 202 ARG ARG B . n 
B 1 201 PHE 201 203 203 PHE PHE B . n 
B 1 202 LEU 202 204 204 LEU LEU B . n 
B 1 203 GLU 203 205 205 GLU GLU B . n 
B 1 204 HIS 204 206 206 HIS HIS B . n 
B 1 205 PRO 205 207 207 PRO PRO B . n 
B 1 206 LEU 206 208 208 LEU LEU B . n 
B 1 207 ALA 207 209 209 ALA ALA B . n 
B 1 208 ASP 208 210 210 ASP ASP B . n 
B 1 209 CYS 209 211 211 CYS CYS B . n 
B 1 210 GLY 210 212 212 GLY GLY B . n 
B 1 211 PHE 211 213 213 PHE PHE B . n 
B 1 212 LEU 212 214 214 LEU LEU B . n 
B 1 213 GLU 213 215 215 GLU GLU B . n 
B 1 214 GLY 214 216 216 GLY GLY B . n 
B 1 215 ASN 215 217 217 ASN ASN B . n 
B 1 216 PRO 216 218 218 PRO PRO B . n 
B 1 217 VAL 217 219 219 VAL VAL B . n 
B 1 218 HIS 218 220 220 HIS HIS B . n 
B 1 219 GLU 219 221 221 GLU GLU B . n 
B 1 220 GLU 220 222 222 GLU GLU B . n 
B 1 221 ASN 221 223 223 ASN ASN B . n 
B 1 222 THR 222 224 224 THR THR B . n 
B 1 223 ARG 223 225 225 ARG ARG B . n 
B 1 224 ILE 224 226 226 ILE ILE B . n 
B 1 225 ALA 225 227 227 ALA ALA B . n 
B 1 226 ARG 226 228 228 ARG ARG B . n 
B 1 227 MET 227 229 229 MET MET B . n 
B 1 228 ALA 228 230 230 ALA ALA B . n 
B 1 229 GLY 229 231 231 GLY GLY B . n 
B 1 230 CYS 230 232 232 CYS CYS B . n 
B 1 231 ASP 231 233 233 ASP ASP B . n 
B 1 232 PHE 232 234 234 PHE PHE B . n 
B 1 233 ILE 233 235 235 ILE ILE B . n 
B 1 234 VAL 234 236 236 VAL VAL B . n 
B 1 235 ASN 235 237 237 ASN ASN B . n 
B 1 236 VAL 236 238 238 VAL VAL B . n 
B 1 237 THR 237 239 239 THR THR B . n 
B 1 238 LEU 238 240 240 LEU LEU B . n 
B 1 239 ASP 239 241 241 ASP ASP B . n 
B 1 240 GLY 240 242 242 GLY GLY B . n 
B 1 241 ALA 241 243 243 ALA ALA B . n 
B 1 242 ARG 242 244 244 ARG ARG B . n 
B 1 243 ARG 243 245 245 ARG ARG B . n 
B 1 244 ILE 244 246 246 ILE ILE B . n 
B 1 245 THR 245 247 247 THR THR B . n 
B 1 246 SER 246 248 248 SER SER B . n 
B 1 247 VAL 247 249 249 VAL VAL B . n 
B 1 248 VAL 248 250 250 VAL VAL B . n 
B 1 249 ALA 249 251 251 ALA ALA B . n 
B 1 250 GLY 250 252 252 GLY GLY B . n 
B 1 251 ASP 251 253 253 ASP ASP B . n 
B 1 252 MET 252 254 254 MET MET B . n 
B 1 253 GLU 253 255 255 GLU GLU B . n 
B 1 254 GLN 254 256 256 GLN GLN B . n 
B 1 255 ALA 255 257 257 ALA ALA B . n 
B 1 256 PHE 256 258 258 PHE PHE B . n 
B 1 257 LEU 257 259 259 LEU LEU B . n 
B 1 258 LYS 258 260 260 LYS LYS B . n 
B 1 259 GLY 259 261 261 GLY GLY B . n 
B 1 260 VAL 260 262 262 VAL VAL B . n 
B 1 261 ALA 261 263 263 ALA ALA B . n 
B 1 262 PHE 262 264 264 PHE PHE B . n 
B 1 263 VAL 263 265 265 VAL VAL B . n 
B 1 264 GLU 264 266 266 GLU GLU B . n 
B 1 265 THR 265 267 267 THR THR B . n 
B 1 266 VAL 266 268 268 VAL VAL B . n 
B 1 267 VAL 267 269 269 VAL VAL B . n 
B 1 268 LYS 268 270 270 LYS LYS B . n 
B 1 269 ALA 269 271 271 ALA ALA B . n 
B 1 270 ALA 270 272 272 ALA ALA B . n 
B 1 271 VAL 271 273 273 VAL VAL B . n 
B 1 272 PRO 272 274 274 PRO PRO B . n 
B 1 273 ALA 273 275 275 ALA ALA B . n 
B 1 274 PRO 274 276 276 PRO PRO B . n 
B 1 275 VAL 275 277 277 VAL VAL B . n 
B 1 276 ASP 276 278 278 ASP ASP B . n 
B 1 277 VAL 277 279 279 VAL VAL B . n 
B 1 278 VAL 278 280 280 VAL VAL B . n 
B 1 279 VAL 279 281 281 VAL VAL B . n 
B 1 280 THR 280 282 282 THR THR B . n 
B 1 281 SER 281 283 283 SER SER B . n 
B 1 282 SER 282 284 284 SER SER B . n 
B 1 283 ALA 283 285 285 ALA ALA B . n 
B 1 284 GLY 284 286 286 GLY GLY B . n 
B 1 285 HIS 285 287 287 HIS HIS B . n 
B 1 286 PRO 286 288 288 PRO PRO B . n 
B 1 287 LEU 287 289 289 LEU LEU B . n 
B 1 288 ASP 288 290 290 ASP ASP B . n 
B 1 289 LEU 289 291 291 LEU LEU B . n 
B 1 290 THR 290 292 292 THR THR B . n 
B 1 291 PHE 291 293 293 PHE PHE B . n 
B 1 292 TYR 292 294 294 TYR TYR B . n 
B 1 293 GLN 293 295 295 GLN GLN B . n 
B 1 294 ALA 294 296 296 ALA ALA B . n 
B 1 295 VAL 295 297 297 VAL VAL B . n 
B 1 296 LYS 296 298 298 LYS LYS B . n 
B 1 297 GLY 297 299 299 GLY GLY B . n 
B 1 298 LEU 298 300 300 LEU LEU B . n 
B 1 299 THR 299 301 301 THR THR B . n 
B 1 300 GLY 300 302 302 GLY GLY B . n 
B 1 301 ALA 301 303 303 ALA ALA B . n 
B 1 302 LEU 302 304 304 LEU LEU B . n 
B 1 303 PRO 303 305 305 PRO PRO B . n 
B 1 304 ILE 304 306 306 ILE ILE B . n 
B 1 305 VAL 305 307 307 VAL VAL B . n 
B 1 306 LYS 306 308 308 LYS LYS B . n 
B 1 307 PRO 307 309 309 PRO PRO B . n 
B 1 308 GLY 308 310 310 GLY GLY B . n 
B 1 309 GLY 309 311 311 GLY GLY B . n 
B 1 310 THR 310 312 312 THR THR B . n 
B 1 311 ILE 311 313 313 ILE ILE B . n 
B 1 312 VAL 312 314 314 VAL VAL B . n 
B 1 313 ILE 313 315 315 ILE ILE B . n 
B 1 314 ALA 314 316 316 ALA ALA B . n 
B 1 315 ALA 315 317 317 ALA ALA B . n 
B 1 316 ALA 316 318 318 ALA ALA B . n 
B 1 317 LEU 317 319 319 LEU LEU B . n 
B 1 318 ALA 318 320 320 ALA ALA B . n 
B 1 319 GLU 319 321 321 GLU GLU B . n 
B 1 320 GLY 320 322 322 GLY GLY B . n 
B 1 321 LEU 321 323 323 LEU LEU B . n 
B 1 322 GLY 322 324 324 GLY GLY B . n 
B 1 323 SER 323 325 325 SER SER B . n 
B 1 324 PRO 324 326 326 PRO PRO B . n 
B 1 325 GLU 325 327 327 GLU GLU B . n 
B 1 326 PHE 326 328 328 PHE PHE B . n 
B 1 327 GLN 327 329 329 GLN GLN B . n 
B 1 328 SER 328 330 330 SER SER B . n 
B 1 329 LEU 329 331 331 LEU LEU B . n 
B 1 330 PHE 330 332 332 PHE PHE B . n 
B 1 331 GLU 331 333 333 GLU GLU B . n 
B 1 332 GLU 332 334 334 GLU GLU B . n 
B 1 333 HIS 333 335 335 HIS HIS B . n 
B 1 334 PRO 334 336 336 PRO PRO B . n 
B 1 335 THR 335 337 337 THR THR B . n 
B 1 336 LEU 336 338 338 LEU LEU B . n 
B 1 337 GLU 337 339 339 GLU GLU B . n 
B 1 338 GLY 338 340 340 GLY GLY B . n 
B 1 339 PHE 339 341 341 PHE PHE B . n 
B 1 340 MET 340 342 342 MET MET B . n 
B 1 341 GLU 341 343 343 GLU GLU B . n 
B 1 342 ALA 342 344 344 ALA ALA B . n 
B 1 343 ILE 343 345 345 ILE ILE B . n 
B 1 344 LEU 344 346 346 LEU LEU B . n 
B 1 345 LYS 345 347 347 LYS LYS B . n 
B 1 346 GLU 346 348 348 GLU GLU B . n 
B 1 347 GLU 347 349 349 GLU GLU B . n 
B 1 348 SER 348 350 350 SER SER B . n 
B 1 349 PHE 349 351 351 PHE PHE B . n 
B 1 350 THR 350 352 352 THR THR B . n 
B 1 351 VAL 351 353 353 VAL VAL B . n 
B 1 352 ASP 352 354 354 ASP ASP B . n 
B 1 353 GLN 353 355 355 GLN GLN B . n 
B 1 354 TRP 354 356 356 TRP TRP B . n 
B 1 355 GLN 355 357 357 GLN GLN B . n 
B 1 356 LEU 356 358 358 LEU LEU B . n 
B 1 357 GLU 357 359 359 GLU GLU B . n 
B 1 358 GLU 358 360 360 GLU GLU B . n 
B 1 359 LEU 359 361 361 LEU LEU B . n 
B 1 360 ALA 360 362 362 ALA ALA B . n 
B 1 361 LYS 361 363 363 LYS LYS B . n 
B 1 362 VAL 362 364 364 VAL VAL B . n 
B 1 363 ARG 363 365 365 ARG ARG B . n 
B 1 364 ARG 364 366 366 ARG ARG B . n 
B 1 365 LYS 365 367 367 LYS LYS B . n 
B 1 366 ALA 366 368 368 ALA ALA B . n 
B 1 367 ARG 367 369 369 ARG ARG B . n 
B 1 368 VAL 368 370 370 VAL VAL B . n 
B 1 369 LYS 369 371 371 LYS LYS B . n 
B 1 370 PHE 370 372 372 PHE PHE B . n 
B 1 371 VAL 371 373 373 VAL VAL B . n 
B 1 372 SER 372 374 374 SER SER B . n 
B 1 373 ASP 373 375 375 ASP ASP B . n 
B 1 374 GLY 374 376 376 GLY GLY B . n 
B 1 375 VAL 375 377 377 VAL VAL B . n 
B 1 376 PRO 376 378 378 PRO PRO B . n 
B 1 377 ALA 377 379 379 ALA ALA B . n 
B 1 378 ALA 378 380 380 ALA ALA B . n 
B 1 379 VAL 379 381 381 VAL VAL B . n 
B 1 380 LEU 380 382 382 LEU LEU B . n 
B 1 381 SER 381 383 383 SER SER B . n 
B 1 382 ARG 382 384 384 ARG ARG B . n 
B 1 383 CYS 383 385 385 CYS CYS B . n 
B 1 384 HIS 384 386 386 HIS HIS B . n 
B 1 385 VAL 385 387 387 VAL VAL B . n 
B 1 386 GLU 386 388 388 GLU GLU B . n 
B 1 387 PRO 387 389 389 PRO PRO B . n 
B 1 388 VAL 388 390 390 VAL VAL B . n 
B 1 389 ALA 389 391 391 ALA ALA B . n 
B 1 390 THR 390 392 392 THR THR B . n 
B 1 391 VAL 391 393 393 VAL VAL B . n 
B 1 392 GLU 392 394 394 GLU GLU B . n 
B 1 393 LEU 393 395 395 LEU LEU B . n 
B 1 394 ALA 394 396 396 ALA ALA B . n 
B 1 395 VAL 395 397 397 VAL VAL B . n 
B 1 396 ALA 396 398 398 ALA ALA B . n 
B 1 397 GLN 397 399 399 GLN GLN B . n 
B 1 398 ALA 398 400 400 ALA ALA B . n 
B 1 399 LEU 399 401 401 LEU LEU B . n 
B 1 400 GLU 400 402 402 GLU GLU B . n 
B 1 401 GLN 401 403 403 GLN GLN B . n 
B 1 402 TYR 402 404 404 TYR TYR B . n 
B 1 403 GLY 403 405 405 GLY GLY B . n 
B 1 404 PRO 404 406 406 PRO PRO B . n 
B 1 405 GLU 405 407 407 GLU GLU B . n 
B 1 406 ALA 406 408 408 ALA ALA B . n 
B 1 407 ARG 407 409 409 ARG ARG B . n 
B 1 408 VAL 408 410 410 VAL VAL B . n 
B 1 409 ALA 409 411 411 ALA ALA B . n 
B 1 410 VAL 410 412 412 VAL VAL B . n 
B 1 411 ILE 411 413 413 ILE ILE B . n 
B 1 412 PRO 412 414 414 PRO PRO B . n 
B 1 413 LYS 413 415 415 LYS LYS B . n 
B 1 414 GLY 414 416 416 GLY GLY B . n 
B 1 415 PRO 415 417 417 PRO PRO B . n 
B 1 416 TYR 416 418 418 TYR TYR B . n 
B 1 417 VAL 417 419 419 VAL VAL B . n 
B 1 418 LEU 418 420 420 LEU LEU B . n 
B 1 419 PRO 419 421 421 PRO PRO B . n 
B 1 420 VAL 420 422 422 VAL VAL B . n 
B 1 421 VAL 421 423 423 VAL VAL B . n 
B 1 422 ASP 422 424 424 ASP ASP B . n 
B 1 423 PRO 423 425 425 PRO PRO B . n 
B 1 424 THR 424 426 426 THR THR B . n 
B 1 425 LEU 425 427 ?   ?   ?   B . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 4EY ? ? 4EY ? ? 'SUBJECT OF INVESTIGATION' ? 
2 LAC ? ? LAC ? ? 'SUBJECT OF INVESTIGATION' ? 
3 NI  ? ? NI  ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
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 
C 2 EDO 1   501  505 EDO EDO A . 
D 2 EDO 1   502  506 EDO EDO A . 
E 3 4EY 1   503  507 4EY 4EY A . 
F 4 PEG 1   504  504 PEG PEG A . 
G 5 LAC 1   505  502 LAC LAC A . 
H 6 NI  1   506  2   NI  NI  A . 
I 2 EDO 1   701  701 EDO EDO B . 
J 3 4EY 1   702  702 4EY 4EY B . 
K 4 PEG 1   703  503 PEG PEG B . 
L 4 PEG 1   704  601 PEG PEG B . 
M 5 LAC 1   705  502 LAC LAC B . 
N 6 NI  1   706  1   NI  NI  B . 
O 7 HOH 1   601  254 HOH HOH A . 
O 7 HOH 2   602  199 HOH HOH A . 
O 7 HOH 3   603  307 HOH HOH A . 
O 7 HOH 4   604  469 HOH HOH A . 
O 7 HOH 5   605  457 HOH HOH A . 
O 7 HOH 6   606  435 HOH HOH A . 
O 7 HOH 7   607  427 HOH HOH A . 
O 7 HOH 8   608  383 HOH HOH A . 
O 7 HOH 9   609  405 HOH HOH A . 
O 7 HOH 10  610  508 HOH HOH A . 
O 7 HOH 11  611  297 HOH HOH A . 
O 7 HOH 12  612  239 HOH HOH A . 
O 7 HOH 13  613  344 HOH HOH A . 
O 7 HOH 14  614  541 HOH HOH A . 
O 7 HOH 15  615  461 HOH HOH A . 
O 7 HOH 16  616  488 HOH HOH A . 
O 7 HOH 17  617  324 HOH HOH A . 
O 7 HOH 18  618  423 HOH HOH A . 
O 7 HOH 19  619  90  HOH HOH A . 
O 7 HOH 20  620  444 HOH HOH A . 
O 7 HOH 21  621  236 HOH HOH A . 
O 7 HOH 22  622  180 HOH HOH A . 
O 7 HOH 23  623  428 HOH HOH A . 
O 7 HOH 24  624  81  HOH HOH A . 
O 7 HOH 25  625  352 HOH HOH A . 
O 7 HOH 26  626  228 HOH HOH A . 
O 7 HOH 27  627  123 HOH HOH A . 
O 7 HOH 28  628  382 HOH HOH A . 
O 7 HOH 29  629  53  HOH HOH A . 
O 7 HOH 30  630  486 HOH HOH A . 
O 7 HOH 31  631  195 HOH HOH A . 
O 7 HOH 32  632  447 HOH HOH A . 
O 7 HOH 33  633  265 HOH HOH A . 
O 7 HOH 34  634  158 HOH HOH A . 
O 7 HOH 35  635  146 HOH HOH A . 
O 7 HOH 36  636  512 HOH HOH A . 
O 7 HOH 37  637  102 HOH HOH A . 
O 7 HOH 38  638  326 HOH HOH A . 
O 7 HOH 39  639  79  HOH HOH A . 
O 7 HOH 40  640  264 HOH HOH A . 
O 7 HOH 41  641  103 HOH HOH A . 
O 7 HOH 42  642  253 HOH HOH A . 
O 7 HOH 43  643  231 HOH HOH A . 
O 7 HOH 44  644  289 HOH HOH A . 
O 7 HOH 45  645  24  HOH HOH A . 
O 7 HOH 46  646  193 HOH HOH A . 
O 7 HOH 47  647  164 HOH HOH A . 
O 7 HOH 48  648  479 HOH HOH A . 
O 7 HOH 49  649  366 HOH HOH A . 
O 7 HOH 50  650  463 HOH HOH A . 
O 7 HOH 51  651  45  HOH HOH A . 
O 7 HOH 52  652  143 HOH HOH A . 
O 7 HOH 53  653  358 HOH HOH A . 
O 7 HOH 54  654  288 HOH HOH A . 
O 7 HOH 55  655  426 HOH HOH A . 
O 7 HOH 56  656  142 HOH HOH A . 
O 7 HOH 57  657  43  HOH HOH A . 
O 7 HOH 58  658  186 HOH HOH A . 
O 7 HOH 59  659  342 HOH HOH A . 
O 7 HOH 60  660  226 HOH HOH A . 
O 7 HOH 61  661  207 HOH HOH A . 
O 7 HOH 62  662  205 HOH HOH A . 
O 7 HOH 63  663  482 HOH HOH A . 
O 7 HOH 64  664  391 HOH HOH A . 
O 7 HOH 65  665  150 HOH HOH A . 
O 7 HOH 66  666  441 HOH HOH A . 
O 7 HOH 67  667  159 HOH HOH A . 
O 7 HOH 68  668  117 HOH HOH A . 
O 7 HOH 69  669  345 HOH HOH A . 
O 7 HOH 70  670  380 HOH HOH A . 
O 7 HOH 71  671  556 HOH HOH A . 
O 7 HOH 72  672  166 HOH HOH A . 
O 7 HOH 73  673  266 HOH HOH A . 
O 7 HOH 74  674  62  HOH HOH A . 
O 7 HOH 75  675  201 HOH HOH A . 
O 7 HOH 76  676  108 HOH HOH A . 
O 7 HOH 77  677  119 HOH HOH A . 
O 7 HOH 78  678  449 HOH HOH A . 
O 7 HOH 79  679  473 HOH HOH A . 
O 7 HOH 80  680  86  HOH HOH A . 
O 7 HOH 81  681  121 HOH HOH A . 
O 7 HOH 82  682  395 HOH HOH A . 
O 7 HOH 83  683  107 HOH HOH A . 
O 7 HOH 84  684  88  HOH HOH A . 
O 7 HOH 85  685  51  HOH HOH A . 
O 7 HOH 86  686  118 HOH HOH A . 
O 7 HOH 87  687  110 HOH HOH A . 
O 7 HOH 88  688  175 HOH HOH A . 
O 7 HOH 89  689  202 HOH HOH A . 
O 7 HOH 90  690  317 HOH HOH A . 
O 7 HOH 91  691  381 HOH HOH A . 
O 7 HOH 92  692  225 HOH HOH A . 
O 7 HOH 93  693  359 HOH HOH A . 
O 7 HOH 94  694  29  HOH HOH A . 
O 7 HOH 95  695  467 HOH HOH A . 
O 7 HOH 96  696  456 HOH HOH A . 
O 7 HOH 97  697  478 HOH HOH A . 
O 7 HOH 98  698  306 HOH HOH A . 
O 7 HOH 99  699  12  HOH HOH A . 
O 7 HOH 100 700  196 HOH HOH A . 
O 7 HOH 101 701  84  HOH HOH A . 
O 7 HOH 102 702  113 HOH HOH A . 
O 7 HOH 103 703  371 HOH HOH A . 
O 7 HOH 104 704  374 HOH HOH A . 
O 7 HOH 105 705  115 HOH HOH A . 
O 7 HOH 106 706  112 HOH HOH A . 
O 7 HOH 107 707  7   HOH HOH A . 
O 7 HOH 108 708  422 HOH HOH A . 
O 7 HOH 109 709  57  HOH HOH A . 
O 7 HOH 110 710  443 HOH HOH A . 
O 7 HOH 111 711  416 HOH HOH A . 
O 7 HOH 112 712  23  HOH HOH A . 
O 7 HOH 113 713  39  HOH HOH A . 
O 7 HOH 114 714  87  HOH HOH A . 
O 7 HOH 115 715  64  HOH HOH A . 
O 7 HOH 116 716  262 HOH HOH A . 
O 7 HOH 117 717  120 HOH HOH A . 
O 7 HOH 118 718  339 HOH HOH A . 
O 7 HOH 119 719  255 HOH HOH A . 
O 7 HOH 120 720  480 HOH HOH A . 
O 7 HOH 121 721  376 HOH HOH A . 
O 7 HOH 122 722  31  HOH HOH A . 
O 7 HOH 123 723  534 HOH HOH A . 
O 7 HOH 124 724  465 HOH HOH A . 
O 7 HOH 125 725  242 HOH HOH A . 
O 7 HOH 126 726  474 HOH HOH A . 
O 7 HOH 127 727  109 HOH HOH A . 
O 7 HOH 128 728  21  HOH HOH A . 
O 7 HOH 129 729  167 HOH HOH A . 
O 7 HOH 130 730  401 HOH HOH A . 
O 7 HOH 131 731  214 HOH HOH A . 
O 7 HOH 132 732  295 HOH HOH A . 
O 7 HOH 133 733  285 HOH HOH A . 
O 7 HOH 134 734  184 HOH HOH A . 
O 7 HOH 135 735  181 HOH HOH A . 
O 7 HOH 136 736  442 HOH HOH A . 
O 7 HOH 137 737  446 HOH HOH A . 
O 7 HOH 138 738  4   HOH HOH A . 
O 7 HOH 139 739  41  HOH HOH A . 
O 7 HOH 140 740  318 HOH HOH A . 
O 7 HOH 141 741  240 HOH HOH A . 
O 7 HOH 142 742  496 HOH HOH A . 
O 7 HOH 143 743  349 HOH HOH A . 
O 7 HOH 144 744  417 HOH HOH A . 
O 7 HOH 145 745  248 HOH HOH A . 
O 7 HOH 146 746  578 HOH HOH A . 
O 7 HOH 147 747  122 HOH HOH A . 
O 7 HOH 148 748  197 HOH HOH A . 
O 7 HOH 149 749  439 HOH HOH A . 
O 7 HOH 150 750  215 HOH HOH A . 
O 7 HOH 151 751  290 HOH HOH A . 
O 7 HOH 152 752  165 HOH HOH A . 
O 7 HOH 153 753  360 HOH HOH A . 
O 7 HOH 154 754  400 HOH HOH A . 
O 7 HOH 155 755  144 HOH HOH A . 
O 7 HOH 156 756  470 HOH HOH A . 
O 7 HOH 157 757  411 HOH HOH A . 
O 7 HOH 158 758  283 HOH HOH A . 
O 7 HOH 159 759  559 HOH HOH A . 
O 7 HOH 160 760  396 HOH HOH A . 
O 7 HOH 161 761  410 HOH HOH A . 
O 7 HOH 162 762  351 HOH HOH A . 
O 7 HOH 163 763  386 HOH HOH A . 
O 7 HOH 164 764  249 HOH HOH A . 
O 7 HOH 165 765  420 HOH HOH A . 
O 7 HOH 166 766  350 HOH HOH A . 
O 7 HOH 167 767  168 HOH HOH A . 
O 7 HOH 168 768  270 HOH HOH A . 
O 7 HOH 169 769  258 HOH HOH A . 
O 7 HOH 170 770  466 HOH HOH A . 
O 7 HOH 171 771  499 HOH HOH A . 
O 7 HOH 172 772  18  HOH HOH A . 
O 7 HOH 173 773  162 HOH HOH A . 
O 7 HOH 174 774  48  HOH HOH A . 
O 7 HOH 175 775  445 HOH HOH A . 
O 7 HOH 176 776  192 HOH HOH A . 
O 7 HOH 177 777  20  HOH HOH A . 
O 7 HOH 178 778  367 HOH HOH A . 
O 7 HOH 179 779  93  HOH HOH A . 
O 7 HOH 180 780  116 HOH HOH A . 
O 7 HOH 181 781  419 HOH HOH A . 
O 7 HOH 182 782  30  HOH HOH A . 
O 7 HOH 183 783  35  HOH HOH A . 
O 7 HOH 184 784  11  HOH HOH A . 
O 7 HOH 185 785  251 HOH HOH A . 
O 7 HOH 186 786  572 HOH HOH A . 
O 7 HOH 187 787  414 HOH HOH A . 
O 7 HOH 188 788  56  HOH HOH A . 
O 7 HOH 189 789  377 HOH HOH A . 
O 7 HOH 190 790  147 HOH HOH A . 
O 7 HOH 191 791  554 HOH HOH A . 
O 7 HOH 192 792  2   HOH HOH A . 
O 7 HOH 193 793  341 HOH HOH A . 
O 7 HOH 194 794  379 HOH HOH A . 
O 7 HOH 195 795  89  HOH HOH A . 
O 7 HOH 196 796  533 HOH HOH A . 
O 7 HOH 197 797  145 HOH HOH A . 
O 7 HOH 198 798  532 HOH HOH A . 
O 7 HOH 199 799  141 HOH HOH A . 
O 7 HOH 200 800  331 HOH HOH A . 
O 7 HOH 201 801  576 HOH HOH A . 
O 7 HOH 202 802  22  HOH HOH A . 
O 7 HOH 203 803  94  HOH HOH A . 
O 7 HOH 204 804  10  HOH HOH A . 
O 7 HOH 205 805  505 HOH HOH A . 
O 7 HOH 206 806  531 HOH HOH A . 
O 7 HOH 207 807  111 HOH HOH A . 
O 7 HOH 208 808  91  HOH HOH A . 
O 7 HOH 209 809  32  HOH HOH A . 
O 7 HOH 210 810  385 HOH HOH A . 
O 7 HOH 211 811  263 HOH HOH A . 
O 7 HOH 212 812  85  HOH HOH A . 
O 7 HOH 213 813  169 HOH HOH A . 
O 7 HOH 214 814  54  HOH HOH A . 
O 7 HOH 215 815  244 HOH HOH A . 
O 7 HOH 216 816  237 HOH HOH A . 
O 7 HOH 217 817  434 HOH HOH A . 
O 7 HOH 218 818  124 HOH HOH A . 
O 7 HOH 219 819  104 HOH HOH A . 
O 7 HOH 220 820  354 HOH HOH A . 
O 7 HOH 221 821  229 HOH HOH A . 
O 7 HOH 222 822  425 HOH HOH A . 
O 7 HOH 223 823  178 HOH HOH A . 
O 7 HOH 224 824  551 HOH HOH A . 
O 7 HOH 225 825  213 HOH HOH A . 
O 7 HOH 226 826  495 HOH HOH A . 
O 7 HOH 227 827  330 HOH HOH A . 
O 7 HOH 228 828  221 HOH HOH A . 
O 7 HOH 229 829  362 HOH HOH A . 
O 7 HOH 230 830  542 HOH HOH A . 
O 7 HOH 231 831  105 HOH HOH A . 
O 7 HOH 232 832  387 HOH HOH A . 
O 7 HOH 233 833  114 HOH HOH A . 
O 7 HOH 234 834  462 HOH HOH A . 
O 7 HOH 235 835  506 HOH HOH A . 
O 7 HOH 236 836  390 HOH HOH A . 
O 7 HOH 237 837  487 HOH HOH A . 
O 7 HOH 238 838  510 HOH HOH A . 
O 7 HOH 239 839  106 HOH HOH A . 
O 7 HOH 240 840  553 HOH HOH A . 
O 7 HOH 241 841  543 HOH HOH A . 
O 7 HOH 242 842  552 HOH HOH A . 
O 7 HOH 243 843  230 HOH HOH A . 
O 7 HOH 244 844  489 HOH HOH A . 
O 7 HOH 245 845  340 HOH HOH A . 
O 7 HOH 246 846  571 HOH HOH A . 
O 7 HOH 247 847  458 HOH HOH A . 
O 7 HOH 248 848  421 HOH HOH A . 
O 7 HOH 249 849  481 HOH HOH A . 
O 7 HOH 250 850  497 HOH HOH A . 
O 7 HOH 251 851  507 HOH HOH A . 
O 7 HOH 252 852  361 HOH HOH A . 
O 7 HOH 253 853  394 HOH HOH A . 
O 7 HOH 254 854  579 HOH HOH A . 
O 7 HOH 255 855  502 HOH HOH A . 
O 7 HOH 256 856  484 HOH HOH A . 
O 7 HOH 257 857  558 HOH HOH A . 
O 7 HOH 258 858  557 HOH HOH A . 
O 7 HOH 259 859  82  HOH HOH A . 
O 7 HOH 260 860  372 HOH HOH A . 
O 7 HOH 261 861  316 HOH HOH A . 
O 7 HOH 262 862  343 HOH HOH A . 
O 7 HOH 263 863  577 HOH HOH A . 
O 7 HOH 264 864  384 HOH HOH A . 
O 7 HOH 265 865  334 HOH HOH A . 
O 7 HOH 266 866  101 HOH HOH A . 
O 7 HOH 267 867  346 HOH HOH A . 
O 7 HOH 268 868  291 HOH HOH A . 
O 7 HOH 269 869  409 HOH HOH A . 
O 7 HOH 270 870  83  HOH HOH A . 
O 7 HOH 271 871  348 HOH HOH A . 
O 7 HOH 272 872  151 HOH HOH A . 
O 7 HOH 273 873  313 HOH HOH A . 
O 7 HOH 274 874  332 HOH HOH A . 
O 7 HOH 275 875  504 HOH HOH A . 
O 7 HOH 276 876  498 HOH HOH A . 
O 7 HOH 277 877  514 HOH HOH A . 
O 7 HOH 278 878  320 HOH HOH A . 
O 7 HOH 279 879  408 HOH HOH A . 
O 7 HOH 280 880  560 HOH HOH A . 
O 7 HOH 281 881  555 HOH HOH A . 
O 7 HOH 282 882  309 HOH HOH A . 
O 7 HOH 283 883  513 HOH HOH A . 
O 7 HOH 284 884  468 HOH HOH A . 
O 7 HOH 285 885  406 HOH HOH A . 
O 7 HOH 286 886  494 HOH HOH A . 
O 7 HOH 287 887  459 HOH HOH A . 
O 7 HOH 288 888  545 HOH HOH A . 
O 7 HOH 289 889  475 HOH HOH A . 
O 7 HOH 290 890  511 HOH HOH A . 
O 7 HOH 291 891  338 HOH HOH A . 
O 7 HOH 292 892  509 HOH HOH A . 
O 7 HOH 293 893  329 HOH HOH A . 
O 7 HOH 294 894  490 HOH HOH A . 
O 7 HOH 295 895  544 HOH HOH A . 
O 7 HOH 296 896  485 HOH HOH A . 
O 7 HOH 297 897  503 HOH HOH A . 
O 7 HOH 298 898  500 HOH HOH A . 
O 7 HOH 299 899  347 HOH HOH A . 
O 7 HOH 300 900  418 HOH HOH A . 
O 7 HOH 301 901  438 HOH HOH A . 
O 7 HOH 302 902  353 HOH HOH A . 
O 7 HOH 303 903  284 HOH HOH A . 
O 7 HOH 304 904  574 HOH HOH A . 
O 7 HOH 305 905  493 HOH HOH A . 
O 7 HOH 306 906  483 HOH HOH A . 
O 7 HOH 307 907  573 HOH HOH A . 
O 7 HOH 308 908  575 HOH HOH A . 
O 7 HOH 309 909  373 HOH HOH A . 
P 7 HOH 1   801  450 HOH HOH B . 
P 7 HOH 2   802  365 HOH HOH B . 
P 7 HOH 3   803  304 HOH HOH B . 
P 7 HOH 4   804  398 HOH HOH B . 
P 7 HOH 5   805  455 HOH HOH B . 
P 7 HOH 6   806  36  HOH HOH B . 
P 7 HOH 7   807  548 HOH HOH B . 
P 7 HOH 8   808  190 HOH HOH B . 
P 7 HOH 9   809  430 HOH HOH B . 
P 7 HOH 10  810  397 HOH HOH B . 
P 7 HOH 11  811  518 HOH HOH B . 
P 7 HOH 12  812  63  HOH HOH B . 
P 7 HOH 13  813  275 HOH HOH B . 
P 7 HOH 14  814  569 HOH HOH B . 
P 7 HOH 15  815  252 HOH HOH B . 
P 7 HOH 16  816  452 HOH HOH B . 
P 7 HOH 17  817  546 HOH HOH B . 
P 7 HOH 18  818  323 HOH HOH B . 
P 7 HOH 19  819  564 HOH HOH B . 
P 7 HOH 20  820  273 HOH HOH B . 
P 7 HOH 21  821  34  HOH HOH B . 
P 7 HOH 22  822  132 HOH HOH B . 
P 7 HOH 23  823  206 HOH HOH B . 
P 7 HOH 24  824  526 HOH HOH B . 
P 7 HOH 25  825  156 HOH HOH B . 
P 7 HOH 26  826  98  HOH HOH B . 
P 7 HOH 27  827  437 HOH HOH B . 
P 7 HOH 28  828  501 HOH HOH B . 
P 7 HOH 29  829  173 HOH HOH B . 
P 7 HOH 30  830  402 HOH HOH B . 
P 7 HOH 31  831  137 HOH HOH B . 
P 7 HOH 32  832  256 HOH HOH B . 
P 7 HOH 33  833  403 HOH HOH B . 
P 7 HOH 34  834  393 HOH HOH B . 
P 7 HOH 35  835  296 HOH HOH B . 
P 7 HOH 36  836  60  HOH HOH B . 
P 7 HOH 37  837  71  HOH HOH B . 
P 7 HOH 38  838  453 HOH HOH B . 
P 7 HOH 39  839  293 HOH HOH B . 
P 7 HOH 40  840  357 HOH HOH B . 
P 7 HOH 41  841  310 HOH HOH B . 
P 7 HOH 42  842  314 HOH HOH B . 
P 7 HOH 43  843  448 HOH HOH B . 
P 7 HOH 44  844  516 HOH HOH B . 
P 7 HOH 45  845  250 HOH HOH B . 
P 7 HOH 46  846  527 HOH HOH B . 
P 7 HOH 47  847  139 HOH HOH B . 
P 7 HOH 48  848  148 HOH HOH B . 
P 7 HOH 49  849  33  HOH HOH B . 
P 7 HOH 50  850  149 HOH HOH B . 
P 7 HOH 51  851  404 HOH HOH B . 
P 7 HOH 52  852  44  HOH HOH B . 
P 7 HOH 53  853  187 HOH HOH B . 
P 7 HOH 54  854  140 HOH HOH B . 
P 7 HOH 55  855  241 HOH HOH B . 
P 7 HOH 56  856  161 HOH HOH B . 
P 7 HOH 57  857  176 HOH HOH B . 
P 7 HOH 58  858  128 HOH HOH B . 
P 7 HOH 59  859  50  HOH HOH B . 
P 7 HOH 60  860  217 HOH HOH B . 
P 7 HOH 61  861  210 HOH HOH B . 
P 7 HOH 62  862  211 HOH HOH B . 
P 7 HOH 63  863  549 HOH HOH B . 
P 7 HOH 64  864  58  HOH HOH B . 
P 7 HOH 65  865  477 HOH HOH B . 
P 7 HOH 66  866  209 HOH HOH B . 
P 7 HOH 67  867  536 HOH HOH B . 
P 7 HOH 68  868  100 HOH HOH B . 
P 7 HOH 69  869  472 HOH HOH B . 
P 7 HOH 70  870  261 HOH HOH B . 
P 7 HOH 71  871  287 HOH HOH B . 
P 7 HOH 72  872  97  HOH HOH B . 
P 7 HOH 73  873  378 HOH HOH B . 
P 7 HOH 74  874  279 HOH HOH B . 
P 7 HOH 75  875  223 HOH HOH B . 
P 7 HOH 76  876  174 HOH HOH B . 
P 7 HOH 77  877  278 HOH HOH B . 
P 7 HOH 78  878  163 HOH HOH B . 
P 7 HOH 79  879  271 HOH HOH B . 
P 7 HOH 80  880  194 HOH HOH B . 
P 7 HOH 81  881  567 HOH HOH B . 
P 7 HOH 82  882  260 HOH HOH B . 
P 7 HOH 83  883  235 HOH HOH B . 
P 7 HOH 84  884  17  HOH HOH B . 
P 7 HOH 85  885  134 HOH HOH B . 
P 7 HOH 86  886  337 HOH HOH B . 
P 7 HOH 87  887  294 HOH HOH B . 
P 7 HOH 88  888  308 HOH HOH B . 
P 7 HOH 89  889  399 HOH HOH B . 
P 7 HOH 90  890  67  HOH HOH B . 
P 7 HOH 91  891  9   HOH HOH B . 
P 7 HOH 92  892  177 HOH HOH B . 
P 7 HOH 93  893  529 HOH HOH B . 
P 7 HOH 94  894  325 HOH HOH B . 
P 7 HOH 95  895  160 HOH HOH B . 
P 7 HOH 96  896  388 HOH HOH B . 
P 7 HOH 97  897  8   HOH HOH B . 
P 7 HOH 98  898  27  HOH HOH B . 
P 7 HOH 99  899  200 HOH HOH B . 
P 7 HOH 100 900  191 HOH HOH B . 
P 7 HOH 101 901  520 HOH HOH B . 
P 7 HOH 102 902  185 HOH HOH B . 
P 7 HOH 103 903  14  HOH HOH B . 
P 7 HOH 104 904  492 HOH HOH B . 
P 7 HOH 105 905  539 HOH HOH B . 
P 7 HOH 106 906  369 HOH HOH B . 
P 7 HOH 107 907  203 HOH HOH B . 
P 7 HOH 108 908  171 HOH HOH B . 
P 7 HOH 109 909  272 HOH HOH B . 
P 7 HOH 110 910  454 HOH HOH B . 
P 7 HOH 111 911  13  HOH HOH B . 
P 7 HOH 112 912  127 HOH HOH B . 
P 7 HOH 113 913  59  HOH HOH B . 
P 7 HOH 114 914  276 HOH HOH B . 
P 7 HOH 115 915  157 HOH HOH B . 
P 7 HOH 116 916  277 HOH HOH B . 
P 7 HOH 117 917  243 HOH HOH B . 
P 7 HOH 118 918  522 HOH HOH B . 
P 7 HOH 119 919  208 HOH HOH B . 
P 7 HOH 120 920  281 HOH HOH B . 
P 7 HOH 121 921  274 HOH HOH B . 
P 7 HOH 122 922  524 HOH HOH B . 
P 7 HOH 123 923  433 HOH HOH B . 
P 7 HOH 124 924  222 HOH HOH B . 
P 7 HOH 125 925  183 HOH HOH B . 
P 7 HOH 126 926  315 HOH HOH B . 
P 7 HOH 127 927  216 HOH HOH B . 
P 7 HOH 128 928  267 HOH HOH B . 
P 7 HOH 129 929  16  HOH HOH B . 
P 7 HOH 130 930  40  HOH HOH B . 
P 7 HOH 131 931  355 HOH HOH B . 
P 7 HOH 132 932  37  HOH HOH B . 
P 7 HOH 133 933  415 HOH HOH B . 
P 7 HOH 134 934  198 HOH HOH B . 
P 7 HOH 135 935  392 HOH HOH B . 
P 7 HOH 136 936  227 HOH HOH B . 
P 7 HOH 137 937  96  HOH HOH B . 
P 7 HOH 138 938  451 HOH HOH B . 
P 7 HOH 139 939  76  HOH HOH B . 
P 7 HOH 140 940  259 HOH HOH B . 
P 7 HOH 141 941  429 HOH HOH B . 
P 7 HOH 142 942  311 HOH HOH B . 
P 7 HOH 143 943  302 HOH HOH B . 
P 7 HOH 144 944  212 HOH HOH B . 
P 7 HOH 145 945  130 HOH HOH B . 
P 7 HOH 146 946  182 HOH HOH B . 
P 7 HOH 147 947  99  HOH HOH B . 
P 7 HOH 148 948  189 HOH HOH B . 
P 7 HOH 149 949  368 HOH HOH B . 
P 7 HOH 150 950  550 HOH HOH B . 
P 7 HOH 151 951  42  HOH HOH B . 
P 7 HOH 152 952  55  HOH HOH B . 
P 7 HOH 153 953  135 HOH HOH B . 
P 7 HOH 154 954  179 HOH HOH B . 
P 7 HOH 155 955  257 HOH HOH B . 
P 7 HOH 156 956  220 HOH HOH B . 
P 7 HOH 157 957  46  HOH HOH B . 
P 7 HOH 158 958  138 HOH HOH B . 
P 7 HOH 159 959  301 HOH HOH B . 
P 7 HOH 160 960  413 HOH HOH B . 
P 7 HOH 161 961  299 HOH HOH B . 
P 7 HOH 162 962  188 HOH HOH B . 
P 7 HOH 163 963  476 HOH HOH B . 
P 7 HOH 164 964  28  HOH HOH B . 
P 7 HOH 165 965  523 HOH HOH B . 
P 7 HOH 166 966  561 HOH HOH B . 
P 7 HOH 167 967  436 HOH HOH B . 
P 7 HOH 168 968  525 HOH HOH B . 
P 7 HOH 169 969  129 HOH HOH B . 
P 7 HOH 170 970  519 HOH HOH B . 
P 7 HOH 171 971  566 HOH HOH B . 
P 7 HOH 172 972  246 HOH HOH B . 
P 7 HOH 173 973  407 HOH HOH B . 
P 7 HOH 174 974  530 HOH HOH B . 
P 7 HOH 175 975  292 HOH HOH B . 
P 7 HOH 176 976  535 HOH HOH B . 
P 7 HOH 177 977  218 HOH HOH B . 
P 7 HOH 178 978  464 HOH HOH B . 
P 7 HOH 179 979  312 HOH HOH B . 
P 7 HOH 180 980  568 HOH HOH B . 
P 7 HOH 181 981  528 HOH HOH B . 
P 7 HOH 182 982  491 HOH HOH B . 
P 7 HOH 183 983  336 HOH HOH B . 
P 7 HOH 184 984  515 HOH HOH B . 
P 7 HOH 185 985  333 HOH HOH B . 
P 7 HOH 186 986  356 HOH HOH B . 
P 7 HOH 187 987  136 HOH HOH B . 
P 7 HOH 188 988  563 HOH HOH B . 
P 7 HOH 189 989  540 HOH HOH B . 
P 7 HOH 190 990  565 HOH HOH B . 
P 7 HOH 191 991  153 HOH HOH B . 
P 7 HOH 192 992  432 HOH HOH B . 
P 7 HOH 193 993  570 HOH HOH B . 
P 7 HOH 194 994  389 HOH HOH B . 
P 7 HOH 195 995  562 HOH HOH B . 
P 7 HOH 196 996  233 HOH HOH B . 
P 7 HOH 197 997  440 HOH HOH B . 
P 7 HOH 198 998  521 HOH HOH B . 
P 7 HOH 199 999  412 HOH HOH B . 
P 7 HOH 200 1000 547 HOH HOH B . 
P 7 HOH 201 1001 224 HOH HOH B . 
P 7 HOH 202 1002 431 HOH HOH B . 
P 7 HOH 203 1003 268 HOH HOH B . 
P 7 HOH 204 1004 581 HOH HOH B . 
P 7 HOH 205 1005 537 HOH HOH B . 
P 7 HOH 206 1006 538 HOH HOH B . 
P 7 HOH 207 1007 580 HOH HOH B . 
# 
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 A ARG 3   ? CG  ? A ARG 1   CG  
2   1 Y 1 A ARG 3   ? CD  ? A ARG 1   CD  
3   1 Y 1 A ARG 3   ? NE  ? A ARG 1   NE  
4   1 Y 1 A ARG 3   ? CZ  ? A ARG 1   CZ  
5   1 Y 1 A ARG 3   ? NH1 ? A ARG 1   NH1 
6   1 Y 1 A ARG 3   ? NH2 ? A ARG 1   NH2 
7   1 Y 1 A ASP 20  ? CG  ? A ASP 18  CG  
8   1 Y 1 A ASP 20  ? OD1 ? A ASP 18  OD1 
9   1 Y 1 A ASP 20  ? OD2 ? A ASP 18  OD2 
10  1 Y 1 A GLU 47  ? CG  ? A GLU 45  CG  
11  1 Y 1 A GLU 47  ? CD  ? A GLU 45  CD  
12  1 Y 1 A GLU 47  ? OE1 ? A GLU 45  OE1 
13  1 Y 1 A GLU 47  ? OE2 ? A GLU 45  OE2 
14  1 Y 1 A ARG 62  ? CG  ? A ARG 60  CG  
15  1 Y 1 A ARG 62  ? CD  ? A ARG 60  CD  
16  1 Y 1 A ARG 62  ? NE  ? A ARG 60  NE  
17  1 Y 1 A ARG 62  ? CZ  ? A ARG 60  CZ  
18  1 Y 1 A ARG 62  ? NH1 ? A ARG 60  NH1 
19  1 Y 1 A ARG 62  ? NH2 ? A ARG 60  NH2 
20  1 Y 1 A GLN 96  ? CG  ? A GLN 94  CG  
21  1 Y 1 A GLN 96  ? CD  ? A GLN 94  CD  
22  1 Y 1 A GLN 96  ? OE1 ? A GLN 94  OE1 
23  1 Y 1 A GLN 96  ? NE2 ? A GLN 94  NE2 
24  1 Y 1 A GLU 122 ? CG  ? A GLU 120 CG  
25  1 Y 1 A GLU 122 ? CD  ? A GLU 120 CD  
26  1 Y 1 A GLU 122 ? OE1 ? A GLU 120 OE1 
27  1 Y 1 A GLU 122 ? OE2 ? A GLU 120 OE2 
28  1 Y 1 A ARG 125 ? CG  ? A ARG 123 CG  
29  1 Y 1 A ARG 125 ? CD  ? A ARG 123 CD  
30  1 Y 1 A ARG 125 ? NE  ? A ARG 123 NE  
31  1 Y 1 A ARG 125 ? CZ  ? A ARG 123 CZ  
32  1 Y 1 A ARG 125 ? NH1 ? A ARG 123 NH1 
33  1 Y 1 A ARG 125 ? NH2 ? A ARG 123 NH2 
34  1 Y 1 A ARG 128 ? CG  ? A ARG 126 CG  
35  1 Y 1 A ARG 128 ? CD  ? A ARG 126 CD  
36  1 Y 1 A ARG 128 ? NE  ? A ARG 126 NE  
37  1 Y 1 A ARG 128 ? CZ  ? A ARG 126 CZ  
38  1 Y 1 A ARG 128 ? NH1 ? A ARG 126 NH1 
39  1 Y 1 A ARG 128 ? NH2 ? A ARG 126 NH2 
40  1 Y 1 A GLU 215 ? CG  ? A GLU 213 CG  
41  1 Y 1 A GLU 215 ? CD  ? A GLU 213 CD  
42  1 Y 1 A GLU 215 ? OE1 ? A GLU 213 OE1 
43  1 Y 1 A GLU 215 ? OE2 ? A GLU 213 OE2 
44  1 Y 1 A LYS 260 ? CG  ? A LYS 258 CG  
45  1 Y 1 A LYS 260 ? CD  ? A LYS 258 CD  
46  1 Y 1 A LYS 260 ? CE  ? A LYS 258 CE  
47  1 Y 1 A LYS 260 ? NZ  ? A LYS 258 NZ  
48  1 Y 1 A GLU 333 ? CG  ? A GLU 331 CG  
49  1 Y 1 A GLU 333 ? CD  ? A GLU 331 CD  
50  1 Y 1 A GLU 333 ? OE1 ? A GLU 331 OE1 
51  1 Y 1 A GLU 333 ? OE2 ? A GLU 331 OE2 
52  1 Y 1 A GLU 334 ? CG  ? A GLU 332 CG  
53  1 Y 1 A GLU 334 ? CD  ? A GLU 332 CD  
54  1 Y 1 A GLU 334 ? OE1 ? A GLU 332 OE1 
55  1 Y 1 A GLU 334 ? OE2 ? A GLU 332 OE2 
56  1 Y 1 A GLU 402 ? CG  ? A GLU 400 CG  
57  1 Y 1 A GLU 402 ? CD  ? A GLU 400 CD  
58  1 Y 1 A GLU 402 ? OE1 ? A GLU 400 OE1 
59  1 Y 1 A GLU 402 ? OE2 ? A GLU 400 OE2 
60  1 Y 1 A GLU 407 ? CG  ? A GLU 405 CG  
61  1 Y 1 A GLU 407 ? CD  ? A GLU 405 CD  
62  1 Y 1 A GLU 407 ? OE1 ? A GLU 405 OE1 
63  1 Y 1 A GLU 407 ? OE2 ? A GLU 405 OE2 
64  1 Y 1 A LEU 420 ? CD1 ? A LEU 418 CD1 
65  1 Y 1 A LEU 420 ? CD2 ? A LEU 418 CD2 
66  1 Y 1 A THR 426 ? OG1 ? A THR 424 OG1 
67  1 Y 1 A THR 426 ? CG2 ? A THR 424 CG2 
68  1 Y 1 B ARG 3   ? CG  ? B ARG 1   CG  
69  1 Y 1 B ARG 3   ? CD  ? B ARG 1   CD  
70  1 Y 1 B ARG 3   ? NE  ? B ARG 1   NE  
71  1 Y 1 B ARG 3   ? CZ  ? B ARG 1   CZ  
72  1 Y 1 B ARG 3   ? NH1 ? B ARG 1   NH1 
73  1 Y 1 B ARG 3   ? NH2 ? B ARG 1   NH2 
74  1 Y 1 B ASP 19  ? CG  ? B ASP 17  CG  
75  1 Y 1 B ASP 19  ? OD1 ? B ASP 17  OD1 
76  1 Y 1 B ASP 19  ? OD2 ? B ASP 17  OD2 
77  1 Y 1 B ARG 21  ? NE  ? B ARG 19  NE  
78  1 Y 1 B ARG 21  ? CZ  ? B ARG 19  CZ  
79  1 Y 1 B ARG 21  ? NH1 ? B ARG 19  NH1 
80  1 Y 1 B ARG 21  ? NH2 ? B ARG 19  NH2 
81  1 Y 1 B ARG 29  ? CG  ? B ARG 27  CG  
82  1 Y 1 B ARG 29  ? CD  ? B ARG 27  CD  
83  1 Y 1 B ARG 29  ? NE  ? B ARG 27  NE  
84  1 Y 1 B ARG 29  ? CZ  ? B ARG 27  CZ  
85  1 Y 1 B ARG 29  ? NH1 ? B ARG 27  NH1 
86  1 Y 1 B ARG 29  ? NH2 ? B ARG 27  NH2 
87  1 Y 1 B GLU 47  ? CG  ? B GLU 45  CG  
88  1 Y 1 B GLU 47  ? CD  ? B GLU 45  CD  
89  1 Y 1 B GLU 47  ? OE1 ? B GLU 45  OE1 
90  1 Y 1 B GLU 47  ? OE2 ? B GLU 45  OE2 
91  1 Y 1 B ASP 56  ? OD1 ? B ASP 54  OD1 
92  1 Y 1 B ASP 56  ? OD2 ? B ASP 54  OD2 
93  1 Y 1 B ARG 62  ? CG  ? B ARG 60  CG  
94  1 Y 1 B ARG 62  ? CD  ? B ARG 60  CD  
95  1 Y 1 B ARG 62  ? NE  ? B ARG 60  NE  
96  1 Y 1 B ARG 62  ? CZ  ? B ARG 60  CZ  
97  1 Y 1 B ARG 62  ? NH1 ? B ARG 60  NH1 
98  1 Y 1 B ARG 62  ? NH2 ? B ARG 60  NH2 
99  1 Y 1 B GLN 96  ? CG  ? B GLN 94  CG  
100 1 Y 1 B GLN 96  ? CD  ? B GLN 94  CD  
101 1 Y 1 B GLN 96  ? OE1 ? B GLN 94  OE1 
102 1 Y 1 B GLN 96  ? NE2 ? B GLN 94  NE2 
103 1 Y 1 B GLU 122 ? CG  ? B GLU 120 CG  
104 1 Y 1 B GLU 122 ? CD  ? B GLU 120 CD  
105 1 Y 1 B GLU 122 ? OE1 ? B GLU 120 OE1 
106 1 Y 1 B GLU 122 ? OE2 ? B GLU 120 OE2 
107 1 Y 1 B ARG 125 ? CG  ? B ARG 123 CG  
108 1 Y 1 B ARG 125 ? CD  ? B ARG 123 CD  
109 1 Y 1 B ARG 125 ? NE  ? B ARG 123 NE  
110 1 Y 1 B ARG 125 ? CZ  ? B ARG 123 CZ  
111 1 Y 1 B ARG 125 ? NH1 ? B ARG 123 NH1 
112 1 Y 1 B ARG 125 ? NH2 ? B ARG 123 NH2 
113 1 Y 1 B ARG 136 ? NE  ? B ARG 134 NE  
114 1 Y 1 B ARG 136 ? CZ  ? B ARG 134 CZ  
115 1 Y 1 B ARG 136 ? NH1 ? B ARG 134 NH1 
116 1 Y 1 B ARG 136 ? NH2 ? B ARG 134 NH2 
117 1 Y 1 B GLU 138 ? CG  ? B GLU 136 CG  
118 1 Y 1 B GLU 138 ? CD  ? B GLU 136 CD  
119 1 Y 1 B GLU 138 ? OE1 ? B GLU 136 OE1 
120 1 Y 1 B GLU 138 ? OE2 ? B GLU 136 OE2 
121 1 Y 1 B ASP 162 ? CG  ? B ASP 160 CG  
122 1 Y 1 B ASP 162 ? OD1 ? B ASP 160 OD1 
123 1 Y 1 B ASP 162 ? OD2 ? B ASP 160 OD2 
124 1 Y 1 B GLU 215 ? CG  ? B GLU 213 CG  
125 1 Y 1 B GLU 215 ? CD  ? B GLU 213 CD  
126 1 Y 1 B GLU 215 ? OE1 ? B GLU 213 OE1 
127 1 Y 1 B GLU 215 ? OE2 ? B GLU 213 OE2 
128 1 Y 1 B LYS 260 ? CG  ? B LYS 258 CG  
129 1 Y 1 B LYS 260 ? CD  ? B LYS 258 CD  
130 1 Y 1 B LYS 260 ? CE  ? B LYS 258 CE  
131 1 Y 1 B LYS 260 ? NZ  ? B LYS 258 NZ  
132 1 Y 1 B GLU 266 ? CD  ? B GLU 264 CD  
133 1 Y 1 B GLU 266 ? OE1 ? B GLU 264 OE1 
134 1 Y 1 B GLU 266 ? OE2 ? B GLU 264 OE2 
135 1 Y 1 B GLU 333 ? CG  ? B GLU 331 CG  
136 1 Y 1 B GLU 333 ? CD  ? B GLU 331 CD  
137 1 Y 1 B GLU 333 ? OE1 ? B GLU 331 OE1 
138 1 Y 1 B GLU 333 ? OE2 ? B GLU 331 OE2 
139 1 Y 1 B GLU 334 ? CG  ? B GLU 332 CG  
140 1 Y 1 B GLU 334 ? CD  ? B GLU 332 CD  
141 1 Y 1 B GLU 334 ? OE1 ? B GLU 332 OE1 
142 1 Y 1 B GLU 334 ? OE2 ? B GLU 332 OE2 
143 1 Y 1 B GLU 343 ? CD  ? B GLU 341 CD  
144 1 Y 1 B GLU 343 ? OE1 ? B GLU 341 OE1 
145 1 Y 1 B GLU 343 ? OE2 ? B GLU 341 OE2 
146 1 Y 1 B GLU 349 ? CG  ? B GLU 347 CG  
147 1 Y 1 B GLU 349 ? CD  ? B GLU 347 CD  
148 1 Y 1 B GLU 349 ? OE1 ? B GLU 347 OE1 
149 1 Y 1 B GLU 349 ? OE2 ? B GLU 347 OE2 
150 1 Y 1 B ARG 384 ? CG  ? B ARG 382 CG  
151 1 Y 1 B ARG 384 ? CD  ? B ARG 382 CD  
152 1 Y 1 B ARG 384 ? NE  ? B ARG 382 NE  
153 1 Y 1 B ARG 384 ? CZ  ? B ARG 382 CZ  
154 1 Y 1 B ARG 384 ? NH1 ? B ARG 382 NH1 
155 1 Y 1 B ARG 384 ? NH2 ? B ARG 382 NH2 
156 1 Y 1 B ASP 424 ? CG  ? B ASP 422 CG  
157 1 Y 1 B ASP 424 ? OD1 ? B ASP 422 OD1 
158 1 Y 1 B ASP 424 ? OD2 ? B ASP 422 OD2 
159 1 Y 1 B THR 426 ? OG1 ? B THR 424 OG1 
160 1 Y 1 B THR 426 ? CG2 ? B THR 424 CG2 
# 
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       ? ? ? ? ? ? ? ? ? ? ? PHENIX    ? ? ? '(1.18.2_3874: ???)' 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? HKL-2000  ? ? ? .                    2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? SCALEPACK ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER    ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   91.20 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9EIA 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     79.420 
_cell.length_a_esd                 ? 
_cell.length_b                     45.514 
_cell.length_b_esd                 ? 
_cell.length_c                     119.140 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_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                         9EIA 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_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                   9EIA 
_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             2.27 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          45.87 
_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              6.5 
_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    
;0.1 M Imidazole/MES monohydrate, pH 6.5, 20 % PEG 500 MME, 20% PEG 20,000, and 120 mM each of ethylene glycols (diethylene glycol, triethylene glycol, tetraethylene glycol and pentaethylene glycol)
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            294 
# 
_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 EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2022-06-14 
_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   1.127231 
_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                        'APS BEAMLINE 21-ID-D' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.127231 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   21-ID-D 
_diffrn_source.pdbx_synchrotron_site       APS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9EIA 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.74 
_reflns.d_resolution_low                               33.07 
_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                                     84457 
_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                           96.2 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                2.5 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          10.3 
_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                                ? 
_reflns.pdbx_Rpim_I_all                                0.083 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_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                              0.112 
_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                                    1.74 
_reflns_shell.d_res_low                                     1.80 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.52 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             8214 
_reflns_shell.percent_possible_obs                          ? 
_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                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               0.469 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.610 
_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                                  0.567 
_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]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_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                                 9EIA 
_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                            1.74 
_refine.ls_d_res_low                             33.07 
_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                     84408 
_refine.ls_number_reflns_R_free                  4103 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    95.81 
_refine.ls_percent_reflns_R_free                 4.86 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1757 
_refine.ls_R_factor_R_free                       0.2123 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1738 
_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                    'FLAT BULK SOLVENT MODEL' 
_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                          1.35 
_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               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_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                 19.75 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.21 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_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_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.74 
_refine_hist.d_res_low                        33.07 
_refine_hist.number_atoms_solvent             516 
_refine_hist.number_atoms_total               6899 
_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        6288 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         95 
_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' ? 0.007  ? 6585 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.982  ? 9025 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 13.704 ? 940  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.064  ? 1084 ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.007  ? 1163 ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_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 
_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 
'X-RAY DIFFRACTION' 1.74 1.76  . . 112 2485 84.00 . . . . 0.3113 . . . . . . . . . . . 0.3470 
'X-RAY DIFFRACTION' 1.76 1.78  . . 149 2581 94.00 . . . . 0.2715 . . . . . . . . . . . 0.3230 
'X-RAY DIFFRACTION' 1.78 1.80  . . 162 2764 95.00 . . . . 0.2579 . . . . . . . . . . . 0.2887 
'X-RAY DIFFRACTION' 1.80 1.83  . . 160 2749 97.00 . . . . 0.2300 . . . . . . . . . . . 0.2545 
'X-RAY DIFFRACTION' 1.83 1.85  . . 164 2791 98.00 . . . . 0.2128 . . . . . . . . . . . 0.2539 
'X-RAY DIFFRACTION' 1.85 1.88  . . 157 2744 97.00 . . . . 0.2101 . . . . . . . . . . . 0.2870 
'X-RAY DIFFRACTION' 1.88 1.91  . . 131 2872 98.00 . . . . 0.1973 . . . . . . . . . . . 0.2442 
'X-RAY DIFFRACTION' 1.91 1.94  . . 140 2779 98.00 . . . . 0.1874 . . . . . . . . . . . 0.2461 
'X-RAY DIFFRACTION' 1.94 1.97  . . 157 2845 98.00 . . . . 0.1822 . . . . . . . . . . . 0.2001 
'X-RAY DIFFRACTION' 1.97 2.00  . . 146 2766 98.00 . . . . 0.1752 . . . . . . . . . . . 0.2236 
'X-RAY DIFFRACTION' 2.00 2.04  . . 160 2818 97.00 . . . . 0.1803 . . . . . . . . . . . 0.2453 
'X-RAY DIFFRACTION' 2.04 2.08  . . 147 2813 97.00 . . . . 0.1828 . . . . . . . . . . . 0.2309 
'X-RAY DIFFRACTION' 2.08 2.12  . . 137 2767 98.00 . . . . 0.1847 . . . . . . . . . . . 0.2063 
'X-RAY DIFFRACTION' 2.12 2.17  . . 132 2792 95.00 . . . . 0.1789 . . . . . . . . . . . 0.2403 
'X-RAY DIFFRACTION' 2.17 2.22  . . 147 2636 94.00 . . . . 0.1775 . . . . . . . . . . . 0.2374 
'X-RAY DIFFRACTION' 2.22 2.27  . . 125 2489 85.00 . . . . 0.1811 . . . . . . . . . . . 0.2249 
'X-RAY DIFFRACTION' 2.27 2.33  . . 141 2670 93.00 . . . . 0.1735 . . . . . . . . . . . 0.2102 
'X-RAY DIFFRACTION' 2.33 2.40  . . 132 2907 99.00 . . . . 0.1667 . . . . . . . . . . . 0.2199 
'X-RAY DIFFRACTION' 2.40 2.48  . . 153 2818 99.00 . . . . 0.1674 . . . . . . . . . . . 0.2100 
'X-RAY DIFFRACTION' 2.48 2.57  . . 162 2831 99.00 . . . . 0.1665 . . . . . . . . . . . 0.1937 
'X-RAY DIFFRACTION' 2.57 2.67  . . 132 2869 98.00 . . . . 0.1651 . . . . . . . . . . . 0.2228 
'X-RAY DIFFRACTION' 2.67 2.79  . . 143 2858 99.00 . . . . 0.1711 . . . . . . . . . . . 0.2256 
'X-RAY DIFFRACTION' 2.79 2.94  . . 131 2853 97.00 . . . . 0.1738 . . . . . . . . . . . 0.2153 
'X-RAY DIFFRACTION' 2.94 3.12  . . 137 2807 97.00 . . . . 0.1788 . . . . . . . . . . . 0.2235 
'X-RAY DIFFRACTION' 3.13 3.37  . . 122 2862 97.00 . . . . 0.1666 . . . . . . . . . . . 0.2133 
'X-RAY DIFFRACTION' 3.37 3.70  . . 124 2759 95.00 . . . . 0.1588 . . . . . . . . . . . 0.1641 
'X-RAY DIFFRACTION' 3.70 4.24  . . 125 2545 86.00 . . . . 0.1424 . . . . . . . . . . . 0.1684 
'X-RAY DIFFRACTION' 4.24 5.34  . . 148 2838 96.00 . . . . 0.1413 . . . . . . . . . . . 0.1724 
'X-RAY DIFFRACTION' 5.34 33.07 . . 127 2997 97.00 . . . . 0.1695 . . . . . . . . . . . 0.1771 
# 
_struct.entry_id                     9EIA 
_struct.title                        
'A broad-substrate spectrum lactate racemase A from Isosphaera pallida in complex with copurified D-lactate' 
_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        9EIA 
_struct_keywords.text            
'Catalytic activity, isomerase activity, racemase and epimerase activity racemase acting on hydroxy acids and derivatives, ISOMERASE' 
_struct_keywords.pdbx_keywords   ISOMERASE 
# 
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 2 ? 
D N N 2 ? 
E N N 3 ? 
F N N 4 ? 
G N N 5 ? 
H N N 6 ? 
I N N 2 ? 
J N N 3 ? 
K N N 4 ? 
L N N 4 ? 
M N N 5 ? 
N N N 6 ? 
O N N 7 ? 
P N N 7 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    E8QWZ4_ISOPI 
_struct_ref.pdbx_db_accession          E8QWZ4 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;RVTLDYGKTGLNVDLPDDRTLPPLTIRPAPPLDDPEAEVVRCLAEPIGSPPLLDLARGKRSACILVCDITRPVPNPVLLR
PILRTLHAAGLATQDILILVATGLHRPSTPAEKVEMLSEEIARTYRVEDHYGTRLEEHTYLGTTPNGVPAWIDSRYVQAD
LKIATGLIEPHLMAGYSGGRKLICPGIAAFETVKLWHGPRFLEHPLADCGFLEGNPVHEENTRIARMAGCDFIVNVTLDG
ARRITSVVAGDMEQAFLKGVAFVETVVKAAVPAPVDVVVTSSAGHPLDLTFYQAVKGLTGALPIVKPGGTIVIAAALAEG
LGSPEFQSLFEEHPTLEGFMEAILKEESFTVDQWQLEELAKVRRKARVKFVSDGVPAAVLSRCHVEPVATVELAVAQALE
QYGPEARVAVIPKGPYVLPVVDPTL
;
_struct_ref.pdbx_align_begin           2 
# 
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 9EIA A 1 ? 425 ? E8QWZ4 2 ? 426 ? 3 427 
2 1 9EIA B 1 ? 425 ? E8QWZ4 2 ? 426 ? 3 427 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_and_software_defined_assembly PISA monomeric 1 
2 author_and_software_defined_assembly PISA monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E,F,G,H,O 
2 1 B,I,J,K,L,M,N,P 
# 
_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 ASP A 34  ? GLU A 45  ? ASP A 36  GLU A 47  1 ? 12 
HELX_P HELX_P2  AA2 PRO A 51  ? ARG A 57  ? PRO A 53  ARG A 59  1 ? 7  
HELX_P HELX_P3  AA3 PRO A 74  ? ALA A 89  ? PRO A 76  ALA A 91  1 ? 16 
HELX_P HELX_P4  AA4 ALA A 92  ? GLN A 94  ? ALA A 94  GLN A 96  5 ? 3  
HELX_P HELX_P5  AA5 THR A 109 ? SER A 118 ? THR A 111 SER A 120 1 ? 10 
HELX_P HELX_P6  AA6 SER A 118 ? TYR A 125 ? SER A 120 TYR A 127 1 ? 8  
HELX_P HELX_P7  AA7 ARG A 134 ? GLU A 136 ? ARG A 136 GLU A 138 5 ? 3  
HELX_P HELX_P8  AA8 SER A 154 ? GLN A 158 ? SER A 156 GLN A 160 1 ? 5  
HELX_P HELX_P9  AA9 GLY A 178 ? ILE A 183 ? GLY A 180 ILE A 185 5 ? 6  
HELX_P HELX_P10 AB1 ALA A 189 ? HIS A 197 ? ALA A 191 HIS A 199 1 ? 9  
HELX_P HELX_P11 AB2 GLY A 198 ? GLU A 203 ? GLY A 200 GLU A 205 1 ? 6  
HELX_P HELX_P12 AB3 ASN A 215 ? GLY A 229 ? ASN A 217 GLY A 231 1 ? 15 
HELX_P HELX_P13 AB4 ASP A 251 ? VAL A 267 ? ASP A 253 VAL A 269 1 ? 17 
HELX_P HELX_P14 AB5 PRO A 286 ? LEU A 289 ? PRO A 288 LEU A 291 5 ? 4  
HELX_P HELX_P15 AB6 THR A 290 ? LEU A 302 ? THR A 292 LEU A 304 1 ? 13 
HELX_P HELX_P16 AB7 SER A 323 ? HIS A 333 ? SER A 325 HIS A 335 1 ? 11 
HELX_P HELX_P17 AB8 THR A 335 ? LYS A 345 ? THR A 337 LYS A 347 1 ? 11 
HELX_P HELX_P18 AB9 ASP A 352 ? ARG A 364 ? ASP A 354 ARG A 366 1 ? 13 
HELX_P HELX_P19 AC1 PRO A 376 ? SER A 381 ? PRO A 378 SER A 383 1 ? 6  
HELX_P HELX_P20 AC2 THR A 390 ? GLY A 403 ? THR A 392 GLY A 405 1 ? 14 
HELX_P HELX_P21 AC3 LYS A 413 ? VAL A 417 ? LYS A 415 VAL A 419 5 ? 5  
HELX_P HELX_P22 AC4 ASP B 34  ? GLU B 45  ? ASP B 36  GLU B 47  1 ? 12 
HELX_P HELX_P23 AC5 PRO B 51  ? ALA B 56  ? PRO B 53  ALA B 58  1 ? 6  
HELX_P HELX_P24 AC6 PRO B 74  ? ALA B 89  ? PRO B 76  ALA B 91  1 ? 16 
HELX_P HELX_P25 AC7 ALA B 92  ? GLN B 94  ? ALA B 94  GLN B 96  5 ? 3  
HELX_P HELX_P26 AC8 THR B 109 ? SER B 118 ? THR B 111 SER B 120 1 ? 10 
HELX_P HELX_P27 AC9 SER B 118 ? TYR B 125 ? SER B 120 TYR B 127 1 ? 8  
HELX_P HELX_P28 AD1 ARG B 134 ? GLU B 136 ? ARG B 136 GLU B 138 5 ? 3  
HELX_P HELX_P29 AD2 SER B 154 ? GLN B 158 ? SER B 156 GLN B 160 1 ? 5  
HELX_P HELX_P30 AD3 GLY B 178 ? ILE B 183 ? GLY B 180 ILE B 185 5 ? 6  
HELX_P HELX_P31 AD4 ALA B 189 ? HIS B 197 ? ALA B 191 HIS B 199 1 ? 9  
HELX_P HELX_P32 AD5 GLY B 198 ? GLU B 203 ? GLY B 200 GLU B 205 1 ? 6  
HELX_P HELX_P33 AD6 ASN B 215 ? GLY B 229 ? ASN B 217 GLY B 231 1 ? 15 
HELX_P HELX_P34 AD7 ASP B 251 ? VAL B 267 ? ASP B 253 VAL B 269 1 ? 17 
HELX_P HELX_P35 AD8 PRO B 286 ? LEU B 289 ? PRO B 288 LEU B 291 5 ? 4  
HELX_P HELX_P36 AD9 THR B 290 ? LEU B 302 ? THR B 292 LEU B 304 1 ? 13 
HELX_P HELX_P37 AE1 SER B 323 ? HIS B 333 ? SER B 325 HIS B 335 1 ? 11 
HELX_P HELX_P38 AE2 THR B 335 ? LYS B 345 ? THR B 337 LYS B 347 1 ? 11 
HELX_P HELX_P39 AE3 ASP B 352 ? ARG B 364 ? ASP B 354 ARG B 366 1 ? 13 
HELX_P HELX_P40 AE4 PRO B 376 ? SER B 381 ? PRO B 378 SER B 383 1 ? 6  
HELX_P HELX_P41 AE5 THR B 390 ? GLY B 403 ? THR B 392 GLY B 405 1 ? 14 
HELX_P HELX_P42 AE6 LYS B 413 ? VAL B 417 ? LYS B 415 VAL B 419 5 ? 5  
# 
_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 
covale1 covale none ? A LYS 181 NZ  ? ? ? 1_555 E 4EY . C7 ? ? A LYS 183 A 4EY 503 1_555 ? ? ? ? ? ? ? 1.426 ? ? 
covale2 covale none ? B LYS 181 NZ  ? ? ? 1_555 J 4EY . C7 ? ? B LYS 183 B 4EY 702 1_555 ? ? ? ? ? ? ? 1.432 ? ? 
metalc1 metalc ?    ? A HIS 197 NE2 A ? ? 1_555 H NI  . NI ? ? A HIS 199 A NI  506 1_555 ? ? ? ? ? ? ? 2.050 ? ? 
metalc2 metalc ?    ? A HIS 197 NE2 B ? ? 1_555 H NI  . NI ? ? A HIS 199 A NI  506 1_555 ? ? ? ? ? ? ? 2.077 ? ? 
metalc3 metalc ?    ? E 4EY .   S7  ? ? ? 1_555 H NI  . NI ? ? A 4EY 503 A NI  506 1_555 ? ? ? ? ? ? ? 2.202 ? ? 
metalc4 metalc ?    ? E 4EY .   S2  ? ? ? 1_555 H NI  . NI ? ? A 4EY 503 A NI  506 1_555 ? ? ? ? ? ? ? 2.190 ? ? 
metalc5 metalc ?    ? B HIS 197 NE2 ? ? ? 1_555 N NI  . NI ? ? B HIS 199 B NI  706 1_555 ? ? ? ? ? ? ? 2.079 ? ? 
metalc6 metalc ?    ? J 4EY .   S7  ? ? ? 1_555 N NI  . NI ? ? B 4EY 702 B NI  706 1_555 ? ? ? ? ? ? ? 2.195 ? ? 
metalc7 metalc ?    ? J 4EY .   S2  ? ? ? 1_555 N NI  . NI ? ? B 4EY 702 B NI  706 1_555 ? ? ? ? ? ? ? 2.257 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
covale ? ? 
metalc ? ? 
# 
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 NE2 A A HIS 197 ? A HIS 199 ? 1_555 NI ? H NI . ? A NI 506 ? 1_555 NE2 B A HIS 197 ? A HIS 199 ? 1_555 7.8   ? 
2 NE2 A A HIS 197 ? A HIS 199 ? 1_555 NI ? H NI . ? A NI 506 ? 1_555 S7  ? E 4EY .   ? A 4EY 503 ? 1_555 93.7  ? 
3 NE2 B A HIS 197 ? A HIS 199 ? 1_555 NI ? H NI . ? A NI 506 ? 1_555 S7  ? E 4EY .   ? A 4EY 503 ? 1_555 92.9  ? 
4 NE2 A A HIS 197 ? A HIS 199 ? 1_555 NI ? H NI . ? A NI 506 ? 1_555 S2  ? E 4EY .   ? A 4EY 503 ? 1_555 94.7  ? 
5 NE2 B A HIS 197 ? A HIS 199 ? 1_555 NI ? H NI . ? A NI 506 ? 1_555 S2  ? E 4EY .   ? A 4EY 503 ? 1_555 95.9  ? 
6 S7  ? E 4EY .   ? A 4EY 503 ? 1_555 NI ? H NI . ? A NI 506 ? 1_555 S2  ? E 4EY .   ? A 4EY 503 ? 1_555 170.7 ? 
7 NE2 ? B HIS 197 ? B HIS 199 ? 1_555 NI ? N NI . ? B NI 706 ? 1_555 S7  ? J 4EY .   ? B 4EY 702 ? 1_555 91.6  ? 
8 NE2 ? B HIS 197 ? B HIS 199 ? 1_555 NI ? N NI . ? B NI 706 ? 1_555 S2  ? J 4EY .   ? B 4EY 702 ? 1_555 96.0  ? 
9 S7  ? J 4EY .   ? B 4EY 702 ? 1_555 NI ? N NI . ? B NI 706 ? 1_555 S2  ? J 4EY .   ? B 4EY 702 ? 1_555 172.1 ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 4EY E . ? LYS A 181 ? 4EY A 503 ? 1_555 LYS A 183 ? 1_555 C7 NZ LYS 1 4EY None 'Covalent chemical modification' 
2 4EY J . ? LYS B 181 ? 4EY B 702 ? 1_555 LYS B 183 ? 1_555 C7 NZ LYS 1 4EY None 'Covalent chemical modification' 
# 
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 CYS 184 A . ? CYS 186 A PRO 185 A ? PRO 187 A 1 13.13 
2 HIS 285 A . ? HIS 287 A PRO 286 A ? PRO 288 A 1 7.52  
3 CYS 184 B . ? CYS 186 B PRO 185 B ? PRO 187 B 1 18.55 
4 HIS 285 B . ? HIS 287 B PRO 286 B ? PRO 288 B 1 5.50  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2 ? 
AA2 ? 6 ? 
AA3 ? 2 ? 
AA4 ? 2 ? 
AA5 ? 2 ? 
AA6 ? 5 ? 
AA7 ? 2 ? 
AA8 ? 6 ? 
AA9 ? 2 ? 
AB1 ? 2 ? 
AB2 ? 2 ? 
AB3 ? 5 ? 
# 
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 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? parallel      
AA2 3 4 ? parallel      
AA2 4 5 ? parallel      
AA2 5 6 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA5 1 2 ? parallel      
AA6 1 2 ? parallel      
AA6 2 3 ? parallel      
AA6 3 4 ? parallel      
AA6 4 5 ? parallel      
AA7 1 2 ? anti-parallel 
AA8 1 2 ? parallel      
AA8 2 3 ? parallel      
AA8 3 4 ? parallel      
AA8 4 5 ? parallel      
AA8 5 6 ? anti-parallel 
AA9 1 2 ? anti-parallel 
AB1 1 2 ? anti-parallel 
AB2 1 2 ? parallel      
AB3 1 2 ? parallel      
AB3 2 3 ? parallel      
AB3 3 4 ? parallel      
AB3 4 5 ? 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 VAL A 2   ? LEU A 4   ? VAL A 4   LEU A 6   
AA1 2 LEU A 11  ? VAL A 13  ? LEU A 13  VAL A 15  
AA2 1 ARG A 126 ? ASP A 129 ? ARG A 128 ASP A 131 
AA2 2 ILE A 96  ? ALA A 101 ? ILE A 98  ALA A 103 
AA2 3 ALA A 62  ? CYS A 67  ? ALA A 64  CYS A 69  
AA2 4 LEU A 161 ? LEU A 167 ? LEU A 163 LEU A 169 
AA2 5 PHE A 232 ? LEU A 238 ? PHE A 234 LEU A 240 
AA2 6 ILE A 244 ? GLY A 250 ? ILE A 246 GLY A 252 
AA3 1 HIS A 138 ? THR A 143 ? HIS A 140 THR A 145 
AA3 2 PRO A 149 ? ASP A 153 ? PRO A 151 ASP A 155 
AA4 1 PRO A 170 ? HIS A 171 ? PRO A 172 HIS A 173 
AA4 2 GLY A 175 ? TYR A 176 ? GLY A 177 TYR A 178 
AA5 1 LYS A 268 ? VAL A 271 ? LYS A 270 VAL A 273 
AA5 2 LEU A 418 ? VAL A 421 ? LEU A 420 VAL A 423 
AA6 1 GLU A 386 ? PRO A 387 ? GLU A 388 PRO A 389 
AA6 2 ARG A 367 ? VAL A 371 ? ARG A 369 VAL A 373 
AA6 3 VAL A 305 ? ALA A 314 ? VAL A 307 ALA A 316 
AA6 4 VAL A 275 ? SER A 281 ? VAL A 277 SER A 283 
AA6 5 VAL A 408 ? ILE A 411 ? VAL A 410 ILE A 413 
AA7 1 VAL B 2   ? LEU B 4   ? VAL B 4   LEU B 6   
AA7 2 LEU B 11  ? VAL B 13  ? LEU B 13  VAL B 15  
AA8 1 ARG B 126 ? ASP B 129 ? ARG B 128 ASP B 131 
AA8 2 ILE B 96  ? VAL B 100 ? ILE B 98  VAL B 102 
AA8 3 ALA B 62  ? VAL B 66  ? ALA B 64  VAL B 68  
AA8 4 LEU B 161 ? LEU B 167 ? LEU B 163 LEU B 169 
AA8 5 PHE B 232 ? LEU B 238 ? PHE B 234 LEU B 240 
AA8 6 ILE B 244 ? GLY B 250 ? ILE B 246 GLY B 252 
AA9 1 HIS B 138 ? THR B 143 ? HIS B 140 THR B 145 
AA9 2 PRO B 149 ? ASP B 153 ? PRO B 151 ASP B 155 
AB1 1 PRO B 170 ? HIS B 171 ? PRO B 172 HIS B 173 
AB1 2 GLY B 175 ? TYR B 176 ? GLY B 177 TYR B 178 
AB2 1 LYS B 268 ? VAL B 271 ? LYS B 270 VAL B 273 
AB2 2 LEU B 418 ? VAL B 421 ? LEU B 420 VAL B 423 
AB3 1 GLU B 386 ? PRO B 387 ? GLU B 388 PRO B 389 
AB3 2 ARG B 367 ? VAL B 371 ? ARG B 369 VAL B 373 
AB3 3 VAL B 305 ? ALA B 314 ? VAL B 307 ALA B 316 
AB3 4 VAL B 275 ? SER B 281 ? VAL B 277 SER B 283 
AB3 5 VAL B 408 ? ILE B 411 ? VAL B 410 ILE B 413 
# 
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 N VAL A 2   ? N VAL A 4   O VAL A 13  ? O VAL A 15  
AA2 1 2 O GLU A 128 ? O GLU A 130 N VAL A 100 ? N VAL A 102 
AA2 2 3 O ALA A 101 ? O ALA A 103 N VAL A 66  ? N VAL A 68  
AA2 3 4 N LEU A 65  ? N LEU A 67  O ILE A 163 ? O ILE A 165 
AA2 4 5 N ALA A 164 ? N ALA A 166 O PHE A 232 ? O PHE A 234 
AA2 5 6 N ASN A 235 ? N ASN A 237 O VAL A 248 ? O VAL A 250 
AA3 1 2 N GLY A 142 ? N GLY A 144 O ALA A 150 ? O ALA A 152 
AA4 1 2 N HIS A 171 ? N HIS A 173 O GLY A 175 ? O GLY A 177 
AA5 1 2 N VAL A 271 ? N VAL A 273 O VAL A 420 ? O VAL A 422 
AA6 1 2 O GLU A 386 ? O GLU A 388 N PHE A 370 ? N PHE A 372 
AA6 2 3 O VAL A 371 ? O VAL A 373 N ILE A 313 ? N ILE A 315 
AA6 3 4 O VAL A 312 ? O VAL A 314 N VAL A 278 ? N VAL A 280 
AA6 4 5 N VAL A 279 ? N VAL A 281 O ALA A 409 ? O ALA A 411 
AA7 1 2 N VAL B 2   ? N VAL B 4   O VAL B 13  ? O VAL B 15  
AA8 1 2 O GLU B 128 ? O GLU B 130 N VAL B 100 ? N VAL B 102 
AA8 2 3 O LEU B 97  ? O LEU B 99  N ILE B 64  ? N ILE B 66  
AA8 3 4 N LEU B 65  ? N LEU B 67  O ILE B 163 ? O ILE B 165 
AA8 4 5 N ALA B 164 ? N ALA B 166 O VAL B 234 ? O VAL B 236 
AA8 5 6 N ASN B 235 ? N ASN B 237 O VAL B 248 ? O VAL B 250 
AA9 1 2 N THR B 139 ? N THR B 141 O ILE B 152 ? O ILE B 154 
AB1 1 2 N HIS B 171 ? N HIS B 173 O GLY B 175 ? O GLY B 177 
AB2 1 2 N ALA B 269 ? N ALA B 271 O VAL B 420 ? O VAL B 422 
AB3 1 2 O GLU B 386 ? O GLU B 388 N VAL B 368 ? N VAL B 370 
AB3 2 3 O ARG B 367 ? O ARG B 369 N ILE B 311 ? N ILE B 313 
AB3 3 4 O VAL B 312 ? O VAL B 314 N THR B 280 ? N THR B 282 
AB3 4 5 N VAL B 279 ? N VAL B 281 O ALA B 409 ? O ALA B 411 
# 
_pdbx_entry_details.entry_id                   9EIA 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   Y 
# 
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 TYR A 8   ? ? -168.47 104.48 
2 1 SER A 120 ? ? 84.00   152.41 
3 1 LEU A 214 ? ? -116.47 -71.18 
4 1 CYS A 232 ? ? -161.56 119.82 
5 1 TYR B 8   ? ? -165.75 107.09 
6 1 PRO B 74  ? ? -74.68  49.07  
7 1 SER B 120 ? ? 80.41   148.39 
8 1 HIS B 199 ? ? -87.68  30.63  
# 
_pdbx_unobs_or_zero_occ_residues.id               1 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num    1 
_pdbx_unobs_or_zero_occ_residues.polymer_flag     Y 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag   1 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id     B 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id     LEU 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id      427 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code     ? 
_pdbx_unobs_or_zero_occ_residues.label_asym_id    B 
_pdbx_unobs_or_zero_occ_residues.label_comp_id    LEU 
_pdbx_unobs_or_zero_occ_residues.label_seq_id     425 
# 
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 
4EY C2   C  Y N 1   
4EY C3   C  Y N 2   
4EY C1   C  N N 3   
4EY C4   C  Y N 4   
4EY C5   C  Y N 5   
4EY C6   C  Y N 6   
4EY O2   O  N N 7   
4EY O2P  O  N N 8   
4EY P    P  N N 9   
4EY O3P  O  N N 10  
4EY O1P  O  N N 11  
4EY O5R  O  N N 12  
4EY C5R  C  N N 13  
4EY C4R  C  N R 14  
4EY O4R  O  N N 15  
4EY C3R  C  N S 16  
4EY O3R  O  N N 17  
4EY C2R  C  N R 18  
4EY O2R  O  N N 19  
4EY C1R  C  N R 20  
4EY N1   N  Y N 21  
4EY C7   C  N N 22  
4EY S7   S  N N 23  
4EY S2   S  N N 24  
4EY H1   H  N N 25  
4EY H2   H  N N 26  
4EY H3   H  N N 27  
4EY H4   H  N N 28  
4EY H5   H  N N 29  
4EY H6   H  N N 30  
4EY H7   H  N N 31  
4EY H8   H  N N 32  
4EY H9   H  N N 33  
4EY H10  H  N N 34  
4EY H11  H  N N 35  
4EY H12  H  N N 36  
4EY H13  H  N N 37  
4EY H14  H  N N 38  
4EY H15  H  N N 39  
ALA N    N  N N 40  
ALA CA   C  N S 41  
ALA C    C  N N 42  
ALA O    O  N N 43  
ALA CB   C  N N 44  
ALA OXT  O  N N 45  
ALA H    H  N N 46  
ALA H2   H  N N 47  
ALA HA   H  N N 48  
ALA HB1  H  N N 49  
ALA HB2  H  N N 50  
ALA HB3  H  N N 51  
ALA HXT  H  N N 52  
ARG N    N  N N 53  
ARG CA   C  N S 54  
ARG C    C  N N 55  
ARG O    O  N N 56  
ARG CB   C  N N 57  
ARG CG   C  N N 58  
ARG CD   C  N N 59  
ARG NE   N  N N 60  
ARG CZ   C  N N 61  
ARG NH1  N  N N 62  
ARG NH2  N  N N 63  
ARG OXT  O  N N 64  
ARG H    H  N N 65  
ARG H2   H  N N 66  
ARG HA   H  N N 67  
ARG HB2  H  N N 68  
ARG HB3  H  N N 69  
ARG HG2  H  N N 70  
ARG HG3  H  N N 71  
ARG HD2  H  N N 72  
ARG HD3  H  N N 73  
ARG HE   H  N N 74  
ARG HH11 H  N N 75  
ARG HH12 H  N N 76  
ARG HH21 H  N N 77  
ARG HH22 H  N N 78  
ARG HXT  H  N N 79  
ASN N    N  N N 80  
ASN CA   C  N S 81  
ASN C    C  N N 82  
ASN O    O  N N 83  
ASN CB   C  N N 84  
ASN CG   C  N N 85  
ASN OD1  O  N N 86  
ASN ND2  N  N N 87  
ASN OXT  O  N N 88  
ASN H    H  N N 89  
ASN H2   H  N N 90  
ASN HA   H  N N 91  
ASN HB2  H  N N 92  
ASN HB3  H  N N 93  
ASN HD21 H  N N 94  
ASN HD22 H  N N 95  
ASN HXT  H  N N 96  
ASP N    N  N N 97  
ASP CA   C  N S 98  
ASP C    C  N N 99  
ASP O    O  N N 100 
ASP CB   C  N N 101 
ASP CG   C  N N 102 
ASP OD1  O  N N 103 
ASP OD2  O  N N 104 
ASP OXT  O  N N 105 
ASP H    H  N N 106 
ASP H2   H  N N 107 
ASP HA   H  N N 108 
ASP HB2  H  N N 109 
ASP HB3  H  N N 110 
ASP HD2  H  N N 111 
ASP HXT  H  N N 112 
CYS N    N  N N 113 
CYS CA   C  N R 114 
CYS C    C  N N 115 
CYS O    O  N N 116 
CYS CB   C  N N 117 
CYS SG   S  N N 118 
CYS OXT  O  N N 119 
CYS H    H  N N 120 
CYS H2   H  N N 121 
CYS HA   H  N N 122 
CYS HB2  H  N N 123 
CYS HB3  H  N N 124 
CYS HG   H  N N 125 
CYS HXT  H  N N 126 
EDO C1   C  N N 127 
EDO O1   O  N N 128 
EDO C2   C  N N 129 
EDO O2   O  N N 130 
EDO H11  H  N N 131 
EDO H12  H  N N 132 
EDO HO1  H  N N 133 
EDO H21  H  N N 134 
EDO H22  H  N N 135 
EDO HO2  H  N N 136 
GLN N    N  N N 137 
GLN CA   C  N S 138 
GLN C    C  N N 139 
GLN O    O  N N 140 
GLN CB   C  N N 141 
GLN CG   C  N N 142 
GLN CD   C  N N 143 
GLN OE1  O  N N 144 
GLN NE2  N  N N 145 
GLN OXT  O  N N 146 
GLN H    H  N N 147 
GLN H2   H  N N 148 
GLN HA   H  N N 149 
GLN HB2  H  N N 150 
GLN HB3  H  N N 151 
GLN HG2  H  N N 152 
GLN HG3  H  N N 153 
GLN HE21 H  N N 154 
GLN HE22 H  N N 155 
GLN HXT  H  N N 156 
GLU N    N  N N 157 
GLU CA   C  N S 158 
GLU C    C  N N 159 
GLU O    O  N N 160 
GLU CB   C  N N 161 
GLU CG   C  N N 162 
GLU CD   C  N N 163 
GLU OE1  O  N N 164 
GLU OE2  O  N N 165 
GLU OXT  O  N N 166 
GLU H    H  N N 167 
GLU H2   H  N N 168 
GLU HA   H  N N 169 
GLU HB2  H  N N 170 
GLU HB3  H  N N 171 
GLU HG2  H  N N 172 
GLU HG3  H  N N 173 
GLU HE2  H  N N 174 
GLU HXT  H  N N 175 
GLY N    N  N N 176 
GLY CA   C  N N 177 
GLY C    C  N N 178 
GLY O    O  N N 179 
GLY OXT  O  N N 180 
GLY H    H  N N 181 
GLY H2   H  N N 182 
GLY HA2  H  N N 183 
GLY HA3  H  N N 184 
GLY HXT  H  N N 185 
HIS N    N  N N 186 
HIS CA   C  N S 187 
HIS C    C  N N 188 
HIS O    O  N N 189 
HIS CB   C  N N 190 
HIS CG   C  Y N 191 
HIS ND1  N  Y N 192 
HIS CD2  C  Y N 193 
HIS CE1  C  Y N 194 
HIS NE2  N  Y N 195 
HIS OXT  O  N N 196 
HIS H    H  N N 197 
HIS H2   H  N N 198 
HIS HA   H  N N 199 
HIS HB2  H  N N 200 
HIS HB3  H  N N 201 
HIS HD1  H  N N 202 
HIS HD2  H  N N 203 
HIS HE1  H  N N 204 
HIS HE2  H  N N 205 
HIS HXT  H  N N 206 
HOH O    O  N N 207 
HOH H1   H  N N 208 
HOH H2   H  N N 209 
ILE N    N  N N 210 
ILE CA   C  N S 211 
ILE C    C  N N 212 
ILE O    O  N N 213 
ILE CB   C  N S 214 
ILE CG1  C  N N 215 
ILE CG2  C  N N 216 
ILE CD1  C  N N 217 
ILE OXT  O  N N 218 
ILE H    H  N N 219 
ILE H2   H  N N 220 
ILE HA   H  N N 221 
ILE HB   H  N N 222 
ILE HG12 H  N N 223 
ILE HG13 H  N N 224 
ILE HG21 H  N N 225 
ILE HG22 H  N N 226 
ILE HG23 H  N N 227 
ILE HD11 H  N N 228 
ILE HD12 H  N N 229 
ILE HD13 H  N N 230 
ILE HXT  H  N N 231 
LAC C    C  N N 232 
LAC CA   C  N R 233 
LAC CB   C  N N 234 
LAC O    O  N N 235 
LAC OHN  O  N N 236 
LAC OXT  O  N N 237 
LAC HA   H  N N 238 
LAC HB1  H  N N 239 
LAC HB2  H  N N 240 
LAC HB3  H  N N 241 
LAC H    H  N N 242 
LAC HXT  H  N N 243 
LEU N    N  N N 244 
LEU CA   C  N S 245 
LEU C    C  N N 246 
LEU O    O  N N 247 
LEU CB   C  N N 248 
LEU CG   C  N N 249 
LEU CD1  C  N N 250 
LEU CD2  C  N N 251 
LEU OXT  O  N N 252 
LEU H    H  N N 253 
LEU H2   H  N N 254 
LEU HA   H  N N 255 
LEU HB2  H  N N 256 
LEU HB3  H  N N 257 
LEU HG   H  N N 258 
LEU HD11 H  N N 259 
LEU HD12 H  N N 260 
LEU HD13 H  N N 261 
LEU HD21 H  N N 262 
LEU HD22 H  N N 263 
LEU HD23 H  N N 264 
LEU HXT  H  N N 265 
LYS N    N  N N 266 
LYS CA   C  N S 267 
LYS C    C  N N 268 
LYS O    O  N N 269 
LYS CB   C  N N 270 
LYS CG   C  N N 271 
LYS CD   C  N N 272 
LYS CE   C  N N 273 
LYS NZ   N  N N 274 
LYS OXT  O  N N 275 
LYS H    H  N N 276 
LYS H2   H  N N 277 
LYS HA   H  N N 278 
LYS HB2  H  N N 279 
LYS HB3  H  N N 280 
LYS HG2  H  N N 281 
LYS HG3  H  N N 282 
LYS HD2  H  N N 283 
LYS HD3  H  N N 284 
LYS HE2  H  N N 285 
LYS HE3  H  N N 286 
LYS HZ1  H  N N 287 
LYS HZ2  H  N N 288 
LYS HZ3  H  N N 289 
LYS HXT  H  N N 290 
MET N    N  N N 291 
MET CA   C  N S 292 
MET C    C  N N 293 
MET O    O  N N 294 
MET CB   C  N N 295 
MET CG   C  N N 296 
MET SD   S  N N 297 
MET CE   C  N N 298 
MET OXT  O  N N 299 
MET H    H  N N 300 
MET H2   H  N N 301 
MET HA   H  N N 302 
MET HB2  H  N N 303 
MET HB3  H  N N 304 
MET HG2  H  N N 305 
MET HG3  H  N N 306 
MET HE1  H  N N 307 
MET HE2  H  N N 308 
MET HE3  H  N N 309 
MET HXT  H  N N 310 
NI  NI   NI N N 311 
PEG C1   C  N N 312 
PEG O1   O  N N 313 
PEG C2   C  N N 314 
PEG O2   O  N N 315 
PEG C3   C  N N 316 
PEG C4   C  N N 317 
PEG O4   O  N N 318 
PEG H11  H  N N 319 
PEG H12  H  N N 320 
PEG HO1  H  N N 321 
PEG H21  H  N N 322 
PEG H22  H  N N 323 
PEG H31  H  N N 324 
PEG H32  H  N N 325 
PEG H41  H  N N 326 
PEG H42  H  N N 327 
PEG HO4  H  N N 328 
PHE N    N  N N 329 
PHE CA   C  N S 330 
PHE C    C  N N 331 
PHE O    O  N N 332 
PHE CB   C  N N 333 
PHE CG   C  Y N 334 
PHE CD1  C  Y N 335 
PHE CD2  C  Y N 336 
PHE CE1  C  Y N 337 
PHE CE2  C  Y N 338 
PHE CZ   C  Y N 339 
PHE OXT  O  N N 340 
PHE H    H  N N 341 
PHE H2   H  N N 342 
PHE HA   H  N N 343 
PHE HB2  H  N N 344 
PHE HB3  H  N N 345 
PHE HD1  H  N N 346 
PHE HD2  H  N N 347 
PHE HE1  H  N N 348 
PHE HE2  H  N N 349 
PHE HZ   H  N N 350 
PHE HXT  H  N N 351 
PRO N    N  N N 352 
PRO CA   C  N S 353 
PRO C    C  N N 354 
PRO O    O  N N 355 
PRO CB   C  N N 356 
PRO CG   C  N N 357 
PRO CD   C  N N 358 
PRO OXT  O  N N 359 
PRO H    H  N N 360 
PRO HA   H  N N 361 
PRO HB2  H  N N 362 
PRO HB3  H  N N 363 
PRO HG2  H  N N 364 
PRO HG3  H  N N 365 
PRO HD2  H  N N 366 
PRO HD3  H  N N 367 
PRO HXT  H  N N 368 
SER N    N  N N 369 
SER CA   C  N S 370 
SER C    C  N N 371 
SER O    O  N N 372 
SER CB   C  N N 373 
SER OG   O  N N 374 
SER OXT  O  N N 375 
SER H    H  N N 376 
SER H2   H  N N 377 
SER HA   H  N N 378 
SER HB2  H  N N 379 
SER HB3  H  N N 380 
SER HG   H  N N 381 
SER HXT  H  N N 382 
THR N    N  N N 383 
THR CA   C  N S 384 
THR C    C  N N 385 
THR O    O  N N 386 
THR CB   C  N R 387 
THR OG1  O  N N 388 
THR CG2  C  N N 389 
THR OXT  O  N N 390 
THR H    H  N N 391 
THR H2   H  N N 392 
THR HA   H  N N 393 
THR HB   H  N N 394 
THR HG1  H  N N 395 
THR HG21 H  N N 396 
THR HG22 H  N N 397 
THR HG23 H  N N 398 
THR HXT  H  N N 399 
TRP N    N  N N 400 
TRP CA   C  N S 401 
TRP C    C  N N 402 
TRP O    O  N N 403 
TRP CB   C  N N 404 
TRP CG   C  Y N 405 
TRP CD1  C  Y N 406 
TRP CD2  C  Y N 407 
TRP NE1  N  Y N 408 
TRP CE2  C  Y N 409 
TRP CE3  C  Y N 410 
TRP CZ2  C  Y N 411 
TRP CZ3  C  Y N 412 
TRP CH2  C  Y N 413 
TRP OXT  O  N N 414 
TRP H    H  N N 415 
TRP H2   H  N N 416 
TRP HA   H  N N 417 
TRP HB2  H  N N 418 
TRP HB3  H  N N 419 
TRP HD1  H  N N 420 
TRP HE1  H  N N 421 
TRP HE3  H  N N 422 
TRP HZ2  H  N N 423 
TRP HZ3  H  N N 424 
TRP HH2  H  N N 425 
TRP HXT  H  N N 426 
TYR N    N  N N 427 
TYR CA   C  N S 428 
TYR C    C  N N 429 
TYR O    O  N N 430 
TYR CB   C  N N 431 
TYR CG   C  Y N 432 
TYR CD1  C  Y N 433 
TYR CD2  C  Y N 434 
TYR CE1  C  Y N 435 
TYR CE2  C  Y N 436 
TYR CZ   C  Y N 437 
TYR OH   O  N N 438 
TYR OXT  O  N N 439 
TYR H    H  N N 440 
TYR H2   H  N N 441 
TYR HA   H  N N 442 
TYR HB2  H  N N 443 
TYR HB3  H  N N 444 
TYR HD1  H  N N 445 
TYR HD2  H  N N 446 
TYR HE1  H  N N 447 
TYR HE2  H  N N 448 
TYR HH   H  N N 449 
TYR HXT  H  N N 450 
VAL N    N  N N 451 
VAL CA   C  N S 452 
VAL C    C  N N 453 
VAL O    O  N N 454 
VAL CB   C  N N 455 
VAL CG1  C  N N 456 
VAL CG2  C  N N 457 
VAL OXT  O  N N 458 
VAL H    H  N N 459 
VAL H2   H  N N 460 
VAL HA   H  N N 461 
VAL HB   H  N N 462 
VAL HG11 H  N N 463 
VAL HG12 H  N N 464 
VAL HG13 H  N N 465 
VAL HG21 H  N N 466 
VAL HG22 H  N N 467 
VAL HG23 H  N N 468 
VAL HXT  H  N N 469 
# 
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 
4EY O4R C4R  sing N N 1   
4EY O4R C1R  sing N N 2   
4EY O3R C3R  sing N N 3   
4EY C4R C3R  sing N N 4   
4EY C4R C5R  sing N N 5   
4EY C1R N1   sing N N 6   
4EY C1R C2R  sing N N 7   
4EY O2  C1   doub N N 8   
4EY C3R C2R  sing N N 9   
4EY C6  N1   doub Y N 10  
4EY C6  C5   sing Y N 11  
4EY C5R O5R  sing N N 12  
4EY N1  C2   sing Y N 13  
4EY O2R C2R  sing N N 14  
4EY C1  C5   sing N N 15  
4EY C1  S2   sing N N 16  
4EY C5  C4   doub Y N 17  
4EY C2  C3   doub Y N 18  
4EY O5R P    sing N N 19  
4EY C4  C3   sing Y N 20  
4EY C3  C7   sing N N 21  
4EY C7  S7   doub N N 22  
4EY P   O3P  doub N N 23  
4EY P   O1P  sing N N 24  
4EY P   O2P  sing N N 25  
4EY C2  H1   sing N N 26  
4EY C4  H2   sing N N 27  
4EY C6  H3   sing N N 28  
4EY O2P H4   sing N N 29  
4EY O1P H5   sing N N 30  
4EY C5R H6   sing N N 31  
4EY C5R H7   sing N N 32  
4EY C4R H8   sing N N 33  
4EY C3R H9   sing N N 34  
4EY O3R H10  sing N N 35  
4EY C2R H11  sing N N 36  
4EY O2R H12  sing N N 37  
4EY C1R H13  sing N N 38  
4EY C7  H14  sing N N 39  
4EY S2  H15  sing N N 40  
ALA N   CA   sing N N 41  
ALA N   H    sing N N 42  
ALA N   H2   sing N N 43  
ALA CA  C    sing N N 44  
ALA CA  CB   sing N N 45  
ALA CA  HA   sing N N 46  
ALA C   O    doub N N 47  
ALA C   OXT  sing N N 48  
ALA CB  HB1  sing N N 49  
ALA CB  HB2  sing N N 50  
ALA CB  HB3  sing N N 51  
ALA OXT HXT  sing N N 52  
ARG N   CA   sing N N 53  
ARG N   H    sing N N 54  
ARG N   H2   sing N N 55  
ARG CA  C    sing N N 56  
ARG CA  CB   sing N N 57  
ARG CA  HA   sing N N 58  
ARG C   O    doub N N 59  
ARG C   OXT  sing N N 60  
ARG CB  CG   sing N N 61  
ARG CB  HB2  sing N N 62  
ARG CB  HB3  sing N N 63  
ARG CG  CD   sing N N 64  
ARG CG  HG2  sing N N 65  
ARG CG  HG3  sing N N 66  
ARG CD  NE   sing N N 67  
ARG CD  HD2  sing N N 68  
ARG CD  HD3  sing N N 69  
ARG NE  CZ   sing N N 70  
ARG NE  HE   sing N N 71  
ARG CZ  NH1  sing N N 72  
ARG CZ  NH2  doub N N 73  
ARG NH1 HH11 sing N N 74  
ARG NH1 HH12 sing N N 75  
ARG NH2 HH21 sing N N 76  
ARG NH2 HH22 sing N N 77  
ARG OXT HXT  sing N N 78  
ASN N   CA   sing N N 79  
ASN N   H    sing N N 80  
ASN N   H2   sing N N 81  
ASN CA  C    sing N N 82  
ASN CA  CB   sing N N 83  
ASN CA  HA   sing N N 84  
ASN C   O    doub N N 85  
ASN C   OXT  sing N N 86  
ASN CB  CG   sing N N 87  
ASN CB  HB2  sing N N 88  
ASN CB  HB3  sing N N 89  
ASN CG  OD1  doub N N 90  
ASN CG  ND2  sing N N 91  
ASN ND2 HD21 sing N N 92  
ASN ND2 HD22 sing N N 93  
ASN OXT HXT  sing N N 94  
ASP N   CA   sing N N 95  
ASP N   H    sing N N 96  
ASP N   H2   sing N N 97  
ASP CA  C    sing N N 98  
ASP CA  CB   sing N N 99  
ASP CA  HA   sing N N 100 
ASP C   O    doub N N 101 
ASP C   OXT  sing N N 102 
ASP CB  CG   sing N N 103 
ASP CB  HB2  sing N N 104 
ASP CB  HB3  sing N N 105 
ASP CG  OD1  doub N N 106 
ASP CG  OD2  sing N N 107 
ASP OD2 HD2  sing N N 108 
ASP OXT HXT  sing N N 109 
CYS N   CA   sing N N 110 
CYS N   H    sing N N 111 
CYS N   H2   sing N N 112 
CYS CA  C    sing N N 113 
CYS CA  CB   sing N N 114 
CYS CA  HA   sing N N 115 
CYS C   O    doub N N 116 
CYS C   OXT  sing N N 117 
CYS CB  SG   sing N N 118 
CYS CB  HB2  sing N N 119 
CYS CB  HB3  sing N N 120 
CYS SG  HG   sing N N 121 
CYS OXT HXT  sing N N 122 
EDO C1  O1   sing N N 123 
EDO C1  C2   sing N N 124 
EDO C1  H11  sing N N 125 
EDO C1  H12  sing N N 126 
EDO O1  HO1  sing N N 127 
EDO C2  O2   sing N N 128 
EDO C2  H21  sing N N 129 
EDO C2  H22  sing N N 130 
EDO O2  HO2  sing N N 131 
GLN N   CA   sing N N 132 
GLN N   H    sing N N 133 
GLN N   H2   sing N N 134 
GLN CA  C    sing N N 135 
GLN CA  CB   sing N N 136 
GLN CA  HA   sing N N 137 
GLN C   O    doub N N 138 
GLN C   OXT  sing N N 139 
GLN CB  CG   sing N N 140 
GLN CB  HB2  sing N N 141 
GLN CB  HB3  sing N N 142 
GLN CG  CD   sing N N 143 
GLN CG  HG2  sing N N 144 
GLN CG  HG3  sing N N 145 
GLN CD  OE1  doub N N 146 
GLN CD  NE2  sing N N 147 
GLN NE2 HE21 sing N N 148 
GLN NE2 HE22 sing N N 149 
GLN OXT HXT  sing N N 150 
GLU N   CA   sing N N 151 
GLU N   H    sing N N 152 
GLU N   H2   sing N N 153 
GLU CA  C    sing N N 154 
GLU CA  CB   sing N N 155 
GLU CA  HA   sing N N 156 
GLU C   O    doub N N 157 
GLU C   OXT  sing N N 158 
GLU CB  CG   sing N N 159 
GLU CB  HB2  sing N N 160 
GLU CB  HB3  sing N N 161 
GLU CG  CD   sing N N 162 
GLU CG  HG2  sing N N 163 
GLU CG  HG3  sing N N 164 
GLU CD  OE1  doub N N 165 
GLU CD  OE2  sing N N 166 
GLU OE2 HE2  sing N N 167 
GLU OXT HXT  sing N N 168 
GLY N   CA   sing N N 169 
GLY N   H    sing N N 170 
GLY N   H2   sing N N 171 
GLY CA  C    sing N N 172 
GLY CA  HA2  sing N N 173 
GLY CA  HA3  sing N N 174 
GLY C   O    doub N N 175 
GLY C   OXT  sing N N 176 
GLY OXT HXT  sing N N 177 
HIS N   CA   sing N N 178 
HIS N   H    sing N N 179 
HIS N   H2   sing N N 180 
HIS CA  C    sing N N 181 
HIS CA  CB   sing N N 182 
HIS CA  HA   sing N N 183 
HIS C   O    doub N N 184 
HIS C   OXT  sing N N 185 
HIS CB  CG   sing N N 186 
HIS CB  HB2  sing N N 187 
HIS CB  HB3  sing N N 188 
HIS CG  ND1  sing Y N 189 
HIS CG  CD2  doub Y N 190 
HIS ND1 CE1  doub Y N 191 
HIS ND1 HD1  sing N N 192 
HIS CD2 NE2  sing Y N 193 
HIS CD2 HD2  sing N N 194 
HIS CE1 NE2  sing Y N 195 
HIS CE1 HE1  sing N N 196 
HIS NE2 HE2  sing N N 197 
HIS OXT HXT  sing N N 198 
HOH O   H1   sing N N 199 
HOH O   H2   sing N N 200 
ILE N   CA   sing N N 201 
ILE N   H    sing N N 202 
ILE N   H2   sing N N 203 
ILE CA  C    sing N N 204 
ILE CA  CB   sing N N 205 
ILE CA  HA   sing N N 206 
ILE C   O    doub N N 207 
ILE C   OXT  sing N N 208 
ILE CB  CG1  sing N N 209 
ILE CB  CG2  sing N N 210 
ILE CB  HB   sing N N 211 
ILE CG1 CD1  sing N N 212 
ILE CG1 HG12 sing N N 213 
ILE CG1 HG13 sing N N 214 
ILE CG2 HG21 sing N N 215 
ILE CG2 HG22 sing N N 216 
ILE CG2 HG23 sing N N 217 
ILE CD1 HD11 sing N N 218 
ILE CD1 HD12 sing N N 219 
ILE CD1 HD13 sing N N 220 
ILE OXT HXT  sing N N 221 
LAC C   CA   sing N N 222 
LAC C   O    doub N N 223 
LAC C   OXT  sing N N 224 
LAC CA  CB   sing N N 225 
LAC CA  OHN  sing N N 226 
LAC CA  HA   sing N N 227 
LAC CB  HB1  sing N N 228 
LAC CB  HB2  sing N N 229 
LAC CB  HB3  sing N N 230 
LAC OHN H    sing N N 231 
LAC OXT HXT  sing N N 232 
LEU N   CA   sing N N 233 
LEU N   H    sing N N 234 
LEU N   H2   sing N N 235 
LEU CA  C    sing N N 236 
LEU CA  CB   sing N N 237 
LEU CA  HA   sing N N 238 
LEU C   O    doub N N 239 
LEU C   OXT  sing N N 240 
LEU CB  CG   sing N N 241 
LEU CB  HB2  sing N N 242 
LEU CB  HB3  sing N N 243 
LEU CG  CD1  sing N N 244 
LEU CG  CD2  sing N N 245 
LEU CG  HG   sing N N 246 
LEU CD1 HD11 sing N N 247 
LEU CD1 HD12 sing N N 248 
LEU CD1 HD13 sing N N 249 
LEU CD2 HD21 sing N N 250 
LEU CD2 HD22 sing N N 251 
LEU CD2 HD23 sing N N 252 
LEU OXT HXT  sing N N 253 
LYS N   CA   sing N N 254 
LYS N   H    sing N N 255 
LYS N   H2   sing N N 256 
LYS CA  C    sing N N 257 
LYS CA  CB   sing N N 258 
LYS CA  HA   sing N N 259 
LYS C   O    doub N N 260 
LYS C   OXT  sing N N 261 
LYS CB  CG   sing N N 262 
LYS CB  HB2  sing N N 263 
LYS CB  HB3  sing N N 264 
LYS CG  CD   sing N N 265 
LYS CG  HG2  sing N N 266 
LYS CG  HG3  sing N N 267 
LYS CD  CE   sing N N 268 
LYS CD  HD2  sing N N 269 
LYS CD  HD3  sing N N 270 
LYS CE  NZ   sing N N 271 
LYS CE  HE2  sing N N 272 
LYS CE  HE3  sing N N 273 
LYS NZ  HZ1  sing N N 274 
LYS NZ  HZ2  sing N N 275 
LYS NZ  HZ3  sing N N 276 
LYS OXT HXT  sing N N 277 
MET N   CA   sing N N 278 
MET N   H    sing N N 279 
MET N   H2   sing N N 280 
MET CA  C    sing N N 281 
MET CA  CB   sing N N 282 
MET CA  HA   sing N N 283 
MET C   O    doub N N 284 
MET C   OXT  sing N N 285 
MET CB  CG   sing N N 286 
MET CB  HB2  sing N N 287 
MET CB  HB3  sing N N 288 
MET CG  SD   sing N N 289 
MET CG  HG2  sing N N 290 
MET CG  HG3  sing N N 291 
MET SD  CE   sing N N 292 
MET CE  HE1  sing N N 293 
MET CE  HE2  sing N N 294 
MET CE  HE3  sing N N 295 
MET OXT HXT  sing N N 296 
PEG C1  O1   sing N N 297 
PEG C1  C2   sing N N 298 
PEG C1  H11  sing N N 299 
PEG C1  H12  sing N N 300 
PEG O1  HO1  sing N N 301 
PEG C2  O2   sing N N 302 
PEG C2  H21  sing N N 303 
PEG C2  H22  sing N N 304 
PEG O2  C3   sing N N 305 
PEG C3  C4   sing N N 306 
PEG C3  H31  sing N N 307 
PEG C3  H32  sing N N 308 
PEG C4  O4   sing N N 309 
PEG C4  H41  sing N N 310 
PEG C4  H42  sing N N 311 
PEG O4  HO4  sing N N 312 
PHE N   CA   sing N N 313 
PHE N   H    sing N N 314 
PHE N   H2   sing N N 315 
PHE CA  C    sing N N 316 
PHE CA  CB   sing N N 317 
PHE CA  HA   sing N N 318 
PHE C   O    doub N N 319 
PHE C   OXT  sing N N 320 
PHE CB  CG   sing N N 321 
PHE CB  HB2  sing N N 322 
PHE CB  HB3  sing N N 323 
PHE CG  CD1  doub Y N 324 
PHE CG  CD2  sing Y N 325 
PHE CD1 CE1  sing Y N 326 
PHE CD1 HD1  sing N N 327 
PHE CD2 CE2  doub Y N 328 
PHE CD2 HD2  sing N N 329 
PHE CE1 CZ   doub Y N 330 
PHE CE1 HE1  sing N N 331 
PHE CE2 CZ   sing Y N 332 
PHE CE2 HE2  sing N N 333 
PHE CZ  HZ   sing N N 334 
PHE OXT HXT  sing N N 335 
PRO N   CA   sing N N 336 
PRO N   CD   sing N N 337 
PRO N   H    sing N N 338 
PRO CA  C    sing N N 339 
PRO CA  CB   sing N N 340 
PRO CA  HA   sing N N 341 
PRO C   O    doub N N 342 
PRO C   OXT  sing N N 343 
PRO CB  CG   sing N N 344 
PRO CB  HB2  sing N N 345 
PRO CB  HB3  sing N N 346 
PRO CG  CD   sing N N 347 
PRO CG  HG2  sing N N 348 
PRO CG  HG3  sing N N 349 
PRO CD  HD2  sing N N 350 
PRO CD  HD3  sing N N 351 
PRO OXT HXT  sing N N 352 
SER N   CA   sing N N 353 
SER N   H    sing N N 354 
SER N   H2   sing N N 355 
SER CA  C    sing N N 356 
SER CA  CB   sing N N 357 
SER CA  HA   sing N N 358 
SER C   O    doub N N 359 
SER C   OXT  sing N N 360 
SER CB  OG   sing N N 361 
SER CB  HB2  sing N N 362 
SER CB  HB3  sing N N 363 
SER OG  HG   sing N N 364 
SER OXT HXT  sing N N 365 
THR N   CA   sing N N 366 
THR N   H    sing N N 367 
THR N   H2   sing N N 368 
THR CA  C    sing N N 369 
THR CA  CB   sing N N 370 
THR CA  HA   sing N N 371 
THR C   O    doub N N 372 
THR C   OXT  sing N N 373 
THR CB  OG1  sing N N 374 
THR CB  CG2  sing N N 375 
THR CB  HB   sing N N 376 
THR OG1 HG1  sing N N 377 
THR CG2 HG21 sing N N 378 
THR CG2 HG22 sing N N 379 
THR CG2 HG23 sing N N 380 
THR OXT HXT  sing N N 381 
TRP N   CA   sing N N 382 
TRP N   H    sing N N 383 
TRP N   H2   sing N N 384 
TRP CA  C    sing N N 385 
TRP CA  CB   sing N N 386 
TRP CA  HA   sing N N 387 
TRP C   O    doub N N 388 
TRP C   OXT  sing N N 389 
TRP CB  CG   sing N N 390 
TRP CB  HB2  sing N N 391 
TRP CB  HB3  sing N N 392 
TRP CG  CD1  doub Y N 393 
TRP CG  CD2  sing Y N 394 
TRP CD1 NE1  sing Y N 395 
TRP CD1 HD1  sing N N 396 
TRP CD2 CE2  doub Y N 397 
TRP CD2 CE3  sing Y N 398 
TRP NE1 CE2  sing Y N 399 
TRP NE1 HE1  sing N N 400 
TRP CE2 CZ2  sing Y N 401 
TRP CE3 CZ3  doub Y N 402 
TRP CE3 HE3  sing N N 403 
TRP CZ2 CH2  doub Y N 404 
TRP CZ2 HZ2  sing N N 405 
TRP CZ3 CH2  sing Y N 406 
TRP CZ3 HZ3  sing N N 407 
TRP CH2 HH2  sing N N 408 
TRP OXT HXT  sing N N 409 
TYR N   CA   sing N N 410 
TYR N   H    sing N N 411 
TYR N   H2   sing N N 412 
TYR CA  C    sing N N 413 
TYR CA  CB   sing N N 414 
TYR CA  HA   sing N N 415 
TYR C   O    doub N N 416 
TYR C   OXT  sing N N 417 
TYR CB  CG   sing N N 418 
TYR CB  HB2  sing N N 419 
TYR CB  HB3  sing N N 420 
TYR CG  CD1  doub Y N 421 
TYR CG  CD2  sing Y N 422 
TYR CD1 CE1  sing Y N 423 
TYR CD1 HD1  sing N N 424 
TYR CD2 CE2  doub Y N 425 
TYR CD2 HD2  sing N N 426 
TYR CE1 CZ   doub Y N 427 
TYR CE1 HE1  sing N N 428 
TYR CE2 CZ   sing Y N 429 
TYR CE2 HE2  sing N N 430 
TYR CZ  OH   sing N N 431 
TYR OH  HH   sing N N 432 
TYR OXT HXT  sing N N 433 
VAL N   CA   sing N N 434 
VAL N   H    sing N N 435 
VAL N   H2   sing N N 436 
VAL CA  C    sing N N 437 
VAL CA  CB   sing N N 438 
VAL CA  HA   sing N N 439 
VAL C   O    doub N N 440 
VAL C   OXT  sing N N 441 
VAL CB  CG1  sing N N 442 
VAL CB  CG2  sing N N 443 
VAL CB  HB   sing N N 444 
VAL CG1 HG11 sing N N 445 
VAL CG1 HG12 sing N N 446 
VAL CG1 HG13 sing N N 447 
VAL CG2 HG21 sing N N 448 
VAL CG2 HG22 sing N N 449 
VAL CG2 HG23 sing N N 450 
VAL OXT HXT  sing N N 451 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)' 'United States' GM128959 1 
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)' 'United States' GM140931 2 
# 
_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      PDB 
_pdbx_initial_refinement_model.accession_code   5HUQ 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9EIA 
_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]   0.012591 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000264 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.021971 
_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]   0.008395 
_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 
C  
N  
NI 
O  
P  
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   . ARG A 1 1   ? -10.583 8.329   11.906  1.00 29.69 ?  3    ARG A N   1 
ATOM   2    C  CA  . ARG A 1 1   ? -9.956  7.433   10.935  1.00 21.49 ?  3    ARG A CA  1 
ATOM   3    C  C   . ARG A 1 1   ? -8.658  8.028   10.413  1.00 19.75 ?  3    ARG A C   1 
ATOM   4    O  O   . ARG A 1 1   ? -8.590  9.199   10.062  1.00 21.80 ?  3    ARG A O   1 
ATOM   5    C  CB  . ARG A 1 1   ? -10.902 7.144   9.767   1.00 20.30 ?  3    ARG A CB  1 
ATOM   6    N  N   . VAL A 1 2   ? -7.616  7.212   10.350  1.00 17.01 ?  4    VAL A N   1 
ATOM   7    C  CA  . VAL A 1 2   ? -6.335  7.650   9.828   1.00 16.20 ?  4    VAL A CA  1 
ATOM   8    C  C   . VAL A 1 2   ? -5.713  6.476   9.098   1.00 15.83 ?  4    VAL A C   1 
ATOM   9    O  O   . VAL A 1 2   ? -5.943  5.316   9.449   1.00 16.24 ?  4    VAL A O   1 
ATOM   10   C  CB  . VAL A 1 2   ? -5.409  8.173   10.952  1.00 19.53 ?  4    VAL A CB  1 
ATOM   11   C  CG1 . VAL A 1 2   ? -5.039  7.065   11.905  1.00 16.70 ?  4    VAL A CG1 1 
ATOM   12   C  CG2 . VAL A 1 2   ? -4.164  8.790   10.366  1.00 25.55 ?  4    VAL A CG2 1 
ATOM   13   N  N   . THR A 1 3   ? -4.943  6.775   8.056   1.00 13.76 ?  5    THR A N   1 
ATOM   14   C  CA  . THR A 1 3   ? -4.207  5.750   7.328   1.00 12.11 ?  5    THR A CA  1 
ATOM   15   C  C   . THR A 1 3   ? -2.753  5.831   7.780   1.00 13.56 ?  5    THR A C   1 
ATOM   16   O  O   . THR A 1 3   ? -2.079  6.834   7.525   1.00 14.63 ?  5    THR A O   1 
ATOM   17   C  CB  . THR A 1 3   ? -4.307  5.927   5.816   1.00 15.49 ?  5    THR A CB  1 
ATOM   18   O  OG1 . THR A 1 3   ? -5.683  5.892   5.411   1.00 16.01 ?  5    THR A OG1 1 
ATOM   19   C  CG2 . THR A 1 3   ? -3.593  4.779   5.116   1.00 13.58 ?  5    THR A CG2 1 
ATOM   20   N  N   . LEU A 1 4   ? -2.282  4.789   8.457   1.00 9.46  ?  6    LEU A N   1 
ATOM   21   C  CA  . LEU A 1 4   ? -0.866  4.688   8.806   1.00 9.54  ?  6    LEU A CA  1 
ATOM   22   C  C   . LEU A 1 4   ? -0.099  4.108   7.623   1.00 11.13 ?  6    LEU A C   1 
ATOM   23   O  O   . LEU A 1 4   ? -0.621  3.246   6.912   1.00 13.30 ?  6    LEU A O   1 
ATOM   24   C  CB  . LEU A 1 4   ? -0.663  3.776   10.022  1.00 10.51 ?  6    LEU A CB  1 
ATOM   25   C  CG  . LEU A 1 4   ? -1.421  4.038   11.323  1.00 15.01 ?  6    LEU A CG  1 
ATOM   26   C  CD1 . LEU A 1 4   ? -1.104  2.954   12.375  1.00 12.78 ?  6    LEU A CD1 1 
ATOM   27   C  CD2 . LEU A 1 4   ? -1.075  5.423   11.862  1.00 15.88 ?  6    LEU A CD2 1 
ATOM   28   N  N   . ASP A 1 5   ? 1.145   4.557   7.411   1.00 9.99  ?  7    ASP A N   1 
ATOM   29   C  CA  . ASP A 1 5   ? 1.992   3.844   6.449   1.00 11.11 ?  7    ASP A CA  1 
ATOM   30   C  C   . ASP A 1 5   ? 2.188   2.404   6.889   1.00 9.19  ?  7    ASP A C   1 
ATOM   31   O  O   . ASP A 1 5   ? 2.368   2.124   8.074   1.00 11.34 ?  7    ASP A O   1 
ATOM   32   C  CB  . ASP A 1 5   ? 3.377   4.479   6.252   1.00 9.32  ?  7    ASP A CB  1 
ATOM   33   C  CG  . ASP A 1 5   ? 3.338   5.884   5.705   1.00 21.23 ?  7    ASP A CG  1 
ATOM   34   O  OD1 . ASP A 1 5   ? 4.412   6.534   5.766   1.00 20.96 ?  7    ASP A OD1 1 
ATOM   35   O  OD2 . ASP A 1 5   ? 2.300   6.308   5.146   1.00 19.15 ?  7    ASP A OD2 1 
ATOM   36   N  N   . TYR A 1 6   ? 2.154   1.492   5.917   1.00 8.65  ?  8    TYR A N   1 
ATOM   37   C  CA  . TYR A 1 6   ? 2.169   0.057   6.191   1.00 10.17 ?  8    TYR A CA  1 
ATOM   38   C  C   . TYR A 1 6   ? 2.409   -0.714  4.900   1.00 9.89  ?  8    TYR A C   1 
ATOM   39   O  O   . TYR A 1 6   ? 1.496   -0.848  4.081   1.00 10.39 ?  8    TYR A O   1 
ATOM   40   C  CB  . TYR A 1 6   ? 0.844   -0.379  6.817   1.00 10.29 ?  8    TYR A CB  1 
ATOM   41   C  CG  . TYR A 1 6   ? 0.812   -1.781  7.376   1.00 7.97  ?  8    TYR A CG  1 
ATOM   42   C  CD1 . TYR A 1 6   ? 1.216   -2.043  8.694   1.00 10.27 ?  8    TYR A CD1 1 
ATOM   43   C  CD2 . TYR A 1 6   ? 0.333   -2.837  6.616   1.00 13.06 ?  8    TYR A CD2 1 
ATOM   44   C  CE1 . TYR A 1 6   ? 1.143   -3.330  9.231   1.00 11.33 ?  8    TYR A CE1 1 
ATOM   45   C  CE2 . TYR A 1 6   ? 0.269   -4.129  7.139   1.00 16.41 ?  8    TYR A CE2 1 
ATOM   46   C  CZ  . TYR A 1 6   ? 0.688   -4.369  8.449   1.00 13.94 ?  8    TYR A CZ  1 
ATOM   47   O  OH  . TYR A 1 6   ? 0.631   -5.645  8.970   1.00 15.11 ?  8    TYR A OH  1 
ATOM   48   N  N   . GLY A 1 7   ? 3.618   -1.228  4.718   1.00 9.32  ?  9    GLY A N   1 
ATOM   49   C  CA  . GLY A 1 7   ? 3.958   -1.929  3.489   1.00 10.17 ?  9    GLY A CA  1 
ATOM   50   C  C   . GLY A 1 7   ? 3.627   -1.090  2.270   1.00 11.40 ?  9    GLY A C   1 
ATOM   51   O  O   . GLY A 1 7   ? 3.836   0.125   2.248   1.00 11.60 ?  9    GLY A O   1 
ATOM   52   N  N   . LYS A 1 8   ? 3.076   -1.737  1.248   1.00 11.89 ?  10   LYS A N   1 
ATOM   53   C  CA  . LYS A 1 8   ? 2.695   -1.050  0.021   1.00 14.88 ?  10   LYS A CA  1 
ATOM   54   C  C   . LYS A 1 8   ? 1.276   -0.504  0.043   1.00 16.04 ?  10   LYS A C   1 
ATOM   55   O  O   . LYS A 1 8   ? 0.882   0.150   -0.928  1.00 12.49 ?  10   LYS A O   1 
ATOM   56   C  CB  . LYS A 1 8   ? 2.867   -2.000  -1.181  1.00 15.39 ?  10   LYS A CB  1 
ATOM   57   C  CG  . LYS A 1 8   ? 4.280   -2.594  -1.228  1.00 15.71 ?  10   LYS A CG  1 
ATOM   58   C  CD  . LYS A 1 8   ? 4.438   -3.583  -2.367  1.00 24.89 ?  10   LYS A CD  1 
ATOM   59   C  CE  . LYS A 1 8   ? 5.876   -4.032  -2.492  1.00 26.05 ?  10   LYS A CE  1 
ATOM   60   N  NZ  . LYS A 1 8   ? 6.046   -4.951  -3.647  1.00 31.30 ?  10   LYS A NZ  1 
ATOM   61   N  N   . THR A 1 9   ? 0.525   -0.715  1.129   1.00 12.06 ?  11   THR A N   1 
ATOM   62   C  CA  . THR A 1 9   ? -0.925  -0.515  1.135   1.00 15.23 ?  11   THR A CA  1 
ATOM   63   C  C   . THR A 1 9   ? -1.398  0.597   2.053   1.00 13.77 ?  11   THR A C   1 
ATOM   64   O  O   . THR A 1 9   ? -2.470  1.164   1.813   1.00 13.08 ?  11   THR A O   1 
ATOM   65   C  CB  . THR A 1 9   ? -1.637  -1.805  1.582   1.00 16.22 ?  11   THR A CB  1 
ATOM   66   O  OG1 . THR A 1 9   ? -1.246  -2.120  2.934   1.00 13.86 ?  11   THR A OG1 1 
ATOM   67   C  CG2 . THR A 1 9   ? -1.286  -2.981  0.659   1.00 12.42 ?  11   THR A CG2 1 
ATOM   68   N  N   . GLY A 1 10  ? -0.645  0.900   3.109   1.00 11.21 ?  12   GLY A N   1 
ATOM   69   C  CA  . GLY A 1 10  ? -1.198  1.633   4.230   1.00 8.99  ?  12   GLY A CA  1 
ATOM   70   C  C   . GLY A 1 10  ? -2.086  0.732   5.069   1.00 11.37 ?  12   GLY A C   1 
ATOM   71   O  O   . GLY A 1 10  ? -2.323  -0.433  4.753   1.00 10.30 ?  12   GLY A O   1 
ATOM   72   N  N   . LEU A 1 11  ? -2.574  1.292   6.177   1.00 9.70  ?  13   LEU A N   1 
ATOM   73   C  CA  . LEU A 1 11  ? -3.417  0.565   7.124   1.00 9.65  ?  13   LEU A CA  1 
ATOM   74   C  C   . LEU A 1 11  ? -4.450  1.530   7.682   1.00 13.58 ?  13   LEU A C   1 
ATOM   75   O  O   . LEU A 1 11  ? -4.085  2.507   8.333   1.00 12.30 ?  13   LEU A O   1 
ATOM   76   C  CB  . LEU A 1 11  ? -2.577  -0.027  8.252   1.00 7.83  ?  13   LEU A CB  1 
ATOM   77   C  CG  . LEU A 1 11  ? -3.285  -0.893  9.293   1.00 9.29  ?  13   LEU A CG  1 
ATOM   78   C  CD1 . LEU A 1 11  ? -3.668  -2.217  8.685   1.00 13.83 ?  13   LEU A CD1 1 
ATOM   79   C  CD2 . LEU A 1 11  ? -2.378  -1.099  10.544  1.00 9.59  ?  13   LEU A CD2 1 
ATOM   80   N  N   . ASN A 1 12  ? -5.735  1.256   7.441   1.00 11.00 ?  14   ASN A N   1 
ATOM   81   C  CA  A ASN A 1 12  ? -6.805  2.147   7.883   0.56 12.95 ?  14   ASN A CA  1 
ATOM   82   C  CA  B ASN A 1 12  ? -6.798  2.150   7.888   0.44 12.94 ?  14   ASN A CA  1 
ATOM   83   C  C   . ASN A 1 12  ? -7.180  1.838   9.329   1.00 14.22 ?  14   ASN A C   1 
ATOM   84   O  O   . ASN A 1 12  ? -7.739  0.771   9.614   1.00 11.71 ?  14   ASN A O   1 
ATOM   85   C  CB  A ASN A 1 12  ? -8.024  2.004   6.975   0.56 11.79 ?  14   ASN A CB  1 
ATOM   86   C  CB  B ASN A 1 12  ? -8.023  2.037   6.987   0.44 11.82 ?  14   ASN A CB  1 
ATOM   87   C  CG  A ASN A 1 12  ? -7.916  2.844   5.739   0.56 12.11 ?  14   ASN A CG  1 
ATOM   88   C  CG  B ASN A 1 12  ? -9.217  2.736   7.585   0.44 13.49 ?  14   ASN A CG  1 
ATOM   89   O  OD1 A ASN A 1 12  ? -7.071  3.739   5.655   0.56 17.52 ?  14   ASN A OD1 1 
ATOM   90   O  OD1 B ASN A 1 12  ? -9.191  3.945   7.797   0.44 20.70 ?  14   ASN A OD1 1 
ATOM   91   N  ND2 A ASN A 1 12  ? -8.800  2.601   4.781   0.56 12.18 ?  14   ASN A ND2 1 
ATOM   92   N  ND2 B ASN A 1 12  ? -10.265 1.977   7.887   0.44 21.95 ?  14   ASN A ND2 1 
ATOM   93   N  N   . VAL A 1 13  ? -6.911  2.787   10.231  1.00 12.04 ?  15   VAL A N   1 
ATOM   94   C  CA  . VAL A 1 13  ? -7.150  2.645   11.665  1.00 10.77 ?  15   VAL A CA  1 
ATOM   95   C  C   . VAL A 1 13  ? -8.211  3.649   12.091  1.00 13.42 ?  15   VAL A C   1 
ATOM   96   O  O   . VAL A 1 13  ? -8.231  4.785   11.603  1.00 18.17 ?  15   VAL A O   1 
ATOM   97   C  CB  . VAL A 1 13  ? -5.844  2.880   12.452  1.00 12.41 ?  15   VAL A CB  1 
ATOM   98   C  CG1 . VAL A 1 13  ? -6.087  2.766   13.941  1.00 14.41 ?  15   VAL A CG1 1 
ATOM   99   C  CG2 . VAL A 1 13  ? -4.776  1.903   11.997  1.00 9.98  ?  15   VAL A CG2 1 
ATOM   100  N  N   . ASP A 1 14  ? -9.104  3.236   12.988  1.00 15.46 ?  16   ASP A N   1 
ATOM   101  C  CA  . ASP A 1 14  ? -10.060 4.161   13.587  1.00 20.67 ?  16   ASP A CA  1 
ATOM   102  C  C   . ASP A 1 14  ? -9.659  4.375   15.047  1.00 19.81 ?  16   ASP A C   1 
ATOM   103  O  O   . ASP A 1 14  ? -9.597  3.420   15.823  1.00 23.77 ?  16   ASP A O   1 
ATOM   104  C  CB  . ASP A 1 14  ? -11.486 3.626   13.457  1.00 26.01 ?  16   ASP A CB  1 
ATOM   105  C  CG  . ASP A 1 14  ? -12.541 4.654   13.846  1.00 31.30 ?  16   ASP A CG  1 
ATOM   106  O  OD1 . ASP A 1 14  ? -13.710 4.252   14.026  1.00 37.08 ?  16   ASP A OD1 1 
ATOM   107  O  OD2 . ASP A 1 14  ? -12.211 5.860   13.948  1.00 31.80 ?  16   ASP A OD2 1 
ATOM   108  N  N   . LEU A 1 15  ? -9.355  5.618   15.404  1.00 18.68 ?  17   LEU A N   1 
ATOM   109  C  CA  . LEU A 1 15  ? -8.870  5.950   16.738  1.00 19.43 ?  17   LEU A CA  1 
ATOM   110  C  C   . LEU A 1 15  ? -9.948  6.685   17.549  1.00 21.92 ?  17   LEU A C   1 
ATOM   111  O  O   . LEU A 1 15  ? -10.858 7.293   16.973  1.00 19.95 ?  17   LEU A O   1 
ATOM   112  C  CB  . LEU A 1 15  ? -7.607  6.810   16.623  1.00 19.28 ?  17   LEU A CB  1 
ATOM   113  C  CG  . LEU A 1 15  ? -6.365  6.088   16.091  1.00 23.26 ?  17   LEU A CG  1 
ATOM   114  C  CD1 . LEU A 1 15  ? -5.233  7.076   15.873  1.00 23.19 ?  17   LEU A CD1 1 
ATOM   115  C  CD2 . LEU A 1 15  ? -5.902  4.970   17.046  1.00 19.50 ?  17   LEU A CD2 1 
ATOM   116  N  N   . PRO A 1 16  ? -9.894  6.633   18.885  1.00 19.22 ?  18   PRO A N   1 
ATOM   117  C  CA  . PRO A 1 16  ? -10.968 7.248   19.689  1.00 23.97 ?  18   PRO A CA  1 
ATOM   118  C  C   . PRO A 1 16  ? -11.012 8.763   19.522  1.00 24.89 ?  18   PRO A C   1 
ATOM   119  O  O   . PRO A 1 16  ? -10.005 9.457   19.691  1.00 25.47 ?  18   PRO A O   1 
ATOM   120  C  CB  . PRO A 1 16  ? -10.617 6.838   21.127  1.00 29.13 ?  18   PRO A CB  1 
ATOM   121  C  CG  . PRO A 1 16  ? -9.153  6.482   21.084  1.00 30.15 ?  18   PRO A CG  1 
ATOM   122  C  CD  . PRO A 1 16  ? -8.948  5.874   19.722  1.00 23.32 ?  18   PRO A CD  1 
ATOM   123  N  N   . ASP A 1 17  ? -12.203 9.276   19.204  1.00 23.20 ?  19   ASP A N   1 
ATOM   124  C  CA  . ASP A 1 17  ? -12.326 10.680  18.819  1.00 26.11 ?  19   ASP A CA  1 
ATOM   125  C  C   . ASP A 1 17  ? -11.973 11.625  19.966  1.00 25.89 ?  19   ASP A C   1 
ATOM   126  O  O   . ASP A 1 17  ? -11.278 12.626  19.756  1.00 31.43 ?  19   ASP A O   1 
ATOM   127  C  CB  . ASP A 1 17  ? -13.742 10.965  18.312  1.00 34.39 ?  19   ASP A CB  1 
ATOM   128  C  CG  . ASP A 1 17  ? -14.020 10.313  16.970  1.00 40.24 ?  19   ASP A CG  1 
ATOM   129  O  OD1 . ASP A 1 17  ? -14.668 9.242   16.950  1.00 47.49 ?  19   ASP A OD1 1 
ATOM   130  O  OD2 . ASP A 1 17  ? -13.566 10.854  15.937  1.00 41.57 ?  19   ASP A OD2 1 
ATOM   131  N  N   . ASP A 1 18  ? -12.426 11.330  21.183  1.00 21.87 ?  20   ASP A N   1 
ATOM   132  C  CA  . ASP A 1 18  ? -12.253 12.273  22.285  1.00 27.33 ?  20   ASP A CA  1 
ATOM   133  C  C   . ASP A 1 18  ? -10.895 12.161  22.967  1.00 25.76 ?  20   ASP A C   1 
ATOM   134  O  O   . ASP A 1 18  ? -10.656 12.863  23.958  1.00 26.23 ?  20   ASP A O   1 
ATOM   135  C  CB  . ASP A 1 18  ? -13.367 12.084  23.321  1.00 27.47 ?  20   ASP A CB  1 
ATOM   136  N  N   . ARG A 1 19  ? -10.008 11.304  22.470  1.00 20.79 ?  21   ARG A N   1 
ATOM   137  C  CA  . ARG A 1 19  ? -8.722  11.060  23.105  1.00 22.66 ?  21   ARG A CA  1 
ATOM   138  C  C   . ARG A 1 19  ? -7.538  11.420  22.219  1.00 18.11 ?  21   ARG A C   1 
ATOM   139  O  O   . ARG A 1 19  ? -6.416  11.520  22.731  1.00 20.34 ?  21   ARG A O   1 
ATOM   140  C  CB  . ARG A 1 19  ? -8.587  9.578   23.507  1.00 24.81 ?  21   ARG A CB  1 
ATOM   141  C  CG  . ARG A 1 19  ? -9.777  8.989   24.277  1.00 32.40 ?  21   ARG A CG  1 
ATOM   142  C  CD  . ARG A 1 19  ? -9.966  9.610   25.654  1.00 27.15 ?  21   ARG A CD  1 
ATOM   143  N  NE  . ARG A 1 19  ? -8.903  9.290   26.596  1.00 37.77 ?  21   ARG A NE  1 
ATOM   144  C  CZ  . ARG A 1 19  ? -8.908  8.247   27.426  1.00 31.13 ?  21   ARG A CZ  1 
ATOM   145  N  NH1 . ARG A 1 19  ? -9.933  7.406   27.458  1.00 33.82 ?  21   ARG A NH1 1 
ATOM   146  N  NH2 . ARG A 1 19  ? -7.885  8.061   28.248  1.00 24.00 ?  21   ARG A NH2 1 
ATOM   147  N  N   . THR A 1 20  ? -7.748  11.620  20.920  1.00 16.29 ?  22   THR A N   1 
ATOM   148  C  CA  . THR A 1 20  ? -6.670  11.641  19.937  1.00 17.13 ?  22   THR A CA  1 
ATOM   149  C  C   . THR A 1 20  ? -6.409  13.063  19.454  1.00 16.04 ?  22   THR A C   1 
ATOM   150  O  O   . THR A 1 20  ? -7.334  13.755  19.018  1.00 15.91 ?  22   THR A O   1 
ATOM   151  C  CB  . THR A 1 20  ? -7.000  10.733  18.741  1.00 21.05 ?  22   THR A CB  1 
ATOM   152  O  OG1 . THR A 1 20  ? -7.313  9.407   19.197  1.00 22.08 ?  22   THR A OG1 1 
ATOM   153  C  CG2 . THR A 1 20  ? -5.809  10.661  17.784  1.00 18.63 ?  22   THR A CG2 1 
ATOM   154  N  N   . LEU A 1 21  ? -5.143  13.476  19.511  1.00 18.37 ?  23   LEU A N   1 
ATOM   155  C  CA  . LEU A 1 21  ? -4.692  14.748  18.959  1.00 18.70 ?  23   LEU A CA  1 
ATOM   156  C  C   . LEU A 1 21  ? -4.692  14.730  17.425  1.00 23.05 ?  23   LEU A C   1 
ATOM   157  O  O   . LEU A 1 21  ? -4.657  13.664  16.802  1.00 18.37 ?  23   LEU A O   1 
ATOM   158  C  CB  . LEU A 1 21  ? -3.280  15.062  19.461  1.00 14.54 ?  23   LEU A CB  1 
ATOM   159  C  CG  . LEU A 1 21  ? -3.020  15.167  20.963  1.00 21.86 ?  23   LEU A CG  1 
ATOM   160  C  CD1 . LEU A 1 21  ? -1.591  15.655  21.197  1.00 22.94 ?  23   LEU A CD1 1 
ATOM   161  C  CD2 . LEU A 1 21  ? -4.014  16.112  21.610  1.00 26.31 ?  23   LEU A CD2 1 
ATOM   162  N  N   . PRO A 1 22  ? -4.703  15.903  16.793  1.00 20.79 ?  24   PRO A N   1 
ATOM   163  C  CA  . PRO A 1 22  ? -4.548  15.957  15.334  1.00 21.67 ?  24   PRO A CA  1 
ATOM   164  C  C   . PRO A 1 22  ? -3.272  15.250  14.915  1.00 14.19 ?  24   PRO A C   1 
ATOM   165  O  O   . PRO A 1 22  ? -2.230  15.404  15.571  1.00 17.60 ?  24   PRO A O   1 
ATOM   166  C  CB  . PRO A 1 22  ? -4.473  17.465  15.040  1.00 25.45 ?  24   PRO A CB  1 
ATOM   167  C  CG  . PRO A 1 22  ? -5.187  18.101  16.195  1.00 27.73 ?  24   PRO A CG  1 
ATOM   168  C  CD  . PRO A 1 22  ? -4.810  17.250  17.382  1.00 24.72 ?  24   PRO A CD  1 
ATOM   169  N  N   . PRO A 1 23  ? -3.320  14.467  13.838  1.00 17.07 ?  25   PRO A N   1 
ATOM   170  C  CA  . PRO A 1 23  ? -2.150  13.677  13.442  1.00 15.79 ?  25   PRO A CA  1 
ATOM   171  C  C   . PRO A 1 23  ? -0.942  14.565  13.193  1.00 17.65 ?  25   PRO A C   1 
ATOM   172  O  O   . PRO A 1 23  ? -1.058  15.688  12.699  1.00 18.07 ?  25   PRO A O   1 
ATOM   173  C  CB  . PRO A 1 23  ? -2.614  12.984  12.155  1.00 14.88 ?  25   PRO A CB  1 
ATOM   174  C  CG  . PRO A 1 23  ? -4.132  12.905  12.322  1.00 21.33 ?  25   PRO A CG  1 
ATOM   175  C  CD  . PRO A 1 23  ? -4.453  14.251  12.918  1.00 17.06 ?  25   PRO A CD  1 
ATOM   176  N  N   . LEU A 1 24  ? 0.221   14.054  13.567  1.00 11.92 ?  26   LEU A N   1 
ATOM   177  C  CA  . LEU A 1 24  ? 1.482   14.743  13.336  1.00 15.54 ?  26   LEU A CA  1 
ATOM   178  C  C   . LEU A 1 24  ? 1.944   14.436  11.921  1.00 14.77 ?  26   LEU A C   1 
ATOM   179  O  O   . LEU A 1 24  ? 2.203   13.273  11.593  1.00 13.53 ?  26   LEU A O   1 
ATOM   180  C  CB  . LEU A 1 24  ? 2.535   14.298  14.348  1.00 11.95 ?  26   LEU A CB  1 
ATOM   181  C  CG  . LEU A 1 24  ? 2.393   14.868  15.762  1.00 17.36 ?  26   LEU A CG  1 
ATOM   182  C  CD1 . LEU A 1 24  ? 1.347   14.147  16.570  1.00 21.99 ?  26   LEU A CD1 1 
ATOM   183  C  CD2 . LEU A 1 24  ? 3.733   14.753  16.456  1.00 18.22 ?  26   LEU A CD2 1 
ATOM   184  N  N   . THR A 1 25  ? 2.064   15.474  11.097  1.00 14.82 ?  27   THR A N   1 
ATOM   185  C  CA  . THR A 1 25  ? 2.454   15.333  9.702   1.00 12.98 ?  27   THR A CA  1 
ATOM   186  C  C   . THR A 1 25  ? 3.476   16.412  9.366   1.00 16.16 ?  27   THR A C   1 
ATOM   187  O  O   . THR A 1 25  ? 3.506   17.470  9.997   1.00 19.14 ?  27   THR A O   1 
ATOM   188  C  CB  . THR A 1 25  ? 1.241   15.448  8.755   1.00 21.20 ?  27   THR A CB  1 
ATOM   189  O  OG1 . THR A 1 25  ? 0.660   16.753  8.868   1.00 23.41 ?  27   THR A OG1 1 
ATOM   190  C  CG2 . THR A 1 25  ? 0.178   14.394  9.080   1.00 24.50 ?  27   THR A CG2 1 
ATOM   191  N  N   . ILE A 1 26  ? 4.310   16.153  8.359   1.00 17.94 ?  28   ILE A N   1 
ATOM   192  C  CA  . ILE A 1 26  ? 5.250   17.199  7.954   1.00 16.76 ?  28   ILE A CA  1 
ATOM   193  C  C   . ILE A 1 26  ? 4.501   18.324  7.238   1.00 17.41 ?  28   ILE A C   1 
ATOM   194  O  O   . ILE A 1 26  ? 3.404   18.142  6.689   1.00 16.98 ?  28   ILE A O   1 
ATOM   195  C  CB  . ILE A 1 26  ? 6.372   16.633  7.071   1.00 22.15 ?  28   ILE A CB  1 
ATOM   196  C  CG1 . ILE A 1 26  ? 5.822   16.263  5.702   1.00 18.54 ?  28   ILE A CG1 1 
ATOM   197  C  CG2 . ILE A 1 26  ? 7.036   15.437  7.741   1.00 23.17 ?  28   ILE A CG2 1 
ATOM   198  C  CD1 . ILE A 1 26  ? 6.876   15.791  4.739   1.00 25.70 ?  28   ILE A CD1 1 
ATOM   199  N  N   . ARG A 1 27  ? 5.121   19.500  7.231   1.00 16.77 ?  29   ARG A N   1 
ATOM   200  C  CA  . ARG A 1 27  ? 4.535   20.683  6.605   1.00 17.65 ?  29   ARG A CA  1 
ATOM   201  C  C   . ARG A 1 27  ? 4.396   20.494  5.093   1.00 18.07 ?  29   ARG A C   1 
ATOM   202  O  O   . ARG A 1 27  ? 5.300   19.961  4.442   1.00 15.25 ?  29   ARG A O   1 
ATOM   203  C  CB  . ARG A 1 27  ? 5.396   21.919  6.907   1.00 20.52 ?  29   ARG A CB  1 
ATOM   204  C  CG  . ARG A 1 27  ? 5.031   23.175  6.087   1.00 23.65 ?  29   ARG A CG  1 
ATOM   205  C  CD  . ARG A 1 27  ? 5.832   24.416  6.505   1.00 31.26 ?  29   ARG A CD  1 
ATOM   206  N  NE  . ARG A 1 27  ? 7.152   24.529  5.872   1.00 28.68 ?  29   ARG A NE  1 
ATOM   207  C  CZ  . ARG A 1 27  ? 7.356   24.838  4.589   1.00 30.11 ?  29   ARG A CZ  1 
ATOM   208  N  NH1 . ARG A 1 27  ? 6.331   25.062  3.780   1.00 32.31 ?  29   ARG A NH1 1 
ATOM   209  N  NH2 . ARG A 1 27  ? 8.591   24.926  4.107   1.00 33.13 ?  29   ARG A NH2 1 
ATOM   210  N  N   . PRO A 1 28  ? 3.272   20.944  4.494   1.00 16.14 ?  30   PRO A N   1 
ATOM   211  C  CA  . PRO A 1 28  ? 3.004   20.725  3.048   1.00 16.48 ?  30   PRO A CA  1 
ATOM   212  C  C   . PRO A 1 28  ? 3.723   21.686  2.104   1.00 24.15 ?  30   PRO A C   1 
ATOM   213  O  O   . PRO A 1 28  ? 3.127   22.578  1.467   1.00 25.41 ?  30   PRO A O   1 
ATOM   214  C  CB  . PRO A 1 28  ? 1.478   20.885  2.974   1.00 20.02 ?  30   PRO A CB  1 
ATOM   215  C  CG  . PRO A 1 28  ? 1.146   21.844  4.056   1.00 20.32 ?  30   PRO A CG  1 
ATOM   216  C  CD  . PRO A 1 28  ? 2.084   21.462  5.204   1.00 17.15 ?  30   PRO A CD  1 
ATOM   217  N  N   . ALA A 1 29  ? 5.024   21.477  1.940   1.00 17.64 ?  31   ALA A N   1 
ATOM   218  C  CA  . ALA A 1 29  ? 5.791   22.270  0.991   1.00 17.35 ?  31   ALA A CA  1 
ATOM   219  C  C   . ALA A 1 29  ? 5.454   21.859  -0.448  1.00 13.24 ?  31   ALA A C   1 
ATOM   220  O  O   . ALA A 1 29  ? 5.044   20.724  -0.699  1.00 12.98 ?  31   ALA A O   1 
ATOM   221  C  CB  . ALA A 1 29  ? 7.289   22.108  1.242   1.00 12.78 ?  31   ALA A CB  1 
ATOM   222  N  N   . PRO A 1 30  ? 5.609   22.769  -1.404  1.00 15.30 ?  32   PRO A N   1 
ATOM   223  C  CA  . PRO A 1 30  ? 5.236   22.469  -2.797  1.00 10.26 ?  32   PRO A CA  1 
ATOM   224  C  C   . PRO A 1 30  ? 6.202   21.481  -3.430  1.00 13.26 ?  32   PRO A C   1 
ATOM   225  O  O   . PRO A 1 30  ? 7.428   21.701  -3.421  1.00 12.88 ?  32   PRO A O   1 
ATOM   226  C  CB  . PRO A 1 30  ? 5.313   23.846  -3.480  1.00 10.72 ?  32   PRO A CB  1 
ATOM   227  C  CG  . PRO A 1 30  ? 6.171   24.690  -2.561  1.00 14.67 ?  32   PRO A CG  1 
ATOM   228  C  CD  . PRO A 1 30  ? 5.816   24.211  -1.193  1.00 12.48 ?  32   PRO A CD  1 
ATOM   229  N  N   . PRO A 1 31  ? 5.691   20.375  -3.975  1.00 14.29 ?  33   PRO A N   1 
ATOM   230  C  CA  . PRO A 1 31  ? 6.523   19.515  -4.826  1.00 11.72 ?  33   PRO A CA  1 
ATOM   231  C  C   . PRO A 1 31  ? 7.084   20.286  -6.009  1.00 15.57 ?  33   PRO A C   1 
ATOM   232  O  O   . PRO A 1 31  ? 6.475   21.241  -6.507  1.00 14.23 ?  33   PRO A O   1 
ATOM   233  C  CB  . PRO A 1 31  ? 5.549   18.426  -5.299  1.00 18.39 ?  33   PRO A CB  1 
ATOM   234  C  CG  . PRO A 1 31  ? 4.405   18.492  -4.338  1.00 21.30 ?  33   PRO A CG  1 
ATOM   235  C  CD  . PRO A 1 31  ? 4.287   19.935  -3.971  1.00 15.82 ?  33   PRO A CD  1 
ATOM   236  N  N   . LEU A 1 32  ? 8.267   19.872  -6.451  1.00 11.72 ?  34   LEU A N   1 
ATOM   237  C  CA  . LEU A 1 32  ? 8.786   20.354  -7.727  1.00 12.73 ?  34   LEU A CA  1 
ATOM   238  C  C   . LEU A 1 32  ? 7.950   19.778  -8.861  1.00 14.80 ?  34   LEU A C   1 
ATOM   239  O  O   . LEU A 1 32  ? 7.648   18.580  -8.888  1.00 13.54 ?  34   LEU A O   1 
ATOM   240  C  CB  . LEU A 1 32  ? 10.250  19.963  -7.903  1.00 11.28 ?  34   LEU A CB  1 
ATOM   241  C  CG  . LEU A 1 32  ? 11.161  20.379  -6.742  1.00 15.01 ?  34   LEU A CG  1 
ATOM   242  C  CD1 . LEU A 1 32  ? 12.582  19.939  -7.031  1.00 12.95 ?  34   LEU A CD1 1 
ATOM   243  C  CD2 . LEU A 1 32  ? 11.093  21.866  -6.477  1.00 20.38 ?  34   LEU A CD2 1 
ATOM   244  N  N   . ASP A 1 33  ? 7.549   20.651  -9.779  1.00 14.07 ?  35   ASP A N   1 
ATOM   245  C  CA  . ASP A 1 33  ? 6.790   20.225  -10.948 1.00 13.64 ?  35   ASP A CA  1 
ATOM   246  C  C   . ASP A 1 33  ? 7.578   19.219  -11.783 1.00 14.82 ?  35   ASP A C   1 
ATOM   247  O  O   . ASP A 1 33  ? 7.038   18.190  -12.215 1.00 13.84 ?  35   ASP A O   1 
ATOM   248  C  CB  . ASP A 1 33  ? 6.442   21.459  -11.771 1.00 10.83 ?  35   ASP A CB  1 
ATOM   249  C  CG  . ASP A 1 33  ? 5.974   21.104  -13.163 1.00 14.40 ?  35   ASP A CG  1 
ATOM   250  O  OD1 . ASP A 1 33  ? 4.917   20.442  -13.253 1.00 17.11 ?  35   ASP A OD1 1 
ATOM   251  O  OD2 . ASP A 1 33  ? 6.685   21.440  -14.142 1.00 13.32 ?  35   ASP A OD2 1 
ATOM   252  N  N   . ASP A 1 34  ? 8.867   19.481  -11.992 1.00 12.37 ?  36   ASP A N   1 
ATOM   253  C  CA  . ASP A 1 34  ? 9.692   18.675  -12.891 1.00 12.85 ?  36   ASP A CA  1 
ATOM   254  C  C   . ASP A 1 34  ? 11.039  18.464  -12.218 1.00 13.67 ?  36   ASP A C   1 
ATOM   255  O  O   . ASP A 1 34  ? 12.022  19.158  -12.512 1.00 11.20 ?  36   ASP A O   1 
ATOM   256  C  CB  . ASP A 1 34  ? 9.794   19.332  -14.273 1.00 15.81 ?  36   ASP A CB  1 
ATOM   257  C  CG  . ASP A 1 34  ? 10.258  18.374  -15.347 1.00 19.18 ?  36   ASP A CG  1 
ATOM   258  O  OD1 . ASP A 1 34  ? 9.836   18.555  -16.511 1.00 22.04 ?  36   ASP A OD1 1 
ATOM   259  O  OD2 . ASP A 1 34  ? 11.105  17.484  -15.058 1.00 17.02 ?  36   ASP A OD2 1 
ATOM   260  N  N   . PRO A 1 35  ? 11.115  17.489  -11.306 1.00 10.04 ?  37   PRO A N   1 
ATOM   261  C  CA  . PRO A 1 35  ? 12.358  17.279  -10.535 1.00 13.26 ?  37   PRO A CA  1 
ATOM   262  C  C   . PRO A 1 35  ? 13.552  16.920  -11.392 1.00 12.62 ?  37   PRO A C   1 
ATOM   263  O  O   . PRO A 1 35  ? 14.669  17.351  -11.077 1.00 12.88 ?  37   PRO A O   1 
ATOM   264  C  CB  . PRO A 1 35  ? 12.007  16.122  -9.580  1.00 14.59 ?  37   PRO A CB  1 
ATOM   265  C  CG  . PRO A 1 35  ? 10.551  15.883  -9.710  1.00 14.81 ?  37   PRO A CG  1 
ATOM   266  C  CD  . PRO A 1 35  ? 10.078  16.488  -10.996 1.00 14.54 ?  37   PRO A CD  1 
ATOM   267  N  N   . GLU A 1 36  ? 13.363  16.112  -12.442 1.00 13.10 ?  38   GLU A N   1 
ATOM   268  C  CA  . GLU A 1 36  ? 14.488  15.796  -13.317 1.00 10.91 ?  38   GLU A CA  1 
ATOM   269  C  C   . GLU A 1 36  ? 15.034  17.056  -13.984 1.00 10.11 ?  38   GLU A C   1 
ATOM   270  O  O   . GLU A 1 36  ? 16.249  17.249  -14.044 1.00 11.59 ?  38   GLU A O   1 
ATOM   271  C  CB  . GLU A 1 36  ? 14.087  14.758  -14.367 1.00 15.87 ?  38   GLU A CB  1 
ATOM   272  C  CG  . GLU A 1 36  ? 15.295  14.044  -14.973 1.00 18.20 ?  38   GLU A CG  1 
ATOM   273  C  CD  . GLU A 1 36  ? 14.920  12.833  -15.825 1.00 24.10 ?  38   GLU A CD  1 
ATOM   274  O  OE1 . GLU A 1 36  ? 15.730  12.439  -16.690 1.00 24.74 ?  38   GLU A OE1 1 
ATOM   275  O  OE2 . GLU A 1 36  ? 13.825  12.266  -15.631 1.00 33.01 ?  38   GLU A OE2 1 
ATOM   276  N  N   . ALA A 1 37  ? 14.151  17.930  -14.487 1.00 11.10 ?  39   ALA A N   1 
ATOM   277  C  CA  . ALA A 1 37  ? 14.605  19.216  -15.009 1.00 15.59 ?  39   ALA A CA  1 
ATOM   278  C  C   . ALA A 1 37  ? 15.327  20.025  -13.943 1.00 13.42 ?  39   ALA A C   1 
ATOM   279  O  O   . ALA A 1 37  ? 16.267  20.768  -14.248 1.00 14.72 ?  39   ALA A O   1 
ATOM   280  C  CB  . ALA A 1 37  ? 13.420  20.023  -15.552 1.00 14.65 ?  39   ALA A CB  1 
ATOM   281  N  N   . GLU A 1 38  ? 14.889  19.915  -12.691 1.00 13.41 ?  40   GLU A N   1 
ATOM   282  C  CA  . GLU A 1 38  ? 15.584  20.618  -11.621 1.00 12.45 ?  40   GLU A CA  1 
ATOM   283  C  C   . GLU A 1 38  ? 16.963  20.024  -11.373 1.00 12.62 ?  40   GLU A C   1 
ATOM   284  O  O   . GLU A 1 38  ? 17.923  20.764  -11.127 1.00 10.89 ?  40   GLU A O   1 
ATOM   285  C  CB  . GLU A 1 38  ? 14.756  20.597  -10.343 1.00 13.57 ?  40   GLU A CB  1 
ATOM   286  C  CG  . GLU A 1 38  ? 15.228  21.647  -9.343  1.00 19.86 ?  40   GLU A CG  1 
ATOM   287  C  CD  . GLU A 1 38  ? 15.239  23.055  -9.931  1.00 28.15 ?  40   GLU A CD  1 
ATOM   288  O  OE1 . GLU A 1 38  ? 16.099  23.861  -9.510  1.00 41.10 ?  40   GLU A OE1 1 
ATOM   289  O  OE2 . GLU A 1 38  ? 14.391  23.362  -10.800 1.00 28.42 ?  40   GLU A OE2 1 
ATOM   290  N  N   . VAL A 1 39  ? 17.083  18.694  -11.417 1.00 10.53 ?  41   VAL A N   1 
ATOM   291  C  CA  . VAL A 1 39  ? 18.403  18.086  -11.254 1.00 8.62  ?  41   VAL A CA  1 
ATOM   292  C  C   . VAL A 1 39  ? 19.336  18.577  -12.351 1.00 12.47 ?  41   VAL A C   1 
ATOM   293  O  O   . VAL A 1 39  ? 20.503  18.903  -12.100 1.00 10.63 ?  41   VAL A O   1 
ATOM   294  C  CB  . VAL A 1 39  ? 18.300  16.547  -11.262 1.00 9.73  ?  41   VAL A CB  1 
ATOM   295  C  CG1 . VAL A 1 39  ? 19.708  15.929  -11.304 1.00 11.00 ?  41   VAL A CG1 1 
ATOM   296  C  CG2 . VAL A 1 39  ? 17.503  16.038  -10.055 1.00 12.94 ?  41   VAL A CG2 1 
ATOM   297  N  N   . VAL A 1 40  ? 18.829  18.644  -13.585 1.00 8.65  ?  42   VAL A N   1 
ATOM   298  C  CA  . VAL A 1 40  ? 19.639  19.131  -14.701 1.00 13.17 ?  42   VAL A CA  1 
ATOM   299  C  C   . VAL A 1 40  ? 20.152  20.538  -14.411 1.00 13.93 ?  42   VAL A C   1 
ATOM   300  O  O   . VAL A 1 40  ? 21.345  20.827  -14.576 1.00 13.25 ?  42   VAL A O   1 
ATOM   301  C  CB  . VAL A 1 40  ? 18.836  19.066  -16.019 1.00 15.93 ?  42   VAL A CB  1 
ATOM   302  C  CG1 . VAL A 1 40  ? 19.579  19.829  -17.123 1.00 16.27 ?  42   VAL A CG1 1 
ATOM   303  C  CG2 . VAL A 1 40  ? 18.625  17.623  -16.440 1.00 12.97 ?  42   VAL A CG2 1 
ATOM   304  N  N   . ARG A 1 41  ? 19.270  21.428  -13.946 1.00 10.30 ?  43   ARG A N   1 
ATOM   305  C  CA  . ARG A 1 41  ? 19.698  22.789  -13.617 1.00 11.70 ?  43   ARG A CA  1 
ATOM   306  C  C   . ARG A 1 41  ? 20.729  22.802  -12.490 1.00 13.24 ?  43   ARG A C   1 
ATOM   307  O  O   . ARG A 1 41  ? 21.664  23.606  -12.505 1.00 11.70 ?  43   ARG A O   1 
ATOM   308  C  CB  . ARG A 1 41  ? 18.493  23.643  -13.229 1.00 17.04 ?  43   ARG A CB  1 
ATOM   309  C  CG  . ARG A 1 41  ? 17.642  24.077  -14.417 1.00 19.36 ?  43   ARG A CG  1 
ATOM   310  C  CD  . ARG A 1 41  ? 16.549  25.035  -13.977 1.00 22.38 ?  43   ARG A CD  1 
ATOM   311  N  NE  . ARG A 1 41  ? 15.401  24.353  -13.384 1.00 20.53 ?  43   ARG A NE  1 
ATOM   312  C  CZ  . ARG A 1 41  ? 14.400  23.841  -14.095 1.00 22.65 ?  43   ARG A CZ  1 
ATOM   313  N  NH1 . ARG A 1 41  ? 14.424  23.914  -15.419 1.00 22.88 ?  43   ARG A NH1 1 
ATOM   314  N  NH2 . ARG A 1 41  ? 13.387  23.247  -13.491 1.00 21.18 ?  43   ARG A NH2 1 
ATOM   315  N  N   . CYS A 1 42  ? 20.554  21.947  -11.485 1.00 12.72 ?  44   CYS A N   1 
ATOM   316  C  CA  . CYS A 1 42  ? 21.497  21.940  -10.370 1.00 12.15 ?  44   CYS A CA  1 
ATOM   317  C  C   . CYS A 1 42  ? 22.856  21.374  -10.772 1.00 12.12 ?  44   CYS A C   1 
ATOM   318  O  O   . CYS A 1 42  ? 23.871  21.747  -10.171 1.00 11.44 ?  44   CYS A O   1 
ATOM   319  C  CB  . CYS A 1 42  ? 20.916  21.154  -9.194  1.00 14.85 ?  44   CYS A CB  1 
ATOM   320  S  SG  . CYS A 1 42  ? 19.519  21.977  -8.349  1.00 22.54 ?  44   CYS A SG  1 
ATOM   321  N  N   . LEU A 1 43  ? 22.913  20.488  -11.777 1.00 11.88 ?  45   LEU A N   1 
ATOM   322  C  CA  . LEU A 1 43  ? 24.225  19.993  -12.200 1.00 12.83 ?  45   LEU A CA  1 
ATOM   323  C  C   . LEU A 1 43  ? 24.989  21.067  -12.956 1.00 14.36 ?  45   LEU A C   1 
ATOM   324  O  O   . LEU A 1 43  ? 26.228  21.090  -12.930 1.00 14.89 ?  45   LEU A O   1 
ATOM   325  C  CB  . LEU A 1 43  ? 24.125  18.744  -13.086 1.00 11.71 ?  45   LEU A CB  1 
ATOM   326  C  CG  . LEU A 1 43  ? 23.500  17.433  -12.581 1.00 16.30 ?  45   LEU A CG  1 
ATOM   327  C  CD1 . LEU A 1 43  ? 23.586  16.334  -13.644 1.00 13.75 ?  45   LEU A CD1 1 
ATOM   328  C  CD2 . LEU A 1 43  ? 23.961  16.958  -11.268 1.00 23.83 ?  45   LEU A CD2 1 
ATOM   329  N  N   . ALA A 1 44  ? 24.268  21.974  -13.615 1.00 13.42 ?  46   ALA A N   1 
ATOM   330  C  CA  . ALA A 1 44  ? 24.902  23.090  -14.308 1.00 13.83 ?  46   ALA A CA  1 
ATOM   331  C  C   . ALA A 1 44  ? 25.276  24.233  -13.377 1.00 13.77 ?  46   ALA A C   1 
ATOM   332  O  O   . ALA A 1 44  ? 26.178  25.007  -13.714 1.00 13.32 ?  46   ALA A O   1 
ATOM   333  C  CB  . ALA A 1 44  ? 23.977  23.631  -15.402 1.00 13.77 ?  46   ALA A CB  1 
ATOM   334  N  N   . GLU A 1 45  ? 24.582  24.386  -12.244 1.00 13.39 ?  47   GLU A N   1 
ATOM   335  C  CA  . GLU A 1 45  ? 24.817  25.488  -11.302 1.00 12.62 ?  47   GLU A CA  1 
ATOM   336  C  C   . GLU A 1 45  ? 24.751  24.936  -9.882  1.00 15.23 ?  47   GLU A C   1 
ATOM   337  O  O   . GLU A 1 45  ? 23.790  25.180  -9.139  1.00 17.25 ?  47   GLU A O   1 
ATOM   338  C  CB  . GLU A 1 45  ? 23.800  26.618  -11.506 1.00 14.15 ?  47   GLU A CB  1 
ATOM   339  N  N   . PRO A 1 46  ? 25.779  24.176  -9.466  1.00 13.48 ?  48   PRO A N   1 
ATOM   340  C  CA  . PRO A 1 46  ? 25.734  23.517  -8.152  1.00 13.24 ?  48   PRO A CA  1 
ATOM   341  C  C   . PRO A 1 46  ? 26.216  24.395  -6.999  1.00 15.68 ?  48   PRO A C   1 
ATOM   342  O  O   . PRO A 1 46  ? 26.685  25.523  -7.195  1.00 15.50 ?  48   PRO A O   1 
ATOM   343  C  CB  . PRO A 1 46  ? 26.652  22.304  -8.347  1.00 12.27 ?  48   PRO A CB  1 
ATOM   344  C  CG  . PRO A 1 46  ? 27.627  22.740  -9.392  1.00 16.80 ?  48   PRO A CG  1 
ATOM   345  C  CD  . PRO A 1 46  ? 26.920  23.724  -10.284 1.00 14.85 ?  48   PRO A CD  1 
ATOM   346  N  N   . ILE A 1 47  ? 26.094  23.860  -5.788  1.00 11.65 ?  49   ILE A N   1 
ATOM   347  C  CA  . ILE A 1 47  ? 26.500  24.534  -4.558  1.00 14.82 ?  49   ILE A CA  1 
ATOM   348  C  C   . ILE A 1 47  ? 27.938  24.127  -4.245  1.00 11.67 ?  49   ILE A C   1 
ATOM   349  O  O   . ILE A 1 47  ? 28.220  22.939  -4.057  1.00 15.38 ?  49   ILE A O   1 
ATOM   350  C  CB  . ILE A 1 47  ? 25.560  24.150  -3.398  1.00 11.93 ?  49   ILE A CB  1 
ATOM   351  C  CG1 . ILE A 1 47  ? 24.092  24.411  -3.766  1.00 18.55 ?  49   ILE A CG1 1 
ATOM   352  C  CG2 . ILE A 1 47  ? 25.985  24.809  -2.081  1.00 14.37 ?  49   ILE A CG2 1 
ATOM   353  C  CD1 . ILE A 1 47  ? 23.075  23.842  -2.781  1.00 15.19 ?  49   ILE A CD1 1 
ATOM   354  N  N   . GLY A 1 48  ? 28.851  25.101  -4.195  1.00 12.41 ?  50   GLY A N   1 
ATOM   355  C  CA  . GLY A 1 48  ? 30.205  24.838  -3.723  1.00 15.11 ?  50   GLY A CA  1 
ATOM   356  C  C   . GLY A 1 48  ? 31.053  23.934  -4.594  1.00 15.37 ?  50   GLY A C   1 
ATOM   357  O  O   . GLY A 1 48  ? 32.044  23.367  -4.117  1.00 11.98 ?  50   GLY A O   1 
ATOM   358  N  N   . SER A 1 49  ? 30.693  23.783  -5.863  1.00 17.19 ?  51   SER A N   1 
ATOM   359  C  CA  . SER A 1 49  ? 31.320  22.852  -6.788  1.00 17.65 ?  51   SER A CA  1 
ATOM   360  C  C   . SER A 1 49  ? 31.354  23.485  -8.163  1.00 18.16 ?  51   SER A C   1 
ATOM   361  O  O   . SER A 1 49  ? 30.484  24.302  -8.479  1.00 16.41 ?  51   SER A O   1 
ATOM   362  C  CB  . SER A 1 49  ? 30.531  21.536  -6.856  1.00 20.10 ?  51   SER A CB  1 
ATOM   363  O  OG  . SER A 1 49  ? 31.019  20.722  -7.901  1.00 24.91 ?  51   SER A OG  1 
ATOM   364  N  N   . PRO A 1 50  ? 32.313  23.122  -9.008  1.00 16.04 ?  52   PRO A N   1 
ATOM   365  C  CA  . PRO A 1 50  ? 32.164  23.419  -10.423 1.00 16.34 ?  52   PRO A CA  1 
ATOM   366  C  C   . PRO A 1 50  ? 31.018  22.599  -10.994 1.00 16.28 ?  52   PRO A C   1 
ATOM   367  O  O   . PRO A 1 50  ? 30.580  21.617  -10.373 1.00 12.21 ?  52   PRO A O   1 
ATOM   368  C  CB  . PRO A 1 50  ? 33.523  23.021  -11.026 1.00 17.05 ?  52   PRO A CB  1 
ATOM   369  C  CG  . PRO A 1 50  ? 34.138  22.111  -10.034 1.00 21.23 ?  52   PRO A CG  1 
ATOM   370  C  CD  . PRO A 1 50  ? 33.604  22.479  -8.692  1.00 15.41 ?  52   PRO A CD  1 
ATOM   371  N  N   . PRO A 1 51  ? 30.478  22.989  -12.146 1.00 14.71 ?  53   PRO A N   1 
ATOM   372  C  CA  . PRO A 1 51  ? 29.456  22.156  -12.791 1.00 14.28 ?  53   PRO A CA  1 
ATOM   373  C  C   . PRO A 1 51  ? 29.977  20.748  -13.038 1.00 15.01 ?  53   PRO A C   1 
ATOM   374  O  O   . PRO A 1 51  ? 31.157  20.551  -13.337 1.00 15.66 ?  53   PRO A O   1 
ATOM   375  C  CB  . PRO A 1 51  ? 29.179  22.889  -14.107 1.00 14.13 ?  53   PRO A CB  1 
ATOM   376  C  CG  . PRO A 1 51  ? 29.585  24.316  -13.850 1.00 16.08 ?  53   PRO A CG  1 
ATOM   377  C  CD  . PRO A 1 51  ? 30.773  24.212  -12.914 1.00 14.16 ?  53   PRO A CD  1 
ATOM   378  N  N   . LEU A 1 52  ? 29.078  19.766  -12.916 1.00 12.77 ?  54   LEU A N   1 
ATOM   379  C  CA  . LEU A 1 52  ? 29.462  18.368  -13.094 1.00 14.87 ?  54   LEU A CA  1 
ATOM   380  C  C   . LEU A 1 52  ? 30.169  18.141  -14.424 1.00 12.31 ?  54   LEU A C   1 
ATOM   381  O  O   . LEU A 1 52  ? 31.123  17.362  -14.494 1.00 15.87 ?  54   LEU A O   1 
ATOM   382  C  CB  . LEU A 1 52  ? 28.238  17.451  -13.007 1.00 15.75 ?  54   LEU A CB  1 
ATOM   383  C  CG  . LEU A 1 52  ? 28.624  15.962  -13.022 1.00 13.72 ?  54   LEU A CG  1 
ATOM   384  C  CD1 . LEU A 1 52  ? 29.650  15.640  -11.910 1.00 13.97 ?  54   LEU A CD1 1 
ATOM   385  C  CD2 . LEU A 1 52  ? 27.378  15.084  -12.902 1.00 15.05 ?  54   LEU A CD2 1 
ATOM   386  N  N   . LEU A 1 53  ? 29.713  18.802  -15.495 1.00 11.80 ?  55   LEU A N   1 
ATOM   387  C  CA  . LEU A 1 53  ? 30.347  18.570  -16.791 1.00 11.99 ?  55   LEU A CA  1 
ATOM   388  C  C   . LEU A 1 53  ? 31.824  18.949  -16.729 1.00 17.17 ?  55   LEU A C   1 
ATOM   389  O  O   . LEU A 1 53  ? 32.685  18.246  -17.270 1.00 15.97 ?  55   LEU A O   1 
ATOM   390  C  CB  . LEU A 1 53  ? 29.600  19.351  -17.879 1.00 14.80 ?  55   LEU A CB  1 
ATOM   391  C  CG  . LEU A 1 53  ? 30.036  19.128  -19.328 1.00 19.09 ?  55   LEU A CG  1 
ATOM   392  C  CD1 . LEU A 1 53  ? 29.629  17.746  -19.778 1.00 15.89 ?  55   LEU A CD1 1 
ATOM   393  C  CD2 . LEU A 1 53  ? 29.413  20.170  -20.234 1.00 18.81 ?  55   LEU A CD2 1 
ATOM   394  N  N   . ASP A 1 54  ? 32.137  20.008  -15.991 1.00 20.83 ?  56   ASP A N   1 
ATOM   395  C  CA  . ASP A 1 54  ? 33.514  20.484  -15.901 1.00 14.82 ?  56   ASP A CA  1 
ATOM   396  C  C   . ASP A 1 54  ? 34.355  19.615  -14.966 1.00 21.58 ?  56   ASP A C   1 
ATOM   397  O  O   . ASP A 1 54  ? 35.533  19.367  -15.252 1.00 18.57 ?  56   ASP A O   1 
ATOM   398  C  CB  . ASP A 1 54  ? 33.505  21.943  -15.464 1.00 18.28 ?  56   ASP A CB  1 
ATOM   399  C  CG  . ASP A 1 54  ? 32.748  22.840  -16.450 1.00 32.67 ?  56   ASP A CG  1 
ATOM   400  O  OD1 . ASP A 1 54  ? 32.302  23.931  -16.043 1.00 40.72 ?  56   ASP A OD1 1 
ATOM   401  O  OD2 . ASP A 1 54  ? 32.607  22.466  -17.639 1.00 37.36 ?  56   ASP A OD2 1 
ATOM   402  N  N   . LEU A 1 55  ? 33.766  19.129  -13.862 1.00 16.00 ?  57   LEU A N   1 
ATOM   403  C  CA  . LEU A 1 55  ? 34.444  18.131  -13.029 1.00 17.55 ?  57   LEU A CA  1 
ATOM   404  C  C   . LEU A 1 55  ? 34.801  16.881  -13.812 1.00 19.40 ?  57   LEU A C   1 
ATOM   405  O  O   . LEU A 1 55  ? 35.839  16.261  -13.554 1.00 18.57 ?  57   LEU A O   1 
ATOM   406  C  CB  . LEU A 1 55  ? 33.590  17.729  -11.816 1.00 15.73 ?  57   LEU A CB  1 
ATOM   407  C  CG  . LEU A 1 55  ? 33.365  18.653  -10.638 1.00 23.92 ?  57   LEU A CG  1 
ATOM   408  C  CD1 . LEU A 1 55  ? 32.340  18.075  -9.656  1.00 21.48 ?  57   LEU A CD1 1 
ATOM   409  C  CD2 . LEU A 1 55  ? 34.718  18.724  -9.952  1.00 19.35 ?  57   LEU A CD2 1 
ATOM   410  N  N   . ALA A 1 56  ? 33.928  16.457  -14.730 1.00 13.80 ?  58   ALA A N   1 
ATOM   411  C  CA  . ALA A 1 56  ? 34.112  15.179  -15.398 1.00 14.37 ?  58   ALA A CA  1 
ATOM   412  C  C   . ALA A 1 56  ? 35.081  15.269  -16.568 1.00 20.62 ?  58   ALA A C   1 
ATOM   413  O  O   . ALA A 1 56  ? 35.514  14.228  -17.071 1.00 17.38 ?  58   ALA A O   1 
ATOM   414  C  CB  . ALA A 1 56  ? 32.754  14.635  -15.865 1.00 12.10 ?  58   ALA A CB  1 
ATOM   415  N  N   . ARG A 1 57  ? 35.453  16.481  -16.977 1.00 20.06 ?  59   ARG A N   1 
ATOM   416  C  CA  . ARG A 1 57  ? 36.409  16.660  -18.062 1.00 22.25 ?  59   ARG A CA  1 
ATOM   417  C  C   . ARG A 1 57  ? 37.709  15.931  -17.759 1.00 21.38 ?  59   ARG A C   1 
ATOM   418  O  O   . ARG A 1 57  ? 38.341  16.165  -16.726 1.00 20.16 ?  59   ARG A O   1 
ATOM   419  C  CB  . ARG A 1 57  ? 36.689  18.146  -18.285 1.00 28.18 ?  59   ARG A CB  1 
ATOM   420  C  CG  . ARG A 1 57  ? 37.648  18.410  -19.442 1.00 37.75 ?  59   ARG A CG  1 
ATOM   421  C  CD  . ARG A 1 57  ? 37.754  19.890  -19.790 1.00 37.12 ?  59   ARG A CD  1 
ATOM   422  N  NE  . ARG A 1 57  ? 36.460  20.564  -19.755 1.00 42.56 ?  59   ARG A NE  1 
ATOM   423  C  CZ  . ARG A 1 57  ? 36.175  21.599  -18.970 1.00 43.33 ?  59   ARG A CZ  1 
ATOM   424  N  NH1 . ARG A 1 57  ? 37.098  22.094  -18.154 1.00 48.55 ?  59   ARG A NH1 1 
ATOM   425  N  NH2 . ARG A 1 57  ? 34.968  22.148  -19.003 1.00 41.63 ?  59   ARG A NH2 1 
ATOM   426  N  N   . GLY A 1 58  ? 38.109  15.047  -18.673 1.00 27.07 ?  60   GLY A N   1 
ATOM   427  C  CA  . GLY A 1 58  ? 39.366  14.338  -18.564 1.00 29.15 ?  60   GLY A CA  1 
ATOM   428  C  C   . GLY A 1 58  ? 39.347  13.126  -17.665 1.00 32.77 ?  60   GLY A C   1 
ATOM   429  O  O   . GLY A 1 58  ? 40.359  12.423  -17.585 1.00 33.02 ?  60   GLY A O   1 
ATOM   430  N  N   . LYS A 1 59  ? 38.239  12.857  -16.982 1.00 21.49 ?  61   LYS A N   1 
ATOM   431  C  CA  . LYS A 1 59  ? 38.170  11.726  -16.071 1.00 23.06 ?  61   LYS A CA  1 
ATOM   432  C  C   . LYS A 1 59  ? 38.031  10.428  -16.858 1.00 19.90 ?  61   LYS A C   1 
ATOM   433  O  O   . LYS A 1 59  ? 37.344  10.378  -17.879 1.00 27.01 ?  61   LYS A O   1 
ATOM   434  C  CB  . LYS A 1 59  ? 36.995  11.894  -15.111 1.00 20.03 ?  61   LYS A CB  1 
ATOM   435  C  CG  . LYS A 1 59  ? 37.156  13.009  -14.073 1.00 25.04 ?  61   LYS A CG  1 
ATOM   436  C  CD  . LYS A 1 59  ? 38.555  13.075  -13.473 1.00 23.79 ?  61   LYS A CD  1 
ATOM   437  C  CE  . LYS A 1 59  ? 38.691  14.255  -12.506 1.00 31.48 ?  61   LYS A CE  1 
ATOM   438  N  NZ  . LYS A 1 59  ? 38.488  15.581  -13.168 1.00 32.20 ?  61   LYS A NZ  1 
ATOM   439  N  N   . ARG A 1 60  ? 38.684  9.373   -16.370 1.00 20.26 ?  62   ARG A N   1 
ATOM   440  C  CA  . ARG A 1 60  ? 38.717  8.092   -17.064 1.00 21.03 ?  62   ARG A CA  1 
ATOM   441  C  C   . ARG A 1 60  ? 37.745  7.065   -16.495 1.00 23.74 ?  62   ARG A C   1 
ATOM   442  O  O   . ARG A 1 60  ? 37.362  6.133   -17.210 1.00 25.84 ?  62   ARG A O   1 
ATOM   443  C  CB  . ARG A 1 60  ? 40.141  7.517   -17.035 1.00 26.08 ?  62   ARG A CB  1 
ATOM   444  N  N   . SER A 1 61  ? 37.326  7.215   -15.243 1.00 19.62 ?  63   SER A N   1 
ATOM   445  C  CA  . SER A 1 61  ? 36.420  6.262   -14.620 1.00 17.42 ?  63   SER A CA  1 
ATOM   446  C  C   . SER A 1 61  ? 35.542  7.017   -13.635 1.00 17.65 ?  63   SER A C   1 
ATOM   447  O  O   . SER A 1 61  ? 35.905  8.095   -13.159 1.00 12.55 ?  63   SER A O   1 
ATOM   448  C  CB  . SER A 1 61  ? 37.186  5.145   -13.909 1.00 19.11 ?  63   SER A CB  1 
ATOM   449  O  OG  . SER A 1 61  ? 38.014  5.693   -12.893 1.00 16.86 ?  63   SER A OG  1 
ATOM   450  N  N   . ALA A 1 62  ? 34.361  6.463   -13.355 1.00 15.15 ?  64   ALA A N   1 
ATOM   451  C  CA  . ALA A 1 62  ? 33.499  7.070   -12.351 1.00 12.38 ?  64   ALA A CA  1 
ATOM   452  C  C   . ALA A 1 62  ? 32.828  5.991   -11.523 1.00 11.94 ?  64   ALA A C   1 
ATOM   453  O  O   . ALA A 1 62  ? 32.535  4.898   -12.015 1.00 13.04 ?  64   ALA A O   1 
ATOM   454  C  CB  . ALA A 1 62  ? 32.429  7.974   -12.970 1.00 13.73 ?  64   ALA A CB  1 
ATOM   455  N  N   . CYS A 1 63  ? 32.564  6.325   -10.261 1.00 8.08  ?  65   CYS A N   1 
ATOM   456  C  CA  . CYS A 1 63  ? 31.812  5.457   -9.371  1.00 7.10  ?  65   CYS A CA  1 
ATOM   457  C  C   . CYS A 1 63  ? 30.695  6.285   -8.760  1.00 9.80  ?  65   CYS A C   1 
ATOM   458  O  O   . CYS A 1 63  ? 30.958  7.323   -8.149  1.00 12.17 ?  65   CYS A O   1 
ATOM   459  C  CB  . CYS A 1 63  ? 32.710  4.838   -8.288  1.00 10.89 ?  65   CYS A CB  1 
ATOM   460  S  SG  . CYS A 1 63  ? 31.832  3.677   -7.165  1.00 13.62 ?  65   CYS A SG  1 
ATOM   461  N  N   . ILE A 1 64  ? 29.454  5.855   -8.973  1.00 8.76  ?  66   ILE A N   1 
ATOM   462  C  CA  . ILE A 1 64  ? 28.269  6.532   -8.460  1.00 8.17  ?  66   ILE A CA  1 
ATOM   463  C  C   . ILE A 1 64  ? 27.667  5.688   -7.350  1.00 8.00  ?  66   ILE A C   1 
ATOM   464  O  O   . ILE A 1 64  ? 27.220  4.559   -7.602  1.00 9.32  ?  66   ILE A O   1 
ATOM   465  C  CB  . ILE A 1 64  ? 27.220  6.752   -9.566  1.00 8.19  ?  66   ILE A CB  1 
ATOM   466  C  CG1 . ILE A 1 64  ? 27.840  7.470   -10.764 1.00 11.40 ?  66   ILE A CG1 1 
ATOM   467  C  CG2 . ILE A 1 64  ? 26.037  7.512   -9.004  1.00 9.60  ?  66   ILE A CG2 1 
ATOM   468  C  CD1 . ILE A 1 64  ? 26.880  7.556   -11.951 1.00 11.59 ?  66   ILE A CD1 1 
ATOM   469  N  N   . LEU A 1 65  ? 27.599  6.251   -6.141  1.00 7.96  ?  67   LEU A N   1 
ATOM   470  C  CA  . LEU A 1 65  ? 26.973  5.576   -5.007  1.00 9.00  ?  67   LEU A CA  1 
ATOM   471  C  C   . LEU A 1 65  ? 25.470  5.829   -5.016  1.00 9.12  ?  67   LEU A C   1 
ATOM   472  O  O   . LEU A 1 65  ? 25.041  6.975   -5.161  1.00 9.69  ?  67   LEU A O   1 
ATOM   473  C  CB  . LEU A 1 65  ? 27.546  6.084   -3.689  1.00 6.38  ?  67   LEU A CB  1 
ATOM   474  C  CG  . LEU A 1 65  ? 29.064  5.997   -3.559  1.00 8.33  ?  67   LEU A CG  1 
ATOM   475  C  CD1 . LEU A 1 65  ? 29.488  6.340   -2.152  1.00 9.89  ?  67   LEU A CD1 1 
ATOM   476  C  CD2 . LEU A 1 65  ? 29.504  4.580   -3.897  1.00 7.47  ?  67   LEU A CD2 1 
ATOM   477  N  N   . VAL A 1 66  ? 24.680  4.761   -4.826  1.00 9.16  ?  68   VAL A N   1 
ATOM   478  C  CA  . VAL A 1 66  ? 23.225  4.829   -4.711  1.00 8.73  ?  68   VAL A CA  1 
ATOM   479  C  C   . VAL A 1 66  ? 22.810  4.067   -3.457  1.00 9.56  ?  68   VAL A C   1 
ATOM   480  O  O   . VAL A 1 66  ? 23.490  3.137   -3.013  1.00 9.71  ?  68   VAL A O   1 
ATOM   481  C  CB  . VAL A 1 66  ? 22.490  4.264   -5.963  1.00 9.19  ?  68   VAL A CB  1 
ATOM   482  C  CG1 . VAL A 1 66  ? 22.895  5.029   -7.228  1.00 9.49  ?  68   VAL A CG1 1 
ATOM   483  C  CG2 . VAL A 1 66  ? 22.781  2.780   -6.130  1.00 10.12 ?  68   VAL A CG2 1 
ATOM   484  N  N   . CYS A 1 67  ? 21.687  4.473   -2.874  1.00 8.42  ?  69   CYS A N   1 
ATOM   485  C  CA  . CYS A 1 67  ? 21.158  3.786   -1.705  1.00 7.18  ?  69   CYS A CA  1 
ATOM   486  C  C   . CYS A 1 67  ? 20.585  2.421   -2.086  1.00 9.97  ?  69   CYS A C   1 
ATOM   487  O  O   . CYS A 1 67  ? 20.258  2.158   -3.251  1.00 11.51 ?  69   CYS A O   1 
ATOM   488  C  CB  . CYS A 1 67  ? 20.079  4.641   -1.044  1.00 9.41  ?  69   CYS A CB  1 
ATOM   489  S  SG  . CYS A 1 67  ? 20.710  6.200   -0.374  1.00 13.37 ?  69   CYS A SG  1 
ATOM   490  N  N   . ASP A 1 68  ? 20.452  1.538   -1.093  1.00 8.37  ?  70   ASP A N   1 
ATOM   491  C  CA  . ASP A 1 68  ? 19.877  0.224   -1.364  1.00 10.58 ?  70   ASP A CA  1 
ATOM   492  C  C   . ASP A 1 68  ? 18.346  0.295   -1.238  1.00 11.77 ?  70   ASP A C   1 
ATOM   493  O  O   . ASP A 1 68  ? 17.760  1.384   -1.202  1.00 7.97  ?  70   ASP A O   1 
ATOM   494  C  CB  . ASP A 1 68  ? 20.525  -0.853  -0.469  1.00 9.10  ?  70   ASP A CB  1 
ATOM   495  C  CG  . ASP A 1 68  ? 20.157  -0.716  1.011   1.00 11.65 ?  70   ASP A CG  1 
ATOM   496  O  OD1 . ASP A 1 68  ? 20.635  -1.545  1.813   1.00 14.68 ?  70   ASP A OD1 1 
ATOM   497  O  OD2 . ASP A 1 68  ? 19.451  0.228   1.398   1.00 9.95  ?  70   ASP A OD2 1 
ATOM   498  N  N   . ILE A 1 69  ? 17.690  -0.867  -1.140  1.00 9.35  ?  71   ILE A N   1 
ATOM   499  C  CA  . ILE A 1 69  ? 16.230  -0.926  -1.261  1.00 9.83  ?  71   ILE A CA  1 
ATOM   500  C  C   . ILE A 1 69  ? 15.544  -0.198  -0.105  1.00 11.75 ?  71   ILE A C   1 
ATOM   501  O  O   . ILE A 1 69  ? 14.435  0.324   -0.277  1.00 10.68 ?  71   ILE A O   1 
ATOM   502  C  CB  . ILE A 1 69  ? 15.760  -2.393  -1.348  1.00 13.66 ?  71   ILE A CB  1 
ATOM   503  C  CG1 . ILE A 1 69  ? 14.311  -2.478  -1.851  1.00 15.19 ?  71   ILE A CG1 1 
ATOM   504  C  CG2 . ILE A 1 69  ? 15.916  -3.101  0.024   1.00 13.96 ?  71   ILE A CG2 1 
ATOM   505  C  CD1 . ILE A 1 69  ? 14.161  -1.994  -3.256  1.00 13.27 ?  71   ILE A CD1 1 
ATOM   506  N  N   . THR A 1 70  ? 16.190  -0.122  1.062   1.00 9.70  ?  72   THR A N   1 
ATOM   507  C  CA  . THR A 1 70  ? 15.572  0.432   2.272   1.00 8.59  ?  72   THR A CA  1 
ATOM   508  C  C   . THR A 1 70  ? 15.321  1.932   2.199   1.00 12.40 ?  72   THR A C   1 
ATOM   509  O  O   . THR A 1 70  ? 14.599  2.456   3.054   1.00 10.28 ?  72   THR A O   1 
ATOM   510  C  CB  . THR A 1 70  ? 16.420  0.124   3.519   1.00 10.92 ?  72   THR A CB  1 
ATOM   511  O  OG1 . THR A 1 70  ? 17.621  0.912   3.500   1.00 9.55  ?  72   THR A OG1 1 
ATOM   512  C  CG2 . THR A 1 70  ? 16.783  -1.382  3.581   1.00 12.21 ?  72   THR A CG2 1 
ATOM   513  N  N   . ARG A 1 71  ? 15.878  2.636   1.210   1.00 11.24 ?  73   ARG A N   1 
ATOM   514  C  CA  . ARG A 1 71  ? 15.608  4.054   1.026   1.00 10.64 ?  73   ARG A CA  1 
ATOM   515  C  C   . ARG A 1 71  ? 14.825  4.255   -0.261  1.00 9.92  ?  73   ARG A C   1 
ATOM   516  O  O   . ARG A 1 71  ? 15.301  3.853   -1.326  1.00 11.25 ?  73   ARG A O   1 
ATOM   517  C  CB  . ARG A 1 71  ? 16.909  4.867   0.952   1.00 6.59  ?  73   ARG A CB  1 
ATOM   518  C  CG  . ARG A 1 71  ? 17.986  4.454   1.968   1.00 9.39  ?  73   ARG A CG  1 
ATOM   519  C  CD  . ARG A 1 71  ? 17.428  4.490   3.370   1.00 11.33 ?  73   ARG A CD  1 
ATOM   520  N  NE  . ARG A 1 71  ? 18.453  4.823   4.372   1.00 10.56 ?  73   ARG A NE  1 
ATOM   521  C  CZ  . ARG A 1 71  ? 18.733  4.090   5.436   1.00 9.50  ?  73   ARG A CZ  1 
ATOM   522  N  NH1 . ARG A 1 71  ? 18.102  2.937   5.646   1.00 9.59  ?  73   ARG A NH1 1 
ATOM   523  N  NH2 . ARG A 1 71  ? 19.671  4.509   6.288   1.00 8.06  ?  73   ARG A NH2 1 
ATOM   524  N  N   . PRO A 1 72  ? 13.701  4.902   -0.222  1.00 8.18  ?  74   PRO A N   1 
ATOM   525  C  CA  . PRO A 1 72  ? 12.891  5.124   -1.429  1.00 10.25 ?  74   PRO A CA  1 
ATOM   526  C  C   . PRO A 1 72  ? 13.352  6.301   -2.296  1.00 15.68 ?  74   PRO A C   1 
ATOM   527  O  O   . PRO A 1 72  ? 12.556  7.171   -2.672  1.00 13.99 ?  74   PRO A O   1 
ATOM   528  C  CB  . PRO A 1 72  ? 11.494  5.363   -0.849  1.00 13.31 ?  74   PRO A CB  1 
ATOM   529  C  CG  . PRO A 1 72  ? 11.762  6.050   0.468   1.00 9.11  ?  74   PRO A CG  1 
ATOM   530  C  CD  . PRO A 1 72  ? 13.053  5.427   0.999   1.00 12.16 ?  74   PRO A CD  1 
ATOM   531  N  N   . VAL A 1 73  ? 14.645  6.328   -2.616  1.00 12.64 ?  75   VAL A N   1 
ATOM   532  C  CA  . VAL A 1 73  ? 15.182  7.352   -3.526  1.00 13.47 ?  75   VAL A CA  1 
ATOM   533  C  C   . VAL A 1 73  ? 14.626  7.122   -4.927  1.00 14.03 ?  75   VAL A C   1 
ATOM   534  O  O   . VAL A 1 73  ? 14.712  5.995   -5.449  1.00 12.07 ?  75   VAL A O   1 
ATOM   535  C  CB  . VAL A 1 73  ? 16.709  7.315   -3.547  1.00 11.64 ?  75   VAL A CB  1 
ATOM   536  C  CG1 . VAL A 1 73  ? 17.269  8.551   -4.295  1.00 13.18 ?  75   VAL A CG1 1 
ATOM   537  C  CG2 . VAL A 1 73  ? 17.288  7.223   -2.132  1.00 11.22 ?  75   VAL A CG2 1 
ATOM   538  N  N   . PRO A 1 74  ? 14.057  8.142   -5.575  1.00 16.97 ?  76   PRO A N   1 
ATOM   539  C  CA  . PRO A 1 74  ? 13.687  8.006   -6.991  1.00 14.95 ?  76   PRO A CA  1 
ATOM   540  C  C   . PRO A 1 74  ? 14.920  8.087   -7.884  1.00 15.65 ?  76   PRO A C   1 
ATOM   541  O  O   . PRO A 1 74  ? 15.135  9.075   -8.600  1.00 12.63 ?  76   PRO A O   1 
ATOM   542  C  CB  . PRO A 1 74  ? 12.718  9.180   -7.214  1.00 17.16 ?  76   PRO A CB  1 
ATOM   543  C  CG  . PRO A 1 74  ? 13.183  10.215  -6.258  1.00 20.13 ?  76   PRO A CG  1 
ATOM   544  C  CD  . PRO A 1 74  ? 13.763  9.489   -5.050  1.00 15.22 ?  76   PRO A CD  1 
ATOM   545  N  N   . ASN A 1 75  ? 15.723  7.022   -7.852  1.00 11.89 ?  77   ASN A N   1 
ATOM   546  C  CA  . ASN A 1 75  ? 17.055  7.063   -8.454  1.00 15.34 ?  77   ASN A CA  1 
ATOM   547  C  C   . ASN A 1 75  ? 17.077  7.455   -9.923  1.00 14.81 ?  77   ASN A C   1 
ATOM   548  O  O   . ASN A 1 75  ? 17.957  8.251   -10.302 1.00 12.06 ?  77   ASN A O   1 
ATOM   549  C  CB  . ASN A 1 75  ? 17.748  5.715   -8.248  1.00 14.74 ?  77   ASN A CB  1 
ATOM   550  C  CG  . ASN A 1 75  ? 18.104  5.478   -6.800  1.00 15.06 ?  77   ASN A CG  1 
ATOM   551  O  OD1 . ASN A 1 75  ? 18.903  6.224   -6.199  1.00 15.78 ?  77   ASN A OD1 1 
ATOM   552  N  ND2 . ASN A 1 75  ? 17.488  4.474   -6.209  1.00 14.43 ?  77   ASN A ND2 1 
ATOM   553  N  N   . PRO A 1 76  ? 16.182  6.970   -10.788 1.00 14.22 ?  78   PRO A N   1 
ATOM   554  C  CA  . PRO A 1 76  ? 16.278  7.367   -12.200 1.00 13.73 ?  78   PRO A CA  1 
ATOM   555  C  C   . PRO A 1 76  ? 16.161  8.863   -12.420 1.00 13.87 ?  78   PRO A C   1 
ATOM   556  O  O   . PRO A 1 76  ? 16.756  9.378   -13.370 1.00 17.46 ?  78   PRO A O   1 
ATOM   557  C  CB  . PRO A 1 76  ? 15.105  6.618   -12.855 1.00 14.89 ?  78   PRO A CB  1 
ATOM   558  C  CG  . PRO A 1 76  ? 14.928  5.425   -12.016 1.00 14.04 ?  78   PRO A CG  1 
ATOM   559  C  CD  . PRO A 1 76  ? 15.143  5.939   -10.595 1.00 13.86 ?  78   PRO A CD  1 
ATOM   560  N  N   . VAL A 1 77  ? 15.392  9.567   -11.584 1.00 10.91 ?  79   VAL A N   1 
ATOM   561  C  CA  . VAL A 1 77  ? 15.271  11.019  -11.687 1.00 12.21 ?  79   VAL A CA  1 
ATOM   562  C  C   . VAL A 1 77  ? 16.620  11.692  -11.447 1.00 14.89 ?  79   VAL A C   1 
ATOM   563  O  O   . VAL A 1 77  ? 16.928  12.737  -12.036 1.00 12.84 ?  79   VAL A O   1 
ATOM   564  C  CB  . VAL A 1 77  ? 14.209  11.511  -10.682 1.00 14.65 ?  79   VAL A CB  1 
ATOM   565  C  CG1 . VAL A 1 77  ? 14.281  13.016  -10.496 1.00 16.69 ?  79   VAL A CG1 1 
ATOM   566  C  CG2 . VAL A 1 77  ? 12.801  11.043  -11.126 1.00 12.72 ?  79   VAL A CG2 1 
ATOM   567  N  N   . LEU A 1 78  ? 17.412  11.137  -10.533 1.00 14.67 ?  80   LEU A N   1 
ATOM   568  C  CA  . LEU A 1 78  ? 18.732  11.684  -10.242 1.00 13.84 ?  80   LEU A CA  1 
ATOM   569  C  C   . LEU A 1 78  ? 19.764  11.170  -11.234 1.00 10.73 ?  80   LEU A C   1 
ATOM   570  O  O   . LEU A 1 78  ? 20.649  11.921  -11.661 1.00 15.00 ?  80   LEU A O   1 
ATOM   571  C  CB  . LEU A 1 78  ? 19.171  11.302  -8.821  1.00 11.36 ?  80   LEU A CB  1 
ATOM   572  C  CG  . LEU A 1 78  ? 18.523  11.922  -7.570  1.00 17.11 ?  80   LEU A CG  1 
ATOM   573  C  CD1 . LEU A 1 78  ? 17.031  11.656  -7.442  1.00 19.00 ?  80   LEU A CD1 1 
ATOM   574  C  CD2 . LEU A 1 78  ? 19.232  11.411  -6.313  1.00 17.32 ?  80   LEU A CD2 1 
ATOM   575  N  N   . LEU A 1 79  ? 19.661  9.892   -11.609 1.00 11.08 ?  81   LEU A N   1 
ATOM   576  C  CA  . LEU A 1 79  ? 20.730  9.227   -12.359 1.00 14.89 ?  81   LEU A CA  1 
ATOM   577  C  C   . LEU A 1 79  ? 20.709  9.568   -13.841 1.00 13.24 ?  81   LEU A C   1 
ATOM   578  O  O   . LEU A 1 79  ? 21.765  9.692   -14.462 1.00 12.90 ?  81   LEU A O   1 
ATOM   579  C  CB  . LEU A 1 79  ? 20.631  7.712   -12.199 1.00 13.28 ?  81   LEU A CB  1 
ATOM   580  C  CG  . LEU A 1 79  ? 21.064  7.153   -10.860 1.00 11.91 ?  81   LEU A CG  1 
ATOM   581  C  CD1 . LEU A 1 79  ? 20.928  5.651   -10.900 1.00 20.26 ?  81   LEU A CD1 1 
ATOM   582  C  CD2 . LEU A 1 79  ? 22.515  7.537   -10.551 1.00 13.81 ?  81   LEU A CD2 1 
ATOM   583  N  N   . ARG A 1 80  ? 19.532  9.664   -14.455 1.00 12.61 ?  82   ARG A N   1 
ATOM   584  C  CA  . ARG A 1 80  ? 19.539  9.957   -15.883 1.00 12.82 ?  82   ARG A CA  1 
ATOM   585  C  C   . ARG A 1 80  ? 20.298  11.242  -16.191 1.00 12.49 ?  82   ARG A C   1 
ATOM   586  O  O   . ARG A 1 80  ? 21.138  11.227  -17.109 1.00 12.89 ?  82   ARG A O   1 
ATOM   587  C  CB  . ARG A 1 80  ? 18.102  9.959   -16.421 1.00 14.99 ?  82   ARG A CB  1 
ATOM   588  C  CG  . ARG A 1 80  ? 17.561  8.545   -16.677 1.00 17.83 ?  82   ARG A CG  1 
ATOM   589  C  CD  . ARG A 1 80  ? 16.223  8.558   -17.429 1.00 20.13 ?  82   ARG A CD  1 
ATOM   590  N  NE  . ARG A 1 80  ? 15.220  9.242   -16.622 1.00 23.22 ?  82   ARG A NE  1 
ATOM   591  C  CZ  . ARG A 1 80  ? 14.278  8.626   -15.913 1.00 24.62 ?  82   ARG A CZ  1 
ATOM   592  N  NH1 . ARG A 1 80  ? 14.180  7.301   -15.935 1.00 21.91 ?  82   ARG A NH1 1 
ATOM   593  N  NH2 . ARG A 1 80  ? 13.427  9.341   -15.187 1.00 22.39 ?  82   ARG A NH2 1 
ATOM   594  N  N   . PRO A 1 81  ? 20.099  12.355  -15.472 1.00 12.73 ?  83   PRO A N   1 
ATOM   595  C  CA  . PRO A 1 81  ? 20.903  13.558  -15.771 1.00 12.93 ?  83   PRO A CA  1 
ATOM   596  C  C   . PRO A 1 81  ? 22.394  13.379  -15.511 1.00 12.40 ?  83   PRO A C   1 
ATOM   597  O  O   . PRO A 1 81  ? 23.219  13.897  -16.278 1.00 12.24 ?  83   PRO A O   1 
ATOM   598  C  CB  . PRO A 1 81  ? 20.301  14.623  -14.845 1.00 15.85 ?  83   PRO A CB  1 
ATOM   599  C  CG  . PRO A 1 81  ? 18.914  14.148  -14.567 1.00 14.66 ?  83   PRO A CG  1 
ATOM   600  C  CD  . PRO A 1 81  ? 19.003  12.647  -14.530 1.00 10.25 ?  83   PRO A CD  1 
ATOM   601  N  N   . ILE A 1 82  ? 22.756  12.685  -14.433 1.00 8.84  ?  84   ILE A N   1 
ATOM   602  C  CA  . ILE A 1 82  ? 24.172  12.443  -14.137 1.00 9.74  ?  84   ILE A CA  1 
ATOM   603  C  C   . ILE A 1 82  ? 24.807  11.637  -15.261 1.00 13.08 ?  84   ILE A C   1 
ATOM   604  O  O   . ILE A 1 82  ? 25.893  11.966  -15.763 1.00 13.15 ?  84   ILE A O   1 
ATOM   605  C  CB  . ILE A 1 82  ? 24.326  11.709  -12.791 1.00 11.41 ?  84   ILE A CB  1 
ATOM   606  C  CG1 . ILE A 1 82  ? 23.888  12.585  -11.621 1.00 14.84 ?  84   ILE A CG1 1 
ATOM   607  C  CG2 . ILE A 1 82  ? 25.778  11.239  -12.597 1.00 10.61 ?  84   ILE A CG2 1 
ATOM   608  C  CD1 . ILE A 1 82  ? 23.747  11.796  -10.306 1.00 11.53 ?  84   ILE A CD1 1 
ATOM   609  N  N   . LEU A 1 83  ? 24.141  10.548  -15.654 1.00 9.76  ?  85   LEU A N   1 
ATOM   610  C  CA  . LEU A 1 83  ? 24.687  9.656   -16.675 1.00 12.60 ?  85   LEU A CA  1 
ATOM   611  C  C   . LEU A 1 83  ? 24.764  10.329  -18.042 1.00 13.53 ?  85   LEU A C   1 
ATOM   612  O  O   . LEU A 1 83  ? 25.705  10.073  -18.800 1.00 13.34 ?  85   LEU A O   1 
ATOM   613  C  CB  . LEU A 1 83  ? 23.851  8.377   -16.741 1.00 13.93 ?  85   LEU A CB  1 
ATOM   614  C  CG  . LEU A 1 83  ? 23.914  7.465   -15.511 1.00 12.18 ?  85   LEU A CG  1 
ATOM   615  C  CD1 . LEU A 1 83  ? 22.889  6.350   -15.602 1.00 14.81 ?  85   LEU A CD1 1 
ATOM   616  C  CD2 . LEU A 1 83  ? 25.336  6.878   -15.350 1.00 12.95 ?  85   LEU A CD2 1 
ATOM   617  N  N   . ARG A 1 84  ? 23.799  11.188  -18.378 1.00 12.21 ?  86   ARG A N   1 
ATOM   618  C  CA  . ARG A 1 84  ? 23.918  11.961  -19.611 1.00 13.95 ?  86   ARG A CA  1 
ATOM   619  C  C   . ARG A 1 84  ? 25.141  12.865  -19.561 1.00 13.82 ?  86   ARG A C   1 
ATOM   620  O  O   . ARG A 1 84  ? 25.898  12.961  -20.537 1.00 12.74 ?  86   ARG A O   1 
ATOM   621  C  CB  . ARG A 1 84  ? 22.654  12.785  -19.859 1.00 13.31 ?  86   ARG A CB  1 
ATOM   622  C  CG  . ARG A 1 84  ? 21.444  11.936  -20.215 1.00 18.33 ?  86   ARG A CG  1 
ATOM   623  C  CD  . ARG A 1 84  ? 20.285  12.779  -20.769 1.00 18.92 ?  86   ARG A CD  1 
ATOM   624  N  NE  . ARG A 1 84  ? 19.641  13.622  -19.760 1.00 23.24 ?  86   ARG A NE  1 
ATOM   625  C  CZ  . ARG A 1 84  ? 18.506  13.314  -19.135 1.00 27.41 ?  86   ARG A CZ  1 
ATOM   626  N  NH1 . ARG A 1 84  ? 17.890  12.162  -19.390 1.00 24.61 ?  86   ARG A NH1 1 
ATOM   627  N  NH2 . ARG A 1 84  ? 17.992  14.145  -18.233 1.00 26.23 ?  86   ARG A NH2 1 
ATOM   628  N  N   . THR A 1 85  ? 25.352  13.530  -18.423 1.00 11.76 ?  87   THR A N   1 
ATOM   629  C  CA  . THR A 1 85  ? 26.481  14.447  -18.297 1.00 12.21 ?  87   THR A CA  1 
ATOM   630  C  C   . THR A 1 85  ? 27.813  13.711  -18.396 1.00 13.29 ?  87   THR A C   1 
ATOM   631  O  O   . THR A 1 85  ? 28.750  14.186  -19.058 1.00 13.34 ?  87   THR A O   1 
ATOM   632  C  CB  . THR A 1 85  ? 26.366  15.213  -16.980 1.00 17.54 ?  87   THR A CB  1 
ATOM   633  O  OG1 . THR A 1 85  ? 25.207  16.056  -17.040 1.00 15.56 ?  87   THR A OG1 1 
ATOM   634  C  CG2 . THR A 1 85  ? 27.612  16.061  -16.740 1.00 17.27 ?  87   THR A CG2 1 
ATOM   635  N  N   . LEU A 1 86  ? 27.916  12.539  -17.760 1.00 12.08 ?  88   LEU A N   1 
ATOM   636  C  CA  . LEU A 1 86  ? 29.142  11.753  -17.861 1.00 12.00 ?  88   LEU A CA  1 
ATOM   637  C  C   . LEU A 1 86  ? 29.384  11.278  -19.288 1.00 14.30 ?  88   LEU A C   1 
ATOM   638  O  O   . LEU A 1 86  ? 30.530  11.243  -19.753 1.00 13.49 ?  88   LEU A O   1 
ATOM   639  C  CB  . LEU A 1 86  ? 29.081  10.559  -16.914 1.00 11.72 ?  88   LEU A CB  1 
ATOM   640  C  CG  . LEU A 1 86  ? 28.976  10.931  -15.439 1.00 15.65 ?  88   LEU A CG  1 
ATOM   641  C  CD1 . LEU A 1 86  ? 29.021  9.681   -14.565 1.00 14.97 ?  88   LEU A CD1 1 
ATOM   642  C  CD2 . LEU A 1 86  ? 30.065  11.901  -15.055 1.00 17.95 ?  88   LEU A CD2 1 
ATOM   643  N  N   . HIS A 1 87  ? 28.323  10.873  -19.987 1.00 10.15 ?  89   HIS A N   1 
ATOM   644  C  CA  . HIS A 1 87  ? 28.481  10.482  -21.382 1.00 12.61 ?  89   HIS A CA  1 
ATOM   645  C  C   . HIS A 1 87  ? 28.974  11.662  -22.207 1.00 13.34 ?  89   HIS A C   1 
ATOM   646  O  O   . HIS A 1 87  ? 29.908  11.526  -23.010 1.00 14.69 ?  89   HIS A O   1 
ATOM   647  C  CB  . HIS A 1 87  ? 27.158  9.936   -21.930 1.00 12.57 ?  89   HIS A CB  1 
ATOM   648  C  CG  . HIS A 1 87  ? 27.305  9.179   -23.216 1.00 21.44 ?  89   HIS A CG  1 
ATOM   649  N  ND1 . HIS A 1 87  ? 27.723  7.866   -23.266 1.00 29.06 ?  89   HIS A ND1 1 
ATOM   650  C  CD2 . HIS A 1 87  ? 27.101  9.558   -24.500 1.00 24.27 ?  89   HIS A CD2 1 
ATOM   651  C  CE1 . HIS A 1 87  ? 27.762  7.465   -24.526 1.00 22.38 ?  89   HIS A CE1 1 
ATOM   652  N  NE2 . HIS A 1 87  ? 27.389  8.473   -25.294 1.00 22.11 ?  89   HIS A NE2 1 
ATOM   653  N  N   . ALA A 1 88  ? 28.375  12.841  -21.991 1.00 12.50 ?  90   ALA A N   1 
ATOM   654  C  CA  . ALA A 1 88  ? 28.784  14.040  -22.719 1.00 14.62 ?  90   ALA A CA  1 
ATOM   655  C  C   . ALA A 1 88  ? 30.255  14.355  -22.480 1.00 15.99 ?  90   ALA A C   1 
ATOM   656  O  O   . ALA A 1 88  ? 30.961  14.804  -23.396 1.00 16.38 ?  90   ALA A O   1 
ATOM   657  C  CB  . ALA A 1 88  ? 27.906  15.228  -22.310 1.00 13.80 ?  90   ALA A CB  1 
ATOM   658  N  N   . ALA A 1 89  ? 30.735  14.111  -21.258 1.00 12.38 ?  91   ALA A N   1 
ATOM   659  C  CA  . ALA A 1 89  ? 32.118  14.395  -20.879 1.00 14.01 ?  91   ALA A CA  1 
ATOM   660  C  C   . ALA A 1 89  ? 33.098  13.384  -21.449 1.00 17.29 ?  91   ALA A C   1 
ATOM   661  O  O   . ALA A 1 89  ? 34.314  13.577  -21.318 1.00 22.13 ?  91   ALA A O   1 
ATOM   662  C  CB  . ALA A 1 89  ? 32.253  14.420  -19.358 1.00 14.16 ?  91   ALA A CB  1 
ATOM   663  N  N   . GLY A 1 90  ? 32.609  12.307  -22.055 1.00 15.10 ?  92   GLY A N   1 
ATOM   664  C  CA  . GLY A 1 90  ? 33.486  11.372  -22.722 1.00 17.51 ?  92   GLY A CA  1 
ATOM   665  C  C   . GLY A 1 90  ? 33.694  10.058  -22.017 1.00 20.17 ?  92   GLY A C   1 
ATOM   666  O  O   . GLY A 1 90  ? 34.484  9.243   -22.509 1.00 19.80 ?  92   GLY A O   1 
ATOM   667  N  N   . LEU A 1 91  ? 33.029  9.811   -20.884 1.00 13.94 ?  93   LEU A N   1 
ATOM   668  C  CA  . LEU A 1 91  ? 33.186  8.536   -20.205 1.00 16.00 ?  93   LEU A CA  1 
ATOM   669  C  C   . LEU A 1 91  ? 32.310  7.497   -20.885 1.00 22.45 ?  93   LEU A C   1 
ATOM   670  O  O   . LEU A 1 91  ? 31.120  7.731   -21.109 1.00 21.53 ?  93   LEU A O   1 
ATOM   671  C  CB  . LEU A 1 91  ? 32.818  8.647   -18.726 1.00 15.17 ?  93   LEU A CB  1 
ATOM   672  C  CG  . LEU A 1 91  ? 33.806  9.320   -17.767 1.00 24.80 ?  93   LEU A CG  1 
ATOM   673  C  CD1 . LEU A 1 91  ? 33.759  10.838  -17.893 1.00 21.03 ?  93   LEU A CD1 1 
ATOM   674  C  CD2 . LEU A 1 91  ? 33.594  8.893   -16.318 1.00 25.67 ?  93   LEU A CD2 1 
ATOM   675  N  N   . ALA A 1 92  ? 32.899  6.358   -21.228 1.00 22.70 ?  94   ALA A N   1 
ATOM   676  C  CA  . ALA A 1 92  ? 32.131  5.265   -21.806 1.00 25.45 ?  94   ALA A CA  1 
ATOM   677  C  C   . ALA A 1 92  ? 31.310  4.578   -20.721 1.00 23.65 ?  94   ALA A C   1 
ATOM   678  O  O   . ALA A 1 92  ? 31.685  4.589   -19.544 1.00 21.76 ?  94   ALA A O   1 
ATOM   679  C  CB  . ALA A 1 92  ? 33.067  4.258   -22.472 1.00 26.82 ?  94   ALA A CB  1 
ATOM   680  N  N   . THR A 1 93  ? 30.189  3.959   -21.124 1.00 23.96 ?  95   THR A N   1 
ATOM   681  C  CA  . THR A 1 93  ? 29.357  3.287   -20.127 1.00 24.06 ?  95   THR A CA  1 
ATOM   682  C  C   . THR A 1 93  ? 30.147  2.220   -19.376 1.00 18.81 ?  95   THR A C   1 
ATOM   683  O  O   . THR A 1 93  ? 29.919  2.014   -18.178 1.00 19.97 ?  95   THR A O   1 
ATOM   684  C  CB  . THR A 1 93  ? 28.094  2.667   -20.752 1.00 23.93 ?  95   THR A CB  1 
ATOM   685  O  OG1 . THR A 1 93  ? 28.442  1.665   -21.715 1.00 25.03 ?  95   THR A OG1 1 
ATOM   686  C  CG2 . THR A 1 93  ? 27.191  3.728   -21.392 1.00 25.15 ?  95   THR A CG2 1 
ATOM   687  N  N   . GLN A 1 94  ? 31.085  1.542   -20.051 1.00 18.65 ?  96   GLN A N   1 
ATOM   688  C  CA  . GLN A 1 94  ? 31.948  0.571   -19.381 1.00 21.39 ?  96   GLN A CA  1 
ATOM   689  C  C   . GLN A 1 94  ? 32.868  1.206   -18.335 1.00 22.14 ?  96   GLN A C   1 
ATOM   690  O  O   . GLN A 1 94  ? 33.353  0.496   -17.445 1.00 23.15 ?  96   GLN A O   1 
ATOM   691  C  CB  . GLN A 1 94  ? 32.794  -0.191  -20.413 1.00 23.83 ?  96   GLN A CB  1 
ATOM   692  N  N   . ASP A 1 95  ? 33.117  2.513   -18.408 1.00 21.96 ?  97   ASP A N   1 
ATOM   693  C  CA  . ASP A 1 95  ? 33.940  3.192   -17.412 1.00 22.05 ?  97   ASP A CA  1 
ATOM   694  C  C   . ASP A 1 95  ? 33.157  3.624   -16.180 1.00 21.03 ?  97   ASP A C   1 
ATOM   695  O  O   . ASP A 1 95  ? 33.748  4.213   -15.272 1.00 17.79 ?  97   ASP A O   1 
ATOM   696  C  CB  . ASP A 1 95  ? 34.612  4.442   -18.003 1.00 25.32 ?  97   ASP A CB  1 
ATOM   697  C  CG  . ASP A 1 95  ? 35.367  4.169   -19.292 1.00 40.22 ?  97   ASP A CG  1 
ATOM   698  O  OD1 . ASP A 1 95  ? 35.275  5.017   -20.215 1.00 38.34 ?  97   ASP A OD1 1 
ATOM   699  O  OD2 . ASP A 1 95  ? 36.081  3.140   -19.363 1.00 31.66 ?  97   ASP A OD2 1 
ATOM   700  N  N   . ILE A 1 96  ? 31.851  3.384   -16.137 1.00 14.82 ?  98   ILE A N   1 
ATOM   701  C  CA  . ILE A 1 96  ? 31.001  3.864   -15.051 1.00 14.67 ?  98   ILE A CA  1 
ATOM   702  C  C   . ILE A 1 96  ? 30.527  2.680   -14.220 1.00 14.42 ?  98   ILE A C   1 
ATOM   703  O  O   . ILE A 1 96  ? 29.988  1.703   -14.758 1.00 19.59 ?  98   ILE A O   1 
ATOM   704  C  CB  . ILE A 1 96  ? 29.812  4.682   -15.591 1.00 15.00 ?  98   ILE A CB  1 
ATOM   705  C  CG1 . ILE A 1 96  ? 30.331  5.896   -16.370 1.00 15.89 ?  98   ILE A CG1 1 
ATOM   706  C  CG2 . ILE A 1 96  ? 28.889  5.118   -14.443 1.00 14.80 ?  98   ILE A CG2 1 
ATOM   707  C  CD1 . ILE A 1 96  ? 29.299  6.502   -17.333 1.00 18.23 ?  98   ILE A CD1 1 
ATOM   708  N  N   . LEU A 1 97  ? 30.726  2.763   -12.911 1.00 12.95 ?  99   LEU A N   1 
ATOM   709  C  CA  . LEU A 1 97  ? 30.221  1.774   -11.973 1.00 8.19  ?  99   LEU A CA  1 
ATOM   710  C  C   . LEU A 1 97  ? 29.135  2.414   -11.119 1.00 9.62  ?  99   LEU A C   1 
ATOM   711  O  O   . LEU A 1 97  ? 29.333  3.504   -10.576 1.00 11.14 ?  99   LEU A O   1 
ATOM   712  C  CB  . LEU A 1 97  ? 31.339  1.255   -11.067 1.00 10.96 ?  99   LEU A CB  1 
ATOM   713  C  CG  . LEU A 1 97  ? 30.879  0.380   -9.915  1.00 10.20 ?  99   LEU A CG  1 
ATOM   714  C  CD1 . LEU A 1 97  ? 30.268  -0.898  -10.423 1.00 11.87 ?  99   LEU A CD1 1 
ATOM   715  C  CD2 . LEU A 1 97  ? 32.048  0.098   -8.946  1.00 12.20 ?  99   LEU A CD2 1 
ATOM   716  N  N   . ILE A 1 98  ? 27.993  1.751   -11.009 1.00 8.96  ?  100  ILE A N   1 
ATOM   717  C  CA  . ILE A 1 98  ? 26.994  2.101   -10.007 1.00 6.35  ?  100  ILE A CA  1 
ATOM   718  C  C   . ILE A 1 98  ? 27.179  1.132   -8.845  1.00 8.37  ?  100  ILE A C   1 
ATOM   719  O  O   . ILE A 1 98  ? 27.056  -0.086  -9.010  1.00 9.48  ?  100  ILE A O   1 
ATOM   720  C  CB  . ILE A 1 98  ? 25.563  2.050   -10.582 1.00 9.22  ?  100  ILE A CB  1 
ATOM   721  C  CG1 . ILE A 1 98  ? 25.409  3.113   -11.677 1.00 10.16 ?  100  ILE A CG1 1 
ATOM   722  C  CG2 . ILE A 1 98  ? 24.568  2.331   -9.469  1.00 10.94 ?  100  ILE A CG2 1 
ATOM   723  C  CD1 . ILE A 1 98  ? 24.107  3.018   -12.497 1.00 14.08 ?  100  ILE A CD1 1 
ATOM   724  N  N   . LEU A 1 99  ? 27.514  1.663   -7.673  1.00 10.35 ?  101  LEU A N   1 
ATOM   725  C  CA  . LEU A 1 99  ? 27.831  0.865   -6.496  1.00 7.42  ?  101  LEU A CA  1 
ATOM   726  C  C   . LEU A 1 99  ? 26.726  1.052   -5.462  1.00 8.49  ?  101  LEU A C   1 
ATOM   727  O  O   . LEU A 1 99  ? 26.488  2.177   -5.024  1.00 8.80  ?  101  LEU A O   1 
ATOM   728  C  CB  . LEU A 1 99  ? 29.181  1.301   -5.928  1.00 8.07  ?  101  LEU A CB  1 
ATOM   729  C  CG  . LEU A 1 99  ? 29.702  0.573   -4.710  1.00 10.39 ?  101  LEU A CG  1 
ATOM   730  C  CD1 . LEU A 1 99  ? 29.686  -0.946  -4.909  1.00 12.75 ?  101  LEU A CD1 1 
ATOM   731  C  CD2 . LEU A 1 99  ? 31.114  1.080   -4.338  1.00 9.22  ?  101  LEU A CD2 1 
ATOM   732  N  N   . VAL A 1 100 ? 26.048  -0.036  -5.086  1.00 8.46  ?  102  VAL A N   1 
ATOM   733  C  CA  . VAL A 1 100 ? 24.956  0.045   -4.113  1.00 6.41  ?  102  VAL A CA  1 
ATOM   734  C  C   . VAL A 1 100 ? 25.561  0.114   -2.717  1.00 9.25  ?  102  VAL A C   1 
ATOM   735  O  O   . VAL A 1 100 ? 26.257  -0.806  -2.267  1.00 8.18  ?  102  VAL A O   1 
ATOM   736  C  CB  . VAL A 1 100 ? 23.974  -1.137  -4.246  1.00 9.58  ?  102  VAL A CB  1 
ATOM   737  C  CG1 . VAL A 1 100 ? 22.787  -0.973  -3.251  1.00 9.47  ?  102  VAL A CG1 1 
ATOM   738  C  CG2 . VAL A 1 100 ? 23.419  -1.218  -5.672  1.00 7.74  ?  102  VAL A CG2 1 
ATOM   739  N  N   . ALA A 1 101 ? 25.291  1.222   -2.031  1.00 7.81  ?  103  ALA A N   1 
ATOM   740  C  CA  . ALA A 1 101 ? 25.900  1.531   -0.747  1.00 9.34  ?  103  ALA A CA  1 
ATOM   741  C  C   . ALA A 1 101 ? 25.072  0.868   0.353   1.00 8.48  ?  103  ALA A C   1 
ATOM   742  O  O   . ALA A 1 101 ? 24.281  1.491   1.066   1.00 10.11 ?  103  ALA A O   1 
ATOM   743  C  CB  . ALA A 1 101 ? 26.007  3.039   -0.561  1.00 8.26  ?  103  ALA A CB  1 
ATOM   744  N  N   . THR A 1 102 ? 25.291  -0.435  0.499   1.00 8.32  ?  104  THR A N   1 
ATOM   745  C  CA  . THR A 1 102 ? 24.551  -1.246  1.454   1.00 8.97  ?  104  THR A CA  1 
ATOM   746  C  C   . THR A 1 102 ? 24.889  -0.974  2.916   1.00 8.98  ?  104  THR A C   1 
ATOM   747  O  O   . THR A 1 102 ? 24.121  -1.396  3.783   1.00 9.91  ?  104  THR A O   1 
ATOM   748  C  CB  . THR A 1 102 ? 24.819  -2.720  1.169   1.00 8.39  ?  104  THR A CB  1 
ATOM   749  O  OG1 . THR A 1 102 ? 26.240  -2.919  1.204   1.00 12.78 ?  104  THR A OG1 1 
ATOM   750  C  CG2 . THR A 1 102 ? 24.285  -3.117  -0.191  1.00 7.90  ?  104  THR A CG2 1 
ATOM   751  N  N   . GLY A 1 103 ? 26.005  -0.323  3.222   1.00 7.79  ?  105  GLY A N   1 
ATOM   752  C  CA  . GLY A 1 103 ? 26.482  -0.354  4.597   1.00 7.95  ?  105  GLY A CA  1 
ATOM   753  C  C   . GLY A 1 103 ? 26.783  -1.796  4.961   1.00 9.98  ?  105  GLY A C   1 
ATOM   754  O  O   . GLY A 1 103 ? 27.533  -2.492  4.267   1.00 10.48 ?  105  GLY A O   1 
ATOM   755  N  N   . LEU A 1 104 ? 26.188  -2.275  6.052   1.00 7.77  ?  106  LEU A N   1 
ATOM   756  C  CA  . LEU A 1 104 ? 26.297  -3.677  6.430   1.00 11.10 ?  106  LEU A CA  1 
ATOM   757  C  C   . LEU A 1 104 ? 25.047  -4.466  6.075   1.00 10.77 ?  106  LEU A C   1 
ATOM   758  O  O   . LEU A 1 104 ? 24.909  -5.623  6.486   1.00 10.55 ?  106  LEU A O   1 
ATOM   759  C  CB  . LEU A 1 104 ? 26.599  -3.802  7.925   1.00 13.75 ?  106  LEU A CB  1 
ATOM   760  C  CG  . LEU A 1 104 ? 28.077  -3.906  8.318   1.00 11.91 ?  106  LEU A CG  1 
ATOM   761  C  CD1 . LEU A 1 104 ? 28.657  -5.232  7.807   1.00 15.73 ?  106  LEU A CD1 1 
ATOM   762  C  CD2 . LEU A 1 104 ? 28.918  -2.749  7.785   1.00 12.96 ?  106  LEU A CD2 1 
ATOM   763  N  N   . HIS A 1 105 ? 24.129  -3.864  5.335   1.00 8.83  ?  107  HIS A N   1 
ATOM   764  C  CA  . HIS A 1 105 ? 22.975  -4.621  4.880   1.00 9.95  ?  107  HIS A CA  1 
ATOM   765  C  C   . HIS A 1 105 ? 23.380  -5.689  3.866   1.00 11.80 ?  107  HIS A C   1 
ATOM   766  O  O   . HIS A 1 105 ? 24.425  -5.607  3.212   1.00 10.36 ?  107  HIS A O   1 
ATOM   767  C  CB  . HIS A 1 105 ? 21.933  -3.727  4.207   1.00 6.29  ?  107  HIS A CB  1 
ATOM   768  C  CG  . HIS A 1 105 ? 21.454  -2.590  5.049   1.00 11.57 ?  107  HIS A CG  1 
ATOM   769  N  ND1 . HIS A 1 105 ? 20.772  -1.512  4.516   1.00 9.60  ?  107  HIS A ND1 1 
ATOM   770  C  CD2 . HIS A 1 105 ? 21.551  -2.356  6.378   1.00 9.20  ?  107  HIS A CD2 1 
ATOM   771  C  CE1 . HIS A 1 105 ? 20.488  -0.658  5.484   1.00 10.72 ?  107  HIS A CE1 1 
ATOM   772  N  NE2 . HIS A 1 105 ? 20.955  -1.142  6.620   1.00 10.99 ?  107  HIS A NE2 1 
ATOM   773  N  N   . ARG A 1 106 ? 22.488  -6.685  3.709   1.00 12.21 ?  108  ARG A N   1 
ATOM   774  C  CA  . ARG A 1 106 ? 22.564  -7.704  2.667   1.00 13.18 ?  108  ARG A CA  1 
ATOM   775  C  C   . ARG A 1 106 ? 22.649  -7.051  1.292   1.00 11.76 ?  108  ARG A C   1 
ATOM   776  O  O   . ARG A 1 106 ? 22.188  -5.914  1.114   1.00 12.56 ?  108  ARG A O   1 
ATOM   777  C  CB  . ARG A 1 106 ? 21.341  -8.621  2.732   1.00 13.59 ?  108  ARG A CB  1 
ATOM   778  C  CG  . ARG A 1 106 ? 20.029  -7.901  2.496   1.00 11.44 ?  108  ARG A CG  1 
ATOM   779  C  CD  . ARG A 1 106 ? 18.957  -8.872  2.072   1.00 10.12 ?  108  ARG A CD  1 
ATOM   780  N  NE  . ARG A 1 106 ? 17.655  -8.228  1.902   1.00 15.58 ?  108  ARG A NE  1 
ATOM   781  C  CZ  . ARG A 1 106 ? 17.256  -7.621  0.788   1.00 15.68 ?  108  ARG A CZ  1 
ATOM   782  N  NH1 . ARG A 1 106 ? 18.071  -7.526  -0.254  1.00 14.49 ?  108  ARG A NH1 1 
ATOM   783  N  NH2 . ARG A 1 106 ? 16.048  -7.078  0.723   1.00 16.12 ?  108  ARG A NH2 1 
ATOM   784  N  N   . PRO A 1 107 ? 23.203  -7.732  0.290   1.00 12.83 ?  109  PRO A N   1 
ATOM   785  C  CA  . PRO A 1 107 ? 23.243  -7.146  -1.048  1.00 12.14 ?  109  PRO A CA  1 
ATOM   786  C  C   . PRO A 1 107 ? 21.842  -7.029  -1.630  1.00 13.35 ?  109  PRO A C   1 
ATOM   787  O  O   . PRO A 1 107 ? 20.926  -7.765  -1.266  1.00 12.72 ?  109  PRO A O   1 
ATOM   788  C  CB  . PRO A 1 107 ? 24.087  -8.139  -1.848  1.00 12.38 ?  109  PRO A CB  1 
ATOM   789  C  CG  . PRO A 1 107 ? 23.885  -9.443  -1.134  1.00 15.27 ?  109  PRO A CG  1 
ATOM   790  C  CD  . PRO A 1 107 ? 23.761  -9.096  0.317   1.00 14.89 ?  109  PRO A CD  1 
ATOM   791  N  N   . SER A 1 108 ? 21.686  -6.088  -2.549  1.00 12.13 ?  110  SER A N   1 
ATOM   792  C  CA  . SER A 1 108 ? 20.433  -5.986  -3.280  1.00 11.28 ?  110  SER A CA  1 
ATOM   793  C  C   . SER A 1 108 ? 20.304  -7.147  -4.264  1.00 15.33 ?  110  SER A C   1 
ATOM   794  O  O   . SER A 1 108 ? 21.292  -7.642  -4.811  1.00 14.15 ?  110  SER A O   1 
ATOM   795  C  CB  . SER A 1 108 ? 20.369  -4.649  -4.016  1.00 15.67 ?  110  SER A CB  1 
ATOM   796  O  OG  . SER A 1 108 ? 21.388  -4.550  -4.999  1.00 13.49 ?  110  SER A OG  1 
ATOM   797  N  N   . THR A 1 109 ? 19.074  -7.586  -4.494  1.00 14.53 ?  111  THR A N   1 
ATOM   798  C  CA  . THR A 1 109 ? 18.820  -8.643  -5.465  1.00 18.71 ?  111  THR A CA  1 
ATOM   799  C  C   . THR A 1 109 ? 18.728  -8.067  -6.875  1.00 18.68 ?  111  THR A C   1 
ATOM   800  O  O   . THR A 1 109 ? 18.654  -6.850  -7.070  1.00 15.43 ?  111  THR A O   1 
ATOM   801  C  CB  . THR A 1 109 ? 17.539  -9.380  -5.091  1.00 19.44 ?  111  THR A CB  1 
ATOM   802  O  OG1 . THR A 1 109 ? 16.436  -8.495  -5.272  1.00 16.96 ?  111  THR A OG1 1 
ATOM   803  C  CG2 . THR A 1 109 ? 17.594  -9.867  -3.636  1.00 19.47 ?  111  THR A CG2 1 
ATOM   804  N  N   . PRO A 1 110 ? 18.742  -8.928  -7.906  1.00 20.20 ?  112  PRO A N   1 
ATOM   805  C  CA  . PRO A 1 110 ? 18.503  -8.421  -9.275  1.00 18.89 ?  112  PRO A CA  1 
ATOM   806  C  C   . PRO A 1 110 ? 17.193  -7.664  -9.425  1.00 18.20 ?  112  PRO A C   1 
ATOM   807  O  O   . PRO A 1 110 ? 17.155  -6.613  -10.085 1.00 17.12 ?  112  PRO A O   1 
ATOM   808  C  CB  . PRO A 1 110 ? 18.509  -9.699  -10.124 1.00 19.76 ?  112  PRO A CB  1 
ATOM   809  C  CG  . PRO A 1 110 ? 19.418  -10.633 -9.366  1.00 17.95 ?  112  PRO A CG  1 
ATOM   810  C  CD  . PRO A 1 110 ? 19.147  -10.348 -7.905  1.00 18.74 ?  112  PRO A CD  1 
ATOM   811  N  N   . ALA A 1 111 ? 16.107  -8.178  -8.841  1.00 15.58 ?  113  ALA A N   1 
ATOM   812  C  CA  . ALA A 1 111 ? 14.821  -7.504  -8.974  1.00 17.97 ?  113  ALA A CA  1 
ATOM   813  C  C   . ALA A 1 111 ? 14.824  -6.170  -8.240  1.00 16.66 ?  113  ALA A C   1 
ATOM   814  O  O   . ALA A 1 111 ? 14.184  -5.206  -8.679  1.00 16.37 ?  113  ALA A O   1 
ATOM   815  C  CB  . ALA A 1 111 ? 13.700  -8.397  -8.447  1.00 20.20 ?  113  ALA A CB  1 
ATOM   816  N  N   . GLU A 1 112 ? 15.544  -6.102  -7.118  1.00 13.69 ?  114  GLU A N   1 
ATOM   817  C  CA  . GLU A 1 112 ? 15.644  -4.859  -6.365  1.00 14.96 ?  114  GLU A CA  1 
ATOM   818  C  C   . GLU A 1 112 ? 16.416  -3.814  -7.156  1.00 12.76 ?  114  GLU A C   1 
ATOM   819  O  O   . GLU A 1 112 ? 16.042  -2.635  -7.159  1.00 13.70 ?  114  GLU A O   1 
ATOM   820  C  CB  . GLU A 1 112 ? 16.295  -5.169  -5.017  1.00 14.72 ?  114  GLU A CB  1 
ATOM   821  C  CG  . GLU A 1 112 ? 15.241  -5.491  -3.959  1.00 18.01 ?  114  GLU A CG  1 
ATOM   822  C  CD  . GLU A 1 112 ? 15.846  -5.941  -2.643  1.00 20.26 ?  114  GLU A CD  1 
ATOM   823  O  OE1 . GLU A 1 112 ? 15.066  -6.365  -1.750  1.00 17.36 ?  114  GLU A OE1 1 
ATOM   824  O  OE2 . GLU A 1 112 ? 17.098  -5.969  -2.544  1.00 19.52 ?  114  GLU A OE2 1 
ATOM   825  N  N   . LYS A 1 113 ? 17.470  -4.236  -7.871  1.00 11.91 ?  115  LYS A N   1 
ATOM   826  C  CA  . LYS A 1 113 ? 18.214  -3.299  -8.705  1.00 12.49 ?  115  LYS A CA  1 
ATOM   827  C  C   . LYS A 1 113 ? 17.322  -2.709  -9.784  1.00 15.56 ?  115  LYS A C   1 
ATOM   828  O  O   . LYS A 1 113 ? 17.456  -1.533  -10.141 1.00 14.81 ?  115  LYS A O   1 
ATOM   829  C  CB  . LYS A 1 113 ? 19.421  -3.994  -9.333  1.00 13.08 ?  115  LYS A CB  1 
ATOM   830  C  CG  . LYS A 1 113 ? 20.606  -4.114  -8.381  1.00 10.89 ?  115  LYS A CG  1 
ATOM   831  C  CD  . LYS A 1 113 ? 21.696  -5.014  -8.948  1.00 15.50 ?  115  LYS A CD  1 
ATOM   832  C  CE  . LYS A 1 113 ? 22.836  -5.194  -7.930  1.00 12.26 ?  115  LYS A CE  1 
ATOM   833  N  NZ  . LYS A 1 113 ? 22.478  -6.314  -7.013  1.00 12.84 ?  115  LYS A NZ  1 
ATOM   834  N  N   . VAL A 1 114 ? 16.399  -3.511  -10.314 1.00 13.75 ?  116  VAL A N   1 
ATOM   835  C  CA  . VAL A 1 114 ? 15.471  -2.984  -11.303 1.00 16.44 ?  116  VAL A CA  1 
ATOM   836  C  C   . VAL A 1 114 ? 14.501  -2.014  -10.649 1.00 13.98 ?  116  VAL A C   1 
ATOM   837  O  O   . VAL A 1 114 ? 14.213  -0.943  -11.200 1.00 16.81 ?  116  VAL A O   1 
ATOM   838  C  CB  . VAL A 1 114 ? 14.733  -4.126  -12.024 1.00 18.04 ?  116  VAL A CB  1 
ATOM   839  C  CG1 . VAL A 1 114 ? 13.595  -3.555  -12.850 1.00 19.58 ?  116  VAL A CG1 1 
ATOM   840  C  CG2 . VAL A 1 114 ? 15.701  -4.901  -12.901 1.00 16.23 ?  116  VAL A CG2 1 
ATOM   841  N  N   . GLU A 1 115 ? 13.996  -2.348  -9.452  1.00 14.49 ?  117  GLU A N   1 
ATOM   842  C  CA  . GLU A 1 115 ? 13.050  -1.437  -8.817  1.00 18.10 ?  117  GLU A CA  1 
ATOM   843  C  C   . GLU A 1 115 ? 13.742  -0.159  -8.343  1.00 18.57 ?  117  GLU A C   1 
ATOM   844  O  O   . GLU A 1 115 ? 13.146  0.918   -8.414  1.00 17.17 ?  117  GLU A O   1 
ATOM   845  C  CB  . GLU A 1 115 ? 12.301  -2.150  -7.680  1.00 20.30 ?  117  GLU A CB  1 
ATOM   846  C  CG  . GLU A 1 115 ? 11.690  -1.247  -6.582  1.00 26.30 ?  117  GLU A CG  1 
ATOM   847  C  CD  . GLU A 1 115 ? 11.235  -2.021  -5.334  1.00 33.69 ?  117  GLU A CD  1 
ATOM   848  O  OE1 . GLU A 1 115 ? 11.265  -3.270  -5.363  1.00 31.51 ?  117  GLU A OE1 1 
ATOM   849  O  OE2 . GLU A 1 115 ? 10.770  -1.390  -4.348  1.00 27.39 ?  117  GLU A OE2 1 
ATOM   850  N  N   . MET A 1 116 ? 15.010  -0.237  -7.922  1.00 15.44 ?  118  MET A N   1 
ATOM   851  C  CA  . MET A 1 116 ? 15.704  0.981   -7.497  1.00 15.92 ?  118  MET A CA  1 
ATOM   852  C  C   . MET A 1 116 ? 16.105  1.859   -8.673  1.00 16.13 ?  118  MET A C   1 
ATOM   853  O  O   . MET A 1 116 ? 16.032  3.094   -8.580  1.00 17.08 ?  118  MET A O   1 
ATOM   854  C  CB  . MET A 1 116 ? 16.968  0.689   -6.668  1.00 14.41 ?  118  MET A CB  1 
ATOM   855  C  CG  . MET A 1 116 ? 16.803  0.017   -5.311  1.00 20.42 ?  118  MET A CG  1 
ATOM   856  S  SD  . MET A 1 116 ? 18.167  -1.129  -4.926  1.00 22.58 ?  118  MET A SD  1 
ATOM   857  C  CE  . MET A 1 116 ? 19.632  -0.155  -5.316  1.00 21.72 ?  118  MET A CE  1 
ATOM   858  N  N   . LEU A 1 117 ? 16.579  1.257   -9.767  1.00 9.91  ?  119  LEU A N   1 
ATOM   859  C  CA  . LEU A 1 117 ? 17.297  2.009   -10.783 1.00 10.33 ?  119  LEU A CA  1 
ATOM   860  C  C   . LEU A 1 117 ? 16.569  2.129   -12.109 1.00 15.52 ?  119  LEU A C   1 
ATOM   861  O  O   . LEU A 1 117 ? 17.019  2.907   -12.959 1.00 16.56 ?  119  LEU A O   1 
ATOM   862  C  CB  . LEU A 1 117 ? 18.672  1.379   -11.055 1.00 15.06 ?  119  LEU A CB  1 
ATOM   863  C  CG  . LEU A 1 117 ? 19.569  1.199   -9.838  1.00 19.09 ?  119  LEU A CG  1 
ATOM   864  C  CD1 . LEU A 1 117 ? 20.771  0.340   -10.211 1.00 16.43 ?  119  LEU A CD1 1 
ATOM   865  C  CD2 . LEU A 1 117 ? 20.005  2.543   -9.301  1.00 21.64 ?  119  LEU A CD2 1 
ATOM   866  N  N   . SER A 1 118 ? 15.478  1.383   -12.297 1.00 16.80 ?  120  SER A N   1 
ATOM   867  C  CA  . SER A 1 118 ? 14.738  1.229   -13.554 1.00 18.17 ?  120  SER A CA  1 
ATOM   868  C  C   . SER A 1 118 ? 15.411  0.152   -14.393 1.00 18.81 ?  120  SER A C   1 
ATOM   869  O  O   . SER A 1 118 ? 16.619  -0.081  -14.266 1.00 16.54 ?  120  SER A O   1 
ATOM   870  C  CB  . SER A 1 118 ? 14.628  2.538   -14.346 1.00 23.88 ?  120  SER A CB  1 
ATOM   871  O  OG  . SER A 1 118 ? 15.829  2.810   -15.058 1.00 18.21 ?  120  SER A OG  1 
ATOM   872  N  N   . GLU A 1 119 ? 14.641  -0.524  -15.250 1.00 17.16 ?  121  GLU A N   1 
ATOM   873  C  CA  . GLU A 1 119 ? 15.219  -1.620  -16.021 1.00 21.78 ?  121  GLU A CA  1 
ATOM   874  C  C   . GLU A 1 119 ? 16.295  -1.120  -16.979 1.00 20.23 ?  121  GLU A C   1 
ATOM   875  O  O   . GLU A 1 119 ? 17.331  -1.778  -17.146 1.00 22.67 ?  121  GLU A O   1 
ATOM   876  C  CB  . GLU A 1 119 ? 14.124  -2.376  -16.780 1.00 26.51 ?  121  GLU A CB  1 
ATOM   877  C  CG  . GLU A 1 119 ? 14.606  -3.671  -17.403 1.00 33.61 ?  121  GLU A CG  1 
ATOM   878  C  CD  . GLU A 1 119 ? 13.463  -4.586  -17.794 1.00 53.93 ?  121  GLU A CD  1 
ATOM   879  O  OE1 . GLU A 1 119 ? 12.331  -4.364  -17.312 1.00 56.93 ?  121  GLU A OE1 1 
ATOM   880  O  OE2 . GLU A 1 119 ? 13.697  -5.535  -18.572 1.00 57.81 ?  121  GLU A OE2 1 
ATOM   881  N  N   . GLU A 1 120 ? 16.095  0.058   -17.578 1.00 18.94 ?  122  GLU A N   1 
ATOM   882  C  CA  . GLU A 1 120 ? 17.049  0.551   -18.567 1.00 16.58 ?  122  GLU A CA  1 
ATOM   883  C  C   . GLU A 1 120 ? 18.444  0.687   -17.967 1.00 19.31 ?  122  GLU A C   1 
ATOM   884  O  O   . GLU A 1 120 ? 19.424  0.206   -18.542 1.00 18.63 ?  122  GLU A O   1 
ATOM   885  C  CB  . GLU A 1 120 ? 16.578  1.887   -19.153 1.00 22.94 ?  122  GLU A CB  1 
ATOM   886  N  N   . ILE A 1 121 ? 18.542  1.303   -16.783 1.00 16.57 ?  123  ILE A N   1 
ATOM   887  C  CA  . ILE A 1 121 ? 19.848  1.526   -16.164 1.00 18.75 ?  123  ILE A CA  1 
ATOM   888  C  C   . ILE A 1 121 ? 20.434  0.214   -15.638 1.00 15.54 ?  123  ILE A C   1 
ATOM   889  O  O   . ILE A 1 121 ? 21.625  -0.069  -15.824 1.00 15.69 ?  123  ILE A O   1 
ATOM   890  C  CB  . ILE A 1 121 ? 19.718  2.596   -15.063 1.00 12.51 ?  123  ILE A CB  1 
ATOM   891  C  CG1 . ILE A 1 121 ? 19.392  3.953   -15.700 1.00 14.22 ?  123  ILE A CG1 1 
ATOM   892  C  CG2 . ILE A 1 121 ? 20.990  2.675   -14.235 1.00 14.56 ?  123  ILE A CG2 1 
ATOM   893  C  CD1 . ILE A 1 121 ? 19.103  5.089   -14.699 1.00 15.60 ?  123  ILE A CD1 1 
ATOM   894  N  N   . ALA A 1 122 ? 19.607  -0.621  -15.001 1.00 15.16 ?  124  ALA A N   1 
ATOM   895  C  CA  . ALA A 1 122 ? 20.094  -1.891  -14.459 1.00 15.32 ?  124  ALA A CA  1 
ATOM   896  C  C   . ALA A 1 122 ? 20.622  -2.822  -15.549 1.00 21.07 ?  124  ALA A C   1 
ATOM   897  O  O   . ALA A 1 122 ? 21.512  -3.637  -15.290 1.00 20.13 ?  124  ALA A O   1 
ATOM   898  C  CB  . ALA A 1 122 ? 18.981  -2.587  -13.670 1.00 16.99 ?  124  ALA A CB  1 
ATOM   899  N  N   . ARG A 1 123 ? 20.098  -2.724  -16.774 1.00 19.02 ?  125  ARG A N   1 
ATOM   900  C  CA  . ARG A 1 123 ? 20.559  -3.607  -17.840 1.00 20.96 ?  125  ARG A CA  1 
ATOM   901  C  C   . ARG A 1 123 ? 21.750  -3.050  -18.614 1.00 22.02 ?  125  ARG A C   1 
ATOM   902  O  O   . ARG A 1 123 ? 22.429  -3.815  -19.306 1.00 29.63 ?  125  ARG A O   1 
ATOM   903  C  CB  . ARG A 1 123 ? 19.408  -3.906  -18.819 1.00 29.51 ?  125  ARG A CB  1 
ATOM   904  N  N   . THR A 1 124 ? 22.031  -1.750  -18.511 1.00 18.16 ?  126  THR A N   1 
ATOM   905  C  CA  . THR A 1 124 ? 23.053  -1.092  -19.323 1.00 20.18 ?  126  THR A CA  1 
ATOM   906  C  C   . THR A 1 124 ? 24.375  -0.886  -18.590 1.00 21.25 ?  126  THR A C   1 
ATOM   907  O  O   . THR A 1 124 ? 25.451  -1.037  -19.186 1.00 18.01 ?  126  THR A O   1 
ATOM   908  C  CB  . THR A 1 124 ? 22.521  0.260   -19.814 1.00 23.54 ?  126  THR A CB  1 
ATOM   909  O  OG1 . THR A 1 124 ? 21.395  0.036   -20.665 1.00 26.98 ?  126  THR A OG1 1 
ATOM   910  C  CG2 . THR A 1 124 ? 23.573  1.022   -20.594 1.00 25.53 ?  126  THR A CG2 1 
ATOM   911  N  N   . TYR A 1 125 ? 24.325  -0.533  -17.313 1.00 16.28 ?  127  TYR A N   1 
ATOM   912  C  CA  . TYR A 1 125 ? 25.510  -0.183  -16.549 1.00 18.15 ?  127  TYR A CA  1 
ATOM   913  C  C   . TYR A 1 125 ? 25.886  -1.332  -15.628 1.00 16.98 ?  127  TYR A C   1 
ATOM   914  O  O   . TYR A 1 125 ? 25.039  -2.139  -15.246 1.00 17.93 ?  127  TYR A O   1 
ATOM   915  C  CB  . TYR A 1 125 ? 25.252  1.081   -15.722 1.00 17.29 ?  127  TYR A CB  1 
ATOM   916  C  CG  . TYR A 1 125 ? 25.090  2.295   -16.579 1.00 16.61 ?  127  TYR A CG  1 
ATOM   917  C  CD1 . TYR A 1 125 ? 26.181  3.084   -16.901 1.00 20.78 ?  127  TYR A CD1 1 
ATOM   918  C  CD2 . TYR A 1 125 ? 23.853  2.621   -17.130 1.00 16.91 ?  127  TYR A CD2 1 
ATOM   919  C  CE1 . TYR A 1 125 ? 26.040  4.185   -17.717 1.00 21.66 ?  127  TYR A CE1 1 
ATOM   920  C  CE2 . TYR A 1 125 ? 23.709  3.717   -17.944 1.00 22.92 ?  127  TYR A CE2 1 
ATOM   921  C  CZ  . TYR A 1 125 ? 24.807  4.496   -18.238 1.00 18.73 ?  127  TYR A CZ  1 
ATOM   922  O  OH  . TYR A 1 125 ? 24.664  5.596   -19.060 1.00 25.36 ?  127  TYR A OH  1 
ATOM   923  N  N   . ARG A 1 126 ? 27.167  -1.413  -15.285 1.00 16.37 ?  128  ARG A N   1 
ATOM   924  C  CA  . ARG A 1 126 ? 27.586  -2.332  -14.236 1.00 13.69 ?  128  ARG A CA  1 
ATOM   925  C  C   . ARG A 1 126 ? 27.055  -1.821  -12.902 1.00 13.79 ?  128  ARG A C   1 
ATOM   926  O  O   . ARG A 1 126 ? 27.295  -0.665  -12.534 1.00 13.57 ?  128  ARG A O   1 
ATOM   927  C  CB  . ARG A 1 126 ? 29.108  -2.455  -14.198 1.00 19.27 ?  128  ARG A CB  1 
ATOM   928  N  N   . VAL A 1 127 ? 26.306  -2.667  -12.206 1.00 14.82 ?  129  VAL A N   1 
ATOM   929  C  CA  . VAL A 1 127 ? 25.728  -2.357  -10.902 1.00 11.54 ?  129  VAL A CA  1 
ATOM   930  C  C   . VAL A 1 127 ? 26.171  -3.461  -9.960  1.00 12.42 ?  129  VAL A C   1 
ATOM   931  O  O   . VAL A 1 127 ? 25.816  -4.631  -10.169 1.00 14.79 ?  129  VAL A O   1 
ATOM   932  C  CB  . VAL A 1 127 ? 24.196  -2.269  -10.956 1.00 14.20 ?  129  VAL A CB  1 
ATOM   933  C  CG1 . VAL A 1 127 ? 23.637  -1.858  -9.600  1.00 13.78 ?  129  VAL A CG1 1 
ATOM   934  C  CG2 . VAL A 1 127 ? 23.775  -1.300  -12.027 1.00 13.52 ?  129  VAL A CG2 1 
ATOM   935  N  N   . GLU A 1 128 ? 26.978  -3.096  -8.953  1.00 11.85 ?  130  GLU A N   1 
ATOM   936  C  CA  . GLU A 1 128 ? 27.539  -4.014  -7.968  1.00 11.17 ?  130  GLU A CA  1 
ATOM   937  C  C   . GLU A 1 128 ? 27.196  -3.545  -6.555  1.00 11.19 ?  130  GLU A C   1 
ATOM   938  O  O   . GLU A 1 128 ? 26.829  -2.393  -6.329  1.00 12.61 ?  130  GLU A O   1 
ATOM   939  C  CB  . GLU A 1 128 ? 29.064  -4.153  -8.138  1.00 13.18 ?  130  GLU A CB  1 
ATOM   940  C  CG  . GLU A 1 128 ? 29.472  -4.226  -9.624  1.00 14.97 ?  130  GLU A CG  1 
ATOM   941  C  CD  . GLU A 1 128 ? 30.930  -4.642  -9.838  1.00 29.76 ?  130  GLU A CD  1 
ATOM   942  O  OE1 . GLU A 1 128 ? 31.789  -4.222  -9.035  1.00 28.90 ?  130  GLU A OE1 1 
ATOM   943  O  OE2 . GLU A 1 128 ? 31.222  -5.365  -10.822 1.00 30.13 ?  130  GLU A OE2 1 
ATOM   944  N  N   . ASP A 1 129 ? 27.322  -4.463  -5.606  1.00 13.18 ?  131  ASP A N   1 
ATOM   945  C  CA  . ASP A 1 129 ? 26.907  -4.250  -4.227  1.00 9.96  ?  131  ASP A CA  1 
ATOM   946  C  C   . ASP A 1 129 ? 28.138  -4.100  -3.355  1.00 12.12 ?  131  ASP A C   1 
ATOM   947  O  O   . ASP A 1 129 ? 29.151  -4.762  -3.583  1.00 11.19 ?  131  ASP A O   1 
ATOM   948  C  CB  . ASP A 1 129 ? 26.107  -5.446  -3.715  1.00 10.66 ?  131  ASP A CB  1 
ATOM   949  C  CG  . ASP A 1 129 ? 24.704  -5.509  -4.316  1.00 14.38 ?  131  ASP A CG  1 
ATOM   950  O  OD1 . ASP A 1 129 ? 23.809  -4.704  -3.953  1.00 15.63 ?  131  ASP A OD1 1 
ATOM   951  O  OD2 . ASP A 1 129 ? 24.545  -6.349  -5.235  1.00 14.68 ?  131  ASP A OD2 1 
ATOM   952  N  N   . HIS A 1 130 ? 28.030  -3.265  -2.334  1.00 8.42  ?  132  HIS A N   1 
ATOM   953  C  CA  . HIS A 1 130 ? 29.030  -3.239  -1.272  1.00 8.35  ?  132  HIS A CA  1 
ATOM   954  C  C   . HIS A 1 130 ? 28.846  -4.425  -0.318  1.00 8.82  ?  132  HIS A C   1 
ATOM   955  O  O   . HIS A 1 130 ? 27.717  -4.817  0.001   1.00 10.64 ?  132  HIS A O   1 
ATOM   956  C  CB  . HIS A 1 130 ? 28.910  -1.916  -0.518  1.00 8.66  ?  132  HIS A CB  1 
ATOM   957  C  CG  . HIS A 1 130 ? 29.754  -1.837  0.713   1.00 7.25  ?  132  HIS A CG  1 
ATOM   958  N  ND1 . HIS A 1 130 ? 29.216  -1.880  1.980   1.00 8.15  ?  132  HIS A ND1 1 
ATOM   959  C  CD2 . HIS A 1 130 ? 31.087  -1.703  0.872   1.00 8.94  ?  132  HIS A CD2 1 
ATOM   960  C  CE1 . HIS A 1 130 ? 30.191  -1.788  2.871   1.00 7.45  ?  132  HIS A CE1 1 
ATOM   961  N  NE2 . HIS A 1 130 ? 31.335  -1.666  2.223   1.00 9.68  ?  132  HIS A NE2 1 
ATOM   962  N  N   . TYR A 1 131 ? 29.966  -5.003  0.136   1.00 9.42  ?  133  TYR A N   1 
ATOM   963  C  CA  . TYR A 1 131 ? 29.968  -6.116  1.099   1.00 9.03  ?  133  TYR A CA  1 
ATOM   964  C  C   . TYR A 1 131 ? 30.816  -5.717  2.302   1.00 14.30 ?  133  TYR A C   1 
ATOM   965  O  O   . TYR A 1 131 ? 32.042  -5.867  2.280   1.00 12.22 ?  133  TYR A O   1 
ATOM   966  C  CB  . TYR A 1 131 ? 30.498  -7.400  0.466   1.00 12.58 ?  133  TYR A CB  1 
ATOM   967  C  CG  . TYR A 1 131 ? 29.541  -8.056  -0.521  1.00 13.18 ?  133  TYR A CG  1 
ATOM   968  C  CD1 . TYR A 1 131 ? 29.567  -7.730  -1.868  1.00 13.25 ?  133  TYR A CD1 1 
ATOM   969  C  CD2 . TYR A 1 131 ? 28.645  -9.028  -0.100  1.00 13.98 ?  133  TYR A CD2 1 
ATOM   970  C  CE1 . TYR A 1 131 ? 28.694  -8.330  -2.770  1.00 19.57 ?  133  TYR A CE1 1 
ATOM   971  C  CE2 . TYR A 1 131 ? 27.775  -9.642  -0.992  1.00 16.92 ?  133  TYR A CE2 1 
ATOM   972  C  CZ  . TYR A 1 131 ? 27.805  -9.290  -2.325  1.00 18.88 ?  133  TYR A CZ  1 
ATOM   973  O  OH  . TYR A 1 131 ? 26.941  -9.906  -3.217  1.00 19.01 ?  133  TYR A OH  1 
ATOM   974  N  N   . GLY A 1 132 ? 30.161  -5.236  3.360   1.00 10.33 ?  134  GLY A N   1 
ATOM   975  C  CA  . GLY A 1 132 ? 30.900  -4.671  4.474   1.00 9.81  ?  134  GLY A CA  1 
ATOM   976  C  C   . GLY A 1 132 ? 31.706  -5.669  5.272   1.00 13.30 ?  134  GLY A C   1 
ATOM   977  O  O   . GLY A 1 132 ? 32.661  -5.275  5.949   1.00 12.10 ?  134  GLY A O   1 
ATOM   978  N  N   . THR A 1 133 ? 31.363  -6.953  5.208   1.00 12.50 ?  135  THR A N   1 
ATOM   979  C  CA  . THR A 1 133 ? 32.158  -7.926  5.947   1.00 13.98 ?  135  THR A CA  1 
ATOM   980  C  C   . THR A 1 133 ? 33.338  -8.465  5.146   1.00 18.39 ?  135  THR A C   1 
ATOM   981  O  O   . THR A 1 133 ? 34.062  -9.333  5.646   1.00 20.29 ?  135  THR A O   1 
ATOM   982  C  CB  . THR A 1 133 ? 31.282  -9.085  6.438   1.00 17.13 ?  135  THR A CB  1 
ATOM   983  O  OG1 . THR A 1 133 ? 30.832  -9.879  5.330   1.00 18.95 ?  135  THR A OG1 1 
ATOM   984  C  CG2 . THR A 1 133 ? 30.075  -8.545  7.196   1.00 20.25 ?  135  THR A CG2 1 
ATOM   985  N  N   . ARG A 1 134 ? 33.574  -7.954  3.941   1.00 17.57 ?  136  ARG A N   1 
ATOM   986  C  CA  . ARG A 1 134 ? 34.699  -8.377  3.104   1.00 15.20 ?  136  ARG A CA  1 
ATOM   987  C  C   . ARG A 1 134 ? 35.776  -7.288  3.159   1.00 14.07 ?  136  ARG A C   1 
ATOM   988  O  O   . ARG A 1 134 ? 35.802  -6.380  2.329   1.00 12.87 ?  136  ARG A O   1 
ATOM   989  C  CB  . ARG A 1 134 ? 34.243  -8.626  1.666   1.00 15.92 ?  136  ARG A CB  1 
ATOM   990  C  CG  . ARG A 1 134 ? 33.384  -9.874  1.487   1.00 21.10 ?  136  ARG A CG  1 
ATOM   991  C  CD  . ARG A 1 134 ? 33.102  -10.098 0.009   1.00 21.71 ?  136  ARG A CD  1 
ATOM   992  N  NE  . ARG A 1 134 ? 32.021  -11.053 -0.218  1.00 36.48 ?  136  ARG A NE  1 
ATOM   993  C  CZ  . ARG A 1 134 ? 31.462  -11.271 -1.405  1.00 35.35 ?  136  ARG A CZ  1 
ATOM   994  N  NH1 . ARG A 1 134 ? 31.888  -10.604 -2.472  1.00 33.45 ?  136  ARG A NH1 1 
ATOM   995  N  NH2 . ARG A 1 134 ? 30.476  -12.149 -1.529  1.00 31.79 ?  136  ARG A NH2 1 
ATOM   996  N  N   . LEU A 1 135 ? 36.685  -7.393  4.134   1.00 13.02 ?  137  LEU A N   1 
ATOM   997  C  CA  . LEU A 1 135 ? 37.686  -6.341  4.291   1.00 10.81 ?  137  LEU A CA  1 
ATOM   998  C  C   . LEU A 1 135 ? 38.603  -6.251  3.074   1.00 15.73 ?  137  LEU A C   1 
ATOM   999  O  O   . LEU A 1 135 ? 39.092  -5.167  2.731   1.00 13.80 ?  137  LEU A O   1 
ATOM   1000 C  CB  . LEU A 1 135 ? 38.507  -6.576  5.569   1.00 13.47 ?  137  LEU A CB  1 
ATOM   1001 C  CG  . LEU A 1 135 ? 39.430  -5.410  5.929   1.00 17.53 ?  137  LEU A CG  1 
ATOM   1002 C  CD1 . LEU A 1 135 ? 38.610  -4.211  6.387   1.00 12.59 ?  137  LEU A CD1 1 
ATOM   1003 C  CD2 . LEU A 1 135 ? 40.444  -5.809  7.022   1.00 12.88 ?  137  LEU A CD2 1 
ATOM   1004 N  N   . GLU A 1 136 ? 38.814  -7.368  2.384   1.00 16.57 ?  138  GLU A N   1 
ATOM   1005 C  CA  . GLU A 1 136 ? 39.696  -7.363  1.224   1.00 17.71 ?  138  GLU A CA  1 
ATOM   1006 C  C   . GLU A 1 136 ? 39.182  -6.478  0.093   1.00 18.11 ?  138  GLU A C   1 
ATOM   1007 O  O   . GLU A 1 136 ? 39.973  -6.080  -0.767  1.00 14.72 ?  138  GLU A O   1 
ATOM   1008 C  CB  . GLU A 1 136 ? 39.907  -8.800  0.754   1.00 21.35 ?  138  GLU A CB  1 
ATOM   1009 C  CG  . GLU A 1 136 ? 38.745  -9.424  0.018   1.00 16.01 ?  138  GLU A CG  1 
ATOM   1010 C  CD  . GLU A 1 136 ? 37.752  -10.096 0.957   1.00 29.18 ?  138  GLU A CD  1 
ATOM   1011 O  OE1 . GLU A 1 136 ? 36.714  -10.588 0.461   1.00 27.14 ?  138  GLU A OE1 1 
ATOM   1012 O  OE2 . GLU A 1 136 ? 37.973  -10.088 2.196   1.00 27.95 ?  138  GLU A OE2 1 
ATOM   1013 N  N   . GLU A 1 137 ? 37.891  -6.141  0.077   1.00 15.38 ?  139  GLU A N   1 
ATOM   1014 C  CA  . GLU A 1 137 ? 37.357  -5.225  -0.922  1.00 14.01 ?  139  GLU A CA  1 
ATOM   1015 C  C   . GLU A 1 137 ? 37.462  -3.755  -0.502  1.00 13.36 ?  139  GLU A C   1 
ATOM   1016 O  O   . GLU A 1 137 ? 36.922  -2.888  -1.192  1.00 13.48 ?  139  GLU A O   1 
ATOM   1017 C  CB  . GLU A 1 137 ? 35.902  -5.598  -1.252  1.00 17.15 ?  139  GLU A CB  1 
ATOM   1018 C  CG  . GLU A 1 137 ? 35.716  -7.084  -1.583  1.00 19.34 ?  139  GLU A CG  1 
ATOM   1019 C  CD  . GLU A 1 137 ? 34.369  -7.428  -2.228  1.00 22.48 ?  139  GLU A CD  1 
ATOM   1020 O  OE1 . GLU A 1 137 ? 34.283  -8.513  -2.842  1.00 24.08 ?  139  GLU A OE1 1 
ATOM   1021 O  OE2 . GLU A 1 137 ? 33.404  -6.627  -2.126  1.00 19.57 ?  139  GLU A OE2 1 
ATOM   1022 N  N   . HIS A 1 138 ? 38.185  -3.439  0.577   1.00 10.67 ?  140  HIS A N   1 
ATOM   1023 C  CA  . HIS A 1 138 ? 38.253  -2.077  1.079   1.00 10.62 ?  140  HIS A CA  1 
ATOM   1024 C  C   . HIS A 1 138 ? 39.698  -1.605  1.130   1.00 14.91 ?  140  HIS A C   1 
ATOM   1025 O  O   . HIS A 1 138 ? 40.624  -2.409  1.243   1.00 16.33 ?  140  HIS A O   1 
ATOM   1026 C  CB  . HIS A 1 138 ? 37.624  -1.957  2.486   1.00 10.30 ?  140  HIS A CB  1 
ATOM   1027 C  CG  . HIS A 1 138 ? 36.166  -2.281  2.510   1.00 11.50 ?  140  HIS A CG  1 
ATOM   1028 N  ND1 . HIS A 1 138 ? 35.692  -3.575  2.413   1.00 11.70 ?  140  HIS A ND1 1 
ATOM   1029 C  CD2 . HIS A 1 138 ? 35.074  -1.484  2.615   1.00 11.10 ?  140  HIS A CD2 1 
ATOM   1030 C  CE1 . HIS A 1 138 ? 34.368  -3.559  2.432   1.00 12.31 ?  140  HIS A CE1 1 
ATOM   1031 N  NE2 . HIS A 1 138 ? 33.970  -2.305  2.566   1.00 11.19 ?  140  HIS A NE2 1 
ATOM   1032 N  N   . THR A 1 139 ? 39.866  -0.285  1.071   1.00 12.41 ?  141  THR A N   1 
ATOM   1033 C  CA  . THR A 1 139 ? 41.166  0.378   1.201   1.00 10.52 ?  141  THR A CA  1 
ATOM   1034 C  C   . THR A 1 139 ? 41.243  1.166   2.508   1.00 9.75  ?  141  THR A C   1 
ATOM   1035 O  O   . THR A 1 139 ? 40.311  1.892   2.859   1.00 10.65 ?  141  THR A O   1 
ATOM   1036 C  CB  . THR A 1 139 ? 41.404  1.314   0.013   1.00 15.25 ?  141  THR A CB  1 
ATOM   1037 O  OG1 . THR A 1 139 ? 41.414  0.551   -1.195  1.00 16.96 ?  141  THR A OG1 1 
ATOM   1038 C  CG2 . THR A 1 139 ? 42.734  2.067   0.150   1.00 15.39 ?  141  THR A CG2 1 
ATOM   1039 N  N   . TYR A 1 140 ? 42.375  1.059   3.212   1.00 10.92 ?  142  TYR A N   1 
ATOM   1040 C  CA  . TYR A 1 140 ? 42.573  1.823   4.439   1.00 9.66  ?  142  TYR A CA  1 
ATOM   1041 C  C   . TYR A 1 140 ? 43.018  3.247   4.105   1.00 12.08 ?  142  TYR A C   1 
ATOM   1042 O  O   . TYR A 1 140 ? 43.946  3.445   3.310   1.00 13.52 ?  142  TYR A O   1 
ATOM   1043 C  CB  . TYR A 1 140 ? 43.620  1.142   5.316   1.00 13.24 ?  142  TYR A CB  1 
ATOM   1044 C  CG  . TYR A 1 140 ? 44.018  1.930   6.540   1.00 11.62 ?  142  TYR A CG  1 
ATOM   1045 C  CD1 . TYR A 1 140 ? 43.169  2.026   7.637   1.00 12.91 ?  142  TYR A CD1 1 
ATOM   1046 C  CD2 . TYR A 1 140 ? 45.260  2.562   6.613   1.00 14.04 ?  142  TYR A CD2 1 
ATOM   1047 C  CE1 . TYR A 1 140 ? 43.542  2.730   8.771   1.00 14.63 ?  142  TYR A CE1 1 
ATOM   1048 C  CE2 . TYR A 1 140 ? 45.637  3.261   7.741   1.00 14.23 ?  142  TYR A CE2 1 
ATOM   1049 C  CZ  . TYR A 1 140 ? 44.776  3.346   8.819   1.00 16.26 ?  142  TYR A CZ  1 
ATOM   1050 O  OH  . TYR A 1 140 ? 45.147  4.045   9.952   1.00 15.05 ?  142  TYR A OH  1 
ATOM   1051 N  N   . LEU A 1 141 ? 42.353  4.242   4.703   1.00 8.50  ?  143  LEU A N   1 
ATOM   1052 C  CA  . LEU A 1 141 ? 42.625  5.646   4.408   1.00 10.44 ?  143  LEU A CA  1 
ATOM   1053 C  C   . LEU A 1 141 ? 43.211  6.412   5.586   1.00 15.45 ?  143  LEU A C   1 
ATOM   1054 O  O   . LEU A 1 141 ? 43.518  7.601   5.440   1.00 17.87 ?  143  LEU A O   1 
ATOM   1055 C  CB  . LEU A 1 141 ? 41.347  6.356   3.941   1.00 13.78 ?  143  LEU A CB  1 
ATOM   1056 C  CG  . LEU A 1 141 ? 40.686  5.689   2.733   1.00 15.58 ?  143  LEU A CG  1 
ATOM   1057 C  CD1 . LEU A 1 141 ? 39.325  6.347   2.405   1.00 16.57 ?  143  LEU A CD1 1 
ATOM   1058 C  CD2 . LEU A 1 141 ? 41.613  5.776   1.537   1.00 15.05 ?  143  LEU A CD2 1 
ATOM   1059 N  N   . GLY A 1 142 ? 43.381  5.780   6.740   1.00 13.26 ?  144  GLY A N   1 
ATOM   1060 C  CA  . GLY A 1 142 ? 43.822  6.469   7.936   1.00 14.05 ?  144  GLY A CA  1 
ATOM   1061 C  C   . GLY A 1 142 ? 42.892  6.196   9.101   1.00 17.79 ?  144  GLY A C   1 
ATOM   1062 O  O   . GLY A 1 142 ? 41.848  5.560   8.969   1.00 14.30 ?  144  GLY A O   1 
ATOM   1063 N  N   . THR A 1 143 ? 43.315  6.677   10.269  1.00 13.69 ?  145  THR A N   1 
ATOM   1064 C  CA  . THR A 1 143 ? 42.533  6.531   11.490  1.00 13.24 ?  145  THR A CA  1 
ATOM   1065 C  C   . THR A 1 143 ? 42.197  7.911   12.045  1.00 18.25 ?  145  THR A C   1 
ATOM   1066 O  O   . THR A 1 143 ? 43.054  8.801   12.078  1.00 19.83 ?  145  THR A O   1 
ATOM   1067 C  CB  . THR A 1 143 ? 43.298  5.686   12.522  1.00 16.29 ?  145  THR A CB  1 
ATOM   1068 O  OG1 . THR A 1 143 ? 43.396  4.343   12.044  1.00 17.05 ?  145  THR A OG1 1 
ATOM   1069 C  CG2 . THR A 1 143 ? 42.591  5.672   13.867  1.00 16.83 ?  145  THR A CG2 1 
ATOM   1070 N  N   . THR A 1 144 ? 40.935  8.099   12.464  1.00 13.65 ?  146  THR A N   1 
ATOM   1071 C  CA  . THR A 1 144 ? 40.509  9.388   12.988  1.00 13.05 ?  146  THR A CA  1 
ATOM   1072 C  C   . THR A 1 144 ? 41.089  9.624   14.380  1.00 14.89 ?  146  THR A C   1 
ATOM   1073 O  O   . THR A 1 144 ? 41.538  8.689   15.044  1.00 17.33 ?  146  THR A O   1 
ATOM   1074 C  CB  . THR A 1 144 ? 38.988  9.469   13.067  1.00 14.19 ?  146  THR A CB  1 
ATOM   1075 O  OG1 . THR A 1 144 ? 38.522  8.606   14.112  1.00 11.29 ?  146  THR A OG1 1 
ATOM   1076 C  CG2 . THR A 1 144 ? 38.340  9.096   11.721  1.00 13.01 ?  146  THR A CG2 1 
ATOM   1077 N  N   . PRO A 1 145 ? 41.064  10.873  14.854  1.00 17.26 ?  147  PRO A N   1 
ATOM   1078 C  CA  . PRO A 1 145 ? 41.507  11.137  16.232  1.00 19.33 ?  147  PRO A CA  1 
ATOM   1079 C  C   . PRO A 1 145 ? 40.745  10.357  17.284  1.00 21.35 ?  147  PRO A C   1 
ATOM   1080 O  O   . PRO A 1 145 ? 41.314  10.066  18.344  1.00 20.88 ?  147  PRO A O   1 
ATOM   1081 C  CB  . PRO A 1 145 ? 41.285  12.649  16.365  1.00 19.53 ?  147  PRO A CB  1 
ATOM   1082 C  CG  . PRO A 1 145 ? 41.556  13.146  14.978  1.00 19.38 ?  147  PRO A CG  1 
ATOM   1083 C  CD  . PRO A 1 145 ? 40.845  12.130  14.115  1.00 20.05 ?  147  PRO A CD  1 
ATOM   1084 N  N   . ASN A 1 146 ? 39.483  9.994   17.031  1.00 16.27 ?  148  ASN A N   1 
ATOM   1085 C  CA  . ASN A 1 146 ? 38.735  9.140   17.948  1.00 16.99 ?  148  ASN A CA  1 
ATOM   1086 C  C   . ASN A 1 146 ? 39.138  7.674   17.868  1.00 17.94 ?  148  ASN A C   1 
ATOM   1087 O  O   . ASN A 1 146 ? 38.578  6.857   18.611  1.00 21.80 ?  148  ASN A O   1 
ATOM   1088 C  CB  . ASN A 1 146 ? 37.223  9.237   17.691  1.00 18.22 ?  148  ASN A CB  1 
ATOM   1089 C  CG  . ASN A 1 146 ? 36.605  10.483  18.281  1.00 25.14 ?  148  ASN A CG  1 
ATOM   1090 O  OD1 . ASN A 1 146 ? 37.027  10.961  19.331  1.00 29.79 ?  148  ASN A OD1 1 
ATOM   1091 N  ND2 . ASN A 1 146 ? 35.558  10.984  17.636  1.00 24.47 ?  148  ASN A ND2 1 
ATOM   1092 N  N   . GLY A 1 147 ? 40.078  7.316   16.999  1.00 15.52 ?  149  GLY A N   1 
ATOM   1093 C  CA  . GLY A 1 147 ? 40.533  5.944   16.898  1.00 15.04 ?  149  GLY A CA  1 
ATOM   1094 C  C   . GLY A 1 147 ? 39.745  5.053   15.961  1.00 16.51 ?  149  GLY A C   1 
ATOM   1095 O  O   . GLY A 1 147 ? 39.865  3.828   16.048  1.00 14.93 ?  149  GLY A O   1 
ATOM   1096 N  N   . VAL A 1 148 ? 38.944  5.609   15.059  1.00 14.49 ?  150  VAL A N   1 
ATOM   1097 C  CA  . VAL A 1 148 ? 38.154  4.811   14.125  1.00 11.54 ?  150  VAL A CA  1 
ATOM   1098 C  C   . VAL A 1 148 ? 38.953  4.661   12.832  1.00 11.10 ?  150  VAL A C   1 
ATOM   1099 O  O   . VAL A 1 148 ? 39.279  5.677   12.201  1.00 13.61 ?  150  VAL A O   1 
ATOM   1100 C  CB  . VAL A 1 148 ? 36.787  5.442   13.850  1.00 11.43 ?  150  VAL A CB  1 
ATOM   1101 C  CG1 . VAL A 1 148 ? 36.002  4.558   12.869  1.00 12.98 ?  150  VAL A CG1 1 
ATOM   1102 C  CG2 . VAL A 1 148 ? 36.023  5.613   15.144  1.00 13.90 ?  150  VAL A CG2 1 
ATOM   1103 N  N   . PRO A 1 149 ? 39.307  3.449   12.425  1.00 13.04 ?  151  PRO A N   1 
ATOM   1104 C  CA  . PRO A 1 149 ? 40.021  3.284   11.156  1.00 14.16 ?  151  PRO A CA  1 
ATOM   1105 C  C   . PRO A 1 149 ? 39.039  3.420   10.005  1.00 12.64 ?  151  PRO A C   1 
ATOM   1106 O  O   . PRO A 1 149 ? 37.909  2.942   10.087  1.00 14.87 ?  151  PRO A O   1 
ATOM   1107 C  CB  . PRO A 1 149 ? 40.588  1.862   11.255  1.00 13.95 ?  151  PRO A CB  1 
ATOM   1108 C  CG  . PRO A 1 149 ? 39.544  1.129   12.099  1.00 14.80 ?  151  PRO A CG  1 
ATOM   1109 C  CD  . PRO A 1 149 ? 39.023  2.163   13.086  1.00 15.26 ?  151  PRO A CD  1 
ATOM   1110 N  N   . ALA A 1 150 ? 39.468  4.087   8.935   1.00 10.30 ?  152  ALA A N   1 
ATOM   1111 C  CA  . ALA A 1 150 ? 38.612  4.351   7.777   1.00 9.63  ?  152  ALA A CA  1 
ATOM   1112 C  C   . ALA A 1 150 ? 38.927  3.344   6.670   1.00 15.64 ?  152  ALA A C   1 
ATOM   1113 O  O   . ALA A 1 150 ? 39.966  3.443   6.005   1.00 17.03 ?  152  ALA A O   1 
ATOM   1114 C  CB  . ALA A 1 150 ? 38.806  5.784   7.289   1.00 13.44 ?  152  ALA A CB  1 
ATOM   1115 N  N   . TRP A 1 151 ? 38.017  2.391   6.463   1.00 10.10 ?  153  TRP A N   1 
ATOM   1116 C  CA  . TRP A 1 151 ? 38.120  1.363   5.428   1.00 7.56  ?  153  TRP A CA  1 
ATOM   1117 C  C   . TRP A 1 151 ? 36.961  1.546   4.446   1.00 8.45  ?  153  TRP A C   1 
ATOM   1118 O  O   . TRP A 1 151 ? 35.809  1.283   4.796   1.00 9.05  ?  153  TRP A O   1 
ATOM   1119 C  CB  . TRP A 1 151 ? 38.061  -0.036  6.046   1.00 8.18  ?  153  TRP A CB  1 
ATOM   1120 C  CG  . TRP A 1 151 ? 39.254  -0.448  6.902   1.00 10.72 ?  153  TRP A CG  1 
ATOM   1121 C  CD1 . TRP A 1 151 ? 39.385  -0.293  8.251   1.00 10.12 ?  153  TRP A CD1 1 
ATOM   1122 C  CD2 . TRP A 1 151 ? 40.436  -1.136  6.461   1.00 10.06 ?  153  TRP A CD2 1 
ATOM   1123 N  NE1 . TRP A 1 151 ? 40.580  -0.831  8.677   1.00 12.51 ?  153  TRP A NE1 1 
ATOM   1124 C  CE2 . TRP A 1 151 ? 41.249  -1.343  7.600   1.00 14.97 ?  153  TRP A CE2 1 
ATOM   1125 C  CE3 . TRP A 1 151 ? 40.897  -1.578  5.213   1.00 11.82 ?  153  TRP A CE3 1 
ATOM   1126 C  CZ2 . TRP A 1 151 ? 42.499  -1.979  7.531   1.00 17.00 ?  153  TRP A CZ2 1 
ATOM   1127 C  CZ3 . TRP A 1 151 ? 42.145  -2.213  5.147   1.00 17.36 ?  153  TRP A CZ3 1 
ATOM   1128 C  CH2 . TRP A 1 151 ? 42.922  -2.406  6.299   1.00 18.10 ?  153  TRP A CH2 1 
ATOM   1129 N  N   . ILE A 1 152 ? 37.266  1.925   3.208   1.00 8.51  ?  154  ILE A N   1 
ATOM   1130 C  CA  . ILE A 1 152 ? 36.263  2.343   2.235   1.00 8.26  ?  154  ILE A CA  1 
ATOM   1131 C  C   . ILE A 1 152 ? 36.427  1.512   0.961   1.00 11.18 ?  154  ILE A C   1 
ATOM   1132 O  O   . ILE A 1 152 ? 37.552  1.205   0.553   1.00 10.32 ?  154  ILE A O   1 
ATOM   1133 C  CB  . ILE A 1 152 ? 36.386  3.859   1.953   1.00 8.97  ?  154  ILE A CB  1 
ATOM   1134 C  CG1 . ILE A 1 152 ? 36.196  4.666   3.243   1.00 11.59 ?  154  ILE A CG1 1 
ATOM   1135 C  CG2 . ILE A 1 152 ? 35.367  4.297   0.872   1.00 8.43  ?  154  ILE A CG2 1 
ATOM   1136 C  CD1 . ILE A 1 152 ? 34.871  4.381   3.958   1.00 10.40 ?  154  ILE A CD1 1 
ATOM   1137 N  N   . ASP A 1 153 ? 35.303  1.153   0.327   1.00 8.01  ?  155  ASP A N   1 
ATOM   1138 C  CA  . ASP A 1 153 ? 35.326  0.262   -0.836  1.00 9.33  ?  155  ASP A CA  1 
ATOM   1139 C  C   . ASP A 1 153 ? 36.322  0.716   -1.890  1.00 10.95 ?  155  ASP A C   1 
ATOM   1140 O  O   . ASP A 1 153 ? 36.305  1.872   -2.326  1.00 8.01  ?  155  ASP A O   1 
ATOM   1141 C  CB  . ASP A 1 153 ? 33.925  0.185   -1.457  1.00 7.05  ?  155  ASP A CB  1 
ATOM   1142 C  CG  . ASP A 1 153 ? 33.757  -1.002  -2.410  1.00 12.95 ?  155  ASP A CG  1 
ATOM   1143 O  OD1 . ASP A 1 153 ? 34.364  -0.990  -3.509  1.00 12.04 ?  155  ASP A OD1 1 
ATOM   1144 O  OD2 . ASP A 1 153 ? 33.004  -1.952  -2.077  1.00 15.05 ?  155  ASP A OD2 1 
ATOM   1145 N  N   . SER A 1 154 ? 37.166  -0.221  -2.330  1.00 9.95  ?  156  SER A N   1 
ATOM   1146 C  CA  . SER A 1 154 ? 38.270  0.130   -3.216  1.00 11.77 ?  156  SER A CA  1 
ATOM   1147 C  C   . SER A 1 154 ? 37.806  0.587   -4.587  1.00 9.60  ?  156  SER A C   1 
ATOM   1148 O  O   . SER A 1 154 ? 38.504  1.375   -5.237  1.00 13.14 ?  156  SER A O   1 
ATOM   1149 C  CB  . SER A 1 154 ? 39.230  -1.047  -3.341  1.00 13.10 ?  156  SER A CB  1 
ATOM   1150 O  OG  . SER A 1 154 ? 39.760  -1.370  -2.059  1.00 12.61 ?  156  SER A OG  1 
ATOM   1151 N  N   . ARG A 1 155 ? 36.643  0.123   -5.042  1.00 9.38  ?  157  ARG A N   1 
ATOM   1152 C  CA  . ARG A 1 155 ? 36.135  0.558   -6.342  1.00 12.47 ?  157  ARG A CA  1 
ATOM   1153 C  C   . ARG A 1 155 ? 35.822  2.052   -6.350  1.00 12.69 ?  157  ARG A C   1 
ATOM   1154 O  O   . ARG A 1 155 ? 35.992  2.729   -7.370  1.00 13.71 ?  157  ARG A O   1 
ATOM   1155 C  CB  . ARG A 1 155 ? 34.891  -0.254  -6.706  1.00 12.01 ?  157  ARG A CB  1 
ATOM   1156 C  CG  . ARG A 1 155 ? 35.188  -1.723  -6.997  1.00 12.73 ?  157  ARG A CG  1 
ATOM   1157 C  CD  . ARG A 1 155 ? 33.933  -2.590  -6.992  1.00 13.78 ?  157  ARG A CD  1 
ATOM   1158 N  NE  . ARG A 1 155 ? 33.381  -2.724  -5.638  1.00 12.68 ?  157  ARG A NE  1 
ATOM   1159 C  CZ  . ARG A 1 155 ? 32.427  -3.574  -5.291  1.00 15.56 ?  157  ARG A CZ  1 
ATOM   1160 N  NH1 . ARG A 1 155 ? 31.857  -4.359  -6.210  1.00 15.00 ?  157  ARG A NH1 1 
ATOM   1161 N  NH2 . ARG A 1 155 ? 32.040  -3.639  -4.023  1.00 12.68 ?  157  ARG A NH2 1 
ATOM   1162 N  N   . TYR A 1 156 ? 35.348  2.578   -5.225  1.00 11.02 ?  158  TYR A N   1 
ATOM   1163 C  CA  . TYR A 1 156 ? 35.115  4.011   -5.103  1.00 10.00 ?  158  TYR A CA  1 
ATOM   1164 C  C   . TYR A 1 156 ? 36.420  4.779   -4.926  1.00 13.25 ?  158  TYR A C   1 
ATOM   1165 O  O   . TYR A 1 156 ? 36.638  5.818   -5.567  1.00 11.20 ?  158  TYR A O   1 
ATOM   1166 C  CB  . TYR A 1 156 ? 34.193  4.237   -3.915  1.00 8.99  ?  158  TYR A CB  1 
ATOM   1167 C  CG  . TYR A 1 156 ? 33.855  5.654   -3.627  1.00 10.66 ?  158  TYR A CG  1 
ATOM   1168 C  CD1 . TYR A 1 156 ? 32.835  6.304   -4.322  1.00 9.89  ?  158  TYR A CD1 1 
ATOM   1169 C  CD2 . TYR A 1 156 ? 34.534  6.348   -2.645  1.00 9.79  ?  158  TYR A CD2 1 
ATOM   1170 C  CE1 . TYR A 1 156 ? 32.520  7.614   -4.046  1.00 8.05  ?  158  TYR A CE1 1 
ATOM   1171 C  CE2 . TYR A 1 156 ? 34.205  7.660   -2.349  1.00 10.21 ?  158  TYR A CE2 1 
ATOM   1172 C  CZ  . TYR A 1 156 ? 33.187  8.277   -3.051  1.00 10.26 ?  158  TYR A CZ  1 
ATOM   1173 O  OH  . TYR A 1 156 ? 32.843  9.586   -2.765  1.00 12.93 ?  158  TYR A OH  1 
ATOM   1174 N  N   . VAL A 1 157 ? 37.293  4.286   -4.039  1.00 9.88  ?  159  VAL A N   1 
ATOM   1175 C  CA  . VAL A 1 157 ? 38.543  4.986   -3.743  1.00 11.53 ?  159  VAL A CA  1 
ATOM   1176 C  C   . VAL A 1 157 ? 39.399  5.107   -4.997  1.00 14.24 ?  159  VAL A C   1 
ATOM   1177 O  O   . VAL A 1 157 ? 40.046  6.136   -5.228  1.00 12.01 ?  159  VAL A O   1 
ATOM   1178 C  CB  . VAL A 1 157 ? 39.293  4.263   -2.610  1.00 11.38 ?  159  VAL A CB  1 
ATOM   1179 C  CG1 . VAL A 1 157 ? 40.687  4.850   -2.448  1.00 14.70 ?  159  VAL A CG1 1 
ATOM   1180 C  CG2 . VAL A 1 157 ? 38.510  4.387   -1.304  1.00 11.43 ?  159  VAL A CG2 1 
ATOM   1181 N  N   . GLN A 1 158 ? 39.388  4.081   -5.843  1.00 11.75 ?  160  GLN A N   1 
ATOM   1182 C  CA  . GLN A 1 158 ? 40.217  4.094   -7.042  1.00 14.80 ?  160  GLN A CA  1 
ATOM   1183 C  C   . GLN A 1 158 ? 39.576  4.804   -8.233  1.00 16.91 ?  160  GLN A C   1 
ATOM   1184 O  O   . GLN A 1 158 ? 40.259  5.014   -9.239  1.00 17.90 ?  160  GLN A O   1 
ATOM   1185 C  CB  . GLN A 1 158 ? 40.598  2.655   -7.411  1.00 14.38 ?  160  GLN A CB  1 
ATOM   1186 C  CG  . GLN A 1 158 ? 41.569  2.070   -6.364  1.00 18.20 ?  160  GLN A CG  1 
ATOM   1187 C  CD  . GLN A 1 158 ? 41.941  0.615   -6.606  1.00 34.09 ?  160  GLN A CD  1 
ATOM   1188 O  OE1 . GLN A 1 158 ? 41.527  0.010   -7.597  1.00 39.92 ?  160  GLN A OE1 1 
ATOM   1189 N  NE2 . GLN A 1 158 ? 42.685  0.030   -5.664  1.00 30.41 ?  160  GLN A NE2 1 
ATOM   1190 N  N   . ALA A 1 159 ? 38.303  5.191   -8.168  1.00 12.78 ?  161  ALA A N   1 
ATOM   1191 C  CA  . ALA A 1 159 ? 37.686  5.837   -9.330  1.00 12.12 ?  161  ALA A CA  1 
ATOM   1192 C  C   . ALA A 1 159 ? 38.153  7.289   -9.464  1.00 13.46 ?  161  ALA A C   1 
ATOM   1193 O  O   . ALA A 1 159 ? 38.307  7.991   -8.466  1.00 13.88 ?  161  ALA A O   1 
ATOM   1194 C  CB  . ALA A 1 159 ? 36.159  5.799   -9.221  1.00 15.66 ?  161  ALA A CB  1 
ATOM   1195 N  N   . ASP A 1 160 ? 38.355  7.747   -10.718 1.00 15.64 ?  162  ASP A N   1 
ATOM   1196 C  CA  . ASP A 1 160 ? 38.781  9.138   -10.950 1.00 14.49 ?  162  ASP A CA  1 
ATOM   1197 C  C   . ASP A 1 160 ? 37.753  10.145  -10.463 1.00 16.67 ?  162  ASP A C   1 
ATOM   1198 O  O   . ASP A 1 160 ? 38.121  11.216  -9.963  1.00 15.64 ?  162  ASP A O   1 
ATOM   1199 C  CB  . ASP A 1 160 ? 39.029  9.446   -12.433 1.00 15.64 ?  162  ASP A CB  1 
ATOM   1200 C  CG  . ASP A 1 160 ? 40.177  8.675   -13.040 1.00 30.50 ?  162  ASP A CG  1 
ATOM   1201 O  OD1 . ASP A 1 160 ? 40.833  7.881   -12.335 1.00 34.37 ?  162  ASP A OD1 1 
ATOM   1202 O  OD2 . ASP A 1 160 ? 40.434  8.910   -14.246 1.00 33.32 ?  162  ASP A OD2 1 
ATOM   1203 N  N   . LEU A 1 161 ? 36.473  9.874   -10.707 1.00 13.76 ?  163  LEU A N   1 
ATOM   1204 C  CA  . LEU A 1 161 ? 35.365  10.764  -10.369 1.00 12.22 ?  163  LEU A CA  1 
ATOM   1205 C  C   . LEU A 1 161 ? 34.430  10.042  -9.407  1.00 11.07 ?  163  LEU A C   1 
ATOM   1206 O  O   . LEU A 1 161 ? 33.930  8.956   -9.728  1.00 11.32 ?  163  LEU A O   1 
ATOM   1207 C  CB  . LEU A 1 161 ? 34.604  11.174  -11.628 1.00 13.48 ?  163  LEU A CB  1 
ATOM   1208 C  CG  . LEU A 1 161 ? 33.441  12.143  -11.440 1.00 17.46 ?  163  LEU A CG  1 
ATOM   1209 C  CD1 . LEU A 1 161 ? 33.913  13.475  -10.860 1.00 16.64 ?  163  LEU A CD1 1 
ATOM   1210 C  CD2 . LEU A 1 161 ? 32.744  12.322  -12.792 1.00 15.88 ?  163  LEU A CD2 1 
ATOM   1211 N  N   . LYS A 1 162 ? 34.186  10.648  -8.246  1.00 8.87  ?  164  LYS A N   1 
ATOM   1212 C  CA  . LYS A 1 162 ? 33.394  10.048  -7.174  1.00 9.63  ?  164  LYS A CA  1 
ATOM   1213 C  C   . LYS A 1 162 ? 32.090  10.826  -7.015  1.00 8.84  ?  164  LYS A C   1 
ATOM   1214 O  O   . LYS A 1 162 ? 32.122  12.031  -6.745  1.00 11.87 ?  164  LYS A O   1 
ATOM   1215 C  CB  . LYS A 1 162 ? 34.190  10.069  -5.865  1.00 7.08  ?  164  LYS A CB  1 
ATOM   1216 C  CG  . LYS A 1 162 ? 35.485  9.268   -5.905  1.00 12.67 ?  164  LYS A CG  1 
ATOM   1217 C  CD  . LYS A 1 162 ? 36.373  9.694   -4.731  1.00 11.43 ?  164  LYS A CD  1 
ATOM   1218 C  CE  . LYS A 1 162 ? 37.605  8.822   -4.515  1.00 16.45 ?  164  LYS A CE  1 
ATOM   1219 N  NZ  . LYS A 1 162 ? 38.431  8.663   -5.745  1.00 17.55 ?  164  LYS A NZ  1 
ATOM   1220 N  N   . ILE A 1 163 ? 30.948  10.145  -7.175  1.00 9.29  ?  165  ILE A N   1 
ATOM   1221 C  CA  . ILE A 1 163 ? 29.634  10.782  -7.110  1.00 8.35  ?  165  ILE A CA  1 
ATOM   1222 C  C   . ILE A 1 163 ? 28.753  10.006  -6.137  1.00 8.59  ?  165  ILE A C   1 
ATOM   1223 O  O   . ILE A 1 163 ? 28.835  8.776   -6.066  1.00 8.32  ?  165  ILE A O   1 
ATOM   1224 C  CB  . ILE A 1 163 ? 28.976  10.844  -8.506  1.00 10.15 ?  165  ILE A CB  1 
ATOM   1225 C  CG1 . ILE A 1 163 ? 29.827  11.681  -9.475  1.00 11.65 ?  165  ILE A CG1 1 
ATOM   1226 C  CG2 . ILE A 1 163 ? 27.553  11.382  -8.423  1.00 9.74  ?  165  ILE A CG2 1 
ATOM   1227 C  CD1 . ILE A 1 163 ? 29.490  11.367  -10.963 1.00 12.86 ?  165  ILE A CD1 1 
ATOM   1228 N  N   . ALA A 1 164 ? 27.923  10.717  -5.370  1.00 8.05  ?  166  ALA A N   1 
ATOM   1229 C  CA  . ALA A 1 164 ? 27.030  10.046  -4.424  1.00 9.29  ?  166  ALA A CA  1 
ATOM   1230 C  C   . ALA A 1 164 ? 25.634  10.650  -4.513  1.00 10.72 ?  166  ALA A C   1 
ATOM   1231 O  O   . ALA A 1 164 ? 25.494  11.863  -4.635  1.00 12.92 ?  166  ALA A O   1 
ATOM   1232 C  CB  . ALA A 1 164 ? 27.580  10.151  -2.995  1.00 10.50 ?  166  ALA A CB  1 
ATOM   1233 N  N   . THR A 1 165 ? 24.605  9.801   -4.490  1.00 9.59  ?  167  THR A N   1 
ATOM   1234 C  CA  . THR A 1 165 ? 23.217  10.245  -4.547  1.00 7.14  ?  167  THR A CA  1 
ATOM   1235 C  C   . THR A 1 165 ? 22.505  9.790   -3.280  1.00 13.12 ?  167  THR A C   1 
ATOM   1236 O  O   . THR A 1 165 ? 22.925  8.828   -2.622  1.00 15.17 ?  167  THR A O   1 
ATOM   1237 C  CB  . THR A 1 165 ? 22.497  9.659   -5.759  1.00 10.76 ?  167  THR A CB  1 
ATOM   1238 O  OG1 . THR A 1 165 ? 22.478  8.235   -5.639  1.00 12.10 ?  167  THR A OG1 1 
ATOM   1239 C  CG2 . THR A 1 165 ? 23.203  10.056  -7.068  1.00 9.98  ?  167  THR A CG2 1 
ATOM   1240 N  N   . GLY A 1 166 ? 21.412  10.448  -2.930  1.00 8.54  ?  168  GLY A N   1 
ATOM   1241 C  CA  . GLY A 1 166 ? 20.733  10.018  -1.723  1.00 10.90 ?  168  GLY A CA  1 
ATOM   1242 C  C   . GLY A 1 166 ? 19.559  10.880  -1.345  1.00 9.91  ?  168  GLY A C   1 
ATOM   1243 O  O   . GLY A 1 166 ? 19.117  11.740  -2.113  1.00 10.25 ?  168  GLY A O   1 
ATOM   1244 N  N   . LEU A 1 167 ? 19.087  10.640  -0.117  1.00 11.10 ?  169  LEU A N   1 
ATOM   1245 C  CA  . LEU A 1 167 ? 17.809  11.140  0.369   1.00 11.55 ?  169  LEU A CA  1 
ATOM   1246 C  C   . LEU A 1 167 ? 17.988  11.670  1.787   1.00 12.06 ?  169  LEU A C   1 
ATOM   1247 O  O   . LEU A 1 167 ? 18.518  10.968  2.655   1.00 11.23 ?  169  LEU A O   1 
ATOM   1248 C  CB  . LEU A 1 167 ? 16.768  10.010  0.316   1.00 8.59  ?  169  LEU A CB  1 
ATOM   1249 C  CG  . LEU A 1 167 ? 15.513  10.129  1.170   1.00 12.61 ?  169  LEU A CG  1 
ATOM   1250 C  CD1 . LEU A 1 167 ? 14.656  11.227  0.596   1.00 13.42 ?  169  LEU A CD1 1 
ATOM   1251 C  CD2 . LEU A 1 167 ? 14.768  8.790   1.180   1.00 11.73 ?  169  LEU A CD2 1 
ATOM   1252 N  N   . ILE A 1 168 ? 17.568  12.909  2.025   1.00 10.78 ?  170  ILE A N   1 
ATOM   1253 C  CA  . ILE A 1 168 ? 17.721  13.541  3.333   1.00 9.94  ?  170  ILE A CA  1 
ATOM   1254 C  C   . ILE A 1 168 ? 16.419  13.355  4.119   1.00 10.47 ?  170  ILE A C   1 
ATOM   1255 O  O   . ILE A 1 168 ? 15.389  13.942  3.777   1.00 10.55 ?  170  ILE A O   1 
ATOM   1256 C  CB  . ILE A 1 168 ? 18.105  15.020  3.199   1.00 11.07 ?  170  ILE A CB  1 
ATOM   1257 C  CG1 . ILE A 1 168 ? 19.394  15.157  2.368   1.00 11.37 ?  170  ILE A CG1 1 
ATOM   1258 C  CG2 . ILE A 1 168 ? 18.263  15.674  4.592   1.00 13.92 ?  170  ILE A CG2 1 
ATOM   1259 C  CD1 . ILE A 1 168 ? 19.770  16.610  2.022   1.00 11.15 ?  170  ILE A CD1 1 
ATOM   1260 N  N   . GLU A 1 169 ? 16.473  12.534  5.164   1.00 12.03 ?  171  GLU A N   1 
ATOM   1261 C  CA  . GLU A 1 169 ? 15.409  12.193  6.098   1.00 8.81  ?  171  GLU A CA  1 
ATOM   1262 C  C   . GLU A 1 169 ? 16.007  12.164  7.496   1.00 8.42  ?  171  GLU A C   1 
ATOM   1263 O  O   . GLU A 1 169 ? 17.217  11.994  7.649   1.00 10.16 ?  171  GLU A O   1 
ATOM   1264 C  CB  . GLU A 1 169 ? 14.801  10.806  5.827   1.00 11.06 ?  171  GLU A CB  1 
ATOM   1265 C  CG  . GLU A 1 169 ? 14.041  10.543  4.513   1.00 10.91 ?  171  GLU A CG  1 
ATOM   1266 C  CD  . GLU A 1 169 ? 12.621  11.083  4.536   1.00 16.63 ?  171  GLU A CD  1 
ATOM   1267 O  OE1 . GLU A 1 169 ? 11.879  10.892  3.530   1.00 16.71 ?  171  GLU A OE1 1 
ATOM   1268 O  OE2 . GLU A 1 169 ? 12.269  11.784  5.521   1.00 13.19 ?  171  GLU A OE2 1 
ATOM   1269 N  N   . PRO A 1 170 ? 15.180  12.260  8.544   1.00 10.62 ?  172  PRO A N   1 
ATOM   1270 C  CA  . PRO A 1 170 ? 15.707  12.070  9.905   1.00 10.47 ?  172  PRO A CA  1 
ATOM   1271 C  C   . PRO A 1 170 ? 16.334  10.690  10.077  1.00 10.04 ?  172  PRO A C   1 
ATOM   1272 O  O   . PRO A 1 170 ? 15.897  9.705   9.484   1.00 9.01  ?  172  PRO A O   1 
ATOM   1273 C  CB  . PRO A 1 170 ? 14.467  12.226  10.793  1.00 11.40 ?  172  PRO A CB  1 
ATOM   1274 C  CG  . PRO A 1 170 ? 13.486  13.033  9.959   1.00 11.53 ?  172  PRO A CG  1 
ATOM   1275 C  CD  . PRO A 1 170 ? 13.741  12.606  8.543   1.00 12.51 ?  172  PRO A CD  1 
ATOM   1276 N  N   . HIS A 1 171 ? 17.371  10.621  10.911  1.00 7.75  ?  173  HIS A N   1 
ATOM   1277 C  CA  . HIS A 1 171 ? 18.031  9.350   11.168  1.00 9.92  ?  173  HIS A CA  1 
ATOM   1278 C  C   . HIS A 1 171 ? 18.338  9.246   12.657  1.00 9.42  ?  173  HIS A C   1 
ATOM   1279 O  O   . HIS A 1 171 ? 18.864  10.187  13.259  1.00 9.16  ?  173  HIS A O   1 
ATOM   1280 C  CB  . HIS A 1 171 ? 19.320  9.179   10.348  1.00 8.90  ?  173  HIS A CB  1 
ATOM   1281 C  CG  . HIS A 1 171 ? 19.905  7.796   10.437  1.00 9.37  ?  173  HIS A CG  1 
ATOM   1282 N  ND1 . HIS A 1 171 ? 20.845  7.437   11.384  1.00 8.15  ?  173  HIS A ND1 1 
ATOM   1283 C  CD2 . HIS A 1 171 ? 19.647  6.678   9.715   1.00 8.53  ?  173  HIS A CD2 1 
ATOM   1284 C  CE1 . HIS A 1 171 ? 21.143  6.155   11.233  1.00 9.06  ?  173  HIS A CE1 1 
ATOM   1285 N  NE2 . HIS A 1 171 ? 20.420  5.671   10.235  1.00 8.58  ?  173  HIS A NE2 1 
ATOM   1286 N  N   . LEU A 1 172 ? 18.065  8.068   13.221  1.00 9.90  ?  174  LEU A N   1 
ATOM   1287 C  CA  . LEU A 1 172 ? 18.069  7.885   14.668  1.00 9.95  ?  174  LEU A CA  1 
ATOM   1288 C  C   . LEU A 1 172 ? 19.473  7.907   15.260  1.00 10.28 ?  174  LEU A C   1 
ATOM   1289 O  O   . LEU A 1 172 ? 19.604  8.041   16.480  1.00 11.05 ?  174  LEU A O   1 
ATOM   1290 C  CB  . LEU A 1 172 ? 17.388  6.559   15.016  1.00 10.30 ?  174  LEU A CB  1 
ATOM   1291 C  CG  . LEU A 1 172 ? 18.132  5.234   14.797  1.00 13.01 ?  174  LEU A CG  1 
ATOM   1292 C  CD1 . LEU A 1 172 ? 17.333  4.104   15.476  1.00 10.63 ?  174  LEU A CD1 1 
ATOM   1293 C  CD2 . LEU A 1 172 ? 18.512  4.903   13.333  1.00 11.34 ?  174  LEU A CD2 1 
ATOM   1294 N  N   . MET A 1 173 ? 20.515  7.722   14.451  1.00 8.76  ?  175  MET A N   1 
ATOM   1295 C  CA  . MET A 1 173 ? 21.876  7.858   14.963  1.00 9.34  ?  175  MET A CA  1 
ATOM   1296 C  C   . MET A 1 173 ? 22.607  9.069   14.410  1.00 9.84  ?  175  MET A C   1 
ATOM   1297 O  O   . MET A 1 173 ? 23.311  9.761   15.163  1.00 11.25 ?  175  MET A O   1 
ATOM   1298 C  CB  . MET A 1 173 ? 22.738  6.616   14.686  1.00 11.98 ?  175  MET A CB  1 
ATOM   1299 C  CG  . MET A 1 173 ? 22.252  5.264   15.226  1.00 16.52 ?  175  MET A CG  1 
ATOM   1300 S  SD  . MET A 1 173 ? 22.960  3.861   14.314  1.00 20.00 ?  175  MET A SD  1 
ATOM   1301 C  CE  . MET A 1 173 ? 21.906  2.521   14.857  1.00 21.57 ?  175  MET A CE  1 
ATOM   1302 N  N   . ALA A 1 174 ? 22.484  9.336   13.111  1.00 8.14  ?  176  ALA A N   1 
ATOM   1303 C  CA  . ALA A 1 174 ? 23.298  10.341  12.451  1.00 5.65  ?  176  ALA A CA  1 
ATOM   1304 C  C   . ALA A 1 174 ? 22.582  11.677  12.315  1.00 8.59  ?  176  ALA A C   1 
ATOM   1305 O  O   . ALA A 1 174 ? 23.106  12.586  11.661  1.00 10.23 ?  176  ALA A O   1 
ATOM   1306 C  CB  . ALA A 1 174 ? 23.737  9.833   11.080  1.00 10.98 ?  176  ALA A CB  1 
ATOM   1307 N  N   . GLY A 1 175 ? 21.398  11.810  12.909  1.00 9.44  ?  177  GLY A N   1 
ATOM   1308 C  CA  . GLY A 1 175 ? 20.658  13.057  12.832  1.00 8.70  ?  177  GLY A CA  1 
ATOM   1309 C  C   . GLY A 1 175 ? 19.801  13.138  11.591  1.00 9.75  ?  177  GLY A C   1 
ATOM   1310 O  O   . GLY A 1 175 ? 18.571  13.195  11.674  1.00 9.36  ?  177  GLY A O   1 
ATOM   1311 N  N   . TYR A 1 176 ? 20.460  13.165  10.435  1.00 8.78  ?  178  TYR A N   1 
ATOM   1312 C  CA  . TYR A 1 176 ? 19.810  13.105  9.138   1.00 10.77 ?  178  TYR A CA  1 
ATOM   1313 C  C   . TYR A 1 176 ? 20.617  12.167  8.255   1.00 7.72  ?  178  TYR A C   1 
ATOM   1314 O  O   . TYR A 1 176 ? 21.841  12.078  8.385   1.00 9.41  ?  178  TYR A O   1 
ATOM   1315 C  CB  . TYR A 1 176 ? 19.728  14.483  8.462   1.00 8.38  ?  178  TYR A CB  1 
ATOM   1316 C  CG  . TYR A 1 176 ? 18.741  15.387  9.141   1.00 9.72  ?  178  TYR A CG  1 
ATOM   1317 C  CD1 . TYR A 1 176 ? 17.376  15.327  8.832   1.00 9.04  ?  178  TYR A CD1 1 
ATOM   1318 C  CD2 . TYR A 1 176 ? 19.162  16.292  10.101  1.00 13.69 ?  178  TYR A CD2 1 
ATOM   1319 C  CE1 . TYR A 1 176 ? 16.471  16.134  9.474   1.00 11.70 ?  178  TYR A CE1 1 
ATOM   1320 C  CE2 . TYR A 1 176 ? 18.257  17.111  10.741  1.00 10.78 ?  178  TYR A CE2 1 
ATOM   1321 C  CZ  . TYR A 1 176 ? 16.918  17.029  10.420  1.00 15.59 ?  178  TYR A CZ  1 
ATOM   1322 O  OH  . TYR A 1 176 ? 16.026  17.846  11.067  1.00 17.60 ?  178  TYR A OH  1 
ATOM   1323 N  N   . SER A 1 177 ? 19.916  11.452  7.385   1.00 7.69  ?  179  SER A N   1 
ATOM   1324 C  CA  A SER A 1 177 ? 20.535  10.663  6.331   0.70 6.51  ?  179  SER A CA  1 
ATOM   1325 C  CA  B SER A 1 177 ? 20.588  10.676  6.360   0.30 6.60  ?  179  SER A CA  1 
ATOM   1326 C  C   . SER A 1 177 ? 20.974  11.580  5.191   1.00 9.11  ?  179  SER A C   1 
ATOM   1327 O  O   . SER A 1 177 ? 20.543  12.734  5.085   1.00 9.87  ?  179  SER A O   1 
ATOM   1328 C  CB  A SER A 1 177 ? 19.560  9.603   5.808   0.70 8.13  ?  179  SER A CB  1 
ATOM   1329 C  CB  B SER A 1 177 ? 19.696  9.534   5.884   0.30 8.18  ?  179  SER A CB  1 
ATOM   1330 O  OG  A SER A 1 177 ? 19.384  8.539   6.731   0.70 7.38  ?  179  SER A OG  1 
ATOM   1331 O  OG  B SER A 1 177 ? 18.515  10.033  5.299   0.30 10.35 ?  179  SER A OG  1 
ATOM   1332 N  N   . GLY A 1 178 ? 21.816  11.051  4.314   1.00 7.10  ?  180  GLY A N   1 
ATOM   1333 C  CA  . GLY A 1 178 ? 22.207  11.770  3.117   1.00 7.93  ?  180  GLY A CA  1 
ATOM   1334 C  C   . GLY A 1 178 ? 23.655  12.213  3.168   1.00 7.62  ?  180  GLY A C   1 
ATOM   1335 O  O   . GLY A 1 178 ? 24.377  11.968  4.135   1.00 7.88  ?  180  GLY A O   1 
ATOM   1336 N  N   . GLY A 1 179 ? 24.058  12.912  2.093   1.00 8.65  ?  181  GLY A N   1 
ATOM   1337 C  CA  . GLY A 1 179 ? 25.407  13.436  1.984   1.00 10.36 ?  181  GLY A CA  1 
ATOM   1338 C  C   . GLY A 1 179 ? 26.491  12.417  2.288   1.00 7.31  ?  181  GLY A C   1 
ATOM   1339 O  O   . GLY A 1 179 ? 26.558  11.351  1.674   1.00 8.24  ?  181  GLY A O   1 
ATOM   1340 N  N   . ARG A 1 180 ? 27.303  12.756  3.283   1.00 7.72  ?  182  ARG A N   1 
ATOM   1341 C  CA  A ARG A 1 180 ? 28.438  11.940  3.718   0.50 8.28  ?  182  ARG A CA  1 
ATOM   1342 C  CA  B ARG A 1 180 ? 28.436  11.941  3.721   0.50 8.28  ?  182  ARG A CA  1 
ATOM   1343 C  C   . ARG A 1 180 ? 28.081  10.496  4.077   1.00 8.96  ?  182  ARG A C   1 
ATOM   1344 O  O   . ARG A 1 180 ? 28.963  9.618   4.024   1.00 9.66  ?  182  ARG A O   1 
ATOM   1345 C  CB  A ARG A 1 180 ? 29.087  12.656  4.913   0.50 9.30  ?  182  ARG A CB  1 
ATOM   1346 C  CB  B ARG A 1 180 ? 29.085  12.655  4.917   0.50 9.31  ?  182  ARG A CB  1 
ATOM   1347 C  CG  A ARG A 1 180 ? 28.442  12.355  6.273   0.50 9.38  ?  182  ARG A CG  1 
ATOM   1348 C  CG  B ARG A 1 180 ? 28.337  12.510  6.260   0.50 9.33  ?  182  ARG A CG  1 
ATOM   1349 C  CD  A ARG A 1 180 ? 26.984  12.840  6.323   0.50 9.32  ?  182  ARG A CD  1 
ATOM   1350 C  CD  B ARG A 1 180 ? 26.964  13.232  6.264   0.50 9.01  ?  182  ARG A CD  1 
ATOM   1351 N  NE  A ARG A 1 180 ? 26.452  12.886  7.676   0.50 9.70  ?  182  ARG A NE  1 
ATOM   1352 N  NE  B ARG A 1 180 ? 26.352  13.238  7.590   0.50 9.18  ?  182  ARG A NE  1 
ATOM   1353 C  CZ  A ARG A 1 180 ? 25.169  12.777  7.991   0.50 8.43  ?  182  ARG A CZ  1 
ATOM   1354 C  CZ  B ARG A 1 180 ? 25.117  12.841  7.877   0.50 8.41  ?  182  ARG A CZ  1 
ATOM   1355 N  NH1 A ARG A 1 180 ? 24.267  12.513  7.052   0.50 8.45  ?  182  ARG A NH1 1 
ATOM   1356 N  NH1 B ARG A 1 180 ? 24.697  12.908  9.133   0.50 9.88  ?  182  ARG A NH1 1 
ATOM   1357 N  NH2 A ARG A 1 180 ? 24.804  12.856  9.264   0.50 9.83  ?  182  ARG A NH2 1 
ATOM   1358 N  NH2 B ARG A 1 180 ? 24.323  12.331  6.936   0.50 8.32  ?  182  ARG A NH2 1 
ATOM   1359 N  N   . LYS A 1 181 ? 26.829  10.214  4.450   1.00 9.64  ?  183  LYS A N   1 
ATOM   1360 C  CA  . LYS A 1 181 ? 26.475  8.878   4.937   1.00 10.97 ?  183  LYS A CA  1 
ATOM   1361 C  C   . LYS A 1 181 ? 26.536  7.804   3.846   1.00 8.42  ?  183  LYS A C   1 
ATOM   1362 O  O   . LYS A 1 181 ? 26.665  6.616   4.173   1.00 7.27  ?  183  LYS A O   1 
ATOM   1363 C  CB  . LYS A 1 181 ? 25.085  8.936   5.588   1.00 7.21  ?  183  LYS A CB  1 
ATOM   1364 C  CG  . LYS A 1 181 ? 24.822  7.928   6.691   1.00 9.80  ?  183  LYS A CG  1 
ATOM   1365 C  CD  . LYS A 1 181 ? 23.595  8.340   7.515   1.00 6.51  ?  183  LYS A CD  1 
ATOM   1366 C  CE  . LYS A 1 181 ? 23.178  7.255   8.497   1.00 8.12  ?  183  LYS A CE  1 
ATOM   1367 N  NZ  . LYS A 1 181 ? 22.967  5.925   7.827   1.00 8.21  ?  183  LYS A NZ  1 
ATOM   1368 N  N   . LEU A 1 182 ? 26.455  8.195   2.564   1.00 7.54  ?  184  LEU A N   1 
ATOM   1369 C  CA  . LEU A 1 182 ? 26.674  7.248   1.475   1.00 7.05  ?  184  LEU A CA  1 
ATOM   1370 C  C   . LEU A 1 182 ? 28.076  6.647   1.528   1.00 8.98  ?  184  LEU A C   1 
ATOM   1371 O  O   . LEU A 1 182 ? 28.269  5.504   1.114   1.00 7.85  ?  184  LEU A O   1 
ATOM   1372 C  CB  . LEU A 1 182 ? 26.446  7.923   0.120   1.00 6.13  ?  184  LEU A CB  1 
ATOM   1373 C  CG  . LEU A 1 182 ? 25.009  7.937   -0.423  1.00 8.29  ?  184  LEU A CG  1 
ATOM   1374 C  CD1 . LEU A 1 182 ? 24.548  6.515   -0.801  1.00 8.44  ?  184  LEU A CD1 1 
ATOM   1375 C  CD2 . LEU A 1 182 ? 24.076  8.599   0.589   1.00 12.41 ?  184  LEU A CD2 1 
ATOM   1376 N  N   . ILE A 1 183 ? 29.055  7.377   2.060   1.00 10.11 ?  185  ILE A N   1 
ATOM   1377 C  CA  . ILE A 1 183 ? 30.414  6.843   2.162   1.00 12.00 ?  185  ILE A CA  1 
ATOM   1378 C  C   . ILE A 1 183 ? 30.618  6.090   3.473   1.00 12.29 ?  185  ILE A C   1 
ATOM   1379 O  O   . ILE A 1 183 ? 31.074  4.936   3.485   1.00 9.85  ?  185  ILE A O   1 
ATOM   1380 C  CB  . ILE A 1 183 ? 31.451  7.971   2.009   1.00 9.83  ?  185  ILE A CB  1 
ATOM   1381 C  CG1 . ILE A 1 183 ? 31.456  8.515   0.585   1.00 11.77 ?  185  ILE A CG1 1 
ATOM   1382 C  CG2 . ILE A 1 183 ? 32.837  7.436   2.390   1.00 11.59 ?  185  ILE A CG2 1 
ATOM   1383 C  CD1 . ILE A 1 183 ? 31.924  9.931   0.490   1.00 18.49 ?  185  ILE A CD1 1 
ATOM   1384 N  N   . CYS A 1 184 ? 30.299  6.744   4.586   1.00 10.25 ?  186  CYS A N   1 
ATOM   1385 C  CA  . CYS A 1 184 ? 30.363  6.134   5.919   1.00 8.05  ?  186  CYS A CA  1 
ATOM   1386 C  C   . CYS A 1 184 ? 28.969  6.148   6.530   1.00 10.92 ?  186  CYS A C   1 
ATOM   1387 O  O   . CYS A 1 184 ? 28.501  7.225   6.950   1.00 8.03  ?  186  CYS A O   1 
ATOM   1388 C  CB  . CYS A 1 184 ? 31.339  6.888   6.822   1.00 13.83 ?  186  CYS A CB  1 
ATOM   1389 S  SG  . CYS A 1 184 ? 31.505  6.150   8.460   1.00 14.80 ?  186  CYS A SG  1 
ATOM   1390 N  N   . PRO A 1 185 ? 28.270  4.994   6.634   1.00 9.71  ?  187  PRO A N   1 
ATOM   1391 C  CA  . PRO A 1 185 ? 28.751  3.611   6.472   1.00 8.40  ?  187  PRO A CA  1 
ATOM   1392 C  C   . PRO A 1 185 ? 28.511  2.983   5.099   1.00 9.55  ?  187  PRO A C   1 
ATOM   1393 O  O   . PRO A 1 185 ? 28.852  1.811   4.913   1.00 8.66  ?  187  PRO A O   1 
ATOM   1394 C  CB  . PRO A 1 185 ? 27.909  2.852   7.497   1.00 9.49  ?  187  PRO A CB  1 
ATOM   1395 C  CG  . PRO A 1 185 ? 26.559  3.522   7.333   1.00 9.18  ?  187  PRO A CG  1 
ATOM   1396 C  CD  . PRO A 1 185 ? 26.863  5.008   7.083   1.00 7.69  ?  187  PRO A CD  1 
ATOM   1397 N  N   . GLY A 1 186 ? 27.913  3.745   4.184   1.00 8.47  ?  188  GLY A N   1 
ATOM   1398 C  CA  . GLY A 1 186 ? 27.366  3.170   2.958   1.00 8.16  ?  188  GLY A CA  1 
ATOM   1399 C  C   . GLY A 1 186 ? 28.319  2.243   2.230   1.00 8.34  ?  188  GLY A C   1 
ATOM   1400 O  O   . GLY A 1 186 ? 27.912  1.193   1.741   1.00 8.15  ?  188  GLY A O   1 
ATOM   1401 N  N   . ILE A 1 187 ? 29.609  2.596   2.176   1.00 7.61  ?  189  ILE A N   1 
ATOM   1402 C  CA  . ILE A 1 187 ? 30.595  1.709   1.560   1.00 4.73  ?  189  ILE A CA  1 
ATOM   1403 C  C   . ILE A 1 187 ? 31.793  1.514   2.489   1.00 9.08  ?  189  ILE A C   1 
ATOM   1404 O  O   . ILE A 1 187 ? 32.931  1.388   2.028   1.00 7.29  ?  189  ILE A O   1 
ATOM   1405 C  CB  . ILE A 1 187 ? 31.038  2.230   0.189   1.00 6.50  ?  189  ILE A CB  1 
ATOM   1406 C  CG1 . ILE A 1 187 ? 31.441  3.710   0.247   1.00 6.98  ?  189  ILE A CG1 1 
ATOM   1407 C  CG2 . ILE A 1 187 ? 29.899  2.071   -0.821  1.00 6.88  ?  189  ILE A CG2 1 
ATOM   1408 C  CD1 . ILE A 1 187 ? 32.271  4.151   -0.979  1.00 9.41  ?  189  ILE A CD1 1 
ATOM   1409 N  N   . ALA A 1 188 ? 31.545  1.445   3.785   1.00 6.59  ?  190  ALA A N   1 
ATOM   1410 C  CA  . ALA A 1 188 ? 32.603  1.249   4.770   1.00 7.83  ?  190  ALA A CA  1 
ATOM   1411 C  C   . ALA A 1 188 ? 32.585  -0.182  5.310   1.00 10.26 ?  190  ALA A C   1 
ATOM   1412 O  O   . ALA A 1 188 ? 31.535  -0.820  5.405   1.00 10.81 ?  190  ALA A O   1 
ATOM   1413 C  CB  . ALA A 1 188 ? 32.448  2.249   5.923   1.00 11.78 ?  190  ALA A CB  1 
ATOM   1414 N  N   . ALA A 1 189 ? 33.761  -0.673  5.703   1.00 9.50  ?  191  ALA A N   1 
ATOM   1415 C  CA  . ALA A 1 189 ? 33.868  -2.044  6.179   1.00 9.62  ?  191  ALA A CA  1 
ATOM   1416 C  C   . ALA A 1 189 ? 33.376  -2.149  7.624   1.00 9.40  ?  191  ALA A C   1 
ATOM   1417 O  O   . ALA A 1 189 ? 33.333  -1.161  8.361   1.00 10.70 ?  191  ALA A O   1 
ATOM   1418 C  CB  . ALA A 1 189 ? 35.319  -2.524  6.088   1.00 10.53 ?  191  ALA A CB  1 
ATOM   1419 N  N   . PHE A 1 190 ? 32.995  -3.371  8.021   1.00 9.40  ?  192  PHE A N   1 
ATOM   1420 C  CA  . PHE A 1 190 ? 32.651  -3.627  9.421   1.00 10.32 ?  192  PHE A CA  1 
ATOM   1421 C  C   . PHE A 1 190 ? 33.747  -3.163  10.378  1.00 11.28 ?  192  PHE A C   1 
ATOM   1422 O  O   . PHE A 1 190 ? 33.455  -2.746  11.502  1.00 11.55 ?  192  PHE A O   1 
ATOM   1423 C  CB  . PHE A 1 190 ? 32.399  -5.119  9.635   1.00 15.38 ?  192  PHE A CB  1 
ATOM   1424 C  CG  . PHE A 1 190 ? 31.918  -5.472  11.025  1.00 15.27 ?  192  PHE A CG  1 
ATOM   1425 C  CD1 . PHE A 1 190 ? 30.734  -4.964  11.521  1.00 13.67 ?  192  PHE A CD1 1 
ATOM   1426 C  CD2 . PHE A 1 190 ? 32.663  -6.326  11.832  1.00 17.92 ?  192  PHE A CD2 1 
ATOM   1427 C  CE1 . PHE A 1 190 ? 30.290  -5.313  12.803  1.00 11.31 ?  192  PHE A CE1 1 
ATOM   1428 C  CE2 . PHE A 1 190 ? 32.230  -6.663  13.106  1.00 18.02 ?  192  PHE A CE2 1 
ATOM   1429 C  CZ  . PHE A 1 190 ? 31.042  -6.151  13.589  1.00 17.44 ?  192  PHE A CZ  1 
ATOM   1430 N  N   . GLU A 1 191 ? 35.009  -3.251  9.961   1.00 11.16 ?  193  GLU A N   1 
ATOM   1431 C  CA  . GLU A 1 191 ? 36.106  -2.809  10.820  1.00 10.47 ?  193  GLU A CA  1 
ATOM   1432 C  C   . GLU A 1 191 ? 35.974  -1.331  11.182  1.00 12.47 ?  193  GLU A C   1 
ATOM   1433 O  O   . GLU A 1 191 ? 36.395  -0.913  12.273  1.00 14.05 ?  193  GLU A O   1 
ATOM   1434 C  CB  . GLU A 1 191 ? 37.443  -3.070  10.119  1.00 14.61 ?  193  GLU A CB  1 
ATOM   1435 C  CG  . GLU A 1 191 ? 37.811  -4.555  10.019  1.00 20.77 ?  193  GLU A CG  1 
ATOM   1436 C  CD  . GLU A 1 191 ? 37.970  -5.240  11.382  1.00 36.57 ?  193  GLU A CD  1 
ATOM   1437 O  OE1 . GLU A 1 191 ? 37.007  -5.897  11.838  1.00 32.50 ?  193  GLU A OE1 1 
ATOM   1438 O  OE2 . GLU A 1 191 ? 39.051  -5.111  12.000  1.00 38.27 ?  193  GLU A OE2 1 
ATOM   1439 N  N   . THR A 1 192 ? 35.409  -0.530  10.277  1.00 12.51 ?  194  THR A N   1 
ATOM   1440 C  CA  . THR A 1 192 ? 35.067  0.857   10.572  1.00 10.45 ?  194  THR A CA  1 
ATOM   1441 C  C   . THR A 1 192 ? 33.736  0.956   11.315  1.00 9.74  ?  194  THR A C   1 
ATOM   1442 O  O   . THR A 1 192 ? 33.651  1.603   12.366  1.00 8.86  ?  194  THR A O   1 
ATOM   1443 C  CB  . THR A 1 192 ? 34.983  1.669   9.282   1.00 10.84 ?  194  THR A CB  1 
ATOM   1444 O  OG1 . THR A 1 192 ? 36.272  1.705   8.663   1.00 12.78 ?  194  THR A OG1 1 
ATOM   1445 C  CG2 . THR A 1 192 ? 34.513  3.117   9.582   1.00 9.18  ?  194  THR A CG2 1 
ATOM   1446 N  N   . VAL A 1 193 ? 32.684  0.330   10.767  1.00 9.30  ?  195  VAL A N   1 
ATOM   1447 C  CA  . VAL A 1 193 ? 31.334  0.550   11.272  1.00 9.72  ?  195  VAL A CA  1 
ATOM   1448 C  C   . VAL A 1 193 ? 31.128  -0.020  12.678  1.00 12.49 ?  195  VAL A C   1 
ATOM   1449 O  O   . VAL A 1 193 ? 30.368  0.554   13.467  1.00 10.69 ?  195  VAL A O   1 
ATOM   1450 C  CB  . VAL A 1 193 ? 30.322  -0.030  10.261  1.00 9.31  ?  195  VAL A CB  1 
ATOM   1451 C  CG1 . VAL A 1 193 ? 28.897  0.157   10.740  1.00 12.96 ?  195  VAL A CG1 1 
ATOM   1452 C  CG2 . VAL A 1 193 ? 30.549  0.623   8.913   1.00 10.95 ?  195  VAL A CG2 1 
ATOM   1453 N  N   . LYS A 1 194 ? 31.793  -1.131  13.039  1.00 8.12  ?  196  LYS A N   1 
ATOM   1454 C  CA  . LYS A 1 194 ? 31.583  -1.665  14.385  1.00 9.92  ?  196  LYS A CA  1 
ATOM   1455 C  C   . LYS A 1 194 ? 31.974  -0.650  15.467  1.00 12.05 ?  196  LYS A C   1 
ATOM   1456 O  O   . LYS A 1 194 ? 31.351  -0.610  16.541  1.00 10.97 ?  196  LYS A O   1 
ATOM   1457 C  CB  . LYS A 1 194 ? 32.360  -2.972  14.573  1.00 12.08 ?  196  LYS A CB  1 
ATOM   1458 C  CG  . LYS A 1 194 ? 33.863  -2.806  14.807  1.00 10.57 ?  196  LYS A CG  1 
ATOM   1459 C  CD  . LYS A 1 194 ? 34.578  -4.177  14.742  1.00 13.97 ?  196  LYS A CD  1 
ATOM   1460 C  CE  . LYS A 1 194 ? 36.016  -4.035  15.205  1.00 19.13 ?  196  LYS A CE  1 
ATOM   1461 N  NZ  . LYS A 1 194 ? 36.834  -5.260  14.904  1.00 20.00 ?  196  LYS A NZ  1 
ATOM   1462 N  N   . LEU A 1 195 ? 32.970  0.203   15.190  1.00 11.96 ?  197  LEU A N   1 
ATOM   1463 C  CA  . LEU A 1 195 ? 33.381  1.203   16.173  1.00 13.02 ?  197  LEU A CA  1 
ATOM   1464 C  C   . LEU A 1 195 ? 32.534  2.465   16.090  1.00 12.50 ?  197  LEU A C   1 
ATOM   1465 O  O   . LEU A 1 195 ? 32.224  3.069   17.124  1.00 13.09 ?  197  LEU A O   1 
ATOM   1466 C  CB  . LEU A 1 195 ? 34.858  1.559   15.992  1.00 11.77 ?  197  LEU A CB  1 
ATOM   1467 C  CG  . LEU A 1 195 ? 35.832  0.465   16.426  1.00 16.06 ?  197  LEU A CG  1 
ATOM   1468 C  CD1 . LEU A 1 195 ? 37.225  0.784   15.887  1.00 16.26 ?  197  LEU A CD1 1 
ATOM   1469 C  CD2 . LEU A 1 195 ? 35.846  0.337   17.942  1.00 16.51 ?  197  LEU A CD2 1 
ATOM   1470 N  N   . TRP A 1 196 ? 32.162  2.878   14.872  1.00 12.73 ?  198  TRP A N   1 
ATOM   1471 C  CA  . TRP A 1 196 ? 31.375  4.093   14.684  1.00 12.01 ?  198  TRP A CA  1 
ATOM   1472 C  C   . TRP A 1 196 ? 29.938  3.899   15.167  1.00 12.79 ?  198  TRP A C   1 
ATOM   1473 O  O   . TRP A 1 196 ? 29.310  4.849   15.658  1.00 15.76 ?  198  TRP A O   1 
ATOM   1474 C  CB  . TRP A 1 196 ? 31.451  4.504   13.208  1.00 13.80 ?  198  TRP A CB  1 
ATOM   1475 C  CG  . TRP A 1 196 ? 30.637  5.653   12.863  1.00 10.57 ?  198  TRP A CG  1 
ATOM   1476 C  CD1 . TRP A 1 196 ? 30.796  6.935   13.298  1.00 12.04 ?  198  TRP A CD1 1 
ATOM   1477 C  CD2 . TRP A 1 196 ? 29.513  5.657   11.980  1.00 9.98  ?  198  TRP A CD2 1 
ATOM   1478 N  NE1 . TRP A 1 196 ? 29.828  7.745   12.740  1.00 11.42 ?  198  TRP A NE1 1 
ATOM   1479 C  CE2 . TRP A 1 196 ? 29.029  6.978   11.931  1.00 12.31 ?  198  TRP A CE2 1 
ATOM   1480 C  CE3 . TRP A 1 196 ? 28.888  4.677   11.213  1.00 14.51 ?  198  TRP A CE3 1 
ATOM   1481 C  CZ2 . TRP A 1 196 ? 27.936  7.342   11.157  1.00 10.57 ?  198  TRP A CZ2 1 
ATOM   1482 C  CZ3 . TRP A 1 196 ? 27.787  5.036   10.450  1.00 12.09 ?  198  TRP A CZ3 1 
ATOM   1483 C  CH2 . TRP A 1 196 ? 27.324  6.361   10.432  1.00 12.64 ?  198  TRP A CH2 1 
ATOM   1484 N  N   . HIS A 1 197 ? 29.417  2.672   15.065  1.00 11.61 ?  199  HIS A N   1 
ATOM   1485 C  CA  A HIS A 1 197 ? 28.133  2.290   15.641  0.50 11.86 ?  199  HIS A CA  1 
ATOM   1486 C  CA  B HIS A 1 197 ? 28.135  2.285   15.636  0.50 11.86 ?  199  HIS A CA  1 
ATOM   1487 C  C   . HIS A 1 197 ? 28.289  1.619   17.005  1.00 10.18 ?  199  HIS A C   1 
ATOM   1488 O  O   . HIS A 1 197 ? 27.403  0.877   17.430  1.00 11.25 ?  199  HIS A O   1 
ATOM   1489 C  CB  A HIS A 1 197 ? 27.379  1.357   14.688  0.50 11.48 ?  199  HIS A CB  1 
ATOM   1490 C  CB  B HIS A 1 197 ? 27.403  1.345   14.673  0.50 11.48 ?  199  HIS A CB  1 
ATOM   1491 C  CG  A HIS A 1 197 ? 26.653  2.056   13.576  0.50 11.18 ?  199  HIS A CG  1 
ATOM   1492 C  CG  B HIS A 1 197 ? 26.600  2.044   13.617  0.50 11.23 ?  199  HIS A CG  1 
ATOM   1493 N  ND1 A HIS A 1 197 ? 26.396  3.411   13.579  0.50 13.46 ?  199  HIS A ND1 1 
ATOM   1494 N  ND1 B HIS A 1 197 ? 26.520  3.418   13.519  0.50 13.39 ?  199  HIS A ND1 1 
ATOM   1495 C  CD2 A HIS A 1 197 ? 26.133  1.577   12.421  0.50 9.76  ?  199  HIS A CD2 1 
ATOM   1496 C  CD2 B HIS A 1 197 ? 25.862  1.551   12.594  0.50 10.29 ?  199  HIS A CD2 1 
ATOM   1497 C  CE1 A HIS A 1 197 ? 25.731  3.732   12.481  0.50 14.61 ?  199  HIS A CE1 1 
ATOM   1498 C  CE1 B HIS A 1 197 ? 25.738  3.738   12.502  0.50 14.61 ?  199  HIS A CE1 1 
ATOM   1499 N  NE2 A HIS A 1 197 ? 25.564  2.638   11.757  0.50 10.51 ?  199  HIS A NE2 1 
ATOM   1500 N  NE2 B HIS A 1 197 ? 25.332  2.624   11.919  0.50 10.43 ?  199  HIS A NE2 1 
ATOM   1501 N  N   . GLY A 1 198 ? 29.412  1.851   17.698  1.00 10.88 ?  200  GLY A N   1 
ATOM   1502 C  CA  . GLY A 1 198 ? 29.597  1.297   19.019  1.00 12.22 ?  200  GLY A CA  1 
ATOM   1503 C  C   . GLY A 1 198 ? 28.947  2.154   20.084  1.00 13.04 ?  200  GLY A C   1 
ATOM   1504 O  O   . GLY A 1 198 ? 28.539  3.301   19.861  1.00 11.05 ?  200  GLY A O   1 
ATOM   1505 N  N   . PRO A 1 199 ? 28.827  1.591   21.285  1.00 14.90 ?  201  PRO A N   1 
ATOM   1506 C  CA  . PRO A 1 199 ? 28.108  2.317   22.346  1.00 12.37 ?  201  PRO A CA  1 
ATOM   1507 C  C   . PRO A 1 199 ? 28.749  3.642   22.739  1.00 12.97 ?  201  PRO A C   1 
ATOM   1508 O  O   . PRO A 1 199 ? 28.036  4.539   23.204  1.00 16.12 ?  201  PRO A O   1 
ATOM   1509 C  CB  . PRO A 1 199 ? 28.090  1.317   23.515  1.00 15.20 ?  201  PRO A CB  1 
ATOM   1510 C  CG  . PRO A 1 199 ? 29.084  0.254   23.161  1.00 15.41 ?  201  PRO A CG  1 
ATOM   1511 C  CD  . PRO A 1 199 ? 29.139  0.204   21.660  1.00 14.69 ?  201  PRO A CD  1 
ATOM   1512 N  N   . ARG A 1 200 ? 30.061  3.808   22.565  1.00 11.99 ?  202  ARG A N   1 
ATOM   1513 C  CA  . ARG A 1 200 ? 30.669  5.098   22.888  1.00 14.41 ?  202  ARG A CA  1 
ATOM   1514 C  C   . ARG A 1 200 ? 30.091  6.222   22.026  1.00 17.12 ?  202  ARG A C   1 
ATOM   1515 O  O   . ARG A 1 200 ? 30.030  7.378   22.463  1.00 16.97 ?  202  ARG A O   1 
ATOM   1516 C  CB  . ARG A 1 200 ? 32.187  5.010   22.748  1.00 17.47 ?  202  ARG A CB  1 
ATOM   1517 C  CG  . ARG A 1 200 ? 32.856  4.309   23.928  1.00 20.76 ?  202  ARG A CG  1 
ATOM   1518 C  CD  . ARG A 1 200 ? 34.365  4.356   23.829  1.00 22.21 ?  202  ARG A CD  1 
ATOM   1519 N  NE  . ARG A 1 200 ? 34.861  3.624   22.670  1.00 21.06 ?  202  ARG A NE  1 
ATOM   1520 C  CZ  . ARG A 1 200 ? 35.105  2.317   22.669  1.00 26.64 ?  202  ARG A CZ  1 
ATOM   1521 N  NH1 . ARG A 1 200 ? 34.910  1.604   23.774  1.00 21.51 ?  202  ARG A NH1 1 
ATOM   1522 N  NH2 . ARG A 1 200 ? 35.547  1.722   21.562  1.00 31.43 ?  202  ARG A NH2 1 
ATOM   1523 N  N   . PHE A 1 201 ? 29.624  5.900   20.820  1.00 11.51 ?  203  PHE A N   1 
ATOM   1524 C  CA  . PHE A 1 201 ? 28.915  6.861   19.987  1.00 9.93  ?  203  PHE A CA  1 
ATOM   1525 C  C   . PHE A 1 201 ? 27.409  6.843   20.256  1.00 13.14 ?  203  PHE A C   1 
ATOM   1526 O  O   . PHE A 1 201 ? 26.795  7.898   20.454  1.00 11.99 ?  203  PHE A O   1 
ATOM   1527 C  CB  . PHE A 1 201 ? 29.197  6.572   18.502  1.00 9.50  ?  203  PHE A CB  1 
ATOM   1528 C  CG  . PHE A 1 201 ? 30.564  6.987   18.028  1.00 12.42 ?  203  PHE A CG  1 
ATOM   1529 C  CD1 . PHE A 1 201 ? 31.629  6.095   18.063  1.00 12.25 ?  203  PHE A CD1 1 
ATOM   1530 C  CD2 . PHE A 1 201 ? 30.774  8.249   17.497  1.00 12.89 ?  203  PHE A CD2 1 
ATOM   1531 C  CE1 . PHE A 1 201 ? 32.893  6.472   17.606  1.00 12.49 ?  203  PHE A CE1 1 
ATOM   1532 C  CE2 . PHE A 1 201 ? 32.038  8.639   17.041  1.00 15.94 ?  203  PHE A CE2 1 
ATOM   1533 C  CZ  . PHE A 1 201 ? 33.103  7.739   17.100  1.00 9.27  ?  203  PHE A CZ  1 
ATOM   1534 N  N   . LEU A 1 202 ? 26.794  5.659   20.307  1.00 11.86 ?  204  LEU A N   1 
ATOM   1535 C  CA  . LEU A 1 202 ? 25.336  5.628   20.214  1.00 12.48 ?  204  LEU A CA  1 
ATOM   1536 C  C   . LEU A 1 202 ? 24.646  5.997   21.520  1.00 13.66 ?  204  LEU A C   1 
ATOM   1537 O  O   . LEU A 1 202 ? 23.460  6.328   21.502  1.00 15.81 ?  204  LEU A O   1 
ATOM   1538 C  CB  . LEU A 1 202 ? 24.827  4.258   19.785  1.00 14.75 ?  204  LEU A CB  1 
ATOM   1539 C  CG  . LEU A 1 202 ? 25.284  3.880   18.370  1.00 18.05 ?  204  LEU A CG  1 
ATOM   1540 C  CD1 . LEU A 1 202 ? 24.817  2.462   18.043  1.00 20.30 ?  204  LEU A CD1 1 
ATOM   1541 C  CD2 . LEU A 1 202 ? 24.965  4.908   17.300  1.00 14.45 ?  204  LEU A CD2 1 
ATOM   1542 N  N   . GLU A 1 203 ? 25.345  5.919   22.640  1.00 13.00 ?  205  GLU A N   1 
ATOM   1543 C  CA  . GLU A 1 203 ? 24.785  6.316   23.921  1.00 14.06 ?  205  GLU A CA  1 
ATOM   1544 C  C   . GLU A 1 203 ? 24.910  7.814   24.173  1.00 15.49 ?  205  GLU A C   1 
ATOM   1545 O  O   . GLU A 1 203 ? 24.434  8.292   25.205  1.00 18.82 ?  205  GLU A O   1 
ATOM   1546 C  CB  . GLU A 1 203 ? 25.472  5.544   25.047  1.00 16.60 ?  205  GLU A CB  1 
ATOM   1547 C  CG  . GLU A 1 203 ? 25.169  4.042   25.075  1.00 19.07 ?  205  GLU A CG  1 
ATOM   1548 C  CD  . GLU A 1 203 ? 23.671  3.710   25.113  1.00 21.19 ?  205  GLU A CD  1 
ATOM   1549 O  OE1 . GLU A 1 203 ? 22.930  4.297   25.935  1.00 23.58 ?  205  GLU A OE1 1 
ATOM   1550 O  OE2 . GLU A 1 203 ? 23.241  2.820   24.343  1.00 21.16 ?  205  GLU A OE2 1 
ATOM   1551 N  N   . HIS A 1 204 ? 25.555  8.556   23.274  1.00 13.05 ?  206  HIS A N   1 
ATOM   1552 C  CA  . HIS A 1 204 ? 25.631  10.002  23.416  1.00 12.44 ?  206  HIS A CA  1 
ATOM   1553 C  C   . HIS A 1 204 ? 24.233  10.605  23.311  1.00 14.61 ?  206  HIS A C   1 
ATOM   1554 O  O   . HIS A 1 204 ? 23.457  10.210  22.440  1.00 15.02 ?  206  HIS A O   1 
ATOM   1555 C  CB  . HIS A 1 204 ? 26.523  10.605  22.331  1.00 13.25 ?  206  HIS A CB  1 
ATOM   1556 C  CG  . HIS A 1 204 ? 26.907  12.030  22.590  1.00 14.84 ?  206  HIS A CG  1 
ATOM   1557 N  ND1 . HIS A 1 204 ? 26.057  13.088  22.347  1.00 18.16 ?  206  HIS A ND1 1 
ATOM   1558 C  CD2 . HIS A 1 204 ? 28.048  12.567  23.084  1.00 18.05 ?  206  HIS A CD2 1 
ATOM   1559 C  CE1 . HIS A 1 204 ? 26.663  14.219  22.669  1.00 17.88 ?  206  HIS A CE1 1 
ATOM   1560 N  NE2 . HIS A 1 204 ? 27.871  13.930  23.121  1.00 15.98 ?  206  HIS A NE2 1 
ATOM   1561 N  N   . PRO A 1 205 ? 23.882  11.572  24.166  1.00 16.95 ?  207  PRO A N   1 
ATOM   1562 C  CA  . PRO A 1 205 ? 22.508  12.118  24.109  1.00 15.26 ?  207  PRO A CA  1 
ATOM   1563 C  C   . PRO A 1 205 ? 22.155  12.784  22.788  1.00 18.04 ?  207  PRO A C   1 
ATOM   1564 O  O   . PRO A 1 205 ? 20.965  12.820  22.436  1.00 17.87 ?  207  PRO A O   1 
ATOM   1565 C  CB  . PRO A 1 205 ? 22.470  13.116  25.278  1.00 22.72 ?  207  PRO A CB  1 
ATOM   1566 C  CG  . PRO A 1 205 ? 23.897  13.411  25.579  1.00 24.50 ?  207  PRO A CG  1 
ATOM   1567 C  CD  . PRO A 1 205 ? 24.661  12.151  25.273  1.00 18.70 ?  207  PRO A CD  1 
ATOM   1568 N  N   . LEU A 1 206 ? 23.128  13.278  22.026  1.00 13.15 ?  208  LEU A N   1 
ATOM   1569 C  CA  . LEU A 1 206 ? 22.838  13.923  20.749  1.00 14.11 ?  208  LEU A CA  1 
ATOM   1570 C  C   . LEU A 1 206 ? 22.944  12.969  19.559  1.00 12.37 ?  208  LEU A C   1 
ATOM   1571 O  O   . LEU A 1 206 ? 22.780  13.406  18.412  1.00 12.99 ?  208  LEU A O   1 
ATOM   1572 C  CB  . LEU A 1 206 ? 23.765  15.126  20.542  1.00 16.12 ?  208  LEU A CB  1 
ATOM   1573 C  CG  . LEU A 1 206 ? 23.495  16.275  21.528  1.00 20.84 ?  208  LEU A CG  1 
ATOM   1574 C  CD1 . LEU A 1 206 ? 24.347  17.501  21.219  1.00 26.71 ?  208  LEU A CD1 1 
ATOM   1575 C  CD2 . LEU A 1 206 ? 22.016  16.633  21.510  1.00 21.86 ?  208  LEU A CD2 1 
ATOM   1576 N  N   . ALA A 1 207 ? 23.181  11.678  19.799  1.00 10.86 ?  209  ALA A N   1 
ATOM   1577 C  CA  . ALA A 1 207 ? 23.126  10.687  18.725  1.00 11.17 ?  209  ALA A CA  1 
ATOM   1578 C  C   . ALA A 1 207 ? 21.656  10.301  18.577  1.00 12.34 ?  209  ALA A C   1 
ATOM   1579 O  O   . ALA A 1 207 ? 21.178  9.307   19.129  1.00 13.80 ?  209  ALA A O   1 
ATOM   1580 C  CB  . ALA A 1 207 ? 24.018  9.484   19.031  1.00 10.16 ?  209  ALA A CB  1 
ATOM   1581 N  N   . ASP A 1 208 ? 20.921  11.139  17.846  1.00 13.67 ?  210  ASP A N   1 
ATOM   1582 C  CA  . ASP A 1 208 ? 19.462  11.083  17.845  1.00 12.36 ?  210  ASP A CA  1 
ATOM   1583 C  C   . ASP A 1 208 ? 18.943  11.870  16.649  1.00 8.01  ?  210  ASP A C   1 
ATOM   1584 O  O   . ASP A 1 208 ? 19.661  12.685  16.071  1.00 13.62 ?  210  ASP A O   1 
ATOM   1585 C  CB  . ASP A 1 208 ? 18.910  11.641  19.164  1.00 16.05 ?  210  ASP A CB  1 
ATOM   1586 C  CG  . ASP A 1 208 ? 17.521  11.117  19.506  1.00 30.49 ?  210  ASP A CG  1 
ATOM   1587 O  OD1 . ASP A 1 208 ? 16.988  11.557  20.557  1.00 32.86 ?  210  ASP A OD1 1 
ATOM   1588 O  OD2 . ASP A 1 208 ? 16.970  10.278  18.751  1.00 24.30 ?  210  ASP A OD2 1 
ATOM   1589 N  N   . CYS A 1 209 ? 17.678  11.636  16.289  1.00 12.25 ?  211  CYS A N   1 
ATOM   1590 C  CA  . CYS A 1 209 ? 17.114  12.311  15.132  1.00 8.07  ?  211  CYS A CA  1 
ATOM   1591 C  C   . CYS A 1 209 ? 17.236  13.826  15.239  1.00 12.57 ?  211  CYS A C   1 
ATOM   1592 O  O   . CYS A 1 209 ? 16.939  14.422  16.278  1.00 13.94 ?  211  CYS A O   1 
ATOM   1593 C  CB  . CYS A 1 209 ? 15.639  11.952  14.961  1.00 14.71 ?  211  CYS A CB  1 
ATOM   1594 S  SG  . CYS A 1 209 ? 15.298  10.191  14.901  1.00 30.15 ?  211  CYS A SG  1 
ATOM   1595 N  N   . GLY A 1 210 ? 17.645  14.452  14.138  1.00 13.29 ?  212  GLY A N   1 
ATOM   1596 C  CA  . GLY A 1 210 ? 17.631  15.893  14.012  1.00 10.47 ?  212  GLY A CA  1 
ATOM   1597 C  C   . GLY A 1 210 ? 18.856  16.626  14.515  1.00 11.56 ?  212  GLY A C   1 
ATOM   1598 O  O   . GLY A 1 210 ? 18.946  17.844  14.319  1.00 17.65 ?  212  GLY A O   1 
ATOM   1599 N  N   . PHE A 1 211 ? 19.801  15.945  15.151  1.00 11.68 ?  213  PHE A N   1 
ATOM   1600 C  CA  . PHE A 1 211 ? 21.000  16.595  15.668  1.00 15.85 ?  213  PHE A CA  1 
ATOM   1601 C  C   . PHE A 1 211 ? 22.182  16.359  14.735  1.00 15.36 ?  213  PHE A C   1 
ATOM   1602 O  O   . PHE A 1 211 ? 22.498  15.209  14.408  1.00 10.54 ?  213  PHE A O   1 
ATOM   1603 C  CB  . PHE A 1 211 ? 21.343  16.071  17.060  1.00 16.39 ?  213  PHE A CB  1 
ATOM   1604 C  CG  . PHE A 1 211 ? 20.325  16.418  18.114  1.00 19.58 ?  213  PHE A CG  1 
ATOM   1605 C  CD1 . PHE A 1 211 ? 20.263  17.700  18.645  1.00 21.94 ?  213  PHE A CD1 1 
ATOM   1606 C  CD2 . PHE A 1 211 ? 19.445  15.460  18.580  1.00 15.68 ?  213  PHE A CD2 1 
ATOM   1607 C  CE1 . PHE A 1 211 ? 19.343  18.014  19.630  1.00 21.57 ?  213  PHE A CE1 1 
ATOM   1608 C  CE2 . PHE A 1 211 ? 18.524  15.764  19.565  1.00 20.82 ?  213  PHE A CE2 1 
ATOM   1609 C  CZ  . PHE A 1 211 ? 18.463  17.048  20.080  1.00 21.88 ?  213  PHE A CZ  1 
ATOM   1610 N  N   . LEU A 1 212 ? 22.846  17.447  14.328  1.00 13.12 ?  214  LEU A N   1 
ATOM   1611 C  CA  . LEU A 1 212 ? 24.071  17.371  13.542  1.00 10.93 ?  214  LEU A CA  1 
ATOM   1612 C  C   . LEU A 1 212 ? 25.226  17.965  14.338  1.00 15.05 ?  214  LEU A C   1 
ATOM   1613 O  O   . LEU A 1 212 ? 26.102  17.226  14.791  1.00 12.64 ?  214  LEU A O   1 
ATOM   1614 C  CB  . LEU A 1 212 ? 23.923  18.086  12.194  1.00 13.01 ?  214  LEU A CB  1 
ATOM   1615 C  CG  . LEU A 1 212 ? 22.916  17.473  11.214  1.00 10.84 ?  214  LEU A CG  1 
ATOM   1616 C  CD1 . LEU A 1 212 ? 22.916  18.280  9.933   1.00 13.01 ?  214  LEU A CD1 1 
ATOM   1617 C  CD2 . LEU A 1 212 ? 23.255  16.024  10.906  1.00 12.70 ?  214  LEU A CD2 1 
ATOM   1618 N  N   . GLU A 1 213 ? 25.249  19.282  14.519  1.00 14.04 ?  215  GLU A N   1 
ATOM   1619 C  CA  . GLU A 1 213 ? 26.270  19.889  15.368  1.00 13.66 ?  215  GLU A CA  1 
ATOM   1620 C  C   . GLU A 1 213 ? 26.182  19.303  16.771  1.00 17.32 ?  215  GLU A C   1 
ATOM   1621 O  O   . GLU A 1 213 ? 25.106  19.267  17.374  1.00 21.90 ?  215  GLU A O   1 
ATOM   1622 C  CB  . GLU A 1 213 ? 26.089  21.407  15.404  1.00 22.99 ?  215  GLU A CB  1 
ATOM   1623 N  N   . GLY A 1 214 ? 27.317  18.832  17.286  1.00 17.22 ?  216  GLY A N   1 
ATOM   1624 C  CA  . GLY A 1 214 ? 27.375  18.251  18.612  1.00 21.26 ?  216  GLY A CA  1 
ATOM   1625 C  C   . GLY A 1 214 ? 27.065  16.775  18.669  1.00 17.06 ?  216  GLY A C   1 
ATOM   1626 O  O   . GLY A 1 214 ? 27.308  16.147  19.709  1.00 18.20 ?  216  GLY A O   1 
ATOM   1627 N  N   . ASN A 1 215 ? 26.511  16.205  17.595  1.00 14.80 ?  217  ASN A N   1 
ATOM   1628 C  CA  . ASN A 1 215 ? 26.291  14.769  17.475  1.00 11.71 ?  217  ASN A CA  1 
ATOM   1629 C  C   . ASN A 1 215 ? 27.583  14.100  17.032  1.00 11.48 ?  217  ASN A C   1 
ATOM   1630 O  O   . ASN A 1 215 ? 28.006  14.287  15.885  1.00 10.33 ?  217  ASN A O   1 
ATOM   1631 C  CB  . ASN A 1 215 ? 25.159  14.487  16.469  1.00 9.25  ?  217  ASN A CB  1 
ATOM   1632 C  CG  . ASN A 1 215 ? 24.895  13.008  16.285  1.00 8.37  ?  217  ASN A CG  1 
ATOM   1633 O  OD1 . ASN A 1 215 ? 25.589  12.166  16.854  1.00 10.58 ?  217  ASN A OD1 1 
ATOM   1634 N  ND2 . ASN A 1 215 ? 23.925  12.683  15.434  1.00 10.61 ?  217  ASN A ND2 1 
ATOM   1635 N  N   . PRO A 1 216 ? 28.250  13.324  17.899  1.00 13.48 ?  218  PRO A N   1 
ATOM   1636 C  CA  . PRO A 1 216 ? 29.532  12.727  17.495  1.00 12.83 ?  218  PRO A CA  1 
ATOM   1637 C  C   . PRO A 1 216 ? 29.409  11.741  16.353  1.00 11.51 ?  218  PRO A C   1 
ATOM   1638 O  O   . PRO A 1 216 ? 30.404  11.501  15.657  1.00 11.89 ?  218  PRO A O   1 
ATOM   1639 C  CB  . PRO A 1 216 ? 30.021  12.035  18.779  1.00 16.20 ?  218  PRO A CB  1 
ATOM   1640 C  CG  . PRO A 1 216 ? 28.757  11.691  19.511  1.00 15.68 ?  218  PRO A CG  1 
ATOM   1641 C  CD  . PRO A 1 216 ? 27.806  12.843  19.222  1.00 14.25 ?  218  PRO A CD  1 
ATOM   1642 N  N   . VAL A 1 217 ? 28.227  11.153  16.144  1.00 10.11 ?  219  VAL A N   1 
ATOM   1643 C  CA  . VAL A 1 217 ? 28.023  10.266  14.997  1.00 10.90 ?  219  VAL A CA  1 
ATOM   1644 C  C   . VAL A 1 217 ? 28.194  11.042  13.694  1.00 11.40 ?  219  VAL A C   1 
ATOM   1645 O  O   . VAL A 1 217 ? 28.876  10.589  12.764  1.00 10.61 ?  219  VAL A O   1 
ATOM   1646 C  CB  . VAL A 1 217 ? 26.638  9.593   15.080  1.00 11.94 ?  219  VAL A CB  1 
ATOM   1647 C  CG1 . VAL A 1 217 ? 26.335  8.792   13.815  1.00 10.73 ?  219  VAL A CG1 1 
ATOM   1648 C  CG2 . VAL A 1 217 ? 26.534  8.680   16.335  1.00 12.70 ?  219  VAL A CG2 1 
ATOM   1649 N  N   . HIS A 1 218 ? 27.555  12.215  13.602  1.00 10.17 ?  220  HIS A N   1 
ATOM   1650 C  CA  . HIS A 1 218 ? 27.651  13.042  12.396  1.00 10.08 ?  220  HIS A CA  1 
ATOM   1651 C  C   . HIS A 1 218 ? 29.048  13.643  12.240  1.00 13.85 ?  220  HIS A C   1 
ATOM   1652 O  O   . HIS A 1 218 ? 29.578  13.722  11.120  1.00 11.25 ?  220  HIS A O   1 
ATOM   1653 C  CB  . HIS A 1 218 ? 26.583  14.154  12.437  1.00 11.26 ?  220  HIS A CB  1 
ATOM   1654 C  CG  . HIS A 1 218 ? 26.835  15.277  11.481  1.00 11.06 ?  220  HIS A CG  1 
ATOM   1655 N  ND1 . HIS A 1 218 ? 26.656  15.145  10.121  1.00 11.32 ?  220  HIS A ND1 1 
ATOM   1656 C  CD2 . HIS A 1 218 ? 27.269  16.545  11.681  1.00 11.26 ?  220  HIS A CD2 1 
ATOM   1657 C  CE1 . HIS A 1 218 ? 26.962  16.284  9.524   1.00 13.65 ?  220  HIS A CE1 1 
ATOM   1658 N  NE2 . HIS A 1 218 ? 27.344  17.148  10.448  1.00 11.61 ?  220  HIS A NE2 1 
ATOM   1659 N  N   . GLU A 1 219 ? 29.662  14.079  13.345  1.00 13.90 ?  221  GLU A N   1 
ATOM   1660 C  CA  . GLU A 1 219 ? 31.016  14.615  13.246  1.00 14.56 ?  221  GLU A CA  1 
ATOM   1661 C  C   . GLU A 1 219 ? 31.968  13.574  12.684  1.00 11.57 ?  221  GLU A C   1 
ATOM   1662 O  O   . GLU A 1 219 ? 32.796  13.881  11.821  1.00 12.14 ?  221  GLU A O   1 
ATOM   1663 C  CB  . GLU A 1 219 ? 31.485  15.121  14.612  1.00 16.45 ?  221  GLU A CB  1 
ATOM   1664 C  CG  . GLU A 1 219 ? 30.696  16.353  15.053  1.00 19.91 ?  221  GLU A CG  1 
ATOM   1665 C  CD  . GLU A 1 219 ? 30.816  16.661  16.534  1.00 26.50 ?  221  GLU A CD  1 
ATOM   1666 O  OE1 . GLU A 1 219 ? 31.450  15.877  17.284  1.00 28.02 ?  221  GLU A OE1 1 
ATOM   1667 O  OE2 . GLU A 1 219 ? 30.253  17.697  16.946  1.00 27.90 ?  221  GLU A OE2 1 
ATOM   1668 N  N   . GLU A 1 220 ? 31.796  12.319  13.089  1.00 10.44 ?  222  GLU A N   1 
ATOM   1669 C  CA  . GLU A 1 220 ? 32.751  11.287  12.720  1.00 13.37 ?  222  GLU A CA  1 
ATOM   1670 C  C   . GLU A 1 220 ? 32.479  10.767  11.304  1.00 10.01 ?  222  GLU A C   1 
ATOM   1671 O  O   . GLU A 1 220 ? 33.418  10.489  10.558  1.00 9.71  ?  222  GLU A O   1 
ATOM   1672 C  CB  . GLU A 1 220 ? 32.698  10.166  13.762  1.00 11.50 ?  222  GLU A CB  1 
ATOM   1673 C  CG  . GLU A 1 220 ? 33.767  9.080   13.669  1.00 11.28 ?  222  GLU A CG  1 
ATOM   1674 C  CD  . GLU A 1 220 ? 35.134  9.557   14.160  1.00 17.58 ?  222  GLU A CD  1 
ATOM   1675 O  OE1 . GLU A 1 220 ? 35.278  10.732  14.550  1.00 16.98 ?  222  GLU A OE1 1 
ATOM   1676 O  OE2 . GLU A 1 220 ? 36.063  8.741   14.165  1.00 16.62 ?  222  GLU A OE2 1 
ATOM   1677 N  N   . ASN A 1 221 ? 31.209  10.626  10.870  1.00 10.34 ?  223  ASN A N   1 
ATOM   1678 C  CA  . ASN A 1 221 ? 31.096  10.140  9.496   1.00 9.65  ?  223  ASN A CA  1 
ATOM   1679 C  C   . ASN A 1 221 ? 31.386  11.237  8.472   1.00 9.41  ?  223  ASN A C   1 
ATOM   1680 O  O   . ASN A 1 221 ? 31.830  10.930  7.361   1.00 8.71  ?  223  ASN A O   1 
ATOM   1681 C  CB  . ASN A 1 221 ? 29.747  9.411   9.266   1.00 10.41 ?  223  ASN A CB  1 
ATOM   1682 C  CG  . ASN A 1 221 ? 28.527  10.322  9.145   1.00 11.44 ?  223  ASN A CG  1 
ATOM   1683 O  OD1 . ASN A 1 221 ? 28.511  11.478  9.558   1.00 11.50 ?  223  ASN A OD1 1 
ATOM   1684 N  ND2 . ASN A 1 221 ? 27.452  9.748   8.586   1.00 9.55  ?  223  ASN A ND2 1 
ATOM   1685 N  N   . THR A 1 222 ? 31.228  12.510  8.841   1.00 10.94 ?  224  THR A N   1 
ATOM   1686 C  CA  . THR A 1 222 ? 31.693  13.587  7.971   1.00 13.56 ?  224  THR A CA  1 
ATOM   1687 C  C   . THR A 1 222 ? 33.212  13.536  7.807   1.00 13.12 ?  224  THR A C   1 
ATOM   1688 O  O   . THR A 1 222 ? 33.731  13.677  6.695   1.00 12.38 ?  224  THR A O   1 
ATOM   1689 C  CB  . THR A 1 222 ? 31.254  14.941  8.538   1.00 12.10 ?  224  THR A CB  1 
ATOM   1690 O  OG1 . THR A 1 222 ? 29.821  14.992  8.566   1.00 15.94 ?  224  THR A OG1 1 
ATOM   1691 C  CG2 . THR A 1 222 ? 31.755  16.089  7.661   1.00 15.01 ?  224  THR A CG2 1 
ATOM   1692 N  N   . ARG A 1 223 ? 33.932  13.318  8.906   1.00 10.73 ?  225  ARG A N   1 
ATOM   1693 C  CA  . ARG A 1 223 ? 35.388  13.257  8.849   1.00 13.47 ?  225  ARG A CA  1 
ATOM   1694 C  C   . ARG A 1 223 ? 35.851  12.072  8.010   1.00 14.48 ?  225  ARG A C   1 
ATOM   1695 O  O   . ARG A 1 223 ? 36.727  12.205  7.150   1.00 11.62 ?  225  ARG A O   1 
ATOM   1696 C  CB  . ARG A 1 223 ? 35.945  13.170  10.267  1.00 13.54 ?  225  ARG A CB  1 
ATOM   1697 C  CG  . ARG A 1 223 ? 37.354  12.690  10.364  1.00 20.91 ?  225  ARG A CG  1 
ATOM   1698 C  CD  . ARG A 1 223 ? 37.866  12.749  11.816  1.00 23.92 ?  225  ARG A CD  1 
ATOM   1699 N  NE  . ARG A 1 223 ? 37.879  14.101  12.364  1.00 25.63 ?  225  ARG A NE  1 
ATOM   1700 C  CZ  . ARG A 1 223 ? 38.928  14.917  12.303  1.00 32.76 ?  225  ARG A CZ  1 
ATOM   1701 N  NH1 . ARG A 1 223 ? 40.041  14.524  11.696  1.00 25.68 ?  225  ARG A NH1 1 
ATOM   1702 N  NH2 . ARG A 1 223 ? 38.863  16.134  12.834  1.00 34.62 ?  225  ARG A NH2 1 
ATOM   1703 N  N   . ILE A 1 224 ? 35.255  10.903  8.237   1.00 10.59 ?  226  ILE A N   1 
ATOM   1704 C  CA  . ILE A 1 224 ? 35.632  9.711   7.487   1.00 7.94  ?  226  ILE A CA  1 
ATOM   1705 C  C   . ILE A 1 224 ? 35.309  9.872   6.008   1.00 12.97 ?  226  ILE A C   1 
ATOM   1706 O  O   . ILE A 1 224 ? 36.108  9.499   5.142   1.00 13.50 ?  226  ILE A O   1 
ATOM   1707 C  CB  . ILE A 1 224 ? 34.948  8.482   8.113   1.00 11.77 ?  226  ILE A CB  1 
ATOM   1708 C  CG1 . ILE A 1 224 ? 35.608  8.172   9.460   1.00 13.63 ?  226  ILE A CG1 1 
ATOM   1709 C  CG2 . ILE A 1 224 ? 35.054  7.255   7.200   1.00 13.87 ?  226  ILE A CG2 1 
ATOM   1710 C  CD1 . ILE A 1 224 ? 34.887  7.109   10.246  1.00 11.61 ?  226  ILE A CD1 1 
ATOM   1711 N  N   . ALA A 1 225 ? 34.133  10.432  5.683   1.00 13.20 ?  227  ALA A N   1 
ATOM   1712 C  CA  . ALA A 1 225 ? 33.785  10.625  4.281   1.00 12.17 ?  227  ALA A CA  1 
ATOM   1713 C  C   . ALA A 1 225 ? 34.774  11.565  3.593   1.00 11.69 ?  227  ALA A C   1 
ATOM   1714 O  O   . ALA A 1 225 ? 35.137  11.355  2.428   1.00 13.06 ?  227  ALA A O   1 
ATOM   1715 C  CB  . ALA A 1 225 ? 32.356  11.162  4.159   1.00 13.21 ?  227  ALA A CB  1 
ATOM   1716 N  N   . ARG A 1 226 ? 35.255  12.580  4.312   1.00 13.56 ?  228  ARG A N   1 
ATOM   1717 C  CA  . ARG A 1 226 ? 36.208  13.520  3.724   1.00 13.62 ?  228  ARG A CA  1 
ATOM   1718 C  C   . ARG A 1 226 ? 37.598  12.906  3.554   1.00 13.90 ?  228  ARG A C   1 
ATOM   1719 O  O   . ARG A 1 226 ? 38.360  13.357  2.692   1.00 15.66 ?  228  ARG A O   1 
ATOM   1720 C  CB  . ARG A 1 226 ? 36.289  14.793  4.569   1.00 17.27 ?  228  ARG A CB  1 
ATOM   1721 C  CG  . ARG A 1 226 ? 35.183  15.826  4.273   1.00 18.22 ?  228  ARG A CG  1 
ATOM   1722 C  CD  . ARG A 1 226 ? 35.464  16.668  2.982   1.00 26.34 ?  228  ARG A CD  1 
ATOM   1723 N  NE  . ARG A 1 226 ? 34.421  17.675  2.733   1.00 29.21 ?  228  ARG A NE  1 
ATOM   1724 C  CZ  . ARG A 1 226 ? 33.911  17.987  1.538   1.00 37.05 ?  228  ARG A CZ  1 
ATOM   1725 N  NH1 . ARG A 1 226 ? 34.356  17.392  0.434   1.00 25.36 ?  228  ARG A NH1 1 
ATOM   1726 N  NH2 . ARG A 1 226 ? 32.961  18.920  1.442   1.00 23.68 ?  228  ARG A NH2 1 
ATOM   1727 N  N   . MET A 1 227 ? 37.958  11.891  4.347   1.00 12.66 ?  229  MET A N   1 
ATOM   1728 C  CA  . MET A 1 227 ? 39.201  11.187  4.028   1.00 11.15 ?  229  MET A CA  1 
ATOM   1729 C  C   . MET A 1 227 ? 39.110  10.347  2.761   1.00 16.29 ?  229  MET A C   1 
ATOM   1730 O  O   . MET A 1 227 ? 40.145  10.105  2.131   1.00 15.44 ?  229  MET A O   1 
ATOM   1731 C  CB  . MET A 1 227 ? 39.738  10.307  5.169   1.00 21.22 ?  229  MET A CB  1 
ATOM   1732 C  CG  . MET A 1 227 ? 39.890  10.913  6.587   1.00 16.06 ?  229  MET A CG  1 
ATOM   1733 S  SD  . MET A 1 227 ? 39.551  9.782   7.966   1.00 19.57 ?  229  MET A SD  1 
ATOM   1734 C  CE  . MET A 1 227 ? 40.996  8.750   7.811   1.00 16.06 ?  229  MET A CE  1 
ATOM   1735 N  N   . ALA A 1 228 ? 37.914  9.896   2.371   1.00 13.80 ?  230  ALA A N   1 
ATOM   1736 C  CA  . ALA A 1 228 ? 37.748  9.231   1.082   1.00 15.69 ?  230  ALA A CA  1 
ATOM   1737 C  C   . ALA A 1 228 ? 37.573  10.231  -0.045  1.00 16.87 ?  230  ALA A C   1 
ATOM   1738 O  O   . ALA A 1 228 ? 38.066  10.003  -1.156  1.00 17.12 ?  230  ALA A O   1 
ATOM   1739 C  CB  . ALA A 1 228 ? 36.535  8.294   1.099   1.00 16.57 ?  230  ALA A CB  1 
ATOM   1740 N  N   . GLY A 1 229 ? 36.878  11.326  0.225   1.00 11.84 ?  231  GLY A N   1 
ATOM   1741 C  CA  . GLY A 1 229 ? 36.532  12.294  -0.785  1.00 15.14 ?  231  GLY A CA  1 
ATOM   1742 C  C   . GLY A 1 229 ? 35.213  11.967  -1.457  1.00 12.36 ?  231  GLY A C   1 
ATOM   1743 O  O   . GLY A 1 229 ? 34.722  10.841  -1.425  1.00 11.29 ?  231  GLY A O   1 
ATOM   1744 N  N   . CYS A 1 230 ? 34.641  12.993  -2.062  1.00 9.69  ?  232  CYS A N   1 
ATOM   1745 C  CA  . CYS A 1 230 ? 33.445  12.851  -2.882  1.00 11.75 ?  232  CYS A CA  1 
ATOM   1746 C  C   . CYS A 1 230 ? 33.400  14.101  -3.730  1.00 18.52 ?  232  CYS A C   1 
ATOM   1747 O  O   . CYS A 1 230 ? 33.379  15.208  -3.182  1.00 21.87 ?  232  CYS A O   1 
ATOM   1748 C  CB  . CYS A 1 230 ? 32.181  12.720  -2.037  1.00 13.19 ?  232  CYS A CB  1 
ATOM   1749 S  SG  . CYS A 1 230 ? 30.740  12.394  -3.081  1.00 19.37 ?  232  CYS A SG  1 
ATOM   1750 N  N   . ASP A 1 231 ? 33.440  13.932  -5.049  1.00 10.63 ?  233  ASP A N   1 
ATOM   1751 C  CA  . ASP A 1 231 ? 33.505  15.089  -5.920  1.00 12.84 ?  233  ASP A CA  1 
ATOM   1752 C  C   . ASP A 1 231 ? 32.156  15.781  -6.075  1.00 13.12 ?  233  ASP A C   1 
ATOM   1753 O  O   . ASP A 1 231 ? 32.119  17.000  -6.263  1.00 12.94 ?  233  ASP A O   1 
ATOM   1754 C  CB  . ASP A 1 231 ? 34.077  14.671  -7.273  1.00 13.37 ?  233  ASP A CB  1 
ATOM   1755 C  CG  . ASP A 1 231 ? 35.497  14.119  -7.142  1.00 18.21 ?  233  ASP A CG  1 
ATOM   1756 O  OD1 . ASP A 1 231 ? 35.732  12.948  -7.518  1.00 17.58 ?  233  ASP A OD1 1 
ATOM   1757 O  OD2 . ASP A 1 231 ? 36.365  14.846  -6.599  1.00 21.38 ?  233  ASP A OD2 1 
ATOM   1758 N  N   . PHE A 1 232 ? 31.049  15.049  -5.966  1.00 8.15  ?  234  PHE A N   1 
ATOM   1759 C  CA  . PHE A 1 232 ? 29.759  15.633  -6.304  1.00 10.77 ?  234  PHE A CA  1 
ATOM   1760 C  C   . PHE A 1 232 ? 28.651  14.804  -5.670  1.00 10.90 ?  234  PHE A C   1 
ATOM   1761 O  O   . PHE A 1 232 ? 28.654  13.580  -5.809  1.00 10.51 ?  234  PHE A O   1 
ATOM   1762 C  CB  . PHE A 1 232 ? 29.596  15.661  -7.824  1.00 13.32 ?  234  PHE A CB  1 
ATOM   1763 C  CG  . PHE A 1 232 ? 28.582  16.643  -8.312  1.00 9.85  ?  234  PHE A CG  1 
ATOM   1764 C  CD1 . PHE A 1 232 ? 28.935  17.977  -8.534  1.00 11.10 ?  234  PHE A CD1 1 
ATOM   1765 C  CD2 . PHE A 1 232 ? 27.289  16.237  -8.584  1.00 13.81 ?  234  PHE A CD2 1 
ATOM   1766 C  CE1 . PHE A 1 232 ? 28.004  18.893  -8.997  1.00 13.65 ?  234  PHE A CE1 1 
ATOM   1767 C  CE2 . PHE A 1 232 ? 26.348  17.148  -9.049  1.00 14.72 ?  234  PHE A CE2 1 
ATOM   1768 C  CZ  . PHE A 1 232 ? 26.702  18.479  -9.257  1.00 13.22 ?  234  PHE A CZ  1 
ATOM   1769 N  N   . ILE A 1 233 ? 27.708  15.456  -4.985  1.00 9.73  ?  235  ILE A N   1 
ATOM   1770 C  CA  . ILE A 1 233 ? 26.513  14.753  -4.534  1.00 9.07  ?  235  ILE A CA  1 
ATOM   1771 C  C   . ILE A 1 233 ? 25.274  15.332  -5.208  1.00 9.86  ?  235  ILE A C   1 
ATOM   1772 O  O   . ILE A 1 233 ? 25.257  16.464  -5.681  1.00 8.82  ?  235  ILE A O   1 
ATOM   1773 C  CB  . ILE A 1 233 ? 26.351  14.786  -3.007  1.00 10.18 ?  235  ILE A CB  1 
ATOM   1774 C  CG1 . ILE A 1 233 ? 25.964  16.192  -2.517  1.00 12.53 ?  235  ILE A CG1 1 
ATOM   1775 C  CG2 . ILE A 1 233 ? 27.620  14.270  -2.344  1.00 9.36  ?  235  ILE A CG2 1 
ATOM   1776 C  CD1 . ILE A 1 233 ? 25.326  16.188  -1.072  1.00 10.95 ?  235  ILE A CD1 1 
ATOM   1777 N  N   . VAL A 1 234 ? 24.220  14.519  -5.241  1.00 8.09  ?  236  VAL A N   1 
ATOM   1778 C  CA  . VAL A 1 234 ? 22.870  14.959  -5.579  1.00 8.81  ?  236  VAL A CA  1 
ATOM   1779 C  C   . VAL A 1 234 ? 21.974  14.353  -4.513  1.00 8.78  ?  236  VAL A C   1 
ATOM   1780 O  O   . VAL A 1 234 ? 21.930  13.128  -4.372  1.00 10.12 ?  236  VAL A O   1 
ATOM   1781 C  CB  . VAL A 1 234 ? 22.411  14.515  -6.980  1.00 10.61 ?  236  VAL A CB  1 
ATOM   1782 C  CG1 . VAL A 1 234 ? 20.965  14.995  -7.237  1.00 10.45 ?  236  VAL A CG1 1 
ATOM   1783 C  CG2 . VAL A 1 234 ? 23.359  15.038  -8.092  1.00 11.57 ?  236  VAL A CG2 1 
ATOM   1784 N  N   . ASN A 1 235 ? 21.287  15.193  -3.744  1.00 9.12  ?  237  ASN A N   1 
ATOM   1785 C  CA  . ASN A 1 235 ? 20.372  14.708  -2.710  1.00 10.23 ?  237  ASN A CA  1 
ATOM   1786 C  C   . ASN A 1 235 ? 18.986  15.320  -2.904  1.00 7.75  ?  237  ASN A C   1 
ATOM   1787 O  O   . ASN A 1 235 ? 18.850  16.453  -3.379  1.00 9.66  ?  237  ASN A O   1 
ATOM   1788 C  CB  . ASN A 1 235 ? 20.851  15.060  -1.276  1.00 7.97  ?  237  ASN A CB  1 
ATOM   1789 C  CG  . ASN A 1 235 ? 21.970  14.157  -0.737  1.00 10.09 ?  237  ASN A CG  1 
ATOM   1790 O  OD1 . ASN A 1 235 ? 22.381  14.354  0.396   1.00 12.74 ?  237  ASN A OD1 1 
ATOM   1791 N  ND2 . ASN A 1 235 ? 22.489  13.215  -1.534  1.00 10.14 ?  237  ASN A ND2 1 
ATOM   1792 N  N   . VAL A 1 236 ? 17.947  14.576  -2.506  1.00 7.39  ?  238  VAL A N   1 
ATOM   1793 C  CA  . VAL A 1 236 ? 16.572  15.068  -2.570  1.00 7.00  ?  238  VAL A CA  1 
ATOM   1794 C  C   . VAL A 1 236 ? 15.904  14.953  -1.203  1.00 9.38  ?  238  VAL A C   1 
ATOM   1795 O  O   . VAL A 1 236 ? 16.342  14.209  -0.323  1.00 10.55 ?  238  VAL A O   1 
ATOM   1796 C  CB  . VAL A 1 236 ? 15.720  14.313  -3.625  1.00 10.03 ?  238  VAL A CB  1 
ATOM   1797 C  CG1 . VAL A 1 236 ? 16.310  14.498  -5.027  1.00 10.20 ?  238  VAL A CG1 1 
ATOM   1798 C  CG2 . VAL A 1 236 ? 15.622  12.829  -3.266  1.00 11.15 ?  238  VAL A CG2 1 
ATOM   1799 N  N   . THR A 1 237 ? 14.809  15.700  -1.041  1.00 10.70 ?  239  THR A N   1 
ATOM   1800 C  CA  . THR A 1 237 ? 13.845  15.503  0.030   1.00 7.50  ?  239  THR A CA  1 
ATOM   1801 C  C   . THR A 1 237 ? 12.504  15.104  -0.580  1.00 10.34 ?  239  THR A C   1 
ATOM   1802 O  O   . THR A 1 237 ? 12.185  15.507  -1.703  1.00 10.74 ?  239  THR A O   1 
ATOM   1803 C  CB  . THR A 1 237 ? 13.661  16.780  0.853   1.00 11.16 ?  239  THR A CB  1 
ATOM   1804 O  OG1 . THR A 1 237 ? 13.263  17.846  -0.023  1.00 12.87 ?  239  THR A OG1 1 
ATOM   1805 C  CG2 . THR A 1 237 ? 14.955  17.175  1.535   1.00 11.85 ?  239  THR A CG2 1 
ATOM   1806 N  N   . LEU A 1 238 ? 11.730  14.306  0.161   1.00 9.57  ?  240  LEU A N   1 
ATOM   1807 C  CA  . LEU A 1 238 ? 10.436  13.801  -0.287  1.00 9.76  ?  240  LEU A CA  1 
ATOM   1808 C  C   . LEU A 1 238 ? 9.350   14.208  0.695   1.00 13.47 ?  240  LEU A C   1 
ATOM   1809 O  O   . LEU A 1 238 ? 9.585   14.260  1.906   1.00 16.01 ?  240  LEU A O   1 
ATOM   1810 C  CB  . LEU A 1 238 ? 10.426  12.270  -0.401  1.00 10.78 ?  240  LEU A CB  1 
ATOM   1811 C  CG  . LEU A 1 238 ? 11.455  11.623  -1.317  1.00 11.52 ?  240  LEU A CG  1 
ATOM   1812 C  CD1 . LEU A 1 238 ? 11.416  10.097  -1.148  1.00 13.98 ?  240  LEU A CD1 1 
ATOM   1813 C  CD2 . LEU A 1 238 ? 11.210  12.021  -2.773  1.00 13.18 ?  240  LEU A CD2 1 
ATOM   1814 N  N   . ASP A 1 239 ? 8.141   14.459  0.177   1.00 14.93 ?  241  ASP A N   1 
ATOM   1815 C  CA  . ASP A 1 239 ? 7.025   14.723  1.074   1.00 11.07 ?  241  ASP A CA  1 
ATOM   1816 C  C   . ASP A 1 239 ? 6.342   13.401  1.428   1.00 13.64 ?  241  ASP A C   1 
ATOM   1817 O  O   . ASP A 1 239 ? 6.828   12.319  1.085   1.00 12.67 ?  241  ASP A O   1 
ATOM   1818 C  CB  . ASP A 1 239 ? 6.102   15.770  0.452   1.00 14.63 ?  241  ASP A CB  1 
ATOM   1819 C  CG  . ASP A 1 239 ? 5.300   15.255  -0.737  1.00 15.97 ?  241  ASP A CG  1 
ATOM   1820 O  OD1 . ASP A 1 239 ? 5.411   14.066  -1.110  1.00 18.12 ?  241  ASP A OD1 1 
ATOM   1821 O  OD2 . ASP A 1 239 ? 4.534   16.073  -1.314  1.00 22.80 ?  241  ASP A OD2 1 
ATOM   1822 N  N   . GLY A 1 240 ? 5.179   13.472  2.089   1.00 15.60 ?  242  GLY A N   1 
ATOM   1823 C  CA  . GLY A 1 240 ? 4.540   12.255  2.573   1.00 18.29 ?  242  GLY A CA  1 
ATOM   1824 C  C   . GLY A 1 240 ? 4.076   11.329  1.468   1.00 20.00 ?  242  GLY A C   1 
ATOM   1825 O  O   . GLY A 1 240 ? 4.041   10.106  1.650   1.00 20.98 ?  242  GLY A O   1 
ATOM   1826 N  N   . ALA A 1 241 ? 3.711   11.890  0.317   1.00 14.90 ?  243  ALA A N   1 
ATOM   1827 C  CA  . ALA A 1 241 ? 3.306   11.123  -0.847  1.00 16.74 ?  243  ALA A CA  1 
ATOM   1828 C  C   . ALA A 1 241 ? 4.495   10.748  -1.736  1.00 14.84 ?  243  ALA A C   1 
ATOM   1829 O  O   . ALA A 1 241 ? 4.293   10.292  -2.865  1.00 13.32 ?  243  ALA A O   1 
ATOM   1830 C  CB  . ALA A 1 241 ? 2.253   11.909  -1.643  1.00 21.11 ?  243  ALA A CB  1 
ATOM   1831 N  N   . ARG A 1 242 ? 5.727   10.916  -1.230  1.00 14.21 ?  244  ARG A N   1 
ATOM   1832 C  CA  . ARG A 1 242 ? 6.970   10.530  -1.906  1.00 15.41 ?  244  ARG A CA  1 
ATOM   1833 C  C   . ARG A 1 242 ? 7.224   11.351  -3.168  1.00 14.85 ?  244  ARG A C   1 
ATOM   1834 O  O   . ARG A 1 242 ? 7.856   10.877  -4.116  1.00 16.24 ?  244  ARG A O   1 
ATOM   1835 C  CB  . ARG A 1 242 ? 6.999   9.032   -2.235  1.00 17.98 ?  244  ARG A CB  1 
ATOM   1836 C  CG  . ARG A 1 242 ? 6.721   8.121   -1.056  1.00 15.39 ?  244  ARG A CG  1 
ATOM   1837 C  CD  . ARG A 1 242 ? 7.959   7.886   -0.218  1.00 19.59 ?  244  ARG A CD  1 
ATOM   1838 N  NE  . ARG A 1 242 ? 7.644   7.111   0.976   1.00 19.38 ?  244  ARG A NE  1 
ATOM   1839 C  CZ  . ARG A 1 242 ? 7.641   5.785   1.043   1.00 17.29 ?  244  ARG A CZ  1 
ATOM   1840 N  NH1 . ARG A 1 242 ? 7.946   5.051   -0.020  1.00 16.31 ?  244  ARG A NH1 1 
ATOM   1841 N  NH2 . ARG A 1 242 ? 7.325   5.198   2.189   1.00 13.66 ?  244  ARG A NH2 1 
ATOM   1842 N  N   . ARG A 1 243 ? 6.744   12.585  -3.197  1.00 11.11 ?  245  ARG A N   1 
ATOM   1843 C  CA  . ARG A 1 243 ? 7.111   13.501  -4.268  1.00 10.46 ?  245  ARG A CA  1 
ATOM   1844 C  C   . ARG A 1 243 ? 8.301   14.353  -3.840  1.00 11.72 ?  245  ARG A C   1 
ATOM   1845 O  O   . ARG A 1 243 ? 8.414   14.742  -2.673  1.00 10.95 ?  245  ARG A O   1 
ATOM   1846 C  CB  . ARG A 1 243 ? 5.925   14.380  -4.635  1.00 14.30 ?  245  ARG A CB  1 
ATOM   1847 C  CG  . ARG A 1 243 ? 4.742   13.516  -4.983  1.00 18.79 ?  245  ARG A CG  1 
ATOM   1848 C  CD  . ARG A 1 243 ? 3.480   14.289  -5.037  1.00 26.30 ?  245  ARG A CD  1 
ATOM   1849 N  NE  . ARG A 1 243 ? 3.178   14.985  -3.795  1.00 21.14 ?  245  ARG A NE  1 
ATOM   1850 C  CZ  . ARG A 1 243 ? 2.078   15.708  -3.633  1.00 20.52 ?  245  ARG A CZ  1 
ATOM   1851 N  NH1 . ARG A 1 243 ? 1.200   15.789  -4.627  1.00 21.32 ?  245  ARG A NH1 1 
ATOM   1852 N  NH2 . ARG A 1 243 ? 1.848   16.332  -2.492  1.00 16.60 ?  245  ARG A NH2 1 
ATOM   1853 N  N   . ILE A 1 244 ? 9.170   14.658  -4.799  1.00 8.43  ?  246  ILE A N   1 
ATOM   1854 C  CA  . ILE A 1 244 ? 10.398  15.399  -4.511  1.00 7.30  ?  246  ILE A CA  1 
ATOM   1855 C  C   . ILE A 1 244 ? 10.054  16.859  -4.221  1.00 9.75  ?  246  ILE A C   1 
ATOM   1856 O  O   . ILE A 1 244 ? 9.381   17.524  -5.017  1.00 11.07 ?  246  ILE A O   1 
ATOM   1857 C  CB  . ILE A 1 244 ? 11.381  15.272  -5.682  1.00 8.96  ?  246  ILE A CB  1 
ATOM   1858 C  CG1 . ILE A 1 244 ? 11.871  13.817  -5.810  1.00 10.51 ?  246  ILE A CG1 1 
ATOM   1859 C  CG2 . ILE A 1 244 ? 12.565  16.255  -5.535  1.00 8.91  ?  246  ILE A CG2 1 
ATOM   1860 C  CD1 . ILE A 1 244 ? 12.701  13.560  -7.090  1.00 11.92 ?  246  ILE A CD1 1 
ATOM   1861 N  N   . THR A 1 245 ? 10.524  17.371  -3.079  1.00 8.78  ?  247  THR A N   1 
ATOM   1862 C  CA  . THR A 1 245 ? 10.274  18.759  -2.689  1.00 8.74  ?  247  THR A CA  1 
ATOM   1863 C  C   . THR A 1 245 ? 11.526  19.630  -2.739  1.00 12.18 ?  247  THR A C   1 
ATOM   1864 O  O   . THR A 1 245 ? 11.415  20.860  -2.651  1.00 9.64  ?  247  THR A O   1 
ATOM   1865 C  CB  . THR A 1 245 ? 9.666   18.831  -1.272  1.00 9.24  ?  247  THR A CB  1 
ATOM   1866 O  OG1 . THR A 1 245 ? 10.480  18.083  -0.340  1.00 11.02 ?  247  THR A OG1 1 
ATOM   1867 C  CG2 . THR A 1 245 ? 8.246   18.273  -1.257  1.00 11.30 ?  247  THR A CG2 1 
ATOM   1868 N  N   . SER A 1 246 ? 12.709  19.036  -2.861  1.00 11.11 ?  248  SER A N   1 
ATOM   1869 C  CA  . SER A 1 246 ? 13.912  19.838  -3.066  1.00 12.52 ?  248  SER A CA  1 
ATOM   1870 C  C   . SER A 1 246 ? 15.006  18.967  -3.666  1.00 9.97  ?  248  SER A C   1 
ATOM   1871 O  O   . SER A 1 246 ? 15.023  17.746  -3.494  1.00 9.28  ?  248  SER A O   1 
ATOM   1872 C  CB  . SER A 1 246 ? 14.405  20.492  -1.770  1.00 13.51 ?  248  SER A CB  1 
ATOM   1873 O  OG  . SER A 1 246 ? 15.120  19.578  -0.954  1.00 14.05 ?  248  SER A OG  1 
ATOM   1874 N  N   . VAL A 1 247 ? 15.895  19.620  -4.409  1.00 9.13  ?  249  VAL A N   1 
ATOM   1875 C  CA  . VAL A 1 247 ? 17.101  19.009  -4.960  1.00 8.76  ?  249  VAL A CA  1 
ATOM   1876 C  C   . VAL A 1 247 ? 18.275  19.878  -4.545  1.00 9.84  ?  249  VAL A C   1 
ATOM   1877 O  O   . VAL A 1 247 ? 18.216  21.105  -4.695  1.00 11.57 ?  249  VAL A O   1 
ATOM   1878 C  CB  . VAL A 1 247 ? 17.038  18.900  -6.502  1.00 10.67 ?  249  VAL A CB  1 
ATOM   1879 C  CG1 . VAL A 1 247 ? 18.331  18.267  -7.048  1.00 10.57 ?  249  VAL A CG1 1 
ATOM   1880 C  CG2 . VAL A 1 247 ? 15.858  18.052  -6.918  1.00 11.19 ?  249  VAL A CG2 1 
ATOM   1881 N  N   . VAL A 1 248 ? 19.329  19.256  -4.009  1.00 8.63  ?  250  VAL A N   1 
ATOM   1882 C  CA  . VAL A 1 248 ? 20.603  19.935  -3.793  1.00 10.00 ?  250  VAL A CA  1 
ATOM   1883 C  C   . VAL A 1 248 ? 21.691  19.149  -4.511  1.00 11.58 ?  250  VAL A C   1 
ATOM   1884 O  O   . VAL A 1 248 ? 21.664  17.915  -4.549  1.00 12.18 ?  250  VAL A O   1 
ATOM   1885 C  CB  . VAL A 1 248 ? 20.972  20.113  -2.304  1.00 12.32 ?  250  VAL A CB  1 
ATOM   1886 C  CG1 . VAL A 1 248 ? 19.959  21.019  -1.611  1.00 13.94 ?  250  VAL A CG1 1 
ATOM   1887 C  CG2 . VAL A 1 248 ? 21.059  18.773  -1.595  1.00 11.98 ?  250  VAL A CG2 1 
ATOM   1888 N  N   . ALA A 1 249 ? 22.639  19.867  -5.097  1.00 11.27 ?  251  ALA A N   1 
ATOM   1889 C  CA  . ALA A 1 249 ? 23.733  19.217  -5.801  1.00 11.64 ?  251  ALA A CA  1 
ATOM   1890 C  C   . ALA A 1 249 ? 25.004  20.010  -5.575  1.00 10.25 ?  251  ALA A C   1 
ATOM   1891 O  O   . ALA A 1 249 ? 24.957  21.235  -5.452  1.00 10.01 ?  251  ALA A O   1 
ATOM   1892 C  CB  . ALA A 1 249 ? 23.448  19.102  -7.293  1.00 11.62 ?  251  ALA A CB  1 
ATOM   1893 N  N   . GLY A 1 250 ? 26.129  19.305  -5.519  1.00 9.35  ?  252  GLY A N   1 
ATOM   1894 C  CA  . GLY A 1 250 ? 27.418  19.975  -5.414  1.00 9.19  ?  252  GLY A CA  1 
ATOM   1895 C  C   . GLY A 1 250 ? 28.322  19.392  -4.347  1.00 9.03  ?  252  GLY A C   1 
ATOM   1896 O  O   . GLY A 1 250 ? 28.447  18.170  -4.217  1.00 9.92  ?  252  GLY A O   1 
ATOM   1897 N  N   . ASP A 1 251 ? 28.989  20.281  -3.609  1.00 9.65  ?  253  ASP A N   1 
ATOM   1898 C  CA  . ASP A 1 251 ? 29.923  19.878  -2.562  1.00 12.63 ?  253  ASP A CA  1 
ATOM   1899 C  C   . ASP A 1 251 ? 29.245  18.980  -1.534  1.00 10.60 ?  253  ASP A C   1 
ATOM   1900 O  O   . ASP A 1 251 ? 28.117  19.242  -1.109  1.00 11.07 ?  253  ASP A O   1 
ATOM   1901 C  CB  . ASP A 1 251 ? 30.478  21.116  -1.849  1.00 12.30 ?  253  ASP A CB  1 
ATOM   1902 C  CG  . ASP A 1 251 ? 31.391  20.757  -0.686  1.00 19.28 ?  253  ASP A CG  1 
ATOM   1903 O  OD1 . ASP A 1 251 ? 30.994  20.926  0.493   1.00 15.60 ?  253  ASP A OD1 1 
ATOM   1904 O  OD2 . ASP A 1 251 ? 32.526  20.329  -0.962  1.00 19.48 ?  253  ASP A OD2 1 
ATOM   1905 N  N   . MET A 1 252 ? 29.964  17.947  -1.089  1.00 10.91 ?  254  MET A N   1 
ATOM   1906 C  CA  . MET A 1 252 ? 29.341  16.948  -0.225  1.00 11.22 ?  254  MET A CA  1 
ATOM   1907 C  C   . MET A 1 252 ? 28.879  17.547  1.100   1.00 15.50 ?  254  MET A C   1 
ATOM   1908 O  O   . MET A 1 252 ? 27.815  17.179  1.608   1.00 11.86 ?  254  MET A O   1 
ATOM   1909 C  CB  . MET A 1 252 ? 30.294  15.752  -0.050  1.00 14.86 ?  254  MET A CB  1 
ATOM   1910 C  CG  . MET A 1 252 ? 29.797  14.605  0.823   1.00 14.21 ?  254  MET A CG  1 
ATOM   1911 S  SD  . MET A 1 252 ? 31.159  13.691  1.591   1.00 17.31 ?  254  MET A SD  1 
ATOM   1912 C  CE  . MET A 1 252 ? 31.802  14.887  2.782   1.00 20.70 ?  254  MET A CE  1 
ATOM   1913 N  N   . GLU A 1 253 ? 29.622  18.508  1.660   1.00 11.28 ?  255  GLU A N   1 
ATOM   1914 C  CA  . GLU A 1 253 ? 29.097  19.099  2.891   1.00 13.28 ?  255  GLU A CA  1 
ATOM   1915 C  C   . GLU A 1 253 ? 28.162  20.284  2.658   1.00 14.02 ?  255  GLU A C   1 
ATOM   1916 O  O   . GLU A 1 253 ? 27.128  20.383  3.329   1.00 15.87 ?  255  GLU A O   1 
ATOM   1917 C  CB  . GLU A 1 253 ? 30.232  19.513  3.837   1.00 14.69 ?  255  GLU A CB  1 
ATOM   1918 C  CG  . GLU A 1 253 ? 31.163  18.363  4.192   1.00 15.54 ?  255  GLU A CG  1 
ATOM   1919 C  CD  . GLU A 1 253 ? 32.342  18.822  5.044   1.00 23.46 ?  255  GLU A CD  1 
ATOM   1920 O  OE1 . GLU A 1 253 ? 32.111  19.379  6.138   1.00 23.38 ?  255  GLU A OE1 1 
ATOM   1921 O  OE2 . GLU A 1 253 ? 33.490  18.622  4.618   1.00 34.02 ?  255  GLU A OE2 1 
ATOM   1922 N  N   . GLN A 1 254 ? 28.476  21.184  1.725   1.00 10.83 ?  256  GLN A N   1 
ATOM   1923 C  CA  . GLN A 1 254 ? 27.659  22.390  1.590   1.00 13.26 ?  256  GLN A CA  1 
ATOM   1924 C  C   . GLN A 1 254 ? 26.285  22.071  1.020   1.00 14.84 ?  256  GLN A C   1 
ATOM   1925 O  O   . GLN A 1 254 ? 25.282  22.665  1.437   1.00 13.75 ?  256  GLN A O   1 
ATOM   1926 C  CB  . GLN A 1 254 ? 28.354  23.416  0.697   1.00 18.83 ?  256  GLN A CB  1 
ATOM   1927 C  CG  . GLN A 1 254 ? 29.599  24.040  1.297   1.00 20.02 ?  256  GLN A CG  1 
ATOM   1928 C  CD  . GLN A 1 254 ? 30.427  24.742  0.239   1.00 25.49 ?  256  GLN A CD  1 
ATOM   1929 O  OE1 . GLN A 1 254 ? 31.598  24.409  0.012   1.00 31.32 ?  256  GLN A OE1 1 
ATOM   1930 N  NE2 . GLN A 1 254 ? 29.804  25.689  -0.451  1.00 22.62 ?  256  GLN A NE2 1 
ATOM   1931 N  N   . ALA A 1 255 ? 26.221  21.163  0.043   1.00 10.87 ?  257  ALA A N   1 
ATOM   1932 C  CA  . ALA A 1 255 ? 24.924  20.831  -0.538  1.00 9.36  ?  257  ALA A CA  1 
ATOM   1933 C  C   . ALA A 1 255 ? 24.076  20.071  0.472   1.00 9.65  ?  257  ALA A C   1 
ATOM   1934 O  O   . ALA A 1 255 ? 22.879  20.347  0.624   1.00 12.40 ?  257  ALA A O   1 
ATOM   1935 C  CB  . ALA A 1 255 ? 25.103  20.030  -1.838  1.00 11.30 ?  257  ALA A CB  1 
ATOM   1936 N  N   . PHE A 1 256 ? 24.698  19.155  1.215   1.00 10.02 ?  258  PHE A N   1 
ATOM   1937 C  CA  . PHE A 1 256 ? 23.979  18.434  2.258   1.00 8.86  ?  258  PHE A CA  1 
ATOM   1938 C  C   . PHE A 1 256 ? 23.362  19.408  3.252   1.00 11.14 ?  258  PHE A C   1 
ATOM   1939 O  O   . PHE A 1 256 ? 22.160  19.361  3.516   1.00 13.35 ?  258  PHE A O   1 
ATOM   1940 C  CB  . PHE A 1 256 ? 24.927  17.453  2.952   1.00 9.69  ?  258  PHE A CB  1 
ATOM   1941 C  CG  . PHE A 1 256 ? 24.346  16.777  4.169   1.00 10.34 ?  258  PHE A CG  1 
ATOM   1942 C  CD1 . PHE A 1 256 ? 23.309  15.864  4.040   1.00 8.17  ?  258  PHE A CD1 1 
ATOM   1943 C  CD2 . PHE A 1 256 ? 24.863  17.024  5.439   1.00 10.66 ?  258  PHE A CD2 1 
ATOM   1944 C  CE1 . PHE A 1 256 ? 22.788  15.216  5.145   1.00 9.21  ?  258  PHE A CE1 1 
ATOM   1945 C  CE2 . PHE A 1 256 ? 24.347  16.364  6.558   1.00 11.34 ?  258  PHE A CE2 1 
ATOM   1946 C  CZ  . PHE A 1 256 ? 23.299  15.459  6.395   1.00 8.42  ?  258  PHE A CZ  1 
ATOM   1947 N  N   . LEU A 1 257 ? 24.159  20.343  3.762   1.00 11.32 ?  259  LEU A N   1 
ATOM   1948 C  CA  . LEU A 1 257 ? 23.672  21.248  4.795   1.00 12.27 ?  259  LEU A CA  1 
ATOM   1949 C  C   . LEU A 1 257 ? 22.574  22.168  4.279   1.00 12.24 ?  259  LEU A C   1 
ATOM   1950 O  O   . LEU A 1 257 ? 21.673  22.548  5.039   1.00 12.03 ?  259  LEU A O   1 
ATOM   1951 C  CB  . LEU A 1 257 ? 24.836  22.055  5.349   1.00 12.35 ?  259  LEU A CB  1 
ATOM   1952 C  CG  . LEU A 1 257 ? 25.797  21.238  6.221   1.00 14.85 ?  259  LEU A CG  1 
ATOM   1953 C  CD1 . LEU A 1 257 ? 26.911  22.130  6.729   1.00 20.43 ?  259  LEU A CD1 1 
ATOM   1954 C  CD2 . LEU A 1 257 ? 25.117  20.564  7.396   1.00 13.28 ?  259  LEU A CD2 1 
ATOM   1955 N  N   . LYS A 1 258 ? 22.621  22.536  3.002   1.00 8.94  ?  260  LYS A N   1 
ATOM   1956 C  CA  . LYS A 1 258 ? 21.507  23.275  2.416   1.00 10.20 ?  260  LYS A CA  1 
ATOM   1957 C  C   . LYS A 1 258 ? 20.241  22.425  2.358   1.00 12.87 ?  260  LYS A C   1 
ATOM   1958 O  O   . LYS A 1 258 ? 19.133  22.920  2.616   1.00 11.80 ?  260  LYS A O   1 
ATOM   1959 C  CB  . LYS A 1 258 ? 21.894  23.760  1.020   1.00 10.69 ?  260  LYS A CB  1 
ATOM   1960 N  N   . GLY A 1 259 ? 20.377  21.152  1.995   1.00 9.27  ?  261  GLY A N   1 
ATOM   1961 C  CA  . GLY A 1 259 ? 19.221  20.265  2.007   1.00 10.57 ?  261  GLY A CA  1 
ATOM   1962 C  C   . GLY A 1 259 ? 18.643  20.094  3.400   1.00 9.65  ?  261  GLY A C   1 
ATOM   1963 O  O   . GLY A 1 259 ? 17.424  20.084  3.581   1.00 9.91  ?  261  GLY A O   1 
ATOM   1964 N  N   . VAL A 1 260 ? 19.518  19.989  4.408   1.00 8.57  ?  262  VAL A N   1 
ATOM   1965 C  CA  . VAL A 1 260 ? 19.065  19.848  5.788   1.00 7.87  ?  262  VAL A CA  1 
ATOM   1966 C  C   . VAL A 1 260 ? 18.338  21.107  6.247   1.00 11.69 ?  262  VAL A C   1 
ATOM   1967 O  O   . VAL A 1 260 ? 17.291  21.031  6.908   1.00 12.48 ?  262  VAL A O   1 
ATOM   1968 C  CB  . VAL A 1 260 ? 20.258  19.511  6.700   1.00 12.85 ?  262  VAL A CB  1 
ATOM   1969 C  CG1 . VAL A 1 260 ? 19.884  19.725  8.173   1.00 13.04 ?  262  VAL A CG1 1 
ATOM   1970 C  CG2 . VAL A 1 260 ? 20.673  18.081  6.460   1.00 10.49 ?  262  VAL A CG2 1 
ATOM   1971 N  N   . ALA A 1 261 ? 18.873  22.282  5.899   1.00 9.73  ?  263  ALA A N   1 
ATOM   1972 C  CA  . ALA A 1 261 ? 18.214  23.531  6.263   1.00 12.14 ?  263  ALA A CA  1 
ATOM   1973 C  C   . ALA A 1 261 ? 16.776  23.569  5.745   1.00 16.38 ?  263  ALA A C   1 
ATOM   1974 O  O   . ALA A 1 261 ? 15.867  24.029  6.451   1.00 18.03 ?  263  ALA A O   1 
ATOM   1975 C  CB  . ALA A 1 261 ? 19.015  24.723  5.727   1.00 15.32 ?  263  ALA A CB  1 
ATOM   1976 N  N   . PHE A 1 262 ? 16.542  23.076  4.527   1.00 12.67 ?  264  PHE A N   1 
ATOM   1977 C  CA  . PHE A 1 262 ? 15.165  22.997  4.030   1.00 13.35 ?  264  PHE A CA  1 
ATOM   1978 C  C   . PHE A 1 262 ? 14.352  21.951  4.791   1.00 14.76 ?  264  PHE A C   1 
ATOM   1979 O  O   . PHE A 1 262 ? 13.224  22.221  5.215   1.00 13.83 ?  264  PHE A O   1 
ATOM   1980 C  CB  . PHE A 1 262 ? 15.146  22.681  2.538   1.00 12.27 ?  264  PHE A CB  1 
ATOM   1981 C  CG  . PHE A 1 262 ? 13.775  22.445  2.009   1.00 15.45 ?  264  PHE A CG  1 
ATOM   1982 C  CD1 . PHE A 1 262 ? 12.903  23.505  1.821   1.00 17.56 ?  264  PHE A CD1 1 
ATOM   1983 C  CD2 . PHE A 1 262 ? 13.331  21.160  1.754   1.00 12.05 ?  264  PHE A CD2 1 
ATOM   1984 C  CE1 . PHE A 1 262 ? 11.621  23.287  1.340   1.00 23.46 ?  264  PHE A CE1 1 
ATOM   1985 C  CE2 . PHE A 1 262 ? 12.041  20.931  1.277   1.00 16.41 ?  264  PHE A CE2 1 
ATOM   1986 C  CZ  . PHE A 1 262 ? 11.194  21.999  1.063   1.00 19.08 ?  264  PHE A CZ  1 
ATOM   1987 N  N   . VAL A 1 263 ? 14.899  20.741  4.969   1.00 13.29 ?  265  VAL A N   1 
ATOM   1988 C  CA  . VAL A 1 263 ? 14.076  19.676  5.540   1.00 12.34 ?  265  VAL A CA  1 
ATOM   1989 C  C   . VAL A 1 263 ? 13.715  20.013  6.981   1.00 13.16 ?  265  VAL A C   1 
ATOM   1990 O  O   . VAL A 1 263 ? 12.630  19.665  7.459   1.00 13.80 ?  265  VAL A O   1 
ATOM   1991 C  CB  . VAL A 1 263 ? 14.785  18.308  5.433   1.00 15.06 ?  265  VAL A CB  1 
ATOM   1992 C  CG1 . VAL A 1 263 ? 15.892  18.167  6.443   1.00 18.78 ?  265  VAL A CG1 1 
ATOM   1993 C  CG2 . VAL A 1 263 ? 13.779  17.159  5.528   1.00 22.45 ?  265  VAL A CG2 1 
ATOM   1994 N  N   . GLU A 1 264 ? 14.598  20.714  7.691   1.00 11.70 ?  266  GLU A N   1 
ATOM   1995 C  CA  . GLU A 1 264 ? 14.276  21.138  9.048   1.00 12.51 ?  266  GLU A CA  1 
ATOM   1996 C  C   . GLU A 1 264 ? 13.048  22.033  9.115   1.00 15.49 ?  266  GLU A C   1 
ATOM   1997 O  O   . GLU A 1 264 ? 12.401  22.090  10.163  1.00 19.78 ?  266  GLU A O   1 
ATOM   1998 C  CB  . GLU A 1 264 ? 15.470  21.859  9.663   1.00 16.04 ?  266  GLU A CB  1 
ATOM   1999 C  CG  . GLU A 1 264 ? 16.440  20.932  10.300  1.00 20.24 ?  266  GLU A CG  1 
ATOM   2000 C  CD  . GLU A 1 264 ? 17.656  21.671  10.802  1.00 29.38 ?  266  GLU A CD  1 
ATOM   2001 O  OE1 . GLU A 1 264 ? 17.734  22.899  10.562  1.00 30.81 ?  266  GLU A OE1 1 
ATOM   2002 O  OE2 . GLU A 1 264 ? 18.491  21.040  11.479  1.00 36.99 ?  266  GLU A OE2 1 
ATOM   2003 N  N   . THR A 1 265 ? 12.711  22.741  8.034   1.00 18.07 ?  267  THR A N   1 
ATOM   2004 C  CA  . THR A 1 265 ? 11.532  23.606  8.054   1.00 15.72 ?  267  THR A CA  1 
ATOM   2005 C  C   . THR A 1 265 ? 10.231  22.869  7.778   1.00 22.64 ?  267  THR A C   1 
ATOM   2006 O  O   . THR A 1 265 ? 9.165   23.498  7.807   1.00 17.56 ?  267  THR A O   1 
ATOM   2007 C  CB  . THR A 1 265 ? 11.661  24.748  7.038   1.00 17.16 ?  267  THR A CB  1 
ATOM   2008 O  OG1 . THR A 1 265 ? 11.460  24.241  5.711   1.00 18.55 ?  267  THR A OG1 1 
ATOM   2009 C  CG2 . THR A 1 265 ? 13.022  25.444  7.143   1.00 23.08 ?  267  THR A CG2 1 
ATOM   2010 N  N   . VAL A 1 266 ? 10.274  21.578  7.460   1.00 12.41 ?  268  VAL A N   1 
ATOM   2011 C  CA  . VAL A 1 266 ? 9.036   20.853  7.193   1.00 13.54 ?  268  VAL A CA  1 
ATOM   2012 C  C   . VAL A 1 266 ? 8.884   19.599  8.034   1.00 15.10 ?  268  VAL A C   1 
ATOM   2013 O  O   . VAL A 1 266 ? 7.747   19.134  8.222   1.00 13.34 ?  268  VAL A O   1 
ATOM   2014 C  CB  . VAL A 1 266 ? 8.908   20.502  5.687   1.00 23.97 ?  268  VAL A CB  1 
ATOM   2015 C  CG1 . VAL A 1 266 ? 8.968   21.751  4.832   1.00 20.47 ?  268  VAL A CG1 1 
ATOM   2016 C  CG2 . VAL A 1 266 ? 9.958   19.500  5.243   1.00 17.42 ?  268  VAL A CG2 1 
ATOM   2017 N  N   . VAL A 1 267 ? 9.958   19.008  8.571   1.00 12.97 ?  269  VAL A N   1 
ATOM   2018 C  CA  A VAL A 1 267 ? 9.799   17.695  9.201   0.56 14.71 ?  269  VAL A CA  1 
ATOM   2019 C  CA  B VAL A 1 267 ? 9.841   17.700  9.207   0.44 14.70 ?  269  VAL A CA  1 
ATOM   2020 C  C   . VAL A 1 267 ? 9.333   17.779  10.644  1.00 11.37 ?  269  VAL A C   1 
ATOM   2021 O  O   . VAL A 1 267 ? 8.833   16.779  11.169  1.00 12.17 ?  269  VAL A O   1 
ATOM   2022 C  CB  A VAL A 1 267 ? 11.075  16.832  9.197   0.56 13.86 ?  269  VAL A CB  1 
ATOM   2023 C  CB  B VAL A 1 267 ? 11.197  16.973  9.155   0.44 13.84 ?  269  VAL A CB  1 
ATOM   2024 C  CG1 A VAL A 1 267 ? 11.307  16.206  7.826   0.56 11.48 ?  269  VAL A CG1 1 
ATOM   2025 C  CG1 B VAL A 1 267 ? 12.109  17.439  10.293  0.44 14.68 ?  269  VAL A CG1 1 
ATOM   2026 C  CG2 A VAL A 1 267 ? 12.284  17.620  9.714   0.56 15.10 ?  269  VAL A CG2 1 
ATOM   2027 C  CG2 B VAL A 1 267 ? 10.991  15.473  9.193   0.44 12.88 ?  269  VAL A CG2 1 
ATOM   2028 N  N   . LYS A 1 268 ? 9.467   18.927  11.300  1.00 11.25 ?  270  LYS A N   1 
ATOM   2029 C  CA  . LYS A 1 268 ? 9.086   19.024  12.704  1.00 13.97 ?  270  LYS A CA  1 
ATOM   2030 C  C   . LYS A 1 268 ? 7.571   19.150  12.858  1.00 14.71 ?  270  LYS A C   1 
ATOM   2031 O  O   . LYS A 1 268 ? 6.918   19.899  12.127  1.00 15.72 ?  270  LYS A O   1 
ATOM   2032 C  CB  . LYS A 1 268 ? 9.798   20.208  13.366  1.00 18.12 ?  270  LYS A CB  1 
ATOM   2033 C  CG  . LYS A 1 268 ? 11.308  20.128  13.241  1.00 22.49 ?  270  LYS A CG  1 
ATOM   2034 C  CD  . LYS A 1 268 ? 12.035  20.636  14.492  1.00 25.95 ?  270  LYS A CD  1 
ATOM   2035 C  CE  . LYS A 1 268 ? 13.508  20.241  14.447  1.00 32.72 ?  270  LYS A CE  1 
ATOM   2036 N  NZ  . LYS A 1 268 ? 14.240  20.635  15.692  1.00 39.81 ?  270  LYS A NZ  1 
ATOM   2037 N  N   . ALA A 1 269 ? 7.012   18.387  13.796  1.00 15.55 ?  271  ALA A N   1 
ATOM   2038 C  CA  . ALA A 1 269 ? 5.591   18.442  14.125  1.00 17.04 ?  271  ALA A CA  1 
ATOM   2039 C  C   . ALA A 1 269 ? 5.471   18.426  15.642  1.00 14.88 ?  271  ALA A C   1 
ATOM   2040 O  O   . ALA A 1 269 ? 5.993   17.519  16.291  1.00 15.51 ?  271  ALA A O   1 
ATOM   2041 C  CB  . ALA A 1 269 ? 4.837   17.262  13.507  1.00 17.78 ?  271  ALA A CB  1 
ATOM   2042 N  N   . ALA A 1 270 ? 4.797   19.415  16.219  1.00 16.27 ?  272  ALA A N   1 
ATOM   2043 C  CA  . ALA A 1 270 ? 4.864   19.614  17.661  1.00 19.73 ?  272  ALA A CA  1 
ATOM   2044 C  C   . ALA A 1 270 ? 3.559   19.237  18.350  1.00 19.46 ?  272  ALA A C   1 
ATOM   2045 O  O   . ALA A 1 270 ? 2.471   19.363  17.779  1.00 22.65 ?  272  ALA A O   1 
ATOM   2046 C  CB  . ALA A 1 270 ? 5.217   21.067  18.004  1.00 21.17 ?  272  ALA A CB  1 
ATOM   2047 N  N   . VAL A 1 271 ? 3.692   18.770  19.585  1.00 17.29 ?  273  VAL A N   1 
ATOM   2048 C  CA  . VAL A 1 271 ? 2.567   18.587  20.501  1.00 19.82 ?  273  VAL A CA  1 
ATOM   2049 C  C   . VAL A 1 271 ? 2.800   19.508  21.691  1.00 18.61 ?  273  VAL A C   1 
ATOM   2050 O  O   . VAL A 1 271 ? 3.948   19.871  22.001  1.00 20.65 ?  273  VAL A O   1 
ATOM   2051 C  CB  . VAL A 1 271 ? 2.422   17.115  20.951  1.00 14.87 ?  273  VAL A CB  1 
ATOM   2052 C  CG1 . VAL A 1 271 ? 2.034   16.234  19.777  1.00 24.45 ?  273  VAL A CG1 1 
ATOM   2053 C  CG2 . VAL A 1 271 ? 3.698   16.618  21.608  1.00 16.59 ?  273  VAL A CG2 1 
ATOM   2054 N  N   . PRO A 1 272 ? 1.733   19.906  22.392  1.00 25.27 ?  274  PRO A N   1 
ATOM   2055 C  CA  . PRO A 1 272 ? 1.927   20.781  23.562  1.00 26.66 ?  274  PRO A CA  1 
ATOM   2056 C  C   . PRO A 1 272 ? 2.606   20.096  24.740  1.00 24.31 ?  274  PRO A C   1 
ATOM   2057 O  O   . PRO A 1 272 ? 3.288   20.768  25.526  1.00 26.07 ?  274  PRO A O   1 
ATOM   2058 C  CB  . PRO A 1 272 ? 0.500   21.226  23.909  1.00 27.10 ?  274  PRO A CB  1 
ATOM   2059 C  CG  . PRO A 1 272 ? -0.397  20.245  23.238  1.00 24.93 ?  274  PRO A CG  1 
ATOM   2060 C  CD  . PRO A 1 272 ? 0.318   19.797  22.003  1.00 22.50 ?  274  PRO A CD  1 
ATOM   2061 N  N   . ALA A 1 273 ? 2.449   18.782  24.888  1.00 20.38 ?  275  ALA A N   1 
ATOM   2062 C  CA  . ALA A 1 273 ? 3.012   18.061  26.022  1.00 18.52 ?  275  ALA A CA  1 
ATOM   2063 C  C   . ALA A 1 273 ? 3.164   16.601  25.631  1.00 16.74 ?  275  ALA A C   1 
ATOM   2064 O  O   . ALA A 1 273 ? 2.431   16.122  24.756  1.00 16.80 ?  275  ALA A O   1 
ATOM   2065 C  CB  . ALA A 1 273 ? 2.111   18.189  27.260  1.00 22.03 ?  275  ALA A CB  1 
ATOM   2066 N  N   . PRO A 1 274 ? 4.087   15.870  26.255  1.00 20.27 ?  276  PRO A N   1 
ATOM   2067 C  CA  . PRO A 1 274 ? 4.204   14.437  25.960  1.00 17.97 ?  276  PRO A CA  1 
ATOM   2068 C  C   . PRO A 1 274 ? 2.930   13.708  26.355  1.00 17.61 ?  276  PRO A C   1 
ATOM   2069 O  O   . PRO A 1 274 ? 2.178   14.161  27.223  1.00 17.59 ?  276  PRO A O   1 
ATOM   2070 C  CB  . PRO A 1 274 ? 5.401   13.992  26.814  1.00 17.94 ?  276  PRO A CB  1 
ATOM   2071 C  CG  . PRO A 1 274 ? 5.538   15.055  27.859  1.00 24.48 ?  276  PRO A CG  1 
ATOM   2072 C  CD  . PRO A 1 274 ? 5.100   16.323  27.223  1.00 18.68 ?  276  PRO A CD  1 
ATOM   2073 N  N   . VAL A 1 275 ? 2.678   12.571  25.699  1.00 13.85 ?  277  VAL A N   1 
ATOM   2074 C  CA  . VAL A 1 275 ? 1.427   11.850  25.884  1.00 14.12 ?  277  VAL A CA  1 
ATOM   2075 C  C   . VAL A 1 275 ? 1.705   10.414  26.306  1.00 11.42 ?  277  VAL A C   1 
ATOM   2076 O  O   . VAL A 1 275 ? 2.805   9.878   26.132  1.00 13.39 ?  277  VAL A O   1 
ATOM   2077 C  CB  . VAL A 1 275 ? 0.529   11.875  24.618  1.00 20.59 ?  277  VAL A CB  1 
ATOM   2078 C  CG1 . VAL A 1 275 ? 0.214   13.310  24.210  1.00 24.47 ?  277  VAL A CG1 1 
ATOM   2079 C  CG2 . VAL A 1 275 ? 1.207   11.147  23.459  1.00 16.71 ?  277  VAL A CG2 1 
ATOM   2080 N  N   . ASP A 1 276 ? 0.665   9.783   26.864  1.00 14.79 ?  278  ASP A N   1 
ATOM   2081 C  CA  . ASP A 1 276 ? 0.808   8.422   27.372  1.00 16.61 ?  278  ASP A CA  1 
ATOM   2082 C  C   . ASP A 1 276 ? 0.854   7.377   26.266  1.00 13.50 ?  278  ASP A C   1 
ATOM   2083 O  O   . ASP A 1 276 ? 1.436   6.305   26.463  1.00 14.92 ?  278  ASP A O   1 
ATOM   2084 C  CB  . ASP A 1 276 ? -0.333  8.086   28.328  1.00 22.58 ?  278  ASP A CB  1 
ATOM   2085 C  CG  . ASP A 1 276 ? -0.138  8.701   29.697  1.00 27.53 ?  278  ASP A CG  1 
ATOM   2086 O  OD1 . ASP A 1 276 ? 0.834   8.312   30.373  1.00 36.23 ?  278  ASP A OD1 1 
ATOM   2087 O  OD2 . ASP A 1 276 ? -0.971  9.539   30.102  1.00 37.21 ?  278  ASP A OD2 1 
ATOM   2088 N  N   . VAL A 1 277 ? 0.219   7.637   25.122  1.00 13.65 ?  279  VAL A N   1 
ATOM   2089 C  CA  . VAL A 1 277 ? 0.116   6.654   24.050  1.00 11.13 ?  279  VAL A CA  1 
ATOM   2090 C  C   . VAL A 1 277 ? 0.497   7.328   22.742  1.00 12.19 ?  279  VAL A C   1 
ATOM   2091 O  O   . VAL A 1 277 ? -0.145  8.306   22.348  1.00 13.63 ?  279  VAL A O   1 
ATOM   2092 C  CB  . VAL A 1 277 ? -1.302  6.076   23.930  1.00 14.67 ?  279  VAL A CB  1 
ATOM   2093 C  CG1 . VAL A 1 277 ? -1.314  4.934   22.924  1.00 13.87 ?  279  VAL A CG1 1 
ATOM   2094 C  CG2 . VAL A 1 277 ? -1.836  5.641   25.300  1.00 16.65 ?  279  VAL A CG2 1 
ATOM   2095 N  N   . VAL A 1 278 ? 1.504   6.793   22.046  1.00 11.81 ?  280  VAL A N   1 
ATOM   2096 C  CA  . VAL A 1 278 ? 1.879   7.293   20.719  1.00 10.54 ?  280  VAL A CA  1 
ATOM   2097 C  C   . VAL A 1 278 ? 1.682   6.160   19.724  1.00 11.88 ?  280  VAL A C   1 
ATOM   2098 O  O   . VAL A 1 278 ? 2.255   5.078   19.893  1.00 11.59 ?  280  VAL A O   1 
ATOM   2099 C  CB  . VAL A 1 278 ? 3.331   7.815   20.662  1.00 8.59  ?  280  VAL A CB  1 
ATOM   2100 C  CG1 . VAL A 1 278 ? 3.602   8.402   19.249  1.00 10.28 ?  280  VAL A CG1 1 
ATOM   2101 C  CG2 . VAL A 1 278 ? 3.588   8.862   21.730  1.00 10.59 ?  280  VAL A CG2 1 
ATOM   2102 N  N   . VAL A 1 279 ? 0.850   6.397   18.700  1.00 8.80  ?  281  VAL A N   1 
ATOM   2103 C  CA  . VAL A 1 279 ? 0.669   5.458   17.596  1.00 10.28 ?  281  VAL A CA  1 
ATOM   2104 C  C   . VAL A 1 279 ? 1.560   5.881   16.433  1.00 11.00 ?  281  VAL A C   1 
ATOM   2105 O  O   . VAL A 1 279 ? 1.519   7.043   15.999  1.00 8.33  ?  281  VAL A O   1 
ATOM   2106 C  CB  . VAL A 1 279 ? -0.797  5.409   17.143  1.00 9.67  ?  281  VAL A CB  1 
ATOM   2107 C  CG1 . VAL A 1 279 ? -0.933  4.502   15.924  1.00 12.11 ?  281  VAL A CG1 1 
ATOM   2108 C  CG2 . VAL A 1 279 ? -1.702  4.981   18.295  1.00 9.63  ?  281  VAL A CG2 1 
ATOM   2109 N  N   . THR A 1 280 ? 2.342   4.947   15.897  1.00 8.54  ?  282  THR A N   1 
ATOM   2110 C  CA  . THR A 1 280 ? 3.248   5.336   14.819  1.00 9.18  ?  282  THR A CA  1 
ATOM   2111 C  C   . THR A 1 280 ? 3.379   4.186   13.831  1.00 9.19  ?  282  THR A C   1 
ATOM   2112 O  O   . THR A 1 280 ? 2.786   3.116   13.994  1.00 9.89  ?  282  THR A O   1 
ATOM   2113 C  CB  . THR A 1 280 ? 4.616   5.769   15.382  1.00 11.69 ?  282  THR A CB  1 
ATOM   2114 O  OG1 . THR A 1 280 ? 5.414   6.372   14.347  1.00 11.70 ?  282  THR A OG1 1 
ATOM   2115 C  CG2 . THR A 1 280 ? 5.356   4.564   15.979  1.00 10.43 ?  282  THR A CG2 1 
ATOM   2116 N  N   . SER A 1 281 ? 4.124   4.435   12.772  1.00 12.01 ?  283  SER A N   1 
ATOM   2117 C  CA  . SER A 1 281 ? 4.422   3.436   11.761  1.00 10.10 ?  283  SER A CA  1 
ATOM   2118 C  C   . SER A 1 281 ? 5.931   3.334   11.626  1.00 10.47 ?  283  SER A C   1 
ATOM   2119 O  O   . SER A 1 281 ? 6.687   4.024   12.318  1.00 10.69 ?  283  SER A O   1 
ATOM   2120 C  CB  . SER A 1 281 ? 3.806   3.813   10.409  1.00 12.53 ?  283  SER A CB  1 
ATOM   2121 O  OG  . SER A 1 281 ? 4.519   4.938   9.889   1.00 9.42  ?  283  SER A OG  1 
ATOM   2122 N  N   . SER A 1 282 ? 6.359   2.478   10.703  1.00 7.86  ?  284  SER A N   1 
ATOM   2123 C  CA  . SER A 1 282 ? 7.746   2.417   10.268  1.00 11.65 ?  284  SER A CA  1 
ATOM   2124 C  C   . SER A 1 282 ? 7.904   2.967   8.847   1.00 14.62 ?  284  SER A C   1 
ATOM   2125 O  O   . SER A 1 282 ? 8.799   2.555   8.109   1.00 10.86 ?  284  SER A O   1 
ATOM   2126 C  CB  . SER A 1 282 ? 8.262   0.977   10.379  1.00 11.69 ?  284  SER A CB  1 
ATOM   2127 O  OG  . SER A 1 282 ? 9.590   0.879   9.913   1.00 13.70 ?  284  SER A OG  1 
ATOM   2128 N  N   . ALA A 1 283 ? 7.043   3.926   8.471   1.00 9.52  ?  285  ALA A N   1 
ATOM   2129 C  CA  . ALA A 1 283 ? 7.077   4.649   7.196   1.00 11.47 ?  285  ALA A CA  1 
ATOM   2130 C  C   . ALA A 1 283 ? 6.753   3.765   5.989   1.00 9.10  ?  285  ALA A C   1 
ATOM   2131 O  O   . ALA A 1 283 ? 7.064   4.132   4.860   1.00 10.03 ?  285  ALA A O   1 
ATOM   2132 C  CB  . ALA A 1 283 ? 8.423   5.357   6.978   1.00 11.50 ?  285  ALA A CB  1 
ATOM   2133 N  N   . GLY A 1 284 ? 6.141   2.608   6.195   1.00 8.74  ?  286  GLY A N   1 
ATOM   2134 C  CA  . GLY A 1 284 ? 5.710   1.807   5.059   1.00 10.22 ?  286  GLY A CA  1 
ATOM   2135 C  C   . GLY A 1 284 ? 6.859   1.227   4.236   1.00 12.78 ?  286  GLY A C   1 
ATOM   2136 O  O   . GLY A 1 284 ? 8.035   1.246   4.621   1.00 8.01  ?  286  GLY A O   1 
ATOM   2137 N  N   . HIS A 1 285 ? 6.477   0.678   3.082   1.00 9.70  ?  287  HIS A N   1 
ATOM   2138 C  CA  . HIS A 1 285 ? 7.455   0.127   2.154   1.00 8.18  ?  287  HIS A CA  1 
ATOM   2139 C  C   . HIS A 1 285 ? 8.264   1.273   1.547   1.00 10.22 ?  287  HIS A C   1 
ATOM   2140 O  O   . HIS A 1 285 ? 7.693   2.288   1.146   1.00 10.89 ?  287  HIS A O   1 
ATOM   2141 C  CB  . HIS A 1 285 ? 6.752   -0.661  1.035   1.00 11.19 ?  287  HIS A CB  1 
ATOM   2142 C  CG  . HIS A 1 285 ? 7.693   -1.271  0.042   1.00 10.75 ?  287  HIS A CG  1 
ATOM   2143 N  ND1 . HIS A 1 285 ? 8.214   -2.538  0.198   1.00 11.13 ?  287  HIS A ND1 1 
ATOM   2144 C  CD2 . HIS A 1 285 ? 8.211   -0.789  -1.114  1.00 11.90 ?  287  HIS A CD2 1 
ATOM   2145 C  CE1 . HIS A 1 285 ? 9.012   -2.813  -0.819  1.00 10.32 ?  287  HIS A CE1 1 
ATOM   2146 N  NE2 . HIS A 1 285 ? 9.028   -1.769  -1.630  1.00 15.78 ?  287  HIS A NE2 1 
ATOM   2147 N  N   . PRO A 1 286 ? 9.593   1.144   1.459   1.00 8.22  ?  288  PRO A N   1 
ATOM   2148 C  CA  . PRO A 1 286 ? 10.434  -0.024  1.731   1.00 9.85  ?  288  PRO A CA  1 
ATOM   2149 C  C   . PRO A 1 286 ? 11.073  -0.076  3.119   1.00 11.32 ?  288  PRO A C   1 
ATOM   2150 O  O   . PRO A 1 286 ? 11.706  -1.078  3.430   1.00 10.39 ?  288  PRO A O   1 
ATOM   2151 C  CB  . PRO A 1 286 ? 11.540  0.110   0.670   1.00 10.31 ?  288  PRO A CB  1 
ATOM   2152 C  CG  . PRO A 1 286 ? 11.734  1.594   0.553   1.00 10.67 ?  288  PRO A CG  1 
ATOM   2153 C  CD  . PRO A 1 286 ? 10.342  2.219   0.782   1.00 9.59  ?  288  PRO A CD  1 
ATOM   2154 N  N   . LEU A 1 287 ? 10.936  0.976   3.933   1.00 8.68  ?  289  LEU A N   1 
ATOM   2155 C  CA  . LEU A 1 287 ? 11.659  0.968   5.208   1.00 8.51  ?  289  LEU A CA  1 
ATOM   2156 C  C   . LEU A 1 287 ? 11.171  -0.160  6.110   1.00 9.88  ?  289  LEU A C   1 
ATOM   2157 O  O   . LEU A 1 287 ? 11.975  -0.791  6.807   1.00 11.07 ?  289  LEU A O   1 
ATOM   2158 C  CB  . LEU A 1 287 ? 11.529  2.324   5.920   1.00 7.31  ?  289  LEU A CB  1 
ATOM   2159 C  CG  . LEU A 1 287 ? 12.391  2.516   7.166   1.00 10.33 ?  289  LEU A CG  1 
ATOM   2160 C  CD1 . LEU A 1 287 ? 13.844  2.107   6.921   1.00 7.07  ?  289  LEU A CD1 1 
ATOM   2161 C  CD2 . LEU A 1 287 ? 12.327  3.945   7.701   1.00 11.49 ?  289  LEU A CD2 1 
ATOM   2162 N  N   . ASP A 1 288 ? 9.876   -0.473  6.076   1.00 7.78  ?  290  ASP A N   1 
ATOM   2163 C  CA  . ASP A 1 288 ? 9.323   -1.364  7.083   1.00 10.00 ?  290  ASP A CA  1 
ATOM   2164 C  C   . ASP A 1 288 ? 9.416   -2.832  6.680   1.00 9.60  ?  290  ASP A C   1 
ATOM   2165 O  O   . ASP A 1 288 ? 8.668   -3.651  7.220   1.00 11.08 ?  290  ASP A O   1 
ATOM   2166 C  CB  . ASP A 1 288 ? 7.871   -0.961  7.449   1.00 8.98  ?  290  ASP A CB  1 
ATOM   2167 C  CG  . ASP A 1 288 ? 6.811   -1.399  6.434   1.00 10.20 ?  290  ASP A CG  1 
ATOM   2168 O  OD1 . ASP A 1 288 ? 7.125   -1.861  5.307   1.00 11.67 ?  290  ASP A OD1 1 
ATOM   2169 O  OD2 . ASP A 1 288 ? 5.606   -1.260  6.786   1.00 11.93 ?  290  ASP A OD2 1 
ATOM   2170 N  N   . LEU A 1 289 ? 10.350  -3.176  5.776   1.00 8.67  ?  291  LEU A N   1 
ATOM   2171 C  CA  . LEU A 1 289 ? 10.553  -4.568  5.376   1.00 9.80  ?  291  LEU A CA  1 
ATOM   2172 C  C   . LEU A 1 289 ? 10.985  -5.468  6.529   1.00 11.43 ?  291  LEU A C   1 
ATOM   2173 O  O   . LEU A 1 289 ? 10.660  -6.659  6.521   1.00 9.99  ?  291  LEU A O   1 
ATOM   2174 C  CB  . LEU A 1 289 ? 11.598  -4.653  4.260   1.00 10.30 ?  291  LEU A CB  1 
ATOM   2175 C  CG  . LEU A 1 289 ? 11.104  -4.267  2.853   1.00 10.62 ?  291  LEU A CG  1 
ATOM   2176 C  CD1 . LEU A 1 289 ? 12.292  -4.122  1.892   1.00 16.63 ?  291  LEU A CD1 1 
ATOM   2177 C  CD2 . LEU A 1 289 ? 10.116  -5.322  2.369   1.00 15.54 ?  291  LEU A CD2 1 
ATOM   2178 N  N   . THR A 1 290 ? 11.775  -4.958  7.485   1.00 11.31 ?  292  THR A N   1 
ATOM   2179 C  CA  . THR A 1 290 ? 12.278  -5.795  8.569   1.00 10.67 ?  292  THR A CA  1 
ATOM   2180 C  C   . THR A 1 290 ? 12.082  -5.141  9.934   1.00 10.57 ?  292  THR A C   1 
ATOM   2181 O  O   . THR A 1 290 ? 12.051  -3.917  10.068  1.00 7.74  ?  292  THR A O   1 
ATOM   2182 C  CB  . THR A 1 290 ? 13.777  -6.119  8.407   1.00 11.70 ?  292  THR A CB  1 
ATOM   2183 O  OG1 . THR A 1 290 ? 14.534  -4.894  8.337   1.00 8.82  ?  292  THR A OG1 1 
ATOM   2184 C  CG2 . THR A 1 290 ? 14.011  -6.990  7.145   1.00 10.53 ?  292  THR A CG2 1 
ATOM   2185 N  N   . PHE A 1 291 ? 11.989  -5.988  10.957  1.00 9.45  ?  293  PHE A N   1 
ATOM   2186 C  CA  . PHE A 1 291 ? 11.899  -5.486  12.320  1.00 11.12 ?  293  PHE A CA  1 
ATOM   2187 C  C   . PHE A 1 291 ? 13.141  -4.670  12.667  1.00 9.44  ?  293  PHE A C   1 
ATOM   2188 O  O   . PHE A 1 291 ? 13.038  -3.647  13.357  1.00 8.92  ?  293  PHE A O   1 
ATOM   2189 C  CB  . PHE A 1 291 ? 11.705  -6.673  13.272  1.00 12.57 ?  293  PHE A CB  1 
ATOM   2190 C  CG  . PHE A 1 291 ? 11.642  -6.308  14.721  1.00 10.47 ?  293  PHE A CG  1 
ATOM   2191 C  CD1 . PHE A 1 291 ? 10.428  -6.064  15.342  1.00 11.63 ?  293  PHE A CD1 1 
ATOM   2192 C  CD2 . PHE A 1 291 ? 12.805  -6.205  15.465  1.00 10.38 ?  293  PHE A CD2 1 
ATOM   2193 C  CE1 . PHE A 1 291 ? 10.381  -5.737  16.695  1.00 13.55 ?  293  PHE A CE1 1 
ATOM   2194 C  CE2 . PHE A 1 291 ? 12.768  -5.873  16.805  1.00 15.59 ?  293  PHE A CE2 1 
ATOM   2195 C  CZ  . PHE A 1 291 ? 11.576  -5.644  17.427  1.00 12.36 ?  293  PHE A CZ  1 
ATOM   2196 N  N   . TYR A 1 292 ? 14.297  -5.074  12.126  1.00 9.10  ?  294  TYR A N   1 
ATOM   2197 C  CA  . TYR A 1 292 ? 15.547  -4.334  12.298  1.00 9.08  ?  294  TYR A CA  1 
ATOM   2198 C  C   . TYR A 1 292 ? 15.377  -2.854  11.957  1.00 9.95  ?  294  TYR A C   1 
ATOM   2199 O  O   . TYR A 1 292 ? 15.812  -1.976  12.715  1.00 9.24  ?  294  TYR A O   1 
ATOM   2200 C  CB  . TYR A 1 292 ? 16.635  -4.992  11.429  1.00 10.48 ?  294  TYR A CB  1 
ATOM   2201 C  CG  . TYR A 1 292 ? 17.936  -4.227  11.273  1.00 6.42  ?  294  TYR A CG  1 
ATOM   2202 C  CD1 . TYR A 1 292 ? 18.997  -4.394  12.168  1.00 10.91 ?  294  TYR A CD1 1 
ATOM   2203 C  CD2 . TYR A 1 292 ? 18.122  -3.361  10.187  1.00 9.34  ?  294  TYR A CD2 1 
ATOM   2204 C  CE1 . TYR A 1 292 ? 20.186  -3.709  11.993  1.00 9.80  ?  294  TYR A CE1 1 
ATOM   2205 C  CE2 . TYR A 1 292 ? 19.310  -2.659  10.014  1.00 9.98  ?  294  TYR A CE2 1 
ATOM   2206 C  CZ  . TYR A 1 292 ? 20.334  -2.836  10.919  1.00 11.86 ?  294  TYR A CZ  1 
ATOM   2207 O  OH  . TYR A 1 292 ? 21.499  -2.139  10.731  1.00 11.83 ?  294  TYR A OH  1 
ATOM   2208 N  N   . GLN A 1 293 ? 14.720  -2.553  10.816  1.00 8.20  ?  295  GLN A N   1 
ATOM   2209 C  CA  . GLN A 1 293 ? 14.524  -1.153  10.442  1.00 9.44  ?  295  GLN A CA  1 
ATOM   2210 C  C   . GLN A 1 293 ? 13.370  -0.510  11.200  1.00 10.10 ?  295  GLN A C   1 
ATOM   2211 O  O   . GLN A 1 293 ? 13.413  0.700   11.459  1.00 11.04 ?  295  GLN A O   1 
ATOM   2212 C  CB  . GLN A 1 293 ? 14.272  -1.022  8.931   1.00 10.85 ?  295  GLN A CB  1 
ATOM   2213 C  CG  . GLN A 1 293 ? 15.473  -1.417  8.067   1.00 11.45 ?  295  GLN A CG  1 
ATOM   2214 C  CD  . GLN A 1 293 ? 16.603  -0.393  8.112   1.00 13.26 ?  295  GLN A CD  1 
ATOM   2215 O  OE1 . GLN A 1 293 ? 16.460  0.688   8.683   1.00 10.53 ?  295  GLN A OE1 1 
ATOM   2216 N  NE2 . GLN A 1 293 ? 17.739  -0.742  7.517   1.00 10.65 ?  295  GLN A NE2 1 
ATOM   2217 N  N   . ALA A 1 294 ? 12.329  -1.292  11.538  1.00 7.66  ?  296  ALA A N   1 
ATOM   2218 C  CA  . ALA A 1 294 ? 11.157  -0.766  12.230  1.00 7.37  ?  296  ALA A CA  1 
ATOM   2219 C  C   . ALA A 1 294 ? 11.482  -0.205  13.605  1.00 9.78  ?  296  ALA A C   1 
ATOM   2220 O  O   . ALA A 1 294 ? 10.700  0.588   14.139  1.00 10.05 ?  296  ALA A O   1 
ATOM   2221 C  CB  . ALA A 1 294 ? 10.075  -1.852  12.338  1.00 13.25 ?  296  ALA A CB  1 
ATOM   2222 N  N   . VAL A 1 295 ? 12.622  -0.575  14.193  1.00 9.04  ?  297  VAL A N   1 
ATOM   2223 C  CA  . VAL A 1 295 ? 13.043  0.076   15.428  1.00 7.92  ?  297  VAL A CA  1 
ATOM   2224 C  C   . VAL A 1 295 ? 13.093  1.593   15.261  1.00 8.59  ?  297  VAL A C   1 
ATOM   2225 O  O   . VAL A 1 295 ? 12.891  2.337   16.225  1.00 9.67  ?  297  VAL A O   1 
ATOM   2226 C  CB  . VAL A 1 295 ? 14.408  -0.503  15.861  1.00 7.44  ?  297  VAL A CB  1 
ATOM   2227 C  CG1 . VAL A 1 295 ? 15.005  0.293   17.016  1.00 9.63  ?  297  VAL A CG1 1 
ATOM   2228 C  CG2 . VAL A 1 295 ? 14.236  -1.974  16.242  1.00 11.19 ?  297  VAL A CG2 1 
ATOM   2229 N  N   . LYS A 1 296 ? 13.318  2.076   14.025  1.00 9.94  ?  298  LYS A N   1 
ATOM   2230 C  CA  . LYS A 1 296 ? 13.333  3.518   13.760  1.00 8.84  ?  298  LYS A CA  1 
ATOM   2231 C  C   . LYS A 1 296 ? 12.007  4.201   14.101  1.00 12.03 ?  298  LYS A C   1 
ATOM   2232 O  O   . LYS A 1 296 ? 12.004  5.356   14.544  1.00 8.74  ?  298  LYS A O   1 
ATOM   2233 C  CB  . LYS A 1 296 ? 13.696  3.777   12.296  1.00 8.67  ?  298  LYS A CB  1 
ATOM   2234 C  CG  . LYS A 1 296 ? 15.122  3.406   11.945  1.00 10.12 ?  298  LYS A CG  1 
ATOM   2235 C  CD  . LYS A 1 296 ? 15.366  3.493   10.421  1.00 10.59 ?  298  LYS A CD  1 
ATOM   2236 C  CE  . LYS A 1 296 ? 16.858  3.629   10.137  1.00 11.87 ?  298  LYS A CE  1 
ATOM   2237 N  NZ  . LYS A 1 296 ? 17.156  3.314   8.706   1.00 12.52 ?  298  LYS A NZ  1 
ATOM   2238 N  N   . GLY A 1 297 ? 10.867  3.540   13.880  1.00 8.32  ?  299  GLY A N   1 
ATOM   2239 C  CA  . GLY A 1 297 ? 9.611   4.152   14.288  1.00 9.56  ?  299  GLY A CA  1 
ATOM   2240 C  C   . GLY A 1 297 ? 9.509   4.290   15.792  1.00 9.71  ?  299  GLY A C   1 
ATOM   2241 O  O   . GLY A 1 297 ? 8.946   5.265   16.302  1.00 8.93  ?  299  GLY A O   1 
ATOM   2242 N  N   . LEU A 1 298 ? 10.071  3.323   16.524  1.00 11.66 ?  300  LEU A N   1 
ATOM   2243 C  CA  . LEU A 1 298 ? 10.057  3.389   17.983  1.00 11.46 ?  300  LEU A CA  1 
ATOM   2244 C  C   . LEU A 1 298 ? 10.942  4.517   18.503  1.00 10.36 ?  300  LEU A C   1 
ATOM   2245 O  O   . LEU A 1 298 ? 10.526  5.287   19.373  1.00 10.84 ?  300  LEU A O   1 
ATOM   2246 C  CB  . LEU A 1 298 ? 10.486  2.047   18.572  1.00 10.30 ?  300  LEU A CB  1 
ATOM   2247 C  CG  . LEU A 1 298 ? 9.650   0.859   18.124  1.00 13.45 ?  300  LEU A CG  1 
ATOM   2248 C  CD1 . LEU A 1 298 ? 10.256  -0.416  18.702  1.00 11.64 ?  300  LEU A CD1 1 
ATOM   2249 C  CD2 . LEU A 1 298 ? 8.183   1.053   18.553  1.00 13.29 ?  300  LEU A CD2 1 
ATOM   2250 N  N   . THR A 1 299 ? 12.184  4.614   18.022  1.00 12.16 ?  301  THR A N   1 
ATOM   2251 C  CA  . THR A 1 299 ? 13.026  5.711   18.489  1.00 11.35 ?  301  THR A CA  1 
ATOM   2252 C  C   . THR A 1 299 ? 12.480  7.061   18.044  1.00 11.26 ?  301  THR A C   1 
ATOM   2253 O  O   . THR A 1 299 ? 12.623  8.056   18.764  1.00 13.11 ?  301  THR A O   1 
ATOM   2254 C  CB  . THR A 1 299 ? 14.472  5.537   18.004  1.00 14.08 ?  301  THR A CB  1 
ATOM   2255 O  OG1 . THR A 1 299 ? 14.498  5.433   16.574  1.00 14.71 ?  301  THR A OG1 1 
ATOM   2256 C  CG2 . THR A 1 299 ? 15.091  4.288   18.601  1.00 13.94 ?  301  THR A CG2 1 
ATOM   2257 N  N   . GLY A 1 300 ? 11.828  7.116   16.879  1.00 12.10 ?  302  GLY A N   1 
ATOM   2258 C  CA  . GLY A 1 300 ? 11.267  8.375   16.422  1.00 11.71 ?  302  GLY A CA  1 
ATOM   2259 C  C   . GLY A 1 300 ? 10.176  8.919   17.326  1.00 15.31 ?  302  GLY A C   1 
ATOM   2260 O  O   . GLY A 1 300 ? 10.028  10.135  17.458  1.00 17.79 ?  302  GLY A O   1 
ATOM   2261 N  N   . ALA A 1 301 ? 9.411   8.033   17.973  1.00 11.64 ?  303  ALA A N   1 
ATOM   2262 C  CA  . ALA A 1 301 ? 8.316   8.436   18.856  1.00 11.91 ?  303  ALA A CA  1 
ATOM   2263 C  C   . ALA A 1 301 ? 8.784   8.870   20.243  1.00 15.38 ?  303  ALA A C   1 
ATOM   2264 O  O   . ALA A 1 301 ? 8.010   9.495   20.979  1.00 15.19 ?  303  ALA A O   1 
ATOM   2265 C  CB  . ALA A 1 301 ? 7.317   7.281   19.013  1.00 13.43 ?  303  ALA A CB  1 
ATOM   2266 N  N   . LEU A 1 302 ? 10.015  8.544   20.626  1.00 12.95 ?  304  LEU A N   1 
ATOM   2267 C  CA  . LEU A 1 302 ? 10.461  8.787   21.997  1.00 13.88 ?  304  LEU A CA  1 
ATOM   2268 C  C   . LEU A 1 302 ? 10.282  10.221  22.494  1.00 15.36 ?  304  LEU A C   1 
ATOM   2269 O  O   . LEU A 1 302 ? 9.815   10.389  23.634  1.00 17.90 ?  304  LEU A O   1 
ATOM   2270 C  CB  . LEU A 1 302 ? 11.932  8.367   22.140  1.00 14.20 ?  304  LEU A CB  1 
ATOM   2271 C  CG  . LEU A 1 302 ? 12.158  6.870   22.353  1.00 16.43 ?  304  LEU A CG  1 
ATOM   2272 C  CD1 . LEU A 1 302 ? 13.641  6.573   22.617  1.00 17.25 ?  304  LEU A CD1 1 
ATOM   2273 C  CD2 . LEU A 1 302 ? 11.298  6.312   23.479  1.00 16.60 ?  304  LEU A CD2 1 
ATOM   2274 N  N   . PRO A 1 303 ? 10.615  11.273  21.740  1.00 14.62 ?  305  PRO A N   1 
ATOM   2275 C  CA  . PRO A 1 303 ? 10.523  12.628  22.310  1.00 17.42 ?  305  PRO A CA  1 
ATOM   2276 C  C   . PRO A 1 303 ? 9.136   13.035  22.782  1.00 18.95 ?  305  PRO A C   1 
ATOM   2277 O  O   . PRO A 1 303 ? 9.045   13.950  23.609  1.00 18.93 ?  305  PRO A O   1 
ATOM   2278 C  CB  . PRO A 1 303 ? 10.992  13.528  21.156  1.00 17.32 ?  305  PRO A CB  1 
ATOM   2279 C  CG  . PRO A 1 303 ? 11.851  12.662  20.324  1.00 18.23 ?  305  PRO A CG  1 
ATOM   2280 C  CD  . PRO A 1 303 ? 11.213  11.303  20.391  1.00 17.41 ?  305  PRO A CD  1 
ATOM   2281 N  N   . ILE A 1 304 ? 8.054   12.428  22.284  1.00 13.20 ?  306  ILE A N   1 
ATOM   2282 C  CA  . ILE A 1 304 ? 6.718   12.862  22.676  1.00 15.00 ?  306  ILE A CA  1 
ATOM   2283 C  C   . ILE A 1 304 ? 5.972   11.834  23.521  1.00 14.20 ?  306  ILE A C   1 
ATOM   2284 O  O   . ILE A 1 304 ? 4.813   12.074  23.863  1.00 16.87 ?  306  ILE A O   1 
ATOM   2285 C  CB  . ILE A 1 304 ? 5.871   13.271  21.455  1.00 13.75 ?  306  ILE A CB  1 
ATOM   2286 C  CG1 . ILE A 1 304 ? 5.628   12.087  20.522  1.00 10.54 ?  306  ILE A CG1 1 
ATOM   2287 C  CG2 . ILE A 1 304 ? 6.537   14.417  20.696  1.00 14.49 ?  306  ILE A CG2 1 
ATOM   2288 C  CD1 . ILE A 1 304 ? 4.355   12.208  19.731  1.00 12.43 ?  306  ILE A CD1 1 
ATOM   2289 N  N   . VAL A 1 305 ? 6.593   10.717  23.903  1.00 14.40 ?  307  VAL A N   1 
ATOM   2290 C  CA  . VAL A 1 305 ? 5.945   9.779   24.824  1.00 12.37 ?  307  VAL A CA  1 
ATOM   2291 C  C   . VAL A 1 305 ? 6.400   10.075  26.256  1.00 14.21 ?  307  VAL A C   1 
ATOM   2292 O  O   . VAL A 1 305 ? 7.578   10.365  26.509  1.00 15.57 ?  307  VAL A O   1 
ATOM   2293 C  CB  . VAL A 1 305 ? 6.229   8.316   24.430  1.00 12.24 ?  307  VAL A CB  1 
ATOM   2294 C  CG1 . VAL A 1 305 ? 7.677   7.923   24.776  1.00 12.98 ?  307  VAL A CG1 1 
ATOM   2295 C  CG2 . VAL A 1 305 ? 5.250   7.390   25.114  1.00 14.16 ?  307  VAL A CG2 1 
ATOM   2296 N  N   . LYS A 1 306 ? 5.460   10.009  27.196  1.00 14.39 ?  308  LYS A N   1 
ATOM   2297 C  CA  . LYS A 1 306 ? 5.788   10.184  28.608  1.00 15.27 ?  308  LYS A CA  1 
ATOM   2298 C  C   . LYS A 1 306 ? 6.605   8.990   29.100  1.00 15.13 ?  308  LYS A C   1 
ATOM   2299 O  O   . LYS A 1 306 ? 6.382   7.859   28.649  1.00 15.64 ?  308  LYS A O   1 
ATOM   2300 C  CB  . LYS A 1 306 ? 4.504   10.304  29.439  1.00 20.39 ?  308  LYS A CB  1 
ATOM   2301 C  CG  . LYS A 1 306 ? 3.764   11.611  29.233  1.00 18.72 ?  308  LYS A CG  1 
ATOM   2302 C  CD  . LYS A 1 306 ? 2.439   11.633  29.975  1.00 26.46 ?  308  LYS A CD  1 
ATOM   2303 C  CE  . LYS A 1 306 ? 2.609   11.132  31.400  1.00 26.62 ?  308  LYS A CE  1 
ATOM   2304 N  NZ  . LYS A 1 306 ? 1.337   10.626  31.988  1.00 35.49 ?  308  LYS A NZ  1 
ATOM   2305 N  N   . PRO A 1 307 ? 7.564   9.200   29.998  1.00 13.83 ?  309  PRO A N   1 
ATOM   2306 C  CA  . PRO A 1 307 ? 8.219   8.057   30.644  1.00 15.97 ?  309  PRO A CA  1 
ATOM   2307 C  C   . PRO A 1 307 ? 7.187   7.087   31.201  1.00 20.68 ?  309  PRO A C   1 
ATOM   2308 O  O   . PRO A 1 307 ? 6.246   7.482   31.899  1.00 17.48 ?  309  PRO A O   1 
ATOM   2309 C  CB  . PRO A 1 307 ? 9.037   8.707   31.766  1.00 15.53 ?  309  PRO A CB  1 
ATOM   2310 C  CG  . PRO A 1 307 ? 9.298   10.080  31.289  1.00 19.36 ?  309  PRO A CG  1 
ATOM   2311 C  CD  . PRO A 1 307 ? 8.039   10.486  30.546  1.00 19.11 ?  309  PRO A CD  1 
ATOM   2312 N  N   . GLY A 1 308 ? 7.346   5.812   30.859  1.00 12.68 ?  310  GLY A N   1 
ATOM   2313 C  CA  . GLY A 1 308 ? 6.400   4.797   31.247  1.00 12.85 ?  310  GLY A CA  1 
ATOM   2314 C  C   . GLY A 1 308 ? 5.191   4.691   30.346  1.00 15.66 ?  310  GLY A C   1 
ATOM   2315 O  O   . GLY A 1 308 ? 4.320   3.838   30.601  1.00 18.80 ?  310  GLY A O   1 
ATOM   2316 N  N   . GLY A 1 309 ? 5.108   5.517   29.304  1.00 11.95 ?  311  GLY A N   1 
ATOM   2317 C  CA  . GLY A 1 309 ? 4.013   5.448   28.348  1.00 12.78 ?  311  GLY A CA  1 
ATOM   2318 C  C   . GLY A 1 309 ? 4.204   4.282   27.387  1.00 11.07 ?  311  GLY A C   1 
ATOM   2319 O  O   . GLY A 1 309 ? 5.083   3.436   27.549  1.00 13.05 ?  311  GLY A O   1 
ATOM   2320 N  N   . THR A 1 310 ? 3.332   4.227   26.378  1.00 12.26 ?  312  THR A N   1 
ATOM   2321 C  CA  . THR A 1 310 ? 3.303   3.107   25.446  1.00 11.82 ?  312  THR A CA  1 
ATOM   2322 C  C   . THR A 1 310 ? 3.379   3.628   24.020  1.00 11.62 ?  312  THR A C   1 
ATOM   2323 O  O   . THR A 1 310 ? 2.622   4.528   23.640  1.00 12.15 ?  312  THR A O   1 
ATOM   2324 C  CB  . THR A 1 310 ? 2.032   2.264   25.616  1.00 14.61 ?  312  THR A CB  1 
ATOM   2325 O  OG1 . THR A 1 310 ? 2.062   1.593   26.882  1.00 16.19 ?  312  THR A OG1 1 
ATOM   2326 C  CG2 . THR A 1 310 ? 1.915   1.198   24.496  1.00 13.40 ?  312  THR A CG2 1 
ATOM   2327 N  N   . ILE A 1 311 ? 4.278   3.047   23.230  1.00 10.34 ?  313  ILE A N   1 
ATOM   2328 C  CA  . ILE A 1 311 ? 4.309   3.254   21.790  1.00 10.48 ?  313  ILE A CA  1 
ATOM   2329 C  C   . ILE A 1 311 ? 3.625   2.078   21.113  1.00 9.33  ?  313  ILE A C   1 
ATOM   2330 O  O   . ILE A 1 311 ? 3.973   0.921   21.360  1.00 8.46  ?  313  ILE A O   1 
ATOM   2331 C  CB  . ILE A 1 311 ? 5.747   3.422   21.278  1.00 13.12 ?  313  ILE A CB  1 
ATOM   2332 C  CG1 . ILE A 1 311 ? 6.414   4.613   21.970  1.00 12.27 ?  313  ILE A CG1 1 
ATOM   2333 C  CG2 . ILE A 1 311 ? 5.755   3.580   19.758  1.00 9.99  ?  313  ILE A CG2 1 
ATOM   2334 C  CD1 . ILE A 1 311 ? 7.928   4.546   21.921  1.00 14.12 ?  313  ILE A CD1 1 
ATOM   2335 N  N   . VAL A 1 312 ? 2.650   2.378   20.263  1.00 8.01  ?  314  VAL A N   1 
ATOM   2336 C  CA  . VAL A 1 312 ? 1.970   1.390   19.438  1.00 9.79  ?  314  VAL A CA  1 
ATOM   2337 C  C   . VAL A 1 312 ? 2.481   1.579   18.013  1.00 11.56 ?  314  VAL A C   1 
ATOM   2338 O  O   . VAL A 1 312 ? 2.315   2.659   17.436  1.00 11.00 ?  314  VAL A O   1 
ATOM   2339 C  CB  . VAL A 1 312 ? 0.446   1.571   19.501  1.00 8.68  ?  314  VAL A CB  1 
ATOM   2340 C  CG1 . VAL A 1 312 ? -0.249  0.569   18.601  1.00 12.36 ?  314  VAL A CG1 1 
ATOM   2341 C  CG2 . VAL A 1 312 ? -0.067  1.450   20.950  1.00 9.09  ?  314  VAL A CG2 1 
ATOM   2342 N  N   . ILE A 1 313 ? 3.112   0.557   17.442  1.00 8.51  ?  315  ILE A N   1 
ATOM   2343 C  CA  . ILE A 1 313 ? 3.663   0.680   16.094  1.00 8.39  ?  315  ILE A CA  1 
ATOM   2344 C  C   . ILE A 1 313 ? 3.022   -0.354  15.178  1.00 9.30  ?  315  ILE A C   1 
ATOM   2345 O  O   . ILE A 1 313 ? 2.784   -1.502  15.576  1.00 11.44 ?  315  ILE A O   1 
ATOM   2346 C  CB  . ILE A 1 313 ? 5.201   0.550   16.091  1.00 9.89  ?  315  ILE A CB  1 
ATOM   2347 C  CG1 . ILE A 1 313 ? 5.740   0.780   14.672  1.00 10.06 ?  315  ILE A CG1 1 
ATOM   2348 C  CG2 . ILE A 1 313 ? 5.632   -0.812  16.610  1.00 8.39  ?  315  ILE A CG2 1 
ATOM   2349 C  CD1 . ILE A 1 313 ? 7.283   1.019   14.646  1.00 11.31 ?  315  ILE A CD1 1 
ATOM   2350 N  N   . ALA A 1 314 ? 2.718   0.060   13.953  1.00 8.53  ?  316  ALA A N   1 
ATOM   2351 C  CA  . ALA A 1 314 ? 2.247   -0.845  12.919  1.00 8.57  ?  316  ALA A CA  1 
ATOM   2352 C  C   . ALA A 1 314 ? 3.304   -0.895  11.828  1.00 10.14 ?  316  ALA A C   1 
ATOM   2353 O  O   . ALA A 1 314 ? 3.790   0.153   11.399  1.00 12.26 ?  316  ALA A O   1 
ATOM   2354 C  CB  . ALA A 1 314 ? 0.904   -0.373  12.358  1.00 8.34  ?  316  ALA A CB  1 
ATOM   2355 N  N   . ALA A 1 315 ? 3.699   -2.103  11.425  1.00 10.02 ?  317  ALA A N   1 
ATOM   2356 C  CA  . ALA A 1 315 ? 4.716   -2.245  10.389  1.00 11.19 ?  317  ALA A CA  1 
ATOM   2357 C  C   . ALA A 1 315 ? 4.512   -3.574  9.674   1.00 10.26 ?  317  ALA A C   1 
ATOM   2358 O  O   . ALA A 1 315 ? 4.294   -4.594  10.324  1.00 11.85 ?  317  ALA A O   1 
ATOM   2359 C  CB  . ALA A 1 315 ? 6.130   -2.170  10.976  1.00 11.61 ?  317  ALA A CB  1 
ATOM   2360 N  N   . ALA A 1 316 ? 4.623   -3.563  8.345   1.00 10.00 ?  318  ALA A N   1 
ATOM   2361 C  CA  . ALA A 1 316 ? 4.269   -4.761  7.571   1.00 11.26 ?  318  ALA A CA  1 
ATOM   2362 C  C   . ALA A 1 316 ? 5.273   -5.901  7.782   1.00 15.46 ?  318  ALA A C   1 
ATOM   2363 O  O   . ALA A 1 316 ? 4.877   -7.074  7.811   1.00 11.76 ?  318  ALA A O   1 
ATOM   2364 C  CB  . ALA A 1 316 ? 4.153   -4.417  6.084   1.00 13.07 ?  318  ALA A CB  1 
ATOM   2365 N  N   . LEU A 1 317 ? 6.570   -5.578  7.926   1.00 10.50 ?  319  LEU A N   1 
ATOM   2366 C  CA  . LEU A 1 317 ? 7.632   -6.582  8.133   1.00 14.82 ?  319  LEU A CA  1 
ATOM   2367 C  C   . LEU A 1 317 ? 7.592   -7.693  7.078   1.00 12.13 ?  319  LEU A C   1 
ATOM   2368 O  O   . LEU A 1 317 ? 7.750   -8.875  7.389   1.00 13.73 ?  319  LEU A O   1 
ATOM   2369 C  CB  . LEU A 1 317 ? 7.560   -7.184  9.541   1.00 11.13 ?  319  LEU A CB  1 
ATOM   2370 C  CG  . LEU A 1 317 ? 7.477   -6.209  10.714  1.00 11.54 ?  319  LEU A CG  1 
ATOM   2371 C  CD1 . LEU A 1 317 ? 7.538   -6.930  12.068  1.00 13.61 ?  319  LEU A CD1 1 
ATOM   2372 C  CD2 . LEU A 1 317 ? 8.581   -5.143  10.623  1.00 11.39 ?  319  LEU A CD2 1 
ATOM   2373 N  N   . ALA A 1 318 ? 7.414   -7.312  5.808   1.00 12.05 ?  320  ALA A N   1 
ATOM   2374 C  CA  . ALA A 1 318 ? 7.235   -8.326  4.762   1.00 14.98 ?  320  ALA A CA  1 
ATOM   2375 C  C   . ALA A 1 318 ? 8.446   -9.256  4.631   1.00 18.73 ?  320  ALA A C   1 
ATOM   2376 O  O   . ALA A 1 318 ? 8.304   -10.405 4.194   1.00 17.78 ?  320  ALA A O   1 
ATOM   2377 C  CB  . ALA A 1 318 ? 6.927   -7.649  3.426   1.00 18.01 ?  320  ALA A CB  1 
ATOM   2378 N  N   . GLU A 1 319 ? 9.629   -8.806  5.028   1.00 10.30 ?  321  GLU A N   1 
ATOM   2379 C  CA  . GLU A 1 319 ? 10.831  -9.618  4.902   1.00 16.16 ?  321  GLU A CA  1 
ATOM   2380 C  C   . GLU A 1 319 ? 11.246  -10.250 6.235   1.00 15.20 ?  321  GLU A C   1 
ATOM   2381 O  O   . GLU A 1 319 ? 12.260  -10.952 6.298   1.00 19.23 ?  321  GLU A O   1 
ATOM   2382 C  CB  . GLU A 1 319 ? 11.957  -8.756  4.293   1.00 14.67 ?  321  GLU A CB  1 
ATOM   2383 C  CG  . GLU A 1 319 ? 13.302  -9.440  4.121   1.00 24.17 ?  321  GLU A CG  1 
ATOM   2384 C  CD  . GLU A 1 319 ? 14.372  -8.557  3.484   1.00 23.13 ?  321  GLU A CD  1 
ATOM   2385 O  OE1 . GLU A 1 319 ? 14.031  -7.570  2.783   1.00 23.57 ?  321  GLU A OE1 1 
ATOM   2386 O  OE2 . GLU A 1 319 ? 15.567  -8.858  3.701   1.00 26.29 ?  321  GLU A OE2 1 
ATOM   2387 N  N   . GLY A 1 320 ? 10.472  -10.038 7.295   1.00 10.32 ?  322  GLY A N   1 
ATOM   2388 C  CA  . GLY A 1 320 ? 10.710  -10.685 8.566   1.00 11.71 ?  322  GLY A CA  1 
ATOM   2389 C  C   . GLY A 1 320 ? 11.526  -9.872  9.556   1.00 16.07 ?  322  GLY A C   1 
ATOM   2390 O  O   . GLY A 1 320 ? 11.372  -8.653  9.643   1.00 14.96 ?  322  GLY A O   1 
ATOM   2391 N  N   . LEU A 1 321 ? 12.386  -10.543 10.325  1.00 10.62 ?  323  LEU A N   1 
ATOM   2392 C  CA  . LEU A 1 321 ? 13.100  -9.875  11.411  1.00 11.40 ?  323  LEU A CA  1 
ATOM   2393 C  C   . LEU A 1 321 ? 14.348  -9.128  10.948  1.00 11.49 ?  323  LEU A C   1 
ATOM   2394 O  O   . LEU A 1 321 ? 14.694  -8.100  11.535  1.00 11.82 ?  323  LEU A O   1 
ATOM   2395 C  CB  . LEU A 1 321 ? 13.501  -10.891 12.483  1.00 14.40 ?  323  LEU A CB  1 
ATOM   2396 C  CG  . LEU A 1 321 ? 12.380  -11.500 13.324  1.00 15.42 ?  323  LEU A CG  1 
ATOM   2397 C  CD1 . LEU A 1 321 ? 12.980  -12.200 14.544  1.00 21.73 ?  323  LEU A CD1 1 
ATOM   2398 C  CD2 . LEU A 1 321 ? 11.422  -10.424 13.767  1.00 18.66 ?  323  LEU A CD2 1 
ATOM   2399 N  N   . GLY A 1 322 ? 15.056  -9.630  9.957   1.00 11.57 ?  324  GLY A N   1 
ATOM   2400 C  CA  . GLY A 1 322 ? 16.320  -9.025  9.593   1.00 14.26 ?  324  GLY A CA  1 
ATOM   2401 C  C   . GLY A 1 322 ? 17.386  -10.082 9.379   1.00 17.96 ?  324  GLY A C   1 
ATOM   2402 O  O   . GLY A 1 322 ? 17.084  -11.252 9.154   1.00 15.64 ?  324  GLY A O   1 
ATOM   2403 N  N   . SER A 1 323 ? 18.645  -9.655  9.473   1.00 12.38 ?  325  SER A N   1 
ATOM   2404 C  CA  . SER A 1 323 ? 19.772  -10.502 9.084   1.00 14.21 ?  325  SER A CA  1 
ATOM   2405 C  C   . SER A 1 323 ? 19.950  -11.676 10.044  1.00 14.25 ?  325  SER A C   1 
ATOM   2406 O  O   . SER A 1 323 ? 19.522  -11.622 11.197  1.00 15.19 ?  325  SER A O   1 
ATOM   2407 C  CB  . SER A 1 323 ? 21.060  -9.686  9.054   1.00 18.47 ?  325  SER A CB  1 
ATOM   2408 O  OG  . SER A 1 323 ? 21.492  -9.397  10.372  1.00 17.61 ?  325  SER A OG  1 
ATOM   2409 N  N   . PRO A 1 324 ? 20.613  -12.746 9.602   1.00 13.94 ?  326  PRO A N   1 
ATOM   2410 C  CA  . PRO A 1 324 ? 20.900  -13.843 10.543  1.00 18.84 ?  326  PRO A CA  1 
ATOM   2411 C  C   . PRO A 1 324 ? 21.673  -13.386 11.772  1.00 17.45 ?  326  PRO A C   1 
ATOM   2412 O  O   . PRO A 1 324 ? 21.361  -13.839 12.883  1.00 16.55 ?  326  PRO A O   1 
ATOM   2413 C  CB  . PRO A 1 324 ? 21.693  -14.857 9.704   1.00 21.75 ?  326  PRO A CB  1 
ATOM   2414 C  CG  . PRO A 1 324 ? 21.552  -14.434 8.277   1.00 23.76 ?  326  PRO A CG  1 
ATOM   2415 C  CD  . PRO A 1 324 ? 20.907  -13.084 8.199   1.00 19.60 ?  326  PRO A CD  1 
ATOM   2416 N  N   . GLU A 1 325 ? 22.639  -12.473 11.615  1.00 13.50 ?  327  GLU A N   1 
ATOM   2417 C  CA  . GLU A 1 325 ? 23.403  -11.993 12.768  1.00 16.23 ?  327  GLU A CA  1 
ATOM   2418 C  C   . GLU A 1 325 ? 22.498  -11.252 13.750  1.00 14.81 ?  327  GLU A C   1 
ATOM   2419 O  O   . GLU A 1 325 ? 22.583  -11.453 14.970  1.00 15.42 ?  327  GLU A O   1 
ATOM   2420 C  CB  . GLU A 1 325 ? 24.544  -11.080 12.307  1.00 16.17 ?  327  GLU A CB  1 
ATOM   2421 C  CG  . GLU A 1 325 ? 25.570  -11.759 11.399  1.00 19.92 ?  327  GLU A CG  1 
ATOM   2422 C  CD  . GLU A 1 325 ? 25.236  -11.616 9.905   1.00 27.63 ?  327  GLU A CD  1 
ATOM   2423 O  OE1 . GLU A 1 325 ? 26.164  -11.341 9.116   1.00 41.69 ?  327  GLU A OE1 1 
ATOM   2424 O  OE2 . GLU A 1 325 ? 24.050  -11.753 9.517   1.00 24.37 ?  327  GLU A OE2 1 
ATOM   2425 N  N   . PHE A 1 326 ? 21.637  -10.371 13.232  1.00 11.70 ?  328  PHE A N   1 
ATOM   2426 C  CA  . PHE A 1 326 ? 20.677  -9.673  14.085  1.00 12.50 ?  328  PHE A CA  1 
ATOM   2427 C  C   . PHE A 1 326 ? 19.787  -10.669 14.824  1.00 14.88 ?  328  PHE A C   1 
ATOM   2428 O  O   . PHE A 1 326 ? 19.572  -10.550 16.036  1.00 11.66 ?  328  PHE A O   1 
ATOM   2429 C  CB  . PHE A 1 326 ? 19.828  -8.720  13.230  1.00 11.78 ?  328  PHE A CB  1 
ATOM   2430 C  CG  . PHE A 1 326 ? 18.817  -7.904  14.005  1.00 11.43 ?  328  PHE A CG  1 
ATOM   2431 C  CD1 . PHE A 1 326 ? 19.216  -7.038  15.016  1.00 13.41 ?  328  PHE A CD1 1 
ATOM   2432 C  CD2 . PHE A 1 326 ? 17.464  -7.977  13.691  1.00 11.31 ?  328  PHE A CD2 1 
ATOM   2433 C  CE1 . PHE A 1 326 ? 18.269  -6.265  15.714  1.00 13.52 ?  328  PHE A CE1 1 
ATOM   2434 C  CE2 . PHE A 1 326 ? 16.519  -7.222  14.382  1.00 13.48 ?  328  PHE A CE2 1 
ATOM   2435 C  CZ  . PHE A 1 326 ? 16.921  -6.357  15.388  1.00 12.28 ?  328  PHE A CZ  1 
ATOM   2436 N  N   . GLN A 1 327 ? 19.249  -11.658 14.102  1.00 13.38 ?  329  GLN A N   1 
ATOM   2437 C  CA  . GLN A 1 327 ? 18.364  -12.626 14.744  1.00 12.81 ?  329  GLN A CA  1 
ATOM   2438 C  C   . GLN A 1 327 ? 19.094  -13.418 15.824  1.00 16.21 ?  329  GLN A C   1 
ATOM   2439 O  O   . GLN A 1 327 ? 18.523  -13.705 16.885  1.00 15.66 ?  329  GLN A O   1 
ATOM   2440 C  CB  . GLN A 1 327 ? 17.757  -13.559 13.695  1.00 17.69 ?  329  GLN A CB  1 
ATOM   2441 C  CG  . GLN A 1 327 ? 16.903  -12.822 12.677  1.00 20.23 ?  329  GLN A CG  1 
ATOM   2442 C  CD  . GLN A 1 327 ? 16.002  -13.740 11.877  1.00 23.11 ?  329  GLN A CD  1 
ATOM   2443 O  OE1 . GLN A 1 327 ? 15.415  -14.678 12.421  1.00 23.37 ?  329  GLN A OE1 1 
ATOM   2444 N  NE2 . GLN A 1 327 ? 15.856  -13.453 10.586  1.00 20.15 ?  329  GLN A NE2 1 
ATOM   2445 N  N   . SER A 1 328 ? 20.365  -13.751 15.591  1.00 15.93 ?  330  SER A N   1 
ATOM   2446 C  CA  . SER A 1 328 ? 21.099  -14.537 16.583  1.00 16.29 ?  330  SER A CA  1 
ATOM   2447 C  C   . SER A 1 328 ? 21.246  -13.797 17.911  1.00 18.72 ?  330  SER A C   1 
ATOM   2448 O  O   . SER A 1 328 ? 21.400  -14.436 18.955  1.00 19.43 ?  330  SER A O   1 
ATOM   2449 C  CB  . SER A 1 328 ? 22.475  -14.931 16.046  1.00 19.66 ?  330  SER A CB  1 
ATOM   2450 O  OG  . SER A 1 328 ? 23.387  -13.841 16.122  1.00 22.37 ?  330  SER A OG  1 
ATOM   2451 N  N   . LEU A 1 329 ? 21.195  -12.458 17.905  1.00 15.31 ?  331  LEU A N   1 
ATOM   2452 C  CA  . LEU A 1 329 ? 21.366  -11.719 19.153  1.00 18.08 ?  331  LEU A CA  1 
ATOM   2453 C  C   . LEU A 1 329 ? 20.198  -11.928 20.109  1.00 17.56 ?  331  LEU A C   1 
ATOM   2454 O  O   . LEU A 1 329 ? 20.380  -11.867 21.333  1.00 18.43 ?  331  LEU A O   1 
ATOM   2455 C  CB  . LEU A 1 329 ? 21.553  -10.231 18.864  1.00 15.73 ?  331  LEU A CB  1 
ATOM   2456 C  CG  . LEU A 1 329 ? 22.924  -9.885  18.303  1.00 13.51 ?  331  LEU A CG  1 
ATOM   2457 C  CD1 . LEU A 1 329 ? 22.875  -8.541  17.602  1.00 23.14 ?  331  LEU A CD1 1 
ATOM   2458 C  CD2 . LEU A 1 329 ? 23.964  -9.876  19.416  1.00 17.37 ?  331  LEU A CD2 1 
ATOM   2459 N  N   . PHE A 1 330 ? 18.998  -12.161 19.578  1.00 18.57 ?  332  PHE A N   1 
ATOM   2460 C  CA  . PHE A 1 330 ? 17.844  -12.422 20.427  1.00 18.78 ?  332  PHE A CA  1 
ATOM   2461 C  C   . PHE A 1 330 ? 17.953  -13.778 21.113  1.00 23.07 ?  332  PHE A C   1 
ATOM   2462 O  O   . PHE A 1 330 ? 17.458  -13.945 22.233  1.00 22.44 ?  332  PHE A O   1 
ATOM   2463 C  CB  . PHE A 1 330 ? 16.565  -12.343 19.594  1.00 19.04 ?  332  PHE A CB  1 
ATOM   2464 C  CG  . PHE A 1 330 ? 16.254  -10.963 19.085  1.00 19.04 ?  332  PHE A CG  1 
ATOM   2465 C  CD1 . PHE A 1 330 ? 15.550  -10.063 19.867  1.00 19.96 ?  332  PHE A CD1 1 
ATOM   2466 C  CD2 . PHE A 1 330 ? 16.694  -10.556 17.832  1.00 20.91 ?  332  PHE A CD2 1 
ATOM   2467 C  CE1 . PHE A 1 330 ? 15.257  -8.784  19.402  1.00 21.46 ?  332  PHE A CE1 1 
ATOM   2468 C  CE2 . PHE A 1 330 ? 16.417  -9.268  17.359  1.00 21.87 ?  332  PHE A CE2 1 
ATOM   2469 C  CZ  . PHE A 1 330 ? 15.692  -8.388  18.144  1.00 20.14 ?  332  PHE A CZ  1 
ATOM   2470 N  N   . GLU A 1 331 ? 18.580  -14.755 20.450  1.00 19.70 ?  333  GLU A N   1 
ATOM   2471 C  CA  . GLU A 1 331 ? 18.838  -16.052 21.076  1.00 20.51 ?  333  GLU A CA  1 
ATOM   2472 C  C   . GLU A 1 331 ? 19.988  -15.963 22.075  1.00 22.49 ?  333  GLU A C   1 
ATOM   2473 O  O   . GLU A 1 331 ? 19.949  -16.591 23.138  1.00 30.12 ?  333  GLU A O   1 
ATOM   2474 C  CB  . GLU A 1 331 ? 19.159  -17.092 20.004  1.00 22.26 ?  333  GLU A CB  1 
ATOM   2475 N  N   . GLU A 1 332 ? 21.024  -15.198 21.743  1.00 18.29 ?  334  GLU A N   1 
ATOM   2476 C  CA  . GLU A 1 332 ? 22.187  -15.092 22.618  1.00 19.72 ?  334  GLU A CA  1 
ATOM   2477 C  C   . GLU A 1 332 ? 21.886  -14.276 23.873  1.00 22.67 ?  334  GLU A C   1 
ATOM   2478 O  O   . GLU A 1 332 ? 22.476  -14.534 24.931  1.00 24.84 ?  334  GLU A O   1 
ATOM   2479 C  CB  . GLU A 1 332 ? 23.358  -14.479 21.850  1.00 23.48 ?  334  GLU A CB  1 
ATOM   2480 N  N   . HIS A 1 333 ? 20.976  -13.301 23.785  1.00 18.24 ?  335  HIS A N   1 
ATOM   2481 C  CA  . HIS A 1 333 ? 20.658  -12.396 24.893  1.00 19.25 ?  335  HIS A CA  1 
ATOM   2482 C  C   . HIS A 1 333 ? 19.151  -12.328 25.093  1.00 21.95 ?  335  HIS A C   1 
ATOM   2483 O  O   . HIS A 1 333 ? 18.473  -11.489 24.479  1.00 19.63 ?  335  HIS A O   1 
ATOM   2484 C  CB  . HIS A 1 333 ? 21.209  -10.993 24.638  1.00 19.82 ?  335  HIS A CB  1 
ATOM   2485 C  CG  . HIS A 1 333 ? 22.649  -10.970 24.243  1.00 19.36 ?  335  HIS A CG  1 
ATOM   2486 N  ND1 . HIS A 1 333 ? 23.670  -11.057 25.163  1.00 20.42 ?  335  HIS A ND1 1 
ATOM   2487 C  CD2 . HIS A 1 333 ? 23.241  -10.852 23.030  1.00 21.57 ?  335  HIS A CD2 1 
ATOM   2488 C  CE1 . HIS A 1 333 ? 24.830  -11.017 24.532  1.00 24.25 ?  335  HIS A CE1 1 
ATOM   2489 N  NE2 . HIS A 1 333 ? 24.599  -10.892 23.237  1.00 22.10 ?  335  HIS A NE2 1 
ATOM   2490 N  N   . PRO A 1 334 ? 18.587  -13.187 25.952  1.00 24.31 ?  336  PRO A N   1 
ATOM   2491 C  CA  . PRO A 1 334 ? 17.125  -13.167 26.152  1.00 24.67 ?  336  PRO A CA  1 
ATOM   2492 C  C   . PRO A 1 334 ? 16.611  -11.898 26.816  1.00 25.77 ?  336  PRO A C   1 
ATOM   2493 O  O   . PRO A 1 334 ? 15.408  -11.640 26.739  1.00 20.29 ?  336  PRO A O   1 
ATOM   2494 C  CB  . PRO A 1 334 ? 16.863  -14.390 27.044  1.00 26.03 ?  336  PRO A CB  1 
ATOM   2495 C  CG  . PRO A 1 334 ? 18.181  -14.678 27.702  1.00 27.03 ?  336  PRO A CG  1 
ATOM   2496 C  CD  . PRO A 1 334 ? 19.249  -14.239 26.740  1.00 27.15 ?  336  PRO A CD  1 
ATOM   2497 N  N   . THR A 1 335 ? 17.458  -11.119 27.488  1.00 15.01 ?  337  THR A N   1 
ATOM   2498 C  CA  . THR A 1 335 ? 17.056  -9.821  28.018  1.00 17.38 ?  337  THR A CA  1 
ATOM   2499 C  C   . THR A 1 335 ? 17.915  -8.710  27.422  1.00 14.26 ?  337  THR A C   1 
ATOM   2500 O  O   . THR A 1 335 ? 19.085  -8.921  27.078  1.00 13.34 ?  337  THR A O   1 
ATOM   2501 C  CB  . THR A 1 335 ? 17.142  -9.769  29.560  1.00 18.05 ?  337  THR A CB  1 
ATOM   2502 O  OG1 . THR A 1 335 ? 18.511  -9.639  29.982  1.00 20.88 ?  337  THR A OG1 1 
ATOM   2503 C  CG2 . THR A 1 335 ? 16.524  -11.017 30.185  1.00 24.06 ?  337  THR A CG2 1 
ATOM   2504 N  N   . LEU A 1 336 ? 17.319  -7.518  27.306  1.00 14.75 ?  338  LEU A N   1 
ATOM   2505 C  CA  . LEU A 1 336 ? 18.062  -6.348  26.845  1.00 13.40 ?  338  LEU A CA  1 
ATOM   2506 C  C   . LEU A 1 336 ? 19.116  -5.929  27.862  1.00 14.90 ?  338  LEU A C   1 
ATOM   2507 O  O   . LEU A 1 336 ? 20.183  -5.429  27.488  1.00 14.69 ?  338  LEU A O   1 
ATOM   2508 C  CB  . LEU A 1 336 ? 17.102  -5.186  26.586  1.00 16.66 ?  338  LEU A CB  1 
ATOM   2509 C  CG  . LEU A 1 336 ? 16.232  -5.376  25.345  1.00 18.66 ?  338  LEU A CG  1 
ATOM   2510 C  CD1 . LEU A 1 336 ? 15.155  -4.286  25.267  1.00 15.52 ?  338  LEU A CD1 1 
ATOM   2511 C  CD2 . LEU A 1 336 ? 17.079  -5.441  24.083  1.00 16.71 ?  338  LEU A CD2 1 
ATOM   2512 N  N   . GLU A 1 337 ? 18.836  -6.139  29.147  1.00 15.32 ?  339  GLU A N   1 
ATOM   2513 C  CA  . GLU A 1 337 ? 19.799  -5.820  30.192  1.00 17.48 ?  339  GLU A CA  1 
ATOM   2514 C  C   . GLU A 1 337 ? 21.072  -6.652  30.071  1.00 15.98 ?  339  GLU A C   1 
ATOM   2515 O  O   . GLU A 1 337 ? 22.175  -6.133  30.281  1.00 14.56 ?  339  GLU A O   1 
ATOM   2516 C  CB  . GLU A 1 337 ? 19.164  -6.014  31.568  1.00 17.55 ?  339  GLU A CB  1 
ATOM   2517 C  CG  . GLU A 1 337 ? 17.988  -5.092  31.874  1.00 22.57 ?  339  GLU A CG  1 
ATOM   2518 C  CD  . GLU A 1 337 ? 16.717  -5.404  31.082  1.00 33.04 ?  339  GLU A CD  1 
ATOM   2519 O  OE1 . GLU A 1 337 ? 15.888  -4.480  30.948  1.00 40.91 ?  339  GLU A OE1 1 
ATOM   2520 O  OE2 . GLU A 1 337 ? 16.543  -6.549  30.598  1.00 23.39 ?  339  GLU A OE2 1 
ATOM   2521 N  N   . GLY A 1 338 ? 20.946  -7.944  29.759  1.00 14.48 ?  340  GLY A N   1 
ATOM   2522 C  CA  . GLY A 1 338 ? 22.134  -8.765  29.589  1.00 14.95 ?  340  GLY A CA  1 
ATOM   2523 C  C   . GLY A 1 338 ? 22.895  -8.407  28.329  1.00 16.31 ?  340  GLY A C   1 
ATOM   2524 O  O   . GLY A 1 338 ? 24.130  -8.404  28.317  1.00 12.09 ?  340  GLY A O   1 
ATOM   2525 N  N   . PHE A 1 339 ? 22.163  -8.105  27.245  1.00 10.13 ?  341  PHE A N   1 
ATOM   2526 C  CA  . PHE A 1 339 ? 22.790  -7.599  26.035  1.00 11.74 ?  341  PHE A CA  1 
ATOM   2527 C  C   . PHE A 1 339 ? 23.595  -6.348  26.321  1.00 11.96 ?  341  PHE A C   1 
ATOM   2528 O  O   . PHE A 1 339 ? 24.711  -6.185  25.816  1.00 10.48 ?  341  PHE A O   1 
ATOM   2529 C  CB  . PHE A 1 339 ? 21.727  -7.303  24.966  1.00 14.60 ?  341  PHE A CB  1 
ATOM   2530 C  CG  . PHE A 1 339 ? 22.250  -6.489  23.805  1.00 15.26 ?  341  PHE A CG  1 
ATOM   2531 C  CD1 . PHE A 1 339 ? 23.118  -7.067  22.889  1.00 12.48 ?  341  PHE A CD1 1 
ATOM   2532 C  CD2 . PHE A 1 339 ? 21.888  -5.155  23.636  1.00 13.32 ?  341  PHE A CD2 1 
ATOM   2533 C  CE1 . PHE A 1 339 ? 23.630  -6.334  21.822  1.00 15.97 ?  341  PHE A CE1 1 
ATOM   2534 C  CE2 . PHE A 1 339 ? 22.398  -4.408  22.565  1.00 13.13 ?  341  PHE A CE2 1 
ATOM   2535 C  CZ  . PHE A 1 339 ? 23.253  -5.005  21.652  1.00 13.53 ?  341  PHE A CZ  1 
ATOM   2536 N  N   . MET A 1 340 ? 23.052  -5.451  27.145  1.00 10.15 ?  342  MET A N   1 
ATOM   2537 C  CA  . MET A 1 340 ? 23.729  -4.184  27.328  1.00 12.31 ?  342  MET A CA  1 
ATOM   2538 C  C   . MET A 1 340 ? 24.958  -4.398  28.206  1.00 13.69 ?  342  MET A C   1 
ATOM   2539 O  O   . MET A 1 340 ? 26.004  -3.779  27.985  1.00 10.91 ?  342  MET A O   1 
ATOM   2540 C  CB  . MET A 1 340 ? 22.778  -3.175  27.951  1.00 13.90 ?  342  MET A CB  1 
ATOM   2541 C  CG  . MET A 1 340 ? 21.813  -2.524  26.910  1.00 12.54 ?  342  MET A CG  1 
ATOM   2542 S  SD  . MET A 1 340 ? 22.527  -1.772  25.447  1.00 18.99 ?  342  MET A SD  1 
ATOM   2543 C  CE  . MET A 1 340 ? 23.023  -0.191  26.136  1.00 21.72 ?  342  MET A CE  1 
ATOM   2544 N  N   . GLU A 1 341 ? 24.852  -5.309  29.184  1.00 11.20 ?  343  GLU A N   1 
ATOM   2545 C  CA  . GLU A 1 341 ? 26.027  -5.711  29.960  1.00 13.76 ?  343  GLU A CA  1 
ATOM   2546 C  C   . GLU A 1 341 ? 27.140  -6.218  29.047  1.00 12.04 ?  343  GLU A C   1 
ATOM   2547 O  O   . GLU A 1 341 ? 28.313  -5.878  29.234  1.00 15.38 ?  343  GLU A O   1 
ATOM   2548 C  CB  . GLU A 1 341 ? 25.653  -6.810  30.963  1.00 15.74 ?  343  GLU A CB  1 
ATOM   2549 C  CG  . GLU A 1 341 ? 26.814  -7.277  31.855  1.00 17.05 ?  343  GLU A CG  1 
ATOM   2550 C  CD  . GLU A 1 341 ? 27.281  -6.218  32.858  1.00 24.27 ?  343  GLU A CD  1 
ATOM   2551 O  OE1 . GLU A 1 341 ? 26.529  -5.249  33.110  1.00 21.32 ?  343  GLU A OE1 1 
ATOM   2552 O  OE2 . GLU A 1 341 ? 28.422  -6.332  33.365  1.00 19.93 ?  343  GLU A OE2 1 
ATOM   2553 N  N   . ALA A 1 342 ? 26.789  -7.046  28.062  1.00 13.11 ?  344  ALA A N   1 
ATOM   2554 C  CA  . ALA A 1 342 ? 27.791  -7.625  27.169  1.00 14.33 ?  344  ALA A CA  1 
ATOM   2555 C  C   . ALA A 1 342 ? 28.532  -6.547  26.382  1.00 14.65 ?  344  ALA A C   1 
ATOM   2556 O  O   . ALA A 1 342 ? 29.769  -6.576  26.277  1.00 15.89 ?  344  ALA A O   1 
ATOM   2557 C  CB  . ALA A 1 342 ? 27.122  -8.625  26.225  1.00 14.38 ?  344  ALA A CB  1 
ATOM   2558 N  N   . ILE A 1 343 ? 27.802  -5.584  25.804  1.00 11.89 ?  345  ILE A N   1 
ATOM   2559 C  CA  . ILE A 1 343 ? 28.475  -4.667  24.893  1.00 11.94 ?  345  ILE A CA  1 
ATOM   2560 C  C   . ILE A 1 343 ? 29.029  -3.426  25.588  1.00 14.56 ?  345  ILE A C   1 
ATOM   2561 O  O   . ILE A 1 343 ? 29.912  -2.765  25.030  1.00 13.55 ?  345  ILE A O   1 
ATOM   2562 C  CB  . ILE A 1 343 ? 27.561  -4.260  23.723  1.00 13.52 ?  345  ILE A CB  1 
ATOM   2563 C  CG1 . ILE A 1 343 ? 26.315  -3.517  24.204  1.00 14.10 ?  345  ILE A CG1 1 
ATOM   2564 C  CG2 . ILE A 1 343 ? 27.157  -5.508  22.912  1.00 14.28 ?  345  ILE A CG2 1 
ATOM   2565 C  CD1 . ILE A 1 343 ? 25.673  -2.675  23.087  1.00 17.46 ?  345  ILE A CD1 1 
ATOM   2566 N  N   . LEU A 1 344 ? 28.555  -3.096  26.796  1.00 11.84 ?  346  LEU A N   1 
ATOM   2567 C  CA  . LEU A 1 344 ? 29.051  -1.899  27.456  1.00 11.22 ?  346  LEU A CA  1 
ATOM   2568 C  C   . LEU A 1 344 ? 30.359  -2.145  28.202  1.00 16.51 ?  346  LEU A C   1 
ATOM   2569 O  O   . LEU A 1 344 ? 31.138  -1.206  28.399  1.00 18.60 ?  346  LEU A O   1 
ATOM   2570 C  CB  . LEU A 1 344 ? 28.015  -1.367  28.452  1.00 16.55 ?  346  LEU A CB  1 
ATOM   2571 C  CG  . LEU A 1 344 ? 26.801  -0.638  27.895  1.00 16.80 ?  346  LEU A CG  1 
ATOM   2572 C  CD1 . LEU A 1 344 ? 25.994  -0.046  29.053  1.00 19.05 ?  346  LEU A CD1 1 
ATOM   2573 C  CD2 . LEU A 1 344 ? 27.219  0.443   26.920  1.00 19.76 ?  346  LEU A CD2 1 
ATOM   2574 N  N   . LYS A 1 345 ? 30.609  -3.370  28.655  1.00 16.45 ?  347  LYS A N   1 
ATOM   2575 C  CA  . LYS A 1 345 ? 31.731  -3.595  29.566  1.00 18.80 ?  347  LYS A CA  1 
ATOM   2576 C  C   . LYS A 1 345 ? 32.960  -4.173  28.874  1.00 23.68 ?  347  LYS A C   1 
ATOM   2577 O  O   . LYS A 1 345 ? 34.000  -4.328  29.525  1.00 23.77 ?  347  LYS A O   1 
ATOM   2578 C  CB  . LYS A 1 345 ? 31.314  -4.518  30.724  1.00 21.42 ?  347  LYS A CB  1 
ATOM   2579 C  CG  . LYS A 1 345 ? 30.113  -4.048  31.577  1.00 22.44 ?  347  LYS A CG  1 
ATOM   2580 C  CD  . LYS A 1 345 ? 30.117  -2.561  31.918  1.00 25.25 ?  347  LYS A CD  1 
ATOM   2581 C  CE  . LYS A 1 345 ? 28.895  -2.152  32.783  1.00 17.50 ?  347  LYS A CE  1 
ATOM   2582 N  NZ  . LYS A 1 345 ? 28.648  -2.952  34.033  1.00 16.65 ?  347  LYS A NZ  1 
ATOM   2583 N  N   . GLU A 1 346 ? 32.866  -4.500  27.584  1.00 18.30 ?  348  GLU A N   1 
ATOM   2584 C  CA  . GLU A 1 346 ? 33.973  -5.044  26.807  1.00 20.04 ?  348  GLU A CA  1 
ATOM   2585 C  C   . GLU A 1 346 ? 33.792  -4.642  25.352  1.00 23.63 ?  348  GLU A C   1 
ATOM   2586 O  O   . GLU A 1 346 ? 32.691  -4.280  24.917  1.00 22.65 ?  348  GLU A O   1 
ATOM   2587 C  CB  . GLU A 1 346 ? 34.052  -6.574  26.880  1.00 22.15 ?  348  GLU A CB  1 
ATOM   2588 C  CG  . GLU A 1 346 ? 34.556  -7.148  28.175  1.00 28.96 ?  348  GLU A CG  1 
ATOM   2589 C  CD  . GLU A 1 346 ? 36.062  -7.162  28.263  1.00 39.79 ?  348  GLU A CD  1 
ATOM   2590 O  OE1 . GLU A 1 346 ? 36.581  -7.204  29.397  1.00 39.33 ?  348  GLU A OE1 1 
ATOM   2591 O  OE2 . GLU A 1 346 ? 36.723  -7.152  27.201  1.00 46.19 ?  348  GLU A OE2 1 
ATOM   2592 N  N   . GLU A 1 347 ? 34.876  -4.755  24.586  1.00 15.78 ?  349  GLU A N   1 
ATOM   2593 C  CA  . GLU A 1 347 ? 34.820  -4.480  23.147  1.00 20.71 ?  349  GLU A CA  1 
ATOM   2594 C  C   . GLU A 1 347 ? 34.205  -5.681  22.427  1.00 22.77 ?  349  GLU A C   1 
ATOM   2595 O  O   . GLU A 1 347 ? 34.882  -6.520  21.828  1.00 23.53 ?  349  GLU A O   1 
ATOM   2596 C  CB  . GLU A 1 347 ? 36.202  -4.135  22.601  1.00 24.73 ?  349  GLU A CB  1 
ATOM   2597 C  CG  . GLU A 1 347 ? 36.782  -2.845  23.175  1.00 24.57 ?  349  GLU A CG  1 
ATOM   2598 C  CD  . GLU A 1 347 ? 35.941  -1.617  22.818  1.00 30.83 ?  349  GLU A CD  1 
ATOM   2599 O  OE1 . GLU A 1 347 ? 36.205  -0.991  21.765  1.00 25.99 ?  349  GLU A OE1 1 
ATOM   2600 O  OE2 . GLU A 1 347 ? 35.032  -1.262  23.602  1.00 28.44 ?  349  GLU A OE2 1 
ATOM   2601 N  N   . SER A 1 348 ? 32.876  -5.738  22.447  1.00 18.16 ?  350  SER A N   1 
ATOM   2602 C  CA  . SER A 1 348 ? 32.139  -6.857  21.877  1.00 16.80 ?  350  SER A CA  1 
ATOM   2603 C  C   . SER A 1 348 ? 31.338  -6.331  20.698  1.00 13.83 ?  350  SER A C   1 
ATOM   2604 O  O   . SER A 1 348 ? 30.546  -5.400  20.868  1.00 16.68 ?  350  SER A O   1 
ATOM   2605 C  CB  . SER A 1 348 ? 31.232  -7.495  22.933  1.00 16.68 ?  350  SER A CB  1 
ATOM   2606 O  OG  . SER A 1 348 ? 30.328  -8.410  22.349  1.00 19.39 ?  350  SER A OG  1 
ATOM   2607 N  N   . PHE A 1 349 ? 31.570  -6.903  19.505  1.00 14.99 ?  351  PHE A N   1 
ATOM   2608 C  CA  . PHE A 1 349 ? 31.027  -6.375  18.252  1.00 13.79 ?  351  PHE A CA  1 
ATOM   2609 C  C   . PHE A 1 349 ? 30.411  -7.491  17.419  1.00 16.82 ?  351  PHE A C   1 
ATOM   2610 O  O   . PHE A 1 349 ? 31.131  -8.338  16.878  1.00 18.87 ?  351  PHE A O   1 
ATOM   2611 C  CB  . PHE A 1 349 ? 32.110  -5.668  17.432  1.00 13.19 ?  351  PHE A CB  1 
ATOM   2612 C  CG  . PHE A 1 349 ? 32.735  -4.507  18.137  1.00 12.55 ?  351  PHE A CG  1 
ATOM   2613 C  CD1 . PHE A 1 349 ? 31.964  -3.417  18.529  1.00 13.42 ?  351  PHE A CD1 1 
ATOM   2614 C  CD2 . PHE A 1 349 ? 34.081  -4.522  18.451  1.00 17.23 ?  351  PHE A CD2 1 
ATOM   2615 C  CE1 . PHE A 1 349 ? 32.531  -2.348  19.204  1.00 16.42 ?  351  PHE A CE1 1 
ATOM   2616 C  CE2 . PHE A 1 349 ? 34.661  -3.449  19.115  1.00 15.11 ?  351  PHE A CE2 1 
ATOM   2617 C  CZ  . PHE A 1 349 ? 33.886  -2.364  19.500  1.00 11.31 ?  351  PHE A CZ  1 
ATOM   2618 N  N   . THR A 1 350 ? 29.095  -7.439  17.256  1.00 12.60 ?  352  THR A N   1 
ATOM   2619 C  CA  . THR A 1 350 ? 28.341  -8.323  16.378  1.00 13.24 ?  352  THR A CA  1 
ATOM   2620 C  C   . THR A 1 350 ? 27.641  -7.479  15.323  1.00 13.50 ?  352  THR A C   1 
ATOM   2621 O  O   . THR A 1 350 ? 27.106  -6.413  15.640  1.00 13.15 ?  352  THR A O   1 
ATOM   2622 C  CB  . THR A 1 350 ? 27.311  -9.130  17.191  1.00 13.82 ?  352  THR A CB  1 
ATOM   2623 O  OG1 . THR A 1 350 ? 28.001  -9.958  18.147  1.00 16.80 ?  352  THR A OG1 1 
ATOM   2624 C  CG2 . THR A 1 350 ? 26.409  -9.989  16.289  1.00 14.90 ?  352  THR A CG2 1 
ATOM   2625 N  N   . VAL A 1 351 ? 27.661  -7.952  14.071  1.00 12.33 ?  353  VAL A N   1 
ATOM   2626 C  CA  . VAL A 1 351 ? 26.943  -7.272  12.993  1.00 12.30 ?  353  VAL A CA  1 
ATOM   2627 C  C   . VAL A 1 351 ? 25.499  -7.020  13.408  1.00 14.00 ?  353  VAL A C   1 
ATOM   2628 O  O   . VAL A 1 351 ? 24.823  -7.907  13.945  1.00 13.00 ?  353  VAL A O   1 
ATOM   2629 C  CB  . VAL A 1 351 ? 27.013  -8.098  11.692  1.00 13.53 ?  353  VAL A CB  1 
ATOM   2630 C  CG1 . VAL A 1 351 ? 26.000  -7.572  10.661  1.00 13.82 ?  353  VAL A CG1 1 
ATOM   2631 C  CG2 . VAL A 1 351 ? 28.415  -8.067  11.110  1.00 17.88 ?  353  VAL A CG2 1 
ATOM   2632 N  N   . ASP A 1 352 ? 25.038  -5.786  13.195  1.00 12.57 ?  354  ASP A N   1 
ATOM   2633 C  CA  . ASP A 1 352 ? 23.665  -5.327  13.401  1.00 10.97 ?  354  ASP A CA  1 
ATOM   2634 C  C   . ASP A 1 352 ? 23.271  -5.153  14.875  1.00 10.51 ?  354  ASP A C   1 
ATOM   2635 O  O   . ASP A 1 352 ? 22.115  -4.868  15.151  1.00 11.65 ?  354  ASP A O   1 
ATOM   2636 C  CB  . ASP A 1 352 ? 22.653  -6.238  12.672  1.00 12.54 ?  354  ASP A CB  1 
ATOM   2637 C  CG  . ASP A 1 352 ? 22.745  -6.100  11.161  1.00 17.13 ?  354  ASP A CG  1 
ATOM   2638 O  OD1 . ASP A 1 352 ? 23.485  -5.196  10.719  1.00 14.99 ?  354  ASP A OD1 1 
ATOM   2639 O  OD2 . ASP A 1 352 ? 22.080  -6.866  10.411  1.00 16.01 ?  354  ASP A OD2 1 
ATOM   2640 N  N   . GLN A 1 353 ? 24.212  -5.241  15.834  1.00 8.45  ?  355  GLN A N   1 
ATOM   2641 C  CA  . GLN A 1 353 ? 23.830  -5.112  17.243  1.00 9.79  ?  355  GLN A CA  1 
ATOM   2642 C  C   . GLN A 1 353 ? 23.358  -3.704  17.588  1.00 11.29 ?  355  GLN A C   1 
ATOM   2643 O  O   . GLN A 1 353 ? 22.643  -3.520  18.586  1.00 10.20 ?  355  GLN A O   1 
ATOM   2644 C  CB  . GLN A 1 353 ? 24.993  -5.488  18.181  1.00 11.10 ?  355  GLN A CB  1 
ATOM   2645 C  CG  . GLN A 1 353 ? 26.101  -4.442  18.237  1.00 9.85  ?  355  GLN A CG  1 
ATOM   2646 C  CD  . GLN A 1 353 ? 27.283  -4.884  19.107  1.00 14.31 ?  355  GLN A CD  1 
ATOM   2647 O  OE1 . GLN A 1 353 ? 27.563  -6.075  19.224  1.00 14.62 ?  355  GLN A OE1 1 
ATOM   2648 N  NE2 . GLN A 1 353 ? 28.002  -3.920  19.667  1.00 14.42 ?  355  GLN A NE2 1 
ATOM   2649 N  N   . TRP A 1 354 ? 23.751  -2.704  16.796  1.00 9.06  ?  356  TRP A N   1 
ATOM   2650 C  CA  . TRP A 1 354 ? 23.371  -1.327  17.086  1.00 9.75  ?  356  TRP A CA  1 
ATOM   2651 C  C   . TRP A 1 354 ? 21.854  -1.134  17.103  1.00 7.74  ?  356  TRP A C   1 
ATOM   2652 O  O   . TRP A 1 354 ? 21.359  -0.319  17.881  1.00 7.94  ?  356  TRP A O   1 
ATOM   2653 C  CB  . TRP A 1 354 ? 24.017  -0.378  16.072  1.00 10.39 ?  356  TRP A CB  1 
ATOM   2654 C  CG  . TRP A 1 354 ? 24.099  -0.924  14.673  1.00 8.49  ?  356  TRP A CG  1 
ATOM   2655 C  CD1 . TRP A 1 354 ? 23.135  -0.858  13.704  1.00 11.23 ?  356  TRP A CD1 1 
ATOM   2656 C  CD2 . TRP A 1 354 ? 25.210  -1.625  14.090  1.00 10.19 ?  356  TRP A CD2 1 
ATOM   2657 N  NE1 . TRP A 1 354 ? 23.582  -1.477  12.550  1.00 11.34 ?  356  TRP A NE1 1 
ATOM   2658 C  CE2 . TRP A 1 354 ? 24.857  -1.943  12.766  1.00 9.07  ?  356  TRP A CE2 1 
ATOM   2659 C  CE3 . TRP A 1 354 ? 26.476  -2.011  14.570  1.00 9.35  ?  356  TRP A CE3 1 
ATOM   2660 C  CZ2 . TRP A 1 354 ? 25.715  -2.633  11.904  1.00 11.12 ?  356  TRP A CZ2 1 
ATOM   2661 C  CZ3 . TRP A 1 354 ? 27.336  -2.694  13.711  1.00 9.42  ?  356  TRP A CZ3 1 
ATOM   2662 C  CH2 . TRP A 1 354 ? 26.953  -2.989  12.389  1.00 9.27  ?  356  TRP A CH2 1 
ATOM   2663 N  N   . GLN A 1 355 ? 21.090  -1.875  16.287  1.00 10.62 ?  357  GLN A N   1 
ATOM   2664 C  CA  . GLN A 1 355 ? 19.640  -1.671  16.356  1.00 8.48  ?  357  GLN A CA  1 
ATOM   2665 C  C   . GLN A 1 355 ? 19.041  -2.302  17.603  1.00 10.59 ?  357  GLN A C   1 
ATOM   2666 O  O   . GLN A 1 355 ? 17.998  -1.841  18.082  1.00 11.65 ?  357  GLN A O   1 
ATOM   2667 C  CB  . GLN A 1 355 ? 18.908  -2.205  15.113  1.00 10.37 ?  357  GLN A CB  1 
ATOM   2668 C  CG  . GLN A 1 355 ? 19.050  -1.314  13.886  1.00 11.49 ?  357  GLN A CG  1 
ATOM   2669 C  CD  . GLN A 1 355 ? 18.522  0.093   14.091  1.00 13.22 ?  357  GLN A CD  1 
ATOM   2670 O  OE1 . GLN A 1 355 ? 19.192  0.941   14.685  1.00 14.78 ?  357  GLN A OE1 1 
ATOM   2671 N  NE2 . GLN A 1 355 ? 17.334  0.367   13.549  1.00 8.34  ?  357  GLN A NE2 1 
ATOM   2672 N  N   . LEU A 1 356 ? 19.678  -3.350  18.142  1.00 11.67 ?  358  LEU A N   1 
ATOM   2673 C  CA  . LEU A 1 356 ? 19.262  -3.856  19.445  1.00 10.56 ?  358  LEU A CA  1 
ATOM   2674 C  C   . LEU A 1 356 ? 19.599  -2.855  20.537  1.00 8.22  ?  358  LEU A C   1 
ATOM   2675 O  O   . LEU A 1 356 ? 18.847  -2.721  21.508  1.00 11.96 ?  358  LEU A O   1 
ATOM   2676 C  CB  . LEU A 1 356 ? 19.918  -5.209  19.738  1.00 14.83 ?  358  LEU A CB  1 
ATOM   2677 C  CG  . LEU A 1 356 ? 19.265  -6.041  20.850  1.00 15.74 ?  358  LEU A CG  1 
ATOM   2678 C  CD1 . LEU A 1 356 ? 17.766  -6.151  20.654  1.00 14.81 ?  358  LEU A CD1 1 
ATOM   2679 C  CD2 . LEU A 1 356 ? 19.904  -7.430  20.975  1.00 18.50 ?  358  LEU A CD2 1 
ATOM   2680 N  N   . GLU A 1 357 ? 20.709  -2.125  20.383  1.00 10.29 ?  359  GLU A N   1 
ATOM   2681 C  CA  . GLU A 1 357 ? 21.036  -1.058  21.327  1.00 10.34 ?  359  GLU A CA  1 
ATOM   2682 C  C   . GLU A 1 357 ? 20.003  0.064   21.258  1.00 11.50 ?  359  GLU A C   1 
ATOM   2683 O  O   . GLU A 1 357 ? 19.629  0.638   22.287  1.00 11.71 ?  359  GLU A O   1 
ATOM   2684 C  CB  . GLU A 1 357 ? 22.439  -0.517  21.037  1.00 15.51 ?  359  GLU A CB  1 
ATOM   2685 C  CG  . GLU A 1 357 ? 22.907  0.598   21.978  1.00 14.12 ?  359  GLU A CG  1 
ATOM   2686 C  CD  . GLU A 1 357 ? 24.398  0.900   21.837  1.00 19.73 ?  359  GLU A CD  1 
ATOM   2687 O  OE1 . GLU A 1 357 ? 25.052  0.312   20.947  1.00 17.98 ?  359  GLU A OE1 1 
ATOM   2688 O  OE2 . GLU A 1 357 ? 24.907  1.744   22.603  1.00 20.36 ?  359  GLU A OE2 1 
ATOM   2689 N  N   . GLU A 1 358 ? 19.529  0.398   20.051  1.00 10.63 ?  360  GLU A N   1 
ATOM   2690 C  CA  . GLU A 1 358 ? 18.487  1.412   19.942  1.00 10.17 ?  360  GLU A CA  1 
ATOM   2691 C  C   . GLU A 1 358 ? 17.172  0.928   20.546  1.00 8.32  ?  360  GLU A C   1 
ATOM   2692 O  O   . GLU A 1 358 ? 16.453  1.704   21.190  1.00 11.21 ?  360  GLU A O   1 
ATOM   2693 C  CB  . GLU A 1 358 ? 18.301  1.832   18.485  1.00 8.99  ?  360  GLU A CB  1 
ATOM   2694 C  CG  . GLU A 1 358 ? 19.534  2.471   17.830  1.00 9.24  ?  360  GLU A CG  1 
ATOM   2695 C  CD  . GLU A 1 358 ? 19.867  3.842   18.422  1.00 14.64 ?  360  GLU A CD  1 
ATOM   2696 O  OE1 . GLU A 1 358 ? 18.968  4.467   19.026  1.00 16.29 ?  360  GLU A OE1 1 
ATOM   2697 O  OE2 . GLU A 1 358 ? 21.008  4.339   18.213  1.00 17.64 ?  360  GLU A OE2 1 
ATOM   2698 N  N   . LEU A 1 359 ? 16.842  -0.350  20.362  1.00 8.84  ?  361  LEU A N   1 
ATOM   2699 C  CA  . LEU A 1 359 ? 15.639  -0.882  21.007  1.00 7.55  ?  361  LEU A CA  1 
ATOM   2700 C  C   . LEU A 1 359 ? 15.768  -0.838  22.527  1.00 9.80  ?  361  LEU A C   1 
ATOM   2701 O  O   . LEU A 1 359 ? 14.794  -0.585  23.237  1.00 9.11  ?  361  LEU A O   1 
ATOM   2702 C  CB  . LEU A 1 359 ? 15.378  -2.307  20.529  1.00 7.18  ?  361  LEU A CB  1 
ATOM   2703 C  CG  . LEU A 1 359 ? 14.144  -3.020  21.081  1.00 11.54 ?  361  LEU A CG  1 
ATOM   2704 C  CD1 . LEU A 1 359 ? 12.827  -2.260  20.717  1.00 12.28 ?  361  LEU A CD1 1 
ATOM   2705 C  CD2 . LEU A 1 359 ? 14.126  -4.444  20.539  1.00 11.95 ?  361  LEU A CD2 1 
ATOM   2706 N  N   . ALA A 1 360 ? 16.974  -1.073  23.051  1.00 7.78  ?  362  ALA A N   1 
ATOM   2707 C  CA  . ALA A 1 360 ? 17.179  -0.955  24.488  1.00 12.05 ?  362  ALA A CA  1 
ATOM   2708 C  C   . ALA A 1 360 ? 16.913  0.468   24.959  1.00 11.13 ?  362  ALA A C   1 
ATOM   2709 O  O   . ALA A 1 360 ? 16.289  0.686   26.006  1.00 10.24 ?  362  ALA A O   1 
ATOM   2710 C  CB  . ALA A 1 360 ? 18.609  -1.385  24.831  1.00 9.02  ?  362  ALA A CB  1 
ATOM   2711 N  N   . LYS A 1 361 ? 17.375  1.452   24.182  1.00 10.74 ?  363  LYS A N   1 
ATOM   2712 C  CA  . LYS A 1 361 ? 17.100  2.854   24.487  1.00 13.58 ?  363  LYS A CA  1 
ATOM   2713 C  C   . LYS A 1 361 ? 15.598  3.120   24.556  1.00 12.65 ?  363  LYS A C   1 
ATOM   2714 O  O   . LYS A 1 361 ? 15.125  3.821   25.462  1.00 11.56 ?  363  LYS A O   1 
ATOM   2715 C  CB  . LYS A 1 361 ? 17.769  3.735   23.429  1.00 12.69 ?  363  LYS A CB  1 
ATOM   2716 C  CG  . LYS A 1 361 ? 17.600  5.241   23.607  1.00 14.27 ?  363  LYS A CG  1 
ATOM   2717 C  CD  . LYS A 1 361 ? 18.416  5.958   22.527  1.00 19.67 ?  363  LYS A CD  1 
ATOM   2718 C  CE  . LYS A 1 361 ? 17.986  7.402   22.282  1.00 31.50 ?  363  LYS A CE  1 
ATOM   2719 N  NZ  . LYS A 1 361 ? 19.049  8.152   21.528  1.00 23.82 ?  363  LYS A NZ  1 
ATOM   2720 N  N   . VAL A 1 362 ? 14.835  2.557   23.610  1.00 9.23  ?  364  VAL A N   1 
ATOM   2721 C  CA  . VAL A 1 362 ? 13.381  2.701   23.619  1.00 9.01  ?  364  VAL A CA  1 
ATOM   2722 C  C   . VAL A 1 362 ? 12.782  2.103   24.891  1.00 11.85 ?  364  VAL A C   1 
ATOM   2723 O  O   . VAL A 1 362 ? 11.962  2.734   25.567  1.00 12.61 ?  364  VAL A O   1 
ATOM   2724 C  CB  . VAL A 1 362 ? 12.773  2.054   22.362  1.00 10.52 ?  364  VAL A CB  1 
ATOM   2725 C  CG1 . VAL A 1 362 ? 11.263  1.991   22.493  1.00 8.86  ?  364  VAL A CG1 1 
ATOM   2726 C  CG2 . VAL A 1 362 ? 13.158  2.846   21.128  1.00 10.77 ?  364  VAL A CG2 1 
ATOM   2727 N  N   . ARG A 1 363 ? 13.163  0.872   25.227  1.00 11.80 ?  365  ARG A N   1 
ATOM   2728 C  CA  . ARG A 1 363 ? 12.470  0.206   26.326  1.00 11.40 ?  365  ARG A CA  1 
ATOM   2729 C  C   . ARG A 1 363 ? 12.873  0.732   27.702  1.00 15.14 ?  365  ARG A C   1 
ATOM   2730 O  O   . ARG A 1 363 ? 12.177  0.440   28.677  1.00 14.67 ?  365  ARG A O   1 
ATOM   2731 C  CB  . ARG A 1 363 ? 12.681  -1.308  26.257  1.00 11.60 ?  365  ARG A CB  1 
ATOM   2732 C  CG  . ARG A 1 363 ? 12.249  -1.960  24.955  1.00 12.69 ?  365  ARG A CG  1 
ATOM   2733 C  CD  . ARG A 1 363 ? 10.733  -1.945  24.750  1.00 14.74 ?  365  ARG A CD  1 
ATOM   2734 N  NE  . ARG A 1 363 ? 10.059  -1.909  26.035  1.00 20.75 ?  365  ARG A NE  1 
ATOM   2735 C  CZ  . ARG A 1 363 ? 9.700   -2.987  26.713  1.00 24.87 ?  365  ARG A CZ  1 
ATOM   2736 N  NH1 . ARG A 1 363 ? 9.939   -4.195  26.211  1.00 20.93 ?  365  ARG A NH1 1 
ATOM   2737 N  NH2 . ARG A 1 363 ? 9.097   -2.852  27.885  1.00 22.02 ?  365  ARG A NH2 1 
ATOM   2738 N  N   . ARG A 1 364 ? 13.956  1.506   27.817  1.00 16.16 ?  366  ARG A N   1 
ATOM   2739 C  CA  . ARG A 1 364 ? 14.214  2.183   29.084  1.00 16.23 ?  366  ARG A CA  1 
ATOM   2740 C  C   . ARG A 1 364 ? 13.187  3.280   29.350  1.00 16.94 ?  366  ARG A C   1 
ATOM   2741 O  O   . ARG A 1 364 ? 13.012  3.687   30.505  1.00 17.63 ?  366  ARG A O   1 
ATOM   2742 C  CB  . ARG A 1 364 ? 15.627  2.773   29.096  1.00 16.32 ?  366  ARG A CB  1 
ATOM   2743 C  CG  . ARG A 1 364 ? 16.714  1.722   29.205  1.00 13.76 ?  366  ARG A CG  1 
ATOM   2744 C  CD  . ARG A 1 364 ? 18.087  2.320   29.592  1.00 18.50 ?  366  ARG A CD  1 
ATOM   2745 N  NE  . ARG A 1 364 ? 18.589  3.259   28.588  1.00 16.23 ?  366  ARG A NE  1 
ATOM   2746 C  CZ  . ARG A 1 364 ? 19.277  2.907   27.504  1.00 14.35 ?  366  ARG A CZ  1 
ATOM   2747 N  NH1 . ARG A 1 364 ? 19.564  1.633   27.274  1.00 15.40 ?  366  ARG A NH1 1 
ATOM   2748 N  NH2 . ARG A 1 364 ? 19.690  3.833   26.650  1.00 18.05 ?  366  ARG A NH2 1 
ATOM   2749 N  N   . LYS A 1 365 ? 12.489  3.751   28.317  1.00 13.24 ?  367  LYS A N   1 
ATOM   2750 C  CA  . LYS A 1 365 ? 11.527  4.837   28.470  1.00 13.01 ?  367  LYS A CA  1 
ATOM   2751 C  C   . LYS A 1 365 ? 10.081  4.398   28.310  1.00 16.15 ?  367  LYS A C   1 
ATOM   2752 O  O   . LYS A 1 365 ? 9.205   4.935   28.994  1.00 16.53 ?  367  LYS A O   1 
ATOM   2753 C  CB  . LYS A 1 365 ? 11.830  5.954   27.460  1.00 15.11 ?  367  LYS A CB  1 
ATOM   2754 C  CG  . LYS A 1 365 ? 10.934  7.190   27.605  1.00 13.97 ?  367  LYS A CG  1 
ATOM   2755 C  CD  . LYS A 1 365 ? 11.403  8.323   26.723  1.00 17.70 ?  367  LYS A CD  1 
ATOM   2756 C  CE  . LYS A 1 365 ? 10.615  9.577   27.029  1.00 19.12 ?  367  LYS A CE  1 
ATOM   2757 N  NZ  . LYS A 1 365 ? 11.069  10.750  26.239  1.00 19.15 ?  367  LYS A NZ  1 
ATOM   2758 N  N   . ALA A 1 366 ? 9.809   3.411   27.465  1.00 12.68 ?  368  ALA A N   1 
ATOM   2759 C  CA  . ALA A 1 366 ? 8.428   3.142   27.086  1.00 10.97 ?  368  ALA A CA  1 
ATOM   2760 C  C   . ALA A 1 366 ? 8.201   1.659   26.850  1.00 11.72 ?  368  ALA A C   1 
ATOM   2761 O  O   . ALA A 1 366 ? 9.109   0.932   26.452  1.00 13.63 ?  368  ALA A O   1 
ATOM   2762 C  CB  . ALA A 1 366 ? 8.039   3.916   25.822  1.00 12.92 ?  368  ALA A CB  1 
ATOM   2763 N  N   . ARG A 1 367 ? 6.953   1.238   27.073  1.00 11.35 ?  369  ARG A N   1 
ATOM   2764 C  CA  . ARG A 1 367 ? 6.441   -0.049  26.639  1.00 13.19 ?  369  ARG A CA  1 
ATOM   2765 C  C   . ARG A 1 367 ? 6.126   0.015   25.143  1.00 11.51 ?  369  ARG A C   1 
ATOM   2766 O  O   . ARG A 1 367 ? 5.840   1.083   24.604  1.00 11.98 ?  369  ARG A O   1 
ATOM   2767 C  CB  . ARG A 1 367 ? 5.169   -0.391  27.415  1.00 15.07 ?  369  ARG A CB  1 
ATOM   2768 C  CG  . ARG A 1 367 ? 5.351   -0.319  28.931  1.00 23.25 ?  369  ARG A CG  1 
ATOM   2769 C  CD  . ARG A 1 367 ? 4.044   -0.580  29.668  1.00 35.12 ?  369  ARG A CD  1 
ATOM   2770 N  NE  . ARG A 1 367 ? 3.589   -1.946  29.436  1.00 47.87 ?  369  ARG A NE  1 
ATOM   2771 C  CZ  . ARG A 1 367 ? 3.907   -2.978  30.211  1.00 48.38 ?  369  ARG A CZ  1 
ATOM   2772 N  NH1 . ARG A 1 367 ? 4.674   -2.793  31.279  1.00 49.04 ?  369  ARG A NH1 1 
ATOM   2773 N  NH2 . ARG A 1 367 ? 3.458   -4.193  29.918  1.00 46.01 ?  369  ARG A NH2 1 
ATOM   2774 N  N   . VAL A 1 368 ? 6.182   -1.128  24.468  1.00 10.80 ?  370  VAL A N   1 
ATOM   2775 C  CA  . VAL A 1 368 ? 5.897   -1.160  23.032  1.00 10.70 ?  370  VAL A CA  1 
ATOM   2776 C  C   . VAL A 1 368 ? 4.844   -2.218  22.750  1.00 10.93 ?  370  VAL A C   1 
ATOM   2777 O  O   . VAL A 1 368 ? 5.002   -3.377  23.152  1.00 12.20 ?  370  VAL A O   1 
ATOM   2778 C  CB  . VAL A 1 368 ? 7.161   -1.449  22.199  1.00 11.28 ?  370  VAL A CB  1 
ATOM   2779 C  CG1 . VAL A 1 368 ? 6.814   -1.557  20.699  1.00 8.65  ?  370  VAL A CG1 1 
ATOM   2780 C  CG2 . VAL A 1 368 ? 8.211   -0.391  22.446  1.00 10.66 ?  370  VAL A CG2 1 
ATOM   2781 N  N   . LYS A 1 369 ? 3.788   -1.831  22.032  1.00 9.80  ?  371  LYS A N   1 
ATOM   2782 C  CA  . LYS A 1 369 ? 2.851   -2.772  21.438  1.00 9.84  ?  371  LYS A CA  1 
ATOM   2783 C  C   . LYS A 1 369 ? 3.102   -2.764  19.932  1.00 11.18 ?  371  LYS A C   1 
ATOM   2784 O  O   . LYS A 1 369 ? 3.208   -1.688  19.333  1.00 10.73 ?  371  LYS A O   1 
ATOM   2785 C  CB  . LYS A 1 369 ? 1.402   -2.381  21.756  1.00 10.99 ?  371  LYS A CB  1 
ATOM   2786 C  CG  . LYS A 1 369 ? 0.983   -2.657  23.210  1.00 11.15 ?  371  LYS A CG  1 
ATOM   2787 C  CD  . LYS A 1 369 ? -0.391  -2.013  23.517  1.00 14.80 ?  371  LYS A CD  1 
ATOM   2788 C  CE  . LYS A 1 369 ? -0.711  -2.016  25.029  1.00 16.24 ?  371  LYS A CE  1 
ATOM   2789 N  NZ  . LYS A 1 369 ? -0.995  -3.419  25.502  1.00 16.86 ?  371  LYS A NZ  1 
ATOM   2790 N  N   . PHE A 1 370 ? 3.209   -3.954  19.330  1.00 10.62 ?  372  PHE A N   1 
ATOM   2791 C  CA  A PHE A 1 370 ? 3.620   -4.119  17.937  0.50 10.20 ?  372  PHE A CA  1 
ATOM   2792 C  CA  B PHE A 1 370 ? 3.615   -4.109  17.935  0.50 10.22 ?  372  PHE A CA  1 
ATOM   2793 C  C   . PHE A 1 370 ? 2.524   -4.835  17.161  1.00 11.82 ?  372  PHE A C   1 
ATOM   2794 O  O   . PHE A 1 370 ? 2.144   -5.953  17.516  1.00 12.63 ?  372  PHE A O   1 
ATOM   2795 C  CB  A PHE A 1 370 ? 4.933   -4.910  17.853  0.50 11.72 ?  372  PHE A CB  1 
ATOM   2796 C  CB  B PHE A 1 370 ? 4.950   -4.862  17.842  0.50 11.73 ?  372  PHE A CB  1 
ATOM   2797 C  CG  A PHE A 1 370 ? 5.771   -4.580  16.644  0.50 11.80 ?  372  PHE A CG  1 
ATOM   2798 C  CG  B PHE A 1 370 ? 5.794   -4.473  16.648  0.50 11.78 ?  372  PHE A CG  1 
ATOM   2799 C  CD1 A PHE A 1 370 ? 6.984   -3.935  16.788  0.50 11.85 ?  372  PHE A CD1 1 
ATOM   2800 C  CD1 B PHE A 1 370 ? 5.296   -4.585  15.352  0.50 10.50 ?  372  PHE A CD1 1 
ATOM   2801 C  CD2 A PHE A 1 370 ? 5.356   -4.946  15.368  0.50 10.04 ?  372  PHE A CD2 1 
ATOM   2802 C  CD2 B PHE A 1 370 ? 7.070   -3.971  16.824  0.50 11.86 ?  372  PHE A CD2 1 
ATOM   2803 C  CE1 A PHE A 1 370 ? 7.763   -3.624  15.680  0.50 12.62 ?  372  PHE A CE1 1 
ATOM   2804 C  CE1 B PHE A 1 370 ? 6.064   -4.222  14.258  0.50 11.48 ?  372  PHE A CE1 1 
ATOM   2805 C  CE2 A PHE A 1 370 ? 6.122   -4.644  14.261  0.50 11.34 ?  372  PHE A CE2 1 
ATOM   2806 C  CE2 B PHE A 1 370 ? 7.847   -3.593  15.732  0.50 12.62 ?  372  PHE A CE2 1 
ATOM   2807 C  CZ  A PHE A 1 370 ? 7.334   -3.984  14.413  0.50 9.90  ?  372  PHE A CZ  1 
ATOM   2808 C  CZ  B PHE A 1 370 ? 7.345   -3.721  14.446  0.50 9.74  ?  372  PHE A CZ  1 
ATOM   2809 N  N   . VAL A 1 371 ? 2.038   -4.201  16.095  1.00 9.39  ?  373  VAL A N   1 
ATOM   2810 C  CA  . VAL A 1 371 ? 0.983   -4.741  15.244  1.00 10.28 ?  373  VAL A CA  1 
ATOM   2811 C  C   . VAL A 1 371 ? 1.604   -5.056  13.891  1.00 9.95  ?  373  VAL A C   1 
ATOM   2812 O  O   . VAL A 1 371 ? 2.126   -4.160  13.219  1.00 10.30 ?  373  VAL A O   1 
ATOM   2813 C  CB  . VAL A 1 371 ? -0.186  -3.755  15.096  1.00 10.82 ?  373  VAL A CB  1 
ATOM   2814 C  CG1 . VAL A 1 371 ? -1.307  -4.370  14.248  1.00 15.39 ?  373  VAL A CG1 1 
ATOM   2815 C  CG2 . VAL A 1 371 ? -0.720  -3.344  16.485  1.00 12.48 ?  373  VAL A CG2 1 
ATOM   2816 N  N   . SER A 1 372 ? 1.567   -6.323  13.494  1.00 10.60 ?  374  SER A N   1 
ATOM   2817 C  CA  . SER A 1 372 ? 2.125   -6.712  12.201  1.00 13.93 ?  374  SER A CA  1 
ATOM   2818 C  C   . SER A 1 372 ? 1.541   -8.056  11.789  1.00 16.94 ?  374  SER A C   1 
ATOM   2819 O  O   . SER A 1 372 ? 1.322   -8.919  12.648  1.00 16.47 ?  374  SER A O   1 
ATOM   2820 C  CB  . SER A 1 372 ? 3.646   -6.822  12.280  1.00 10.73 ?  374  SER A CB  1 
ATOM   2821 O  OG  . SER A 1 372 ? 4.213   -7.203  11.024  1.00 14.25 ?  374  SER A OG  1 
ATOM   2822 N  N   . ASP A 1 373 ? 1.314   -8.246  10.486  1.00 14.59 ?  375  ASP A N   1 
ATOM   2823 C  CA  . ASP A 1 373 ? 1.020   -9.585  9.992   1.00 14.53 ?  375  ASP A CA  1 
ATOM   2824 C  C   . ASP A 1 373 ? 2.190   -10.186 9.229   1.00 18.11 ?  375  ASP A C   1 
ATOM   2825 O  O   . ASP A 1 373 ? 2.005   -11.176 8.522   1.00 18.51 ?  375  ASP A O   1 
ATOM   2826 C  CB  . ASP A 1 373 ? -0.258  -9.607  9.134   1.00 18.25 ?  375  ASP A CB  1 
ATOM   2827 C  CG  . ASP A 1 373 ? -0.162  -8.769  7.861   1.00 25.77 ?  375  ASP A CG  1 
ATOM   2828 O  OD1 . ASP A 1 373 ? 0.839   -8.052  7.640   1.00 24.51 ?  375  ASP A OD1 1 
ATOM   2829 O  OD2 . ASP A 1 373 ? -1.123  -8.833  7.064   1.00 27.58 ?  375  ASP A OD2 1 
ATOM   2830 N  N   . GLY A 1 374 ? 3.402   -9.654  9.407   1.00 13.89 ?  376  GLY A N   1 
ATOM   2831 C  CA  . GLY A 1 374 ? 4.550   -10.146 8.666   1.00 16.29 ?  376  GLY A CA  1 
ATOM   2832 C  C   . GLY A 1 374 ? 5.429   -11.113 9.435   1.00 17.61 ?  376  GLY A C   1 
ATOM   2833 O  O   . GLY A 1 374 ? 6.224   -11.849 8.840   1.00 22.50 ?  376  GLY A O   1 
ATOM   2834 N  N   . VAL A 1 375 ? 5.315   -11.082 10.760  1.00 18.93 ?  377  VAL A N   1 
ATOM   2835 C  CA  . VAL A 1 375 ? 5.998   -11.963 11.713  1.00 16.58 ?  377  VAL A CA  1 
ATOM   2836 C  C   . VAL A 1 375 ? 4.960   -12.519 12.680  1.00 25.00 ?  377  VAL A C   1 
ATOM   2837 O  O   . VAL A 1 375 ? 4.117   -11.750 13.169  1.00 23.64 ?  377  VAL A O   1 
ATOM   2838 C  CB  . VAL A 1 375 ? 7.106   -11.215 12.474  1.00 15.88 ?  377  VAL A CB  1 
ATOM   2839 C  CG1 . VAL A 1 375 ? 7.912   -12.171 13.274  1.00 17.37 ?  377  VAL A CG1 1 
ATOM   2840 C  CG2 . VAL A 1 375 ? 8.053   -10.538 11.480  1.00 21.74 ?  377  VAL A CG2 1 
ATOM   2841 N  N   . PRO A 1 376 ? 4.976   -13.821 12.993  1.00 24.86 ?  378  PRO A N   1 
ATOM   2842 C  CA  . PRO A 1 376 ? 3.992   -14.357 13.946  1.00 21.51 ?  378  PRO A CA  1 
ATOM   2843 C  C   . PRO A 1 376 ? 4.147   -13.727 15.323  1.00 20.42 ?  378  PRO A C   1 
ATOM   2844 O  O   . PRO A 1 376 ? 5.239   -13.313 15.722  1.00 20.02 ?  378  PRO A O   1 
ATOM   2845 C  CB  . PRO A 1 376 ? 4.306   -15.861 13.983  1.00 26.71 ?  378  PRO A CB  1 
ATOM   2846 C  CG  . PRO A 1 376 ? 5.121   -16.138 12.740  1.00 25.62 ?  378  PRO A CG  1 
ATOM   2847 C  CD  . PRO A 1 376 ? 5.901   -14.867 12.505  1.00 23.21 ?  378  PRO A CD  1 
ATOM   2848 N  N   . ALA A 1 377 ? 3.029   -13.658 16.057  1.00 19.00 ?  379  ALA A N   1 
ATOM   2849 C  CA  . ALA A 1 377 ? 3.069   -13.094 17.406  1.00 23.06 ?  379  ALA A CA  1 
ATOM   2850 C  C   . ALA A 1 377 ? 4.086   -13.820 18.286  1.00 18.97 ?  379  ALA A C   1 
ATOM   2851 O  O   . ALA A 1 377 ? 4.778   -13.195 19.097  1.00 17.55 ?  379  ALA A O   1 
ATOM   2852 C  CB  . ALA A 1 377 ? 1.676   -13.135 18.038  1.00 21.34 ?  379  ALA A CB  1 
ATOM   2853 N  N   . ALA A 1 378 ? 4.217   -15.135 18.116  1.00 17.86 ?  380  ALA A N   1 
ATOM   2854 C  CA  . ALA A 1 378 ? 5.143   -15.896 18.952  1.00 20.81 ?  380  ALA A CA  1 
ATOM   2855 C  C   . ALA A 1 378 ? 6.579   -15.412 18.780  1.00 28.91 ?  380  ALA A C   1 
ATOM   2856 O  O   . ALA A 1 378 ? 7.341   -15.341 19.754  1.00 27.19 ?  380  ALA A O   1 
ATOM   2857 C  CB  . ALA A 1 378 ? 5.038   -17.386 18.623  1.00 27.04 ?  380  ALA A CB  1 
ATOM   2858 N  N   . VAL A 1 379 ? 6.962   -15.074 17.548  1.00 24.32 ?  381  VAL A N   1 
ATOM   2859 C  CA  . VAL A 1 379 ? 8.303   -14.558 17.282  1.00 22.74 ?  381  VAL A CA  1 
ATOM   2860 C  C   . VAL A 1 379 ? 8.464   -13.153 17.853  1.00 19.31 ?  381  VAL A C   1 
ATOM   2861 O  O   . VAL A 1 379 ? 9.467   -12.841 18.504  1.00 17.51 ?  381  VAL A O   1 
ATOM   2862 C  CB  . VAL A 1 379 ? 8.584   -14.584 15.770  1.00 22.46 ?  381  VAL A CB  1 
ATOM   2863 C  CG1 . VAL A 1 379 ? 9.952   -14.010 15.475  1.00 19.65 ?  381  VAL A CG1 1 
ATOM   2864 C  CG2 . VAL A 1 379 ? 8.470   -16.006 15.225  1.00 26.96 ?  381  VAL A CG2 1 
ATOM   2865 N  N   . LEU A 1 380 ? 7.479   -12.278 17.621  1.00 16.50 ?  382  LEU A N   1 
ATOM   2866 C  CA  . LEU A 1 380 ? 7.607   -10.898 18.086  1.00 14.37 ?  382  LEU A CA  1 
ATOM   2867 C  C   . LEU A 1 380 ? 7.691   -10.826 19.604  1.00 17.66 ?  382  LEU A C   1 
ATOM   2868 O  O   . LEU A 1 380 ? 8.328   -9.918  20.150  1.00 16.63 ?  382  LEU A O   1 
ATOM   2869 C  CB  . LEU A 1 380 ? 6.424   -10.063 17.585  1.00 13.48 ?  382  LEU A CB  1 
ATOM   2870 C  CG  . LEU A 1 380 ? 6.490   -9.592  16.134  1.00 16.90 ?  382  LEU A CG  1 
ATOM   2871 C  CD1 . LEU A 1 380 ? 5.251   -8.772  15.794  1.00 19.07 ?  382  LEU A CD1 1 
ATOM   2872 C  CD2 . LEU A 1 380 ? 7.756   -8.795  15.865  1.00 17.42 ?  382  LEU A CD2 1 
ATOM   2873 N  N   . SER A 1 381 ? 7.057   -11.774 20.304  1.00 14.49 ?  383  SER A N   1 
ATOM   2874 C  CA  . SER A 1 381 ? 7.058   -11.723 21.759  1.00 19.54 ?  383  SER A CA  1 
ATOM   2875 C  C   . SER A 1 381 ? 8.441   -11.987 22.338  1.00 17.06 ?  383  SER A C   1 
ATOM   2876 O  O   . SER A 1 381 ? 8.686   -11.643 23.498  1.00 23.14 ?  383  SER A O   1 
ATOM   2877 C  CB  . SER A 1 381 ? 6.041   -12.710 22.329  1.00 22.44 ?  383  SER A CB  1 
ATOM   2878 O  OG  . SER A 1 381 ? 6.404   -14.033 22.013  1.00 29.45 ?  383  SER A OG  1 
ATOM   2879 N  N   . ARG A 1 382 ? 9.345   -12.576 21.561  1.00 16.29 ?  384  ARG A N   1 
ATOM   2880 C  CA  . ARG A 1 382 ? 10.730  -12.768 21.984  1.00 20.13 ?  384  ARG A CA  1 
ATOM   2881 C  C   . ARG A 1 382 ? 11.645  -11.660 21.481  1.00 18.09 ?  384  ARG A C   1 
ATOM   2882 O  O   . ARG A 1 382 ? 12.874  -11.774 21.603  1.00 21.13 ?  384  ARG A O   1 
ATOM   2883 C  CB  . ARG A 1 382 ? 11.237  -14.139 21.519  1.00 23.26 ?  384  ARG A CB  1 
ATOM   2884 C  CG  . ARG A 1 382 ? 10.264  -15.265 21.848  1.00 27.04 ?  384  ARG A CG  1 
ATOM   2885 C  CD  . ARG A 1 382 ? 10.849  -16.658 21.684  1.00 34.84 ?  384  ARG A CD  1 
ATOM   2886 N  NE  . ARG A 1 382 ? 10.672  -17.143 20.316  1.00 42.38 ?  384  ARG A NE  1 
ATOM   2887 C  CZ  . ARG A 1 382 ? 9.597   -17.813 19.900  1.00 46.33 ?  384  ARG A CZ  1 
ATOM   2888 N  NH1 . ARG A 1 382 ? 8.591   -18.036 20.736  1.00 45.54 ?  384  ARG A NH1 1 
ATOM   2889 N  NH2 . ARG A 1 382 ? 9.507   -18.231 18.642  1.00 40.96 ?  384  ARG A NH2 1 
ATOM   2890 N  N   . CYS A 1 383 ? 11.070  -10.585 20.932  1.00 19.23 ?  385  CYS A N   1 
ATOM   2891 C  CA  . CYS A 1 383 ? 11.821  -9.423  20.468  1.00 13.70 ?  385  CYS A CA  1 
ATOM   2892 C  C   . CYS A 1 383 ? 11.601  -8.199  21.356  1.00 16.75 ?  385  CYS A C   1 
ATOM   2893 O  O   . CYS A 1 383 ? 11.800  -7.065  20.903  1.00 13.53 ?  385  CYS A O   1 
ATOM   2894 C  CB  . CYS A 1 383 ? 11.448  -9.101  19.021  1.00 14.63 ?  385  CYS A CB  1 
ATOM   2895 S  SG  . CYS A 1 383 ? 11.857  -10.416 17.852  1.00 22.44 ?  385  CYS A SG  1 
ATOM   2896 N  N   . HIS A 1 384 ? 11.174  -8.403  22.610  1.00 13.87 ?  386  HIS A N   1 
ATOM   2897 C  CA  . HIS A 1 384 ? 11.094  -7.336  23.609  1.00 13.39 ?  386  HIS A CA  1 
ATOM   2898 C  C   . HIS A 1 384 ? 10.036  -6.304  23.265  1.00 11.94 ?  386  HIS A C   1 
ATOM   2899 O  O   . HIS A 1 384 ? 10.155  -5.133  23.633  1.00 14.39 ?  386  HIS A O   1 
ATOM   2900 C  CB  . HIS A 1 384 ? 12.454  -6.662  23.808  1.00 13.98 ?  386  HIS A CB  1 
ATOM   2901 C  CG  . HIS A 1 384 ? 13.560  -7.642  24.028  1.00 19.27 ?  386  HIS A CG  1 
ATOM   2902 N  ND1 . HIS A 1 384 ? 14.594  -7.814  23.131  1.00 24.02 ?  386  HIS A ND1 1 
ATOM   2903 C  CD2 . HIS A 1 384 ? 13.758  -8.548  25.012  1.00 18.10 ?  386  HIS A CD2 1 
ATOM   2904 C  CE1 . HIS A 1 384 ? 15.397  -8.767  23.570  1.00 21.38 ?  386  HIS A CE1 1 
ATOM   2905 N  NE2 . HIS A 1 384 ? 14.909  -9.232  24.704  1.00 19.27 ?  386  HIS A NE2 1 
ATOM   2906 N  N   . VAL A 1 385 ? 9.006   -6.737  22.539  1.00 13.20 ?  387  VAL A N   1 
ATOM   2907 C  CA  . VAL A 1 385 ? 7.820   -5.943  22.263  1.00 12.90 ?  387  VAL A CA  1 
ATOM   2908 C  C   . VAL A 1 385 ? 6.623   -6.842  22.546  1.00 14.10 ?  387  VAL A C   1 
ATOM   2909 O  O   . VAL A 1 385 ? 6.743   -8.069  22.592  1.00 13.91 ?  387  VAL A O   1 
ATOM   2910 C  CB  . VAL A 1 385 ? 7.769   -5.422  20.806  1.00 13.74 ?  387  VAL A CB  1 
ATOM   2911 C  CG1 . VAL A 1 385 ? 8.959   -4.527  20.496  1.00 11.83 ?  387  VAL A CG1 1 
ATOM   2912 C  CG2 . VAL A 1 385 ? 7.684   -6.599  19.812  1.00 13.30 ?  387  VAL A CG2 1 
ATOM   2913 N  N   . GLU A 1 386 ? 5.450   -6.222  22.729  1.00 13.36 ?  388  GLU A N   1 
ATOM   2914 C  CA  . GLU A 1 386 ? 4.236   -6.987  22.970  1.00 13.74 ?  388  GLU A CA  1 
ATOM   2915 C  C   . GLU A 1 386 ? 3.428   -7.045  21.681  1.00 13.94 ?  388  GLU A C   1 
ATOM   2916 O  O   . GLU A 1 386 ? 2.924   -6.001  21.236  1.00 14.71 ?  388  GLU A O   1 
ATOM   2917 C  CB  . GLU A 1 386 ? 3.399   -6.354  24.090  1.00 15.50 ?  388  GLU A CB  1 
ATOM   2918 C  CG  . GLU A 1 386 ? 2.124   -7.138  24.441  1.00 16.96 ?  388  GLU A CG  1 
ATOM   2919 C  CD  . GLU A 1 386 ? 1.054   -6.274  25.131  1.00 21.86 ?  388  GLU A CD  1 
ATOM   2920 O  OE1 . GLU A 1 386 ? -0.093  -6.752  25.321  1.00 24.71 ?  388  GLU A OE1 1 
ATOM   2921 O  OE2 . GLU A 1 386 ? 1.344   -5.108  25.456  1.00 23.76 ?  388  GLU A OE2 1 
ATOM   2922 N  N   . PRO A 1 387 ? 3.252   -8.211  21.056  1.00 14.34 ?  389  PRO A N   1 
ATOM   2923 C  CA  . PRO A 1 387 ? 2.389   -8.275  19.860  1.00 13.50 ?  389  PRO A CA  1 
ATOM   2924 C  C   . PRO A 1 387 ? 0.920   -8.097  20.230  1.00 15.54 ?  389  PRO A C   1 
ATOM   2925 O  O   . PRO A 1 387 ? 0.433   -8.663  21.212  1.00 15.86 ?  389  PRO A O   1 
ATOM   2926 C  CB  . PRO A 1 387 ? 2.657   -9.674  19.284  1.00 15.60 ?  389  PRO A CB  1 
ATOM   2927 C  CG  . PRO A 1 387 ? 3.308   -10.453 20.396  1.00 18.50 ?  389  PRO A CG  1 
ATOM   2928 C  CD  . PRO A 1 387 ? 3.879   -9.504  21.392  1.00 18.60 ?  389  PRO A CD  1 
ATOM   2929 N  N   . VAL A 1 388 ? 0.217   -7.282  19.454  1.00 13.55 ?  390  VAL A N   1 
ATOM   2930 C  CA  . VAL A 1 388 ? -1.210  -7.076  19.644  1.00 13.46 ?  390  VAL A CA  1 
ATOM   2931 C  C   . VAL A 1 388 ? -1.864  -7.190  18.278  1.00 13.30 ?  390  VAL A C   1 
ATOM   2932 O  O   . VAL A 1 388 ? -1.284  -6.772  17.267  1.00 13.16 ?  390  VAL A O   1 
ATOM   2933 C  CB  . VAL A 1 388 ? -1.522  -5.715  20.313  1.00 13.92 ?  390  VAL A CB  1 
ATOM   2934 C  CG1 . VAL A 1 388 ? -3.014  -5.561  20.550  1.00 13.01 ?  390  VAL A CG1 1 
ATOM   2935 C  CG2 . VAL A 1 388 ? -0.761  -5.555  21.615  1.00 12.48 ?  390  VAL A CG2 1 
ATOM   2936 N  N   . ALA A 1 389 ? -3.067  -7.767  18.243  1.00 15.10 ?  391  ALA A N   1 
ATOM   2937 C  CA  . ALA A 1 389 ? -3.659  -8.156  16.963  1.00 16.24 ?  391  ALA A CA  1 
ATOM   2938 C  C   . ALA A 1 389 ? -3.988  -6.954  16.085  1.00 15.32 ?  391  ALA A C   1 
ATOM   2939 O  O   . ALA A 1 389 ? -3.881  -7.036  14.857  1.00 14.94 ?  391  ALA A O   1 
ATOM   2940 C  CB  . ALA A 1 389 ? -4.909  -9.005  17.202  1.00 18.23 ?  391  ALA A CB  1 
ATOM   2941 N  N   . THR A 1 390 ? -4.427  -5.841  16.676  1.00 12.95 ?  392  THR A N   1 
ATOM   2942 C  CA  . THR A 1 390 ? -4.812  -4.671  15.894  1.00 14.22 ?  392  THR A CA  1 
ATOM   2943 C  C   . THR A 1 390 ? -4.375  -3.414  16.630  1.00 12.90 ?  392  THR A C   1 
ATOM   2944 O  O   . THR A 1 390 ? -4.215  -3.423  17.852  1.00 12.65 ?  392  THR A O   1 
ATOM   2945 C  CB  . THR A 1 390 ? -6.341  -4.594  15.624  1.00 14.48 ?  392  THR A CB  1 
ATOM   2946 O  OG1 . THR A 1 390 ? -7.016  -4.095  16.785  1.00 15.58 ?  392  THR A OG1 1 
ATOM   2947 C  CG2 . THR A 1 390 ? -6.947  -5.963  15.224  1.00 14.86 ?  392  THR A CG2 1 
ATOM   2948 N  N   . VAL A 1 391 ? -4.193  -2.325  15.873  1.00 10.70 ?  393  VAL A N   1 
ATOM   2949 C  CA  . VAL A 1 391 ? -3.861  -1.041  16.490  1.00 13.47 ?  393  VAL A CA  1 
ATOM   2950 C  C   . VAL A 1 391 ? -5.004  -0.554  17.375  1.00 12.76 ?  393  VAL A C   1 
ATOM   2951 O  O   . VAL A 1 391 ? -4.781  -0.023  18.469  1.00 13.55 ?  393  VAL A O   1 
ATOM   2952 C  CB  . VAL A 1 391 ? -3.496  -0.009  15.403  1.00 13.56 ?  393  VAL A CB  1 
ATOM   2953 C  CG1 . VAL A 1 391 ? -3.325  1.378   15.996  1.00 10.40 ?  393  VAL A CG1 1 
ATOM   2954 C  CG2 . VAL A 1 391 ? -2.234  -0.445  14.682  1.00 13.30 ?  393  VAL A CG2 1 
ATOM   2955 N  N   . GLU A 1 392 ? -6.250  -0.714  16.917  1.00 11.72 ?  394  GLU A N   1 
ATOM   2956 C  CA  . GLU A 1 392 ? -7.373  -0.270  17.734  1.00 14.92 ?  394  GLU A CA  1 
ATOM   2957 C  C   . GLU A 1 392 ? -7.420  -1.020  19.067  1.00 14.63 ?  394  GLU A C   1 
ATOM   2958 O  O   . GLU A 1 392 ? -7.666  -0.418  20.121  1.00 14.14 ?  394  GLU A O   1 
ATOM   2959 C  CB  . GLU A 1 392 ? -8.668  -0.435  16.933  1.00 14.58 ?  394  GLU A CB  1 
ATOM   2960 C  CG  . GLU A 1 392 ? -9.748  0.582   17.247  1.00 27.10 ?  394  GLU A CG  1 
ATOM   2961 C  CD  . GLU A 1 392 ? -11.073 0.207   16.606  1.00 28.46 ?  394  GLU A CD  1 
ATOM   2962 O  OE1 . GLU A 1 392 ? -11.057 -0.039  15.385  1.00 25.34 ?  394  GLU A OE1 1 
ATOM   2963 O  OE2 . GLU A 1 392 ? -12.118 0.223   17.292  1.00 25.28 ?  394  GLU A OE2 1 
ATOM   2964 N  N   . LEU A 1 393 ? -7.148  -2.326  19.056  1.00 13.22 ?  395  LEU A N   1 
ATOM   2965 C  CA  . LEU A 1 393 ? -7.102  -3.060  20.315  1.00 12.15 ?  395  LEU A CA  1 
ATOM   2966 C  C   . LEU A 1 393 ? -5.937  -2.588  21.185  1.00 13.29 ?  395  LEU A C   1 
ATOM   2967 O  O   . LEU A 1 393 ? -6.089  -2.411  22.400  1.00 13.34 ?  395  LEU A O   1 
ATOM   2968 C  CB  . LEU A 1 393 ? -6.987  -4.559  20.046  1.00 12.81 ?  395  LEU A CB  1 
ATOM   2969 C  CG  . LEU A 1 393 ? -6.756  -5.434  21.272  1.00 19.08 ?  395  LEU A CG  1 
ATOM   2970 C  CD1 . LEU A 1 393 ? -7.914  -5.237  22.254  1.00 18.89 ?  395  LEU A CD1 1 
ATOM   2971 C  CD2 . LEU A 1 393 ? -6.591  -6.904  20.876  1.00 16.86 ?  395  LEU A CD2 1 
ATOM   2972 N  N   . ALA A 1 394 ? -4.765  -2.380  20.579  1.00 11.98 ?  396  ALA A N   1 
ATOM   2973 C  CA  . ALA A 1 394 ? -3.597  -1.938  21.339  1.00 14.83 ?  396  ALA A CA  1 
ATOM   2974 C  C   . ALA A 1 394 ? -3.842  -0.600  22.032  1.00 11.69 ?  396  ALA A C   1 
ATOM   2975 O  O   . ALA A 1 394 ? -3.447  -0.413  23.189  1.00 11.24 ?  396  ALA A O   1 
ATOM   2976 C  CB  . ALA A 1 394 ? -2.387  -1.845  20.407  1.00 13.43 ?  396  ALA A CB  1 
ATOM   2977 N  N   . VAL A 1 395 ? -4.478  0.346   21.332  1.00 10.59 ?  397  VAL A N   1 
ATOM   2978 C  CA  . VAL A 1 395 ? -4.804  1.648   21.920  1.00 12.73 ?  397  VAL A CA  1 
ATOM   2979 C  C   . VAL A 1 395 ? -5.806  1.497   23.067  1.00 15.50 ?  397  VAL A C   1 
ATOM   2980 O  O   . VAL A 1 395 ? -5.623  2.076   24.149  1.00 14.01 ?  397  VAL A O   1 
ATOM   2981 C  CB  . VAL A 1 395 ? -5.319  2.601   20.824  1.00 12.23 ?  397  VAL A CB  1 
ATOM   2982 C  CG1 . VAL A 1 395 ? -5.894  3.893   21.424  1.00 13.23 ?  397  VAL A CG1 1 
ATOM   2983 C  CG2 . VAL A 1 395 ? -4.186  2.933   19.842  1.00 12.63 ?  397  VAL A CG2 1 
ATOM   2984 N  N   . ALA A 1 396 ? -6.872  0.711   22.855  1.00 14.25 ?  398  ALA A N   1 
ATOM   2985 C  CA  . ALA A 1 396 ? -7.833  0.457   23.931  1.00 14.10 ?  398  ALA A CA  1 
ATOM   2986 C  C   . ALA A 1 396 ? -7.161  -0.142  25.164  1.00 15.83 ?  398  ALA A C   1 
ATOM   2987 O  O   . ALA A 1 396 ? -7.477  0.241   26.299  1.00 15.98 ?  398  ALA A O   1 
ATOM   2988 C  CB  . ALA A 1 396 ? -8.942  -0.468  23.432  1.00 16.90 ?  398  ALA A CB  1 
ATOM   2989 N  N   . GLN A 1 397 ? -6.254  -1.105  24.964  1.00 12.86 ?  399  GLN A N   1 
ATOM   2990 C  CA  . GLN A 1 397 ? -5.518  -1.696  26.081  1.00 14.42 ?  399  GLN A CA  1 
ATOM   2991 C  C   . GLN A 1 397 ? -4.691  -0.651  26.815  1.00 19.81 ?  399  GLN A C   1 
ATOM   2992 O  O   . GLN A 1 397 ? -4.705  -0.583  28.050  1.00 19.41 ?  399  GLN A O   1 
ATOM   2993 C  CB  . GLN A 1 397 ? -4.606  -2.819  25.578  1.00 10.76 ?  399  GLN A CB  1 
ATOM   2994 C  CG  . GLN A 1 397 ? -5.315  -4.105  25.195  1.00 17.24 ?  399  GLN A CG  1 
ATOM   2995 C  CD  . GLN A 1 397 ? -4.399  -5.084  24.487  1.00 20.56 ?  399  GLN A CD  1 
ATOM   2996 O  OE1 . GLN A 1 397 ? -3.249  -4.768  24.170  1.00 19.03 ?  399  GLN A OE1 1 
ATOM   2997 N  NE2 . GLN A 1 397 ? -4.890  -6.298  24.279  1.00 21.98 ?  399  GLN A NE2 1 
ATOM   2998 N  N   . ALA A 1 398 ? -3.945  0.165   26.064  1.00 15.50 ?  400  ALA A N   1 
ATOM   2999 C  CA  . ALA A 1 398 ? -3.080  1.163   26.685  1.00 19.38 ?  400  ALA A CA  1 
ATOM   3000 C  C   . ALA A 1 398 ? -3.901  2.213   27.424  1.00 22.59 ?  400  ALA A C   1 
ATOM   3001 O  O   . ALA A 1 398 ? -3.554  2.612   28.542  1.00 22.34 ?  400  ALA A O   1 
ATOM   3002 C  CB  . ALA A 1 398 ? -2.190  1.809   25.619  1.00 14.99 ?  400  ALA A CB  1 
ATOM   3003 N  N   . LEU A 1 399 ? -5.011  2.651   26.824  1.00 16.75 ?  401  LEU A N   1 
ATOM   3004 C  CA  . LEU A 1 399 ? -5.863  3.640   27.472  1.00 21.63 ?  401  LEU A CA  1 
ATOM   3005 C  C   . LEU A 1 399 ? -6.459  3.105   28.770  1.00 21.72 ?  401  LEU A C   1 
ATOM   3006 O  O   . LEU A 1 399 ? -6.726  3.879   29.694  1.00 25.27 ?  401  LEU A O   1 
ATOM   3007 C  CB  . LEU A 1 399 ? -6.973  4.069   26.517  1.00 18.74 ?  401  LEU A CB  1 
ATOM   3008 C  CG  . LEU A 1 399 ? -6.538  5.020   25.400  1.00 16.43 ?  401  LEU A CG  1 
ATOM   3009 C  CD1 . LEU A 1 399 ? -7.740  5.452   24.567  1.00 18.35 ?  401  LEU A CD1 1 
ATOM   3010 C  CD2 . LEU A 1 399 ? -5.797  6.220   25.964  1.00 24.07 ?  401  LEU A CD2 1 
ATOM   3011 N  N   . GLU A 1 400 ? -6.681  1.793   28.852  1.00 20.27 ?  402  GLU A N   1 
ATOM   3012 C  CA  . GLU A 1 400 ? -7.160  1.194   30.093  1.00 26.08 ?  402  GLU A CA  1 
ATOM   3013 C  C   . GLU A 1 400 ? -6.149  1.368   31.230  1.00 29.86 ?  402  GLU A C   1 
ATOM   3014 O  O   . GLU A 1 400 ? -6.531  1.711   32.354  1.00 29.27 ?  402  GLU A O   1 
ATOM   3015 C  CB  . GLU A 1 400 ? -7.489  -0.288  29.871  1.00 28.33 ?  402  GLU A CB  1 
ATOM   3016 N  N   . GLN A 1 401 ? -4.852  1.138   30.980  1.00 27.20 ?  403  GLN A N   1 
ATOM   3017 C  CA  . GLN A 1 401 ? -3.945  1.234   32.122  1.00 27.69 ?  403  GLN A CA  1 
ATOM   3018 C  C   . GLN A 1 401 ? -3.590  2.673   32.480  1.00 26.36 ?  403  GLN A C   1 
ATOM   3019 O  O   . GLN A 1 401 ? -3.198  2.926   33.625  1.00 31.82 ?  403  GLN A O   1 
ATOM   3020 C  CB  . GLN A 1 401 ? -2.635  0.458   31.920  1.00 41.82 ?  403  GLN A CB  1 
ATOM   3021 C  CG  . GLN A 1 401 ? -1.713  0.953   30.812  1.00 37.49 ?  403  GLN A CG  1 
ATOM   3022 C  CD  . GLN A 1 401 ? -0.458  0.084   30.669  1.00 46.51 ?  403  GLN A CD  1 
ATOM   3023 O  OE1 . GLN A 1 401 ? -0.260  -0.856  31.429  1.00 57.40 ?  403  GLN A OE1 1 
ATOM   3024 N  NE2 . GLN A 1 401 ? 0.381   0.390   29.674  1.00 48.96 ?  403  GLN A NE2 1 
ATOM   3025 N  N   . TYR A 1 402 ? -3.722  3.620   31.553  1.00 23.49 ?  404  TYR A N   1 
ATOM   3026 C  CA  . TYR A 1 402 ? -3.320  4.991   31.851  1.00 22.46 ?  404  TYR A CA  1 
ATOM   3027 C  C   . TYR A 1 402 ? -4.464  5.868   32.352  1.00 21.62 ?  404  TYR A C   1 
ATOM   3028 O  O   . TYR A 1 402 ? -4.194  6.929   32.919  1.00 25.69 ?  404  TYR A O   1 
ATOM   3029 C  CB  . TYR A 1 402 ? -2.661  5.635   30.624  1.00 22.64 ?  404  TYR A CB  1 
ATOM   3030 C  CG  . TYR A 1 402 ? -1.348  4.957   30.280  1.00 22.56 ?  404  TYR A CG  1 
ATOM   3031 C  CD1 . TYR A 1 402 ? -0.284  4.966   31.163  1.00 19.88 ?  404  TYR A CD1 1 
ATOM   3032 C  CD2 . TYR A 1 402 ? -1.190  4.279   29.079  1.00 23.30 ?  404  TYR A CD2 1 
ATOM   3033 C  CE1 . TYR A 1 402 ? 0.915   4.320   30.857  1.00 17.74 ?  404  TYR A CE1 1 
ATOM   3034 C  CE2 . TYR A 1 402 ? -0.006  3.637   28.764  1.00 19.19 ?  404  TYR A CE2 1 
ATOM   3035 C  CZ  . TYR A 1 402 ? 1.037   3.659   29.651  1.00 17.83 ?  404  TYR A CZ  1 
ATOM   3036 O  OH  . TYR A 1 402 ? 2.193   3.000   29.317  1.00 15.91 ?  404  TYR A OH  1 
ATOM   3037 N  N   . GLY A 1 403 ? -5.719  5.463   32.165  1.00 21.69 ?  405  GLY A N   1 
ATOM   3038 C  CA  . GLY A 1 403 ? -6.836  6.153   32.771  1.00 25.60 ?  405  GLY A CA  1 
ATOM   3039 C  C   . GLY A 1 403 ? -7.533  7.167   31.880  1.00 30.88 ?  405  GLY A C   1 
ATOM   3040 O  O   . GLY A 1 403 ? -7.218  7.325   30.694  1.00 21.55 ?  405  GLY A O   1 
ATOM   3041 N  N   . PRO A 1 404 ? -8.493  7.898   32.461  1.00 28.22 ?  406  PRO A N   1 
ATOM   3042 C  CA  . PRO A 1 404 ? -9.387  8.737   31.643  1.00 25.90 ?  406  PRO A CA  1 
ATOM   3043 C  C   . PRO A 1 404 ? -8.755  10.017  31.116  1.00 24.20 ?  406  PRO A C   1 
ATOM   3044 O  O   . PRO A 1 404 ? -9.300  10.606  30.176  1.00 25.33 ?  406  PRO A O   1 
ATOM   3045 C  CB  . PRO A 1 404 ? -10.539 9.062   32.603  1.00 29.53 ?  406  PRO A CB  1 
ATOM   3046 C  CG  . PRO A 1 404 ? -10.463 8.009   33.680  1.00 25.18 ?  406  PRO A CG  1 
ATOM   3047 C  CD  . PRO A 1 404 ? -9.001  7.710   33.831  1.00 28.21 ?  406  PRO A CD  1 
ATOM   3048 N  N   . GLU A 1 405 ? -7.648  10.481  31.685  1.00 20.57 ?  407  GLU A N   1 
ATOM   3049 C  CA  . GLU A 1 405 ? -7.017  11.698  31.199  1.00 29.37 ?  407  GLU A CA  1 
ATOM   3050 C  C   . GLU A 1 405 ? -5.962  11.424  30.134  1.00 28.26 ?  407  GLU A C   1 
ATOM   3051 O  O   . GLU A 1 405 ? -5.375  12.372  29.600  1.00 24.60 ?  407  GLU A O   1 
ATOM   3052 C  CB  . GLU A 1 405 ? -6.391  12.468  32.364  1.00 27.62 ?  407  GLU A CB  1 
ATOM   3053 N  N   . ALA A 1 406 ? -5.716  10.159  29.813  1.00 24.13 ?  408  ALA A N   1 
ATOM   3054 C  CA  . ALA A 1 406 ? -4.663  9.813   28.869  1.00 21.98 ?  408  ALA A CA  1 
ATOM   3055 C  C   . ALA A 1 406 ? -5.033  10.262  27.465  1.00 21.01 ?  408  ALA A C   1 
ATOM   3056 O  O   . ALA A 1 406 ? -6.198  10.187  27.056  1.00 20.07 ?  408  ALA A O   1 
ATOM   3057 C  CB  . ALA A 1 406 ? -4.407  8.308   28.887  1.00 23.99 ?  408  ALA A CB  1 
ATOM   3058 N  N   . ARG A 1 407 ? -4.030  10.722  26.721  1.00 17.82 ?  409  ARG A N   1 
ATOM   3059 C  CA  . ARG A 1 407 ? -4.232  11.168  25.351  1.00 19.63 ?  409  ARG A CA  1 
ATOM   3060 C  C   . ARG A 1 407 ? -3.404  10.314  24.398  1.00 17.77 ?  409  ARG A C   1 
ATOM   3061 O  O   . ARG A 1 407 ? -2.443  9.653   24.803  1.00 15.87 ?  409  ARG A O   1 
ATOM   3062 C  CB  . ARG A 1 407 ? -3.868  12.646  25.192  1.00 18.43 ?  409  ARG A CB  1 
ATOM   3063 C  CG  . ARG A 1 407 ? -4.735  13.562  26.052  1.00 29.28 ?  409  ARG A CG  1 
ATOM   3064 C  CD  . ARG A 1 407 ? -6.005  13.916  25.292  1.00 32.06 ?  409  ARG A CD  1 
ATOM   3065 N  NE  . ARG A 1 407 ? -6.886  14.824  26.023  1.00 50.79 ?  409  ARG A NE  1 
ATOM   3066 C  CZ  . ARG A 1 407 ? -7.841  14.432  26.862  1.00 53.25 ?  409  ARG A CZ  1 
ATOM   3067 N  NH1 . ARG A 1 407 ? -8.038  13.140  27.099  1.00 42.49 ?  409  ARG A NH1 1 
ATOM   3068 N  NH2 . ARG A 1 407 ? -8.600  15.337  27.470  1.00 57.62 ?  409  ARG A NH2 1 
ATOM   3069 N  N   . VAL A 1 408 ? -3.794  10.355  23.122  1.00 15.54 ?  410  VAL A N   1 
ATOM   3070 C  CA  . VAL A 1 408 ? -3.172  9.586   22.046  1.00 16.31 ?  410  VAL A CA  1 
ATOM   3071 C  C   . VAL A 1 408 ? -2.606  10.561  21.021  1.00 16.18 ?  410  VAL A C   1 
ATOM   3072 O  O   . VAL A 1 408 ? -3.325  11.446  20.546  1.00 15.69 ?  410  VAL A O   1 
ATOM   3073 C  CB  . VAL A 1 408 ? -4.191  8.650   21.356  1.00 14.90 ?  410  VAL A CB  1 
ATOM   3074 C  CG1 . VAL A 1 408 ? -3.522  7.868   20.221  1.00 14.26 ?  410  VAL A CG1 1 
ATOM   3075 C  CG2 . VAL A 1 408 ? -4.850  7.704   22.357  1.00 16.19 ?  410  VAL A CG2 1 
ATOM   3076 N  N   . ALA A 1 409 ? -1.339  10.384  20.652  1.00 11.67 ?  411  ALA A N   1 
ATOM   3077 C  CA  . ALA A 1 409 ? -0.793  11.065  19.485  1.00 11.82 ?  411  ALA A CA  1 
ATOM   3078 C  C   . ALA A 1 409 ? -0.580  10.038  18.385  1.00 11.20 ?  411  ALA A C   1 
ATOM   3079 O  O   . ALA A 1 409 ? -0.339  8.864   18.667  1.00 12.62 ?  411  ALA A O   1 
ATOM   3080 C  CB  . ALA A 1 409 ? 0.528   11.779  19.806  1.00 11.18 ?  411  ALA A CB  1 
ATOM   3081 N  N   . VAL A 1 410 ? -0.710  10.461  17.132  1.00 9.61  ?  412  VAL A N   1 
ATOM   3082 C  CA  . VAL A 1 410 ? -0.554  9.538   16.011  1.00 10.46 ?  412  VAL A CA  1 
ATOM   3083 C  C   . VAL A 1 410 ? 0.351   10.168  14.955  1.00 10.94 ?  412  VAL A C   1 
ATOM   3084 O  O   . VAL A 1 410 ? 0.213   11.354  14.623  1.00 11.62 ?  412  VAL A O   1 
ATOM   3085 C  CB  . VAL A 1 410 ? -1.915  9.115   15.417  1.00 11.86 ?  412  VAL A CB  1 
ATOM   3086 C  CG1 . VAL A 1 410 ? -2.698  10.316  14.925  1.00 15.29 ?  412  VAL A CG1 1 
ATOM   3087 C  CG2 . VAL A 1 410 ? -1.732  8.088   14.276  1.00 11.74 ?  412  VAL A CG2 1 
ATOM   3088 N  N   . ILE A 1 411 ? 1.291   9.372   14.451  1.00 9.69  ?  413  ILE A N   1 
ATOM   3089 C  CA  . ILE A 1 411 ? 2.304   9.808   13.492  1.00 10.31 ?  413  ILE A CA  1 
ATOM   3090 C  C   . ILE A 1 411 ? 2.213   8.901   12.272  1.00 9.91  ?  413  ILE A C   1 
ATOM   3091 O  O   . ILE A 1 411 ? 2.916   7.882   12.199  1.00 9.36  ?  413  ILE A O   1 
ATOM   3092 C  CB  . ILE A 1 411 ? 3.720   9.767   14.089  1.00 10.28 ?  413  ILE A CB  1 
ATOM   3093 C  CG1 . ILE A 1 411 ? 3.751   10.323  15.518  1.00 10.04 ?  413  ILE A CG1 1 
ATOM   3094 C  CG2 . ILE A 1 411 ? 4.693   10.508  13.151  1.00 11.74 ?  413  ILE A CG2 1 
ATOM   3095 C  CD1 . ILE A 1 411 ? 5.075   10.028  16.268  1.00 13.71 ?  413  ILE A CD1 1 
ATOM   3096 N  N   . PRO A 1 412 ? 1.354   9.213   11.309  1.00 10.24 ?  414  PRO A N   1 
ATOM   3097 C  CA  . PRO A 1 412 ? 1.117   8.262   10.213  1.00 9.66  ?  414  PRO A CA  1 
ATOM   3098 C  C   . PRO A 1 412 ? 2.363   7.901   9.412   1.00 12.24 ?  414  PRO A C   1 
ATOM   3099 O  O   . PRO A 1 412 ? 2.476   6.752   8.975   1.00 11.19 ?  414  PRO A O   1 
ATOM   3100 C  CB  . PRO A 1 412 ? 0.080   8.998   9.356   1.00 11.48 ?  414  PRO A CB  1 
ATOM   3101 C  CG  . PRO A 1 412 ? -0.691  9.785   10.358  1.00 11.83 ?  414  PRO A CG  1 
ATOM   3102 C  CD  . PRO A 1 412 ? 0.385   10.319  11.291  1.00 11.01 ?  414  PRO A CD  1 
ATOM   3103 N  N   . LYS A 1 413 ? 3.315   8.822   9.234   1.00 8.35  ?  415  LYS A N   1 
ATOM   3104 C  CA  . LYS A 1 413 ? 4.498   8.569   8.428   1.00 8.45  ?  415  LYS A CA  1 
ATOM   3105 C  C   . LYS A 1 413 ? 5.700   8.167   9.296   1.00 9.32  ?  415  LYS A C   1 
ATOM   3106 O  O   . LYS A 1 413 ? 6.819   8.060   8.780   1.00 12.48 ?  415  LYS A O   1 
ATOM   3107 C  CB  . LYS A 1 413 ? 4.840   9.818   7.620   1.00 12.17 ?  415  LYS A CB  1 
ATOM   3108 C  CG  . LYS A 1 413 ? 3.720   10.202  6.689   1.00 25.62 ?  415  LYS A CG  1 
ATOM   3109 C  CD  . LYS A 1 413 ? 3.471   9.286   5.598   1.00 27.20 ?  415  LYS A CD  1 
ATOM   3110 C  CE  . LYS A 1 413 ? 2.326   9.789   4.719   1.00 22.40 ?  415  LYS A CE  1 
ATOM   3111 N  NZ  . LYS A 1 413 ? 2.133   8.768   3.666   1.00 23.61 ?  415  LYS A NZ  1 
ATOM   3112 N  N   . GLY A 1 414 ? 5.495   7.950   10.596  1.00 8.93  ?  416  GLY A N   1 
ATOM   3113 C  CA  . GLY A 1 414 ? 6.513   7.374   11.454  1.00 8.66  ?  416  GLY A CA  1 
ATOM   3114 C  C   . GLY A 1 414 ? 7.825   8.141   11.436  1.00 9.06  ?  416  GLY A C   1 
ATOM   3115 O  O   . GLY A 1 414 ? 7.845   9.354   11.641  1.00 9.75  ?  416  GLY A O   1 
ATOM   3116 N  N   . PRO A 1 415 ? 8.947   7.453   11.183  1.00 7.41  ?  417  PRO A N   1 
ATOM   3117 C  CA  . PRO A 1 415 ? 10.262  8.094   11.343  1.00 10.09 ?  417  PRO A CA  1 
ATOM   3118 C  C   . PRO A 1 415 ? 10.594  9.144   10.290  1.00 10.74 ?  417  PRO A C   1 
ATOM   3119 O  O   . PRO A 1 415 ? 11.672  9.752   10.368  1.00 12.09 ?  417  PRO A O   1 
ATOM   3120 C  CB  . PRO A 1 415 ? 11.240  6.903   11.270  1.00 10.71 ?  417  PRO A CB  1 
ATOM   3121 C  CG  . PRO A 1 415 ? 10.516  5.900   10.363  1.00 9.87  ?  417  PRO A CG  1 
ATOM   3122 C  CD  . PRO A 1 415 ? 9.057   6.042   10.757  1.00 9.26  ?  417  PRO A CD  1 
ATOM   3123 N  N   . TYR A 1 416 ? 9.735   9.381   9.310   1.00 8.70  ?  418  TYR A N   1 
ATOM   3124 C  CA  . TYR A 1 416 ? 9.974   10.497  8.399   1.00 10.24 ?  418  TYR A CA  1 
ATOM   3125 C  C   . TYR A 1 416 ? 9.399   11.811  8.921   1.00 12.00 ?  418  TYR A C   1 
ATOM   3126 O  O   . TYR A 1 416 ? 9.445   12.825  8.211   1.00 14.23 ?  418  TYR A O   1 
ATOM   3127 C  CB  . TYR A 1 416 ? 9.404   10.189  7.017   1.00 11.10 ?  418  TYR A CB  1 
ATOM   3128 C  CG  . TYR A 1 416 ? 10.038  9.031   6.273   1.00 9.34  ?  418  TYR A CG  1 
ATOM   3129 C  CD1 . TYR A 1 416 ? 9.406   8.502   5.161   1.00 11.11 ?  418  TYR A CD1 1 
ATOM   3130 C  CD2 . TYR A 1 416 ? 11.251  8.460   6.672   1.00 9.49  ?  418  TYR A CD2 1 
ATOM   3131 C  CE1 . TYR A 1 416 ? 9.956   7.435   4.445   1.00 9.13  ?  418  TYR A CE1 1 
ATOM   3132 C  CE2 . TYR A 1 416 ? 11.816  7.378   5.957   1.00 10.52 ?  418  TYR A CE2 1 
ATOM   3133 C  CZ  . TYR A 1 416 ? 11.158  6.878   4.840   1.00 15.67 ?  418  TYR A CZ  1 
ATOM   3134 O  OH  . TYR A 1 416 ? 11.670  5.818   4.114   1.00 14.32 ?  418  TYR A OH  1 
ATOM   3135 N  N   . VAL A 1 417 ? 8.847   11.798  10.134  1.00 11.50 ?  419  VAL A N   1 
ATOM   3136 C  CA  . VAL A 1 417 ? 8.411   12.973  10.879  1.00 9.35  ?  419  VAL A CA  1 
ATOM   3137 C  C   . VAL A 1 417 ? 9.352   13.113  12.064  1.00 14.76 ?  419  VAL A C   1 
ATOM   3138 O  O   . VAL A 1 417 ? 9.865   12.111  12.572  1.00 13.32 ?  419  VAL A O   1 
ATOM   3139 C  CB  . VAL A 1 417 ? 6.951   12.811  11.360  1.00 10.78 ?  419  VAL A CB  1 
ATOM   3140 C  CG1 . VAL A 1 417 ? 6.480   14.026  12.148  1.00 12.76 ?  419  VAL A CG1 1 
ATOM   3141 C  CG2 . VAL A 1 417 ? 6.032   12.558  10.163  1.00 12.22 ?  419  VAL A CG2 1 
ATOM   3142 N  N   . LEU A 1 418 ? 9.578   14.353  12.513  1.00 11.03 ?  420  LEU A N   1 
ATOM   3143 C  CA  . LEU A 1 418 ? 10.399  14.597  13.701  1.00 10.74 ?  420  LEU A CA  1 
ATOM   3144 C  C   . LEU A 1 418 ? 9.477   15.193  14.763  1.00 15.35 ?  420  LEU A C   1 
ATOM   3145 O  O   . LEU A 1 418 ? 9.253   16.412  14.790  1.00 14.83 ?  420  LEU A O   1 
ATOM   3146 C  CB  . LEU A 1 418 ? 11.563  15.542  13.378  1.00 15.90 ?  420  LEU A CB  1 
ATOM   3147 C  CG  . LEU A 1 418 ? 12.716  15.735  14.374  1.00 22.16 ?  420  LEU A CG  1 
ATOM   3148 N  N   . PRO A 1 419 ? 8.859   14.377  15.610  1.00 13.14 ?  421  PRO A N   1 
ATOM   3149 C  CA  . PRO A 1 419 ? 7.916   14.927  16.595  1.00 14.74 ?  421  PRO A CA  1 
ATOM   3150 C  C   . PRO A 1 419 ? 8.652   15.603  17.737  1.00 14.35 ?  421  PRO A C   1 
ATOM   3151 O  O   . PRO A 1 419 ? 9.688   15.127  18.197  1.00 15.19 ?  421  PRO A O   1 
ATOM   3152 C  CB  . PRO A 1 419 ? 7.138   13.696  17.076  1.00 16.25 ?  421  PRO A CB  1 
ATOM   3153 C  CG  . PRO A 1 419 ? 8.044   12.535  16.794  1.00 17.59 ?  421  PRO A CG  1 
ATOM   3154 C  CD  . PRO A 1 419 ? 8.948   12.906  15.654  1.00 14.47 ?  421  PRO A CD  1 
ATOM   3155 N  N   . VAL A 1 420 ? 8.117   16.743  18.188  1.00 16.76 ?  422  VAL A N   1 
ATOM   3156 C  CA  . VAL A 1 420 ? 8.764   17.520  19.243  1.00 19.17 ?  422  VAL A CA  1 
ATOM   3157 C  C   . VAL A 1 420 ? 7.715   18.019  20.230  1.00 16.36 ?  422  VAL A C   1 
ATOM   3158 O  O   . VAL A 1 420 ? 6.533   18.145  19.903  1.00 19.04 ?  422  VAL A O   1 
ATOM   3159 C  CB  . VAL A 1 420 ? 9.576   18.715  18.678  1.00 22.48 ?  422  VAL A CB  1 
ATOM   3160 C  CG1 . VAL A 1 420 ? 10.756  18.230  17.834  1.00 20.09 ?  422  VAL A CG1 1 
ATOM   3161 C  CG2 . VAL A 1 420 ? 8.686   19.639  17.886  1.00 19.31 ?  422  VAL A CG2 1 
ATOM   3162 N  N   . VAL A 1 421 ? 8.156   18.309  21.449  1.00 14.69 ?  423  VAL A N   1 
ATOM   3163 C  CA  . VAL A 1 421 ? 7.281   18.908  22.459  1.00 18.10 ?  423  VAL A CA  1 
ATOM   3164 C  C   . VAL A 1 421 ? 7.514   20.414  22.464  1.00 20.41 ?  423  VAL A C   1 
ATOM   3165 O  O   . VAL A 1 421 ? 8.640   20.873  22.687  1.00 26.19 ?  423  VAL A O   1 
ATOM   3166 C  CB  . VAL A 1 421 ? 7.535   18.310  23.850  1.00 19.55 ?  423  VAL A CB  1 
ATOM   3167 C  CG1 . VAL A 1 421 ? 6.747   19.079  24.924  1.00 20.95 ?  423  VAL A CG1 1 
ATOM   3168 C  CG2 . VAL A 1 421 ? 7.166   16.837  23.866  1.00 18.14 ?  423  VAL A CG2 1 
ATOM   3169 N  N   . ASP A 1 422 ? 6.456   21.183  22.212  1.00 25.35 ?  424  ASP A N   1 
ATOM   3170 C  CA  . ASP A 1 422 ? 6.517   22.645  22.280  1.00 34.17 ?  424  ASP A CA  1 
ATOM   3171 C  C   . ASP A 1 422 ? 5.554   23.127  23.353  1.00 32.96 ?  424  ASP A C   1 
ATOM   3172 O  O   . ASP A 1 422 ? 4.337   23.230  23.101  1.00 29.72 ?  424  ASP A O   1 
ATOM   3173 C  CB  . ASP A 1 422 ? 6.183   23.294  20.937  1.00 38.56 ?  424  ASP A CB  1 
ATOM   3174 C  CG  . ASP A 1 422 ? 6.589   24.769  20.880  1.00 46.77 ?  424  ASP A CG  1 
ATOM   3175 O  OD1 . ASP A 1 422 ? 6.588   25.446  21.933  1.00 46.47 ?  424  ASP A OD1 1 
ATOM   3176 O  OD2 . ASP A 1 422 ? 6.917   25.255  19.776  1.00 46.89 ?  424  ASP A OD2 1 
ATOM   3177 N  N   . PRO A 1 423 ? 6.047   23.436  24.557  1.00 34.49 ?  425  PRO A N   1 
ATOM   3178 C  CA  . PRO A 1 423 ? 5.145   23.893  25.627  1.00 39.22 ?  425  PRO A CA  1 
ATOM   3179 C  C   . PRO A 1 423 ? 4.419   25.183  25.290  1.00 41.43 ?  425  PRO A C   1 
ATOM   3180 O  O   . PRO A 1 423 ? 3.275   25.369  25.726  1.00 46.21 ?  425  PRO A O   1 
ATOM   3181 C  CB  . PRO A 1 423 ? 6.095   24.070  26.823  1.00 40.60 ?  425  PRO A CB  1 
ATOM   3182 C  CG  . PRO A 1 423 ? 7.275   23.204  26.497  1.00 34.34 ?  425  PRO A CG  1 
ATOM   3183 C  CD  . PRO A 1 423 ? 7.445   23.365  25.019  1.00 35.14 ?  425  PRO A CD  1 
ATOM   3184 N  N   . THR A 1 424 ? 5.040   26.070  24.503  1.00 42.47 ?  426  THR A N   1 
ATOM   3185 C  CA  . THR A 1 424 ? 4.396   27.325  24.124  1.00 47.70 ?  426  THR A CA  1 
ATOM   3186 C  C   . THR A 1 424 ? 3.084   27.109  23.375  1.00 46.90 ?  426  THR A C   1 
ATOM   3187 O  O   . THR A 1 424 ? 2.274   28.037  23.291  1.00 42.70 ?  426  THR A O   1 
ATOM   3188 C  CB  . THR A 1 424 ? 5.344   28.175  23.272  1.00 41.62 ?  426  THR A CB  1 
ATOM   3189 N  N   . LEU A 1 425 ? 2.847   25.917  22.838  1.00 45.24 ?  427  LEU A N   1 
ATOM   3190 C  CA  . LEU A 1 425 ? 1.557   25.640  22.210  1.00 44.91 ?  427  LEU A CA  1 
ATOM   3191 C  C   . LEU A 1 425 ? 0.467   25.546  23.272  1.00 43.66 ?  427  LEU A C   1 
ATOM   3192 O  O   . LEU A 1 425 ? -0.715  25.711  22.970  1.00 45.86 ?  427  LEU A O   1 
ATOM   3193 C  CB  . LEU A 1 425 ? 1.604   24.349  21.386  1.00 36.34 ?  427  LEU A CB  1 
ATOM   3194 C  CG  . LEU A 1 425 ? 2.511   24.296  20.155  1.00 38.64 ?  427  LEU A CG  1 
ATOM   3195 C  CD1 . LEU A 1 425 ? 2.449   22.904  19.533  1.00 31.55 ?  427  LEU A CD1 1 
ATOM   3196 C  CD2 . LEU A 1 425 ? 2.124   25.364  19.132  1.00 42.32 ?  427  LEU A CD2 1 
ATOM   3197 N  N   . ARG B 1 1   ? 54.480  4.500   -51.124 1.00 29.30 ?  3    ARG B N   1 
ATOM   3198 C  CA  . ARG B 1 1   ? 53.768  5.198   -52.206 1.00 23.63 ?  3    ARG B CA  1 
ATOM   3199 C  C   . ARG B 1 1   ? 52.352  4.643   -52.433 1.00 21.95 ?  3    ARG B C   1 
ATOM   3200 O  O   . ARG B 1 1   ? 52.177  3.514   -52.882 1.00 22.09 ?  3    ARG B O   1 
ATOM   3201 C  CB  . ARG B 1 1   ? 54.570  5.122   -53.503 1.00 34.30 ?  3    ARG B CB  1 
ATOM   3202 N  N   . VAL B 1 2   ? 51.333  5.442   -52.125 1.00 18.79 ?  4    VAL B N   1 
ATOM   3203 C  CA  . VAL B 1 2   ? 49.948  5.005   -52.240 1.00 16.28 ?  4    VAL B CA  1 
ATOM   3204 C  C   . VAL B 1 2   ? 49.114  6.176   -52.740 1.00 16.10 ?  4    VAL B C   1 
ATOM   3205 O  O   . VAL B 1 2   ? 49.432  7.338   -52.480 1.00 17.95 ?  4    VAL B O   1 
ATOM   3206 C  CB  . VAL B 1 2   ? 49.414  4.472   -50.887 1.00 23.55 ?  4    VAL B CB  1 
ATOM   3207 C  CG1 . VAL B 1 2   ? 49.187  5.608   -49.912 1.00 24.71 ?  4    VAL B CG1 1 
ATOM   3208 C  CG2 . VAL B 1 2   ? 48.135  3.676   -51.083 1.00 24.81 ?  4    VAL B CG2 1 
ATOM   3209 N  N   . THR B 1 3   ? 48.036  5.867   -53.464 1.00 16.92 ?  5    THR B N   1 
ATOM   3210 C  CA  . THR B 1 3   ? 47.090  6.882   -53.910 1.00 14.53 ?  5    THR B CA  1 
ATOM   3211 C  C   . THR B 1 3   ? 45.858  6.831   -53.010 1.00 14.92 ?  5    THR B C   1 
ATOM   3212 O  O   . THR B 1 3   ? 45.124  5.837   -53.026 1.00 17.68 ?  5    THR B O   1 
ATOM   3213 C  CB  . THR B 1 3   ? 46.678  6.677   -55.370 1.00 17.95 ?  5    THR B CB  1 
ATOM   3214 O  OG1 . THR B 1 3   ? 47.834  6.636   -56.219 1.00 20.54 ?  5    THR B OG1 1 
ATOM   3215 C  CG2 . THR B 1 3   ? 45.781  7.825   -55.819 1.00 16.53 ?  5    THR B CG2 1 
ATOM   3216 N  N   . LEU B 1 4   ? 45.626  7.900   -52.244 1.00 11.64 ?  6    LEU B N   1 
ATOM   3217 C  CA  . LEU B 1 4   ? 44.381  8.044   -51.489 1.00 13.50 ?  6    LEU B CA  1 
ATOM   3218 C  C   . LEU B 1 4   ? 43.265  8.578   -52.383 1.00 14.21 ?  6    LEU B C   1 
ATOM   3219 O  O   . LEU B 1 4   ? 43.502  9.403   -53.269 1.00 13.05 ?  6    LEU B O   1 
ATOM   3220 C  CB  . LEU B 1 4   ? 44.565  9.008   -50.320 1.00 7.99  ?  6    LEU B CB  1 
ATOM   3221 C  CG  . LEU B 1 4   ? 45.681  8.638   -49.324 1.00 10.34 ?  6    LEU B CG  1 
ATOM   3222 C  CD1 . LEU B 1 4   ? 45.700  9.656   -48.228 1.00 13.99 ?  6    LEU B CD1 1 
ATOM   3223 C  CD2 . LEU B 1 4   ? 45.414  7.230   -48.755 1.00 13.94 ?  6    LEU B CD2 1 
ATOM   3224 N  N   . ASP B 1 5   ? 42.034  8.132   -52.116 1.00 12.11 ?  7    ASP B N   1 
ATOM   3225 C  CA  . ASP B 1 5   ? 40.870  8.722   -52.772 1.00 14.69 ?  7    ASP B CA  1 
ATOM   3226 C  C   . ASP B 1 5   ? 40.775  10.186  -52.347 1.00 12.44 ?  7    ASP B C   1 
ATOM   3227 O  O   . ASP B 1 5   ? 40.908  10.498  -51.164 1.00 13.41 ?  7    ASP B O   1 
ATOM   3228 C  CB  . ASP B 1 5   ? 39.597  8.000   -52.341 1.00 13.55 ?  7    ASP B CB  1 
ATOM   3229 C  CG  . ASP B 1 5   ? 39.275  6.794   -53.190 1.00 26.76 ?  7    ASP B CG  1 
ATOM   3230 O  OD1 . ASP B 1 5   ? 40.042  6.491   -54.138 1.00 24.53 ?  7    ASP B OD1 1 
ATOM   3231 O  OD2 . ASP B 1 5   ? 38.249  6.136   -52.882 1.00 21.96 ?  7    ASP B OD2 1 
ATOM   3232 N  N   . TYR B 1 6   ? 40.525  11.089  -53.296 1.00 12.32 ?  8    TYR B N   1 
ATOM   3233 C  CA  . TYR B 1 6   ? 40.578  12.524  -53.003 1.00 10.06 ?  8    TYR B CA  1 
ATOM   3234 C  C   . TYR B 1 6   ? 39.923  13.320  -54.127 1.00 11.24 ?  8    TYR B C   1 
ATOM   3235 O  O   . TYR B 1 6   ? 40.497  13.421  -55.212 1.00 13.41 ?  8    TYR B O   1 
ATOM   3236 C  CB  . TYR B 1 6   ? 42.040  12.962  -52.807 1.00 11.13 ?  8    TYR B CB  1 
ATOM   3237 C  CG  . TYR B 1 6   ? 42.216  14.380  -52.299 1.00 12.44 ?  8    TYR B CG  1 
ATOM   3238 C  CD1 . TYR B 1 6   ? 42.201  14.650  -50.940 1.00 11.29 ?  8    TYR B CD1 1 
ATOM   3239 C  CD2 . TYR B 1 6   ? 42.391  15.449  -53.181 1.00 17.36 ?  8    TYR B CD2 1 
ATOM   3240 C  CE1 . TYR B 1 6   ? 42.354  15.935  -50.463 1.00 16.53 ?  8    TYR B CE1 1 
ATOM   3241 C  CE2 . TYR B 1 6   ? 42.545  16.742  -52.717 1.00 19.52 ?  8    TYR B CE2 1 
ATOM   3242 C  CZ  . TYR B 1 6   ? 42.531  16.980  -51.353 1.00 22.99 ?  8    TYR B CZ  1 
ATOM   3243 O  OH  . TYR B 1 6   ? 42.686  18.258  -50.875 1.00 18.44 ?  8    TYR B OH  1 
ATOM   3244 N  N   . GLY B 1 7   ? 38.732  13.867  -53.886 1.00 15.03 ?  9    GLY B N   1 
ATOM   3245 C  CA  . GLY B 1 7   ? 37.993  14.537  -54.950 1.00 14.82 ?  9    GLY B CA  1 
ATOM   3246 C  C   . GLY B 1 7   ? 37.925  13.689  -56.199 1.00 13.39 ?  9    GLY B C   1 
ATOM   3247 O  O   . GLY B 1 7   ? 37.716  12.476  -56.152 1.00 12.69 ?  9    GLY B O   1 
ATOM   3248 N  N   . LYS B 1 8   ? 38.138  14.326  -57.347 1.00 16.83 ?  10   LYS B N   1 
ATOM   3249 C  CA  . LYS B 1 8   ? 38.117  13.618  -58.620 1.00 17.00 ?  10   LYS B CA  1 
ATOM   3250 C  C   . LYS B 1 8   ? 39.495  13.156  -59.070 1.00 17.21 ?  10   LYS B C   1 
ATOM   3251 O  O   . LYS B 1 8   ? 39.608  12.544  -60.136 1.00 18.20 ?  10   LYS B O   1 
ATOM   3252 C  CB  . LYS B 1 8   ? 37.502  14.513  -59.701 1.00 19.22 ?  10   LYS B CB  1 
ATOM   3253 C  CG  . LYS B 1 8   ? 36.007  14.709  -59.548 1.00 21.33 ?  10   LYS B CG  1 
ATOM   3254 C  CD  . LYS B 1 8   ? 35.487  15.838  -60.446 1.00 25.67 ?  10   LYS B CD  1 
ATOM   3255 C  CE  . LYS B 1 8   ? 34.029  16.160  -60.117 1.00 26.46 ?  10   LYS B CE  1 
ATOM   3256 N  NZ  . LYS B 1 8   ? 33.609  17.479  -60.675 1.00 36.83 ?  10   LYS B NZ  1 
ATOM   3257 N  N   . THR B 1 9   ? 40.541  13.415  -58.281 1.00 17.72 ?  11   THR B N   1 
ATOM   3258 C  CA  . THR B 1 9   ? 41.911  13.194  -58.715 1.00 18.86 ?  11   THR B CA  1 
ATOM   3259 C  C   . THR B 1 9   ? 42.629  12.062  -58.002 1.00 17.69 ?  11   THR B C   1 
ATOM   3260 O  O   . THR B 1 9   ? 43.559  11.492  -58.571 1.00 17.95 ?  11   THR B O   1 
ATOM   3261 C  CB  . THR B 1 9   ? 42.742  14.466  -58.501 1.00 19.52 ?  11   THR B CB  1 
ATOM   3262 O  OG1 . THR B 1 9   ? 42.676  14.829  -57.112 1.00 16.55 ?  11   THR B OG1 1 
ATOM   3263 C  CG2 . THR B 1 9   ? 42.224  15.623  -59.357 1.00 19.16 ?  11   THR B CG2 1 
ATOM   3264 N  N   . GLY B 1 10  ? 42.257  11.743  -56.768 1.00 11.26 ?  12   GLY B N   1 
ATOM   3265 C  CA  . GLY B 1 10  ? 43.158  11.026  -55.887 1.00 12.76 ?  12   GLY B CA  1 
ATOM   3266 C  C   . GLY B 1 10  ? 44.272  11.926  -55.379 1.00 15.35 ?  12   GLY B C   1 
ATOM   3267 O  O   . GLY B 1 10  ? 44.401  13.097  -55.754 1.00 12.87 ?  12   GLY B O   1 
ATOM   3268 N  N   . LEU B 1 11  ? 45.097  11.363  -54.490 1.00 10.89 ?  13   LEU B N   1 
ATOM   3269 C  CA  . LEU B 1 11  ? 46.173  12.117  -53.852 1.00 12.05 ?  13   LEU B CA  1 
ATOM   3270 C  C   . LEU B 1 11  ? 47.329  11.165  -53.631 1.00 12.54 ?  13   LEU B C   1 
ATOM   3271 O  O   . LEU B 1 11  ? 47.150  10.146  -52.963 1.00 12.39 ?  13   LEU B O   1 
ATOM   3272 C  CB  . LEU B 1 11  ? 45.729  12.722  -52.514 1.00 10.38 ?  13   LEU B CB  1 
ATOM   3273 C  CG  . LEU B 1 11  ? 46.758  13.566  -51.760 1.00 12.88 ?  13   LEU B CG  1 
ATOM   3274 C  CD1 . LEU B 1 11  ? 46.989  14.894  -52.476 1.00 13.08 ?  13   LEU B CD1 1 
ATOM   3275 C  CD2 . LEU B 1 11  ? 46.303  13.806  -50.311 1.00 12.35 ?  13   LEU B CD2 1 
ATOM   3276 N  N   . ASN B 1 12  ? 48.502  11.499  -54.174 1.00 14.05 ?  14   ASN B N   1 
ATOM   3277 C  CA  . ASN B 1 12  ? 49.650  10.600  -54.142 1.00 13.53 ?  14   ASN B CA  1 
ATOM   3278 C  C   . ASN B 1 12  ? 50.481  10.881  -52.895 1.00 15.67 ?  14   ASN B C   1 
ATOM   3279 O  O   . ASN B 1 12  ? 51.021  11.984  -52.741 1.00 15.12 ?  14   ASN B O   1 
ATOM   3280 C  CB  . ASN B 1 12  ? 50.497  10.750  -55.410 1.00 17.43 ?  14   ASN B CB  1 
ATOM   3281 C  CG  . ASN B 1 12  ? 50.049  9.802   -56.522 1.00 30.80 ?  14   ASN B CG  1 
ATOM   3282 O  OD1 . ASN B 1 12  ? 49.204  8.932   -56.300 1.00 27.78 ?  14   ASN B OD1 1 
ATOM   3283 N  ND2 . ASN B 1 12  ? 50.610  9.970   -57.723 1.00 25.98 ?  14   ASN B ND2 1 
ATOM   3284 N  N   . VAL B 1 13  ? 50.578  9.883   -52.013 1.00 12.28 ?  15   VAL B N   1 
ATOM   3285 C  CA  . VAL B 1 13  ? 51.243  10.005  -50.717 1.00 15.86 ?  15   VAL B CA  1 
ATOM   3286 C  C   . VAL B 1 13  ? 52.382  8.994   -50.645 1.00 16.66 ?  15   VAL B C   1 
ATOM   3287 O  O   . VAL B 1 13  ? 52.244  7.865   -51.123 1.00 19.09 ?  15   VAL B O   1 
ATOM   3288 C  CB  . VAL B 1 13  ? 50.232  9.789   -49.564 1.00 16.26 ?  15   VAL B CB  1 
ATOM   3289 C  CG1 . VAL B 1 13  ? 50.920  9.898   -48.201 1.00 17.46 ?  15   VAL B CG1 1 
ATOM   3290 C  CG2 . VAL B 1 13  ? 49.102  10.817  -49.653 1.00 14.14 ?  15   VAL B CG2 1 
ATOM   3291 N  N   . ASP B 1 14  ? 53.509  9.390   -50.049 1.00 15.08 ?  16   ASP B N   1 
ATOM   3292 C  CA  . ASP B 1 14  ? 54.582  8.451   -49.726 1.00 16.37 ?  16   ASP B CA  1 
ATOM   3293 C  C   . ASP B 1 14  ? 54.641  8.250   -48.215 1.00 18.57 ?  16   ASP B C   1 
ATOM   3294 O  O   . ASP B 1 14  ? 54.881  9.203   -47.467 1.00 24.47 ?  16   ASP B O   1 
ATOM   3295 C  CB  . ASP B 1 14  ? 55.932  8.935   -50.255 1.00 20.57 ?  16   ASP B CB  1 
ATOM   3296 C  CG  . ASP B 1 14  ? 56.889  7.782   -50.553 1.00 32.10 ?  16   ASP B CG  1 
ATOM   3297 O  OD1 . ASP B 1 14  ? 56.471  6.603   -50.476 1.00 37.80 ?  16   ASP B OD1 1 
ATOM   3298 O  OD2 . ASP B 1 14  ? 58.068  8.053   -50.865 1.00 40.44 ?  16   ASP B OD2 1 
ATOM   3299 N  N   . LEU B 1 15  ? 54.420  7.013   -47.776 1.00 19.05 ?  17   LEU B N   1 
ATOM   3300 C  CA  . LEU B 1 15  ? 54.405  6.650   -46.368 1.00 20.68 ?  17   LEU B CA  1 
ATOM   3301 C  C   . LEU B 1 15  ? 55.676  5.890   -45.995 1.00 16.69 ?  17   LEU B C   1 
ATOM   3302 O  O   . LEU B 1 15  ? 56.261  5.213   -46.840 1.00 21.14 ?  17   LEU B O   1 
ATOM   3303 C  CB  . LEU B 1 15  ? 53.178  5.788   -46.061 1.00 18.39 ?  17   LEU B CB  1 
ATOM   3304 C  CG  . LEU B 1 15  ? 51.874  6.578   -46.200 1.00 19.46 ?  17   LEU B CG  1 
ATOM   3305 C  CD1 . LEU B 1 15  ? 50.647  5.662   -46.119 1.00 25.54 ?  17   LEU B CD1 1 
ATOM   3306 C  CD2 . LEU B 1 15  ? 51.795  7.656   -45.143 1.00 17.66 ?  17   LEU B CD2 1 
ATOM   3307 N  N   . PRO B 1 16  ? 56.122  5.971   -44.744 1.00 21.46 ?  18   PRO B N   1 
ATOM   3308 C  CA  . PRO B 1 16  ? 57.422  5.377   -44.389 1.00 20.70 ?  18   PRO B CA  1 
ATOM   3309 C  C   . PRO B 1 16  ? 57.429  3.861   -44.548 1.00 23.69 ?  18   PRO B C   1 
ATOM   3310 O  O   . PRO B 1 16  ? 56.560  3.155   -44.033 1.00 23.43 ?  18   PRO B O   1 
ATOM   3311 C  CB  . PRO B 1 16  ? 57.618  5.809   -42.931 1.00 24.92 ?  18   PRO B CB  1 
ATOM   3312 C  CG  . PRO B 1 16  ? 56.258  6.059   -42.418 1.00 27.72 ?  18   PRO B CG  1 
ATOM   3313 C  CD  . PRO B 1 16  ? 55.497  6.645   -43.592 1.00 21.41 ?  18   PRO B CD  1 
ATOM   3314 N  N   . ASP B 1 17  ? 58.440  3.359   -45.262 1.00 24.97 ?  19   ASP B N   1 
ATOM   3315 C  CA  . ASP B 1 17  ? 58.459  1.946   -45.628 1.00 31.16 ?  19   ASP B CA  1 
ATOM   3316 C  C   . ASP B 1 17  ? 58.606  1.041   -44.409 1.00 29.68 ?  19   ASP B C   1 
ATOM   3317 O  O   . ASP B 1 17  ? 58.024  -0.051  -44.371 1.00 30.66 ?  19   ASP B O   1 
ATOM   3318 C  CB  . ASP B 1 17  ? 59.585  1.679   -46.631 1.00 35.39 ?  19   ASP B CB  1 
ATOM   3319 N  N   . ASP B 1 18  ? 59.357  1.479   -43.399 1.00 25.11 ?  20   ASP B N   1 
ATOM   3320 C  CA  . ASP B 1 18  ? 59.637  0.615   -42.261 1.00 34.44 ?  20   ASP B CA  1 
ATOM   3321 C  C   . ASP B 1 18  ? 58.498  0.543   -41.252 1.00 34.67 ?  20   ASP B C   1 
ATOM   3322 O  O   . ASP B 1 18  ? 58.564  -0.276  -40.329 1.00 30.42 ?  20   ASP B O   1 
ATOM   3323 C  CB  . ASP B 1 18  ? 60.915  1.068   -41.540 1.00 35.28 ?  20   ASP B CB  1 
ATOM   3324 C  CG  . ASP B 1 18  ? 60.854  2.523   -41.076 1.00 42.42 ?  20   ASP B CG  1 
ATOM   3325 O  OD1 . ASP B 1 18  ? 60.075  3.317   -41.649 1.00 47.18 ?  20   ASP B OD1 1 
ATOM   3326 O  OD2 . ASP B 1 18  ? 61.568  2.872   -40.111 1.00 47.30 ?  20   ASP B OD2 1 
ATOM   3327 N  N   . ARG B 1 19  ? 57.456  1.361   -41.388 1.00 27.20 ?  21   ARG B N   1 
ATOM   3328 C  CA  . ARG B 1 19  ? 56.452  1.416   -40.340 1.00 23.49 ?  21   ARG B CA  1 
ATOM   3329 C  C   . ARG B 1 19  ? 55.024  1.226   -40.850 1.00 22.67 ?  21   ARG B C   1 
ATOM   3330 O  O   . ARG B 1 19  ? 54.099  1.168   -40.034 1.00 21.85 ?  21   ARG B O   1 
ATOM   3331 C  CB  . ARG B 1 19  ? 56.593  2.734   -39.555 1.00 39.71 ?  21   ARG B CB  1 
ATOM   3332 C  CG  . ARG B 1 19  ? 57.780  2.703   -38.555 1.00 40.24 ?  21   ARG B CG  1 
ATOM   3333 C  CD  . ARG B 1 19  ? 58.137  4.065   -37.972 1.00 39.71 ?  21   ARG B CD  1 
ATOM   3334 N  N   . THR B 1 20  ? 54.827  1.053   -42.157 1.00 20.21 ?  22   THR B N   1 
ATOM   3335 C  CA  . THR B 1 20  ? 53.498  1.031   -42.769 1.00 18.46 ?  22   THR B CA  1 
ATOM   3336 C  C   . THR B 1 20  ? 53.086  -0.386  -43.154 1.00 21.00 ?  22   THR B C   1 
ATOM   3337 O  O   . THR B 1 20  ? 53.828  -1.086  -43.852 1.00 21.48 ?  22   THR B O   1 
ATOM   3338 C  CB  . THR B 1 20  ? 53.467  1.940   -44.001 1.00 16.94 ?  22   THR B CB  1 
ATOM   3339 O  OG1 . THR B 1 20  ? 53.949  3.244   -43.647 1.00 20.75 ?  22   THR B OG1 1 
ATOM   3340 C  CG2 . THR B 1 20  ? 52.048  2.055   -44.560 1.00 20.38 ?  22   THR B CG2 1 
ATOM   3341 N  N   . LEU B 1 21  ? 51.890  -0.790  -42.723 1.00 17.63 ?  23   LEU B N   1 
ATOM   3342 C  CA  . LEU B 1 21  ? 51.319  -2.082  -43.084 1.00 16.74 ?  23   LEU B CA  1 
ATOM   3343 C  C   . LEU B 1 21  ? 50.833  -2.079  -44.533 1.00 19.93 ?  23   LEU B C   1 
ATOM   3344 O  O   . LEU B 1 21  ? 50.637  -1.017  -45.127 1.00 18.94 ?  23   LEU B O   1 
ATOM   3345 C  CB  . LEU B 1 21  ? 50.167  -2.421  -42.145 1.00 16.96 ?  23   LEU B CB  1 
ATOM   3346 C  CG  . LEU B 1 21  ? 50.529  -2.576  -40.665 1.00 28.50 ?  23   LEU B CG  1 
ATOM   3347 C  CD1 . LEU B 1 21  ? 49.282  -2.688  -39.824 1.00 22.02 ?  23   LEU B CD1 1 
ATOM   3348 C  CD2 . LEU B 1 21  ? 51.365  -3.821  -40.513 1.00 30.15 ?  23   LEU B CD2 1 
ATOM   3349 N  N   . PRO B 1 22  ? 50.642  -3.256  -45.131 1.00 19.83 ?  24   PRO B N   1 
ATOM   3350 C  CA  . PRO B 1 22  ? 50.081  -3.312  -46.492 1.00 22.76 ?  24   PRO B CA  1 
ATOM   3351 C  C   . PRO B 1 22  ? 48.723  -2.635  -46.540 1.00 16.58 ?  24   PRO B C   1 
ATOM   3352 O  O   . PRO B 1 22  ? 47.918  -2.795  -45.610 1.00 17.21 ?  24   PRO B O   1 
ATOM   3353 C  CB  . PRO B 1 22  ? 49.967  -4.819  -46.762 1.00 25.90 ?  24   PRO B CB  1 
ATOM   3354 C  CG  . PRO B 1 22  ? 51.062  -5.413  -45.902 1.00 27.66 ?  24   PRO B CG  1 
ATOM   3355 C  CD  . PRO B 1 22  ? 50.965  -4.605  -44.627 1.00 24.69 ?  24   PRO B CD  1 
ATOM   3356 N  N   . PRO B 1 23  ? 48.439  -1.873  -47.599 1.00 18.16 ?  25   PRO B N   1 
ATOM   3357 C  CA  . PRO B 1 23  ? 47.196  -1.085  -47.636 1.00 17.78 ?  25   PRO B CA  1 
ATOM   3358 C  C   . PRO B 1 23  ? 45.955  -1.945  -47.483 1.00 17.80 ?  25   PRO B C   1 
ATOM   3359 O  O   . PRO B 1 23  ? 45.882  -3.070  -47.979 1.00 19.92 ?  25   PRO B O   1 
ATOM   3360 C  CB  . PRO B 1 23  ? 47.242  -0.418  -49.015 1.00 18.21 ?  25   PRO B CB  1 
ATOM   3361 C  CG  . PRO B 1 23  ? 48.721  -0.370  -49.346 1.00 25.22 ?  25   PRO B CG  1 
ATOM   3362 C  CD  . PRO B 1 23  ? 49.257  -1.658  -48.803 1.00 20.82 ?  25   PRO B CD  1 
ATOM   3363 N  N   . LEU B 1 24  ? 44.965  -1.378  -46.800 1.00 16.37 ?  26   LEU B N   1 
ATOM   3364 C  CA  . LEU B 1 24  ? 43.706  -2.041  -46.510 1.00 15.31 ?  26   LEU B CA  1 
ATOM   3365 C  C   . LEU B 1 24  ? 42.779  -1.779  -47.690 1.00 16.39 ?  26   LEU B C   1 
ATOM   3366 O  O   . LEU B 1 24  ? 42.320  -0.652  -47.881 1.00 14.54 ?  26   LEU B O   1 
ATOM   3367 C  CB  . LEU B 1 24  ? 43.126  -1.492  -45.208 1.00 16.49 ?  26   LEU B CB  1 
ATOM   3368 C  CG  . LEU B 1 24  ? 43.440  -2.302  -43.941 1.00 24.91 ?  26   LEU B CG  1 
ATOM   3369 C  CD1 . LEU B 1 24  ? 44.884  -2.402  -43.790 1.00 22.06 ?  26   LEU B CD1 1 
ATOM   3370 C  CD2 . LEU B 1 24  ? 42.885  -1.605  -42.712 1.00 23.61 ?  26   LEU B CD2 1 
ATOM   3371 N  N   . THR B 1 25  ? 42.520  -2.807  -48.496 1.00 16.25 ?  27   THR B N   1 
ATOM   3372 C  CA  . THR B 1 25  ? 41.684  -2.648  -49.679 1.00 14.99 ?  27   THR B CA  1 
ATOM   3373 C  C   . THR B 1 25  ? 40.623  -3.733  -49.708 1.00 18.28 ?  27   THR B C   1 
ATOM   3374 O  O   . THR B 1 25  ? 40.764  -4.784  -49.085 1.00 20.80 ?  27   THR B O   1 
ATOM   3375 C  CB  . THR B 1 25  ? 42.499  -2.697  -50.993 1.00 22.88 ?  27   THR B CB  1 
ATOM   3376 O  OG1 . THR B 1 25  ? 43.193  -3.950  -51.105 1.00 26.12 ?  27   THR B OG1 1 
ATOM   3377 C  CG2 . THR B 1 25  ? 43.487  -1.547  -51.066 1.00 24.06 ?  27   THR B CG2 1 
ATOM   3378 N  N   . ILE B 1 26  ? 39.559  -3.488  -50.457 1.00 20.46 ?  28   ILE B N   1 
ATOM   3379 C  CA  . ILE B 1 26  ? 38.527  -4.513  -50.518 1.00 21.77 ?  28   ILE B CA  1 
ATOM   3380 C  C   . ILE B 1 26  ? 39.017  -5.636  -51.419 1.00 16.71 ?  28   ILE B C   1 
ATOM   3381 O  O   . ILE B 1 26  ? 39.931  -5.454  -52.230 1.00 23.01 ?  28   ILE B O   1 
ATOM   3382 C  CB  . ILE B 1 26  ? 37.183  -3.940  -50.991 1.00 29.81 ?  28   ILE B CB  1 
ATOM   3383 C  CG1 . ILE B 1 26  ? 37.267  -3.535  -52.452 1.00 24.74 ?  28   ILE B CG1 1 
ATOM   3384 C  CG2 . ILE B 1 26  ? 36.781  -2.756  -50.109 1.00 27.35 ?  28   ILE B CG2 1 
ATOM   3385 C  CD1 . ILE B 1 26  ? 35.913  -3.241  -53.050 1.00 21.78 ?  28   ILE B CD1 1 
ATOM   3386 N  N   . ARG B 1 27  ? 38.452  -6.819  -51.232 1.00 17.47 ?  29   ARG B N   1 
ATOM   3387 C  CA  . ARG B 1 27  ? 38.945  -7.992  -51.933 1.00 18.01 ?  29   ARG B CA  1 
ATOM   3388 C  C   . ARG B 1 27  ? 38.642  -7.867  -53.427 1.00 19.10 ?  29   ARG B C   1 
ATOM   3389 O  O   . ARG B 1 27  ? 37.569  -7.389  -53.806 1.00 18.92 ?  29   ARG B O   1 
ATOM   3390 C  CB  . ARG B 1 27  ? 38.314  -9.264  -51.361 1.00 19.01 ?  29   ARG B CB  1 
ATOM   3391 N  N   . PRO B 1 28  ? 39.564  -8.276  -54.294 1.00 22.49 ?  30   PRO B N   1 
ATOM   3392 C  CA  . PRO B 1 28  ? 39.359  -8.104  -55.745 1.00 21.49 ?  30   PRO B CA  1 
ATOM   3393 C  C   . PRO B 1 28  ? 38.355  -9.061  -56.378 1.00 27.51 ?  30   PRO B C   1 
ATOM   3394 O  O   . PRO B 1 28  ? 38.751  -10.037 -57.022 1.00 35.78 ?  30   PRO B O   1 
ATOM   3395 C  CB  . PRO B 1 28  ? 40.765  -8.340  -56.312 1.00 20.67 ?  30   PRO B CB  1 
ATOM   3396 C  CG  . PRO B 1 28  ? 41.390  -9.281  -55.345 1.00 28.66 ?  30   PRO B CG  1 
ATOM   3397 C  CD  . PRO B 1 28  ? 40.909  -8.793  -53.987 1.00 21.58 ?  30   PRO B CD  1 
ATOM   3398 N  N   . ALA B 1 29  ? 37.063  -8.771  -56.249 1.00 20.75 ?  31   ALA B N   1 
ATOM   3399 C  CA  . ALA B 1 29  ? 36.020  -9.577  -56.866 1.00 20.88 ?  31   ALA B CA  1 
ATOM   3400 C  C   . ALA B 1 29  ? 35.865  -9.213  -58.344 1.00 14.96 ?  31   ALA B C   1 
ATOM   3401 O  O   . ALA B 1 29  ? 36.140  -8.079  -58.743 1.00 16.61 ?  31   ALA B O   1 
ATOM   3402 C  CB  . ALA B 1 29  ? 34.697  -9.373  -56.139 1.00 19.00 ?  31   ALA B CB  1 
ATOM   3403 N  N   . PRO B 1 30  ? 35.440  -10.154 -59.182 1.00 18.24 ?  32   PRO B N   1 
ATOM   3404 C  CA  . PRO B 1 30  ? 35.354  -9.870  -60.622 1.00 13.96 ?  32   PRO B CA  1 
ATOM   3405 C  C   . PRO B 1 30  ? 34.230  -8.894  -60.913 1.00 14.72 ?  32   PRO B C   1 
ATOM   3406 O  O   . PRO B 1 30  ? 33.084  -9.134  -60.508 1.00 16.16 ?  32   PRO B O   1 
ATOM   3407 C  CB  . PRO B 1 30  ? 35.056  -11.246 -61.238 1.00 16.43 ?  32   PRO B CB  1 
ATOM   3408 C  CG  . PRO B 1 30  ? 34.440  -12.026 -60.134 1.00 21.90 ?  32   PRO B CG  1 
ATOM   3409 C  CD  . PRO B 1 30  ? 35.151  -11.570 -58.891 1.00 17.83 ?  32   PRO B CD  1 
ATOM   3410 N  N   . PRO B 1 31  ? 34.514  -7.792  -61.602 1.00 12.79 ?  33   PRO B N   1 
ATOM   3411 C  CA  . PRO B 1 31  ? 33.433  -6.912  -62.050 1.00 12.78 ?  33   PRO B CA  1 
ATOM   3412 C  C   . PRO B 1 31  ? 32.546  -7.633  -63.045 1.00 15.51 ?  33   PRO B C   1 
ATOM   3413 O  O   . PRO B 1 31  ? 32.984  -8.538  -63.763 1.00 15.11 ?  33   PRO B O   1 
ATOM   3414 C  CB  . PRO B 1 31  ? 34.167  -5.748  -62.725 1.00 16.75 ?  33   PRO B CB  1 
ATOM   3415 C  CG  . PRO B 1 31  ? 35.603  -5.860  -62.271 1.00 20.77 ?  33   PRO B CG  1 
ATOM   3416 C  CD  . PRO B 1 31  ? 35.832  -7.320  -62.063 1.00 15.58 ?  33   PRO B CD  1 
ATOM   3417 N  N   . LEU B 1 32  ? 31.288  -7.219  -63.089 1.00 12.64 ?  34   LEU B N   1 
ATOM   3418 C  CA  . LEU B 1 32  ? 30.398  -7.737  -64.124 1.00 12.63 ?  34   LEU B CA  1 
ATOM   3419 C  C   . LEU B 1 32  ? 30.778  -7.122  -65.465 1.00 16.36 ?  34   LEU B C   1 
ATOM   3420 O  O   . LEU B 1 32  ? 30.989  -5.910  -65.571 1.00 18.54 ?  34   LEU B O   1 
ATOM   3421 C  CB  . LEU B 1 32  ? 28.936  -7.438  -63.791 1.00 16.69 ?  34   LEU B CB  1 
ATOM   3422 C  CG  . LEU B 1 32  ? 28.481  -7.874  -62.390 1.00 18.76 ?  34   LEU B CG  1 
ATOM   3423 C  CD1 . LEU B 1 32  ? 27.046  -7.463  -62.138 1.00 14.40 ?  34   LEU B CD1 1 
ATOM   3424 C  CD2 . LEU B 1 32  ? 28.664  -9.373  -62.171 1.00 28.29 ?  34   LEU B CD2 1 
ATOM   3425 N  N   . ASP B 1 33  ? 30.898  -7.973  -66.485 1.00 14.54 ?  35   ASP B N   1 
ATOM   3426 C  CA  . ASP B 1 33  ? 31.271  -7.511  -67.814 1.00 12.71 ?  35   ASP B CA  1 
ATOM   3427 C  C   . ASP B 1 33  ? 30.265  -6.514  -68.367 1.00 20.16 ?  35   ASP B C   1 
ATOM   3428 O  O   . ASP B 1 33  ? 30.639  -5.500  -68.971 1.00 16.89 ?  35   ASP B O   1 
ATOM   3429 C  CB  . ASP B 1 33  ? 31.374  -8.708  -68.750 1.00 15.63 ?  35   ASP B CB  1 
ATOM   3430 C  CG  . ASP B 1 33  ? 31.435  -8.298  -70.209 1.00 18.22 ?  35   ASP B CG  1 
ATOM   3431 O  OD1 . ASP B 1 33  ? 32.422  -7.634  -70.609 1.00 19.76 ?  35   ASP B OD1 1 
ATOM   3432 O  OD2 . ASP B 1 33  ? 30.476  -8.629  -70.939 1.00 18.22 ?  35   ASP B OD2 1 
ATOM   3433 N  N   . ASP B 1 34  ? 28.981  -6.813  -68.218 1.00 15.88 ?  36   ASP B N   1 
ATOM   3434 C  CA  . ASP B 1 34  ? 27.907  -6.006  -68.797 1.00 17.66 ?  36   ASP B CA  1 
ATOM   3435 C  C   . ASP B 1 34  ? 26.840  -5.856  -67.724 1.00 19.01 ?  36   ASP B C   1 
ATOM   3436 O  O   . ASP B 1 34  ? 25.875  -6.633  -67.679 1.00 17.26 ?  36   ASP B O   1 
ATOM   3437 C  CB  . ASP B 1 34  ? 27.345  -6.651  -70.066 1.00 19.78 ?  36   ASP B CB  1 
ATOM   3438 C  CG  . ASP B 1 34  ? 26.581  -5.657  -70.944 1.00 25.73 ?  36   ASP B CG  1 
ATOM   3439 O  OD1 . ASP B 1 34  ? 26.706  -5.739  -72.190 1.00 21.99 ?  36   ASP B OD1 1 
ATOM   3440 O  OD2 . ASP B 1 34  ? 25.848  -4.807  -70.392 1.00 20.85 ?  36   ASP B OD2 1 
ATOM   3441 N  N   . PRO B 1 35  ? 26.997  -4.879  -66.824 1.00 17.93 ?  37   PRO B N   1 
ATOM   3442 C  CA  . PRO B 1 35  ? 26.062  -4.789  -65.696 1.00 16.32 ?  37   PRO B CA  1 
ATOM   3443 C  C   . PRO B 1 35  ? 24.650  -4.467  -66.119 1.00 14.99 ?  37   PRO B C   1 
ATOM   3444 O  O   . PRO B 1 35  ? 23.713  -4.948  -65.473 1.00 15.55 ?  37   PRO B O   1 
ATOM   3445 C  CB  . PRO B 1 35  ? 26.649  -3.669  -64.825 1.00 16.25 ?  37   PRO B CB  1 
ATOM   3446 C  CG  . PRO B 1 35  ? 28.068  -3.495  -65.310 1.00 22.50 ?  37   PRO B CG  1 
ATOM   3447 C  CD  . PRO B 1 35  ? 28.056  -3.857  -66.755 1.00 16.02 ?  37   PRO B CD  1 
ATOM   3448 N  N   . GLU B 1 36  ? 24.465  -3.678  -67.182 1.00 15.92 ?  38   GLU B N   1 
ATOM   3449 C  CA  . GLU B 1 36  ? 23.104  -3.382  -67.623 1.00 17.44 ?  38   GLU B CA  1 
ATOM   3450 C  C   . GLU B 1 36  ? 22.395  -4.643  -68.097 1.00 18.55 ?  38   GLU B C   1 
ATOM   3451 O  O   . GLU B 1 36  ? 21.221  -4.854  -67.776 1.00 17.10 ?  38   GLU B O   1 
ATOM   3452 C  CB  . GLU B 1 36  ? 23.106  -2.327  -68.726 1.00 18.56 ?  38   GLU B CB  1 
ATOM   3453 C  CG  . GLU B 1 36  ? 21.732  -1.688  -68.917 1.00 23.31 ?  38   GLU B CG  1 
ATOM   3454 C  CD  . GLU B 1 36  ? 21.763  -0.455  -69.804 1.00 31.08 ?  38   GLU B CD  1 
ATOM   3455 O  OE1 . GLU B 1 36  ? 22.825  0.203   -69.897 1.00 34.89 ?  38   GLU B OE1 1 
ATOM   3456 O  OE2 . GLU B 1 36  ? 20.709  -0.135  -70.393 1.00 31.01 ?  38   GLU B OE2 1 
ATOM   3457 N  N   . ALA B 1 37  ? 23.090  -5.497  -68.857 1.00 16.15 ?  39   ALA B N   1 
ATOM   3458 C  CA  . ALA B 1 37  ? 22.521  -6.792  -69.221 1.00 17.27 ?  39   ALA B CA  1 
ATOM   3459 C  C   . ALA B 1 37  ? 22.229  -7.645  -67.990 1.00 18.38 ?  39   ALA B C   1 
ATOM   3460 O  O   . ALA B 1 37  ? 21.252  -8.400  -67.972 1.00 16.17 ?  39   ALA B O   1 
ATOM   3461 C  CB  . ALA B 1 37  ? 23.463  -7.527  -70.181 1.00 18.12 ?  39   ALA B CB  1 
ATOM   3462 N  N   . GLU B 1 38  ? 23.049  -7.535  -66.943 1.00 14.87 ?  40   GLU B N   1 
ATOM   3463 C  CA  . GLU B 1 38  ? 22.764  -8.290  -65.730 1.00 15.13 ?  40   GLU B CA  1 
ATOM   3464 C  C   . GLU B 1 38  ? 21.508  -7.772  -65.043 1.00 14.42 ?  40   GLU B C   1 
ATOM   3465 O  O   . GLU B 1 38  ? 20.702  -8.562  -64.541 1.00 16.49 ?  40   GLU B O   1 
ATOM   3466 C  CB  . GLU B 1 38  ? 23.960  -8.232  -64.779 1.00 15.71 ?  40   GLU B CB  1 
ATOM   3467 C  CG  . GLU B 1 38  ? 23.859  -9.183  -63.583 1.00 17.95 ?  40   GLU B CG  1 
ATOM   3468 C  CD  . GLU B 1 38  ? 23.755  -10.648 -63.973 1.00 25.45 ?  40   GLU B CD  1 
ATOM   3469 O  OE1 . GLU B 1 38  ? 24.274  -11.035 -65.038 1.00 26.15 ?  40   GLU B OE1 1 
ATOM   3470 O  OE2 . GLU B 1 38  ? 23.203  -11.434 -63.174 1.00 34.68 ?  40   GLU B OE2 1 
ATOM   3471 N  N   . VAL B 1 39  ? 21.326  -6.450  -65.008 1.00 14.33 ?  41   VAL B N   1 
ATOM   3472 C  CA  . VAL B 1 39  ? 20.101  -5.886  -64.443 1.00 13.06 ?  41   VAL B CA  1 
ATOM   3473 C  C   . VAL B 1 39  ? 18.885  -6.420  -65.194 1.00 18.34 ?  41   VAL B C   1 
ATOM   3474 O  O   . VAL B 1 39  ? 17.884  -6.823  -64.585 1.00 15.66 ?  41   VAL B O   1 
ATOM   3475 C  CB  . VAL B 1 39  ? 20.146  -4.348  -64.474 1.00 16.49 ?  41   VAL B CB  1 
ATOM   3476 C  CG1 . VAL B 1 39  ? 18.780  -3.758  -64.070 1.00 14.77 ?  41   VAL B CG1 1 
ATOM   3477 C  CG2 . VAL B 1 39  ? 21.256  -3.821  -63.565 1.00 19.67 ?  41   VAL B CG2 1 
ATOM   3478 N  N   . VAL B 1 40  ? 18.967  -6.452  -66.527 1.00 16.24 ?  42   VAL B N   1 
ATOM   3479 C  CA  . VAL B 1 40  ? 17.868  -6.997  -67.330 1.00 18.39 ?  42   VAL B CA  1 
ATOM   3480 C  C   . VAL B 1 40  ? 17.562  -8.424  -66.901 1.00 18.72 ?  42   VAL B C   1 
ATOM   3481 O  O   . VAL B 1 40  ? 16.397  -8.800  -66.727 1.00 21.00 ?  42   VAL B O   1 
ATOM   3482 C  CB  . VAL B 1 40  ? 18.198  -6.925  -68.831 1.00 20.91 ?  42   VAL B CB  1 
ATOM   3483 C  CG1 . VAL B 1 40  ? 17.215  -7.790  -69.627 1.00 24.01 ?  42   VAL B CG1 1 
ATOM   3484 C  CG2 . VAL B 1 40  ? 18.156  -5.503  -69.317 1.00 17.72 ?  42   VAL B CG2 1 
ATOM   3485 N  N   . ARG B 1 41  ? 18.606  -9.240  -66.707 1.00 16.59 ?  43   ARG B N   1 
ATOM   3486 C  CA  . ARG B 1 41  ? 18.383  -10.627 -66.303 1.00 17.99 ?  43   ARG B CA  1 
ATOM   3487 C  C   . ARG B 1 41  ? 17.765  -10.703 -64.918 1.00 20.58 ?  43   ARG B C   1 
ATOM   3488 O  O   . ARG B 1 41  ? 16.909  -11.558 -64.661 1.00 21.24 ?  43   ARG B O   1 
ATOM   3489 C  CB  . ARG B 1 41  ? 19.686  -11.429 -66.340 1.00 20.03 ?  43   ARG B CB  1 
ATOM   3490 C  CG  . ARG B 1 41  ? 20.145  -11.808 -67.750 1.00 19.89 ?  43   ARG B CG  1 
ATOM   3491 C  CD  . ARG B 1 41  ? 21.391  -12.688 -67.681 1.00 24.93 ?  43   ARG B CD  1 
ATOM   3492 N  NE  . ARG B 1 41  ? 22.610  -11.902 -67.478 1.00 23.92 ?  43   ARG B NE  1 
ATOM   3493 C  CZ  . ARG B 1 41  ? 23.297  -11.348 -68.471 1.00 22.66 ?  43   ARG B CZ  1 
ATOM   3494 N  NH1 . ARG B 1 41  ? 22.871  -11.486 -69.718 1.00 29.91 ?  43   ARG B NH1 1 
ATOM   3495 N  NH2 . ARG B 1 41  ? 24.394  -10.646 -68.225 1.00 26.63 ?  43   ARG B NH2 1 
ATOM   3496 N  N   . CYS B 1 42  ? 18.188  -9.816  -64.009 1.00 18.87 ?  44   CYS B N   1 
ATOM   3497 C  CA  . CYS B 1 42  ? 17.693  -9.865  -62.639 1.00 21.28 ?  44   CYS B CA  1 
ATOM   3498 C  C   . CYS B 1 42  ? 16.261  -9.345  -62.528 1.00 19.95 ?  44   CYS B C   1 
ATOM   3499 O  O   . CYS B 1 42  ? 15.517  -9.785  -61.644 1.00 20.34 ?  44   CYS B O   1 
ATOM   3500 C  CB  . CYS B 1 42  ? 18.631  -9.081  -61.717 1.00 20.48 ?  44   CYS B CB  1 
ATOM   3501 S  SG  . CYS B 1 42  ? 20.243  -9.902  -61.477 1.00 26.14 ?  44   CYS B SG  1 
ATOM   3502 N  N   . LEU B 1 43  ? 15.856  -8.414  -63.404 1.00 20.17 ?  45   LEU B N   1 
ATOM   3503 C  CA  . LEU B 1 43  ? 14.466  -7.966  -63.408 1.00 21.56 ?  45   LEU B CA  1 
ATOM   3504 C  C   . LEU B 1 43  ? 13.526  -9.093  -63.813 1.00 26.52 ?  45   LEU B C   1 
ATOM   3505 O  O   . LEU B 1 43  ? 12.363  -9.114  -63.383 1.00 21.58 ?  45   LEU B O   1 
ATOM   3506 C  CB  . LEU B 1 43  ? 14.283  -6.773  -64.350 1.00 17.57 ?  45   LEU B CB  1 
ATOM   3507 C  CG  . LEU B 1 43  ? 14.959  -5.443  -63.990 1.00 23.27 ?  45   LEU B CG  1 
ATOM   3508 C  CD1 . LEU B 1 43  ? 14.510  -4.323  -64.912 1.00 19.49 ?  45   LEU B CD1 1 
ATOM   3509 C  CD2 . LEU B 1 43  ? 14.689  -5.072  -62.537 1.00 27.45 ?  45   LEU B CD2 1 
ATOM   3510 N  N   . ALA B 1 44  ? 14.014  -10.036 -64.626 1.00 22.91 ?  46   ALA B N   1 
ATOM   3511 C  CA  . ALA B 1 44  ? 13.208  -11.158 -65.097 1.00 21.20 ?  46   ALA B CA  1 
ATOM   3512 C  C   . ALA B 1 44  ? 13.242  -12.362 -64.172 1.00 23.70 ?  46   ALA B C   1 
ATOM   3513 O  O   . ALA B 1 44  ? 12.331  -13.192 -64.237 1.00 26.53 ?  46   ALA B O   1 
ATOM   3514 C  CB  . ALA B 1 44  ? 13.664  -11.600 -66.494 1.00 20.69 ?  46   ALA B CB  1 
ATOM   3515 N  N   . GLU B 1 45  ? 14.270  -12.504 -63.333 1.00 20.37 ?  47   GLU B N   1 
ATOM   3516 C  CA  . GLU B 1 45  ? 14.331  -13.588 -62.353 1.00 23.43 ?  47   GLU B CA  1 
ATOM   3517 C  C   . GLU B 1 45  ? 14.909  -13.016 -61.069 1.00 26.86 ?  47   GLU B C   1 
ATOM   3518 O  O   . GLU B 1 45  ? 16.103  -13.174 -60.776 1.00 29.43 ?  47   GLU B O   1 
ATOM   3519 C  CB  . GLU B 1 45  ? 15.160  -14.769 -62.870 1.00 22.20 ?  47   GLU B CB  1 
ATOM   3520 N  N   . PRO B 1 46  ? 14.088  -12.331 -60.279 1.00 22.58 ?  48   PRO B N   1 
ATOM   3521 C  CA  . PRO B 1 46  ? 14.586  -11.629 -59.091 1.00 23.98 ?  48   PRO B CA  1 
ATOM   3522 C  C   . PRO B 1 46  ? 14.628  -12.532 -57.863 1.00 28.74 ?  48   PRO B C   1 
ATOM   3523 O  O   . PRO B 1 46  ? 14.301  -13.714 -57.908 1.00 23.87 ?  48   PRO B O   1 
ATOM   3524 C  CB  . PRO B 1 46  ? 13.588  -10.486 -58.914 1.00 23.78 ?  48   PRO B CB  1 
ATOM   3525 C  CG  . PRO B 1 46  ? 12.318  -10.981 -59.539 1.00 28.11 ?  48   PRO B CG  1 
ATOM   3526 C  CD  . PRO B 1 46  ? 12.687  -11.981 -60.596 1.00 25.30 ?  48   PRO B CD  1 
ATOM   3527 N  N   . ILE B 1 47  ? 15.056  -11.938 -56.752 1.00 19.66 ?  49   ILE B N   1 
ATOM   3528 C  CA  . ILE B 1 47  ? 15.179  -12.622 -55.471 1.00 21.15 ?  49   ILE B CA  1 
ATOM   3529 C  C   . ILE B 1 47  ? 13.909  -12.395 -54.658 1.00 24.50 ?  49   ILE B C   1 
ATOM   3530 O  O   . ILE B 1 47  ? 13.576  -11.255 -54.318 1.00 24.48 ?  49   ILE B O   1 
ATOM   3531 C  CB  . ILE B 1 47  ? 16.418  -12.124 -54.700 1.00 21.85 ?  49   ILE B CB  1 
ATOM   3532 C  CG1 . ILE B 1 47  ? 17.705  -12.426 -55.477 1.00 22.45 ?  49   ILE B CG1 1 
ATOM   3533 C  CG2 . ILE B 1 47  ? 16.446  -12.691 -53.298 1.00 19.31 ?  49   ILE B CG2 1 
ATOM   3534 C  CD1 . ILE B 1 47  ? 18.858  -11.463 -55.170 1.00 23.13 ?  49   ILE B CD1 1 
ATOM   3535 N  N   . GLY B 1 48  ? 13.208  -13.481 -54.328 1.00 23.03 ?  50   GLY B N   1 
ATOM   3536 C  CA  . GLY B 1 48  ? 12.087  -13.398 -53.404 1.00 30.38 ?  50   GLY B CA  1 
ATOM   3537 C  C   . GLY B 1 48  ? 10.929  -12.571 -53.909 1.00 26.49 ?  50   GLY B C   1 
ATOM   3538 O  O   . GLY B 1 48  ? 10.178  -11.998 -53.108 1.00 30.65 ?  50   GLY B O   1 
ATOM   3539 N  N   . SER B 1 49  ? 10.746  -12.508 -55.224 1.00 30.85 ?  51   SER B N   1 
ATOM   3540 C  CA  . SER B 1 49  ? 9.769   -11.599 -55.797 1.00 25.11 ?  51   SER B CA  1 
ATOM   3541 C  C   . SER B 1 49  ? 9.353   -12.134 -57.155 1.00 29.01 ?  51   SER B C   1 
ATOM   3542 O  O   . SER B 1 49  ? 10.136  -12.838 -57.804 1.00 25.62 ?  51   SER B O   1 
ATOM   3543 C  CB  . SER B 1 49  ? 10.364  -10.188 -55.919 1.00 23.56 ?  51   SER B CB  1 
ATOM   3544 O  OG  . SER B 1 49  ? 9.607   -9.372  -56.785 1.00 30.57 ?  51   SER B OG  1 
ATOM   3545 N  N   . PRO B 1 50  ? 8.134   -11.843 -57.606 1.00 29.79 ?  52   PRO B N   1 
ATOM   3546 C  CA  . PRO B 1 50  ? 7.807   -12.044 -59.023 1.00 26.72 ?  52   PRO B CA  1 
ATOM   3547 C  C   . PRO B 1 50  ? 8.667   -11.142 -59.889 1.00 28.11 ?  52   PRO B C   1 
ATOM   3548 O  O   . PRO B 1 50  ? 9.214   -10.143 -59.399 1.00 26.13 ?  52   PRO B O   1 
ATOM   3549 C  CB  . PRO B 1 50  ? 6.319   -11.649 -59.120 1.00 28.64 ?  52   PRO B CB  1 
ATOM   3550 C  CG  . PRO B 1 50  ? 5.812   -11.636 -57.717 1.00 30.66 ?  52   PRO B CG  1 
ATOM   3551 C  CD  . PRO B 1 50  ? 6.996   -11.318 -56.833 1.00 27.79 ?  52   PRO B CD  1 
ATOM   3552 N  N   . PRO B 1 51  ? 8.816   -11.463 -61.174 1.00 23.38 ?  53   PRO B N   1 
ATOM   3553 C  CA  . PRO B 1 51  ? 9.473   -10.533 -62.100 1.00 24.49 ?  53   PRO B CA  1 
ATOM   3554 C  C   . PRO B 1 51  ? 8.852   -9.146  -62.020 1.00 27.98 ?  53   PRO B C   1 
ATOM   3555 O  O   . PRO B 1 51  ? 7.647   -8.999  -61.803 1.00 25.94 ?  53   PRO B O   1 
ATOM   3556 C  CB  . PRO B 1 51  ? 9.229   -11.174 -63.473 1.00 21.92 ?  53   PRO B CB  1 
ATOM   3557 C  CG  . PRO B 1 51  ? 9.047   -12.617 -63.183 1.00 21.73 ?  53   PRO B CG  1 
ATOM   3558 C  CD  . PRO B 1 51  ? 8.390   -12.707 -61.843 1.00 25.65 ?  53   PRO B CD  1 
ATOM   3559 N  N   . LEU B 1 52  ? 9.690   -8.119  -62.208 1.00 20.21 ?  54   LEU B N   1 
ATOM   3560 C  CA  . LEU B 1 52  ? 9.190   -6.746  -62.170 1.00 20.47 ?  54   LEU B CA  1 
ATOM   3561 C  C   . LEU B 1 52  ? 8.068   -6.534  -63.182 1.00 25.65 ?  54   LEU B C   1 
ATOM   3562 O  O   . LEU B 1 52  ? 7.075   -5.855  -62.885 1.00 24.91 ?  54   LEU B O   1 
ATOM   3563 C  CB  . LEU B 1 52  ? 10.322  -5.752  -62.426 1.00 21.26 ?  54   LEU B CB  1 
ATOM   3564 C  CG  . LEU B 1 52  ? 9.897   -4.291  -62.575 1.00 20.18 ?  54   LEU B CG  1 
ATOM   3565 C  CD1 . LEU B 1 52  ? 9.206   -3.769  -61.313 1.00 18.76 ?  54   LEU B CD1 1 
ATOM   3566 C  CD2 . LEU B 1 52  ? 11.085  -3.423  -62.942 1.00 20.76 ?  54   LEU B CD2 1 
ATOM   3567 N  N   . LEU B 1 53  ? 8.215   -7.087  -64.389 1.00 22.13 ?  55   LEU B N   1 
ATOM   3568 C  CA  . LEU B 1 53  ? 7.134   -7.016  -65.372 1.00 27.11 ?  55   LEU B CA  1 
ATOM   3569 C  C   . LEU B 1 53  ? 5.819   -7.517  -64.784 1.00 22.98 ?  55   LEU B C   1 
ATOM   3570 O  O   . LEU B 1 53  ? 4.777   -6.860  -64.910 1.00 25.33 ?  55   LEU B O   1 
ATOM   3571 C  CB  . LEU B 1 53  ? 7.508   -7.815  -66.622 1.00 26.34 ?  55   LEU B CB  1 
ATOM   3572 C  CG  . LEU B 1 53  ? 6.491   -7.794  -67.771 1.00 24.56 ?  55   LEU B CG  1 
ATOM   3573 C  CD1 . LEU B 1 53  ? 6.136   -6.379  -68.182 1.00 25.42 ?  55   LEU B CD1 1 
ATOM   3574 C  CD2 . LEU B 1 53  ? 7.044   -8.572  -68.950 1.00 25.81 ?  55   LEU B CD2 1 
ATOM   3575 N  N   . ASP B 1 54  ? 5.858   -8.668  -64.104 1.00 25.89 ?  56   ASP B N   1 
ATOM   3576 C  CA  . ASP B 1 54  ? 4.639   -9.241  -63.539 1.00 26.24 ?  56   ASP B CA  1 
ATOM   3577 C  C   . ASP B 1 54  ? 4.045   -8.345  -62.450 1.00 29.20 ?  56   ASP B C   1 
ATOM   3578 O  O   . ASP B 1 54  ? 2.822   -8.183  -62.370 1.00 24.35 ?  56   ASP B O   1 
ATOM   3579 C  CB  . ASP B 1 54  ? 4.920   -10.644 -62.992 1.00 24.26 ?  56   ASP B CB  1 
ATOM   3580 C  CG  . ASP B 1 54  ? 5.422   -11.612 -64.068 1.00 19.24 ?  56   ASP B CG  1 
ATOM   3581 N  N   . LEU B 1 55  ? 4.891   -7.756  -61.598 1.00 20.80 ?  57   LEU B N   1 
ATOM   3582 C  CA  . LEU B 1 55  ? 4.389   -6.833  -60.578 1.00 19.25 ?  57   LEU B CA  1 
ATOM   3583 C  C   . LEU B 1 55  ? 3.789   -5.571  -61.172 1.00 22.30 ?  57   LEU B C   1 
ATOM   3584 O  O   . LEU B 1 55  ? 2.908   -4.961  -60.558 1.00 25.58 ?  57   LEU B O   1 
ATOM   3585 C  CB  . LEU B 1 55  ? 5.496   -6.433  -59.593 1.00 18.64 ?  57   LEU B CB  1 
ATOM   3586 C  CG  . LEU B 1 55  ? 6.248   -7.564  -58.942 1.00 22.10 ?  57   LEU B CG  1 
ATOM   3587 C  CD1 . LEU B 1 55  ? 7.515   -7.018  -58.301 1.00 20.23 ?  57   LEU B CD1 1 
ATOM   3588 C  CD2 . LEU B 1 55  ? 5.320   -8.175  -57.910 1.00 29.42 ?  57   LEU B CD2 1 
ATOM   3589 N  N   . ALA B 1 56  ? 4.256   -5.149  -62.334 1.00 18.72 ?  58   ALA B N   1 
ATOM   3590 C  CA  . ALA B 1 56  ? 3.779   -3.901  -62.899 1.00 17.53 ?  58   ALA B CA  1 
ATOM   3591 C  C   . ALA B 1 56  ? 2.464   -4.058  -63.658 1.00 27.68 ?  58   ALA B C   1 
ATOM   3592 O  O   . ALA B 1 56  ? 1.920   -3.045  -64.107 1.00 24.99 ?  58   ALA B O   1 
ATOM   3593 C  CB  . ALA B 1 56  ? 4.839   -3.301  -63.827 1.00 20.75 ?  58   ALA B CB  1 
ATOM   3594 N  N   . ARG B 1 57  ? 1.955   -5.286  -63.822 1.00 25.46 ?  59   ARG B N   1 
ATOM   3595 C  CA  . ARG B 1 57  ? 0.673   -5.490  -64.500 1.00 29.27 ?  59   ARG B CA  1 
ATOM   3596 C  C   . ARG B 1 57  ? -0.466  -4.974  -63.630 1.00 30.87 ?  59   ARG B C   1 
ATOM   3597 O  O   . ARG B 1 57  ? -0.544  -5.288  -62.435 1.00 36.02 ?  59   ARG B O   1 
ATOM   3598 C  CB  . ARG B 1 57  ? 0.443   -6.973  -64.814 1.00 29.62 ?  59   ARG B CB  1 
ATOM   3599 C  CG  . ARG B 1 57  ? 1.582   -7.671  -65.543 1.00 33.66 ?  59   ARG B CG  1 
ATOM   3600 C  CD  . ARG B 1 57  ? 1.833   -7.052  -66.898 1.00 33.57 ?  59   ARG B CD  1 
ATOM   3601 N  NE  . ARG B 1 57  ? 2.497   -7.971  -67.823 1.00 27.89 ?  59   ARG B NE  1 
ATOM   3602 C  CZ  . ARG B 1 57  ? 2.624   -7.736  -69.124 1.00 24.18 ?  59   ARG B CZ  1 
ATOM   3603 N  NH1 . ARG B 1 57  ? 2.105   -6.634  -69.641 1.00 36.56 ?  59   ARG B NH1 1 
ATOM   3604 N  NH2 . ARG B 1 57  ? 3.260   -8.598  -69.909 1.00 27.56 ?  59   ARG B NH2 1 
ATOM   3605 N  N   . GLY B 1 58  ? -1.362  -4.196  -64.232 1.00 32.32 ?  60   GLY B N   1 
ATOM   3606 C  CA  . GLY B 1 58  ? -2.496  -3.663  -63.507 1.00 38.37 ?  60   GLY B CA  1 
ATOM   3607 C  C   . GLY B 1 58  ? -2.197  -2.455  -62.648 1.00 37.41 ?  60   GLY B C   1 
ATOM   3608 O  O   . GLY B 1 58  ? -3.096  -1.986  -61.941 1.00 38.59 ?  60   GLY B O   1 
ATOM   3609 N  N   . LYS B 1 59  ? -0.968  -1.937  -62.690 1.00 37.64 ?  61   LYS B N   1 
ATOM   3610 C  CA  . LYS B 1 59  ? -0.581  -0.741  -61.954 1.00 34.36 ?  61   LYS B CA  1 
ATOM   3611 C  C   . LYS B 1 59  ? -0.741  0.484   -62.846 1.00 25.17 ?  61   LYS B C   1 
ATOM   3612 O  O   . LYS B 1 59  ? -0.424  0.441   -64.035 1.00 26.91 ?  61   LYS B O   1 
ATOM   3613 C  CB  . LYS B 1 59  ? 0.872   -0.847  -61.481 1.00 24.11 ?  61   LYS B CB  1 
ATOM   3614 C  CG  . LYS B 1 59  ? 1.172   -2.116  -60.694 1.00 26.19 ?  61   LYS B CG  1 
ATOM   3615 C  CD  . LYS B 1 59  ? 0.467   -2.129  -59.354 1.00 31.84 ?  61   LYS B CD  1 
ATOM   3616 C  CE  . LYS B 1 59  ? 0.833   -3.364  -58.547 1.00 30.37 ?  61   LYS B CE  1 
ATOM   3617 N  NZ  . LYS B 1 59  ? 1.096   -3.012  -57.116 1.00 37.33 ?  61   LYS B NZ  1 
ATOM   3618 N  N   . ARG B 1 60  ? -1.221  1.583   -62.261 1.00 26.92 ?  62   ARG B N   1 
ATOM   3619 C  CA  . ARG B 1 60  ? -1.488  2.801   -63.016 1.00 35.33 ?  62   ARG B CA  1 
ATOM   3620 C  C   . ARG B 1 60  ? -0.453  3.900   -62.805 1.00 35.92 ?  62   ARG B C   1 
ATOM   3621 O  O   . ARG B 1 60  ? -0.448  4.874   -63.567 1.00 36.36 ?  62   ARG B O   1 
ATOM   3622 C  CB  . ARG B 1 60  ? -2.881  3.347   -62.664 1.00 34.33 ?  62   ARG B CB  1 
ATOM   3623 N  N   . SER B 1 61  ? 0.416   3.776   -61.801 1.00 29.81 ?  63   SER B N   1 
ATOM   3624 C  CA  . SER B 1 61  ? 1.386   4.814   -61.487 1.00 27.18 ?  63   SER B CA  1 
ATOM   3625 C  C   . SER B 1 61  ? 2.592   4.166   -60.819 1.00 26.18 ?  63   SER B C   1 
ATOM   3626 O  O   . SER B 1 61  ? 2.474   3.111   -60.189 1.00 23.45 ?  63   SER B O   1 
ATOM   3627 C  CB  . SER B 1 61  ? 0.777   5.895   -60.579 1.00 25.07 ?  63   SER B CB  1 
ATOM   3628 O  OG  . SER B 1 61  ? 0.521   5.379   -59.278 1.00 27.31 ?  63   SER B OG  1 
ATOM   3629 N  N   . ALA B 1 62  ? 3.751   4.800   -60.965 1.00 23.30 ?  64   ALA B N   1 
ATOM   3630 C  CA  . ALA B 1 62  ? 4.983   4.263   -60.395 1.00 23.34 ?  64   ALA B CA  1 
ATOM   3631 C  C   . ALA B 1 62  ? 5.821   5.374   -59.784 1.00 20.44 ?  64   ALA B C   1 
ATOM   3632 O  O   . ALA B 1 62  ? 5.924   6.471   -60.342 1.00 17.89 ?  64   ALA B O   1 
ATOM   3633 C  CB  . ALA B 1 62  ? 5.816   3.528   -61.452 1.00 23.19 ?  64   ALA B CB  1 
ATOM   3634 N  N   . CYS B 1 63  ? 6.447   5.072   -58.648 1.00 22.83 ?  65   CYS B N   1 
ATOM   3635 C  CA  . CYS B 1 63  ? 7.445   5.952   -58.060 1.00 17.99 ?  65   CYS B CA  1 
ATOM   3636 C  C   . CYS B 1 63  ? 8.738   5.171   -57.865 1.00 13.45 ?  65   CYS B C   1 
ATOM   3637 O  O   . CYS B 1 63  ? 8.727   4.103   -57.245 1.00 17.64 ?  65   CYS B O   1 
ATOM   3638 C  CB  . CYS B 1 63  ? 6.976   6.527   -56.725 1.00 20.28 ?  65   CYS B CB  1 
ATOM   3639 S  SG  . CYS B 1 63  ? 8.136   7.749   -56.030 1.00 22.46 ?  65   CYS B SG  1 
ATOM   3640 N  N   . ILE B 1 64  ? 9.829   5.708   -58.404 1.00 15.19 ?  66   ILE B N   1 
ATOM   3641 C  CA  . ILE B 1 64  ? 11.162  5.099   -58.333 1.00 15.37 ?  66   ILE B CA  1 
ATOM   3642 C  C   . ILE B 1 64  ? 12.063  5.998   -57.503 1.00 14.57 ?  66   ILE B C   1 
ATOM   3643 O  O   . ILE B 1 64  ? 12.311  7.152   -57.876 1.00 15.38 ?  66   ILE B O   1 
ATOM   3644 C  CB  . ILE B 1 64  ? 11.771  4.901   -59.727 1.00 16.26 ?  66   ILE B CB  1 
ATOM   3645 C  CG1 . ILE B 1 64  ? 10.840  4.107   -60.640 1.00 11.52 ?  66   ILE B CG1 1 
ATOM   3646 C  CG2 . ILE B 1 64  ? 13.138  4.197   -59.636 1.00 17.64 ?  66   ILE B CG2 1 
ATOM   3647 C  CD1 . ILE B 1 64  ? 11.285  4.248   -62.083 1.00 16.54 ?  66   ILE B CD1 1 
ATOM   3648 N  N   . LEU B 1 65  ? 12.618  5.452   -56.421 1.00 16.14 ?  67   LEU B N   1 
ATOM   3649 C  CA  . LEU B 1 65  ? 13.532  6.208   -55.573 1.00 18.08 ?  67   LEU B CA  1 
ATOM   3650 C  C   . LEU B 1 65  ? 14.957  6.039   -56.075 1.00 16.44 ?  67   LEU B C   1 
ATOM   3651 O  O   . LEU B 1 65  ? 15.386  4.913   -56.353 1.00 13.39 ?  67   LEU B O   1 
ATOM   3652 C  CB  . LEU B 1 65  ? 13.432  5.744   -54.121 1.00 14.05 ?  67   LEU B CB  1 
ATOM   3653 C  CG  . LEU B 1 65  ? 12.044  5.787   -53.481 1.00 18.15 ?  67   LEU B CG  1 
ATOM   3654 C  CD1 . LEU B 1 65  ? 12.142  5.386   -52.015 1.00 15.58 ?  67   LEU B CD1 1 
ATOM   3655 C  CD2 . LEU B 1 65  ? 11.427  7.174   -53.664 1.00 15.73 ?  67   LEU B CD2 1 
ATOM   3656 N  N   . VAL B 1 66  ? 15.687  7.158   -56.193 1.00 15.77 ?  68   VAL B N   1 
ATOM   3657 C  CA  . VAL B 1 66  ? 17.105  7.129   -56.527 1.00 16.54 ?  68   VAL B CA  1 
ATOM   3658 C  C   . VAL B 1 66  ? 17.890  7.936   -55.500 1.00 14.51 ?  68   VAL B C   1 
ATOM   3659 O  O   . VAL B 1 66  ? 17.373  8.852   -54.851 1.00 13.04 ?  68   VAL B O   1 
ATOM   3660 C  CB  . VAL B 1 66  ? 17.410  7.656   -57.943 1.00 12.66 ?  68   VAL B CB  1 
ATOM   3661 C  CG1 . VAL B 1 66  ? 16.657  6.835   -59.007 1.00 14.81 ?  68   VAL B CG1 1 
ATOM   3662 C  CG2 . VAL B 1 66  ? 17.107  9.138   -58.038 1.00 14.97 ?  68   VAL B CG2 1 
ATOM   3663 N  N   . CYS B 1 67  ? 19.172  7.598   -55.382 1.00 15.46 ?  69   CYS B N   1 
ATOM   3664 C  CA  . CYS B 1 67  ? 20.049  8.316   -54.465 1.00 12.00 ?  69   CYS B CA  1 
ATOM   3665 C  C   . CYS B 1 67  ? 20.430  9.682   -55.025 1.00 14.09 ?  69   CYS B C   1 
ATOM   3666 O  O   . CYS B 1 67  ? 20.396  9.912   -56.237 1.00 15.31 ?  69   CYS B O   1 
ATOM   3667 C  CB  . CYS B 1 67  ? 21.309  7.496   -54.201 1.00 10.16 ?  69   CYS B CB  1 
ATOM   3668 S  SG  . CYS B 1 67  ? 20.953  5.946   -53.348 1.00 19.09 ?  69   CYS B SG  1 
ATOM   3669 N  N   . ASP B 1 68  ? 20.832  10.594  -54.122 1.00 14.18 ?  70   ASP B N   1 
ATOM   3670 C  CA  . ASP B 1 68  ? 21.270  11.920  -54.522 1.00 13.07 ?  70   ASP B CA  1 
ATOM   3671 C  C   . ASP B 1 68  ? 22.754  11.884  -54.890 1.00 14.71 ?  70   ASP B C   1 
ATOM   3672 O  O   . ASP B 1 68  ? 23.350  10.816  -55.033 1.00 16.50 ?  70   ASP B O   1 
ATOM   3673 C  CB  . ASP B 1 68  ? 20.918  12.949  -53.443 1.00 14.99 ?  70   ASP B CB  1 
ATOM   3674 C  CG  . ASP B 1 68  ? 21.800  12.860  -52.181 1.00 16.37 ?  70   ASP B CG  1 
ATOM   3675 O  OD1 . ASP B 1 68  ? 22.636  11.943  -52.041 1.00 13.24 ?  70   ASP B OD1 1 
ATOM   3676 O  OD2 . ASP B 1 68  ? 21.600  13.723  -51.305 1.00 15.45 ?  70   ASP B OD2 1 
ATOM   3677 N  N   . ILE B 1 69  ? 23.356  13.062  -55.078 1.00 13.65 ?  71   ILE B N   1 
ATOM   3678 C  CA  . ILE B 1 69  ? 24.698  13.148  -55.637 1.00 17.77 ?  71   ILE B CA  1 
ATOM   3679 C  C   . ILE B 1 69  ? 25.732  12.478  -54.741 1.00 17.35 ?  71   ILE B C   1 
ATOM   3680 O  O   . ILE B 1 69  ? 26.795  12.070  -55.225 1.00 14.96 ?  71   ILE B O   1 
ATOM   3681 C  CB  . ILE B 1 69  ? 25.073  14.627  -55.897 1.00 17.22 ?  71   ILE B CB  1 
ATOM   3682 C  CG1 . ILE B 1 69  ? 26.212  14.721  -56.916 1.00 18.26 ?  71   ILE B CG1 1 
ATOM   3683 C  CG2 . ILE B 1 69  ? 25.418  15.354  -54.586 1.00 16.80 ?  71   ILE B CG2 1 
ATOM   3684 C  CD1 . ILE B 1 69  ? 25.893  14.076  -58.270 1.00 20.86 ?  71   ILE B CD1 1 
ATOM   3685 N  N   . THR B 1 70  ? 25.438  12.314  -53.458 1.00 11.14 ?  72   THR B N   1 
ATOM   3686 C  CA  . THR B 1 70  ? 26.496  11.856  -52.546 1.00 12.46 ?  72   THR B CA  1 
ATOM   3687 C  C   . THR B 1 70  ? 26.764  10.362  -52.657 1.00 12.70 ?  72   THR B C   1 
ATOM   3688 O  O   . THR B 1 70  ? 27.708  9.869   -52.020 1.00 14.26 ?  72   THR B O   1 
ATOM   3689 C  CB  . THR B 1 70  ? 26.153  12.184  -51.089 1.00 15.44 ?  72   THR B CB  1 
ATOM   3690 O  OG1 . THR B 1 70  ? 25.068  11.358  -50.644 1.00 13.08 ?  72   THR B OG1 1 
ATOM   3691 C  CG2 . THR B 1 70  ? 25.786  13.654  -50.914 1.00 15.07 ?  72   THR B CG2 1 
ATOM   3692 N  N   . ARG B 1 71  ? 25.942  9.628   -53.412 1.00 10.45 ?  73   ARG B N   1 
ATOM   3693 C  CA  . ARG B 1 71  ? 26.149  8.207   -53.648 1.00 9.81  ?  73   ARG B CA  1 
ATOM   3694 C  C   . ARG B 1 71  ? 26.471  7.980   -55.112 1.00 14.47 ?  73   ARG B C   1 
ATOM   3695 O  O   . ARG B 1 71  ? 25.623  8.259   -55.973 1.00 15.25 ?  73   ARG B O   1 
ATOM   3696 C  CB  . ARG B 1 71  ? 24.933  7.371   -53.252 1.00 9.79  ?  73   ARG B CB  1 
ATOM   3697 C  CG  . ARG B 1 71  ? 24.232  7.809   -51.960 1.00 17.05 ?  73   ARG B CG  1 
ATOM   3698 C  CD  . ARG B 1 71  ? 25.204  7.810   -50.795 1.00 13.86 ?  73   ARG B CD  1 
ATOM   3699 N  NE  . ARG B 1 71  ? 24.582  7.481   -49.517 1.00 14.24 ?  73   ARG B NE  1 
ATOM   3700 C  CZ  . ARG B 1 71  ? 24.627  8.246   -48.427 1.00 13.36 ?  73   ARG B CZ  1 
ATOM   3701 N  NH1 . ARG B 1 71  ? 25.236  9.428   -48.444 1.00 10.81 ?  73   ARG B NH1 1 
ATOM   3702 N  NH2 . ARG B 1 71  ? 24.062  7.815   -47.307 1.00 12.51 ?  73   ARG B NH2 1 
ATOM   3703 N  N   . PRO B 1 72  ? 27.627  7.437   -55.431 1.00 10.48 ?  74   PRO B N   1 
ATOM   3704 C  CA  . PRO B 1 72  ? 28.035  7.232   -56.828 1.00 15.45 ?  74   PRO B CA  1 
ATOM   3705 C  C   . PRO B 1 72  ? 27.322  6.074   -57.523 1.00 14.46 ?  74   PRO B C   1 
ATOM   3706 O  O   . PRO B 1 72  ? 27.953  5.228   -58.168 1.00 16.87 ?  74   PRO B O   1 
ATOM   3707 C  CB  . PRO B 1 72  ? 29.541  6.979   -56.703 1.00 13.62 ?  74   PRO B CB  1 
ATOM   3708 C  CG  . PRO B 1 72  ? 29.687  6.301   -55.382 1.00 11.48 ?  74   PRO B CG  1 
ATOM   3709 C  CD  . PRO B 1 72  ? 28.657  6.965   -54.477 1.00 12.74 ?  74   PRO B CD  1 
ATOM   3710 N  N   . VAL B 1 73  ? 25.996  6.045   -57.408 1.00 15.92 ?  75   VAL B N   1 
ATOM   3711 C  CA  . VAL B 1 73  ? 25.219  5.004   -58.088 1.00 20.75 ?  75   VAL B CA  1 
ATOM   3712 C  C   . VAL B 1 73  ? 25.276  5.251   -59.588 1.00 18.81 ?  75   VAL B C   1 
ATOM   3713 O  O   . VAL B 1 73  ? 24.987  6.371   -60.030 1.00 18.02 ?  75   VAL B O   1 
ATOM   3714 C  CB  . VAL B 1 73  ? 23.767  5.006   -57.610 1.00 19.72 ?  75   VAL B CB  1 
ATOM   3715 C  CG1 . VAL B 1 73  ? 23.044  3.755   -58.154 1.00 20.01 ?  75   VAL B CG1 1 
ATOM   3716 C  CG2 . VAL B 1 73  ? 23.666  5.094   -56.085 1.00 17.42 ?  75   VAL B CG2 1 
ATOM   3717 N  N   . PRO B 1 74  ? 25.635  4.270   -60.395 1.00 19.48 ?  76   PRO B N   1 
ATOM   3718 C  CA  . PRO B 1 74  ? 25.502  4.453   -61.856 1.00 16.35 ?  76   PRO B CA  1 
ATOM   3719 C  C   . PRO B 1 74  ? 24.051  4.245   -62.270 1.00 20.71 ?  76   PRO B C   1 
ATOM   3720 O  O   . PRO B 1 74  ? 23.677  3.243   -62.885 1.00 18.05 ?  76   PRO B O   1 
ATOM   3721 C  CB  . PRO B 1 74  ? 26.449  3.385   -62.411 1.00 19.04 ?  76   PRO B CB  1 
ATOM   3722 C  CG  . PRO B 1 74  ? 26.459  2.318   -61.379 1.00 23.30 ?  76   PRO B CG  1 
ATOM   3723 C  CD  . PRO B 1 74  ? 26.135  2.931   -60.039 1.00 18.71 ?  76   PRO B CD  1 
ATOM   3724 N  N   . ASN B 1 75  ? 23.212  5.211   -61.891 1.00 17.03 ?  77   ASN B N   1 
ATOM   3725 C  CA  . ASN B 1 75  ? 21.765  5.074   -62.059 1.00 18.73 ?  77   ASN B CA  1 
ATOM   3726 C  C   . ASN B 1 75  ? 21.305  4.701   -63.464 1.00 19.87 ?  77   ASN B C   1 
ATOM   3727 O  O   . ASN B 1 75  ? 20.350  3.910   -63.567 1.00 20.78 ?  77   ASN B O   1 
ATOM   3728 C  CB  . ASN B 1 75  ? 21.056  6.364   -61.622 1.00 19.68 ?  77   ASN B CB  1 
ATOM   3729 C  CG  . ASN B 1 75  ? 21.201  6.646   -60.140 1.00 19.58 ?  77   ASN B CG  1 
ATOM   3730 O  OD1 . ASN B 1 75  ? 20.673  5.915   -59.299 1.00 19.56 ?  77   ASN B OD1 1 
ATOM   3731 N  ND2 . ASN B 1 75  ? 21.879  7.739   -59.814 1.00 22.57 ?  77   ASN B ND2 1 
ATOM   3732 N  N   . PRO B 1 76  ? 21.893  5.210   -64.559 1.00 19.58 ?  78   PRO B N   1 
ATOM   3733 C  CA  . PRO B 1 76  ? 21.371  4.839   -65.888 1.00 22.12 ?  78   PRO B CA  1 
ATOM   3734 C  C   . PRO B 1 76  ? 21.454  3.348   -66.170 1.00 23.04 ?  78   PRO B C   1 
ATOM   3735 O  O   . PRO B 1 76  ? 20.587  2.810   -66.872 1.00 20.60 ?  78   PRO B O   1 
ATOM   3736 C  CB  . PRO B 1 76  ? 22.256  5.649   -66.851 1.00 23.20 ?  78   PRO B CB  1 
ATOM   3737 C  CG  . PRO B 1 76  ? 22.771  6.796   -66.028 1.00 23.34 ?  78   PRO B CG  1 
ATOM   3738 C  CD  . PRO B 1 76  ? 22.994  6.194   -64.674 1.00 16.10 ?  78   PRO B CD  1 
ATOM   3739 N  N   . VAL B 1 77  ? 22.472  2.664   -65.633 1.00 16.83 ?  79   VAL B N   1 
ATOM   3740 C  CA  . VAL B 1 77  ? 22.589  1.215   -65.784 1.00 18.98 ?  79   VAL B CA  1 
ATOM   3741 C  C   . VAL B 1 77  ? 21.401  0.501   -65.148 1.00 21.14 ?  79   VAL B C   1 
ATOM   3742 O  O   . VAL B 1 77  ? 20.960  -0.553  -65.627 1.00 20.18 ?  79   VAL B O   1 
ATOM   3743 C  CB  . VAL B 1 77  ? 23.933  0.755   -65.168 1.00 17.34 ?  79   VAL B CB  1 
ATOM   3744 C  CG1 . VAL B 1 77  ? 24.022  -0.752  -65.088 1.00 18.57 ?  79   VAL B CG1 1 
ATOM   3745 C  CG2 . VAL B 1 77  ? 25.097  1.327   -65.963 1.00 21.64 ?  79   VAL B CG2 1 
ATOM   3746 N  N   . LEU B 1 78  ? 20.866  1.053   -64.064 1.00 18.12 ?  80   LEU B N   1 
ATOM   3747 C  CA  . LEU B 1 78  ? 19.719  0.473   -63.380 1.00 16.86 ?  80   LEU B CA  1 
ATOM   3748 C  C   . LEU B 1 78  ? 18.397  0.928   -63.988 1.00 19.86 ?  80   LEU B C   1 
ATOM   3749 O  O   . LEU B 1 78  ? 17.460  0.131   -64.101 1.00 20.27 ?  80   LEU B O   1 
ATOM   3750 C  CB  . LEU B 1 78  ? 19.755  0.851   -61.893 1.00 17.24 ?  80   LEU B CB  1 
ATOM   3751 C  CG  . LEU B 1 78  ? 20.897  0.300   -61.014 1.00 16.56 ?  80   LEU B CG  1 
ATOM   3752 C  CD1 . LEU B 1 78  ? 22.234  0.973   -61.275 1.00 24.67 ?  80   LEU B CD1 1 
ATOM   3753 C  CD2 . LEU B 1 78  ? 20.524  0.477   -59.547 1.00 20.56 ?  80   LEU B CD2 1 
ATOM   3754 N  N   . LEU B 1 79  ? 18.314  2.196   -64.388 1.00 15.93 ?  81   LEU B N   1 
ATOM   3755 C  CA  . LEU B 1 79  ? 17.027  2.811   -64.710 1.00 17.58 ?  81   LEU B CA  1 
ATOM   3756 C  C   . LEU B 1 79  ? 16.558  2.472   -66.117 1.00 22.03 ?  81   LEU B C   1 
ATOM   3757 O  O   . LEU B 1 79  ? 15.357  2.284   -66.336 1.00 21.43 ?  81   LEU B O   1 
ATOM   3758 C  CB  . LEU B 1 79  ? 17.124  4.325   -64.548 1.00 19.05 ?  81   LEU B CB  1 
ATOM   3759 C  CG  . LEU B 1 79  ? 17.040  4.850   -63.118 1.00 20.81 ?  81   LEU B CG  1 
ATOM   3760 C  CD1 . LEU B 1 79  ? 17.311  6.340   -63.098 1.00 19.73 ?  81   LEU B CD1 1 
ATOM   3761 C  CD2 . LEU B 1 79  ? 15.685  4.540   -62.516 1.00 22.47 ?  81   LEU B CD2 1 
ATOM   3762 N  N   . ARG B 1 80  ? 17.470  2.417   -67.090 1.00 23.51 ?  82   ARG B N   1 
ATOM   3763 C  CA  . ARG B 1 80  ? 17.044  2.068   -68.446 1.00 24.96 ?  82   ARG B CA  1 
ATOM   3764 C  C   . ARG B 1 80  ? 16.333  0.720   -68.499 1.00 22.07 ?  82   ARG B C   1 
ATOM   3765 O  O   . ARG B 1 80  ? 15.240  0.650   -69.092 1.00 25.00 ?  82   ARG B O   1 
ATOM   3766 C  CB  . ARG B 1 80  ? 18.238  2.130   -69.403 1.00 27.29 ?  82   ARG B CB  1 
ATOM   3767 C  CG  . ARG B 1 80  ? 18.675  3.543   -69.751 1.00 22.02 ?  82   ARG B CG  1 
ATOM   3768 C  CD  . ARG B 1 80  ? 19.698  3.536   -70.876 1.00 29.02 ?  82   ARG B CD  1 
ATOM   3769 N  NE  . ARG B 1 80  ? 20.940  2.894   -70.452 1.00 31.07 ?  82   ARG B NE  1 
ATOM   3770 C  CZ  . ARG B 1 80  ? 22.045  3.547   -70.099 1.00 29.95 ?  82   ARG B CZ  1 
ATOM   3771 N  NH1 . ARG B 1 80  ? 22.071  4.871   -70.131 1.00 27.01 ?  82   ARG B NH1 1 
ATOM   3772 N  NH2 . ARG B 1 80  ? 23.123  2.871   -69.714 1.00 24.20 ?  82   ARG B NH2 1 
ATOM   3773 N  N   . PRO B 1 81  ? 16.851  -0.361  -67.899 1.00 22.09 ?  83   PRO B N   1 
ATOM   3774 C  CA  . PRO B 1 81  ? 16.054  -1.600  -67.845 1.00 23.69 ?  83   PRO B CA  1 
ATOM   3775 C  C   . PRO B 1 81  ? 14.755  -1.459  -67.059 1.00 24.40 ?  83   PRO B C   1 
ATOM   3776 O  O   . PRO B 1 81  ? 13.741  -2.054  -67.449 1.00 22.53 ?  83   PRO B O   1 
ATOM   3777 C  CB  . PRO B 1 81  ? 17.010  -2.600  -67.175 1.00 20.98 ?  83   PRO B CB  1 
ATOM   3778 C  CG  . PRO B 1 81  ? 18.388  -2.041  -67.432 1.00 20.31 ?  83   PRO B CG  1 
ATOM   3779 C  CD  . PRO B 1 81  ? 18.205  -0.564  -67.335 1.00 18.09 ?  83   PRO B CD  1 
ATOM   3780 N  N   . ILE B 1 82  ? 14.757  -0.710  -65.950 1.00 17.96 ?  84   ILE B N   1 
ATOM   3781 C  CA  . ILE B 1 82  ? 13.534  -0.533  -65.167 1.00 16.86 ?  84   ILE B CA  1 
ATOM   3782 C  C   . ILE B 1 82  ? 12.493  0.218   -65.981 1.00 21.88 ?  84   ILE B C   1 
ATOM   3783 O  O   . ILE B 1 82  ? 11.318  -0.169  -66.034 1.00 22.87 ?  84   ILE B O   1 
ATOM   3784 C  CB  . ILE B 1 82  ? 13.830  0.201   -63.847 1.00 18.69 ?  84   ILE B CB  1 
ATOM   3785 C  CG1 . ILE B 1 82  ? 14.641  -0.680  -62.902 1.00 20.15 ?  84   ILE B CG1 1 
ATOM   3786 C  CG2 . ILE B 1 82  ? 12.530  0.624   -63.170 1.00 20.17 ?  84   ILE B CG2 1 
ATOM   3787 C  CD1 . ILE B 1 82  ? 15.141  0.086   -61.683 1.00 17.41 ?  84   ILE B CD1 1 
ATOM   3788 N  N   . LEU B 1 83  ? 12.909  1.307   -66.628 1.00 17.24 ?  85   LEU B N   1 
ATOM   3789 C  CA  . LEU B 1 83  ? 11.951  2.133   -67.350 1.00 21.09 ?  85   LEU B CA  1 
ATOM   3790 C  C   . LEU B 1 83  ? 11.406  1.401   -68.571 1.00 25.67 ?  85   LEU B C   1 
ATOM   3791 O  O   . LEU B 1 83  ? 10.213  1.502   -68.876 1.00 25.08 ?  85   LEU B O   1 
ATOM   3792 C  CB  . LEU B 1 83  ? 12.598  3.463   -67.735 1.00 22.79 ?  85   LEU B CB  1 
ATOM   3793 C  CG  . LEU B 1 83  ? 12.856  4.425   -66.564 1.00 21.99 ?  85   LEU B CG  1 
ATOM   3794 C  CD1 . LEU B 1 83  ? 13.779  5.560   -66.989 1.00 20.85 ?  85   LEU B CD1 1 
ATOM   3795 C  CD2 . LEU B 1 83  ? 11.555  4.977   -65.993 1.00 26.47 ?  85   LEU B CD2 1 
ATOM   3796 N  N   . ARG B 1 84  ? 12.250  0.632   -69.261 1.00 22.52 ?  86   ARG B N   1 
ATOM   3797 C  CA  . ARG B 1 84  ? 11.757  -0.162  -70.381 1.00 24.11 ?  86   ARG B CA  1 
ATOM   3798 C  C   . ARG B 1 84  ? 10.750  -1.205  -69.914 1.00 30.05 ?  86   ARG B C   1 
ATOM   3799 O  O   . ARG B 1 84  ? 9.748   -1.457  -70.594 1.00 28.31 ?  86   ARG B O   1 
ATOM   3800 C  CB  . ARG B 1 84  ? 12.919  -0.821  -71.121 1.00 26.88 ?  86   ARG B CB  1 
ATOM   3801 C  CG  . ARG B 1 84  ? 13.479  0.026   -72.250 1.00 36.75 ?  86   ARG B CG  1 
ATOM   3802 C  CD  . ARG B 1 84  ? 14.104  -0.836  -73.344 1.00 40.93 ?  86   ARG B CD  1 
ATOM   3803 N  NE  . ARG B 1 84  ? 14.700  -2.050  -72.803 1.00 42.12 ?  86   ARG B NE  1 
ATOM   3804 C  CZ  . ARG B 1 84  ? 15.955  -2.132  -72.374 1.00 44.45 ?  86   ARG B CZ  1 
ATOM   3805 N  NH1 . ARG B 1 84  ? 16.416  -3.276  -71.883 1.00 45.06 ?  86   ARG B NH1 1 
ATOM   3806 N  NH2 . ARG B 1 84  ? 16.751  -1.069  -72.443 1.00 39.42 ?  86   ARG B NH2 1 
ATOM   3807 N  N   . THR B 1 85  ? 10.986  -1.809  -68.746 1.00 23.48 ?  87   THR B N   1 
ATOM   3808 C  CA  . THR B 1 85  ? 10.019  -2.749  -68.193 1.00 25.22 ?  87   THR B CA  1 
ATOM   3809 C  C   . THR B 1 85  ? 8.692   -2.062  -67.889 1.00 31.01 ?  87   THR B C   1 
ATOM   3810 O  O   . THR B 1 85  ? 7.622   -2.631  -68.141 1.00 32.22 ?  87   THR B O   1 
ATOM   3811 C  CB  . THR B 1 85  ? 10.580  -3.410  -66.932 1.00 26.39 ?  87   THR B CB  1 
ATOM   3812 O  OG1 . THR B 1 85  ? 11.739  -4.183  -67.270 1.00 25.46 ?  87   THR B OG1 1 
ATOM   3813 C  CG2 . THR B 1 85  ? 9.530   -4.321  -66.285 1.00 23.22 ?  87   THR B CG2 1 
ATOM   3814 N  N   . LEU B 1 86  ? 8.737   -0.830  -67.367 1.00 28.02 ?  88   LEU B N   1 
ATOM   3815 C  CA  . LEU B 1 86  ? 7.501   -0.142  -67.004 1.00 26.90 ?  88   LEU B CA  1 
ATOM   3816 C  C   . LEU B 1 86  ? 6.677   0.208   -68.238 1.00 30.79 ?  88   LEU B C   1 
ATOM   3817 O  O   . LEU B 1 86  ? 5.458   0.006   -68.254 1.00 28.73 ?  88   LEU B O   1 
ATOM   3818 C  CB  . LEU B 1 86  ? 7.805   1.115   -66.189 1.00 26.78 ?  88   LEU B CB  1 
ATOM   3819 C  CG  . LEU B 1 86  ? 8.427   0.854   -64.814 1.00 23.85 ?  88   LEU B CG  1 
ATOM   3820 C  CD1 . LEU B 1 86  ? 8.331   2.096   -63.946 1.00 23.17 ?  88   LEU B CD1 1 
ATOM   3821 C  CD2 . LEU B 1 86  ? 7.768   -0.337  -64.142 1.00 23.19 ?  88   LEU B CD2 1 
ATOM   3822 N  N   . HIS B 1 87  ? 7.321   0.746   -69.279 1.00 26.23 ?  89   HIS B N   1 
ATOM   3823 C  CA  . HIS B 1 87  ? 6.584   1.055   -70.502 1.00 33.97 ?  89   HIS B CA  1 
ATOM   3824 C  C   . HIS B 1 87  ? 5.991   -0.196  -71.132 1.00 35.52 ?  89   HIS B C   1 
ATOM   3825 O  O   . HIS B 1 87  ? 4.903   -0.134  -71.719 1.00 31.34 ?  89   HIS B O   1 
ATOM   3826 C  CB  . HIS B 1 87  ? 7.475   1.782   -71.512 1.00 27.18 ?  89   HIS B CB  1 
ATOM   3827 C  CG  . HIS B 1 87  ? 8.050   3.066   -70.996 1.00 38.26 ?  89   HIS B CG  1 
ATOM   3828 N  ND1 . HIS B 1 87  ? 7.272   4.171   -70.716 1.00 41.25 ?  89   HIS B ND1 1 
ATOM   3829 C  CD2 . HIS B 1 87  ? 9.330   3.438   -70.756 1.00 39.02 ?  89   HIS B CD2 1 
ATOM   3830 C  CE1 . HIS B 1 87  ? 8.046   5.156   -70.294 1.00 44.37 ?  89   HIS B CE1 1 
ATOM   3831 N  NE2 . HIS B 1 87  ? 9.299   4.735   -70.306 1.00 43.04 ?  89   HIS B NE2 1 
ATOM   3832 N  N   . ALA B 1 88  ? 6.670   -1.341  -71.013 1.00 30.54 ?  90   ALA B N   1 
ATOM   3833 C  CA  . ALA B 1 88  ? 6.114   -2.573  -71.567 1.00 34.42 ?  90   ALA B CA  1 
ATOM   3834 C  C   . ALA B 1 88  ? 4.855   -3.010  -70.826 1.00 39.51 ?  90   ALA B C   1 
ATOM   3835 O  O   . ALA B 1 88  ? 3.998   -3.686  -71.408 1.00 34.76 ?  90   ALA B O   1 
ATOM   3836 C  CB  . ALA B 1 88  ? 7.160   -3.687  -71.544 1.00 30.01 ?  90   ALA B CB  1 
ATOM   3837 N  N   . ALA B 1 89  ? 4.718   -2.637  -69.554 1.00 35.61 ?  91   ALA B N   1 
ATOM   3838 C  CA  . ALA B 1 89  ? 3.520   -2.949  -68.784 1.00 35.68 ?  91   ALA B CA  1 
ATOM   3839 C  C   . ALA B 1 89  ? 2.373   -1.983  -69.055 1.00 36.05 ?  91   ALA B C   1 
ATOM   3840 O  O   . ALA B 1 89  ? 1.278   -2.178  -68.518 1.00 41.12 ?  91   ALA B O   1 
ATOM   3841 C  CB  . ALA B 1 89  ? 3.842   -2.953  -67.288 1.00 30.86 ?  91   ALA B CB  1 
ATOM   3842 N  N   . GLY B 1 90  ? 2.598   -0.948  -69.856 1.00 33.90 ?  92   GLY B N   1 
ATOM   3843 C  CA  . GLY B 1 90  ? 1.568   -0.001  -70.203 1.00 28.05 ?  92   GLY B CA  1 
ATOM   3844 C  C   . GLY B 1 90  ? 1.624   1.312   -69.463 1.00 39.00 ?  92   GLY B C   1 
ATOM   3845 O  O   . GLY B 1 90  ? 0.739   2.150   -69.663 1.00 40.68 ?  92   GLY B O   1 
ATOM   3846 N  N   . LEU B 1 91  ? 2.625   1.528   -68.613 1.00 37.33 ?  93   LEU B N   1 
ATOM   3847 C  CA  . LEU B 1 91  ? 2.716   2.799   -67.914 1.00 37.56 ?  93   LEU B CA  1 
ATOM   3848 C  C   . LEU B 1 91  ? 3.246   3.870   -68.854 1.00 35.05 ?  93   LEU B C   1 
ATOM   3849 O  O   . LEU B 1 91  ? 4.269   3.683   -69.521 1.00 37.96 ?  93   LEU B O   1 
ATOM   3850 C  CB  . LEU B 1 91  ? 3.590   2.699   -66.662 1.00 30.28 ?  93   LEU B CB  1 
ATOM   3851 C  CG  . LEU B 1 91  ? 3.022   1.886   -65.493 1.00 35.59 ?  93   LEU B CG  1 
ATOM   3852 C  CD1 . LEU B 1 91  ? 3.024   0.390   -65.762 1.00 35.82 ?  93   LEU B CD1 1 
ATOM   3853 C  CD2 . LEU B 1 91  ? 3.766   2.213   -64.203 1.00 37.61 ?  93   LEU B CD2 1 
ATOM   3854 N  N   . ALA B 1 92  ? 2.527   4.982   -68.919 1.00 37.56 ?  94   ALA B N   1 
ATOM   3855 C  CA  . ALA B 1 92  ? 2.965   6.124   -69.692 1.00 36.57 ?  94   ALA B CA  1 
ATOM   3856 C  C   . ALA B 1 92  ? 4.067   6.860   -68.943 1.00 39.49 ?  94   ALA B C   1 
ATOM   3857 O  O   . ALA B 1 92  ? 4.247   6.695   -67.735 1.00 38.27 ?  94   ALA B O   1 
ATOM   3858 C  CB  . ALA B 1 92  ? 1.794   7.068   -69.963 1.00 40.38 ?  94   ALA B CB  1 
ATOM   3859 N  N   . THR B 1 93  ? 4.806   7.684   -69.684 1.00 39.23 ?  95   THR B N   1 
ATOM   3860 C  CA  . THR B 1 93  ? 5.845   8.505   -69.072 1.00 38.39 ?  95   THR B CA  1 
ATOM   3861 C  C   . THR B 1 93  ? 5.293   9.358   -67.935 1.00 42.23 ?  95   THR B C   1 
ATOM   3862 O  O   . THR B 1 93  ? 5.919   9.470   -66.872 1.00 39.09 ?  95   THR B O   1 
ATOM   3863 C  CB  . THR B 1 93  ? 6.496   9.379   -70.142 1.00 36.92 ?  95   THR B CB  1 
ATOM   3864 O  OG1 . THR B 1 93  ? 7.120   8.534   -71.115 1.00 45.30 ?  95   THR B OG1 1 
ATOM   3865 C  CG2 . THR B 1 93  ? 7.531   10.305  -69.535 1.00 39.06 ?  95   THR B CG2 1 
ATOM   3866 N  N   . GLN B 1 94  ? 4.112   9.951   -68.130 1.00 31.14 ?  96   GLN B N   1 
ATOM   3867 C  CA  . GLN B 1 94  ? 3.524   10.818  -67.115 1.00 30.61 ?  96   GLN B CA  1 
ATOM   3868 C  C   . GLN B 1 94  ? 3.044   10.054  -65.888 1.00 27.98 ?  96   GLN B C   1 
ATOM   3869 O  O   . GLN B 1 94  ? 2.757   10.684  -64.865 1.00 33.34 ?  96   GLN B O   1 
ATOM   3870 C  CB  . GLN B 1 94  ? 2.359   11.619  -67.713 1.00 41.21 ?  96   GLN B CB  1 
ATOM   3871 N  N   . ASP B 1 95  ? 2.936   8.729   -65.962 1.00 25.09 ?  97   ASP B N   1 
ATOM   3872 C  CA  . ASP B 1 95  ? 2.585   7.915   -64.807 1.00 33.50 ?  97   ASP B CA  1 
ATOM   3873 C  C   . ASP B 1 95  ? 3.797   7.546   -63.962 1.00 28.76 ?  97   ASP B C   1 
ATOM   3874 O  O   . ASP B 1 95  ? 3.638   6.837   -62.966 1.00 30.76 ?  97   ASP B O   1 
ATOM   3875 C  CB  . ASP B 1 95  ? 1.871   6.632   -65.250 1.00 32.43 ?  97   ASP B CB  1 
ATOM   3876 C  CG  . ASP B 1 95  ? 0.684   6.902   -66.176 1.00 46.71 ?  97   ASP B CG  1 
ATOM   3877 O  OD1 . ASP B 1 95  ? 0.242   5.959   -66.873 1.00 44.53 ?  97   ASP B OD1 1 
ATOM   3878 O  OD2 . ASP B 1 95  ? 0.174   8.044   -66.181 1.00 41.59 ?  97   ASP B OD2 1 
ATOM   3879 N  N   . ILE B 1 96  ? 4.992   8.005   -64.337 1.00 27.47 ?  98   ILE B N   1 
ATOM   3880 C  CA  . ILE B 1 96  ? 6.244   7.593   -63.700 1.00 27.79 ?  98   ILE B CA  1 
ATOM   3881 C  C   . ILE B 1 96  ? 6.913   8.818   -63.089 1.00 24.87 ?  98   ILE B C   1 
ATOM   3882 O  O   . ILE B 1 96  ? 7.163   9.808   -63.789 1.00 28.18 ?  98   ILE B O   1 
ATOM   3883 C  CB  . ILE B 1 96  ? 7.195   6.909   -64.694 1.00 28.49 ?  98   ILE B CB  1 
ATOM   3884 C  CG1 . ILE B 1 96  ? 6.580   5.623   -65.244 1.00 27.28 ?  98   ILE B CG1 1 
ATOM   3885 C  CG2 . ILE B 1 96  ? 8.550   6.611   -64.028 1.00 27.69 ?  98   ILE B CG2 1 
ATOM   3886 C  CD1 . ILE B 1 96  ? 7.185   5.196   -66.563 1.00 27.77 ?  98   ILE B CD1 1 
ATOM   3887 N  N   . LEU B 1 97  ? 7.225   8.741   -61.793 1.00 24.21 ?  99   LEU B N   1 
ATOM   3888 C  CA  . LEU B 1 97  ? 7.987   9.773   -61.101 1.00 18.71 ?  99   LEU B CA  1 
ATOM   3889 C  C   . LEU B 1 97  ? 9.313   9.198   -60.620 1.00 18.17 ?  99   LEU B C   1 
ATOM   3890 O  O   . LEU B 1 97  ? 9.333   8.157   -59.959 1.00 18.27 ?  99   LEU B O   1 
ATOM   3891 C  CB  . LEU B 1 97  ? 7.226   10.334  -59.895 1.00 22.21 ?  99   LEU B CB  1 
ATOM   3892 C  CG  . LEU B 1 97  ? 8.063   11.262  -59.004 1.00 20.69 ?  99   LEU B CG  1 
ATOM   3893 C  CD1 . LEU B 1 97  ? 8.477   12.508  -59.757 1.00 18.24 ?  99   LEU B CD1 1 
ATOM   3894 C  CD2 . LEU B 1 97  ? 7.336   11.629  -57.696 1.00 22.47 ?  99   LEU B CD2 1 
ATOM   3895 N  N   . ILE B 1 98  ? 10.402  9.886   -60.929 1.00 14.95 ?  100  ILE B N   1 
ATOM   3896 C  CA  . ILE B 1 98  ? 11.710  9.589   -60.341 1.00 13.99 ?  100  ILE B CA  1 
ATOM   3897 C  C   . ILE B 1 98  ? 11.891  10.554  -59.179 1.00 14.51 ?  100  ILE B C   1 
ATOM   3898 O  O   . ILE B 1 98  ? 11.975  11.769  -59.380 1.00 17.57 ?  100  ILE B O   1 
ATOM   3899 C  CB  . ILE B 1 98  ? 12.841  9.721   -61.368 1.00 15.74 ?  100  ILE B CB  1 
ATOM   3900 C  CG1 . ILE B 1 98  ? 12.634  8.719   -62.506 1.00 20.02 ?  100  ILE B CG1 1 
ATOM   3901 C  CG2 . ILE B 1 98  ? 14.234  9.526   -60.669 1.00 16.79 ?  100  ILE B CG2 1 
ATOM   3902 C  CD1 . ILE B 1 98  ? 13.751  8.668   -63.531 1.00 23.40 ?  100  ILE B CD1 1 
ATOM   3903 N  N   . LEU B 1 99  ? 11.962  10.025  -57.961 1.00 19.14 ?  101  LEU B N   1 
ATOM   3904 C  CA  . LEU B 1 99  ? 12.048  10.833  -56.747 1.00 19.69 ?  101  LEU B CA  1 
ATOM   3905 C  C   . LEU B 1 99  ? 13.445  10.706  -56.139 1.00 16.21 ?  101  LEU B C   1 
ATOM   3906 O  O   . LEU B 1 99  ? 13.840  9.616   -55.721 1.00 17.98 ?  101  LEU B O   1 
ATOM   3907 C  CB  . LEU B 1 99  ? 10.991  10.397  -55.743 1.00 16.61 ?  101  LEU B CB  1 
ATOM   3908 C  CG  . LEU B 1 99  ? 10.844  11.316  -54.538 1.00 18.77 ?  101  LEU B CG  1 
ATOM   3909 C  CD1 . LEU B 1 99  ? 10.533  12.720  -54.969 1.00 23.38 ?  101  LEU B CD1 1 
ATOM   3910 C  CD2 . LEU B 1 99  ? 9.774   10.785  -53.596 1.00 20.29 ?  101  LEU B CD2 1 
ATOM   3911 N  N   . VAL B 1 100 ? 14.173  11.819  -56.082 1.00 15.22 ?  102  VAL B N   1 
ATOM   3912 C  CA  . VAL B 1 100 ? 15.520  11.849  -55.508 1.00 14.12 ?  102  VAL B CA  1 
ATOM   3913 C  C   . VAL B 1 100 ? 15.401  11.773  -53.988 1.00 16.52 ?  102  VAL B C   1 
ATOM   3914 O  O   . VAL B 1 100 ? 14.879  12.693  -53.351 1.00 19.64 ?  102  VAL B O   1 
ATOM   3915 C  CB  . VAL B 1 100 ? 16.288  13.103  -55.941 1.00 17.80 ?  102  VAL B CB  1 
ATOM   3916 C  CG1 . VAL B 1 100 ? 17.710  13.104  -55.333 1.00 14.92 ?  102  VAL B CG1 1 
ATOM   3917 C  CG2 . VAL B 1 100 ? 16.378  13.184  -57.457 1.00 12.67 ?  102  VAL B CG2 1 
ATOM   3918 N  N   . ALA B 1 101 ? 15.916  10.691  -53.401 1.00 15.04 ?  103  ALA B N   1 
ATOM   3919 C  CA  . ALA B 1 101 ? 15.766  10.423  -51.971 1.00 14.24 ?  103  ALA B CA  1 
ATOM   3920 C  C   . ALA B 1 101 ? 16.890  11.125  -51.204 1.00 15.31 ?  103  ALA B C   1 
ATOM   3921 O  O   . ALA B 1 101 ? 17.877  10.528  -50.769 1.00 16.62 ?  103  ALA B O   1 
ATOM   3922 C  CB  . ALA B 1 101 ? 15.740  8.923   -51.708 1.00 14.02 ?  103  ALA B CB  1 
ATOM   3923 N  N   . THR B 1 102 ? 16.717  12.436  -51.033 1.00 15.08 ?  104  THR B N   1 
ATOM   3924 C  CA  . THR B 1 102 ? 17.723  13.290  -50.409 1.00 16.19 ?  104  THR B CA  1 
ATOM   3925 C  C   . THR B 1 102 ? 17.882  13.049  -48.912 1.00 19.89 ?  104  THR B C   1 
ATOM   3926 O  O   . THR B 1 102 ? 18.873  13.504  -48.333 1.00 15.38 ?  104  THR B O   1 
ATOM   3927 C  CB  . THR B 1 102 ? 17.340  14.751  -50.609 1.00 20.12 ?  104  THR B CB  1 
ATOM   3928 O  OG1 . THR B 1 102 ? 15.979  14.905  -50.189 1.00 17.53 ?  104  THR B OG1 1 
ATOM   3929 C  CG2 . THR B 1 102 ? 17.471  15.157  -52.080 1.00 21.50 ?  104  THR B CG2 1 
ATOM   3930 N  N   . GLY B 1 103 ? 16.929  12.393  -48.271 1.00 16.74 ?  105  GLY B N   1 
ATOM   3931 C  CA  . GLY B 1 103 ? 16.906  12.399  -46.819 1.00 16.08 ?  105  GLY B CA  1 
ATOM   3932 C  C   . GLY B 1 103 ? 16.675  13.821  -46.362 1.00 20.06 ?  105  GLY B C   1 
ATOM   3933 O  O   . GLY B 1 103 ? 15.687  14.459  -46.744 1.00 18.56 ?  105  GLY B O   1 
ATOM   3934 N  N   . LEU B 1 104 ? 17.596  14.345  -45.553 1.00 16.46 ?  106  LEU B N   1 
ATOM   3935 C  CA  . LEU B 1 104 ? 17.581  15.747  -45.164 1.00 15.52 ?  106  LEU B CA  1 
ATOM   3936 C  C   . LEU B 1 104 ? 18.638  16.577  -45.884 1.00 18.51 ?  106  LEU B C   1 
ATOM   3937 O  O   . LEU B 1 104 ? 18.811  17.753  -45.552 1.00 19.79 ?  106  LEU B O   1 
ATOM   3938 C  CB  . LEU B 1 104 ? 17.731  15.883  -43.647 1.00 22.43 ?  106  LEU B CB  1 
ATOM   3939 C  CG  . LEU B 1 104 ? 16.424  16.007  -42.859 1.00 22.91 ?  106  LEU B CG  1 
ATOM   3940 C  CD1 . LEU B 1 104 ? 15.708  17.311  -43.200 1.00 23.79 ?  106  LEU B CD1 1 
ATOM   3941 C  CD2 . LEU B 1 104 ? 15.494  14.820  -43.082 1.00 22.04 ?  106  LEU B CD2 1 
ATOM   3942 N  N   . HIS B 1 105 ? 19.325  16.014  -46.883 1.00 14.82 ?  107  HIS B N   1 
ATOM   3943 C  CA  . HIS B 1 105 ? 20.283  16.787  -47.664 1.00 14.32 ?  107  HIS B CA  1 
ATOM   3944 C  C   . HIS B 1 105 ? 19.570  17.865  -48.485 1.00 17.30 ?  107  HIS B C   1 
ATOM   3945 O  O   . HIS B 1 105 ? 18.360  17.805  -48.721 1.00 20.59 ?  107  HIS B O   1 
ATOM   3946 C  CB  . HIS B 1 105 ? 21.063  15.889  -48.641 1.00 13.20 ?  107  HIS B CB  1 
ATOM   3947 C  CG  . HIS B 1 105 ? 21.790  14.743  -47.997 1.00 15.46 ?  107  HIS B CG  1 
ATOM   3948 N  ND1 . HIS B 1 105 ? 22.277  13.673  -48.722 1.00 13.56 ?  107  HIS B ND1 1 
ATOM   3949 C  CD2 . HIS B 1 105 ? 22.149  14.519  -46.709 1.00 17.80 ?  107  HIS B CD2 1 
ATOM   3950 C  CE1 . HIS B 1 105 ? 22.880  12.826  -47.901 1.00 13.25 ?  107  HIS B CE1 1 
ATOM   3951 N  NE2 . HIS B 1 105 ? 22.813  13.314  -46.676 1.00 13.12 ?  107  HIS B NE2 1 
ATOM   3952 N  N   . ARG B 1 106 ? 20.357  18.823  -48.987 1.00 18.10 ?  108  ARG B N   1 
ATOM   3953 C  CA  . ARG B 1 106 ? 19.833  19.813  -49.932 1.00 24.13 ?  108  ARG B CA  1 
ATOM   3954 C  C   . ARG B 1 106 ? 19.327  19.115  -51.194 1.00 20.89 ?  108  ARG B C   1 
ATOM   3955 O  O   . ARG B 1 106 ? 19.757  18.000  -51.510 1.00 16.62 ?  108  ARG B O   1 
ATOM   3956 C  CB  . ARG B 1 106 ? 20.924  20.816  -50.303 1.00 22.95 ?  108  ARG B CB  1 
ATOM   3957 C  CG  . ARG B 1 106 ? 22.179  20.155  -50.858 1.00 15.77 ?  108  ARG B CG  1 
ATOM   3958 C  CD  . ARG B 1 106 ? 23.068  21.147  -51.578 1.00 24.63 ?  108  ARG B CD  1 
ATOM   3959 N  NE  . ARG B 1 106 ? 24.262  20.524  -52.140 1.00 24.96 ?  108  ARG B NE  1 
ATOM   3960 C  CZ  . ARG B 1 106 ? 24.293  19.846  -53.286 1.00 24.23 ?  108  ARG B CZ  1 
ATOM   3961 N  NH1 . ARG B 1 106 ? 23.184  19.672  -53.997 1.00 29.26 ?  108  ARG B NH1 1 
ATOM   3962 N  NH2 . ARG B 1 106 ? 25.432  19.327  -53.717 1.00 25.05 ?  108  ARG B NH2 1 
ATOM   3963 N  N   . PRO B 1 107 ? 18.422  19.751  -51.942 1.00 22.84 ?  109  PRO B N   1 
ATOM   3964 C  CA  . PRO B 1 107 ? 17.976  19.154  -53.204 1.00 21.24 ?  109  PRO B CA  1 
ATOM   3965 C  C   . PRO B 1 107 ? 19.108  19.108  -54.215 1.00 23.82 ?  109  PRO B C   1 
ATOM   3966 O  O   . PRO B 1 107 ? 20.070  19.884  -54.165 1.00 19.13 ?  109  PRO B O   1 
ATOM   3967 C  CB  . PRO B 1 107 ? 16.852  20.087  -53.671 1.00 20.08 ?  109  PRO B CB  1 
ATOM   3968 C  CG  . PRO B 1 107 ? 17.167  21.386  -53.038 1.00 23.35 ?  109  PRO B CG  1 
ATOM   3969 C  CD  . PRO B 1 107 ? 17.756  21.042  -51.689 1.00 21.99 ?  109  PRO B CD  1 
ATOM   3970 N  N   . SER B 1 108 ? 18.993  18.159  -55.135 1.00 17.50 ?  110  SER B N   1 
ATOM   3971 C  CA  . SER B 1 108 ? 19.951  18.073  -56.220 1.00 18.78 ?  110  SER B CA  1 
ATOM   3972 C  C   . SER B 1 108 ? 19.736  19.229  -57.189 1.00 26.50 ?  110  SER B C   1 
ATOM   3973 O  O   . SER B 1 108 ? 18.610  19.693  -57.398 1.00 27.00 ?  110  SER B O   1 
ATOM   3974 C  CB  . SER B 1 108 ? 19.819  16.734  -56.946 1.00 22.26 ?  110  SER B CB  1 
ATOM   3975 O  OG  . SER B 1 108 ? 18.520  16.579  -57.500 1.00 22.70 ?  110  SER B OG  1 
ATOM   3976 N  N   . THR B 1 109 ? 20.833  19.708  -57.761 1.00 25.83 ?  111  THR B N   1 
ATOM   3977 C  CA  . THR B 1 109 ? 20.775  20.720  -58.802 1.00 27.08 ?  111  THR B CA  1 
ATOM   3978 C  C   . THR B 1 109 ? 20.410  20.085  -60.143 1.00 29.27 ?  111  THR B C   1 
ATOM   3979 O  O   . THR B 1 109 ? 20.448  18.861  -60.293 1.00 23.71 ?  111  THR B O   1 
ATOM   3980 C  CB  . THR B 1 109 ? 22.112  21.455  -58.886 1.00 29.38 ?  111  THR B CB  1 
ATOM   3981 O  OG1 . THR B 1 109 ? 23.124  20.584  -59.414 1.00 26.07 ?  111  THR B OG1 1 
ATOM   3982 C  CG2 . THR B 1 109 ? 22.533  21.944  -57.507 1.00 29.35 ?  111  THR B CG2 1 
ATOM   3983 N  N   . PRO B 1 110 ? 19.989  20.894  -61.124 1.00 30.53 ?  112  PRO B N   1 
ATOM   3984 C  CA  . PRO B 1 110 ? 19.751  20.328  -62.465 1.00 24.74 ?  112  PRO B CA  1 
ATOM   3985 C  C   . PRO B 1 110 ? 20.987  19.682  -63.071 1.00 27.42 ?  112  PRO B C   1 
ATOM   3986 O  O   . PRO B 1 110 ? 20.886  18.605  -63.674 1.00 28.64 ?  112  PRO B O   1 
ATOM   3987 C  CB  . PRO B 1 110 ? 19.285  21.551  -63.269 1.00 29.71 ?  112  PRO B CB  1 
ATOM   3988 C  CG  . PRO B 1 110 ? 18.609  22.416  -62.235 1.00 24.73 ?  112  PRO B CG  1 
ATOM   3989 C  CD  . PRO B 1 110 ? 19.496  22.283  -61.019 1.00 27.74 ?  112  PRO B CD  1 
ATOM   3990 N  N   . ALA B 1 111 ? 22.157  20.309  -62.921 1.00 24.77 ?  113  ALA B N   1 
ATOM   3991 C  CA  . ALA B 1 111 ? 23.395  19.701  -63.406 1.00 29.28 ?  113  ALA B CA  1 
ATOM   3992 C  C   . ALA B 1 111 ? 23.702  18.394  -62.683 1.00 27.41 ?  113  ALA B C   1 
ATOM   3993 O  O   . ALA B 1 111 ? 24.228  17.454  -63.290 1.00 29.14 ?  113  ALA B O   1 
ATOM   3994 C  CB  . ALA B 1 111 ? 24.563  20.675  -63.247 1.00 30.12 ?  113  ALA B CB  1 
ATOM   3995 N  N   . GLU B 1 112 ? 23.402  18.319  -61.382 1.00 25.65 ?  114  GLU B N   1 
ATOM   3996 C  CA  . GLU B 1 112 ? 23.575  17.055  -60.668 1.00 25.59 ?  114  GLU B CA  1 
ATOM   3997 C  C   . GLU B 1 112 ? 22.618  15.989  -61.190 1.00 27.59 ?  114  GLU B C   1 
ATOM   3998 O  O   . GLU B 1 112 ? 23.000  14.823  -61.328 1.00 22.92 ?  114  GLU B O   1 
ATOM   3999 C  CB  . GLU B 1 112 ? 23.379  17.254  -59.164 1.00 25.39 ?  114  GLU B CB  1 
ATOM   4000 C  CG  . GLU B 1 112 ? 24.634  17.777  -58.468 1.00 29.43 ?  114  GLU B CG  1 
ATOM   4001 C  CD  . GLU B 1 112 ? 24.388  18.284  -57.054 1.00 30.10 ?  114  GLU B CD  1 
ATOM   4002 O  OE1 . GLU B 1 112 ? 23.217  18.319  -56.604 1.00 23.10 ?  114  GLU B OE1 1 
ATOM   4003 O  OE2 . GLU B 1 112 ? 25.386  18.643  -56.389 1.00 24.98 ?  114  GLU B OE2 1 
ATOM   4004 N  N   . LYS B 1 113 ? 21.368  16.363  -61.482 1.00 24.76 ?  115  LYS B N   1 
ATOM   4005 C  CA  . LYS B 1 113 ? 20.421  15.390  -62.018 1.00 22.05 ?  115  LYS B CA  1 
ATOM   4006 C  C   . LYS B 1 113 ? 20.943  14.764  -63.301 1.00 21.89 ?  115  LYS B C   1 
ATOM   4007 O  O   . LYS B 1 113 ? 20.765  13.563  -63.528 1.00 23.31 ?  115  LYS B O   1 
ATOM   4008 C  CB  . LYS B 1 113 ? 19.061  16.052  -62.248 1.00 23.09 ?  115  LYS B CB  1 
ATOM   4009 C  CG  . LYS B 1 113 ? 18.272  16.264  -60.963 1.00 21.04 ?  115  LYS B CG  1 
ATOM   4010 C  CD  . LYS B 1 113 ? 16.920  16.927  -61.243 1.00 17.86 ?  115  LYS B CD  1 
ATOM   4011 C  CE  . LYS B 1 113 ? 16.177  17.230  -59.941 1.00 25.45 ?  115  LYS B CE  1 
ATOM   4012 N  NZ  . LYS B 1 113 ? 16.881  18.292  -59.147 1.00 20.26 ?  115  LYS B NZ  1 
ATOM   4013 N  N   . VAL B 1 114 ? 21.612  15.552  -64.142 1.00 26.35 ?  116  VAL B N   1 
ATOM   4014 C  CA  . VAL B 1 114 ? 22.164  15.005  -65.381 1.00 26.94 ?  116  VAL B CA  1 
ATOM   4015 C  C   . VAL B 1 114 ? 23.322  14.057  -65.075 1.00 28.50 ?  116  VAL B C   1 
ATOM   4016 O  O   . VAL B 1 114 ? 23.361  12.927  -65.575 1.00 29.61 ?  116  VAL B O   1 
ATOM   4017 C  CB  . VAL B 1 114 ? 22.589  16.139  -66.334 1.00 32.33 ?  116  VAL B CB  1 
ATOM   4018 C  CG1 . VAL B 1 114 ? 23.349  15.577  -67.532 1.00 36.90 ?  116  VAL B CG1 1 
ATOM   4019 C  CG2 . VAL B 1 114 ? 21.369  16.945  -66.800 1.00 26.39 ?  116  VAL B CG2 1 
ATOM   4020 N  N   . GLU B 1 115 ? 24.278  14.505  -64.247 1.00 30.37 ?  117  GLU B N   1 
ATOM   4021 C  CA  . GLU B 1 115 ? 25.386  13.644  -63.821 1.00 30.80 ?  117  GLU B CA  1 
ATOM   4022 C  C   . GLU B 1 115 ? 24.875  12.355  -63.186 1.00 25.79 ?  117  GLU B C   1 
ATOM   4023 O  O   . GLU B 1 115 ? 25.450  11.279  -63.381 1.00 31.43 ?  117  GLU B O   1 
ATOM   4024 C  CB  . GLU B 1 115 ? 26.293  14.405  -62.841 1.00 30.03 ?  117  GLU B CB  1 
ATOM   4025 C  CG  . GLU B 1 115 ? 27.284  13.526  -62.038 1.00 29.44 ?  117  GLU B CG  1 
ATOM   4026 C  CD  . GLU B 1 115 ? 28.165  14.322  -61.062 1.00 43.31 ?  117  GLU B CD  1 
ATOM   4027 O  OE1 . GLU B 1 115 ? 28.990  13.708  -60.334 1.00 35.89 ?  117  GLU B OE1 1 
ATOM   4028 O  OE2 . GLU B 1 115 ? 28.053  15.567  -61.029 1.00 38.16 ?  117  GLU B OE2 1 
ATOM   4029 N  N   . MET B 1 116 ? 23.778  12.454  -62.447 1.00 20.24 ?  118  MET B N   1 
ATOM   4030 C  CA  . MET B 1 116 ? 23.173  11.358  -61.700 1.00 25.22 ?  118  MET B CA  1 
ATOM   4031 C  C   . MET B 1 116 ? 22.416  10.395  -62.611 1.00 26.84 ?  118  MET B C   1 
ATOM   4032 O  O   . MET B 1 116 ? 22.562  9.171   -62.497 1.00 20.57 ?  118  MET B O   1 
ATOM   4033 C  CB  . MET B 1 116 ? 22.241  11.997  -60.675 1.00 27.37 ?  118  MET B CB  1 
ATOM   4034 C  CG  . MET B 1 116 ? 22.804  12.255  -59.299 1.00 23.76 ?  118  MET B CG  1 
ATOM   4035 S  SD  . MET B 1 116 ? 21.557  13.187  -58.373 1.00 29.20 ?  118  MET B SD  1 
ATOM   4036 C  CE  . MET B 1 116 ? 20.179  12.050  -58.315 1.00 25.86 ?  118  MET B CE  1 
ATOM   4037 N  N   . LEU B 1 117 ? 21.621  10.925  -63.539 1.00 22.27 ?  119  LEU B N   1 
ATOM   4038 C  CA  . LEU B 1 117 ? 20.607  10.131  -64.213 1.00 23.93 ?  119  LEU B CA  1 
ATOM   4039 C  C   . LEU B 1 117 ? 20.814  9.970   -65.709 1.00 22.49 ?  119  LEU B C   1 
ATOM   4040 O  O   . LEU B 1 117 ? 20.056  9.211   -66.325 1.00 24.81 ?  119  LEU B O   1 
ATOM   4041 C  CB  . LEU B 1 117 ? 19.219  10.753  -63.991 1.00 25.85 ?  119  LEU B CB  1 
ATOM   4042 C  CG  . LEU B 1 117 ? 18.746  10.905  -62.549 1.00 26.05 ?  119  LEU B CG  1 
ATOM   4043 C  CD1 . LEU B 1 117 ? 17.407  11.600  -62.523 1.00 22.16 ?  119  LEU B CD1 1 
ATOM   4044 C  CD2 . LEU B 1 117 ? 18.654  9.550   -61.898 1.00 23.23 ?  119  LEU B CD2 1 
ATOM   4045 N  N   . SER B 1 118 ? 21.805  10.652  -66.295 1.00 20.71 ?  120  SER B N   1 
ATOM   4046 C  CA  . SER B 1 118 ? 22.030  10.815  -67.735 1.00 31.26 ?  120  SER B CA  1 
ATOM   4047 C  C   . SER B 1 118 ? 21.120  11.906  -68.289 1.00 29.91 ?  120  SER B C   1 
ATOM   4048 O  O   . SER B 1 118 ? 20.014  12.119  -67.784 1.00 25.63 ?  120  SER B O   1 
ATOM   4049 C  CB  . SER B 1 118 ? 21.837  9.506   -68.517 1.00 24.57 ?  120  SER B CB  1 
ATOM   4050 O  OG  . SER B 1 118 ? 20.473  9.284   -68.853 1.00 28.47 ?  120  SER B OG  1 
ATOM   4051 N  N   . GLU B 1 119 ? 21.597  12.612  -69.316 1.00 28.25 ?  121  GLU B N   1 
ATOM   4052 C  CA  . GLU B 1 119 ? 20.816  13.688  -69.912 1.00 26.14 ?  121  GLU B CA  1 
ATOM   4053 C  C   . GLU B 1 119 ? 19.507  13.171  -70.496 1.00 30.13 ?  121  GLU B C   1 
ATOM   4054 O  O   . GLU B 1 119 ? 18.454  13.788  -70.304 1.00 34.76 ?  121  GLU B O   1 
ATOM   4055 C  CB  . GLU B 1 119 ? 21.636  14.397  -70.987 1.00 34.24 ?  121  GLU B CB  1 
ATOM   4056 C  CG  . GLU B 1 119 ? 21.004  15.680  -71.491 1.00 42.56 ?  121  GLU B CG  1 
ATOM   4057 C  CD  . GLU B 1 119 ? 22.032  16.681  -71.980 1.00 60.30 ?  121  GLU B CD  1 
ATOM   4058 O  OE1 . GLU B 1 119 ? 22.225  16.785  -73.211 1.00 64.98 ?  121  GLU B OE1 1 
ATOM   4059 O  OE2 . GLU B 1 119 ? 22.646  17.367  -71.135 1.00 66.73 ?  121  GLU B OE2 1 
ATOM   4060 N  N   . GLU B 1 120 ? 19.554  12.040  -71.207 1.00 31.23 ?  122  GLU B N   1 
ATOM   4061 C  CA  . GLU B 1 120 ? 18.356  11.522  -71.864 1.00 31.56 ?  122  GLU B CA  1 
ATOM   4062 C  C   . GLU B 1 120 ? 17.250  11.229  -70.860 1.00 31.27 ?  122  GLU B C   1 
ATOM   4063 O  O   . GLU B 1 120 ? 16.070  11.465  -71.141 1.00 33.62 ?  122  GLU B O   1 
ATOM   4064 C  CB  . GLU B 1 120 ? 18.697  10.262  -72.664 1.00 34.60 ?  122  GLU B CB  1 
ATOM   4065 N  N   . ILE B 1 121 ? 17.607  10.723  -69.679 1.00 27.62 ?  123  ILE B N   1 
ATOM   4066 C  CA  . ILE B 1 121 ? 16.590  10.438  -68.675 1.00 27.17 ?  123  ILE B CA  1 
ATOM   4067 C  C   . ILE B 1 121 ? 16.176  11.713  -67.944 1.00 29.19 ?  123  ILE B C   1 
ATOM   4068 O  O   . ILE B 1 121 ? 14.984  11.932  -67.690 1.00 26.79 ?  123  ILE B O   1 
ATOM   4069 C  CB  . ILE B 1 121 ? 17.090  9.348   -67.708 1.00 26.11 ?  123  ILE B CB  1 
ATOM   4070 C  CG1 . ILE B 1 121 ? 17.223  8.012   -68.454 1.00 25.09 ?  123  ILE B CG1 1 
ATOM   4071 C  CG2 . ILE B 1 121 ? 16.133  9.203   -66.528 1.00 23.05 ?  123  ILE B CG2 1 
ATOM   4072 C  CD1 . ILE B 1 121 ? 17.604  6.828   -67.583 1.00 29.90 ?  123  ILE B CD1 1 
ATOM   4073 N  N   . ALA B 1 122 ? 17.137  12.584  -67.608 1.00 28.40 ?  124  ALA B N   1 
ATOM   4074 C  CA  . ALA B 1 122 ? 16.791  13.810  -66.891 1.00 25.68 ?  124  ALA B CA  1 
ATOM   4075 C  C   . ALA B 1 122 ? 15.852  14.688  -67.712 1.00 27.30 ?  124  ALA B C   1 
ATOM   4076 O  O   . ALA B 1 122 ? 14.973  15.353  -67.153 1.00 30.43 ?  124  ALA B O   1 
ATOM   4077 C  CB  . ALA B 1 122 ? 18.051  14.589  -66.514 1.00 27.85 ?  124  ALA B CB  1 
ATOM   4078 N  N   . ARG B 1 123 ? 16.016  14.695  -69.039 1.00 27.34 ?  125  ARG B N   1 
ATOM   4079 C  CA  . ARG B 1 123 ? 15.178  15.522  -69.907 1.00 35.07 ?  125  ARG B CA  1 
ATOM   4080 C  C   . ARG B 1 123 ? 13.817  14.905  -70.200 1.00 34.85 ?  125  ARG B C   1 
ATOM   4081 O  O   . ARG B 1 123 ? 12.879  15.641  -70.524 1.00 40.58 ?  125  ARG B O   1 
ATOM   4082 C  CB  . ARG B 1 123 ? 15.891  15.798  -71.236 1.00 31.13 ?  125  ARG B CB  1 
ATOM   4083 N  N   . THR B 1 124 ? 13.681  13.583  -70.100 1.00 30.71 ?  126  THR B N   1 
ATOM   4084 C  CA  . THR B 1 124 ? 12.497  12.889  -70.596 1.00 31.29 ?  126  THR B CA  1 
ATOM   4085 C  C   . THR B 1 124 ? 11.467  12.604  -69.511 1.00 35.82 ?  126  THR B C   1 
ATOM   4086 O  O   . THR B 1 124 ? 10.261  12.667  -69.778 1.00 27.87 ?  126  THR B O   1 
ATOM   4087 C  CB  . THR B 1 124 ? 12.909  11.572  -71.267 1.00 26.61 ?  126  THR B CB  1 
ATOM   4088 O  OG1 . THR B 1 124 ? 13.603  11.858  -72.484 1.00 39.53 ?  126  THR B OG1 1 
ATOM   4089 C  CG2 . THR B 1 124 ? 11.696  10.723  -71.610 1.00 35.24 ?  126  THR B CG2 1 
ATOM   4090 N  N   . TYR B 1 125 ? 11.904  12.294  -68.291 1.00 24.67 ?  127  TYR B N   1 
ATOM   4091 C  CA  . TYR B 1 125 ? 10.996  11.869  -67.237 1.00 26.54 ?  127  TYR B CA  1 
ATOM   4092 C  C   . TYR B 1 125 ? 10.857  12.953  -66.179 1.00 21.77 ?  127  TYR B C   1 
ATOM   4093 O  O   . TYR B 1 125 ? 11.686  13.861  -66.070 1.00 26.21 ?  127  TYR B O   1 
ATOM   4094 C  CB  . TYR B 1 125 ? 11.464  10.559  -66.583 1.00 25.56 ?  127  TYR B CB  1 
ATOM   4095 C  CG  . TYR B 1 125 ? 11.440  9.379   -67.522 1.00 23.51 ?  127  TYR B CG  1 
ATOM   4096 C  CD1 . TYR B 1 125 ? 12.402  9.232   -68.513 1.00 27.96 ?  127  TYR B CD1 1 
ATOM   4097 C  CD2 . TYR B 1 125 ? 10.409  8.448   -67.469 1.00 32.05 ?  127  TYR B CD2 1 
ATOM   4098 C  CE1 . TYR B 1 125 ? 12.363  8.164   -69.394 1.00 30.27 ?  127  TYR B CE1 1 
ATOM   4099 C  CE2 . TYR B 1 125 ? 10.363  7.375   -68.345 1.00 27.02 ?  127  TYR B CE2 1 
ATOM   4100 C  CZ  . TYR B 1 125 ? 11.342  7.243   -69.306 1.00 28.66 ?  127  TYR B CZ  1 
ATOM   4101 O  OH  . TYR B 1 125 ? 11.306  6.182   -70.172 1.00 30.23 ?  127  TYR B OH  1 
ATOM   4102 N  N   . ARG B 1 126 ? 9.792   12.842  -65.392 1.00 23.70 ?  128  ARG B N   1 
ATOM   4103 C  CA  . ARG B 1 126 ? 9.591   13.772  -64.290 1.00 20.70 ?  128  ARG B CA  1 
ATOM   4104 C  C   . ARG B 1 126 ? 10.527  13.392  -63.144 1.00 20.25 ?  128  ARG B C   1 
ATOM   4105 O  O   . ARG B 1 126 ? 10.488  12.260  -62.655 1.00 22.82 ?  128  ARG B O   1 
ATOM   4106 C  CB  . ARG B 1 126 ? 8.131   13.766  -63.839 1.00 28.82 ?  128  ARG B CB  1 
ATOM   4107 C  CG  . ARG B 1 126 ? 7.837   14.707  -62.669 1.00 34.70 ?  128  ARG B CG  1 
ATOM   4108 C  CD  . ARG B 1 126 ? 6.353   15.104  -62.588 1.00 41.00 ?  128  ARG B CD  1 
ATOM   4109 N  NE  . ARG B 1 126 ? 5.527   14.251  -61.733 1.00 40.49 ?  128  ARG B NE  1 
ATOM   4110 C  CZ  . ARG B 1 126 ? 4.876   13.171  -62.155 1.00 37.83 ?  128  ARG B CZ  1 
ATOM   4111 N  NH1 . ARG B 1 126 ? 4.965   12.795  -63.422 1.00 39.97 ?  128  ARG B NH1 1 
ATOM   4112 N  NH2 . ARG B 1 126 ? 4.137   12.462  -61.307 1.00 37.13 ?  128  ARG B NH2 1 
ATOM   4113 N  N   . VAL B 1 127 ? 11.378  14.329  -62.739 1.00 18.93 ?  129  VAL B N   1 
ATOM   4114 C  CA  . VAL B 1 127 ? 12.385  14.108  -61.699 1.00 20.71 ?  129  VAL B CA  1 
ATOM   4115 C  C   . VAL B 1 127 ? 12.225  15.199  -60.650 1.00 22.82 ?  129  VAL B C   1 
ATOM   4116 O  O   . VAL B 1 127 ? 12.500  16.373  -60.928 1.00 24.38 ?  129  VAL B O   1 
ATOM   4117 C  CB  . VAL B 1 127 ? 13.809  14.112  -62.265 1.00 18.79 ?  129  VAL B CB  1 
ATOM   4118 C  CG1 . VAL B 1 127 ? 14.839  13.868  -61.143 1.00 19.57 ?  129  VAL B CG1 1 
ATOM   4119 C  CG2 . VAL B 1 127 ? 13.948  13.068  -63.342 1.00 24.43 ?  129  VAL B CG2 1 
ATOM   4120 N  N   . GLU B 1 128 ? 11.826  14.810  -59.436 1.00 21.93 ?  130  GLU B N   1 
ATOM   4121 C  CA  . GLU B 1 128 ? 11.546  15.735  -58.347 1.00 19.77 ?  130  GLU B CA  1 
ATOM   4122 C  C   . GLU B 1 128 ? 12.424  15.388  -57.147 1.00 22.96 ?  130  GLU B C   1 
ATOM   4123 O  O   . GLU B 1 128 ? 12.873  14.251  -56.998 1.00 23.08 ?  130  GLU B O   1 
ATOM   4124 C  CB  . GLU B 1 128 ? 10.059  15.682  -57.956 1.00 22.78 ?  130  GLU B CB  1 
ATOM   4125 C  CG  . GLU B 1 128 ? 9.151   16.017  -59.137 1.00 28.05 ?  130  GLU B CG  1 
ATOM   4126 C  CD  . GLU B 1 128 ? 7.677   16.157  -58.785 1.00 40.93 ?  130  GLU B CD  1 
ATOM   4127 O  OE1 . GLU B 1 128 ? 6.957   16.822  -59.567 1.00 43.75 ?  130  GLU B OE1 1 
ATOM   4128 O  OE2 . GLU B 1 128 ? 7.228   15.591  -57.760 1.00 35.16 ?  130  GLU B OE2 1 
ATOM   4129 N  N   . ASP B 1 129 ? 12.646  16.377  -56.284 1.00 20.15 ?  131  ASP B N   1 
ATOM   4130 C  CA  . ASP B 1 129 ? 13.424  16.196  -55.062 1.00 20.27 ?  131  ASP B CA  1 
ATOM   4131 C  C   . ASP B 1 129 ? 12.539  16.012  -53.839 1.00 22.52 ?  131  ASP B C   1 
ATOM   4132 O  O   . ASP B 1 129 ? 11.426  16.542  -53.757 1.00 21.13 ?  131  ASP B O   1 
ATOM   4133 C  CB  . ASP B 1 129 ? 14.346  17.393  -54.810 1.00 23.48 ?  131  ASP B CB  1 
ATOM   4134 C  CG  . ASP B 1 129 ? 15.426  17.522  -55.852 1.00 30.52 ?  131  ASP B CG  1 
ATOM   4135 O  OD1 . ASP B 1 129 ? 16.419  16.756  -55.764 1.00 27.50 ?  131  ASP B OD1 1 
ATOM   4136 O  OD2 . ASP B 1 129 ? 15.282  18.374  -56.760 1.00 27.26 ?  131  ASP B OD2 1 
ATOM   4137 N  N   . HIS B 1 130 ? 13.075  15.285  -52.863 1.00 19.35 ?  132  HIS B N   1 
ATOM   4138 C  CA  . HIS B 1 130 ? 12.472  15.173  -51.545 1.00 23.23 ?  132  HIS B CA  1 
ATOM   4139 C  C   . HIS B 1 130 ? 12.886  16.368  -50.695 1.00 22.46 ?  132  HIS B C   1 
ATOM   4140 O  O   . HIS B 1 130 ? 14.046  16.790  -50.730 1.00 26.00 ?  132  HIS B O   1 
ATOM   4141 C  CB  . HIS B 1 130 ? 12.909  13.880  -50.855 1.00 17.79 ?  132  HIS B CB  1 
ATOM   4142 C  CG  . HIS B 1 130 ? 12.512  13.811  -49.419 1.00 18.42 ?  132  HIS B CG  1 
ATOM   4143 N  ND1 . HIS B 1 130 ? 13.418  13.901  -48.383 1.00 14.43 ?  132  HIS B ND1 1 
ATOM   4144 C  CD2 . HIS B 1 130 ? 11.295  13.662  -48.845 1.00 17.86 ?  132  HIS B CD2 1 
ATOM   4145 C  CE1 . HIS B 1 130 ? 12.776  13.814  -47.231 1.00 16.36 ?  132  HIS B CE1 1 
ATOM   4146 N  NE2 . HIS B 1 130 ? 11.485  13.671  -47.484 1.00 21.58 ?  132  HIS B NE2 1 
ATOM   4147 N  N   . TYR B 1 131 ? 11.934  16.903  -49.926 1.00 18.97 ?  133  TYR B N   1 
ATOM   4148 C  CA  . TYR B 1 131 ? 12.150  18.078  -49.076 1.00 20.86 ?  133  TYR B CA  1 
ATOM   4149 C  C   . TYR B 1 131 ? 11.771  17.711  -47.650 1.00 21.46 ?  133  TYR B C   1 
ATOM   4150 O  O   . TYR B 1 131 ? 10.608  17.831  -47.260 1.00 21.41 ?  133  TYR B O   1 
ATOM   4151 C  CB  . TYR B 1 131 ? 11.337  19.279  -49.567 1.00 25.39 ?  133  TYR B CB  1 
ATOM   4152 C  CG  . TYR B 1 131 ? 11.948  19.945  -50.763 1.00 24.14 ?  133  TYR B CG  1 
ATOM   4153 C  CD1 . TYR B 1 131 ? 11.605  19.549  -52.047 1.00 24.35 ?  133  TYR B CD1 1 
ATOM   4154 C  CD2 . TYR B 1 131 ? 12.891  20.954  -50.614 1.00 24.98 ?  133  TYR B CD2 1 
ATOM   4155 C  CE1 . TYR B 1 131 ? 12.171  20.150  -53.153 1.00 25.30 ?  133  TYR B CE1 1 
ATOM   4156 C  CE2 . TYR B 1 131 ? 13.470  21.559  -51.717 1.00 29.02 ?  133  TYR B CE2 1 
ATOM   4157 C  CZ  . TYR B 1 131 ? 13.099  21.148  -52.985 1.00 24.67 ?  133  TYR B CZ  1 
ATOM   4158 O  OH  . TYR B 1 131 ? 13.661  21.739  -54.081 1.00 30.09 ?  133  TYR B OH  1 
ATOM   4159 N  N   . GLY B 1 132 ? 12.763  17.295  -46.859 1.00 17.36 ?  134  GLY B N   1 
ATOM   4160 C  CA  . GLY B 1 132 ? 12.488  16.740  -45.549 1.00 19.31 ?  134  GLY B CA  1 
ATOM   4161 C  C   . GLY B 1 132 ? 11.894  17.709  -44.545 1.00 19.88 ?  134  GLY B C   1 
ATOM   4162 O  O   . GLY B 1 132 ? 11.251  17.268  -43.592 1.00 18.87 ?  134  GLY B O   1 
ATOM   4163 N  N   . THR B 1 133 ? 12.091  19.011  -44.724 1.00 20.98 ?  135  THR B N   1 
ATOM   4164 C  CA  . THR B 1 133 ? 11.568  19.965  -43.751 1.00 24.32 ?  135  THR B CA  1 
ATOM   4165 C  C   . THR B 1 133 ? 10.162  20.451  -44.090 1.00 29.29 ?  135  THR B C   1 
ATOM   4166 O  O   . THR B 1 133 ? 9.689   21.408  -43.470 1.00 32.41 ?  135  THR B O   1 
ATOM   4167 C  CB  . THR B 1 133 ? 12.504  21.164  -43.617 1.00 23.77 ?  135  THR B CB  1 
ATOM   4168 O  OG1 . THR B 1 133 ? 12.618  21.827  -44.883 1.00 31.23 ?  135  THR B OG1 1 
ATOM   4169 C  CG2 . THR B 1 133 ? 13.890  20.705  -43.165 1.00 21.08 ?  135  THR B CG2 1 
ATOM   4170 N  N   . ARG B 1 134 ? 9.489   19.817  -45.047 1.00 30.08 ?  136  ARG B N   1 
ATOM   4171 C  CA  . ARG B 1 134 ? 8.128   20.180  -45.454 1.00 30.36 ?  136  ARG B CA  1 
ATOM   4172 C  C   . ARG B 1 134 ? 7.207   19.026  -45.068 1.00 30.55 ?  136  ARG B C   1 
ATOM   4173 O  O   . ARG B 1 134 ? 6.980   18.105  -45.853 1.00 25.49 ?  136  ARG B O   1 
ATOM   4174 C  CB  . ARG B 1 134 ? 8.072   20.474  -46.946 1.00 25.08 ?  136  ARG B CB  1 
ATOM   4175 C  CG  . ARG B 1 134 ? 9.058   21.564  -47.378 1.00 31.79 ?  136  ARG B CG  1 
ATOM   4176 C  CD  . ARG B 1 134 ? 8.880   21.963  -48.834 1.00 31.90 ?  136  ARG B CD  1 
ATOM   4177 N  N   . LEU B 1 135 ? 6.688   19.080  -43.838 1.00 24.40 ?  137  LEU B N   1 
ATOM   4178 C  CA  . LEU B 1 135 ? 5.844   18.002  -43.339 1.00 24.67 ?  137  LEU B CA  1 
ATOM   4179 C  C   . LEU B 1 135 ? 4.619   17.791  -44.215 1.00 32.09 ?  137  LEU B C   1 
ATOM   4180 O  O   . LEU B 1 135 ? 4.122   16.664  -44.317 1.00 31.90 ?  137  LEU B O   1 
ATOM   4181 C  CB  . LEU B 1 135 ? 5.407   18.297  -41.905 1.00 27.63 ?  137  LEU B CB  1 
ATOM   4182 C  CG  . LEU B 1 135 ? 4.906   17.103  -41.095 1.00 28.36 ?  137  LEU B CG  1 
ATOM   4183 C  CD1 . LEU B 1 135 ? 5.978   16.025  -41.009 1.00 27.78 ?  137  LEU B CD1 1 
ATOM   4184 C  CD2 . LEU B 1 135 ? 4.451   17.530  -39.709 1.00 26.10 ?  137  LEU B CD2 1 
ATOM   4185 N  N   . GLU B 1 136 ? 4.124   18.860  -44.850 1.00 34.21 ?  138  GLU B N   1 
ATOM   4186 C  CA  . GLU B 1 136 ? 2.889   18.785  -45.627 1.00 31.94 ?  138  GLU B CA  1 
ATOM   4187 C  C   . GLU B 1 136 ? 3.022   17.836  -46.811 1.00 37.49 ?  138  GLU B C   1 
ATOM   4188 O  O   . GLU B 1 136 ? 2.020   17.267  -47.269 1.00 35.43 ?  138  GLU B O   1 
ATOM   4189 C  CB  . GLU B 1 136 ? 2.495   20.183  -46.112 1.00 34.09 ?  138  GLU B CB  1 
ATOM   4190 N  N   . GLU B 1 137 ? 4.239   17.657  -47.321 1.00 33.81 ?  139  GLU B N   1 
ATOM   4191 C  CA  . GLU B 1 137 ? 4.486   16.777  -48.451 1.00 26.55 ?  139  GLU B CA  1 
ATOM   4192 C  C   . GLU B 1 137 ? 4.643   15.319  -48.036 1.00 27.44 ?  139  GLU B C   1 
ATOM   4193 O  O   . GLU B 1 137 ? 5.040   14.495  -48.864 1.00 25.96 ?  139  GLU B O   1 
ATOM   4194 C  CB  . GLU B 1 137 ? 5.735   17.239  -49.202 1.00 25.35 ?  139  GLU B CB  1 
ATOM   4195 C  CG  . GLU B 1 137 ? 5.773   18.733  -49.488 1.00 33.92 ?  139  GLU B CG  1 
ATOM   4196 C  CD  . GLU B 1 137 ? 6.777   19.104  -50.571 1.00 40.03 ?  139  GLU B CD  1 
ATOM   4197 O  OE1 . GLU B 1 137 ? 7.644   18.267  -50.905 1.00 40.20 ?  139  GLU B OE1 1 
ATOM   4198 O  OE2 . GLU B 1 137 ? 6.730   20.251  -51.064 1.00 42.08 ?  139  GLU B OE2 1 
ATOM   4199 N  N   . HIS B 1 138 ? 4.350   14.989  -46.784 1.00 25.39 ?  140  HIS B N   1 
ATOM   4200 C  CA  . HIS B 1 138 ? 4.533   13.653  -46.244 1.00 22.85 ?  140  HIS B CA  1 
ATOM   4201 C  C   . HIS B 1 138 ? 3.209   13.130  -45.713 1.00 29.41 ?  140  HIS B C   1 
ATOM   4202 O  O   . HIS B 1 138 ? 2.306   13.900  -45.368 1.00 31.63 ?  140  HIS B O   1 
ATOM   4203 C  CB  . HIS B 1 138 ? 5.585   13.646  -45.116 1.00 24.02 ?  140  HIS B CB  1 
ATOM   4204 C  CG  . HIS B 1 138 ? 6.959   14.037  -45.571 1.00 20.90 ?  140  HIS B CG  1 
ATOM   4205 N  ND1 . HIS B 1 138 ? 7.303   15.338  -45.871 1.00 24.34 ?  140  HIS B ND1 1 
ATOM   4206 C  CD2 . HIS B 1 138 ? 8.069   13.292  -45.802 1.00 20.26 ?  140  HIS B CD2 1 
ATOM   4207 C  CE1 . HIS B 1 138 ? 8.567   15.382  -46.253 1.00 24.94 ?  140  HIS B CE1 1 
ATOM   4208 N  NE2 . HIS B 1 138 ? 9.054   14.154  -46.223 1.00 19.14 ?  140  HIS B NE2 1 
ATOM   4209 N  N   . THR B 1 139 ? 3.110   11.806  -45.636 1.00 26.62 ?  141  THR B N   1 
ATOM   4210 C  CA  . THR B 1 139 ? 1.930   11.115  -45.135 1.00 29.73 ?  141  THR B CA  1 
ATOM   4211 C  C   . THR B 1 139 ? 2.290   10.378  -43.855 1.00 28.75 ?  141  THR B C   1 
ATOM   4212 O  O   . THR B 1 139 ? 3.269   9.622   -43.823 1.00 27.37 ?  141  THR B O   1 
ATOM   4213 C  CB  . THR B 1 139 ? 1.388   10.127  -46.177 1.00 31.86 ?  141  THR B CB  1 
ATOM   4214 O  OG1 . THR B 1 139 ? 0.918   10.843  -47.324 1.00 30.54 ?  141  THR B OG1 1 
ATOM   4215 C  CG2 . THR B 1 139 ? 0.262   9.304   -45.604 1.00 28.95 ?  141  THR B CG2 1 
ATOM   4216 N  N   . TYR B 1 140 ? 1.496   10.593  -42.805 1.00 28.44 ?  142  TYR B N   1 
ATOM   4217 C  CA  . TYR B 1 140 ? 1.686   9.889   -41.541 1.00 25.87 ?  142  TYR B CA  1 
ATOM   4218 C  C   . TYR B 1 140 ? 1.157   8.468   -41.653 1.00 29.23 ?  142  TYR B C   1 
ATOM   4219 O  O   . TYR B 1 140 ? -0.023  8.258   -41.962 1.00 34.64 ?  142  TYR B O   1 
ATOM   4220 C  CB  . TYR B 1 140 ? 1.000   10.637  -40.398 1.00 23.46 ?  142  TYR B CB  1 
ATOM   4221 C  CG  . TYR B 1 140 ? 1.058   9.919   -39.074 1.00 27.70 ?  142  TYR B CG  1 
ATOM   4222 C  CD1 . TYR B 1 140 ? 2.220   9.918   -38.314 1.00 27.64 ?  142  TYR B CD1 1 
ATOM   4223 C  CD2 . TYR B 1 140 ? -0.063  9.275   -38.560 1.00 28.16 ?  142  TYR B CD2 1 
ATOM   4224 C  CE1 . TYR B 1 140 ? 2.272   9.268   -37.095 1.00 32.72 ?  142  TYR B CE1 1 
ATOM   4225 C  CE2 . TYR B 1 140 ? -0.024  8.626   -37.348 1.00 30.04 ?  142  TYR B CE2 1 
ATOM   4226 C  CZ  . TYR B 1 140 ? 1.145   8.628   -36.611 1.00 27.90 ?  142  TYR B CZ  1 
ATOM   4227 O  OH  . TYR B 1 140 ? 1.192   7.983   -35.394 1.00 35.77 ?  142  TYR B OH  1 
ATOM   4228 N  N   . LEU B 1 141 ? 2.023   7.492   -41.401 1.00 22.37 ?  143  LEU B N   1 
ATOM   4229 C  CA  . LEU B 1 141 ? 1.678   6.083   -41.541 1.00 24.16 ?  143  LEU B CA  1 
ATOM   4230 C  C   . LEU B 1 141 ? 1.507   5.381   -40.210 1.00 28.37 ?  143  LEU B C   1 
ATOM   4231 O  O   . LEU B 1 141 ? 1.221   4.177   -40.185 1.00 32.22 ?  143  LEU B O   1 
ATOM   4232 C  CB  . LEU B 1 141 ? 2.744   5.354   -42.367 1.00 25.19 ?  143  LEU B CB  1 
ATOM   4233 C  CG  . LEU B 1 141 ? 3.081   5.996   -43.712 1.00 27.94 ?  143  LEU B CG  1 
ATOM   4234 C  CD1 . LEU B 1 141 ? 4.257   5.275   -44.322 1.00 30.74 ?  143  LEU B CD1 1 
ATOM   4235 C  CD2 . LEU B 1 141 ? 1.885   5.986   -44.672 1.00 30.43 ?  143  LEU B CD2 1 
ATOM   4236 N  N   . GLY B 1 142 ? 1.677   6.093   -39.111 1.00 29.44 ?  144  GLY B N   1 
ATOM   4237 C  CA  . GLY B 1 142 ? 1.637   5.521   -37.787 1.00 26.35 ?  144  GLY B CA  1 
ATOM   4238 C  C   . GLY B 1 142 ? 2.937   5.771   -37.057 1.00 29.55 ?  144  GLY B C   1 
ATOM   4239 O  O   . GLY B 1 142 ? 3.855   6.414   -37.566 1.00 28.63 ?  144  GLY B O   1 
ATOM   4240 N  N   . THR B 1 143 ? 2.998   5.241   -35.842 1.00 28.68 ?  145  THR B N   1 
ATOM   4241 C  CA  . THR B 1 143 ? 4.142   5.415   -34.963 1.00 27.28 ?  145  THR B CA  1 
ATOM   4242 C  C   . THR B 1 143 ? 4.661   4.049   -34.541 1.00 30.90 ?  145  THR B C   1 
ATOM   4243 O  O   . THR B 1 143 ? 3.883   3.150   -34.202 1.00 30.51 ?  145  THR B O   1 
ATOM   4244 C  CB  . THR B 1 143 ? 3.768   6.270   -33.740 1.00 25.91 ?  145  THR B CB  1 
ATOM   4245 O  OG1 . THR B 1 143 ? 3.388   7.577   -34.185 1.00 32.60 ?  145  THR B OG1 1 
ATOM   4246 C  CG2 . THR B 1 143 ? 4.940   6.413   -32.798 1.00 28.58 ?  145  THR B CG2 1 
ATOM   4247 N  N   . THR B 1 144 ? 5.981   3.895   -34.576 1.00 28.70 ?  146  THR B N   1 
ATOM   4248 C  CA  . THR B 1 144 ? 6.599   2.631   -34.244 1.00 27.28 ?  146  THR B CA  1 
ATOM   4249 C  C   . THR B 1 144 ? 6.538   2.394   -32.740 1.00 31.50 ?  146  THR B C   1 
ATOM   4250 O  O   . THR B 1 144 ? 6.370   3.335   -31.962 1.00 33.21 ?  146  THR B O   1 
ATOM   4251 C  CB  . THR B 1 144 ? 8.054   2.622   -34.705 1.00 32.00 ?  146  THR B CB  1 
ATOM   4252 O  OG1 . THR B 1 144 ? 8.816   3.490   -33.856 1.00 26.49 ?  146  THR B OG1 1 
ATOM   4253 C  CG2 . THR B 1 144 ? 8.160   3.112   -36.144 1.00 24.50 ?  146  THR B CG2 1 
ATOM   4254 N  N   . PRO B 1 145 ? 6.680   1.141   -32.302 1.00 26.37 ?  147  PRO B N   1 
ATOM   4255 C  CA  . PRO B 1 145 ? 6.730   0.878   -30.856 1.00 32.47 ?  147  PRO B CA  1 
ATOM   4256 C  C   . PRO B 1 145 ? 7.894   1.555   -30.146 1.00 36.82 ?  147  PRO B C   1 
ATOM   4257 O  O   . PRO B 1 145 ? 7.870   1.650   -28.913 1.00 37.15 ?  147  PRO B O   1 
ATOM   4258 C  CB  . PRO B 1 145 ? 6.825   -0.654  -30.784 1.00 36.97 ?  147  PRO B CB  1 
ATOM   4259 C  CG  . PRO B 1 145 ? 7.261   -1.080  -32.167 1.00 36.48 ?  147  PRO B CG  1 
ATOM   4260 C  CD  . PRO B 1 145 ? 6.574   -0.113  -33.065 1.00 32.45 ?  147  PRO B CD  1 
ATOM   4261 N  N   . ASN B 1 146 ? 8.901   2.041   -30.872 1.00 30.50 ?  148  ASN B N   1 
ATOM   4262 C  CA  . ASN B 1 146 ? 9.942   2.859   -30.263 1.00 31.87 ?  148  ASN B CA  1 
ATOM   4263 C  C   . ASN B 1 146 ? 9.559   4.329   -30.188 1.00 29.59 ?  148  ASN B C   1 
ATOM   4264 O  O   . ASN B 1 146 ? 10.342  5.132   -29.673 1.00 33.65 ?  148  ASN B O   1 
ATOM   4265 C  CB  . ASN B 1 146 ? 11.270  2.717   -31.027 1.00 25.77 ?  148  ASN B CB  1 
ATOM   4266 C  CG  . ASN B 1 146 ? 12.113  1.562   -30.525 1.00 29.87 ?  148  ASN B CG  1 
ATOM   4267 O  OD1 . ASN B 1 146 ? 12.174  1.298   -29.324 1.00 37.93 ?  148  ASN B OD1 1 
ATOM   4268 N  ND2 . ASN B 1 146 ? 12.789  0.881   -31.442 1.00 30.28 ?  148  ASN B ND2 1 
ATOM   4269 N  N   . GLY B 1 147 ? 8.389   4.702   -30.695 1.00 30.03 ?  149  GLY B N   1 
ATOM   4270 C  CA  . GLY B 1 147 ? 7.924   6.067   -30.585 1.00 28.47 ?  149  GLY B CA  1 
ATOM   4271 C  C   . GLY B 1 147 ? 8.343   6.994   -31.702 1.00 32.69 ?  149  GLY B C   1 
ATOM   4272 O  O   . GLY B 1 147 ? 8.244   8.217   -31.536 1.00 32.48 ?  149  GLY B O   1 
ATOM   4273 N  N   . VAL B 1 148 ? 8.798   6.466   -32.834 1.00 25.19 ?  150  VAL B N   1 
ATOM   4274 C  CA  . VAL B 1 148 ? 9.153   7.284   -33.989 1.00 22.93 ?  150  VAL B CA  1 
ATOM   4275 C  C   . VAL B 1 148 ? 7.928   7.384   -34.896 1.00 22.93 ?  150  VAL B C   1 
ATOM   4276 O  O   . VAL B 1 148 ? 7.430   6.345   -35.357 1.00 22.82 ?  150  VAL B O   1 
ATOM   4277 C  CB  . VAL B 1 148 ? 10.347  6.706   -34.756 1.00 19.81 ?  150  VAL B CB  1 
ATOM   4278 C  CG1 . VAL B 1 148 ? 10.620  7.568   -35.992 1.00 21.56 ?  150  VAL B CG1 1 
ATOM   4279 C  CG2 . VAL B 1 148 ? 11.586  6.627   -33.855 1.00 23.26 ?  150  VAL B CG2 1 
ATOM   4280 N  N   . PRO B 1 149 ? 7.427   8.587   -35.184 1.00 24.66 ?  151  PRO B N   1 
ATOM   4281 C  CA  . PRO B 1 149 ? 6.327   8.715   -36.146 1.00 29.69 ?  151  PRO B CA  1 
ATOM   4282 C  C   . PRO B 1 149 ? 6.884   8.580   -37.554 1.00 30.11 ?  151  PRO B C   1 
ATOM   4283 O  O   . PRO B 1 149 ? 7.915   9.174   -37.880 1.00 27.59 ?  151  PRO B O   1 
ATOM   4284 C  CB  . PRO B 1 149 ? 5.793   10.127  -35.893 1.00 26.02 ?  151  PRO B CB  1 
ATOM   4285 C  CG  . PRO B 1 149 ? 7.027   10.889  -35.449 1.00 24.32 ?  151  PRO B CG  1 
ATOM   4286 C  CD  . PRO B 1 149 ? 7.869   9.899   -34.671 1.00 27.27 ?  151  PRO B CD  1 
ATOM   4287 N  N   . ALA B 1 150 ? 6.207   7.788   -38.380 1.00 22.76 ?  152  ALA B N   1 
ATOM   4288 C  CA  . ALA B 1 150 ? 6.642   7.547   -39.756 1.00 24.21 ?  152  ALA B CA  1 
ATOM   4289 C  C   . ALA B 1 150 ? 5.928   8.530   -40.668 1.00 22.27 ?  152  ALA B C   1 
ATOM   4290 O  O   . ALA B 1 150 ? 4.730   8.391   -40.933 1.00 22.96 ?  152  ALA B O   1 
ATOM   4291 C  CB  . ALA B 1 150 ? 6.377   6.101   -40.162 1.00 22.46 ?  152  ALA B CB  1 
ATOM   4292 N  N   . TRP B 1 151 ? 6.662   9.546   -41.128 1.00 21.63 ?  153  TRP B N   1 
ATOM   4293 C  CA  . TRP B 1 151 ? 6.206   10.494  -42.138 1.00 22.54 ?  153  TRP B CA  1 
ATOM   4294 C  C   . TRP B 1 151 ? 7.010   10.238  -43.409 1.00 24.91 ?  153  TRP B C   1 
ATOM   4295 O  O   . TRP B 1 151 ? 8.225   10.473  -43.436 1.00 22.23 ?  153  TRP B O   1 
ATOM   4296 C  CB  . TRP B 1 151 ? 6.404   11.942  -41.689 1.00 21.37 ?  153  TRP B CB  1 
ATOM   4297 C  CG  . TRP B 1 151 ? 5.552   12.374  -40.553 1.00 24.75 ?  153  TRP B CG  1 
ATOM   4298 C  CD1 . TRP B 1 151 ? 5.791   12.176  -39.222 1.00 24.90 ?  153  TRP B CD1 1 
ATOM   4299 C  CD2 . TRP B 1 151 ? 4.287   13.041  -40.642 1.00 23.02 ?  153  TRP B CD2 1 
ATOM   4300 N  NE1 . TRP B 1 151 ? 4.763   12.708  -38.476 1.00 29.20 ?  153  TRP B NE1 1 
ATOM   4301 C  CE2 . TRP B 1 151 ? 3.824   13.237  -39.325 1.00 30.01 ?  153  TRP B CE2 1 
ATOM   4302 C  CE3 . TRP B 1 151 ? 3.501   13.492  -41.712 1.00 32.62 ?  153  TRP B CE3 1 
ATOM   4303 C  CZ2 . TRP B 1 151 ? 2.613   13.874  -39.046 1.00 27.43 ?  153  TRP B CZ2 1 
ATOM   4304 C  CZ3 . TRP B 1 151 ? 2.302   14.126  -41.433 1.00 33.13 ?  153  TRP B CZ3 1 
ATOM   4305 C  CH2 . TRP B 1 151 ? 1.870   14.309  -40.110 1.00 27.38 ?  153  TRP B CH2 1 
ATOM   4306 N  N   . ILE B 1 152 ? 6.334   9.790   -44.464 1.00 19.71 ?  154  ILE B N   1 
ATOM   4307 C  CA  . ILE B 1 152 ? 6.981   9.383   -45.706 1.00 17.95 ?  154  ILE B CA  1 
ATOM   4308 C  C   . ILE B 1 152 ? 6.384   10.192  -46.845 1.00 23.71 ?  154  ILE B C   1 
ATOM   4309 O  O   . ILE B 1 152 ? 5.180   10.472  -46.841 1.00 27.83 ?  154  ILE B O   1 
ATOM   4310 C  CB  . ILE B 1 152 ? 6.809   7.868   -45.945 1.00 19.90 ?  154  ILE B CB  1 
ATOM   4311 C  CG1 . ILE B 1 152 ? 7.389   7.077   -44.767 1.00 22.99 ?  154  ILE B CG1 1 
ATOM   4312 C  CG2 . ILE B 1 152 ? 7.443   7.453   -47.266 1.00 18.54 ?  154  ILE B CG2 1 
ATOM   4313 C  CD1 . ILE B 1 152 ? 8.912   7.245   -44.581 1.00 21.39 ?  154  ILE B CD1 1 
ATOM   4314 N  N   . ASP B 1 153 ? 7.224   10.570  -47.816 1.00 19.37 ?  155  ASP B N   1 
ATOM   4315 C  CA  . ASP B 1 153 ? 6.785   11.415  -48.928 1.00 19.72 ?  155  ASP B CA  1 
ATOM   4316 C  C   . ASP B 1 153 ? 5.530   10.866  -49.602 1.00 21.66 ?  155  ASP B C   1 
ATOM   4317 O  O   . ASP B 1 153 ? 5.485   9.707   -50.021 1.00 18.83 ?  155  ASP B O   1 
ATOM   4318 C  CB  . ASP B 1 153 ? 7.910   11.562  -49.955 1.00 19.67 ?  155  ASP B CB  1 
ATOM   4319 C  CG  . ASP B 1 153 ? 7.678   12.715  -50.909 1.00 26.30 ?  155  ASP B CG  1 
ATOM   4320 O  OD1 . ASP B 1 153 ? 6.713   12.639  -51.709 1.00 22.52 ?  155  ASP B OD1 1 
ATOM   4321 O  OD2 . ASP B 1 153 ? 8.446   13.698  -50.879 1.00 20.66 ?  155  ASP B OD2 1 
ATOM   4322 N  N   . SER B 1 154 ? 4.513   11.727  -49.724 1.00 24.86 ?  156  SER B N   1 
ATOM   4323 C  CA  . SER B 1 154 ? 3.204   11.272  -50.189 1.00 22.09 ?  156  SER B CA  1 
ATOM   4324 C  C   . SER B 1 154 ? 3.221   10.822  -51.643 1.00 21.13 ?  156  SER B C   1 
ATOM   4325 O  O   . SER B 1 154 ? 2.385   9.994   -52.034 1.00 25.65 ?  156  SER B O   1 
ATOM   4326 C  CB  . SER B 1 154 ? 2.160   12.374  -49.992 1.00 23.98 ?  156  SER B CB  1 
ATOM   4327 O  OG  . SER B 1 154 ? 2.088   12.787  -48.634 1.00 25.16 ?  156  SER B OG  1 
ATOM   4328 N  N   . ARG B 1 155 ? 4.127   11.365  -52.463 1.00 19.91 ?  157  ARG B N   1 
ATOM   4329 C  CA  . ARG B 1 155 ? 4.205   10.941  -53.861 1.00 24.31 ?  157  ARG B CA  1 
ATOM   4330 C  C   . ARG B 1 155 ? 4.596   9.477   -53.977 1.00 24.46 ?  157  ARG B C   1 
ATOM   4331 O  O   . ARG B 1 155 ? 4.150   8.777   -54.898 1.00 22.25 ?  157  ARG B O   1 
ATOM   4332 C  CB  . ARG B 1 155 ? 5.202   11.806  -54.620 1.00 19.19 ?  157  ARG B CB  1 
ATOM   4333 C  CG  . ARG B 1 155 ? 4.765   13.244  -54.782 1.00 23.24 ?  157  ARG B CG  1 
ATOM   4334 C  CD  . ARG B 1 155 ? 5.914   14.122  -55.221 1.00 20.49 ?  157  ARG B CD  1 
ATOM   4335 N  NE  . ARG B 1 155 ? 6.906   14.289  -54.161 1.00 28.67 ?  157  ARG B NE  1 
ATOM   4336 C  CZ  . ARG B 1 155 ? 7.845   15.228  -54.166 1.00 22.16 ?  157  ARG B CZ  1 
ATOM   4337 N  NH1 . ARG B 1 155 ? 7.925   16.080  -55.180 1.00 29.84 ?  157  ARG B NH1 1 
ATOM   4338 N  NH2 . ARG B 1 155 ? 8.705   15.319  -53.157 1.00 25.56 ?  157  ARG B NH2 1 
ATOM   4339 N  N   . TYR B 1 156 ? 5.424   8.992   -53.050 1.00 20.17 ?  158  TYR B N   1 
ATOM   4340 C  CA  . TYR B 1 156 ? 5.759   7.578   -53.035 1.00 19.96 ?  158  TYR B CA  1 
ATOM   4341 C  C   . TYR B 1 156 ? 4.636   6.756   -52.416 1.00 18.85 ?  158  TYR B C   1 
ATOM   4342 O  O   . TYR B 1 156 ? 4.261   5.712   -52.960 1.00 21.92 ?  158  TYR B O   1 
ATOM   4343 C  CB  . TYR B 1 156 ? 7.090   7.383   -52.290 1.00 17.79 ?  158  TYR B CB  1 
ATOM   4344 C  CG  . TYR B 1 156 ? 7.545   5.958   -52.105 1.00 17.22 ?  158  TYR B CG  1 
ATOM   4345 C  CD1 . TYR B 1 156 ? 8.317   5.319   -53.070 1.00 16.13 ?  158  TYR B CD1 1 
ATOM   4346 C  CD2 . TYR B 1 156 ? 7.217   5.253   -50.960 1.00 19.44 ?  158  TYR B CD2 1 
ATOM   4347 C  CE1 . TYR B 1 156 ? 8.742   4.021   -52.898 1.00 14.39 ?  158  TYR B CE1 1 
ATOM   4348 C  CE2 . TYR B 1 156 ? 7.637   3.959   -50.779 1.00 19.44 ?  158  TYR B CE2 1 
ATOM   4349 C  CZ  . TYR B 1 156 ? 8.404   3.350   -51.750 1.00 18.71 ?  158  TYR B CZ  1 
ATOM   4350 O  OH  . TYR B 1 156 ? 8.818   2.051   -51.566 1.00 17.61 ?  158  TYR B OH  1 
ATOM   4351 N  N   . VAL B 1 157 ? 4.069   7.227   -51.301 1.00 19.24 ?  159  VAL B N   1 
ATOM   4352 C  CA  . VAL B 1 157 ? 3.079   6.444   -50.559 1.00 23.63 ?  159  VAL B CA  1 
ATOM   4353 C  C   . VAL B 1 157 ? 1.875   6.121   -51.435 1.00 24.56 ?  159  VAL B C   1 
ATOM   4354 O  O   . VAL B 1 157 ? 1.345   5.003   -51.405 1.00 25.87 ?  159  VAL B O   1 
ATOM   4355 C  CB  . VAL B 1 157 ? 2.655   7.197   -49.280 1.00 26.96 ?  159  VAL B CB  1 
ATOM   4356 C  CG1 . VAL B 1 157 ? 1.505   6.471   -48.559 1.00 25.92 ?  159  VAL B CG1 1 
ATOM   4357 C  CG2 . VAL B 1 157 ? 3.848   7.370   -48.348 1.00 21.56 ?  159  VAL B CG2 1 
ATOM   4358 N  N   . GLN B 1 158 ? 1.439   7.079   -52.235 1.00 21.60 ?  160  GLN B N   1 
ATOM   4359 C  CA  . GLN B 1 158 ? 0.220   6.914   -53.011 1.00 27.91 ?  160  GLN B CA  1 
ATOM   4360 C  C   . GLN B 1 158 ? 0.464   6.225   -54.350 1.00 30.44 ?  160  GLN B C   1 
ATOM   4361 O  O   . GLN B 1 158 ? -0.501  5.938   -55.061 1.00 24.54 ?  160  GLN B O   1 
ATOM   4362 C  CB  . GLN B 1 158 ? -0.433  8.281   -53.231 1.00 25.90 ?  160  GLN B CB  1 
ATOM   4363 C  CG  . GLN B 1 158 ? -1.092  8.900   -51.971 1.00 30.13 ?  160  GLN B CG  1 
ATOM   4364 C  CD  . GLN B 1 158 ? -1.936  7.929   -51.152 1.00 34.21 ?  160  GLN B CD  1 
ATOM   4365 O  OE1 . GLN B 1 158 ? -2.698  7.132   -51.698 1.00 43.07 ?  160  GLN B OE1 1 
ATOM   4366 N  NE2 . GLN B 1 158 ? -1.823  8.016   -49.829 1.00 38.83 ?  160  GLN B NE2 1 
ATOM   4367 N  N   . ALA B 1 159 ? 1.717   5.940   -54.710 1.00 24.77 ?  161  ALA B N   1 
ATOM   4368 C  CA  . ALA B 1 159 ? 1.993   5.326   -56.004 1.00 21.30 ?  161  ALA B CA  1 
ATOM   4369 C  C   . ALA B 1 159 ? 1.570   3.858   -56.015 1.00 24.60 ?  161  ALA B C   1 
ATOM   4370 O  O   . ALA B 1 159 ? 1.729   3.139   -55.026 1.00 22.01 ?  161  ALA B O   1 
ATOM   4371 C  CB  . ALA B 1 159 ? 3.481   5.454   -56.347 1.00 24.02 ?  161  ALA B CB  1 
ATOM   4372 N  N   . ASP B 1 160 ? 1.020   3.402   -57.148 1.00 23.01 ?  162  ASP B N   1 
ATOM   4373 C  CA  . ASP B 1 160 ? 0.546   2.022   -57.198 1.00 20.17 ?  162  ASP B CA  1 
ATOM   4374 C  C   . ASP B 1 160 ? 1.711   1.044   -57.160 1.00 20.28 ?  162  ASP B C   1 
ATOM   4375 O  O   . ASP B 1 160 ? 1.625   -0.011  -56.520 1.00 25.05 ?  162  ASP B O   1 
ATOM   4376 C  CB  . ASP B 1 160 ? -0.314  1.798   -58.447 1.00 28.31 ?  162  ASP B CB  1 
ATOM   4377 N  N   . LEU B 1 161 ? 2.815   1.394   -57.814 1.00 24.06 ?  163  LEU B N   1 
ATOM   4378 C  CA  . LEU B 1 161 ? 4.022   0.576   -57.860 1.00 19.39 ?  163  LEU B CA  1 
ATOM   4379 C  C   . LEU B 1 161 ? 5.173   1.357   -57.235 1.00 20.21 ?  163  LEU B C   1 
ATOM   4380 O  O   . LEU B 1 161 ? 5.471   2.476   -57.671 1.00 19.03 ?  163  LEU B O   1 
ATOM   4381 C  CB  . LEU B 1 161 ? 4.355   0.205   -59.303 1.00 19.12 ?  163  LEU B CB  1 
ATOM   4382 C  CG  . LEU B 1 161 ? 5.548   -0.735  -59.477 1.00 18.65 ?  163  LEU B CG  1 
ATOM   4383 C  CD1 . LEU B 1 161 ? 5.278   -2.056  -58.812 1.00 17.49 ?  163  LEU B CD1 1 
ATOM   4384 C  CD2 . LEU B 1 161 ? 5.856   -0.903  -60.958 1.00 26.25 ?  163  LEU B CD2 1 
ATOM   4385 N  N   . LYS B 1 162 ? 5.824   0.762   -56.235 1.00 20.26 ?  164  LYS B N   1 
ATOM   4386 C  CA  . LYS B 1 162 ? 6.888   1.422   -55.480 1.00 19.25 ?  164  LYS B CA  1 
ATOM   4387 C  C   . LYS B 1 162 ? 8.207   0.691   -55.719 1.00 16.42 ?  164  LYS B C   1 
ATOM   4388 O  O   . LYS B 1 162 ? 8.319   -0.500  -55.404 1.00 19.75 ?  164  LYS B O   1 
ATOM   4389 C  CB  . LYS B 1 162 ? 6.558   1.442   -53.991 1.00 17.11 ?  164  LYS B CB  1 
ATOM   4390 C  CG  . LYS B 1 162 ? 5.280   2.183   -53.630 1.00 20.34 ?  164  LYS B CG  1 
ATOM   4391 C  CD  . LYS B 1 162 ? 4.806   1.775   -52.236 1.00 25.83 ?  164  LYS B CD  1 
ATOM   4392 C  CE  . LYS B 1 162 ? 3.756   2.732   -51.690 1.00 28.06 ?  164  LYS B CE  1 
ATOM   4393 N  NZ  . LYS B 1 162 ? 2.665   2.931   -52.683 1.00 31.12 ?  164  LYS B NZ  1 
ATOM   4394 N  N   . ILE B 1 163 ? 9.202   1.407   -56.254 1.00 16.82 ?  165  ILE B N   1 
ATOM   4395 C  CA  . ILE B 1 163 ? 10.517  0.847   -56.567 1.00 18.07 ?  165  ILE B CA  1 
ATOM   4396 C  C   . ILE B 1 163 ? 11.604  1.711   -55.929 1.00 15.44 ?  165  ILE B C   1 
ATOM   4397 O  O   . ILE B 1 163 ? 11.497  2.943   -55.901 1.00 15.35 ?  165  ILE B O   1 
ATOM   4398 C  CB  . ILE B 1 163 ? 10.737  0.755   -58.094 1.00 21.47 ?  165  ILE B CB  1 
ATOM   4399 C  CG1 . ILE B 1 163 ? 9.592   -0.018  -58.766 1.00 19.63 ?  165  ILE B CG1 1 
ATOM   4400 C  CG2 . ILE B 1 163 ? 12.094  0.130   -58.407 1.00 18.33 ?  165  ILE B CG2 1 
ATOM   4401 C  CD1 . ILE B 1 163 ? 9.389   0.333   -60.253 1.00 20.20 ?  165  ILE B CD1 1 
ATOM   4402 N  N   . ALA B 1 164 ? 12.671  1.075   -55.439 1.00 14.60 ?  166  ALA B N   1 
ATOM   4403 C  CA  . ALA B 1 164 ? 13.824  1.835   -54.959 1.00 14.54 ?  166  ALA B CA  1 
ATOM   4404 C  C   . ALA B 1 164 ? 15.119  1.253   -55.520 1.00 15.89 ?  166  ALA B C   1 
ATOM   4405 O  O   . ALA B 1 164 ? 15.264  0.033   -55.636 1.00 17.11 ?  166  ALA B O   1 
ATOM   4406 C  CB  . ALA B 1 164 ? 13.865  1.849   -53.415 1.00 16.71 ?  166  ALA B CB  1 
ATOM   4407 N  N   . THR B 1 165 ? 16.060  2.132   -55.863 1.00 11.73 ?  167  THR B N   1 
ATOM   4408 C  CA  . THR B 1 165 ? 17.371  1.747   -56.365 1.00 14.43 ?  167  THR B CA  1 
ATOM   4409 C  C   . THR B 1 165 ? 18.430  2.271   -55.408 1.00 12.91 ?  167  THR B C   1 
ATOM   4410 O  O   . THR B 1 165 ? 18.234  3.298   -54.755 1.00 18.58 ?  167  THR B O   1 
ATOM   4411 C  CB  . THR B 1 165 ? 17.635  2.322   -57.757 1.00 19.92 ?  167  THR B CB  1 
ATOM   4412 O  OG1 . THR B 1 165 ? 17.716  3.754   -57.671 1.00 16.29 ?  167  THR B OG1 1 
ATOM   4413 C  CG2 . THR B 1 165 ? 16.513  1.928   -58.728 1.00 16.28 ?  167  THR B CG2 1 
ATOM   4414 N  N   . GLY B 1 166 ? 19.562  1.591   -55.341 1.00 13.82 ?  168  GLY B N   1 
ATOM   4415 C  CA  . GLY B 1 166 ? 20.611  2.109   -54.482 1.00 14.19 ?  168  GLY B CA  1 
ATOM   4416 C  C   . GLY B 1 166 ? 21.872  1.281   -54.529 1.00 13.35 ?  168  GLY B C   1 
ATOM   4417 O  O   . GLY B 1 166 ? 22.089  0.463   -55.429 1.00 11.61 ?  168  GLY B O   1 
ATOM   4418 N  N   . LEU B 1 167 ? 22.706  1.524   -53.519 1.00 10.47 ?  169  LEU B N   1 
ATOM   4419 C  CA  . LEU B 1 167 ? 24.096  1.099   -53.509 1.00 13.39 ?  169  LEU B CA  1 
ATOM   4420 C  C   . LEU B 1 167 ? 24.424  0.612   -52.102 1.00 11.08 ?  169  LEU B C   1 
ATOM   4421 O  O   . LEU B 1 167 ? 24.162  1.321   -51.128 1.00 12.51 ?  169  LEU B O   1 
ATOM   4422 C  CB  . LEU B 1 167 ? 25.003  2.268   -53.918 1.00 14.43 ?  169  LEU B CB  1 
ATOM   4423 C  CG  . LEU B 1 167 ? 26.488  2.199   -53.576 1.00 13.73 ?  169  LEU B CG  1 
ATOM   4424 C  CD1 . LEU B 1 167 ? 27.120  1.088   -54.390 1.00 13.14 ?  169  LEU B CD1 1 
ATOM   4425 C  CD2 . LEU B 1 167 ? 27.202  3.541   -53.818 1.00 13.56 ?  169  LEU B CD2 1 
ATOM   4426 N  N   . ILE B 1 168 ? 24.949  -0.604  -51.992 1.00 9.64  ?  170  ILE B N   1 
ATOM   4427 C  CA  . ILE B 1 168 ? 25.249  -1.214  -50.705 1.00 12.55 ?  170  ILE B CA  1 
ATOM   4428 C  C   . ILE B 1 168 ? 26.728  -0.966  -50.406 1.00 13.65 ?  170  ILE B C   1 
ATOM   4429 O  O   . ILE B 1 168 ? 27.610  -1.498  -51.085 1.00 13.04 ?  170  ILE B O   1 
ATOM   4430 C  CB  . ILE B 1 168 ? 24.909  -2.710  -50.694 1.00 14.09 ?  170  ILE B CB  1 
ATOM   4431 C  CG1 . ILE B 1 168 ? 23.426  -2.906  -51.024 1.00 11.04 ?  170  ILE B CG1 1 
ATOM   4432 C  CG2 . ILE B 1 168 ? 25.240  -3.315  -49.339 1.00 13.07 ?  170  ILE B CG2 1 
ATOM   4433 C  CD1 . ILE B 1 168 ? 22.999  -4.363  -51.158 1.00 11.42 ?  170  ILE B CD1 1 
ATOM   4434 N  N   . GLU B 1 169 ? 26.980  -0.125  -49.416 1.00 12.74 ?  171  GLU B N   1 
ATOM   4435 C  CA  . GLU B 1 169 ? 28.267  0.202   -48.818 1.00 11.68 ?  171  GLU B CA  1 
ATOM   4436 C  C   . GLU B 1 169 ? 28.125  0.206   -47.307 1.00 10.64 ?  171  GLU B C   1 
ATOM   4437 O  O   . GLU B 1 169 ? 27.026  0.382   -46.784 1.00 13.95 ?  171  GLU B O   1 
ATOM   4438 C  CB  . GLU B 1 169 ? 28.791  1.578   -49.265 1.00 14.59 ?  171  GLU B CB  1 
ATOM   4439 C  CG  . GLU B 1 169 ? 29.046  1.878   -50.722 1.00 14.20 ?  171  GLU B CG  1 
ATOM   4440 C  CD  . GLU B 1 169 ? 30.316  1.181   -51.235 1.00 22.70 ?  171  GLU B CD  1 
ATOM   4441 O  OE1 . GLU B 1 169 ? 30.645  1.325   -52.440 1.00 18.70 ?  171  GLU B OE1 1 
ATOM   4442 O  OE2 . GLU B 1 169 ? 30.995  0.492   -50.430 1.00 15.58 ?  171  GLU B OE2 1 
ATOM   4443 N  N   . PRO B 1 170 ? 29.222  0.051   -46.572 1.00 11.63 ?  172  PRO B N   1 
ATOM   4444 C  CA  . PRO B 1 170 ? 29.146  0.261   -45.122 1.00 8.37  ?  172  PRO B CA  1 
ATOM   4445 C  C   . PRO B 1 170 ? 28.587  1.640   -44.804 1.00 9.30  ?  172  PRO B C   1 
ATOM   4446 O  O   . PRO B 1 170 ? 28.771  2.598   -45.562 1.00 10.38 ?  172  PRO B O   1 
ATOM   4447 C  CB  . PRO B 1 170 ? 30.606  0.131   -44.668 1.00 15.21 ?  172  PRO B CB  1 
ATOM   4448 C  CG  . PRO B 1 170 ? 31.272  -0.633  -45.780 1.00 13.28 ?  172  PRO B CG  1 
ATOM   4449 C  CD  . PRO B 1 170 ? 30.607  -0.177  -47.022 1.00 14.19 ?  172  PRO B CD  1 
ATOM   4450 N  N   . HIS B 1 171 ? 27.884  1.730   -43.668 1.00 10.67 ?  173  HIS B N   1 
ATOM   4451 C  CA  . HIS B 1 171 ? 27.318  2.996   -43.205 1.00 9.94  ?  173  HIS B CA  1 
ATOM   4452 C  C   . HIS B 1 171 ? 27.505  3.120   -41.694 1.00 11.11 ?  173  HIS B C   1 
ATOM   4453 O  O   . HIS B 1 171 ? 27.220  2.181   -40.949 1.00 10.19 ?  173  HIS B O   1 
ATOM   4454 C  CB  . HIS B 1 171 ? 25.820  3.126   -43.566 1.00 11.13 ?  173  HIS B CB  1 
ATOM   4455 C  CG  . HIS B 1 171 ? 25.271  4.506   -43.334 1.00 11.58 ?  173  HIS B CG  1 
ATOM   4456 N  ND1 . HIS B 1 171 ? 24.694  4.886   -42.138 1.00 10.82 ?  173  HIS B ND1 1 
ATOM   4457 C  CD2 . HIS B 1 171 ? 25.234  5.597   -44.133 1.00 11.73 ?  173  HIS B CD2 1 
ATOM   4458 C  CE1 . HIS B 1 171 ? 24.344  6.159   -42.205 1.00 9.50  ?  173  HIS B CE1 1 
ATOM   4459 N  NE2 . HIS B 1 171 ? 24.647  6.612   -43.409 1.00 10.62 ?  173  HIS B NE2 1 
ATOM   4460 N  N   . LEU B 1 172 ? 27.918  4.313   -41.251 1.00 9.98  ?  174  LEU B N   1 
ATOM   4461 C  CA  . LEU B 1 172 ? 28.332  4.547   -39.868 1.00 12.59 ?  174  LEU B CA  1 
ATOM   4462 C  C   . LEU B 1 172 ? 27.187  4.503   -38.859 1.00 12.54 ?  174  LEU B C   1 
ATOM   4463 O  O   . LEU B 1 172 ? 27.459  4.387   -37.660 1.00 11.26 ?  174  LEU B O   1 
ATOM   4464 C  CB  . LEU B 1 172 ? 29.059  5.892   -39.760 1.00 9.73  ?  174  LEU B CB  1 
ATOM   4465 C  CG  . LEU B 1 172 ? 28.259  7.189   -39.644 1.00 13.64 ?  174  LEU B CG  1 
ATOM   4466 C  CD1 . LEU B 1 172 ? 29.186  8.349   -39.383 1.00 12.39 ?  174  LEU B CD1 1 
ATOM   4467 C  CD2 . LEU B 1 172 ? 27.420  7.477   -40.906 1.00 10.54 ?  174  LEU B CD2 1 
ATOM   4468 N  N   . MET B 1 173 ? 25.924  4.618   -39.284 1.00 13.40 ?  175  MET B N   1 
ATOM   4469 C  CA  . MET B 1 173 ? 24.812  4.412   -38.357 1.00 13.81 ?  175  MET B CA  1 
ATOM   4470 C  C   . MET B 1 173 ? 24.001  3.166   -38.666 1.00 12.93 ?  175  MET B C   1 
ATOM   4471 O  O   . MET B 1 173 ? 23.721  2.380   -37.753 1.00 15.77 ?  175  MET B O   1 
ATOM   4472 C  CB  . MET B 1 173 ? 23.845  5.614   -38.290 1.00 14.34 ?  175  MET B CB  1 
ATOM   4473 C  CG  . MET B 1 173 ? 24.469  6.991   -38.101 1.00 20.85 ?  175  MET B CG  1 
ATOM   4474 S  SD  . MET B 1 173 ? 23.510  8.346   -38.822 1.00 23.30 ?  175  MET B SD  1 
ATOM   4475 C  CE  . MET B 1 173 ? 24.754  9.633   -38.784 1.00 25.21 ?  175  MET B CE  1 
ATOM   4476 N  N   . ALA B 1 174 ? 23.611  2.971   -39.926 1.00 12.66 ?  176  ALA B N   1 
ATOM   4477 C  CA  . ALA B 1 174 ? 22.676  1.921   -40.313 1.00 10.05 ?  176  ALA B CA  1 
ATOM   4478 C  C   . ALA B 1 174 ? 23.353  0.598   -40.663 1.00 13.18 ?  176  ALA B C   1 
ATOM   4479 O  O   . ALA B 1 174 ? 22.666  -0.324  -41.116 1.00 13.75 ?  176  ALA B O   1 
ATOM   4480 C  CB  . ALA B 1 174 ? 21.833  2.395   -41.501 1.00 11.14 ?  176  ALA B CB  1 
ATOM   4481 N  N   . GLY B 1 175 ? 24.675  0.483   -40.459 1.00 12.20 ?  177  GLY B N   1 
ATOM   4482 C  CA  . GLY B 1 175 ? 25.431  -0.729  -40.745 1.00 13.82 ?  177  GLY B CA  1 
ATOM   4483 C  C   . GLY B 1 175 ? 25.836  -0.831  -42.205 1.00 12.49 ?  177  GLY B C   1 
ATOM   4484 O  O   . GLY B 1 175 ? 27.024  -0.824  -42.546 1.00 11.88 ?  177  GLY B O   1 
ATOM   4485 N  N   . TYR B 1 176 ? 24.839  -0.910  -43.079 1.00 9.42  ?  178  TYR B N   1 
ATOM   4486 C  CA  . TYR B 1 176 ? 25.043  -0.825  -44.518 1.00 12.90 ?  178  TYR B CA  1 
ATOM   4487 C  C   . TYR B 1 176 ? 23.986  0.083   -45.117 1.00 11.96 ?  178  TYR B C   1 
ATOM   4488 O  O   . TYR B 1 176 ? 22.842  0.102   -44.651 1.00 13.84 ?  178  TYR B O   1 
ATOM   4489 C  CB  . TYR B 1 176 ? 24.946  -2.185  -45.190 1.00 12.61 ?  178  TYR B CB  1 
ATOM   4490 C  CG  . TYR B 1 176 ? 26.121  -3.065  -44.868 1.00 10.02 ?  178  TYR B CG  1 
ATOM   4491 C  CD1 . TYR B 1 176 ? 27.311  -2.938  -45.559 1.00 12.12 ?  178  TYR B CD1 1 
ATOM   4492 C  CD2 . TYR B 1 176 ? 26.033  -4.021  -43.867 1.00 13.75 ?  178  TYR B CD2 1 
ATOM   4493 C  CE1 . TYR B 1 176 ? 28.403  -3.739  -45.257 1.00 15.66 ?  178  TYR B CE1 1 
ATOM   4494 C  CE2 . TYR B 1 176 ? 27.113  -4.817  -43.548 1.00 13.21 ?  178  TYR B CE2 1 
ATOM   4495 C  CZ  . TYR B 1 176 ? 28.293  -4.677  -44.254 1.00 20.87 ?  178  TYR B CZ  1 
ATOM   4496 O  OH  . TYR B 1 176 ? 29.366  -5.471  -43.963 1.00 22.57 ?  178  TYR B OH  1 
ATOM   4497 N  N   . SER B 1 177 ? 24.384  0.821   -46.151 1.00 10.68 ?  179  SER B N   1 
ATOM   4498 C  CA  . SER B 1 177 ? 23.452  1.570   -46.985 1.00 10.78 ?  179  SER B CA  1 
ATOM   4499 C  C   . SER B 1 177 ? 22.692  0.619   -47.912 1.00 13.58 ?  179  SER B C   1 
ATOM   4500 O  O   . SER B 1 177 ? 23.064  -0.540  -48.096 1.00 12.63 ?  179  SER B O   1 
ATOM   4501 C  CB  . SER B 1 177 ? 24.207  2.612   -47.815 1.00 11.75 ?  179  SER B CB  1 
ATOM   4502 O  OG  . SER B 1 177 ? 24.614  3.720   -46.997 1.00 15.29 ?  179  SER B OG  1 
ATOM   4503 N  N   . GLY B 1 178 ? 21.617  1.131   -48.505 1.00 10.76 ?  180  GLY B N   1 
ATOM   4504 C  CA  . GLY B 1 178 ? 20.862  0.424   -49.527 1.00 12.35 ?  180  GLY B CA  1 
ATOM   4505 C  C   . GLY B 1 178 ? 19.495  -0.031  -49.038 1.00 13.99 ?  180  GLY B C   1 
ATOM   4506 O  O   . GLY B 1 178 ? 19.086  0.210   -47.901 1.00 14.18 ?  180  GLY B O   1 
ATOM   4507 N  N   . GLY B 1 179 ? 18.772  -0.689  -49.947 1.00 14.30 ?  181  GLY B N   1 
ATOM   4508 C  CA  . GLY B 1 179 ? 17.499  -1.275  -49.569 1.00 13.49 ?  181  GLY B CA  1 
ATOM   4509 C  C   . GLY B 1 179 ? 16.539  -0.279  -48.936 1.00 10.04 ?  181  GLY B C   1 
ATOM   4510 O  O   . GLY B 1 179 ? 16.260  0.797   -49.481 1.00 11.64 ?  181  GLY B O   1 
ATOM   4511 N  N   . ARG B 1 180 ? 16.052  -0.670  -47.755 1.00 13.30 ?  182  ARG B N   1 
ATOM   4512 C  CA  A ARG B 1 180 ? 15.097  0.119   -46.981 0.50 15.34 ?  182  ARG B CA  1 
ATOM   4513 C  CA  B ARG B 1 180 ? 15.109  0.112   -46.958 0.50 15.35 ?  182  ARG B CA  1 
ATOM   4514 C  C   . ARG B 1 180 ? 15.532  1.556   -46.741 1.00 15.87 ?  182  ARG B C   1 
ATOM   4515 O  O   . ARG B 1 180 ? 14.678  2.416   -46.496 1.00 14.22 ?  182  ARG B O   1 
ATOM   4516 C  CB  A ARG B 1 180 ? 14.854  -0.576  -45.636 0.50 14.00 ?  182  ARG B CB  1 
ATOM   4517 C  CB  B ARG B 1 180 ? 14.928  -0.589  -45.607 0.50 14.01 ?  182  ARG B CB  1 
ATOM   4518 C  CG  A ARG B 1 180 ? 15.965  -0.397  -44.572 0.50 14.44 ?  182  ARG B CG  1 
ATOM   4519 C  CG  B ARG B 1 180 ? 16.061  -0.372  -44.561 0.50 14.39 ?  182  ARG B CG  1 
ATOM   4520 C  CD  A ARG B 1 180 ? 17.217  -1.248  -44.873 0.50 13.54 ?  182  ARG B CD  1 
ATOM   4521 C  CD  B ARG B 1 180 ? 17.404  -1.043  -44.948 0.50 13.37 ?  182  ARG B CD  1 
ATOM   4522 N  NE  A ARG B 1 180 ? 18.270  -1.097  -43.858 0.50 14.22 ?  182  ARG B NE  1 
ATOM   4523 N  NE  B ARG B 1 180 ? 18.388  -1.008  -43.854 0.50 14.13 ?  182  ARG B NE  1 
ATOM   4524 C  CZ  A ARG B 1 180 ? 19.484  -0.591  -44.064 0.50 15.48 ?  182  ARG B CZ  1 
ATOM   4525 C  CZ  B ARG B 1 180 ? 19.657  -0.611  -43.953 0.50 15.47 ?  182  ARG B CZ  1 
ATOM   4526 N  NH1 A ARG B 1 180 ? 20.339  -0.529  -43.050 0.50 14.19 ?  182  ARG B NH1 1 
ATOM   4527 N  NH1 B ARG B 1 180 ? 20.438  -0.660  -42.879 0.50 13.89 ?  182  ARG B NH1 1 
ATOM   4528 N  NH2 A ARG B 1 180 ? 19.852  -0.150  -45.266 0.50 13.80 ?  182  ARG B NH2 1 
ATOM   4529 N  NH2 B ARG B 1 180 ? 20.145  -0.144  -45.100 0.50 12.88 ?  182  ARG B NH2 1 
ATOM   4530 N  N   . LYS B 1 181 ? 16.831  1.841   -46.798 1.00 12.75 ?  183  LYS B N   1 
ATOM   4531 C  CA  . LYS B 1 181 ? 17.296  3.164   -46.407 1.00 11.51 ?  183  LYS B CA  1 
ATOM   4532 C  C   . LYS B 1 181 ? 16.890  4.232   -47.416 1.00 13.13 ?  183  LYS B C   1 
ATOM   4533 O  O   . LYS B 1 181 ? 16.834  5.414   -47.057 1.00 13.27 ?  183  LYS B O   1 
ATOM   4534 C  CB  . LYS B 1 181 ? 18.814  3.094   -46.187 1.00 14.59 ?  183  LYS B CB  1 
ATOM   4535 C  CG  . LYS B 1 181 ? 19.435  4.246   -45.435 1.00 13.56 ?  183  LYS B CG  1 
ATOM   4536 C  CD  . LYS B 1 181 ? 20.876  3.889   -45.041 1.00 12.05 ?  183  LYS B CD  1 
ATOM   4537 C  CE  . LYS B 1 181 ? 21.430  4.957   -44.135 1.00 14.44 ?  183  LYS B CE  1 
ATOM   4538 N  NZ  . LYS B 1 181 ? 21.497  6.279   -44.823 1.00 10.31 ?  183  LYS B NZ  1 
ATOM   4539 N  N   . LEU B 1 182 ? 16.561  3.830   -48.651 1.00 13.80 ?  184  LEU B N   1 
ATOM   4540 C  CA  . LEU B 1 182 ? 15.963  4.739   -49.627 1.00 13.40 ?  184  LEU B CA  1 
ATOM   4541 C  C   . LEU B 1 182 ? 14.644  5.320   -49.137 1.00 15.52 ?  184  LEU B C   1 
ATOM   4542 O  O   . LEU B 1 182 ? 14.312  6.462   -49.477 1.00 16.42 ?  184  LEU B O   1 
ATOM   4543 C  CB  . LEU B 1 182 ? 15.743  4.020   -50.960 1.00 14.14 ?  184  LEU B CB  1 
ATOM   4544 C  CG  . LEU B 1 182 ? 16.915  4.076   -51.935 1.00 10.89 ?  184  LEU B CG  1 
ATOM   4545 C  CD1 . LEU B 1 182 ? 17.169  5.501   -52.386 1.00 9.97  ?  184  LEU B CD1 1 
ATOM   4546 C  CD2 . LEU B 1 182 ? 18.204  3.476   -51.303 1.00 12.72 ?  184  LEU B CD2 1 
ATOM   4547 N  N   . ILE B 1 183 ? 13.882  4.556   -48.357 1.00 15.18 ?  185  ILE B N   1 
ATOM   4548 C  CA  . ILE B 1 183 ? 12.636  5.065   -47.776 1.00 20.06 ?  185  ILE B CA  1 
ATOM   4549 C  C   . ILE B 1 183 ? 12.914  5.827   -46.485 1.00 17.97 ?  185  ILE B C   1 
ATOM   4550 O  O   . ILE B 1 183 ? 12.511  6.987   -46.322 1.00 17.10 ?  185  ILE B O   1 
ATOM   4551 C  CB  . ILE B 1 183 ? 11.652  3.907   -47.532 1.00 19.19 ?  185  ILE B CB  1 
ATOM   4552 C  CG1 . ILE B 1 183 ? 11.340  3.199   -48.855 1.00 18.12 ?  185  ILE B CG1 1 
ATOM   4553 C  CG2 . ILE B 1 183 ? 10.391  4.407   -46.799 1.00 19.35 ?  185  ILE B CG2 1 
ATOM   4554 C  CD1 . ILE B 1 183 ? 10.560  1.911   -48.675 1.00 26.51 ?  185  ILE B CD1 1 
ATOM   4555 N  N   . CYS B 1 184 ? 13.575  5.177   -45.537 1.00 17.09 ?  186  CYS B N   1 
ATOM   4556 C  CA  . CYS B 1 184 ? 13.912  5.824   -44.270 1.00 13.28 ?  186  CYS B CA  1 
ATOM   4557 C  C   . CYS B 1 184 ? 15.423  5.869   -44.120 1.00 13.20 ?  186  CYS B C   1 
ATOM   4558 O  O   . CYS B 1 184 ? 16.033  4.840   -43.789 1.00 14.92 ?  186  CYS B O   1 
ATOM   4559 C  CB  . CYS B 1 184 ? 13.281  5.083   -43.093 1.00 15.14 ?  186  CYS B CB  1 
ATOM   4560 S  SG  . CYS B 1 184 ? 13.581  5.884   -41.477 1.00 21.05 ?  186  CYS B SG  1 
ATOM   4561 N  N   . PRO B 1 185 ? 16.071  7.029   -44.284 1.00 13.30 ?  187  PRO B N   1 
ATOM   4562 C  CA  . PRO B 1 185 ? 15.533  8.395   -44.240 1.00 12.68 ?  187  PRO B CA  1 
ATOM   4563 C  C   . PRO B 1 185 ? 15.269  9.009   -45.608 1.00 14.33 ?  187  PRO B C   1 
ATOM   4564 O  O   . PRO B 1 185 ? 14.914  10.185  -45.664 1.00 13.05 ?  187  PRO B O   1 
ATOM   4565 C  CB  . PRO B 1 185 ? 16.674  9.200   -43.609 1.00 14.74 ?  187  PRO B CB  1 
ATOM   4566 C  CG  . PRO B 1 185 ? 17.870  8.458   -44.032 1.00 13.86 ?  187  PRO B CG  1 
ATOM   4567 C  CD  . PRO B 1 185 ? 17.524  7.015   -44.050 1.00 12.90 ?  187  PRO B CD  1 
ATOM   4568 N  N   . GLY B 1 186 ? 15.534  8.260   -46.683 1.00 14.08 ?  188  GLY B N   1 
ATOM   4569 C  CA  . GLY B 1 186 ? 15.648  8.872   -47.999 1.00 13.41 ?  188  GLY B CA  1 
ATOM   4570 C  C   . GLY B 1 186 ? 14.478  9.770   -48.374 1.00 13.26 ?  188  GLY B C   1 
ATOM   4571 O  O   . GLY B 1 186 ? 14.667  10.815  -48.996 1.00 14.87 ?  188  GLY B O   1 
ATOM   4572 N  N   . ILE B 1 187 ? 13.262  9.387   -47.994 1.00 13.02 ?  189  ILE B N   1 
ATOM   4573 C  CA  . ILE B 1 187 ? 12.095  10.222  -48.303 1.00 16.77 ?  189  ILE B CA  1 
ATOM   4574 C  C   . ILE B 1 187 ? 11.256  10.420  -47.051 1.00 19.76 ?  189  ILE B C   1 
ATOM   4575 O  O   . ILE B 1 187 ? 10.015  10.504  -47.111 1.00 15.54 ?  189  ILE B O   1 
ATOM   4576 C  CB  . ILE B 1 187 ? 11.250  9.630   -49.445 1.00 18.29 ?  189  ILE B CB  1 
ATOM   4577 C  CG1 . ILE B 1 187 ? 10.915  8.168   -49.160 1.00 16.51 ?  189  ILE B CG1 1 
ATOM   4578 C  CG2 . ILE B 1 187 ? 11.944  9.830   -50.781 1.00 18.08 ?  189  ILE B CG2 1 
ATOM   4579 C  CD1 . ILE B 1 187 ? 9.763   7.654   -50.023 1.00 21.06 ?  189  ILE B CD1 1 
ATOM   4580 N  N   . ALA B 1 188 ? 11.938  10.541  -45.915 1.00 14.85 ?  190  ALA B N   1 
ATOM   4581 C  CA  . ALA B 1 188 ? 11.300  10.685  -44.613 1.00 17.11 ?  190  ALA B CA  1 
ATOM   4582 C  C   . ALA B 1 188 ? 11.398  12.125  -44.132 1.00 16.81 ?  190  ALA B C   1 
ATOM   4583 O  O   . ALA B 1 188 ? 12.360  12.838  -44.434 1.00 16.76 ?  190  ALA B O   1 
ATOM   4584 C  CB  . ALA B 1 188 ? 11.939  9.746   -43.586 1.00 16.96 ?  190  ALA B CB  1 
ATOM   4585 N  N   . ALA B 1 189 ? 10.390  12.554  -43.371 1.00 17.68 ?  191  ALA B N   1 
ATOM   4586 C  CA  . ALA B 1 189 ? 10.390  13.929  -42.905 1.00 16.00 ?  191  ALA B CA  1 
ATOM   4587 C  C   . ALA B 1 189 ? 11.327  14.091  -41.707 1.00 18.70 ?  191  ALA B C   1 
ATOM   4588 O  O   . ALA B 1 189 ? 11.631  13.141  -40.988 1.00 19.13 ?  191  ALA B O   1 
ATOM   4589 C  CB  . ALA B 1 189 ? 8.977   14.387  -42.525 1.00 22.22 ?  191  ALA B CB  1 
ATOM   4590 N  N   . PHE B 1 190 ? 11.762  15.331  -41.491 1.00 17.33 ?  192  PHE B N   1 
ATOM   4591 C  CA  . PHE B 1 190 ? 12.549  15.657  -40.304 1.00 18.11 ?  192  PHE B CA  1 
ATOM   4592 C  C   . PHE B 1 190 ? 11.861  15.196  -39.018 1.00 23.83 ?  192  PHE B C   1 
ATOM   4593 O  O   . PHE B 1 190 ? 12.524  14.753  -38.074 1.00 20.08 ?  192  PHE B O   1 
ATOM   4594 C  CB  . PHE B 1 190 ? 12.818  17.163  -40.275 1.00 19.53 ?  192  PHE B CB  1 
ATOM   4595 C  CG  . PHE B 1 190 ? 13.681  17.607  -39.126 1.00 22.27 ?  192  PHE B CG  1 
ATOM   4596 C  CD1 . PHE B 1 190 ? 14.983  17.153  -39.010 1.00 20.53 ?  192  PHE B CD1 1 
ATOM   4597 C  CD2 . PHE B 1 190 ? 13.176  18.453  -38.151 1.00 24.55 ?  192  PHE B CD2 1 
ATOM   4598 C  CE1 . PHE B 1 190 ? 15.780  17.558  -37.947 1.00 22.30 ?  192  PHE B CE1 1 
ATOM   4599 C  CE2 . PHE B 1 190 ? 13.963  18.858  -37.082 1.00 28.09 ?  192  PHE B CE2 1 
ATOM   4600 C  CZ  . PHE B 1 190 ? 15.266  18.411  -36.980 1.00 27.57 ?  192  PHE B CZ  1 
ATOM   4601 N  N   . GLU B 1 191 ? 10.525  15.281  -38.960 1.00 24.01 ?  193  GLU B N   1 
ATOM   4602 C  CA  . GLU B 1 191 ? 9.821   14.817  -37.763 1.00 20.67 ?  193  GLU B CA  1 
ATOM   4603 C  C   . GLU B 1 191 ? 10.095  13.341  -37.490 1.00 23.35 ?  193  GLU B C   1 
ATOM   4604 O  O   . GLU B 1 191 ? 10.067  12.905  -36.330 1.00 23.90 ?  193  GLU B O   1 
ATOM   4605 C  CB  . GLU B 1 191 ? 8.313   15.076  -37.898 1.00 28.64 ?  193  GLU B CB  1 
ATOM   4606 C  CG  . GLU B 1 191 ? 7.945   16.552  -38.050 1.00 25.41 ?  193  GLU B CG  1 
ATOM   4607 C  CD  . GLU B 1 191 ? 8.584   17.437  -36.988 1.00 40.29 ?  193  GLU B CD  1 
ATOM   4608 O  OE1 . GLU B 1 191 ? 8.431   17.120  -35.789 1.00 42.00 ?  193  GLU B OE1 1 
ATOM   4609 O  OE2 . GLU B 1 191 ? 9.240   18.445  -37.349 1.00 41.04 ?  193  GLU B OE2 1 
ATOM   4610 N  N   . THR B 1 192 ? 10.381  12.562  -38.541 1.00 20.95 ?  194  THR B N   1 
ATOM   4611 C  CA  . THR B 1 192 ? 10.792  11.176  -38.363 1.00 18.18 ?  194  THR B CA  1 
ATOM   4612 C  C   . THR B 1 192 ? 12.294  11.078  -38.100 1.00 14.08 ?  194  THR B C   1 
ATOM   4613 O  O   . THR B 1 192 ? 12.713  10.431  -37.136 1.00 21.75 ?  194  THR B O   1 
ATOM   4614 C  CB  . THR B 1 192 ? 10.408  10.359  -39.600 1.00 21.78 ?  194  THR B CB  1 
ATOM   4615 O  OG1 . THR B 1 192 ? 8.990   10.421  -39.784 1.00 21.56 ?  194  THR B OG1 1 
ATOM   4616 C  CG2 . THR B 1 192 ? 10.837  8.901   -39.448 1.00 19.78 ?  194  THR B CG2 1 
ATOM   4617 N  N   . VAL B 1 193 ? 13.106  11.757  -38.921 1.00 18.64 ?  195  VAL B N   1 
ATOM   4618 C  CA  . VAL B 1 193 ? 14.562  11.562  -38.906 1.00 18.41 ?  195  VAL B CA  1 
ATOM   4619 C  C   . VAL B 1 193 ? 15.196  12.111  -37.625 1.00 20.52 ?  195  VAL B C   1 
ATOM   4620 O  O   . VAL B 1 193 ? 16.178  11.552  -37.117 1.00 14.88 ?  195  VAL B O   1 
ATOM   4621 C  CB  . VAL B 1 193 ? 15.203  12.195  -40.160 1.00 14.73 ?  195  VAL B CB  1 
ATOM   4622 C  CG1 . VAL B 1 193 ? 16.728  12.008  -40.154 1.00 14.88 ?  195  VAL B CG1 1 
ATOM   4623 C  CG2 . VAL B 1 193 ? 14.609  11.600  -41.441 1.00 13.97 ?  195  VAL B CG2 1 
ATOM   4624 N  N   . LYS B 1 194 ? 14.682  13.228  -37.100 1.00 22.99 ?  196  LYS B N   1 
ATOM   4625 C  CA  . LYS B 1 194 ? 15.294  13.817  -35.909 1.00 22.41 ?  196  LYS B CA  1 
ATOM   4626 C  C   . LYS B 1 194 ? 15.250  12.852  -34.731 1.00 20.01 ?  196  LYS B C   1 
ATOM   4627 O  O   . LYS B 1 194 ? 16.147  12.866  -33.879 1.00 20.33 ?  196  LYS B O   1 
ATOM   4628 C  CB  . LYS B 1 194 ? 14.599  15.133  -35.547 1.00 25.65 ?  196  LYS B CB  1 
ATOM   4629 C  CG  . LYS B 1 194 ? 13.257  14.960  -34.851 1.00 27.40 ?  196  LYS B CG  1 
ATOM   4630 C  CD  . LYS B 1 194 ? 12.462  16.260  -34.819 1.00 28.60 ?  196  LYS B CD  1 
ATOM   4631 C  CE  . LYS B 1 194 ? 11.337  16.189  -33.796 1.00 32.08 ?  196  LYS B CE  1 
ATOM   4632 N  NZ  . LYS B 1 194 ? 10.678  17.513  -33.617 1.00 39.26 ?  196  LYS B NZ  1 
ATOM   4633 N  N   . LEU B 1 195 ? 14.230  12.000  -34.674 1.00 20.17 ?  197  LEU B N   1 
ATOM   4634 C  CA  . LEU B 1 195 ? 14.121  11.013  -33.613 1.00 22.79 ?  197  LEU B CA  1 
ATOM   4635 C  C   . LEU B 1 195 ? 14.882  9.737   -33.952 1.00 18.21 ?  197  LEU B C   1 
ATOM   4636 O  O   . LEU B 1 195 ? 15.526  9.147   -33.081 1.00 20.01 ?  197  LEU B O   1 
ATOM   4637 C  CB  . LEU B 1 195 ? 12.641  10.706  -33.344 1.00 23.71 ?  197  LEU B CB  1 
ATOM   4638 C  CG  . LEU B 1 195 ? 11.815  11.905  -32.853 1.00 24.39 ?  197  LEU B CG  1 
ATOM   4639 C  CD1 . LEU B 1 195 ? 10.388  11.486  -32.537 1.00 25.07 ?  197  LEU B CD1 1 
ATOM   4640 C  CD2 . LEU B 1 195 ? 12.467  12.515  -31.611 1.00 23.55 ?  197  LEU B CD2 1 
ATOM   4641 N  N   . TRP B 1 196 ? 14.819  9.299   -35.210 1.00 17.14 ?  198  TRP B N   1 
ATOM   4642 C  CA  . TRP B 1 196 ? 15.549  8.101   -35.605 1.00 16.97 ?  198  TRP B CA  1 
ATOM   4643 C  C   . TRP B 1 196 ? 17.058  8.342   -35.574 1.00 16.96 ?  198  TRP B C   1 
ATOM   4644 O  O   . TRP B 1 196 ? 17.812  7.469   -35.138 1.00 20.24 ?  198  TRP B O   1 
ATOM   4645 C  CB  . TRP B 1 196 ? 15.080  7.650   -36.984 1.00 17.58 ?  198  TRP B CB  1 
ATOM   4646 C  CG  . TRP B 1 196 ? 15.805  6.492   -37.567 1.00 14.59 ?  198  TRP B CG  1 
ATOM   4647 C  CD1 . TRP B 1 196 ? 15.813  5.199   -37.115 1.00 21.67 ?  198  TRP B CD1 1 
ATOM   4648 C  CD2 . TRP B 1 196 ? 16.611  6.514   -38.749 1.00 15.72 ?  198  TRP B CD2 1 
ATOM   4649 N  NE1 . TRP B 1 196 ? 16.594  4.413   -37.952 1.00 17.39 ?  198  TRP B NE1 1 
ATOM   4650 C  CE2 . TRP B 1 196 ? 17.095  5.201   -38.956 1.00 16.80 ?  198  TRP B CE2 1 
ATOM   4651 C  CE3 . TRP B 1 196 ? 16.979  7.520   -39.650 1.00 16.38 ?  198  TRP B CE3 1 
ATOM   4652 C  CZ2 . TRP B 1 196 ? 17.915  4.871   -40.033 1.00 15.71 ?  198  TRP B CZ2 1 
ATOM   4653 C  CZ3 . TRP B 1 196 ? 17.801  7.191   -40.718 1.00 15.98 ?  198  TRP B CZ3 1 
ATOM   4654 C  CH2 . TRP B 1 196 ? 18.261  5.877   -40.898 1.00 17.43 ?  198  TRP B CH2 1 
ATOM   4655 N  N   . HIS B 1 197 ? 17.519  9.518   -36.011 1.00 16.04 ?  199  HIS B N   1 
ATOM   4656 C  CA  . HIS B 1 197 ? 18.934  9.854   -35.835 1.00 15.16 ?  199  HIS B CA  1 
ATOM   4657 C  C   . HIS B 1 197 ? 19.194  10.516  -34.484 1.00 16.81 ?  199  HIS B C   1 
ATOM   4658 O  O   . HIS B 1 197 ? 20.069  11.377  -34.388 1.00 15.71 ?  199  HIS B O   1 
ATOM   4659 C  CB  . HIS B 1 197 ? 19.439  10.801  -36.934 1.00 11.86 ?  199  HIS B CB  1 
ATOM   4660 C  CG  . HIS B 1 197 ? 19.796  10.119  -38.217 1.00 13.34 ?  199  HIS B CG  1 
ATOM   4661 N  ND1 . HIS B 1 197 ? 20.085  8.774   -38.291 1.00 19.83 ?  199  HIS B ND1 1 
ATOM   4662 C  CD2 . HIS B 1 197 ? 19.939  10.604  -39.474 1.00 13.79 ?  199  HIS B CD2 1 
ATOM   4663 C  CE1 . HIS B 1 197 ? 20.387  8.459   -39.540 1.00 18.07 ?  199  HIS B CE1 1 
ATOM   4664 N  NE2 . HIS B 1 197 ? 20.304  9.552   -40.280 1.00 15.39 ?  199  HIS B NE2 1 
ATOM   4665 N  N   . GLY B 1 198 ? 18.421  10.182  -33.453 1.00 18.68 ?  200  GLY B N   1 
ATOM   4666 C  CA  . GLY B 1 198 ? 18.622  10.784  -32.153 1.00 17.79 ?  200  GLY B CA  1 
ATOM   4667 C  C   . GLY B 1 198 ? 19.687  10.049  -31.366 1.00 18.36 ?  200  GLY B C   1 
ATOM   4668 O  O   . GLY B 1 198 ? 20.042  8.912   -31.684 1.00 18.67 ?  200  GLY B O   1 
ATOM   4669 N  N   . PRO B 1 199 ? 20.211  10.685  -30.309 1.00 19.05 ?  201  PRO B N   1 
ATOM   4670 C  CA  . PRO B 1 199 ? 21.243  10.027  -29.486 1.00 20.51 ?  201  PRO B CA  1 
ATOM   4671 C  C   . PRO B 1 199 ? 20.863  8.650   -28.967 1.00 19.84 ?  201  PRO B C   1 
ATOM   4672 O  O   . PRO B 1 199 ? 21.736  7.783   -28.866 1.00 20.15 ?  201  PRO B O   1 
ATOM   4673 C  CB  . PRO B 1 199 ? 21.448  11.023  -28.333 1.00 22.19 ?  201  PRO B CB  1 
ATOM   4674 C  CG  . PRO B 1 199 ? 21.068  12.343  -28.900 1.00 22.15 ?  201  PRO B CG  1 
ATOM   4675 C  CD  . PRO B 1 199 ? 19.930  12.058  -29.854 1.00 20.93 ?  201  PRO B CD  1 
ATOM   4676 N  N   . ARG B 1 200 ? 19.589  8.415   -28.634 1.00 21.67 ?  202  ARG B N   1 
ATOM   4677 C  CA  . ARG B 1 200 ? 19.208  7.100   -28.130 1.00 23.33 ?  202  ARG B CA  1 
ATOM   4678 C  C   . ARG B 1 200 ? 19.425  6.001   -29.165 1.00 19.94 ?  202  ARG B C   1 
ATOM   4679 O  O   . ARG B 1 200 ? 19.623  4.838   -28.796 1.00 21.15 ?  202  ARG B O   1 
ATOM   4680 C  CB  . ARG B 1 200 ? 17.751  7.103   -27.664 1.00 27.80 ?  202  ARG B CB  1 
ATOM   4681 C  CG  . ARG B 1 200 ? 17.595  7.499   -26.206 1.00 38.82 ?  202  ARG B CG  1 
ATOM   4682 C  CD  . ARG B 1 200 ? 16.130  7.533   -25.811 1.00 40.99 ?  202  ARG B CD  1 
ATOM   4683 N  NE  . ARG B 1 200 ? 15.372  8.505   -26.594 1.00 43.46 ?  202  ARG B NE  1 
ATOM   4684 C  CZ  . ARG B 1 200 ? 14.050  8.476   -26.731 1.00 48.33 ?  202  ARG B CZ  1 
ATOM   4685 N  NH1 . ARG B 1 200 ? 13.347  7.521   -26.138 1.00 51.47 ?  202  ARG B NH1 1 
ATOM   4686 N  NH2 . ARG B 1 200 ? 13.429  9.395   -27.463 1.00 48.75 ?  202  ARG B NH2 1 
ATOM   4687 N  N   . PHE B 1 201 ? 19.383  6.334   -30.459 1.00 15.46 ?  203  PHE B N   1 
ATOM   4688 C  CA  . PHE B 1 201 ? 19.788  5.345   -31.452 1.00 17.86 ?  203  PHE B CA  1 
ATOM   4689 C  C   . PHE B 1 201 ? 21.297  5.381   -31.698 1.00 15.47 ?  203  PHE B C   1 
ATOM   4690 O  O   . PHE B 1 201 ? 21.951  4.336   -31.713 1.00 16.47 ?  203  PHE B O   1 
ATOM   4691 C  CB  . PHE B 1 201 ? 19.043  5.568   -32.778 1.00 16.48 ?  203  PHE B CB  1 
ATOM   4692 C  CG  . PHE B 1 201 ? 17.594  5.158   -32.767 1.00 18.23 ?  203  PHE B CG  1 
ATOM   4693 C  CD1 . PHE B 1 201 ? 16.602  6.051   -32.381 1.00 22.40 ?  203  PHE B CD1 1 
ATOM   4694 C  CD2 . PHE B 1 201 ? 17.216  3.893   -33.197 1.00 23.90 ?  203  PHE B CD2 1 
ATOM   4695 C  CE1 . PHE B 1 201 ? 15.244  5.685   -32.411 1.00 21.14 ?  203  PHE B CE1 1 
ATOM   4696 C  CE2 . PHE B 1 201 ? 15.865  3.511   -33.226 1.00 18.90 ?  203  PHE B CE2 1 
ATOM   4697 C  CZ  . PHE B 1 201 ? 14.882  4.413   -32.823 1.00 23.07 ?  203  PHE B CZ  1 
ATOM   4698 N  N   . LEU B 1 202 ? 21.867  6.576   -31.907 1.00 16.08 ?  204  LEU B N   1 
ATOM   4699 C  CA  . LEU B 1 202 ? 23.225  6.670   -32.441 1.00 13.94 ?  204  LEU B CA  1 
ATOM   4700 C  C   . LEU B 1 202 ? 24.299  6.364   -31.412 1.00 18.29 ?  204  LEU B C   1 
ATOM   4701 O  O   . LEU B 1 202 ? 25.424  6.057   -31.806 1.00 17.48 ?  204  LEU B O   1 
ATOM   4702 C  CB  . LEU B 1 202 ? 23.496  8.055   -33.035 1.00 16.78 ?  204  LEU B CB  1 
ATOM   4703 C  CG  . LEU B 1 202 ? 22.564  8.420   -34.200 1.00 17.75 ?  204  LEU B CG  1 
ATOM   4704 C  CD1 . LEU B 1 202 ? 23.051  9.689   -34.865 1.00 18.20 ?  204  LEU B CD1 1 
ATOM   4705 C  CD2 . LEU B 1 202 ? 22.456  7.280   -35.198 1.00 19.84 ?  204  LEU B CD2 1 
ATOM   4706 N  N   . GLU B 1 203 ? 23.993  6.465   -30.115 1.00 18.07 ?  205  GLU B N   1 
ATOM   4707 C  CA  . GLU B 1 203 ? 24.940  6.040   -29.079 1.00 19.94 ?  205  GLU B CA  1 
ATOM   4708 C  C   . GLU B 1 203 ? 24.875  4.551   -28.768 1.00 17.77 ?  205  GLU B C   1 
ATOM   4709 O  O   . GLU B 1 203 ? 25.660  4.079   -27.939 1.00 21.51 ?  205  GLU B O   1 
ATOM   4710 C  CB  . GLU B 1 203 ? 24.726  6.861   -27.800 1.00 17.39 ?  205  GLU B CB  1 
ATOM   4711 C  CG  . GLU B 1 203 ? 24.859  8.369   -28.005 1.00 15.41 ?  205  GLU B CG  1 
ATOM   4712 C  CD  . GLU B 1 203 ? 26.268  8.775   -28.472 1.00 24.88 ?  205  GLU B CD  1 
ATOM   4713 O  OE1 . GLU B 1 203 ? 27.264  8.135   -28.039 1.00 24.05 ?  205  GLU B OE1 1 
ATOM   4714 O  OE2 . GLU B 1 203 ? 26.403  9.729   -29.262 1.00 26.38 ?  205  GLU B OE2 1 
ATOM   4715 N  N   . HIS B 1 204 ? 23.990  3.803   -29.414 1.00 16.68 ?  206  HIS B N   1 
ATOM   4716 C  CA  . HIS B 1 204 ? 24.008  2.359   -29.248 1.00 16.56 ?  206  HIS B CA  1 
ATOM   4717 C  C   . HIS B 1 204 ? 25.319  1.789   -29.785 1.00 20.94 ?  206  HIS B C   1 
ATOM   4718 O  O   . HIS B 1 204 ? 25.789  2.210   -30.851 1.00 19.67 ?  206  HIS B O   1 
ATOM   4719 C  CB  . HIS B 1 204 ? 22.822  1.708   -29.966 1.00 16.42 ?  206  HIS B CB  1 
ATOM   4720 C  CG  . HIS B 1 204 ? 22.583  0.287   -29.557 1.00 18.61 ?  206  HIS B CG  1 
ATOM   4721 N  ND1 . HIS B 1 204 ? 23.357  -0.757  -30.018 1.00 21.13 ?  206  HIS B ND1 1 
ATOM   4722 C  CD2 . HIS B 1 204 ? 21.659  -0.265  -28.734 1.00 24.56 ?  206  HIS B CD2 1 
ATOM   4723 C  CE1 . HIS B 1 204 ? 22.921  -1.890  -29.496 1.00 27.17 ?  206  HIS B CE1 1 
ATOM   4724 N  NE2 . HIS B 1 204 ? 21.890  -1.620  -28.714 1.00 22.65 ?  206  HIS B NE2 1 
ATOM   4725 N  N   . PRO B 1 205 ? 25.940  0.839   -29.074 1.00 20.47 ?  207  PRO B N   1 
ATOM   4726 C  CA  . PRO B 1 205 ? 27.234  0.303   -29.528 1.00 25.87 ?  207  PRO B CA  1 
ATOM   4727 C  C   . PRO B 1 205 ? 27.172  -0.416  -30.862 1.00 21.60 ?  207  PRO B C   1 
ATOM   4728 O  O   . PRO B 1 205 ? 28.203  -0.512  -31.537 1.00 22.85 ?  207  PRO B O   1 
ATOM   4729 C  CB  . PRO B 1 205 ? 27.629  -0.659  -28.396 1.00 24.32 ?  207  PRO B CB  1 
ATOM   4730 C  CG  . PRO B 1 205 ? 26.321  -1.012  -27.753 1.00 27.06 ?  207  PRO B CG  1 
ATOM   4731 C  CD  . PRO B 1 205 ? 25.557  0.276   -27.769 1.00 21.29 ?  207  PRO B CD  1 
ATOM   4732 N  N   . LEU B 1 206 ? 26.013  -0.929  -31.270 1.00 17.68 ?  208  LEU B N   1 
ATOM   4733 C  CA  . LEU B 1 206 ? 25.886  -1.576  -32.571 1.00 19.73 ?  208  LEU B CA  1 
ATOM   4734 C  C   . LEU B 1 206 ? 25.373  -0.640  -33.657 1.00 19.75 ?  208  LEU B C   1 
ATOM   4735 O  O   . LEU B 1 206 ? 25.145  -1.092  -34.785 1.00 15.93 ?  208  LEU B O   1 
ATOM   4736 C  CB  . LEU B 1 206 ? 24.984  -2.807  -32.486 1.00 18.24 ?  208  LEU B CB  1 
ATOM   4737 C  CG  . LEU B 1 206 ? 25.351  -3.807  -31.386 1.00 29.68 ?  208  LEU B CG  1 
ATOM   4738 C  CD1 . LEU B 1 206 ? 24.463  -5.050  -31.481 1.00 31.17 ?  208  LEU B CD1 1 
ATOM   4739 C  CD2 . LEU B 1 206 ? 26.824  -4.163  -31.456 1.00 25.20 ?  208  LEU B CD2 1 
ATOM   4740 N  N   . ALA B 1 207 ? 25.210  0.651   -33.357 1.00 17.19 ?  209  ALA B N   1 
ATOM   4741 C  CA  . ALA B 1 207 ? 24.937  1.648   -34.398 1.00 18.40 ?  209  ALA B CA  1 
ATOM   4742 C  C   . ALA B 1 207 ? 26.280  2.033   -35.013 1.00 16.75 ?  209  ALA B C   1 
ATOM   4743 O  O   . ALA B 1 207 ? 26.908  3.044   -34.666 1.00 15.92 ?  209  ALA B O   1 
ATOM   4744 C  CB  . ALA B 1 207 ? 24.181  2.846   -33.829 1.00 14.91 ?  209  ALA B CB  1 
ATOM   4745 N  N   . ASP B 1 208 ? 26.748  1.180   -35.929 1.00 13.75 ?  210  ASP B N   1 
ATOM   4746 C  CA  . ASP B 1 208 ? 28.094  1.333   -36.459 1.00 14.67 ?  210  ASP B CA  1 
ATOM   4747 C  C   . ASP B 1 208 ? 28.224  0.520   -37.740 1.00 14.50 ?  210  ASP B C   1 
ATOM   4748 O  O   . ASP B 1 208 ? 27.401  -0.353  -38.022 1.00 14.15 ?  210  ASP B O   1 
ATOM   4749 C  CB  . ASP B 1 208 ? 29.134  0.869   -35.436 1.00 17.25 ?  210  ASP B CB  1 
ATOM   4750 C  CG  . ASP B 1 208 ? 30.389  1.710   -35.456 1.00 30.29 ?  210  ASP B CG  1 
ATOM   4751 O  OD1 . ASP B 1 208 ? 30.824  2.141   -36.546 1.00 28.29 ?  210  ASP B OD1 1 
ATOM   4752 O  OD2 . ASP B 1 208 ? 30.957  1.925   -34.360 1.00 43.97 ?  210  ASP B OD2 1 
ATOM   4753 N  N   . CYS B 1 209 ? 29.294  0.795   -38.494 1.00 14.80 ?  211  CYS B N   1 
ATOM   4754 C  CA  . CYS B 1 209 ? 29.534  0.111   -39.769 1.00 11.93 ?  211  CYS B CA  1 
ATOM   4755 C  C   . CYS B 1 209 ? 29.525  -1.403  -39.620 1.00 15.76 ?  211  CYS B C   1 
ATOM   4756 O  O   . CYS B 1 209 ? 30.218  -1.966  -38.762 1.00 13.99 ?  211  CYS B O   1 
ATOM   4757 C  CB  . CYS B 1 209 ? 30.882  0.532   -40.348 1.00 22.00 ?  211  CYS B CB  1 
ATOM   4758 S  SG  . CYS B 1 209 ? 31.198  2.289   -40.353 1.00 28.33 ?  211  CYS B SG  1 
ATOM   4759 N  N   . GLY B 1 210 ? 28.776  -2.061  -40.500 1.00 14.37 ?  212  GLY B N   1 
ATOM   4760 C  CA  . GLY B 1 210 ? 28.821  -3.503  -40.626 1.00 13.38 ?  212  GLY B CA  1 
ATOM   4761 C  C   . GLY B 1 210 ? 27.802  -4.267  -39.798 1.00 17.15 ?  212  GLY B C   1 
ATOM   4762 O  O   . GLY B 1 210 ? 27.670  -5.481  -39.991 1.00 18.74 ?  212  GLY B O   1 
ATOM   4763 N  N   . PHE B 1 211 ? 27.072  -3.608  -38.896 1.00 15.55 ?  213  PHE B N   1 
ATOM   4764 C  CA  . PHE B 1 211 ? 26.120  -4.283  -38.013 1.00 18.91 ?  213  PHE B CA  1 
ATOM   4765 C  C   . PHE B 1 211 ? 24.693  -4.074  -38.501 1.00 14.84 ?  213  PHE B C   1 
ATOM   4766 O  O   . PHE B 1 211 ? 24.261  -2.931  -38.673 1.00 14.06 ?  213  PHE B O   1 
ATOM   4767 C  CB  . PHE B 1 211 ? 26.235  -3.770  -36.577 1.00 18.01 ?  213  PHE B CB  1 
ATOM   4768 C  CG  . PHE B 1 211 ? 27.527  -4.123  -35.908 1.00 16.03 ?  213  PHE B CG  1 
ATOM   4769 C  CD1 . PHE B 1 211 ? 27.733  -5.403  -35.407 1.00 18.52 ?  213  PHE B CD1 1 
ATOM   4770 C  CD2 . PHE B 1 211 ? 28.552  -3.191  -35.798 1.00 18.08 ?  213  PHE B CD2 1 
ATOM   4771 C  CE1 . PHE B 1 211 ? 28.929  -5.742  -34.776 1.00 25.43 ?  213  PHE B CE1 1 
ATOM   4772 C  CE2 . PHE B 1 211 ? 29.758  -3.526  -35.177 1.00 23.62 ?  213  PHE B CE2 1 
ATOM   4773 C  CZ  . PHE B 1 211 ? 29.949  -4.801  -34.668 1.00 22.12 ?  213  PHE B CZ  1 
ATOM   4774 N  N   . LEU B 1 212 ? 23.960  -5.179  -38.689 1.00 15.75 ?  214  LEU B N   1 
ATOM   4775 C  CA  . LEU B 1 212 ? 22.536  -5.132  -39.022 1.00 17.68 ?  214  LEU B CA  1 
ATOM   4776 C  C   . LEU B 1 212 ? 21.720  -5.759  -37.899 1.00 21.56 ?  214  LEU B C   1 
ATOM   4777 O  O   . LEU B 1 212 ? 20.990  -5.047  -37.207 1.00 18.38 ?  214  LEU B O   1 
ATOM   4778 C  CB  . LEU B 1 212 ? 22.263  -5.832  -40.359 1.00 16.30 ?  214  LEU B CB  1 
ATOM   4779 C  CG  . LEU B 1 212 ? 22.833  -5.138  -41.602 1.00 15.26 ?  214  LEU B CG  1 
ATOM   4780 C  CD1 . LEU B 1 212 ? 22.538  -5.948  -42.869 1.00 18.88 ?  214  LEU B CD1 1 
ATOM   4781 C  CD2 . LEU B 1 212 ? 22.283  -3.737  -41.746 1.00 16.95 ?  214  LEU B CD2 1 
ATOM   4782 N  N   . GLU B 1 213 ? 21.831  -7.069  -37.688 1.00 26.31 ?  215  GLU B N   1 
ATOM   4783 C  CA  . GLU B 1 213 ? 21.139  -7.709  -36.578 1.00 29.29 ?  215  GLU B CA  1 
ATOM   4784 C  C   . GLU B 1 213 ? 21.632  -7.126  -35.259 1.00 19.81 ?  215  GLU B C   1 
ATOM   4785 O  O   . GLU B 1 213 ? 22.837  -7.074  -34.997 1.00 24.18 ?  215  GLU B O   1 
ATOM   4786 C  CB  . GLU B 1 213 ? 21.361  -9.223  -36.625 1.00 35.56 ?  215  GLU B CB  1 
ATOM   4787 N  N   . GLY B 1 214 ? 20.691  -6.645  -34.446 1.00 23.19 ?  216  GLY B N   1 
ATOM   4788 C  CA  . GLY B 1 214 ? 21.005  -6.028  -33.178 1.00 24.70 ?  216  GLY B CA  1 
ATOM   4789 C  C   . GLY B 1 214 ? 21.260  -4.537  -33.236 1.00 26.49 ?  216  GLY B C   1 
ATOM   4790 O  O   . GLY B 1 214 ? 21.326  -3.895  -32.182 1.00 23.99 ?  216  GLY B O   1 
ATOM   4791 N  N   . ASN B 1 215 ? 21.414  -3.972  -34.429 1.00 24.04 ?  217  ASN B N   1 
ATOM   4792 C  CA  . ASN B 1 215 ? 21.599  -2.542  -34.614 1.00 19.78 ?  217  ASN B CA  1 
ATOM   4793 C  C   . ASN B 1 215 ? 20.226  -1.884  -34.612 1.00 16.07 ?  217  ASN B C   1 
ATOM   4794 O  O   . ASN B 1 215 ? 19.458  -2.075  -35.557 1.00 16.65 ?  217  ASN B O   1 
ATOM   4795 C  CB  . ASN B 1 215 ? 22.337  -2.263  -35.928 1.00 16.96 ?  217  ASN B CB  1 
ATOM   4796 C  CG  . ASN B 1 215 ? 22.507  -0.777  -36.209 1.00 15.60 ?  217  ASN B CG  1 
ATOM   4797 O  OD1 . ASN B 1 215 ? 22.047  0.073   -35.447 1.00 17.04 ?  217  ASN B OD1 1 
ATOM   4798 N  ND2 . ASN B 1 215 ? 23.172  -0.459  -37.320 1.00 13.37 ?  217  ASN B ND2 1 
ATOM   4799 N  N   . PRO B 1 216 ? 19.882  -1.101  -33.587 1.00 18.46 ?  218  PRO B N   1 
ATOM   4800 C  CA  . PRO B 1 216 ? 18.534  -0.508  -33.555 1.00 18.35 ?  218  PRO B CA  1 
ATOM   4801 C  C   . PRO B 1 216 ? 18.260  0.440   -34.702 1.00 18.47 ?  218  PRO B C   1 
ATOM   4802 O  O   . PRO B 1 216 ? 17.092  0.629   -35.066 1.00 16.45 ?  218  PRO B O   1 
ATOM   4803 C  CB  . PRO B 1 216 ? 18.503  0.227   -32.207 1.00 22.49 ?  218  PRO B CB  1 
ATOM   4804 C  CG  . PRO B 1 216 ? 19.935  0.506   -31.899 1.00 18.30 ?  218  PRO B CG  1 
ATOM   4805 C  CD  . PRO B 1 216 ? 20.691  -0.695  -32.426 1.00 18.78 ?  218  PRO B CD  1 
ATOM   4806 N  N   . VAL B 1 217 ? 19.297  1.060   -35.273 1.00 17.71 ?  219  VAL B N   1 
ATOM   4807 C  CA  . VAL B 1 217 ? 19.090  1.937   -36.422 1.00 14.47 ?  219  VAL B CA  1 
ATOM   4808 C  C   . VAL B 1 217 ? 18.524  1.135   -37.585 1.00 15.56 ?  219  VAL B C   1 
ATOM   4809 O  O   . VAL B 1 217 ? 17.562  1.552   -38.245 1.00 15.57 ?  219  VAL B O   1 
ATOM   4810 C  CB  . VAL B 1 217 ? 20.410  2.642   -36.802 1.00 13.22 ?  219  VAL B CB  1 
ATOM   4811 C  CG1 . VAL B 1 217 ? 20.239  3.463   -38.074 1.00 15.94 ?  219  VAL B CG1 1 
ATOM   4812 C  CG2 . VAL B 1 217 ? 20.874  3.550   -35.660 1.00 13.57 ?  219  VAL B CG2 1 
ATOM   4813 N  N   . HIS B 1 218 ? 19.085  -0.053  -37.814 1.00 15.82 ?  220  HIS B N   1 
ATOM   4814 C  CA  . HIS B 1 218 ? 18.652  -0.904  -38.913 1.00 17.37 ?  220  HIS B CA  1 
ATOM   4815 C  C   . HIS B 1 218 ? 17.272  -1.493  -38.648 1.00 17.66 ?  220  HIS B C   1 
ATOM   4816 O  O   . HIS B 1 218 ? 16.417  -1.511  -39.542 1.00 17.72 ?  220  HIS B O   1 
ATOM   4817 C  CB  . HIS B 1 218 ? 19.673  -2.019  -39.138 1.00 14.66 ?  220  HIS B CB  1 
ATOM   4818 C  CG  . HIS B 1 218 ? 19.178  -3.104  -40.043 1.00 12.84 ?  220  HIS B CG  1 
ATOM   4819 N  ND1 . HIS B 1 218 ? 18.955  -2.898  -41.387 1.00 14.91 ?  220  HIS B ND1 1 
ATOM   4820 C  CD2 . HIS B 1 218 ? 18.847  -4.393  -39.797 1.00 14.14 ?  220  HIS B CD2 1 
ATOM   4821 C  CE1 . HIS B 1 218 ? 18.524  -4.019  -41.936 1.00 16.17 ?  220  HIS B CE1 1 
ATOM   4822 N  NE2 . HIS B 1 218 ? 18.444  -4.941  -40.993 1.00 17.95 ?  220  HIS B NE2 1 
ATOM   4823 N  N   . GLU B 1 219 ? 17.036  -1.978  -37.426 1.00 18.81 ?  221  GLU B N   1 
ATOM   4824 C  CA  . GLU B 1 219 ? 15.721  -2.524  -37.092 1.00 17.93 ?  221  GLU B CA  1 
ATOM   4825 C  C   . GLU B 1 219 ? 14.626  -1.487  -37.295 1.00 20.83 ?  221  GLU B C   1 
ATOM   4826 O  O   . GLU B 1 219 ? 13.545  -1.809  -37.795 1.00 19.49 ?  221  GLU B O   1 
ATOM   4827 C  CB  . GLU B 1 219 ? 15.716  -3.061  -35.656 1.00 16.40 ?  221  GLU B CB  1 
ATOM   4828 C  CG  . GLU B 1 219 ? 16.625  -4.272  -35.503 1.00 30.17 ?  221  GLU B CG  1 
ATOM   4829 C  CD  . GLU B 1 219 ? 17.001  -4.585  -34.066 1.00 36.54 ?  221  GLU B CD  1 
ATOM   4830 O  OE1 . GLU B 1 219 ? 17.590  -5.662  -33.835 1.00 37.67 ?  221  GLU B OE1 1 
ATOM   4831 O  OE2 . GLU B 1 219 ? 16.700  -3.771  -33.171 1.00 39.78 ?  221  GLU B OE2 1 
ATOM   4832 N  N   . GLU B 1 220 ? 14.906  -0.223  -36.970 1.00 19.57 ?  222  GLU B N   1 
ATOM   4833 C  CA  . GLU B 1 220 ? 13.873  0.801   -37.066 1.00 19.39 ?  222  GLU B CA  1 
ATOM   4834 C  C   . GLU B 1 220 ? 13.629  1.253   -38.505 1.00 18.81 ?  222  GLU B C   1 
ATOM   4835 O  O   . GLU B 1 220 ? 12.471  1.408   -38.913 1.00 19.14 ?  222  GLU B O   1 
ATOM   4836 C  CB  . GLU B 1 220 ? 14.236  1.980   -36.166 1.00 21.36 ?  222  GLU B CB  1 
ATOM   4837 C  CG  . GLU B 1 220 ? 13.128  3.002   -35.993 1.00 18.04 ?  222  GLU B CG  1 
ATOM   4838 C  CD  . GLU B 1 220 ? 12.118  2.605   -34.937 1.00 25.07 ?  222  GLU B CD  1 
ATOM   4839 O  OE1 . GLU B 1 220 ? 11.225  3.424   -34.672 1.00 27.24 ?  222  GLU B OE1 1 
ATOM   4840 O  OE2 . GLU B 1 220 ? 12.202  1.478   -34.393 1.00 29.59 ?  222  GLU B OE2 1 
ATOM   4841 N  N   . ASN B 1 221 ? 14.685  1.491   -39.303 1.00 15.47 ?  223  ASN B N   1 
ATOM   4842 C  CA  . ASN B 1 221 ? 14.378  1.946   -40.658 1.00 20.08 ?  223  ASN B CA  1 
ATOM   4843 C  C   . ASN B 1 221 ? 13.824  0.820   -41.528 1.00 16.97 ?  223  ASN B C   1 
ATOM   4844 O  O   . ASN B 1 221 ? 13.083  1.099   -42.479 1.00 17.29 ?  223  ASN B O   1 
ATOM   4845 C  CB  . ASN B 1 221 ? 15.580  2.677   -41.297 1.00 15.78 ?  223  ASN B CB  1 
ATOM   4846 C  CG  . ASN B 1 221 ? 16.708  1.764   -41.786 1.00 15.34 ?  223  ASN B CG  1 
ATOM   4847 O  OD1 . ASN B 1 221 ? 16.847  0.614   -41.392 1.00 15.34 ?  223  ASN B OD1 1 
ATOM   4848 N  ND2 . ASN B 1 221 ? 17.563  2.333   -42.633 1.00 15.03 ?  223  ASN B ND2 1 
ATOM   4849 N  N   . THR B 1 222 ? 14.087  -0.441  -41.174 1.00 17.01 ?  224  THR B N   1 
ATOM   4850 C  CA  . THR B 1 222 ? 13.415  -1.548  -41.853 1.00 19.72 ?  224  THR B CA  1 
ATOM   4851 C  C   . THR B 1 222 ? 11.941  -1.602  -41.471 1.00 20.65 ?  224  THR B C   1 
ATOM   4852 O  O   . THR B 1 222 ? 11.081  -1.862  -42.320 1.00 20.07 ?  224  THR B O   1 
ATOM   4853 C  CB  . THR B 1 222 ? 14.095  -2.878  -41.519 1.00 21.01 ?  224  THR B CB  1 
ATOM   4854 O  OG1 . THR B 1 222 ? 15.465  -2.855  -41.948 1.00 15.73 ?  224  THR B OG1 1 
ATOM   4855 C  CG2 . THR B 1 222 ? 13.372  -4.042  -42.212 1.00 18.60 ?  224  THR B CG2 1 
ATOM   4856 N  N   . ARG B 1 223 ? 11.630  -1.343  -40.201 1.00 21.54 ?  225  ARG B N   1 
ATOM   4857 C  CA  . ARG B 1 223 ? 10.238  -1.313  -39.765 1.00 25.84 ?  225  ARG B CA  1 
ATOM   4858 C  C   . ARG B 1 223 ? 9.475   -0.173  -40.440 1.00 20.33 ?  225  ARG B C   1 
ATOM   4859 O  O   . ARG B 1 223 ? 8.366   -0.368  -40.952 1.00 22.99 ?  225  ARG B O   1 
ATOM   4860 C  CB  . ARG B 1 223 ? 10.191  -1.208  -38.237 1.00 24.76 ?  225  ARG B CB  1 
ATOM   4861 C  CG  . ARG B 1 223 ? 8.914   -0.668  -37.652 1.00 31.61 ?  225  ARG B CG  1 
ATOM   4862 C  CD  . ARG B 1 223 ? 8.888   -0.836  -36.124 1.00 32.42 ?  225  ARG B CD  1 
ATOM   4863 N  NE  . ARG B 1 223 ? 9.137   -2.206  -35.670 1.00 41.81 ?  225  ARG B NE  1 
ATOM   4864 C  CZ  . ARG B 1 223 ? 8.176   -3.086  -35.382 1.00 44.61 ?  225  ARG B CZ  1 
ATOM   4865 N  NH1 . ARG B 1 223 ? 6.902   -2.745  -35.513 1.00 40.08 ?  225  ARG B NH1 1 
ATOM   4866 N  NH2 . ARG B 1 223 ? 8.483   -4.310  -34.968 1.00 46.14 ?  225  ARG B NH2 1 
ATOM   4867 N  N   . ILE B 1 224 ? 10.068  1.018   -40.491 1.00 20.86 ?  226  ILE B N   1 
ATOM   4868 C  CA  . ILE B 1 224 ? 9.393   2.158   -41.105 1.00 21.25 ?  226  ILE B CA  1 
ATOM   4869 C  C   . ILE B 1 224 ? 9.205   1.946   -42.607 1.00 25.23 ?  226  ILE B C   1 
ATOM   4870 O  O   . ILE B 1 224 ? 8.157   2.296   -43.171 1.00 21.13 ?  226  ILE B O   1 
ATOM   4871 C  CB  . ILE B 1 224 ? 10.172  3.446   -40.790 1.00 19.29 ?  226  ILE B CB  1 
ATOM   4872 C  CG1 . ILE B 1 224 ? 9.991   3.803   -39.306 1.00 20.76 ?  226  ILE B CG1 1 
ATOM   4873 C  CG2 . ILE B 1 224 ? 9.756   4.577   -41.715 1.00 17.62 ?  226  ILE B CG2 1 
ATOM   4874 C  CD1 . ILE B 1 224 ? 11.009  4.799   -38.767 1.00 20.27 ?  226  ILE B CD1 1 
ATOM   4875 N  N   . ALA B 1 225 ? 10.201  1.362   -43.284 1.00 22.23 ?  227  ALA B N   1 
ATOM   4876 C  CA  . ALA B 1 225 ? 10.034  1.111   -44.714 1.00 20.55 ?  227  ALA B CA  1 
ATOM   4877 C  C   . ALA B 1 225 ? 8.944   0.080   -44.976 1.00 18.56 ?  227  ALA B C   1 
ATOM   4878 O  O   . ALA B 1 225 ? 8.252   0.158   -45.998 1.00 26.80 ?  227  ALA B O   1 
ATOM   4879 C  CB  . ALA B 1 225 ? 11.345  0.643   -45.343 1.00 19.86 ?  227  ALA B CB  1 
ATOM   4880 N  N   . ARG B 1 226 ? 8.788   -0.900  -44.084 1.00 22.41 ?  228  ARG B N   1 
ATOM   4881 C  CA  . ARG B 1 226 ? 7.737   -1.896  -44.275 1.00 26.43 ?  228  ARG B CA  1 
ATOM   4882 C  C   . ARG B 1 226 ? 6.354   -1.309  -44.021 1.00 28.92 ?  228  ARG B C   1 
ATOM   4883 O  O   . ARG B 1 226 ? 5.383   -1.754  -44.643 1.00 26.57 ?  228  ARG B O   1 
ATOM   4884 C  CB  . ARG B 1 226 ? 7.990   -3.116  -43.384 1.00 26.16 ?  228  ARG B CB  1 
ATOM   4885 C  CG  . ARG B 1 226 ? 8.993   -4.127  -43.967 1.00 31.36 ?  228  ARG B CG  1 
ATOM   4886 C  CD  . ARG B 1 226 ? 8.803   -4.351  -45.484 1.00 40.21 ?  228  ARG B CD  1 
ATOM   4887 N  NE  . ARG B 1 226 ? 9.310   -5.650  -45.944 1.00 35.04 ?  228  ARG B NE  1 
ATOM   4888 C  CZ  . ARG B 1 226 ? 9.433   -5.998  -47.226 1.00 37.70 ?  228  ARG B CZ  1 
ATOM   4889 N  NH1 . ARG B 1 226 ? 9.058   -5.160  -48.189 1.00 32.47 ?  228  ARG B NH1 1 
ATOM   4890 N  NH2 . ARG B 1 226 ? 9.925   -7.187  -47.554 1.00 29.62 ?  228  ARG B NH2 1 
ATOM   4891 N  N   . MET B 1 227 ? 6.233   -0.317  -43.124 1.00 25.54 ?  229  MET B N   1 
ATOM   4892 C  CA  . MET B 1 227 ? 4.957   0.391   -43.001 1.00 29.07 ?  229  MET B CA  1 
ATOM   4893 C  C   . MET B 1 227 ? 4.626   1.185   -44.256 1.00 26.81 ?  229  MET B C   1 
ATOM   4894 O  O   . MET B 1 227 ? 3.447   1.338   -44.598 1.00 26.28 ?  229  MET B O   1 
ATOM   4895 C  CB  . MET B 1 227 ? 4.944   1.340   -41.796 1.00 22.67 ?  229  MET B CB  1 
ATOM   4896 C  CG  . MET B 1 227 ? 5.382   0.773   -40.466 1.00 22.82 ?  229  MET B CG  1 
ATOM   4897 S  SD  . MET B 1 227 ? 5.764   2.130   -39.315 1.00 31.50 ?  229  MET B SD  1 
ATOM   4898 C  CE  . MET B 1 227 ? 4.166   2.935   -39.136 1.00 28.86 ?  229  MET B CE  1 
ATOM   4899 N  N   . ALA B 1 228 ? 5.640   1.715   -44.943 1.00 25.84 ?  230  ALA B N   1 
ATOM   4900 C  CA  . ALA B 1 228 ? 5.394   2.436   -46.185 1.00 22.12 ?  230  ALA B CA  1 
ATOM   4901 C  C   . ALA B 1 228 ? 5.186   1.492   -47.360 1.00 25.75 ?  230  ALA B C   1 
ATOM   4902 O  O   . ALA B 1 228 ? 4.445   1.822   -48.294 1.00 26.67 ?  230  ALA B O   1 
ATOM   4903 C  CB  . ALA B 1 228 ? 6.554   3.387   -46.483 1.00 27.08 ?  230  ALA B CB  1 
ATOM   4904 N  N   . GLY B 1 229 ? 5.827   0.329   -47.330 1.00 23.52 ?  231  GLY B N   1 
ATOM   4905 C  CA  . GLY B 1 229 ? 5.765   -0.613  -48.425 1.00 25.47 ?  231  GLY B CA  1 
ATOM   4906 C  C   . GLY B 1 229 ? 6.794   -0.359  -49.508 1.00 22.68 ?  231  GLY B C   1 
ATOM   4907 O  O   . GLY B 1 229 ? 7.177   0.787   -49.778 1.00 22.82 ?  231  GLY B O   1 
ATOM   4908 N  N   . CYS B 1 230 ? 7.240   -1.439  -50.138 1.00 23.73 ?  232  CYS B N   1 
ATOM   4909 C  CA  . CYS B 1 230 ? 8.160   -1.369  -51.267 1.00 24.49 ?  232  CYS B CA  1 
ATOM   4910 C  C   . CYS B 1 230 ? 7.961   -2.620  -52.108 1.00 20.10 ?  232  CYS B C   1 
ATOM   4911 O  O   . CYS B 1 230 ? 8.095   -3.735  -51.596 1.00 28.18 ?  232  CYS B O   1 
ATOM   4912 C  CB  . CYS B 1 230 ? 9.611   -1.259  -50.786 1.00 21.23 ?  232  CYS B CB  1 
ATOM   4913 S  SG  . CYS B 1 230 ? 10.770  -1.022  -52.162 1.00 24.25 ?  232  CYS B SG  1 
ATOM   4914 N  N   . ASP B 1 231 ? 7.630   -2.448  -53.387 1.00 23.43 ?  233  ASP B N   1 
ATOM   4915 C  CA  . ASP B 1 231 ? 7.342   -3.623  -54.200 1.00 25.98 ?  233  ASP B CA  1 
ATOM   4916 C  C   . ASP B 1 231 ? 8.605   -4.256  -54.783 1.00 30.31 ?  233  ASP B C   1 
ATOM   4917 O  O   . ASP B 1 231 ? 8.656   -5.486  -54.930 1.00 21.45 ?  233  ASP B O   1 
ATOM   4918 C  CB  . ASP B 1 231 ? 6.351   -3.268  -55.315 1.00 24.53 ?  233  ASP B CB  1 
ATOM   4919 C  CG  . ASP B 1 231 ? 5.057   -2.652  -54.775 1.00 25.91 ?  233  ASP B CG  1 
ATOM   4920 O  OD1 . ASP B 1 231 ? 4.400   -3.306  -53.939 1.00 32.30 ?  233  ASP B OD1 1 
ATOM   4921 O  OD2 . ASP B 1 231 ? 4.701   -1.524  -55.176 1.00 23.45 ?  233  ASP B OD2 1 
ATOM   4922 N  N   . PHE B 1 232 ? 9.636   -3.461  -55.079 1.00 21.30 ?  234  PHE B N   1 
ATOM   4923 C  CA  . PHE B 1 232 ? 10.786  -3.971  -55.816 1.00 18.29 ?  234  PHE B CA  1 
ATOM   4924 C  C   . PHE B 1 232 ? 12.001  -3.079  -55.578 1.00 17.28 ?  234  PHE B C   1 
ATOM   4925 O  O   . PHE B 1 232 ? 11.889  -1.852  -55.624 1.00 14.96 ?  234  PHE B O   1 
ATOM   4926 C  CB  . PHE B 1 232 ? 10.459  -4.036  -57.311 1.00 18.10 ?  234  PHE B CB  1 
ATOM   4927 C  CG  . PHE B 1 232 ? 11.283  -5.029  -58.073 1.00 18.40 ?  234  PHE B CG  1 
ATOM   4928 C  CD1 . PHE B 1 232 ? 10.989  -6.379  -57.999 1.00 23.50 ?  234  PHE B CD1 1 
ATOM   4929 C  CD2 . PHE B 1 232 ? 12.319  -4.614  -58.896 1.00 21.91 ?  234  PHE B CD2 1 
ATOM   4930 C  CE1 . PHE B 1 232 ? 11.722  -7.304  -58.709 1.00 22.04 ?  234  PHE B CE1 1 
ATOM   4931 C  CE2 . PHE B 1 232 ? 13.063  -5.537  -59.602 1.00 19.92 ?  234  PHE B CE2 1 
ATOM   4932 C  CZ  . PHE B 1 232 ? 12.762  -6.881  -59.513 1.00 19.40 ?  234  PHE B CZ  1 
ATOM   4933 N  N   . ILE B 1 233 ? 13.167  -3.689  -55.352 1.00 17.89 ?  235  ILE B N   1 
ATOM   4934 C  CA  . ILE B 1 233 ? 14.399  -2.903  -55.312 1.00 17.26 ?  235  ILE B CA  1 
ATOM   4935 C  C   . ILE B 1 233 ? 15.395  -3.413  -56.353 1.00 15.26 ?  235  ILE B C   1 
ATOM   4936 O  O   . ILE B 1 233 ? 15.350  -4.561  -56.789 1.00 15.49 ?  235  ILE B O   1 
ATOM   4937 C  CB  . ILE B 1 233 ? 15.052  -2.896  -53.916 1.00 17.84 ?  235  ILE B CB  1 
ATOM   4938 C  CG1 . ILE B 1 233 ? 15.610  -4.266  -53.563 1.00 18.88 ?  235  ILE B CG1 1 
ATOM   4939 C  CG2 . ILE B 1 233 ? 14.065  -2.475  -52.852 1.00 17.86 ?  235  ILE B CG2 1 
ATOM   4940 C  CD1 . ILE B 1 233 ? 16.587  -4.209  -52.386 1.00 14.22 ?  235  ILE B CD1 1 
ATOM   4941 N  N   . VAL B 1 234 ? 16.317  -2.530  -56.742 1.00 14.72 ?  236  VAL B N   1 
ATOM   4942 C  CA  . VAL B 1 234 ? 17.540  -2.913  -57.452 1.00 16.63 ?  236  VAL B CA  1 
ATOM   4943 C  C   . VAL B 1 234 ? 18.713  -2.227  -56.759 1.00 12.78 ?  236  VAL B C   1 
ATOM   4944 O  O   . VAL B 1 234 ? 18.778  -0.995  -56.730 1.00 12.37 ?  236  VAL B O   1 
ATOM   4945 C  CB  . VAL B 1 234 ? 17.510  -2.525  -58.938 1.00 19.52 ?  236  VAL B CB  1 
ATOM   4946 C  CG1 . VAL B 1 234 ? 18.751  -3.093  -59.647 1.00 15.27 ?  236  VAL B CG1 1 
ATOM   4947 C  CG2 . VAL B 1 234 ? 16.243  -3.036  -59.609 1.00 16.61 ?  236  VAL B CG2 1 
ATOM   4948 N  N   . ASN B 1 235 ? 19.639  -3.014  -56.211 1.00 14.19 ?  237  ASN B N   1 
ATOM   4949 C  CA  . ASN B 1 235 ? 20.824  -2.479  -55.545 1.00 12.92 ?  237  ASN B CA  1 
ATOM   4950 C  C   . ASN B 1 235 ? 22.080  -3.068  -56.187 1.00 12.05 ?  237  ASN B C   1 
ATOM   4951 O  O   . ASN B 1 235 ? 22.082  -4.226  -56.623 1.00 13.55 ?  237  ASN B O   1 
ATOM   4952 C  CB  . ASN B 1 235 ? 20.847  -2.830  -54.042 1.00 10.61 ?  237  ASN B CB  1 
ATOM   4953 C  CG  . ASN B 1 235 ? 19.893  -1.977  -53.192 1.00 13.70 ?  237  ASN B CG  1 
ATOM   4954 O  OD1 . ASN B 1 235 ? 19.886  -2.108  -51.969 1.00 14.71 ?  237  ASN B OD1 1 
ATOM   4955 N  ND2 . ASN B 1 235 ? 19.099  -1.110  -53.826 1.00 13.64 ?  237  ASN B ND2 1 
ATOM   4956 N  N   . VAL B 1 236 ? 23.170  -2.292  -56.199 1.00 12.99 ?  238  VAL B N   1 
ATOM   4957 C  CA  . VAL B 1 236 ? 24.446  -2.777  -56.716 1.00 10.87 ?  238  VAL B CA  1 
ATOM   4958 C  C   . VAL B 1 236 ? 25.508  -2.633  -55.634 1.00 14.75 ?  238  VAL B C   1 
ATOM   4959 O  O   . VAL B 1 236 ? 25.347  -1.886  -54.664 1.00 11.83 ?  238  VAL B O   1 
ATOM   4960 C  CB  . VAL B 1 236 ? 24.910  -2.027  -57.990 1.00 13.50 ?  238  VAL B CB  1 
ATOM   4961 C  CG1 . VAL B 1 236 ? 23.875  -2.167  -59.121 1.00 13.26 ?  238  VAL B CG1 1 
ATOM   4962 C  CG2 . VAL B 1 236 ? 25.205  -0.552  -57.681 1.00 16.23 ?  238  VAL B CG2 1 
ATOM   4963 N  N   . THR B 1 237 ? 26.611  -3.363  -55.823 1.00 10.29 ?  239  THR B N   1 
ATOM   4964 C  CA  . THR B 1 237 ? 27.859  -3.122  -55.103 1.00 12.81 ?  239  THR B CA  1 
ATOM   4965 C  C   . THR B 1 237 ? 28.920  -2.676  -56.103 1.00 15.89 ?  239  THR B C   1 
ATOM   4966 O  O   . THR B 1 237 ? 28.845  -3.008  -57.294 1.00 13.39 ?  239  THR B O   1 
ATOM   4967 C  CB  . THR B 1 237 ? 28.349  -4.357  -54.375 1.00 15.65 ?  239  THR B CB  1 
ATOM   4968 O  OG1 . THR B 1 237 ? 28.537  -5.424  -55.310 1.00 16.19 ?  239  THR B OG1 1 
ATOM   4969 C  CG2 . THR B 1 237 ? 27.342  -4.792  -53.305 1.00 17.01 ?  239  THR B CG2 1 
ATOM   4970 N  N   . LEU B 1 238 ? 29.895  -1.902  -55.623 1.00 11.87 ?  240  LEU B N   1 
ATOM   4971 C  CA  . LEU B 1 238 ? 30.937  -1.334  -56.466 1.00 12.31 ?  240  LEU B CA  1 
ATOM   4972 C  C   . LEU B 1 238 ? 32.306  -1.731  -55.932 1.00 19.86 ?  240  LEU B C   1 
ATOM   4973 O  O   . LEU B 1 238 ? 32.501  -1.822  -54.719 1.00 18.66 ?  240  LEU B O   1 
ATOM   4974 C  CB  . LEU B 1 238 ? 30.856  0.194   -56.497 1.00 10.33 ?  240  LEU B CB  1 
ATOM   4975 C  CG  . LEU B 1 238 ? 29.549  0.819   -57.020 1.00 14.33 ?  240  LEU B CG  1 
ATOM   4976 C  CD1 . LEU B 1 238 ? 29.636  2.331   -56.950 1.00 14.58 ?  240  LEU B CD1 1 
ATOM   4977 C  CD2 . LEU B 1 238 ? 29.287  0.358   -58.440 1.00 18.54 ?  240  LEU B CD2 1 
ATOM   4978 N  N   . ASP B 1 239 ? 33.270  -1.926  -56.828 1.00 13.53 ?  241  ASP B N   1 
ATOM   4979 C  CA  . ASP B 1 239 ? 34.629  -2.131  -56.337 1.00 15.48 ?  241  ASP B CA  1 
ATOM   4980 C  C   . ASP B 1 239 ? 35.334  -0.781  -56.167 1.00 17.10 ?  241  ASP B C   1 
ATOM   4981 O  O   . ASP B 1 239 ? 34.731  0.288   -56.299 1.00 14.19 ?  241  ASP B O   1 
ATOM   4982 C  CB  . ASP B 1 239 ? 35.406  -3.109  -57.229 1.00 17.56 ?  241  ASP B CB  1 
ATOM   4983 C  CG  . ASP B 1 239 ? 35.658  -2.596  -58.649 1.00 18.15 ?  241  ASP B CG  1 
ATOM   4984 O  OD1 . ASP B 1 239 ? 35.570  -1.382  -58.927 1.00 18.52 ?  241  ASP B OD1 1 
ATOM   4985 O  OD2 . ASP B 1 239 ? 36.025  -3.440  -59.497 1.00 23.70 ?  241  ASP B OD2 1 
ATOM   4986 N  N   . GLY B 1 240 ? 36.634  -0.813  -55.846 1.00 16.67 ?  242  GLY B N   1 
ATOM   4987 C  CA  . GLY B 1 240 ? 37.358  0.430   -55.614 1.00 17.83 ?  242  GLY B CA  1 
ATOM   4988 C  C   . GLY B 1 240 ? 37.441  1.324   -56.837 1.00 21.66 ?  242  GLY B C   1 
ATOM   4989 O  O   . GLY B 1 240 ? 37.538  2.550   -56.711 1.00 22.21 ?  242  GLY B O   1 
ATOM   4990 N  N   . ALA B 1 241 ? 37.421  0.734   -58.031 1.00 15.51 ?  243  ALA B N   1 
ATOM   4991 C  CA  . ALA B 1 241 ? 37.456  1.502   -59.264 1.00 15.96 ?  243  ALA B CA  1 
ATOM   4992 C  C   . ALA B 1 241 ? 36.054  1.889   -59.746 1.00 16.61 ?  243  ALA B C   1 
ATOM   4993 O  O   . ALA B 1 241 ? 35.904  2.342   -60.887 1.00 19.38 ?  243  ALA B O   1 
ATOM   4994 C  CB  . ALA B 1 241 ? 38.215  0.718   -60.336 1.00 18.96 ?  243  ALA B CB  1 
ATOM   4995 N  N   . ARG B 1 242 ? 35.034  1.720   -58.893 1.00 15.90 ?  244  ARG B N   1 
ATOM   4996 C  CA  . ARG B 1 242 ? 33.637  2.080   -59.176 1.00 17.56 ?  244  ARG B CA  1 
ATOM   4997 C  C   . ARG B 1 242 ? 33.002  1.217   -60.263 1.00 18.33 ?  244  ARG B C   1 
ATOM   4998 O  O   . ARG B 1 242 ? 32.051  1.645   -60.927 1.00 18.92 ?  244  ARG B O   1 
ATOM   4999 C  CB  . ARG B 1 242 ? 33.482  3.563   -59.534 1.00 24.84 ?  244  ARG B CB  1 
ATOM   5000 C  CG  . ARG B 1 242 ? 34.119  4.508   -58.510 1.00 21.98 ?  244  ARG B CG  1 
ATOM   5001 C  CD  . ARG B 1 242 ? 33.203  4.698   -57.305 1.00 20.91 ?  244  ARG B CD  1 
ATOM   5002 N  NE  . ARG B 1 242 ? 33.862  5.466   -56.242 1.00 20.15 ?  244  ARG B NE  1 
ATOM   5003 C  CZ  . ARG B 1 242 ? 33.832  6.791   -56.147 1.00 20.24 ?  244  ARG B CZ  1 
ATOM   5004 N  NH1 . ARG B 1 242 ? 33.173  7.510   -57.047 1.00 16.41 ?  244  ARG B NH1 1 
ATOM   5005 N  NH2 . ARG B 1 242 ? 34.473  7.405   -55.155 1.00 18.23 ?  244  ARG B NH2 1 
ATOM   5006 N  N   . ARG B 1 243 ? 33.463  -0.012  -60.427 1.00 17.67 ?  245  ARG B N   1 
ATOM   5007 C  CA  . ARG B 1 243 ? 32.822  -0.949  -61.340 1.00 13.80 ?  245  ARG B CA  1 
ATOM   5008 C  C   . ARG B 1 243 ? 31.857  -1.847  -60.571 1.00 14.25 ?  245  ARG B C   1 
ATOM   5009 O  O   . ARG B 1 243 ? 32.131  -2.250  -59.439 1.00 12.85 ?  245  ARG B O   1 
ATOM   5010 C  CB  . ARG B 1 243 ? 33.873  -1.790  -62.068 1.00 16.46 ?  245  ARG B CB  1 
ATOM   5011 C  CG  . ARG B 1 243 ? 34.993  -0.946  -62.646 1.00 19.03 ?  245  ARG B CG  1 
ATOM   5012 C  CD  . ARG B 1 243 ? 36.133  -1.802  -63.170 1.00 25.13 ?  245  ARG B CD  1 
ATOM   5013 N  NE  . ARG B 1 243 ? 36.824  -2.524  -62.104 1.00 22.96 ?  245  ARG B NE  1 
ATOM   5014 C  CZ  . ARG B 1 243 ? 37.992  -3.136  -62.270 1.00 23.73 ?  245  ARG B CZ  1 
ATOM   5015 N  NH1 . ARG B 1 243 ? 38.584  -3.102  -63.456 1.00 25.90 ?  245  ARG B NH1 1 
ATOM   5016 N  NH2 . ARG B 1 243 ? 38.561  -3.780  -61.264 1.00 24.74 ?  245  ARG B NH2 1 
ATOM   5017 N  N   . ILE B 1 244 ? 30.725  -2.165  -61.194 1.00 12.33 ?  246  ILE B N   1 
ATOM   5018 C  CA  . ILE B 1 244 ? 29.706  -2.968  -60.534 1.00 9.57  ?  246  ILE B CA  1 
ATOM   5019 C  C   . ILE B 1 244 ? 30.210  -4.395  -60.388 1.00 15.15 ?  246  ILE B C   1 
ATOM   5020 O  O   . ILE B 1 244 ? 30.723  -4.986  -61.345 1.00 14.89 ?  246  ILE B O   1 
ATOM   5021 C  CB  . ILE B 1 244 ? 28.393  -2.892  -61.331 1.00 15.45 ?  246  ILE B CB  1 
ATOM   5022 C  CG1 . ILE B 1 244 ? 27.833  -1.462  -61.263 1.00 14.69 ?  246  ILE B CG1 1 
ATOM   5023 C  CG2 . ILE B 1 244 ? 27.384  -3.943  -60.851 1.00 11.12 ?  246  ILE B CG2 1 
ATOM   5024 C  CD1 . ILE B 1 244 ? 26.609  -1.211  -62.221 1.00 14.58 ?  246  ILE B CD1 1 
ATOM   5025 N  N   . THR B 1 245 ? 30.111  -4.941  -59.169 1.00 12.59 ?  247  THR B N   1 
ATOM   5026 C  CA  . THR B 1 245 ? 30.542  -6.305  -58.886 1.00 9.40  ?  247  THR B CA  1 
ATOM   5027 C  C   . THR B 1 245 ? 29.376  -7.224  -58.551 1.00 16.96 ?  247  THR B C   1 
ATOM   5028 O  O   . THR B 1 245 ? 29.558  -8.448  -58.499 1.00 14.08 ?  247  THR B O   1 
ATOM   5029 C  CB  . THR B 1 245 ? 31.568  -6.309  -57.735 1.00 14.25 ?  247  THR B CB  1 
ATOM   5030 O  OG1 . THR B 1 245 ? 31.067  -5.523  -56.653 1.00 17.03 ?  247  THR B OG1 1 
ATOM   5031 C  CG2 . THR B 1 245 ? 32.885  -5.712  -58.193 1.00 14.59 ?  247  THR B CG2 1 
ATOM   5032 N  N   . SER B 1 246 ? 28.184  -6.670  -58.329 1.00 14.74 ?  248  SER B N   1 
ATOM   5033 C  CA  . SER B 1 246 ? 26.998  -7.494  -58.140 1.00 15.55 ?  248  SER B CA  1 
ATOM   5034 C  C   . SER B 1 246 ? 25.754  -6.642  -58.326 1.00 17.52 ?  248  SER B C   1 
ATOM   5035 O  O   . SER B 1 246 ? 25.776  -5.422  -58.138 1.00 12.42 ?  248  SER B O   1 
ATOM   5036 C  CB  . SER B 1 246 ? 26.980  -8.161  -56.760 1.00 16.07 ?  248  SER B CB  1 
ATOM   5037 O  OG  . SER B 1 246 ? 26.440  -7.279  -55.794 1.00 18.92 ?  248  SER B OG  1 
ATOM   5038 N  N   . VAL B 1 247 ? 24.664  -7.319  -58.698 1.00 14.34 ?  249  VAL B N   1 
ATOM   5039 C  CA  . VAL B 1 247 ? 23.335  -6.731  -58.826 1.00 16.81 ?  249  VAL B CA  1 
ATOM   5040 C  C   . VAL B 1 247 ? 22.366  -7.619  -58.068 1.00 15.13 ?  249  VAL B C   1 
ATOM   5041 O  O   . VAL B 1 247 ? 22.343  -8.835  -58.290 1.00 15.11 ?  249  VAL B O   1 
ATOM   5042 C  CB  . VAL B 1 247 ? 22.883  -6.625  -60.295 1.00 16.48 ?  249  VAL B CB  1 
ATOM   5043 C  CG1 . VAL B 1 247 ? 21.445  -6.149  -60.355 1.00 16.10 ?  249  VAL B CG1 1 
ATOM   5044 C  CG2 . VAL B 1 247 ? 23.796  -5.691  -61.071 1.00 16.41 ?  249  VAL B CG2 1 
ATOM   5045 N  N   . VAL B 1 248 ? 21.555  -7.026  -57.191 1.00 12.52 ?  250  VAL B N   1 
ATOM   5046 C  CA  . VAL B 1 248 ? 20.485  -7.769  -56.526 1.00 13.01 ?  250  VAL B CA  1 
ATOM   5047 C  C   . VAL B 1 248 ? 19.173  -7.054  -56.825 1.00 16.69 ?  250  VAL B C   1 
ATOM   5048 O  O   . VAL B 1 248 ? 19.090  -5.819  -56.750 1.00 15.28 ?  250  VAL B O   1 
ATOM   5049 C  CB  . VAL B 1 248 ? 20.704  -7.920  -55.004 1.00 16.74 ?  250  VAL B CB  1 
ATOM   5050 C  CG1 . VAL B 1 248 ? 21.879  -8.863  -54.697 1.00 15.53 ?  250  VAL B CG1 1 
ATOM   5051 C  CG2 . VAL B 1 248 ? 20.859  -6.567  -54.305 1.00 14.56 ?  250  VAL B CG2 1 
ATOM   5052 N  N   . ALA B 1 249 ? 18.168  -7.823  -57.210 1.00 15.21 ?  251  ALA B N   1 
ATOM   5053 C  CA  . ALA B 1 249 ? 16.860  -7.278  -57.536 1.00 14.75 ?  251  ALA B CA  1 
ATOM   5054 C  C   . ALA B 1 249 ? 15.790  -8.129  -56.870 1.00 17.13 ?  251  ALA B C   1 
ATOM   5055 O  O   . ALA B 1 249 ? 15.951  -9.341  -56.713 1.00 18.08 ?  251  ALA B O   1 
ATOM   5056 C  CB  . ALA B 1 249 ? 16.619  -7.243  -59.047 1.00 17.52 ?  251  ALA B CB  1 
ATOM   5057 N  N   . GLY B 1 250 ? 14.702  -7.485  -56.460 1.00 16.81 ?  252  GLY B N   1 
ATOM   5058 C  CA  . GLY B 1 250 ? 13.606  -8.238  -55.885 1.00 17.71 ?  252  GLY B CA  1 
ATOM   5059 C  C   . GLY B 1 250 ? 13.061  -7.676  -54.590 1.00 16.62 ?  252  GLY B C   1 
ATOM   5060 O  O   . GLY B 1 250 ? 12.862  -6.465  -54.468 1.00 16.81 ?  252  GLY B O   1 
ATOM   5061 N  N   . ASP B 1 251 ? 12.806  -8.561  -53.628 1.00 18.81 ?  253  ASP B N   1 
ATOM   5062 C  CA  . ASP B 1 251 ? 12.144  -8.179  -52.388 1.00 19.04 ?  253  ASP B CA  1 
ATOM   5063 C  C   . ASP B 1 251 ? 13.019  -7.225  -51.587 1.00 22.41 ?  253  ASP B C   1 
ATOM   5064 O  O   . ASP B 1 251 ? 14.238  -7.392  -51.520 1.00 21.96 ?  253  ASP B O   1 
ATOM   5065 C  CB  . ASP B 1 251 ? 11.834  -9.418  -51.552 1.00 22.46 ?  253  ASP B CB  1 
ATOM   5066 C  CG  . ASP B 1 251 ? 11.316  -9.071  -50.175 1.00 27.54 ?  253  ASP B CG  1 
ATOM   5067 O  OD1 . ASP B 1 251 ? 10.125  -8.698  -50.077 1.00 29.00 ?  253  ASP B OD1 1 
ATOM   5068 O  OD2 . ASP B 1 251 ? 12.093  -9.154  -49.196 1.00 22.86 ?  253  ASP B OD2 1 
ATOM   5069 N  N   . MET B 1 252 ? 12.385  -6.215  -50.978 1.00 21.63 ?  254  MET B N   1 
ATOM   5070 C  CA  . MET B 1 252 ? 13.134  -5.199  -50.239 1.00 21.61 ?  254  MET B CA  1 
ATOM   5071 C  C   . MET B 1 252 ? 14.094  -5.796  -49.226 1.00 20.82 ?  254  MET B C   1 
ATOM   5072 O  O   . MET B 1 252 ? 15.225  -5.319  -49.086 1.00 17.59 ?  254  MET B O   1 
ATOM   5073 C  CB  . MET B 1 252 ? 12.200  -4.243  -49.507 1.00 21.05 ?  254  MET B CB  1 
ATOM   5074 C  CG  . MET B 1 252 ? 12.930  -2.973  -49.093 1.00 22.28 ?  254  MET B CG  1 
ATOM   5075 S  SD  . MET B 1 252 ? 11.970  -1.976  -47.952 1.00 23.40 ?  254  MET B SD  1 
ATOM   5076 C  CE  . MET B 1 252 ? 12.092  -2.965  -46.465 1.00 25.56 ?  254  MET B CE  1 
ATOM   5077 N  N   . GLU B 1 253 ? 13.647  -6.793  -48.463 1.00 19.86 ?  255  GLU B N   1 
ATOM   5078 C  CA  . GLU B 1 253 ? 14.529  -7.344  -47.442 1.00 22.62 ?  255  GLU B CA  1 
ATOM   5079 C  C   . GLU B 1 253 ? 15.400  -8.471  -47.981 1.00 23.91 ?  255  GLU B C   1 
ATOM   5080 O  O   . GLU B 1 253 ? 16.608  -8.479  -47.741 1.00 20.86 ?  255  GLU B O   1 
ATOM   5081 C  CB  . GLU B 1 253 ? 13.703  -7.808  -46.238 1.00 22.72 ?  255  GLU B CB  1 
ATOM   5082 C  CG  . GLU B 1 253 ? 13.009  -6.635  -45.547 1.00 20.90 ?  255  GLU B CG  1 
ATOM   5083 C  CD  . GLU B 1 253 ? 12.197  -7.046  -44.335 1.00 32.20 ?  255  GLU B CD  1 
ATOM   5084 O  OE1 . GLU B 1 253 ? 12.765  -7.629  -43.389 1.00 34.53 ?  255  GLU B OE1 1 
ATOM   5085 O  OE2 . GLU B 1 253 ? 10.982  -6.773  -44.328 1.00 37.63 ?  255  GLU B OE2 1 
ATOM   5086 N  N   . GLN B 1 254 ? 14.837  -9.391  -48.763 1.00 18.09 ?  256  GLN B N   1 
ATOM   5087 C  CA  . GLN B 1 254 ? 15.617  -10.544 -49.218 1.00 22.35 ?  256  GLN B CA  1 
ATOM   5088 C  C   . GLN B 1 254 ? 16.721  -10.141 -50.195 1.00 16.98 ?  256  GLN B C   1 
ATOM   5089 O  O   . GLN B 1 254 ? 17.851  -10.632 -50.103 1.00 20.68 ?  256  GLN B O   1 
ATOM   5090 C  CB  . GLN B 1 254 ? 14.684  -11.570 -49.853 1.00 27.47 ?  256  GLN B CB  1 
ATOM   5091 C  CG  . GLN B 1 254 ? 13.836  -12.305 -48.837 1.00 29.83 ?  256  GLN B CG  1 
ATOM   5092 C  CD  . GLN B 1 254 ? 13.440  -13.693 -49.304 1.00 49.39 ?  256  GLN B CD  1 
ATOM   5093 O  OE1 . GLN B 1 254 ? 13.870  -14.157 -50.364 1.00 37.64 ?  256  GLN B OE1 1 
ATOM   5094 N  NE2 . GLN B 1 254 ? 12.599  -14.359 -48.519 1.00 60.04 ?  256  GLN B NE2 1 
ATOM   5095 N  N   . ALA B 1 255 ? 16.415  -9.269  -51.157 1.00 20.38 ?  257  ALA B N   1 
ATOM   5096 C  CA  . ALA B 1 255 ? 17.449  -8.856  -52.102 1.00 16.84 ?  257  ALA B CA  1 
ATOM   5097 C  C   . ALA B 1 255 ? 18.546  -8.072  -51.388 1.00 20.04 ?  257  ALA B C   1 
ATOM   5098 O  O   . ALA B 1 255 ? 19.739  -8.291  -51.632 1.00 18.44 ?  257  ALA B O   1 
ATOM   5099 C  CB  . ALA B 1 255 ? 16.844  -8.032  -53.238 1.00 18.16 ?  257  ALA B CB  1 
ATOM   5100 N  N   . PHE B 1 256 ? 18.153  -7.172  -50.483 1.00 16.57 ?  258  PHE B N   1 
ATOM   5101 C  CA  . PHE B 1 256 ? 19.124  -6.390  -49.727 1.00 15.88 ?  258  PHE B CA  1 
ATOM   5102 C  C   . PHE B 1 256 ? 20.052  -7.299  -48.931 1.00 15.22 ?  258  PHE B C   1 
ATOM   5103 O  O   . PHE B 1 256 ? 21.278  -7.154  -48.981 1.00 18.01 ?  258  PHE B O   1 
ATOM   5104 C  CB  . PHE B 1 256 ? 18.384  -5.411  -48.807 1.00 15.35 ?  258  PHE B CB  1 
ATOM   5105 C  CG  . PHE B 1 256 ? 19.281  -4.679  -47.849 1.00 13.69 ?  258  PHE B CG  1 
ATOM   5106 C  CD1 . PHE B 1 256 ? 20.186  -3.728  -48.316 1.00 16.99 ?  258  PHE B CD1 1 
ATOM   5107 C  CD2 . PHE B 1 256 ? 19.224  -4.938  -46.486 1.00 14.61 ?  258  PHE B CD2 1 
ATOM   5108 C  CE1 . PHE B 1 256 ? 21.039  -3.047  -47.428 1.00 12.83 ?  258  PHE B CE1 1 
ATOM   5109 C  CE2 . PHE B 1 256 ? 20.076  -4.265  -45.590 1.00 17.07 ?  258  PHE B CE2 1 
ATOM   5110 C  CZ  . PHE B 1 256 ? 20.978  -3.315  -46.073 1.00 15.03 ?  258  PHE B CZ  1 
ATOM   5111 N  N   . LEU B 1 257 ? 19.486  -8.276  -48.223 1.00 15.14 ?  259  LEU B N   1 
ATOM   5112 C  CA  . LEU B 1 257 ? 20.310  -9.148  -47.397 1.00 20.32 ?  259  LEU B CA  1 
ATOM   5113 C  C   . LEU B 1 257 ? 21.219  -10.036 -48.237 1.00 19.61 ?  259  LEU B C   1 
ATOM   5114 O  O   . LEU B 1 257 ? 22.310  -10.396 -47.784 1.00 19.29 ?  259  LEU B O   1 
ATOM   5115 C  CB  . LEU B 1 257 ? 19.428  -10.000 -46.488 1.00 19.09 ?  259  LEU B CB  1 
ATOM   5116 C  CG  . LEU B 1 257 ? 18.688  -9.226  -45.401 1.00 22.58 ?  259  LEU B CG  1 
ATOM   5117 C  CD1 . LEU B 1 257 ? 17.812  -10.170 -44.571 1.00 22.37 ?  259  LEU B CD1 1 
ATOM   5118 C  CD2 . LEU B 1 257 ? 19.640  -8.425  -44.509 1.00 20.69 ?  259  LEU B CD2 1 
ATOM   5119 N  N   . LYS B 1 258 ? 20.789  -10.411 -49.445 1.00 17.98 ?  260  LYS B N   1 
ATOM   5120 C  CA  . LYS B 1 258 ? 21.682  -11.136 -50.346 1.00 18.83 ?  260  LYS B CA  1 
ATOM   5121 C  C   . LYS B 1 258 ? 22.831  -10.247 -50.811 1.00 14.46 ?  260  LYS B C   1 
ATOM   5122 O  O   . LYS B 1 258 ? 23.965  -10.716 -50.972 1.00 18.88 ?  260  LYS B O   1 
ATOM   5123 C  CB  . LYS B 1 258 ? 20.901  -11.665 -51.551 1.00 20.03 ?  260  LYS B CB  1 
ATOM   5124 N  N   . GLY B 1 259 ? 22.552  -8.963  -51.036 1.00 13.87 ?  261  GLY B N   1 
ATOM   5125 C  CA  . GLY B 1 259 ? 23.599  -8.053  -51.456 1.00 14.32 ?  261  GLY B CA  1 
ATOM   5126 C  C   . GLY B 1 259 ? 24.588  -7.787  -50.342 1.00 18.30 ?  261  GLY B C   1 
ATOM   5127 O  O   . GLY B 1 259 ? 25.794  -7.694  -50.583 1.00 14.65 ?  261  GLY B O   1 
ATOM   5128 N  N   . VAL B 1 260 ? 24.088  -7.683  -49.103 1.00 13.48 ?  262  VAL B N   1 
ATOM   5129 C  CA  . VAL B 1 260 ? 24.963  -7.519  -47.946 1.00 15.14 ?  262  VAL B CA  1 
ATOM   5130 C  C   . VAL B 1 260 ? 25.812  -8.761  -47.741 1.00 17.05 ?  262  VAL B C   1 
ATOM   5131 O  O   . VAL B 1 260 ? 27.011  -8.664  -47.444 1.00 18.12 ?  262  VAL B O   1 
ATOM   5132 C  CB  . VAL B 1 260 ? 24.143  -7.186  -46.687 1.00 14.18 ?  262  VAL B CB  1 
ATOM   5133 C  CG1 . VAL B 1 260 ? 25.013  -7.329  -45.423 1.00 15.38 ?  262  VAL B CG1 1 
ATOM   5134 C  CG2 . VAL B 1 260 ? 23.574  -5.780  -46.792 1.00 13.68 ?  262  VAL B CG2 1 
ATOM   5135 N  N   . ALA B 1 261 ? 25.214  -9.948  -47.906 1.00 19.37 ?  263  ALA B N   1 
ATOM   5136 C  CA  . ALA B 1 261 ? 25.987  -11.183 -47.796 1.00 17.00 ?  263  ALA B CA  1 
ATOM   5137 C  C   . ALA B 1 261 ? 27.162  -11.179 -48.762 1.00 19.25 ?  263  ALA B C   1 
ATOM   5138 O  O   . ALA B 1 261 ? 28.253  -11.644 -48.425 1.00 18.29 ?  263  ALA B O   1 
ATOM   5139 C  CB  . ALA B 1 261 ? 25.086  -12.394 -48.060 1.00 21.72 ?  263  ALA B CB  1 
ATOM   5140 N  N   . PHE B 1 262 ? 26.966  -10.653 -49.972 1.00 19.06 ?  264  PHE B N   1 
ATOM   5141 C  CA  . PHE B 1 262 ? 28.086  -10.568 -50.901 1.00 19.93 ?  264  PHE B CA  1 
ATOM   5142 C  C   . PHE B 1 262 ? 29.114  -9.536  -50.445 1.00 19.56 ?  264  PHE B C   1 
ATOM   5143 O  O   . PHE B 1 262 ? 30.321  -9.825  -50.383 1.00 18.94 ?  264  PHE B O   1 
ATOM   5144 C  CB  . PHE B 1 262 ? 27.610  -10.246 -52.316 1.00 18.48 ?  264  PHE B CB  1 
ATOM   5145 C  CG  . PHE B 1 262 ? 28.750  -10.018 -53.262 1.00 17.81 ?  264  PHE B CG  1 
ATOM   5146 C  CD1 . PHE B 1 262 ? 29.601  -11.059 -53.593 1.00 21.88 ?  264  PHE B CD1 1 
ATOM   5147 C  CD2 . PHE B 1 262 ? 29.003  -8.760  -53.777 1.00 15.50 ?  264  PHE B CD2 1 
ATOM   5148 C  CE1 . PHE B 1 262 ? 30.681  -10.861 -54.438 1.00 24.88 ?  264  PHE B CE1 1 
ATOM   5149 C  CE2 . PHE B 1 262 ? 30.072  -8.551  -54.635 1.00 20.68 ?  264  PHE B CE2 1 
ATOM   5150 C  CZ  . PHE B 1 262 ? 30.913  -9.603  -54.967 1.00 22.34 ?  264  PHE B CZ  1 
ATOM   5151 N  N   . VAL B 1 263 ? 28.664  -8.322  -50.126 1.00 16.68 ?  265  VAL B N   1 
ATOM   5152 C  CA  . VAL B 1 263 ? 29.658  -7.277  -49.949 1.00 17.15 ?  265  VAL B CA  1 
ATOM   5153 C  C   . VAL B 1 263 ? 30.426  -7.528  -48.656 1.00 16.29 ?  265  VAL B C   1 
ATOM   5154 O  O   . VAL B 1 263 ? 31.566  -7.080  -48.515 1.00 17.53 ?  265  VAL B O   1 
ATOM   5155 C  CB  . VAL B 1 263 ? 29.012  -5.864  -49.962 1.00 21.23 ?  265  VAL B CB  1 
ATOM   5156 C  CG1 . VAL B 1 263 ? 28.102  -5.642  -48.780 1.00 26.36 ?  265  VAL B CG1 1 
ATOM   5157 C  CG2 . VAL B 1 263 ? 30.004  -4.753  -50.227 1.00 30.98 ?  265  VAL B CG2 1 
ATOM   5158 N  N   . GLU B 1 264 ? 29.842  -8.276  -47.709 1.00 15.28 ?  266  GLU B N   1 
ATOM   5159 C  CA  . GLU B 1 264 ? 30.586  -8.651  -46.502 1.00 17.62 ?  266  GLU B CA  1 
ATOM   5160 C  C   . GLU B 1 264 ? 31.802  -9.504  -46.834 1.00 23.21 ?  266  GLU B C   1 
ATOM   5161 O  O   . GLU B 1 264 ? 32.803  -9.460  -46.104 1.00 23.93 ?  266  GLU B O   1 
ATOM   5162 C  CB  . GLU B 1 264 ? 29.695  -9.404  -45.511 1.00 24.20 ?  266  GLU B CB  1 
ATOM   5163 C  CG  . GLU B 1 264 ? 28.821  -8.500  -44.692 1.00 23.94 ?  266  GLU B CG  1 
ATOM   5164 N  N   . THR B 1 265 ? 31.746  -10.273 -47.930 1.00 20.47 ?  267  THR B N   1 
ATOM   5165 C  CA  . THR B 1 265 ? 32.885  -11.080 -48.356 1.00 20.94 ?  267  THR B CA  1 
ATOM   5166 C  C   . THR B 1 265 ? 33.985  -10.266 -49.026 1.00 21.59 ?  267  THR B C   1 
ATOM   5167 O  O   . THR B 1 265 ? 35.058  -10.815 -49.277 1.00 25.70 ?  267  THR B O   1 
ATOM   5168 C  CB  . THR B 1 265 ? 32.433  -12.196 -49.313 1.00 21.10 ?  267  THR B CB  1 
ATOM   5169 O  OG1 . THR B 1 265 ? 32.197  -11.653 -50.626 1.00 24.84 ?  267  THR B OG1 1 
ATOM   5170 C  CG2 . THR B 1 265 ? 31.167  -12.882 -48.814 1.00 31.25 ?  267  THR B CG2 1 
ATOM   5171 N  N   . VAL B 1 266 ? 33.768  -8.989  -49.329 1.00 15.47 ?  268  VAL B N   1 
ATOM   5172 C  CA  . VAL B 1 266 ? 34.824  -8.237  -49.995 1.00 17.50 ?  268  VAL B CA  1 
ATOM   5173 C  C   . VAL B 1 266 ? 35.282  -7.023  -49.191 1.00 18.77 ?  268  VAL B C   1 
ATOM   5174 O  O   . VAL B 1 266 ? 36.447  -6.628  -49.292 1.00 18.81 ?  268  VAL B O   1 
ATOM   5175 C  CB  . VAL B 1 266 ? 34.409  -7.813  -51.419 1.00 23.60 ?  268  VAL B CB  1 
ATOM   5176 C  CG1 . VAL B 1 266 ? 34.171  -9.045  -52.295 1.00 23.89 ?  268  VAL B CG1 1 
ATOM   5177 C  CG2 . VAL B 1 266 ? 33.217  -6.908  -51.400 1.00 20.13 ?  268  VAL B CG2 1 
ATOM   5178 N  N   . VAL B 1 267 ? 34.407  -6.431  -48.372 1.00 17.61 ?  269  VAL B N   1 
ATOM   5179 C  CA  . VAL B 1 267 ? 34.782  -5.132  -47.801 1.00 18.95 ?  269  VAL B CA  1 
ATOM   5180 C  C   . VAL B 1 267 ? 35.661  -5.233  -46.569 1.00 16.62 ?  269  VAL B C   1 
ATOM   5181 O  O   . VAL B 1 267 ? 36.296  -4.238  -46.212 1.00 15.72 ?  269  VAL B O   1 
ATOM   5182 C  CB  . VAL B 1 267 ? 33.589  -4.236  -47.427 1.00 18.31 ?  269  VAL B CB  1 
ATOM   5183 C  CG1 . VAL B 1 267 ? 32.866  -3.802  -48.686 1.00 22.98 ?  269  VAL B CG1 1 
ATOM   5184 C  CG2 . VAL B 1 267 ? 32.648  -4.955  -46.442 1.00 19.16 ?  269  VAL B CG2 1 
ATOM   5185 N  N   . LYS B 1 268 ? 35.704  -6.379  -45.900 1.00 12.97 ?  270  LYS B N   1 
ATOM   5186 C  CA  . LYS B 1 268 ? 36.498  -6.500  -44.683 1.00 18.44 ?  270  LYS B CA  1 
ATOM   5187 C  C   . LYS B 1 268 ? 37.986  -6.624  -45.000 1.00 17.94 ?  270  LYS B C   1 
ATOM   5188 O  O   . LYS B 1 268 ? 38.391  -7.406  -45.869 1.00 21.05 ?  270  LYS B O   1 
ATOM   5189 C  CB  . LYS B 1 268 ? 36.023  -7.695  -43.854 1.00 21.03 ?  270  LYS B CB  1 
ATOM   5190 C  CG  . LYS B 1 268 ? 34.721  -7.422  -43.130 1.00 20.29 ?  270  LYS B CG  1 
ATOM   5191 C  CD  . LYS B 1 268 ? 34.248  -8.612  -42.291 1.00 32.83 ?  270  LYS B CD  1 
ATOM   5192 C  CE  . LYS B 1 268 ? 32.728  -8.722  -42.299 1.00 30.12 ?  270  LYS B CE  1 
ATOM   5193 N  NZ  . LYS B 1 268 ? 32.212  -9.064  -40.935 1.00 45.30 ?  270  LYS B NZ  1 
ATOM   5194 N  N   . ALA B 1 269 ? 38.802  -5.831  -44.306 1.00 15.96 ?  271  ALA B N   1 
ATOM   5195 C  CA  . ALA B 1 269 ? 40.249  -5.881  -44.470 1.00 16.10 ?  271  ALA B CA  1 
ATOM   5196 C  C   . ALA B 1 269 ? 40.861  -5.814  -43.081 1.00 16.55 ?  271  ALA B C   1 
ATOM   5197 O  O   . ALA B 1 269 ? 40.474  -4.961  -42.283 1.00 16.82 ?  271  ALA B O   1 
ATOM   5198 C  CB  . ALA B 1 269 ? 40.759  -4.730  -45.346 1.00 22.34 ?  271  ALA B CB  1 
ATOM   5199 N  N   . ALA B 1 270 ? 41.809  -6.698  -42.794 1.00 21.48 ?  272  ALA B N   1 
ATOM   5200 C  CA  . ALA B 1 270 ? 42.247  -6.924  -41.423 1.00 20.09 ?  272  ALA B CA  1 
ATOM   5201 C  C   . ALA B 1 270 ? 43.653  -6.400  -41.168 1.00 25.96 ?  272  ALA B C   1 
ATOM   5202 O  O   . ALA B 1 270 ? 44.489  -6.319  -42.075 1.00 24.61 ?  272  ALA B O   1 
ATOM   5203 C  CB  . ALA B 1 270 ? 42.194  -8.416  -41.076 1.00 25.09 ?  272  ALA B CB  1 
ATOM   5204 N  N   . VAL B 1 271 ? 43.886  -6.030  -39.915 1.00 19.39 ?  273  VAL B N   1 
ATOM   5205 C  CA  . VAL B 1 271 ? 45.228  -5.776  -39.396 1.00 20.27 ?  273  VAL B CA  1 
ATOM   5206 C  C   . VAL B 1 271 ? 45.453  -6.744  -38.245 1.00 18.23 ?  273  VAL B C   1 
ATOM   5207 O  O   . VAL B 1 271 ? 44.491  -7.221  -37.624 1.00 21.53 ?  273  VAL B O   1 
ATOM   5208 C  CB  . VAL B 1 271 ? 45.400  -4.309  -38.942 1.00 19.46 ?  273  VAL B CB  1 
ATOM   5209 C  CG1 . VAL B 1 271 ? 45.437  -3.375  -40.163 1.00 20.84 ?  273  VAL B CG1 1 
ATOM   5210 C  CG2 . VAL B 1 271 ? 44.300  -3.927  -37.976 1.00 16.51 ?  273  VAL B CG2 1 
ATOM   5211 N  N   . PRO B 1 272 ? 46.716  -7.045  -37.913 1.00 20.50 ?  274  PRO B N   1 
ATOM   5212 C  CA  . PRO B 1 272 ? 46.955  -7.960  -36.783 1.00 23.71 ?  274  PRO B CA  1 
ATOM   5213 C  C   . PRO B 1 272 ? 46.513  -7.385  -35.448 1.00 25.95 ?  274  PRO B C   1 
ATOM   5214 O  O   . PRO B 1 272 ? 46.012  -8.120  -34.586 1.00 31.29 ?  274  PRO B O   1 
ATOM   5215 C  CB  . PRO B 1 272 ? 48.475  -8.187  -36.837 1.00 21.79 ?  274  PRO B CB  1 
ATOM   5216 C  CG  . PRO B 1 272 ? 48.862  -7.874  -38.255 1.00 30.50 ?  274  PRO B CG  1 
ATOM   5217 C  CD  . PRO B 1 272 ? 47.954  -6.732  -38.643 1.00 23.31 ?  274  PRO B CD  1 
ATOM   5218 N  N   . ALA B 1 273 ? 46.659  -6.079  -35.263 1.00 23.89 ?  275  ALA B N   1 
ATOM   5219 C  CA  . ALA B 1 273 ? 46.388  -5.440  -33.983 1.00 20.26 ?  275  ALA B CA  1 
ATOM   5220 C  C   . ALA B 1 273 ? 46.120  -3.970  -34.243 1.00 17.12 ?  275  ALA B C   1 
ATOM   5221 O  O   . ALA B 1 273 ? 46.510  -3.450  -35.294 1.00 17.15 ?  275  ALA B O   1 
ATOM   5222 C  CB  . ALA B 1 273 ? 47.578  -5.606  -33.020 1.00 19.40 ?  275  ALA B CB  1 
ATOM   5223 N  N   . PRO B 1 274 ? 45.446  -3.276  -33.323 1.00 22.02 ?  276  PRO B N   1 
ATOM   5224 C  CA  . PRO B 1 274 ? 45.230  -1.835  -33.517 1.00 17.93 ?  276  PRO B CA  1 
ATOM   5225 C  C   . PRO B 1 274 ? 46.551  -1.085  -33.625 1.00 17.92 ?  276  PRO B C   1 
ATOM   5226 O  O   . PRO B 1 274 ? 47.565  -1.473  -33.038 1.00 17.79 ?  276  PRO B O   1 
ATOM   5227 C  CB  . PRO B 1 274 ? 44.429  -1.418  -32.278 1.00 19.39 ?  276  PRO B CB  1 
ATOM   5228 C  CG  . PRO B 1 274 ? 44.576  -2.551  -31.309 1.00 32.04 ?  276  PRO B CG  1 
ATOM   5229 C  CD  . PRO B 1 274 ? 44.706  -3.778  -32.154 1.00 21.80 ?  276  PRO B CD  1 
ATOM   5230 N  N   . VAL B 1 275 ? 46.538  -0.014  -34.415 1.00 15.04 ?  277  VAL B N   1 
ATOM   5231 C  CA  . VAL B 1 275 ? 47.751  0.718   -34.740 1.00 12.44 ?  277  VAL B CA  1 
ATOM   5232 C  C   . VAL B 1 275 ? 47.663  2.128   -34.179 1.00 14.53 ?  277  VAL B C   1 
ATOM   5233 O  O   . VAL B 1 275 ? 46.590  2.639   -33.851 1.00 11.49 ?  277  VAL B O   1 
ATOM   5234 C  CB  . VAL B 1 275 ? 48.037  0.753   -36.259 1.00 16.82 ?  277  VAL B CB  1 
ATOM   5235 C  CG1 . VAL B 1 275 ? 48.372  -0.649  -36.772 1.00 24.32 ?  277  VAL B CG1 1 
ATOM   5236 C  CG2 . VAL B 1 275 ? 46.822  1.324   -37.015 1.00 15.97 ?  277  VAL B CG2 1 
ATOM   5237 N  N   . ASP B 1 276 ? 48.834  2.756   -34.069 1.00 12.51 ?  278  ASP B N   1 
ATOM   5238 C  CA  . ASP B 1 276 ? 48.897  4.101   -33.516 1.00 15.18 ?  278  ASP B CA  1 
ATOM   5239 C  C   . ASP B 1 276 ? 48.461  5.165   -34.512 1.00 14.09 ?  278  ASP B C   1 
ATOM   5240 O  O   . ASP B 1 276 ? 47.961  6.213   -34.094 1.00 11.92 ?  278  ASP B O   1 
ATOM   5241 C  CB  . ASP B 1 276 ? 50.318  4.417   -33.044 1.00 20.70 ?  278  ASP B CB  1 
ATOM   5242 C  CG  . ASP B 1 276 ? 50.749  3.551   -31.885 1.00 26.16 ?  278  ASP B CG  1 
ATOM   5243 O  OD1 . ASP B 1 276 ? 51.545  2.616   -32.107 1.00 36.19 ?  278  ASP B OD1 1 
ATOM   5244 O  OD2 . ASP B 1 276 ? 50.279  3.803   -30.761 1.00 31.83 ?  278  ASP B OD2 1 
ATOM   5245 N  N   . VAL B 1 277 ? 48.669  4.944   -35.812 1.00 10.79 ?  279  VAL B N   1 
ATOM   5246 C  CA  . VAL B 1 277 ? 48.326  5.938   -36.832 1.00 9.93  ?  279  VAL B CA  1 
ATOM   5247 C  C   . VAL B 1 277 ? 47.546  5.263   -37.958 1.00 10.41 ?  279  VAL B C   1 
ATOM   5248 O  O   . VAL B 1 277 ? 48.037  4.306   -38.566 1.00 10.86 ?  279  VAL B O   1 
ATOM   5249 C  CB  . VAL B 1 277 ? 49.586  6.617   -37.393 1.00 13.48 ?  279  VAL B CB  1 
ATOM   5250 C  CG1 . VAL B 1 277 ? 49.221  7.727   -38.349 1.00 13.76 ?  279  VAL B CG1 1 
ATOM   5251 C  CG2 . VAL B 1 277 ? 50.485  7.165   -36.251 1.00 12.01 ?  279  VAL B CG2 1 
ATOM   5252 N  N   . VAL B 1 278 ? 46.370  5.798   -38.285 1.00 11.15 ?  280  VAL B N   1 
ATOM   5253 C  CA  . VAL B 1 278 ? 45.570  5.315   -39.408 1.00 11.10 ?  280  VAL B CA  1 
ATOM   5254 C  C   . VAL B 1 278 ? 45.451  6.452   -40.416 1.00 9.34  ?  280  VAL B C   1 
ATOM   5255 O  O   . VAL B 1 278 ? 44.942  7.526   -40.083 1.00 12.52 ?  280  VAL B O   1 
ATOM   5256 C  CB  . VAL B 1 278 ? 44.171  4.830   -38.976 1.00 13.51 ?  280  VAL B CB  1 
ATOM   5257 C  CG1 . VAL B 1 278 ? 43.394  4.349   -40.197 1.00 13.62 ?  280  VAL B CG1 1 
ATOM   5258 C  CG2 . VAL B 1 278 ? 44.278  3.705   -37.952 1.00 13.83 ?  280  VAL B CG2 1 
ATOM   5259 N  N   . VAL B 1 279 ? 45.922  6.224   -41.639 1.00 7.47  ?  281  VAL B N   1 
ATOM   5260 C  CA  . VAL B 1 279 ? 45.754  7.181   -42.729 1.00 9.78  ?  281  VAL B CA  1 
ATOM   5261 C  C   . VAL B 1 279 ? 44.541  6.768   -43.549 1.00 10.16 ?  281  VAL B C   1 
ATOM   5262 O  O   . VAL B 1 279 ? 44.453  5.609   -43.969 1.00 10.09 ?  281  VAL B O   1 
ATOM   5263 C  CB  . VAL B 1 279 ? 47.014  7.230   -43.603 1.00 12.77 ?  281  VAL B CB  1 
ATOM   5264 C  CG1 . VAL B 1 279 ? 46.774  8.090   -44.823 1.00 11.35 ?  281  VAL B CG1 1 
ATOM   5265 C  CG2 . VAL B 1 279 ? 48.175  7.757   -42.770 1.00 10.78 ?  281  VAL B CG2 1 
ATOM   5266 N  N   . THR B 1 280 ? 43.620  7.704   -43.803 1.00 7.30  ?  282  THR B N   1 
ATOM   5267 C  CA  . THR B 1 280 ? 42.404  7.337   -44.524 1.00 9.61  ?  282  THR B CA  1 
ATOM   5268 C  C   . THR B 1 280 ? 41.922  8.485   -45.409 1.00 9.23  ?  282  THR B C   1 
ATOM   5269 O  O   . THR B 1 280 ? 42.495  9.569   -45.455 1.00 9.44  ?  282  THR B O   1 
ATOM   5270 C  CB  . THR B 1 280 ? 41.296  6.864   -43.562 1.00 9.80  ?  282  THR B CB  1 
ATOM   5271 O  OG1 . THR B 1 280 ? 40.226  6.295   -44.328 1.00 11.92 ?  282  THR B OG1 1 
ATOM   5272 C  CG2 . THR B 1 280 ? 40.726  8.029   -42.722 1.00 10.19 ?  282  THR B CG2 1 
ATOM   5273 N  N   . SER B 1 281 ? 40.846  8.223   -46.128 1.00 11.63 ?  283  SER B N   1 
ATOM   5274 C  CA  . SER B 1 281 ? 40.252  9.200   -47.015 1.00 10.59 ?  283  SER B CA  1 
ATOM   5275 C  C   . SER B 1 281 ? 38.765  9.278   -46.696 1.00 11.40 ?  283  SER B C   1 
ATOM   5276 O  O   . SER B 1 281 ? 38.264  8.615   -45.781 1.00 11.53 ?  283  SER B O   1 
ATOM   5277 C  CB  . SER B 1 281 ? 40.463  8.795   -48.475 1.00 11.55 ?  283  SER B CB  1 
ATOM   5278 O  OG  . SER B 1 281 ? 39.621  7.683   -48.751 1.00 9.66  ?  283  SER B OG  1 
ATOM   5279 N  N   . SER B 1 282 ? 38.049  10.082  -47.475 1.00 11.30 ?  284  SER B N   1 
ATOM   5280 C  CA  . SER B 1 282 ? 36.597  10.111  -47.431 1.00 11.62 ?  284  SER B CA  1 
ATOM   5281 C  C   . SER B 1 282 ? 36.013  9.553   -48.726 1.00 11.29 ?  284  SER B C   1 
ATOM   5282 O  O   . SER B 1 282 ? 34.932  9.962   -49.161 1.00 13.05 ?  284  SER B O   1 
ATOM   5283 C  CB  . SER B 1 282 ? 36.097  11.531  -47.163 1.00 13.99 ?  284  SER B CB  1 
ATOM   5284 O  OG  . SER B 1 282 ? 34.676  11.598  -47.208 1.00 18.38 ?  284  SER B OG  1 
ATOM   5285 N  N   . ALA B 1 283 ? 36.727  8.605   -49.345 1.00 11.55 ?  285  ALA B N   1 
ATOM   5286 C  CA  . ALA B 1 283 ? 36.299  7.874   -50.541 1.00 14.07 ?  285  ALA B CA  1 
ATOM   5287 C  C   . ALA B 1 283 ? 36.206  8.746   -51.785 1.00 13.53 ?  285  ALA B C   1 
ATOM   5288 O  O   . ALA B 1 283 ? 35.539  8.355   -52.746 1.00 12.47 ?  285  ALA B O   1 
ATOM   5289 C  CB  . ALA B 1 283 ? 34.957  7.164   -50.317 1.00 13.38 ?  285  ALA B CB  1 
ATOM   5290 N  N   . GLY B 1 284 ? 36.826  9.924   -51.790 1.00 12.41 ?  286  GLY B N   1 
ATOM   5291 C  CA  . GLY B 1 284 ? 36.887  10.769  -52.981 1.00 9.33  ?  286  GLY B CA  1 
ATOM   5292 C  C   . GLY B 1 284 ? 35.513  11.307  -53.398 1.00 11.86 ?  286  GLY B C   1 
ATOM   5293 O  O   . GLY B 1 284 ? 34.529  11.214  -52.676 1.00 11.25 ?  286  GLY B O   1 
ATOM   5294 N  N   . HIS B 1 285 ? 35.477  11.869  -54.609 1.00 9.02  ?  287  HIS B N   1 
ATOM   5295 C  CA  . HIS B 1 285 ? 34.220  12.358  -55.168 1.00 11.20 ?  287  HIS B CA  1 
ATOM   5296 C  C   . HIS B 1 285 ? 33.289  11.182  -55.465 1.00 12.09 ?  287  HIS B C   1 
ATOM   5297 O  O   . HIS B 1 285 ? 33.726  10.173  -56.019 1.00 13.32 ?  287  HIS B O   1 
ATOM   5298 C  CB  . HIS B 1 285 ? 34.485  13.145  -56.462 1.00 12.88 ?  287  HIS B CB  1 
ATOM   5299 C  CG  . HIS B 1 285 ? 33.256  13.758  -57.060 1.00 15.64 ?  287  HIS B CG  1 
ATOM   5300 N  ND1 . HIS B 1 285 ? 32.856  15.045  -56.771 1.00 18.64 ?  287  HIS B ND1 1 
ATOM   5301 C  CD2 . HIS B 1 285 ? 32.339  13.263  -57.926 1.00 18.66 ?  287  HIS B CD2 1 
ATOM   5302 C  CE1 . HIS B 1 285 ? 31.743  15.318  -57.436 1.00 22.18 ?  287  HIS B CE1 1 
ATOM   5303 N  NE2 . HIS B 1 285 ? 31.409  14.253  -58.144 1.00 18.14 ?  287  HIS B NE2 1 
ATOM   5304 N  N   . PRO B 1 286 ? 31.982  11.298  -55.165 1.00 10.89 ?  288  PRO B N   1 
ATOM   5305 C  CA  . PRO B 1 286 ? 31.250  12.466  -54.669 1.00 11.22 ?  288  PRO B CA  1 
ATOM   5306 C  C   . PRO B 1 286 ? 31.075  12.524  -53.152 1.00 14.35 ?  288  PRO B C   1 
ATOM   5307 O  O   . PRO B 1 286 ? 30.525  13.503  -52.646 1.00 14.30 ?  288  PRO B O   1 
ATOM   5308 C  CB  . PRO B 1 286 ? 29.890  12.303  -55.343 1.00 13.19 ?  288  PRO B CB  1 
ATOM   5309 C  CG  . PRO B 1 286 ? 29.703  10.793  -55.350 1.00 14.40 ?  288  PRO B CG  1 
ATOM   5310 C  CD  . PRO B 1 286 ? 31.062  10.197  -55.529 1.00 14.28 ?  288  PRO B CD  1 
ATOM   5311 N  N   . LEU B 1 287 ? 31.499  11.489  -52.424 1.00 10.62 ?  289  LEU B N   1 
ATOM   5312 C  CA  . LEU B 1 287 ? 31.249  11.512  -50.985 1.00 9.58  ?  289  LEU B CA  1 
ATOM   5313 C  C   . LEU B 1 287 ? 32.025  12.634  -50.298 1.00 12.35 ?  289  LEU B C   1 
ATOM   5314 O  O   . LEU B 1 287 ? 31.508  13.265  -49.364 1.00 13.30 ?  289  LEU B O   1 
ATOM   5315 C  CB  . LEU B 1 287 ? 31.587  10.160  -50.340 1.00 13.53 ?  289  LEU B CB  1 
ATOM   5316 C  CG  . LEU B 1 287 ? 31.157  10.033  -48.868 1.00 10.67 ?  289  LEU B CG  1 
ATOM   5317 C  CD1 . LEU B 1 287 ? 29.653  10.240  -48.679 1.00 12.22 ?  289  LEU B CD1 1 
ATOM   5318 C  CD2 . LEU B 1 287 ? 31.577  8.672   -48.307 1.00 15.70 ?  289  LEU B CD2 1 
ATOM   5319 N  N   . ASP B 1 288 ? 33.260  12.911  -50.732 1.00 13.11 ?  290  ASP B N   1 
ATOM   5320 C  CA  . ASP B 1 288 ? 34.078  13.838  -49.951 1.00 14.41 ?  290  ASP B CA  1 
ATOM   5321 C  C   . ASP B 1 288 ? 33.814  15.301  -50.300 1.00 14.84 ?  290  ASP B C   1 
ATOM   5322 O  O   . ASP B 1 288 ? 34.662  16.153  -50.012 1.00 14.03 ?  290  ASP B O   1 
ATOM   5323 C  CB  . ASP B 1 288 ? 35.582  13.493  -50.021 1.00 11.97 ?  290  ASP B CB  1 
ATOM   5324 C  CG  . ASP B 1 288 ? 36.291  13.897  -51.336 1.00 13.18 ?  290  ASP B CG  1 
ATOM   5325 O  OD1 . ASP B 1 288 ? 35.665  14.371  -52.291 1.00 11.69 ?  290  ASP B OD1 1 
ATOM   5326 O  OD2 . ASP B 1 288 ? 37.550  13.777  -51.385 1.00 14.49 ?  290  ASP B OD2 1 
ATOM   5327 N  N   . LEU B 1 289 ? 32.625  15.617  -50.838 1.00 10.59 ?  291  LEU B N   1 
ATOM   5328 C  CA  . LEU B 1 289 ? 32.266  16.999  -51.157 1.00 14.02 ?  291  LEU B CA  1 
ATOM   5329 C  C   . LEU B 1 289 ? 32.193  17.909  -49.927 1.00 14.60 ?  291  LEU B C   1 
ATOM   5330 O  O   . LEU B 1 289 ? 32.450  19.112  -50.044 1.00 12.95 ?  291  LEU B O   1 
ATOM   5331 C  CB  . LEU B 1 289 ? 30.916  17.031  -51.881 1.00 13.57 ?  291  LEU B CB  1 
ATOM   5332 C  CG  . LEU B 1 289 ? 30.940  16.663  -53.364 1.00 14.32 ?  291  LEU B CG  1 
ATOM   5333 C  CD1 . LEU B 1 289 ? 29.499  16.400  -53.869 1.00 15.96 ?  291  LEU B CD1 1 
ATOM   5334 C  CD2 . LEU B 1 289 ? 31.639  17.740  -54.203 1.00 15.01 ?  291  LEU B CD2 1 
ATOM   5335 N  N   . THR B 1 290 ? 31.793  17.386  -48.759 1.00 12.60 ?  292  THR B N   1 
ATOM   5336 C  CA  . THR B 1 290 ? 31.618  18.210  -47.565 1.00 15.82 ?  292  THR B CA  1 
ATOM   5337 C  C   . THR B 1 290 ? 32.275  17.578  -46.341 1.00 13.59 ?  292  THR B C   1 
ATOM   5338 O  O   . THR B 1 290 ? 32.411  16.355  -46.235 1.00 11.36 ?  292  THR B O   1 
ATOM   5339 C  CB  . THR B 1 290 ? 30.132  18.478  -47.223 1.00 14.24 ?  292  THR B CB  1 
ATOM   5340 O  OG1 . THR B 1 290 ? 29.423  17.239  -47.065 1.00 14.68 ?  292  THR B OG1 1 
ATOM   5341 C  CG2 . THR B 1 290 ? 29.464  19.361  -48.284 1.00 12.37 ?  292  THR B CG2 1 
ATOM   5342 N  N   . PHE B 1 291 ? 32.654  18.440  -45.397 1.00 11.34 ?  293  PHE B N   1 
ATOM   5343 C  CA  . PHE B 1 291 ? 33.156  17.963  -44.109 1.00 10.45 ?  293  PHE B CA  1 
ATOM   5344 C  C   . PHE B 1 291 ? 32.105  17.116  -43.407 1.00 14.33 ?  293  PHE B C   1 
ATOM   5345 O  O   . PHE B 1 291 ? 32.431  16.108  -42.765 1.00 11.22 ?  293  PHE B O   1 
ATOM   5346 C  CB  . PHE B 1 291 ? 33.570  19.171  -43.256 1.00 12.55 ?  293  PHE B CB  1 
ATOM   5347 C  CG  . PHE B 1 291 ? 34.127  18.815  -41.910 1.00 12.55 ?  293  PHE B CG  1 
ATOM   5348 C  CD1 . PHE B 1 291 ? 35.467  18.549  -41.760 1.00 14.88 ?  293  PHE B CD1 1 
ATOM   5349 C  CD2 . PHE B 1 291 ? 33.296  18.737  -40.804 1.00 14.59 ?  293  PHE B CD2 1 
ATOM   5350 C  CE1 . PHE B 1 291 ? 35.998  18.210  -40.513 1.00 15.51 ?  293  PHE B CE1 1 
ATOM   5351 C  CE2 . PHE B 1 291 ? 33.807  18.412  -39.554 1.00 18.70 ?  293  PHE B CE2 1 
ATOM   5352 C  CZ  . PHE B 1 291 ? 35.157  18.144  -39.407 1.00 16.10 ?  293  PHE B CZ  1 
ATOM   5353 N  N   . TYR B 1 292 ? 30.829  17.494  -43.560 1.00 11.15 ?  294  TYR B N   1 
ATOM   5354 C  CA  . TYR B 1 292 ? 29.709  16.723  -43.023 1.00 12.69 ?  294  TYR B CA  1 
ATOM   5355 C  C   . TYR B 1 292 ? 29.802  15.242  -43.398 1.00 13.19 ?  294  TYR B C   1 
ATOM   5356 O  O   . TYR B 1 292 ? 29.689  14.362  -42.533 1.00 11.61 ?  294  TYR B O   1 
ATOM   5357 C  CB  . TYR B 1 292 ? 28.400  17.345  -43.528 1.00 13.09 ?  294  TYR B CB  1 
ATOM   5358 C  CG  . TYR B 1 292 ? 27.145  16.548  -43.243 1.00 14.61 ?  294  TYR B CG  1 
ATOM   5359 C  CD1 . TYR B 1 292 ? 26.640  15.668  -44.198 1.00 15.48 ?  294  TYR B CD1 1 
ATOM   5360 C  CD2 . TYR B 1 292 ? 26.427  16.712  -42.047 1.00 11.91 ?  294  TYR B CD2 1 
ATOM   5361 C  CE1 . TYR B 1 292 ? 25.488  14.935  -43.961 1.00 16.95 ?  294  TYR B CE1 1 
ATOM   5362 C  CE2 . TYR B 1 292 ? 25.261  15.982  -41.803 1.00 13.08 ?  294  TYR B CE2 1 
ATOM   5363 C  CZ  . TYR B 1 292 ? 24.799  15.091  -42.772 1.00 16.57 ?  294  TYR B CZ  1 
ATOM   5364 O  OH  . TYR B 1 292 ? 23.641  14.359  -42.570 1.00 18.58 ?  294  TYR B OH  1 
ATOM   5365 N  N   . GLN B 1 293 ? 30.038  14.944  -44.684 1.00 10.24 ?  295  GLN B N   1 
ATOM   5366 C  CA  . GLN B 1 293 ? 30.164  13.548  -45.104 1.00 13.75 ?  295  GLN B CA  1 
ATOM   5367 C  C   . GLN B 1 293 ? 31.526  12.946  -44.753 1.00 11.45 ?  295  GLN B C   1 
ATOM   5368 O  O   . GLN B 1 293 ? 31.607  11.748  -44.458 1.00 11.64 ?  295  GLN B O   1 
ATOM   5369 C  CB  . GLN B 1 293 ? 29.930  13.395  -46.614 1.00 13.47 ?  295  GLN B CB  1 
ATOM   5370 C  CG  . GLN B 1 293 ? 28.499  13.734  -47.070 1.00 12.47 ?  295  GLN B CG  1 
ATOM   5371 C  CD  . GLN B 1 293 ? 27.447  12.700  -46.660 1.00 15.42 ?  295  GLN B CD  1 
ATOM   5372 O  OE1 . GLN B 1 293 ? 27.762  11.645  -46.107 1.00 13.91 ?  295  GLN B OE1 1 
ATOM   5373 N  NE2 . GLN B 1 293 ? 26.177  13.006  -46.949 1.00 13.95 ?  295  GLN B NE2 1 
ATOM   5374 N  N   . ALA B 1 294 ? 32.591  13.751  -44.771 1.00 10.30 ?  296  ALA B N   1 
ATOM   5375 C  CA  . ALA B 1 294 ? 33.935  13.227  -44.525 1.00 9.93  ?  296  ALA B CA  1 
ATOM   5376 C  C   . ALA B 1 294 ? 34.113  12.664  -43.118 1.00 15.42 ?  296  ALA B C   1 
ATOM   5377 O  O   . ALA B 1 294 ? 35.073  11.916  -42.881 1.00 13.35 ?  296  ALA B O   1 
ATOM   5378 C  CB  . ALA B 1 294 ? 34.967  14.321  -44.797 1.00 10.65 ?  296  ALA B CB  1 
ATOM   5379 N  N   . VAL B 1 295 ? 33.235  13.020  -42.173 1.00 10.99 ?  297  VAL B N   1 
ATOM   5380 C  CA  . VAL B 1 295 ? 33.235  12.378  -40.857 1.00 9.89  ?  297  VAL B CA  1 
ATOM   5381 C  C   . VAL B 1 295 ? 33.150  10.857  -40.995 1.00 13.03 ?  297  VAL B C   1 
ATOM   5382 O  O   . VAL B 1 295 ? 33.650  10.114  -40.140 1.00 11.40 ?  297  VAL B O   1 
ATOM   5383 C  CB  . VAL B 1 295 ? 32.067  12.954  -40.016 1.00 12.79 ?  297  VAL B CB  1 
ATOM   5384 C  CG1 . VAL B 1 295 ? 31.855  12.167  -38.723 1.00 14.48 ?  297  VAL B CG1 1 
ATOM   5385 C  CG2 . VAL B 1 295 ? 32.298  14.433  -39.728 1.00 11.93 ?  297  VAL B CG2 1 
ATOM   5386 N  N   . LYS B 1 296 ? 32.533  10.365  -42.079 1.00 9.58  ?  298  LYS B N   1 
ATOM   5387 C  CA  . LYS B 1 296 ? 32.425  8.918   -42.292 1.00 9.90  ?  298  LYS B CA  1 
ATOM   5388 C  C   . LYS B 1 296 ? 33.792  8.244   -42.386 1.00 11.12 ?  298  LYS B C   1 
ATOM   5389 O  O   . LYS B 1 296 ? 33.943  7.085   -41.983 1.00 10.95 ?  298  LYS B O   1 
ATOM   5390 C  CB  . LYS B 1 296 ? 31.632  8.617   -43.567 1.00 13.87 ?  298  LYS B CB  1 
ATOM   5391 C  CG  . LYS B 1 296 ? 30.195  9.019   -43.489 1.00 11.31 ?  298  LYS B CG  1 
ATOM   5392 C  CD  . LYS B 1 296 ? 29.527  8.927   -44.852 1.00 10.85 ?  298  LYS B CD  1 
ATOM   5393 C  CE  . LYS B 1 296 ? 28.047  8.731   -44.651 1.00 14.43 ?  298  LYS B CE  1 
ATOM   5394 N  NZ  . LYS B 1 296 ? 27.280  8.820   -45.927 1.00 12.43 ?  298  LYS B NZ  1 
ATOM   5395 N  N   . GLY B 1 297 ? 34.785  8.926   -42.967 1.00 11.04 ?  299  GLY B N   1 
ATOM   5396 C  CA  . GLY B 1 297 ? 36.124  8.360   -43.013 1.00 11.21 ?  299  GLY B CA  1 
ATOM   5397 C  C   . GLY B 1 297 ? 36.740  8.240   -41.633 1.00 11.20 ?  299  GLY B C   1 
ATOM   5398 O  O   . GLY B 1 297 ? 37.503  7.304   -41.364 1.00 11.25 ?  299  GLY B O   1 
ATOM   5399 N  N   . LEU B 1 298 ? 36.393  9.157   -40.729 1.00 11.13 ?  300  LEU B N   1 
ATOM   5400 C  CA  . LEU B 1 298 ? 36.938  9.101   -39.373 1.00 8.46  ?  300  LEU B CA  1 
ATOM   5401 C  C   . LEU B 1 298 ? 36.294  7.975   -38.572 1.00 12.52 ?  300  LEU B C   1 
ATOM   5402 O  O   . LEU B 1 298 ? 36.991  7.207   -37.893 1.00 13.91 ?  300  LEU B O   1 
ATOM   5403 C  CB  . LEU B 1 298 ? 36.738  10.444  -38.666 1.00 9.10  ?  300  LEU B CB  1 
ATOM   5404 C  CG  . LEU B 1 298 ? 37.369  11.654  -39.358 1.00 9.76  ?  300  LEU B CG  1 
ATOM   5405 C  CD1 . LEU B 1 298 ? 36.969  12.942  -38.636 1.00 14.73 ?  300  LEU B CD1 1 
ATOM   5406 C  CD2 . LEU B 1 298 ? 38.889  11.519  -39.395 1.00 13.48 ?  300  LEU B CD2 1 
ATOM   5407 N  N   . THR B 1 299 ? 34.961  7.862   -38.634 1.00 11.05 ?  301  THR B N   1 
ATOM   5408 C  CA  . THR B 1 299 ? 34.295  6.793   -37.901 1.00 12.62 ?  301  THR B CA  1 
ATOM   5409 C  C   . THR B 1 299 ? 34.684  5.433   -38.456 1.00 13.10 ?  301  THR B C   1 
ATOM   5410 O  O   . THR B 1 299 ? 34.776  4.463   -37.700 1.00 14.96 ?  301  THR B O   1 
ATOM   5411 C  CB  . THR B 1 299 ? 32.774  6.951   -37.941 1.00 13.08 ?  301  THR B CB  1 
ATOM   5412 O  OG1 . THR B 1 299 ? 32.327  7.075   -39.294 1.00 17.54 ?  301  THR B OG1 1 
ATOM   5413 C  CG2 . THR B 1 299 ? 32.330  8.185   -37.180 1.00 15.35 ?  301  THR B CG2 1 
ATOM   5414 N  N   . GLY B 1 300 ? 34.930  5.355   -39.766 1.00 13.55 ?  302  GLY B N   1 
ATOM   5415 C  CA  . GLY B 1 300 ? 35.317  4.098   -40.380 1.00 12.63 ?  302  GLY B CA  1 
ATOM   5416 C  C   . GLY B 1 300 ? 36.667  3.601   -39.906 1.00 14.39 ?  302  GLY B C   1 
ATOM   5417 O  O   . GLY B 1 300 ? 36.920  2.395   -39.902 1.00 16.61 ?  302  GLY B O   1 
ATOM   5418 N  N   . ALA B 1 301 ? 37.553  4.515   -39.505 1.00 10.17 ?  303  ALA B N   1 
ATOM   5419 C  CA  . ALA B 1 301 ? 38.883  4.123   -39.050 1.00 13.72 ?  303  ALA B CA  1 
ATOM   5420 C  C   . ALA B 1 301 ? 38.909  3.683   -37.594 1.00 14.21 ?  303  ALA B C   1 
ATOM   5421 O  O   . ALA B 1 301 ? 39.873  3.024   -37.179 1.00 16.74 ?  303  ALA B O   1 
ATOM   5422 C  CB  . ALA B 1 301 ? 39.870  5.282   -39.245 1.00 16.10 ?  303  ALA B CB  1 
ATOM   5423 N  N   . LEU B 1 302 ? 37.887  4.029   -36.812 1.00 14.77 ?  304  LEU B N   1 
ATOM   5424 C  CA  . LEU B 1 302 ? 37.911  3.775   -35.371 1.00 16.65 ?  304  LEU B CA  1 
ATOM   5425 C  C   . LEU B 1 302 ? 38.212  2.337   -34.959 1.00 18.55 ?  304  LEU B C   1 
ATOM   5426 O  O   . LEU B 1 302 ? 38.955  2.160   -33.979 1.00 18.87 ?  304  LEU B O   1 
ATOM   5427 C  CB  . LEU B 1 302 ? 36.576  4.202   -34.750 1.00 15.63 ?  304  LEU B CB  1 
ATOM   5428 C  CG  . LEU B 1 302 ? 36.383  5.701   -34.560 1.00 18.58 ?  304  LEU B CG  1 
ATOM   5429 C  CD1 . LEU B 1 302 ? 35.031  5.974   -33.897 1.00 15.72 ?  304  LEU B CD1 1 
ATOM   5430 C  CD2 . LEU B 1 302 ? 37.529  6.286   -33.743 1.00 17.22 ?  304  LEU B CD2 1 
ATOM   5431 N  N   . PRO B 1 303 ? 37.679  1.294   -35.611 1.00 16.86 ?  305  PRO B N   1 
ATOM   5432 C  CA  . PRO B 1 303 ? 37.944  -0.077  -35.141 1.00 17.05 ?  305  PRO B CA  1 
ATOM   5433 C  C   . PRO B 1 303 ? 39.408  -0.459  -35.074 1.00 18.14 ?  305  PRO B C   1 
ATOM   5434 O  O   . PRO B 1 303 ? 39.751  -1.364  -34.301 1.00 19.95 ?  305  PRO B O   1 
ATOM   5435 C  CB  . PRO B 1 303 ? 37.213  -0.947  -36.175 1.00 18.42 ?  305  PRO B CB  1 
ATOM   5436 C  CG  . PRO B 1 303 ? 36.110  -0.090  -36.655 1.00 18.95 ?  305  PRO B CG  1 
ATOM   5437 C  CD  . PRO B 1 303 ? 36.710  1.288   -36.732 1.00 15.76 ?  305  PRO B CD  1 
ATOM   5438 N  N   . ILE B 1 304 ? 40.287  0.153   -35.866 1.00 12.42 ?  306  ILE B N   1 
ATOM   5439 C  CA  . ILE B 1 304 ? 41.671  -0.298  -35.903 1.00 13.73 ?  306  ILE B CA  1 
ATOM   5440 C  C   . ILE B 1 304 ? 42.645  0.710   -35.310 1.00 13.74 ?  306  ILE B C   1 
ATOM   5441 O  O   . ILE B 1 304 ? 43.850  0.424   -35.276 1.00 16.36 ?  306  ILE B O   1 
ATOM   5442 C  CB  . ILE B 1 304 ? 42.105  -0.689  -37.329 1.00 14.63 ?  306  ILE B CB  1 
ATOM   5443 C  CG1 . ILE B 1 304 ? 42.059  0.519   -38.271 1.00 11.31 ?  306  ILE B CG1 1 
ATOM   5444 C  CG2 . ILE B 1 304 ? 41.201  -1.809  -37.877 1.00 14.36 ?  306  ILE B CG2 1 
ATOM   5445 C  CD1 . ILE B 1 304 ? 42.870  0.311   -39.534 1.00 13.76 ?  306  ILE B CD1 1 
ATOM   5446 N  N   . VAL B 1 305 ? 42.183  1.863   -34.832 1.00 13.97 ?  307  VAL B N   1 
ATOM   5447 C  CA  . VAL B 1 305 ? 43.094  2.813   -34.190 1.00 15.21 ?  307  VAL B CA  1 
ATOM   5448 C  C   . VAL B 1 305 ? 43.141  2.543   -32.690 1.00 13.72 ?  307  VAL B C   1 
ATOM   5449 O  O   . VAL B 1 305 ? 42.134  2.210   -32.069 1.00 13.94 ?  307  VAL B O   1 
ATOM   5450 C  CB  . VAL B 1 305 ? 42.701  4.276   -34.505 1.00 17.20 ?  307  VAL B CB  1 
ATOM   5451 C  CG1 . VAL B 1 305 ? 41.410  4.669   -33.817 1.00 15.15 ?  307  VAL B CG1 1 
ATOM   5452 C  CG2 . VAL B 1 305 ? 43.825  5.221   -34.074 1.00 14.73 ?  307  VAL B CG2 1 
ATOM   5453 N  N   . LYS B 1 306 ? 44.336  2.639   -32.108 1.00 12.62 ?  308  LYS B N   1 
ATOM   5454 C  CA  . LYS B 1 306 ? 44.466  2.466   -30.673 1.00 14.30 ?  308  LYS B CA  1 
ATOM   5455 C  C   . LYS B 1 306 ? 43.836  3.649   -29.948 1.00 16.51 ?  308  LYS B C   1 
ATOM   5456 O  O   . LYS B 1 306 ? 43.894  4.783   -30.444 1.00 16.32 ?  308  LYS B O   1 
ATOM   5457 C  CB  . LYS B 1 306 ? 45.947  2.352   -30.282 1.00 14.63 ?  308  LYS B CB  1 
ATOM   5458 C  CG  . LYS B 1 306 ? 46.572  1.014   -30.657 1.00 19.68 ?  308  LYS B CG  1 
ATOM   5459 C  CD  . LYS B 1 306 ? 48.096  1.079   -30.735 1.00 27.69 ?  308  LYS B CD  1 
ATOM   5460 C  CE  . LYS B 1 306 ? 48.737  1.116   -29.377 1.00 31.55 ?  308  LYS B CE  1 
ATOM   5461 N  NZ  . LYS B 1 306 ? 50.222  0.972   -29.505 1.00 33.74 ?  308  LYS B NZ  1 
ATOM   5462 N  N   . PRO B 1 307 ? 43.223  3.425   -28.787 1.00 17.36 ?  309  PRO B N   1 
ATOM   5463 C  CA  . PRO B 1 307 ? 42.797  4.554   -27.952 1.00 17.78 ?  309  PRO B CA  1 
ATOM   5464 C  C   . PRO B 1 307 ? 43.954  5.523   -27.747 1.00 15.29 ?  309  PRO B C   1 
ATOM   5465 O  O   . PRO B 1 307 ? 45.075  5.124   -27.412 1.00 17.61 ?  309  PRO B O   1 
ATOM   5466 C  CB  . PRO B 1 307 ? 42.368  3.888   -26.635 1.00 19.42 ?  309  PRO B CB  1 
ATOM   5467 C  CG  . PRO B 1 307 ? 42.151  2.458   -26.967 1.00 24.54 ?  309  PRO B CG  1 
ATOM   5468 C  CD  . PRO B 1 307 ? 43.076  2.130   -28.103 1.00 22.72 ?  309  PRO B CD  1 
ATOM   5469 N  N   . GLY B 1 308 ? 43.694  6.799   -28.001 1.00 13.25 ?  310  GLY B N   1 
ATOM   5470 C  CA  . GLY B 1 308 ? 44.735  7.802   -27.965 1.00 13.79 ?  310  GLY B CA  1 
ATOM   5471 C  C   . GLY B 1 308 ? 45.569  7.905   -29.220 1.00 16.93 ?  310  GLY B C   1 
ATOM   5472 O  O   . GLY B 1 308 ? 46.475  8.754   -29.273 1.00 16.57 ?  310  GLY B O   1 
ATOM   5473 N  N   . GLY B 1 309 ? 45.325  7.056   -30.214 1.00 14.16 ?  311  GLY B N   1 
ATOM   5474 C  CA  . GLY B 1 309 ? 46.015  7.140   -31.484 1.00 9.33  ?  311  GLY B CA  1 
ATOM   5475 C  C   . GLY B 1 309 ? 45.535  8.332   -32.311 1.00 9.68  ?  311  GLY B C   1 
ATOM   5476 O  O   . GLY B 1 309 ? 44.795  9.209   -31.859 1.00 11.93 ?  311  GLY B O   1 
ATOM   5477 N  N   . THR B 1 310 ? 46.016  8.372   -33.546 1.00 8.63  ?  312  THR B N   1 
ATOM   5478 C  CA  . THR B 1 310 ? 45.749  9.496   -34.437 1.00 10.12 ?  312  THR B CA  1 
ATOM   5479 C  C   . THR B 1 310 ? 45.179  8.981   -35.746 1.00 10.11 ?  312  THR B C   1 
ATOM   5480 O  O   . THR B 1 310 ? 45.725  8.043   -36.340 1.00 10.49 ?  312  THR B O   1 
ATOM   5481 C  CB  . THR B 1 310 ? 47.020  10.300  -34.701 1.00 12.83 ?  312  THR B CB  1 
ATOM   5482 O  OG1 . THR B 1 310 ? 47.421  10.948  -33.486 1.00 13.92 ?  312  THR B OG1 1 
ATOM   5483 C  CG2 . THR B 1 310 ? 46.800  11.363  -35.787 1.00 12.87 ?  312  THR B CG2 1 
ATOM   5484 N  N   . ILE B 1 311 ? 44.098  9.605   -36.199 1.00 8.56  ?  313  ILE B N   1 
ATOM   5485 C  CA  . ILE B 1 311 ? 43.586  9.373   -37.540 1.00 6.59  ?  313  ILE B CA  1 
ATOM   5486 C  C   . ILE B 1 311 ? 43.984  10.564  -38.396 1.00 8.47  ?  313  ILE B C   1 
ATOM   5487 O  O   . ILE B 1 311 ? 43.690  11.711  -38.044 1.00 10.69 ?  313  ILE B O   1 
ATOM   5488 C  CB  . ILE B 1 311 ? 42.066  9.178   -37.551 1.00 8.91  ?  313  ILE B CB  1 
ATOM   5489 C  CG1 . ILE B 1 311 ? 41.669  7.995   -36.676 1.00 9.46  ?  313  ILE B CG1 1 
ATOM   5490 C  CG2 . ILE B 1 311 ? 41.588  8.992   -39.006 1.00 9.91  ?  313  ILE B CG2 1 
ATOM   5491 C  CD1 . ILE B 1 311 ? 40.197  7.988   -36.312 1.00 12.86 ?  313  ILE B CD1 1 
ATOM   5492 N  N   . VAL B 1 312 ? 44.661  10.291  -39.506 1.00 9.39  ?  314  VAL B N   1 
ATOM   5493 C  CA  . VAL B 1 312 ? 45.012  11.290  -40.510 1.00 8.14  ?  314  VAL B CA  1 
ATOM   5494 C  C   . VAL B 1 312 ? 44.085  11.075  -41.707 1.00 8.88  ?  314  VAL B C   1 
ATOM   5495 O  O   . VAL B 1 312 ? 44.109  10.002  -42.323 1.00 11.38 ?  314  VAL B O   1 
ATOM   5496 C  CB  . VAL B 1 312 ? 46.480  11.151  -40.935 1.00 9.04  ?  314  VAL B CB  1 
ATOM   5497 C  CG1 . VAL B 1 312 ? 46.815  12.154  -42.049 1.00 11.94 ?  314  VAL B CG1 1 
ATOM   5498 C  CG2 . VAL B 1 312 ? 47.437  11.304  -39.726 1.00 9.00  ?  314  VAL B CG2 1 
ATOM   5499 N  N   . ILE B 1 313 ? 43.277  12.071  -42.069 1.00 9.53  ?  315  ILE B N   1 
ATOM   5500 C  CA  . ILE B 1 313 ? 42.325  11.912  -43.173 1.00 7.32  ?  315  ILE B CA  1 
ATOM   5501 C  C   . ILE B 1 313 ? 42.577  12.988  -44.223 1.00 9.61  ?  315  ILE B C   1 
ATOM   5502 O  O   . ILE B 1 313 ? 42.862  14.141  -43.890 1.00 12.39 ?  315  ILE B O   1 
ATOM   5503 C  CB  . ILE B 1 313 ? 40.853  11.959  -42.708 1.00 7.41  ?  315  ILE B CB  1 
ATOM   5504 C  CG1 . ILE B 1 313 ? 39.909  11.699  -43.897 1.00 7.34  ?  315  ILE B CG1 1 
ATOM   5505 C  CG2 . ILE B 1 313 ? 40.504  13.328  -42.111 1.00 8.19  ?  315  ILE B CG2 1 
ATOM   5506 C  CD1 . ILE B 1 313 ? 38.417  11.589  -43.475 1.00 11.82 ?  315  ILE B CD1 1 
ATOM   5507 N  N   . ALA B 1 314 ? 42.504  12.595  -45.492 1.00 8.23  ?  316  ALA B N   1 
ATOM   5508 C  CA  . ALA B 1 314 ? 42.557  13.519  -46.613 1.00 9.06  ?  316  ALA B CA  1 
ATOM   5509 C  C   . ALA B 1 314 ? 41.202  13.512  -47.307 1.00 11.90 ?  316  ALA B C   1 
ATOM   5510 O  O   . ALA B 1 314 ? 40.641  12.443  -47.567 1.00 12.48 ?  316  ALA B O   1 
ATOM   5511 C  CB  . ALA B 1 314 ? 43.654  13.128  -47.606 1.00 12.06 ?  316  ALA B CB  1 
ATOM   5512 N  N   . ALA B 1 315 ? 40.669  14.698  -47.584 1.00 9.33  ?  317  ALA B N   1 
ATOM   5513 C  CA  . ALA B 1 315 ? 39.373  14.832  -48.242 1.00 10.13 ?  317  ALA B CA  1 
ATOM   5514 C  C   . ALA B 1 315 ? 39.364  16.152  -48.995 1.00 12.90 ?  317  ALA B C   1 
ATOM   5515 O  O   . ALA B 1 315 ? 39.855  17.152  -48.481 1.00 12.41 ?  317  ALA B O   1 
ATOM   5516 C  CB  . ALA B 1 315 ? 38.218  14.797  -47.231 1.00 14.54 ?  317  ALA B CB  1 
ATOM   5517 N  N   . ALA B 1 316 ? 38.792  16.164  -50.205 1.00 14.32 ?  318  ALA B N   1 
ATOM   5518 C  CA  . ALA B 1 316 ? 38.912  17.367  -51.029 1.00 17.27 ?  318  ALA B CA  1 
ATOM   5519 C  C   . ALA B 1 316 ? 38.002  18.489  -50.531 1.00 16.69 ?  318  ALA B C   1 
ATOM   5520 O  O   . ALA B 1 316 ? 38.380  19.665  -50.599 1.00 15.89 ?  318  ALA B O   1 
ATOM   5521 C  CB  . ALA B 1 316 ? 38.617  17.054  -52.495 1.00 13.82 ?  318  ALA B CB  1 
ATOM   5522 N  N   . LEU B 1 317 ? 36.803  18.151  -50.032 1.00 12.82 ?  319  LEU B N   1 
ATOM   5523 C  CA  . LEU B 1 317 ? 35.884  19.133  -49.437 1.00 14.13 ?  319  LEU B CA  1 
ATOM   5524 C  C   . LEU B 1 317 ? 35.520  20.229  -50.440 1.00 16.92 ?  319  LEU B C   1 
ATOM   5525 O  O   . LEU B 1 317 ? 35.448  21.410  -50.091 1.00 16.14 ?  319  LEU B O   1 
ATOM   5526 C  CB  . LEU B 1 317 ? 36.472  19.758  -48.169 1.00 15.82 ?  319  LEU B CB  1 
ATOM   5527 C  CG  . LEU B 1 317 ? 36.885  18.819  -47.040 1.00 14.85 ?  319  LEU B CG  1 
ATOM   5528 C  CD1 . LEU B 1 317 ? 37.274  19.627  -45.802 1.00 14.56 ?  319  LEU B CD1 1 
ATOM   5529 C  CD2 . LEU B 1 317 ? 35.757  17.869  -46.730 1.00 12.99 ?  319  LEU B CD2 1 
ATOM   5530 N  N   . ALA B 1 318 ? 35.286  19.833  -51.695 1.00 17.33 ?  320  ALA B N   1 
ATOM   5531 C  CA  . ALA B 1 318 ? 35.089  20.823  -52.752 1.00 19.87 ?  320  ALA B CA  1 
ATOM   5532 C  C   . ALA B 1 318 ? 33.880  21.714  -52.487 1.00 18.34 ?  320  ALA B C   1 
ATOM   5533 O  O   . ALA B 1 318 ? 33.859  22.867  -52.930 1.00 22.61 ?  320  ALA B O   1 
ATOM   5534 C  CB  . ALA B 1 318 ? 34.960  20.134  -54.115 1.00 19.71 ?  320  ALA B CB  1 
ATOM   5535 N  N   . GLU B 1 319 ? 32.879  21.218  -51.765 1.00 16.16 ?  321  GLU B N   1 
ATOM   5536 C  CA  . GLU B 1 319 ? 31.694  22.002  -51.439 1.00 19.14 ?  321  GLU B CA  1 
ATOM   5537 C  C   . GLU B 1 319 ? 31.766  22.666  -50.067 1.00 17.56 ?  321  GLU B C   1 
ATOM   5538 O  O   . GLU B 1 319 ? 30.794  23.309  -49.658 1.00 21.18 ?  321  GLU B O   1 
ATOM   5539 C  CB  . GLU B 1 319 ? 30.443  21.115  -51.507 1.00 22.02 ?  321  GLU B CB  1 
ATOM   5540 C  CG  . GLU B 1 319 ? 29.146  21.854  -51.715 1.00 28.19 ?  321  GLU B CG  1 
ATOM   5541 C  CD  . GLU B 1 319 ? 27.972  20.908  -51.948 1.00 34.38 ?  321  GLU B CD  1 
ATOM   5542 O  OE1 . GLU B 1 319 ? 26.927  21.085  -51.275 1.00 33.60 ?  321  GLU B OE1 1 
ATOM   5543 O  OE2 . GLU B 1 319 ? 28.102  19.978  -52.776 1.00 27.89 ?  321  GLU B OE2 1 
ATOM   5544 N  N   . GLY B 1 320 ? 32.873  22.521  -49.336 1.00 15.54 ?  322  GLY B N   1 
ATOM   5545 C  CA  . GLY B 1 320 ? 32.971  23.139  -48.024 1.00 21.97 ?  322  GLY B CA  1 
ATOM   5546 C  C   . GLY B 1 320 ? 32.490  22.299  -46.849 1.00 18.17 ?  322  GLY B C   1 
ATOM   5547 O  O   . GLY B 1 320 ? 32.642  21.080  -46.849 1.00 14.75 ?  322  GLY B O   1 
ATOM   5548 N  N   . LEU B 1 321 ? 31.879  22.944  -45.853 1.00 16.42 ?  323  LEU B N   1 
ATOM   5549 C  CA  . LEU B 1 321 ? 31.565  22.280  -44.588 1.00 12.73 ?  323  LEU B CA  1 
ATOM   5550 C  C   . LEU B 1 321 ? 30.284  21.469  -44.649 1.00 16.37 ?  323  LEU B C   1 
ATOM   5551 O  O   . LEU B 1 321 ? 30.171  20.434  -43.984 1.00 16.98 ?  323  LEU B O   1 
ATOM   5552 C  CB  . LEU B 1 321 ? 31.448  23.313  -43.470 1.00 13.93 ?  323  LEU B CB  1 
ATOM   5553 C  CG  . LEU B 1 321 ? 32.745  24.044  -43.101 1.00 18.15 ?  323  LEU B CG  1 
ATOM   5554 C  CD1 . LEU B 1 321 ? 32.546  24.839  -41.826 1.00 20.16 ?  323  LEU B CD1 1 
ATOM   5555 C  CD2 . LEU B 1 321 ? 33.864  23.061  -42.925 1.00 23.98 ?  323  LEU B CD2 1 
ATOM   5556 N  N   . GLY B 1 322 ? 29.287  21.946  -45.383 1.00 14.01 ?  324  GLY B N   1 
ATOM   5557 C  CA  . GLY B 1 322 ? 27.991  21.319  -45.305 1.00 15.61 ?  324  GLY B CA  1 
ATOM   5558 C  C   . GLY B 1 322 ? 26.916  22.367  -45.086 1.00 18.44 ?  324  GLY B C   1 
ATOM   5559 O  O   . GLY B 1 322 ? 27.136  23.565  -45.289 1.00 18.09 ?  324  GLY B O   1 
ATOM   5560 N  N   . SER B 1 323 ? 25.749  21.902  -44.657 1.00 16.88 ?  325  SER B N   1 
ATOM   5561 C  CA  . SER B 1 323 ? 24.558  22.737  -44.588 1.00 21.52 ?  325  SER B CA  1 
ATOM   5562 C  C   . SER B 1 323 ? 24.749  23.914  -43.627 1.00 23.02 ?  325  SER B C   1 
ATOM   5563 O  O   . SER B 1 323 ? 25.576  23.863  -42.712 1.00 19.98 ?  325  SER B O   1 
ATOM   5564 C  CB  . SER B 1 323 ? 23.366  21.886  -44.156 1.00 21.14 ?  325  SER B CB  1 
ATOM   5565 O  OG  . SER B 1 323 ? 23.460  21.581  -42.772 1.00 23.41 ?  325  SER B OG  1 
ATOM   5566 N  N   . PRO B 1 324 ? 23.987  24.996  -43.818 1.00 28.33 ?  326  PRO B N   1 
ATOM   5567 C  CA  . PRO B 1 324 ? 24.049  26.103  -42.848 1.00 23.39 ?  326  PRO B CA  1 
ATOM   5568 C  C   . PRO B 1 324 ? 23.664  25.681  -41.439 1.00 21.77 ?  326  PRO B C   1 
ATOM   5569 O  O   . PRO B 1 324 ? 24.196  26.227  -40.464 1.00 22.52 ?  326  PRO B O   1 
ATOM   5570 C  CB  . PRO B 1 324 ? 23.058  27.126  -43.425 1.00 26.29 ?  326  PRO B CB  1 
ATOM   5571 C  CG  . PRO B 1 324 ? 22.974  26.770  -44.884 1.00 26.81 ?  326  PRO B CG  1 
ATOM   5572 C  CD  . PRO B 1 324 ? 23.021  25.275  -44.899 1.00 23.95 ?  326  PRO B CD  1 
ATOM   5573 N  N   . GLU B 1 325 ? 22.756  24.712  -41.308 1.00 23.26 ?  327  GLU B N   1 
ATOM   5574 C  CA  . GLU B 1 325 ? 22.362  24.216  -39.994 1.00 25.53 ?  327  GLU B CA  1 
ATOM   5575 C  C   . GLU B 1 325 ? 23.523  23.487  -39.332 1.00 21.18 ?  327  GLU B C   1 
ATOM   5576 O  O   . GLU B 1 325 ? 23.829  23.716  -38.155 1.00 20.89 ?  327  GLU B O   1 
ATOM   5577 C  CB  . GLU B 1 325 ? 21.161  23.287  -40.146 1.00 25.23 ?  327  GLU B CB  1 
ATOM   5578 C  CG  . GLU B 1 325 ? 19.855  24.018  -40.443 1.00 27.56 ?  327  GLU B CG  1 
ATOM   5579 C  CD  . GLU B 1 325 ? 19.569  24.091  -41.940 1.00 33.55 ?  327  GLU B CD  1 
ATOM   5580 O  OE1 . GLU B 1 325 ? 20.513  23.912  -42.747 1.00 26.62 ?  327  GLU B OE1 1 
ATOM   5581 O  OE2 . GLU B 1 325 ? 18.398  24.324  -42.315 1.00 41.67 ?  327  GLU B OE2 1 
ATOM   5582 N  N   . PHE B 1 326 ? 24.178  22.601  -40.089 1.00 18.15 ?  328  PHE B N   1 
ATOM   5583 C  CA  . PHE B 1 326 ? 25.378  21.919  -39.614 1.00 18.34 ?  328  PHE B CA  1 
ATOM   5584 C  C   . PHE B 1 326 ? 26.426  22.922  -39.139 1.00 20.94 ?  328  PHE B C   1 
ATOM   5585 O  O   . PHE B 1 326 ? 26.973  22.793  -38.037 1.00 18.17 ?  328  PHE B O   1 
ATOM   5586 C  CB  . PHE B 1 326 ? 25.931  21.032  -40.737 1.00 15.27 ?  328  PHE B CB  1 
ATOM   5587 C  CG  . PHE B 1 326 ? 27.167  20.248  -40.364 1.00 15.67 ?  328  PHE B CG  1 
ATOM   5588 C  CD1 . PHE B 1 326 ? 27.144  19.340  -39.320 1.00 14.84 ?  328  PHE B CD1 1 
ATOM   5589 C  CD2 . PHE B 1 326 ? 28.345  20.405  -41.081 1.00 15.16 ?  328  PHE B CD2 1 
ATOM   5590 C  CE1 . PHE B 1 326 ? 28.273  18.602  -38.984 1.00 16.11 ?  328  PHE B CE1 1 
ATOM   5591 C  CE2 . PHE B 1 326 ? 29.491  19.675  -40.749 1.00 18.07 ?  328  PHE B CE2 1 
ATOM   5592 C  CZ  . PHE B 1 326 ? 29.450  18.772  -39.697 1.00 18.79 ?  328  PHE B CZ  1 
ATOM   5593 N  N   . GLN B 1 327 ? 26.712  23.940  -39.958 1.00 19.44 ?  329  GLN B N   1 
ATOM   5594 C  CA  . GLN B 1 327 ? 27.738  24.916  -39.590 1.00 19.62 ?  329  GLN B CA  1 
ATOM   5595 C  C   . GLN B 1 327 ? 27.364  25.697  -38.334 1.00 19.97 ?  329  GLN B C   1 
ATOM   5596 O  O   . GLN B 1 327 ? 28.248  26.073  -37.551 1.00 19.12 ?  329  GLN B O   1 
ATOM   5597 C  CB  . GLN B 1 327 ? 27.986  25.877  -40.751 1.00 19.67 ?  329  GLN B CB  1 
ATOM   5598 C  CG  . GLN B 1 327 ? 28.470  25.187  -42.001 1.00 21.44 ?  329  GLN B CG  1 
ATOM   5599 C  CD  . GLN B 1 327 ? 28.888  26.164  -43.065 1.00 27.28 ?  329  GLN B CD  1 
ATOM   5600 O  OE1 . GLN B 1 327 ? 29.521  27.184  -42.769 1.00 26.84 ?  329  GLN B OE1 1 
ATOM   5601 N  NE2 . GLN B 1 327 ? 28.554  25.858  -44.316 1.00 22.72 ?  329  GLN B NE2 1 
ATOM   5602 N  N   . SER B 1 328 ? 26.066  25.929  -38.116 1.00 20.44 ?  330  SER B N   1 
ATOM   5603 C  CA  . SER B 1 328 ? 25.624  26.706  -36.959 1.00 20.42 ?  330  SER B CA  1 
ATOM   5604 C  C   . SER B 1 328 ? 25.959  26.012  -35.646 1.00 25.91 ?  330  SER B C   1 
ATOM   5605 O  O   . SER B 1 328 ? 26.156  26.681  -34.625 1.00 23.14 ?  330  SER B O   1 
ATOM   5606 C  CB  . SER B 1 328 ? 24.124  26.987  -37.052 1.00 21.91 ?  330  SER B CB  1 
ATOM   5607 O  OG  . SER B 1 328 ? 23.342  25.853  -36.694 1.00 22.96 ?  330  SER B OG  1 
ATOM   5608 N  N   . LEU B 1 329 ? 26.066  24.683  -35.654 1.00 26.04 ?  331  LEU B N   1 
ATOM   5609 C  CA  . LEU B 1 329 ? 26.327  23.972  -34.406 1.00 22.54 ?  331  LEU B CA  1 
ATOM   5610 C  C   . LEU B 1 329 ? 27.739  24.218  -33.891 1.00 21.69 ?  331  LEU B C   1 
ATOM   5611 O  O   . LEU B 1 329 ? 27.965  24.185  -32.676 1.00 22.07 ?  331  LEU B O   1 
ATOM   5612 C  CB  . LEU B 1 329 ? 26.075  22.473  -34.585 1.00 17.53 ?  331  LEU B CB  1 
ATOM   5613 C  CG  . LEU B 1 329 ? 24.614  22.113  -34.877 1.00 22.59 ?  331  LEU B CG  1 
ATOM   5614 C  CD1 . LEU B 1 329 ? 24.525  20.720  -35.448 1.00 26.63 ?  331  LEU B CD1 1 
ATOM   5615 C  CD2 . LEU B 1 329 ? 23.722  22.237  -33.635 1.00 23.37 ?  331  LEU B CD2 1 
ATOM   5616 N  N   . PHE B 1 330 ? 28.698  24.467  -34.782 1.00 20.38 ?  332  PHE B N   1 
ATOM   5617 C  CA  . PHE B 1 330 ? 30.038  24.797  -34.308 1.00 20.36 ?  332  PHE B CA  1 
ATOM   5618 C  C   . PHE B 1 330 ? 30.072  26.177  -33.665 1.00 29.98 ?  332  PHE B C   1 
ATOM   5619 O  O   . PHE B 1 330 ? 30.819  26.391  -32.702 1.00 27.97 ?  332  PHE B O   1 
ATOM   5620 C  CB  . PHE B 1 330 ? 31.046  24.725  -35.449 1.00 23.04 ?  332  PHE B CB  1 
ATOM   5621 C  CG  . PHE B 1 330 ? 31.181  23.359  -36.052 1.00 24.91 ?  332  PHE B CG  1 
ATOM   5622 C  CD1 . PHE B 1 330 ? 30.344  22.949  -37.079 1.00 22.91 ?  332  PHE B CD1 1 
ATOM   5623 C  CD2 . PHE B 1 330 ? 32.146  22.483  -35.589 1.00 20.36 ?  332  PHE B CD2 1 
ATOM   5624 C  CE1 . PHE B 1 330 ? 30.472  21.685  -37.640 1.00 22.14 ?  332  PHE B CE1 1 
ATOM   5625 C  CE2 . PHE B 1 330 ? 32.281  21.225  -36.141 1.00 21.74 ?  332  PHE B CE2 1 
ATOM   5626 C  CZ  . PHE B 1 330 ? 31.442  20.825  -37.172 1.00 21.75 ?  332  PHE B CZ  1 
ATOM   5627 N  N   . GLU B 1 331 ? 29.283  27.118  -34.192 1.00 24.11 ?  333  GLU B N   1 
ATOM   5628 C  CA  . GLU B 1 331 ? 29.169  28.440  -33.586 1.00 27.86 ?  333  GLU B CA  1 
ATOM   5629 C  C   . GLU B 1 331 ? 28.423  28.382  -32.258 1.00 23.87 ?  333  GLU B C   1 
ATOM   5630 O  O   . GLU B 1 331 ? 28.810  29.052  -31.297 1.00 34.65 ?  333  GLU B O   1 
ATOM   5631 C  CB  . GLU B 1 331 ? 28.456  29.397  -34.548 1.00 26.09 ?  333  GLU B CB  1 
ATOM   5632 N  N   . GLU B 1 332 ? 27.346  27.595  -32.184 1.00 25.89 ?  334  GLU B N   1 
ATOM   5633 C  CA  . GLU B 1 332 ? 26.562  27.532  -30.952 1.00 26.84 ?  334  GLU B CA  1 
ATOM   5634 C  C   . GLU B 1 332 ? 27.311  26.822  -29.819 1.00 27.54 ?  334  GLU B C   1 
ATOM   5635 O  O   . GLU B 1 332 ? 27.137  27.180  -28.647 1.00 27.95 ?  334  GLU B O   1 
ATOM   5636 C  CB  . GLU B 1 332 ? 25.222  26.846  -31.216 1.00 27.25 ?  334  GLU B CB  1 
ATOM   5637 N  N   . HIS B 1 333 ? 28.131  25.820  -30.134 1.00 24.67 ?  335  HIS B N   1 
ATOM   5638 C  CA  . HIS B 1 333 ? 28.828  25.022  -29.120 1.00 28.85 ?  335  HIS B CA  1 
ATOM   5639 C  C   . HIS B 1 333 ? 30.319  24.970  -29.418 1.00 26.66 ?  335  HIS B C   1 
ATOM   5640 O  O   . HIS B 1 333 ? 30.755  24.176  -30.270 1.00 31.39 ?  335  HIS B O   1 
ATOM   5641 C  CB  . HIS B 1 333 ? 28.267  23.603  -29.041 1.00 26.68 ?  335  HIS B CB  1 
ATOM   5642 C  CG  . HIS B 1 333 ? 26.775  23.541  -28.979 1.00 23.98 ?  335  HIS B CG  1 
ATOM   5643 N  ND1 . HIS B 1 333 ? 26.079  23.635  -27.792 1.00 28.59 ?  335  HIS B ND1 1 
ATOM   5644 C  CD2 . HIS B 1 333 ? 25.843  23.392  -29.951 1.00 25.70 ?  335  HIS B CD2 1 
ATOM   5645 C  CE1 . HIS B 1 333 ? 24.783  23.553  -28.037 1.00 29.15 ?  335  HIS B CE1 1 
ATOM   5646 N  NE2 . HIS B 1 333 ? 24.613  23.403  -29.339 1.00 28.04 ?  335  HIS B NE2 1 
ATOM   5647 N  N   . PRO B 1 334 ? 31.141  25.762  -28.720 1.00 27.16 ?  336  PRO B N   1 
ATOM   5648 C  CA  . PRO B 1 334 ? 32.586  25.714  -28.980 1.00 29.74 ?  336  PRO B CA  1 
ATOM   5649 C  C   . PRO B 1 334 ? 33.257  24.441  -28.486 1.00 28.46 ?  336  PRO B C   1 
ATOM   5650 O  O   . PRO B 1 334 ? 34.374  24.147  -28.925 1.00 27.66 ?  336  PRO B O   1 
ATOM   5651 C  CB  . PRO B 1 334 ? 33.116  26.952  -28.246 1.00 27.27 ?  336  PRO B CB  1 
ATOM   5652 C  CG  . PRO B 1 334 ? 32.133  27.188  -27.171 1.00 33.51 ?  336  PRO B CG  1 
ATOM   5653 C  CD  . PRO B 1 334 ? 30.795  26.787  -27.720 1.00 28.36 ?  336  PRO B CD  1 
ATOM   5654 N  N   . THR B 1 335 ? 32.628  23.672  -27.600 1.00 21.27 ?  337  THR B N   1 
ATOM   5655 C  CA  . THR B 1 335 ? 33.180  22.400  -27.165 1.00 21.43 ?  337  THR B CA  1 
ATOM   5656 C  C   . THR B 1 335 ? 32.245  21.269  -27.564 1.00 17.36 ?  337  THR B C   1 
ATOM   5657 O  O   . THR B 1 335 ? 31.019  21.439  -27.591 1.00 18.29 ?  337  THR B O   1 
ATOM   5658 C  CB  . THR B 1 335 ? 33.400  22.362  -25.648 1.00 18.78 ?  337  THR B CB  1 
ATOM   5659 O  OG1 . THR B 1 335 ? 32.128  22.371  -24.984 1.00 20.72 ?  337  THR B OG1 1 
ATOM   5660 C  CG2 . THR B 1 335 ? 34.248  23.554  -25.182 1.00 25.45 ?  337  THR B CG2 1 
ATOM   5661 N  N   . LEU B 1 336 ? 32.833  20.108  -27.879 1.00 15.76 ?  338  LEU B N   1 
ATOM   5662 C  CA  . LEU B 1 336 ? 32.001  18.950  -28.198 1.00 18.71 ?  338  LEU B CA  1 
ATOM   5663 C  C   . LEU B 1 336 ? 31.275  18.427  -26.966 1.00 12.98 ?  338  LEU B C   1 
ATOM   5664 O  O   . LEU B 1 336 ? 30.173  17.872  -27.083 1.00 15.17 ?  338  LEU B O   1 
ATOM   5665 C  CB  . LEU B 1 336 ? 32.824  17.813  -28.803 1.00 23.21 ?  338  LEU B CB  1 
ATOM   5666 C  CG  . LEU B 1 336 ? 33.277  18.010  -30.247 1.00 25.64 ?  338  LEU B CG  1 
ATOM   5667 C  CD1 . LEU B 1 336 ? 34.618  17.301  -30.496 1.00 24.80 ?  338  LEU B CD1 1 
ATOM   5668 C  CD2 . LEU B 1 336 ? 32.173  17.617  -31.207 1.00 21.97 ?  338  LEU B CD2 1 
ATOM   5669 N  N   . GLU B 1 337 ? 31.892  18.561  -25.793 1.00 14.95 ?  339  GLU B N   1 
ATOM   5670 C  CA  . GLU B 1 337 ? 31.237  18.152  -24.553 1.00 17.17 ?  339  GLU B CA  1 
ATOM   5671 C  C   . GLU B 1 337 ? 29.947  18.934  -24.325 1.00 19.60 ?  339  GLU B C   1 
ATOM   5672 O  O   . GLU B 1 337 ? 28.907  18.356  -23.983 1.00 17.40 ?  339  GLU B O   1 
ATOM   5673 C  CB  . GLU B 1 337 ? 32.209  18.338  -23.383 1.00 16.41 ?  339  GLU B CB  1 
ATOM   5674 C  CG  . GLU B 1 337 ? 33.457  17.443  -23.488 1.00 26.65 ?  339  GLU B CG  1 
ATOM   5675 C  CD  . GLU B 1 337 ? 34.521  17.975  -24.463 1.00 32.37 ?  339  GLU B CD  1 
ATOM   5676 O  OE1 . GLU B 1 337 ? 34.483  19.172  -24.818 1.00 31.38 ?  339  GLU B OE1 1 
ATOM   5677 O  OE2 . GLU B 1 337 ? 35.396  17.187  -24.884 1.00 41.64 ?  339  GLU B OE2 1 
ATOM   5678 N  N   . GLY B 1 338 ? 29.994  20.255  -24.510 1.00 16.95 ?  340  GLY B N   1 
ATOM   5679 C  CA  . GLY B 1 338 ? 28.786  21.053  -24.372 1.00 14.18 ?  340  GLY B CA  1 
ATOM   5680 C  C   . GLY B 1 338 ? 27.771  20.792  -25.466 1.00 14.62 ?  340  GLY B C   1 
ATOM   5681 O  O   . GLY B 1 338 ? 26.562  20.916  -25.242 1.00 16.14 ?  340  GLY B O   1 
ATOM   5682 N  N   . PHE B 1 339 ? 28.243  20.453  -26.664 1.00 15.29 ?  341  PHE B N   1 
ATOM   5683 C  CA  . PHE B 1 339 ? 27.332  20.041  -27.722 1.00 16.74 ?  341  PHE B CA  1 
ATOM   5684 C  C   . PHE B 1 339 ? 26.601  18.755  -27.344 1.00 14.99 ?  341  PHE B C   1 
ATOM   5685 O  O   . PHE B 1 339 ? 25.367  18.680  -27.449 1.00 14.26 ?  341  PHE B O   1 
ATOM   5686 C  CB  . PHE B 1 339 ? 28.097  19.871  -29.038 1.00 13.32 ?  341  PHE B CB  1 
ATOM   5687 C  CG  . PHE B 1 339 ? 27.331  19.080  -30.074 1.00 12.93 ?  341  PHE B CG  1 
ATOM   5688 C  CD1 . PHE B 1 339 ? 26.277  19.663  -30.769 1.00 13.92 ?  341  PHE B CD1 1 
ATOM   5689 C  CD2 . PHE B 1 339 ? 27.646  17.746  -30.325 1.00 15.04 ?  341  PHE B CD2 1 
ATOM   5690 C  CE1 . PHE B 1 339 ? 25.557  18.938  -31.703 1.00 16.35 ?  341  PHE B CE1 1 
ATOM   5691 C  CE2 . PHE B 1 339 ? 26.932  17.011  -31.259 1.00 16.16 ?  341  PHE B CE2 1 
ATOM   5692 C  CZ  . PHE B 1 339 ? 25.881  17.609  -31.953 1.00 13.49 ?  341  PHE B CZ  1 
ATOM   5693 N  N   . MET B 1 340 ? 27.355  17.718  -26.928 1.00 14.54 ?  342  MET B N   1 
ATOM   5694 C  CA  . MET B 1 340 ? 26.750  16.486  -26.405 1.00 12.14 ?  342  MET B CA  1 
ATOM   5695 C  C   . MET B 1 340 ? 25.790  16.738  -25.254 1.00 15.65 ?  342  MET B C   1 
ATOM   5696 O  O   . MET B 1 340 ? 24.723  16.116  -25.184 1.00 14.23 ?  342  MET B O   1 
ATOM   5697 C  CB  . MET B 1 340 ? 27.837  15.496  -25.978 1.00 12.41 ?  342  MET B CB  1 
ATOM   5698 C  CG  . MET B 1 340 ? 28.684  14.795  -27.058 1.00 13.60 ?  342  MET B CG  1 
ATOM   5699 S  SD  . MET B 1 340 ? 27.687  14.146  -28.424 1.00 17.59 ?  342  MET B SD  1 
ATOM   5700 C  CE  . MET B 1 340 ? 27.076  12.666  -27.586 1.00 16.25 ?  342  MET B CE  1 
ATOM   5701 N  N   . GLU B 1 341 ? 26.153  17.633  -24.335 1.00 12.77 ?  343  GLU B N   1 
ATOM   5702 C  CA  . GLU B 1 341 ? 25.260  17.928  -23.215 1.00 13.56 ?  343  GLU B CA  1 
ATOM   5703 C  C   . GLU B 1 341 ? 23.922  18.446  -23.718 1.00 18.09 ?  343  GLU B C   1 
ATOM   5704 O  O   . GLU B 1 341 ? 22.859  18.024  -23.244 1.00 16.22 ?  343  GLU B O   1 
ATOM   5705 C  CB  . GLU B 1 341 ? 25.920  18.943  -22.272 1.00 19.58 ?  343  GLU B CB  1 
ATOM   5706 C  CG  . GLU B 1 341 ? 25.206  19.102  -20.933 1.00 29.45 ?  343  GLU B CG  1 
ATOM   5707 N  N   . ALA B 1 342 ? 23.956  19.329  -24.712 1.00 18.78 ?  344  ALA B N   1 
ATOM   5708 C  CA  . ALA B 1 342 ? 22.722  19.879  -25.258 1.00 14.79 ?  344  ALA B CA  1 
ATOM   5709 C  C   . ALA B 1 342 ? 21.881  18.812  -25.951 1.00 17.79 ?  344  ALA B C   1 
ATOM   5710 O  O   . ALA B 1 342 ? 20.673  18.718  -25.707 1.00 20.40 ?  344  ALA B O   1 
ATOM   5711 C  CB  . ALA B 1 342 ? 23.041  21.020  -26.223 1.00 17.03 ?  344  ALA B CB  1 
ATOM   5712 N  N   . ILE B 1 343 ? 22.485  18.007  -26.839 1.00 17.01 ?  345  ILE B N   1 
ATOM   5713 C  CA  . ILE B 1 343 ? 21.637  17.134  -27.658 1.00 15.53 ?  345  ILE B CA  1 
ATOM   5714 C  C   . ILE B 1 343 ? 21.110  15.947  -26.856 1.00 15.13 ?  345  ILE B C   1 
ATOM   5715 O  O   . ILE B 1 343 ? 20.018  15.447  -27.136 1.00 18.09 ?  345  ILE B O   1 
ATOM   5716 C  CB  . ILE B 1 343 ? 22.345  16.678  -28.955 1.00 16.33 ?  345  ILE B CB  1 
ATOM   5717 C  CG1 . ILE B 1 343 ? 23.584  15.819  -28.689 1.00 18.07 ?  345  ILE B CG1 1 
ATOM   5718 C  CG2 . ILE B 1 343 ? 22.653  17.878  -29.849 1.00 15.87 ?  345  ILE B CG2 1 
ATOM   5719 C  CD1 . ILE B 1 343 ? 23.886  14.838  -29.838 1.00 21.90 ?  345  ILE B CD1 1 
ATOM   5720 N  N   . LEU B 1 344 ? 21.836  15.499  -25.827 1.00 18.09 ?  346  LEU B N   1 
ATOM   5721 C  CA  . LEU B 1 344 ? 21.349  14.380  -25.023 1.00 15.63 ?  346  LEU B CA  1 
ATOM   5722 C  C   . LEU B 1 344 ? 20.070  14.725  -24.265 1.00 18.85 ?  346  LEU B C   1 
ATOM   5723 O  O   . LEU B 1 344 ? 19.340  13.814  -23.856 1.00 19.38 ?  346  LEU B O   1 
ATOM   5724 C  CB  . LEU B 1 344 ? 22.434  13.922  -24.041 1.00 14.46 ?  346  LEU B CB  1 
ATOM   5725 C  CG  . LEU B 1 344 ? 23.525  13.109  -24.719 1.00 16.22 ?  346  LEU B CG  1 
ATOM   5726 C  CD1 . LEU B 1 344 ? 24.728  12.957  -23.786 1.00 15.92 ?  346  LEU B CD1 1 
ATOM   5727 C  CD2 . LEU B 1 344 ? 22.995  11.755  -25.132 1.00 23.43 ?  346  LEU B CD2 1 
ATOM   5728 N  N   . LYS B 1 345 ? 19.778  16.016  -24.077 1.00 20.50 ?  347  LYS B N   1 
ATOM   5729 C  CA  . LYS B 1 345 ? 18.534  16.427  -23.429 1.00 23.27 ?  347  LYS B CA  1 
ATOM   5730 C  C   . LYS B 1 345 ? 17.317  16.254  -24.331 1.00 34.38 ?  347  LYS B C   1 
ATOM   5731 O  O   . LYS B 1 345 ? 16.194  16.148  -23.823 1.00 33.10 ?  347  LYS B O   1 
ATOM   5732 C  CB  . LYS B 1 345 ? 18.625  17.891  -22.990 1.00 26.92 ?  347  LYS B CB  1 
ATOM   5733 C  CG  . LYS B 1 345 ? 19.600  18.165  -21.858 1.00 21.41 ?  347  LYS B CG  1 
ATOM   5734 C  CD  . LYS B 1 345 ? 20.059  19.616  -21.900 1.00 23.14 ?  347  LYS B CD  1 
ATOM   5735 C  CE  . LYS B 1 345 ? 21.030  19.933  -20.780 1.00 25.62 ?  347  LYS B CE  1 
ATOM   5736 N  NZ  . LYS B 1 345 ? 21.139  21.410  -20.556 1.00 30.30 ?  347  LYS B NZ  1 
ATOM   5737 N  N   . GLU B 1 346 ? 17.513  16.237  -25.652 1.00 27.91 ?  348  GLU B N   1 
ATOM   5738 C  CA  . GLU B 1 346 ? 16.413  16.159  -26.624 1.00 27.95 ?  348  GLU B CA  1 
ATOM   5739 C  C   . GLU B 1 346 ? 15.359  17.243  -26.396 1.00 30.79 ?  348  GLU B C   1 
ATOM   5740 O  O   . GLU B 1 346 ? 14.174  17.051  -26.675 1.00 31.11 ?  348  GLU B O   1 
ATOM   5741 C  CB  . GLU B 1 346 ? 15.780  14.767  -26.630 1.00 25.01 ?  348  GLU B CB  1 
ATOM   5742 C  CG  . GLU B 1 346 ? 16.803  13.660  -26.475 1.00 29.61 ?  348  GLU B CG  1 
ATOM   5743 C  CD  . GLU B 1 346 ? 16.300  12.316  -26.928 1.00 39.23 ?  348  GLU B CD  1 
ATOM   5744 O  OE1 . GLU B 1 346 ? 17.095  11.350  -26.913 1.00 33.93 ?  348  GLU B OE1 1 
ATOM   5745 O  OE2 . GLU B 1 346 ? 15.120  12.226  -27.332 1.00 46.39 ?  348  GLU B OE2 1 
ATOM   5746 N  N   . GLU B 1 347 ? 15.781  18.403  -25.896 1.00 34.68 ?  349  GLU B N   1 
ATOM   5747 C  CA  . GLU B 1 347 ? 14.897  19.555  -25.794 1.00 35.42 ?  349  GLU B CA  1 
ATOM   5748 C  C   . GLU B 1 347 ? 14.870  20.371  -27.076 1.00 40.45 ?  349  GLU B C   1 
ATOM   5749 O  O   . GLU B 1 347 ? 14.016  21.252  -27.222 1.00 44.64 ?  349  GLU B O   1 
ATOM   5750 C  CB  . GLU B 1 347 ? 15.312  20.450  -24.619 1.00 34.14 ?  349  GLU B CB  1 
ATOM   5751 N  N   . SER B 1 348 ? 15.783  20.094  -28.001 1.00 35.28 ?  350  SER B N   1 
ATOM   5752 C  CA  . SER B 1 348 ? 15.785  20.711  -29.313 1.00 33.62 ?  350  SER B CA  1 
ATOM   5753 C  C   . SER B 1 348 ? 16.412  19.724  -30.284 1.00 31.74 ?  350  SER B C   1 
ATOM   5754 O  O   . SER B 1 348 ? 17.139  18.806  -29.891 1.00 31.51 ?  350  SER B O   1 
ATOM   5755 C  CB  . SER B 1 348 ? 16.550  22.040  -29.325 1.00 29.96 ?  350  SER B CB  1 
ATOM   5756 O  OG  . SER B 1 348 ? 17.828  21.882  -28.728 1.00 45.86 ?  350  SER B OG  1 
ATOM   5757 N  N   . PHE B 1 349 ? 16.116  19.918  -31.560 1.00 24.18 ?  351  PHE B N   1 
ATOM   5758 C  CA  . PHE B 1 349 ? 16.676  19.092  -32.617 1.00 23.67 ?  351  PHE B CA  1 
ATOM   5759 C  C   . PHE B 1 349 ? 17.094  20.034  -33.732 1.00 28.27 ?  351  PHE B C   1 
ATOM   5760 O  O   . PHE B 1 349 ? 16.324  20.921  -34.114 1.00 23.54 ?  351  PHE B O   1 
ATOM   5761 C  CB  . PHE B 1 349 ? 15.657  18.058  -33.113 1.00 26.98 ?  351  PHE B CB  1 
ATOM   5762 C  CG  . PHE B 1 349 ? 15.343  16.973  -32.109 1.00 25.56 ?  351  PHE B CG  1 
ATOM   5763 C  CD1 . PHE B 1 349 ? 14.232  17.078  -31.289 1.00 31.54 ?  351  PHE B CD1 1 
ATOM   5764 C  CD2 . PHE B 1 349 ? 16.143  15.847  -31.992 1.00 34.66 ?  351  PHE B CD2 1 
ATOM   5765 C  CE1 . PHE B 1 349 ? 13.930  16.094  -30.358 1.00 26.06 ?  351  PHE B CE1 1 
ATOM   5766 C  CE2 . PHE B 1 349 ? 15.840  14.855  -31.062 1.00 29.59 ?  351  PHE B CE2 1 
ATOM   5767 C  CZ  . PHE B 1 349 ? 14.727  14.983  -30.250 1.00 25.70 ?  351  PHE B CZ  1 
ATOM   5768 N  N   . THR B 1 350 ? 18.322  19.876  -34.212 1.00 20.81 ?  352  THR B N   1 
ATOM   5769 C  CA  . THR B 1 350 ? 18.865  20.680  -35.297 1.00 23.99 ?  352  THR B CA  1 
ATOM   5770 C  C   . THR B 1 350 ? 19.195  19.752  -36.455 1.00 24.59 ?  352  THR B C   1 
ATOM   5771 O  O   . THR B 1 350 ? 19.761  18.676  -36.239 1.00 18.84 ?  352  THR B O   1 
ATOM   5772 C  CB  . THR B 1 350 ? 20.115  21.444  -34.831 1.00 22.20 ?  352  THR B CB  1 
ATOM   5773 O  OG1 . THR B 1 350 ? 19.764  22.296  -33.733 1.00 26.57 ?  352  THR B OG1 1 
ATOM   5774 C  CG2 . THR B 1 350 ? 20.720  22.281  -35.954 1.00 21.18 ?  352  THR B CG2 1 
ATOM   5775 N  N   . VAL B 1 351 ? 18.806  20.151  -37.671 1.00 21.14 ?  353  VAL B N   1 
ATOM   5776 C  CA  . VAL B 1 351 ? 19.170  19.387  -38.856 1.00 17.76 ?  353  VAL B CA  1 
ATOM   5777 C  C   . VAL B 1 351 ? 20.671  19.139  -38.851 1.00 16.36 ?  353  VAL B C   1 
ATOM   5778 O  O   . VAL B 1 351 ? 21.464  20.049  -38.586 1.00 17.22 ?  353  VAL B O   1 
ATOM   5779 C  CB  . VAL B 1 351 ? 18.734  20.128  -40.136 1.00 19.35 ?  353  VAL B CB  1 
ATOM   5780 C  CG1 . VAL B 1 351 ? 19.326  19.449  -41.369 1.00 21.71 ?  353  VAL B CG1 1 
ATOM   5781 C  CG2 . VAL B 1 351 ? 17.222  20.179  -40.253 1.00 23.01 ?  353  VAL B CG2 1 
ATOM   5782 N  N   . ASP B 1 352 ? 21.064  17.895  -39.121 1.00 17.27 ?  354  ASP B N   1 
ATOM   5783 C  CA  . ASP B 1 352 ? 22.454  17.485  -39.328 1.00 12.84 ?  354  ASP B CA  1 
ATOM   5784 C  C   . ASP B 1 352 ? 23.259  17.411  -38.035 1.00 17.04 ?  354  ASP B C   1 
ATOM   5785 O  O   . ASP B 1 352 ? 24.481  17.210  -38.091 1.00 14.60 ?  354  ASP B O   1 
ATOM   5786 C  CB  . ASP B 1 352 ? 23.165  18.405  -40.337 1.00 18.41 ?  354  ASP B CB  1 
ATOM   5787 C  CG  . ASP B 1 352 ? 22.643  18.215  -41.764 1.00 17.83 ?  354  ASP B CG  1 
ATOM   5788 O  OD1 . ASP B 1 352 ? 21.923  17.222  -41.987 1.00 21.97 ?  354  ASP B OD1 1 
ATOM   5789 O  OD2 . ASP B 1 352 ? 22.942  19.049  -42.653 1.00 19.97 ?  354  ASP B OD2 1 
ATOM   5790 N  N   . GLN B 1 353 ? 22.619  17.552  -36.869 1.00 16.20 ?  355  GLN B N   1 
ATOM   5791 C  CA  . GLN B 1 353 ? 23.364  17.408  -35.617 1.00 19.22 ?  355  GLN B CA  1 
ATOM   5792 C  C   . GLN B 1 353 ? 23.955  16.012  -35.457 1.00 17.32 ?  355  GLN B C   1 
ATOM   5793 O  O   . GLN B 1 353 ? 24.963  15.858  -34.765 1.00 15.66 ?  355  GLN B O   1 
ATOM   5794 C  CB  . GLN B 1 353 ? 22.470  17.744  -34.408 1.00 17.20 ?  355  GLN B CB  1 
ATOM   5795 C  CG  . GLN B 1 353 ? 21.376  16.708  -34.146 1.00 18.11 ?  355  GLN B CG  1 
ATOM   5796 C  CD  . GLN B 1 353 ? 20.523  17.048  -32.948 1.00 18.96 ?  355  GLN B CD  1 
ATOM   5797 O  OE1 . GLN B 1 353 ? 20.118  18.198  -32.768 1.00 21.58 ?  355  GLN B OE1 1 
ATOM   5798 N  NE2 . GLN B 1 353 ? 20.244  16.049  -32.115 1.00 17.14 ?  355  GLN B NE2 1 
ATOM   5799 N  N   . TRP B 1 354 ? 23.387  15.005  -36.127 1.00 16.03 ?  356  TRP B N   1 
ATOM   5800 C  CA  . TRP B 1 354 ? 23.877  13.639  -35.972 1.00 15.92 ?  356  TRP B CA  1 
ATOM   5801 C  C   . TRP B 1 354 ? 25.331  13.475  -36.441 1.00 16.99 ?  356  TRP B C   1 
ATOM   5802 O  O   . TRP B 1 354 ? 26.072  12.664  -35.864 1.00 12.79 ?  356  TRP B O   1 
ATOM   5803 C  CB  . TRP B 1 354 ? 22.933  12.675  -36.704 1.00 15.29 ?  356  TRP B CB  1 
ATOM   5804 C  CG  . TRP B 1 354 ? 22.400  13.199  -38.000 1.00 16.89 ?  356  TRP B CG  1 
ATOM   5805 C  CD1 . TRP B 1 354 ? 23.005  13.133  -39.224 1.00 15.66 ?  356  TRP B CD1 1 
ATOM   5806 C  CD2 . TRP B 1 354 ? 21.149  13.876  -38.207 1.00 18.77 ?  356  TRP B CD2 1 
ATOM   5807 N  NE1 . TRP B 1 354 ? 22.213  13.730  -40.175 1.00 16.01 ?  356  TRP B NE1 1 
ATOM   5808 C  CE2 . TRP B 1 354 ? 21.064  14.183  -39.579 1.00 16.54 ?  356  TRP B CE2 1 
ATOM   5809 C  CE3 . TRP B 1 354 ? 20.104  14.252  -37.364 1.00 16.36 ?  356  TRP B CE3 1 
ATOM   5810 C  CZ2 . TRP B 1 354 ? 19.970  14.855  -40.131 1.00 20.40 ?  356  TRP B CZ2 1 
ATOM   5811 C  CZ3 . TRP B 1 354 ? 19.004  14.912  -37.918 1.00 15.80 ?  356  TRP B CZ3 1 
ATOM   5812 C  CH2 . TRP B 1 354 ? 18.952  15.202  -39.290 1.00 15.70 ?  356  TRP B CH2 1 
ATOM   5813 N  N   . GLN B 1 355 ? 25.790  14.252  -37.446 1.00 15.03 ?  357  GLN B N   1 
ATOM   5814 C  CA  . GLN B 1 355 ? 27.170  14.054  -37.883 1.00 12.02 ?  357  GLN B CA  1 
ATOM   5815 C  C   . GLN B 1 355 ? 28.165  14.659  -36.905 1.00 12.62 ?  357  GLN B C   1 
ATOM   5816 O  O   . GLN B 1 355 ? 29.274  14.143  -36.776 1.00 13.26 ?  357  GLN B O   1 
ATOM   5817 C  CB  . GLN B 1 355 ? 27.434  14.624  -39.282 1.00 16.00 ?  357  GLN B CB  1 
ATOM   5818 C  CG  . GLN B 1 355 ? 26.994  13.698  -40.424 1.00 19.70 ?  357  GLN B CG  1 
ATOM   5819 C  CD  . GLN B 1 355 ? 27.584  12.314  -40.342 1.00 16.89 ?  357  GLN B CD  1 
ATOM   5820 O  OE1 . GLN B 1 355 ? 27.097  11.478  -39.590 1.00 18.84 ?  357  GLN B OE1 1 
ATOM   5821 N  NE2 . GLN B 1 355 ? 28.597  12.040  -41.169 1.00 15.62 ?  357  GLN B NE2 1 
ATOM   5822 N  N   . LEU B 1 356 ? 27.800  15.748  -36.220 1.00 15.39 ?  358  LEU B N   1 
ATOM   5823 C  CA  . LEU B 1 356 ? 28.656  16.245  -35.149 1.00 13.88 ?  358  LEU B CA  1 
ATOM   5824 C  C   . LEU B 1 356 ? 28.694  15.262  -33.989 1.00 11.22 ?  358  LEU B C   1 
ATOM   5825 O  O   . LEU B 1 356 ? 29.734  15.105  -33.340 1.00 13.71 ?  358  LEU B O   1 
ATOM   5826 C  CB  . LEU B 1 356 ? 28.179  17.632  -34.696 1.00 12.87 ?  358  LEU B CB  1 
ATOM   5827 C  CG  . LEU B 1 356 ? 29.126  18.496  -33.864 1.00 16.07 ?  358  LEU B CG  1 
ATOM   5828 C  CD1 . LEU B 1 356 ? 30.489  18.628  -34.544 1.00 27.21 ?  358  LEU B CD1 1 
ATOM   5829 C  CD2 . LEU B 1 356 ? 28.527  19.880  -33.640 1.00 18.56 ?  358  LEU B CD2 1 
ATOM   5830 N  N   . GLU B 1 357 ? 27.583  14.574  -33.730 1.00 13.18 ?  359  GLU B N   1 
ATOM   5831 C  CA  . GLU B 1 357 ? 27.574  13.525  -32.717 1.00 16.85 ?  359  GLU B CA  1 
ATOM   5832 C  C   . GLU B 1 357 ? 28.505  12.389  -33.113 1.00 13.33 ?  359  GLU B C   1 
ATOM   5833 O  O   . GLU B 1 357 ? 29.191  11.813  -32.263 1.00 14.48 ?  359  GLU B O   1 
ATOM   5834 C  CB  . GLU B 1 357 ? 26.144  13.006  -32.517 1.00 15.99 ?  359  GLU B CB  1 
ATOM   5835 C  CG  . GLU B 1 357 ? 25.988  11.937  -31.426 1.00 15.94 ?  359  GLU B CG  1 
ATOM   5836 C  CD  . GLU B 1 357 ? 24.532  11.476  -31.246 1.00 22.63 ?  359  GLU B CD  1 
ATOM   5837 O  OE1 . GLU B 1 357 ? 24.292  10.491  -30.502 1.00 19.38 ?  359  GLU B OE1 1 
ATOM   5838 O  OE2 . GLU B 1 357 ? 23.632  12.082  -31.875 1.00 20.11 ?  359  GLU B OE2 1 
ATOM   5839 N  N   . GLU B 1 358 ? 28.538  12.046  -34.404 1.00 9.65  ?  360  GLU B N   1 
ATOM   5840 C  CA  . GLU B 1 358 ? 29.500  11.043  -34.853 1.00 10.15 ?  360  GLU B CA  1 
ATOM   5841 C  C   . GLU B 1 358 ? 30.933  11.548  -34.713 1.00 10.64 ?  360  GLU B C   1 
ATOM   5842 O  O   . GLU B 1 358 ? 31.837  10.772  -34.394 1.00 11.60 ?  360  GLU B O   1 
ATOM   5843 C  CB  . GLU B 1 358 ? 29.198  10.634  -36.299 1.00 10.43 ?  360  GLU B CB  1 
ATOM   5844 C  CG  . GLU B 1 358 ? 27.847  9.970   -36.442 1.00 11.27 ?  360  GLU B CG  1 
ATOM   5845 C  CD  . GLU B 1 358 ? 27.787  8.569   -35.837 1.00 17.58 ?  360  GLU B CD  1 
ATOM   5846 O  OE1 . GLU B 1 358 ? 26.655  8.041   -35.700 1.00 18.26 ?  360  GLU B OE1 1 
ATOM   5847 O  OE2 . GLU B 1 358 ? 28.854  7.993   -35.505 1.00 14.25 ?  360  GLU B OE2 1 
ATOM   5848 N  N   . LEU B 1 359 ? 31.164  12.845  -34.936 1.00 11.50 ?  361  LEU B N   1 
ATOM   5849 C  CA  . LEU B 1 359 ? 32.516  13.366  -34.756 1.00 13.79 ?  361  LEU B CA  1 
ATOM   5850 C  C   . LEU B 1 359 ? 32.909  13.351  -33.282 1.00 11.63 ?  361  LEU B C   1 
ATOM   5851 O  O   . LEU B 1 359 ? 34.066  13.081  -32.944 1.00 12.27 ?  361  LEU B O   1 
ATOM   5852 C  CB  . LEU B 1 359 ? 32.610  14.778  -35.345 1.00 10.29 ?  361  LEU B CB  1 
ATOM   5853 C  CG  . LEU B 1 359 ? 33.940  15.503  -35.102 1.00 13.75 ?  361  LEU B CG  1 
ATOM   5854 C  CD1 . LEU B 1 359 ? 35.071  14.826  -35.878 1.00 15.20 ?  361  LEU B CD1 1 
ATOM   5855 C  CD2 . LEU B 1 359 ? 33.793  16.930  -35.563 1.00 12.27 ?  361  LEU B CD2 1 
ATOM   5856 N  N   . ALA B 1 360 ? 31.956  13.616  -32.384 1.00 10.47 ?  362  ALA B N   1 
ATOM   5857 C  CA  . ALA B 1 360 ? 32.244  13.483  -30.954 1.00 12.99 ?  362  ALA B CA  1 
ATOM   5858 C  C   . ALA B 1 360 ? 32.649  12.055  -30.607 1.00 12.75 ?  362  ALA B C   1 
ATOM   5859 O  O   . ALA B 1 360 ? 33.547  11.833  -29.784 1.00 13.57 ?  362  ALA B O   1 
ATOM   5860 C  CB  . ALA B 1 360 ? 31.027  13.911  -30.125 1.00 14.95 ?  362  ALA B CB  1 
ATOM   5861 N  N   . LYS B 1 361 ? 31.998  11.073  -31.225 1.00 11.56 ?  363  LYS B N   1 
ATOM   5862 C  CA  . LYS B 1 361 ? 32.349  9.669   -30.986 1.00 16.17 ?  363  LYS B CA  1 
ATOM   5863 C  C   . LYS B 1 361 ? 33.792  9.377   -31.400 1.00 13.62 ?  363  LYS B C   1 
ATOM   5864 O  O   . LYS B 1 361 ? 34.512  8.635   -30.714 1.00 14.77 ?  363  LYS B O   1 
ATOM   5865 C  CB  . LYS B 1 361 ? 31.357  8.770   -31.741 1.00 14.71 ?  363  LYS B CB  1 
ATOM   5866 C  CG  . LYS B 1 361 ? 31.672  7.280   -31.740 1.00 15.04 ?  363  LYS B CG  1 
ATOM   5867 C  CD  . LYS B 1 361 ? 30.473  6.499   -32.289 1.00 17.19 ?  363  LYS B CD  1 
ATOM   5868 C  CE  . LYS B 1 361 ? 30.826  5.088   -32.749 1.00 23.98 ?  363  LYS B CE  1 
ATOM   5869 N  NZ  . LYS B 1 361 ? 29.595  4.317   -33.206 1.00 25.88 ?  363  LYS B NZ  1 
ATOM   5870 N  N   . VAL B 1 362 ? 34.246  9.976   -32.507 1.00 12.04 ?  364  VAL B N   1 
ATOM   5871 C  CA  . VAL B 1 362 ? 35.629  9.787   -32.935 1.00 9.55  ?  364  VAL B CA  1 
ATOM   5872 C  C   . VAL B 1 362 ? 36.584  10.430  -31.937 1.00 9.47  ?  364  VAL B C   1 
ATOM   5873 O  O   . VAL B 1 362 ? 37.586  9.830   -31.529 1.00 13.10 ?  364  VAL B O   1 
ATOM   5874 C  CB  . VAL B 1 362 ? 35.840  10.361  -34.347 1.00 10.78 ?  364  VAL B CB  1 
ATOM   5875 C  CG1 . VAL B 1 362 ? 37.309  10.343  -34.747 1.00 10.59 ?  364  VAL B CG1 1 
ATOM   5876 C  CG2 . VAL B 1 362 ? 34.992  9.593   -35.370 1.00 9.09  ?  364  VAL B CG2 1 
ATOM   5877 N  N   . ARG B 1 363 ? 36.299  11.676  -31.553 1.00 11.92 ?  365  ARG B N   1 
ATOM   5878 C  CA  . ARG B 1 363 ? 37.258  12.439  -30.763 1.00 14.97 ?  365  ARG B CA  1 
ATOM   5879 C  C   . ARG B 1 363 ? 37.356  11.935  -29.330 1.00 17.15 ?  365  ARG B C   1 
ATOM   5880 O  O   . ARG B 1 363 ? 38.331  12.255  -28.644 1.00 17.87 ?  365  ARG B O   1 
ATOM   5881 C  CB  . ARG B 1 363 ? 36.889  13.919  -30.795 1.00 13.56 ?  365  ARG B CB  1 
ATOM   5882 C  CG  . ARG B 1 363 ? 37.038  14.578  -32.175 1.00 14.75 ?  365  ARG B CG  1 
ATOM   5883 C  CD  . ARG B 1 363 ? 38.495  14.642  -32.633 1.00 20.53 ?  365  ARG B CD  1 
ATOM   5884 N  NE  . ARG B 1 363 ? 39.167  15.805  -32.044 1.00 23.43 ?  365  ARG B NE  1 
ATOM   5885 C  CZ  . ARG B 1 363 ? 40.125  15.745  -31.126 1.00 23.73 ?  365  ARG B CZ  1 
ATOM   5886 N  NH1 . ARG B 1 363 ? 40.574  14.579  -30.685 1.00 24.68 ?  365  ARG B NH1 1 
ATOM   5887 N  NH2 . ARG B 1 363 ? 40.648  16.860  -30.654 1.00 29.06 ?  365  ARG B NH2 1 
ATOM   5888 N  N   . ARG B 1 364 ? 36.381  11.147  -28.861 1.00 17.87 ?  366  ARG B N   1 
ATOM   5889 C  CA  . ARG B 1 364 ? 36.534  10.506  -27.555 1.00 18.31 ?  366  ARG B CA  1 
ATOM   5890 C  C   . ARG B 1 364 ? 37.632  9.463   -27.567 1.00 22.68 ?  366  ARG B C   1 
ATOM   5891 O  O   . ARG B 1 364 ? 38.131  9.088   -26.501 1.00 21.76 ?  366  ARG B O   1 
ATOM   5892 C  CB  . ARG B 1 364 ? 35.244  9.822   -27.110 1.00 24.00 ?  366  ARG B CB  1 
ATOM   5893 C  CG  . ARG B 1 364 ? 34.159  10.780  -26.698 1.00 27.91 ?  366  ARG B CG  1 
ATOM   5894 C  CD  . ARG B 1 364 ? 33.011  10.081  -25.987 1.00 27.57 ?  366  ARG B CD  1 
ATOM   5895 N  NE  . ARG B 1 364 ? 32.299  9.115   -26.818 1.00 27.62 ?  366  ARG B NE  1 
ATOM   5896 C  CZ  . ARG B 1 364 ? 31.173  9.377   -27.484 1.00 25.58 ?  366  ARG B CZ  1 
ATOM   5897 N  NH1 . ARG B 1 364 ? 30.646  10.592  -27.467 1.00 23.43 ?  366  ARG B NH1 1 
ATOM   5898 N  NH2 . ARG B 1 364 ? 30.591  8.426   -28.196 1.00 25.68 ?  366  ARG B NH2 1 
ATOM   5899 N  N   . LYS B 1 365 ? 38.006  8.977   -28.741 1.00 16.38 ?  367  LYS B N   1 
ATOM   5900 C  CA  . LYS B 1 365 ? 38.953  7.885   -28.847 1.00 17.69 ?  367  LYS B CA  1 
ATOM   5901 C  C   . LYS B 1 365 ? 40.259  8.281   -29.509 1.00 15.57 ?  367  LYS B C   1 
ATOM   5902 O  O   . LYS B 1 365 ? 41.301  7.729   -29.148 1.00 16.83 ?  367  LYS B O   1 
ATOM   5903 C  CB  . LYS B 1 365 ? 38.332  6.711   -29.624 1.00 16.96 ?  367  LYS B CB  1 
ATOM   5904 C  CG  . LYS B 1 365 ? 39.260  5.492   -29.731 1.00 17.68 ?  367  LYS B CG  1 
ATOM   5905 C  CD  . LYS B 1 365 ? 38.636  4.334   -30.510 1.00 24.06 ?  367  LYS B CD  1 
ATOM   5906 C  CE  . LYS B 1 365 ? 39.455  3.052   -30.328 1.00 25.22 ?  367  LYS B CE  1 
ATOM   5907 N  NZ  . LYS B 1 365 ? 38.934  1.937   -31.186 1.00 24.47 ?  367  LYS B NZ  1 
ATOM   5908 N  N   . ALA B 1 366 ? 40.252  9.240   -30.439 1.00 14.88 ?  368  ALA B N   1 
ATOM   5909 C  CA  . ALA B 1 366 ? 41.426  9.468   -31.274 1.00 11.71 ?  368  ALA B CA  1 
ATOM   5910 C  C   . ALA B 1 366 ? 41.620  10.951  -31.557 1.00 15.02 ?  368  ALA B C   1 
ATOM   5911 O  O   . ALA B 1 366 ? 40.653  11.717  -31.638 1.00 14.74 ?  368  ALA B O   1 
ATOM   5912 C  CB  . ALA B 1 366 ? 41.302  8.688   -32.605 1.00 13.59 ?  368  ALA B CB  1 
ATOM   5913 N  N   . ARG B 1 367 ? 42.885  11.348  -31.718 1.00 11.14 ?  369  ARG B N   1 
ATOM   5914 C  CA  . ARG B 1 367 ? 43.202  12.634  -32.324 1.00 12.14 ?  369  ARG B CA  1 
ATOM   5915 C  C   . ARG B 1 367 ? 42.941  12.566  -33.823 1.00 11.63 ?  369  ARG B C   1 
ATOM   5916 O  O   . ARG B 1 367 ? 42.997  11.494  -34.428 1.00 12.26 ?  369  ARG B O   1 
ATOM   5917 C  CB  . ARG B 1 367 ? 44.667  12.998  -32.104 1.00 13.61 ?  369  ARG B CB  1 
ATOM   5918 C  CG  . ARG B 1 367 ? 45.085  13.066  -30.658 1.00 11.80 ?  369  ARG B CG  1 
ATOM   5919 C  CD  . ARG B 1 367 ? 46.601  13.237  -30.542 1.00 13.87 ?  369  ARG B CD  1 
ATOM   5920 N  NE  . ARG B 1 367 ? 46.995  13.211  -29.136 1.00 15.09 ?  369  ARG B NE  1 
ATOM   5921 C  CZ  . ARG B 1 367 ? 47.860  14.061  -28.590 1.00 21.31 ?  369  ARG B CZ  1 
ATOM   5922 N  NH1 . ARG B 1 367 ? 48.445  14.990  -29.342 1.00 15.10 ?  369  ARG B NH1 1 
ATOM   5923 N  NH2 . ARG B 1 367 ? 48.152  13.969  -27.295 1.00 16.79 ?  369  ARG B NH2 1 
ATOM   5924 N  N   . VAL B 1 368 ? 42.651  13.717  -34.428 1.00 11.98 ?  370  VAL B N   1 
ATOM   5925 C  CA  . VAL B 1 368 ? 42.352  13.773  -35.860 1.00 12.19 ?  370  VAL B CA  1 
ATOM   5926 C  C   . VAL B 1 368 ? 43.200  14.871  -36.489 1.00 12.16 ?  370  VAL B C   1 
ATOM   5927 O  O   . VAL B 1 368 ? 43.131  16.037  -36.071 1.00 12.30 ?  370  VAL B O   1 
ATOM   5928 C  CB  . VAL B 1 368 ? 40.862  14.024  -36.152 1.00 11.77 ?  370  VAL B CB  1 
ATOM   5929 C  CG1 . VAL B 1 368 ? 40.655  14.231  -37.665 1.00 9.10  ?  370  VAL B CG1 1 
ATOM   5930 C  CG2 . VAL B 1 368 ? 40.009  12.882  -35.668 1.00 11.57 ?  370  VAL B CG2 1 
ATOM   5931 N  N   . LYS B 1 369 ? 43.981  14.502  -37.494 1.00 9.12  ?  371  LYS B N   1 
ATOM   5932 C  CA  . LYS B 1 369 ? 44.704  15.442  -38.342 1.00 8.09  ?  371  LYS B CA  1 
ATOM   5933 C  C   . LYS B 1 369 ? 43.995  15.437  -39.694 1.00 12.48 ?  371  LYS B C   1 
ATOM   5934 O  O   . LYS B 1 369 ? 43.746  14.369  -40.263 1.00 11.80 ?  371  LYS B O   1 
ATOM   5935 C  CB  . LYS B 1 369 ? 46.181  15.054  -38.474 1.00 10.45 ?  371  LYS B CB  1 
ATOM   5936 C  CG  . LYS B 1 369 ? 47.017  15.310  -37.204 1.00 13.20 ?  371  LYS B CG  1 
ATOM   5937 C  CD  . LYS B 1 369 ? 48.380  14.618  -37.288 1.00 9.93  ?  371  LYS B CD  1 
ATOM   5938 C  CE  . LYS B 1 369 ? 49.162  14.727  -35.982 1.00 14.13 ?  371  LYS B CE  1 
ATOM   5939 N  NZ  . LYS B 1 369 ? 49.453  16.171  -35.660 1.00 16.33 ?  371  LYS B NZ  1 
ATOM   5940 N  N   . PHE B 1 370 ? 43.642  16.616  -40.191 1.00 9.54  ?  372  PHE B N   1 
ATOM   5941 C  CA  A PHE B 1 370 ? 42.818  16.746  -41.387 0.50 10.77 ?  372  PHE B CA  1 
ATOM   5942 C  CA  B PHE B 1 370 ? 42.823  16.738  -41.390 0.50 10.76 ?  372  PHE B CA  1 
ATOM   5943 C  C   . PHE B 1 370 ? 43.594  17.482  -42.472 1.00 11.39 ?  372  PHE B C   1 
ATOM   5944 O  O   . PHE B 1 370 ? 44.148  18.565  -42.226 1.00 14.69 ?  372  PHE B O   1 
ATOM   5945 C  CB  A PHE B 1 370 ? 41.512  17.474  -41.056 0.50 11.08 ?  372  PHE B CB  1 
ATOM   5946 C  CB  B PHE B 1 370 ? 41.500  17.438  -41.066 0.50 11.07 ?  372  PHE B CB  1 
ATOM   5947 C  CG  A PHE B 1 370 ? 40.376  17.118  -41.966 0.50 11.59 ?  372  PHE B CG  1 
ATOM   5948 C  CG  B PHE B 1 370 ? 40.371  17.036  -41.968 0.50 11.57 ?  372  PHE B CG  1 
ATOM   5949 C  CD1 A PHE B 1 370 ? 39.285  16.415  -41.485 0.50 12.10 ?  372  PHE B CD1 1 
ATOM   5950 C  CD1 B PHE B 1 370 ? 39.208  16.497  -41.444 0.50 12.13 ?  372  PHE B CD1 1 
ATOM   5951 C  CD2 A PHE B 1 370 ? 40.394  17.495  -43.300 0.50 12.62 ?  372  PHE B CD2 1 
ATOM   5952 C  CD2 B PHE B 1 370 ? 40.463  17.223  -43.339 0.50 12.68 ?  372  PHE B CD2 1 
ATOM   5953 C  CE1 A PHE B 1 370 ? 38.225  16.078  -42.326 0.50 14.04 ?  372  PHE B CE1 1 
ATOM   5954 C  CE1 B PHE B 1 370 ? 38.154  16.124  -42.281 0.50 14.04 ?  372  PHE B CE1 1 
ATOM   5955 C  CE2 A PHE B 1 370 ? 39.342  17.166  -44.147 0.50 13.49 ?  372  PHE B CE2 1 
ATOM   5956 C  CE2 B PHE B 1 370 ? 39.419  16.856  -44.184 0.50 13.42 ?  372  PHE B CE2 1 
ATOM   5957 C  CZ  A PHE B 1 370 ? 38.257  16.452  -43.657 0.50 12.41 ?  372  PHE B CZ  1 
ATOM   5958 C  CZ  B PHE B 1 370 ? 38.263  16.303  -43.651 0.50 12.30 ?  372  PHE B CZ  1 
ATOM   5959 N  N   . VAL B 1 371 ? 43.652  16.888  -43.661 1.00 9.63  ?  373  VAL B N   1 
ATOM   5960 C  CA  . VAL B 1 371 ? 44.415  17.431  -44.786 1.00 10.73 ?  373  VAL B CA  1 
ATOM   5961 C  C   . VAL B 1 371 ? 43.447  17.716  -45.929 1.00 14.66 ?  373  VAL B C   1 
ATOM   5962 O  O   . VAL B 1 371 ? 42.807  16.794  -46.446 1.00 14.41 ?  373  VAL B O   1 
ATOM   5963 C  CB  . VAL B 1 371 ? 45.511  16.463  -45.251 1.00 15.37 ?  373  VAL B CB  1 
ATOM   5964 C  CG1 . VAL B 1 371 ? 46.286  17.068  -46.435 1.00 16.09 ?  373  VAL B CG1 1 
ATOM   5965 C  CG2 . VAL B 1 371 ? 46.438  16.091  -44.084 1.00 14.34 ?  373  VAL B CG2 1 
ATOM   5966 N  N   . SER B 1 372 ? 43.355  18.980  -46.341 1.00 12.77 ?  374  SER B N   1 
ATOM   5967 C  CA  . SER B 1 372 ? 42.393  19.357  -47.374 1.00 16.27 ?  374  SER B CA  1 
ATOM   5968 C  C   . SER B 1 372 ? 42.794  20.699  -47.960 1.00 22.50 ?  374  SER B C   1 
ATOM   5969 O  O   . SER B 1 372 ? 43.323  21.556  -47.247 1.00 15.40 ?  374  SER B O   1 
ATOM   5970 C  CB  . SER B 1 372 ? 40.964  19.457  -46.821 1.00 16.90 ?  374  SER B CB  1 
ATOM   5971 O  OG  . SER B 1 372 ? 40.013  19.703  -47.874 1.00 15.42 ?  374  SER B OG  1 
ATOM   5972 N  N   . ASP B 1 373 ? 42.517  20.895  -49.247 1.00 18.19 ?  375  ASP B N   1 
ATOM   5973 C  CA  . ASP B 1 373 ? 42.652  22.236  -49.804 1.00 18.92 ?  375  ASP B CA  1 
ATOM   5974 C  C   . ASP B 1 373 ? 41.305  22.859  -50.155 1.00 21.43 ?  375  ASP B C   1 
ATOM   5975 O  O   . ASP B 1 373 ? 41.268  23.959  -50.717 1.00 24.05 ?  375  ASP B O   1 
ATOM   5976 C  CB  . ASP B 1 373 ? 43.594  22.253  -51.019 1.00 25.93 ?  375  ASP B CB  1 
ATOM   5977 C  CG  . ASP B 1 373 ? 43.246  21.223  -52.077 1.00 24.99 ?  375  ASP B CG  1 
ATOM   5978 O  OD1 . ASP B 1 373 ? 42.166  20.598  -52.015 1.00 29.06 ?  375  ASP B OD1 1 
ATOM   5979 O  OD2 . ASP B 1 373 ? 44.071  21.064  -53.004 1.00 31.54 ?  375  ASP B OD2 1 
ATOM   5980 N  N   . GLY B 1 374 ? 40.199  22.215  -49.791 1.00 16.45 ?  376  GLY B N   1 
ATOM   5981 C  CA  . GLY B 1 374 ? 38.890  22.766  -50.074 1.00 22.20 ?  376  GLY B CA  1 
ATOM   5982 C  C   . GLY B 1 374 ? 38.355  23.697  -49.015 1.00 24.89 ?  376  GLY B C   1 
ATOM   5983 O  O   . GLY B 1 374 ? 37.390  24.422  -49.261 1.00 21.61 ?  376  GLY B O   1 
ATOM   5984 N  N   . VAL B 1 375 ? 38.958  23.697  -47.832 1.00 19.58 ?  377  VAL B N   1 
ATOM   5985 C  CA  . VAL B 1 375 ? 38.492  24.509  -46.709 1.00 18.55 ?  377  VAL B CA  1 
ATOM   5986 C  C   . VAL B 1 375 ? 39.745  25.084  -46.054 1.00 22.35 ?  377  VAL B C   1 
ATOM   5987 O  O   . VAL B 1 375 ? 40.742  24.362  -45.912 1.00 25.18 ?  377  VAL B O   1 
ATOM   5988 C  CB  . VAL B 1 375 ? 37.647  23.673  -45.728 1.00 23.01 ?  377  VAL B CB  1 
ATOM   5989 C  CG1 . VAL B 1 375 ? 37.422  24.394  -44.425 1.00 22.53 ?  377  VAL B CG1 1 
ATOM   5990 C  CG2 . VAL B 1 375 ? 36.300  23.273  -46.361 1.00 20.34 ?  377  VAL B CG2 1 
ATOM   5991 N  N   . PRO B 1 376 ? 39.758  26.360  -45.663 1.00 27.51 ?  378  PRO B N   1 
ATOM   5992 C  CA  . PRO B 1 376 ? 40.967  26.934  -45.056 1.00 22.89 ?  378  PRO B CA  1 
ATOM   5993 C  C   . PRO B 1 376 ? 41.261  26.331  -43.691 1.00 20.53 ?  378  PRO B C   1 
ATOM   5994 O  O   . PRO B 1 376 ? 40.357  25.963  -42.936 1.00 20.41 ?  378  PRO B O   1 
ATOM   5995 C  CB  . PRO B 1 376 ? 40.623  28.425  -44.927 1.00 28.14 ?  378  PRO B CB  1 
ATOM   5996 C  CG  . PRO B 1 376 ? 39.531  28.650  -45.939 1.00 31.72 ?  378  PRO B CG  1 
ATOM   5997 C  CD  . PRO B 1 376 ? 38.719  27.384  -45.869 1.00 27.29 ?  378  PRO B CD  1 
ATOM   5998 N  N   . ALA B 1 377 ? 42.556  26.270  -43.366 1.00 21.43 ?  379  ALA B N   1 
ATOM   5999 C  CA  . ALA B 1 377 ? 42.982  25.732  -42.074 1.00 22.19 ?  379  ALA B CA  1 
ATOM   6000 C  C   . ALA B 1 377 ? 42.284  26.420  -40.904 1.00 23.12 ?  379  ALA B C   1 
ATOM   6001 O  O   . ALA B 1 377 ? 41.940  25.773  -39.910 1.00 19.62 ?  379  ALA B O   1 
ATOM   6002 C  CB  . ALA B 1 377 ? 44.501  25.857  -41.929 1.00 19.55 ?  379  ALA B CB  1 
ATOM   6003 N  N   . ALA B 1 378 ? 42.057  27.734  -41.007 1.00 31.13 ?  380  ALA B N   1 
ATOM   6004 C  CA  . ALA B 1 378 ? 41.431  28.461  -39.906 1.00 25.49 ?  380  ALA B CA  1 
ATOM   6005 C  C   . ALA B 1 378 ? 39.991  28.010  -39.683 1.00 28.43 ?  380  ALA B C   1 
ATOM   6006 O  O   . ALA B 1 378 ? 39.515  27.979  -38.542 1.00 32.02 ?  380  ALA B O   1 
ATOM   6007 C  CB  . ALA B 1 378 ? 41.488  29.967  -40.172 1.00 29.61 ?  380  ALA B CB  1 
ATOM   6008 N  N   . VAL B 1 379 ? 39.279  27.664  -40.759 1.00 20.70 ?  381  VAL B N   1 
ATOM   6009 C  CA  . VAL B 1 379 ? 37.935  27.113  -40.608 1.00 24.08 ?  381  VAL B CA  1 
ATOM   6010 C  C   . VAL B 1 379 ? 37.995  25.709  -40.019 1.00 22.65 ?  381  VAL B C   1 
ATOM   6011 O  O   . VAL B 1 379 ? 37.222  25.373  -39.112 1.00 23.50 ?  381  VAL B O   1 
ATOM   6012 C  CB  . VAL B 1 379 ? 37.184  27.130  -41.954 1.00 23.10 ?  381  VAL B CB  1 
ATOM   6013 C  CG1 . VAL B 1 379 ? 35.824  26.490  -41.811 1.00 26.09 ?  381  VAL B CG1 1 
ATOM   6014 C  CG2 . VAL B 1 379 ? 37.021  28.559  -42.457 1.00 29.11 ?  381  VAL B CG2 1 
ATOM   6015 N  N   . LEU B 1 380 ? 38.913  24.869  -40.514 1.00 18.37 ?  382  LEU B N   1 
ATOM   6016 C  CA  . LEU B 1 380 ? 38.965  23.484  -40.041 1.00 20.04 ?  382  LEU B CA  1 
ATOM   6017 C  C   . LEU B 1 380 ? 39.360  23.413  -38.571 1.00 21.56 ?  382  LEU B C   1 
ATOM   6018 O  O   . LEU B 1 380 ? 38.866  22.555  -37.828 1.00 18.42 ?  382  LEU B O   1 
ATOM   6019 C  CB  . LEU B 1 380 ? 39.948  22.664  -40.883 1.00 18.83 ?  382  LEU B CB  1 
ATOM   6020 C  CG  . LEU B 1 380 ? 39.502  22.143  -42.247 1.00 25.58 ?  382  LEU B CG  1 
ATOM   6021 C  CD1 . LEU B 1 380 ? 40.703  21.554  -42.992 1.00 18.75 ?  382  LEU B CD1 1 
ATOM   6022 C  CD2 . LEU B 1 380 ? 38.358  21.139  -42.147 1.00 19.33 ?  382  LEU B CD2 1 
ATOM   6023 N  N   . SER B 1 381 ? 40.258  24.296  -38.132 1.00 20.43 ?  383  SER B N   1 
ATOM   6024 C  CA  . SER B 1 381 ? 40.686  24.262  -36.741 1.00 21.02 ?  383  SER B CA  1 
ATOM   6025 C  C   . SER B 1 381 ? 39.567  24.619  -35.775 1.00 25.24 ?  383  SER B C   1 
ATOM   6026 O  O   . SER B 1 381 ? 39.718  24.372  -34.578 1.00 27.50 ?  383  SER B O   1 
ATOM   6027 C  CB  . SER B 1 381 ? 41.873  25.197  -36.532 1.00 24.16 ?  383  SER B CB  1 
ATOM   6028 O  OG  . SER B 1 381 ? 41.507  26.533  -36.818 1.00 28.60 ?  383  SER B OG  1 
ATOM   6029 N  N   . ARG B 1 382 ? 38.454  25.172  -36.263 1.00 28.34 ?  384  ARG B N   1 
ATOM   6030 C  CA  . ARG B 1 382 ? 37.263  25.386  -35.455 1.00 21.62 ?  384  ARG B CA  1 
ATOM   6031 C  C   . ARG B 1 382 ? 36.286  24.219  -35.535 1.00 25.23 ?  384  ARG B C   1 
ATOM   6032 O  O   . ARG B 1 382 ? 35.231  24.261  -34.892 1.00 24.87 ?  384  ARG B O   1 
ATOM   6033 C  CB  . ARG B 1 382 ? 36.558  26.678  -35.889 1.00 28.66 ?  384  ARG B CB  1 
ATOM   6034 N  N   . CYS B 1 383 ? 36.602  23.185  -36.315 1.00 22.51 ?  385  CYS B N   1 
ATOM   6035 C  CA  . CYS B 1 383 ? 35.744  22.015  -36.439 1.00 16.50 ?  385  CYS B CA  1 
ATOM   6036 C  C   . CYS B 1 383 ? 36.258  20.824  -35.631 1.00 19.64 ?  385  CYS B C   1 
ATOM   6037 O  O   . CYS B 1 383 ? 35.924  19.678  -35.953 1.00 13.92 ?  385  CYS B O   1 
ATOM   6038 C  CB  . CYS B 1 383 ? 35.601  21.637  -37.911 1.00 17.40 ?  385  CYS B CB  1 
ATOM   6039 S  SG  . CYS B 1 383 ? 34.810  22.969  -38.879 1.00 24.34 ?  385  CYS B SG  1 
ATOM   6040 N  N   . HIS B 1 384 ? 37.085  21.075  -34.605 1.00 16.79 ?  386  HIS B N   1 
ATOM   6041 C  CA  . HIS B 1 384 ? 37.506  20.052  -33.641 1.00 17.94 ?  386  HIS B CA  1 
ATOM   6042 C  C   . HIS B 1 384 ? 38.407  18.996  -34.271 1.00 15.98 ?  386  HIS B C   1 
ATOM   6043 O  O   . HIS B 1 384 ? 38.432  17.842  -33.833 1.00 14.39 ?  386  HIS B O   1 
ATOM   6044 C  CB  . HIS B 1 384 ? 36.300  19.394  -32.963 1.00 17.19 ?  386  HIS B CB  1 
ATOM   6045 C  CG  . HIS B 1 384 ? 35.398  20.372  -32.278 1.00 24.39 ?  386  HIS B CG  1 
ATOM   6046 N  ND1 . HIS B 1 384 ? 34.154  20.713  -32.771 1.00 27.89 ?  386  HIS B ND1 1 
ATOM   6047 C  CD2 . HIS B 1 384 ? 35.569  21.099  -31.151 1.00 21.86 ?  386  HIS B CD2 1 
ATOM   6048 C  CE1 . HIS B 1 384 ? 33.594  21.600  -31.967 1.00 24.62 ?  386  HIS B CE1 1 
ATOM   6049 N  NE2 . HIS B 1 384 ? 34.434  21.855  -30.981 1.00 28.90 ?  386  HIS B NE2 1 
ATOM   6050 N  N   . VAL B 1 385 ? 39.157  19.393  -35.295 1.00 17.25 ?  387  VAL B N   1 
ATOM   6051 C  CA  . VAL B 1 385 ? 40.199  18.577  -35.902 1.00 13.17 ?  387  VAL B CA  1 
ATOM   6052 C  C   . VAL B 1 385 ? 41.428  19.469  -36.016 1.00 14.76 ?  387  VAL B C   1 
ATOM   6053 O  O   . VAL B 1 385 ? 41.336  20.692  -35.898 1.00 12.72 ?  387  VAL B O   1 
ATOM   6054 C  CB  . VAL B 1 385 ? 39.785  18.038  -37.293 1.00 15.52 ?  387  VAL B CB  1 
ATOM   6055 C  CG1 . VAL B 1 385 ? 38.479  17.263  -37.210 1.00 11.53 ?  387  VAL B CG1 1 
ATOM   6056 C  CG2 . VAL B 1 385 ? 39.636  19.180  -38.280 1.00 15.65 ?  387  VAL B CG2 1 
ATOM   6057 N  N   . GLU B 1 386 ? 42.599  18.850  -36.235 1.00 11.44 ?  388  GLU B N   1 
ATOM   6058 C  CA  . GLU B 1 386 ? 43.799  19.659  -36.416 1.00 12.29 ?  388  GLU B CA  1 
ATOM   6059 C  C   . GLU B 1 386 ? 44.145  19.728  -37.900 1.00 10.66 ?  388  GLU B C   1 
ATOM   6060 O  O   . GLU B 1 386 ? 44.551  18.713  -38.480 1.00 11.11 ?  388  GLU B O   1 
ATOM   6061 C  CB  . GLU B 1 386 ? 44.986  19.103  -35.610 1.00 12.05 ?  388  GLU B CB  1 
ATOM   6062 C  CG  . GLU B 1 386 ? 46.337  19.831  -35.916 1.00 16.34 ?  388  GLU B CG  1 
ATOM   6063 C  CD  . GLU B 1 386 ? 47.602  19.053  -35.502 1.00 20.04 ?  388  GLU B CD  1 
ATOM   6064 O  OE1 . GLU B 1 386 ? 47.500  17.877  -35.098 1.00 19.24 ?  388  GLU B OE1 1 
ATOM   6065 O  OE2 . GLU B 1 386 ? 48.713  19.645  -35.546 1.00 21.49 ?  388  GLU B OE2 1 
ATOM   6066 N  N   . PRO B 1 387 ? 44.043  20.888  -38.544 1.00 11.83 ?  389  PRO B N   1 
ATOM   6067 C  CA  . PRO B 1 387 ? 44.476  20.985  -39.947 1.00 12.36 ?  389  PRO B CA  1 
ATOM   6068 C  C   . PRO B 1 387 ? 45.990  20.824  -40.057 1.00 12.24 ?  389  PRO B C   1 
ATOM   6069 O  O   . PRO B 1 387 ? 46.752  21.421  -39.292 1.00 17.46 ?  389  PRO B O   1 
ATOM   6070 C  CB  . PRO B 1 387 ? 44.027  22.393  -40.367 1.00 16.40 ?  389  PRO B CB  1 
ATOM   6071 C  CG  . PRO B 1 387 ? 43.949  23.157  -39.068 1.00 23.43 ?  389  PRO B CG  1 
ATOM   6072 C  CD  . PRO B 1 387 ? 43.583  22.173  -37.992 1.00 15.31 ?  389  PRO B CD  1 
ATOM   6073 N  N   . VAL B 1 388 ? 46.426  19.991  -41.001 1.00 13.12 ?  390  VAL B N   1 
ATOM   6074 C  CA  . VAL B 1 388 ? 47.848  19.783  -41.274 1.00 15.31 ?  390  VAL B CA  1 
ATOM   6075 C  C   . VAL B 1 388 ? 48.041  19.910  -42.775 1.00 16.82 ?  390  VAL B C   1 
ATOM   6076 O  O   . VAL B 1 388 ? 47.159  19.517  -43.549 1.00 13.56 ?  390  VAL B O   1 
ATOM   6077 C  CB  . VAL B 1 388 ? 48.338  18.408  -40.770 1.00 12.84 ?  390  VAL B CB  1 
ATOM   6078 C  CG1 . VAL B 1 388 ? 49.861  18.245  -40.941 1.00 12.02 ?  390  VAL B CG1 1 
ATOM   6079 C  CG2 . VAL B 1 388 ? 47.950  18.232  -39.316 1.00 14.04 ?  390  VAL B CG2 1 
ATOM   6080 N  N   . ALA B 1 389 ? 49.188  20.458  -43.186 1.00 16.36 ?  391  ALA B N   1 
ATOM   6081 C  CA  . ALA B 1 389 ? 49.358  20.855  -44.585 1.00 19.61 ?  391  ALA B CA  1 
ATOM   6082 C  C   . ALA B 1 389 ? 49.411  19.654  -45.524 1.00 17.84 ?  391  ALA B C   1 
ATOM   6083 O  O   . ALA B 1 389 ? 48.884  19.717  -46.641 1.00 18.88 ?  391  ALA B O   1 
ATOM   6084 C  CB  . ALA B 1 389 ? 50.621  21.703  -44.749 1.00 21.36 ?  391  ALA B CB  1 
ATOM   6085 N  N   . THR B 1 390 ? 50.095  18.579  -45.125 1.00 13.19 ?  392  THR B N   1 
ATOM   6086 C  CA  . THR B 1 390 ? 50.219  17.394  -45.963 1.00 13.50 ?  392  THR B CA  1 
ATOM   6087 C  C   . THR B 1 390 ? 50.035  16.148  -45.110 1.00 14.59 ?  392  THR B C   1 
ATOM   6088 O  O   . THR B 1 390 ? 50.247  16.169  -43.897 1.00 15.12 ?  392  THR B O   1 
ATOM   6089 C  CB  . THR B 1 390 ? 51.576  17.298  -46.671 1.00 20.97 ?  392  THR B CB  1 
ATOM   6090 O  OG1 . THR B 1 390 ? 52.559  16.863  -45.732 1.00 16.85 ?  392  THR B OG1 1 
ATOM   6091 C  CG2 . THR B 1 390 ? 52.008  18.645  -47.263 1.00 20.18 ?  392  THR B CG2 1 
ATOM   6092 N  N   . VAL B 1 391 ? 49.667  15.049  -45.775 1.00 14.00 ?  393  VAL B N   1 
ATOM   6093 C  CA  . VAL B 1 391 ? 49.566  13.754  -45.106 1.00 14.38 ?  393  VAL B CA  1 
ATOM   6094 C  C   . VAL B 1 391 ? 50.938  13.316  -44.597 1.00 13.48 ?  393  VAL B C   1 
ATOM   6095 O  O   . VAL B 1 391 ? 51.080  12.839  -43.459 1.00 14.91 ?  393  VAL B O   1 
ATOM   6096 C  CB  . VAL B 1 391 ? 48.955  12.712  -46.065 1.00 15.25 ?  393  VAL B CB  1 
ATOM   6097 C  CG1 . VAL B 1 391 ? 48.964  11.325  -45.453 1.00 13.42 ?  393  VAL B CG1 1 
ATOM   6098 C  CG2 . VAL B 1 391 ? 47.522  13.123  -46.471 1.00 13.30 ?  393  VAL B CG2 1 
ATOM   6099 N  N   . GLU B 1 392 ? 51.970  13.463  -45.435 1.00 13.87 ?  394  GLU B N   1 
ATOM   6100 C  CA  . GLU B 1 392 ? 53.316  13.072  -45.022 1.00 17.21 ?  394  GLU B CA  1 
ATOM   6101 C  C   . GLU B 1 392 ? 53.741  13.780  -43.744 1.00 18.50 ?  394  GLU B C   1 
ATOM   6102 O  O   . GLU B 1 392 ? 54.361  13.166  -42.863 1.00 14.26 ?  394  GLU B O   1 
ATOM   6103 C  CB  . GLU B 1 392 ? 54.334  13.362  -46.127 1.00 20.25 ?  394  GLU B CB  1 
ATOM   6104 C  CG  . GLU B 1 392 ? 55.624  12.570  -45.931 1.00 26.92 ?  394  GLU B CG  1 
ATOM   6105 C  CD  . GLU B 1 392 ? 56.554  12.641  -47.122 1.00 36.42 ?  394  GLU B CD  1 
ATOM   6106 O  OE1 . GLU B 1 392 ? 56.053  12.651  -48.273 1.00 24.26 ?  394  GLU B OE1 1 
ATOM   6107 O  OE2 . GLU B 1 392 ? 57.786  12.655  -46.895 1.00 30.86 ?  394  GLU B OE2 1 
ATOM   6108 N  N   . LEU B 1 393 ? 53.444  15.076  -43.632 1.00 12.63 ?  395  LEU B N   1 
ATOM   6109 C  CA  . LEU B 1 393 ? 53.810  15.799  -42.415 1.00 18.07 ?  395  LEU B CA  1 
ATOM   6110 C  C   . LEU B 1 393 ? 52.977  15.331  -41.227 1.00 16.76 ?  395  LEU B C   1 
ATOM   6111 O  O   . LEU B 1 393 ? 53.498  15.184  -40.110 1.00 14.48 ?  395  LEU B O   1 
ATOM   6112 C  CB  . LEU B 1 393 ? 53.629  17.301  -42.633 1.00 16.81 ?  395  LEU B CB  1 
ATOM   6113 C  CG  . LEU B 1 393 ? 53.727  18.161  -41.363 1.00 17.65 ?  395  LEU B CG  1 
ATOM   6114 C  CD1 . LEU B 1 393 ? 55.112  18.100  -40.727 1.00 17.66 ?  395  LEU B CD1 1 
ATOM   6115 C  CD2 . LEU B 1 393 ? 53.316  19.594  -41.661 1.00 18.65 ?  395  LEU B CD2 1 
ATOM   6116 N  N   . ALA B 1 394 ? 51.677  15.131  -41.450 1.00 10.35 ?  396  ALA B N   1 
ATOM   6117 C  CA  . ALA B 1 394 ? 50.791  14.651  -40.394 1.00 10.19 ?  396  ALA B CA  1 
ATOM   6118 C  C   . ALA B 1 394 ? 51.275  13.328  -39.829 1.00 12.21 ?  396  ALA B C   1 
ATOM   6119 O  O   . ALA B 1 394 ? 51.241  13.117  -38.611 1.00 11.91 ?  396  ALA B O   1 
ATOM   6120 C  CB  . ALA B 1 394 ? 49.360  14.494  -40.936 1.00 12.77 ?  396  ALA B CB  1 
ATOM   6121 N  N   . VAL B 1 395 ? 51.699  12.412  -40.707 1.00 11.29 ?  397  VAL B N   1 
ATOM   6122 C  CA  . VAL B 1 395 ? 52.187  11.107  -40.268 1.00 13.35 ?  397  VAL B CA  1 
ATOM   6123 C  C   . VAL B 1 395 ? 53.488  11.256  -39.492 1.00 11.61 ?  397  VAL B C   1 
ATOM   6124 O  O   . VAL B 1 395 ? 53.686  10.606  -38.460 1.00 13.63 ?  397  VAL B O   1 
ATOM   6125 C  CB  . VAL B 1 395 ? 52.356  10.174  -41.483 1.00 12.63 ?  397  VAL B CB  1 
ATOM   6126 C  CG1 . VAL B 1 395 ? 53.027  8.873   -41.092 1.00 11.59 ?  397  VAL B CG1 1 
ATOM   6127 C  CG2 . VAL B 1 395 ? 50.996  9.884   -42.122 1.00 9.87  ?  397  VAL B CG2 1 
ATOM   6128 N  N   . ALA B 1 396 ? 54.401  12.093  -39.992 1.00 11.47 ?  398  ALA B N   1 
ATOM   6129 C  CA  . ALA B 1 396 ? 55.673  12.317  -39.312 1.00 15.50 ?  398  ALA B CA  1 
ATOM   6130 C  C   . ALA B 1 396 ? 55.449  12.865  -37.908 1.00 16.69 ?  398  ALA B C   1 
ATOM   6131 O  O   . ALA B 1 396 ? 56.101  12.426  -36.949 1.00 14.41 ?  398  ALA B O   1 
ATOM   6132 C  CB  . ALA B 1 396 ? 56.540  13.276  -40.132 1.00 16.44 ?  398  ALA B CB  1 
ATOM   6133 N  N   . GLN B 1 397 ? 54.519  13.820  -37.770 1.00 10.08 ?  399  GLN B N   1 
ATOM   6134 C  CA  . GLN B 1 397 ? 54.196  14.380  -36.462 1.00 9.53  ?  399  GLN B CA  1 
ATOM   6135 C  C   . GLN B 1 397 ? 53.692  13.292  -35.525 1.00 16.64 ?  399  GLN B C   1 
ATOM   6136 O  O   . GLN B 1 397 ? 54.144  13.181  -34.374 1.00 13.04 ?  399  GLN B O   1 
ATOM   6137 C  CB  . GLN B 1 397 ? 53.138  15.487  -36.594 1.00 13.77 ?  399  GLN B CB  1 
ATOM   6138 C  CG  . GLN B 1 397 ? 53.635  16.813  -37.177 1.00 18.28 ?  399  GLN B CG  1 
ATOM   6139 C  CD  . GLN B 1 397 ? 52.508  17.745  -37.617 1.00 18.34 ?  399  GLN B CD  1 
ATOM   6140 O  OE1 . GLN B 1 397 ? 51.350  17.334  -37.763 1.00 19.53 ?  399  GLN B OE1 1 
ATOM   6141 N  NE2 . GLN B 1 397 ? 52.852  19.010  -37.857 1.00 17.29 ?  399  GLN B NE2 1 
ATOM   6142 N  N   . ALA B 1 398 ? 52.756  12.468  -36.016 1.00 11.64 ?  400  ALA B N   1 
ATOM   6143 C  CA  . ALA B 1 398 ? 52.176  11.406  -35.200 1.00 12.25 ?  400  ALA B CA  1 
ATOM   6144 C  C   . ALA B 1 398 ? 53.210  10.353  -34.844 1.00 9.51  ?  400  ALA B C   1 
ATOM   6145 O  O   . ALA B 1 398 ? 53.265  9.889   -33.699 1.00 14.85 ?  400  ALA B O   1 
ATOM   6146 C  CB  . ALA B 1 398 ? 50.996  10.759  -35.936 1.00 11.34 ?  400  ALA B CB  1 
ATOM   6147 N  N   . LEU B 1 399 ? 54.048  9.957   -35.806 1.00 9.59  ?  401  LEU B N   1 
ATOM   6148 C  CA  . LEU B 1 399 ? 55.030  8.930   -35.481 1.00 11.43 ?  401  LEU B CA  1 
ATOM   6149 C  C   . LEU B 1 399 ? 56.059  9.452   -34.490 1.00 17.63 ?  401  LEU B C   1 
ATOM   6150 O  O   . LEU B 1 399 ? 56.611  8.673   -33.703 1.00 16.09 ?  401  LEU B O   1 
ATOM   6151 C  CB  . LEU B 1 399 ? 55.742  8.426   -36.726 1.00 12.53 ?  401  LEU B CB  1 
ATOM   6152 C  CG  . LEU B 1 399 ? 54.868  7.521   -37.599 1.00 16.99 ?  401  LEU B CG  1 
ATOM   6153 C  CD1 . LEU B 1 399 ? 55.523  7.386   -38.955 1.00 14.24 ?  401  LEU B CD1 1 
ATOM   6154 C  CD2 . LEU B 1 399 ? 54.515  6.194   -36.958 1.00 19.13 ?  401  LEU B CD2 1 
ATOM   6155 N  N   . GLU B 1 400 ? 56.327  10.757  -34.516 1.00 15.29 ?  402  GLU B N   1 
ATOM   6156 C  CA  . GLU B 1 400 ? 57.222  11.343  -33.523 1.00 19.40 ?  402  GLU B CA  1 
ATOM   6157 C  C   . GLU B 1 400 ? 56.628  11.223  -32.120 1.00 17.98 ?  402  GLU B C   1 
ATOM   6158 O  O   . GLU B 1 400 ? 57.344  10.940  -31.150 1.00 20.16 ?  402  GLU B O   1 
ATOM   6159 C  CB  . GLU B 1 400 ? 57.494  12.811  -33.862 1.00 16.70 ?  402  GLU B CB  1 
ATOM   6160 C  CG  . GLU B 1 400 ? 58.708  13.419  -33.138 1.00 23.54 ?  402  GLU B CG  1 
ATOM   6161 C  CD  . GLU B 1 400 ? 60.024  12.773  -33.540 1.00 33.47 ?  402  GLU B CD  1 
ATOM   6162 O  OE1 . GLU B 1 400 ? 60.930  12.643  -32.687 1.00 27.60 ?  402  GLU B OE1 1 
ATOM   6163 O  OE2 . GLU B 1 400 ? 60.163  12.404  -34.723 1.00 34.13 ?  402  GLU B OE2 1 
ATOM   6164 N  N   . GLN B 1 401 ? 55.319  11.445  -31.993 1.00 15.42 ?  403  GLN B N   1 
ATOM   6165 C  CA  . GLN B 1 401 ? 54.669  11.300  -30.697 1.00 14.62 ?  403  GLN B CA  1 
ATOM   6166 C  C   . GLN B 1 401 ? 54.703  9.849   -30.228 1.00 18.09 ?  403  GLN B C   1 
ATOM   6167 O  O   . GLN B 1 401 ? 55.086  9.568   -29.086 1.00 16.67 ?  403  GLN B O   1 
ATOM   6168 C  CB  . GLN B 1 401 ? 53.224  11.812  -30.750 1.00 16.11 ?  403  GLN B CB  1 
ATOM   6169 C  CG  . GLN B 1 401 ? 52.490  11.615  -29.420 1.00 15.61 ?  403  GLN B CG  1 
ATOM   6170 C  CD  . GLN B 1 401 ? 51.008  11.952  -29.445 1.00 22.30 ?  403  GLN B CD  1 
ATOM   6171 O  OE1 . GLN B 1 401 ? 50.478  12.482  -30.427 1.00 20.22 ?  403  GLN B OE1 1 
ATOM   6172 N  NE2 . GLN B 1 401 ? 50.319  11.634  -28.340 1.00 17.20 ?  403  GLN B NE2 1 
ATOM   6173 N  N   . TYR B 1 402 ? 54.328  8.909   -31.097 1.00 14.34 ?  404  TYR B N   1 
ATOM   6174 C  CA  . TYR B 1 402 ? 54.120  7.535   -30.651 1.00 13.77 ?  404  TYR B CA  1 
ATOM   6175 C  C   . TYR B 1 402 ? 55.393  6.682   -30.633 1.00 16.16 ?  404  TYR B C   1 
ATOM   6176 O  O   . TYR B 1 402 ? 55.367  5.575   -30.083 1.00 17.38 ?  404  TYR B O   1 
ATOM   6177 C  CB  . TYR B 1 402 ? 53.039  6.874   -31.523 1.00 15.01 ?  404  TYR B CB  1 
ATOM   6178 C  CG  . TYR B 1 402 ? 51.727  7.626   -31.442 1.00 16.96 ?  404  TYR B CG  1 
ATOM   6179 C  CD1 . TYR B 1 402 ? 51.106  7.861   -30.215 1.00 14.43 ?  404  TYR B CD1 1 
ATOM   6180 C  CD2 . TYR B 1 402 ? 51.107  8.109   -32.588 1.00 15.73 ?  404  TYR B CD2 1 
ATOM   6181 C  CE1 . TYR B 1 402 ? 49.903  8.560   -30.133 1.00 16.80 ?  404  TYR B CE1 1 
ATOM   6182 C  CE2 . TYR B 1 402 ? 49.917  8.812   -32.513 1.00 12.55 ?  404  TYR B CE2 1 
ATOM   6183 C  CZ  . TYR B 1 402 ? 49.319  9.035   -31.289 1.00 12.45 ?  404  TYR B CZ  1 
ATOM   6184 O  OH  . TYR B 1 402 ? 48.141  9.733   -31.220 1.00 12.33 ?  404  TYR B OH  1 
ATOM   6185 N  N   . GLY B 1 403 ? 56.504  7.146   -31.205 1.00 18.65 ?  405  GLY B N   1 
ATOM   6186 C  CA  . GLY B 1 403 ? 57.781  6.491   -30.993 1.00 20.90 ?  405  GLY B CA  1 
ATOM   6187 C  C   . GLY B 1 403 ? 58.210  5.480   -32.046 1.00 18.21 ?  405  GLY B C   1 
ATOM   6188 O  O   . GLY B 1 403 ? 57.498  5.202   -33.014 1.00 19.16 ?  405  GLY B O   1 
ATOM   6189 N  N   . PRO B 1 404 ? 59.388  4.876   -31.842 1.00 19.44 ?  406  PRO B N   1 
ATOM   6190 C  CA  . PRO B 1 404 ? 59.969  4.006   -32.880 1.00 22.80 ?  406  PRO B CA  1 
ATOM   6191 C  C   . PRO B 1 404 ? 59.196  2.729   -33.164 1.00 18.57 ?  406  PRO B C   1 
ATOM   6192 O  O   . PRO B 1 404 ? 59.431  2.120   -34.213 1.00 28.94 ?  406  PRO B O   1 
ATOM   6193 C  CB  . PRO B 1 404 ? 61.362  3.681   -32.316 1.00 27.20 ?  406  PRO B CB  1 
ATOM   6194 C  CG  . PRO B 1 404 ? 61.184  3.813   -30.842 1.00 25.02 ?  406  PRO B CG  1 
ATOM   6195 C  CD  . PRO B 1 404 ? 60.293  5.019   -30.688 1.00 23.76 ?  406  PRO B CD  1 
ATOM   6196 N  N   . GLU B 1 405 ? 58.318  2.277   -32.275 1.00 17.44 ?  407  GLU B N   1 
ATOM   6197 C  CA  . GLU B 1 405 ? 57.576  1.050   -32.522 1.00 23.54 ?  407  GLU B CA  1 
ATOM   6198 C  C   . GLU B 1 405 ? 56.190  1.306   -33.093 1.00 19.16 ?  407  GLU B C   1 
ATOM   6199 O  O   . GLU B 1 405 ? 55.445  0.351   -33.332 1.00 21.46 ?  407  GLU B O   1 
ATOM   6200 C  CB  . GLU B 1 405 ? 57.463  0.216   -31.239 1.00 27.51 ?  407  GLU B CB  1 
ATOM   6201 C  CG  . GLU B 1 405 ? 58.780  -0.414  -30.811 1.00 34.17 ?  407  GLU B CG  1 
ATOM   6202 C  CD  . GLU B 1 405 ? 59.661  0.538   -30.031 1.00 45.68 ?  407  GLU B CD  1 
ATOM   6203 O  OE1 . GLU B 1 405 ? 59.113  1.368   -29.266 1.00 52.39 ?  407  GLU B OE1 1 
ATOM   6204 O  OE2 . GLU B 1 405 ? 60.899  0.470   -30.192 1.00 53.19 ?  407  GLU B OE2 1 
ATOM   6205 N  N   . ALA B 1 406 ? 55.832  2.563   -33.303 1.00 18.04 ?  408  ALA B N   1 
ATOM   6206 C  CA  . ALA B 1 406 ? 54.512  2.888   -33.826 1.00 17.70 ?  408  ALA B CA  1 
ATOM   6207 C  C   . ALA B 1 406 ? 54.378  2.410   -35.266 1.00 20.10 ?  408  ALA B C   1 
ATOM   6208 O  O   . ALA B 1 406 ? 55.346  2.395   -36.032 1.00 20.29 ?  408  ALA B O   1 
ATOM   6209 C  CB  . ALA B 1 406 ? 54.271  4.395   -33.743 1.00 20.95 ?  408  ALA B CB  1 
ATOM   6210 N  N   . ARG B 1 407 ? 53.158  2.016   -35.633 1.00 15.39 ?  409  ARG B N   1 
ATOM   6211 C  CA  . ARG B 1 407 ? 52.878  1.476   -36.951 1.00 13.39 ?  409  ARG B CA  1 
ATOM   6212 C  C   . ARG B 1 407 ? 51.799  2.328   -37.608 1.00 14.01 ?  409  ARG B C   1 
ATOM   6213 O  O   . ARG B 1 407 ? 51.030  3.011   -36.926 1.00 12.50 ?  409  ARG B O   1 
ATOM   6214 C  CB  . ARG B 1 407 ? 52.429  0.018   -36.859 1.00 16.99 ?  409  ARG B CB  1 
ATOM   6215 C  CG  . ARG B 1 407 ? 53.520  -0.891  -36.252 1.00 22.41 ?  409  ARG B CG  1 
ATOM   6216 C  CD  . ARG B 1 407 ? 54.679  -1.078  -37.210 1.00 28.67 ?  409  ARG B CD  1 
ATOM   6217 N  NE  . ARG B 1 407 ? 54.277  -1.724  -38.462 1.00 40.68 ?  409  ARG B NE  1 
ATOM   6218 C  CZ  . ARG B 1 407 ? 55.120  -2.348  -39.286 1.00 43.64 ?  409  ARG B CZ  1 
ATOM   6219 N  NH1 . ARG B 1 407 ? 56.415  -2.392  -38.998 1.00 45.34 ?  409  ARG B NH1 1 
ATOM   6220 N  NH2 . ARG B 1 407 ? 54.677  -2.909  -40.405 1.00 36.97 ?  409  ARG B NH2 1 
ATOM   6221 N  N   . VAL B 1 408 ? 51.750  2.284   -38.940 1.00 13.16 ?  410  VAL B N   1 
ATOM   6222 C  CA  . VAL B 1 408 ? 50.793  3.069   -39.714 1.00 14.08 ?  410  VAL B CA  1 
ATOM   6223 C  C   . VAL B 1 408 ? 49.971  2.094   -40.537 1.00 12.46 ?  410  VAL B C   1 
ATOM   6224 O  O   . VAL B 1 408 ? 50.528  1.211   -41.194 1.00 11.69 ?  410  VAL B O   1 
ATOM   6225 C  CB  . VAL B 1 408 ? 51.492  4.084   -40.640 1.00 15.03 ?  410  VAL B CB  1 
ATOM   6226 C  CG1 . VAL B 1 408 ? 50.469  4.856   -41.468 1.00 11.33 ?  410  VAL B CG1 1 
ATOM   6227 C  CG2 . VAL B 1 408 ? 52.370  5.036   -39.856 1.00 13.99 ?  410  VAL B CG2 1 
ATOM   6228 N  N   . ALA B 1 409 ? 48.656  2.249   -40.506 1.00 12.31 ?  411  ALA B N   1 
ATOM   6229 C  CA  . ALA B 1 409 ? 47.786  1.562   -41.449 1.00 12.72 ?  411  ALA B CA  1 
ATOM   6230 C  C   . ALA B 1 409 ? 47.212  2.610   -42.385 1.00 10.00 ?  411  ALA B C   1 
ATOM   6231 O  O   . ALA B 1 409 ? 46.989  3.754   -41.977 1.00 11.69 ?  411  ALA B O   1 
ATOM   6232 C  CB  . ALA B 1 409 ? 46.656  0.804   -40.744 1.00 12.04 ?  411  ALA B CB  1 
ATOM   6233 N  N   . VAL B 1 410 ? 47.013  2.235   -43.652 1.00 11.15 ?  412  VAL B N   1 
ATOM   6234 C  CA  . VAL B 1 410 ? 46.446  3.148   -44.642 1.00 10.86 ?  412  VAL B CA  1 
ATOM   6235 C  C   . VAL B 1 410 ? 45.255  2.473   -45.317 1.00 11.67 ?  412  VAL B C   1 
ATOM   6236 O  O   . VAL B 1 410 ? 45.301  1.278   -45.635 1.00 10.61 ?  412  VAL B O   1 
ATOM   6237 C  CB  . VAL B 1 410 ? 47.509  3.616   -45.671 1.00 17.95 ?  412  VAL B CB  1 
ATOM   6238 C  CG1 . VAL B 1 410 ? 48.128  2.450   -46.418 1.00 14.22 ?  412  VAL B CG1 1 
ATOM   6239 C  CG2 . VAL B 1 410 ? 46.920  4.667   -46.640 1.00 13.84 ?  412  VAL B CG2 1 
ATOM   6240 N  N   . ILE B 1 411 ? 44.176  3.238   -45.484 1.00 10.60 ?  413  ILE B N   1 
ATOM   6241 C  CA  . ILE B 1 411 ? 42.924  2.804   -46.106 1.00 11.06 ?  413  ILE B CA  1 
ATOM   6242 C  C   . ILE B 1 411 ? 42.628  3.723   -47.286 1.00 11.29 ?  413  ILE B C   1 
ATOM   6243 O  O   . ILE B 1 411 ? 41.961  4.753   -47.112 1.00 10.25 ?  413  ILE B O   1 
ATOM   6244 C  CB  . ILE B 1 411 ? 41.765  2.841   -45.093 1.00 9.87  ?  413  ILE B CB  1 
ATOM   6245 C  CG1 . ILE B 1 411 ? 42.200  2.260   -43.743 1.00 10.02 ?  413  ILE B CG1 1 
ATOM   6246 C  CG2 . ILE B 1 411 ? 40.499  2.194   -45.673 1.00 9.71  ?  413  ILE B CG2 1 
ATOM   6247 C  CD1 . ILE B 1 411 ? 41.190  2.523   -42.589 1.00 14.72 ?  413  ILE B CD1 1 
ATOM   6248 N  N   . PRO B 1 412 ? 43.101  3.403   -48.490 1.00 11.59 ?  414  PRO B N   1 
ATOM   6249 C  CA  . PRO B 1 412 ? 42.942  4.343   -49.610 1.00 12.67 ?  414  PRO B CA  1 
ATOM   6250 C  C   . PRO B 1 412 ? 41.504  4.689   -49.924 1.00 10.01 ?  414  PRO B C   1 
ATOM   6251 O  O   . PRO B 1 412 ? 41.226  5.855   -50.233 1.00 13.79 ?  414  PRO B O   1 
ATOM   6252 C  CB  . PRO B 1 412 ? 43.606  3.603   -50.773 1.00 11.16 ?  414  PRO B CB  1 
ATOM   6253 C  CG  . PRO B 1 412 ? 44.701  2.820   -50.090 1.00 12.55 ?  414  PRO B CG  1 
ATOM   6254 C  CD  . PRO B 1 412 ? 44.031  2.312   -48.815 1.00 12.67 ?  414  PRO B CD  1 
ATOM   6255 N  N   . LYS B 1 413 ? 40.574  3.736   -49.801 1.00 10.77 ?  415  LYS B N   1 
ATOM   6256 C  CA  . LYS B 1 413 ? 39.186  3.960   -50.177 1.00 11.53 ?  415  LYS B CA  1 
ATOM   6257 C  C   . LYS B 1 413 ? 38.322  4.353   -48.979 1.00 11.63 ?  415  LYS B C   1 
ATOM   6258 O  O   . LYS B 1 413 ? 37.090  4.375   -49.092 1.00 11.03 ?  415  LYS B O   1 
ATOM   6259 C  CB  . LYS B 1 413 ? 38.619  2.697   -50.831 1.00 14.07 ?  415  LYS B CB  1 
ATOM   6260 C  CG  . LYS B 1 413 ? 39.416  2.361   -52.080 1.00 26.00 ?  415  LYS B CG  1 
ATOM   6261 C  CD  . LYS B 1 413 ? 39.279  3.322   -53.161 1.00 29.54 ?  415  LYS B CD  1 
ATOM   6262 C  CE  . LYS B 1 413 ? 40.113  2.861   -54.361 1.00 27.18 ?  415  LYS B CE  1 
ATOM   6263 N  NZ  . LYS B 1 413 ? 39.966  3.880   -55.410 1.00 25.22 ?  415  LYS B NZ  1 
ATOM   6264 N  N   . GLY B 1 414 ? 38.940  4.641   -47.832 1.00 11.01 ?  416  GLY B N   1 
ATOM   6265 C  CA  . GLY B 1 414 ? 38.252  5.181   -46.674 1.00 10.12 ?  416  GLY B CA  1 
ATOM   6266 C  C   . GLY B 1 414 ? 37.021  4.399   -46.236 1.00 10.95 ?  416  GLY B C   1 
ATOM   6267 O  O   . GLY B 1 414 ? 37.081  3.188   -46.017 1.00 10.18 ?  416  GLY B O   1 
ATOM   6268 N  N   . PRO B 1 415 ? 35.870  5.077   -46.122 1.00 11.35 ?  417  PRO B N   1 
ATOM   6269 C  CA  . PRO B 1 415 ? 34.685  4.427   -45.538 1.00 10.78 ?  417  PRO B CA  1 
ATOM   6270 C  C   . PRO B 1 415 ? 34.030  3.386   -46.438 1.00 12.78 ?  417  PRO B C   1 
ATOM   6271 O  O   . PRO B 1 415 ? 33.017  2.799   -46.033 1.00 12.04 ?  417  PRO B O   1 
ATOM   6272 C  CB  . PRO B 1 415 ? 33.736  5.609   -45.276 1.00 10.52 ?  417  PRO B CB  1 
ATOM   6273 C  CG  . PRO B 1 415 ? 34.123  6.599   -46.357 1.00 13.19 ?  417  PRO B CG  1 
ATOM   6274 C  CD  . PRO B 1 415 ? 35.615  6.483   -46.463 1.00 10.69 ?  417  PRO B CD  1 
ATOM   6275 N  N   . TYR B 1 416 ? 34.543  3.154   -47.645 1.00 9.09  ?  418  TYR B N   1 
ATOM   6276 C  CA  . TYR B 1 416 ? 34.075  2.037   -48.456 1.00 13.17 ?  418  TYR B CA  1 
ATOM   6277 C  C   . TYR B 1 416 ? 34.767  0.726   -48.087 1.00 13.60 ?  418  TYR B C   1 
ATOM   6278 O  O   . TYR B 1 416 ? 34.440  -0.317  -48.666 1.00 16.67 ?  418  TYR B O   1 
ATOM   6279 C  CB  . TYR B 1 416 ? 34.269  2.353   -49.953 1.00 11.86 ?  418  TYR B CB  1 
ATOM   6280 C  CG  . TYR B 1 416 ? 33.366  3.466   -50.484 1.00 12.50 ?  418  TYR B CG  1 
ATOM   6281 C  CD1 . TYR B 1 416 ? 32.326  3.986   -49.715 1.00 11.65 ?  418  TYR B CD1 1 
ATOM   6282 C  CD2 . TYR B 1 416 ? 33.570  3.999   -51.758 1.00 13.46 ?  418  TYR B CD2 1 
ATOM   6283 C  CE1 . TYR B 1 416 ? 31.492  5.011   -50.210 1.00 14.74 ?  418  TYR B CE1 1 
ATOM   6284 C  CE2 . TYR B 1 416 ? 32.755  5.018   -52.263 1.00 16.30 ?  418  TYR B CE2 1 
ATOM   6285 C  CZ  . TYR B 1 416 ? 31.722  5.525   -51.483 1.00 20.51 ?  418  TYR B CZ  1 
ATOM   6286 O  OH  . TYR B 1 416 ? 30.919  6.538   -51.991 1.00 15.71 ?  418  TYR B OH  1 
ATOM   6287 N  N   . VAL B 1 417 ? 35.721  0.764   -47.151 1.00 10.75 ?  419  VAL B N   1 
ATOM   6288 C  CA  . VAL B 1 417 ? 36.369  -0.414  -46.586 1.00 13.02 ?  419  VAL B CA  1 
ATOM   6289 C  C   . VAL B 1 417 ? 35.868  -0.582  -45.157 1.00 13.56 ?  419  VAL B C   1 
ATOM   6290 O  O   . VAL B 1 417 ? 35.523  0.398   -44.486 1.00 15.25 ?  419  VAL B O   1 
ATOM   6291 C  CB  . VAL B 1 417 ? 37.913  -0.268  -46.619 1.00 13.11 ?  419  VAL B CB  1 
ATOM   6292 C  CG1 . VAL B 1 417 ? 38.609  -1.441  -45.960 1.00 15.05 ?  419  VAL B CG1 1 
ATOM   6293 C  CG2 . VAL B 1 417 ? 38.410  -0.103  -48.064 1.00 15.25 ?  419  VAL B CG2 1 
ATOM   6294 N  N   . LEU B 1 418 ? 35.828  -1.831  -44.691 1.00 13.07 ?  420  LEU B N   1 
ATOM   6295 C  CA  . LEU B 1 418 ? 35.464  -2.157  -43.311 1.00 13.03 ?  420  LEU B CA  1 
ATOM   6296 C  C   . LEU B 1 418 ? 36.695  -2.720  -42.606 1.00 16.44 ?  420  LEU B C   1 
ATOM   6297 O  O   . LEU B 1 418 ? 36.954  -3.932  -42.658 1.00 18.85 ?  420  LEU B O   1 
ATOM   6298 C  CB  . LEU B 1 418 ? 34.303  -3.159  -43.293 1.00 18.53 ?  420  LEU B CB  1 
ATOM   6299 C  CG  . LEU B 1 418 ? 33.465  -3.354  -42.029 1.00 25.15 ?  420  LEU B CG  1 
ATOM   6300 C  CD1 . LEU B 1 418 ? 32.717  -2.083  -41.722 1.00 26.90 ?  420  LEU B CD1 1 
ATOM   6301 C  CD2 . LEU B 1 418 ? 32.476  -4.505  -42.208 1.00 21.54 ?  420  LEU B CD2 1 
ATOM   6302 N  N   . PRO B 1 419 ? 37.518  -1.884  -41.978 1.00 13.71 ?  421  PRO B N   1 
ATOM   6303 C  CA  . PRO B 1 419 ? 38.732  -2.404  -41.328 1.00 13.73 ?  421  PRO B CA  1 
ATOM   6304 C  C   . PRO B 1 419 ? 38.392  -3.098  -40.020 1.00 16.11 ?  421  PRO B C   1 
ATOM   6305 O  O   . PRO B 1 419 ? 37.495  -2.675  -39.287 1.00 17.71 ?  421  PRO B O   1 
ATOM   6306 C  CB  . PRO B 1 419 ? 39.586  -1.149  -41.107 1.00 17.41 ?  421  PRO B CB  1 
ATOM   6307 C  CG  . PRO B 1 419 ? 38.600  -0.039  -40.994 1.00 19.27 ?  421  PRO B CG  1 
ATOM   6308 C  CD  . PRO B 1 419 ? 37.386  -0.424  -41.847 1.00 14.99 ?  421  PRO B CD  1 
ATOM   6309 N  N   . VAL B 1 420 ? 39.092  -4.206  -39.749 1.00 19.84 ?  422  VAL B N   1 
ATOM   6310 C  CA  . VAL B 1 420 ? 38.855  -5.007  -38.552 1.00 16.43 ?  422  VAL B CA  1 
ATOM   6311 C  C   . VAL B 1 420 ? 40.192  -5.491  -38.006 1.00 16.55 ?  422  VAL B C   1 
ATOM   6312 O  O   . VAL B 1 420 ? 41.196  -5.543  -38.714 1.00 17.91 ?  422  VAL B O   1 
ATOM   6313 C  CB  . VAL B 1 420 ? 37.940  -6.223  -38.814 1.00 19.76 ?  422  VAL B CB  1 
ATOM   6314 C  CG1 . VAL B 1 420 ? 36.623  -5.805  -39.481 1.00 19.23 ?  422  VAL B CG1 1 
ATOM   6315 C  CG2 . VAL B 1 420 ? 38.672  -7.251  -39.640 1.00 18.69 ?  422  VAL B CG2 1 
ATOM   6316 N  N   . VAL B 1 421 ? 40.187  -5.871  -36.736 1.00 18.13 ?  423  VAL B N   1 
ATOM   6317 C  CA  . VAL B 1 421 ? 41.368  -6.431  -36.085 1.00 18.65 ?  423  VAL B CA  1 
ATOM   6318 C  C   . VAL B 1 421 ? 41.218  -7.946  -36.062 1.00 24.81 ?  423  VAL B C   1 
ATOM   6319 O  O   . VAL B 1 421 ? 40.225  -8.464  -35.538 1.00 33.83 ?  423  VAL B O   1 
ATOM   6320 C  CB  . VAL B 1 421 ? 41.551  -5.871  -34.664 1.00 22.20 ?  423  VAL B CB  1 
ATOM   6321 C  CG1 . VAL B 1 421 ? 42.605  -6.691  -33.892 1.00 25.97 ?  423  VAL B CG1 1 
ATOM   6322 C  CG2 . VAL B 1 421 ? 41.965  -4.399  -34.709 1.00 20.76 ?  423  VAL B CG2 1 
ATOM   6323 N  N   . ASP B 1 422 ? 42.205  -8.651  -36.612 1.00 25.13 ?  424  ASP B N   1 
ATOM   6324 C  CA  . ASP B 1 422 ? 42.220  -10.115 -36.654 1.00 34.22 ?  424  ASP B CA  1 
ATOM   6325 C  C   . ASP B 1 422 ? 43.462  -10.645 -35.950 1.00 31.04 ?  424  ASP B C   1 
ATOM   6326 O  O   . ASP B 1 422 ? 44.537  -10.728 -36.570 1.00 28.53 ?  424  ASP B O   1 
ATOM   6327 C  CB  . ASP B 1 422 ? 42.185  -10.614 -38.097 1.00 32.84 ?  424  ASP B CB  1 
ATOM   6328 N  N   . PRO B 1 423 ? 43.364  -11.024 -34.660 1.00 36.42 ?  425  PRO B N   1 
ATOM   6329 C  CA  . PRO B 1 423 ? 44.544  -11.510 -33.919 1.00 38.33 ?  425  PRO B CA  1 
ATOM   6330 C  C   . PRO B 1 423 ? 45.429  -12.485 -34.690 1.00 44.37 ?  425  PRO B C   1 
ATOM   6331 O  O   . PRO B 1 423 ? 46.659  -12.370 -34.649 1.00 55.51 ?  425  PRO B O   1 
ATOM   6332 C  CB  . PRO B 1 423 ? 43.911  -12.176 -32.693 1.00 42.25 ?  425  PRO B CB  1 
ATOM   6333 C  CG  . PRO B 1 423 ? 42.711  -11.300 -32.416 1.00 41.95 ?  425  PRO B CG  1 
ATOM   6334 C  CD  . PRO B 1 423 ? 42.173  -10.932 -33.792 1.00 37.20 ?  425  PRO B CD  1 
ATOM   6335 N  N   . THR B 1 424 ? 44.829  -13.437 -35.399 1.00 44.21 ?  426  THR B N   1 
ATOM   6336 C  CA  . THR B 1 424 ? 45.583  -14.269 -36.330 1.00 40.41 ?  426  THR B CA  1 
ATOM   6337 C  C   . THR B 1 424 ? 46.143  -13.403 -37.454 1.00 40.77 ?  426  THR B C   1 
ATOM   6338 O  O   . THR B 1 424 ? 47.329  -13.468 -37.774 1.00 45.07 ?  426  THR B O   1 
ATOM   6339 C  CB  . THR B 1 424 ? 44.713  -15.389 -36.932 1.00 36.79 ?  426  THR B CB  1 
HETATM 6340 C  C1  . EDO C 2 .   ? 34.304  8.324   20.634  1.00 30.00 ?  501  EDO A C1  1 
HETATM 6341 O  O1  . EDO C 2 .   ? 35.136  8.120   21.747  1.00 42.02 ?  501  EDO A O1  1 
HETATM 6342 C  C2  . EDO C 2 .   ? 32.884  8.688   21.071  1.00 33.69 ?  501  EDO A C2  1 
HETATM 6343 O  O2  . EDO C 2 .   ? 32.791  10.075  21.288  1.00 42.35 ?  501  EDO A O2  1 
HETATM 6344 C  C1  . EDO D 2 .   ? 2.274   13.547  5.891   1.00 23.48 ?  502  EDO A C1  1 
HETATM 6345 O  O1  . EDO D 2 .   ? 2.181   13.758  4.518   1.00 33.74 ?  502  EDO A O1  1 
HETATM 6346 C  C2  . EDO D 2 .   ? 3.757   13.560  6.228   1.00 24.84 ?  502  EDO A C2  1 
HETATM 6347 O  O2  . EDO D 2 .   ? 3.896   13.558  7.602   1.00 26.47 ?  502  EDO A O2  1 
HETATM 6348 C  C2  . 4EY E 3 .   ? 22.994  3.582   6.283   1.00 8.92  ?  503  4EY A C2  1 
HETATM 6349 C  C3  . 4EY E 3 .   ? 23.264  3.573   7.670   1.00 8.68  ?  503  4EY A C3  1 
HETATM 6350 C  C1  . 4EY E 3 .   ? 24.158  0.021   8.180   1.00 10.34 ?  503  4EY A C1  1 
HETATM 6351 C  C4  . 4EY E 3 .   ? 23.595  2.376   8.277   1.00 12.29 ?  503  4EY A C4  1 
HETATM 6352 C  C5  . 4EY E 3 .   ? 23.712  1.227   7.506   1.00 9.11  ?  503  4EY A C5  1 
HETATM 6353 C  C6  . 4EY E 3 .   ? 23.460  1.297   6.138   1.00 7.55  ?  503  4EY A C6  1 
HETATM 6354 O  O2  . 4EY E 3 .   ? 24.185  -1.086  7.631   1.00 12.17 ?  503  4EY A O2  1 
HETATM 6355 O  O2P . 4EY E 3 .   ? 21.069  6.935   5.864   1.00 8.44  -1 503  4EY A O2P 1 
HETATM 6356 P  P   . 4EY E 3 .   ? 21.454  6.972   4.330   1.00 7.82  ?  503  4EY A P   1 
HETATM 6357 O  O3P . 4EY E 3 .   ? 22.063  8.286   4.006   1.00 11.31 ?  503  4EY A O3P 1 
HETATM 6358 O  O1P . 4EY E 3 .   ? 20.177  6.670   3.439   1.00 9.28  -1 503  4EY A O1P 1 
HETATM 6359 O  O5R . 4EY E 3 .   ? 22.516  5.768   4.174   1.00 7.26  ?  503  4EY A O5R 1 
HETATM 6360 C  C5R . 4EY E 3 .   ? 23.275  5.647   2.982   1.00 7.31  ?  503  4EY A C5R 1 
HETATM 6361 C  C4R . 4EY E 3 .   ? 23.284  4.174   2.565   1.00 6.96  ?  503  4EY A C4R 1 
HETATM 6362 O  O4R . 4EY E 3 .   ? 23.875  3.344   3.591   1.00 9.35  ?  503  4EY A O4R 1 
HETATM 6363 C  C3R . 4EY E 3 .   ? 21.854  3.626   2.365   1.00 5.88  ?  503  4EY A C3R 1 
HETATM 6364 O  O3R . 4EY E 3 .   ? 21.857  2.671   1.288   1.00 9.58  ?  503  4EY A O3R 1 
HETATM 6365 C  C2R . 4EY E 3 .   ? 21.510  2.967   3.709   1.00 7.62  ?  503  4EY A C2R 1 
HETATM 6366 O  O2R . 4EY E 3 .   ? 20.581  1.884   3.548   1.00 11.45 ?  503  4EY A O2R 1 
HETATM 6367 C  C1R . 4EY E 3 .   ? 22.890  2.432   4.144   1.00 8.19  ?  503  4EY A C1R 1 
HETATM 6368 N  N1  . 4EY E 3 .   ? 23.108  2.447   5.585   1.00 7.97  ?  503  4EY A N1  1 
HETATM 6369 C  C7  . 4EY E 3 .   ? 23.192  4.729   8.571   1.00 8.20  ?  503  4EY A C7  1 
HETATM 6370 S  S7  . 4EY E 3 .   ? 24.001  4.633   9.966   1.00 8.89  ?  503  4EY A S7  1 
HETATM 6371 S  S2  . 4EY E 3 .   ? 24.845  0.342   9.773   1.00 12.51 ?  503  4EY A S2  1 
HETATM 6372 C  C1  . PEG F 4 .   ? 23.345  8.453   -22.252 1.00 29.38 ?  504  PEG A C1  1 
HETATM 6373 O  O1  . PEG F 4 .   ? 23.869  7.324   -22.898 1.00 41.45 ?  504  PEG A O1  1 
HETATM 6374 C  C2  . PEG F 4 .   ? 23.067  8.111   -20.789 1.00 27.77 ?  504  PEG A C2  1 
HETATM 6375 O  O2  . PEG F 4 .   ? 21.766  7.611   -20.685 1.00 37.08 ?  504  PEG A O2  1 
HETATM 6376 C  C3  . PEG F 4 .   ? 21.569  6.777   -19.580 1.00 36.37 ?  504  PEG A C3  1 
HETATM 6377 C  C4  . PEG F 4 .   ? 20.137  6.942   -19.090 1.00 35.28 ?  504  PEG A C4  1 
HETATM 6378 O  O4  . PEG F 4 .   ? 19.326  5.970   -19.688 1.00 43.11 ?  504  PEG A O4  1 
HETATM 6379 C  C   . LAC G 5 .   ? 20.084  2.005   8.720   1.00 12.93 ?  505  LAC A C   1 
HETATM 6380 C  CA  . LAC G 5 .   ? 20.762  1.119   9.743   1.00 17.57 ?  505  LAC A CA  1 
HETATM 6381 C  CB  . LAC G 5 .   ? 19.826  0.959   10.945  1.00 13.85 ?  505  LAC A CB  1 
HETATM 6382 O  O   . LAC G 5 .   ? 19.885  3.217   8.996   1.00 12.33 ?  505  LAC A O   1 
HETATM 6383 O  OHN . LAC G 5 .   ? 20.989  -0.093  9.107   1.00 11.31 ?  505  LAC A OHN 1 
HETATM 6384 O  OXT . LAC G 5 .   ? 19.707  1.496   7.621   1.00 12.94 ?  505  LAC A OXT 1 
HETATM 6385 NI NI  . NI  H 6 .   ? 24.448  2.478   10.045  1.00 10.27 ?  506  NI  A NI  1 
HETATM 6386 C  C1  . EDO I 2 .   ? 37.671  18.321  -56.470 1.00 34.90 ?  701  EDO B C1  1 
HETATM 6387 O  O1  . EDO I 2 .   ? 36.559  18.006  -57.254 1.00 42.41 ?  701  EDO B O1  1 
HETATM 6388 C  C2  . EDO I 2 .   ? 38.893  18.212  -57.366 1.00 36.67 ?  701  EDO B C2  1 
HETATM 6389 O  O2  . EDO I 2 .   ? 39.048  16.871  -57.745 1.00 30.50 ?  701  EDO B O2  1 
HETATM 6390 C  C2  . 4EY J 3 .   ? 20.833  8.658   -46.296 1.00 12.23 ?  702  4EY B C2  1 
HETATM 6391 C  C3  . 4EY J 3 .   ? 21.063  8.681   -44.908 1.00 13.60 ?  702  4EY B C3  1 
HETATM 6392 C  C1  . 4EY J 3 .   ? 20.297  12.237  -44.170 1.00 15.99 ?  702  4EY B C1  1 
HETATM 6393 C  C4  . 4EY J 3 .   ? 20.903  9.886   -44.231 1.00 15.63 ?  702  4EY B C4  1 
HETATM 6394 C  C5  . 4EY J 3 .   ? 20.526  11.017  -44.942 1.00 12.40 ?  702  4EY B C5  1 
HETATM 6395 C  C6  . 4EY J 3 .   ? 20.315  10.928  -46.314 1.00 12.64 ?  702  4EY B C6  1 
HETATM 6396 O  O2  . 4EY J 3 .   ? 20.080  13.309  -44.714 1.00 18.47 ?  702  4EY B O2  1 
HETATM 6397 O  O2P . 4EY J 3 .   ? 22.667  5.511   -49.873 1.00 11.60 -1 702  4EY B O2P 1 
HETATM 6398 P  P   . 4EY J 3 .   ? 21.773  5.230   -48.586 1.00 11.09 ?  702  4EY B P   1 
HETATM 6399 O  O3P . 4EY J 3 .   ? 22.657  5.344   -47.391 1.00 11.34 ?  702  4EY B O3P 1 
HETATM 6400 O  O1P . 4EY J 3 .   ? 21.113  3.787   -48.603 1.00 13.92 -1 702  4EY B O1P 1 
HETATM 6401 O  O5R . 4EY J 3 .   ? 20.682  6.413   -48.458 1.00 13.84 ?  702  4EY B O5R 1 
HETATM 6402 C  C5R . 4EY J 3 .   ? 19.595  6.508   -49.397 1.00 11.12 ?  702  4EY B C5R 1 
HETATM 6403 C  C4R . 4EY J 3 .   ? 19.432  7.994   -49.732 1.00 10.74 ?  702  4EY B C4R 1 
HETATM 6404 O  O4R . 4EY J 3 .   ? 19.190  8.778   -48.537 1.00 13.41 ?  702  4EY B O4R 1 
HETATM 6405 C  C3R . 4EY J 3 .   ? 20.711  8.559   -50.388 1.00 12.83 ?  702  4EY B C3R 1 
HETATM 6406 O  O3R . 4EY J 3 .   ? 20.348  9.490   -51.430 1.00 16.46 ?  702  4EY B O3R 1 
HETATM 6407 C  C2R . 4EY J 3 .   ? 21.438  9.250   -49.218 1.00 11.46 ?  702  4EY B C2R 1 
HETATM 6408 O  O2R . 4EY J 3 .   ? 22.202  10.353  -49.684 1.00 13.07 ?  702  4EY B O2R 1 
HETATM 6409 C  C1R . 4EY J 3 .   ? 20.242  9.760   -48.380 1.00 14.64 ?  702  4EY B C1R 1 
HETATM 6410 N  N1  . 4EY J 3 .   ? 20.504  9.782   -46.940 1.00 13.27 ?  702  4EY B N1  1 
HETATM 6411 C  C7  . 4EY J 3 .   ? 21.442  7.514   -44.100 1.00 15.86 ?  702  4EY B C7  1 
HETATM 6412 S  S7  . 4EY J 3 .   ? 21.188  7.627   -42.495 1.00 12.18 ?  702  4EY B S7  1 
HETATM 6413 S  S2  . 4EY J 3 .   ? 20.176  11.951  -42.432 1.00 17.80 ?  702  4EY B S2  1 
HETATM 6414 C  C1  . PEG K 4 .   ? 28.328  -12.471 -57.901 1.00 30.19 ?  703  PEG B C1  1 
HETATM 6415 O  O1  . PEG K 4 .   ? 28.080  -11.672 -59.027 1.00 34.85 ?  703  PEG B O1  1 
HETATM 6416 C  C2  . PEG K 4 .   ? 27.704  -11.810 -56.670 1.00 31.13 ?  703  PEG B C2  1 
HETATM 6417 O  O2  . PEG K 4 .   ? 26.320  -12.039 -56.667 1.00 43.80 ?  703  PEG B O2  1 
HETATM 6418 C  C3  . PEG K 4 .   ? 25.619  -11.477 -55.588 1.00 32.76 ?  703  PEG B C3  1 
HETATM 6419 C  C4  . PEG K 4 .   ? 24.237  -12.125 -55.478 1.00 36.42 ?  703  PEG B C4  1 
HETATM 6420 O  O4  . PEG K 4 .   ? 23.508  -11.927 -56.661 1.00 38.18 ?  703  PEG B O4  1 
HETATM 6421 C  C1  . PEG L 4 .   ? 30.317  -1.413  -68.276 1.00 38.52 ?  704  PEG B C1  1 
HETATM 6422 O  O1  . PEG L 4 .   ? 29.653  -0.937  -69.416 1.00 36.67 ?  704  PEG B O1  1 
HETATM 6423 C  C2  . PEG L 4 .   ? 31.720  -1.872  -68.668 1.00 39.09 ?  704  PEG B C2  1 
HETATM 6424 O  O2  . PEG L 4 .   ? 32.324  -2.533  -67.589 1.00 43.26 ?  704  PEG B O2  1 
HETATM 6425 C  C3  . PEG L 4 .   ? 33.676  -2.216  -67.415 1.00 38.01 ?  704  PEG B C3  1 
HETATM 6426 C  C4  . PEG L 4 .   ? 34.297  -3.279  -66.516 1.00 35.47 ?  704  PEG B C4  1 
HETATM 6427 O  O4  . PEG L 4 .   ? 33.658  -4.492  -66.811 1.00 40.45 ?  704  PEG B O4  1 
HETATM 6428 C  C   . LAC M 5 .   ? 24.392  10.277  -44.901 1.00 16.63 ?  705  LAC B C   1 
HETATM 6429 C  CA  . LAC M 5 .   ? 24.070  11.148  -43.703 1.00 23.49 ?  705  LAC B CA  1 
HETATM 6430 C  CB  . LAC M 5 .   ? 25.325  11.306  -42.843 1.00 18.02 ?  705  LAC B CB  1 
HETATM 6431 O  O   . LAC M 5 .   ? 24.673  9.066   -44.741 1.00 14.38 ?  705  LAC B O   1 
HETATM 6432 O  OHN . LAC M 5 .   ? 23.663  12.390  -44.212 1.00 17.89 ?  705  LAC B OHN 1 
HETATM 6433 O  OXT . LAC M 5 .   ? 24.370  10.800  -46.055 1.00 14.10 -1 705  LAC B OXT 1 
HETATM 6434 NI NI  . NI  N 6 .   ? 20.697  9.758   -42.311 1.00 14.88 ?  706  NI  B NI  1 
HETATM 6435 O  O   . HOH O 7 .   ? 0.044   6.993   5.320   1.00 25.41 ?  601  HOH A O   1 
HETATM 6436 O  O   . HOH O 7 .   ? 12.692  -6.439  -1.691  1.00 22.09 ?  602  HOH A O   1 
HETATM 6437 O  O   . HOH O 7 .   ? 27.280  5.709   14.721  1.00 21.07 ?  603  HOH A O   1 
HETATM 6438 O  O   . HOH O 7 .   ? 13.399  10.648  25.543  1.00 37.51 ?  604  HOH A O   1 
HETATM 6439 O  O   . HOH O 7 .   ? 1.699   -11.540 13.445  1.00 33.89 ?  605  HOH A O   1 
HETATM 6440 O  O   . HOH O 7 .   ? 11.835  -5.532  -6.095  1.00 26.46 ?  606  HOH A O   1 
HETATM 6441 O  O   . HOH O 7 .   ? 7.223   -11.705 6.604   1.00 32.45 ?  607  HOH A O   1 
HETATM 6442 O  O   . HOH O 7 .   ? 14.364  -13.080 23.079  1.00 31.50 ?  608  HOH A O   1 
HETATM 6443 O  O   . HOH O 7 .   ? 26.107  -12.108 -2.427  1.00 31.85 ?  609  HOH A O   1 
HETATM 6444 O  O   . HOH O 7 .   ? 0.549   8.796   1.752   1.00 29.75 ?  610  HOH A O   1 
HETATM 6445 O  O   . HOH O 7 .   ? 22.388  24.920  -7.091  1.00 28.95 ?  611  HOH A O   1 
HETATM 6446 O  O   . HOH O 7 .   ? 28.948  0.213   -16.488 1.00 25.02 ?  612  HOH A O   1 
HETATM 6447 O  O   . HOH O 7 .   ? 14.460  -11.178 7.525   1.00 19.73 ?  613  HOH A O   1 
HETATM 6448 O  O   . HOH O 7 .   ? 27.697  1.116   -24.079 1.00 34.62 ?  614  HOH A O   1 
HETATM 6449 O  O   . HOH O 7 .   ? 29.734  -10.193 24.075  1.00 33.84 ?  615  HOH A O   1 
HETATM 6450 O  O   . HOH O 7 .   ? -3.017  16.986  11.656  1.00 30.06 ?  616  HOH A O   1 
HETATM 6451 O  O   . HOH O 7 .   ? 9.398   9.370   -5.525  1.00 33.72 ?  617  HOH A O   1 
HETATM 6452 O  O   . HOH O 7 .   ? 16.358  25.676  8.376   1.00 29.08 ?  618  HOH A O   1 
HETATM 6453 O  O   . HOH O 7 .   ? 23.266  -3.408  8.865   1.00 18.18 ?  619  HOH A O   1 
HETATM 6454 O  O   . HOH O 7 .   ? -12.128 8.290   14.832  1.00 30.10 ?  620  HOH A O   1 
HETATM 6455 O  O   . HOH O 7 .   ? 11.001  1.021   -3.433  1.00 29.02 ?  621  HOH A O   1 
HETATM 6456 O  O   . HOH O 7 .   ? 10.587  15.582  3.895   1.00 16.48 ?  622  HOH A O   1 
HETATM 6457 O  O   . HOH O 7 .   ? 8.260   25.372  1.576   1.00 35.18 ?  623  HOH A O   1 
HETATM 6458 O  O   . HOH O 7 .   ? 17.997  8.034   3.085   1.00 13.60 ?  624  HOH A O   1 
HETATM 6459 O  O   . HOH O 7 .   ? -0.866  -8.695  23.780  1.00 24.34 ?  625  HOH A O   1 
HETATM 6460 O  O   . HOH O 7 .   ? 11.599  10.892  14.074  1.00 19.29 ?  626  HOH A O   1 
HETATM 6461 O  O   . HOH O 7 .   ? 3.003   -8.164  6.204   1.00 19.70 ?  627  HOH A O   1 
HETATM 6462 O  O   . HOH O 7 .   ? 10.835  -10.562 24.486  1.00 21.32 ?  628  HOH A O   1 
HETATM 6463 O  O   . HOH O 7 .   ? 10.381  13.558  5.886   1.00 18.08 ?  629  HOH A O   1 
HETATM 6464 O  O   . HOH O 7 .   ? 4.264   19.858  10.739  1.00 30.73 ?  630  HOH A O   1 
HETATM 6465 O  O   . HOH O 7 .   ? 16.948  19.322  13.025  1.00 24.08 ?  631  HOH A O   1 
HETATM 6466 O  O   . HOH O 7 .   ? 33.469  20.556  -20.452 1.00 38.53 ?  632  HOH A O   1 
HETATM 6467 O  O   . HOH O 7 .   ? 47.578  4.964   10.337  1.00 22.45 ?  633  HOH A O   1 
HETATM 6468 O  O   . HOH O 7 .   ? 32.623  17.531  -2.211  1.00 19.50 ?  634  HOH A O   1 
HETATM 6469 O  O   . HOH O 7 .   ? 32.670  -0.752  22.565  1.00 18.42 ?  635  HOH A O   1 
HETATM 6470 O  O   . HOH O 7 .   ? 20.520  -16.329 12.990  1.00 28.97 ?  636  HOH A O   1 
HETATM 6471 O  O   . HOH O 7 .   ? -0.357  14.208  27.927  1.00 31.99 ?  637  HOH A O   1 
HETATM 6472 O  O   . HOH O 7 .   ? 22.722  -11.700 27.532  1.00 27.03 ?  638  HOH A O   1 
HETATM 6473 O  O   . HOH O 7 .   ? 7.847   7.282   14.802  1.00 14.31 ?  639  HOH A O   1 
HETATM 6474 O  O   . HOH O 7 .   ? 14.092  -9.464  -4.545  1.00 20.74 ?  640  HOH A O   1 
HETATM 6475 O  O   . HOH O 7 .   ? 16.873  7.947   7.300   1.00 13.20 ?  641  HOH A O   1 
HETATM 6476 O  O   . HOH O 7 .   ? 22.379  -10.039 -5.048  1.00 24.79 ?  642  HOH A O   1 
HETATM 6477 O  O   . HOH O 7 .   ? 37.663  11.646  15.236  1.00 19.69 ?  643  HOH A O   1 
HETATM 6478 O  O   . HOH O 7 .   ? 2.324   17.026  4.544   1.00 29.51 ?  644  HOH A O   1 
HETATM 6479 O  O   . HOH O 7 .   ? 21.600  6.633   19.406  1.00 15.01 ?  645  HOH A O   1 
HETATM 6480 O  O   . HOH O 7 .   ? 4.581   18.430  0.552   1.00 21.39 ?  646  HOH A O   1 
HETATM 6481 O  O   . HOH O 7 .   ? 33.621  16.348  11.284  1.00 20.99 ?  647  HOH A O   1 
HETATM 6482 O  O   . HOH O 7 .   ? 15.275  11.347  -19.071 1.00 35.57 ?  648  HOH A O   1 
HETATM 6483 O  O   . HOH O 7 .   ? 43.008  1.361   -3.385  1.00 30.42 ?  649  HOH A O   1 
HETATM 6484 O  O   . HOH O 7 .   ? 33.390  19.336  -6.204  1.00 32.82 ?  650  HOH A O   1 
HETATM 6485 O  O   . HOH O 7 .   ? 8.177   16.455  -7.377  1.00 14.40 ?  651  HOH A O   1 
HETATM 6486 O  O   . HOH O 7 .   ? 26.580  -1.126  19.306  1.00 17.50 ?  652  HOH A O   1 
HETATM 6487 O  O   . HOH O 7 .   ? 28.381  -8.330  20.520  1.00 15.94 ?  653  HOH A O   1 
HETATM 6488 O  O   . HOH O 7 .   ? 14.603  9.348   20.011  1.00 29.26 ?  654  HOH A O   1 
HETATM 6489 O  O   . HOH O 7 .   ? 35.693  15.873  -21.237 1.00 29.66 ?  655  HOH A O   1 
HETATM 6490 O  O   . HOH O 7 .   ? 29.029  -1.817  17.118  1.00 13.26 ?  656  HOH A O   1 
HETATM 6491 O  O   . HOH O 7 .   ? 9.365   22.607  -1.804  1.00 17.79 ?  657  HOH A O   1 
HETATM 6492 O  O   . HOH O 7 .   ? 15.724  6.093   26.755  1.00 19.55 ?  658  HOH A O   1 
HETATM 6493 O  O   . HOH O 7 .   ? 29.524  -8.492  3.443   1.00 16.56 ?  659  HOH A O   1 
HETATM 6494 O  O   . HOH O 7 .   ? 25.356  18.705  -16.632 1.00 18.97 ?  660  HOH A O   1 
HETATM 6495 O  O   . HOH O 7 .   ? 40.655  -3.888  -2.334  1.00 24.08 ?  661  HOH A O   1 
HETATM 6496 O  O   . HOH O 7 .   ? 10.249  7.055   -4.055  1.00 23.30 ?  662  HOH A O   1 
HETATM 6497 O  O   . HOH O 7 .   ? 7.345   -9.324  24.897  1.00 31.33 ?  663  HOH A O   1 
HETATM 6498 O  O   . HOH O 7 .   ? 26.586  -7.666  5.971   1.00 28.43 ?  664  HOH A O   1 
HETATM 6499 O  O   . HOH O 7 .   ? 28.595  6.838   -20.829 1.00 23.92 ?  665  HOH A O   1 
HETATM 6500 O  O   . HOH O 7 .   ? 40.131  8.296   -1.451  1.00 32.94 ?  666  HOH A O   1 
HETATM 6501 O  O   . HOH O 7 .   ? 30.545  -7.591  32.270  1.00 20.13 ?  667  HOH A O   1 
HETATM 6502 O  O   . HOH O 7 .   ? 32.569  -4.346  -0.905  1.00 14.40 ?  668  HOH A O   1 
HETATM 6503 O  O   . HOH O 7 .   ? 16.446  -9.867  6.049   1.00 22.45 ?  669  HOH A O   1 
HETATM 6504 O  O   . HOH O 7 .   ? 3.256   -3.343  26.188  1.00 27.65 ?  670  HOH A O   1 
HETATM 6505 O  O   . HOH O 7 .   ? 2.082   15.524  29.563  1.00 32.03 ?  671  HOH A O   1 
HETATM 6506 O  O   . HOH O 7 .   ? 27.336  26.946  -9.409  1.00 18.63 ?  672  HOH A O   1 
HETATM 6507 O  O   . HOH O 7 .   ? 33.584  24.395  -2.135  1.00 20.71 ?  673  HOH A O   1 
HETATM 6508 O  O   . HOH O 7 .   ? 33.560  2.994   19.484  1.00 18.11 ?  674  HOH A O   1 
HETATM 6509 O  O   . HOH O 7 .   ? 29.845  26.378  -10.110 1.00 21.53 ?  675  HOH A O   1 
HETATM 6510 O  O   . HOH O 7 .   ? 13.829  -1.777  5.083   1.00 13.98 ?  676  HOH A O   1 
HETATM 6511 O  O   . HOH O 7 .   ? 20.757  1.768   24.678  1.00 15.14 ?  677  HOH A O   1 
HETATM 6512 O  O   . HOH O 7 .   ? 14.786  10.819  21.971  1.00 36.89 ?  678  HOH A O   1 
HETATM 6513 O  O   . HOH O 7 .   ? 28.134  17.268  22.046  1.00 30.47 ?  679  HOH A O   1 
HETATM 6514 O  O   . HOH O 7 .   ? 27.446  -5.151  3.563   1.00 13.81 ?  680  HOH A O   1 
HETATM 6515 O  O   . HOH O 7 .   ? 9.264   17.531  2.035   1.00 13.93 ?  681  HOH A O   1 
HETATM 6516 O  O   . HOH O 7 .   ? 43.673  2.074   13.538  1.00 18.88 ?  682  HOH A O   1 
HETATM 6517 O  O   . HOH O 7 .   ? 15.224  -3.992  5.853   1.00 11.59 ?  683  HOH A O   1 
HETATM 6518 O  O   . HOH O 7 .   ? 20.280  -10.408 -1.004  1.00 21.78 ?  684  HOH A O   1 
HETATM 6519 O  O   . HOH O 7 .   ? 22.466  -8.609  -8.498  1.00 26.29 ?  685  HOH A O   1 
HETATM 6520 O  O   . HOH O 7 .   ? 9.371   11.979  3.563   1.00 20.29 ?  686  HOH A O   1 
HETATM 6521 O  O   . HOH O 7 .   ? 23.026  -7.153  7.861   1.00 17.50 ?  687  HOH A O   1 
HETATM 6522 O  O   . HOH O 7 .   ? 26.673  7.451   -19.112 1.00 22.37 ?  688  HOH A O   1 
HETATM 6523 O  O   . HOH O 7 .   ? 20.703  16.095  -19.270 1.00 22.62 ?  689  HOH A O   1 
HETATM 6524 O  O   . HOH O 7 .   ? 11.886  -5.505  -10.136 1.00 24.33 ?  690  HOH A O   1 
HETATM 6525 O  O   . HOH O 7 .   ? 1.347   -0.987  27.455  1.00 25.43 ?  691  HOH A O   1 
HETATM 6526 O  O   . HOH O 7 .   ? 26.060  -8.670  -5.500  1.00 24.01 ?  692  HOH A O   1 
HETATM 6527 O  O   . HOH O 7 .   ? 26.748  -10.572 21.563  1.00 23.75 ?  693  HOH A O   1 
HETATM 6528 O  O   . HOH O 7 .   ? -1.871  13.088  16.996  1.00 16.88 ?  694  HOH A O   1 
HETATM 6529 O  O   . HOH O 7 .   ? 3.517   7.233   31.773  1.00 33.35 ?  695  HOH A O   1 
HETATM 6530 O  O   . HOH O 7 .   ? 0.793   -14.927 15.094  1.00 29.82 ?  696  HOH A O   1 
HETATM 6531 O  O   . HOH O 7 .   ? 11.235  12.759  -14.863 1.00 33.66 ?  697  HOH A O   1 
HETATM 6532 O  O   . HOH O 7 .   ? 40.817  14.363  3.399   1.00 21.80 ?  698  HOH A O   1 
HETATM 6533 O  O   . HOH O 7 .   ? 12.797  13.894  2.866   1.00 13.98 ?  699  HOH A O   1 
HETATM 6534 O  O   . HOH O 7 .   ? 2.184   0.772   -3.269  1.00 28.16 ?  700  HOH A O   1 
HETATM 6535 O  O   . HOH O 7 .   ? 20.011  -4.243  1.291   1.00 12.08 ?  701  HOH A O   1 
HETATM 6536 O  O   . HOH O 7 .   ? 2.653   11.739  9.253   1.00 12.14 ?  702  HOH A O   1 
HETATM 6537 O  O   . HOH O 7 .   ? 28.198  19.734  10.029  1.00 30.74 ?  703  HOH A O   1 
HETATM 6538 O  O   . HOH O 7 .   ? 12.352  -8.150  0.676   1.00 21.66 ?  704  HOH A O   1 
HETATM 6539 O  O   . HOH O 7 .   ? -9.022  0.172   13.535  1.00 19.82 ?  705  HOH A O   1 
HETATM 6540 O  O   . HOH O 7 .   ? 0.298   -4.385  3.248   1.00 21.53 ?  706  HOH A O   1 
HETATM 6541 O  O   . HOH O 7 .   ? 21.673  8.132   22.785  1.00 21.68 ?  707  HOH A O   1 
HETATM 6542 O  O   . HOH O 7 .   ? 14.183  2.498   32.707  1.00 32.98 ?  708  HOH A O   1 
HETATM 6543 O  O   . HOH O 7 .   ? 27.145  25.162  -16.298 1.00 18.81 ?  709  HOH A O   1 
HETATM 6544 O  O   . HOH O 7 .   ? 40.052  -10.967 3.795   1.00 34.35 ?  710  HOH A O   1 
HETATM 6545 O  O   . HOH O 7 .   ? -9.857  1.637   26.552  1.00 33.02 ?  711  HOH A O   1 
HETATM 6546 O  O   . HOH O 7 .   ? 14.269  5.017   4.651   1.00 13.37 ?  712  HOH A O   1 
HETATM 6547 O  O   . HOH O 7 .   ? 10.839  15.068  -13.711 1.00 19.90 ?  713  HOH A O   1 
HETATM 6548 O  O   . HOH O 7 .   ? 26.037  -6.703  1.160   1.00 14.13 ?  714  HOH A O   1 
HETATM 6549 O  O   . HOH O 7 .   ? 13.905  7.277   13.893  1.00 14.11 ?  715  HOH A O   1 
HETATM 6550 O  O   . HOH O 7 .   ? 15.596  5.114   -16.915 1.00 24.85 ?  716  HOH A O   1 
HETATM 6551 O  O   . HOH O 7 .   ? 18.203  7.268   18.758  1.00 17.69 ?  717  HOH A O   1 
HETATM 6552 O  O   . HOH O 7 .   ? 15.827  -5.833  4.018   1.00 20.48 ?  718  HOH A O   1 
HETATM 6553 O  O   . HOH O 7 .   ? 36.159  -3.413  -3.823  1.00 21.77 ?  719  HOH A O   1 
HETATM 6554 O  O   . HOH O 7 .   ? 18.542  9.915   -20.913 1.00 39.12 ?  720  HOH A O   1 
HETATM 6555 O  O   . HOH O 7 .   ? 19.044  -0.720  28.684  1.00 22.62 ?  721  HOH A O   1 
HETATM 6556 O  O   . HOH O 7 .   ? 20.528  6.760   -3.987  1.00 12.39 ?  722  HOH A O   1 
HETATM 6557 O  O   . HOH O 7 .   ? -5.812  9.147   33.445  1.00 30.29 ?  723  HOH A O   1 
HETATM 6558 O  O   . HOH O 7 .   ? 22.554  19.760  16.344  1.00 29.17 ?  724  HOH A O   1 
HETATM 6559 O  O   . HOH O 7 .   ? 40.979  8.579   -4.239  1.00 29.49 ?  725  HOH A O   1 
HETATM 6560 O  O   . HOH O 7 .   ? 29.939  15.506  24.149  1.00 36.52 ?  726  HOH A O   1 
HETATM 6561 O  O   . HOH O 7 .   ? 19.326  -6.898  9.918   1.00 14.79 ?  727  HOH A O   1 
HETATM 6562 O  O   . HOH O 7 .   ? 10.780  17.544  22.063  1.00 20.79 ?  728  HOH A O   1 
HETATM 6563 O  O   . HOH O 7 .   ? 13.618  1.640   -2.613  1.00 14.19 ?  729  HOH A O   1 
HETATM 6564 O  O   . HOH O 7 .   ? 34.732  13.471  14.835  1.00 24.85 ?  730  HOH A O   1 
HETATM 6565 O  O   . HOH O 7 .   ? 18.982  10.693  22.722  1.00 25.98 ?  731  HOH A O   1 
HETATM 6566 O  O   . HOH O 7 .   ? 38.122  11.374  -7.159  1.00 25.69 ?  732  HOH A O   1 
HETATM 6567 O  O   . HOH O 7 .   ? 8.463   -5.954  -2.619  1.00 26.56 ?  733  HOH A O   1 
HETATM 6568 O  O   . HOH O 7 .   ? 12.160  11.805  16.699  1.00 19.22 ?  734  HOH A O   1 
HETATM 6569 O  O   . HOH O 7 .   ? 14.980  3.307   -4.662  1.00 17.37 ?  735  HOH A O   1 
HETATM 6570 O  O   . HOH O 7 .   ? 41.912  9.171   0.148   1.00 32.80 ?  736  HOH A O   1 
HETATM 6571 O  O   . HOH O 7 .   ? 11.857  -0.135  -15.083 1.00 26.43 ?  737  HOH A O   1 
HETATM 6572 O  O   . HOH O 7 .   ? 27.765  15.563  3.918   1.00 10.07 ?  738  HOH A O   1 
HETATM 6573 O  O   . HOH O 7 .   ? 5.123   1.130   8.370   1.00 11.35 ?  739  HOH A O   1 
HETATM 6574 O  O   . HOH O 7 .   ? 33.855  2.033   26.356  1.00 35.93 ?  740  HOH A O   1 
HETATM 6575 O  O   . HOH O 7 .   ? 31.482  13.190  -25.652 1.00 27.10 ?  741  HOH A O   1 
HETATM 6576 O  O   . HOH O 7 .   ? 33.722  -8.703  19.162  1.00 30.84 ?  742  HOH A O   1 
HETATM 6577 O  O   . HOH O 7 .   ? 2.373   -16.854 16.836  1.00 28.68 ?  743  HOH A O   1 
HETATM 6578 O  O   . HOH O 7 .   ? -2.157  9.351   6.237   1.00 32.67 ?  744  HOH A O   1 
HETATM 6579 O  O   . HOH O 7 .   ? 15.334  13.709  18.496  1.00 24.87 ?  745  HOH A O   1 
HETATM 6580 O  O   . HOH O 7 .   ? 34.254  -3.592  -10.276 1.00 31.70 ?  746  HOH A O   1 
HETATM 6581 O  O   . HOH O 7 .   ? 2.325   2.414   3.244   1.00 12.17 ?  747  HOH A O   1 
HETATM 6582 O  O   . HOH O 7 .   ? 6.600   18.399  2.468   1.00 18.99 ?  748  HOH A O   1 
HETATM 6583 O  O   . HOH O 7 .   ? 11.125  15.727  24.356  1.00 32.31 ?  749  HOH A O   1 
HETATM 6584 O  O   . HOH O 7 .   ? 13.219  9.436   12.727  1.00 20.53 ?  750  HOH A O   1 
HETATM 6585 O  O   . HOH O 7 .   ? 31.063  9.006   -23.646 1.00 22.76 ?  751  HOH A O   1 
HETATM 6586 O  O   . HOH O 7 .   ? 30.194  -6.569  -5.559  1.00 23.14 ?  752  HOH A O   1 
HETATM 6587 O  O   . HOH O 7 .   ? 24.844  -13.480 18.537  1.00 28.00 ?  753  HOH A O   1 
HETATM 6588 O  O   . HOH O 7 .   ? 28.913  -10.464 13.596  1.00 21.49 ?  754  HOH A O   1 
HETATM 6589 O  O   . HOH O 7 .   ? 31.012  -2.881  22.407  1.00 18.02 ?  755  HOH A O   1 
HETATM 6590 O  O   . HOH O 7 .   ? 33.424  18.109  -20.018 1.00 27.69 ?  756  HOH A O   1 
HETATM 6591 O  O   . HOH O 7 .   ? 36.619  12.340  -20.159 1.00 28.09 ?  757  HOH A O   1 
HETATM 6592 O  O   . HOH O 7 .   ? 36.143  15.429  -2.002  1.00 28.81 ?  758  HOH A O   1 
HETATM 6593 O  O   . HOH O 7 .   ? -4.518  -2.984  29.599  1.00 37.24 ?  759  HOH A O   1 
HETATM 6594 O  O   . HOH O 7 .   ? 38.667  -1.888  13.720  1.00 19.40 ?  760  HOH A O   1 
HETATM 6595 O  O   . HOH O 7 .   ? 21.194  26.061  -13.905 1.00 26.68 ?  761  HOH A O   1 
HETATM 6596 O  O   . HOH O 7 .   ? -3.587  -8.589  23.140  1.00 21.18 ?  762  HOH A O   1 
HETATM 6597 O  O   . HOH O 7 .   ? -1.686  -2.816  28.224  1.00 27.68 ?  763  HOH A O   1 
HETATM 6598 O  O   . HOH O 7 .   ? 23.962  -6.049  -11.848 1.00 24.96 ?  764  HOH A O   1 
HETATM 6599 O  O   . HOH O 7 .   ? 25.091  -3.012  32.008  1.00 26.99 ?  765  HOH A O   1 
HETATM 6600 O  O   . HOH O 7 .   ? -3.656  -9.471  20.488  1.00 18.49 ?  766  HOH A O   1 
HETATM 6601 O  O   . HOH O 7 .   ? 22.995  19.586  -16.589 1.00 18.17 ?  767  HOH A O   1 
HETATM 6602 O  O   . HOH O 7 .   ? -4.769  9.525   7.205   1.00 31.65 ?  768  HOH A O   1 
HETATM 6603 O  O   . HOH O 7 .   ? 30.017  4.120   -24.007 1.00 24.76 ?  769  HOH A O   1 
HETATM 6604 O  O   . HOH O 7 .   ? 9.491   -0.332  29.425  1.00 28.86 ?  770  HOH A O   1 
HETATM 6605 O  O   . HOH O 7 .   ? -9.221  5.343   29.635  1.00 31.53 ?  771  HOH A O   1 
HETATM 6606 O  O   . HOH O 7 .   ? 28.449  16.532  6.533   1.00 15.89 ?  772  HOH A O   1 
HETATM 6607 O  O   . HOH O 7 .   ? 9.789   3.674   3.605   1.00 11.32 ?  773  HOH A O   1 
HETATM 6608 O  O   . HOH O 7 .   ? -1.441  11.442  27.966  1.00 20.82 ?  774  HOH A O   1 
HETATM 6609 O  O   . HOH O 7 .   ? 13.541  1.416   -17.792 1.00 28.03 ?  775  HOH A O   1 
HETATM 6610 O  O   . HOH O 7 .   ? 12.439  16.078  -17.217 1.00 28.21 ?  776  HOH A O   1 
HETATM 6611 O  O   . HOH O 7 .   ? 27.261  20.370  -15.545 1.00 15.03 ?  777  HOH A O   1 
HETATM 6612 O  O   . HOH O 7 .   ? 44.409  -0.775  2.242   1.00 18.99 ?  778  HOH A O   1 
HETATM 6613 O  O   . HOH O 7 .   ? 7.074   -4.658  4.508   1.00 10.62 ?  779  HOH A O   1 
HETATM 6614 O  O   . HOH O 7 .   ? 41.404  -1.792  11.298  1.00 19.11 ?  780  HOH A O   1 
HETATM 6615 O  O   . HOH O 7 .   ? 14.659  -7.233  28.455  1.00 20.34 ?  781  HOH A O   1 
HETATM 6616 O  O   . HOH O 7 .   ? 20.703  8.822   1.485   1.00 12.16 ?  782  HOH A O   1 
HETATM 6617 O  O   . HOH O 7 .   ? 17.354  3.446   -3.359  1.00 13.04 ?  783  HOH A O   1 
HETATM 6618 O  O   . HOH O 7 .   ? 8.487   13.731  -7.480  1.00 17.05 ?  784  HOH A O   1 
HETATM 6619 O  O   . HOH O 7 .   ? 9.056   12.791  27.182  1.00 30.57 ?  785  HOH A O   1 
HETATM 6620 O  O   . HOH O 7 .   ? 11.079  -5.934  -19.826 1.00 42.28 ?  786  HOH A O   1 
HETATM 6621 O  O   . HOH O 7 .   ? 38.361  14.016  -9.124  1.00 31.39 ?  787  HOH A O   1 
HETATM 6622 O  O   . HOH O 7 .   ? 15.812  6.800   11.833  1.00 12.89 ?  788  HOH A O   1 
HETATM 6623 O  O   . HOH O 7 .   ? 22.573  -3.505  31.556  1.00 22.58 ?  789  HOH A O   1 
HETATM 6624 O  O   . HOH O 7 .   ? 31.953  1.826   21.471  1.00 16.39 ?  790  HOH A O   1 
HETATM 6625 O  O   . HOH O 7 .   ? 33.151  22.482  1.773   1.00 36.03 ?  791  HOH A O   1 
HETATM 6626 O  O   . HOH O 7 .   ? 8.784   9.752   14.411  1.00 12.68 ?  792  HOH A O   1 
HETATM 6627 O  O   . HOH O 7 .   ? 24.199  -9.597  7.506   1.00 22.21 ?  793  HOH A O   1 
HETATM 6628 O  O   . HOH O 7 .   ? 6.273   -3.614  26.069  1.00 24.18 ?  794  HOH A O   1 
HETATM 6629 O  O   . HOH O 7 .   ? 15.852  -10.998 -7.975  1.00 22.40 ?  795  HOH A O   1 
HETATM 6630 O  O   . HOH O 7 .   ? 30.399  -11.815 2.140   1.00 36.35 ?  796  HOH A O   1 
HETATM 6631 O  O   . HOH O 7 .   ? 31.941  -0.611  25.247  1.00 29.00 ?  797  HOH A O   1 
HETATM 6632 O  O   . HOH O 7 .   ? 28.340  -0.519  -19.637 1.00 31.98 ?  798  HOH A O   1 
HETATM 6633 O  O   . HOH O 7 .   ? 29.163  -4.327  16.168  1.00 12.63 ?  799  HOH A O   1 
HETATM 6634 O  O   . HOH O 7 .   ? 42.312  -4.614  2.325   1.00 24.84 ?  800  HOH A O   1 
HETATM 6635 O  O   . HOH O 7 .   ? 33.476  -13.576 0.415   1.00 39.44 ?  801  HOH A O   1 
HETATM 6636 O  O   . HOH O 7 .   ? 22.305  16.743  -16.991 1.00 19.62 ?  802  HOH A O   1 
HETATM 6637 O  O   . HOH O 7 .   ? 6.592   -4.464  1.807   1.00 17.88 ?  803  HOH A O   1 
HETATM 6638 O  O   . HOH O 7 .   ? 25.046  11.753  -0.872  1.00 10.80 ?  804  HOH A O   1 
HETATM 6639 O  O   . HOH O 7 .   ? 40.821  11.970  10.346  1.00 25.39 ?  805  HOH A O   1 
HETATM 6640 O  O   . HOH O 7 .   ? -0.541  2.759   -1.359  1.00 31.14 ?  806  HOH A O   1 
HETATM 6641 O  O   . HOH O 7 .   ? 20.682  -7.295  6.036   1.00 20.51 ?  807  HOH A O   1 
HETATM 6642 O  O   . HOH O 7 .   ? 15.024  22.486  -4.713  1.00 20.00 ?  808  HOH A O   1 
HETATM 6643 O  O   . HOH O 7 .   ? 21.628  22.618  -5.796  1.00 21.37 ?  809  HOH A O   1 
HETATM 6644 O  O   . HOH O 7 .   ? 21.982  23.174  7.971   1.00 24.60 ?  810  HOH A O   1 
HETATM 6645 O  O   . HOH O 7 .   ? 29.821  23.345  -18.386 1.00 30.42 ?  811  HOH A O   1 
HETATM 6646 O  O   . HOH O 7 .   ? 18.825  -3.811  -1.337  1.00 12.12 ?  812  HOH A O   1 
HETATM 6647 O  O   . HOH O 7 .   ? 16.351  21.576  -17.153 1.00 15.64 ?  813  HOH A O   1 
HETATM 6648 O  O   . HOH O 7 .   ? 15.642  5.487   7.258   1.00 13.89 ?  814  HOH A O   1 
HETATM 6649 O  O   . HOH O 7 .   ? -9.261  2.118   20.512  1.00 22.91 ?  815  HOH A O   1 
HETATM 6650 O  O   . HOH O 7 .   ? 8.502   5.436   -2.967  1.00 22.99 ?  816  HOH A O   1 
HETATM 6651 O  O   . HOH O 7 .   ? 3.957   16.094  3.006   1.00 28.26 ?  817  HOH A O   1 
HETATM 6652 O  O   . HOH O 7 .   ? 11.969  -13.541 10.069  1.00 20.25 ?  818  HOH A O   1 
HETATM 6653 O  O   . HOH O 7 .   ? 14.328  7.103   9.540   1.00 14.58 ?  819  HOH A O   1 
HETATM 6654 O  O   . HOH O 7 .   ? -7.502  -7.162  25.571  1.00 26.03 ?  820  HOH A O   1 
HETATM 6655 O  O   . HOH O 7 .   ? 11.009  -4.663  -2.670  1.00 28.77 ?  821  HOH A O   1 
HETATM 6656 O  O   . HOH O 7 .   ? 37.093  -9.918  5.791   1.00 27.20 ?  822  HOH A O   1 
HETATM 6657 O  O   . HOH O 7 .   ? 27.847  -7.263  -6.704  1.00 20.91 ?  823  HOH A O   1 
HETATM 6658 O  O   . HOH O 7 .   ? 39.143  2.614   18.763  1.00 31.75 ?  824  HOH A O   1 
HETATM 6659 O  O   . HOH O 7 .   ? 14.135  11.225  18.054  1.00 25.84 ?  825  HOH A O   1 
HETATM 6660 O  O   . HOH O 7 .   ? 35.521  -7.523  16.511  1.00 32.16 ?  826  HOH A O   1 
HETATM 6661 O  O   . HOH O 7 .   ? 20.382  -11.684 28.240  1.00 24.85 ?  827  HOH A O   1 
HETATM 6662 O  O   . HOH O 7 .   ? -8.626  4.500   2.373   1.00 22.40 ?  828  HOH A O   1 
HETATM 6663 O  O   . HOH O 7 .   ? 16.357  -1.726  27.943  1.00 17.81 ?  829  HOH A O   1 
HETATM 6664 O  O   . HOH O 7 .   ? 44.605  8.664   15.563  1.00 36.01 ?  830  HOH A O   1 
HETATM 6665 O  O   . HOH O 7 .   ? 34.553  -1.355  26.682  1.00 32.40 ?  831  HOH A O   1 
HETATM 6666 O  O   . HOH O 7 .   ? 16.919  23.307  -6.546  1.00 26.11 ?  832  HOH A O   1 
HETATM 6667 O  O   . HOH O 7 .   ? 10.236  22.206  -11.250 1.00 17.38 ?  833  HOH A O   1 
HETATM 6668 O  O   . HOH O 7 .   ? 33.534  20.379  -3.942  1.00 29.92 ?  834  HOH A O   1 
HETATM 6669 O  O   . HOH O 7 .   ? 35.370  5.074   19.923  1.00 32.42 ?  835  HOH A O   1 
HETATM 6670 O  O   . HOH O 7 .   ? 35.289  -5.654  7.648   1.00 18.42 ?  836  HOH A O   1 
HETATM 6671 O  O   . HOH O 7 .   ? 1.690   18.318  12.449  1.00 30.03 ?  837  HOH A O   1 
HETATM 6672 O  O   . HOH O 7 .   ? 5.143   20.213  28.067  1.00 34.03 ?  838  HOH A O   1 
HETATM 6673 O  O   . HOH O 7 .   ? 17.996  -3.641  6.159   1.00 13.61 ?  839  HOH A O   1 
HETATM 6674 O  O   . HOH O 7 .   ? 35.604  20.535  0.585   1.00 38.05 ?  840  HOH A O   1 
HETATM 6675 O  O   . HOH O 7 .   ? 37.103  3.981   18.828  1.00 32.36 ?  841  HOH A O   1 
HETATM 6676 O  O   . HOH O 7 .   ? 36.249  16.989  -4.165  1.00 33.25 ?  842  HOH A O   1 
HETATM 6677 O  O   . HOH O 7 .   ? 29.057  19.014  7.174   1.00 29.39 ?  843  HOH A O   1 
HETATM 6678 O  O   . HOH O 7 .   ? 6.704   12.662  6.229   1.00 24.71 ?  844  HOH A O   1 
HETATM 6679 O  O   . HOH O 7 .   ? 17.565  -7.536  5.977   1.00 22.41 ?  845  HOH A O   1 
HETATM 6680 O  O   . HOH O 7 .   ? -13.927 14.439  20.718  1.00 39.38 ?  846  HOH A O   1 
HETATM 6681 O  O   . HOH O 7 .   ? -2.395  -11.975 7.045   1.00 33.30 ?  847  HOH A O   1 
HETATM 6682 O  O   . HOH O 7 .   ? 7.234   -6.368  25.821  1.00 32.59 ?  848  HOH A O   1 
HETATM 6683 O  O   . HOH O 7 .   ? 19.176  25.520  -9.548  1.00 38.03 ?  849  HOH A O   1 
HETATM 6684 O  O   . HOH O 7 .   ? 6.874   5.728   34.940  1.00 40.52 ?  850  HOH A O   1 
HETATM 6685 O  O   . HOH O 7 .   ? 35.308  -5.698  -5.175  1.00 30.52 ?  851  HOH A O   1 
HETATM 6686 O  O   . HOH O 7 .   ? 35.974  -9.029  24.159  1.00 36.07 ?  852  HOH A O   1 
HETATM 6687 O  O   . HOH O 7 .   ? 36.449  22.159  -13.155 1.00 21.09 ?  853  HOH A O   1 
HETATM 6688 O  O   . HOH O 7 .   ? -1.775  -11.244 19.985  1.00 37.17 ?  854  HOH A O   1 
HETATM 6689 O  O   . HOH O 7 .   ? 39.762  20.662  -16.138 1.00 26.01 ?  855  HOH A O   1 
HETATM 6690 O  O   . HOH O 7 .   ? 14.160  23.505  13.404  1.00 37.90 ?  856  HOH A O   1 
HETATM 6691 O  O   . HOH O 7 .   ? -4.267  -6.232  27.937  1.00 35.03 ?  857  HOH A O   1 
HETATM 6692 O  O   . HOH O 7 .   ? 13.004  -5.857  27.617  1.00 33.17 ?  858  HOH A O   1 
HETATM 6693 O  O   . HOH O 7 .   ? 15.735  7.568   4.666   1.00 13.44 ?  859  HOH A O   1 
HETATM 6694 O  O   . HOH O 7 .   ? 29.555  19.324  12.640  1.00 34.24 ?  860  HOH A O   1 
HETATM 6695 O  O   . HOH O 7 .   ? 8.964   2.669   -2.801  1.00 27.53 ?  861  HOH A O   1 
HETATM 6696 O  O   . HOH O 7 .   ? 26.870  -8.577  3.104   1.00 20.82 ?  862  HOH A O   1 
HETATM 6697 O  O   . HOH O 7 .   ? 35.017  -13.562 -1.307  1.00 40.48 ?  863  HOH A O   1 
HETATM 6698 O  O   . HOH O 7 .   ? 14.511  -0.512  31.605  1.00 38.80 ?  864  HOH A O   1 
HETATM 6699 O  O   . HOH O 7 .   ? 7.017   7.698   -6.187  1.00 40.24 ?  865  HOH A O   1 
HETATM 6700 O  O   . HOH O 7 .   ? -9.556  2.450   0.952   1.00 20.67 ?  866  HOH A O   1 
HETATM 6701 O  O   . HOH O 7 .   ? 19.895  -9.876  5.748   1.00 27.97 ?  867  HOH A O   1 
HETATM 6702 O  O   . HOH O 7 .   ? 20.530  23.711  -17.145 1.00 28.13 ?  868  HOH A O   1 
HETATM 6703 O  O   . HOH O 7 .   ? 37.712  14.094  16.467  1.00 29.95 ?  869  HOH A O   1 
HETATM 6704 O  O   . HOH O 7 .   ? 18.366  -4.702  3.663   1.00 13.98 ?  870  HOH A O   1 
HETATM 6705 O  O   . HOH O 7 .   ? -1.114  13.110  -2.752  1.00 39.13 ?  871  HOH A O   1 
HETATM 6706 O  O   . HOH O 7 .   ? 26.178  -4.855  -18.201 1.00 38.09 ?  872  HOH A O   1 
HETATM 6707 O  O   . HOH O 7 .   ? 47.125  4.866   13.500  1.00 33.40 ?  873  HOH A O   1 
HETATM 6708 O  O   . HOH O 7 .   ? 7.646   -6.554  0.020   1.00 27.60 ?  874  HOH A O   1 
HETATM 6709 O  O   . HOH O 7 .   ? 10.887  4.870   -6.306  1.00 39.71 ?  875  HOH A O   1 
HETATM 6710 O  O   . HOH O 7 .   ? 4.969   -1.868  -6.137  1.00 42.73 ?  876  HOH A O   1 
HETATM 6711 O  O   . HOH O 7 .   ? 1.594   -14.802 10.872  1.00 40.62 ?  877  HOH A O   1 
HETATM 6712 O  O   . HOH O 7 .   ? 21.162  -11.580 -3.553  1.00 31.64 ?  878  HOH A O   1 
HETATM 6713 O  O   . HOH O 7 .   ? 25.505  21.781  11.189  1.00 32.70 ?  879  HOH A O   1 
HETATM 6714 O  O   . HOH O 7 .   ? -5.091  -2.665  32.681  1.00 37.99 ?  880  HOH A O   1 
HETATM 6715 O  O   . HOH O 7 .   ? 29.902  23.563  4.851   1.00 36.35 ?  881  HOH A O   1 
HETATM 6716 O  O   . HOH O 7 .   ? 12.067  -7.560  -4.408  1.00 32.34 ?  882  HOH A O   1 
HETATM 6717 O  O   . HOH O 7 .   ? 23.166  -18.612 20.590  1.00 41.88 ?  883  HOH A O   1 
HETATM 6718 O  O   . HOH O 7 .   ? 13.158  14.539  24.188  1.00 35.70 ?  884  HOH A O   1 
HETATM 6719 O  O   . HOH O 7 .   ? 27.321  -12.323 5.011   1.00 32.65 ?  885  HOH A O   1 
HETATM 6720 O  O   . HOH O 7 .   ? 0.322   -16.929 19.083  1.00 36.13 ?  886  HOH A O   1 
HETATM 6721 O  O   . HOH O 7 .   ? 6.067   -18.942 15.652  1.00 38.66 ?  887  HOH A O   1 
HETATM 6722 O  O   . HOH O 7 .   ? -6.038  -1.032  35.784  1.00 43.19 ?  888  HOH A O   1 
HETATM 6723 O  O   . HOH O 7 .   ? -0.529  17.354  1.146   1.00 29.78 ?  889  HOH A O   1 
HETATM 6724 O  O   . HOH O 7 .   ? 5.078   1.531   -2.403  1.00 32.57 ?  890  HOH A O   1 
HETATM 6725 O  O   . HOH O 7 .   ? 27.679  22.720  -17.261 1.00 23.95 ?  891  HOH A O   1 
HETATM 6726 O  O   . HOH O 7 .   ? 0.685   8.234   -0.652  1.00 38.97 ?  892  HOH A O   1 
HETATM 6727 O  O   . HOH O 7 .   ? 6.227   5.787   -4.105  1.00 28.66 ?  893  HOH A O   1 
HETATM 6728 O  O   . HOH O 7 .   ? -0.292  17.744  4.005   1.00 33.96 ?  894  HOH A O   1 
HETATM 6729 O  O   . HOH O 7 .   ? 18.453  27.618  7.760   1.00 36.93 ?  895  HOH A O   1 
HETATM 6730 O  O   . HOH O 7 .   ? 10.879  28.523  7.380   1.00 33.72 ?  896  HOH A O   1 
HETATM 6731 O  O   . HOH O 7 .   ? 9.352   9.760   -8.357  1.00 37.96 ?  897  HOH A O   1 
HETATM 6732 O  O   . HOH O 7 .   ? 20.818  26.093  -16.372 1.00 36.07 ?  898  HOH A O   1 
HETATM 6733 O  O   . HOH O 7 .   ? 21.241  -11.929 0.945   1.00 28.71 ?  899  HOH A O   1 
HETATM 6734 O  O   . HOH O 7 .   ? 26.075  -10.995 2.470   1.00 34.33 ?  900  HOH A O   1 
HETATM 6735 O  O   . HOH O 7 .   ? 15.794  8.698   25.455  1.00 37.08 ?  901  HOH A O   1 
HETATM 6736 O  O   . HOH O 7 .   ? -6.970  -10.154 20.117  1.00 41.90 ?  902  HOH A O   1 
HETATM 6737 O  O   . HOH O 7 .   ? 35.076  -0.925  -10.704 1.00 26.86 ?  903  HOH A O   1 
HETATM 6738 O  O   . HOH O 7 .   ? -7.901  13.886  11.873  1.00 38.89 ?  904  HOH A O   1 
HETATM 6739 O  O   . HOH O 7 .   ? -14.802 -0.214  21.579  1.00 39.10 ?  905  HOH A O   1 
HETATM 6740 O  O   . HOH O 7 .   ? 18.734  28.021  3.482   1.00 41.50 ?  906  HOH A O   1 
HETATM 6741 O  O   . HOH O 7 .   ? -6.346  15.691  9.638   1.00 40.28 ?  907  HOH A O   1 
HETATM 6742 O  O   . HOH O 7 .   ? 31.495  -10.935 10.606  1.00 37.80 ?  908  HOH A O   1 
HETATM 6743 O  O   . HOH O 7 .   ? 20.594  27.199  8.194   1.00 32.02 ?  909  HOH A O   1 
HETATM 6744 O  O   . HOH P 7 .   ? 13.898  20.271  -56.421 1.00 33.88 ?  801  HOH B O   1 
HETATM 6745 O  O   . HOH P 7 .   ? 31.748  6.353   -28.006 1.00 28.80 ?  802  HOH B O   1 
HETATM 6746 O  O   . HOH P 7 .   ? 35.271  -1.851  -39.529 1.00 24.65 ?  803  HOH B O   1 
HETATM 6747 O  O   . HOH P 7 .   ? 27.722  18.765  -56.885 1.00 27.02 ?  804  HOH B O   1 
HETATM 6748 O  O   . HOH P 7 .   ? 18.501  19.565  -26.320 1.00 32.07 ?  805  HOH B O   1 
HETATM 6749 O  O   . HOH P 7 .   ? 21.396  15.841  -43.928 1.00 26.34 ?  806  HOH B O   1 
HETATM 6750 O  O   . HOH P 7 .   ? 17.163  10.270  -29.118 1.00 33.89 ?  807  HOH B O   1 
HETATM 6751 O  O   . HOH P 7 .   ? 34.746  17.098  -55.836 1.00 23.43 ?  808  HOH B O   1 
HETATM 6752 O  O   . HOH P 7 .   ? 20.595  22.332  -54.124 1.00 27.27 ?  809  HOH B O   1 
HETATM 6753 O  O   . HOH P 7 .   ? 28.831  20.099  -55.172 1.00 30.40 ?  810  HOH B O   1 
HETATM 6754 O  O   . HOH P 7 .   ? 4.449   -10.813 -69.667 1.00 37.88 ?  811  HOH B O   1 
HETATM 6755 O  O   . HOH P 7 .   ? 32.997  -1.012  -50.807 1.00 19.89 ?  812  HOH B O   1 
HETATM 6756 O  O   . HOH P 7 .   ? 29.263  -6.782  -41.794 1.00 25.27 ?  813  HOH B O   1 
HETATM 6757 O  O   . HOH P 7 .   ? 59.350  9.430   -30.787 1.00 35.54 ?  814  HOH B O   1 
HETATM 6758 O  O   . HOH P 7 .   ? 32.190  -3.133  -52.558 1.00 22.33 ?  815  HOH B O   1 
HETATM 6759 O  O   . HOH P 7 .   ? 9.239   16.378  -50.288 1.00 22.39 ?  816  HOH B O   1 
HETATM 6760 O  O   . HOH P 7 .   ? 53.814  12.328  -49.454 1.00 24.63 ?  817  HOH B O   1 
HETATM 6761 O  O   . HOH P 7 .   ? 40.035  -7.146  -47.814 1.00 30.54 ?  818  HOH B O   1 
HETATM 6762 O  O   . HOH P 7 .   ? 5.210   -3.830  -46.150 1.00 35.05 ?  819  HOH B O   1 
HETATM 6763 O  O   . HOH P 7 .   ? 29.992  1.506   -32.007 1.00 29.93 ?  820  HOH B O   1 
HETATM 6764 O  O   . HOH P 7 .   ? 33.026  0.633   -53.151 1.00 21.46 ?  821  HOH B O   1 
HETATM 6765 O  O   . HOH P 7 .   ? 29.099  23.775  -47.745 1.00 21.19 ?  822  HOH B O   1 
HETATM 6766 O  O   . HOH P 7 .   ? 34.246  6.526   -29.209 1.00 22.87 ?  823  HOH B O   1 
HETATM 6767 O  O   . HOH P 7 .   ? 17.671  -7.424  -41.193 1.00 32.96 ?  824  HOH B O   1 
HETATM 6768 O  O   . HOH P 7 .   ? 27.144  4.333   -47.284 1.00 15.53 ?  825  HOH B O   1 
HETATM 6769 O  O   . HOH P 7 .   ? 25.402  -0.276  -69.965 1.00 32.73 ?  826  HOH B O   1 
HETATM 6770 O  O   . HOH P 7 .   ? 29.988  3.021   -61.804 1.00 29.47 ?  827  HOH B O   1 
HETATM 6771 O  O   . HOH P 7 .   ? 22.620  21.966  -18.453 1.00 25.00 ?  828  HOH B O   1 
HETATM 6772 O  O   . HOH P 7 .   ? 21.492  13.234  -32.905 1.00 19.84 ?  829  HOH B O   1 
HETATM 6773 O  O   . HOH P 7 .   ? 19.173  11.540  -25.186 1.00 33.81 ?  830  HOH B O   1 
HETATM 6774 O  O   . HOH P 7 .   ? 24.806  4.269   -50.796 1.00 15.82 ?  831  HOH B O   1 
HETATM 6775 O  O   . HOH P 7 .   ? 39.658  20.691  -52.841 1.00 26.52 ?  832  HOH B O   1 
HETATM 6776 O  O   . HOH P 7 .   ? 6.712   -3.952  -48.468 1.00 38.21 ?  833  HOH B O   1 
HETATM 6777 O  O   . HOH P 7 .   ? 33.229  3.248   -35.919 1.00 28.96 ?  834  HOH B O   1 
HETATM 6778 O  O   . HOH P 7 .   ? 60.540  4.813   -45.986 1.00 35.11 ?  835  HOH B O   1 
HETATM 6779 O  O   . HOH P 7 .   ? 32.074  5.200   -41.906 1.00 13.31 ?  836  HOH B O   1 
HETATM 6780 O  O   . HOH P 7 .   ? 20.042  5.253   -56.802 1.00 14.40 ?  837  HOH B O   1 
HETATM 6781 O  O   . HOH P 7 .   ? 19.515  6.508   -36.943 1.00 24.54 ?  838  HOH B O   1 
HETATM 6782 O  O   . HOH P 7 .   ? 17.345  22.016  -57.074 1.00 26.84 ?  839  HOH B O   1 
HETATM 6783 O  O   . HOH P 7 .   ? 37.051  -5.760  -57.793 1.00 27.54 ?  840  HOH B O   1 
HETATM 6784 O  O   . HOH P 7 .   ? 12.054  21.826  -25.508 1.00 31.90 ?  841  HOH B O   1 
HETATM 6785 O  O   . HOH P 7 .   ? 32.429  -1.275  -37.434 1.00 29.89 ?  842  HOH B O   1 
HETATM 6786 O  O   . HOH P 7 .   ? 11.059  9.062   -28.653 1.00 39.33 ?  843  HOH B O   1 
HETATM 6787 O  O   . HOH P 7 .   ? 24.769  -5.792  -74.032 1.00 32.55 ?  844  HOH B O   1 
HETATM 6788 O  O   . HOH P 7 .   ? 41.553  17.122  -56.316 1.00 24.94 ?  845  HOH B O   1 
HETATM 6789 O  O   . HOH P 7 .   ? 12.710  -4.339  -38.049 1.00 30.79 ?  846  HOH B O   1 
HETATM 6790 O  O   . HOH P 7 .   ? 21.887  16.491  -52.101 1.00 19.61 ?  847  HOH B O   1 
HETATM 6791 O  O   . HOH P 7 .   ? 26.466  5.722   -34.372 1.00 18.71 ?  848  HOH B O   1 
HETATM 6792 O  O   . HOH P 7 .   ? 38.124  5.246   -43.036 1.00 18.52 ?  849  HOH B O   1 
HETATM 6793 O  O   . HOH P 7 .   ? 28.891  10.659  -29.673 1.00 17.50 ?  850  HOH B O   1 
HETATM 6794 O  O   . HOH P 7 .   ? 29.631  5.315   -60.266 1.00 26.46 ?  851  HOH B O   1 
HETATM 6795 O  O   . HOH P 7 .   ? 15.526  17.045  -47.465 1.00 17.43 ?  852  HOH B O   1 
HETATM 6796 O  O   . HOH P 7 .   ? 9.562   -5.979  -51.367 1.00 26.76 ?  853  HOH B O   1 
HETATM 6797 O  O   . HOH P 7 .   ? 29.136  14.151  -50.431 1.00 14.93 ?  854  HOH B O   1 
HETATM 6798 O  O   . HOH P 7 .   ? 25.369  22.575  -23.486 1.00 22.31 ?  855  HOH B O   1 
HETATM 6799 O  O   . HOH P 7 .   ? 28.234  6.972   -47.651 1.00 14.34 ?  856  HOH B O   1 
HETATM 6800 O  O   . HOH P 7 .   ? 14.154  -7.872  -67.922 1.00 20.36 ?  857  HOH B O   1 
HETATM 6801 O  O   . HOH P 7 .   ? 31.850  -10.200 -58.344 1.00 21.43 ?  858  HOH B O   1 
HETATM 6802 O  O   . HOH P 7 .   ? 29.812  -1.661  -52.923 1.00 15.67 ?  859  HOH B O   1 
HETATM 6803 O  O   . HOH P 7 .   ? 11.855  -6.896  -67.248 1.00 23.88 ?  860  HOH B O   1 
HETATM 6804 O  O   . HOH P 7 .   ? 30.430  24.387  -25.659 1.00 28.28 ?  861  HOH B O   1 
HETATM 6805 O  O   . HOH P 7 .   ? 25.050  8.935   -59.117 1.00 22.74 ?  862  HOH B O   1 
HETATM 6806 O  O   . HOH P 7 .   ? 35.893  24.105  -51.609 1.00 31.59 ?  863  HOH B O   1 
HETATM 6807 O  O   . HOH P 7 .   ? 34.063  1.704   -42.592 1.00 21.43 ?  864  HOH B O   1 
HETATM 6808 O  O   . HOH P 7 .   ? 36.330  4.838   -54.322 1.00 28.77 ?  865  HOH B O   1 
HETATM 6809 O  O   . HOH P 7 .   ? 22.636  16.206  -21.220 1.00 23.59 ?  866  HOH B O   1 
HETATM 6810 O  O   . HOH P 7 .   ? 9.884   0.510   -32.910 1.00 35.39 ?  867  HOH B O   1 
HETATM 6811 O  O   . HOH P 7 .   ? 31.067  -3.719  -63.940 1.00 19.04 ?  868  HOH B O   1 
HETATM 6812 O  O   . HOH P 7 .   ? 4.952   14.776  -51.582 1.00 30.35 ?  869  HOH B O   1 
HETATM 6813 O  O   . HOH P 7 .   ? 33.822  -5.476  -69.674 1.00 27.85 ?  870  HOH B O   1 
HETATM 6814 O  O   . HOH P 7 .   ? 22.892  -10.827 -45.143 1.00 30.73 ?  871  HOH B O   1 
HETATM 6815 O  O   . HOH P 7 .   ? 46.777  11.004  -27.525 1.00 26.49 ?  872  HOH B O   1 
HETATM 6816 O  O   . HOH P 7 .   ? 20.123  7.199   -70.602 1.00 28.40 ?  873  HOH B O   1 
HETATM 6817 O  O   . HOH P 7 .   ? 14.905  8.900   -30.418 1.00 33.12 ?  874  HOH B O   1 
HETATM 6818 O  O   . HOH P 7 .   ? 56.899  3.300   -29.943 1.00 25.29 ?  875  HOH B O   1 
HETATM 6819 O  O   . HOH P 7 .   ? 27.939  16.406  -49.223 1.00 17.47 ?  876  HOH B O   1 
HETATM 6820 O  O   . HOH P 7 .   ? 42.637  5.645   -54.464 1.00 29.28 ?  877  HOH B O   1 
HETATM 6821 O  O   . HOH P 7 .   ? 41.241  0.863   -49.906 1.00 14.05 ?  878  HOH B O   1 
HETATM 6822 O  O   . HOH P 7 .   ? 58.621  11.406  -37.364 1.00 23.94 ?  879  HOH B O   1 
HETATM 6823 O  O   . HOH P 7 .   ? 49.550  12.639  -33.046 1.00 17.33 ?  880  HOH B O   1 
HETATM 6824 O  O   . HOH P 7 .   ? 25.234  28.781  -40.373 1.00 33.27 ?  881  HOH B O   1 
HETATM 6825 O  O   . HOH P 7 .   ? 37.621  11.769  -61.890 1.00 28.07 ?  882  HOH B O   1 
HETATM 6826 O  O   . HOH P 7 .   ? 48.835  21.635  -37.488 1.00 23.04 ?  883  HOH B O   1 
HETATM 6827 O  O   . HOH P 7 .   ? 38.490  11.585  -49.983 1.00 11.92 ?  884  HOH B O   1 
HETATM 6828 O  O   . HOH P 7 .   ? 25.309  19.081  -44.105 1.00 18.54 ?  885  HOH B O   1 
HETATM 6829 O  O   . HOH P 7 .   ? 29.543  5.099   -35.968 1.00 20.90 ?  886  HOH B O   1 
HETATM 6830 O  O   . HOH P 7 .   ? 18.493  14.306  -34.302 1.00 24.53 ?  887  HOH B O   1 
HETATM 6831 O  O   . HOH P 7 .   ? 11.258  18.716  -56.908 1.00 30.18 ?  888  HOH B O   1 
HETATM 6832 O  O   . HOH P 7 .   ? 35.620  20.086  -27.695 1.00 32.69 ?  889  HOH B O   1 
HETATM 6833 O  O   . HOH P 7 .   ? 15.961  18.759  -50.215 1.00 21.74 ?  890  HOH B O   1 
HETATM 6834 O  O   . HOH P 7 .   ? 15.906  -3.543  -47.026 1.00 16.60 ?  891  HOH B O   1 
HETATM 6835 O  O   . HOH P 7 .   ? 27.792  24.464  -25.731 1.00 30.35 ?  892  HOH B O   1 
HETATM 6836 O  O   . HOH P 7 .   ? 26.014  25.728  -46.680 1.00 35.61 ?  893  HOH B O   1 
HETATM 6837 O  O   . HOH P 7 .   ? 24.303  6.395   -69.370 1.00 37.05 ?  894  HOH B O   1 
HETATM 6838 O  O   . HOH P 7 .   ? 28.553  7.241   -50.652 1.00 14.12 ?  895  HOH B O   1 
HETATM 6839 O  O   . HOH P 7 .   ? 29.009  11.079  -59.347 1.00 31.75 ?  896  HOH B O   1 
HETATM 6840 O  O   . HOH P 7 .   ? 27.613  4.320   -31.215 1.00 19.20 ?  897  HOH B O   1 
HETATM 6841 O  O   . HOH P 7 .   ? 26.515  -2.396  -69.099 1.00 21.89 ?  898  HOH B O   1 
HETATM 6842 O  O   . HOH P 7 .   ? 46.378  15.908  -33.425 1.00 23.41 ?  899  HOH B O   1 
HETATM 6843 O  O   . HOH P 7 .   ? 56.034  10.893  -42.908 1.00 22.77 ?  900  HOH B O   1 
HETATM 6844 O  O   . HOH P 7 .   ? 0.096   -4.731  -68.215 1.00 33.33 ?  901  HOH B O   1 
HETATM 6845 O  O   . HOH P 7 .   ? 35.472  -6.126  -55.227 1.00 20.24 ?  902  HOH B O   1 
HETATM 6846 O  O   . HOH P 7 .   ? 47.981  -0.397  -44.107 1.00 13.32 ?  903  HOH B O   1 
HETATM 6847 O  O   . HOH P 7 .   ? 18.630  22.718  -20.459 1.00 36.95 ?  904  HOH B O   1 
HETATM 6848 O  O   . HOH P 7 .   ? 44.369  27.587  -45.106 1.00 34.68 ?  905  HOH B O   1 
HETATM 6849 O  O   . HOH P 7 .   ? 16.977  19.912  -45.710 1.00 33.43 ?  906  HOH B O   1 
HETATM 6850 O  O   . HOH P 7 .   ? 31.938  6.894   -59.527 1.00 23.25 ?  907  HOH B O   1 
HETATM 6851 O  O   . HOH P 7 .   ? 10.520  -8.439  -65.434 1.00 23.29 ?  908  HOH B O   1 
HETATM 6852 O  O   . HOH P 7 .   ? 21.224  -5.251  -29.687 1.00 32.34 ?  909  HOH B O   1 
HETATM 6853 O  O   . HOH P 7 .   ? 18.008  16.701  -35.174 1.00 26.30 ?  910  HOH B O   1 
HETATM 6854 O  O   . HOH P 7 .   ? 22.055  22.572  -30.274 1.00 33.29 ?  911  HOH B O   1 
HETATM 6855 O  O   . HOH P 7 .   ? 42.661  -6.556  -52.122 1.00 30.98 ?  912  HOH B O   1 
HETATM 6856 O  O   . HOH P 7 .   ? 39.545  10.191  -55.817 1.00 15.90 ?  913  HOH B O   1 
HETATM 6857 O  O   . HOH P 7 .   ? 26.686  18.309  -50.663 1.00 29.91 ?  914  HOH B O   1 
HETATM 6858 O  O   . HOH P 7 .   ? 33.111  -5.015  -54.723 1.00 18.85 ?  915  HOH B O   1 
HETATM 6859 O  O   . HOH P 7 .   ? 51.337  21.271  -38.726 1.00 22.01 ?  916  HOH B O   1 
HETATM 6860 O  O   . HOH P 7 .   ? 34.715  0.550   -39.963 1.00 19.76 ?  917  HOH B O   1 
HETATM 6861 O  O   . HOH P 7 .   ? 21.919  10.715  -72.169 1.00 35.92 ?  918  HOH B O   1 
HETATM 6862 O  O   . HOH P 7 .   ? 26.901  10.760  -57.788 1.00 21.80 ?  919  HOH B O   1 
HETATM 6863 O  O   . HOH P 7 .   ? 21.056  19.421  -44.802 1.00 27.99 ?  920  HOH B O   1 
HETATM 6864 O  O   . HOH P 7 .   ? 16.020  -4.385  -44.329 1.00 20.23 ?  921  HOH B O   1 
HETATM 6865 O  O   . HOH P 7 .   ? 5.649   -0.394  -36.622 1.00 34.18 ?  922  HOH B O   1 
HETATM 6866 O  O   . HOH P 7 .   ? 3.990   -2.080  -51.350 1.00 37.98 ?  923  HOH B O   1 
HETATM 6867 O  O   . HOH P 7 .   ? 22.727  19.334  -47.406 1.00 22.23 ?  924  HOH B O   1 
HETATM 6868 O  O   . HOH P 7 .   ? 37.726  23.220  -32.770 1.00 23.04 ?  925  HOH B O   1 
HETATM 6869 O  O   . HOH P 7 .   ? 32.347  3.029   -43.226 1.00 22.71 ?  926  HOH B O   1 
HETATM 6870 O  O   . HOH P 7 .   ? 50.260  -2.112  -33.882 1.00 26.19 ?  927  HOH B O   1 
HETATM 6871 O  O   . HOH P 7 .   ? 42.574  16.499  -33.263 1.00 23.65 ?  928  HOH B O   1 
HETATM 6872 O  O   . HOH P 7 .   ? 35.158  17.123  -53.056 1.00 16.47 ?  929  HOH B O   1 
HETATM 6873 O  O   . HOH P 7 .   ? 30.505  -1.093  -63.881 1.00 19.85 ?  930  HOH B O   1 
HETATM 6874 O  O   . HOH P 7 .   ? 47.627  -4.483  -49.820 1.00 33.36 ?  931  HOH B O   1 
HETATM 6875 O  O   . HOH P 7 .   ? 19.038  -10.312 -58.433 1.00 28.74 ?  932  HOH B O   1 
HETATM 6876 O  O   . HOH P 7 .   ? 33.337  1.386   -37.799 1.00 32.37 ?  933  HOH B O   1 
HETATM 6877 O  O   . HOH P 7 .   ? 21.631  3.285   -51.434 1.00 18.00 ?  934  HOH B O   1 
HETATM 6878 O  O   . HOH P 7 .   ? 47.872  5.567   -28.080 1.00 27.81 ?  935  HOH B O   1 
HETATM 6879 O  O   . HOH P 7 .   ? 20.308  -9.159  -70.618 1.00 21.60 ?  936  HOH B O   1 
HETATM 6880 O  O   . HOH P 7 .   ? 17.331  22.661  -37.733 1.00 27.14 ?  937  HOH B O   1 
HETATM 6881 O  O   . HOH P 7 .   ? 9.649   18.427  -55.113 1.00 30.80 ?  938  HOH B O   1 
HETATM 6882 O  O   . HOH P 7 .   ? 20.167  20.700  -31.272 1.00 30.41 ?  939  HOH B O   1 
HETATM 6883 O  O   . HOH P 7 .   ? 49.744  8.211   -59.887 1.00 23.02 ?  940  HOH B O   1 
HETATM 6884 O  O   . HOH P 7 .   ? 38.689  -2.886  -55.665 1.00 27.20 ?  941  HOH B O   1 
HETATM 6885 O  O   . HOH P 7 .   ? 22.725  23.095  -62.194 1.00 29.52 ?  942  HOH B O   1 
HETATM 6886 O  O   . HOH P 7 .   ? -1.196  11.728  -43.105 1.00 30.21 ?  943  HOH B O   1 
HETATM 6887 O  O   . HOH P 7 .   ? 25.139  -10.162 -59.274 1.00 24.41 ?  944  HOH B O   1 
HETATM 6888 O  O   . HOH P 7 .   ? 29.604  5.636   -43.272 1.00 11.80 ?  945  HOH B O   1 
HETATM 6889 O  O   . HOH P 7 .   ? 22.961  8.764   -57.271 1.00 18.83 ?  946  HOH B O   1 
HETATM 6890 O  O   . HOH P 7 .   ? 37.040  2.704   -43.104 1.00 14.30 ?  947  HOH B O   1 
HETATM 6891 O  O   . HOH P 7 .   ? 18.654  16.249  -29.630 1.00 21.60 ?  948  HOH B O   1 
HETATM 6892 O  O   . HOH P 7 .   ? 19.908  21.759  -44.682 1.00 29.92 ?  949  HOH B O   1 
HETATM 6893 O  O   . HOH P 7 .   ? 40.786  30.100  -36.911 1.00 36.57 ?  950  HOH B O   1 
HETATM 6894 O  O   . HOH P 7 .   ? 32.602  8.713   -53.104 1.00 13.56 ?  951  HOH B O   1 
HETATM 6895 O  O   . HOH P 7 .   ? 25.367  15.673  -47.983 1.00 16.79 ?  952  HOH B O   1 
HETATM 6896 O  O   . HOH P 7 .   ? 34.178  14.120  -27.991 1.00 23.71 ?  953  HOH B O   1 
HETATM 6897 O  O   . HOH P 7 .   ? 50.583  22.168  -41.189 1.00 19.83 ?  954  HOH B O   1 
HETATM 6898 O  O   . HOH P 7 .   ? 26.744  22.358  -48.584 1.00 23.13 ?  955  HOH B O   1 
HETATM 6899 O  O   . HOH P 7 .   ? 16.867  0.296   -52.429 1.00 14.94 ?  956  HOH B O   1 
HETATM 6900 O  O   . HOH P 7 .   ? 31.769  25.931  -46.200 1.00 24.27 ?  957  HOH B O   1 
HETATM 6901 O  O   . HOH P 7 .   ? 22.158  15.827  -54.842 1.00 17.62 ?  958  HOH B O   1 
HETATM 6902 O  O   . HOH P 7 .   ? 12.482  7.918   -29.931 1.00 40.01 ?  959  HOH B O   1 
HETATM 6903 O  O   . HOH P 7 .   ? 55.708  20.007  -37.625 1.00 35.01 ?  960  HOH B O   1 
HETATM 6904 O  O   . HOH P 7 .   ? 43.803  -5.420  -47.627 1.00 33.07 ?  961  HOH B O   1 
HETATM 6905 O  O   . HOH P 7 .   ? 30.138  5.296   -45.954 1.00 17.10 ?  962  HOH B O   1 
HETATM 6906 O  O   . HOH P 7 .   ? 34.815  2.966   -54.755 1.00 27.72 ?  963  HOH B O   1 
HETATM 6907 O  O   . HOH P 7 .   ? 43.640  29.447  -43.015 1.00 26.49 ?  964  HOH B O   1 
HETATM 6908 O  O   . HOH P 7 .   ? 6.830   21.833  -42.393 1.00 36.62 ?  965  HOH B O   1 
HETATM 6909 O  O   . HOH P 7 .   ? 40.656  9.672   -60.599 1.00 35.40 ?  966  HOH B O   1 
HETATM 6910 O  O   . HOH P 7 .   ? 41.794  18.957  -32.653 1.00 30.52 ?  967  HOH B O   1 
HETATM 6911 O  O   . HOH P 7 .   ? 9.281   17.428  -40.856 1.00 26.18 ?  968  HOH B O   1 
HETATM 6912 O  O   . HOH P 7 .   ? 53.896  13.022  -52.070 1.00 26.06 ?  969  HOH B O   1 
HETATM 6913 O  O   . HOH P 7 .   ? 0.502   11.337  -54.163 1.00 29.01 ?  970  HOH B O   1 
HETATM 6914 O  O   . HOH P 7 .   ? 47.912  -3.071  -30.282 1.00 31.96 ?  971  HOH B O   1 
HETATM 6915 O  O   . HOH P 7 .   ? 48.305  23.991  -40.670 1.00 31.67 ?  972  HOH B O   1 
HETATM 6916 O  O   . HOH P 7 .   ? 20.166  -12.918 -70.978 1.00 33.61 ?  973  HOH B O   1 
HETATM 6917 O  O   . HOH P 7 .   ? 53.491  2.381   -29.339 1.00 33.84 ?  974  HOH B O   1 
HETATM 6918 O  O   . HOH P 7 .   ? 25.568  19.719  -48.397 1.00 26.59 ?  975  HOH B O   1 
HETATM 6919 O  O   . HOH P 7 .   ? 40.727  8.460   -57.414 1.00 36.79 ?  976  HOH B O   1 
HETATM 6920 O  O   . HOH P 7 .   ? 27.261  4.910   -50.131 1.00 15.90 ?  977  HOH B O   1 
HETATM 6921 O  O   . HOH P 7 .   ? 59.280  9.277   -36.760 1.00 33.58 ?  978  HOH B O   1 
HETATM 6922 O  O   . HOH P 7 .   ? 31.277  10.005  -59.308 1.00 25.87 ?  979  HOH B O   1 
HETATM 6923 O  O   . HOH P 7 .   ? 61.401  8.112   -32.530 1.00 40.28 ?  980  HOH B O   1 
HETATM 6924 O  O   . HOH P 7 .   ? 42.484  11.159  -27.737 1.00 32.95 ?  981  HOH B O   1 
HETATM 6925 O  O   . HOH P 7 .   ? 37.555  17.168  -28.139 1.00 41.12 ?  982  HOH B O   1 
HETATM 6926 O  O   . HOH P 7 .   ? 15.944  20.898  -48.301 1.00 30.55 ?  983  HOH B O   1 
HETATM 6927 O  O   . HOH P 7 .   ? 39.046  -12.791 -54.185 1.00 36.62 ?  984  HOH B O   1 
HETATM 6928 O  O   . HOH P 7 .   ? 19.937  23.179  -46.658 1.00 34.33 ?  985  HOH B O   1 
HETATM 6929 O  O   . HOH P 7 .   ? 50.089  10.131  -61.732 1.00 21.86 ?  986  HOH B O   1 
HETATM 6930 O  O   . HOH P 7 .   ? 24.177  16.893  -50.341 1.00 17.64 ?  987  HOH B O   1 
HETATM 6931 O  O   . HOH P 7 .   ? 15.685  24.346  -46.078 1.00 37.26 ?  988  HOH B O   1 
HETATM 6932 O  O   . HOH P 7 .   ? 23.092  -0.726  -24.837 1.00 38.41 ?  989  HOH B O   1 
HETATM 6933 O  O   . HOH P 7 .   ? 2.119   -1.584  -47.254 1.00 39.07 ?  990  HOH B O   1 
HETATM 6934 O  O   . HOH P 7 .   ? 21.588  25.548  -20.763 1.00 39.34 ?  991  HOH B O   1 
HETATM 6935 O  O   . HOH P 7 .   ? 26.873  22.838  -21.486 1.00 30.05 ?  992  HOH B O   1 
HETATM 6936 O  O   . HOH P 7 .   ? 57.864  10.119  -41.459 1.00 38.71 ?  993  HOH B O   1 
HETATM 6937 O  O   . HOH P 7 .   ? 35.033  10.993  -60.002 1.00 35.32 ?  994  HOH B O   1 
HETATM 6938 O  O   . HOH P 7 .   ? 28.506  7.720   -62.122 1.00 34.09 ?  995  HOH B O   1 
HETATM 6939 O  O   . HOH P 7 .   ? 18.307  23.391  -17.894 1.00 26.34 ?  996  HOH B O   1 
HETATM 6940 O  O   . HOH P 7 .   ? 18.425  -11.363 -70.768 1.00 38.28 ?  997  HOH B O   1 
HETATM 6941 O  O   . HOH P 7 .   ? 27.849  20.070  -59.965 1.00 35.85 ?  998  HOH B O   1 
HETATM 6942 O  O   . HOH P 7 .   ? 29.653  23.714  -21.362 1.00 30.89 ?  999  HOH B O   1 
HETATM 6943 O  O   . HOH P 7 .   ? 18.784  25.344  -37.279 1.00 39.15 ?  1000 HOH B O   1 
HETATM 6944 O  O   . HOH P 7 .   ? 9.764   -10.563 -67.203 1.00 28.73 ?  1001 HOH B O   1 
HETATM 6945 O  O   . HOH P 7 .   ? 33.681  -12.905 -55.674 1.00 34.54 ?  1002 HOH B O   1 
HETATM 6946 O  O   . HOH P 7 .   ? 33.757  3.850   -30.666 1.00 33.13 ?  1003 HOH B O   1 
HETATM 6947 O  O   . HOH P 7 .   ? -0.258  12.682  -36.266 1.00 42.46 ?  1004 HOH B O   1 
HETATM 6948 O  O   . HOH P 7 .   ? 41.174  -4.868  -30.890 1.00 33.93 ?  1005 HOH B O   1 
HETATM 6949 O  O   . HOH P 7 .   ? 12.463  23.188  -39.516 1.00 41.59 ?  1006 HOH B O   1 
HETATM 6950 O  O   . HOH P 7 .   ? -2.146  13.383  -39.321 1.00 41.24 ?  1007 HOH B O   1 
# 
