data_9EIF
# 
_entry.id   9EIF 
# 
_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   9EIF         pdb_00009eif 10.2210/pdb9eif/pdb 
WWPDB D_1000290542 ?            ?                   
# 
_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                        9EIF 
_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 '3-methanethioyl-1-(5-O-phosphono-beta-D-ribofuranosyl)-5-(sulfanylcarbonyl)pyridin-1-ium' 396.353   2   ? ? ? ? 
3 non-polymer syn 'TRIETHYLENE GLYCOL'                                                                       150.173   1   ? ? ? ? 
4 non-polymer syn 'DI(HYDROXYETHYL)ETHER'                                                                    106.120   2   ? ? ? ? 
5 non-polymer syn DEAMINOHYDROXYVALINE                                                                       118.131   2   ? ? ? ? 
6 non-polymer syn 'NICKEL (II) ION'                                                                          58.693    2   ? ? ? ? 
7 water       nat water                                                                                      18.015    635 ? ? ? ? 
# 
_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 '3-methanethioyl-1-(5-O-phosphono-beta-D-ribofuranosyl)-5-(sulfanylcarbonyl)pyridin-1-ium' 4EY 
3 'TRIETHYLENE GLYCOL'                                                                       PGE 
4 'DI(HYDROXYETHYL)ETHER'                                                                    PEG 
5 DEAMINOHYDROXYVALINE                                                                       VAD 
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 
GLN 'L-peptide linking' y GLUTAMINE                                                                                  ? 
'C5 H10 N2 O3'        146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                                                                            ? 
'C5 H9 N O4'          147.129 
GLY 'peptide linking'   y GLYCINE                                                                                    ? 
'C2 H5 N O2'          75.067  
HIS 'L-peptide linking' y HISTIDINE                                                                                  ? 
'C6 H10 N3 O2 1'      156.162 
HOH non-polymer         . WATER                                                                                      ? 'H2 O' 
18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                                                                 ? 
'C6 H13 N O2'         131.173 
LEU 'L-peptide linking' y LEUCINE                                                                                    ? 
'C6 H13 N O2'         131.173 
LYS 'L-peptide linking' y LYSINE                                                                                     ? 
'C6 H15 N2 O2 1'      147.195 
MET 'L-peptide linking' y METHIONINE                                                                                 ? 
'C5 H11 N O2 S'       149.211 
NI  non-polymer         . 'NICKEL (II) ION'                                                                          ? 'Ni 2' 
58.693  
PEG non-polymer         . 'DI(HYDROXYETHYL)ETHER'                                                                    ? 'C4 H10 O3' 
106.120 
PGE non-polymer         . 'TRIETHYLENE GLYCOL'                                                                       ? 'C6 H14 O4' 
150.173 
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 
VAD 'L-peptide linking' n DEAMINOHYDROXYVALINE                                                                       ? 'C5 H10 O3' 
118.131 
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 VAD ? ? VAD ? ? '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 4EY 1   501 501 4EY 4EY A . 
D 3 PGE 1   502 502 PGE PGE A . 
E 4 PEG 1   503 504 PEG PEG A . 
F 5 VAD 1   504 505 VAD LIG A . 
G 4 PEG 1   505 506 PEG PEG A . 
H 6 NI  1   506 1   NI  NI  A . 
I 2 4EY 1   501 501 4EY 4EY B . 
J 5 VAD 1   502 502 VAD LIG B . 
K 6 NI  1   503 2   NI  NI  B . 
L 7 HOH 1   601 653 HOH HOH A . 
L 7 HOH 2   602 597 HOH HOH A . 
L 7 HOH 3   603 249 HOH HOH A . 
L 7 HOH 4   604 234 HOH HOH A . 
L 7 HOH 5   605 230 HOH HOH A . 
L 7 HOH 6   606 681 HOH HOH A . 
L 7 HOH 7   607 626 HOH HOH A . 
L 7 HOH 8   608 541 HOH HOH A . 
L 7 HOH 9   609 459 HOH HOH A . 
L 7 HOH 10  610 243 HOH HOH A . 
L 7 HOH 11  611 480 HOH HOH A . 
L 7 HOH 12  612 690 HOH HOH A . 
L 7 HOH 13  613 328 HOH HOH A . 
L 7 HOH 14  614 270 HOH HOH A . 
L 7 HOH 15  615 432 HOH HOH A . 
L 7 HOH 16  616 163 HOH HOH A . 
L 7 HOH 17  617 700 HOH HOH A . 
L 7 HOH 18  618 27  HOH HOH A . 
L 7 HOH 19  619 107 HOH HOH A . 
L 7 HOH 20  620 169 HOH HOH A . 
L 7 HOH 21  621 686 HOH HOH A . 
L 7 HOH 22  622 32  HOH HOH A . 
L 7 HOH 23  623 381 HOH HOH A . 
L 7 HOH 24  624 80  HOH HOH A . 
L 7 HOH 25  625 90  HOH HOH A . 
L 7 HOH 26  626 165 HOH HOH A . 
L 7 HOH 27  627 474 HOH HOH A . 
L 7 HOH 28  628 72  HOH HOH A . 
L 7 HOH 29  629 463 HOH HOH A . 
L 7 HOH 30  630 500 HOH HOH A . 
L 7 HOH 31  631 215 HOH HOH A . 
L 7 HOH 32  632 427 HOH HOH A . 
L 7 HOH 33  633 100 HOH HOH A . 
L 7 HOH 34  634 278 HOH HOH A . 
L 7 HOH 35  635 112 HOH HOH A . 
L 7 HOH 36  636 186 HOH HOH A . 
L 7 HOH 37  637 82  HOH HOH A . 
L 7 HOH 38  638 470 HOH HOH A . 
L 7 HOH 39  639 263 HOH HOH A . 
L 7 HOH 40  640 116 HOH HOH A . 
L 7 HOH 41  641 205 HOH HOH A . 
L 7 HOH 42  642 324 HOH HOH A . 
L 7 HOH 43  643 126 HOH HOH A . 
L 7 HOH 44  644 86  HOH HOH A . 
L 7 HOH 45  645 88  HOH HOH A . 
L 7 HOH 46  646 53  HOH HOH A . 
L 7 HOH 47  647 461 HOH HOH A . 
L 7 HOH 48  648 410 HOH HOH A . 
L 7 HOH 49  649 174 HOH HOH A . 
L 7 HOH 50  650 632 HOH HOH A . 
L 7 HOH 51  651 64  HOH HOH A . 
L 7 HOH 52  652 251 HOH HOH A . 
L 7 HOH 53  653 359 HOH HOH A . 
L 7 HOH 54  654 111 HOH HOH A . 
L 7 HOH 55  655 418 HOH HOH A . 
L 7 HOH 56  656 433 HOH HOH A . 
L 7 HOH 57  657 141 HOH HOH A . 
L 7 HOH 58  658 363 HOH HOH A . 
L 7 HOH 59  659 422 HOH HOH A . 
L 7 HOH 60  660 120 HOH HOH A . 
L 7 HOH 61  661 71  HOH HOH A . 
L 7 HOH 62  662 188 HOH HOH A . 
L 7 HOH 63  663 633 HOH HOH A . 
L 7 HOH 64  664 18  HOH HOH A . 
L 7 HOH 65  665 507 HOH HOH A . 
L 7 HOH 66  666 77  HOH HOH A . 
L 7 HOH 67  667 684 HOH HOH A . 
L 7 HOH 68  668 412 HOH HOH A . 
L 7 HOH 69  669 193 HOH HOH A . 
L 7 HOH 70  670 124 HOH HOH A . 
L 7 HOH 71  671 530 HOH HOH A . 
L 7 HOH 72  672 144 HOH HOH A . 
L 7 HOH 73  673 92  HOH HOH A . 
L 7 HOH 74  674 58  HOH HOH A . 
L 7 HOH 75  675 473 HOH HOH A . 
L 7 HOH 76  676 51  HOH HOH A . 
L 7 HOH 77  677 170 HOH HOH A . 
L 7 HOH 78  678 146 HOH HOH A . 
L 7 HOH 79  679 308 HOH HOH A . 
L 7 HOH 80  680 321 HOH HOH A . 
L 7 HOH 81  681 518 HOH HOH A . 
L 7 HOH 82  682 305 HOH HOH A . 
L 7 HOH 83  683 139 HOH HOH A . 
L 7 HOH 84  684 453 HOH HOH A . 
L 7 HOH 85  685 464 HOH HOH A . 
L 7 HOH 86  686 21  HOH HOH A . 
L 7 HOH 87  687 357 HOH HOH A . 
L 7 HOH 88  688 19  HOH HOH A . 
L 7 HOH 89  689 52  HOH HOH A . 
L 7 HOH 90  690 421 HOH HOH A . 
L 7 HOH 91  691 11  HOH HOH A . 
L 7 HOH 92  692 108 HOH HOH A . 
L 7 HOH 93  693 160 HOH HOH A . 
L 7 HOH 94  694 268 HOH HOH A . 
L 7 HOH 95  695 526 HOH HOH A . 
L 7 HOH 96  696 420 HOH HOH A . 
L 7 HOH 97  697 438 HOH HOH A . 
L 7 HOH 98  698 8   HOH HOH A . 
L 7 HOH 99  699 158 HOH HOH A . 
L 7 HOH 100 700 175 HOH HOH A . 
L 7 HOH 101 701 619 HOH HOH A . 
L 7 HOH 102 702 477 HOH HOH A . 
L 7 HOH 103 703 103 HOH HOH A . 
L 7 HOH 104 704 417 HOH HOH A . 
L 7 HOH 105 705 358 HOH HOH A . 
L 7 HOH 106 706 537 HOH HOH A . 
L 7 HOH 107 707 437 HOH HOH A . 
L 7 HOH 108 708 171 HOH HOH A . 
L 7 HOH 109 709 39  HOH HOH A . 
L 7 HOH 110 710 451 HOH HOH A . 
L 7 HOH 111 711 523 HOH HOH A . 
L 7 HOH 112 712 502 HOH HOH A . 
L 7 HOH 113 713 362 HOH HOH A . 
L 7 HOH 114 714 307 HOH HOH A . 
L 7 HOH 115 715 442 HOH HOH A . 
L 7 HOH 116 716 398 HOH HOH A . 
L 7 HOH 117 717 178 HOH HOH A . 
L 7 HOH 118 718 62  HOH HOH A . 
L 7 HOH 119 719 493 HOH HOH A . 
L 7 HOH 120 720 164 HOH HOH A . 
L 7 HOH 121 721 130 HOH HOH A . 
L 7 HOH 122 722 75  HOH HOH A . 
L 7 HOH 123 723 404 HOH HOH A . 
L 7 HOH 124 724 330 HOH HOH A . 
L 7 HOH 125 725 1   HOH HOH A . 
L 7 HOH 126 726 532 HOH HOH A . 
L 7 HOH 127 727 271 HOH HOH A . 
L 7 HOH 128 728 468 HOH HOH A . 
L 7 HOH 129 729 413 HOH HOH A . 
L 7 HOH 130 730 172 HOH HOH A . 
L 7 HOH 131 731 456 HOH HOH A . 
L 7 HOH 132 732 612 HOH HOH A . 
L 7 HOH 133 733 311 HOH HOH A . 
L 7 HOH 134 734 67  HOH HOH A . 
L 7 HOH 135 735 221 HOH HOH A . 
L 7 HOH 136 736 661 HOH HOH A . 
L 7 HOH 137 737 42  HOH HOH A . 
L 7 HOH 138 738 6   HOH HOH A . 
L 7 HOH 139 739 344 HOH HOH A . 
L 7 HOH 140 740 296 HOH HOH A . 
L 7 HOH 141 741 416 HOH HOH A . 
L 7 HOH 142 742 83  HOH HOH A . 
L 7 HOH 143 743 499 HOH HOH A . 
L 7 HOH 144 744 467 HOH HOH A . 
L 7 HOH 145 745 13  HOH HOH A . 
L 7 HOH 146 746 59  HOH HOH A . 
L 7 HOH 147 747 143 HOH HOH A . 
L 7 HOH 148 748 15  HOH HOH A . 
L 7 HOH 149 749 295 HOH HOH A . 
L 7 HOH 150 750 29  HOH HOH A . 
L 7 HOH 151 751 628 HOH HOH A . 
L 7 HOH 152 752 200 HOH HOH A . 
L 7 HOH 153 753 10  HOH HOH A . 
L 7 HOH 154 754 20  HOH HOH A . 
L 7 HOH 155 755 409 HOH HOH A . 
L 7 HOH 156 756 449 HOH HOH A . 
L 7 HOH 157 757 654 HOH HOH A . 
L 7 HOH 158 758 302 HOH HOH A . 
L 7 HOH 159 759 524 HOH HOH A . 
L 7 HOH 160 760 101 HOH HOH A . 
L 7 HOH 161 761 543 HOH HOH A . 
L 7 HOH 162 762 99  HOH HOH A . 
L 7 HOH 163 763 598 HOH HOH A . 
L 7 HOH 164 764 494 HOH HOH A . 
L 7 HOH 165 765 220 HOH HOH A . 
L 7 HOH 166 766 192 HOH HOH A . 
L 7 HOH 167 767 128 HOH HOH A . 
L 7 HOH 168 768 431 HOH HOH A . 
L 7 HOH 169 769 94  HOH HOH A . 
L 7 HOH 170 770 540 HOH HOH A . 
L 7 HOH 171 771 46  HOH HOH A . 
L 7 HOH 172 772 439 HOH HOH A . 
L 7 HOH 173 773 426 HOH HOH A . 
L 7 HOH 174 774 333 HOH HOH A . 
L 7 HOH 175 775 341 HOH HOH A . 
L 7 HOH 176 776 348 HOH HOH A . 
L 7 HOH 177 777 389 HOH HOH A . 
L 7 HOH 178 778 109 HOH HOH A . 
L 7 HOH 179 779 258 HOH HOH A . 
L 7 HOH 180 780 411 HOH HOH A . 
L 7 HOH 181 781 452 HOH HOH A . 
L 7 HOH 182 782 594 HOH HOH A . 
L 7 HOH 183 783 519 HOH HOH A . 
L 7 HOH 184 784 674 HOH HOH A . 
L 7 HOH 185 785 388 HOH HOH A . 
L 7 HOH 186 786 98  HOH HOH A . 
L 7 HOH 187 787 23  HOH HOH A . 
L 7 HOH 188 788 347 HOH HOH A . 
L 7 HOH 189 789 207 HOH HOH A . 
L 7 HOH 190 790 350 HOH HOH A . 
L 7 HOH 191 791 458 HOH HOH A . 
L 7 HOH 192 792 197 HOH HOH A . 
L 7 HOH 193 793 408 HOH HOH A . 
L 7 HOH 194 794 415 HOH HOH A . 
L 7 HOH 195 795 436 HOH HOH A . 
L 7 HOH 196 796 525 HOH HOH A . 
L 7 HOH 197 797 508 HOH HOH A . 
L 7 HOH 198 798 689 HOH HOH A . 
L 7 HOH 199 799 512 HOH HOH A . 
L 7 HOH 200 800 81  HOH HOH A . 
L 7 HOH 201 801 206 HOH HOH A . 
L 7 HOH 202 802 187 HOH HOH A . 
L 7 HOH 203 803 423 HOH HOH A . 
L 7 HOH 204 804 535 HOH HOH A . 
L 7 HOH 205 805 290 HOH HOH A . 
L 7 HOH 206 806 393 HOH HOH A . 
L 7 HOH 207 807 3   HOH HOH A . 
L 7 HOH 208 808 45  HOH HOH A . 
L 7 HOH 209 809 462 HOH HOH A . 
L 7 HOH 210 810 644 HOH HOH A . 
L 7 HOH 211 811 345 HOH HOH A . 
L 7 HOH 212 812 465 HOH HOH A . 
L 7 HOH 213 813 466 HOH HOH A . 
L 7 HOH 214 814 24  HOH HOH A . 
L 7 HOH 215 815 96  HOH HOH A . 
L 7 HOH 216 816 310 HOH HOH A . 
L 7 HOH 217 817 283 HOH HOH A . 
L 7 HOH 218 818 446 HOH HOH A . 
L 7 HOH 219 819 516 HOH HOH A . 
L 7 HOH 220 820 179 HOH HOH A . 
L 7 HOH 221 821 297 HOH HOH A . 
L 7 HOH 222 822 511 HOH HOH A . 
L 7 HOH 223 823 31  HOH HOH A . 
L 7 HOH 224 824 611 HOH HOH A . 
L 7 HOH 225 825 699 HOH HOH A . 
L 7 HOH 226 826 697 HOH HOH A . 
L 7 HOH 227 827 273 HOH HOH A . 
L 7 HOH 228 828 41  HOH HOH A . 
L 7 HOH 229 829 38  HOH HOH A . 
L 7 HOH 230 830 651 HOH HOH A . 
L 7 HOH 231 831 469 HOH HOH A . 
L 7 HOH 232 832 114 HOH HOH A . 
L 7 HOH 233 833 48  HOH HOH A . 
L 7 HOH 234 834 595 HOH HOH A . 
L 7 HOH 235 835 434 HOH HOH A . 
L 7 HOH 236 836 630 HOH HOH A . 
L 7 HOH 237 837 517 HOH HOH A . 
L 7 HOH 238 838 151 HOH HOH A . 
L 7 HOH 239 839 5   HOH HOH A . 
L 7 HOH 240 840 216 HOH HOH A . 
L 7 HOH 241 841 435 HOH HOH A . 
L 7 HOH 242 842 414 HOH HOH A . 
L 7 HOH 243 843 232 HOH HOH A . 
L 7 HOH 244 844 17  HOH HOH A . 
L 7 HOH 245 845 349 HOH HOH A . 
L 7 HOH 246 846 375 HOH HOH A . 
L 7 HOH 247 847 180 HOH HOH A . 
L 7 HOH 248 848 118 HOH HOH A . 
L 7 HOH 249 849 122 HOH HOH A . 
L 7 HOH 250 850 454 HOH HOH A . 
L 7 HOH 251 851 444 HOH HOH A . 
L 7 HOH 252 852 521 HOH HOH A . 
L 7 HOH 253 853 475 HOH HOH A . 
L 7 HOH 254 854 264 HOH HOH A . 
L 7 HOH 255 855 2   HOH HOH A . 
L 7 HOH 256 856 316 HOH HOH A . 
L 7 HOH 257 857 616 HOH HOH A . 
L 7 HOH 258 858 340 HOH HOH A . 
L 7 HOH 259 859 14  HOH HOH A . 
L 7 HOH 260 860 514 HOH HOH A . 
L 7 HOH 261 861 219 HOH HOH A . 
L 7 HOH 262 862 505 HOH HOH A . 
L 7 HOH 263 863 455 HOH HOH A . 
L 7 HOH 264 864 430 HOH HOH A . 
L 7 HOH 265 865 337 HOH HOH A . 
L 7 HOH 266 866 503 HOH HOH A . 
L 7 HOH 267 867 506 HOH HOH A . 
L 7 HOH 268 868 4   HOH HOH A . 
L 7 HOH 269 869 529 HOH HOH A . 
L 7 HOH 270 870 50  HOH HOH A . 
L 7 HOH 271 871 190 HOH HOH A . 
L 7 HOH 272 872 161 HOH HOH A . 
L 7 HOH 273 873 336 HOH HOH A . 
L 7 HOH 274 874 544 HOH HOH A . 
L 7 HOH 275 875 687 HOH HOH A . 
L 7 HOH 276 876 531 HOH HOH A . 
L 7 HOH 277 877 620 HOH HOH A . 
L 7 HOH 278 878 460 HOH HOH A . 
L 7 HOH 279 879 97  HOH HOH A . 
L 7 HOH 280 880 663 HOH HOH A . 
L 7 HOH 281 881 441 HOH HOH A . 
L 7 HOH 282 882 445 HOH HOH A . 
L 7 HOH 283 883 244 HOH HOH A . 
L 7 HOH 284 884 640 HOH HOH A . 
L 7 HOH 285 885 662 HOH HOH A . 
L 7 HOH 286 886 615 HOH HOH A . 
L 7 HOH 287 887 457 HOH HOH A . 
L 7 HOH 288 888 443 HOH HOH A . 
L 7 HOH 289 889 339 HOH HOH A . 
L 7 HOH 290 890 520 HOH HOH A . 
L 7 HOH 291 891 657 HOH HOH A . 
L 7 HOH 292 892 384 HOH HOH A . 
L 7 HOH 293 893 256 HOH HOH A . 
L 7 HOH 294 894 385 HOH HOH A . 
L 7 HOH 295 895 515 HOH HOH A . 
L 7 HOH 296 896 646 HOH HOH A . 
L 7 HOH 297 897 424 HOH HOH A . 
L 7 HOH 298 898 658 HOH HOH A . 
L 7 HOH 299 899 536 HOH HOH A . 
L 7 HOH 300 900 472 HOH HOH A . 
L 7 HOH 301 901 253 HOH HOH A . 
L 7 HOH 302 902 246 HOH HOH A . 
L 7 HOH 303 903 656 HOH HOH A . 
L 7 HOH 304 904 501 HOH HOH A . 
L 7 HOH 305 905 406 HOH HOH A . 
L 7 HOH 306 906 584 HOH HOH A . 
L 7 HOH 307 907 241 HOH HOH A . 
L 7 HOH 308 908 471 HOH HOH A . 
L 7 HOH 309 909 605 HOH HOH A . 
L 7 HOH 310 910 618 HOH HOH A . 
L 7 HOH 311 911 156 HOH HOH A . 
L 7 HOH 312 912 621 HOH HOH A . 
L 7 HOH 313 913 655 HOH HOH A . 
L 7 HOH 314 914 450 HOH HOH A . 
L 7 HOH 315 915 322 HOH HOH A . 
L 7 HOH 316 916 642 HOH HOH A . 
L 7 HOH 317 917 534 HOH HOH A . 
L 7 HOH 318 918 698 HOH HOH A . 
L 7 HOH 319 919 245 HOH HOH A . 
L 7 HOH 320 920 604 HOH HOH A . 
L 7 HOH 321 921 610 HOH HOH A . 
L 7 HOH 322 922 428 HOH HOH A . 
L 7 HOH 323 923 419 HOH HOH A . 
L 7 HOH 324 924 36  HOH HOH A . 
L 7 HOH 325 925 688 HOH HOH A . 
L 7 HOH 326 926 198 HOH HOH A . 
L 7 HOH 327 927 539 HOH HOH A . 
L 7 HOH 328 928 504 HOH HOH A . 
L 7 HOH 329 929 583 HOH HOH A . 
L 7 HOH 330 930 440 HOH HOH A . 
L 7 HOH 331 931 89  HOH HOH A . 
L 7 HOH 332 932 641 HOH HOH A . 
L 7 HOH 333 933 285 HOH HOH A . 
L 7 HOH 334 934 407 HOH HOH A . 
L 7 HOH 335 935 335 HOH HOH A . 
L 7 HOH 336 936 448 HOH HOH A . 
L 7 HOH 337 937 289 HOH HOH A . 
L 7 HOH 338 938 631 HOH HOH A . 
L 7 HOH 339 939 261 HOH HOH A . 
L 7 HOH 340 940 528 HOH HOH A . 
L 7 HOH 341 941 643 HOH HOH A . 
L 7 HOH 342 942 527 HOH HOH A . 
L 7 HOH 343 943 496 HOH HOH A . 
L 7 HOH 344 944 425 HOH HOH A . 
L 7 HOH 345 945 394 HOH HOH A . 
L 7 HOH 346 946 613 HOH HOH A . 
L 7 HOH 347 947 495 HOH HOH A . 
L 7 HOH 348 948 513 HOH HOH A . 
L 7 HOH 349 949 590 HOH HOH A . 
L 7 HOH 350 950 538 HOH HOH A . 
L 7 HOH 351 951 228 HOH HOH A . 
L 7 HOH 352 952 627 HOH HOH A . 
L 7 HOH 353 953 237 HOH HOH A . 
L 7 HOH 354 954 429 HOH HOH A . 
L 7 HOH 355 955 664 HOH HOH A . 
L 7 HOH 356 956 478 HOH HOH A . 
L 7 HOH 357 957 629 HOH HOH A . 
L 7 HOH 358 958 522 HOH HOH A . 
L 7 HOH 359 959 390 HOH HOH A . 
L 7 HOH 360 960 399 HOH HOH A . 
L 7 HOH 361 961 660 HOH HOH A . 
L 7 HOH 362 962 659 HOH HOH A . 
L 7 HOH 363 963 617 HOH HOH A . 
L 7 HOH 364 964 614 HOH HOH A . 
M 7 HOH 1   601 293 HOH HOH B . 
M 7 HOH 2   602 592 HOH HOH B . 
M 7 HOH 3   603 491 HOH HOH B . 
M 7 HOH 4   604 483 HOH HOH B . 
M 7 HOH 5   605 572 HOH HOH B . 
M 7 HOH 6   606 303 HOH HOH B . 
M 7 HOH 7   607 488 HOH HOH B . 
M 7 HOH 8   608 132 HOH HOH B . 
M 7 HOH 9   609 696 HOH HOH B . 
M 7 HOH 10  610 329 HOH HOH B . 
M 7 HOH 11  611 227 HOH HOH B . 
M 7 HOH 12  612 218 HOH HOH B . 
M 7 HOH 13  613 498 HOH HOH B . 
M 7 HOH 14  614 47  HOH HOH B . 
M 7 HOH 15  615 562 HOH HOH B . 
M 7 HOH 16  616 287 HOH HOH B . 
M 7 HOH 17  617 476 HOH HOH B . 
M 7 HOH 18  618 551 HOH HOH B . 
M 7 HOH 19  619 555 HOH HOH B . 
M 7 HOH 20  620 226 HOH HOH B . 
M 7 HOH 21  621 202 HOH HOH B . 
M 7 HOH 22  622 487 HOH HOH B . 
M 7 HOH 23  623 559 HOH HOH B . 
M 7 HOH 24  624 275 HOH HOH B . 
M 7 HOH 25  625 274 HOH HOH B . 
M 7 HOH 26  626 95  HOH HOH B . 
M 7 HOH 27  627 93  HOH HOH B . 
M 7 HOH 28  628 685 HOH HOH B . 
M 7 HOH 29  629 191 HOH HOH B . 
M 7 HOH 30  630 318 HOH HOH B . 
M 7 HOH 31  631 573 HOH HOH B . 
M 7 HOH 32  632 569 HOH HOH B . 
M 7 HOH 33  633 49  HOH HOH B . 
M 7 HOH 34  634 694 HOH HOH B . 
M 7 HOH 35  635 332 HOH HOH B . 
M 7 HOH 36  636 372 HOH HOH B . 
M 7 HOH 37  637 315 HOH HOH B . 
M 7 HOH 38  638 203 HOH HOH B . 
M 7 HOH 39  639 231 HOH HOH B . 
M 7 HOH 40  640 282 HOH HOH B . 
M 7 HOH 41  641 252 HOH HOH B . 
M 7 HOH 42  642 692 HOH HOH B . 
M 7 HOH 43  643 338 HOH HOH B . 
M 7 HOH 44  644 57  HOH HOH B . 
M 7 HOH 45  645 568 HOH HOH B . 
M 7 HOH 46  646 301 HOH HOH B . 
M 7 HOH 47  647 76  HOH HOH B . 
M 7 HOH 48  648 142 HOH HOH B . 
M 7 HOH 49  649 153 HOH HOH B . 
M 7 HOH 50  650 106 HOH HOH B . 
M 7 HOH 51  651 37  HOH HOH B . 
M 7 HOH 52  652 259 HOH HOH B . 
M 7 HOH 53  653 257 HOH HOH B . 
M 7 HOH 54  654 173 HOH HOH B . 
M 7 HOH 55  655 196 HOH HOH B . 
M 7 HOH 56  656 195 HOH HOH B . 
M 7 HOH 57  657 309 HOH HOH B . 
M 7 HOH 58  658 266 HOH HOH B . 
M 7 HOH 59  659 222 HOH HOH B . 
M 7 HOH 60  660 135 HOH HOH B . 
M 7 HOH 61  661 267 HOH HOH B . 
M 7 HOH 62  662 79  HOH HOH B . 
M 7 HOH 63  663 117 HOH HOH B . 
M 7 HOH 64  664 300 HOH HOH B . 
M 7 HOH 65  665 152 HOH HOH B . 
M 7 HOH 66  666 61  HOH HOH B . 
M 7 HOH 67  667 366 HOH HOH B . 
M 7 HOH 68  668 286 HOH HOH B . 
M 7 HOH 69  669 184 HOH HOH B . 
M 7 HOH 70  670 182 HOH HOH B . 
M 7 HOH 71  671 34  HOH HOH B . 
M 7 HOH 72  672 185 HOH HOH B . 
M 7 HOH 73  673 26  HOH HOH B . 
M 7 HOH 74  674 102 HOH HOH B . 
M 7 HOH 75  675 550 HOH HOH B . 
M 7 HOH 76  676 7   HOH HOH B . 
M 7 HOH 77  677 666 HOH HOH B . 
M 7 HOH 78  678 360 HOH HOH B . 
M 7 HOH 79  679 370 HOH HOH B . 
M 7 HOH 80  680 121 HOH HOH B . 
M 7 HOH 81  681 85  HOH HOH B . 
M 7 HOH 82  682 70  HOH HOH B . 
M 7 HOH 83  683 73  HOH HOH B . 
M 7 HOH 84  684 55  HOH HOH B . 
M 7 HOH 85  685 331 HOH HOH B . 
M 7 HOH 86  686 623 HOH HOH B . 
M 7 HOH 87  687 490 HOH HOH B . 
M 7 HOH 88  688 254 HOH HOH B . 
M 7 HOH 89  689 131 HOH HOH B . 
M 7 HOH 90  690 110 HOH HOH B . 
M 7 HOH 91  691 625 HOH HOH B . 
M 7 HOH 92  692 166 HOH HOH B . 
M 7 HOH 93  693 28  HOH HOH B . 
M 7 HOH 94  694 486 HOH HOH B . 
M 7 HOH 95  695 248 HOH HOH B . 
M 7 HOH 96  696 30  HOH HOH B . 
M 7 HOH 97  697 149 HOH HOH B . 
M 7 HOH 98  698 68  HOH HOH B . 
M 7 HOH 99  699 65  HOH HOH B . 
M 7 HOH 100 700 317 HOH HOH B . 
M 7 HOH 101 701 217 HOH HOH B . 
M 7 HOH 102 702 74  HOH HOH B . 
M 7 HOH 103 703 140 HOH HOH B . 
M 7 HOH 104 704 262 HOH HOH B . 
M 7 HOH 105 705 125 HOH HOH B . 
M 7 HOH 106 706 580 HOH HOH B . 
M 7 HOH 107 707 223 HOH HOH B . 
M 7 HOH 108 708 606 HOH HOH B . 
M 7 HOH 109 709 78  HOH HOH B . 
M 7 HOH 110 710 492 HOH HOH B . 
M 7 HOH 111 711 298 HOH HOH B . 
M 7 HOH 112 712 181 HOH HOH B . 
M 7 HOH 113 713 591 HOH HOH B . 
M 7 HOH 114 714 155 HOH HOH B . 
M 7 HOH 115 715 693 HOH HOH B . 
M 7 HOH 116 716 9   HOH HOH B . 
M 7 HOH 117 717 147 HOH HOH B . 
M 7 HOH 118 718 589 HOH HOH B . 
M 7 HOH 119 719 136 HOH HOH B . 
M 7 HOH 120 720 485 HOH HOH B . 
M 7 HOH 121 721 134 HOH HOH B . 
M 7 HOH 122 722 326 HOH HOH B . 
M 7 HOH 123 723 150 HOH HOH B . 
M 7 HOH 124 724 22  HOH HOH B . 
M 7 HOH 125 725 104 HOH HOH B . 
M 7 HOH 126 726 157 HOH HOH B . 
M 7 HOH 127 727 56  HOH HOH B . 
M 7 HOH 128 728 236 HOH HOH B . 
M 7 HOH 129 729 129 HOH HOH B . 
M 7 HOH 130 730 637 HOH HOH B . 
M 7 HOH 131 731 291 HOH HOH B . 
M 7 HOH 132 732 240 HOH HOH B . 
M 7 HOH 133 733 680 HOH HOH B . 
M 7 HOH 134 734 199 HOH HOH B . 
M 7 HOH 135 735 566 HOH HOH B . 
M 7 HOH 136 736 16  HOH HOH B . 
M 7 HOH 137 737 189 HOH HOH B . 
M 7 HOH 138 738 601 HOH HOH B . 
M 7 HOH 139 739 213 HOH HOH B . 
M 7 HOH 140 740 233 HOH HOH B . 
M 7 HOH 141 741 138 HOH HOH B . 
M 7 HOH 142 742 276 HOH HOH B . 
M 7 HOH 143 743 159 HOH HOH B . 
M 7 HOH 144 744 35  HOH HOH B . 
M 7 HOH 145 745 119 HOH HOH B . 
M 7 HOH 146 746 279 HOH HOH B . 
M 7 HOH 147 747 127 HOH HOH B . 
M 7 HOH 148 748 208 HOH HOH B . 
M 7 HOH 149 749 84  HOH HOH B . 
M 7 HOH 150 750 167 HOH HOH B . 
M 7 HOH 151 751 280 HOH HOH B . 
M 7 HOH 152 752 702 HOH HOH B . 
M 7 HOH 153 753 224 HOH HOH B . 
M 7 HOH 154 754 255 HOH HOH B . 
M 7 HOH 155 755 183 HOH HOH B . 
M 7 HOH 156 756 176 HOH HOH B . 
M 7 HOH 157 757 133 HOH HOH B . 
M 7 HOH 158 758 43  HOH HOH B . 
M 7 HOH 159 759 162 HOH HOH B . 
M 7 HOH 160 760 66  HOH HOH B . 
M 7 HOH 161 761 546 HOH HOH B . 
M 7 HOH 162 762 703 HOH HOH B . 
M 7 HOH 163 763 60  HOH HOH B . 
M 7 HOH 164 764 63  HOH HOH B . 
M 7 HOH 165 765 145 HOH HOH B . 
M 7 HOH 166 766 214 HOH HOH B . 
M 7 HOH 167 767 647 HOH HOH B . 
M 7 HOH 168 768 353 HOH HOH B . 
M 7 HOH 169 769 599 HOH HOH B . 
M 7 HOH 170 770 87  HOH HOH B . 
M 7 HOH 171 771 586 HOH HOH B . 
M 7 HOH 172 772 177 HOH HOH B . 
M 7 HOH 173 773 69  HOH HOH B . 
M 7 HOH 174 774 575 HOH HOH B . 
M 7 HOH 175 775 376 HOH HOH B . 
M 7 HOH 176 776 607 HOH HOH B . 
M 7 HOH 177 777 639 HOH HOH B . 
M 7 HOH 178 778 225 HOH HOH B . 
M 7 HOH 179 779 115 HOH HOH B . 
M 7 HOH 180 780 209 HOH HOH B . 
M 7 HOH 181 781 277 HOH HOH B . 
M 7 HOH 182 782 211 HOH HOH B . 
M 7 HOH 183 783 54  HOH HOH B . 
M 7 HOH 184 784 547 HOH HOH B . 
M 7 HOH 185 785 148 HOH HOH B . 
M 7 HOH 186 786 609 HOH HOH B . 
M 7 HOH 187 787 682 HOH HOH B . 
M 7 HOH 188 788 292 HOH HOH B . 
M 7 HOH 189 789 239 HOH HOH B . 
M 7 HOH 190 790 650 HOH HOH B . 
M 7 HOH 191 791 44  HOH HOH B . 
M 7 HOH 192 792 235 HOH HOH B . 
M 7 HOH 193 793 105 HOH HOH B . 
M 7 HOH 194 794 365 HOH HOH B . 
M 7 HOH 195 795 304 HOH HOH B . 
M 7 HOH 196 796 250 HOH HOH B . 
M 7 HOH 197 797 481 HOH HOH B . 
M 7 HOH 198 798 91  HOH HOH B . 
M 7 HOH 199 799 482 HOH HOH B . 
M 7 HOH 200 800 588 HOH HOH B . 
M 7 HOH 201 801 400 HOH HOH B . 
M 7 HOH 202 802 40  HOH HOH B . 
M 7 HOH 203 803 549 HOH HOH B . 
M 7 HOH 204 804 554 HOH HOH B . 
M 7 HOH 205 805 265 HOH HOH B . 
M 7 HOH 206 806 25  HOH HOH B . 
M 7 HOH 207 807 571 HOH HOH B . 
M 7 HOH 208 808 201 HOH HOH B . 
M 7 HOH 209 809 602 HOH HOH B . 
M 7 HOH 210 810 312 HOH HOH B . 
M 7 HOH 211 811 314 HOH HOH B . 
M 7 HOH 212 812 552 HOH HOH B . 
M 7 HOH 213 813 272 HOH HOH B . 
M 7 HOH 214 814 382 HOH HOH B . 
M 7 HOH 215 815 386 HOH HOH B . 
M 7 HOH 216 816 334 HOH HOH B . 
M 7 HOH 217 817 634 HOH HOH B . 
M 7 HOH 218 818 557 HOH HOH B . 
M 7 HOH 219 819 603 HOH HOH B . 
M 7 HOH 220 820 325 HOH HOH B . 
M 7 HOH 221 821 194 HOH HOH B . 
M 7 HOH 222 822 600 HOH HOH B . 
M 7 HOH 223 823 380 HOH HOH B . 
M 7 HOH 224 824 212 HOH HOH B . 
M 7 HOH 225 825 545 HOH HOH B . 
M 7 HOH 226 826 565 HOH HOH B . 
M 7 HOH 227 827 563 HOH HOH B . 
M 7 HOH 228 828 560 HOH HOH B . 
M 7 HOH 229 829 288 HOH HOH B . 
M 7 HOH 230 830 299 HOH HOH B . 
M 7 HOH 231 831 556 HOH HOH B . 
M 7 HOH 232 832 593 HOH HOH B . 
M 7 HOH 233 833 33  HOH HOH B . 
M 7 HOH 234 834 123 HOH HOH B . 
M 7 HOH 235 835 548 HOH HOH B . 
M 7 HOH 236 836 210 HOH HOH B . 
M 7 HOH 237 837 624 HOH HOH B . 
M 7 HOH 238 838 574 HOH HOH B . 
M 7 HOH 239 839 596 HOH HOH B . 
M 7 HOH 240 840 327 HOH HOH B . 
M 7 HOH 241 841 343 HOH HOH B . 
M 7 HOH 242 842 354 HOH HOH B . 
M 7 HOH 243 843 319 HOH HOH B . 
M 7 HOH 244 844 701 HOH HOH B . 
M 7 HOH 245 845 564 HOH HOH B . 
M 7 HOH 246 846 608 HOH HOH B . 
M 7 HOH 247 847 489 HOH HOH B . 
M 7 HOH 248 848 638 HOH HOH B . 
M 7 HOH 249 849 392 HOH HOH B . 
M 7 HOH 250 850 137 HOH HOH B . 
M 7 HOH 251 851 281 HOH HOH B . 
M 7 HOH 252 852 229 HOH HOH B . 
M 7 HOH 253 853 585 HOH HOH B . 
M 7 HOH 254 854 582 HOH HOH B . 
M 7 HOH 255 855 695 HOH HOH B . 
M 7 HOH 256 856 346 HOH HOH B . 
M 7 HOH 257 857 553 HOH HOH B . 
M 7 HOH 258 858 636 HOH HOH B . 
M 7 HOH 259 859 704 HOH HOH B . 
M 7 HOH 260 860 113 HOH HOH B . 
M 7 HOH 261 861 377 HOH HOH B . 
M 7 HOH 262 862 648 HOH HOH B . 
M 7 HOH 263 863 645 HOH HOH B . 
M 7 HOH 264 864 581 HOH HOH B . 
M 7 HOH 265 865 313 HOH HOH B . 
M 7 HOH 266 866 576 HOH HOH B . 
M 7 HOH 267 867 154 HOH HOH B . 
M 7 HOH 268 868 691 HOH HOH B . 
M 7 HOH 269 869 369 HOH HOH B . 
M 7 HOH 270 870 587 HOH HOH B . 
M 7 HOH 271 871 649 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 ARG 59  ? CG  ? A ARG 57  CG  
8   1 Y 1 A ARG 59  ? CD  ? A ARG 57  CD  
9   1 Y 1 A ARG 59  ? NE  ? A ARG 57  NE  
10  1 Y 1 A ARG 59  ? CZ  ? A ARG 57  CZ  
11  1 Y 1 A ARG 59  ? NH1 ? A ARG 57  NH1 
12  1 Y 1 A ARG 59  ? NH2 ? A ARG 57  NH2 
13  1 Y 1 A GLU 122 ? CG  ? A GLU 120 CG  
14  1 Y 1 A GLU 122 ? CD  ? A GLU 120 CD  
15  1 Y 1 A GLU 122 ? OE1 ? A GLU 120 OE1 
16  1 Y 1 A GLU 122 ? OE2 ? A GLU 120 OE2 
17  1 Y 1 A ARG 125 ? CG  ? A ARG 123 CG  
18  1 Y 1 A ARG 125 ? CD  ? A ARG 123 CD  
19  1 Y 1 A ARG 125 ? NE  ? A ARG 123 NE  
20  1 Y 1 A ARG 125 ? CZ  ? A ARG 123 CZ  
21  1 Y 1 A ARG 125 ? NH1 ? A ARG 123 NH1 
22  1 Y 1 A ARG 125 ? NH2 ? A ARG 123 NH2 
23  1 Y 1 A ARG 128 ? CG  ? A ARG 126 CG  
24  1 Y 1 A ARG 128 ? CD  ? A ARG 126 CD  
25  1 Y 1 A ARG 128 ? NE  ? A ARG 126 NE  
26  1 Y 1 A ARG 128 ? CZ  ? A ARG 126 CZ  
27  1 Y 1 A ARG 128 ? NH1 ? A ARG 126 NH1 
28  1 Y 1 A ARG 128 ? NH2 ? A ARG 126 NH2 
29  1 Y 1 A GLU 333 ? CG  ? A GLU 331 CG  
30  1 Y 1 A GLU 333 ? CD  ? A GLU 331 CD  
31  1 Y 1 A GLU 333 ? OE1 ? A GLU 331 OE1 
32  1 Y 1 A GLU 333 ? OE2 ? A GLU 331 OE2 
33  1 Y 1 A GLU 334 ? CG  ? A GLU 332 CG  
34  1 Y 1 A GLU 334 ? CD  ? A GLU 332 CD  
35  1 Y 1 A GLU 334 ? OE1 ? A GLU 332 OE1 
36  1 Y 1 A GLU 334 ? OE2 ? A GLU 332 OE2 
37  1 Y 1 A ARG 369 ? NE  ? A ARG 367 NE  
38  1 Y 1 A ARG 369 ? CZ  ? A ARG 367 CZ  
39  1 Y 1 A ARG 369 ? NH1 ? A ARG 367 NH1 
40  1 Y 1 A ARG 369 ? NH2 ? A ARG 367 NH2 
41  1 Y 1 A GLU 402 ? CG  ? A GLU 400 CG  
42  1 Y 1 A GLU 402 ? CD  ? A GLU 400 CD  
43  1 Y 1 A GLU 402 ? OE1 ? A GLU 400 OE1 
44  1 Y 1 A GLU 402 ? OE2 ? A GLU 400 OE2 
45  1 Y 1 A GLU 407 ? CG  ? A GLU 405 CG  
46  1 Y 1 A GLU 407 ? CD  ? A GLU 405 CD  
47  1 Y 1 A GLU 407 ? OE1 ? A GLU 405 OE1 
48  1 Y 1 A GLU 407 ? OE2 ? A GLU 405 OE2 
49  1 Y 1 A THR 426 ? OG1 ? A THR 424 OG1 
50  1 Y 1 A THR 426 ? CG2 ? A THR 424 CG2 
51  1 Y 1 B ARG 3   ? CG  ? B ARG 1   CG  
52  1 Y 1 B ARG 3   ? CD  ? B ARG 1   CD  
53  1 Y 1 B ARG 3   ? NE  ? B ARG 1   NE  
54  1 Y 1 B ARG 3   ? CZ  ? B ARG 1   CZ  
55  1 Y 1 B ARG 3   ? NH1 ? B ARG 1   NH1 
56  1 Y 1 B ARG 3   ? NH2 ? B ARG 1   NH2 
57  1 Y 1 B ARG 29  ? CG  ? B ARG 27  CG  
58  1 Y 1 B ARG 29  ? CD  ? B ARG 27  CD  
59  1 Y 1 B ARG 29  ? NE  ? B ARG 27  NE  
60  1 Y 1 B ARG 29  ? CZ  ? B ARG 27  CZ  
61  1 Y 1 B ARG 29  ? NH1 ? B ARG 27  NH1 
62  1 Y 1 B ARG 29  ? NH2 ? B ARG 27  NH2 
63  1 Y 1 B GLU 47  ? CG  ? B GLU 45  CG  
64  1 Y 1 B GLU 47  ? CD  ? B GLU 45  CD  
65  1 Y 1 B GLU 47  ? OE1 ? B GLU 45  OE1 
66  1 Y 1 B GLU 47  ? OE2 ? B GLU 45  OE2 
67  1 Y 1 B ARG 62  ? CG  ? B ARG 60  CG  
68  1 Y 1 B ARG 62  ? CD  ? B ARG 60  CD  
69  1 Y 1 B ARG 62  ? NE  ? B ARG 60  NE  
70  1 Y 1 B ARG 62  ? CZ  ? B ARG 60  CZ  
71  1 Y 1 B ARG 62  ? NH1 ? B ARG 60  NH1 
72  1 Y 1 B ARG 62  ? NH2 ? B ARG 60  NH2 
73  1 Y 1 B ARG 86  ? CG  ? B ARG 84  CG  
74  1 Y 1 B ARG 86  ? CD  ? B ARG 84  CD  
75  1 Y 1 B ARG 86  ? NE  ? B ARG 84  NE  
76  1 Y 1 B ARG 86  ? CZ  ? B ARG 84  CZ  
77  1 Y 1 B ARG 86  ? NH1 ? B ARG 84  NH1 
78  1 Y 1 B ARG 86  ? NH2 ? B ARG 84  NH2 
79  1 Y 1 B GLN 96  ? CG  ? B GLN 94  CG  
80  1 Y 1 B GLN 96  ? CD  ? B GLN 94  CD  
81  1 Y 1 B GLN 96  ? OE1 ? B GLN 94  OE1 
82  1 Y 1 B GLN 96  ? NE2 ? B GLN 94  NE2 
83  1 Y 1 B GLU 121 ? CD  ? B GLU 119 CD  
84  1 Y 1 B GLU 121 ? OE1 ? B GLU 119 OE1 
85  1 Y 1 B GLU 121 ? OE2 ? B GLU 119 OE2 
86  1 Y 1 B GLU 122 ? CG  ? B GLU 120 CG  
87  1 Y 1 B GLU 122 ? CD  ? B GLU 120 CD  
88  1 Y 1 B GLU 122 ? OE1 ? B GLU 120 OE1 
89  1 Y 1 B GLU 122 ? OE2 ? B GLU 120 OE2 
90  1 Y 1 B ARG 125 ? CG  ? B ARG 123 CG  
91  1 Y 1 B ARG 125 ? CD  ? B ARG 123 CD  
92  1 Y 1 B ARG 125 ? NE  ? B ARG 123 NE  
93  1 Y 1 B ARG 125 ? CZ  ? B ARG 123 CZ  
94  1 Y 1 B ARG 125 ? NH1 ? B ARG 123 NH1 
95  1 Y 1 B ARG 125 ? NH2 ? B ARG 123 NH2 
96  1 Y 1 B GLU 215 ? CG  ? B GLU 213 CG  
97  1 Y 1 B GLU 215 ? CD  ? B GLU 213 CD  
98  1 Y 1 B GLU 215 ? OE1 ? B GLU 213 OE1 
99  1 Y 1 B GLU 215 ? OE2 ? B GLU 213 OE2 
100 1 Y 1 B LYS 270 ? CG  ? B LYS 268 CG  
101 1 Y 1 B LYS 270 ? CD  ? B LYS 268 CD  
102 1 Y 1 B LYS 270 ? CE  ? B LYS 268 CE  
103 1 Y 1 B LYS 270 ? NZ  ? B LYS 268 NZ  
104 1 Y 1 B ASP 424 ? CG  ? B ASP 422 CG  
105 1 Y 1 B ASP 424 ? OD1 ? B ASP 422 OD1 
106 1 Y 1 B ASP 424 ? OD2 ? B ASP 422 OD2 
# 
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' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .                    2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   91.06 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9EIF 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     79.024 
_cell.length_a_esd                 ? 
_cell.length_b                     45.246 
_cell.length_b_esd                 ? 
_cell.length_c                     118.218 
_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                         9EIF 
_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                   9EIF 
_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             2.23 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          44.85 
_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 monosaccharides (D-Glucose, D-Mannose, D-Galactose, L-Fucose, D-Xylose and N-Acetyl-D-Glucosamine), and 3 mM D-2-hydroxyisovaleric acid (pH adjusted with 95 mM NaOH, pH ~7-8)
;
_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         2024-05-01 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.97934 
_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                        'NSLS-II BEAMLINE 17-ID-2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97934 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   17-ID-2 
_diffrn_source.pdbx_synchrotron_site       NSLS-II 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9EIF 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.65 
_reflns.d_resolution_low                               29.71 
_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                                     100330 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.1 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.9 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          10.9 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.127 
_reflns.pdbx_Rpim_I_all                                0.048 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.998 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.118 
_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                                    1.65 
_reflns_shell.d_res_low                                     1.68 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           2.6 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             4682 
_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                               0.774 
_reflns_shell.pdbx_Rpim_I_all                               0.291 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.762 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          93.4 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.716 
_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                                 9EIF 
_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                            1.65 
_refine.ls_d_res_low                             29.71 
_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                     100303 
_refine.ls_number_reflns_R_free                  10039 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.96 
_refine.ls_percent_reflns_R_free                 5.15 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1673 
_refine.ls_R_factor_R_free                       0.1910 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1660 
_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                          1.34 
_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                 18.27 
_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                            0.17 
_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                       1.65 
_refine_hist.d_res_low                        29.71 
_refine_hist.number_atoms_solvent             635 
_refine_hist.number_atoms_total               7067 
_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        6342 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         90 
_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  ? 6694 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.015  ? 9187 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 14.891 ? 957  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.067  ? 1096 ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.007  ? 1189 ? 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' 1.65 1.67  . . 330 5721 92.00  . . . . 0.2589 . . . . . . . . . . . 0.2928 
'X-RAY DIFFRACTION' 1.67 1.69  . . 332 6241 99.00  . . . . 0.2550 . . . . . . . . . . . 0.2765 
'X-RAY DIFFRACTION' 1.69 1.71  . . 306 6105 99.00  . . . . 0.2471 . . . . . . . . . . . 0.2984 
'X-RAY DIFFRACTION' 1.71 1.73  . . 279 6177 98.00  . . . . 0.2431 . . . . . . . . . . . 0.2469 
'X-RAY DIFFRACTION' 1.73 1.75  . . 355 6072 98.00  . . . . 0.2283 . . . . . . . . . . . 0.2381 
'X-RAY DIFFRACTION' 1.75 1.78  . . 310 6143 100.00 . . . . 0.2214 . . . . . . . . . . . 0.2430 
'X-RAY DIFFRACTION' 1.78 1.80  . . 334 6189 98.00  . . . . 0.2130 . . . . . . . . . . . 0.2742 
'X-RAY DIFFRACTION' 1.80 1.83  . . 333 6160 99.00  . . . . 0.2034 . . . . . . . . . . . 0.2277 
'X-RAY DIFFRACTION' 1.83 1.86  . . 313 6204 100.00 . . . . 0.1979 . . . . . . . . . . . 0.2133 
'X-RAY DIFFRACTION' 1.86 1.89  . . 308 6143 97.00  . . . . 0.1896 . . . . . . . . . . . 0.2208 
'X-RAY DIFFRACTION' 1.89 1.92  . . 393 6105 100.00 . . . . 0.1893 . . . . . . . . . . . 0.2049 
'X-RAY DIFFRACTION' 1.92 1.96  . . 339 6210 99.00  . . . . 0.1800 . . . . . . . . . . . 0.2144 
'X-RAY DIFFRACTION' 1.96 1.99  . . 356 6068 99.00  . . . . 0.1702 . . . . . . . . . . . 0.2004 
'X-RAY DIFFRACTION' 1.99 2.03  . . 300 6328 100.00 . . . . 0.1650 . . . . . . . . . . . 0.2198 
'X-RAY DIFFRACTION' 2.03 2.08  . . 321 6146 98.00  . . . . 0.1667 . . . . . . . . . . . 0.2001 
'X-RAY DIFFRACTION' 2.08 2.13  . . 332 6196 100.00 . . . . 0.1600 . . . . . . . . . . . 0.1958 
'X-RAY DIFFRACTION' 2.13 2.18  . . 360 6127 99.00  . . . . 0.1568 . . . . . . . . . . . 0.2031 
'X-RAY DIFFRACTION' 2.18 2.24  . . 294 6248 100.00 . . . . 0.1597 . . . . . . . . . . . 0.1915 
'X-RAY DIFFRACTION' 2.24 2.30  . . 324 6145 99.00  . . . . 0.1591 . . . . . . . . . . . 0.1860 
'X-RAY DIFFRACTION' 2.30 2.38  . . 348 6283 100.00 . . . . 0.1572 . . . . . . . . . . . 0.1951 
'X-RAY DIFFRACTION' 2.38 2.46  . . 379 6150 100.00 . . . . 0.1558 . . . . . . . . . . . 0.2061 
'X-RAY DIFFRACTION' 2.46 2.56  . . 329 6180 99.00  . . . . 0.1534 . . . . . . . . . . . 0.1886 
'X-RAY DIFFRACTION' 2.56 2.68  . . 359 6228 100.00 . . . . 0.1546 . . . . . . . . . . . 0.1786 
'X-RAY DIFFRACTION' 2.68 2.82  . . 330 6226 100.00 . . . . 0.1555 . . . . . . . . . . . 0.1819 
'X-RAY DIFFRACTION' 2.82 3.00  . . 397 6167 100.00 . . . . 0.1619 . . . . . . . . . . . 0.1748 
'X-RAY DIFFRACTION' 3.00 3.23  . . 376 6152 100.00 . . . . 0.1628 . . . . . . . . . . . 0.1930 
'X-RAY DIFFRACTION' 3.23 3.55  . . 340 6212 100.00 . . . . 0.1538 . . . . . . . . . . . 0.1618 
'X-RAY DIFFRACTION' 3.55 4.07  . . 262 6316 100.00 . . . . 0.1391 . . . . . . . . . . . 0.1541 
'X-RAY DIFFRACTION' 4.07 5.12  . . 304 6264 100.00 . . . . 0.1319 . . . . . . . . . . . 0.1424 
'X-RAY DIFFRACTION' 5.12 29.71 . . 396 6136 100.00 . . . . 0.1603 . . . . . . . . . . . 0.1676 
# 
_struct.entry_id                     9EIF 
_struct.title                        
'A broad-substrate spectrum lactate racemase A from Isosphaera pallida in complex with D-2-Hydroxyisovalerate' 
_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        9EIF 
_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 3 ? 
E N N 4 ? 
F N N 5 ? 
G N N 4 ? 
H N N 6 ? 
I N N 2 ? 
J N N 5 ? 
K N N 6 ? 
L N N 7 ? 
M 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 9EIF A 1 ? 425 ? E8QWZ4 2 ? 426 ? 3 427 
2 1 9EIF 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,L 
2 1 B,I,J,K,M       
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 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 ? GLU A 346 ? THR A 337 GLU A 348 1 ? 12 
HELX_P HELX_P18 AB9 ASP A 352 ? ALA A 366 ? ASP A 354 ALA A 368 1 ? 15 
HELX_P HELX_P19 AC1 PRO A 376 ? SER A 381 ? PRO A 378 SER A 383 1 ? 6  
HELX_P HELX_P20 AC2 ARG A 382 ? HIS A 384 ? ARG A 384 HIS A 386 5 ? 3  
HELX_P HELX_P21 AC3 THR A 390 ? GLY A 403 ? THR A 392 GLY A 405 1 ? 14 
HELX_P HELX_P22 AC4 LYS A 413 ? VAL A 417 ? LYS A 415 VAL A 419 5 ? 5  
HELX_P HELX_P23 AC5 ASP B 34  ? GLU B 45  ? ASP B 36  GLU B 47  1 ? 12 
HELX_P HELX_P24 AC6 PRO B 51  ? ARG B 57  ? PRO B 53  ARG B 59  1 ? 7  
HELX_P HELX_P25 AC7 PRO B 74  ? ALA B 89  ? PRO B 76  ALA B 91  1 ? 16 
HELX_P HELX_P26 AC8 ALA B 92  ? GLN B 94  ? ALA B 94  GLN B 96  5 ? 3  
HELX_P HELX_P27 AC9 THR B 109 ? SER B 118 ? THR B 111 SER B 120 1 ? 10 
HELX_P HELX_P28 AD1 SER B 118 ? TYR B 125 ? SER B 120 TYR B 127 1 ? 8  
HELX_P HELX_P29 AD2 ARG B 134 ? GLU B 136 ? ARG B 136 GLU B 138 5 ? 3  
HELX_P HELX_P30 AD3 SER B 154 ? GLN B 158 ? SER B 156 GLN B 160 1 ? 5  
HELX_P HELX_P31 AD4 GLY B 178 ? ILE B 183 ? GLY B 180 ILE B 185 5 ? 6  
HELX_P HELX_P32 AD5 ALA B 189 ? HIS B 197 ? ALA B 191 HIS B 199 1 ? 9  
HELX_P HELX_P33 AD6 GLY B 198 ? GLU B 203 ? GLY B 200 GLU B 205 1 ? 6  
HELX_P HELX_P34 AD7 ASN B 215 ? GLY B 229 ? ASN B 217 GLY B 231 1 ? 15 
HELX_P HELX_P35 AD8 GLU B 253 ? VAL B 267 ? GLU B 255 VAL B 269 1 ? 15 
HELX_P HELX_P36 AD9 PRO B 286 ? LEU B 289 ? PRO B 288 LEU B 291 5 ? 4  
HELX_P HELX_P37 AE1 THR B 290 ? LEU B 302 ? THR B 292 LEU B 304 1 ? 13 
HELX_P HELX_P38 AE2 SER B 323 ? HIS B 333 ? SER B 325 HIS B 335 1 ? 11 
HELX_P HELX_P39 AE3 THR B 335 ? LYS B 345 ? THR B 337 LYS B 347 1 ? 11 
HELX_P HELX_P40 AE4 ASP B 352 ? ARG B 364 ? ASP B 354 ARG B 366 1 ? 13 
HELX_P HELX_P41 AE5 PRO B 376 ? SER B 381 ? PRO B 378 SER B 383 1 ? 6  
HELX_P HELX_P42 AE6 THR B 390 ? GLY B 403 ? THR B 392 GLY B 405 1 ? 14 
HELX_P HELX_P43 AE7 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 C 4EY . C7 ? ? A LYS 183 A 4EY 501 1_555 ? ? ? ? ? ? ? 1.429 ? ? 
covale2 covale none ? B LYS 181 NZ  ? ? ? 1_555 I 4EY . C7 ? ? B LYS 183 B 4EY 501 1_555 ? ? ? ? ? ? ? 1.430 ? ? 
metalc1 metalc ?    ? A HIS 197 NE2 A ? ? 1_555 H NI  . NI ? ? A HIS 199 A NI  506 1_555 ? ? ? ? ? ? ? 2.119 ? ? 
metalc2 metalc ?    ? A HIS 197 NE2 B ? ? 1_555 H NI  . NI ? ? A HIS 199 A NI  506 1_555 ? ? ? ? ? ? ? 2.101 ? ? 
metalc3 metalc ?    ? C 4EY .   S7  ? ? ? 1_555 H NI  . NI ? ? A 4EY 501 A NI  506 1_555 ? ? ? ? ? ? ? 2.185 ? ? 
metalc4 metalc ?    ? C 4EY .   S2  ? ? ? 1_555 H NI  . NI ? ? A 4EY 501 A NI  506 1_555 ? ? ? ? ? ? ? 2.187 ? ? 
metalc5 metalc ?    ? B HIS 197 NE2 A ? ? 1_555 K NI  . NI ? ? B HIS 199 B NI  503 1_555 ? ? ? ? ? ? ? 2.092 ? ? 
metalc6 metalc ?    ? B HIS 197 NE2 B ? ? 1_555 K NI  . NI ? ? B HIS 199 B NI  503 1_555 ? ? ? ? ? ? ? 2.100 ? ? 
metalc7 metalc ?    ? I 4EY .   S7  ? ? ? 1_555 K NI  . NI ? ? B 4EY 501 B NI  503 1_555 ? ? ? ? ? ? ? 2.214 ? ? 
metalc8 metalc ?    ? I 4EY .   S2  ? ? ? 1_555 K NI  . NI ? ? B 4EY 501 B NI  503 1_555 ? ? ? ? ? ? ? 2.240 ? ? 
# 
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 8.8   ? 
2  NE2 A A HIS 197 ? A HIS 199 ? 1_555 NI ? H NI . ? A NI 506 ? 1_555 S7  ? C 4EY .   ? A 4EY 501 ? 1_555 92.8  ? 
3  NE2 B A HIS 197 ? A HIS 199 ? 1_555 NI ? H NI . ? A NI 506 ? 1_555 S7  ? C 4EY .   ? A 4EY 501 ? 1_555 92.2  ? 
4  NE2 A A HIS 197 ? A HIS 199 ? 1_555 NI ? H NI . ? A NI 506 ? 1_555 S2  ? C 4EY .   ? A 4EY 501 ? 1_555 93.3  ? 
5  NE2 B A HIS 197 ? A HIS 199 ? 1_555 NI ? H NI . ? A NI 506 ? 1_555 S2  ? C 4EY .   ? A 4EY 501 ? 1_555 93.9  ? 
6  S7  ? C 4EY .   ? A 4EY 501 ? 1_555 NI ? H NI . ? A NI 506 ? 1_555 S2  ? C 4EY .   ? A 4EY 501 ? 1_555 173.9 ? 
7  NE2 A B HIS 197 ? B HIS 199 ? 1_555 NI ? K NI . ? B NI 503 ? 1_555 NE2 B B HIS 197 ? B HIS 199 ? 1_555 8.9   ? 
8  NE2 A B HIS 197 ? B HIS 199 ? 1_555 NI ? K NI . ? B NI 503 ? 1_555 S7  ? I 4EY .   ? B 4EY 501 ? 1_555 90.4  ? 
9  NE2 B B HIS 197 ? B HIS 199 ? 1_555 NI ? K NI . ? B NI 503 ? 1_555 S7  ? I 4EY .   ? B 4EY 501 ? 1_555 94.1  ? 
10 NE2 A B HIS 197 ? B HIS 199 ? 1_555 NI ? K NI . ? B NI 503 ? 1_555 S2  ? I 4EY .   ? B 4EY 501 ? 1_555 96.2  ? 
11 NE2 B B HIS 197 ? B HIS 199 ? 1_555 NI ? K NI . ? B NI 503 ? 1_555 S2  ? I 4EY .   ? B 4EY 501 ? 1_555 92.4  ? 
12 S7  ? I 4EY .   ? B 4EY 501 ? 1_555 NI ? K NI . ? B NI 503 ? 1_555 S2  ? I 4EY .   ? B 4EY 501 ? 1_555 173.4 ? 
# 
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 C . ? LYS A 181 ? 4EY A 501 ? 1_555 LYS A 183 ? 1_555 C7 NZ LYS 1 4EY None 'Covalent chemical modification' 
2 4EY I . ? LYS B 181 ? 4EY B 501 ? 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 14.93 
2 HIS 285 A . ? HIS 287 A PRO 286 A ? PRO 288 A 1 5.96  
3 CYS 184 B . ? CYS 186 B PRO 185 B ? PRO 187 B 1 15.81 
4 HIS 285 B . ? HIS 287 B PRO 286 B ? PRO 288 B 1 9.20  
# 
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  ? ALA B 101 ? ILE B 98  ALA B 103 
AA8 3 ALA B 62  ? CYS B 67  ? ALA B 64  CYS B 69  
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 ALA A 269 ? N ALA A 271 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 ALA B 101 ? O ALA B 103 N VAL B 66  ? N VAL B 68  
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 PHE B 232 ? O PHE B 234 
AA8 5 6 N ASN B 235 ? N ASN B 237 O VAL B 248 ? O VAL B 250 
AA9 1 2 N GLY B 142 ? N GLY B 144 O ALA B 150 ? O ALA B 152 
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 VAL B 278 ? N VAL B 280 
AB3 4 5 N VAL B 279 ? N VAL B 281 O ALA B 409 ? O ALA B 411 
# 
_pdbx_entry_details.entry_id                   9EIF 
_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 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             CA 
_pdbx_validate_rmsd_angle.auth_asym_id_1             A 
_pdbx_validate_rmsd_angle.auth_comp_id_1             LEU 
_pdbx_validate_rmsd_angle.auth_seq_id_1              57 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             B 
_pdbx_validate_rmsd_angle.auth_atom_id_2             CB 
_pdbx_validate_rmsd_angle.auth_asym_id_2             A 
_pdbx_validate_rmsd_angle.auth_comp_id_2             LEU 
_pdbx_validate_rmsd_angle.auth_seq_id_2              57 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             B 
_pdbx_validate_rmsd_angle.auth_atom_id_3             CG 
_pdbx_validate_rmsd_angle.auth_asym_id_3             A 
_pdbx_validate_rmsd_angle.auth_comp_id_3             LEU 
_pdbx_validate_rmsd_angle.auth_seq_id_3              57 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             B 
_pdbx_validate_rmsd_angle.angle_value                130.28 
_pdbx_validate_rmsd_angle.angle_target_value         115.30 
_pdbx_validate_rmsd_angle.angle_deviation            14.98 
_pdbx_validate_rmsd_angle.angle_standard_deviation   2.30 
_pdbx_validate_rmsd_angle.linker_flag                N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 TYR A 8   ? ? -168.12 106.76 
2 1 PRO A 74  ? ? -79.40  49.41  
3 1 SER A 120 ? ? 83.76   148.38 
4 1 LEU A 214 ? ? -113.36 -73.19 
5 1 TYR B 8   ? ? -164.10 106.47 
6 1 PRO B 74  ? ? -78.77  48.69  
7 1 SER B 120 ? ? 85.29   145.01 
8 1 LEU B 214 ? ? -113.72 -70.24 
# 
_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 
GLN N    N  N N 127 
GLN CA   C  N S 128 
GLN C    C  N N 129 
GLN O    O  N N 130 
GLN CB   C  N N 131 
GLN CG   C  N N 132 
GLN CD   C  N N 133 
GLN OE1  O  N N 134 
GLN NE2  N  N N 135 
GLN OXT  O  N N 136 
GLN H    H  N N 137 
GLN H2   H  N N 138 
GLN HA   H  N N 139 
GLN HB2  H  N N 140 
GLN HB3  H  N N 141 
GLN HG2  H  N N 142 
GLN HG3  H  N N 143 
GLN HE21 H  N N 144 
GLN HE22 H  N N 145 
GLN HXT  H  N N 146 
GLU N    N  N N 147 
GLU CA   C  N S 148 
GLU C    C  N N 149 
GLU O    O  N N 150 
GLU CB   C  N N 151 
GLU CG   C  N N 152 
GLU CD   C  N N 153 
GLU OE1  O  N N 154 
GLU OE2  O  N N 155 
GLU OXT  O  N N 156 
GLU H    H  N N 157 
GLU H2   H  N N 158 
GLU HA   H  N N 159 
GLU HB2  H  N N 160 
GLU HB3  H  N N 161 
GLU HG2  H  N N 162 
GLU HG3  H  N N 163 
GLU HE2  H  N N 164 
GLU HXT  H  N N 165 
GLY N    N  N N 166 
GLY CA   C  N N 167 
GLY C    C  N N 168 
GLY O    O  N N 169 
GLY OXT  O  N N 170 
GLY H    H  N N 171 
GLY H2   H  N N 172 
GLY HA2  H  N N 173 
GLY HA3  H  N N 174 
GLY HXT  H  N N 175 
HIS N    N  N N 176 
HIS CA   C  N S 177 
HIS C    C  N N 178 
HIS O    O  N N 179 
HIS CB   C  N N 180 
HIS CG   C  Y N 181 
HIS ND1  N  Y N 182 
HIS CD2  C  Y N 183 
HIS CE1  C  Y N 184 
HIS NE2  N  Y N 185 
HIS OXT  O  N N 186 
HIS H    H  N N 187 
HIS H2   H  N N 188 
HIS HA   H  N N 189 
HIS HB2  H  N N 190 
HIS HB3  H  N N 191 
HIS HD1  H  N N 192 
HIS HD2  H  N N 193 
HIS HE1  H  N N 194 
HIS HE2  H  N N 195 
HIS HXT  H  N N 196 
HOH O    O  N N 197 
HOH H1   H  N N 198 
HOH H2   H  N N 199 
ILE N    N  N N 200 
ILE CA   C  N S 201 
ILE C    C  N N 202 
ILE O    O  N N 203 
ILE CB   C  N S 204 
ILE CG1  C  N N 205 
ILE CG2  C  N N 206 
ILE CD1  C  N N 207 
ILE OXT  O  N N 208 
ILE H    H  N N 209 
ILE H2   H  N N 210 
ILE HA   H  N N 211 
ILE HB   H  N N 212 
ILE HG12 H  N N 213 
ILE HG13 H  N N 214 
ILE HG21 H  N N 215 
ILE HG22 H  N N 216 
ILE HG23 H  N N 217 
ILE HD11 H  N N 218 
ILE HD12 H  N N 219 
ILE HD13 H  N N 220 
ILE HXT  H  N N 221 
LEU N    N  N N 222 
LEU CA   C  N S 223 
LEU C    C  N N 224 
LEU O    O  N N 225 
LEU CB   C  N N 226 
LEU CG   C  N N 227 
LEU CD1  C  N N 228 
LEU CD2  C  N N 229 
LEU OXT  O  N N 230 
LEU H    H  N N 231 
LEU H2   H  N N 232 
LEU HA   H  N N 233 
LEU HB2  H  N N 234 
LEU HB3  H  N N 235 
LEU HG   H  N N 236 
LEU HD11 H  N N 237 
LEU HD12 H  N N 238 
LEU HD13 H  N N 239 
LEU HD21 H  N N 240 
LEU HD22 H  N N 241 
LEU HD23 H  N N 242 
LEU HXT  H  N N 243 
LYS N    N  N N 244 
LYS CA   C  N S 245 
LYS C    C  N N 246 
LYS O    O  N N 247 
LYS CB   C  N N 248 
LYS CG   C  N N 249 
LYS CD   C  N N 250 
LYS CE   C  N N 251 
LYS NZ   N  N N 252 
LYS OXT  O  N N 253 
LYS H    H  N N 254 
LYS H2   H  N N 255 
LYS HA   H  N N 256 
LYS HB2  H  N N 257 
LYS HB3  H  N N 258 
LYS HG2  H  N N 259 
LYS HG3  H  N N 260 
LYS HD2  H  N N 261 
LYS HD3  H  N N 262 
LYS HE2  H  N N 263 
LYS HE3  H  N N 264 
LYS HZ1  H  N N 265 
LYS HZ2  H  N N 266 
LYS HZ3  H  N N 267 
LYS HXT  H  N N 268 
MET N    N  N N 269 
MET CA   C  N S 270 
MET C    C  N N 271 
MET O    O  N N 272 
MET CB   C  N N 273 
MET CG   C  N N 274 
MET SD   S  N N 275 
MET CE   C  N N 276 
MET OXT  O  N N 277 
MET H    H  N N 278 
MET H2   H  N N 279 
MET HA   H  N N 280 
MET HB2  H  N N 281 
MET HB3  H  N N 282 
MET HG2  H  N N 283 
MET HG3  H  N N 284 
MET HE1  H  N N 285 
MET HE2  H  N N 286 
MET HE3  H  N N 287 
MET HXT  H  N N 288 
NI  NI   NI N N 289 
PEG C1   C  N N 290 
PEG O1   O  N N 291 
PEG C2   C  N N 292 
PEG O2   O  N N 293 
PEG C3   C  N N 294 
PEG C4   C  N N 295 
PEG O4   O  N N 296 
PEG H11  H  N N 297 
PEG H12  H  N N 298 
PEG HO1  H  N N 299 
PEG H21  H  N N 300 
PEG H22  H  N N 301 
PEG H31  H  N N 302 
PEG H32  H  N N 303 
PEG H41  H  N N 304 
PEG H42  H  N N 305 
PEG HO4  H  N N 306 
PGE C1   C  N N 307 
PGE O1   O  N N 308 
PGE C2   C  N N 309 
PGE O2   O  N N 310 
PGE C3   C  N N 311 
PGE C4   C  N N 312 
PGE O4   O  N N 313 
PGE C6   C  N N 314 
PGE C5   C  N N 315 
PGE O3   O  N N 316 
PGE H1   H  N N 317 
PGE H12  H  N N 318 
PGE HO1  H  N N 319 
PGE H2   H  N N 320 
PGE H22  H  N N 321 
PGE H3   H  N N 322 
PGE H32  H  N N 323 
PGE H4   H  N N 324 
PGE H42  H  N N 325 
PGE HO4  H  N N 326 
PGE H6   H  N N 327 
PGE H62  H  N N 328 
PGE H5   H  N N 329 
PGE H52  H  N N 330 
PHE N    N  N N 331 
PHE CA   C  N S 332 
PHE C    C  N N 333 
PHE O    O  N N 334 
PHE CB   C  N N 335 
PHE CG   C  Y N 336 
PHE CD1  C  Y N 337 
PHE CD2  C  Y N 338 
PHE CE1  C  Y N 339 
PHE CE2  C  Y N 340 
PHE CZ   C  Y N 341 
PHE OXT  O  N N 342 
PHE H    H  N N 343 
PHE H2   H  N N 344 
PHE HA   H  N N 345 
PHE HB2  H  N N 346 
PHE HB3  H  N N 347 
PHE HD1  H  N N 348 
PHE HD2  H  N N 349 
PHE HE1  H  N N 350 
PHE HE2  H  N N 351 
PHE HZ   H  N N 352 
PHE HXT  H  N N 353 
PRO N    N  N N 354 
PRO CA   C  N S 355 
PRO C    C  N N 356 
PRO O    O  N N 357 
PRO CB   C  N N 358 
PRO CG   C  N N 359 
PRO CD   C  N N 360 
PRO OXT  O  N N 361 
PRO H    H  N N 362 
PRO HA   H  N N 363 
PRO HB2  H  N N 364 
PRO HB3  H  N N 365 
PRO HG2  H  N N 366 
PRO HG3  H  N N 367 
PRO HD2  H  N N 368 
PRO HD3  H  N N 369 
PRO HXT  H  N N 370 
SER N    N  N N 371 
SER CA   C  N S 372 
SER C    C  N N 373 
SER O    O  N N 374 
SER CB   C  N N 375 
SER OG   O  N N 376 
SER OXT  O  N N 377 
SER H    H  N N 378 
SER H2   H  N N 379 
SER HA   H  N N 380 
SER HB2  H  N N 381 
SER HB3  H  N N 382 
SER HG   H  N N 383 
SER HXT  H  N N 384 
THR N    N  N N 385 
THR CA   C  N S 386 
THR C    C  N N 387 
THR O    O  N N 388 
THR CB   C  N R 389 
THR OG1  O  N N 390 
THR CG2  C  N N 391 
THR OXT  O  N N 392 
THR H    H  N N 393 
THR H2   H  N N 394 
THR HA   H  N N 395 
THR HB   H  N N 396 
THR HG1  H  N N 397 
THR HG21 H  N N 398 
THR HG22 H  N N 399 
THR HG23 H  N N 400 
THR HXT  H  N N 401 
TRP N    N  N N 402 
TRP CA   C  N S 403 
TRP C    C  N N 404 
TRP O    O  N N 405 
TRP CB   C  N N 406 
TRP CG   C  Y N 407 
TRP CD1  C  Y N 408 
TRP CD2  C  Y N 409 
TRP NE1  N  Y N 410 
TRP CE2  C  Y N 411 
TRP CE3  C  Y N 412 
TRP CZ2  C  Y N 413 
TRP CZ3  C  Y N 414 
TRP CH2  C  Y N 415 
TRP OXT  O  N N 416 
TRP H    H  N N 417 
TRP H2   H  N N 418 
TRP HA   H  N N 419 
TRP HB2  H  N N 420 
TRP HB3  H  N N 421 
TRP HD1  H  N N 422 
TRP HE1  H  N N 423 
TRP HE3  H  N N 424 
TRP HZ2  H  N N 425 
TRP HZ3  H  N N 426 
TRP HH2  H  N N 427 
TRP HXT  H  N N 428 
TYR N    N  N N 429 
TYR CA   C  N S 430 
TYR C    C  N N 431 
TYR O    O  N N 432 
TYR CB   C  N N 433 
TYR CG   C  Y N 434 
TYR CD1  C  Y N 435 
TYR CD2  C  Y N 436 
TYR CE1  C  Y N 437 
TYR CE2  C  Y N 438 
TYR CZ   C  Y N 439 
TYR OH   O  N N 440 
TYR OXT  O  N N 441 
TYR H    H  N N 442 
TYR H2   H  N N 443 
TYR HA   H  N N 444 
TYR HB2  H  N N 445 
TYR HB3  H  N N 446 
TYR HD1  H  N N 447 
TYR HD2  H  N N 448 
TYR HE1  H  N N 449 
TYR HE2  H  N N 450 
TYR HH   H  N N 451 
TYR HXT  H  N N 452 
VAD CA   C  N R 453 
VAD CB   C  N N 454 
VAD CG1  C  N N 455 
VAD CG2  C  N N 456 
VAD C    C  N N 457 
VAD O    O  N N 458 
VAD OXT  O  N N 459 
VAD OE   O  N N 460 
VAD HA   H  N N 461 
VAD HB   H  N N 462 
VAD HG11 H  N N 463 
VAD HG12 H  N N 464 
VAD HG13 H  N N 465 
VAD HG21 H  N N 466 
VAD HG22 H  N N 467 
VAD HG23 H  N N 468 
VAD HXT  H  N N 469 
VAD HOE  H  N N 470 
VAL N    N  N N 471 
VAL CA   C  N S 472 
VAL C    C  N N 473 
VAL O    O  N N 474 
VAL CB   C  N N 475 
VAL CG1  C  N N 476 
VAL CG2  C  N N 477 
VAL OXT  O  N N 478 
VAL H    H  N N 479 
VAL H2   H  N N 480 
VAL HA   H  N N 481 
VAL HB   H  N N 482 
VAL HG11 H  N N 483 
VAL HG12 H  N N 484 
VAL HG13 H  N N 485 
VAL HG21 H  N N 486 
VAL HG22 H  N N 487 
VAL HG23 H  N N 488 
VAL HXT  H  N N 489 
# 
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 
GLN N   CA   sing N N 123 
GLN N   H    sing N N 124 
GLN N   H2   sing N N 125 
GLN CA  C    sing N N 126 
GLN CA  CB   sing N N 127 
GLN CA  HA   sing N N 128 
GLN C   O    doub N N 129 
GLN C   OXT  sing N N 130 
GLN CB  CG   sing N N 131 
GLN CB  HB2  sing N N 132 
GLN CB  HB3  sing N N 133 
GLN CG  CD   sing N N 134 
GLN CG  HG2  sing N N 135 
GLN CG  HG3  sing N N 136 
GLN CD  OE1  doub N N 137 
GLN CD  NE2  sing N N 138 
GLN NE2 HE21 sing N N 139 
GLN NE2 HE22 sing N N 140 
GLN OXT HXT  sing N N 141 
GLU N   CA   sing N N 142 
GLU N   H    sing N N 143 
GLU N   H2   sing N N 144 
GLU CA  C    sing N N 145 
GLU CA  CB   sing N N 146 
GLU CA  HA   sing N N 147 
GLU C   O    doub N N 148 
GLU C   OXT  sing N N 149 
GLU CB  CG   sing N N 150 
GLU CB  HB2  sing N N 151 
GLU CB  HB3  sing N N 152 
GLU CG  CD   sing N N 153 
GLU CG  HG2  sing N N 154 
GLU CG  HG3  sing N N 155 
GLU CD  OE1  doub N N 156 
GLU CD  OE2  sing N N 157 
GLU OE2 HE2  sing N N 158 
GLU OXT HXT  sing N N 159 
GLY N   CA   sing N N 160 
GLY N   H    sing N N 161 
GLY N   H2   sing N N 162 
GLY CA  C    sing N N 163 
GLY CA  HA2  sing N N 164 
GLY CA  HA3  sing N N 165 
GLY C   O    doub N N 166 
GLY C   OXT  sing N N 167 
GLY OXT HXT  sing N N 168 
HIS N   CA   sing N N 169 
HIS N   H    sing N N 170 
HIS N   H2   sing N N 171 
HIS CA  C    sing N N 172 
HIS CA  CB   sing N N 173 
HIS CA  HA   sing N N 174 
HIS C   O    doub N N 175 
HIS C   OXT  sing N N 176 
HIS CB  CG   sing N N 177 
HIS CB  HB2  sing N N 178 
HIS CB  HB3  sing N N 179 
HIS CG  ND1  sing Y N 180 
HIS CG  CD2  doub Y N 181 
HIS ND1 CE1  doub Y N 182 
HIS ND1 HD1  sing N N 183 
HIS CD2 NE2  sing Y N 184 
HIS CD2 HD2  sing N N 185 
HIS CE1 NE2  sing Y N 186 
HIS CE1 HE1  sing N N 187 
HIS NE2 HE2  sing N N 188 
HIS OXT HXT  sing N N 189 
HOH O   H1   sing N N 190 
HOH O   H2   sing N N 191 
ILE N   CA   sing N N 192 
ILE N   H    sing N N 193 
ILE N   H2   sing N N 194 
ILE CA  C    sing N N 195 
ILE CA  CB   sing N N 196 
ILE CA  HA   sing N N 197 
ILE C   O    doub N N 198 
ILE C   OXT  sing N N 199 
ILE CB  CG1  sing N N 200 
ILE CB  CG2  sing N N 201 
ILE CB  HB   sing N N 202 
ILE CG1 CD1  sing N N 203 
ILE CG1 HG12 sing N N 204 
ILE CG1 HG13 sing N N 205 
ILE CG2 HG21 sing N N 206 
ILE CG2 HG22 sing N N 207 
ILE CG2 HG23 sing N N 208 
ILE CD1 HD11 sing N N 209 
ILE CD1 HD12 sing N N 210 
ILE CD1 HD13 sing N N 211 
ILE OXT HXT  sing N N 212 
LEU N   CA   sing N N 213 
LEU N   H    sing N N 214 
LEU N   H2   sing N N 215 
LEU CA  C    sing N N 216 
LEU CA  CB   sing N N 217 
LEU CA  HA   sing N N 218 
LEU C   O    doub N N 219 
LEU C   OXT  sing N N 220 
LEU CB  CG   sing N N 221 
LEU CB  HB2  sing N N 222 
LEU CB  HB3  sing N N 223 
LEU CG  CD1  sing N N 224 
LEU CG  CD2  sing N N 225 
LEU CG  HG   sing N N 226 
LEU CD1 HD11 sing N N 227 
LEU CD1 HD12 sing N N 228 
LEU CD1 HD13 sing N N 229 
LEU CD2 HD21 sing N N 230 
LEU CD2 HD22 sing N N 231 
LEU CD2 HD23 sing N N 232 
LEU OXT HXT  sing N N 233 
LYS N   CA   sing N N 234 
LYS N   H    sing N N 235 
LYS N   H2   sing N N 236 
LYS CA  C    sing N N 237 
LYS CA  CB   sing N N 238 
LYS CA  HA   sing N N 239 
LYS C   O    doub N N 240 
LYS C   OXT  sing N N 241 
LYS CB  CG   sing N N 242 
LYS CB  HB2  sing N N 243 
LYS CB  HB3  sing N N 244 
LYS CG  CD   sing N N 245 
LYS CG  HG2  sing N N 246 
LYS CG  HG3  sing N N 247 
LYS CD  CE   sing N N 248 
LYS CD  HD2  sing N N 249 
LYS CD  HD3  sing N N 250 
LYS CE  NZ   sing N N 251 
LYS CE  HE2  sing N N 252 
LYS CE  HE3  sing N N 253 
LYS NZ  HZ1  sing N N 254 
LYS NZ  HZ2  sing N N 255 
LYS NZ  HZ3  sing N N 256 
LYS OXT HXT  sing N N 257 
MET N   CA   sing N N 258 
MET N   H    sing N N 259 
MET N   H2   sing N N 260 
MET CA  C    sing N N 261 
MET CA  CB   sing N N 262 
MET CA  HA   sing N N 263 
MET C   O    doub N N 264 
MET C   OXT  sing N N 265 
MET CB  CG   sing N N 266 
MET CB  HB2  sing N N 267 
MET CB  HB3  sing N N 268 
MET CG  SD   sing N N 269 
MET CG  HG2  sing N N 270 
MET CG  HG3  sing N N 271 
MET SD  CE   sing N N 272 
MET CE  HE1  sing N N 273 
MET CE  HE2  sing N N 274 
MET CE  HE3  sing N N 275 
MET OXT HXT  sing N N 276 
PEG C1  O1   sing N N 277 
PEG C1  C2   sing N N 278 
PEG C1  H11  sing N N 279 
PEG C1  H12  sing N N 280 
PEG O1  HO1  sing N N 281 
PEG C2  O2   sing N N 282 
PEG C2  H21  sing N N 283 
PEG C2  H22  sing N N 284 
PEG O2  C3   sing N N 285 
PEG C3  C4   sing N N 286 
PEG C3  H31  sing N N 287 
PEG C3  H32  sing N N 288 
PEG C4  O4   sing N N 289 
PEG C4  H41  sing N N 290 
PEG C4  H42  sing N N 291 
PEG O4  HO4  sing N N 292 
PGE C1  O1   sing N N 293 
PGE C1  C2   sing N N 294 
PGE C1  H1   sing N N 295 
PGE C1  H12  sing N N 296 
PGE O1  HO1  sing N N 297 
PGE C2  O2   sing N N 298 
PGE C2  H2   sing N N 299 
PGE C2  H22  sing N N 300 
PGE O2  C3   sing N N 301 
PGE C3  C4   sing N N 302 
PGE C3  H3   sing N N 303 
PGE C3  H32  sing N N 304 
PGE C4  O3   sing N N 305 
PGE C4  H4   sing N N 306 
PGE C4  H42  sing N N 307 
PGE O4  C6   sing N N 308 
PGE O4  HO4  sing N N 309 
PGE C6  C5   sing N N 310 
PGE C6  H6   sing N N 311 
PGE C6  H62  sing N N 312 
PGE C5  O3   sing N N 313 
PGE C5  H5   sing N N 314 
PGE C5  H52  sing N N 315 
PHE N   CA   sing N N 316 
PHE N   H    sing N N 317 
PHE N   H2   sing N N 318 
PHE CA  C    sing N N 319 
PHE CA  CB   sing N N 320 
PHE CA  HA   sing N N 321 
PHE C   O    doub N N 322 
PHE C   OXT  sing N N 323 
PHE CB  CG   sing N N 324 
PHE CB  HB2  sing N N 325 
PHE CB  HB3  sing N N 326 
PHE CG  CD1  doub Y N 327 
PHE CG  CD2  sing Y N 328 
PHE CD1 CE1  sing Y N 329 
PHE CD1 HD1  sing N N 330 
PHE CD2 CE2  doub Y N 331 
PHE CD2 HD2  sing N N 332 
PHE CE1 CZ   doub Y N 333 
PHE CE1 HE1  sing N N 334 
PHE CE2 CZ   sing Y N 335 
PHE CE2 HE2  sing N N 336 
PHE CZ  HZ   sing N N 337 
PHE OXT HXT  sing N N 338 
PRO N   CA   sing N N 339 
PRO N   CD   sing N N 340 
PRO N   H    sing N N 341 
PRO CA  C    sing N N 342 
PRO CA  CB   sing N N 343 
PRO CA  HA   sing N N 344 
PRO C   O    doub N N 345 
PRO C   OXT  sing N N 346 
PRO CB  CG   sing N N 347 
PRO CB  HB2  sing N N 348 
PRO CB  HB3  sing N N 349 
PRO CG  CD   sing N N 350 
PRO CG  HG2  sing N N 351 
PRO CG  HG3  sing N N 352 
PRO CD  HD2  sing N N 353 
PRO CD  HD3  sing N N 354 
PRO OXT HXT  sing N N 355 
SER N   CA   sing N N 356 
SER N   H    sing N N 357 
SER N   H2   sing N N 358 
SER CA  C    sing N N 359 
SER CA  CB   sing N N 360 
SER CA  HA   sing N N 361 
SER C   O    doub N N 362 
SER C   OXT  sing N N 363 
SER CB  OG   sing N N 364 
SER CB  HB2  sing N N 365 
SER CB  HB3  sing N N 366 
SER OG  HG   sing N N 367 
SER OXT HXT  sing N N 368 
THR N   CA   sing N N 369 
THR N   H    sing N N 370 
THR N   H2   sing N N 371 
THR CA  C    sing N N 372 
THR CA  CB   sing N N 373 
THR CA  HA   sing N N 374 
THR C   O    doub N N 375 
THR C   OXT  sing N N 376 
THR CB  OG1  sing N N 377 
THR CB  CG2  sing N N 378 
THR CB  HB   sing N N 379 
THR OG1 HG1  sing N N 380 
THR CG2 HG21 sing N N 381 
THR CG2 HG22 sing N N 382 
THR CG2 HG23 sing N N 383 
THR OXT HXT  sing N N 384 
TRP N   CA   sing N N 385 
TRP N   H    sing N N 386 
TRP N   H2   sing N N 387 
TRP CA  C    sing N N 388 
TRP CA  CB   sing N N 389 
TRP CA  HA   sing N N 390 
TRP C   O    doub N N 391 
TRP C   OXT  sing N N 392 
TRP CB  CG   sing N N 393 
TRP CB  HB2  sing N N 394 
TRP CB  HB3  sing N N 395 
TRP CG  CD1  doub Y N 396 
TRP CG  CD2  sing Y N 397 
TRP CD1 NE1  sing Y N 398 
TRP CD1 HD1  sing N N 399 
TRP CD2 CE2  doub Y N 400 
TRP CD2 CE3  sing Y N 401 
TRP NE1 CE2  sing Y N 402 
TRP NE1 HE1  sing N N 403 
TRP CE2 CZ2  sing Y N 404 
TRP CE3 CZ3  doub Y N 405 
TRP CE3 HE3  sing N N 406 
TRP CZ2 CH2  doub Y N 407 
TRP CZ2 HZ2  sing N N 408 
TRP CZ3 CH2  sing Y N 409 
TRP CZ3 HZ3  sing N N 410 
TRP CH2 HH2  sing N N 411 
TRP OXT HXT  sing N N 412 
TYR N   CA   sing N N 413 
TYR N   H    sing N N 414 
TYR N   H2   sing N N 415 
TYR CA  C    sing N N 416 
TYR CA  CB   sing N N 417 
TYR CA  HA   sing N N 418 
TYR C   O    doub N N 419 
TYR C   OXT  sing N N 420 
TYR CB  CG   sing N N 421 
TYR CB  HB2  sing N N 422 
TYR CB  HB3  sing N N 423 
TYR CG  CD1  doub Y N 424 
TYR CG  CD2  sing Y N 425 
TYR CD1 CE1  sing Y N 426 
TYR CD1 HD1  sing N N 427 
TYR CD2 CE2  doub Y N 428 
TYR CD2 HD2  sing N N 429 
TYR CE1 CZ   doub Y N 430 
TYR CE1 HE1  sing N N 431 
TYR CE2 CZ   sing Y N 432 
TYR CE2 HE2  sing N N 433 
TYR CZ  OH   sing N N 434 
TYR OH  HH   sing N N 435 
TYR OXT HXT  sing N N 436 
VAD CA  CB   sing N N 437 
VAD CA  C    sing N N 438 
VAD CA  OE   sing N N 439 
VAD CA  HA   sing N N 440 
VAD CB  CG1  sing N N 441 
VAD CB  CG2  sing N N 442 
VAD CB  HB   sing N N 443 
VAD CG1 HG11 sing N N 444 
VAD CG1 HG12 sing N N 445 
VAD CG1 HG13 sing N N 446 
VAD CG2 HG21 sing N N 447 
VAD CG2 HG22 sing N N 448 
VAD CG2 HG23 sing N N 449 
VAD C   O    doub N N 450 
VAD C   OXT  sing N N 451 
VAD OXT HXT  sing N N 452 
VAD OE  HOE  sing N N 453 
VAL N   CA   sing N N 454 
VAL N   H    sing N N 455 
VAL N   H2   sing N N 456 
VAL CA  C    sing N N 457 
VAL CA  CB   sing N N 458 
VAL CA  HA   sing N N 459 
VAL C   O    doub N N 460 
VAL C   OXT  sing N N 461 
VAL CB  CG1  sing N N 462 
VAL CB  CG2  sing N N 463 
VAL CB  HB   sing N N 464 
VAL CG1 HG11 sing N N 465 
VAL CG1 HG12 sing N N 466 
VAL CG1 HG13 sing N N 467 
VAL CG2 HG21 sing N N 468 
VAL CG2 HG22 sing N N 469 
VAL CG2 HG23 sing N N 470 
VAL OXT HXT  sing N N 471 
# 
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   9EIA 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9EIF 
_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]   0.012654 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000235 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.022101 
_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]   0.008460 
_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   ? -10.623 8.552   11.854  1.00 19.97 ?  3   ARG A N   1 
ATOM   2    C  CA  . ARG A 1 1   ? -9.942  7.703   10.874  1.00 19.65 ?  3   ARG A CA  1 
ATOM   3    C  C   . ARG A 1 1   ? -8.626  8.309   10.412  1.00 17.03 ?  3   ARG A C   1 
ATOM   4    O  O   . ARG A 1 1   ? -8.548  9.488   10.089  1.00 19.90 ?  3   ARG A O   1 
ATOM   5    C  CB  . ARG A 1 1   ? -10.826 7.444   9.656   1.00 21.48 ?  3   ARG A CB  1 
ATOM   6    N  N   . VAL A 1 2   ? -7.583  7.488   10.370  1.00 12.85 ?  4   VAL A N   1 
ATOM   7    C  CA  . VAL A 1 2   ? -6.283  7.918   9.880   1.00 13.60 ?  4   VAL A CA  1 
ATOM   8    C  C   . VAL A 1 2   ? -5.674  6.742   9.134   1.00 15.04 ?  4   VAL A C   1 
ATOM   9    O  O   . VAL A 1 2   ? -5.910  5.581   9.477   1.00 15.50 ?  4   VAL A O   1 
ATOM   10   C  CB  . VAL A 1 2   ? -5.350  8.408   11.020  1.00 17.75 ?  4   VAL A CB  1 
ATOM   11   C  CG1 . VAL A 1 2   ? -5.018  7.281   11.984  1.00 22.16 ?  4   VAL A CG1 1 
ATOM   12   C  CG2 . VAL A 1 2   ? -4.084  8.995   10.449  1.00 21.70 ?  4   VAL A CG2 1 
ATOM   13   N  N   . THR A 1 3   ? -4.912  7.042   8.088   1.00 12.93 ?  5   THR A N   1 
ATOM   14   C  CA  . THR A 1 3   ? -4.180  6.016   7.354   1.00 11.01 ?  5   THR A CA  1 
ATOM   15   C  C   . THR A 1 3   ? -2.718  6.078   7.780   1.00 13.47 ?  5   THR A C   1 
ATOM   16   O  O   . THR A 1 3   ? -2.029  7.061   7.498   1.00 12.06 ?  5   THR A O   1 
ATOM   17   C  CB  . THR A 1 3   ? -4.288  6.208   5.847   1.00 11.71 ?  5   THR A CB  1 
ATOM   18   O  OG1 . THR A 1 3   ? -5.673  6.220   5.463   1.00 16.66 ?  5   THR A OG1 1 
ATOM   19   C  CG2 . THR A 1 3   ? -3.574  5.048   5.122   1.00 13.64 ?  5   THR A CG2 1 
ATOM   20   N  N   . LEU A 1 4   ? -2.257  5.034   8.458   1.00 8.77  ?  6   LEU A N   1 
ATOM   21   C  CA  . LEU A 1 4   ? -0.850  4.916   8.810   1.00 8.94  ?  6   LEU A CA  1 
ATOM   22   C  C   . LEU A 1 4   ? -0.078  4.347   7.634   1.00 10.85 ?  6   LEU A C   1 
ATOM   23   O  O   . LEU A 1 4   ? -0.583  3.493   6.905   1.00 11.69 ?  6   LEU A O   1 
ATOM   24   C  CB  . LEU A 1 4   ? -0.669  3.975   9.995   1.00 10.69 ?  6   LEU A CB  1 
ATOM   25   C  CG  . LEU A 1 4   ? -1.355  4.355   11.295  1.00 11.68 ?  6   LEU A CG  1 
ATOM   26   C  CD1 . LEU A 1 4   ? -1.026  3.282   12.331  1.00 10.61 ?  6   LEU A CD1 1 
ATOM   27   C  CD2 . LEU A 1 4   ? -0.950  5.765   11.755  1.00 13.17 ?  6   LEU A CD2 1 
ATOM   28   N  N   . ASP A 1 5   ? 1.171   4.792   7.468   1.00 8.21  ?  7   ASP A N   1 
ATOM   29   C  CA  . ASP A 1 5   ? 2.016   4.129   6.488   1.00 8.88  ?  7   ASP A CA  1 
ATOM   30   C  C   . ASP A 1 5   ? 2.186   2.673   6.908   1.00 8.30  ?  7   ASP A C   1 
ATOM   31   O  O   . ASP A 1 5   ? 2.344   2.372   8.096   1.00 9.80  ?  7   ASP A O   1 
ATOM   32   C  CB  . ASP A 1 5   ? 3.399   4.779   6.391   1.00 10.59 ?  7   ASP A CB  1 
ATOM   33   C  CG  . ASP A 1 5   ? 3.405   6.065   5.574   1.00 18.02 ?  7   ASP A CG  1 
ATOM   34   O  OD1 . ASP A 1 5   ? 4.424   6.790   5.658   1.00 17.56 ?  7   ASP A OD1 1 
ATOM   35   O  OD2 . ASP A 1 5   ? 2.365   6.434   4.984   1.00 16.46 ?  7   ASP A OD2 1 
ATOM   36   N  N   . TYR A 1 6   ? 2.151   1.769   5.930   1.00 8.50  ?  8   TYR A N   1 
ATOM   37   C  CA  . TYR A 1 6   ? 2.135   0.336   6.206   1.00 10.25 ?  8   TYR A CA  1 
ATOM   38   C  C   . TYR A 1 6   ? 2.392   -0.410  4.908   1.00 10.33 ?  8   TYR A C   1 
ATOM   39   O  O   . TYR A 1 6   ? 1.521   -0.443  4.036   1.00 9.25  ?  8   TYR A O   1 
ATOM   40   C  CB  . TYR A 1 6   ? 0.787   -0.085  6.810   1.00 9.61  ?  8   TYR A CB  1 
ATOM   41   C  CG  . TYR A 1 6   ? 0.769   -1.496  7.366   1.00 6.50  ?  8   TYR A CG  1 
ATOM   42   C  CD1 . TYR A 1 6   ? 1.161   -1.752  8.684   1.00 7.75  ?  8   TYR A CD1 1 
ATOM   43   C  CD2 . TYR A 1 6   ? 0.349   -2.562  6.583   1.00 12.50 ?  8   TYR A CD2 1 
ATOM   44   C  CE1 . TYR A 1 6   ? 1.121   -3.050  9.203   1.00 11.10 ?  8   TYR A CE1 1 
ATOM   45   C  CE2 . TYR A 1 6   ? 0.330   -3.856  7.085   1.00 12.59 ?  8   TYR A CE2 1 
ATOM   46   C  CZ  . TYR A 1 6   ? 0.711   -4.093  8.391   1.00 11.60 ?  8   TYR A CZ  1 
ATOM   47   O  OH  . TYR A 1 6   ? 0.680   -5.389  8.885   1.00 13.61 ?  8   TYR A OH  1 
ATOM   48   N  N   . GLY A 1 7   ? 3.583   -0.980  4.755   1.00 8.68  ?  9   GLY A N   1 
ATOM   49   C  CA  . GLY A 1 7   ? 3.902   -1.649  3.497   1.00 8.75  ?  9   GLY A CA  1 
ATOM   50   C  C   . GLY A 1 7   ? 3.570   -0.810  2.277   1.00 11.09 ?  9   GLY A C   1 
ATOM   51   O  O   . GLY A 1 7   ? 3.720   0.421   2.270   1.00 10.51 ?  9   GLY A O   1 
ATOM   52   N  N   . LYS A 1 8   ? 3.083   -1.474  1.230   1.00 10.12 ?  10  LYS A N   1 
ATOM   53   C  CA  . LYS A 1 8   ? 2.713   -0.788  -0.002  1.00 9.56  ?  10  LYS A CA  1 
ATOM   54   C  C   . LYS A 1 8   ? 1.295   -0.230  0.004   1.00 12.62 ?  10  LYS A C   1 
ATOM   55   O  O   . LYS A 1 8   ? 0.903   0.410   -0.975  1.00 12.90 ?  10  LYS A O   1 
ATOM   56   C  CB  . LYS A 1 8   ? 2.902   -1.736  -1.205  1.00 11.11 ?  10  LYS A CB  1 
ATOM   57   C  CG  . LYS A 1 8   ? 4.338   -2.249  -1.311  1.00 12.93 ?  10  LYS A CG  1 
ATOM   58   C  CD  . LYS A 1 8   ? 4.432   -3.537  -2.115  1.00 20.63 ?  10  LYS A CD  1 
ATOM   59   C  CE  . LYS A 1 8   ? 5.816   -3.695  -2.742  1.00 25.59 ?  10  LYS A CE  1 
ATOM   60   N  NZ  . LYS A 1 8   ? 5.891   -4.924  -3.588  1.00 30.80 ?  10  LYS A NZ  1 
ATOM   61   N  N   . THR A 1 9   ? 0.547   -0.405  1.089   1.00 10.41 ?  11  THR A N   1 
ATOM   62   C  CA  . THR A 1 9   ? -0.894  -0.168  1.087   1.00 11.49 ?  11  THR A CA  1 
ATOM   63   C  C   . THR A 1 9   ? -1.349  0.929   2.024   1.00 12.41 ?  11  THR A C   1 
ATOM   64   O  O   . THR A 1 9   ? -2.398  1.535   1.778   1.00 12.21 ?  11  THR A O   1 
ATOM   65   C  CB  . THR A 1 9   ? -1.648  -1.443  1.503   1.00 12.02 ?  11  THR A CB  1 
ATOM   66   O  OG1 . THR A 1 9   ? -1.234  -1.824  2.827   1.00 11.48 ?  11  THR A OG1 1 
ATOM   67   C  CG2 . THR A 1 9   ? -1.397  -2.579  0.525   1.00 11.17 ?  11  THR A CG2 1 
ATOM   68   N  N   . GLY A 1 10  ? -0.630  1.164   3.117   1.00 10.99 ?  12  GLY A N   1 
ATOM   69   C  CA  . GLY A 1 10  ? -1.185  1.913   4.218   1.00 10.04 ?  12  GLY A CA  1 
ATOM   70   C  C   . GLY A 1 10  ? -2.113  1.042   5.042   1.00 9.44  ?  12  GLY A C   1 
ATOM   71   O  O   . GLY A 1 10  ? -2.402  -0.115  4.716   1.00 10.90 ?  12  GLY A O   1 
ATOM   72   N  N   . LEU A 1 11  ? -2.583  1.613   6.145   1.00 10.11 ?  13  LEU A N   1 
ATOM   73   C  CA  . LEU A 1 11  ? -3.422  0.894   7.107   1.00 9.90  ?  13  LEU A CA  1 
ATOM   74   C  C   . LEU A 1 11  ? -4.447  1.855   7.672   1.00 11.00 ?  13  LEU A C   1 
ATOM   75   O  O   . LEU A 1 11  ? -4.076  2.867   8.271   1.00 11.52 ?  13  LEU A O   1 
ATOM   76   C  CB  . LEU A 1 11  ? -2.585  0.304   8.240   1.00 12.63 ?  13  LEU A CB  1 
ATOM   77   C  CG  . LEU A 1 11  ? -3.306  -0.630  9.223   1.00 11.95 ?  13  LEU A CG  1 
ATOM   78   C  CD1 . LEU A 1 11  ? -3.715  -1.911  8.534   1.00 13.20 ?  13  LEU A CD1 1 
ATOM   79   C  CD2 . LEU A 1 11  ? -2.380  -0.919  10.408  1.00 12.79 ?  13  LEU A CD2 1 
ATOM   80   N  N   . ASN A 1 12  ? -5.731  1.538   7.493   1.00 10.79 ?  14  ASN A N   1 
ATOM   81   C  CA  . ASN A 1 12  ? -6.811  2.435   7.898   1.00 12.69 ?  14  ASN A CA  1 
ATOM   82   C  C   . ASN A 1 12  ? -7.195  2.140   9.343   1.00 13.25 ?  14  ASN A C   1 
ATOM   83   O  O   . ASN A 1 12  ? -7.776  1.085   9.641   1.00 9.89  ?  14  ASN A O   1 
ATOM   84   C  CB  . ASN A 1 12  ? -8.018  2.272   6.978   1.00 12.81 ?  14  ASN A CB  1 
ATOM   85   C  CG  . ASN A 1 12  ? -7.910  3.131   5.750   1.00 21.64 ?  14  ASN A CG  1 
ATOM   86   O  OD1 . ASN A 1 12  ? -7.109  4.076   5.718   1.00 28.93 ?  14  ASN A OD1 1 
ATOM   87   N  ND2 . ASN A 1 12  ? -8.734  2.845   4.739   1.00 24.36 ?  14  ASN A ND2 1 
ATOM   88   N  N   . VAL A 1 13  ? -6.902  3.086   10.233  1.00 11.28 ?  15  VAL A N   1 
ATOM   89   C  CA  . VAL A 1 13  ? -7.109  2.928   11.668  1.00 11.67 ?  15  VAL A CA  1 
ATOM   90   C  C   . VAL A 1 13  ? -8.175  3.918   12.128  1.00 12.62 ?  15  VAL A C   1 
ATOM   91   O  O   . VAL A 1 13  ? -8.175  5.078   11.701  1.00 15.58 ?  15  VAL A O   1 
ATOM   92   C  CB  . VAL A 1 13  ? -5.784  3.161   12.422  1.00 12.04 ?  15  VAL A CB  1 
ATOM   93   C  CG1 . VAL A 1 13  ? -5.990  3.120   13.948  1.00 14.78 ?  15  VAL A CG1 1 
ATOM   94   C  CG2 . VAL A 1 13  ? -4.725  2.173   11.951  1.00 11.21 ?  15  VAL A CG2 1 
ATOM   95   N  N   . ASP A 1 14  ? -9.083  3.466   12.999  1.00 14.14 ?  16  ASP A N   1 
ATOM   96   C  CA  . ASP A 1 14  ? -10.022 4.362   13.674  1.00 13.98 ?  16  ASP A CA  1 
ATOM   97   C  C   . ASP A 1 14  ? -9.530  4.598   15.098  1.00 15.82 ?  16  ASP A C   1 
ATOM   98   O  O   . ASP A 1 14  ? -9.360  3.647   15.861  1.00 20.26 ?  16  ASP A O   1 
ATOM   99   C  CB  . ASP A 1 14  ? -11.443 3.790   13.680  1.00 17.15 ?  16  ASP A CB  1 
ATOM   100  C  CG  . ASP A 1 14  ? -12.508 4.879   13.790  1.00 29.09 ?  16  ASP A CG  1 
ATOM   101  O  OD1 . ASP A 1 14  ? -13.712 4.548   13.846  1.00 35.27 ?  16  ASP A OD1 1 
ATOM   102  O  OD2 . ASP A 1 14  ? -12.137 6.071   13.835  1.00 29.39 ?  16  ASP A OD2 1 
ATOM   103  N  N   . LEU A 1 15  ? -9.293  5.868   15.446  1.00 13.16 ?  17  LEU A N   1 
ATOM   104  C  CA  . LEU A 1 15  ? -8.773  6.299   16.729  1.00 14.38 ?  17  LEU A CA  1 
ATOM   105  C  C   . LEU A 1 15  ? -9.850  7.073   17.497  1.00 16.24 ?  17  LEU A C   1 
ATOM   106  O  O   . LEU A 1 15  ? -10.731 7.686   16.884  1.00 15.92 ?  17  LEU A O   1 
ATOM   107  C  CB  . LEU A 1 15  ? -7.538  7.188   16.510  1.00 13.73 ?  17  LEU A CB  1 
ATOM   108  C  CG  . LEU A 1 15  ? -6.237  6.509   16.055  1.00 15.65 ?  17  LEU A CG  1 
ATOM   109  C  CD1 . LEU A 1 15  ? -5.104  7.520   15.964  1.00 20.63 ?  17  LEU A CD1 1 
ATOM   110  C  CD2 . LEU A 1 15  ? -5.819  5.332   16.962  1.00 18.68 ?  17  LEU A CD2 1 
ATOM   111  N  N   . PRO A 1 16  ? -9.804  7.087   18.833  1.00 18.39 ?  18  PRO A N   1 
ATOM   112  C  CA  . PRO A 1 16  ? -10.899 7.712   19.609  1.00 17.09 ?  18  PRO A CA  1 
ATOM   113  C  C   . PRO A 1 16  ? -10.924 9.223   19.422  1.00 19.48 ?  18  PRO A C   1 
ATOM   114  O  O   . PRO A 1 16  ? -9.934  9.910   19.686  1.00 17.18 ?  18  PRO A O   1 
ATOM   115  C  CB  . PRO A 1 16  ? -10.566 7.338   21.059  1.00 23.21 ?  18  PRO A CB  1 
ATOM   116  C  CG  . PRO A 1 16  ? -9.609  6.187   20.959  1.00 24.14 ?  18  PRO A CG  1 
ATOM   117  C  CD  . PRO A 1 16  ? -8.816  6.441   19.712  1.00 20.86 ?  18  PRO A CD  1 
ATOM   118  N  N   . ASP A 1 17  ? -12.080 9.741   19.002  1.00 18.84 ?  19  ASP A N   1 
ATOM   119  C  CA  . ASP A 1 17  ? -12.189 11.158  18.657  1.00 26.91 ?  19  ASP A CA  1 
ATOM   120  C  C   . ASP A 1 17  ? -11.854 12.055  19.842  1.00 26.18 ?  19  ASP A C   1 
ATOM   121  O  O   . ASP A 1 17  ? -11.220 13.102  19.682  1.00 32.52 ?  19  ASP A O   1 
ATOM   122  C  CB  . ASP A 1 17  ? -13.603 11.461  18.162  1.00 31.13 ?  19  ASP A CB  1 
ATOM   123  C  CG  . ASP A 1 17  ? -14.053 10.510  17.076  1.00 39.79 ?  19  ASP A CG  1 
ATOM   124  O  OD1 . ASP A 1 17  ? -13.464 10.543  15.979  1.00 40.08 ?  19  ASP A OD1 1 
ATOM   125  O  OD2 . ASP A 1 17  ? -14.986 9.713   17.329  1.00 46.35 ?  19  ASP A OD2 1 
ATOM   126  N  N   . ASP A 1 18  ? -12.279 11.665  21.035  1.00 21.43 ?  20  ASP A N   1 
ATOM   127  C  CA  . ASP A 1 18  ? -12.157 12.525  22.200  1.00 27.06 ?  20  ASP A CA  1 
ATOM   128  C  C   . ASP A 1 18  ? -10.798 12.422  22.865  1.00 23.80 ?  20  ASP A C   1 
ATOM   129  O  O   . ASP A 1 18  ? -10.566 13.092  23.876  1.00 25.17 ?  20  ASP A O   1 
ATOM   130  C  CB  . ASP A 1 18  ? -13.241 12.161  23.212  1.00 30.48 ?  20  ASP A CB  1 
ATOM   131  C  CG  . ASP A 1 18  ? -13.235 10.679  23.539  1.00 39.99 ?  20  ASP A CG  1 
ATOM   132  O  OD1 . ASP A 1 18  ? -13.252 10.320  24.738  1.00 50.01 ?  20  ASP A OD1 1 
ATOM   133  O  OD2 . ASP A 1 18  ? -13.187 9.872   22.583  1.00 44.41 ?  20  ASP A OD2 1 
ATOM   134  N  N   . ARG A 1 19  ? -9.901  11.598  22.340  1.00 20.79 ?  21  ARG A N   1 
ATOM   135  C  CA  . ARG A 1 19  ? -8.663  11.313  23.037  1.00 20.15 ?  21  ARG A CA  1 
ATOM   136  C  C   . ARG A 1 19  ? -7.456  11.680  22.190  1.00 19.97 ?  21  ARG A C   1 
ATOM   137  O  O   . ARG A 1 19  ? -6.355  11.794  22.732  1.00 20.75 ?  21  ARG A O   1 
ATOM   138  C  CB  . ARG A 1 19  ? -8.594  9.814   23.383  1.00 22.69 ?  21  ARG A CB  1 
ATOM   139  C  CG  . ARG A 1 19  ? -9.785  9.361   24.277  1.00 32.20 ?  21  ARG A CG  1 
ATOM   140  C  CD  . ARG A 1 19  ? -9.878  9.914   25.687  1.00 35.66 ?  21  ARG A CD  1 
ATOM   141  N  NE  . ARG A 1 19  ? -8.803  9.565   26.597  1.00 38.80 ?  21  ARG A NE  1 
ATOM   142  C  CZ  . ARG A 1 19  ? -8.786  8.460   27.338  1.00 30.59 ?  21  ARG A CZ  1 
ATOM   143  N  NH1 . ARG A 1 19  ? -7.771  8.232   28.151  1.00 24.47 ?  21  ARG A NH1 1 
ATOM   144  N  NH2 . ARG A 1 19  ? -9.804  7.611   27.309  1.00 31.78 ?  21  ARG A NH2 1 
ATOM   145  N  N   . THR A 1 20  ? -7.648  11.902  20.889  1.00 15.53 ?  22  THR A N   1 
ATOM   146  C  CA  . THR A 1 20  ? -6.577  11.927  19.902  1.00 17.50 ?  22  THR A CA  1 
ATOM   147  C  C   . THR A 1 20  ? -6.318  13.343  19.411  1.00 15.76 ?  22  THR A C   1 
ATOM   148  O  O   . THR A 1 20  ? -7.242  14.043  18.989  1.00 16.90 ?  22  THR A O   1 
ATOM   149  C  CB  . THR A 1 20  ? -6.914  11.009  18.726  1.00 16.15 ?  22  THR A CB  1 
ATOM   150  O  OG1 . THR A 1 20  ? -7.238  9.699   19.219  1.00 17.77 ?  22  THR A OG1 1 
ATOM   151  C  CG2 . THR A 1 20  ? -5.718  10.915  17.762  1.00 16.00 ?  22  THR A CG2 1 
ATOM   152  N  N   . LEU A 1 21  ? -5.055  13.752  19.478  1.00 15.73 ?  23  LEU A N   1 
ATOM   153  C  CA  . LEU A 1 21  ? -4.605  15.028  18.958  1.00 15.79 ?  23  LEU A CA  1 
ATOM   154  C  C   . LEU A 1 21  ? -4.642  15.013  17.427  1.00 17.45 ?  23  LEU A C   1 
ATOM   155  O  O   . LEU A 1 21  ? -4.663  13.948  16.811  1.00 15.89 ?  23  LEU A O   1 
ATOM   156  C  CB  . LEU A 1 21  ? -3.181  15.288  19.441  1.00 13.19 ?  23  LEU A CB  1 
ATOM   157  C  CG  . LEU A 1 21  ? -2.960  15.895  20.831  1.00 21.39 ?  23  LEU A CG  1 
ATOM   158  C  CD1 . LEU A 1 21  ? -3.426  14.954  21.919  1.00 22.31 ?  23  LEU A CD1 1 
ATOM   159  C  CD2 . LEU A 1 21  ? -1.499  16.181  21.001  1.00 20.30 ?  23  LEU A CD2 1 
ATOM   160  N  N   . PRO A 1 22  ? -4.636  16.181  16.790  1.00 20.95 ?  24  PRO A N   1 
ATOM   161  C  CA  . PRO A 1 22  ? -4.492  16.221  15.325  1.00 17.44 ?  24  PRO A CA  1 
ATOM   162  C  C   . PRO A 1 22  ? -3.216  15.516  14.896  1.00 13.23 ?  24  PRO A C   1 
ATOM   163  O  O   . PRO A 1 22  ? -2.172  15.669  15.544  1.00 14.74 ?  24  PRO A O   1 
ATOM   164  C  CB  . PRO A 1 22  ? -4.429  17.723  15.013  1.00 23.94 ?  24  PRO A CB  1 
ATOM   165  C  CG  . PRO A 1 22  ? -5.134  18.381  16.180  1.00 22.85 ?  24  PRO A CG  1 
ATOM   166  C  CD  . PRO A 1 22  ? -4.799  17.527  17.375  1.00 21.58 ?  24  PRO A CD  1 
ATOM   167  N  N   . PRO A 1 23  ? -3.264  14.739  13.817  1.00 15.95 ?  25  PRO A N   1 
ATOM   168  C  CA  . PRO A 1 23  ? -2.090  13.945  13.427  1.00 13.88 ?  25  PRO A CA  1 
ATOM   169  C  C   . PRO A 1 23  ? -0.871  14.812  13.168  1.00 16.02 ?  25  PRO A C   1 
ATOM   170  O  O   . PRO A 1 23  ? -0.971  15.933  12.666  1.00 13.74 ?  25  PRO A O   1 
ATOM   171  C  CB  . PRO A 1 23  ? -2.555  13.231  12.153  1.00 15.40 ?  25  PRO A CB  1 
ATOM   172  C  CG  . PRO A 1 23  ? -4.094  13.183  12.298  1.00 16.03 ?  25  PRO A CG  1 
ATOM   173  C  CD  . PRO A 1 23  ? -4.416  14.508  12.929  1.00 14.68 ?  25  PRO A CD  1 
ATOM   174  N  N   . LEU A 1 24  ? 0.290   14.281  13.539  1.00 10.15 ?  26  LEU A N   1 
ATOM   175  C  CA  . LEU A 1 24  ? 1.558   14.950  13.295  1.00 12.13 ?  26  LEU A CA  1 
ATOM   176  C  C   . LEU A 1 24  ? 1.988   14.649  11.867  1.00 12.80 ?  26  LEU A C   1 
ATOM   177  O  O   . LEU A 1 24  ? 2.238   13.490  11.519  1.00 12.55 ?  26  LEU A O   1 
ATOM   178  C  CB  . LEU A 1 24  ? 2.602   14.467  14.299  1.00 9.87  ?  26  LEU A CB  1 
ATOM   179  C  CG  . LEU A 1 24  ? 2.519   15.062  15.709  1.00 14.56 ?  26  LEU A CG  1 
ATOM   180  C  CD1 . LEU A 1 24  ? 1.345   14.522  16.484  1.00 20.68 ?  26  LEU A CD1 1 
ATOM   181  C  CD2 . LEU A 1 24  ? 3.810   14.741  16.446  1.00 17.67 ?  26  LEU A CD2 1 
ATOM   182  N  N   . THR A 1 25  ? 2.055   15.682  11.035  1.00 14.83 ?  27  THR A N   1 
ATOM   183  C  CA  . THR A 1 25  ? 2.389   15.530  9.627   1.00 13.25 ?  27  THR A CA  1 
ATOM   184  C  C   . THR A 1 25  ? 3.475   16.536  9.276   1.00 16.70 ?  27  THR A C   1 
ATOM   185  O  O   . THR A 1 25  ? 3.652   17.543  9.964   1.00 17.56 ?  27  THR A O   1 
ATOM   186  C  CB  . THR A 1 25  ? 1.159   15.751  8.731   1.00 16.57 ?  27  THR A CB  1 
ATOM   187  O  OG1 . THR A 1 25  ? 0.659   17.077  8.939   1.00 22.53 ?  27  THR A OG1 1 
ATOM   188  C  CG2 . THR A 1 25  ? 0.052   14.762  9.066   1.00 19.08 ?  27  THR A CG2 1 
ATOM   189  N  N   . ILE A 1 26  ? 4.198   16.284  8.202   1.00 17.56 ?  28  ILE A N   1 
ATOM   190  C  CA  . ILE A 1 26  ? 5.177   17.292  7.813   1.00 16.49 ?  28  ILE A CA  1 
ATOM   191  C  C   . ILE A 1 26  ? 4.464   18.434  7.099   1.00 16.78 ?  28  ILE A C   1 
ATOM   192  O  O   . ILE A 1 26  ? 3.382   18.259  6.515   1.00 15.76 ?  28  ILE A O   1 
ATOM   193  C  CB  . ILE A 1 26  ? 6.307   16.721  6.942   1.00 23.14 ?  28  ILE A CB  1 
ATOM   194  C  CG1 . ILE A 1 26  ? 5.763   16.244  5.617   1.00 17.92 ?  28  ILE A CG1 1 
ATOM   195  C  CG2 . ILE A 1 26  ? 7.012   15.585  7.675   1.00 24.82 ?  28  ILE A CG2 1 
ATOM   196  C  CD1 . ILE A 1 26  ? 6.846   15.915  4.624   1.00 20.30 ?  28  ILE A CD1 1 
ATOM   197  N  N   . ARG A 1 27  ? 5.088   19.611  7.164   1.00 14.00 ?  29  ARG A N   1 
ATOM   198  C  CA  . ARG A 1 27  ? 4.548   20.826  6.560   1.00 15.16 ?  29  ARG A CA  1 
ATOM   199  C  C   . ARG A 1 27  ? 4.362   20.637  5.057   1.00 15.64 ?  29  ARG A C   1 
ATOM   200  O  O   . ARG A 1 27  ? 5.233   20.063  4.392   1.00 14.46 ?  29  ARG A O   1 
ATOM   201  C  CB  . ARG A 1 27  ? 5.491   22.013  6.829   1.00 21.24 ?  29  ARG A CB  1 
ATOM   202  C  CG  . ARG A 1 27  ? 5.027   23.347  6.208   1.00 28.23 ?  29  ARG A CG  1 
ATOM   203  C  CD  . ARG A 1 27  ? 5.998   24.550  6.348   1.00 32.08 ?  29  ARG A CD  1 
ATOM   204  N  NE  . ARG A 1 27  ? 7.294   24.457  5.667   1.00 36.38 ?  29  ARG A NE  1 
ATOM   205  C  CZ  . ARG A 1 27  ? 7.529   24.879  4.421   1.00 34.89 ?  29  ARG A CZ  1 
ATOM   206  N  NH1 . ARG A 1 27  ? 8.747   24.781  3.895   1.00 34.19 ?  29  ARG A NH1 1 
ATOM   207  N  NH2 . ARG A 1 27  ? 6.546   25.380  3.685   1.00 36.96 ?  29  ARG A NH2 1 
ATOM   208  N  N   . PRO A 1 28  ? 3.256   21.142  4.479   1.00 13.50 ?  30  PRO A N   1 
ATOM   209  C  CA  . PRO A 1 28  ? 2.956   20.942  3.040   1.00 12.65 ?  30  PRO A CA  1 
ATOM   210  C  C   . PRO A 1 28  ? 3.673   21.899  2.092   1.00 19.19 ?  30  PRO A C   1 
ATOM   211  O  O   . PRO A 1 28  ? 3.063   22.754  1.437   1.00 22.01 ?  30  PRO A O   1 
ATOM   212  C  CB  . PRO A 1 28  ? 1.432   21.131  2.998   1.00 15.95 ?  30  PRO A CB  1 
ATOM   213  C  CG  . PRO A 1 28  ? 1.163   22.142  4.063   1.00 18.04 ?  30  PRO A CG  1 
ATOM   214  C  CD  . PRO A 1 28  ? 2.141   21.798  5.188   1.00 16.34 ?  30  PRO A CD  1 
ATOM   215  N  N   . ALA A 1 29  ? 4.984   21.716  1.953   1.00 14.83 ?  31  ALA A N   1 
ATOM   216  C  CA  . ALA A 1 29  ? 5.769   22.490  0.996   1.00 13.90 ?  31  ALA A CA  1 
ATOM   217  C  C   . ALA A 1 29  ? 5.411   22.097  -0.440  1.00 12.88 ?  31  ALA A C   1 
ATOM   218  O  O   . ALA A 1 29  ? 5.030   20.960  -0.704  1.00 11.89 ?  31  ALA A O   1 
ATOM   219  C  CB  . ALA A 1 29  ? 7.263   22.261  1.234   1.00 13.29 ?  31  ALA A CB  1 
ATOM   220  N  N   . PRO A 1 30  ? 5.545   23.011  -1.393  1.00 11.73 ?  32  PRO A N   1 
ATOM   221  C  CA  . PRO A 1 30  ? 5.213   22.677  -2.782  1.00 11.02 ?  32  PRO A CA  1 
ATOM   222  C  C   . PRO A 1 30  ? 6.201   21.683  -3.366  1.00 10.96 ?  32  PRO A C   1 
ATOM   223  O  O   . PRO A 1 30  ? 7.426   21.906  -3.344  1.00 12.47 ?  32  PRO A O   1 
ATOM   224  C  CB  . PRO A 1 30  ? 5.281   24.030  -3.505  1.00 13.59 ?  32  PRO A CB  1 
ATOM   225  C  CG  . PRO A 1 30  ? 6.132   24.882  -2.634  1.00 14.81 ?  32  PRO A CG  1 
ATOM   226  C  CD  . PRO A 1 30  ? 5.868   24.438  -1.222  1.00 13.94 ?  32  PRO A CD  1 
ATOM   227  N  N   . PRO A 1 31  ? 5.704   20.574  -3.905  1.00 10.33 ?  33  PRO A N   1 
ATOM   228  C  CA  . PRO A 1 31  ? 6.559   19.720  -4.742  1.00 10.05 ?  33  PRO A CA  1 
ATOM   229  C  C   . PRO A 1 31  ? 7.106   20.495  -5.929  1.00 12.08 ?  33  PRO A C   1 
ATOM   230  O  O   . PRO A 1 31  ? 6.499   21.451  -6.415  1.00 11.60 ?  33  PRO A O   1 
ATOM   231  C  CB  . PRO A 1 31  ? 5.611   18.613  -5.212  1.00 12.40 ?  33  PRO A CB  1 
ATOM   232  C  CG  . PRO A 1 31  ? 4.440   18.655  -4.218  1.00 15.41 ?  33  PRO A CG  1 
ATOM   233  C  CD  . PRO A 1 31  ? 4.301   20.118  -3.900  1.00 11.64 ?  33  PRO A CD  1 
ATOM   234  N  N   . LEU A 1 32  ? 8.274   20.067  -6.398  1.00 10.13 ?  34  LEU A N   1 
ATOM   235  C  CA  . LEU A 1 32  ? 8.764   20.537  -7.686  1.00 9.21  ?  34  LEU A CA  1 
ATOM   236  C  C   . LEU A 1 32  ? 7.899   19.967  -8.804  1.00 10.36 ?  34  LEU A C   1 
ATOM   237  O  O   . LEU A 1 32  ? 7.600   18.769  -8.828  1.00 12.34 ?  34  LEU A O   1 
ATOM   238  C  CB  . LEU A 1 32  ? 10.221  20.117  -7.882  1.00 9.77  ?  34  LEU A CB  1 
ATOM   239  C  CG  . LEU A 1 32  ? 11.168  20.743  -6.851  1.00 14.97 ?  34  LEU A CG  1 
ATOM   240  C  CD1 . LEU A 1 32  ? 12.527  20.067  -6.900  1.00 13.36 ?  34  LEU A CD1 1 
ATOM   241  C  CD2 . LEU A 1 32  ? 11.289  22.245  -7.115  1.00 21.59 ?  34  LEU A CD2 1 
ATOM   242  N  N   . ASP A 1 33  ? 7.442   20.844  -9.702  1.00 11.45 ?  35  ASP A N   1 
ATOM   243  C  CA  . ASP A 1 33  ? 6.735   20.404  -10.902 1.00 11.80 ?  35  ASP A CA  1 
ATOM   244  C  C   . ASP A 1 33  ? 7.533   19.402  -11.720 1.00 13.37 ?  35  ASP A C   1 
ATOM   245  O  O   . ASP A 1 33  ? 6.995   18.384  -12.181 1.00 10.07 ?  35  ASP A O   1 
ATOM   246  C  CB  . ASP A 1 33  ? 6.378   21.621  -11.750 1.00 11.34 ?  35  ASP A CB  1 
ATOM   247  C  CG  . ASP A 1 33  ? 5.861   21.237  -13.118 1.00 13.16 ?  35  ASP A CG  1 
ATOM   248  O  OD1 . ASP A 1 33  ? 4.772   20.638  -13.219 1.00 14.10 ?  35  ASP A OD1 1 
ATOM   249  O  OD2 . ASP A 1 33  ? 6.556   21.600  -14.093 1.00 13.23 ?  35  ASP A OD2 1 
ATOM   250  N  N   . ASP A 1 34  ? 8.814   19.681  -11.933 1.00 10.55 ?  36  ASP A N   1 
ATOM   251  C  CA  . ASP A 1 34  ? 9.630   18.880  -12.837 1.00 10.69 ?  36  ASP A CA  1 
ATOM   252  C  C   . ASP A 1 34  ? 10.958  18.628  -12.145 1.00 12.61 ?  36  ASP A C   1 
ATOM   253  O  O   . ASP A 1 34  ? 11.950  19.318  -12.408 1.00 10.77 ?  36  ASP A O   1 
ATOM   254  C  CB  . ASP A 1 34  ? 9.794   19.578  -14.189 1.00 12.64 ?  36  ASP A CB  1 
ATOM   255  C  CG  . ASP A 1 34  ? 10.227  18.627  -15.287 1.00 13.96 ?  36  ASP A CG  1 
ATOM   256  O  OD1 . ASP A 1 34  ? 11.038  17.702  -15.014 1.00 14.12 ?  36  ASP A OD1 1 
ATOM   257  O  OD2 . ASP A 1 34  ? 9.754   18.797  -16.429 1.00 15.56 ?  36  ASP A OD2 1 
ATOM   258  N  N   . PRO A 1 35  ? 11.010  17.649  -11.242 1.00 10.25 ?  37  PRO A N   1 
ATOM   259  C  CA  . PRO A 1 35  ? 12.242  17.468  -10.454 1.00 10.86 ?  37  PRO A CA  1 
ATOM   260  C  C   . PRO A 1 35  ? 13.422  17.037  -11.300 1.00 10.17 ?  37  PRO A C   1 
ATOM   261  O  O   . PRO A 1 35  ? 14.556  17.415  -10.979 1.00 10.71 ?  37  PRO A O   1 
ATOM   262  C  CB  . PRO A 1 35  ? 11.862  16.402  -9.408  1.00 13.09 ?  37  PRO A CB  1 
ATOM   263  C  CG  . PRO A 1 35  ? 10.605  15.766  -9.904  1.00 12.76 ?  37  PRO A CG  1 
ATOM   264  C  CD  . PRO A 1 35  ? 9.916   16.752  -10.817 1.00 13.24 ?  37  PRO A CD  1 
ATOM   265  N  N   . GLU A 1 36  ? 13.200  16.287  -12.384 1.00 11.92 ?  38  GLU A N   1 
ATOM   266  C  CA  . GLU A 1 36  ? 14.333  15.926  -13.231 1.00 10.34 ?  38  GLU A CA  1 
ATOM   267  C  C   . GLU A 1 36  ? 14.902  17.164  -13.921 1.00 9.18  ?  38  GLU A C   1 
ATOM   268  O  O   . GLU A 1 36  ? 16.126  17.325  -14.012 1.00 9.94  ?  38  GLU A O   1 
ATOM   269  C  CB  . GLU A 1 36  ? 13.922  14.862  -14.254 1.00 13.41 ?  38  GLU A CB  1 
ATOM   270  C  CG  . GLU A 1 36  ? 15.126  14.179  -14.921 1.00 13.41 ?  38  GLU A CG  1 
ATOM   271  C  CD  . GLU A 1 36  ? 14.747  12.979  -15.786 1.00 19.96 ?  38  GLU A CD  1 
ATOM   272  O  OE1 . GLU A 1 36  ? 15.573  12.574  -16.636 1.00 21.64 ?  38  GLU A OE1 1 
ATOM   273  O  OE2 . GLU A 1 36  ? 13.637  12.435  -15.622 1.00 24.10 ?  38  GLU A OE2 1 
ATOM   274  N  N   . ALA A 1 37  ? 14.025  18.062  -14.399 1.00 10.93 ?  39  ALA A N   1 
ATOM   275  C  CA  . ALA A 1 37  ? 14.486  19.332  -14.953 1.00 10.42 ?  39  ALA A CA  1 
ATOM   276  C  C   . ALA A 1 37  ? 15.253  20.139  -13.913 1.00 9.78  ?  39  ALA A C   1 
ATOM   277  O  O   . ALA A 1 37  ? 16.228  20.825  -14.243 1.00 10.74 ?  39  ALA A O   1 
ATOM   278  C  CB  . ALA A 1 37  ? 13.291  20.137  -15.481 1.00 11.28 ?  39  ALA A CB  1 
ATOM   279  N  N   . GLU A 1 38  ? 14.819  20.072  -12.651 1.00 9.28  ?  40  GLU A N   1 
ATOM   280  C  CA  . GLU A 1 38  ? 15.520  20.775  -11.585 1.00 11.44 ?  40  GLU A CA  1 
ATOM   281  C  C   . GLU A 1 38  ? 16.889  20.156  -11.329 1.00 11.19 ?  40  GLU A C   1 
ATOM   282  O  O   . GLU A 1 38  ? 17.872  20.882  -11.142 1.00 9.63  ?  40  GLU A O   1 
ATOM   283  C  CB  . GLU A 1 38  ? 14.681  20.780  -10.304 1.00 8.17  ?  40  GLU A CB  1 
ATOM   284  C  CG  . GLU A 1 38  ? 15.255  21.668  -9.176  1.00 12.64 ?  40  GLU A CG  1 
ATOM   285  C  CD  . GLU A 1 38  ? 15.439  23.119  -9.592  1.00 22.49 ?  40  GLU A CD  1 
ATOM   286  O  OE1 . GLU A 1 38  ? 16.368  23.766  -9.054  1.00 25.14 ?  40  GLU A OE1 1 
ATOM   287  O  OE2 . GLU A 1 38  ? 14.673  23.606  -10.458 1.00 20.29 ?  40  GLU A OE2 1 
ATOM   288  N  N   . VAL A 1 39  ? 16.978  18.819  -11.336 1.00 11.94 ?  41  VAL A N   1 
ATOM   289  C  CA  . VAL A 1 39  ? 18.286  18.175  -11.218 1.00 9.57  ?  41  VAL A CA  1 
ATOM   290  C  C   . VAL A 1 39  ? 19.219  18.674  -12.314 1.00 9.53  ?  41  VAL A C   1 
ATOM   291  O  O   . VAL A 1 39  ? 20.380  19.014  -12.057 1.00 10.96 ?  41  VAL A O   1 
ATOM   292  C  CB  . VAL A 1 39  ? 18.163  16.640  -11.264 1.00 9.95  ?  41  VAL A CB  1 
ATOM   293  C  CG1 . VAL A 1 39  ? 19.579  16.028  -11.347 1.00 9.39  ?  41  VAL A CG1 1 
ATOM   294  C  CG2 . VAL A 1 39  ? 17.448  16.127  -10.023 1.00 10.31 ?  41  VAL A CG2 1 
ATOM   295  N  N   . VAL A 1 40  ? 18.716  18.732  -13.553 1.00 9.45  ?  42  VAL A N   1 
ATOM   296  C  CA  . VAL A 1 40  ? 19.518  19.240  -14.669 1.00 10.00 ?  42  VAL A CA  1 
ATOM   297  C  C   . VAL A 1 40  ? 20.029  20.645  -14.367 1.00 12.67 ?  42  VAL A C   1 
ATOM   298  O  O   . VAL A 1 40  ? 21.213  20.943  -14.557 1.00 12.64 ?  42  VAL A O   1 
ATOM   299  C  CB  . VAL A 1 40  ? 18.699  19.209  -15.975 1.00 14.72 ?  42  VAL A CB  1 
ATOM   300  C  CG1 . VAL A 1 40  ? 19.403  20.028  -17.057 1.00 14.69 ?  42  VAL A CG1 1 
ATOM   301  C  CG2 . VAL A 1 40  ? 18.447  17.771  -16.422 1.00 12.21 ?  42  VAL A CG2 1 
ATOM   302  N  N   . ARG A 1 41  ? 19.151  21.525  -13.874 1.00 9.24  ?  43  ARG A N   1 
ATOM   303  C  CA  . ARG A 1 41  ? 19.578  22.887  -13.553 1.00 8.87  ?  43  ARG A CA  1 
ATOM   304  C  C   . ARG A 1 41  ? 20.615  22.900  -12.438 1.00 11.62 ?  43  ARG A C   1 
ATOM   305  O  O   . ARG A 1 41  ? 21.572  23.678  -12.487 1.00 11.80 ?  43  ARG A O   1 
ATOM   306  C  CB  . ARG A 1 41  ? 18.378  23.755  -13.165 1.00 11.47 ?  43  ARG A CB  1 
ATOM   307  C  CG  . ARG A 1 41  ? 17.535  24.184  -14.357 1.00 14.54 ?  43  ARG A CG  1 
ATOM   308  C  CD  . ARG A 1 41  ? 16.399  25.104  -13.952 1.00 13.46 ?  43  ARG A CD  1 
ATOM   309  N  NE  . ARG A 1 41  ? 15.245  24.390  -13.406 1.00 15.33 ?  43  ARG A NE  1 
ATOM   310  C  CZ  . ARG A 1 41  ? 14.261  23.920  -14.164 1.00 14.34 ?  43  ARG A CZ  1 
ATOM   311  N  NH1 . ARG A 1 41  ? 14.340  24.039  -15.483 1.00 15.40 ?  43  ARG A NH1 1 
ATOM   312  N  NH2 . ARG A 1 41  ? 13.234  23.299  -13.614 1.00 14.54 ?  43  ARG A NH2 1 
ATOM   313  N  N   . CYS A 1 42  ? 20.450  22.039  -11.432 1.00 11.64 ?  44  CYS A N   1 
ATOM   314  C  CA  . CYS A 1 42  ? 21.374  22.061  -10.311 1.00 9.44  ?  44  CYS A CA  1 
ATOM   315  C  C   . CYS A 1 42  ? 22.728  21.487  -10.699 1.00 9.50  ?  44  CYS A C   1 
ATOM   316  O  O   . CYS A 1 42  ? 23.745  21.861  -10.104 1.00 10.57 ?  44  CYS A O   1 
ATOM   317  C  CB  . CYS A 1 42  ? 20.790  21.291  -9.128  1.00 10.89 ?  44  CYS A CB  1 
ATOM   318  S  SG  . CYS A 1 42  ? 19.388  22.178  -8.344  1.00 15.67 ?  44  CYS A SG  1 
ATOM   319  N  N   . LEU A 1 43  ? 22.763  20.575  -11.676 1.00 10.60 ?  45  LEU A N   1 
ATOM   320  C  CA  . LEU A 1 43  ? 24.048  20.071  -12.154 1.00 13.24 ?  45  LEU A CA  1 
ATOM   321  C  C   . LEU A 1 43  ? 24.832  21.153  -12.885 1.00 13.74 ?  45  LEU A C   1 
ATOM   322  O  O   . LEU A 1 43  ? 26.071  21.152  -12.855 1.00 13.14 ?  45  LEU A O   1 
ATOM   323  C  CB  . LEU A 1 43  ? 23.849  18.879  -13.085 1.00 11.20 ?  45  LEU A CB  1 
ATOM   324  C  CG  . LEU A 1 43  ? 23.169  17.610  -12.580 1.00 19.19 ?  45  LEU A CG  1 
ATOM   325  C  CD1 . LEU A 1 43  ? 23.537  16.389  -13.422 1.00 12.36 ?  45  LEU A CD1 1 
ATOM   326  C  CD2 . LEU A 1 43  ? 23.414  17.354  -11.123 1.00 17.66 ?  45  LEU A CD2 1 
ATOM   327  N  N   . ALA A 1 44  ? 24.123  22.067  -13.552 1.00 13.83 ?  46  ALA A N   1 
ATOM   328  C  CA  . ALA A 1 44  ? 24.760  23.162  -14.271 1.00 12.17 ?  46  ALA A CA  1 
ATOM   329  C  C   . ALA A 1 44  ? 25.135  24.307  -13.342 1.00 12.89 ?  46  ALA A C   1 
ATOM   330  O  O   . ALA A 1 44  ? 26.057  25.071  -13.648 1.00 12.91 ?  46  ALA A O   1 
ATOM   331  C  CB  . ALA A 1 44  ? 23.832  23.671  -15.377 1.00 13.96 ?  46  ALA A CB  1 
ATOM   332  N  N   . GLU A 1 45  ? 24.445  24.437  -12.212 1.00 10.82 ?  47  GLU A N   1 
ATOM   333  C  CA  . GLU A 1 45  ? 24.627  25.560  -11.291 1.00 15.48 ?  47  GLU A CA  1 
ATOM   334  C  C   . GLU A 1 45  ? 24.554  25.028  -9.868  1.00 11.90 ?  47  GLU A C   1 
ATOM   335  O  O   . GLU A 1 45  ? 23.577  25.256  -9.145  1.00 14.39 ?  47  GLU A O   1 
ATOM   336  C  CB  . GLU A 1 45  ? 23.562  26.626  -11.538 1.00 13.94 ?  47  GLU A CB  1 
ATOM   337  C  CG  . GLU A 1 45  ? 23.916  28.002  -11.063 1.00 29.76 ?  47  GLU A CG  1 
ATOM   338  C  CD  . GLU A 1 45  ? 22.738  28.952  -11.181 1.00 48.83 ?  47  GLU A CD  1 
ATOM   339  O  OE1 . GLU A 1 45  ? 22.074  29.216  -10.155 1.00 55.65 ?  47  GLU A OE1 1 
ATOM   340  O  OE2 . GLU A 1 45  ? 22.462  29.413  -12.309 1.00 48.08 ?  47  GLU A OE2 1 
ATOM   341  N  N   . PRO A 1 46  ? 25.563  24.275  -9.446  1.00 10.07 ?  48  PRO A N   1 
ATOM   342  C  CA  . PRO A 1 46  ? 25.490  23.620  -8.137  1.00 9.57  ?  48  PRO A CA  1 
ATOM   343  C  C   . PRO A 1 46  ? 25.968  24.493  -6.988  1.00 11.86 ?  48  PRO A C   1 
ATOM   344  O  O   . PRO A 1 46  ? 26.393  25.640  -7.172  1.00 12.97 ?  48  PRO A O   1 
ATOM   345  C  CB  . PRO A 1 46  ? 26.395  22.399  -8.317  1.00 10.93 ?  48  PRO A CB  1 
ATOM   346  C  CG  . PRO A 1 46  ? 27.421  22.847  -9.320  1.00 14.94 ?  48  PRO A CG  1 
ATOM   347  C  CD  . PRO A 1 46  ? 26.756  23.864  -10.214 1.00 13.61 ?  48  PRO A CD  1 
ATOM   348  N  N   . ILE A 1 47  ? 25.897  23.924  -5.789  1.00 11.65 ?  49  ILE A N   1 
ATOM   349  C  CA  . ILE A 1 47  ? 26.269  24.590  -4.545  1.00 11.37 ?  49  ILE A CA  1 
ATOM   350  C  C   . ILE A 1 47  ? 27.712  24.214  -4.208  1.00 13.24 ?  49  ILE A C   1 
ATOM   351  O  O   . ILE A 1 47  ? 28.013  23.037  -3.970  1.00 13.71 ?  49  ILE A O   1 
ATOM   352  C  CB  . ILE A 1 47  ? 25.325  24.183  -3.398  1.00 11.00 ?  49  ILE A CB  1 
ATOM   353  C  CG1 . ILE A 1 47  ? 23.843  24.513  -3.703  1.00 13.30 ?  49  ILE A CG1 1 
ATOM   354  C  CG2 . ILE A 1 47  ? 25.790  24.771  -2.079  1.00 12.93 ?  49  ILE A CG2 1 
ATOM   355  C  CD1 . ILE A 1 47  ? 22.841  23.726  -2.837  1.00 16.92 ?  49  ILE A CD1 1 
ATOM   356  N  N   . GLY A 1 48  ? 28.616  25.199  -4.198  1.00 11.99 ?  50  GLY A N   1 
ATOM   357  C  CA  . GLY A 1 48  ? 29.971  24.966  -3.709  1.00 13.10 ?  50  GLY A CA  1 
ATOM   358  C  C   . GLY A 1 48  ? 30.834  24.040  -4.535  1.00 12.76 ?  50  GLY A C   1 
ATOM   359  O  O   . GLY A 1 48  ? 31.821  23.499  -4.024  1.00 14.72 ?  50  GLY A O   1 
ATOM   360  N  N   . SER A 1 49  ? 30.504  23.857  -5.808  1.00 14.46 ?  51  SER A N   1 
ATOM   361  C  CA  . SER A 1 49  ? 31.139  22.924  -6.716  1.00 11.82 ?  51  SER A CA  1 
ATOM   362  C  C   . SER A 1 49  ? 31.191  23.567  -8.091  1.00 12.69 ?  51  SER A C   1 
ATOM   363  O  O   . SER A 1 49  ? 30.357  24.424  -8.395  1.00 13.01 ?  51  SER A O   1 
ATOM   364  C  CB  . SER A 1 49  ? 30.318  21.621  -6.792  1.00 14.51 ?  51  SER A CB  1 
ATOM   365  O  OG  . SER A 1 49  ? 30.877  20.736  -7.728  1.00 24.64 ?  51  SER A OG  1 
ATOM   366  N  N   . PRO A 1 50  ? 32.126  23.172  -8.954  1.00 11.94 ?  52  PRO A N   1 
ATOM   367  C  CA  . PRO A 1 50  ? 31.960  23.512  -10.361 1.00 13.77 ?  52  PRO A CA  1 
ATOM   368  C  C   . PRO A 1 50  ? 30.803  22.719  -10.942 1.00 13.44 ?  52  PRO A C   1 
ATOM   369  O  O   . PRO A 1 50  ? 30.346  21.743  -10.325 1.00 11.64 ?  52  PRO A O   1 
ATOM   370  C  CB  . PRO A 1 50  ? 33.312  23.141  -10.998 1.00 17.19 ?  52  PRO A CB  1 
ATOM   371  C  CG  . PRO A 1 50  ? 33.962  22.238  -10.054 1.00 17.90 ?  52  PRO A CG  1 
ATOM   372  C  CD  . PRO A 1 50  ? 33.424  22.528  -8.677  1.00 12.51 ?  52  PRO A CD  1 
ATOM   373  N  N   . PRO A 1 51  ? 30.256  23.142  -12.082 1.00 15.18 ?  53  PRO A N   1 
ATOM   374  C  CA  . PRO A 1 51  ? 29.255  22.313  -12.775 1.00 13.09 ?  53  PRO A CA  1 
ATOM   375  C  C   . PRO A 1 51  ? 29.772  20.897  -12.982 1.00 13.36 ?  53  PRO A C   1 
ATOM   376  O  O   . PRO A 1 51  ? 30.964  20.683  -13.209 1.00 13.93 ?  53  PRO A O   1 
ATOM   377  C  CB  . PRO A 1 51  ? 29.051  23.042  -14.109 1.00 13.99 ?  53  PRO A CB  1 
ATOM   378  C  CG  . PRO A 1 51  ? 29.434  24.478  -13.810 1.00 15.05 ?  53  PRO A CG  1 
ATOM   379  C  CD  . PRO A 1 51  ? 30.569  24.384  -12.814 1.00 14.92 ?  53  PRO A CD  1 
ATOM   380  N  N   . LEU A 1 52  ? 28.857  19.921  -12.902 1.00 11.50 ?  54  LEU A N   1 
ATOM   381  C  CA  . LEU A 1 52  ? 29.257  18.524  -13.050 1.00 10.20 ?  54  LEU A CA  1 
ATOM   382  C  C   . LEU A 1 52  ? 29.967  18.274  -14.376 1.00 11.94 ?  54  LEU A C   1 
ATOM   383  O  O   . LEU A 1 52  ? 30.921  17.488  -14.434 1.00 11.61 ?  54  LEU A O   1 
ATOM   384  C  CB  . LEU A 1 52  ? 28.041  17.603  -12.914 1.00 10.26 ?  54  LEU A CB  1 
ATOM   385  C  CG  . LEU A 1 52  ? 28.409  16.111  -13.009 1.00 10.79 ?  54  LEU A CG  1 
ATOM   386  C  CD1 . LEU A 1 52  ? 29.427  15.709  -11.917 1.00 11.11 ?  54  LEU A CD1 1 
ATOM   387  C  CD2 . LEU A 1 52  ? 27.161  15.231  -12.931 1.00 10.92 ?  54  LEU A CD2 1 
ATOM   388  N  N   . LEU A 1 53  ? 29.528  18.930  -15.449 1.00 11.17 ?  55  LEU A N   1 
ATOM   389  C  CA  . LEU A 1 53  ? 30.165  18.706  -16.746 1.00 13.19 ?  55  LEU A CA  1 
ATOM   390  C  C   . LEU A 1 53  ? 31.638  19.095  -16.700 1.00 16.52 ?  55  LEU A C   1 
ATOM   391  O  O   . LEU A 1 53  ? 32.500  18.384  -17.234 1.00 12.84 ?  55  LEU A O   1 
ATOM   392  C  CB  . LEU A 1 53  ? 29.435  19.504  -17.829 1.00 14.59 ?  55  LEU A CB  1 
ATOM   393  C  CG  . LEU A 1 53  ? 29.879  19.276  -19.277 1.00 16.06 ?  55  LEU A CG  1 
ATOM   394  C  CD1 . LEU A 1 53  ? 29.468  17.898  -19.718 1.00 15.40 ?  55  LEU A CD1 1 
ATOM   395  C  CD2 . LEU A 1 53  ? 29.281  20.314  -20.214 1.00 15.96 ?  55  LEU A CD2 1 
ATOM   396  N  N   . ASP A 1 54  ? 31.943  20.200  -16.022 1.00 16.90 ?  56  ASP A N   1 
ATOM   397  C  CA  . ASP A 1 54  ? 33.325  20.645  -15.884 1.00 14.89 ?  56  ASP A CA  1 
ATOM   398  C  C   . ASP A 1 54  ? 34.116  19.741  -14.942 1.00 18.80 ?  56  ASP A C   1 
ATOM   399  O  O   . ASP A 1 54  ? 35.301  19.480  -15.184 1.00 19.71 ?  56  ASP A O   1 
ATOM   400  C  CB  . ASP A 1 54  ? 33.335  22.093  -15.410 1.00 14.96 ?  56  ASP A CB  1 
ATOM   401  C  CG  . ASP A 1 54  ? 32.684  23.031  -16.419 1.00 23.80 ?  56  ASP A CG  1 
ATOM   402  O  OD1 . ASP A 1 54  ? 31.991  23.985  -16.005 1.00 34.27 ?  56  ASP A OD1 1 
ATOM   403  O  OD2 . ASP A 1 54  ? 32.829  22.781  -17.631 1.00 32.49 ?  56  ASP A OD2 1 
ATOM   404  N  N   . LEU A 1 55  ? 33.479  19.254  -13.865 1.00 15.03 ?  57  LEU A N   1 
ATOM   405  C  CA  A LEU A 1 55  ? 34.139  18.304  -12.982 0.50 17.31 ?  57  LEU A CA  1 
ATOM   406  C  CA  B LEU A 1 55  ? 34.126  18.280  -12.978 0.50 17.31 ?  57  LEU A CA  1 
ATOM   407  C  C   . LEU A 1 55  ? 34.515  17.026  -13.729 1.00 17.59 ?  57  LEU A C   1 
ATOM   408  O  O   . LEU A 1 55  ? 35.560  16.426  -13.459 1.00 17.42 ?  57  LEU A O   1 
ATOM   409  C  CB  A LEU A 1 55  ? 33.203  17.997  -11.817 0.50 16.61 ?  57  LEU A CB  1 
ATOM   410  C  CB  B LEU A 1 55  ? 33.217  17.804  -11.843 0.50 16.72 ?  57  LEU A CB  1 
ATOM   411  C  CG  A LEU A 1 55  ? 33.685  17.628  -10.430 0.50 19.99 ?  57  LEU A CG  1 
ATOM   412  C  CG  B LEU A 1 55  ? 33.267  18.104  -10.344 0.50 19.03 ?  57  LEU A CG  1 
ATOM   413  C  CD1 A LEU A 1 55  ? 34.872  18.504  -10.043 0.50 17.29 ?  57  LEU A CD1 1 
ATOM   414  C  CD1 B LEU A 1 55  ? 34.674  17.903  -9.707  0.50 20.34 ?  57  LEU A CD1 1 
ATOM   415  C  CD2 A LEU A 1 55  ? 32.504  17.817  -9.475  0.50 13.85 ?  57  LEU A CD2 1 
ATOM   416  C  CD2 B LEU A 1 55  ? 32.537  19.329  -9.899  0.50 23.70 ?  57  LEU A CD2 1 
ATOM   417  N  N   . ALA A 1 56  ? 33.647  16.579  -14.642 1.00 14.33 ?  58  ALA A N   1 
ATOM   418  C  CA  . ALA A 1 56  ? 33.823  15.299  -15.308 1.00 14.58 ?  58  ALA A CA  1 
ATOM   419  C  C   . ALA A 1 56  ? 34.806  15.365  -16.469 1.00 16.88 ?  58  ALA A C   1 
ATOM   420  O  O   . ALA A 1 56  ? 35.233  14.314  -16.951 1.00 18.02 ?  58  ALA A O   1 
ATOM   421  C  CB  . ALA A 1 56  ? 32.461  14.772  -15.787 1.00 12.85 ?  58  ALA A CB  1 
ATOM   422  N  N   . ARG A 1 57  ? 35.190  16.566  -16.897 1.00 17.61 ?  59  ARG A N   1 
ATOM   423  C  CA  . ARG A 1 57  ? 36.130  16.721  -17.998 1.00 20.13 ?  59  ARG A CA  1 
ATOM   424  C  C   . ARG A 1 57  ? 37.419  15.971  -17.711 1.00 17.72 ?  59  ARG A C   1 
ATOM   425  O  O   . ARG A 1 57  ? 38.045  16.163  -16.662 1.00 20.04 ?  59  ARG A O   1 
ATOM   426  C  CB  . ARG A 1 57  ? 36.430  18.205  -18.223 1.00 22.45 ?  59  ARG A CB  1 
ATOM   427  N  N   . GLY A 1 58  ? 37.814  15.112  -18.651 1.00 26.74 ?  60  GLY A N   1 
ATOM   428  C  CA  . GLY A 1 58  ? 39.074  14.406  -18.543 1.00 24.34 ?  60  GLY A CA  1 
ATOM   429  C  C   . GLY A 1 58  ? 39.114  13.292  -17.524 1.00 29.47 ?  60  GLY A C   1 
ATOM   430  O  O   . GLY A 1 58  ? 40.195  12.754  -17.262 1.00 31.28 ?  60  GLY A O   1 
ATOM   431  N  N   . LYS A 1 59  ? 37.982  12.930  -16.926 1.00 18.53 ?  61  LYS A N   1 
ATOM   432  C  CA  . LYS A 1 59  ? 37.953  11.824  -15.982 1.00 18.96 ?  61  LYS A CA  1 
ATOM   433  C  C   . LYS A 1 59  ? 37.791  10.517  -16.747 1.00 14.87 ?  61  LYS A C   1 
ATOM   434  O  O   . LYS A 1 59  ? 37.038  10.446  -17.728 1.00 20.34 ?  61  LYS A O   1 
ATOM   435  C  CB  . LYS A 1 59  ? 36.818  12.011  -14.973 1.00 14.19 ?  61  LYS A CB  1 
ATOM   436  C  CG  . LYS A 1 59  ? 36.948  13.275  -14.115 1.00 17.24 ?  61  LYS A CG  1 
ATOM   437  C  CD  . LYS A 1 59  ? 38.230  13.268  -13.264 1.00 17.48 ?  61  LYS A CD  1 
ATOM   438  C  CE  . LYS A 1 59  ? 38.446  14.560  -12.489 1.00 30.15 ?  61  LYS A CE  1 
ATOM   439  N  NZ  . LYS A 1 59  ? 38.123  15.805  -13.226 1.00 28.96 ?  61  LYS A NZ  1 
ATOM   440  N  N   . ARG A 1 60  ? 38.515  9.481   -16.304 1.00 14.45 ?  62  ARG A N   1 
ATOM   441  C  CA  . ARG A 1 60  ? 38.523  8.198   -16.999 1.00 17.90 ?  62  ARG A CA  1 
ATOM   442  C  C   . ARG A 1 60  ? 37.518  7.198   -16.439 1.00 20.56 ?  62  ARG A C   1 
ATOM   443  O  O   . ARG A 1 60  ? 37.112  6.279   -17.160 1.00 23.28 ?  62  ARG A O   1 
ATOM   444  C  CB  . ARG A 1 60  ? 39.923  7.568   -16.947 1.00 27.47 ?  62  ARG A CB  1 
ATOM   445  C  CG  . ARG A 1 60  ? 41.013  8.370   -17.642 1.00 28.93 ?  62  ARG A CG  1 
ATOM   446  C  CD  . ARG A 1 60  ? 42.417  7.953   -17.160 1.00 38.00 ?  62  ARG A CD  1 
ATOM   447  N  NE  . ARG A 1 60  ? 42.620  8.191   -15.729 1.00 44.08 ?  62  ARG A NE  1 
ATOM   448  C  CZ  . ARG A 1 60  ? 43.280  7.375   -14.910 1.00 48.82 ?  62  ARG A CZ  1 
ATOM   449  N  NH1 . ARG A 1 60  ? 43.815  6.251   -15.373 1.00 49.09 ?  62  ARG A NH1 1 
ATOM   450  N  NH2 . ARG A 1 60  ? 43.412  7.687   -13.622 1.00 42.88 ?  62  ARG A NH2 1 
ATOM   451  N  N   . SER A 1 61  ? 37.116  7.348   -15.183 1.00 15.33 ?  63  SER A N   1 
ATOM   452  C  CA  . SER A 1 61  ? 36.210  6.397   -14.552 1.00 13.27 ?  63  SER A CA  1 
ATOM   453  C  C   . SER A 1 61  ? 35.355  7.147   -13.546 1.00 15.47 ?  63  SER A C   1 
ATOM   454  O  O   . SER A 1 61  ? 35.755  8.197   -13.046 1.00 12.35 ?  63  SER A O   1 
ATOM   455  C  CB  . SER A 1 61  ? 36.971  5.280   -13.845 1.00 14.95 ?  63  SER A CB  1 
ATOM   456  O  OG  . SER A 1 61  ? 37.826  5.824   -12.845 1.00 16.03 ?  63  SER A OG  1 
ATOM   457  N  N   . ALA A 1 62  ? 34.168  6.609   -13.265 1.00 12.99 ?  64  ALA A N   1 
ATOM   458  C  CA  . ALA A 1 62  ? 33.266  7.239   -12.309 1.00 13.67 ?  64  ALA A CA  1 
ATOM   459  C  C   . ALA A 1 62  ? 32.620  6.163   -11.459 1.00 11.01 ?  64  ALA A C   1 
ATOM   460  O  O   . ALA A 1 62  ? 32.333  5.071   -11.953 1.00 13.48 ?  64  ALA A O   1 
ATOM   461  C  CB  . ALA A 1 62  ? 32.179  8.069   -13.013 1.00 14.63 ?  64  ALA A CB  1 
ATOM   462  N  N   . CYS A 1 63  ? 32.402  6.463   -10.180 1.00 8.68  ?  65  CYS A N   1 
ATOM   463  C  CA  . CYS A 1 63  ? 31.619  5.591   -9.310  1.00 8.75  ?  65  CYS A CA  1 
ATOM   464  C  C   . CYS A 1 63  ? 30.495  6.434   -8.738  1.00 8.52  ?  65  CYS A C   1 
ATOM   465  O  O   . CYS A 1 63  ? 30.755  7.495   -8.157  1.00 9.63  ?  65  CYS A O   1 
ATOM   466  C  CB  . CYS A 1 63  ? 32.482  4.978   -8.199  1.00 8.63  ?  65  CYS A CB  1 
ATOM   467  S  SG  . CYS A 1 63  ? 31.576  3.805   -7.118  1.00 11.80 ?  65  CYS A SG  1 
ATOM   468  N  N   . ILE A 1 64  ? 29.257  5.977   -8.928  1.00 9.48  ?  66  ILE A N   1 
ATOM   469  C  CA  . ILE A 1 64  ? 28.060  6.660   -8.442  1.00 7.31  ?  66  ILE A CA  1 
ATOM   470  C  C   . ILE A 1 64  ? 27.470  5.821   -7.322  1.00 9.55  ?  66  ILE A C   1 
ATOM   471  O  O   . ILE A 1 64  ? 27.058  4.680   -7.552  1.00 9.84  ?  66  ILE A O   1 
ATOM   472  C  CB  . ILE A 1 64  ? 27.024  6.866   -9.552  1.00 8.31  ?  66  ILE A CB  1 
ATOM   473  C  CG1 . ILE A 1 64  ? 27.639  7.609   -10.743 1.00 10.08 ?  66  ILE A CG1 1 
ATOM   474  C  CG2 . ILE A 1 64  ? 25.813  7.608   -8.981  1.00 10.78 ?  66  ILE A CG2 1 
ATOM   475  C  CD1 . ILE A 1 64  ? 26.722  7.591   -11.966 1.00 9.59  ?  66  ILE A CD1 1 
ATOM   476  N  N   . LEU A 1 65  ? 27.415  6.388   -6.117  1.00 6.62  ?  67  LEU A N   1 
ATOM   477  C  CA  . LEU A 1 65  ? 26.815  5.698   -4.986  1.00 8.57  ?  67  LEU A CA  1 
ATOM   478  C  C   . LEU A 1 65  ? 25.306  5.909   -5.002  1.00 9.32  ?  67  LEU A C   1 
ATOM   479  O  O   . LEU A 1 65  ? 24.836  7.046   -5.137  1.00 9.20  ?  67  LEU A O   1 
ATOM   480  C  CB  . LEU A 1 65  ? 27.374  6.236   -3.676  1.00 6.76  ?  67  LEU A CB  1 
ATOM   481  C  CG  . LEU A 1 65  ? 28.897  6.155   -3.552  1.00 7.26  ?  67  LEU A CG  1 
ATOM   482  C  CD1 . LEU A 1 65  ? 29.304  6.576   -2.160  1.00 10.71 ?  67  LEU A CD1 1 
ATOM   483  C  CD2 . LEU A 1 65  ? 29.406  4.740   -3.857  1.00 8.75  ?  67  LEU A CD2 1 
ATOM   484  N  N   . VAL A 1 66  ? 24.551  4.820   -4.826  1.00 7.50  ?  68  VAL A N   1 
ATOM   485  C  CA  . VAL A 1 66  ? 23.100  4.903   -4.706  1.00 8.19  ?  68  VAL A CA  1 
ATOM   486  C  C   . VAL A 1 66  ? 22.683  4.162   -3.440  1.00 10.56 ?  68  VAL A C   1 
ATOM   487  O  O   . VAL A 1 66  ? 23.359  3.238   -2.982  1.00 8.73  ?  68  VAL A O   1 
ATOM   488  C  CB  . VAL A 1 66  ? 22.357  4.330   -5.941  1.00 8.17  ?  68  VAL A CB  1 
ATOM   489  C  CG1 . VAL A 1 66  ? 22.681  5.156   -7.192  1.00 8.17  ?  68  VAL A CG1 1 
ATOM   490  C  CG2 . VAL A 1 66  ? 22.630  2.849   -6.125  1.00 9.91  ?  68  VAL A CG2 1 
ATOM   491  N  N   . CYS A 1 67  ? 21.566  4.585   -2.867  1.00 7.11  ?  69  CYS A N   1 
ATOM   492  C  CA  . CYS A 1 67  ? 21.020  3.914   -1.700  1.00 6.62  ?  69  CYS A CA  1 
ATOM   493  C  C   . CYS A 1 67  ? 20.451  2.554   -2.091  1.00 8.35  ?  69  CYS A C   1 
ATOM   494  O  O   . CYS A 1 67  ? 20.101  2.307   -3.253  1.00 9.31  ?  69  CYS A O   1 
ATOM   495  C  CB  . CYS A 1 67  ? 19.928  4.774   -1.066  1.00 8.34  ?  69  CYS A CB  1 
ATOM   496  S  SG  . CYS A 1 67  ? 20.558  6.297   -0.331  1.00 10.26 ?  69  CYS A SG  1 
ATOM   497  N  N   . ASP A 1 68  ? 20.350  1.661   -1.101  1.00 8.23  ?  70  ASP A N   1 
ATOM   498  C  CA  . ASP A 1 68  ? 19.757  0.356   -1.348  1.00 10.09 ?  70  ASP A CA  1 
ATOM   499  C  C   . ASP A 1 68  ? 18.230  0.437   -1.207  1.00 9.48  ?  70  ASP A C   1 
ATOM   500  O  O   . ASP A 1 68  ? 17.642  1.522   -1.176  1.00 6.95  ?  70  ASP A O   1 
ATOM   501  C  CB  . ASP A 1 68  ? 20.380  -0.709  -0.441  1.00 7.55  ?  70  ASP A CB  1 
ATOM   502  C  CG  . ASP A 1 68  ? 20.029  -0.543  1.037   1.00 9.68  ?  70  ASP A CG  1 
ATOM   503  O  OD1 . ASP A 1 68  ? 19.288  0.383   1.418   1.00 9.54  ?  70  ASP A OD1 1 
ATOM   504  O  OD2 . ASP A 1 68  ? 20.517  -1.366  1.840   1.00 11.20 ?  70  ASP A OD2 1 
ATOM   505  N  N   . ILE A 1 69  ? 17.567  -0.723  -1.112  1.00 8.89  ?  71  ILE A N   1 
ATOM   506  C  CA  . ILE A 1 69  ? 16.107  -0.751  -1.226  1.00 9.52  ?  71  ILE A CA  1 
ATOM   507  C  C   . ILE A 1 69  ? 15.429  -0.003  -0.080  1.00 9.10  ?  71  ILE A C   1 
ATOM   508  O  O   . ILE A 1 69  ? 14.322  0.522   -0.252  1.00 11.11 ?  71  ILE A O   1 
ATOM   509  C  CB  . ILE A 1 69  ? 15.611  -2.213  -1.312  1.00 9.12  ?  71  ILE A CB  1 
ATOM   510  C  CG1 . ILE A 1 69  ? 14.179  -2.295  -1.885  1.00 11.23 ?  71  ILE A CG1 1 
ATOM   511  C  CG2 . ILE A 1 69  ? 15.734  -2.923  0.037   1.00 10.24 ?  71  ILE A CG2 1 
ATOM   512  C  CD1 . ILE A 1 69  ? 14.038  -1.724  -3.262  1.00 9.86  ?  71  ILE A CD1 1 
ATOM   513  N  N   . THR A 1 70  ? 16.074  0.081   1.083   1.00 7.25  ?  72  THR A N   1 
ATOM   514  C  CA  . THR A 1 70  ? 15.466  0.634   2.290   1.00 7.31  ?  72  THR A CA  1 
ATOM   515  C  C   . THR A 1 70  ? 15.224  2.132   2.195   1.00 8.89  ?  72  THR A C   1 
ATOM   516  O  O   . THR A 1 70  ? 14.557  2.685   3.072   1.00 8.89  ?  72  THR A O   1 
ATOM   517  C  CB  . THR A 1 70  ? 16.336  0.353   3.526   1.00 7.80  ?  72  THR A CB  1 
ATOM   518  O  OG1 . THR A 1 70  ? 17.536  1.141   3.478   1.00 9.56  ?  72  THR A OG1 1 
ATOM   519  C  CG2 . THR A 1 70  ? 16.707  -1.142  3.604   1.00 11.29 ?  72  THR A CG2 1 
ATOM   520  N  N   . ARG A 1 71  ? 15.777  2.805   1.185   1.00 9.16  ?  73  ARG A N   1 
ATOM   521  C  CA  . ARG A 1 71  ? 15.541  4.233   0.990   1.00 7.27  ?  73  ARG A CA  1 
ATOM   522  C  C   . ARG A 1 71  ? 14.743  4.422   -0.283  1.00 8.25  ?  73  ARG A C   1 
ATOM   523  O  O   . ARG A 1 71  ? 15.198  3.994   -1.352  1.00 9.33  ?  73  ARG A O   1 
ATOM   524  C  CB  . ARG A 1 71  ? 16.850  5.034   0.904   1.00 6.89  ?  73  ARG A CB  1 
ATOM   525  C  CG  . ARG A 1 71  ? 17.946  4.609   1.918   1.00 9.86  ?  73  ARG A CG  1 
ATOM   526  C  CD  . ARG A 1 71  ? 17.428  4.696   3.305   1.00 10.83 ?  73  ARG A CD  1 
ATOM   527  N  NE  . ARG A 1 71  ? 18.451  4.996   4.313   1.00 8.77  ?  73  ARG A NE  1 
ATOM   528  C  CZ  . ARG A 1 71  ? 18.683  4.253   5.389   1.00 8.81  ?  73  ARG A CZ  1 
ATOM   529  N  NH1 . ARG A 1 71  ? 18.017  3.109   5.581   1.00 7.34  ?  73  ARG A NH1 1 
ATOM   530  N  NH2 . ARG A 1 71  ? 19.585  4.657   6.275   1.00 8.95  ?  73  ARG A NH2 1 
ATOM   531  N  N   . PRO A 1 72  ? 13.592  5.065   -0.230  1.00 7.21  ?  74  PRO A N   1 
ATOM   532  C  CA  . PRO A 1 72  ? 12.778  5.289   -1.432  1.00 7.18  ?  74  PRO A CA  1 
ATOM   533  C  C   . PRO A 1 72  ? 13.266  6.449   -2.300  1.00 9.56  ?  74  PRO A C   1 
ATOM   534  O  O   . PRO A 1 72  ? 12.484  7.315   -2.706  1.00 12.01 ?  74  PRO A O   1 
ATOM   535  C  CB  . PRO A 1 72  ? 11.391  5.574   -0.849  1.00 10.90 ?  74  PRO A CB  1 
ATOM   536  C  CG  . PRO A 1 72  ? 11.661  6.210   0.492   1.00 9.27  ?  74  PRO A CG  1 
ATOM   537  C  CD  . PRO A 1 72  ? 12.945  5.569   1.001   1.00 8.50  ?  74  PRO A CD  1 
ATOM   538  N  N   . VAL A 1 73  ? 14.563  6.459   -2.601  1.00 9.69  ?  75  VAL A N   1 
ATOM   539  C  CA  . VAL A 1 73  ? 15.083  7.484   -3.510  1.00 10.42 ?  75  VAL A CA  1 
ATOM   540  C  C   . VAL A 1 73  ? 14.492  7.271   -4.897  1.00 11.32 ?  75  VAL A C   1 
ATOM   541  O  O   . VAL A 1 73  ? 14.518  6.140   -5.410  1.00 10.11 ?  75  VAL A O   1 
ATOM   542  C  CB  . VAL A 1 73  ? 16.609  7.434   -3.569  1.00 8.98  ?  75  VAL A CB  1 
ATOM   543  C  CG1 . VAL A 1 73  ? 17.111  8.691   -4.267  1.00 12.59 ?  75  VAL A CG1 1 
ATOM   544  C  CG2 . VAL A 1 73  ? 17.222  7.277   -2.156  1.00 10.43 ?  75  VAL A CG2 1 
ATOM   545  N  N   . PRO A 1 74  ? 13.961  8.307   -5.544  1.00 10.39 ?  76  PRO A N   1 
ATOM   546  C  CA  . PRO A 1 74  ? 13.547  8.179   -6.956  1.00 10.88 ?  76  PRO A CA  1 
ATOM   547  C  C   . PRO A 1 74  ? 14.765  8.250   -7.868  1.00 11.17 ?  76  PRO A C   1 
ATOM   548  O  O   . PRO A 1 74  ? 15.000  9.227   -8.592  1.00 11.83 ?  76  PRO A O   1 
ATOM   549  C  CB  . PRO A 1 74  ? 12.604  9.371   -7.135  1.00 15.49 ?  76  PRO A CB  1 
ATOM   550  C  CG  . PRO A 1 74  ? 13.052  10.373  -6.137  1.00 16.06 ?  76  PRO A CG  1 
ATOM   551  C  CD  . PRO A 1 74  ? 13.683  9.645   -4.984  1.00 14.09 ?  76  PRO A CD  1 
ATOM   552  N  N   . ASN A 1 75  ? 15.576  7.194   -7.810  1.00 11.05 ?  77  ASN A N   1 
ATOM   553  C  CA  . ASN A 1 75  ? 16.911  7.251   -8.406  1.00 9.56  ?  77  ASN A CA  1 
ATOM   554  C  C   . ASN A 1 75  ? 16.923  7.640   -9.872  1.00 9.25  ?  77  ASN A C   1 
ATOM   555  O  O   . ASN A 1 75  ? 17.811  8.415   -10.256 1.00 10.40 ?  77  ASN A O   1 
ATOM   556  C  CB  . ASN A 1 75  ? 17.636  5.913   -8.207  1.00 11.04 ?  77  ASN A CB  1 
ATOM   557  C  CG  . ASN A 1 75  ? 17.930  5.644   -6.764  1.00 13.73 ?  77  ASN A CG  1 
ATOM   558  O  OD1 . ASN A 1 75  ? 18.700  6.379   -6.145  1.00 13.43 ?  77  ASN A OD1 1 
ATOM   559  N  ND2 . ASN A 1 75  ? 17.319  4.598   -6.206  1.00 12.96 ?  77  ASN A ND2 1 
ATOM   560  N  N   . PRO A 1 76  ? 16.021  7.164   -10.729 1.00 10.86 ?  78  PRO A N   1 
ATOM   561  C  CA  . PRO A 1 76  ? 16.121  7.559   -12.142 1.00 9.67  ?  78  PRO A CA  1 
ATOM   562  C  C   . PRO A 1 76  ? 16.029  9.057   -12.371 1.00 10.74 ?  78  PRO A C   1 
ATOM   563  O  O   . PRO A 1 76  ? 16.627  9.552   -13.328 1.00 12.63 ?  78  PRO A O   1 
ATOM   564  C  CB  . PRO A 1 76  ? 14.940  6.819   -12.787 1.00 12.96 ?  78  PRO A CB  1 
ATOM   565  C  CG  . PRO A 1 76  ? 14.757  5.627   -11.928 1.00 14.82 ?  78  PRO A CG  1 
ATOM   566  C  CD  . PRO A 1 76  ? 14.960  6.155   -10.530 1.00 10.92 ?  78  PRO A CD  1 
ATOM   567  N  N   . VAL A 1 77  ? 15.263  9.781   -11.547 1.00 10.77 ?  79  VAL A N   1 
ATOM   568  C  CA  . VAL A 1 77  ? 15.169  11.237  -11.657 1.00 9.69  ?  79  VAL A CA  1 
ATOM   569  C  C   . VAL A 1 77  ? 16.533  11.887  -11.413 1.00 10.16 ?  79  VAL A C   1 
ATOM   570  O  O   . VAL A 1 77  ? 16.879  12.910  -12.023 1.00 11.39 ?  79  VAL A O   1 
ATOM   571  C  CB  . VAL A 1 77  ? 14.122  11.759  -10.654 1.00 10.21 ?  79  VAL A CB  1 
ATOM   572  C  CG1 . VAL A 1 77  ? 14.143  13.280  -10.581 1.00 16.13 ?  79  VAL A CG1 1 
ATOM   573  C  CG2 . VAL A 1 77  ? 12.722  11.234  -11.010 1.00 14.90 ?  79  VAL A CG2 1 
ATOM   574  N  N   . LEU A 1 78  ? 17.303  11.334  -10.479 1.00 10.64 ?  80  LEU A N   1 
ATOM   575  C  CA  . LEU A 1 78  ? 18.631  11.868  -10.191 1.00 11.80 ?  80  LEU A CA  1 
ATOM   576  C  C   . LEU A 1 78  ? 19.655  11.361  -11.197 1.00 11.97 ?  80  LEU A C   1 
ATOM   577  O  O   . LEU A 1 78  ? 20.547  12.112  -11.622 1.00 10.77 ?  80  LEU A O   1 
ATOM   578  C  CB  . LEU A 1 78  ? 19.046  11.470  -8.768  1.00 9.86  ?  80  LEU A CB  1 
ATOM   579  C  CG  . LEU A 1 78  ? 18.349  12.102  -7.558  1.00 13.82 ?  80  LEU A CG  1 
ATOM   580  C  CD1 . LEU A 1 78  ? 16.892  11.681  -7.394  1.00 17.22 ?  80  LEU A CD1 1 
ATOM   581  C  CD2 . LEU A 1 78  ? 19.089  11.674  -6.300  1.00 15.40 ?  80  LEU A CD2 1 
ATOM   582  N  N   . LEU A 1 79  ? 19.539  10.085  -11.586 1.00 10.00 ?  81  LEU A N   1 
ATOM   583  C  CA  . LEU A 1 79  ? 20.618  9.441   -12.327 1.00 12.90 ?  81  LEU A CA  1 
ATOM   584  C  C   . LEU A 1 79  ? 20.587  9.769   -13.810 1.00 12.46 ?  81  LEU A C   1 
ATOM   585  O  O   . LEU A 1 79  ? 21.646  9.891   -14.431 1.00 11.77 ?  81  LEU A O   1 
ATOM   586  C  CB  . LEU A 1 79  ? 20.576  7.923   -12.155 1.00 10.18 ?  81  LEU A CB  1 
ATOM   587  C  CG  . LEU A 1 79  ? 20.942  7.360   -10.794 1.00 9.32  ?  81  LEU A CG  1 
ATOM   588  C  CD1 . LEU A 1 79  ? 20.643  5.855   -10.766 1.00 11.41 ?  81  LEU A CD1 1 
ATOM   589  C  CD2 . LEU A 1 79  ? 22.422  7.651   -10.488 1.00 10.53 ?  81  LEU A CD2 1 
ATOM   590  N  N   . ARG A 1 80  ? 19.404  9.875   -14.413 1.00 12.18 ?  82  ARG A N   1 
ATOM   591  C  CA  . ARG A 1 80  ? 19.394  10.165  -15.846 1.00 11.13 ?  82  ARG A CA  1 
ATOM   592  C  C   . ARG A 1 80  ? 20.145  11.453  -16.162 1.00 11.61 ?  82  ARG A C   1 
ATOM   593  O  O   . ARG A 1 80  ? 20.961  11.446  -17.098 1.00 12.57 ?  82  ARG A O   1 
ATOM   594  C  CB  . ARG A 1 80  ? 17.961  10.183  -16.393 1.00 14.73 ?  82  ARG A CB  1 
ATOM   595  C  CG  . ARG A 1 80  ? 17.403  8.768   -16.643 1.00 16.21 ?  82  ARG A CG  1 
ATOM   596  C  CD  . ARG A 1 80  ? 16.036  8.794   -17.336 1.00 18.29 ?  82  ARG A CD  1 
ATOM   597  N  NE  . ARG A 1 80  ? 15.044  9.500   -16.526 1.00 18.00 ?  82  ARG A NE  1 
ATOM   598  C  CZ  . ARG A 1 80  ? 14.077  8.908   -15.827 1.00 20.69 ?  82  ARG A CZ  1 
ATOM   599  N  NH1 . ARG A 1 80  ? 13.952  7.581   -15.836 1.00 19.95 ?  82  ARG A NH1 1 
ATOM   600  N  NH2 . ARG A 1 80  ? 13.236  9.645   -15.114 1.00 23.71 ?  82  ARG A NH2 1 
ATOM   601  N  N   . PRO A 1 81  ? 19.944  12.565  -15.445 1.00 11.04 ?  83  PRO A N   1 
ATOM   602  C  CA  . PRO A 1 81  ? 20.775  13.755  -15.709 1.00 9.38  ?  83  PRO A CA  1 
ATOM   603  C  C   . PRO A 1 81  ? 22.253  13.530  -15.435 1.00 10.26 ?  83  PRO A C   1 
ATOM   604  O  O   . PRO A 1 81  ? 23.097  14.009  -16.197 1.00 12.39 ?  83  PRO A O   1 
ATOM   605  C  CB  . PRO A 1 81  ? 20.189  14.797  -14.746 1.00 13.36 ?  83  PRO A CB  1 
ATOM   606  C  CG  . PRO A 1 81  ? 18.753  14.339  -14.553 1.00 11.90 ?  83  PRO A CG  1 
ATOM   607  C  CD  . PRO A 1 81  ? 18.863  12.857  -14.481 1.00 12.28 ?  83  PRO A CD  1 
ATOM   608  N  N   . ILE A 1 82  ? 22.597  12.845  -14.340 1.00 8.11  ?  84  ILE A N   1 
ATOM   609  C  CA  . ILE A 1 82  ? 24.008  12.594  -14.056 1.00 7.50  ?  84  ILE A CA  1 
ATOM   610  C  C   . ILE A 1 82  ? 24.637  11.806  -15.194 1.00 10.00 ?  84  ILE A C   1 
ATOM   611  O  O   . ILE A 1 82  ? 25.722  12.143  -15.691 1.00 11.56 ?  84  ILE A O   1 
ATOM   612  C  CB  . ILE A 1 82  ? 24.164  11.841  -12.721 1.00 9.66  ?  84  ILE A CB  1 
ATOM   613  C  CG1 . ILE A 1 82  ? 23.737  12.717  -11.559 1.00 11.16 ?  84  ILE A CG1 1 
ATOM   614  C  CG2 . ILE A 1 82  ? 25.606  11.320  -12.542 1.00 10.30 ?  84  ILE A CG2 1 
ATOM   615  C  CD1 . ILE A 1 82  ? 23.594  11.937  -10.264 1.00 9.23  ?  84  ILE A CD1 1 
ATOM   616  N  N   . LEU A 1 83  ? 23.972  10.729  -15.597 1.00 9.01  ?  85  LEU A N   1 
ATOM   617  C  CA  . LEU A 1 83  ? 24.512  9.827   -16.607 1.00 9.13  ?  85  LEU A CA  1 
ATOM   618  C  C   . LEU A 1 83  ? 24.605  10.504  -17.966 1.00 12.21 ?  85  LEU A C   1 
ATOM   619  O  O   . LEU A 1 83  ? 25.547  10.246  -18.719 1.00 12.09 ?  85  LEU A O   1 
ATOM   620  C  CB  . LEU A 1 83  ? 23.651  8.561   -16.687 1.00 10.45 ?  85  LEU A CB  1 
ATOM   621  C  CG  . LEU A 1 83  ? 23.712  7.654   -15.445 1.00 7.89  ?  85  LEU A CG  1 
ATOM   622  C  CD1 . LEU A 1 83  ? 22.649  6.550   -15.576 1.00 11.76 ?  85  LEU A CD1 1 
ATOM   623  C  CD2 . LEU A 1 83  ? 25.156  7.093   -15.202 1.00 11.76 ?  85  LEU A CD2 1 
ATOM   624  N  N   . ARG A 1 84  ? 23.636  11.363  -18.303 1.00 10.29 ?  86  ARG A N   1 
ATOM   625  C  CA  . ARG A 1 84  ? 23.743  12.147  -19.532 1.00 11.01 ?  86  ARG A CA  1 
ATOM   626  C  C   . ARG A 1 84  ? 24.961  13.056  -19.492 1.00 13.64 ?  86  ARG A C   1 
ATOM   627  O  O   . ARG A 1 84  ? 25.720  13.137  -20.464 1.00 11.80 ?  86  ARG A O   1 
ATOM   628  C  CB  . ARG A 1 84  ? 22.466  12.966  -19.744 1.00 11.90 ?  86  ARG A CB  1 
ATOM   629  C  CG  . ARG A 1 84  ? 21.307  12.137  -20.266 1.00 14.18 ?  86  ARG A CG  1 
ATOM   630  C  CD  . ARG A 1 84  ? 20.115  12.998  -20.708 1.00 17.72 ?  86  ARG A CD  1 
ATOM   631  N  NE  . ARG A 1 84  ? 19.501  13.762  -19.619 1.00 21.14 ?  86  ARG A NE  1 
ATOM   632  C  CZ  . ARG A 1 84  ? 18.351  13.432  -19.036 1.00 22.38 ?  86  ARG A CZ  1 
ATOM   633  N  NH1 . ARG A 1 84  ? 17.703  12.340  -19.421 1.00 22.10 ?  86  ARG A NH1 1 
ATOM   634  N  NH2 . ARG A 1 84  ? 17.849  14.186  -18.064 1.00 26.00 ?  86  ARG A NH2 1 
ATOM   635  N  N   . THR A 1 85  ? 25.177  13.734  -18.365 1.00 13.63 ?  87  THR A N   1 
ATOM   636  C  CA  . THR A 1 85  ? 26.324  14.630  -18.251 1.00 10.66 ?  87  THR A CA  1 
ATOM   637  C  C   . THR A 1 85  ? 27.637  13.867  -18.355 1.00 12.22 ?  87  THR A C   1 
ATOM   638  O  O   . THR A 1 85  ? 28.584  14.324  -19.015 1.00 12.29 ?  87  THR A O   1 
ATOM   639  C  CB  . THR A 1 85  ? 26.225  15.408  -16.936 1.00 15.54 ?  87  THR A CB  1 
ATOM   640  O  OG1 . THR A 1 85  ? 25.076  16.271  -17.006 1.00 17.14 ?  87  THR A OG1 1 
ATOM   641  C  CG2 . THR A 1 85  ? 27.473  16.257  -16.708 1.00 14.60 ?  87  THR A CG2 1 
ATOM   642  N  N   . LEU A 1 86  ? 27.714  12.689  -17.731 1.00 10.77 ?  88  LEU A N   1 
ATOM   643  C  CA  . LEU A 1 86  ? 28.947  11.909  -17.801 1.00 10.35 ?  88  LEU A CA  1 
ATOM   644  C  C   . LEU A 1 86  ? 29.208  11.435  -19.220 1.00 14.56 ?  88  LEU A C   1 
ATOM   645  O  O   . LEU A 1 86  ? 30.357  11.409  -19.668 1.00 12.96 ?  88  LEU A O   1 
ATOM   646  C  CB  . LEU A 1 86  ? 28.879  10.714  -16.851 1.00 12.72 ?  88  LEU A CB  1 
ATOM   647  C  CG  . LEU A 1 86  ? 28.778  11.085  -15.373 1.00 17.48 ?  88  LEU A CG  1 
ATOM   648  C  CD1 . LEU A 1 86  ? 29.026  9.879   -14.491 1.00 14.81 ?  88  LEU A CD1 1 
ATOM   649  C  CD2 . LEU A 1 86  ? 29.764  12.199  -15.051 1.00 15.63 ?  88  LEU A CD2 1 
ATOM   650  N  N   . HIS A 1 87  ? 28.156  11.033  -19.931 1.00 11.00 ?  89  HIS A N   1 
ATOM   651  C  CA  . HIS A 1 87  ? 28.325  10.634  -21.324 1.00 12.24 ?  89  HIS A CA  1 
ATOM   652  C  C   . HIS A 1 87  ? 28.791  11.814  -22.164 1.00 10.88 ?  89  HIS A C   1 
ATOM   653  O  O   . HIS A 1 87  ? 29.697  11.672  -23.003 1.00 14.61 ?  89  HIS A O   1 
ATOM   654  C  CB  . HIS A 1 87  ? 27.017  10.065  -21.874 1.00 14.44 ?  89  HIS A CB  1 
ATOM   655  C  CG  . HIS A 1 87  ? 27.179  9.294   -23.147 1.00 21.90 ?  89  HIS A CG  1 
ATOM   656  N  ND1 . HIS A 1 87  ? 27.562  7.970   -23.170 1.00 23.57 ?  89  HIS A ND1 1 
ATOM   657  C  CD2 . HIS A 1 87  ? 27.019  9.662   -24.441 1.00 23.00 ?  89  HIS A CD2 1 
ATOM   658  C  CE1 . HIS A 1 87  ? 27.617  7.551   -24.423 1.00 22.88 ?  89  HIS A CE1 1 
ATOM   659  N  NE2 . HIS A 1 87  ? 27.296  8.559   -25.214 1.00 19.25 ?  89  HIS A NE2 1 
ATOM   660  N  N   . ALA A 1 88  ? 28.195  12.995  -21.938 1.00 12.76 ?  90  ALA A N   1 
ATOM   661  C  CA  . ALA A 1 88  ? 28.617  14.195  -22.661 1.00 14.08 ?  90  ALA A CA  1 
ATOM   662  C  C   . ALA A 1 88  ? 30.077  14.503  -22.386 1.00 12.00 ?  90  ALA A C   1 
ATOM   663  O  O   . ALA A 1 88  ? 30.811  14.941  -23.283 1.00 14.42 ?  90  ALA A O   1 
ATOM   664  C  CB  . ALA A 1 88  ? 27.746  15.390  -22.272 1.00 12.74 ?  90  ALA A CB  1 
ATOM   665  N  N   . ALA A 1 89  ? 30.524  14.254  -21.154 1.00 11.30 ?  91  ALA A N   1 
ATOM   666  C  CA  . ALA A 1 89  ? 31.895  14.554  -20.775 1.00 12.68 ?  91  ALA A CA  1 
ATOM   667  C  C   . ALA A 1 89  ? 32.886  13.580  -21.376 1.00 17.13 ?  91  ALA A C   1 
ATOM   668  O  O   . ALA A 1 89  ? 34.092  13.819  -21.291 1.00 20.66 ?  91  ALA A O   1 
ATOM   669  C  CB  . ALA A 1 89  ? 32.028  14.557  -19.252 1.00 10.66 ?  91  ALA A CB  1 
ATOM   670  N  N   . GLY A 1 90  ? 32.414  12.489  -21.966 1.00 14.04 ?  92  GLY A N   1 
ATOM   671  C  CA  . GLY A 1 90  ? 33.294  11.561  -22.640 1.00 15.81 ?  92  GLY A CA  1 
ATOM   672  C  C   . GLY A 1 90  ? 33.486  10.236  -21.950 1.00 17.44 ?  92  GLY A C   1 
ATOM   673  O  O   . GLY A 1 90  ? 34.242  9.405   -22.466 1.00 14.82 ?  92  GLY A O   1 
ATOM   674  N  N   . LEU A 1 91  ? 32.824  9.995   -20.815 1.00 11.74 ?  93  LEU A N   1 
ATOM   675  C  CA  . LEU A 1 91  ? 32.930  8.713   -20.133 1.00 13.79 ?  93  LEU A CA  1 
ATOM   676  C  C   . LEU A 1 91  ? 32.011  7.706   -20.811 1.00 18.45 ?  93  LEU A C   1 
ATOM   677  O  O   . LEU A 1 91  ? 30.838  7.998   -21.064 1.00 20.34 ?  93  LEU A O   1 
ATOM   678  C  CB  . LEU A 1 91  ? 32.561  8.868   -18.651 1.00 14.04 ?  93  LEU A CB  1 
ATOM   679  C  CG  . LEU A 1 91  ? 33.583  9.558   -17.743 1.00 18.23 ?  93  LEU A CG  1 
ATOM   680  C  CD1 . LEU A 1 91  ? 33.381  11.071  -17.738 1.00 21.10 ?  93  LEU A CD1 1 
ATOM   681  C  CD2 . LEU A 1 91  ? 33.456  9.022   -16.330 1.00 20.15 ?  93  LEU A CD2 1 
ATOM   682  N  N   . ALA A 1 92  ? 32.546  6.534   -21.130 1.00 24.12 ?  94  ALA A N   1 
ATOM   683  C  CA  . ALA A 1 92  ? 31.711  5.505   -21.727 1.00 27.32 ?  94  ALA A CA  1 
ATOM   684  C  C   . ALA A 1 92  ? 30.973  4.744   -20.632 1.00 22.68 ?  94  ALA A C   1 
ATOM   685  O  O   . ALA A 1 92  ? 31.391  4.731   -19.471 1.00 19.39 ?  94  ALA A O   1 
ATOM   686  C  CB  . ALA A 1 92  ? 32.553  4.544   -22.564 1.00 28.16 ?  94  ALA A CB  1 
ATOM   687  N  N   . THR A 1 93  ? 29.870  4.089   -21.015 1.00 24.07 ?  95  THR A N   1 
ATOM   688  C  CA  . THR A 1 93  ? 29.061  3.413   -20.006 1.00 19.26 ?  95  THR A CA  1 
ATOM   689  C  C   . THR A 1 93  ? 29.887  2.380   -19.256 1.00 19.89 ?  95  THR A C   1 
ATOM   690  O  O   . THR A 1 93  ? 29.686  2.184   -18.054 1.00 17.79 ?  95  THR A O   1 
ATOM   691  C  CB  . THR A 1 93  ? 27.829  2.745   -20.627 1.00 25.60 ?  95  THR A CB  1 
ATOM   692  O  OG1 . THR A 1 93  ? 28.225  1.800   -21.624 1.00 23.97 ?  95  THR A OG1 1 
ATOM   693  C  CG2 . THR A 1 93  ? 26.941  3.788   -21.282 1.00 22.16 ?  95  THR A CG2 1 
ATOM   694  N  N   . GLN A 1 94  ? 30.845  1.734   -19.936 1.00 20.16 ?  96  GLN A N   1 
ATOM   695  C  CA  . GLN A 1 94  ? 31.697  0.748   -19.284 1.00 22.85 ?  96  GLN A CA  1 
ATOM   696  C  C   . GLN A 1 94  ? 32.643  1.388   -18.266 1.00 19.53 ?  96  GLN A C   1 
ATOM   697  O  O   . GLN A 1 94  ? 33.189  0.682   -17.418 1.00 24.96 ?  96  GLN A O   1 
ATOM   698  C  CB  . GLN A 1 94  ? 32.509  -0.022  -20.336 1.00 24.36 ?  96  GLN A CB  1 
ATOM   699  C  CG  . GLN A 1 94  ? 33.274  0.876   -21.312 1.00 32.22 ?  96  GLN A CG  1 
ATOM   700  C  CD  . GLN A 1 94  ? 32.530  1.134   -22.627 1.00 40.55 ?  96  GLN A CD  1 
ATOM   701  O  OE1 . GLN A 1 94  ? 31.300  1.208   -22.666 1.00 31.81 ?  96  GLN A OE1 1 
ATOM   702  N  NE2 . GLN A 1 94  ? 33.287  1.274   -23.712 1.00 52.14 ?  96  GLN A NE2 1 
ATOM   703  N  N   . ASP A 1 95  ? 32.839  2.701   -18.337 1.00 18.01 ?  97  ASP A N   1 
ATOM   704  C  CA  . ASP A 1 95  ? 33.693  3.442   -17.417 1.00 18.52 ?  97  ASP A CA  1 
ATOM   705  C  C   . ASP A 1 95  ? 32.966  3.856   -16.144 1.00 15.46 ?  97  ASP A C   1 
ATOM   706  O  O   . ASP A 1 95  ? 33.587  4.470   -15.267 1.00 16.78 ?  97  ASP A O   1 
ATOM   707  C  CB  . ASP A 1 95  ? 34.243  4.715   -18.089 1.00 22.88 ?  97  ASP A CB  1 
ATOM   708  C  CG  . ASP A 1 95  ? 35.058  4.436   -19.351 1.00 32.18 ?  97  ASP A CG  1 
ATOM   709  O  OD1 . ASP A 1 95  ? 34.941  5.233   -20.318 1.00 27.69 ?  97  ASP A OD1 1 
ATOM   710  O  OD2 . ASP A 1 95  ? 35.841  3.461   -19.353 1.00 25.81 ?  97  ASP A OD2 1 
ATOM   711  N  N   . ILE A 1 96  ? 31.679  3.547   -16.026 1.00 12.64 ?  98  ILE A N   1 
ATOM   712  C  CA  . ILE A 1 96  ? 30.841  4.052   -14.945 1.00 13.66 ?  98  ILE A CA  1 
ATOM   713  C  C   . ILE A 1 96  ? 30.347  2.875   -14.113 1.00 13.91 ?  98  ILE A C   1 
ATOM   714  O  O   . ILE A 1 96  ? 29.755  1.933   -14.652 1.00 20.11 ?  98  ILE A O   1 
ATOM   715  C  CB  . ILE A 1 96  ? 29.665  4.873   -15.504 1.00 13.26 ?  98  ILE A CB  1 
ATOM   716  C  CG1 . ILE A 1 96  ? 30.190  6.078   -16.296 1.00 14.25 ?  98  ILE A CG1 1 
ATOM   717  C  CG2 . ILE A 1 96  ? 28.719  5.309   -14.372 1.00 12.64 ?  98  ILE A CG2 1 
ATOM   718  C  CD1 . ILE A 1 96  ? 29.134  6.729   -17.205 1.00 15.87 ?  98  ILE A CD1 1 
ATOM   719  N  N   . LEU A 1 97  ? 30.577  2.926   -12.805 1.00 9.13  ?  99  LEU A N   1 
ATOM   720  C  CA  . LEU A 1 97  ? 30.038  1.918   -11.902 1.00 9.06  ?  99  LEU A CA  1 
ATOM   721  C  C   . LEU A 1 97  ? 28.955  2.562   -11.045 1.00 12.96 ?  99  LEU A C   1 
ATOM   722  O  O   . LEU A 1 97  ? 29.174  3.640   -10.486 1.00 10.39 ?  99  LEU A O   1 
ATOM   723  C  CB  . LEU A 1 97  ? 31.133  1.339   -11.008 1.00 10.28 ?  99  LEU A CB  1 
ATOM   724  C  CG  . LEU A 1 97  ? 30.655  0.521   -9.812  1.00 10.52 ?  99  LEU A CG  1 
ATOM   725  C  CD1 . LEU A 1 97  ? 30.047  -0.781  -10.311 1.00 13.24 ?  99  LEU A CD1 1 
ATOM   726  C  CD2 . LEU A 1 97  ? 31.847  0.268   -8.899  1.00 11.90 ?  99  LEU A CD2 1 
ATOM   727  N  N   . ILE A 1 98  ? 27.786  1.925   -10.969 1.00 9.00  ?  100 ILE A N   1 
ATOM   728  C  CA  . ILE A 1 98  ? 26.777  2.277   -9.971  1.00 7.74  ?  100 ILE A CA  1 
ATOM   729  C  C   . ILE A 1 98  ? 26.964  1.316   -8.798  1.00 8.45  ?  100 ILE A C   1 
ATOM   730  O  O   . ILE A 1 98  ? 26.841  0.096   -8.957  1.00 9.17  ?  100 ILE A O   1 
ATOM   731  C  CB  . ILE A 1 98  ? 25.355  2.207   -10.557 1.00 8.54  ?  100 ILE A CB  1 
ATOM   732  C  CG1 . ILE A 1 98  ? 25.209  3.244   -11.687 1.00 12.46 ?  100 ILE A CG1 1 
ATOM   733  C  CG2 . ILE A 1 98  ? 24.335  2.483   -9.446  1.00 9.70  ?  100 ILE A CG2 1 
ATOM   734  C  CD1 . ILE A 1 98  ? 23.857  3.201   -12.435 1.00 11.38 ?  100 ILE A CD1 1 
ATOM   735  N  N   . LEU A 1 99  ? 27.324  1.849   -7.632  1.00 8.99  ?  101 LEU A N   1 
ATOM   736  C  CA  . LEU A 1 99  ? 27.660  1.021   -6.477  1.00 8.83  ?  101 LEU A CA  1 
ATOM   737  C  C   . LEU A 1 99  ? 26.563  1.191   -5.434  1.00 8.69  ?  101 LEU A C   1 
ATOM   738  O  O   . LEU A 1 99  ? 26.294  2.315   -5.003  1.00 9.74  ?  101 LEU A O   1 
ATOM   739  C  CB  . LEU A 1 99  ? 29.033  1.404   -5.919  1.00 7.57  ?  101 LEU A CB  1 
ATOM   740  C  CG  . LEU A 1 99  ? 29.487  0.627   -4.679  1.00 8.46  ?  101 LEU A CG  1 
ATOM   741  C  CD1 . LEU A 1 99  ? 29.519  -0.892  -4.951  1.00 8.95  ?  101 LEU A CD1 1 
ATOM   742  C  CD2 . LEU A 1 99  ? 30.861  1.118   -4.224  1.00 10.83 ?  101 LEU A CD2 1 
ATOM   743  N  N   . VAL A 1 100 ? 25.907  0.088   -5.063  1.00 6.81  ?  102 VAL A N   1 
ATOM   744  C  CA  . VAL A 1 100 ? 24.821  0.151   -4.079  1.00 8.39  ?  102 VAL A CA  1 
ATOM   745  C  C   . VAL A 1 100 ? 25.435  0.257   -2.683  1.00 8.95  ?  102 VAL A C   1 
ATOM   746  O  O   . VAL A 1 100 ? 26.117  -0.665  -2.213  1.00 9.62  ?  102 VAL A O   1 
ATOM   747  C  CB  . VAL A 1 100 ? 23.881  -1.066  -4.191  1.00 8.41  ?  102 VAL A CB  1 
ATOM   748  C  CG1 . VAL A 1 100 ? 22.717  -0.918  -3.204  1.00 7.01  ?  102 VAL A CG1 1 
ATOM   749  C  CG2 . VAL A 1 100 ? 23.317  -1.190  -5.613  1.00 7.61  ?  102 VAL A CG2 1 
ATOM   750  N  N   . ALA A 1 101 ? 25.179  1.386   -2.015  1.00 8.29  ?  103 ALA A N   1 
ATOM   751  C  CA  . ALA A 1 101 ? 25.758  1.711   -0.714  1.00 9.61  ?  103 ALA A CA  1 
ATOM   752  C  C   . ALA A 1 101 ? 24.916  1.053   0.380   1.00 8.13  ?  103 ALA A C   1 
ATOM   753  O  O   . ALA A 1 101 ? 24.137  1.682   1.101   1.00 8.66  ?  103 ALA A O   1 
ATOM   754  C  CB  . ALA A 1 101 ? 25.844  3.222   -0.539  1.00 8.41  ?  103 ALA A CB  1 
ATOM   755  N  N   . THR A 1 102 ? 25.100  -0.261  0.503   1.00 7.56  ?  104 THR A N   1 
ATOM   756  C  CA  . THR A 1 102 ? 24.364  -1.072  1.464   1.00 7.60  ?  104 THR A CA  1 
ATOM   757  C  C   . THR A 1 102 ? 24.723  -0.795  2.922   1.00 8.93  ?  104 THR A C   1 
ATOM   758  O  O   . THR A 1 102 ? 23.966  -1.199  3.808   1.00 9.54  ?  104 THR A O   1 
ATOM   759  C  CB  . THR A 1 102 ? 24.652  -2.545  1.185   1.00 7.10  ?  104 THR A CB  1 
ATOM   760  O  OG1 . THR A 1 102 ? 26.077  -2.732  1.253   1.00 10.33 ?  104 THR A OG1 1 
ATOM   761  C  CG2 . THR A 1 102 ? 24.121  -2.956  -0.198  1.00 8.97  ?  104 THR A CG2 1 
ATOM   762  N  N   . GLY A 1 103 ? 25.863  -0.158  3.199   1.00 8.61  ?  105 GLY A N   1 
ATOM   763  C  CA  . GLY A 1 103 ? 26.350  -0.161  4.577   1.00 6.32  ?  105 GLY A CA  1 
ATOM   764  C  C   . GLY A 1 103 ? 26.668  -1.604  4.947   1.00 9.65  ?  105 GLY A C   1 
ATOM   765  O  O   . GLY A 1 103 ? 27.417  -2.291  4.240   1.00 9.76  ?  105 GLY A O   1 
ATOM   766  N  N   . LEU A 1 104 ? 26.106  -2.072  6.064   1.00 7.80  ?  106 LEU A N   1 
ATOM   767  C  CA  . LEU A 1 104 ? 26.178  -3.474  6.469   1.00 9.07  ?  106 LEU A CA  1 
ATOM   768  C  C   . LEU A 1 104 ? 24.917  -4.263  6.131   1.00 9.41  ?  106 LEU A C   1 
ATOM   769  O  O   . LEU A 1 104 ? 24.787  -5.420  6.558   1.00 10.94 ?  106 LEU A O   1 
ATOM   770  C  CB  . LEU A 1 104 ? 26.478  -3.605  7.964   1.00 12.57 ?  106 LEU A CB  1 
ATOM   771  C  CG  . LEU A 1 104 ? 27.949  -3.744  8.366   1.00 10.96 ?  106 LEU A CG  1 
ATOM   772  C  CD1 . LEU A 1 104 ? 28.459  -5.111  7.873   1.00 10.41 ?  106 LEU A CD1 1 
ATOM   773  C  CD2 . LEU A 1 104 ? 28.830  -2.617  7.805   1.00 8.12  ?  106 LEU A CD2 1 
ATOM   774  N  N   . HIS A 1 105 ? 24.005  -3.685  5.358   1.00 8.18  ?  107 HIS A N   1 
ATOM   775  C  CA  . HIS A 1 105 ? 22.852  -4.447  4.901   1.00 9.00  ?  107 HIS A CA  1 
ATOM   776  C  C   . HIS A 1 105 ? 23.270  -5.533  3.900   1.00 9.64  ?  107 HIS A C   1 
ATOM   777  O  O   . HIS A 1 105 ? 24.309  -5.450  3.239   1.00 10.06 ?  107 HIS A O   1 
ATOM   778  C  CB  . HIS A 1 105 ? 21.814  -3.542  4.220   1.00 7.11  ?  107 HIS A CB  1 
ATOM   779  C  CG  . HIS A 1 105 ? 21.324  -2.402  5.062   1.00 8.80  ?  107 HIS A CG  1 
ATOM   780  N  ND1 . HIS A 1 105 ? 20.667  -1.319  4.516   1.00 10.29 ?  107 HIS A ND1 1 
ATOM   781  C  CD2 . HIS A 1 105 ? 21.399  -2.164  6.396   1.00 8.24  ?  107 HIS A CD2 1 
ATOM   782  C  CE1 . HIS A 1 105 ? 20.353  -0.466  5.476   1.00 10.61 ?  107 HIS A CE1 1 
ATOM   783  N  NE2 . HIS A 1 105 ? 20.795  -0.949  6.625   1.00 7.66  ?  107 HIS A NE2 1 
ATOM   784  N  N   . ARG A 1 106 ? 22.385  -6.529  3.751   1.00 9.70  ?  108 ARG A N   1 
ATOM   785  C  CA  . ARG A 1 106 ? 22.501  -7.533  2.700   1.00 9.07  ?  108 ARG A CA  1 
ATOM   786  C  C   . ARG A 1 106 ? 22.558  -6.863  1.327   1.00 9.47  ?  108 ARG A C   1 
ATOM   787  O  O   . ARG A 1 106 ? 22.111  -5.725  1.153   1.00 9.69  ?  108 ARG A O   1 
ATOM   788  C  CB  . ARG A 1 106 ? 21.292  -8.469  2.736   1.00 10.11 ?  108 ARG A CB  1 
ATOM   789  C  CG  . ARG A 1 106 ? 19.968  -7.734  2.563   1.00 8.82  ?  108 ARG A CG  1 
ATOM   790  C  CD  . ARG A 1 106 ? 18.872  -8.690  2.118   1.00 11.04 ?  108 ARG A CD  1 
ATOM   791  N  NE  . ARG A 1 106 ? 17.562  -8.050  1.973   1.00 9.73  ?  108 ARG A NE  1 
ATOM   792  C  CZ  . ARG A 1 106 ? 17.156  -7.399  0.884   1.00 10.55 ?  108 ARG A CZ  1 
ATOM   793  N  NH1 . ARG A 1 106 ? 17.975  -7.241  -0.156  1.00 11.39 ?  108 ARG A NH1 1 
ATOM   794  N  NH2 . ARG A 1 106 ? 15.925  -6.889  0.842   1.00 12.19 ?  108 ARG A NH2 1 
ATOM   795  N  N   . PRO A 1 107 ? 23.077  -7.560  0.320   1.00 10.82 ?  109 PRO A N   1 
ATOM   796  C  CA  . PRO A 1 107 ? 23.097  -6.982  -1.023  1.00 10.84 ?  109 PRO A CA  1 
ATOM   797  C  C   . PRO A 1 107 ? 21.693  -6.849  -1.595  1.00 9.20  ?  109 PRO A C   1 
ATOM   798  O  O   . PRO A 1 107 ? 20.770  -7.588  -1.238  1.00 11.30 ?  109 PRO A O   1 
ATOM   799  C  CB  . PRO A 1 107 ? 23.937  -7.981  -1.830  1.00 11.53 ?  109 PRO A CB  1 
ATOM   800  C  CG  . PRO A 1 107 ? 23.746  -9.273  -1.091  1.00 14.48 ?  109 PRO A CG  1 
ATOM   801  C  CD  . PRO A 1 107 ? 23.696  -8.896  0.354   1.00 12.35 ?  109 PRO A CD  1 
ATOM   802  N  N   . SER A 1 108 ? 21.541  -5.891  -2.500  1.00 10.72 ?  110 SER A N   1 
ATOM   803  C  CA  . SER A 1 108 ? 20.296  -5.773  -3.237  1.00 8.97  ?  110 SER A CA  1 
ATOM   804  C  C   . SER A 1 108 ? 20.150  -6.951  -4.197  1.00 13.14 ?  110 SER A C   1 
ATOM   805  O  O   . SER A 1 108 ? 21.134  -7.500  -4.699  1.00 12.46 ?  110 SER A O   1 
ATOM   806  C  CB  . SER A 1 108 ? 20.248  -4.448  -4.005  1.00 9.96  ?  110 SER A CB  1 
ATOM   807  O  OG  . SER A 1 108 ? 21.252  -4.393  -5.009  1.00 11.62 ?  110 SER A OG  1 
ATOM   808  N  N   . THR A 1 109 ? 18.910  -7.353  -4.432  1.00 10.55 ?  111 THR A N   1 
ATOM   809  C  CA  . THR A 1 109 ? 18.654  -8.405  -5.402  1.00 13.58 ?  111 THR A CA  1 
ATOM   810  C  C   . THR A 1 109 ? 18.562  -7.834  -6.818  1.00 13.22 ?  111 THR A C   1 
ATOM   811  O  O   . THR A 1 109 ? 18.425  -6.617  -7.010  1.00 12.26 ?  111 THR A O   1 
ATOM   812  C  CB  . THR A 1 109 ? 17.367  -9.143  -5.037  1.00 15.20 ?  111 THR A CB  1 
ATOM   813  O  OG1 . THR A 1 109 ? 16.251  -8.273  -5.242  1.00 15.33 ?  111 THR A OG1 1 
ATOM   814  C  CG2 . THR A 1 109 ? 17.409  -9.646  -3.594  1.00 17.41 ?  111 THR A CG2 1 
ATOM   815  N  N   . PRO A 1 110 ? 18.640  -8.692  -7.843  1.00 15.27 ?  112 PRO A N   1 
ATOM   816  C  CA  . PRO A 1 110 ? 18.389  -8.195  -9.207  1.00 16.63 ?  112 PRO A CA  1 
ATOM   817  C  C   . PRO A 1 110 ? 17.054  -7.470  -9.343  1.00 13.68 ?  112 PRO A C   1 
ATOM   818  O  O   . PRO A 1 110 ? 16.993  -6.412  -9.982  1.00 13.90 ?  112 PRO A O   1 
ATOM   819  C  CB  . PRO A 1 110 ? 18.448  -9.474  -10.057 1.00 16.23 ?  112 PRO A CB  1 
ATOM   820  C  CG  . PRO A 1 110 ? 19.341  -10.387 -9.285  1.00 17.29 ?  112 PRO A CG  1 
ATOM   821  C  CD  . PRO A 1 110 ? 19.073  -10.105 -7.838  1.00 16.18 ?  112 PRO A CD  1 
ATOM   822  N  N   . ALA A 1 111 ? 15.986  -7.990  -8.734  1.00 12.26 ?  113 ALA A N   1 
ATOM   823  C  CA  . ALA A 1 111 ? 14.695  -7.315  -8.847  1.00 12.92 ?  113 ALA A CA  1 
ATOM   824  C  C   . ALA A 1 111 ? 14.726  -5.958  -8.152  1.00 11.44 ?  113 ALA A C   1 
ATOM   825  O  O   . ALA A 1 111 ? 14.113  -4.990  -8.624  1.00 14.12 ?  113 ALA A O   1 
ATOM   826  C  CB  . ALA A 1 111 ? 13.592  -8.187  -8.255  1.00 15.29 ?  113 ALA A CB  1 
ATOM   827  N  N   . GLU A 1 112 ? 15.411  -5.877  -7.018  1.00 12.85 ?  114 GLU A N   1 
ATOM   828  C  CA  . GLU A 1 112 ? 15.494  -4.608  -6.307  1.00 13.05 ?  114 GLU A CA  1 
ATOM   829  C  C   . GLU A 1 112 ? 16.252  -3.575  -7.117  1.00 12.31 ?  114 GLU A C   1 
ATOM   830  O  O   . GLU A 1 112 ? 15.885  -2.398  -7.122  1.00 11.59 ?  114 GLU A O   1 
ATOM   831  C  CB  . GLU A 1 112 ? 16.146  -4.808  -4.944  1.00 10.98 ?  114 GLU A CB  1 
ATOM   832  C  CG  . GLU A 1 112 ? 15.156  -5.392  -3.931  1.00 15.10 ?  114 GLU A CG  1 
ATOM   833  C  CD  . GLU A 1 112 ? 15.807  -5.818  -2.617  1.00 13.85 ?  114 GLU A CD  1 
ATOM   834  O  OE1 . GLU A 1 112 ? 17.061  -5.854  -2.529  1.00 13.79 ?  114 GLU A OE1 1 
ATOM   835  O  OE2 . GLU A 1 112 ? 15.050  -6.114  -1.664  1.00 14.24 ?  114 GLU A OE2 1 
ATOM   836  N  N   . LYS A 1 113 ? 17.319  -3.988  -7.800  1.00 12.04 ?  115 LYS A N   1 
ATOM   837  C  CA  . LYS A 1 113 ? 18.049  -3.034  -8.628  1.00 9.08  ?  115 LYS A CA  1 
ATOM   838  C  C   . LYS A 1 113 ? 17.137  -2.437  -9.696  1.00 14.12 ?  115 LYS A C   1 
ATOM   839  O  O   . LYS A 1 113 ? 17.225  -1.242  -10.014 1.00 11.01 ?  115 LYS A O   1 
ATOM   840  C  CB  . LYS A 1 113 ? 19.264  -3.714  -9.260  1.00 12.48 ?  115 LYS A CB  1 
ATOM   841  C  CG  . LYS A 1 113 ? 20.352  -4.091  -8.238  1.00 9.56  ?  115 LYS A CG  1 
ATOM   842  C  CD  . LYS A 1 113 ? 21.531  -4.757  -8.936  1.00 14.27 ?  115 LYS A CD  1 
ATOM   843  C  CE  . LYS A 1 113 ? 22.706  -5.006  -7.971  1.00 10.73 ?  115 LYS A CE  1 
ATOM   844  N  NZ  . LYS A 1 113 ? 22.349  -6.087  -7.005  1.00 10.10 ?  115 LYS A NZ  1 
ATOM   845  N  N   . VAL A 1 114 ? 16.243  -3.252  -10.256 1.00 11.79 ?  116 VAL A N   1 
ATOM   846  C  CA  . VAL A 1 114 ? 15.282  -2.732  -11.223 1.00 13.58 ?  116 VAL A CA  1 
ATOM   847  C  C   . VAL A 1 114 ? 14.285  -1.794  -10.545 1.00 16.32 ?  116 VAL A C   1 
ATOM   848  O  O   . VAL A 1 114 ? 13.994  -0.708  -11.059 1.00 14.02 ?  116 VAL A O   1 
ATOM   849  C  CB  . VAL A 1 114 ? 14.576  -3.890  -11.953 1.00 14.82 ?  116 VAL A CB  1 
ATOM   850  C  CG1 . VAL A 1 114 ? 13.478  -3.331  -12.842 1.00 16.59 ?  116 VAL A CG1 1 
ATOM   851  C  CG2 . VAL A 1 114 ? 15.588  -4.677  -12.756 1.00 15.95 ?  116 VAL A CG2 1 
ATOM   852  N  N   . GLU A 1 115 ? 13.753  -2.195  -9.381  1.00 11.65 ?  117 GLU A N   1 
ATOM   853  C  CA  . GLU A 1 115 ? 12.861  -1.324  -8.617  1.00 12.84 ?  117 GLU A CA  1 
ATOM   854  C  C   . GLU A 1 115 ? 13.542  -0.003  -8.273  1.00 15.74 ?  117 GLU A C   1 
ATOM   855  O  O   . GLU A 1 115 ? 12.931  1.068   -8.382  1.00 17.57 ?  117 GLU A O   1 
ATOM   856  C  CB  . GLU A 1 115 ? 12.395  -2.027  -7.335  1.00 15.82 ?  117 GLU A CB  1 
ATOM   857  C  CG  . GLU A 1 115 ? 11.418  -1.163  -6.503  1.00 20.70 ?  117 GLU A CG  1 
ATOM   858  C  CD  . GLU A 1 115 ? 10.892  -1.838  -5.231  1.00 25.23 ?  117 GLU A CD  1 
ATOM   859  O  OE1 . GLU A 1 115 ? 11.095  -3.062  -5.052  1.00 23.87 ?  117 GLU A OE1 1 
ATOM   860  O  OE2 . GLU A 1 115 ? 10.262  -1.131  -4.403  1.00 22.39 ?  117 GLU A OE2 1 
ATOM   861  N  N   . MET A 1 116 ? 14.809  -0.060  -7.848  1.00 14.12 ?  118 MET A N   1 
ATOM   862  C  CA  . MET A 1 116 ? 15.526  1.153   -7.458  1.00 13.05 ?  118 MET A CA  1 
ATOM   863  C  C   . MET A 1 116 ? 15.923  2.037   -8.637  1.00 14.07 ?  118 MET A C   1 
ATOM   864  O  O   . MET A 1 116 ? 15.805  3.268   -8.541  1.00 13.56 ?  118 MET A O   1 
ATOM   865  C  CB  . MET A 1 116 ? 16.795  0.818   -6.656  1.00 12.08 ?  118 MET A CB  1 
ATOM   866  C  CG  . MET A 1 116 ? 16.585  0.137   -5.314  1.00 15.53 ?  118 MET A CG  1 
ATOM   867  S  SD  . MET A 1 116 ? 17.976  -0.937  -4.864  1.00 19.45 ?  118 MET A SD  1 
ATOM   868  C  CE  . MET A 1 116 ? 19.406  0.035   -5.343  1.00 23.78 ?  118 MET A CE  1 
ATOM   869  N  N   . LEU A 1 117 ? 16.415  1.457   -9.737  1.00 11.88 ?  119 LEU A N   1 
ATOM   870  C  CA  . LEU A 1 117 ? 17.106  2.266   -10.740 1.00 11.11 ?  119 LEU A CA  1 
ATOM   871  C  C   . LEU A 1 117 ? 16.433  2.364   -12.096 1.00 11.77 ?  119 LEU A C   1 
ATOM   872  O  O   . LEU A 1 117 ? 16.936  3.113   -12.941 1.00 13.68 ?  119 LEU A O   1 
ATOM   873  C  CB  . LEU A 1 117 ? 18.534  1.754   -10.979 1.00 13.44 ?  119 LEU A CB  1 
ATOM   874  C  CG  . LEU A 1 117 ? 19.320  1.393   -9.729  1.00 12.37 ?  119 LEU A CG  1 
ATOM   875  C  CD1 . LEU A 1 117 ? 20.508  0.493   -10.076 1.00 13.37 ?  119 LEU A CD1 1 
ATOM   876  C  CD2 . LEU A 1 117 ? 19.775  2.681   -9.092  1.00 13.89 ?  119 LEU A CD2 1 
ATOM   877  N  N   . SER A 1 118 ? 15.337  1.636   -12.321 1.00 12.38 ?  120 SER A N   1 
ATOM   878  C  CA  . SER A 1 118 ? 14.643  1.439   -13.592 1.00 16.75 ?  120 SER A CA  1 
ATOM   879  C  C   . SER A 1 118 ? 15.306  0.322   -14.388 1.00 13.52 ?  120 SER A C   1 
ATOM   880  O  O   . SER A 1 118 ? 16.515  0.089   -14.270 1.00 14.70 ?  120 SER A O   1 
ATOM   881  C  CB  . SER A 1 118 ? 14.553  2.728   -14.417 1.00 14.32 ?  120 SER A CB  1 
ATOM   882  O  OG  . SER A 1 118 ? 15.734  2.955   -15.156 1.00 17.24 ?  120 SER A OG  1 
ATOM   883  N  N   . GLU A 1 119 ? 14.497  -0.398  -15.172 1.00 16.81 ?  121 GLU A N   1 
ATOM   884  C  CA  . GLU A 1 119 ? 15.027  -1.480  -15.992 1.00 15.51 ?  121 GLU A CA  1 
ATOM   885  C  C   . GLU A 1 119 ? 16.120  -0.990  -16.929 1.00 17.79 ?  121 GLU A C   1 
ATOM   886  O  O   . GLU A 1 119 ? 17.155  -1.652  -17.084 1.00 18.44 ?  121 GLU A O   1 
ATOM   887  C  CB  . GLU A 1 119 ? 13.898  -2.137  -16.792 1.00 21.66 ?  121 GLU A CB  1 
ATOM   888  C  CG  . GLU A 1 119 ? 14.350  -3.395  -17.513 1.00 31.51 ?  121 GLU A CG  1 
ATOM   889  C  CD  . GLU A 1 119 ? 13.246  -4.420  -17.649 1.00 48.91 ?  121 GLU A CD  1 
ATOM   890  O  OE1 . GLU A 1 119 ? 13.543  -5.562  -18.058 1.00 59.99 ?  121 GLU A OE1 1 
ATOM   891  O  OE2 . GLU A 1 119 ? 12.083  -4.084  -17.343 1.00 53.46 ?  121 GLU A OE2 1 
ATOM   892  N  N   . GLU A 1 120 ? 15.922  0.178   -17.547 1.00 15.20 ?  122 GLU A N   1 
ATOM   893  C  CA  . GLU A 1 120 ? 16.887  0.664   -18.529 1.00 15.70 ?  122 GLU A CA  1 
ATOM   894  C  C   . GLU A 1 120 ? 18.264  0.857   -17.904 1.00 18.07 ?  122 GLU A C   1 
ATOM   895  O  O   . GLU A 1 120 ? 19.276  0.445   -18.478 1.00 19.53 ?  122 GLU A O   1 
ATOM   896  C  CB  . GLU A 1 120 ? 16.395  1.969   -19.161 1.00 19.36 ?  122 GLU A CB  1 
ATOM   897  N  N   . ILE A 1 121 ? 18.327  1.476   -16.723 1.00 13.80 ?  123 ILE A N   1 
ATOM   898  C  CA  . ILE A 1 121 ? 19.629  1.725   -16.110 1.00 14.62 ?  123 ILE A CA  1 
ATOM   899  C  C   . ILE A 1 121 ? 20.228  0.428   -15.582 1.00 14.51 ?  123 ILE A C   1 
ATOM   900  O  O   . ILE A 1 121 ? 21.410  0.138   -15.803 1.00 16.89 ?  123 ILE A O   1 
ATOM   901  C  CB  . ILE A 1 121 ? 19.514  2.804   -15.017 1.00 14.00 ?  123 ILE A CB  1 
ATOM   902  C  CG1 . ILE A 1 121 ? 19.195  4.159   -15.665 1.00 14.41 ?  123 ILE A CG1 1 
ATOM   903  C  CG2 . ILE A 1 121 ? 20.801  2.872   -14.187 1.00 12.79 ?  123 ILE A CG2 1 
ATOM   904  C  CD1 . ILE A 1 121 ? 18.922  5.291   -14.663 1.00 16.42 ?  123 ILE A CD1 1 
ATOM   905  N  N   . ALA A 1 122 ? 19.418  -0.381  -14.896 1.00 13.38 ?  124 ALA A N   1 
ATOM   906  C  CA  . ALA A 1 122 ? 19.919  -1.631  -14.333 1.00 15.77 ?  124 ALA A CA  1 
ATOM   907  C  C   . ALA A 1 122 ? 20.438  -2.572  -15.413 1.00 22.11 ?  124 ALA A C   1 
ATOM   908  O  O   . ALA A 1 122 ? 21.367  -3.342  -15.160 1.00 20.57 ?  124 ALA A O   1 
ATOM   909  C  CB  . ALA A 1 122 ? 18.827  -2.311  -13.508 1.00 15.94 ?  124 ALA A CB  1 
ATOM   910  N  N   . ARG A 1 123 ? 19.880  -2.498  -16.628 1.00 18.46 ?  125 ARG A N   1 
ATOM   911  C  CA  . ARG A 1 123 ? 20.341  -3.360  -17.715 1.00 24.40 ?  125 ARG A CA  1 
ATOM   912  C  C   . ARG A 1 123 ? 21.555  -2.803  -18.451 1.00 24.45 ?  125 ARG A C   1 
ATOM   913  O  O   . ARG A 1 123 ? 22.300  -3.580  -19.055 1.00 28.28 ?  125 ARG A O   1 
ATOM   914  C  CB  . ARG A 1 123 ? 19.203  -3.598  -18.722 1.00 26.10 ?  125 ARG A CB  1 
ATOM   915  N  N   . THR A 1 124 ? 21.777  -1.491  -18.414 1.00 15.56 ?  126 THR A N   1 
ATOM   916  C  CA  . THR A 1 124 ? 22.813  -0.869  -19.239 1.00 17.67 ?  126 THR A CA  1 
ATOM   917  C  C   . THR A 1 124 ? 24.135  -0.688  -18.511 1.00 18.69 ?  126 THR A C   1 
ATOM   918  O  O   . THR A 1 124 ? 25.208  -0.818  -19.116 1.00 18.85 ?  126 THR A O   1 
ATOM   919  C  CB  . THR A 1 124 ? 22.319  0.486   -19.756 1.00 24.43 ?  126 THR A CB  1 
ATOM   920  O  OG1 . THR A 1 124 ? 21.116  0.294   -20.501 1.00 22.51 ?  126 THR A OG1 1 
ATOM   921  C  CG2 . THR A 1 124 ? 23.354  1.168   -20.628 1.00 23.39 ?  126 THR A CG2 1 
ATOM   922  N  N   . TYR A 1 125 ? 24.086  -0.395  -17.219 1.00 14.51 ?  127 TYR A N   1 
ATOM   923  C  CA  . TYR A 1 125 ? 25.284  -0.066  -16.467 1.00 16.98 ?  127 TYR A CA  1 
ATOM   924  C  C   . TYR A 1 125 ? 25.665  -1.219  -15.552 1.00 13.71 ?  127 TYR A C   1 
ATOM   925  O  O   . TYR A 1 125 ? 24.816  -2.024  -15.159 1.00 17.48 ?  127 TYR A O   1 
ATOM   926  C  CB  . TYR A 1 125 ? 25.060  1.203   -15.649 1.00 12.92 ?  127 TYR A CB  1 
ATOM   927  C  CG  . TYR A 1 125 ? 24.899  2.410   -16.526 1.00 12.70 ?  127 TYR A CG  1 
ATOM   928  C  CD1 . TYR A 1 125 ? 25.991  3.183   -16.873 1.00 13.25 ?  127 TYR A CD1 1 
ATOM   929  C  CD2 . TYR A 1 125 ? 23.661  2.746   -17.043 1.00 14.07 ?  127 TYR A CD2 1 
ATOM   930  C  CE1 . TYR A 1 125 ? 25.842  4.289   -17.699 1.00 16.54 ?  127 TYR A CE1 1 
ATOM   931  C  CE2 . TYR A 1 125 ? 23.501  3.835   -17.872 1.00 15.67 ?  127 TYR A CE2 1 
ATOM   932  C  CZ  . TYR A 1 125 ? 24.596  4.601   -18.194 1.00 17.47 ?  127 TYR A CZ  1 
ATOM   933  O  OH  . TYR A 1 125 ? 24.436  5.689   -19.016 1.00 19.47 ?  127 TYR A OH  1 
ATOM   934  N  N   . ARG A 1 126 ? 26.954  -1.311  -15.242 1.00 14.92 ?  128 ARG A N   1 
ATOM   935  C  CA  . ARG A 1 126 ? 27.398  -2.221  -14.196 1.00 10.38 ?  128 ARG A CA  1 
ATOM   936  C  C   . ARG A 1 126 ? 26.859  -1.716  -12.867 1.00 13.94 ?  128 ARG A C   1 
ATOM   937  O  O   . ARG A 1 126 ? 27.112  -0.572  -12.482 1.00 13.92 ?  128 ARG A O   1 
ATOM   938  C  CB  . ARG A 1 126 ? 28.923  -2.317  -14.168 1.00 16.79 ?  128 ARG A CB  1 
ATOM   939  N  N   . VAL A 1 127 ? 26.065  -2.540  -12.197 1.00 13.40 ?  129 VAL A N   1 
ATOM   940  C  CA  . VAL A 1 127 ? 25.532  -2.220  -10.884 1.00 10.26 ?  129 VAL A CA  1 
ATOM   941  C  C   . VAL A 1 127 ? 26.020  -3.300  -9.939  1.00 11.78 ?  129 VAL A C   1 
ATOM   942  O  O   . VAL A 1 127 ? 25.706  -4.482  -10.136 1.00 12.18 ?  129 VAL A O   1 
ATOM   943  C  CB  . VAL A 1 127 ? 23.999  -2.164  -10.883 1.00 9.40  ?  129 VAL A CB  1 
ATOM   944  C  CG1 . VAL A 1 127 ? 23.519  -1.745  -9.499  1.00 11.65 ?  129 VAL A CG1 1 
ATOM   945  C  CG2 . VAL A 1 127 ? 23.486  -1.229  -11.969 1.00 11.69 ?  129 VAL A CG2 1 
ATOM   946  N  N   . GLU A 1 128 ? 26.781  -2.902  -8.916  1.00 8.27  ?  130 GLU A N   1 
ATOM   947  C  CA  . GLU A 1 128 ? 27.352  -3.846  -7.967  1.00 9.68  ?  130 GLU A CA  1 
ATOM   948  C  C   . GLU A 1 128 ? 26.983  -3.431  -6.549  1.00 10.32 ?  130 GLU A C   1 
ATOM   949  O  O   . GLU A 1 128 ? 26.604  -2.284  -6.301  1.00 10.65 ?  130 GLU A O   1 
ATOM   950  C  CB  . GLU A 1 128 ? 28.873  -3.925  -8.145  1.00 12.82 ?  130 GLU A CB  1 
ATOM   951  C  CG  . GLU A 1 128 ? 29.208  -4.525  -9.502  1.00 12.63 ?  130 GLU A CG  1 
ATOM   952  C  CD  . GLU A 1 128 ? 30.690  -4.491  -9.856  1.00 20.82 ?  130 GLU A CD  1 
ATOM   953  O  OE1 . GLU A 1 128 ? 31.012  -4.862  -11.011 1.00 25.16 ?  130 GLU A OE1 1 
ATOM   954  O  OE2 . GLU A 1 128 ? 31.531  -4.086  -9.011  1.00 15.70 ?  130 GLU A OE2 1 
ATOM   955  N  N   . ASP A 1 129 ? 27.092  -4.383  -5.618  1.00 10.58 ?  131 ASP A N   1 
ATOM   956  C  CA  . ASP A 1 129 ? 26.745  -4.158  -4.216  1.00 7.38  ?  131 ASP A CA  1 
ATOM   957  C  C   . ASP A 1 129 ? 27.983  -4.017  -3.346  1.00 9.54  ?  131 ASP A C   1 
ATOM   958  O  O   . ASP A 1 129 ? 28.985  -4.712  -3.546  1.00 10.68 ?  131 ASP A O   1 
ATOM   959  C  CB  . ASP A 1 129 ? 25.904  -5.310  -3.672  1.00 11.40 ?  131 ASP A CB  1 
ATOM   960  C  CG  . ASP A 1 129 ? 24.559  -5.371  -4.335  1.00 12.63 ?  131 ASP A CG  1 
ATOM   961  O  OD1 . ASP A 1 129 ? 23.689  -4.554  -3.955  1.00 11.34 ?  131 ASP A OD1 1 
ATOM   962  O  OD2 . ASP A 1 129 ? 24.410  -6.199  -5.263  1.00 12.62 ?  131 ASP A OD2 1 
ATOM   963  N  N   . HIS A 1 130 ? 27.890  -3.136  -2.353  1.00 9.56  ?  132 HIS A N   1 
ATOM   964  C  CA  . HIS A 1 130 ? 28.895  -3.077  -1.299  1.00 8.92  ?  132 HIS A CA  1 
ATOM   965  C  C   . HIS A 1 130 ? 28.690  -4.246  -0.340  1.00 9.17  ?  132 HIS A C   1 
ATOM   966  O  O   . HIS A 1 130 ? 27.551  -4.620  -0.040  1.00 12.77 ?  132 HIS A O   1 
ATOM   967  C  CB  . HIS A 1 130 ? 28.783  -1.743  -0.549  1.00 8.38  ?  132 HIS A CB  1 
ATOM   968  C  CG  . HIS A 1 130 ? 29.595  -1.674  0.714   1.00 7.23  ?  132 HIS A CG  1 
ATOM   969  N  ND1 . HIS A 1 130 ? 29.028  -1.658  1.968   1.00 7.48  ?  132 HIS A ND1 1 
ATOM   970  C  CD2 . HIS A 1 130 ? 30.934  -1.568  0.908   1.00 6.64  ?  132 HIS A CD2 1 
ATOM   971  C  CE1 . HIS A 1 130 ? 29.980  -1.579  2.884   1.00 7.40  ?  132 HIS A CE1 1 
ATOM   972  N  NE2 . HIS A 1 130 ? 31.146  -1.519  2.266   1.00 8.44  ?  132 HIS A NE2 1 
ATOM   973  N  N   . TYR A 1 131 ? 29.798  -4.840  0.121   1.00 9.18  ?  133 TYR A N   1 
ATOM   974  C  CA  . TYR A 1 131 ? 29.792  -5.944  1.089   1.00 10.20 ?  133 TYR A CA  1 
ATOM   975  C  C   . TYR A 1 131 ? 30.642  -5.531  2.288   1.00 9.78  ?  133 TYR A C   1 
ATOM   976  O  O   . TYR A 1 131 ? 31.870  -5.639  2.251   1.00 9.68  ?  133 TYR A O   1 
ATOM   977  C  CB  . TYR A 1 131 ? 30.330  -7.237  0.457   1.00 10.47 ?  133 TYR A CB  1 
ATOM   978  C  CG  . TYR A 1 131 ? 29.363  -7.888  -0.517  1.00 12.36 ?  133 TYR A CG  1 
ATOM   979  C  CD1 . TYR A 1 131 ? 29.373  -7.556  -1.863  1.00 13.86 ?  133 TYR A CD1 1 
ATOM   980  C  CD2 . TYR A 1 131 ? 28.434  -8.825  -0.080  1.00 15.38 ?  133 TYR A CD2 1 
ATOM   981  C  CE1 . TYR A 1 131 ? 28.476  -8.141  -2.750  1.00 17.21 ?  133 TYR A CE1 1 
ATOM   982  C  CE2 . TYR A 1 131 ? 27.543  -9.422  -0.957  1.00 17.97 ?  133 TYR A CE2 1 
ATOM   983  C  CZ  . TYR A 1 131 ? 27.564  -9.074  -2.288  1.00 17.97 ?  133 TYR A CZ  1 
ATOM   984  O  OH  . TYR A 1 131 ? 26.682  -9.664  -3.170  1.00 19.14 ?  133 TYR A OH  1 
ATOM   985  N  N   . GLY A 1 132 ? 29.992  -5.100  3.370   1.00 10.45 ?  134 GLY A N   1 
ATOM   986  C  CA  . GLY A 1 132 ? 30.721  -4.533  4.489   1.00 11.17 ?  134 GLY A CA  1 
ATOM   987  C  C   . GLY A 1 132 ? 31.540  -5.530  5.283   1.00 10.92 ?  134 GLY A C   1 
ATOM   988  O  O   . GLY A 1 132 ? 32.510  -5.133  5.931   1.00 12.29 ?  134 GLY A O   1 
ATOM   989  N  N   . THR A 1 133 ? 31.194  -6.816  5.240   1.00 11.88 ?  135 THR A N   1 
ATOM   990  C  CA  . THR A 1 133 ? 32.006  -7.775  5.981   1.00 13.03 ?  135 THR A CA  1 
ATOM   991  C  C   . THR A 1 133 ? 33.202  -8.273  5.184   1.00 17.54 ?  135 THR A C   1 
ATOM   992  O  O   . THR A 1 133 ? 33.955  -9.110  5.693   1.00 19.65 ?  135 THR A O   1 
ATOM   993  C  CB  . THR A 1 133 ? 31.158  -8.969  6.432   1.00 11.69 ?  135 THR A CB  1 
ATOM   994  O  OG1 . THR A 1 133 ? 30.746  -9.736  5.294   1.00 16.17 ?  135 THR A OG1 1 
ATOM   995  C  CG2 . THR A 1 133 ? 29.918  -8.469  7.182   1.00 16.62 ?  135 THR A CG2 1 
ATOM   996  N  N   . ARG A 1 134 ? 33.394  -7.789  3.958   1.00 12.28 ?  136 ARG A N   1 
ATOM   997  C  CA  . ARG A 1 134 ? 34.537  -8.176  3.120   1.00 11.22 ?  136 ARG A CA  1 
ATOM   998  C  C   . ARG A 1 134 ? 35.590  -7.070  3.188   1.00 12.64 ?  136 ARG A C   1 
ATOM   999  O  O   . ARG A 1 134 ? 35.631  -6.171  2.340   1.00 10.22 ?  136 ARG A O   1 
ATOM   1000 C  CB  . ARG A 1 134 ? 34.104  -8.431  1.680   1.00 12.28 ?  136 ARG A CB  1 
ATOM   1001 C  CG  . ARG A 1 134 ? 33.062  -9.542  1.515   1.00 15.10 ?  136 ARG A CG  1 
ATOM   1002 C  CD  . ARG A 1 134 ? 32.952  -9.950  0.047   1.00 19.85 ?  136 ARG A CD  1 
ATOM   1003 N  NE  . ARG A 1 134 ? 31.778  -10.776 -0.227  1.00 25.21 ?  136 ARG A NE  1 
ATOM   1004 C  CZ  . ARG A 1 134 ? 31.238  -10.933 -1.437  1.00 31.42 ?  136 ARG A CZ  1 
ATOM   1005 N  NH1 . ARG A 1 134 ? 31.764  -10.314 -2.488  1.00 24.70 ?  136 ARG A NH1 1 
ATOM   1006 N  NH2 . ARG A 1 134 ? 30.174  -11.712 -1.601  1.00 31.11 ?  136 ARG A NH2 1 
ATOM   1007 N  N   . LEU A 1 135 ? 36.481  -7.161  4.184   1.00 12.55 ?  137 LEU A N   1 
ATOM   1008 C  CA  . LEU A 1 135 ? 37.498  -6.123  4.328   1.00 9.37  ?  137 LEU A CA  1 
ATOM   1009 C  C   . LEU A 1 135 ? 38.379  -6.038  3.092   1.00 11.85 ?  137 LEU A C   1 
ATOM   1010 O  O   . LEU A 1 135 ? 38.855  -4.953  2.741   1.00 12.49 ?  137 LEU A O   1 
ATOM   1011 C  CB  . LEU A 1 135 ? 38.347  -6.370  5.576   1.00 12.52 ?  137 LEU A CB  1 
ATOM   1012 C  CG  . LEU A 1 135 ? 39.259  -5.203  5.958   1.00 13.85 ?  137 LEU A CG  1 
ATOM   1013 C  CD1 . LEU A 1 135 ? 38.435  -3.974  6.327   1.00 10.96 ?  137 LEU A CD1 1 
ATOM   1014 C  CD2 . LEU A 1 135 ? 40.152  -5.593  7.125   1.00 15.44 ?  137 LEU A CD2 1 
ATOM   1015 N  N   . GLU A 1 136 ? 38.579  -7.167  2.402   1.00 12.61 ?  138 GLU A N   1 
ATOM   1016 C  CA  . GLU A 1 136 ? 39.456  -7.191  1.240   1.00 12.11 ?  138 GLU A CA  1 
ATOM   1017 C  C   . GLU A 1 136 ? 38.940  -6.323  0.107   1.00 14.39 ?  138 GLU A C   1 
ATOM   1018 O  O   . GLU A 1 136 ? 39.720  -5.969  -0.784  1.00 11.87 ?  138 GLU A O   1 
ATOM   1019 C  CB  . GLU A 1 136 ? 39.636  -8.631  0.758   1.00 14.82 ?  138 GLU A CB  1 
ATOM   1020 C  CG  . GLU A 1 136 ? 38.401  -9.203  0.088   1.00 15.07 ?  138 GLU A CG  1 
ATOM   1021 C  CD  . GLU A 1 136 ? 37.459  -9.907  1.071   1.00 21.67 ?  138 GLU A CD  1 
ATOM   1022 O  OE1 . GLU A 1 136 ? 36.533  -10.598 0.605   1.00 22.25 ?  138 GLU A OE1 1 
ATOM   1023 O  OE2 . GLU A 1 136 ? 37.652  -9.783  2.301   1.00 20.38 ?  138 GLU A OE2 1 
ATOM   1024 N  N   . GLU A 1 137 ? 37.656  -5.960  0.120   1.00 11.65 ?  139 GLU A N   1 
ATOM   1025 C  CA  . GLU A 1 137 ? 37.105  -5.079  -0.901  1.00 11.22 ?  139 GLU A CA  1 
ATOM   1026 C  C   . GLU A 1 137 ? 37.233  -3.601  -0.529  1.00 10.59 ?  139 GLU A C   1 
ATOM   1027 O  O   . GLU A 1 137 ? 36.686  -2.747  -1.237  1.00 11.08 ?  139 GLU A O   1 
ATOM   1028 C  CB  . GLU A 1 137 ? 35.637  -5.450  -1.176  1.00 10.90 ?  139 GLU A CB  1 
ATOM   1029 C  CG  . GLU A 1 137 ? 35.500  -6.891  -1.665  1.00 12.17 ?  139 GLU A CG  1 
ATOM   1030 C  CD  . GLU A 1 137 ? 34.134  -7.247  -2.220  1.00 18.99 ?  139 GLU A CD  1 
ATOM   1031 O  OE1 . GLU A 1 137 ? 33.176  -6.477  -2.017  1.00 18.66 ?  139 GLU A OE1 1 
ATOM   1032 O  OE2 . GLU A 1 137 ? 34.025  -8.323  -2.848  1.00 20.47 ?  139 GLU A OE2 1 
ATOM   1033 N  N   . HIS A 1 138 ? 37.955  -3.282  0.543   1.00 9.65  ?  140 HIS A N   1 
ATOM   1034 C  CA  . HIS A 1 138 ? 38.049  -1.926  1.063   1.00 8.91  ?  140 HIS A CA  1 
ATOM   1035 C  C   . HIS A 1 138 ? 39.499  -1.462  1.093   1.00 10.53 ?  140 HIS A C   1 
ATOM   1036 O  O   . HIS A 1 138 ? 40.430  -2.269  1.183   1.00 13.57 ?  140 HIS A O   1 
ATOM   1037 C  CB  . HIS A 1 138 ? 37.469  -1.855  2.481   1.00 10.31 ?  140 HIS A CB  1 
ATOM   1038 C  CG  . HIS A 1 138 ? 36.002  -2.122  2.523   1.00 8.04  ?  140 HIS A CG  1 
ATOM   1039 N  ND1 . HIS A 1 138 ? 35.482  -3.395  2.417   1.00 10.86 ?  140 HIS A ND1 1 
ATOM   1040 C  CD2 . HIS A 1 138 ? 34.940  -1.286  2.647   1.00 8.24  ?  140 HIS A CD2 1 
ATOM   1041 C  CE1 . HIS A 1 138 ? 34.162  -3.334  2.472   1.00 11.97 ?  140 HIS A CE1 1 
ATOM   1042 N  NE2 . HIS A 1 138 ? 33.809  -2.067  2.611   1.00 9.04  ?  140 HIS A NE2 1 
ATOM   1043 N  N   . THR A 1 139 ? 39.665  -0.142  1.055   1.00 11.69 ?  141 THR A N   1 
ATOM   1044 C  CA  . THR A 1 139 ? 40.960  0.519   1.152   1.00 10.78 ?  141 THR A CA  1 
ATOM   1045 C  C   . THR A 1 139 ? 41.024  1.309   2.454   1.00 11.69 ?  141 THR A C   1 
ATOM   1046 O  O   . THR A 1 139 ? 40.091  2.047   2.784   1.00 9.90  ?  141 THR A O   1 
ATOM   1047 C  CB  . THR A 1 139 ? 41.162  1.454   -0.050  1.00 12.59 ?  141 THR A CB  1 
ATOM   1048 O  OG1 . THR A 1 139 ? 41.246  0.662   -1.247  1.00 15.91 ?  141 THR A OG1 1 
ATOM   1049 C  CG2 . THR A 1 139 ? 42.460  2.287   0.088   1.00 12.67 ?  141 THR A CG2 1 
ATOM   1050 N  N   . TYR A 1 140 ? 42.133  1.174   3.178   1.00 10.07 ?  142 TYR A N   1 
ATOM   1051 C  CA  . TYR A 1 140 ? 42.358  1.953   4.392   1.00 9.77  ?  142 TYR A CA  1 
ATOM   1052 C  C   . TYR A 1 140 ? 42.807  3.376   4.050   1.00 12.77 ?  142 TYR A C   1 
ATOM   1053 O  O   . TYR A 1 140 ? 43.746  3.565   3.269   1.00 12.85 ?  142 TYR A O   1 
ATOM   1054 C  CB  . TYR A 1 140 ? 43.423  1.274   5.249   1.00 11.33 ?  142 TYR A CB  1 
ATOM   1055 C  CG  . TYR A 1 140 ? 43.823  2.047   6.490   1.00 11.84 ?  142 TYR A CG  1 
ATOM   1056 C  CD1 . TYR A 1 140 ? 42.972  2.145   7.586   1.00 12.53 ?  142 TYR A CD1 1 
ATOM   1057 C  CD2 . TYR A 1 140 ? 45.066  2.668   6.565   1.00 12.60 ?  142 TYR A CD2 1 
ATOM   1058 C  CE1 . TYR A 1 140 ? 43.353  2.845   8.720   1.00 13.56 ?  142 TYR A CE1 1 
ATOM   1059 C  CE2 . TYR A 1 140 ? 45.453  3.362   7.689   1.00 12.03 ?  142 TYR A CE2 1 
ATOM   1060 C  CZ  . TYR A 1 140 ? 44.599  3.450   8.763   1.00 12.45 ?  142 TYR A CZ  1 
ATOM   1061 O  OH  . TYR A 1 140 ? 44.989  4.145   9.888   1.00 13.46 ?  142 TYR A OH  1 
ATOM   1062 N  N   . LEU A 1 141 ? 42.154  4.375   4.665   1.00 10.34 ?  143 LEU A N   1 
ATOM   1063 C  CA  . LEU A 1 141 ? 42.406  5.784   4.369   1.00 8.66  ?  143 LEU A CA  1 
ATOM   1064 C  C   . LEU A 1 141 ? 42.990  6.570   5.533   1.00 17.10 ?  143 LEU A C   1 
ATOM   1065 O  O   . LEU A 1 141 ? 43.247  7.769   5.378   1.00 18.97 ?  143 LEU A O   1 
ATOM   1066 C  CB  . LEU A 1 141 ? 41.115  6.478   3.919   1.00 11.41 ?  143 LEU A CB  1 
ATOM   1067 C  CG  . LEU A 1 141 ? 40.453  5.807   2.733   1.00 12.83 ?  143 LEU A CG  1 
ATOM   1068 C  CD1 . LEU A 1 141 ? 39.109  6.461   2.439   1.00 12.07 ?  143 LEU A CD1 1 
ATOM   1069 C  CD2 . LEU A 1 141 ? 41.381  5.897   1.542   1.00 15.61 ?  143 LEU A CD2 1 
ATOM   1070 N  N   . GLY A 1 142 ? 43.198  5.948   6.685   1.00 11.96 ?  144 GLY A N   1 
ATOM   1071 C  CA  . GLY A 1 142 ? 43.620  6.648   7.882   1.00 12.85 ?  144 GLY A CA  1 
ATOM   1072 C  C   . GLY A 1 142 ? 42.706  6.332   9.047   1.00 15.24 ?  144 GLY A C   1 
ATOM   1073 O  O   . GLY A 1 142 ? 41.681  5.670   8.912   1.00 11.62 ?  144 GLY A O   1 
ATOM   1074 N  N   . THR A 1 143 ? 43.115  6.820   10.216  1.00 14.41 ?  145 THR A N   1 
ATOM   1075 C  CA  . THR A 1 143 ? 42.351  6.638   11.440  1.00 12.98 ?  145 THR A CA  1 
ATOM   1076 C  C   . THR A 1 143 ? 42.026  8.009   12.019  1.00 15.90 ?  145 THR A C   1 
ATOM   1077 O  O   . THR A 1 143 ? 42.880  8.899   12.031  1.00 14.37 ?  145 THR A O   1 
ATOM   1078 C  CB  . THR A 1 143 ? 43.142  5.762   12.426  1.00 16.32 ?  145 THR A CB  1 
ATOM   1079 O  OG1 . THR A 1 143 ? 43.214  4.429   11.908  1.00 13.49 ?  145 THR A OG1 1 
ATOM   1080 C  CG2 . THR A 1 143 ? 42.514  5.738   13.816  1.00 13.41 ?  145 THR A CG2 1 
ATOM   1081 N  N   . THR A 1 144 ? 40.778  8.192   12.462  1.00 12.32 ?  146 THR A N   1 
ATOM   1082 C  CA  . THR A 1 144 ? 40.348  9.485   12.983  1.00 12.47 ?  146 THR A CA  1 
ATOM   1083 C  C   . THR A 1 144 ? 40.950  9.735   14.362  1.00 12.82 ?  146 THR A C   1 
ATOM   1084 O  O   . THR A 1 144 ? 41.427  8.807   15.022  1.00 14.44 ?  146 THR A O   1 
ATOM   1085 C  CB  . THR A 1 144 ? 38.827  9.558   13.101  1.00 10.94 ?  146 THR A CB  1 
ATOM   1086 O  OG1 . THR A 1 144 ? 38.391  8.665   14.126  1.00 10.56 ?  146 THR A OG1 1 
ATOM   1087 C  CG2 . THR A 1 144 ? 38.127  9.231   11.758  1.00 13.20 ?  146 THR A CG2 1 
ATOM   1088 N  N   . PRO A 1 145 ? 40.910  10.984  14.836  1.00 14.76 ?  147 PRO A N   1 
ATOM   1089 C  CA  . PRO A 1 145 ? 41.368  11.243  16.209  1.00 15.05 ?  147 PRO A CA  1 
ATOM   1090 C  C   . PRO A 1 145 ? 40.594  10.465  17.252  1.00 17.00 ?  147 PRO A C   1 
ATOM   1091 O  O   . PRO A 1 145 ? 41.155  10.129  18.303  1.00 16.26 ?  147 PRO A O   1 
ATOM   1092 C  CB  . PRO A 1 145 ? 41.176  12.756  16.361  1.00 17.56 ?  147 PRO A CB  1 
ATOM   1093 C  CG  . PRO A 1 145 ? 41.316  13.280  14.986  1.00 16.27 ?  147 PRO A CG  1 
ATOM   1094 C  CD  . PRO A 1 145 ? 40.645  12.236  14.105  1.00 13.30 ?  147 PRO A CD  1 
ATOM   1095 N  N   . ASN A 1 146 ? 39.327  10.140  16.983  1.00 16.15 ?  148 ASN A N   1 
ATOM   1096 C  CA  . ASN A 1 146 ? 38.546  9.286   17.873  1.00 14.16 ?  148 ASN A CA  1 
ATOM   1097 C  C   . ASN A 1 146 ? 38.933  7.818   17.785  1.00 15.29 ?  148 ASN A C   1 
ATOM   1098 O  O   . ASN A 1 146 ? 38.328  6.996   18.482  1.00 19.53 ?  148 ASN A O   1 
ATOM   1099 C  CB  . ASN A 1 146 ? 37.049  9.423   17.571  1.00 14.42 ?  148 ASN A CB  1 
ATOM   1100 C  CG  . ASN A 1 146 ? 36.431  10.642  18.229  1.00 21.47 ?  148 ASN A CG  1 
ATOM   1101 O  OD1 . ASN A 1 146 ? 36.839  11.026  19.319  1.00 22.10 ?  148 ASN A OD1 1 
ATOM   1102 N  ND2 . ASN A 1 146 ? 35.419  11.238  17.582  1.00 19.46 ?  148 ASN A ND2 1 
ATOM   1103 N  N   . GLY A 1 147 ? 39.889  7.460   16.936  1.00 14.00 ?  149 GLY A N   1 
ATOM   1104 C  CA  . GLY A 1 147 ? 40.359  6.093   16.869  1.00 13.96 ?  149 GLY A CA  1 
ATOM   1105 C  C   . GLY A 1 147 ? 39.621  5.190   15.910  1.00 13.58 ?  149 GLY A C   1 
ATOM   1106 O  O   . GLY A 1 147 ? 39.786  3.967   15.989  1.00 15.86 ?  149 GLY A O   1 
ATOM   1107 N  N   . VAL A 1 148 ? 38.823  5.732   14.994  1.00 11.61 ?  150 VAL A N   1 
ATOM   1108 C  CA  . VAL A 1 148 ? 38.041  4.918   14.068  1.00 11.98 ?  150 VAL A CA  1 
ATOM   1109 C  C   . VAL A 1 148 ? 38.829  4.783   12.768  1.00 9.98  ?  150 VAL A C   1 
ATOM   1110 O  O   . VAL A 1 148 ? 39.118  5.807   12.125  1.00 11.14 ?  150 VAL A O   1 
ATOM   1111 C  CB  . VAL A 1 148 ? 36.659  5.520   13.793  1.00 10.56 ?  150 VAL A CB  1 
ATOM   1112 C  CG1 . VAL A 1 148 ? 35.926  4.649   12.774  1.00 10.44 ?  150 VAL A CG1 1 
ATOM   1113 C  CG2 . VAL A 1 148 ? 35.842  5.642   15.068  1.00 10.01 ?  150 VAL A CG2 1 
ATOM   1114 N  N   . PRO A 1 149 ? 39.162  3.572   12.332  1.00 10.83 ?  151 PRO A N   1 
ATOM   1115 C  CA  . PRO A 1 149 ? 39.848  3.419   11.049  1.00 11.31 ?  151 PRO A CA  1 
ATOM   1116 C  C   . PRO A 1 149 ? 38.857  3.569   9.913   1.00 11.40 ?  151 PRO A C   1 
ATOM   1117 O  O   . PRO A 1 149 ? 37.703  3.131   10.002  1.00 13.49 ?  151 PRO A O   1 
ATOM   1118 C  CB  . PRO A 1 149 ? 40.411  1.993   11.117  1.00 11.35 ?  151 PRO A CB  1 
ATOM   1119 C  CG  . PRO A 1 149 ? 39.383  1.259   11.959  1.00 9.53  ?  151 PRO A CG  1 
ATOM   1120 C  CD  . PRO A 1 149 ? 38.928  2.276   12.998  1.00 11.84 ?  151 PRO A CD  1 
ATOM   1121 N  N   . ALA A 1 150 ? 39.309  4.197   8.840   1.00 10.55 ?  152 ALA A N   1 
ATOM   1122 C  CA  . ALA A 1 150 ? 38.455  4.466   7.687   1.00 9.82  ?  152 ALA A CA  1 
ATOM   1123 C  C   . ALA A 1 150 ? 38.766  3.444   6.601   1.00 11.00 ?  152 ALA A C   1 
ATOM   1124 O  O   . ALA A 1 150 ? 39.832  3.493   5.976   1.00 11.69 ?  152 ALA A O   1 
ATOM   1125 C  CB  . ALA A 1 150 ? 38.648  5.894   7.175   1.00 10.54 ?  152 ALA A CB  1 
ATOM   1126 N  N   . TRP A 1 151 ? 37.826  2.528   6.374   1.00 9.95  ?  153 TRP A N   1 
ATOM   1127 C  CA  . TRP A 1 151 ? 37.928  1.473   5.369   1.00 10.56 ?  153 TRP A CA  1 
ATOM   1128 C  C   . TRP A 1 151 ? 36.758  1.642   4.408   1.00 9.06  ?  153 TRP A C   1 
ATOM   1129 O  O   . TRP A 1 151 ? 35.607  1.409   4.791   1.00 9.12  ?  153 TRP A O   1 
ATOM   1130 C  CB  . TRP A 1 151 ? 37.875  0.092   6.021   1.00 9.70  ?  153 TRP A CB  1 
ATOM   1131 C  CG  . TRP A 1 151 ? 39.051  -0.303  6.875   1.00 10.31 ?  153 TRP A CG  1 
ATOM   1132 C  CD1 . TRP A 1 151 ? 39.179  -0.159  8.233   1.00 9.64  ?  153 TRP A CD1 1 
ATOM   1133 C  CD2 . TRP A 1 151 ? 40.247  -0.948  6.425   1.00 10.77 ?  153 TRP A CD2 1 
ATOM   1134 N  NE1 . TRP A 1 151 ? 40.391  -0.679  8.648   1.00 12.56 ?  153 TRP A NE1 1 
ATOM   1135 C  CE2 . TRP A 1 151 ? 41.061  -1.166  7.558   1.00 14.74 ?  153 TRP A CE2 1 
ATOM   1136 C  CE3 . TRP A 1 151 ? 40.706  -1.363  5.169   1.00 11.06 ?  153 TRP A CE3 1 
ATOM   1137 C  CZ2 . TRP A 1 151 ? 42.318  -1.789  7.475   1.00 14.57 ?  153 TRP A CZ2 1 
ATOM   1138 C  CZ3 . TRP A 1 151 ? 41.950  -1.991  5.085   1.00 13.16 ?  153 TRP A CZ3 1 
ATOM   1139 C  CH2 . TRP A 1 151 ? 42.744  -2.184  6.235   1.00 13.57 ?  153 TRP A CH2 1 
ATOM   1140 N  N   . ILE A 1 152 ? 37.048  2.016   3.163   1.00 8.81  ?  154 ILE A N   1 
ATOM   1141 C  CA  . ILE A 1 152 ? 36.039  2.469   2.214   1.00 8.91  ?  154 ILE A CA  1 
ATOM   1142 C  C   . ILE A 1 152 ? 36.198  1.649   0.942   1.00 9.45  ?  154 ILE A C   1 
ATOM   1143 O  O   . ILE A 1 152 ? 37.326  1.328   0.545   1.00 9.51  ?  154 ILE A O   1 
ATOM   1144 C  CB  . ILE A 1 152 ? 36.193  3.982   1.942   1.00 9.02  ?  154 ILE A CB  1 
ATOM   1145 C  CG1 . ILE A 1 152 ? 36.035  4.770   3.251   1.00 10.04 ?  154 ILE A CG1 1 
ATOM   1146 C  CG2 . ILE A 1 152 ? 35.229  4.467   0.867   1.00 8.53  ?  154 ILE A CG2 1 
ATOM   1147 C  CD1 . ILE A 1 152 ? 34.665  4.626   3.954   1.00 10.09 ?  154 ILE A CD1 1 
ATOM   1148 N  N   . ASP A 1 153 ? 35.070  1.288   0.320   1.00 7.59  ?  155 ASP A N   1 
ATOM   1149 C  CA  . ASP A 1 153 ? 35.088  0.407   -0.845  1.00 8.71  ?  155 ASP A CA  1 
ATOM   1150 C  C   . ASP A 1 153 ? 36.110  0.855   -1.885  1.00 8.16  ?  155 ASP A C   1 
ATOM   1151 O  O   . ASP A 1 153 ? 36.110  2.008   -2.330  1.00 8.04  ?  155 ASP A O   1 
ATOM   1152 C  CB  . ASP A 1 153 ? 33.695  0.341   -1.477  1.00 6.99  ?  155 ASP A CB  1 
ATOM   1153 C  CG  . ASP A 1 153 ? 33.542  -0.842  -2.426  1.00 10.82 ?  155 ASP A CG  1 
ATOM   1154 O  OD1 . ASP A 1 153 ? 34.172  -0.807  -3.505  1.00 10.15 ?  155 ASP A OD1 1 
ATOM   1155 O  OD2 . ASP A 1 153 ? 32.791  -1.802  -2.101  1.00 11.77 ?  155 ASP A OD2 1 
ATOM   1156 N  N   . SER A 1 154 ? 36.972  -0.080  -2.293  1.00 9.18  ?  156 SER A N   1 
ATOM   1157 C  CA  . SER A 1 154 ? 38.076  0.289   -3.176  1.00 11.14 ?  156 SER A CA  1 
ATOM   1158 C  C   . SER A 1 154 ? 37.599  0.708   -4.558  1.00 9.93  ?  156 SER A C   1 
ATOM   1159 O  O   . SER A 1 154 ? 38.298  1.467   -5.246  1.00 11.03 ?  156 SER A O   1 
ATOM   1160 C  CB  . SER A 1 154 ? 39.062  -0.874  -3.275  1.00 9.23  ?  156 SER A CB  1 
ATOM   1161 O  OG  . SER A 1 154 ? 39.479  -1.261  -1.977  1.00 10.58 ?  156 SER A OG  1 
ATOM   1162 N  N   . ARG A 1 155 ? 36.429  0.231   -4.990  1.00 8.68  ?  157 ARG A N   1 
ATOM   1163 C  CA  . ARG A 1 155 ? 35.934  0.634   -6.300  1.00 10.76 ?  157 ARG A CA  1 
ATOM   1164 C  C   . ARG A 1 155 ? 35.624  2.123   -6.342  1.00 13.06 ?  157 ARG A C   1 
ATOM   1165 O  O   . ARG A 1 155 ? 35.806  2.765   -7.378  1.00 14.87 ?  157 ARG A O   1 
ATOM   1166 C  CB  . ARG A 1 155 ? 34.689  -0.171  -6.668  1.00 11.98 ?  157 ARG A CB  1 
ATOM   1167 C  CG  . ARG A 1 155 ? 34.985  -1.614  -7.002  1.00 11.17 ?  157 ARG A CG  1 
ATOM   1168 C  CD  . ARG A 1 155 ? 33.713  -2.426  -6.969  1.00 9.43  ?  157 ARG A CD  1 
ATOM   1169 N  NE  . ARG A 1 155 ? 33.177  -2.556  -5.616  1.00 11.03 ?  157 ARG A NE  1 
ATOM   1170 C  CZ  . ARG A 1 155 ? 32.245  -3.435  -5.277  1.00 12.34 ?  157 ARG A CZ  1 
ATOM   1171 N  NH1 . ARG A 1 155 ? 31.718  -4.210  -6.218  1.00 11.93 ?  157 ARG A NH1 1 
ATOM   1172 N  NH2 . ARG A 1 155 ? 31.820  -3.522  -4.013  1.00 11.11 ?  157 ARG A NH2 1 
ATOM   1173 N  N   . TYR A 1 156 ? 35.158  2.675   -5.226  1.00 11.21 ?  158 TYR A N   1 
ATOM   1174 C  CA  . TYR A 1 156 ? 34.921  4.103   -5.108  1.00 9.03  ?  158 TYR A CA  1 
ATOM   1175 C  C   . TYR A 1 156 ? 36.223  4.866   -4.933  1.00 10.73 ?  158 TYR A C   1 
ATOM   1176 O  O   . TYR A 1 156 ? 36.452  5.884   -5.596  1.00 10.14 ?  158 TYR A O   1 
ATOM   1177 C  CB  . TYR A 1 156 ? 34.008  4.348   -3.913  1.00 7.54  ?  158 TYR A CB  1 
ATOM   1178 C  CG  . TYR A 1 156 ? 33.639  5.782   -3.634  1.00 6.81  ?  158 TYR A CG  1 
ATOM   1179 C  CD1 . TYR A 1 156 ? 32.595  6.408   -4.319  1.00 9.67  ?  158 TYR A CD1 1 
ATOM   1180 C  CD2 . TYR A 1 156 ? 34.303  6.498   -2.648  1.00 7.34  ?  158 TYR A CD2 1 
ATOM   1181 C  CE1 . TYR A 1 156 ? 32.247  7.721   -4.036  1.00 10.41 ?  158 TYR A CE1 1 
ATOM   1182 C  CE2 . TYR A 1 156 ? 33.943  7.805   -2.355  1.00 9.99  ?  158 TYR A CE2 1 
ATOM   1183 C  CZ  . TYR A 1 156 ? 32.919  8.401   -3.052  1.00 10.74 ?  158 TYR A CZ  1 
ATOM   1184 O  OH  . TYR A 1 156 ? 32.579  9.700   -2.754  1.00 11.17 ?  158 TYR A OH  1 
ATOM   1185 N  N   . VAL A 1 157 ? 37.079  4.384   -4.026  1.00 9.99  ?  159 VAL A N   1 
ATOM   1186 C  CA  . VAL A 1 157 ? 38.338  5.068   -3.731  1.00 9.02  ?  159 VAL A CA  1 
ATOM   1187 C  C   . VAL A 1 157 ? 39.175  5.218   -4.996  1.00 11.81 ?  159 VAL A C   1 
ATOM   1188 O  O   . VAL A 1 157 ? 39.807  6.261   -5.223  1.00 14.00 ?  159 VAL A O   1 
ATOM   1189 C  CB  . VAL A 1 157 ? 39.089  4.305   -2.623  1.00 10.20 ?  159 VAL A CB  1 
ATOM   1190 C  CG1 . VAL A 1 157 ? 40.525  4.823   -2.476  1.00 12.89 ?  159 VAL A CG1 1 
ATOM   1191 C  CG2 . VAL A 1 157 ? 38.322  4.407   -1.304  1.00 13.12 ?  159 VAL A CG2 1 
ATOM   1192 N  N   . GLN A 1 158 ? 39.165  4.200   -5.858  1.00 11.01 ?  160 GLN A N   1 
ATOM   1193 C  CA  . GLN A 1 158 ? 39.997  4.222   -7.057  1.00 11.66 ?  160 GLN A CA  1 
ATOM   1194 C  C   . GLN A 1 158 ? 39.353  4.929   -8.248  1.00 14.44 ?  160 GLN A C   1 
ATOM   1195 O  O   . GLN A 1 158 ? 40.025  5.128   -9.270  1.00 14.04 ?  160 GLN A O   1 
ATOM   1196 C  CB  . GLN A 1 158 ? 40.381  2.792   -7.451  1.00 15.29 ?  160 GLN A CB  1 
ATOM   1197 C  CG  . GLN A 1 158 ? 41.426  2.209   -6.505  1.00 16.92 ?  160 GLN A CG  1 
ATOM   1198 C  CD  . GLN A 1 158 ? 41.595  0.704   -6.663  1.00 25.82 ?  160 GLN A CD  1 
ATOM   1199 O  OE1 . GLN A 1 158 ? 41.352  0.153   -7.740  1.00 32.68 ?  160 GLN A OE1 1 
ATOM   1200 N  NE2 . GLN A 1 158 ? 42.050  0.039   -5.602  1.00 28.84 ?  160 GLN A NE2 1 
ATOM   1201 N  N   . ALA A 1 159 ? 38.083  5.319   -8.157  1.00 10.06 ?  161 ALA A N   1 
ATOM   1202 C  CA  . ALA A 1 159 ? 37.427  5.986   -9.276  1.00 11.95 ?  161 ALA A CA  1 
ATOM   1203 C  C   . ALA A 1 159 ? 37.941  7.420   -9.445  1.00 12.85 ?  161 ALA A C   1 
ATOM   1204 O  O   . ALA A 1 159 ? 38.168  8.128   -8.461  1.00 12.83 ?  161 ALA A O   1 
ATOM   1205 C  CB  . ALA A 1 159 ? 35.916  6.002   -9.055  1.00 11.44 ?  161 ALA A CB  1 
ATOM   1206 N  N   . ASP A 1 160 ? 38.102  7.855   -10.708 1.00 11.53 ?  162 ASP A N   1 
ATOM   1207 C  CA  . ASP A 1 160 ? 38.521  9.235   -10.980 1.00 11.42 ?  162 ASP A CA  1 
ATOM   1208 C  C   . ASP A 1 160 ? 37.512  10.251  -10.474 1.00 12.87 ?  162 ASP A C   1 
ATOM   1209 O  O   . ASP A 1 160 ? 37.886  11.329  -9.991  1.00 12.58 ?  162 ASP A O   1 
ATOM   1210 C  CB  . ASP A 1 160 ? 38.703  9.475   -12.479 1.00 15.10 ?  162 ASP A CB  1 
ATOM   1211 C  CG  . ASP A 1 160 ? 39.985  8.901   -13.025 1.00 27.43 ?  162 ASP A CG  1 
ATOM   1212 O  OD1 . ASP A 1 160 ? 40.756  8.287   -12.256 1.00 30.21 ?  162 ASP A OD1 1 
ATOM   1213 O  OD2 . ASP A 1 160 ? 40.222  9.091   -14.238 1.00 29.99 ?  162 ASP A OD2 1 
ATOM   1214 N  N   . LEU A 1 161 ? 36.228  9.951   -10.644 1.00 10.85 ?  163 LEU A N   1 
ATOM   1215 C  CA  . LEU A 1 161 ? 35.130  10.853  -10.322 1.00 11.56 ?  163 LEU A CA  1 
ATOM   1216 C  C   . LEU A 1 161 ? 34.208  10.132  -9.351  1.00 11.95 ?  163 LEU A C   1 
ATOM   1217 O  O   . LEU A 1 161 ? 33.737  9.025   -9.645  1.00 11.30 ?  163 LEU A O   1 
ATOM   1218 C  CB  . LEU A 1 161 ? 34.388  11.272  -11.593 1.00 10.40 ?  163 LEU A CB  1 
ATOM   1219 C  CG  . LEU A 1 161 ? 33.241  12.271  -11.434 1.00 11.96 ?  163 LEU A CG  1 
ATOM   1220 C  CD1 . LEU A 1 161 ? 33.748  13.616  -10.925 1.00 14.24 ?  163 LEU A CD1 1 
ATOM   1221 C  CD2 . LEU A 1 161 ? 32.520  12.427  -12.773 1.00 15.46 ?  163 LEU A CD2 1 
ATOM   1222 N  N   . LYS A 1 162 ? 33.983  10.750  -8.188  1.00 8.36  ?  164 LYS A N   1 
ATOM   1223 C  CA  . LYS A 1 162 ? 33.205  10.179  -7.098  1.00 8.77  ?  164 LYS A CA  1 
ATOM   1224 C  C   . LYS A 1 162 ? 31.901  10.954  -6.963  1.00 7.96  ?  164 LYS A C   1 
ATOM   1225 O  O   . LYS A 1 162 ? 31.924  12.166  -6.724  1.00 11.32 ?  164 LYS A O   1 
ATOM   1226 C  CB  . LYS A 1 162 ? 34.013  10.257  -5.807  1.00 8.43  ?  164 LYS A CB  1 
ATOM   1227 C  CG  . LYS A 1 162 ? 35.264  9.380   -5.827  1.00 11.23 ?  164 LYS A CG  1 
ATOM   1228 C  CD  . LYS A 1 162 ? 36.165  9.730   -4.631  1.00 9.61  ?  164 LYS A CD  1 
ATOM   1229 C  CE  . LYS A 1 162 ? 37.419  8.848   -4.547  1.00 15.38 ?  164 LYS A CE  1 
ATOM   1230 N  NZ  . LYS A 1 162 ? 38.207  8.891   -5.803  1.00 16.81 ?  164 LYS A NZ  1 
ATOM   1231 N  N   . ILE A 1 163 ? 30.770  10.257  -7.093  1.00 8.74  ?  165 ILE A N   1 
ATOM   1232 C  CA  . ILE A 1 163 ? 29.455  10.888  -7.059  1.00 9.73  ?  165 ILE A CA  1 
ATOM   1233 C  C   . ILE A 1 163 ? 28.588  10.117  -6.073  1.00 8.14  ?  165 ILE A C   1 
ATOM   1234 O  O   . ILE A 1 163 ? 28.660  8.885   -6.010  1.00 8.62  ?  165 ILE A O   1 
ATOM   1235 C  CB  . ILE A 1 163 ? 28.813  10.900  -8.467  1.00 9.04  ?  165 ILE A CB  1 
ATOM   1236 C  CG1 . ILE A 1 163 ? 29.644  11.769  -9.432  1.00 10.46 ?  165 ILE A CG1 1 
ATOM   1237 C  CG2 . ILE A 1 163 ? 27.348  11.349  -8.407  1.00 9.40  ?  165 ILE A CG2 1 
ATOM   1238 C  CD1 . ILE A 1 163 ? 29.306  11.510  -10.903 1.00 11.88 ?  165 ILE A CD1 1 
ATOM   1239 N  N   . ALA A 1 164 ? 27.793  10.830  -5.273  1.00 9.85  ?  166 ALA A N   1 
ATOM   1240 C  CA  . ALA A 1 164 ? 26.878  10.159  -4.352  1.00 8.03  ?  166 ALA A CA  1 
ATOM   1241 C  C   . ALA A 1 164 ? 25.481  10.754  -4.462  1.00 10.39 ?  166 ALA A C   1 
ATOM   1242 O  O   . ALA A 1 164 ? 25.322  11.970  -4.571  1.00 11.23 ?  166 ALA A O   1 
ATOM   1243 C  CB  . ALA A 1 164 ? 27.374  10.253  -2.907  1.00 11.02 ?  166 ALA A CB  1 
ATOM   1244 N  N   . THR A 1 165 ? 24.471  9.890   -4.464  1.00 8.71  ?  167 THR A N   1 
ATOM   1245 C  CA  . THR A 1 165 ? 23.082  10.316  -4.518  1.00 8.04  ?  167 THR A CA  1 
ATOM   1246 C  C   . THR A 1 165 ? 22.362  9.858   -3.258  1.00 13.31 ?  167 THR A C   1 
ATOM   1247 O  O   . THR A 1 165 ? 22.755  8.875   -2.622  1.00 12.77 ?  167 THR A O   1 
ATOM   1248 C  CB  . THR A 1 165 ? 22.372  9.743   -5.740  1.00 10.73 ?  167 THR A CB  1 
ATOM   1249 O  OG1 . THR A 1 165 ? 22.343  8.317   -5.627  1.00 10.72 ?  167 THR A OG1 1 
ATOM   1250 C  CG2 . THR A 1 165 ? 23.094  10.136  -7.027  1.00 10.87 ?  167 THR A CG2 1 
ATOM   1251 N  N   . GLY A 1 166 ? 21.277  10.539  -2.900  1.00 8.37  ?  168 GLY A N   1 
ATOM   1252 C  CA  . GLY A 1 166 ? 20.570  10.097  -1.713  1.00 8.75  ?  168 GLY A CA  1 
ATOM   1253 C  C   . GLY A 1 166 ? 19.415  11.000  -1.339  1.00 8.82  ?  168 GLY A C   1 
ATOM   1254 O  O   . GLY A 1 166 ? 18.975  11.843  -2.126  1.00 8.50  ?  168 GLY A O   1 
ATOM   1255 N  N   . LEU A 1 167 ? 18.967  10.816  -0.097  1.00 8.94  ?  169 LEU A N   1 
ATOM   1256 C  CA  . LEU A 1 167 ? 17.676  11.282  0.380   1.00 7.43  ?  169 LEU A CA  1 
ATOM   1257 C  C   . LEU A 1 167 ? 17.837  11.795  1.803   1.00 8.38  ?  169 LEU A C   1 
ATOM   1258 O  O   . LEU A 1 167 ? 18.340  11.071  2.668   1.00 11.67 ?  169 LEU A O   1 
ATOM   1259 C  CB  . LEU A 1 167 ? 16.671  10.128  0.324   1.00 8.87  ?  169 LEU A CB  1 
ATOM   1260 C  CG  . LEU A 1 167 ? 15.412  10.229  1.170   1.00 8.46  ?  169 LEU A CG  1 
ATOM   1261 C  CD1 . LEU A 1 167 ? 14.563  11.419  0.681   1.00 9.43  ?  169 LEU A CD1 1 
ATOM   1262 C  CD2 . LEU A 1 167 ? 14.616  8.902   1.080   1.00 11.59 ?  169 LEU A CD2 1 
ATOM   1263 N  N   . ILE A 1 168 ? 17.416  13.033  2.049   1.00 7.39  ?  170 ILE A N   1 
ATOM   1264 C  CA  . ILE A 1 168 ? 17.577  13.657  3.362   1.00 6.74  ?  170 ILE A CA  1 
ATOM   1265 C  C   . ILE A 1 168 ? 16.293  13.442  4.161   1.00 9.28  ?  170 ILE A C   1 
ATOM   1266 O  O   . ILE A 1 168 ? 15.255  14.047  3.864   1.00 9.73  ?  170 ILE A O   1 
ATOM   1267 C  CB  . ILE A 1 168 ? 17.933  15.146  3.230   1.00 8.25  ?  170 ILE A CB  1 
ATOM   1268 C  CG1 . ILE A 1 168 ? 19.270  15.280  2.468   1.00 10.68 ?  170 ILE A CG1 1 
ATOM   1269 C  CG2 . ILE A 1 168 ? 18.028  15.809  4.618   1.00 9.78  ?  170 ILE A CG2 1 
ATOM   1270 C  CD1 . ILE A 1 168 ? 19.615  16.714  2.054   1.00 9.25  ?  170 ILE A CD1 1 
ATOM   1271 N  N   . GLU A 1 169 ? 16.362  12.558  5.160   1.00 8.48  ?  171 GLU A N   1 
ATOM   1272 C  CA  . GLU A 1 169 ? 15.294  12.228  6.092   1.00 9.36  ?  171 GLU A CA  1 
ATOM   1273 C  C   . GLU A 1 169 ? 15.898  12.229  7.485   1.00 8.10  ?  171 GLU A C   1 
ATOM   1274 O  O   . GLU A 1 169 ? 17.108  12.060  7.629   1.00 8.76  ?  171 GLU A O   1 
ATOM   1275 C  CB  . GLU A 1 169 ? 14.700  10.835  5.820   1.00 9.19  ?  171 GLU A CB  1 
ATOM   1276 C  CG  . GLU A 1 169 ? 13.959  10.720  4.488   1.00 8.92  ?  171 GLU A CG  1 
ATOM   1277 C  CD  . GLU A 1 169 ? 12.534  11.225  4.542   1.00 11.72 ?  171 GLU A CD  1 
ATOM   1278 O  OE1 . GLU A 1 169 ? 11.774  10.937  3.583   1.00 14.27 ?  171 GLU A OE1 1 
ATOM   1279 O  OE2 . GLU A 1 169 ? 12.175  11.896  5.535   1.00 11.04 ?  171 GLU A OE2 1 
ATOM   1280 N  N   . PRO A 1 170 ? 15.082  12.358  8.533   1.00 8.19  ?  172 PRO A N   1 
ATOM   1281 C  CA  . PRO A 1 170 ? 15.607  12.169  9.893   1.00 8.69  ?  172 PRO A CA  1 
ATOM   1282 C  C   . PRO A 1 170 ? 16.232  10.793  10.055  1.00 10.81 ?  172 PRO A C   1 
ATOM   1283 O  O   . PRO A 1 170 ? 15.802  9.822   9.434   1.00 9.62  ?  172 PRO A O   1 
ATOM   1284 C  CB  . PRO A 1 170 ? 14.359  12.307  10.774  1.00 13.06 ?  172 PRO A CB  1 
ATOM   1285 C  CG  . PRO A 1 170 ? 13.416  13.164  9.938   1.00 9.72  ?  172 PRO A CG  1 
ATOM   1286 C  CD  . PRO A 1 170 ? 13.643  12.693  8.542   1.00 8.05  ?  172 PRO A CD  1 
ATOM   1287 N  N   . HIS A 1 171 ? 17.264  10.720  10.901  1.00 8.27  ?  173 HIS A N   1 
ATOM   1288 C  CA  . HIS A 1 171 ? 17.940  9.455   11.164  1.00 9.12  ?  173 HIS A CA  1 
ATOM   1289 C  C   . HIS A 1 171 ? 18.244  9.344   12.644  1.00 8.88  ?  173 HIS A C   1 
ATOM   1290 O  O   . HIS A 1 171 ? 18.779  10.281  13.244  1.00 9.02  ?  173 HIS A O   1 
ATOM   1291 C  CB  . HIS A 1 171 ? 19.251  9.317   10.372  1.00 8.33  ?  173 HIS A CB  1 
ATOM   1292 C  CG  . HIS A 1 171 ? 19.810  7.923   10.388  1.00 7.21  ?  173 HIS A CG  1 
ATOM   1293 N  ND1 . HIS A 1 171 ? 20.731  7.492   11.326  1.00 7.50  ?  173 HIS A ND1 1 
ATOM   1294 C  CD2 . HIS A 1 171 ? 19.549  6.856   9.594   1.00 7.81  ?  173 HIS A CD2 1 
ATOM   1295 C  CE1 . HIS A 1 171 ? 21.004  6.218   11.110  1.00 9.21  ?  173 HIS A CE1 1 
ATOM   1296 N  NE2 . HIS A 1 171 ? 20.306  5.810   10.062  1.00 7.97  ?  173 HIS A NE2 1 
ATOM   1297 N  N   . LEU A 1 172 ? 17.974  8.162   13.213  1.00 6.64  ?  174 LEU A N   1 
ATOM   1298 C  CA  . LEU A 1 172 ? 17.997  7.985   14.664  1.00 10.00 ?  174 LEU A CA  1 
ATOM   1299 C  C   . LEU A 1 172 ? 19.398  7.993   15.253  1.00 9.31  ?  174 LEU A C   1 
ATOM   1300 O  O   . LEU A 1 172 ? 19.524  8.074   16.481  1.00 10.59 ?  174 LEU A O   1 
ATOM   1301 C  CB  . LEU A 1 172 ? 17.298  6.677   15.043  1.00 8.09  ?  174 LEU A CB  1 
ATOM   1302 C  CG  . LEU A 1 172 ? 18.055  5.355   14.869  1.00 9.93  ?  174 LEU A CG  1 
ATOM   1303 C  CD1 . LEU A 1 172 ? 17.204  4.233   15.517  1.00 8.38  ?  174 LEU A CD1 1 
ATOM   1304 C  CD2 . LEU A 1 172 ? 18.464  5.054   13.409  1.00 9.10  ?  174 LEU A CD2 1 
ATOM   1305 N  N   . MET A 1 173 ? 20.443  7.905   14.426  1.00 8.70  ?  175 MET A N   1 
ATOM   1306 C  CA  . MET A 1 173 ? 21.812  7.984   14.916  1.00 8.39  ?  175 MET A CA  1 
ATOM   1307 C  C   . MET A 1 173 ? 22.528  9.214   14.386  1.00 8.75  ?  175 MET A C   1 
ATOM   1308 O  O   . MET A 1 173 ? 23.137  9.966   15.160  1.00 8.35  ?  175 MET A O   1 
ATOM   1309 C  CB  . MET A 1 173 ? 22.576  6.727   14.488  1.00 9.26  ?  175 MET A CB  1 
ATOM   1310 C  CG  . MET A 1 173 ? 22.119  5.469   15.190  1.00 13.59 ?  175 MET A CG  1 
ATOM   1311 S  SD  . MET A 1 173 ? 22.777  4.046   14.298  1.00 13.06 ?  175 MET A SD  1 
ATOM   1312 C  CE  . MET A 1 173 ? 21.895  2.711   15.135  1.00 12.45 ?  175 MET A CE  1 
ATOM   1313 N  N   . ALA A 1 174 ? 22.455  9.456   13.079  1.00 8.31  ?  176 ALA A N   1 
ATOM   1314 C  CA  . ALA A 1 174 ? 23.253  10.489  12.435  1.00 7.03  ?  176 ALA A CA  1 
ATOM   1315 C  C   . ALA A 1 174 ? 22.500  11.804  12.287  1.00 7.56  ?  176 ALA A C   1 
ATOM   1316 O  O   . ALA A 1 174 ? 22.987  12.709  11.598  1.00 7.76  ?  176 ALA A O   1 
ATOM   1317 C  CB  . ALA A 1 174 ? 23.724  10.016  11.060  1.00 10.04 ?  176 ALA A CB  1 
ATOM   1318 N  N   . GLY A 1 175 ? 21.324  11.913  12.884  1.00 7.46  ?  177 GLY A N   1 
ATOM   1319 C  CA  . GLY A 1 175 ? 20.556  13.149  12.849  1.00 10.09 ?  177 GLY A CA  1 
ATOM   1320 C  C   . GLY A 1 175 ? 19.708  13.257  11.601  1.00 9.44  ?  177 GLY A C   1 
ATOM   1321 O  O   . GLY A 1 175 ? 18.475  13.287  11.676  1.00 9.07  ?  177 GLY A O   1 
ATOM   1322 N  N   . TYR A 1 176 ? 20.370  13.312  10.446  1.00 8.90  ?  178 TYR A N   1 
ATOM   1323 C  CA  . TYR A 1 176 ? 19.713  13.229  9.145   1.00 7.33  ?  178 TYR A CA  1 
ATOM   1324 C  C   . TYR A 1 176 ? 20.526  12.308  8.252   1.00 8.50  ?  178 TYR A C   1 
ATOM   1325 O  O   . TYR A 1 176 ? 21.755  12.240  8.370   1.00 9.63  ?  178 TYR A O   1 
ATOM   1326 C  CB  . TYR A 1 176 ? 19.600  14.596  8.453   1.00 6.60  ?  178 TYR A CB  1 
ATOM   1327 C  CG  . TYR A 1 176 ? 18.642  15.508  9.144   1.00 8.33  ?  178 TYR A CG  1 
ATOM   1328 C  CD1 . TYR A 1 176 ? 17.280  15.445  8.867   1.00 7.67  ?  178 TYR A CD1 1 
ATOM   1329 C  CD2 . TYR A 1 176 ? 19.089  16.433  10.081  1.00 10.81 ?  178 TYR A CD2 1 
ATOM   1330 C  CE1 . TYR A 1 176 ? 16.383  16.261  9.510   1.00 9.42  ?  178 TYR A CE1 1 
ATOM   1331 C  CE2 . TYR A 1 176 ? 18.183  17.265  10.738  1.00 9.33  ?  178 TYR A CE2 1 
ATOM   1332 C  CZ  . TYR A 1 176 ? 16.835  17.165  10.441  1.00 12.16 ?  178 TYR A CZ  1 
ATOM   1333 O  OH  . TYR A 1 176 ? 15.920  17.975  11.075  1.00 14.42 ?  178 TYR A OH  1 
ATOM   1334 N  N   . SER A 1 177 ? 19.824  11.603  7.370   1.00 7.81  ?  179 SER A N   1 
ATOM   1335 C  CA  A SER A 1 177 ? 20.430  10.829  6.297   0.70 6.36  ?  179 SER A CA  1 
ATOM   1336 C  CA  B SER A 1 177 ? 20.466  10.835  6.319   0.30 6.40  ?  179 SER A CA  1 
ATOM   1337 C  C   . SER A 1 177 ? 20.852  11.750  5.156   1.00 8.70  ?  179 SER A C   1 
ATOM   1338 O  O   . SER A 1 177 ? 20.422  12.904  5.068   1.00 9.34  ?  179 SER A O   1 
ATOM   1339 C  CB  A SER A 1 177 ? 19.439  9.790   5.770   0.70 6.98  ?  179 SER A CB  1 
ATOM   1340 C  CB  B SER A 1 177 ? 19.539  9.716   5.848   0.30 7.09  ?  179 SER A CB  1 
ATOM   1341 O  OG  A SER A 1 177 ? 19.297  8.728   6.697   0.70 5.88  ?  179 SER A OG  1 
ATOM   1342 O  OG  B SER A 1 177 ? 18.320  10.226  5.354   0.30 8.51  ?  179 SER A OG  1 
ATOM   1343 N  N   . GLY A 1 178 ? 21.685  11.221  4.263   1.00 6.96  ?  180 GLY A N   1 
ATOM   1344 C  CA  . GLY A 1 178 ? 22.116  11.941  3.077   1.00 6.54  ?  180 GLY A CA  1 
ATOM   1345 C  C   . GLY A 1 178 ? 23.569  12.390  3.152   1.00 8.78  ?  180 GLY A C   1 
ATOM   1346 O  O   . GLY A 1 178 ? 24.298  12.112  4.110   1.00 8.43  ?  180 GLY A O   1 
ATOM   1347 N  N   . GLY A 1 179 ? 23.973  13.104  2.090   1.00 8.29  ?  181 GLY A N   1 
ATOM   1348 C  CA  . GLY A 1 179 ? 25.341  13.575  1.956   1.00 8.45  ?  181 GLY A CA  1 
ATOM   1349 C  C   . GLY A 1 179 ? 26.402  12.534  2.265   1.00 7.84  ?  181 GLY A C   1 
ATOM   1350 O  O   . GLY A 1 179 ? 26.443  11.461  1.660   1.00 9.73  ?  181 GLY A O   1 
ATOM   1351 N  N   . ARG A 1 180 ? 27.230  12.879  3.257   1.00 7.90  ?  182 ARG A N   1 
ATOM   1352 C  CA  A ARG A 1 180 ? 28.355  12.049  3.688   0.50 9.59  ?  182 ARG A CA  1 
ATOM   1353 C  CA  B ARG A 1 180 ? 28.352  12.056  3.714   0.50 9.61  ?  182 ARG A CA  1 
ATOM   1354 C  C   . ARG A 1 180 ? 27.974  10.619  4.058   1.00 7.29  ?  182 ARG A C   1 
ATOM   1355 O  O   . ARG A 1 180 ? 28.836  9.731   4.034   1.00 7.82  ?  182 ARG A O   1 
ATOM   1356 C  CB  A ARG A 1 180 ? 29.032  12.737  4.879   0.50 8.51  ?  182 ARG A CB  1 
ATOM   1357 C  CB  B ARG A 1 180 ? 28.981  12.722  4.944   0.50 8.48  ?  182 ARG A CB  1 
ATOM   1358 C  CG  A ARG A 1 180 ? 28.343  12.566  6.246   0.50 7.51  ?  182 ARG A CG  1 
ATOM   1359 C  CG  B ARG A 1 180 ? 28.185  12.573  6.265   0.50 7.54  ?  182 ARG A CG  1 
ATOM   1360 C  CD  A ARG A 1 180 ? 26.980  13.294  6.303   0.50 8.54  ?  182 ARG A CD  1 
ATOM   1361 C  CD  B ARG A 1 180 ? 26.831  13.332  6.247   0.50 8.51  ?  182 ARG A CD  1 
ATOM   1362 N  NE  A ARG A 1 180 ? 26.341  13.187  7.616   0.50 7.83  ?  182 ARG A NE  1 
ATOM   1363 N  NE  B ARG A 1 180 ? 26.206  13.408  7.571   0.50 7.76  ?  182 ARG A NE  1 
ATOM   1364 C  CZ  A ARG A 1 180 ? 25.065  12.898  7.846   0.50 7.62  ?  182 ARG A CZ  1 
ATOM   1365 C  CZ  B ARG A 1 180 ? 25.003  12.943  7.894   0.50 7.64  ?  182 ARG A CZ  1 
ATOM   1366 N  NH1 A ARG A 1 180 ? 24.235  12.607  6.848   0.50 7.33  ?  182 ARG A NH1 1 
ATOM   1367 N  NH1 B ARG A 1 180 ? 24.240  12.324  6.997   0.50 6.91  ?  182 ARG A NH1 1 
ATOM   1368 N  NH2 A ARG A 1 180 ? 24.631  12.865  9.101   0.50 8.37  ?  182 ARG A NH2 1 
ATOM   1369 N  NH2 B ARG A 1 180 ? 24.569  13.091  9.140   0.50 8.14  ?  182 ARG A NH2 1 
ATOM   1370 N  N   . LYS A 1 181 ? 26.716  10.369  4.419   1.00 6.84  ?  183 LYS A N   1 
ATOM   1371 C  CA  . LYS A 1 181 ? 26.354  9.034   4.911   1.00 8.51  ?  183 LYS A CA  1 
ATOM   1372 C  C   . LYS A 1 181 ? 26.413  7.963   3.819   1.00 8.26  ?  183 LYS A C   1 
ATOM   1373 O  O   . LYS A 1 181 ? 26.535  6.768   4.128   1.00 5.72  ?  183 LYS A O   1 
ATOM   1374 C  CB  . LYS A 1 181 ? 24.959  9.095   5.544   1.00 7.91  ?  183 LYS A CB  1 
ATOM   1375 C  CG  . LYS A 1 181 ? 24.672  8.052   6.613   1.00 7.85  ?  183 LYS A CG  1 
ATOM   1376 C  CD  . LYS A 1 181 ? 23.480  8.508   7.488   1.00 8.15  ?  183 LYS A CD  1 
ATOM   1377 C  CE  . LYS A 1 181 ? 23.141  7.448   8.516   1.00 9.29  ?  183 LYS A CE  1 
ATOM   1378 N  NZ  . LYS A 1 181 ? 22.874  6.115   7.863   1.00 6.48  ?  183 LYS A NZ  1 
ATOM   1379 N  N   . LEU A 1 182 ? 26.341  8.363   2.547   1.00 6.19  ?  184 LEU A N   1 
ATOM   1380 C  CA  . LEU A 1 182 ? 26.537  7.412   1.455   1.00 9.71  ?  184 LEU A CA  1 
ATOM   1381 C  C   . LEU A 1 182 ? 27.935  6.797   1.481   1.00 10.07 ?  184 LEU A C   1 
ATOM   1382 O  O   . LEU A 1 182 ? 28.124  5.655   1.043   1.00 7.29  ?  184 LEU A O   1 
ATOM   1383 C  CB  . LEU A 1 182 ? 26.291  8.111   0.113   1.00 7.51  ?  184 LEU A CB  1 
ATOM   1384 C  CG  . LEU A 1 182 ? 24.849  8.167   -0.409  1.00 7.40  ?  184 LEU A CG  1 
ATOM   1385 C  CD1 . LEU A 1 182 ? 24.371  6.729   -0.745  1.00 8.17  ?  184 LEU A CD1 1 
ATOM   1386 C  CD2 . LEU A 1 182 ? 23.934  8.800   0.617   1.00 10.79 ?  184 LEU A CD2 1 
ATOM   1387 N  N   . ILE A 1 183 ? 28.918  7.523   2.003   1.00 10.35 ?  185 ILE A N   1 
ATOM   1388 C  CA  . ILE A 1 183 ? 30.282  7.010   2.135   1.00 8.02  ?  185 ILE A CA  1 
ATOM   1389 C  C   . ILE A 1 183 ? 30.443  6.287   3.472   1.00 7.70  ?  185 ILE A C   1 
ATOM   1390 O  O   . ILE A 1 183 ? 30.837  5.112   3.517   1.00 9.92  ?  185 ILE A O   1 
ATOM   1391 C  CB  . ILE A 1 183 ? 31.322  8.137   1.977   1.00 8.40  ?  185 ILE A CB  1 
ATOM   1392 C  CG1 . ILE A 1 183 ? 31.264  8.761   0.570   1.00 9.14  ?  185 ILE A CG1 1 
ATOM   1393 C  CG2 . ILE A 1 183 ? 32.745  7.592   2.236   1.00 9.96  ?  185 ILE A CG2 1 
ATOM   1394 C  CD1 . ILE A 1 183 ? 30.305  9.918   0.380   1.00 20.84 ?  185 ILE A CD1 1 
ATOM   1395 N  N   . CYS A 1 184 ? 30.160  6.975   4.574   1.00 8.44  ?  186 CYS A N   1 
ATOM   1396 C  CA  . CYS A 1 184 ? 30.232  6.349   5.900   1.00 7.67  ?  186 CYS A CA  1 
ATOM   1397 C  C   . CYS A 1 184 ? 28.839  6.355   6.513   1.00 9.09  ?  186 CYS A C   1 
ATOM   1398 O  O   . CYS A 1 184 ? 28.372  7.426   6.951   1.00 8.92  ?  186 CYS A O   1 
ATOM   1399 C  CB  . CYS A 1 184 ? 31.209  7.093   6.805   1.00 9.84  ?  186 CYS A CB  1 
ATOM   1400 S  SG  . CYS A 1 184 ? 31.379  6.340   8.439   1.00 11.52 ?  186 CYS A SG  1 
ATOM   1401 N  N   . PRO A 1 185 ? 28.131  5.207   6.596   1.00 8.29  ?  187 PRO A N   1 
ATOM   1402 C  CA  . PRO A 1 185 ? 28.645  3.842   6.435   1.00 8.86  ?  187 PRO A CA  1 
ATOM   1403 C  C   . PRO A 1 185 ? 28.377  3.210   5.074   1.00 8.32  ?  187 PRO A C   1 
ATOM   1404 O  O   . PRO A 1 185 ? 28.666  2.032   4.924   1.00 8.77  ?  187 PRO A O   1 
ATOM   1405 C  CB  . PRO A 1 185 ? 27.844  3.056   7.471   1.00 7.99  ?  187 PRO A CB  1 
ATOM   1406 C  CG  . PRO A 1 185 ? 26.495  3.714   7.381   1.00 7.69  ?  187 PRO A CG  1 
ATOM   1407 C  CD  . PRO A 1 185 ? 26.756  5.189   7.135   1.00 8.05  ?  187 PRO A CD  1 
ATOM   1408 N  N   . GLY A 1 186 ? 27.797  3.956   4.130   1.00 8.23  ?  188 GLY A N   1 
ATOM   1409 C  CA  . GLY A 1 186 ? 27.227  3.327   2.938   1.00 8.52  ?  188 GLY A CA  1 
ATOM   1410 C  C   . GLY A 1 186 ? 28.186  2.387   2.227   1.00 7.50  ?  188 GLY A C   1 
ATOM   1411 O  O   . GLY A 1 186 ? 27.781  1.339   1.714   1.00 6.87  ?  188 GLY A O   1 
ATOM   1412 N  N   . ILE A 1 187 ? 29.466  2.749   2.165   1.00 6.61  ?  189 ILE A N   1 
ATOM   1413 C  CA  . ILE A 1 187 ? 30.436  1.856   1.536   1.00 6.00  ?  189 ILE A CA  1 
ATOM   1414 C  C   . ILE A 1 187 ? 31.632  1.648   2.460   1.00 8.51  ?  189 ILE A C   1 
ATOM   1415 O  O   . ILE A 1 187 ? 32.778  1.513   2.011   1.00 8.94  ?  189 ILE A O   1 
ATOM   1416 C  CB  . ILE A 1 187 ? 30.865  2.386   0.162   1.00 7.70  ?  189 ILE A CB  1 
ATOM   1417 C  CG1 . ILE A 1 187 ? 31.320  3.840   0.266   1.00 10.48 ?  189 ILE A CG1 1 
ATOM   1418 C  CG2 . ILE A 1 187 ? 29.660  2.273   -0.805  1.00 7.61  ?  189 ILE A CG2 1 
ATOM   1419 C  CD1 . ILE A 1 187 ? 32.085  4.343   -0.968  1.00 10.09 ?  189 ILE A CD1 1 
ATOM   1420 N  N   . ALA A 1 188 ? 31.363  1.596   3.758   1.00 7.43  ?  190 ALA A N   1 
ATOM   1421 C  CA  . ALA A 1 188 ? 32.405  1.422   4.759   1.00 7.32  ?  190 ALA A CA  1 
ATOM   1422 C  C   . ALA A 1 188 ? 32.385  -0.005  5.294   1.00 8.43  ?  190 ALA A C   1 
ATOM   1423 O  O   . ALA A 1 188 ? 31.329  -0.632  5.408   1.00 9.92  ?  190 ALA A O   1 
ATOM   1424 C  CB  . ALA A 1 188 ? 32.215  2.414   5.911   1.00 10.92 ?  190 ALA A CB  1 
ATOM   1425 N  N   . ALA A 1 189 ? 33.566  -0.499  5.661   1.00 8.82  ?  191 ALA A N   1 
ATOM   1426 C  CA  . ALA A 1 189 ? 33.678  -1.863  6.156   1.00 7.51  ?  191 ALA A CA  1 
ATOM   1427 C  C   . ALA A 1 189 ? 33.200  -1.958  7.603   1.00 8.18  ?  191 ALA A C   1 
ATOM   1428 O  O   . ALA A 1 189 ? 33.167  -0.973  8.350   1.00 8.23  ?  191 ALA A O   1 
ATOM   1429 C  CB  . ALA A 1 189 ? 35.126  -2.354  6.071   1.00 8.62  ?  191 ALA A CB  1 
ATOM   1430 N  N   . PHE A 1 190 ? 32.837  -3.181  7.990   1.00 7.93  ?  192 PHE A N   1 
ATOM   1431 C  CA  . PHE A 1 190 ? 32.504  -3.458  9.383   1.00 8.94  ?  192 PHE A CA  1 
ATOM   1432 C  C   . PHE A 1 190 ? 33.626  -3.026  10.335  1.00 8.31  ?  192 PHE A C   1 
ATOM   1433 O  O   . PHE A 1 190 ? 33.363  -2.578  11.450  1.00 9.74  ?  192 PHE A O   1 
ATOM   1434 C  CB  . PHE A 1 190 ? 32.220  -4.949  9.554   1.00 11.70 ?  192 PHE A CB  1 
ATOM   1435 C  CG  . PHE A 1 190 ? 31.800  -5.331  10.946  1.00 13.84 ?  192 PHE A CG  1 
ATOM   1436 C  CD1 . PHE A 1 190 ? 30.608  -4.850  11.469  1.00 12.85 ?  192 PHE A CD1 1 
ATOM   1437 C  CD2 . PHE A 1 190 ? 32.602  -6.142  11.742  1.00 13.96 ?  192 PHE A CD2 1 
ATOM   1438 C  CE1 . PHE A 1 190 ? 30.212  -5.190  12.754  1.00 11.69 ?  192 PHE A CE1 1 
ATOM   1439 C  CE2 . PHE A 1 190 ? 32.204  -6.493  13.027  1.00 15.10 ?  192 PHE A CE2 1 
ATOM   1440 C  CZ  . PHE A 1 190 ? 31.004  -6.017  13.531  1.00 14.15 ?  192 PHE A CZ  1 
ATOM   1441 N  N   . GLU A 1 191 ? 34.890  -3.173  9.924   1.00 9.31  ?  193 GLU A N   1 
ATOM   1442 C  CA  . GLU A 1 191 ? 35.990  -2.718  10.772  1.00 10.94 ?  193 GLU A CA  1 
ATOM   1443 C  C   . GLU A 1 191 ? 35.855  -1.238  11.138  1.00 9.34  ?  193 GLU A C   1 
ATOM   1444 O  O   . GLU A 1 191 ? 36.271  -0.829  12.228  1.00 11.60 ?  193 GLU A O   1 
ATOM   1445 C  CB  . GLU A 1 191 ? 37.314  -2.992  10.058  1.00 16.25 ?  193 GLU A CB  1 
ATOM   1446 C  CG  . GLU A 1 191 ? 37.694  -4.484  10.055  1.00 20.82 ?  193 GLU A CG  1 
ATOM   1447 C  CD  . GLU A 1 191 ? 37.398  -5.173  11.395  1.00 33.62 ?  193 GLU A CD  1 
ATOM   1448 O  OE1 . GLU A 1 191 ? 38.116  -4.864  12.371  1.00 35.16 ?  193 GLU A OE1 1 
ATOM   1449 O  OE2 . GLU A 1 191 ? 36.479  -6.022  11.485  1.00 31.78 ?  193 GLU A OE2 1 
ATOM   1450 N  N   . THR A 1 192 ? 35.263  -0.432  10.246  1.00 10.49 ?  194 THR A N   1 
ATOM   1451 C  CA  . THR A 1 192 ? 34.920  0.961   10.545  1.00 10.37 ?  194 THR A CA  1 
ATOM   1452 C  C   . THR A 1 192 ? 33.592  1.078   11.292  1.00 9.69  ?  194 THR A C   1 
ATOM   1453 O  O   . THR A 1 192 ? 33.513  1.718   12.349  1.00 11.62 ?  194 THR A O   1 
ATOM   1454 C  CB  . THR A 1 192 ? 34.838  1.767   9.244   1.00 11.06 ?  194 THR A CB  1 
ATOM   1455 O  OG1 . THR A 1 192 ? 36.126  1.802   8.621   1.00 10.58 ?  194 THR A OG1 1 
ATOM   1456 C  CG2 . THR A 1 192 ? 34.309  3.196   9.502   1.00 9.96  ?  194 THR A CG2 1 
ATOM   1457 N  N   . VAL A 1 193 ? 32.537  0.473   10.742  1.00 8.73  ?  195 VAL A N   1 
ATOM   1458 C  CA  . VAL A 1 193 ? 31.184  0.693   11.243  1.00 9.56  ?  195 VAL A CA  1 
ATOM   1459 C  C   . VAL A 1 193 ? 30.994  0.144   12.649  1.00 11.93 ?  195 VAL A C   1 
ATOM   1460 O  O   . VAL A 1 193 ? 30.231  0.721   13.441  1.00 10.09 ?  195 VAL A O   1 
ATOM   1461 C  CB  . VAL A 1 193 ? 30.185  0.088   10.246  1.00 7.35  ?  195 VAL A CB  1 
ATOM   1462 C  CG1 . VAL A 1 193 ? 28.744  0.243   10.750  1.00 10.82 ?  195 VAL A CG1 1 
ATOM   1463 C  CG2 . VAL A 1 193 ? 30.373  0.783   8.903   1.00 7.27  ?  195 VAL A CG2 1 
ATOM   1464 N  N   . LYS A 1 194 ? 31.651  -0.973  12.992  1.00 8.40  ?  196 LYS A N   1 
ATOM   1465 C  CA  . LYS A 1 194 ? 31.454  -1.512  14.338  1.00 11.33 ?  196 LYS A CA  1 
ATOM   1466 C  C   . LYS A 1 194 ? 31.858  -0.497  15.405  1.00 12.57 ?  196 LYS A C   1 
ATOM   1467 O  O   . LYS A 1 194 ? 31.252  -0.453  16.485  1.00 11.51 ?  196 LYS A O   1 
ATOM   1468 C  CB  . LYS A 1 194 ? 32.232  -2.815  14.541  1.00 11.26 ?  196 LYS A CB  1 
ATOM   1469 C  CG  . LYS A 1 194 ? 33.746  -2.653  14.721  1.00 9.60  ?  196 LYS A CG  1 
ATOM   1470 C  CD  . LYS A 1 194 ? 34.463  -3.991  14.623  1.00 14.08 ?  196 LYS A CD  1 
ATOM   1471 C  CE  . LYS A 1 194 ? 35.878  -3.851  15.190  1.00 16.29 ?  196 LYS A CE  1 
ATOM   1472 N  NZ  . LYS A 1 194 ? 36.687  -5.112  15.014  1.00 18.76 ?  196 LYS A NZ  1 
ATOM   1473 N  N   . LEU A 1 195 ? 32.865  0.333   15.124  1.00 9.42  ?  197 LEU A N   1 
ATOM   1474 C  CA  . LEU A 1 195 ? 33.290  1.323   16.105  1.00 8.90  ?  197 LEU A CA  1 
ATOM   1475 C  C   . LEU A 1 195 ? 32.428  2.576   16.030  1.00 11.61 ?  197 LEU A C   1 
ATOM   1476 O  O   . LEU A 1 195 ? 32.051  3.143   17.063  1.00 12.41 ?  197 LEU A O   1 
ATOM   1477 C  CB  . LEU A 1 195 ? 34.777  1.652   15.900  1.00 11.41 ?  197 LEU A CB  1 
ATOM   1478 C  CG  . LEU A 1 195 ? 35.729  0.497   16.242  1.00 13.19 ?  197 LEU A CG  1 
ATOM   1479 C  CD1 . LEU A 1 195 ? 37.142  0.831   15.797  1.00 15.84 ?  197 LEU A CD1 1 
ATOM   1480 C  CD2 . LEU A 1 195 ? 35.721  0.298   17.759  1.00 13.87 ?  197 LEU A CD2 1 
ATOM   1481 N  N   . TRP A 1 196 ? 32.070  2.992   14.817  1.00 11.04 ?  198 TRP A N   1 
ATOM   1482 C  CA  . TRP A 1 196 ? 31.290  4.212   14.653  1.00 10.81 ?  198 TRP A CA  1 
ATOM   1483 C  C   . TRP A 1 196 ? 29.868  4.020   15.168  1.00 11.45 ?  198 TRP A C   1 
ATOM   1484 O  O   . TRP A 1 196 ? 29.276  4.948   15.737  1.00 13.37 ?  198 TRP A O   1 
ATOM   1485 C  CB  . TRP A 1 196 ? 31.336  4.623   13.181  1.00 9.90  ?  198 TRP A CB  1 
ATOM   1486 C  CG  . TRP A 1 196 ? 30.495  5.767   12.840  1.00 9.64  ?  198 TRP A CG  1 
ATOM   1487 C  CD1 . TRP A 1 196 ? 30.628  7.053   13.274  1.00 9.48  ?  198 TRP A CD1 1 
ATOM   1488 C  CD2 . TRP A 1 196 ? 29.359  5.745   11.961  1.00 9.69  ?  198 TRP A CD2 1 
ATOM   1489 N  NE1 . TRP A 1 196 ? 29.629  7.835   12.728  1.00 8.61  ?  198 TRP A NE1 1 
ATOM   1490 C  CE2 . TRP A 1 196 ? 28.838  7.052   11.924  1.00 10.67 ?  198 TRP A CE2 1 
ATOM   1491 C  CE3 . TRP A 1 196 ? 28.726  4.739   11.218  1.00 8.84  ?  198 TRP A CE3 1 
ATOM   1492 C  CZ2 . TRP A 1 196 ? 27.725  7.385   11.159  1.00 9.21  ?  198 TRP A CZ2 1 
ATOM   1493 C  CZ3 . TRP A 1 196 ? 27.625  5.069   10.458  1.00 9.46  ?  198 TRP A CZ3 1 
ATOM   1494 C  CH2 . TRP A 1 196 ? 27.136  6.391   10.429  1.00 10.48 ?  198 TRP A CH2 1 
ATOM   1495 N  N   . HIS A 1 197 ? 29.321  2.812   15.004  1.00 9.26  ?  199 HIS A N   1 
ATOM   1496 C  CA  A HIS A 1 197 ? 28.047  2.411   15.586  0.50 10.45 ?  199 HIS A CA  1 
ATOM   1497 C  CA  B HIS A 1 197 ? 28.045  2.420   15.594  0.50 10.44 ?  199 HIS A CA  1 
ATOM   1498 C  C   . HIS A 1 197 ? 28.219  1.737   16.949  1.00 10.92 ?  199 HIS A C   1 
ATOM   1499 O  O   . HIS A 1 197 ? 27.344  0.965   17.366  1.00 11.63 ?  199 HIS A O   1 
ATOM   1500 C  CB  A HIS A 1 197 ? 27.313  1.461   14.634  0.50 9.60  ?  199 HIS A CB  1 
ATOM   1501 C  CB  B HIS A 1 197 ? 27.282  1.484   14.651  0.50 9.57  ?  199 HIS A CB  1 
ATOM   1502 C  CG  A HIS A 1 197 ? 26.469  2.143   13.597  0.50 9.96  ?  199 HIS A CG  1 
ATOM   1503 C  CG  B HIS A 1 197 ? 26.522  2.179   13.560  0.50 9.96  ?  199 HIS A CG  1 
ATOM   1504 N  ND1 A HIS A 1 197 ? 26.351  3.513   13.500  0.50 12.76 ?  199 HIS A ND1 1 
ATOM   1505 N  ND1 B HIS A 1 197 ? 26.160  3.508   13.620  0.50 12.94 ?  199 HIS A ND1 1 
ATOM   1506 C  CD2 A HIS A 1 197 ? 25.726  1.629   12.589  0.50 10.52 ?  199 HIS A CD2 1 
ATOM   1507 C  CD2 B HIS A 1 197 ? 26.060  1.717   12.375  0.50 9.93  ?  199 HIS A CD2 1 
ATOM   1508 C  CE1 A HIS A 1 197 ? 25.545  3.812   12.494  0.50 12.68 ?  199 HIS A CE1 1 
ATOM   1509 C  CE1 B HIS A 1 197 ? 25.497  3.831   12.523  0.50 12.67 ?  199 HIS A CE1 1 
ATOM   1510 N  NE2 A HIS A 1 197 ? 25.155  2.687   11.920  0.50 10.67 ?  199 HIS A NE2 1 
ATOM   1511 N  NE2 B HIS A 1 197 ? 25.421  2.763   11.749  0.50 10.88 ?  199 HIS A NE2 1 
ATOM   1512 N  N   . GLY A 1 198 ? 29.340  1.981   17.632  1.00 11.12 ?  200 GLY A N   1 
ATOM   1513 C  CA  . GLY A 1 198 ? 29.570  1.434   18.953  1.00 12.12 ?  200 GLY A CA  1 
ATOM   1514 C  C   . GLY A 1 198 ? 28.884  2.266   20.020  1.00 11.62 ?  200 GLY A C   1 
ATOM   1515 O  O   . GLY A 1 198 ? 28.512  3.422   19.790  1.00 10.95 ?  200 GLY A O   1 
ATOM   1516 N  N   . PRO A 1 199 ? 28.690  1.685   21.211  1.00 14.34 ?  201 PRO A N   1 
ATOM   1517 C  CA  . PRO A 1 199 ? 27.998  2.422   22.291  1.00 13.89 ?  201 PRO A CA  1 
ATOM   1518 C  C   . PRO A 1 199 ? 28.650  3.748   22.671  1.00 13.70 ?  201 PRO A C   1 
ATOM   1519 O  O   . PRO A 1 199 ? 27.946  4.641   23.164  1.00 13.83 ?  201 PRO A O   1 
ATOM   1520 C  CB  . PRO A 1 199 ? 28.026  1.436   23.471  1.00 13.86 ?  201 PRO A CB  1 
ATOM   1521 C  CG  . PRO A 1 199 ? 29.037  0.392   23.099  1.00 16.25 ?  201 PRO A CG  1 
ATOM   1522 C  CD  . PRO A 1 199 ? 29.031  0.309   21.607  1.00 13.00 ?  201 PRO A CD  1 
ATOM   1523 N  N   . ARG A 1 200 ? 29.963  3.917   22.480  1.00 11.30 ?  202 ARG A N   1 
ATOM   1524 C  CA  . ARG A 1 200 ? 30.553  5.211   22.814  1.00 11.45 ?  202 ARG A CA  1 
ATOM   1525 C  C   . ARG A 1 200 ? 29.957  6.327   21.964  1.00 15.64 ?  202 ARG A C   1 
ATOM   1526 O  O   . ARG A 1 200 ? 29.863  7.474   22.418  1.00 16.31 ?  202 ARG A O   1 
ATOM   1527 C  CB  . ARG A 1 200 ? 32.074  5.163   22.653  1.00 12.77 ?  202 ARG A CB  1 
ATOM   1528 C  CG  . ARG A 1 200 ? 32.765  4.356   23.747  1.00 17.88 ?  202 ARG A CG  1 
ATOM   1529 C  CD  . ARG A 1 200 ? 34.288  4.418   23.619  1.00 20.47 ?  202 ARG A CD  1 
ATOM   1530 N  NE  . ARG A 1 200 ? 34.747  3.649   22.465  1.00 21.18 ?  202 ARG A NE  1 
ATOM   1531 C  CZ  . ARG A 1 200 ? 35.032  2.353   22.499  1.00 21.81 ?  202 ARG A CZ  1 
ATOM   1532 N  NH1 . ARG A 1 200 ? 34.906  1.675   23.638  1.00 20.46 ?  202 ARG A NH1 1 
ATOM   1533 N  NH2 . ARG A 1 200 ? 35.429  1.738   21.391  1.00 23.37 ?  202 ARG A NH2 1 
ATOM   1534 N  N   . PHE A 1 201 ? 29.519  6.010   20.746  1.00 11.85 ?  203 PHE A N   1 
ATOM   1535 C  CA  . PHE A 1 201 ? 28.818  6.991   19.930  1.00 10.44 ?  203 PHE A CA  1 
ATOM   1536 C  C   . PHE A 1 201 ? 27.319  6.970   20.225  1.00 10.42 ?  203 PHE A C   1 
ATOM   1537 O  O   . PHE A 1 201 ? 26.704  8.017   20.455  1.00 10.02 ?  203 PHE A O   1 
ATOM   1538 C  CB  . PHE A 1 201 ? 29.066  6.710   18.441  1.00 9.41  ?  203 PHE A CB  1 
ATOM   1539 C  CG  . PHE A 1 201 ? 30.434  7.124   17.959  1.00 9.94  ?  203 PHE A CG  1 
ATOM   1540 C  CD1 . PHE A 1 201 ? 31.491  6.225   18.002  1.00 11.39 ?  203 PHE A CD1 1 
ATOM   1541 C  CD2 . PHE A 1 201 ? 30.667  8.404   17.465  1.00 11.96 ?  203 PHE A CD2 1 
ATOM   1542 C  CE1 . PHE A 1 201 ? 32.752  6.592   17.560  1.00 11.80 ?  203 PHE A CE1 1 
ATOM   1543 C  CE2 . PHE A 1 201 ? 31.926  8.774   17.029  1.00 12.72 ?  203 PHE A CE2 1 
ATOM   1544 C  CZ  . PHE A 1 201 ? 32.973  7.864   17.082  1.00 8.69  ?  203 PHE A CZ  1 
ATOM   1545 N  N   . LEU A 1 202 ? 26.720  5.776   20.240  1.00 9.31  ?  204 LEU A N   1 
ATOM   1546 C  CA  . LEU A 1 202 ? 25.263  5.673   20.204  1.00 9.95  ?  204 LEU A CA  1 
ATOM   1547 C  C   . LEU A 1 202 ? 24.603  6.044   21.522  1.00 11.22 ?  204 LEU A C   1 
ATOM   1548 O  O   . LEU A 1 202 ? 23.408  6.366   21.524  1.00 14.16 ?  204 LEU A O   1 
ATOM   1549 C  CB  . LEU A 1 202 ? 24.862  4.258   19.778  1.00 12.89 ?  204 LEU A CB  1 
ATOM   1550 C  CG  . LEU A 1 202 ? 25.245  3.929   18.323  1.00 12.78 ?  204 LEU A CG  1 
ATOM   1551 C  CD1 . LEU A 1 202 ? 24.469  2.743   17.856  1.00 14.66 ?  204 LEU A CD1 1 
ATOM   1552 C  CD2 . LEU A 1 202 ? 24.930  5.116   17.388  1.00 13.33 ?  204 LEU A CD2 1 
ATOM   1553 N  N   . GLU A 1 203 ? 25.328  6.006   22.631  1.00 10.26 ?  205 GLU A N   1 
ATOM   1554 C  CA  . GLU A 1 203 ? 24.749  6.407   23.907  1.00 11.45 ?  205 GLU A CA  1 
ATOM   1555 C  C   . GLU A 1 203 ? 24.845  7.911   24.142  1.00 14.14 ?  205 GLU A C   1 
ATOM   1556 O  O   . GLU A 1 203 ? 24.344  8.393   25.162  1.00 15.90 ?  205 GLU A O   1 
ATOM   1557 C  CB  . GLU A 1 203 ? 25.439  5.653   25.050  1.00 14.92 ?  205 GLU A CB  1 
ATOM   1558 C  CG  . GLU A 1 203 ? 25.092  4.155   25.135  1.00 13.95 ?  205 GLU A CG  1 
ATOM   1559 C  CD  . GLU A 1 203 ? 23.602  3.864   25.089  1.00 18.38 ?  205 GLU A CD  1 
ATOM   1560 O  OE1 . GLU A 1 203 ? 23.209  2.898   24.408  1.00 16.12 ?  205 GLU A OE1 1 
ATOM   1561 O  OE2 . GLU A 1 203 ? 22.824  4.593   25.740  1.00 16.62 ?  205 GLU A OE2 1 
ATOM   1562 N  N   . HIS A 1 204 ? 25.480  8.658   23.236  1.00 13.39 ?  206 HIS A N   1 
ATOM   1563 C  CA  . HIS A 1 204 ? 25.553  10.107  23.371  1.00 12.82 ?  206 HIS A CA  1 
ATOM   1564 C  C   . HIS A 1 204 ? 24.155  10.703  23.280  1.00 12.81 ?  206 HIS A C   1 
ATOM   1565 O  O   . HIS A 1 204 ? 23.356  10.278  22.441  1.00 12.54 ?  206 HIS A O   1 
ATOM   1566 C  CB  . HIS A 1 204 ? 26.435  10.723  22.277  1.00 13.55 ?  206 HIS A CB  1 
ATOM   1567 C  CG  . HIS A 1 204 ? 26.836  12.149  22.543  1.00 13.22 ?  206 HIS A CG  1 
ATOM   1568 N  ND1 . HIS A 1 204 ? 26.019  13.219  22.234  1.00 14.44 ?  206 HIS A ND1 1 
ATOM   1569 C  CD2 . HIS A 1 204 ? 27.980  12.684  23.035  1.00 14.26 ?  206 HIS A CD2 1 
ATOM   1570 C  CE1 . HIS A 1 204 ? 26.628  14.347  22.552  1.00 16.61 ?  206 HIS A CE1 1 
ATOM   1571 N  NE2 . HIS A 1 204 ? 27.818  14.051  23.046  1.00 12.84 ?  206 HIS A NE2 1 
ATOM   1572 N  N   . PRO A 1 205 ? 23.824  11.691  24.114  1.00 12.85 ?  207 PRO A N   1 
ATOM   1573 C  CA  . PRO A 1 205 ? 22.457  12.227  24.079  1.00 14.26 ?  207 PRO A CA  1 
ATOM   1574 C  C   . PRO A 1 205 ? 22.091  12.908  22.770  1.00 14.74 ?  207 PRO A C   1 
ATOM   1575 O  O   . PRO A 1 205 ? 20.896  12.996  22.468  1.00 15.39 ?  207 PRO A O   1 
ATOM   1576 C  CB  . PRO A 1 205 ? 22.438  13.200  25.268  1.00 18.75 ?  207 PRO A CB  1 
ATOM   1577 C  CG  . PRO A 1 205 ? 23.880  13.576  25.448  1.00 20.48 ?  207 PRO A CG  1 
ATOM   1578 C  CD  . PRO A 1 205 ? 24.619  12.292  25.199  1.00 19.41 ?  207 PRO A CD  1 
ATOM   1579 N  N   . LEU A 1 206 ? 23.059  13.368  21.969  1.00 11.37 ?  208 LEU A N   1 
ATOM   1580 C  CA  . LEU A 1 206 ? 22.757  14.011  20.691  1.00 10.81 ?  208 LEU A CA  1 
ATOM   1581 C  C   . LEU A 1 206 ? 22.867  13.059  19.499  1.00 11.17 ?  208 LEU A C   1 
ATOM   1582 O  O   . LEU A 1 206 ? 22.704  13.496  18.351  1.00 11.69 ?  208 LEU A O   1 
ATOM   1583 C  CB  . LEU A 1 206 ? 23.671  15.232  20.482  1.00 12.35 ?  208 LEU A CB  1 
ATOM   1584 C  CG  . LEU A 1 206 ? 23.443  16.374  21.486  1.00 18.11 ?  208 LEU A CG  1 
ATOM   1585 C  CD1 . LEU A 1 206 ? 24.241  17.599  21.097  1.00 20.49 ?  208 LEU A CD1 1 
ATOM   1586 C  CD2 . LEU A 1 206 ? 21.954  16.727  21.513  1.00 17.96 ?  208 LEU A CD2 1 
ATOM   1587 N  N   . ALA A 1 207 ? 23.124  11.773  19.745  1.00 9.51  ?  209 ALA A N   1 
ATOM   1588 C  CA  . ALA A 1 207 ? 23.055  10.757  18.693  1.00 10.01 ?  209 ALA A CA  1 
ATOM   1589 C  C   . ALA A 1 207 ? 21.582  10.382  18.549  1.00 10.86 ?  209 ALA A C   1 
ATOM   1590 O  O   . ALA A 1 207 ? 21.095  9.379   19.074  1.00 10.43 ?  209 ALA A O   1 
ATOM   1591 C  CB  . ALA A 1 207 ? 23.940  9.553   19.022  1.00 10.24 ?  209 ALA A CB  1 
ATOM   1592 N  N   . ASP A 1 208 ? 20.853  11.242  17.846  1.00 9.82  ?  210 ASP A N   1 
ATOM   1593 C  CA  . ASP A 1 208 ? 19.395  11.170  17.809  1.00 10.27 ?  210 ASP A CA  1 
ATOM   1594 C  C   . ASP A 1 208 ? 18.885  11.970  16.623  1.00 8.53  ?  210 ASP A C   1 
ATOM   1595 O  O   . ASP A 1 208 ? 19.602  12.794  16.053  1.00 9.54  ?  210 ASP A O   1 
ATOM   1596 C  CB  . ASP A 1 208 ? 18.773  11.710  19.101  1.00 13.46 ?  210 ASP A CB  1 
ATOM   1597 C  CG  . ASP A 1 208 ? 17.509  10.956  19.511  1.00 24.48 ?  210 ASP A CG  1 
ATOM   1598 O  OD1 . ASP A 1 208 ? 16.853  10.347  18.633  1.00 18.67 ?  210 ASP A OD1 1 
ATOM   1599 O  OD2 . ASP A 1 208 ? 17.172  10.987  20.716  1.00 32.64 ?  210 ASP A OD2 1 
ATOM   1600 N  N   . CYS A 1 209 ? 17.614  11.741  16.286  1.00 11.18 ?  211 CYS A N   1 
ATOM   1601 C  CA  A CYS A 1 209 ? 17.003  12.400  15.140  0.67 10.26 ?  211 CYS A CA  1 
ATOM   1602 C  CA  B CYS A 1 209 ? 17.032  12.406  15.132  0.33 10.36 ?  211 CYS A CA  1 
ATOM   1603 C  C   . CYS A 1 209 ? 17.125  13.917  15.245  1.00 12.84 ?  211 CYS A C   1 
ATOM   1604 O  O   . CYS A 1 209 ? 16.859  14.505  16.297  1.00 12.59 ?  211 CYS A O   1 
ATOM   1605 C  CB  A CYS A 1 209 ? 15.521  12.005  15.043  0.67 12.43 ?  211 CYS A CB  1 
ATOM   1606 C  CB  B CYS A 1 209 ? 15.576  11.999  14.963  0.33 12.43 ?  211 CYS A CB  1 
ATOM   1607 S  SG  A CYS A 1 209 ? 15.150  10.237  15.357  0.67 13.04 ?  211 CYS A SG  1 
ATOM   1608 S  SG  B CYS A 1 209 ? 15.449  10.463  14.105  0.33 10.49 ?  211 CYS A SG  1 
ATOM   1609 N  N   . GLY A 1 210 ? 17.504  14.548  14.139  1.00 9.55  ?  212 GLY A N   1 
ATOM   1610 C  CA  . GLY A 1 210 ? 17.497  15.987  14.038  1.00 10.91 ?  212 GLY A CA  1 
ATOM   1611 C  C   . GLY A 1 210 ? 18.761  16.696  14.472  1.00 14.07 ?  212 GLY A C   1 
ATOM   1612 O  O   . GLY A 1 210 ? 18.879  17.905  14.224  1.00 17.33 ?  212 GLY A O   1 
ATOM   1613 N  N   . PHE A 1 211 ? 19.706  16.007  15.115  1.00 9.30  ?  213 PHE A N   1 
ATOM   1614 C  CA  . PHE A 1 211 ? 20.914  16.650  15.633  1.00 12.11 ?  213 PHE A CA  1 
ATOM   1615 C  C   . PHE A 1 211 ? 22.099  16.397  14.709  1.00 11.65 ?  213 PHE A C   1 
ATOM   1616 O  O   . PHE A 1 211 ? 22.432  15.244  14.421  1.00 10.04 ?  213 PHE A O   1 
ATOM   1617 C  CB  . PHE A 1 211 ? 21.249  16.145  17.040  1.00 11.95 ?  213 PHE A CB  1 
ATOM   1618 C  CG  . PHE A 1 211 ? 20.204  16.498  18.070  1.00 15.87 ?  213 PHE A CG  1 
ATOM   1619 C  CD1 . PHE A 1 211 ? 20.104  17.791  18.565  1.00 19.77 ?  213 PHE A CD1 1 
ATOM   1620 C  CD2 . PHE A 1 211 ? 19.311  15.545  18.515  1.00 17.73 ?  213 PHE A CD2 1 
ATOM   1621 C  CE1 . PHE A 1 211 ? 19.146  18.112  19.507  1.00 19.59 ?  213 PHE A CE1 1 
ATOM   1622 C  CE2 . PHE A 1 211 ? 18.344  15.864  19.457  1.00 17.85 ?  213 PHE A CE2 1 
ATOM   1623 C  CZ  . PHE A 1 211 ? 18.259  17.148  19.943  1.00 21.41 ?  213 PHE A CZ  1 
ATOM   1624 N  N   . LEU A 1 212 ? 22.745  17.478  14.268  1.00 11.34 ?  214 LEU A N   1 
ATOM   1625 C  CA  . LEU A 1 212 ? 23.969  17.414  13.471  1.00 12.45 ?  214 LEU A CA  1 
ATOM   1626 C  C   . LEU A 1 212 ? 25.127  17.983  14.285  1.00 13.80 ?  214 LEU A C   1 
ATOM   1627 O  O   . LEU A 1 212 ? 25.963  17.233  14.786  1.00 11.33 ?  214 LEU A O   1 
ATOM   1628 C  CB  . LEU A 1 212 ? 23.805  18.184  12.155  1.00 13.45 ?  214 LEU A CB  1 
ATOM   1629 C  CG  . LEU A 1 212 ? 22.832  17.609  11.113  1.00 9.88  ?  214 LEU A CG  1 
ATOM   1630 C  CD1 . LEU A 1 212 ? 22.935  18.399  9.829   1.00 14.75 ?  214 LEU A CD1 1 
ATOM   1631 C  CD2 . LEU A 1 212 ? 23.121  16.140  10.849  1.00 10.04 ?  214 LEU A CD2 1 
ATOM   1632 N  N   . GLU A 1 213 ? 25.174  19.298  14.465  1.00 16.61 ?  215 GLU A N   1 
ATOM   1633 C  CA  . GLU A 1 213 ? 26.239  19.898  15.265  1.00 18.48 ?  215 GLU A CA  1 
ATOM   1634 C  C   . GLU A 1 213 ? 26.179  19.392  16.705  1.00 15.19 ?  215 GLU A C   1 
ATOM   1635 O  O   . GLU A 1 213 ? 25.121  19.404  17.337  1.00 19.35 ?  215 GLU A O   1 
ATOM   1636 C  CB  . GLU A 1 213 ? 26.133  21.424  15.194  1.00 23.70 ?  215 GLU A CB  1 
ATOM   1637 C  CG  . GLU A 1 213 ? 26.387  21.979  13.776  1.00 30.50 ?  215 GLU A CG  1 
ATOM   1638 C  CD  . GLU A 1 213 ? 25.212  21.792  12.813  1.00 40.69 ?  215 GLU A CD  1 
ATOM   1639 O  OE1 . GLU A 1 213 ? 25.407  21.910  11.573  1.00 36.78 ?  215 GLU A OE1 1 
ATOM   1640 O  OE2 . GLU A 1 213 ? 24.096  21.515  13.296  1.00 33.75 ?  215 GLU A OE2 1 
ATOM   1641 N  N   . GLY A 1 214 ? 27.319  18.909  17.207  1.00 14.74 ?  216 GLY A N   1 
ATOM   1642 C  CA  . GLY A 1 214 ? 27.406  18.345  18.542  1.00 15.96 ?  216 GLY A CA  1 
ATOM   1643 C  C   . GLY A 1 214 ? 27.043  16.876  18.635  1.00 14.61 ?  216 GLY A C   1 
ATOM   1644 O  O   . GLY A 1 214 ? 27.252  16.263  19.693  1.00 15.58 ?  216 GLY A O   1 
ATOM   1645 N  N   . ASN A 1 215 ? 26.507  16.295  17.562  1.00 10.87 ?  217 ASN A N   1 
ATOM   1646 C  CA  . ASN A 1 215 ? 26.229  14.866  17.503  1.00 10.09 ?  217 ASN A CA  1 
ATOM   1647 C  C   . ASN A 1 215 ? 27.491  14.164  17.018  1.00 9.77  ?  217 ASN A C   1 
ATOM   1648 O  O   . ASN A 1 215 ? 27.884  14.354  15.860  1.00 9.46  ?  217 ASN A O   1 
ATOM   1649 C  CB  . ASN A 1 215 ? 25.048  14.602  16.567  1.00 11.88 ?  217 ASN A CB  1 
ATOM   1650 C  CG  . ASN A 1 215 ? 24.837  13.122  16.262  1.00 10.47 ?  217 ASN A CG  1 
ATOM   1651 O  OD1 . ASN A 1 215 ? 25.506  12.255  16.825  1.00 9.32  ?  217 ASN A OD1 1 
ATOM   1652 N  ND2 . ASN A 1 215 ? 23.846  12.831  15.417  1.00 9.03  ?  217 ASN A ND2 1 
ATOM   1653 N  N   . PRO A 1 216 ? 28.173  13.380  17.859  1.00 10.70 ?  218 PRO A N   1 
ATOM   1654 C  CA  . PRO A 1 216 ? 29.453  12.788  17.436  1.00 12.69 ?  218 PRO A CA  1 
ATOM   1655 C  C   . PRO A 1 216 ? 29.316  11.833  16.274  1.00 11.18 ?  218 PRO A C   1 
ATOM   1656 O  O   . PRO A 1 216 ? 30.299  11.615  15.553  1.00 9.06  ?  218 PRO A O   1 
ATOM   1657 C  CB  . PRO A 1 216 ? 29.932  12.062  18.701  1.00 10.74 ?  218 PRO A CB  1 
ATOM   1658 C  CG  . PRO A 1 216 ? 28.641  11.708  19.419  1.00 11.53 ?  218 PRO A CG  1 
ATOM   1659 C  CD  . PRO A 1 216 ? 27.781  12.935  19.212  1.00 12.88 ?  218 PRO A CD  1 
ATOM   1660 N  N   . VAL A 1 217 ? 28.135  11.239  16.095  1.00 11.49 ?  219 VAL A N   1 
ATOM   1661 C  CA  . VAL A 1 217 ? 27.904  10.355  14.957  1.00 9.90  ?  219 VAL A CA  1 
ATOM   1662 C  C   . VAL A 1 217 ? 28.078  11.130  13.664  1.00 8.81  ?  219 VAL A C   1 
ATOM   1663 O  O   . VAL A 1 217 ? 28.767  10.684  12.738  1.00 10.27 ?  219 VAL A O   1 
ATOM   1664 C  CB  . VAL A 1 217 ? 26.501  9.723   15.056  1.00 8.24  ?  219 VAL A CB  1 
ATOM   1665 C  CG1 . VAL A 1 217 ? 26.129  8.955   13.768  1.00 8.32  ?  219 VAL A CG1 1 
ATOM   1666 C  CG2 . VAL A 1 217 ? 26.397  8.846   16.305  1.00 9.86  ?  219 VAL A CG2 1 
ATOM   1667 N  N   . HIS A 1 218 ? 27.463  12.316  13.594  1.00 10.51 ?  220 HIS A N   1 
ATOM   1668 C  CA  . HIS A 1 218 ? 27.540  13.144  12.394  1.00 9.01  ?  220 HIS A CA  1 
ATOM   1669 C  C   . HIS A 1 218 ? 28.928  13.754  12.218  1.00 11.40 ?  220 HIS A C   1 
ATOM   1670 O  O   . HIS A 1 218 ? 29.437  13.844  11.093  1.00 10.03 ?  220 HIS A O   1 
ATOM   1671 C  CB  . HIS A 1 218 ? 26.472  14.249  12.456  1.00 7.63  ?  220 HIS A CB  1 
ATOM   1672 C  CG  . HIS A 1 218 ? 26.708  15.337  11.461  1.00 9.97  ?  220 HIS A CG  1 
ATOM   1673 N  ND1 . HIS A 1 218 ? 26.502  15.152  10.112  1.00 9.90  ?  220 HIS A ND1 1 
ATOM   1674 C  CD2 . HIS A 1 218 ? 27.170  16.605  11.605  1.00 11.11 ?  220 HIS A CD2 1 
ATOM   1675 C  CE1 . HIS A 1 218 ? 26.804  16.265  9.466   1.00 11.03 ?  220 HIS A CE1 1 
ATOM   1676 N  NE2 . HIS A 1 218 ? 27.219  17.160  10.345  1.00 10.28 ?  220 HIS A NE2 1 
ATOM   1677 N  N   . GLU A 1 219 ? 29.557  14.191  13.311  1.00 9.31  ?  221 GLU A N   1 
ATOM   1678 C  CA  . GLU A 1 219 ? 30.899  14.746  13.184  1.00 12.06 ?  221 GLU A CA  1 
ATOM   1679 C  C   . GLU A 1 219 ? 31.855  13.700  12.643  1.00 11.29 ?  221 GLU A C   1 
ATOM   1680 O  O   . GLU A 1 219 ? 32.685  13.997  11.780  1.00 11.22 ?  221 GLU A O   1 
ATOM   1681 C  CB  . GLU A 1 219 ? 31.395  15.288  14.533  1.00 12.07 ?  221 GLU A CB  1 
ATOM   1682 C  CG  . GLU A 1 219 ? 30.548  16.465  15.038  1.00 14.77 ?  221 GLU A CG  1 
ATOM   1683 C  CD  . GLU A 1 219 ? 30.770  16.781  16.512  1.00 27.20 ?  221 GLU A CD  1 
ATOM   1684 O  OE1 . GLU A 1 219 ? 31.393  15.963  17.232  1.00 26.10 ?  221 GLU A OE1 1 
ATOM   1685 O  OE2 . GLU A 1 219 ? 30.292  17.849  16.949  1.00 26.51 ?  221 GLU A OE2 1 
ATOM   1686 N  N   . GLU A 1 220 ? 31.701  12.452  13.095  1.00 10.30 ?  222 GLU A N   1 
ATOM   1687 C  CA  . GLU A 1 220 ? 32.610  11.386  12.695  1.00 10.17 ?  222 GLU A CA  1 
ATOM   1688 C  C   . GLU A 1 220 ? 32.346  10.877  11.279  1.00 10.48 ?  222 GLU A C   1 
ATOM   1689 O  O   . GLU A 1 220 ? 33.304  10.623  10.542  1.00 9.48  ?  222 GLU A O   1 
ATOM   1690 C  CB  . GLU A 1 220 ? 32.548  10.234  13.690  1.00 9.29  ?  222 GLU A CB  1 
ATOM   1691 C  CG  . GLU A 1 220 ? 33.696  9.251   13.520  1.00 8.93  ?  222 GLU A CG  1 
ATOM   1692 C  CD  . GLU A 1 220 ? 35.003  9.672   14.185  1.00 15.25 ?  222 GLU A CD  1 
ATOM   1693 O  OE1 . GLU A 1 220 ? 35.157  10.846  14.598  1.00 16.97 ?  222 GLU A OE1 1 
ATOM   1694 O  OE2 . GLU A 1 220 ? 35.895  8.807   14.259  1.00 15.13 ?  222 GLU A OE2 1 
ATOM   1695 N  N   . ASN A 1 221 ? 31.081  10.684  10.863  1.00 9.34  ?  223 ASN A N   1 
ATOM   1696 C  CA  . ASN A 1 221 ? 30.941  10.203  9.490   1.00 9.33  ?  223 ASN A CA  1 
ATOM   1697 C  C   . ASN A 1 221 ? 31.216  11.306  8.472   1.00 9.61  ?  223 ASN A C   1 
ATOM   1698 O  O   . ASN A 1 221 ? 31.684  10.996  7.369   1.00 9.52  ?  223 ASN A O   1 
ATOM   1699 C  CB  . ASN A 1 221 ? 29.588  9.483   9.273   1.00 11.26 ?  223 ASN A CB  1 
ATOM   1700 C  CG  . ASN A 1 221 ? 28.370  10.414  9.143   1.00 9.46  ?  223 ASN A CG  1 
ATOM   1701 O  OD1 . ASN A 1 221 ? 28.378  11.575  9.550   1.00 9.46  ?  223 ASN A OD1 1 
ATOM   1702 N  ND2 . ASN A 1 221 ? 27.280  9.861   8.585   1.00 9.94  ?  223 ASN A ND2 1 
ATOM   1703 N  N   . THR A 1 222 ? 31.047  12.582  8.841   1.00 8.28  ?  224 THR A N   1 
ATOM   1704 C  CA  . THR A 1 222 ? 31.535  13.658  7.978   1.00 8.22  ?  224 THR A CA  1 
ATOM   1705 C  C   . THR A 1 222 ? 33.048  13.592  7.830   1.00 10.96 ?  224 THR A C   1 
ATOM   1706 O  O   . THR A 1 222 ? 33.575  13.707  6.718   1.00 9.78  ?  224 THR A O   1 
ATOM   1707 C  CB  . THR A 1 222 ? 31.108  15.022  8.521   1.00 9.73  ?  224 THR A CB  1 
ATOM   1708 O  OG1 . THR A 1 222 ? 29.673  15.070  8.590   1.00 11.97 ?  224 THR A OG1 1 
ATOM   1709 C  CG2 . THR A 1 222 ? 31.592  16.145  7.603   1.00 11.37 ?  224 THR A CG2 1 
ATOM   1710 N  N   . ARG A 1 223 ? 33.759  13.388  8.934   1.00 9.73  ?  225 ARG A N   1 
ATOM   1711 C  CA  . ARG A 1 223 ? 35.216  13.331  8.866   1.00 11.71 ?  225 ARG A CA  1 
ATOM   1712 C  C   . ARG A 1 223 ? 35.678  12.138  8.030   1.00 10.76 ?  225 ARG A C   1 
ATOM   1713 O  O   . ARG A 1 223 ? 36.569  12.268  7.186   1.00 11.05 ?  225 ARG A O   1 
ATOM   1714 C  CB  . ARG A 1 223 ? 35.780  13.274  10.287  1.00 13.41 ?  225 ARG A CB  1 
ATOM   1715 C  CG  . ARG A 1 223 ? 37.177  12.731  10.387  1.00 20.28 ?  225 ARG A CG  1 
ATOM   1716 C  CD  . ARG A 1 223 ? 37.681  12.836  11.823  1.00 20.98 ?  225 ARG A CD  1 
ATOM   1717 N  NE  . ARG A 1 223 ? 37.683  14.207  12.322  1.00 24.01 ?  225 ARG A NE  1 
ATOM   1718 C  CZ  . ARG A 1 223 ? 38.716  15.037  12.195  1.00 31.45 ?  225 ARG A CZ  1 
ATOM   1719 N  NH1 . ARG A 1 223 ? 39.820  14.633  11.577  1.00 27.86 ?  225 ARG A NH1 1 
ATOM   1720 N  NH2 . ARG A 1 223 ? 38.646  16.271  12.682  1.00 36.77 ?  225 ARG A NH2 1 
ATOM   1721 N  N   . ILE A 1 224 ? 35.060  10.974  8.229   1.00 10.07 ?  226 ILE A N   1 
ATOM   1722 C  CA  . ILE A 1 224 ? 35.460  9.786   7.473   1.00 7.85  ?  226 ILE A CA  1 
ATOM   1723 C  C   . ILE A 1 224 ? 35.128  9.939   5.991   1.00 10.10 ?  226 ILE A C   1 
ATOM   1724 O  O   . ILE A 1 224 ? 35.918  9.542   5.122   1.00 10.35 ?  226 ILE A O   1 
ATOM   1725 C  CB  . ILE A 1 224 ? 34.813  8.530   8.087   1.00 7.89  ?  226 ILE A CB  1 
ATOM   1726 C  CG1 . ILE A 1 224 ? 35.459  8.244   9.454   1.00 11.83 ?  226 ILE A CG1 1 
ATOM   1727 C  CG2 . ILE A 1 224 ? 34.954  7.319   7.142   1.00 9.57  ?  226 ILE A CG2 1 
ATOM   1728 C  CD1 . ILE A 1 224 ? 34.772  7.175   10.277  1.00 11.02 ?  226 ILE A CD1 1 
ATOM   1729 N  N   . ALA A 1 225 ? 33.957  10.504  5.669   1.00 9.97  ?  227 ALA A N   1 
ATOM   1730 C  CA  . ALA A 1 225 ? 33.625  10.710  4.262   1.00 8.91  ?  227 ALA A CA  1 
ATOM   1731 C  C   . ALA A 1 225 ? 34.630  11.641  3.589   1.00 11.31 ?  227 ALA A C   1 
ATOM   1732 O  O   . ALA A 1 225 ? 34.969  11.456  2.413   1.00 10.93 ?  227 ALA A O   1 
ATOM   1733 C  CB  . ALA A 1 225 ? 32.202  11.265  4.134   1.00 10.13 ?  227 ALA A CB  1 
ATOM   1734 N  N   . ARG A 1 226 ? 35.121  12.647  4.321   1.00 12.44 ?  228 ARG A N   1 
ATOM   1735 C  CA  . ARG A 1 226 ? 36.074  13.594  3.742   1.00 12.56 ?  228 ARG A CA  1 
ATOM   1736 C  C   . ARG A 1 226 ? 37.441  12.951  3.526   1.00 12.25 ?  228 ARG A C   1 
ATOM   1737 O  O   . ARG A 1 226 ? 38.200  13.394  2.651   1.00 13.13 ?  228 ARG A O   1 
ATOM   1738 C  CB  . ARG A 1 226 ? 36.195  14.836  4.636   1.00 16.48 ?  228 ARG A CB  1 
ATOM   1739 C  CG  . ARG A 1 226 ? 35.137  15.931  4.391   1.00 19.29 ?  228 ARG A CG  1 
ATOM   1740 C  CD  . ARG A 1 226 ? 35.178  16.506  2.960   1.00 20.88 ?  228 ARG A CD  1 
ATOM   1741 N  NE  . ARG A 1 226 ? 34.191  17.576  2.766   1.00 25.92 ?  228 ARG A NE  1 
ATOM   1742 C  CZ  . ARG A 1 226 ? 33.708  17.959  1.584   1.00 23.22 ?  228 ARG A CZ  1 
ATOM   1743 N  NH1 . ARG A 1 226 ? 34.123  17.371  0.465   1.00 23.71 ?  228 ARG A NH1 1 
ATOM   1744 N  NH2 . ARG A 1 226 ? 32.803  18.937  1.519   1.00 22.19 ?  228 ARG A NH2 1 
ATOM   1745 N  N   . MET A 1 227 ? 37.780  11.909  4.296   1.00 8.62  ?  229 MET A N   1 
ATOM   1746 C  CA  . MET A 1 227 ? 39.020  11.184  4.010   1.00 9.40  ?  229 MET A CA  1 
ATOM   1747 C  C   . MET A 1 227 ? 38.951  10.397  2.714   1.00 8.69  ?  229 MET A C   1 
ATOM   1748 O  O   . MET A 1 227 ? 39.980  10.236  2.049   1.00 12.81 ?  229 MET A O   1 
ATOM   1749 C  CB  . MET A 1 227 ? 39.427  10.285  5.181   1.00 12.45 ?  229 MET A CB  1 
ATOM   1750 C  CG  . MET A 1 227 ? 39.423  11.003  6.531   1.00 15.01 ?  229 MET A CG  1 
ATOM   1751 S  SD  . MET A 1 227 ? 39.394  9.947   7.983   1.00 17.10 ?  229 MET A SD  1 
ATOM   1752 C  CE  . MET A 1 227 ? 40.913  9.042   7.797   1.00 13.22 ?  229 MET A CE  1 
ATOM   1753 N  N   . ALA A 1 228 ? 37.759  9.941   2.319   1.00 9.86  ?  230 ALA A N   1 
ATOM   1754 C  CA  . ALA A 1 228 ? 37.575  9.300   1.018   1.00 9.53  ?  230 ALA A CA  1 
ATOM   1755 C  C   . ALA A 1 228 ? 37.428  10.312  -0.109  1.00 11.17 ?  230 ALA A C   1 
ATOM   1756 O  O   . ALA A 1 228 ? 37.893  10.079  -1.236  1.00 13.73 ?  230 ALA A O   1 
ATOM   1757 C  CB  . ALA A 1 228 ? 36.318  8.422   1.036   1.00 10.23 ?  230 ALA A CB  1 
ATOM   1758 N  N   . GLY A 1 229 ? 36.750  11.413  0.173   1.00 10.69 ?  231 GLY A N   1 
ATOM   1759 C  CA  . GLY A 1 229 ? 36.369  12.380  -0.829  1.00 12.07 ?  231 GLY A CA  1 
ATOM   1760 C  C   . GLY A 1 229 ? 35.031  12.051  -1.463  1.00 12.93 ?  231 GLY A C   1 
ATOM   1761 O  O   . GLY A 1 229 ? 34.545  10.924  -1.430  1.00 9.89  ?  231 GLY A O   1 
ATOM   1762 N  N   . CYS A 1 230 ? 34.431  13.080  -2.040  1.00 9.97  ?  232 CYS A N   1 
ATOM   1763 C  CA  . CYS A 1 230 ? 33.230  12.930  -2.860  1.00 8.74  ?  232 CYS A CA  1 
ATOM   1764 C  C   . CYS A 1 230 ? 33.203  14.178  -3.706  1.00 13.91 ?  232 CYS A C   1 
ATOM   1765 O  O   . CYS A 1 230 ? 33.148  15.279  -3.152  1.00 16.08 ?  232 CYS A O   1 
ATOM   1766 C  CB  . CYS A 1 230 ? 31.966  12.818  -2.019  1.00 12.97 ?  232 CYS A CB  1 
ATOM   1767 S  SG  . CYS A 1 230 ? 30.485  12.533  -3.034  1.00 17.24 ?  232 CYS A SG  1 
ATOM   1768 N  N   . ASP A 1 231 ? 33.288  14.017  -5.024  1.00 9.07  ?  233 ASP A N   1 
ATOM   1769 C  CA  . ASP A 1 231 ? 33.337  15.176  -5.900  1.00 12.38 ?  233 ASP A CA  1 
ATOM   1770 C  C   . ASP A 1 231 ? 31.990  15.860  -6.069  1.00 10.40 ?  233 ASP A C   1 
ATOM   1771 O  O   . ASP A 1 231 ? 31.956  17.067  -6.338  1.00 13.01 ?  233 ASP A O   1 
ATOM   1772 C  CB  . ASP A 1 231 ? 33.890  14.763  -7.258  1.00 10.80 ?  233 ASP A CB  1 
ATOM   1773 C  CG  . ASP A 1 231 ? 35.281  14.154  -7.137  1.00 14.53 ?  233 ASP A CG  1 
ATOM   1774 O  OD1 . ASP A 1 231 ? 36.170  14.848  -6.591  1.00 18.90 ?  233 ASP A OD1 1 
ATOM   1775 O  OD2 . ASP A 1 231 ? 35.469  12.981  -7.518  1.00 14.12 ?  233 ASP A OD2 1 
ATOM   1776 N  N   . PHE A 1 232 ? 30.878  15.130  -5.950  1.00 10.41 ?  234 PHE A N   1 
ATOM   1777 C  CA  . PHE A 1 232 ? 29.584  15.713  -6.290  1.00 8.48  ?  234 PHE A CA  1 
ATOM   1778 C  C   . PHE A 1 232 ? 28.476  14.884  -5.659  1.00 10.43 ?  234 PHE A C   1 
ATOM   1779 O  O   . PHE A 1 232 ? 28.476  13.656  -5.790  1.00 9.84  ?  234 PHE A O   1 
ATOM   1780 C  CB  . PHE A 1 232 ? 29.414  15.754  -7.810  1.00 9.01  ?  234 PHE A CB  1 
ATOM   1781 C  CG  . PHE A 1 232 ? 28.399  16.746  -8.290  1.00 9.78  ?  234 PHE A CG  1 
ATOM   1782 C  CD1 . PHE A 1 232 ? 28.760  18.070  -8.502  1.00 10.43 ?  234 PHE A CD1 1 
ATOM   1783 C  CD2 . PHE A 1 232 ? 27.099  16.342  -8.590  1.00 10.80 ?  234 PHE A CD2 1 
ATOM   1784 C  CE1 . PHE A 1 232 ? 27.829  19.000  -8.985  1.00 10.65 ?  234 PHE A CE1 1 
ATOM   1785 C  CE2 . PHE A 1 232 ? 26.161  17.269  -9.066  1.00 10.77 ?  234 PHE A CE2 1 
ATOM   1786 C  CZ  . PHE A 1 232 ? 26.538  18.601  -9.252  1.00 9.58  ?  234 PHE A CZ  1 
ATOM   1787 N  N   . ILE A 1 233 ? 27.537  15.544  -4.987  1.00 9.10  ?  235 ILE A N   1 
ATOM   1788 C  CA  . ILE A 1 233 ? 26.325  14.857  -4.535  1.00 8.01  ?  235 ILE A CA  1 
ATOM   1789 C  C   . ILE A 1 233 ? 25.098  15.444  -5.207  1.00 8.09  ?  235 ILE A C   1 
ATOM   1790 O  O   . ILE A 1 233 ? 25.086  16.591  -5.655  1.00 8.00  ?  235 ILE A O   1 
ATOM   1791 C  CB  . ILE A 1 233 ? 26.178  14.903  -3.001  1.00 7.51  ?  235 ILE A CB  1 
ATOM   1792 C  CG1 . ILE A 1 233 ? 25.852  16.316  -2.501  1.00 9.66  ?  235 ILE A CG1 1 
ATOM   1793 C  CG2 . ILE A 1 233 ? 27.413  14.349  -2.330  1.00 10.21 ?  235 ILE A CG2 1 
ATOM   1794 C  CD1 . ILE A 1 233 ? 25.166  16.316  -1.148  1.00 11.10 ?  235 ILE A CD1 1 
ATOM   1795 N  N   . VAL A 1 234 ? 24.049  14.619  -5.284  1.00 7.93  ?  236 VAL A N   1 
ATOM   1796 C  CA  . VAL A 1 234 ? 22.686  15.066  -5.568  1.00 8.88  ?  236 VAL A CA  1 
ATOM   1797 C  C   . VAL A 1 234 ? 21.804  14.447  -4.495  1.00 7.85  ?  236 VAL A C   1 
ATOM   1798 O  O   . VAL A 1 234 ? 21.765  13.220  -4.364  1.00 9.41  ?  236 VAL A O   1 
ATOM   1799 C  CB  . VAL A 1 234 ? 22.201  14.645  -6.965  1.00 10.29 ?  236 VAL A CB  1 
ATOM   1800 C  CG1 . VAL A 1 234 ? 20.779  15.134  -7.190  1.00 7.45  ?  236 VAL A CG1 1 
ATOM   1801 C  CG2 . VAL A 1 234 ? 23.128  15.177  -8.066  1.00 9.54  ?  236 VAL A CG2 1 
ATOM   1802 N  N   . ASN A 1 235 ? 21.109  15.282  -3.712  1.00 8.70  ?  237 ASN A N   1 
ATOM   1803 C  CA  . ASN A 1 235 ? 20.207  14.791  -2.673  1.00 8.73  ?  237 ASN A CA  1 
ATOM   1804 C  C   . ASN A 1 235 ? 18.821  15.411  -2.856  1.00 7.74  ?  237 ASN A C   1 
ATOM   1805 O  O   . ASN A 1 235 ? 18.692  16.556  -3.308  1.00 10.26 ?  237 ASN A O   1 
ATOM   1806 C  CB  . ASN A 1 235 ? 20.689  15.150  -1.254  1.00 7.44  ?  237 ASN A CB  1 
ATOM   1807 C  CG  . ASN A 1 235 ? 21.847  14.273  -0.731  1.00 9.30  ?  237 ASN A CG  1 
ATOM   1808 O  OD1 . ASN A 1 235 ? 22.241  14.453  0.417   1.00 11.22 ?  237 ASN A OD1 1 
ATOM   1809 N  ND2 . ASN A 1 235 ? 22.398  13.361  -1.546  1.00 8.36  ?  237 ASN A ND2 1 
ATOM   1810 N  N   . VAL A 1 236 ? 17.782  14.661  -2.474  1.00 6.50  ?  238 VAL A N   1 
ATOM   1811 C  CA  . VAL A 1 236 ? 16.419  15.179  -2.503  1.00 6.19  ?  238 VAL A CA  1 
ATOM   1812 C  C   . VAL A 1 236 ? 15.774  15.061  -1.131  1.00 7.79  ?  238 VAL A C   1 
ATOM   1813 O  O   . VAL A 1 236 ? 16.214  14.309  -0.258  1.00 8.80  ?  238 VAL A O   1 
ATOM   1814 C  CB  . VAL A 1 236 ? 15.535  14.464  -3.557  1.00 7.85  ?  238 VAL A CB  1 
ATOM   1815 C  CG1 . VAL A 1 236 ? 16.078  14.729  -4.975  1.00 9.36  ?  238 VAL A CG1 1 
ATOM   1816 C  CG2 . VAL A 1 236 ? 15.454  12.950  -3.254  1.00 10.80 ?  238 VAL A CG2 1 
ATOM   1817 N  N   . THR A 1 237 ? 14.681  15.809  -0.958  1.00 8.23  ?  239 THR A N   1 
ATOM   1818 C  CA  . THR A 1 237 ? 13.743  15.593  0.132   1.00 6.87  ?  239 THR A CA  1 
ATOM   1819 C  C   . THR A 1 237 ? 12.418  15.175  -0.487  1.00 9.23  ?  239 THR A C   1 
ATOM   1820 O  O   . THR A 1 237 ? 12.103  15.565  -1.618  1.00 9.28  ?  239 THR A O   1 
ATOM   1821 C  CB  . THR A 1 237 ? 13.540  16.859  0.985   1.00 10.45 ?  239 THR A CB  1 
ATOM   1822 O  OG1 . THR A 1 237 ? 13.162  17.939  0.124   1.00 10.81 ?  239 THR A OG1 1 
ATOM   1823 C  CG2 . THR A 1 237 ? 14.825  17.243  1.687   1.00 11.05 ?  239 THR A CG2 1 
ATOM   1824 N  N   . LEU A 1 238 ? 11.658  14.360  0.236   1.00 7.83  ?  240 LEU A N   1 
ATOM   1825 C  CA  . LEU A 1 238 ? 10.374  13.851  -0.242  1.00 8.82  ?  240 LEU A CA  1 
ATOM   1826 C  C   . LEU A 1 238 ? 9.268   14.231  0.728   1.00 8.27  ?  240 LEU A C   1 
ATOM   1827 O  O   . LEU A 1 238 ? 9.464   14.165  1.945   1.00 9.55  ?  240 LEU A O   1 
ATOM   1828 C  CB  . LEU A 1 238 ? 10.401  12.332  -0.363  1.00 10.08 ?  240 LEU A CB  1 
ATOM   1829 C  CG  . LEU A 1 238 ? 11.418  11.737  -1.321  1.00 7.20  ?  240 LEU A CG  1 
ATOM   1830 C  CD1 . LEU A 1 238 ? 11.322  10.223  -1.264  1.00 10.01 ?  240 LEU A CD1 1 
ATOM   1831 C  CD2 . LEU A 1 238 ? 11.167  12.234  -2.738  1.00 11.49 ?  240 LEU A CD2 1 
ATOM   1832 N  N   . ASP A 1 239 ? 8.084   14.560  0.211   1.00 10.65 ?  241 ASP A N   1 
ATOM   1833 C  CA  . ASP A 1 239 ? 6.983   14.804  1.133   1.00 10.34 ?  241 ASP A CA  1 
ATOM   1834 C  C   . ASP A 1 239 ? 6.297   13.482  1.481   1.00 9.82  ?  241 ASP A C   1 
ATOM   1835 O  O   . ASP A 1 239 ? 6.778   12.392  1.143   1.00 11.98 ?  241 ASP A O   1 
ATOM   1836 C  CB  . ASP A 1 239 ? 6.037   15.877  0.577   1.00 12.10 ?  241 ASP A CB  1 
ATOM   1837 C  CG  . ASP A 1 239 ? 5.226   15.433  -0.645  1.00 15.37 ?  241 ASP A CG  1 
ATOM   1838 O  OD1 . ASP A 1 239 ? 5.208   14.245  -1.016  1.00 11.82 ?  241 ASP A OD1 1 
ATOM   1839 O  OD2 . ASP A 1 239 ? 4.572   16.322  -1.244  1.00 14.69 ?  241 ASP A OD2 1 
ATOM   1840 N  N   . GLY A 1 240 ? 5.171   13.561  2.200   1.00 14.09 ?  242 GLY A N   1 
ATOM   1841 C  CA  . GLY A 1 240 ? 4.525   12.345  2.674   1.00 13.99 ?  242 GLY A CA  1 
ATOM   1842 C  C   . GLY A 1 240 ? 4.044   11.438  1.560   1.00 16.74 ?  242 GLY A C   1 
ATOM   1843 O  O   . GLY A 1 240 ? 3.981   10.215  1.730   1.00 18.18 ?  242 GLY A O   1 
ATOM   1844 N  N   . ALA A 1 241 ? 3.704   12.010  0.411   1.00 12.74 ?  243 ALA A N   1 
ATOM   1845 C  CA  . ALA A 1 241 ? 3.283   11.232  -0.742  1.00 12.85 ?  243 ALA A CA  1 
ATOM   1846 C  C   . ALA A 1 241 ? 4.438   10.919  -1.682  1.00 11.30 ?  243 ALA A C   1 
ATOM   1847 O  O   . ALA A 1 241 ? 4.207   10.500  -2.819  1.00 11.70 ?  243 ALA A O   1 
ATOM   1848 C  CB  . ALA A 1 241 ? 2.160   11.961  -1.485  1.00 14.09 ?  243 ALA A CB  1 
ATOM   1849 N  N   . ARG A 1 242 ? 5.679   11.103  -1.215  1.00 11.77 ?  244 ARG A N   1 
ATOM   1850 C  CA  . ARG A 1 242 ? 6.906   10.746  -1.930  1.00 13.16 ?  244 ARG A CA  1 
ATOM   1851 C  C   . ARG A 1 242 ? 7.133   11.610  -3.172  1.00 13.98 ?  244 ARG A C   1 
ATOM   1852 O  O   . ARG A 1 242 ? 7.783   11.178  -4.122  1.00 14.59 ?  244 ARG A O   1 
ATOM   1853 C  CB  . ARG A 1 242 ? 6.937   9.255   -2.298  1.00 13.48 ?  244 ARG A CB  1 
ATOM   1854 C  CG  . ARG A 1 242 ? 6.646   8.322   -1.126  1.00 16.23 ?  244 ARG A CG  1 
ATOM   1855 C  CD  . ARG A 1 242 ? 7.878   8.071   -0.299  1.00 15.62 ?  244 ARG A CD  1 
ATOM   1856 N  NE  . ARG A 1 242 ? 7.584   7.305   0.915   1.00 15.84 ?  244 ARG A NE  1 
ATOM   1857 C  CZ  . ARG A 1 242 ? 7.624   5.976   1.011   1.00 14.03 ?  244 ARG A CZ  1 
ATOM   1858 N  NH1 . ARG A 1 242 ? 7.935   5.227   -0.039  1.00 12.01 ?  244 ARG A NH1 1 
ATOM   1859 N  NH2 . ARG A 1 242 ? 7.342   5.394   2.169   1.00 14.69 ?  244 ARG A NH2 1 
ATOM   1860 N  N   . ARG A 1 243 ? 6.626   12.836  -3.177  1.00 11.28 ?  245 ARG A N   1 
ATOM   1861 C  CA  . ARG A 1 243 ? 6.993   13.797  -4.213  1.00 8.80  ?  245 ARG A CA  1 
ATOM   1862 C  C   . ARG A 1 243 ? 8.258   14.536  -3.782  1.00 10.03 ?  245 ARG A C   1 
ATOM   1863 O  O   . ARG A 1 243 ? 8.409   14.906  -2.610  1.00 10.79 ?  245 ARG A O   1 
ATOM   1864 C  CB  . ARG A 1 243 ? 5.886   14.831  -4.455  1.00 11.00 ?  245 ARG A CB  1 
ATOM   1865 C  CG  . ARG A 1 243 ? 4.626   14.361  -5.213  1.00 21.27 ?  245 ARG A CG  1 
ATOM   1866 C  CD  . ARG A 1 243 ? 3.587   13.783  -4.281  1.00 19.85 ?  245 ARG A CD  1 
ATOM   1867 N  NE  . ARG A 1 243 ? 3.148   14.784  -3.305  1.00 17.95 ?  245 ARG A NE  1 
ATOM   1868 C  CZ  . ARG A 1 243 ? 2.174   15.677  -3.477  1.00 14.80 ?  245 ARG A CZ  1 
ATOM   1869 N  NH1 . ARG A 1 243 ? 1.448   15.720  -4.601  1.00 15.42 ?  245 ARG A NH1 1 
ATOM   1870 N  NH2 . ARG A 1 243 ? 1.912   16.524  -2.493  1.00 14.07 ?  245 ARG A NH2 1 
ATOM   1871 N  N   . ILE A 1 244 ? 9.145   14.794  -4.742  1.00 8.30  ?  246 ILE A N   1 
ATOM   1872 C  CA  . ILE A 1 244 ? 10.360  15.555  -4.454  1.00 8.58  ?  246 ILE A CA  1 
ATOM   1873 C  C   . ILE A 1 244 ? 10.003  17.007  -4.166  1.00 7.81  ?  246 ILE A C   1 
ATOM   1874 O  O   . ILE A 1 244 ? 9.349   17.671  -4.981  1.00 9.87  ?  246 ILE A O   1 
ATOM   1875 C  CB  . ILE A 1 244 ? 11.331  15.457  -5.635  1.00 8.06  ?  246 ILE A CB  1 
ATOM   1876 C  CG1 . ILE A 1 244 ? 11.804  14.011  -5.809  1.00 8.78  ?  246 ILE A CG1 1 
ATOM   1877 C  CG2 . ILE A 1 244 ? 12.516  16.418  -5.435  1.00 9.85  ?  246 ILE A CG2 1 
ATOM   1878 C  CD1 . ILE A 1 244 ? 12.652  13.799  -7.074  1.00 10.67 ?  246 ILE A CD1 1 
ATOM   1879 N  N   . THR A 1 245 ? 10.447  17.515  -3.015  1.00 7.24  ?  247 THR A N   1 
ATOM   1880 C  CA  . THR A 1 245 ? 10.198  18.906  -2.642  1.00 9.31  ?  247 THR A CA  1 
ATOM   1881 C  C   . THR A 1 245 ? 11.440  19.788  -2.715  1.00 10.29 ?  247 THR A C   1 
ATOM   1882 O  O   . THR A 1 245 ? 11.319  21.018  -2.639  1.00 10.77 ?  247 THR A O   1 
ATOM   1883 C  CB  . THR A 1 245 ? 9.618   18.990  -1.224  1.00 9.48  ?  247 THR A CB  1 
ATOM   1884 O  OG1 . THR A 1 245 ? 10.397  18.176  -0.329  1.00 10.01 ?  247 THR A OG1 1 
ATOM   1885 C  CG2 . THR A 1 245 ? 8.158   18.507  -1.219  1.00 8.66  ?  247 THR A CG2 1 
ATOM   1886 N  N   . SER A 1 246 ? 12.624  19.204  -2.844  1.00 9.66  ?  248 SER A N   1 
ATOM   1887 C  CA  . SER A 1 246 ? 13.826  20.010  -3.005  1.00 9.90  ?  248 SER A CA  1 
ATOM   1888 C  C   . SER A 1 246 ? 14.904  19.146  -3.624  1.00 9.70  ?  248 SER A C   1 
ATOM   1889 O  O   . SER A 1 246 ? 14.892  17.923  -3.486  1.00 8.07  ?  248 SER A O   1 
ATOM   1890 C  CB  . SER A 1 246 ? 14.320  20.587  -1.674  1.00 11.39 ?  248 SER A CB  1 
ATOM   1891 O  OG  . SER A 1 246 ? 15.056  19.627  -0.941  1.00 13.99 ?  248 SER A OG  1 
ATOM   1892 N  N   . VAL A 1 247 ? 15.805  19.799  -4.346  1.00 8.61  ?  249 VAL A N   1 
ATOM   1893 C  CA  . VAL A 1 247 ? 16.985  19.156  -4.910  1.00 6.71  ?  249 VAL A CA  1 
ATOM   1894 C  C   . VAL A 1 247 ? 18.190  19.990  -4.513  1.00 9.20  ?  249 VAL A C   1 
ATOM   1895 O  O   . VAL A 1 247 ? 18.197  21.208  -4.723  1.00 9.67  ?  249 VAL A O   1 
ATOM   1896 C  CB  . VAL A 1 247 ? 16.898  19.044  -6.448  1.00 7.55  ?  249 VAL A CB  1 
ATOM   1897 C  CG1 . VAL A 1 247 ? 18.232  18.542  -7.023  1.00 12.04 ?  249 VAL A CG1 1 
ATOM   1898 C  CG2 . VAL A 1 247 ? 15.785  18.105  -6.857  1.00 9.66  ?  249 VAL A CG2 1 
ATOM   1899 N  N   . VAL A 1 248 ? 19.214  19.346  -3.957  1.00 7.85  ?  250 VAL A N   1 
ATOM   1900 C  CA  . VAL A 1 248 ? 20.483  20.014  -3.695  1.00 9.83  ?  250 VAL A CA  1 
ATOM   1901 C  C   . VAL A 1 248 ? 21.566  19.230  -4.411  1.00 12.12 ?  250 VAL A C   1 
ATOM   1902 O  O   . VAL A 1 248 ? 21.553  17.995  -4.417  1.00 11.50 ?  250 VAL A O   1 
ATOM   1903 C  CB  . VAL A 1 248 ? 20.796  20.153  -2.188  1.00 11.69 ?  250 VAL A CB  1 
ATOM   1904 C  CG1 . VAL A 1 248 ? 19.778  21.084  -1.536  1.00 13.35 ?  250 VAL A CG1 1 
ATOM   1905 C  CG2 . VAL A 1 248 ? 20.860  18.792  -1.482  1.00 9.19  ?  250 VAL A CG2 1 
ATOM   1906 N  N   . ALA A 1 249 ? 22.461  19.948  -5.073  1.00 10.09 ?  251 ALA A N   1 
ATOM   1907 C  CA  . ALA A 1 249 ? 23.574  19.312  -5.764  1.00 10.13 ?  251 ALA A CA  1 
ATOM   1908 C  C   . ALA A 1 249 ? 24.832  20.122  -5.547  1.00 9.67  ?  251 ALA A C   1 
ATOM   1909 O  O   . ALA A 1 249 ? 24.773  21.342  -5.406  1.00 10.45 ?  251 ALA A O   1 
ATOM   1910 C  CB  . ALA A 1 249 ? 23.318  19.194  -7.260  1.00 8.99  ?  251 ALA A CB  1 
ATOM   1911 N  N   . GLY A 1 250 ? 25.970  19.430  -5.573  1.00 8.20  ?  252 GLY A N   1 
ATOM   1912 C  CA  . GLY A 1 250 ? 27.270  20.082  -5.460  1.00 9.37  ?  252 GLY A CA  1 
ATOM   1913 C  C   . GLY A 1 250 ? 28.157  19.510  -4.368  1.00 11.89 ?  252 GLY A C   1 
ATOM   1914 O  O   . GLY A 1 250 ? 28.284  18.289  -4.236  1.00 8.84  ?  252 GLY A O   1 
ATOM   1915 N  N   . ASP A 1 251 ? 28.795  20.398  -3.598  1.00 7.23  ?  253 ASP A N   1 
ATOM   1916 C  CA  . ASP A 1 251 ? 29.709  19.998  -2.528  1.00 10.03 ?  253 ASP A CA  1 
ATOM   1917 C  C   . ASP A 1 251 ? 29.047  19.075  -1.513  1.00 10.94 ?  253 ASP A C   1 
ATOM   1918 O  O   . ASP A 1 251 ? 27.928  19.326  -1.061  1.00 10.71 ?  253 ASP A O   1 
ATOM   1919 C  CB  . ASP A 1 251 ? 30.223  21.238  -1.795  1.00 12.58 ?  253 ASP A CB  1 
ATOM   1920 C  CG  . ASP A 1 251 ? 31.221  20.887  -0.714  1.00 17.55 ?  253 ASP A CG  1 
ATOM   1921 O  OD1 . ASP A 1 251 ? 30.868  20.995  0.474   1.00 14.57 ?  253 ASP A OD1 1 
ATOM   1922 O  OD2 . ASP A 1 251 ? 32.366  20.512  -1.042  1.00 16.19 ?  253 ASP A OD2 1 
ATOM   1923 N  N   . MET A 1 252 ? 29.782  18.040  -1.092  1.00 10.59 ?  254 MET A N   1 
ATOM   1924 C  CA  . MET A 1 252 ? 29.155  17.034  -0.246  1.00 10.91 ?  254 MET A CA  1 
ATOM   1925 C  C   . MET A 1 252 ? 28.704  17.611  1.093   1.00 13.85 ?  254 MET A C   1 
ATOM   1926 O  O   . MET A 1 252 ? 27.655  17.212  1.608   1.00 11.64 ?  254 MET A O   1 
ATOM   1927 C  CB  . MET A 1 252 ? 30.086  15.815  -0.136  1.00 12.88 ?  254 MET A CB  1 
ATOM   1928 C  CG  . MET A 1 252 ? 29.663  14.704  0.816   1.00 13.69 ?  254 MET A CG  1 
ATOM   1929 S  SD  . MET A 1 252 ? 31.015  13.787  1.588   1.00 15.43 ?  254 MET A SD  1 
ATOM   1930 C  CE  . MET A 1 252 ? 31.726  14.900  2.795   1.00 15.24 ?  254 MET A CE  1 
ATOM   1931 N  N   . GLU A 1 253 ? 29.419  18.595  1.642   1.00 11.46 ?  255 GLU A N   1 
ATOM   1932 C  CA  . GLU A 1 253 ? 28.929  19.204  2.878   1.00 10.12 ?  255 GLU A CA  1 
ATOM   1933 C  C   . GLU A 1 253 ? 27.991  20.376  2.632   1.00 9.94  ?  255 GLU A C   1 
ATOM   1934 O  O   . GLU A 1 253 ? 26.935  20.451  3.267   1.00 11.24 ?  255 GLU A O   1 
ATOM   1935 C  CB  . GLU A 1 253 ? 30.101  19.666  3.746   1.00 13.65 ?  255 GLU A CB  1 
ATOM   1936 C  CG  . GLU A 1 253 ? 30.909  18.532  4.306   1.00 12.04 ?  255 GLU A CG  1 
ATOM   1937 C  CD  . GLU A 1 253 ? 32.082  19.044  5.128   1.00 19.25 ?  255 GLU A CD  1 
ATOM   1938 O  OE1 . GLU A 1 253 ? 31.882  19.422  6.294   1.00 22.42 ?  255 GLU A OE1 1 
ATOM   1939 O  OE2 . GLU A 1 253 ? 33.200  19.077  4.585   1.00 23.57 ?  255 GLU A OE2 1 
ATOM   1940 N  N   . GLN A 1 254 ? 28.356  21.308  1.742   1.00 10.66 ?  256 GLN A N   1 
ATOM   1941 C  CA  . GLN A 1 254 ? 27.515  22.492  1.578   1.00 10.17 ?  256 GLN A CA  1 
ATOM   1942 C  C   . GLN A 1 254 ? 26.150  22.151  0.995   1.00 10.12 ?  256 GLN A C   1 
ATOM   1943 O  O   . GLN A 1 254 ? 25.143  22.721  1.420   1.00 11.52 ?  256 GLN A O   1 
ATOM   1944 C  CB  . GLN A 1 254 ? 28.200  23.555  0.723   1.00 12.75 ?  256 GLN A CB  1 
ATOM   1945 C  CG  . GLN A 1 254 ? 29.606  23.859  1.228   1.00 14.77 ?  256 GLN A CG  1 
ATOM   1946 C  CD  . GLN A 1 254 ? 30.370  24.736  0.275   1.00 25.59 ?  256 GLN A CD  1 
ATOM   1947 O  OE1 . GLN A 1 254 ? 31.601  24.624  0.143   1.00 29.30 ?  256 GLN A OE1 1 
ATOM   1948 N  NE2 . GLN A 1 254 ? 29.650  25.644  -0.381  1.00 18.76 ?  256 GLN A NE2 1 
ATOM   1949 N  N   . ALA A 1 255 ? 26.084  21.252  0.010   1.00 9.33  ?  257 ALA A N   1 
ATOM   1950 C  CA  . ALA A 1 255 ? 24.768  20.938  -0.537  1.00 11.62 ?  257 ALA A CA  1 
ATOM   1951 C  C   . ALA A 1 255 ? 23.926  20.174  0.484   1.00 7.71  ?  257 ALA A C   1 
ATOM   1952 O  O   . ALA A 1 255 ? 22.723  20.439  0.636   1.00 9.92  ?  257 ALA A O   1 
ATOM   1953 C  CB  . ALA A 1 255 ? 24.910  20.164  -1.849  1.00 9.09  ?  257 ALA A CB  1 
ATOM   1954 N  N   . PHE A 1 256 ? 24.542  19.244  1.210   1.00 10.39 ?  258 PHE A N   1 
ATOM   1955 C  CA  . PHE A 1 256 ? 23.816  18.500  2.237   1.00 9.35  ?  258 PHE A CA  1 
ATOM   1956 C  C   . PHE A 1 256 ? 23.224  19.452  3.272   1.00 10.06 ?  258 PHE A C   1 
ATOM   1957 O  O   . PHE A 1 256 ? 22.036  19.372  3.605   1.00 9.14  ?  258 PHE A O   1 
ATOM   1958 C  CB  . PHE A 1 256 ? 24.759  17.475  2.883   1.00 9.62  ?  258 PHE A CB  1 
ATOM   1959 C  CG  . PHE A 1 256 ? 24.204  16.822  4.116   1.00 8.36  ?  258 PHE A CG  1 
ATOM   1960 C  CD1 . PHE A 1 256 ? 23.160  15.919  4.018   1.00 7.88  ?  258 PHE A CD1 1 
ATOM   1961 C  CD2 . PHE A 1 256 ? 24.741  17.092  5.371   1.00 7.43  ?  258 PHE A CD2 1 
ATOM   1962 C  CE1 . PHE A 1 256 ? 22.635  15.303  5.151   1.00 8.22  ?  258 PHE A CE1 1 
ATOM   1963 C  CE2 . PHE A 1 256 ? 24.232  16.476  6.505   1.00 10.26 ?  258 PHE A CE2 1 
ATOM   1964 C  CZ  . PHE A 1 256 ? 23.177  15.569  6.398   1.00 9.72  ?  258 PHE A CZ  1 
ATOM   1965 N  N   . LEU A 1 257 ? 24.026  20.404  3.750   1.00 9.34  ?  259 LEU A N   1 
ATOM   1966 C  CA  . LEU A 1 257 ? 23.534  21.310  4.785   1.00 8.76  ?  259 LEU A CA  1 
ATOM   1967 C  C   . LEU A 1 257 ? 22.428  22.223  4.270   1.00 11.15 ?  259 LEU A C   1 
ATOM   1968 O  O   . LEU A 1 257 ? 21.528  22.590  5.038   1.00 11.72 ?  259 LEU A O   1 
ATOM   1969 C  CB  . LEU A 1 257 ? 24.694  22.129  5.341   1.00 8.91  ?  259 LEU A CB  1 
ATOM   1970 C  CG  . LEU A 1 257 ? 25.668  21.301  6.182   1.00 11.09 ?  259 LEU A CG  1 
ATOM   1971 C  CD1 . LEU A 1 257 ? 26.779  22.210  6.678   1.00 18.75 ?  259 LEU A CD1 1 
ATOM   1972 C  CD2 . LEU A 1 257 ? 25.015  20.588  7.350   1.00 15.66 ?  259 LEU A CD2 1 
ATOM   1973 N  N   . LYS A 1 258 ? 22.471  22.597  2.989   1.00 10.16 ?  260 LYS A N   1 
ATOM   1974 C  CA  . LYS A 1 258 ? 21.369  23.358  2.401   1.00 12.30 ?  260 LYS A CA  1 
ATOM   1975 C  C   . LYS A 1 258 ? 20.095  22.525  2.357   1.00 10.62 ?  260 LYS A C   1 
ATOM   1976 O  O   . LYS A 1 258 ? 18.994  23.037  2.604   1.00 11.96 ?  260 LYS A O   1 
ATOM   1977 C  CB  . LYS A 1 258 ? 21.746  23.830  0.994   1.00 12.82 ?  260 LYS A CB  1 
ATOM   1978 C  CG  . LYS A 1 258 ? 20.703  24.700  0.319   1.00 20.74 ?  260 LYS A CG  1 
ATOM   1979 C  CD  . LYS A 1 258 ? 20.625  26.068  0.990   1.00 31.56 ?  260 LYS A CD  1 
ATOM   1980 C  CE  . LYS A 1 258 ? 20.329  27.167  -0.023  1.00 45.56 ?  260 LYS A CE  1 
ATOM   1981 N  NZ  . LYS A 1 258 ? 18.917  27.123  -0.500  1.00 43.21 ?  260 LYS A NZ  1 
ATOM   1982 N  N   . GLY A 1 259 ? 20.223  21.240  2.031   1.00 9.79  ?  261 GLY A N   1 
ATOM   1983 C  CA  . GLY A 1 259 ? 19.052  20.379  2.037   1.00 9.57  ?  261 GLY A CA  1 
ATOM   1984 C  C   . GLY A 1 259 ? 18.503  20.190  3.436   1.00 9.53  ?  261 GLY A C   1 
ATOM   1985 O  O   . GLY A 1 259 ? 17.290  20.198  3.634   1.00 8.84  ?  261 GLY A O   1 
ATOM   1986 N  N   . VAL A 1 260 ? 19.389  20.014  4.424   1.00 7.86  ?  262 VAL A N   1 
ATOM   1987 C  CA  . VAL A 1 260 ? 18.944  19.899  5.817   1.00 7.35  ?  262 VAL A CA  1 
ATOM   1988 C  C   . VAL A 1 260 ? 18.241  21.176  6.268   1.00 10.68 ?  262 VAL A C   1 
ATOM   1989 O  O   . VAL A 1 260 ? 17.203  21.129  6.949   1.00 11.56 ?  262 VAL A O   1 
ATOM   1990 C  CB  . VAL A 1 260 ? 20.135  19.584  6.740   1.00 10.22 ?  262 VAL A CB  1 
ATOM   1991 C  CG1 . VAL A 1 260 ? 19.720  19.759  8.205   1.00 11.88 ?  262 VAL A CG1 1 
ATOM   1992 C  CG2 . VAL A 1 260 ? 20.658  18.180  6.467   1.00 10.34 ?  262 VAL A CG2 1 
ATOM   1993 N  N   . ALA A 1 261 ? 18.800  22.336  5.914   1.00 8.92  ?  263 ALA A N   1 
ATOM   1994 C  CA  . ALA A 1 261 ? 18.154  23.594  6.291   1.00 10.82 ?  263 ALA A CA  1 
ATOM   1995 C  C   . ALA A 1 261 ? 16.721  23.650  5.777   1.00 13.82 ?  263 ALA A C   1 
ATOM   1996 O  O   . ALA A 1 261 ? 15.824  24.146  6.466   1.00 12.08 ?  263 ALA A O   1 
ATOM   1997 C  CB  . ALA A 1 261 ? 18.954  24.777  5.750   1.00 13.27 ?  263 ALA A CB  1 
ATOM   1998 N  N   . PHE A 1 262 ? 16.478  23.130  4.576   1.00 10.72 ?  264 PHE A N   1 
ATOM   1999 C  CA  . PHE A 1 262 ? 15.106  23.089  4.076   1.00 10.45 ?  264 PHE A CA  1 
ATOM   2000 C  C   . PHE A 1 262 ? 14.262  22.068  4.831   1.00 12.90 ?  264 PHE A C   1 
ATOM   2001 O  O   . PHE A 1 262 ? 13.134  22.368  5.248   1.00 13.73 ?  264 PHE A O   1 
ATOM   2002 C  CB  . PHE A 1 262 ? 15.085  22.777  2.579   1.00 11.44 ?  264 PHE A CB  1 
ATOM   2003 C  CG  . PHE A 1 262 ? 13.694  22.506  2.058   1.00 12.04 ?  264 PHE A CG  1 
ATOM   2004 C  CD1 . PHE A 1 262 ? 12.779  23.541  1.931   1.00 15.96 ?  264 PHE A CD1 1 
ATOM   2005 C  CD2 . PHE A 1 262 ? 13.290  21.224  1.755   1.00 11.05 ?  264 PHE A CD2 1 
ATOM   2006 C  CE1 . PHE A 1 262 ? 11.490  23.300  1.475   1.00 19.00 ?  264 PHE A CE1 1 
ATOM   2007 C  CE2 . PHE A 1 262 ? 11.995  20.970  1.314   1.00 14.12 ?  264 PHE A CE2 1 
ATOM   2008 C  CZ  . PHE A 1 262 ? 11.102  22.013  1.161   1.00 15.44 ?  264 PHE A CZ  1 
ATOM   2009 N  N   . VAL A 1 263 ? 14.780  20.846  5.008   1.00 11.61 ?  265 VAL A N   1 
ATOM   2010 C  CA  . VAL A 1 263 ? 13.922  19.784  5.536   1.00 8.39  ?  265 VAL A CA  1 
ATOM   2011 C  C   . VAL A 1 263 ? 13.575  20.087  6.986   1.00 12.87 ?  265 VAL A C   1 
ATOM   2012 O  O   . VAL A 1 263 ? 12.496  19.713  7.462   1.00 13.23 ?  265 VAL A O   1 
ATOM   2013 C  CB  . VAL A 1 263 ? 14.585  18.391  5.414   1.00 10.22 ?  265 VAL A CB  1 
ATOM   2014 C  CG1 . VAL A 1 263 ? 15.685  18.196  6.447   1.00 14.17 ?  265 VAL A CG1 1 
ATOM   2015 C  CG2 . VAL A 1 263 ? 13.543  17.259  5.412   1.00 15.22 ?  265 VAL A CG2 1 
ATOM   2016 N  N   . GLU A 1 264 ? 14.469  20.783  7.711   1.00 10.75 ?  266 GLU A N   1 
ATOM   2017 C  CA  . GLU A 1 264 ? 14.159  21.201  9.077   1.00 13.80 ?  266 GLU A CA  1 
ATOM   2018 C  C   . GLU A 1 264 ? 12.911  22.065  9.149   1.00 16.85 ?  266 GLU A C   1 
ATOM   2019 O  O   . GLU A 1 264 ? 12.238  22.079  10.184  1.00 21.14 ?  266 GLU A O   1 
ATOM   2020 C  CB  . GLU A 1 264 ? 15.320  21.983  9.681   1.00 15.64 ?  266 GLU A CB  1 
ATOM   2021 C  CG  . GLU A 1 264 ? 16.454  21.143  10.067  1.00 20.16 ?  266 GLU A CG  1 
ATOM   2022 C  CD  . GLU A 1 264 ? 17.572  21.961  10.663  1.00 25.54 ?  266 GLU A CD  1 
ATOM   2023 O  OE1 . GLU A 1 264 ? 18.233  21.430  11.569  1.00 29.23 ?  266 GLU A OE1 1 
ATOM   2024 O  OE2 . GLU A 1 264 ? 17.772  23.127  10.234  1.00 27.15 ?  266 GLU A OE2 1 
ATOM   2025 N  N   . THR A 1 265 ? 12.604  22.812  8.086   1.00 14.42 ?  267 THR A N   1 
ATOM   2026 C  CA  . THR A 1 265 ? 11.408  23.653  8.082   1.00 13.87 ?  267 THR A CA  1 
ATOM   2027 C  C   . THR A 1 265 ? 10.133  22.869  7.815   1.00 19.22 ?  267 THR A C   1 
ATOM   2028 O  O   . THR A 1 265 ? 9.044   23.433  7.972   1.00 18.05 ?  267 THR A O   1 
ATOM   2029 C  CB  . THR A 1 265 ? 11.511  24.777  7.043   1.00 13.18 ?  267 THR A CB  1 
ATOM   2030 O  OG1 . THR A 1 265 ? 11.308  24.263  5.716   1.00 16.00 ?  267 THR A OG1 1 
ATOM   2031 C  CG2 . THR A 1 265 ? 12.873  25.467  7.129   1.00 22.86 ?  267 THR A CG2 1 
ATOM   2032 N  N   . VAL A 1 266 ? 10.222  21.604  7.399   1.00 13.84 ?  268 VAL A N   1 
ATOM   2033 C  CA  . VAL A 1 266 ? 8.994   20.881  7.099   1.00 14.03 ?  268 VAL A CA  1 
ATOM   2034 C  C   . VAL A 1 266 ? 8.796   19.660  7.990   1.00 16.36 ?  268 VAL A C   1 
ATOM   2035 O  O   . VAL A 1 266 ? 7.651   19.260  8.221   1.00 15.45 ?  268 VAL A O   1 
ATOM   2036 C  CB  . VAL A 1 266 ? 8.915   20.469  5.614   1.00 21.31 ?  268 VAL A CB  1 
ATOM   2037 C  CG1 . VAL A 1 266 ? 8.861   21.698  4.736   1.00 23.67 ?  268 VAL A CG1 1 
ATOM   2038 C  CG2 . VAL A 1 266 ? 10.065  19.590  5.223   1.00 17.11 ?  268 VAL A CG2 1 
ATOM   2039 N  N   . VAL A 1 267 ? 9.874   19.040  8.491   1.00 14.10 ?  269 VAL A N   1 
ATOM   2040 C  CA  . VAL A 1 267 ? 9.655   17.747  9.157   1.00 13.05 ?  269 VAL A CA  1 
ATOM   2041 C  C   . VAL A 1 267 ? 9.261   17.870  10.619  1.00 11.29 ?  269 VAL A C   1 
ATOM   2042 O  O   . VAL A 1 267 ? 8.786   16.882  11.193  1.00 11.14 ?  269 VAL A O   1 
ATOM   2043 C  CB  . VAL A 1 267 ? 10.866  16.789  9.119   1.00 15.56 ?  269 VAL A CB  1 
ATOM   2044 C  CG1 . VAL A 1 267 ? 11.053  16.224  7.719   1.00 17.32 ?  269 VAL A CG1 1 
ATOM   2045 C  CG2 . VAL A 1 267 ? 12.100  17.483  9.632   1.00 16.55 ?  269 VAL A CG2 1 
ATOM   2046 N  N   . LYS A 1 268 ? 9.439   19.031  11.247  1.00 11.16 ?  270 LYS A N   1 
ATOM   2047 C  CA  . LYS A 1 268 ? 9.141   19.161  12.671  1.00 12.01 ?  270 LYS A CA  1 
ATOM   2048 C  C   . LYS A 1 268 ? 7.637   19.299  12.870  1.00 16.35 ?  270 LYS A C   1 
ATOM   2049 O  O   . LYS A 1 268 ? 6.969   20.038  12.140  1.00 15.99 ?  270 LYS A O   1 
ATOM   2050 C  CB  . LYS A 1 268 ? 9.882   20.362  13.265  1.00 15.18 ?  270 LYS A CB  1 
ATOM   2051 C  CG  . LYS A 1 268 ? 11.341  20.048  13.542  1.00 26.98 ?  270 LYS A CG  1 
ATOM   2052 C  CD  . LYS A 1 268 ? 12.038  21.136  14.352  1.00 32.94 ?  270 LYS A CD  1 
ATOM   2053 C  CE  . LYS A 1 268 ? 13.556  20.934  14.347  1.00 37.54 ?  270 LYS A CE  1 
ATOM   2054 N  NZ  . LYS A 1 268 ? 14.217  21.509  15.557  1.00 45.38 ?  270 LYS A NZ  1 
ATOM   2055 N  N   . ALA A 1 269 ? 7.097   18.540  13.819  1.00 13.48 ?  271 ALA A N   1 
ATOM   2056 C  CA  . ALA A 1 269 ? 5.672   18.580  14.131  1.00 14.10 ?  271 ALA A CA  1 
ATOM   2057 C  C   . ALA A 1 269 ? 5.533   18.593  15.646  1.00 16.40 ?  271 ALA A C   1 
ATOM   2058 O  O   . ALA A 1 269 ? 6.038   17.694  16.315  1.00 13.12 ?  271 ALA A O   1 
ATOM   2059 C  CB  . ALA A 1 269 ? 4.938   17.382  13.516  1.00 14.08 ?  271 ALA A CB  1 
ATOM   2060 N  N   . ALA A 1 270 ? 4.875   19.609  16.200  1.00 15.62 ?  272 ALA A N   1 
ATOM   2061 C  CA  . ALA A 1 270 ? 4.920   19.828  17.642  1.00 20.89 ?  272 ALA A CA  1 
ATOM   2062 C  C   . ALA A 1 270 ? 3.609   19.455  18.328  1.00 13.35 ?  272 ALA A C   1 
ATOM   2063 O  O   . ALA A 1 270 ? 2.527   19.551  17.742  1.00 20.35 ?  272 ALA A O   1 
ATOM   2064 C  CB  . ALA A 1 270 ? 5.259   21.289  17.960  1.00 18.27 ?  272 ALA A CB  1 
ATOM   2065 N  N   . VAL A 1 271 ? 3.729   19.004  19.571  1.00 15.82 ?  273 VAL A N   1 
ATOM   2066 C  CA  . VAL A 1 271 ? 2.594   18.873  20.486  1.00 16.96 ?  273 VAL A CA  1 
ATOM   2067 C  C   . VAL A 1 271 ? 2.893   19.742  21.699  1.00 15.84 ?  273 VAL A C   1 
ATOM   2068 O  O   . VAL A 1 271 ? 4.066   20.014  22.010  1.00 18.08 ?  273 VAL A O   1 
ATOM   2069 C  CB  . VAL A 1 271 ? 2.344   17.404  20.898  1.00 16.93 ?  273 VAL A CB  1 
ATOM   2070 C  CG1 . VAL A 1 271 ? 1.929   16.567  19.704  1.00 22.31 ?  273 VAL A CG1 1 
ATOM   2071 C  CG2 . VAL A 1 271 ? 3.576   16.821  21.621  1.00 16.37 ?  273 VAL A CG2 1 
ATOM   2072 N  N   . PRO A 1 272 ? 1.860   20.199  22.417  1.00 21.43 ?  274 PRO A N   1 
ATOM   2073 C  CA  . PRO A 1 272 ? 2.117   21.057  23.588  1.00 22.81 ?  274 PRO A CA  1 
ATOM   2074 C  C   . PRO A 1 272 ? 2.771   20.331  24.748  1.00 22.96 ?  274 PRO A C   1 
ATOM   2075 O  O   . PRO A 1 272 ? 3.465   20.975  25.548  1.00 24.21 ?  274 PRO A O   1 
ATOM   2076 C  CB  . PRO A 1 272 ? 0.721   21.578  23.962  1.00 22.17 ?  274 PRO A CB  1 
ATOM   2077 C  CG  . PRO A 1 272 ? -0.225  20.576  23.394  1.00 25.60 ?  274 PRO A CG  1 
ATOM   2078 C  CD  . PRO A 1 272 ? 0.422   20.085  22.120  1.00 19.63 ?  274 PRO A CD  1 
ATOM   2079 N  N   . ALA A 1 273 ? 2.607   19.014  24.853  1.00 19.23 ?  275 ALA A N   1 
ATOM   2080 C  CA  . ALA A 1 273 ? 3.150   18.269  25.979  1.00 17.96 ?  275 ALA A CA  1 
ATOM   2081 C  C   . ALA A 1 273 ? 3.261   16.808  25.577  1.00 16.76 ?  275 ALA A C   1 
ATOM   2082 O  O   . ALA A 1 273 ? 2.502   16.353  24.711  1.00 18.37 ?  275 ALA A O   1 
ATOM   2083 C  CB  . ALA A 1 273 ? 2.249   18.413  27.216  1.00 20.98 ?  275 ALA A CB  1 
ATOM   2084 N  N   . PRO A 1 274 ? 4.177   16.050  26.182  1.00 21.88 ?  276 PRO A N   1 
ATOM   2085 C  CA  . PRO A 1 274 ? 4.242   14.614  25.884  1.00 15.81 ?  276 PRO A CA  1 
ATOM   2086 C  C   . PRO A 1 274 ? 2.962   13.912  26.302  1.00 15.28 ?  276 PRO A C   1 
ATOM   2087 O  O   . PRO A 1 274 ? 2.233   14.360  27.193  1.00 16.94 ?  276 PRO A O   1 
ATOM   2088 C  CB  . PRO A 1 274 ? 5.444   14.125  26.702  1.00 16.63 ?  276 PRO A CB  1 
ATOM   2089 C  CG  . PRO A 1 274 ? 5.665   15.158  27.725  1.00 22.16 ?  276 PRO A CG  1 
ATOM   2090 C  CD  . PRO A 1 274 ? 5.206   16.461  27.149  1.00 20.42 ?  276 PRO A CD  1 
ATOM   2091 N  N   . VAL A 1 275 ? 2.685   12.800  25.631  1.00 12.71 ?  277 VAL A N   1 
ATOM   2092 C  CA  . VAL A 1 275 ? 1.420   12.099  25.785  1.00 12.74 ?  277 VAL A CA  1 
ATOM   2093 C  C   . VAL A 1 275 ? 1.687   10.668  26.234  1.00 13.76 ?  277 VAL A C   1 
ATOM   2094 O  O   . VAL A 1 275 ? 2.788   10.133  26.073  1.00 12.95 ?  277 VAL A O   1 
ATOM   2095 C  CB  . VAL A 1 275 ? 0.588   12.128  24.478  1.00 19.12 ?  277 VAL A CB  1 
ATOM   2096 C  CG1 . VAL A 1 275 ? 0.220   13.573  24.132  1.00 21.61 ?  277 VAL A CG1 1 
ATOM   2097 C  CG2 . VAL A 1 275 ? 1.335   11.473  23.321  1.00 16.25 ?  277 VAL A CG2 1 
ATOM   2098 N  N   . ASP A 1 276 ? 0.650   10.036  26.803  1.00 14.18 ?  278 ASP A N   1 
ATOM   2099 C  CA  . ASP A 1 276 ? 0.836   8.678   27.309  1.00 12.90 ?  278 ASP A CA  1 
ATOM   2100 C  C   . ASP A 1 276 ? 0.882   7.635   26.203  1.00 12.83 ?  278 ASP A C   1 
ATOM   2101 O  O   . ASP A 1 276 ? 1.461   6.562   26.401  1.00 15.03 ?  278 ASP A O   1 
ATOM   2102 C  CB  . ASP A 1 276 ? -0.271  8.301   28.292  1.00 17.31 ?  278 ASP A CB  1 
ATOM   2103 C  CG  . ASP A 1 276 ? -0.130  9.000   29.622  1.00 22.77 ?  278 ASP A CG  1 
ATOM   2104 O  OD1 . ASP A 1 276 ? 0.870   8.739   30.322  1.00 31.72 ?  278 ASP A OD1 1 
ATOM   2105 O  OD2 . ASP A 1 276 ? -1.018  9.807   29.962  1.00 31.66 ?  278 ASP A OD2 1 
ATOM   2106 N  N   . VAL A 1 277 ? 0.241   7.897   25.064  1.00 10.80 ?  279 VAL A N   1 
ATOM   2107 C  CA  . VAL A 1 277 ? 0.121   6.915   23.994  1.00 10.90 ?  279 VAL A CA  1 
ATOM   2108 C  C   . VAL A 1 277 ? 0.485   7.595   22.685  1.00 12.60 ?  279 VAL A C   1 
ATOM   2109 O  O   . VAL A 1 277 ? -0.164  8.575   22.295  1.00 12.43 ?  279 VAL A O   1 
ATOM   2110 C  CB  . VAL A 1 277 ? -1.297  6.330   23.922  1.00 14.03 ?  279 VAL A CB  1 
ATOM   2111 C  CG1 . VAL A 1 277 ? -1.386  5.257   22.827  1.00 11.24 ?  279 VAL A CG1 1 
ATOM   2112 C  CG2 . VAL A 1 277 ? -1.728  5.788   25.298  1.00 16.35 ?  279 VAL A CG2 1 
ATOM   2113 N  N   . VAL A 1 278 ? 1.501   7.069   21.998  1.00 10.66 ?  280 VAL A N   1 
ATOM   2114 C  CA  . VAL A 1 278 ? 1.900   7.552   20.677  1.00 10.60 ?  280 VAL A CA  1 
ATOM   2115 C  C   . VAL A 1 278 ? 1.692   6.424   19.685  1.00 11.89 ?  280 VAL A C   1 
ATOM   2116 O  O   . VAL A 1 278 ? 2.264   5.338   19.844  1.00 11.09 ?  280 VAL A O   1 
ATOM   2117 C  CB  . VAL A 1 278 ? 3.366   8.016   20.640  1.00 12.21 ?  280 VAL A CB  1 
ATOM   2118 C  CG1 . VAL A 1 278 ? 3.722   8.477   19.234  1.00 10.25 ?  280 VAL A CG1 1 
ATOM   2119 C  CG2 . VAL A 1 278 ? 3.615   9.114   21.675  1.00 12.13 ?  280 VAL A CG2 1 
ATOM   2120 N  N   . VAL A 1 279 ? 0.881   6.683   18.663  1.00 9.69  ?  281 VAL A N   1 
ATOM   2121 C  CA  . VAL A 1 279 ? 0.650   5.737   17.580  1.00 9.69  ?  281 VAL A CA  1 
ATOM   2122 C  C   . VAL A 1 279 ? 1.540   6.146   16.418  1.00 9.89  ?  281 VAL A C   1 
ATOM   2123 O  O   . VAL A 1 279 ? 1.523   7.310   16.003  1.00 8.41  ?  281 VAL A O   1 
ATOM   2124 C  CB  . VAL A 1 279 ? -0.823  5.735   17.140  1.00 9.70  ?  281 VAL A CB  1 
ATOM   2125 C  CG1 . VAL A 1 279 ? -0.992  4.851   15.896  1.00 10.41 ?  281 VAL A CG1 1 
ATOM   2126 C  CG2 . VAL A 1 279 ? -1.727  5.274   18.277  1.00 10.70 ?  281 VAL A CG2 1 
ATOM   2127 N  N   . THR A 1 280 ? 2.280   5.195   15.856  1.00 7.73  ?  282 THR A N   1 
ATOM   2128 C  CA  . THR A 1 280 ? 3.200   5.557   14.786  1.00 7.81  ?  282 THR A CA  1 
ATOM   2129 C  C   . THR A 1 280 ? 3.336   4.393   13.812  1.00 9.38  ?  282 THR A C   1 
ATOM   2130 O  O   . THR A 1 280 ? 2.680   3.356   13.938  1.00 10.49 ?  282 THR A O   1 
ATOM   2131 C  CB  . THR A 1 280 ? 4.559   5.986   15.367  1.00 9.88  ?  282 THR A CB  1 
ATOM   2132 O  OG1 . THR A 1 280 ? 5.358   6.595   14.337  1.00 11.55 ?  282 THR A OG1 1 
ATOM   2133 C  CG2 . THR A 1 280 ? 5.308   4.799   15.975  1.00 9.60  ?  282 THR A CG2 1 
ATOM   2134 N  N   . SER A 1 281 ? 4.183   4.596   12.815  1.00 10.60 ?  283 SER A N   1 
ATOM   2135 C  CA  . SER A 1 281 ? 4.431   3.651   11.752  1.00 10.17 ?  283 SER A CA  1 
ATOM   2136 C  C   . SER A 1 281 ? 5.938   3.537   11.576  1.00 8.24  ?  283 SER A C   1 
ATOM   2137 O  O   . SER A 1 281 ? 6.722   4.195   12.267  1.00 8.74  ?  283 SER A O   1 
ATOM   2138 C  CB  . SER A 1 281 ? 3.778   4.107   10.444  1.00 8.40  ?  283 SER A CB  1 
ATOM   2139 O  OG  . SER A 1 281 ? 4.509   5.189   9.871   1.00 8.33  ?  283 SER A OG  1 
ATOM   2140 N  N   . SER A 1 282 ? 6.331   2.693   10.628  1.00 7.98  ?  284 SER A N   1 
ATOM   2141 C  CA  . SER A 1 282 ? 7.708   2.621   10.174  1.00 9.64  ?  284 SER A CA  1 
ATOM   2142 C  C   . SER A 1 282 ? 7.849   3.184   8.765   1.00 10.72 ?  284 SER A C   1 
ATOM   2143 O  O   . SER A 1 282 ? 8.733   2.771   8.013   1.00 9.51  ?  284 SER A O   1 
ATOM   2144 C  CB  . SER A 1 282 ? 8.224   1.182   10.260  1.00 8.84  ?  284 SER A CB  1 
ATOM   2145 O  OG  . SER A 1 282 ? 9.535   1.105   9.753   1.00 12.25 ?  284 SER A OG  1 
ATOM   2146 N  N   . ALA A 1 283 ? 6.985   4.145   8.409   1.00 8.25  ?  285 ALA A N   1 
ATOM   2147 C  CA  . ALA A 1 283 ? 7.039   4.885   7.148   1.00 8.79  ?  285 ALA A CA  1 
ATOM   2148 C  C   . ALA A 1 283 ? 6.741   4.020   5.927   1.00 8.93  ?  285 ALA A C   1 
ATOM   2149 O  O   . ALA A 1 283 ? 7.060   4.412   4.800   1.00 10.02 ?  285 ALA A O   1 
ATOM   2150 C  CB  . ALA A 1 283 ? 8.392   5.587   6.969   1.00 9.34  ?  285 ALA A CB  1 
ATOM   2151 N  N   . GLY A 1 284 ? 6.109   2.866   6.114   1.00 8.19  ?  286 GLY A N   1 
ATOM   2152 C  CA  . GLY A 1 284 ? 5.661   2.088   4.973   1.00 9.25  ?  286 GLY A CA  1 
ATOM   2153 C  C   . GLY A 1 284 ? 6.802   1.461   4.179   1.00 8.75  ?  286 GLY A C   1 
ATOM   2154 O  O   . GLY A 1 284 ? 7.971   1.468   4.576   1.00 8.03  ?  286 GLY A O   1 
ATOM   2155 N  N   . HIS A 1 285 ? 6.417   0.882   3.035   1.00 7.61  ?  287 HIS A N   1 
ATOM   2156 C  CA  . HIS A 1 285 ? 7.393   0.354   2.088   1.00 9.59  ?  287 HIS A CA  1 
ATOM   2157 C  C   . HIS A 1 285 ? 8.201   1.506   1.491   1.00 7.89  ?  287 HIS A C   1 
ATOM   2158 O  O   . HIS A 1 285 ? 7.621   2.519   1.098   1.00 10.68 ?  287 HIS A O   1 
ATOM   2159 C  CB  . HIS A 1 285 ? 6.679   -0.407  0.966   1.00 9.08  ?  287 HIS A CB  1 
ATOM   2160 C  CG  . HIS A 1 285 ? 7.613   -1.059  0.001   1.00 11.67 ?  287 HIS A CG  1 
ATOM   2161 N  ND1 . HIS A 1 285 ? 8.086   -2.340  0.187   1.00 12.36 ?  287 HIS A ND1 1 
ATOM   2162 C  CD2 . HIS A 1 285 ? 8.199   -0.597  -1.128  1.00 11.10 ?  287 HIS A CD2 1 
ATOM   2163 C  CE1 . HIS A 1 285 ? 8.904   -2.649  -0.803  1.00 14.39 ?  287 HIS A CE1 1 
ATOM   2164 N  NE2 . HIS A 1 285 ? 8.998   -1.607  -1.608  1.00 13.22 ?  287 HIS A NE2 1 
ATOM   2165 N  N   . PRO A 1 286 ? 9.535   1.374   1.371   1.00 7.92  ?  288 PRO A N   1 
ATOM   2166 C  CA  . PRO A 1 286 ? 10.358  0.198   1.633   1.00 8.76  ?  288 PRO A CA  1 
ATOM   2167 C  C   . PRO A 1 286 ? 10.985  0.144   3.015   1.00 10.32 ?  288 PRO A C   1 
ATOM   2168 O  O   . PRO A 1 286 ? 11.570  -0.879  3.337   1.00 10.61 ?  288 PRO A O   1 
ATOM   2169 C  CB  . PRO A 1 286 ? 11.455  0.320   0.566   1.00 9.76  ?  288 PRO A CB  1 
ATOM   2170 C  CG  . PRO A 1 286 ? 11.701  1.808   0.501   1.00 7.70  ?  288 PRO A CG  1 
ATOM   2171 C  CD  . PRO A 1 286 ? 10.321  2.444   0.720   1.00 8.72  ?  288 PRO A CD  1 
ATOM   2172 N  N   . LEU A 1 287 ? 10.902  1.214   3.815   1.00 8.54  ?  289 LEU A N   1 
ATOM   2173 C  CA  . LEU A 1 287 ? 11.595  1.188   5.104   1.00 7.46  ?  289 LEU A CA  1 
ATOM   2174 C  C   . LEU A 1 287 ? 11.084  0.066   6.003   1.00 7.84  ?  289 LEU A C   1 
ATOM   2175 O  O   . LEU A 1 287 ? 11.874  -0.557  6.714   1.00 9.20  ?  289 LEU A O   1 
ATOM   2176 C  CB  . LEU A 1 287 ? 11.464  2.536   5.818   1.00 7.58  ?  289 LEU A CB  1 
ATOM   2177 C  CG  . LEU A 1 287 ? 12.283  2.661   7.109   1.00 6.28  ?  289 LEU A CG  1 
ATOM   2178 C  CD1 . LEU A 1 287 ? 13.773  2.395   6.861   1.00 7.43  ?  289 LEU A CD1 1 
ATOM   2179 C  CD2 . LEU A 1 287 ? 12.071  4.034   7.749   1.00 8.81  ?  289 LEU A CD2 1 
ATOM   2180 N  N   . ASP A 1 288 ? 9.781   -0.223  5.984   1.00 7.51  ?  290 ASP A N   1 
ATOM   2181 C  CA  . ASP A 1 288 ? 9.227   -1.113  7.005   1.00 7.41  ?  290 ASP A CA  1 
ATOM   2182 C  C   . ASP A 1 288 ? 9.322   -2.590  6.617   1.00 9.03  ?  290 ASP A C   1 
ATOM   2183 O  O   . ASP A 1 288 ? 8.602   -3.420  7.187   1.00 7.20  ?  290 ASP A O   1 
ATOM   2184 C  CB  . ASP A 1 288 ? 7.778   -0.701  7.396   1.00 5.67  ?  290 ASP A CB  1 
ATOM   2185 C  CG  . ASP A 1 288 ? 6.682   -1.144  6.417   1.00 8.47  ?  290 ASP A CG  1 
ATOM   2186 O  OD1 . ASP A 1 288 ? 6.950   -1.607  5.293   1.00 8.37  ?  290 ASP A OD1 1 
ATOM   2187 O  OD2 . ASP A 1 288 ? 5.493   -1.009  6.821   1.00 9.80  ?  290 ASP A OD2 1 
ATOM   2188 N  N   . LEU A 1 289 ? 10.256  -2.937  5.724   1.00 9.64  ?  291 LEU A N   1 
ATOM   2189 C  CA  . LEU A 1 289 ? 10.442  -4.330  5.323   1.00 9.05  ?  291 LEU A CA  1 
ATOM   2190 C  C   . LEU A 1 289 ? 10.863  -5.229  6.484   1.00 11.59 ?  291 LEU A C   1 
ATOM   2191 O  O   . LEU A 1 289 ? 10.542  -6.424  6.478   1.00 10.68 ?  291 LEU A O   1 
ATOM   2192 C  CB  . LEU A 1 289 ? 11.494  -4.405  4.214   1.00 9.25  ?  291 LEU A CB  1 
ATOM   2193 C  CG  . LEU A 1 289 ? 11.056  -4.017  2.790   1.00 9.63  ?  291 LEU A CG  1 
ATOM   2194 C  CD1 . LEU A 1 289 ? 12.300  -3.931  1.897   1.00 12.99 ?  291 LEU A CD1 1 
ATOM   2195 C  CD2 . LEU A 1 289 ? 10.034  -4.990  2.212   1.00 15.12 ?  291 LEU A CD2 1 
ATOM   2196 N  N   . THR A 1 290 ? 11.627  -4.709  7.463   1.00 8.76  ?  292 THR A N   1 
ATOM   2197 C  CA  . THR A 1 290 ? 12.140  -5.560  8.532   1.00 9.19  ?  292 THR A CA  1 
ATOM   2198 C  C   . THR A 1 290 ? 11.949  -4.894  9.885   1.00 8.44  ?  292 THR A C   1 
ATOM   2199 O  O   . THR A 1 290 ? 11.920  -3.663  9.996   1.00 8.26  ?  292 THR A O   1 
ATOM   2200 C  CB  . THR A 1 290 ? 13.629  -5.875  8.367   1.00 10.49 ?  292 THR A CB  1 
ATOM   2201 O  OG1 . THR A 1 290 ? 14.374  -4.644  8.323   1.00 9.92  ?  292 THR A OG1 1 
ATOM   2202 C  CG2 . THR A 1 290 ? 13.857  -6.681  7.095   1.00 8.16  ?  292 THR A CG2 1 
ATOM   2203 N  N   . PHE A 1 291 ? 11.845  -5.735  10.918  1.00 7.75  ?  293 PHE A N   1 
ATOM   2204 C  CA  . PHE A 1 291 ? 11.802  -5.244  12.292  1.00 8.76  ?  293 PHE A CA  1 
ATOM   2205 C  C   . PHE A 1 291 ? 13.048  -4.421  12.607  1.00 9.00  ?  293 PHE A C   1 
ATOM   2206 O  O   . PHE A 1 291 ? 12.971  -3.383  13.277  1.00 8.35  ?  293 PHE A O   1 
ATOM   2207 C  CB  . PHE A 1 291 ? 11.667  -6.440  13.247  1.00 8.44  ?  293 PHE A CB  1 
ATOM   2208 C  CG  . PHE A 1 291 ? 11.600  -6.071  14.701  1.00 9.38  ?  293 PHE A CG  1 
ATOM   2209 C  CD1 . PHE A 1 291 ? 10.390  -5.751  15.300  1.00 11.86 ?  293 PHE A CD1 1 
ATOM   2210 C  CD2 . PHE A 1 291 ? 12.751  -6.055  15.478  1.00 11.16 ?  293 PHE A CD2 1 
ATOM   2211 C  CE1 . PHE A 1 291 ? 10.323  -5.427  16.646  1.00 11.93 ?  293 PHE A CE1 1 
ATOM   2212 C  CE2 . PHE A 1 291 ? 12.694  -5.707  16.813  1.00 12.86 ?  293 PHE A CE2 1 
ATOM   2213 C  CZ  . PHE A 1 291 ? 11.491  -5.399  17.403  1.00 10.92 ?  293 PHE A CZ  1 
ATOM   2214 N  N   . TYR A 1 292 ? 14.201  -4.865  12.104  1.00 8.20  ?  294 TYR A N   1 
ATOM   2215 C  CA  . TYR A 1 292 ? 15.455  -4.124  12.249  1.00 9.06  ?  294 TYR A CA  1 
ATOM   2216 C  C   . TYR A 1 292 ? 15.275  -2.645  11.903  1.00 8.85  ?  294 TYR A C   1 
ATOM   2217 O  O   . TYR A 1 292 ? 15.673  -1.760  12.673  1.00 10.47 ?  294 TYR A O   1 
ATOM   2218 C  CB  . TYR A 1 292 ? 16.509  -4.791  11.361  1.00 9.85  ?  294 TYR A CB  1 
ATOM   2219 C  CG  . TYR A 1 292 ? 17.814  -4.052  11.193  1.00 8.41  ?  294 TYR A CG  1 
ATOM   2220 C  CD1 . TYR A 1 292 ? 18.828  -4.156  12.139  1.00 9.16  ?  294 TYR A CD1 1 
ATOM   2221 C  CD2 . TYR A 1 292 ? 18.059  -3.310  10.043  1.00 10.09 ?  294 TYR A CD2 1 
ATOM   2222 C  CE1 . TYR A 1 292 ? 20.038  -3.499  11.968  1.00 10.97 ?  294 TYR A CE1 1 
ATOM   2223 C  CE2 . TYR A 1 292 ? 19.267  -2.637  9.862   1.00 9.03  ?  294 TYR A CE2 1 
ATOM   2224 C  CZ  . TYR A 1 292 ? 20.253  -2.739  10.827  1.00 10.23 ?  294 TYR A CZ  1 
ATOM   2225 O  OH  . TYR A 1 292 ? 21.462  -2.082  10.655  1.00 11.35 ?  294 TYR A OH  1 
ATOM   2226 N  N   . GLN A 1 293 ? 14.635  -2.351  10.763  1.00 6.88  ?  295 GLN A N   1 
ATOM   2227 C  CA  . GLN A 1 293 ? 14.434  -0.947  10.391  1.00 7.68  ?  295 GLN A CA  1 
ATOM   2228 C  C   . GLN A 1 293 ? 13.288  -0.302  11.157  1.00 9.40  ?  295 GLN A C   1 
ATOM   2229 O  O   . GLN A 1 293 ? 13.345  0.901   11.451  1.00 9.71  ?  295 GLN A O   1 
ATOM   2230 C  CB  . GLN A 1 293 ? 14.154  -0.822  8.887   1.00 8.26  ?  295 GLN A CB  1 
ATOM   2231 C  CG  . GLN A 1 293 ? 15.324  -1.212  8.021   1.00 10.23 ?  295 GLN A CG  1 
ATOM   2232 C  CD  . GLN A 1 293 ? 16.434  -0.163  8.032   1.00 9.69  ?  295 GLN A CD  1 
ATOM   2233 O  OE1 . GLN A 1 293 ? 16.261  0.940   8.553   1.00 10.07 ?  295 GLN A OE1 1 
ATOM   2234 N  NE2 . GLN A 1 293 ? 17.603  -0.535  7.507   1.00 8.80  ?  295 GLN A NE2 1 
ATOM   2235 N  N   . ALA A 1 294 ? 12.242  -1.072  11.464  1.00 7.35  ?  296 ALA A N   1 
ATOM   2236 C  CA  . ALA A 1 294 ? 11.058  -0.523  12.109  1.00 8.85  ?  296 ALA A CA  1 
ATOM   2237 C  C   . ALA A 1 294 ? 11.334  0.005   13.514  1.00 8.42  ?  296 ALA A C   1 
ATOM   2238 O  O   . ALA A 1 294 ? 10.542  0.808   14.017  1.00 10.98 ?  296 ALA A O   1 
ATOM   2239 C  CB  . ALA A 1 294 ? 9.951   -1.587  12.146  1.00 10.23 ?  296 ALA A CB  1 
ATOM   2240 N  N   . VAL A 1 295 ? 12.439  -0.404  14.146  1.00 7.97  ?  297 VAL A N   1 
ATOM   2241 C  CA  . VAL A 1 295 ? 12.830  0.206   15.418  1.00 7.90  ?  297 VAL A CA  1 
ATOM   2242 C  C   . VAL A 1 295 ? 12.950  1.727   15.263  1.00 8.20  ?  297 VAL A C   1 
ATOM   2243 O  O   . VAL A 1 295 ? 12.749  2.476   16.225  1.00 8.04  ?  297 VAL A O   1 
ATOM   2244 C  CB  . VAL A 1 295 ? 14.151  -0.432  15.911  1.00 7.49  ?  297 VAL A CB  1 
ATOM   2245 C  CG1 . VAL A 1 295 ? 14.774  0.388   17.051  1.00 9.85  ?  297 VAL A CG1 1 
ATOM   2246 C  CG2 . VAL A 1 295 ? 13.893  -1.882  16.339  1.00 11.30 ?  297 VAL A CG2 1 
ATOM   2247 N  N   . LYS A 1 296 ? 13.213  2.205   14.041  1.00 9.41  ?  298 LYS A N   1 
ATOM   2248 C  CA  . LYS A 1 296 ? 13.274  3.649   13.785  1.00 9.69  ?  298 LYS A CA  1 
ATOM   2249 C  C   . LYS A 1 296 ? 11.963  4.362   14.112  1.00 10.94 ?  298 LYS A C   1 
ATOM   2250 O  O   . LYS A 1 296 ? 11.978  5.531   14.511  1.00 8.34  ?  298 LYS A O   1 
ATOM   2251 C  CB  . LYS A 1 296 ? 13.623  3.915   12.321  1.00 7.22  ?  298 LYS A CB  1 
ATOM   2252 C  CG  . LYS A 1 296 ? 15.071  3.581   11.952  1.00 6.87  ?  298 LYS A CG  1 
ATOM   2253 C  CD  . LYS A 1 296 ? 15.275  3.690   10.427  1.00 7.35  ?  298 LYS A CD  1 
ATOM   2254 C  CE  . LYS A 1 296 ? 16.758  3.906   10.093  1.00 9.69  ?  298 LYS A CE  1 
ATOM   2255 N  NZ  . LYS A 1 296 ? 17.003  3.630   8.638   1.00 9.17  ?  298 LYS A NZ  1 
ATOM   2256 N  N   . GLY A 1 297 ? 10.817  3.714   13.856  1.00 6.40  ?  299 GLY A N   1 
ATOM   2257 C  CA  . GLY A 1 297 ? 9.543   4.306   14.263  1.00 7.66  ?  299 GLY A CA  1 
ATOM   2258 C  C   . GLY A 1 297 ? 9.451   4.458   15.768  1.00 8.75  ?  299 GLY A C   1 
ATOM   2259 O  O   . GLY A 1 297 ? 8.898   5.441   16.279  1.00 9.06  ?  299 GLY A O   1 
ATOM   2260 N  N   . LEU A 1 298 ? 10.020  3.493   16.500  1.00 10.74 ?  300 LEU A N   1 
ATOM   2261 C  CA  . LEU A 1 298 ? 10.011  3.558   17.958  1.00 8.53  ?  300 LEU A CA  1 
ATOM   2262 C  C   . LEU A 1 298 ? 10.905  4.676   18.470  1.00 10.93 ?  300 LEU A C   1 
ATOM   2263 O  O   . LEU A 1 298 ? 10.500  5.444   19.346  1.00 9.95  ?  300 LEU A O   1 
ATOM   2264 C  CB  . LEU A 1 298 ? 10.439  2.216   18.547  1.00 9.31  ?  300 LEU A CB  1 
ATOM   2265 C  CG  . LEU A 1 298 ? 9.564   1.056   18.095  1.00 6.95  ?  300 LEU A CG  1 
ATOM   2266 C  CD1 . LEU A 1 298 ? 10.110  -0.270  18.634  1.00 8.18  ?  300 LEU A CD1 1 
ATOM   2267 C  CD2 . LEU A 1 298 ? 8.109   1.244   18.534  1.00 10.23 ?  300 LEU A CD2 1 
ATOM   2268 N  N   . THR A 1 299 ? 12.148  4.760   17.975  1.00 8.76  ?  301 THR A N   1 
ATOM   2269 C  CA  . THR A 1 299 ? 12.996  5.848   18.455  1.00 9.68  ?  301 THR A CA  1 
ATOM   2270 C  C   . THR A 1 299 ? 12.446  7.200   18.025  1.00 9.36  ?  301 THR A C   1 
ATOM   2271 O  O   . THR A 1 299 ? 12.597  8.191   18.755  1.00 11.02 ?  301 THR A O   1 
ATOM   2272 C  CB  . THR A 1 299 ? 14.442  5.689   17.962  1.00 10.93 ?  301 THR A CB  1 
ATOM   2273 O  OG1 . THR A 1 299 ? 14.471  5.563   16.532  1.00 12.67 ?  301 THR A OG1 1 
ATOM   2274 C  CG2 . THR A 1 299 ? 15.085  4.459   18.592  1.00 11.95 ?  301 THR A CG2 1 
ATOM   2275 N  N   . GLY A 1 300 ? 11.817  7.269   16.850  1.00 11.61 ?  302 GLY A N   1 
ATOM   2276 C  CA  . GLY A 1 300 ? 11.287  8.541   16.383  1.00 9.65  ?  302 GLY A CA  1 
ATOM   2277 C  C   . GLY A 1 300 ? 10.198  9.089   17.283  1.00 11.88 ?  302 GLY A C   1 
ATOM   2278 O  O   . GLY A 1 300 ? 10.032  10.308  17.398  1.00 13.22 ?  302 GLY A O   1 
ATOM   2279 N  N   . ALA A 1 301 ? 9.453   8.205   17.943  1.00 10.62 ?  303 ALA A N   1 
ATOM   2280 C  CA  . ALA A 1 301 ? 8.342   8.632   18.791  1.00 11.25 ?  303 ALA A CA  1 
ATOM   2281 C  C   . ALA A 1 301 ? 8.788   9.081   20.175  1.00 13.17 ?  303 ALA A C   1 
ATOM   2282 O  O   . ALA A 1 301 ? 8.013   9.754   20.871  1.00 13.43 ?  303 ALA A O   1 
ATOM   2283 C  CB  . ALA A 1 301 ? 7.333   7.489   18.938  1.00 13.86 ?  303 ALA A CB  1 
ATOM   2284 N  N   . LEU A 1 302 ? 9.997   8.710   20.599  1.00 11.14 ?  304 LEU A N   1 
ATOM   2285 C  CA  . LEU A 1 302 ? 10.420  8.962   21.978  1.00 11.30 ?  304 LEU A CA  1 
ATOM   2286 C  C   . LEU A 1 302 ? 10.292  10.408  22.455  1.00 13.20 ?  304 LEU A C   1 
ATOM   2287 O  O   . LEU A 1 302 ? 9.924   10.604  23.629  1.00 12.84 ?  304 LEU A O   1 
ATOM   2288 C  CB  . LEU A 1 302 ? 11.871  8.495   22.174  1.00 13.17 ?  304 LEU A CB  1 
ATOM   2289 C  CG  . LEU A 1 302 ? 12.102  6.987   22.261  1.00 14.93 ?  304 LEU A CG  1 
ATOM   2290 C  CD1 . LEU A 1 302 ? 13.613  6.704   22.398  1.00 12.24 ?  304 LEU A CD1 1 
ATOM   2291 C  CD2 . LEU A 1 302 ? 11.342  6.365   23.428  1.00 13.75 ?  304 LEU A CD2 1 
ATOM   2292 N  N   . PRO A 1 303 ? 10.591  11.441  21.658  1.00 13.16 ?  305 PRO A N   1 
ATOM   2293 C  CA  . PRO A 1 303 ? 10.525  12.811  22.199  1.00 15.09 ?  305 PRO A CA  1 
ATOM   2294 C  C   . PRO A 1 303 ? 9.163   13.224  22.724  1.00 15.26 ?  305 PRO A C   1 
ATOM   2295 O  O   . PRO A 1 303 ? 9.097   14.121  23.576  1.00 16.04 ?  305 PRO A O   1 
ATOM   2296 C  CB  . PRO A 1 303 ? 10.927  13.674  20.997  1.00 14.86 ?  305 PRO A CB  1 
ATOM   2297 C  CG  . PRO A 1 303 ? 11.818  12.780  20.198  1.00 16.11 ?  305 PRO A CG  1 
ATOM   2298 C  CD  . PRO A 1 303 ? 11.181  11.435  20.299  1.00 14.21 ?  305 PRO A CD  1 
ATOM   2299 N  N   . ILE A 1 304 ? 8.072   12.616  22.251  1.00 11.46 ?  306 ILE A N   1 
ATOM   2300 C  CA  . ILE A 1 304 ? 6.740   13.075  22.629  1.00 13.29 ?  306 ILE A CA  1 
ATOM   2301 C  C   . ILE A 1 304 ? 5.973   12.047  23.461  1.00 13.77 ?  306 ILE A C   1 
ATOM   2302 O  O   . ILE A 1 304 ? 4.793   12.262  23.755  1.00 14.82 ?  306 ILE A O   1 
ATOM   2303 C  CB  . ILE A 1 304 ? 5.915   13.506  21.405  1.00 12.60 ?  306 ILE A CB  1 
ATOM   2304 C  CG1 . ILE A 1 304 ? 5.640   12.326  20.457  1.00 12.43 ?  306 ILE A CG1 1 
ATOM   2305 C  CG2 . ILE A 1 304 ? 6.587   14.680  20.672  1.00 11.46 ?  306 ILE A CG2 1 
ATOM   2306 C  CD1 . ILE A 1 304 ? 4.379   12.516  19.622  1.00 12.35 ?  306 ILE A CD1 1 
ATOM   2307 N  N   . VAL A 1 305 ? 6.598   10.935  23.861  1.00 11.16 ?  307 VAL A N   1 
ATOM   2308 C  CA  . VAL A 1 305 ? 5.941   10.007  24.782  1.00 12.54 ?  307 VAL A CA  1 
ATOM   2309 C  C   . VAL A 1 305 ? 6.379   10.317  26.209  1.00 10.30 ?  307 VAL A C   1 
ATOM   2310 O  O   . VAL A 1 305 ? 7.541   10.650  26.461  1.00 11.99 ?  307 VAL A O   1 
ATOM   2311 C  CB  . VAL A 1 305 ? 6.218   8.533   24.417  1.00 12.29 ?  307 VAL A CB  1 
ATOM   2312 C  CG1 . VAL A 1 305 ? 7.670   8.148   24.690  1.00 14.62 ?  307 VAL A CG1 1 
ATOM   2313 C  CG2 . VAL A 1 305 ? 5.241   7.597   25.157  1.00 13.62 ?  307 VAL A CG2 1 
ATOM   2314 N  N   . LYS A 1 306 ? 5.437   10.227  27.143  1.00 15.20 ?  308 LYS A N   1 
ATOM   2315 C  CA  . LYS A 1 306 ? 5.781   10.393  28.547  1.00 16.45 ?  308 LYS A CA  1 
ATOM   2316 C  C   . LYS A 1 306 ? 6.583   9.180   29.016  1.00 14.92 ?  308 LYS A C   1 
ATOM   2317 O  O   . LYS A 1 306 ? 6.347   8.059   28.554  1.00 15.24 ?  308 LYS A O   1 
ATOM   2318 C  CB  . LYS A 1 306 ? 4.516   10.536  29.392  1.00 16.28 ?  308 LYS A CB  1 
ATOM   2319 C  CG  . LYS A 1 306 ? 3.759   11.830  29.159  1.00 17.28 ?  308 LYS A CG  1 
ATOM   2320 C  CD  . LYS A 1 306 ? 2.333   11.769  29.732  1.00 23.48 ?  308 LYS A CD  1 
ATOM   2321 C  CE  . LYS A 1 306 ? 2.315   11.450  31.220  1.00 26.17 ?  308 LYS A CE  1 
ATOM   2322 N  NZ  . LYS A 1 306 ? 0.917   11.584  31.773  1.00 25.73 ?  308 LYS A NZ  1 
ATOM   2323 N  N   . PRO A 1 307 ? 7.541   9.375   29.920  1.00 13.35 ?  309 PRO A N   1 
ATOM   2324 C  CA  . PRO A 1 307 ? 8.202   8.222   30.540  1.00 15.53 ?  309 PRO A CA  1 
ATOM   2325 C  C   . PRO A 1 307 ? 7.168   7.262   31.116  1.00 16.92 ?  309 PRO A C   1 
ATOM   2326 O  O   . PRO A 1 307 ? 6.216   7.671   31.801  1.00 15.38 ?  309 PRO A O   1 
ATOM   2327 C  CB  . PRO A 1 307 ? 9.069   8.862   31.631  1.00 16.46 ?  309 PRO A CB  1 
ATOM   2328 C  CG  . PRO A 1 307 ? 9.388   10.222  31.073  1.00 16.53 ?  309 PRO A CG  1 
ATOM   2329 C  CD  . PRO A 1 307 ? 8.085   10.651  30.422  1.00 17.99 ?  309 PRO A CD  1 
ATOM   2330 N  N   . GLY A 1 308 ? 7.339   5.976   30.810  1.00 12.65 ?  310 GLY A N   1 
ATOM   2331 C  CA  . GLY A 1 308 ? 6.370   4.965   31.167  1.00 11.83 ?  310 GLY A CA  1 
ATOM   2332 C  C   . GLY A 1 308 ? 5.158   4.886   30.258  1.00 14.87 ?  310 GLY A C   1 
ATOM   2333 O  O   . GLY A 1 308 ? 4.277   4.043   30.500  1.00 16.77 ?  310 GLY A O   1 
ATOM   2334 N  N   . GLY A 1 309 ? 5.070   5.748   29.246  1.00 12.08 ?  311 GLY A N   1 
ATOM   2335 C  CA  . GLY A 1 309 ? 4.014   5.684   28.250  1.00 12.32 ?  311 GLY A CA  1 
ATOM   2336 C  C   . GLY A 1 309 ? 4.176   4.494   27.316  1.00 11.70 ?  311 GLY A C   1 
ATOM   2337 O  O   . GLY A 1 309 ? 5.030   3.625   27.494  1.00 13.95 ?  311 GLY A O   1 
ATOM   2338 N  N   . THR A 1 310 ? 3.297   4.440   26.312  1.00 11.21 ?  312 THR A N   1 
ATOM   2339 C  CA  . THR A 1 310 ? 3.271   3.328   25.370  1.00 11.70 ?  312 THR A CA  1 
ATOM   2340 C  C   . THR A 1 310 ? 3.337   3.868   23.947  1.00 11.46 ?  312 THR A C   1 
ATOM   2341 O  O   . THR A 1 310 ? 2.607   4.801   23.598  1.00 12.24 ?  312 THR A O   1 
ATOM   2342 C  CB  . THR A 1 310 ? 2.007   2.477   25.554  1.00 12.50 ?  312 THR A CB  1 
ATOM   2343 O  OG1 . THR A 1 310 ? 2.044   1.835   26.837  1.00 14.30 ?  312 THR A OG1 1 
ATOM   2344 C  CG2 . THR A 1 310 ? 1.875   1.410   24.436  1.00 10.67 ?  312 THR A CG2 1 
ATOM   2345 N  N   . ILE A 1 311 ? 4.242   3.305   23.150  1.00 8.34  ?  313 ILE A N   1 
ATOM   2346 C  CA  . ILE A 1 311 ? 4.286   3.527   21.712  1.00 8.69  ?  313 ILE A CA  1 
ATOM   2347 C  C   . ILE A 1 311 ? 3.609   2.348   21.041  1.00 10.58 ?  313 ILE A C   1 
ATOM   2348 O  O   . ILE A 1 311 ? 3.971   1.190   21.294  1.00 9.46  ?  313 ILE A O   1 
ATOM   2349 C  CB  . ILE A 1 311 ? 5.736   3.671   21.224  1.00 7.65  ?  313 ILE A CB  1 
ATOM   2350 C  CG1 . ILE A 1 311 ? 6.387   4.866   21.912  1.00 11.96 ?  313 ILE A CG1 1 
ATOM   2351 C  CG2 . ILE A 1 311 ? 5.754   3.873   19.694  1.00 9.83  ?  313 ILE A CG2 1 
ATOM   2352 C  CD1 . ILE A 1 311 ? 7.921   4.870   21.772  1.00 11.80 ?  313 ILE A CD1 1 
ATOM   2353 N  N   . VAL A 1 312 ? 2.624   2.642   20.195  1.00 9.48  ?  314 VAL A N   1 
ATOM   2354 C  CA  . VAL A 1 312 ? 1.925   1.653   19.382  1.00 6.34  ?  314 VAL A CA  1 
ATOM   2355 C  C   . VAL A 1 312 ? 2.435   1.849   17.958  1.00 9.42  ?  314 VAL A C   1 
ATOM   2356 O  O   . VAL A 1 312 ? 2.248   2.924   17.380  1.00 11.36 ?  314 VAL A O   1 
ATOM   2357 C  CB  . VAL A 1 312 ? 0.397   1.847   19.457  1.00 8.16  ?  314 VAL A CB  1 
ATOM   2358 C  CG1 . VAL A 1 312 ? -0.335  0.822   18.581  1.00 10.88 ?  314 VAL A CG1 1 
ATOM   2359 C  CG2 . VAL A 1 312 ? -0.090  1.754   20.913  1.00 8.31  ?  314 VAL A CG2 1 
ATOM   2360 N  N   . ILE A 1 313 ? 3.097   0.841   17.390  1.00 8.21  ?  315 ILE A N   1 
ATOM   2361 C  CA  . ILE A 1 313 ? 3.630   0.975   16.037  1.00 7.60  ?  315 ILE A CA  1 
ATOM   2362 C  C   . ILE A 1 313 ? 2.963   -0.046  15.138  1.00 7.54  ?  315 ILE A C   1 
ATOM   2363 O  O   . ILE A 1 313 ? 2.732   -1.190  15.543  1.00 11.02 ?  315 ILE A O   1 
ATOM   2364 C  CB  . ILE A 1 313 ? 5.163   0.809   16.008  1.00 8.63  ?  315 ILE A CB  1 
ATOM   2365 C  CG1 . ILE A 1 313 ? 5.704   1.049   14.591  1.00 7.99  ?  315 ILE A CG1 1 
ATOM   2366 C  CG2 . ILE A 1 313 ? 5.553   -0.569  16.533  1.00 8.05  ?  315 ILE A CG2 1 
ATOM   2367 C  CD1 . ILE A 1 313 ? 7.272   1.217   14.551  1.00 8.90  ?  315 ILE A CD1 1 
ATOM   2368 N  N   . ALA A 1 314 ? 2.636   0.377   13.920  1.00 6.99  ?  316 ALA A N   1 
ATOM   2369 C  CA  . ALA A 1 314 ? 2.190   -0.531  12.870  1.00 6.54  ?  316 ALA A CA  1 
ATOM   2370 C  C   . ALA A 1 314 ? 3.277   -0.579  11.808  1.00 8.28  ?  316 ALA A C   1 
ATOM   2371 O  O   . ALA A 1 314 ? 3.778   0.468   11.386  1.00 10.21 ?  316 ALA A O   1 
ATOM   2372 C  CB  . ALA A 1 314 ? 0.864   -0.069  12.253  1.00 10.02 ?  316 ALA A CB  1 
ATOM   2373 N  N   . ALA A 1 315 ? 3.658   -1.786  11.394  1.00 8.06  ?  317 ALA A N   1 
ATOM   2374 C  CA  . ALA A 1 315 ? 4.665   -1.939  10.351  1.00 7.46  ?  317 ALA A CA  1 
ATOM   2375 C  C   . ALA A 1 315 ? 4.441   -3.274  9.655   1.00 9.40  ?  317 ALA A C   1 
ATOM   2376 O  O   . ALA A 1 315 ? 4.164   -4.276  10.312  1.00 10.43 ?  317 ALA A O   1 
ATOM   2377 C  CB  . ALA A 1 315 ? 6.091   -1.872  10.919  1.00 10.93 ?  317 ALA A CB  1 
ATOM   2378 N  N   . ALA A 1 316 ? 4.574   -3.288  8.329   1.00 8.57  ?  318 ALA A N   1 
ATOM   2379 C  CA  . ALA A 1 316 ? 4.203   -4.491  7.589   1.00 8.46  ?  318 ALA A CA  1 
ATOM   2380 C  C   . ALA A 1 316 ? 5.228   -5.616  7.758   1.00 11.32 ?  318 ALA A C   1 
ATOM   2381 O  O   . ALA A 1 316 ? 4.842   -6.790  7.760   1.00 11.12 ?  318 ALA A O   1 
ATOM   2382 C  CB  . ALA A 1 316 ? 3.999   -4.159  6.106   1.00 10.59 ?  318 ALA A CB  1 
ATOM   2383 N  N   . LEU A 1 317 ? 6.524   -5.290  7.875   1.00 9.68  ?  319 LEU A N   1 
ATOM   2384 C  CA  . LEU A 1 317 ? 7.583   -6.294  8.080   1.00 8.34  ?  319 LEU A CA  1 
ATOM   2385 C  C   . LEU A 1 317 ? 7.497   -7.411  7.032   1.00 9.94  ?  319 LEU A C   1 
ATOM   2386 O  O   . LEU A 1 317 ? 7.596   -8.599  7.344   1.00 13.17 ?  319 LEU A O   1 
ATOM   2387 C  CB  . LEU A 1 317 ? 7.511   -6.876  9.498   1.00 9.82  ?  319 LEU A CB  1 
ATOM   2388 C  CG  . LEU A 1 317 ? 7.446   -5.922  10.694  1.00 11.09 ?  319 LEU A CG  1 
ATOM   2389 C  CD1 . LEU A 1 317 ? 7.536   -6.674  12.024  1.00 11.20 ?  319 LEU A CD1 1 
ATOM   2390 C  CD2 . LEU A 1 317 ? 8.548   -4.854  10.610  1.00 10.46 ?  319 LEU A CD2 1 
ATOM   2391 N  N   . ALA A 1 318 ? 7.319   -7.023  5.763   1.00 9.46  ?  320 ALA A N   1 
ATOM   2392 C  CA  . ALA A 1 318 ? 7.093   -8.048  4.741   1.00 9.88  ?  320 ALA A CA  1 
ATOM   2393 C  C   . ALA A 1 318 ? 8.293   -8.985  4.590   1.00 13.44 ?  320 ALA A C   1 
ATOM   2394 O  O   . ALA A 1 318 ? 8.127   -10.142 4.183   1.00 14.99 ?  320 ALA A O   1 
ATOM   2395 C  CB  . ALA A 1 318 ? 6.742   -7.395  3.404   1.00 12.22 ?  320 ALA A CB  1 
ATOM   2396 N  N   . GLU A 1 319 ? 9.496   -8.527  4.934   1.00 9.75  ?  321 GLU A N   1 
ATOM   2397 C  CA  . GLU A 1 319 ? 10.685  -9.360  4.840   1.00 12.06 ?  321 GLU A CA  1 
ATOM   2398 C  C   . GLU A 1 319 ? 11.065  -10.003 6.182   1.00 11.77 ?  321 GLU A C   1 
ATOM   2399 O  O   . GLU A 1 319 ? 12.001  -10.804 6.236   1.00 17.53 ?  321 GLU A O   1 
ATOM   2400 C  CB  . GLU A 1 319 ? 11.854  -8.531  4.271   1.00 12.44 ?  321 GLU A CB  1 
ATOM   2401 C  CG  . GLU A 1 319 ? 13.134  -9.308  4.068   1.00 15.22 ?  321 GLU A CG  1 
ATOM   2402 C  CD  . GLU A 1 319 ? 14.251  -8.471  3.468   1.00 18.83 ?  321 GLU A CD  1 
ATOM   2403 O  OE1 . GLU A 1 319 ? 15.426  -8.869  3.651   1.00 21.31 ?  321 GLU A OE1 1 
ATOM   2404 O  OE2 . GLU A 1 319 ? 13.954  -7.425  2.829   1.00 16.92 ?  321 GLU A OE2 1 
ATOM   2405 N  N   . GLY A 1 320 ? 10.346  -9.699  7.260   1.00 11.02 ?  322 GLY A N   1 
ATOM   2406 C  CA  . GLY A 1 320 ? 10.591  -10.355 8.531   1.00 10.41 ?  322 GLY A CA  1 
ATOM   2407 C  C   . GLY A 1 320 ? 11.410  -9.561  9.536   1.00 13.10 ?  322 GLY A C   1 
ATOM   2408 O  O   . GLY A 1 320 ? 11.241  -8.347  9.665   1.00 12.13 ?  322 GLY A O   1 
ATOM   2409 N  N   . LEU A 1 321 ? 12.281  -10.246 10.275  1.00 9.81  ?  323 LEU A N   1 
ATOM   2410 C  CA  . LEU A 1 321 ? 13.005  -9.591  11.368  1.00 12.55 ?  323 LEU A CA  1 
ATOM   2411 C  C   . LEU A 1 321 ? 14.234  -8.829  10.894  1.00 11.77 ?  323 LEU A C   1 
ATOM   2412 O  O   . LEU A 1 321 ? 14.568  -7.792  11.474  1.00 11.64 ?  323 LEU A O   1 
ATOM   2413 C  CB  . LEU A 1 321 ? 13.428  -10.609 12.428  1.00 12.65 ?  323 LEU A CB  1 
ATOM   2414 C  CG  . LEU A 1 321 ? 12.330  -11.225 13.301  1.00 13.46 ?  323 LEU A CG  1 
ATOM   2415 C  CD1 . LEU A 1 321 ? 12.961  -12.040 14.414  1.00 19.03 ?  323 LEU A CD1 1 
ATOM   2416 C  CD2 . LEU A 1 321 ? 11.479  -10.138 13.891  1.00 14.25 ?  323 LEU A CD2 1 
ATOM   2417 N  N   . GLY A 1 322 ? 14.948  -9.340  9.894   1.00 11.58 ?  324 GLY A N   1 
ATOM   2418 C  CA  . GLY A 1 322 ? 16.204  -8.740  9.492   1.00 11.86 ?  324 GLY A CA  1 
ATOM   2419 C  C   . GLY A 1 322 ? 17.268  -9.800  9.287   1.00 13.56 ?  324 GLY A C   1 
ATOM   2420 O  O   . GLY A 1 322 ? 16.964  -10.976 9.064   1.00 11.57 ?  324 GLY A O   1 
ATOM   2421 N  N   . SER A 1 323 ? 18.526  -9.372  9.397   1.00 11.47 ?  325 SER A N   1 
ATOM   2422 C  CA  . SER A 1 323 ? 19.671  -10.220 9.071   1.00 10.14 ?  325 SER A CA  1 
ATOM   2423 C  C   . SER A 1 323 ? 19.794  -11.407 10.031  1.00 12.17 ?  325 SER A C   1 
ATOM   2424 O  O   . SER A 1 323 ? 19.308  -11.368 11.161  1.00 12.85 ?  325 SER A O   1 
ATOM   2425 C  CB  . SER A 1 323 ? 20.939  -9.378  9.112   1.00 14.55 ?  325 SER A CB  1 
ATOM   2426 O  OG  . SER A 1 323 ? 21.309  -9.185  10.462  1.00 11.76 ?  325 SER A OG  1 
ATOM   2427 N  N   . PRO A 1 324 ? 20.448  -12.485 9.595   1.00 12.32 ?  326 PRO A N   1 
ATOM   2428 C  CA  . PRO A 1 324 ? 20.716  -13.592 10.529  1.00 16.67 ?  326 PRO A CA  1 
ATOM   2429 C  C   . PRO A 1 324 ? 21.505  -13.166 11.757  1.00 14.60 ?  326 PRO A C   1 
ATOM   2430 O  O   . PRO A 1 324 ? 21.248  -13.666 12.859  1.00 13.49 ?  326 PRO A O   1 
ATOM   2431 C  CB  . PRO A 1 324 ? 21.508  -14.588 9.665   1.00 17.85 ?  326 PRO A CB  1 
ATOM   2432 C  CG  . PRO A 1 324 ? 21.074  -14.272 8.252   1.00 16.03 ?  326 PRO A CG  1 
ATOM   2433 C  CD  . PRO A 1 324 ? 20.961  -12.765 8.245   1.00 13.77 ?  326 PRO A CD  1 
ATOM   2434 N  N   . GLU A 1 325 ? 22.478  -12.269 11.591  1.00 11.42 ?  327 GLU A N   1 
ATOM   2435 C  CA  . GLU A 1 325 ? 23.229  -11.761 12.737  1.00 14.43 ?  327 GLU A CA  1 
ATOM   2436 C  C   . GLU A 1 325 ? 22.316  -11.024 13.713  1.00 13.04 ?  327 GLU A C   1 
ATOM   2437 O  O   . GLU A 1 325 ? 22.395  -11.217 14.933  1.00 12.41 ?  327 GLU A O   1 
ATOM   2438 C  CB  . GLU A 1 325 ? 24.346  -10.848 12.238  1.00 14.17 ?  327 GLU A CB  1 
ATOM   2439 C  CG  . GLU A 1 325 ? 25.380  -11.573 11.389  1.00 17.20 ?  327 GLU A CG  1 
ATOM   2440 C  CD  . GLU A 1 325 ? 24.978  -11.751 9.920   1.00 26.60 ?  327 GLU A CD  1 
ATOM   2441 O  OE1 . GLU A 1 325 ? 23.969  -11.173 9.469   1.00 21.56 ?  327 GLU A OE1 1 
ATOM   2442 O  OE2 . GLU A 1 325 ? 25.685  -12.489 9.207   1.00 32.52 ?  327 GLU A OE2 1 
ATOM   2443 N  N   . PHE A 1 326 ? 21.464  -10.145 13.191  1.00 12.11 ?  328 PHE A N   1 
ATOM   2444 C  CA  . PHE A 1 326 ? 20.505  -9.446  14.039  1.00 11.88 ?  328 PHE A CA  1 
ATOM   2445 C  C   . PHE A 1 326 ? 19.619  -10.439 14.787  1.00 14.77 ?  328 PHE A C   1 
ATOM   2446 O  O   . PHE A 1 326 ? 19.458  -10.349 16.009  1.00 11.66 ?  328 PHE A O   1 
ATOM   2447 C  CB  . PHE A 1 326 ? 19.670  -8.496  13.169  1.00 12.40 ?  328 PHE A CB  1 
ATOM   2448 C  CG  . PHE A 1 326 ? 18.675  -7.666  13.930  1.00 11.04 ?  328 PHE A CG  1 
ATOM   2449 C  CD1 . PHE A 1 326 ? 19.097  -6.790  14.912  1.00 12.41 ?  328 PHE A CD1 1 
ATOM   2450 C  CD2 . PHE A 1 326 ? 17.314  -7.709  13.612  1.00 9.93  ?  328 PHE A CD2 1 
ATOM   2451 C  CE1 . PHE A 1 326 ? 18.176  -5.991  15.596  1.00 11.91 ?  328 PHE A CE1 1 
ATOM   2452 C  CE2 . PHE A 1 326 ? 16.398  -6.924  14.289  1.00 12.28 ?  328 PHE A CE2 1 
ATOM   2453 C  CZ  . PHE A 1 326 ? 16.825  -6.058  15.273  1.00 11.50 ?  328 PHE A CZ  1 
ATOM   2454 N  N   . GLN A 1 327 ? 19.047  -11.409 14.063  1.00 12.62 ?  329 GLN A N   1 
ATOM   2455 C  CA  . GLN A 1 327 ? 18.168  -12.388 14.697  1.00 13.48 ?  329 GLN A CA  1 
ATOM   2456 C  C   . GLN A 1 327 ? 18.899  -13.195 15.766  1.00 15.22 ?  329 GLN A C   1 
ATOM   2457 O  O   . GLN A 1 327 ? 18.334  -13.484 16.828  1.00 14.83 ?  329 GLN A O   1 
ATOM   2458 C  CB  . GLN A 1 327 ? 17.576  -13.310 13.635  1.00 14.60 ?  329 GLN A CB  1 
ATOM   2459 C  CG  . GLN A 1 327 ? 16.655  -12.574 12.682  1.00 16.73 ?  329 GLN A CG  1 
ATOM   2460 C  CD  . GLN A 1 327 ? 15.825  -13.515 11.850  1.00 19.93 ?  329 GLN A CD  1 
ATOM   2461 O  OE1 . GLN A 1 327 ? 15.314  -14.514 12.358  1.00 26.58 ?  329 GLN A OE1 1 
ATOM   2462 N  NE2 . GLN A 1 327 ? 15.687  -13.211 10.567  1.00 18.55 ?  329 GLN A NE2 1 
ATOM   2463 N  N   . SER A 1 328 ? 20.164  -13.545 15.518  1.00 14.24 ?  330 SER A N   1 
ATOM   2464 C  CA  . SER A 1 328 ? 20.902  -14.356 16.486  1.00 15.06 ?  330 SER A CA  1 
ATOM   2465 C  C   . SER A 1 328 ? 21.086  -13.632 17.809  1.00 15.47 ?  330 SER A C   1 
ATOM   2466 O  O   . SER A 1 328 ? 21.203  -14.281 18.853  1.00 15.88 ?  330 SER A O   1 
ATOM   2467 C  CB  . SER A 1 328 ? 22.273  -14.755 15.939  1.00 15.65 ?  330 SER A CB  1 
ATOM   2468 O  OG  . SER A 1 328 ? 23.194  -13.672 16.050  1.00 24.25 ?  330 SER A OG  1 
ATOM   2469 N  N   . LEU A 1 329 ? 21.126  -12.292 17.796  1.00 14.17 ?  331 LEU A N   1 
ATOM   2470 C  CA  . LEU A 1 329 ? 21.333  -11.568 19.050  1.00 15.66 ?  331 LEU A CA  1 
ATOM   2471 C  C   . LEU A 1 329 ? 20.154  -11.728 20.004  1.00 17.30 ?  331 LEU A C   1 
ATOM   2472 O  O   . LEU A 1 329 ? 20.348  -11.716 21.227  1.00 17.45 ?  331 LEU A O   1 
ATOM   2473 C  CB  . LEU A 1 329 ? 21.600  -10.091 18.769  1.00 14.45 ?  331 LEU A CB  1 
ATOM   2474 C  CG  . LEU A 1 329 ? 23.005  -9.823  18.211  1.00 16.07 ?  331 LEU A CG  1 
ATOM   2475 C  CD1 . LEU A 1 329 ? 23.054  -8.506  17.428  1.00 17.88 ?  331 LEU A CD1 1 
ATOM   2476 C  CD2 . LEU A 1 329 ? 24.047  -9.831  19.305  1.00 18.10 ?  331 LEU A CD2 1 
ATOM   2477 N  N   . PHE A 1 330 ? 18.935  -11.881 19.475  1.00 13.98 ?  332 PHE A N   1 
ATOM   2478 C  CA  . PHE A 1 330 ? 17.783  -12.141 20.336  1.00 18.60 ?  332 PHE A CA  1 
ATOM   2479 C  C   . PHE A 1 330 ? 17.875  -13.512 20.991  1.00 22.49 ?  332 PHE A C   1 
ATOM   2480 O  O   . PHE A 1 330 ? 17.431  -13.685 22.132  1.00 21.88 ?  332 PHE A O   1 
ATOM   2481 C  CB  . PHE A 1 330 ? 16.485  -12.028 19.537  1.00 19.45 ?  332 PHE A CB  1 
ATOM   2482 C  CG  . PHE A 1 330 ? 16.195  -10.637 19.048  1.00 18.72 ?  332 PHE A CG  1 
ATOM   2483 C  CD1 . PHE A 1 330 ? 15.498  -9.743  19.845  1.00 15.10 ?  332 PHE A CD1 1 
ATOM   2484 C  CD2 . PHE A 1 330 ? 16.650  -10.216 17.802  1.00 20.62 ?  332 PHE A CD2 1 
ATOM   2485 C  CE1 . PHE A 1 330 ? 15.225  -8.451  19.405  1.00 20.35 ?  332 PHE A CE1 1 
ATOM   2486 C  CE2 . PHE A 1 330 ? 16.397  -8.930  17.352  1.00 19.73 ?  332 PHE A CE2 1 
ATOM   2487 C  CZ  . PHE A 1 330 ? 15.672  -8.041  18.155  1.00 17.28 ?  332 PHE A CZ  1 
ATOM   2488 N  N   . GLU A 1 331 ? 18.432  -14.495 20.283  1.00 19.53 ?  333 GLU A N   1 
ATOM   2489 C  CA  . GLU A 1 331 ? 18.630  -15.811 20.882  1.00 20.55 ?  333 GLU A CA  1 
ATOM   2490 C  C   . GLU A 1 331 ? 19.784  -15.798 21.880  1.00 22.35 ?  333 GLU A C   1 
ATOM   2491 O  O   . GLU A 1 331 ? 19.698  -16.421 22.943  1.00 23.20 ?  333 GLU A O   1 
ATOM   2492 C  CB  . GLU A 1 331 ? 18.878  -16.848 19.789  1.00 17.73 ?  333 GLU A CB  1 
ATOM   2493 N  N   . GLU A 1 332 ? 20.874  -15.098 21.559  1.00 16.61 ?  334 GLU A N   1 
ATOM   2494 C  CA  . GLU A 1 332 ? 22.022  -15.078 22.457  1.00 19.62 ?  334 GLU A CA  1 
ATOM   2495 C  C   . GLU A 1 332 ? 21.762  -14.219 23.693  1.00 22.04 ?  334 GLU A C   1 
ATOM   2496 O  O   . GLU A 1 332 ? 22.350  -14.469 24.751  1.00 20.07 ?  334 GLU A O   1 
ATOM   2497 C  CB  . GLU A 1 332 ? 23.262  -14.578 21.715  1.00 17.69 ?  334 GLU A CB  1 
ATOM   2498 N  N   . HIS A 1 333 ? 20.895  -13.211 23.584  1.00 16.61 ?  335 HIS A N   1 
ATOM   2499 C  CA  . HIS A 1 333 ? 20.574  -12.314 24.694  1.00 19.15 ?  335 HIS A CA  1 
ATOM   2500 C  C   . HIS A 1 333 ? 19.070  -12.212 24.879  1.00 17.49 ?  335 HIS A C   1 
ATOM   2501 O  O   . HIS A 1 333 ? 18.426  -11.327 24.296  1.00 15.23 ?  335 HIS A O   1 
ATOM   2502 C  CB  . HIS A 1 333 ? 21.162  -10.917 24.480  1.00 18.47 ?  335 HIS A CB  1 
ATOM   2503 C  CG  . HIS A 1 333 ? 22.601  -10.922 24.087  1.00 16.38 ?  335 HIS A CG  1 
ATOM   2504 N  ND1 . HIS A 1 333 ? 23.611  -11.062 25.010  1.00 18.44 ?  335 HIS A ND1 1 
ATOM   2505 C  CD2 . HIS A 1 333 ? 23.204  -10.778 22.883  1.00 19.03 ?  335 HIS A CD2 1 
ATOM   2506 C  CE1 . HIS A 1 333 ? 24.778  -11.019 24.391  1.00 19.34 ?  335 HIS A CE1 1 
ATOM   2507 N  NE2 . HIS A 1 333 ? 24.559  -10.852 23.098  1.00 20.90 ?  335 HIS A NE2 1 
ATOM   2508 N  N   . PRO A 1 334 ? 18.476  -13.073 25.716  1.00 19.74 ?  336 PRO A N   1 
ATOM   2509 C  CA  . PRO A 1 334 ? 17.012  -13.019 25.906  1.00 19.96 ?  336 PRO A CA  1 
ATOM   2510 C  C   . PRO A 1 334 ? 16.533  -11.755 26.601  1.00 19.00 ?  336 PRO A C   1 
ATOM   2511 O  O   . PRO A 1 334 ? 15.348  -11.428 26.494  1.00 19.70 ?  336 PRO A O   1 
ATOM   2512 C  CB  . PRO A 1 334 ? 16.713  -14.260 26.760  1.00 18.55 ?  336 PRO A CB  1 
ATOM   2513 C  CG  . PRO A 1 334 ? 17.997  -14.584 27.428  1.00 24.31 ?  336 PRO A CG  1 
ATOM   2514 C  CD  . PRO A 1 334 ? 19.102  -14.149 26.502  1.00 23.41 ?  336 PRO A CD  1 
ATOM   2515 N  N   . THR A 1 335 ? 17.394  -11.048 27.328  1.00 14.62 ?  337 THR A N   1 
ATOM   2516 C  CA  . THR A 1 335 ? 17.025  -9.765  27.911  1.00 14.33 ?  337 THR A CA  1 
ATOM   2517 C  C   . THR A 1 335 ? 17.891  -8.647  27.347  1.00 17.58 ?  337 THR A C   1 
ATOM   2518 O  O   . THR A 1 335 ? 19.077  -8.843  27.050  1.00 12.95 ?  337 THR A O   1 
ATOM   2519 C  CB  . THR A 1 335 ? 17.160  -9.777  29.434  1.00 15.42 ?  337 THR A CB  1 
ATOM   2520 O  OG1 . THR A 1 335 ? 18.549  -9.758  29.785  1.00 17.57 ?  337 THR A OG1 1 
ATOM   2521 C  CG2 . THR A 1 335 ? 16.500  -11.027 30.012  1.00 18.73 ?  337 THR A CG2 1 
ATOM   2522 N  N   . LEU A 1 336 ? 17.287  -7.460  27.214  1.00 13.38 ?  338 LEU A N   1 
ATOM   2523 C  CA  . LEU A 1 336 ? 18.051  -6.292  26.780  1.00 12.17 ?  338 LEU A CA  1 
ATOM   2524 C  C   . LEU A 1 336 ? 19.108  -5.903  27.809  1.00 15.25 ?  338 LEU A C   1 
ATOM   2525 O  O   . LEU A 1 336 ? 20.186  -5.411  27.442  1.00 13.38 ?  338 LEU A O   1 
ATOM   2526 C  CB  . LEU A 1 336 ? 17.103  -5.117  26.518  1.00 14.86 ?  338 LEU A CB  1 
ATOM   2527 C  CG  . LEU A 1 336 ? 16.222  -5.297  25.282  1.00 15.54 ?  338 LEU A CG  1 
ATOM   2528 C  CD1 . LEU A 1 336 ? 15.120  -4.215  25.222  1.00 18.35 ?  338 LEU A CD1 1 
ATOM   2529 C  CD2 . LEU A 1 336 ? 17.070  -5.310  24.033  1.00 15.61 ?  338 LEU A CD2 1 
ATOM   2530 N  N   . GLU A 1 337 ? 18.816  -6.112  29.095  1.00 11.52 ?  339 GLU A N   1 
ATOM   2531 C  CA  . GLU A 1 337 ? 19.782  -5.799  30.140  1.00 15.30 ?  339 GLU A CA  1 
ATOM   2532 C  C   . GLU A 1 337 ? 21.041  -6.646  29.997  1.00 15.77 ?  339 GLU A C   1 
ATOM   2533 O  O   . GLU A 1 337 ? 22.157  -6.146  30.196  1.00 14.00 ?  339 GLU A O   1 
ATOM   2534 C  CB  . GLU A 1 337 ? 19.149  -6.003  31.517  1.00 16.24 ?  339 GLU A CB  1 
ATOM   2535 C  CG  . GLU A 1 337 ? 17.984  -5.053  31.833  1.00 25.89 ?  339 GLU A CG  1 
ATOM   2536 C  CD  . GLU A 1 337 ? 16.688  -5.339  31.051  1.00 27.60 ?  339 GLU A CD  1 
ATOM   2537 O  OE1 . GLU A 1 337 ? 15.842  -4.418  30.992  1.00 36.58 ?  339 GLU A OE1 1 
ATOM   2538 O  OE2 . GLU A 1 337 ? 16.488  -6.464  30.517  1.00 20.12 ?  339 GLU A OE2 1 
ATOM   2539 N  N   . GLY A 1 338 ? 20.881  -7.929  29.651  1.00 12.56 ?  340 GLY A N   1 
ATOM   2540 C  CA  . GLY A 1 338 ? 22.044  -8.776  29.423  1.00 10.60 ?  340 GLY A CA  1 
ATOM   2541 C  C   . GLY A 1 338 ? 22.791  -8.385  28.162  1.00 12.47 ?  340 GLY A C   1 
ATOM   2542 O  O   . GLY A 1 338 ? 24.024  -8.406  28.125  1.00 12.48 ?  340 GLY A O   1 
ATOM   2543 N  N   . PHE A 1 339 ? 22.052  -8.034  27.105  1.00 13.92 ?  341 PHE A N   1 
ATOM   2544 C  CA  . PHE A 1 339 ? 22.697  -7.535  25.899  1.00 13.38 ?  341 PHE A CA  1 
ATOM   2545 C  C   . PHE A 1 339 ? 23.517  -6.288  26.202  1.00 10.25 ?  341 PHE A C   1 
ATOM   2546 O  O   . PHE A 1 339 ? 24.637  -6.126  25.694  1.00 11.02 ?  341 PHE A O   1 
ATOM   2547 C  CB  . PHE A 1 339 ? 21.649  -7.226  24.818  1.00 11.42 ?  341 PHE A CB  1 
ATOM   2548 C  CG  . PHE A 1 339 ? 22.197  -6.414  23.676  1.00 11.22 ?  341 PHE A CG  1 
ATOM   2549 C  CD1 . PHE A 1 339 ? 23.050  -6.998  22.747  1.00 11.80 ?  341 PHE A CD1 1 
ATOM   2550 C  CD2 . PHE A 1 339 ? 21.874  -5.065  23.538  1.00 14.27 ?  341 PHE A CD2 1 
ATOM   2551 C  CE1 . PHE A 1 339 ? 23.578  -6.262  21.697  1.00 13.87 ?  341 PHE A CE1 1 
ATOM   2552 C  CE2 . PHE A 1 339 ? 22.396  -4.317  22.494  1.00 13.50 ?  341 PHE A CE2 1 
ATOM   2553 C  CZ  . PHE A 1 339 ? 23.248  -4.920  21.562  1.00 10.35 ?  341 PHE A CZ  1 
ATOM   2554 N  N   . MET A 1 340 ? 22.986  -5.392  27.027  1.00 11.72 ?  342 MET A N   1 
ATOM   2555 C  CA  . MET A 1 340 ? 23.712  -4.150  27.206  1.00 12.57 ?  342 MET A CA  1 
ATOM   2556 C  C   . MET A 1 340 ? 24.921  -4.368  28.102  1.00 12.34 ?  342 MET A C   1 
ATOM   2557 O  O   . MET A 1 340 ? 25.956  -3.729  27.902  1.00 12.55 ?  342 MET A O   1 
ATOM   2558 C  CB  . MET A 1 340 ? 22.799  -3.051  27.745  1.00 12.67 ?  342 MET A CB  1 
ATOM   2559 C  CG  . MET A 1 340 ? 21.795  -2.779  26.652  1.00 13.41 ?  342 MET A CG  1 
ATOM   2560 S  SD  . MET A 1 340 ? 22.358  -1.677  25.371  1.00 15.40 ?  342 MET A SD  1 
ATOM   2561 C  CE  . MET A 1 340 ? 23.376  -0.432  26.158  1.00 16.08 ?  342 MET A CE  1 
ATOM   2562 N  N   . GLU A 1 341 ? 24.826  -5.301  29.057  1.00 12.37 ?  343 GLU A N   1 
ATOM   2563 C  CA  . GLU A 1 341 ? 26.018  -5.705  29.812  1.00 16.39 ?  343 GLU A CA  1 
ATOM   2564 C  C   . GLU A 1 341 ? 27.111  -6.245  28.884  1.00 11.74 ?  343 GLU A C   1 
ATOM   2565 O  O   . GLU A 1 341 ? 28.293  -5.904  29.036  1.00 11.47 ?  343 GLU A O   1 
ATOM   2566 C  CB  . GLU A 1 341 ? 25.633  -6.746  30.869  1.00 13.76 ?  343 GLU A CB  1 
ATOM   2567 C  CG  . GLU A 1 341 ? 26.800  -7.270  31.708  1.00 13.99 ?  343 GLU A CG  1 
ATOM   2568 C  CD  . GLU A 1 341 ? 27.292  -6.260  32.737  1.00 17.78 ?  343 GLU A CD  1 
ATOM   2569 O  OE1 . GLU A 1 341 ? 26.528  -5.338  33.117  1.00 18.10 ?  343 GLU A OE1 1 
ATOM   2570 O  OE2 . GLU A 1 341 ? 28.468  -6.365  33.146  1.00 16.04 ?  343 GLU A OE2 1 
ATOM   2571 N  N   . ALA A 1 342 ? 26.730  -7.072  27.907  1.00 10.46 ?  344 ALA A N   1 
ATOM   2572 C  CA  . ALA A 1 342 ? 27.693  -7.600  26.941  1.00 12.04 ?  344 ALA A CA  1 
ATOM   2573 C  C   . ALA A 1 342 ? 28.422  -6.478  26.200  1.00 13.77 ?  344 ALA A C   1 
ATOM   2574 O  O   . ALA A 1 342 ? 29.657  -6.464  26.124  1.00 14.11 ?  344 ALA A O   1 
ATOM   2575 C  CB  . ALA A 1 342 ? 26.980  -8.525  25.955  1.00 14.07 ?  344 ALA A CB  1 
ATOM   2576 N  N   . ILE A 1 343 ? 27.680  -5.511  25.647  1.00 14.35 ?  345 ILE A N   1 
ATOM   2577 C  CA  . ILE A 1 343 ? 28.353  -4.563  24.767  1.00 13.45 ?  345 ILE A CA  1 
ATOM   2578 C  C   . ILE A 1 343 ? 28.889  -3.329  25.481  1.00 13.99 ?  345 ILE A C   1 
ATOM   2579 O  O   . ILE A 1 343 ? 29.719  -2.616  24.902  1.00 14.97 ?  345 ILE A O   1 
ATOM   2580 C  CB  . ILE A 1 343 ? 27.432  -4.160  23.598  1.00 13.99 ?  345 ILE A CB  1 
ATOM   2581 C  CG1 . ILE A 1 343 ? 26.250  -3.309  24.079  1.00 14.27 ?  345 ILE A CG1 1 
ATOM   2582 C  CG2 . ILE A 1 343 ? 26.952  -5.405  22.863  1.00 17.12 ?  345 ILE A CG2 1 
ATOM   2583 C  CD1 . ILE A 1 343 ? 25.737  -2.367  23.001  1.00 15.46 ?  345 ILE A CD1 1 
ATOM   2584 N  N   . LEU A 1 344 ? 28.466  -3.055  26.717  1.00 12.50 ?  346 LEU A N   1 
ATOM   2585 C  CA  . LEU A 1 344 ? 28.956  -1.865  27.411  1.00 14.98 ?  346 LEU A CA  1 
ATOM   2586 C  C   . LEU A 1 344 ? 30.268  -2.091  28.160  1.00 18.41 ?  346 LEU A C   1 
ATOM   2587 O  O   . LEU A 1 344 ? 31.043  -1.142  28.329  1.00 18.91 ?  346 LEU A O   1 
ATOM   2588 C  CB  . LEU A 1 344 ? 27.913  -1.355  28.411  1.00 12.85 ?  346 LEU A CB  1 
ATOM   2589 C  CG  . LEU A 1 344 ? 26.653  -0.699  27.843  1.00 14.17 ?  346 LEU A CG  1 
ATOM   2590 C  CD1 . LEU A 1 344 ? 25.714  -0.309  28.969  1.00 17.41 ?  346 LEU A CD1 1 
ATOM   2591 C  CD2 . LEU A 1 344 ? 26.950  0.503   26.956  1.00 18.89 ?  346 LEU A CD2 1 
ATOM   2592 N  N   . LYS A 1 345 ? 30.531  -3.304  28.634  1.00 16.16 ?  347 LYS A N   1 
ATOM   2593 C  CA  . LYS A 1 345 ? 31.662  -3.530  29.528  1.00 17.59 ?  347 LYS A CA  1 
ATOM   2594 C  C   . LYS A 1 345 ? 32.871  -4.129  28.826  1.00 20.58 ?  347 LYS A C   1 
ATOM   2595 O  O   . LYS A 1 345 ? 33.916  -4.286  29.462  1.00 21.31 ?  347 LYS A O   1 
ATOM   2596 C  CB  . LYS A 1 345 ? 31.247  -4.422  30.707  1.00 18.85 ?  347 LYS A CB  1 
ATOM   2597 C  CG  . LYS A 1 345 ? 29.918  -4.042  31.388  1.00 24.18 ?  347 LYS A CG  1 
ATOM   2598 C  CD  . LYS A 1 345 ? 29.934  -2.633  31.968  1.00 28.40 ?  347 LYS A CD  1 
ATOM   2599 C  CE  . LYS A 1 345 ? 28.698  -2.335  32.828  1.00 16.17 ?  347 LYS A CE  1 
ATOM   2600 N  NZ  . LYS A 1 345 ? 28.491  -3.175  34.042  1.00 20.92 ?  347 LYS A NZ  1 
ATOM   2601 N  N   . GLU A 1 346 ? 32.755  -4.470  27.544  1.00 16.35 ?  348 GLU A N   1 
ATOM   2602 C  CA  . GLU A 1 346 ? 33.874  -4.964  26.756  1.00 17.23 ?  348 GLU A CA  1 
ATOM   2603 C  C   . GLU A 1 346 ? 33.648  -4.558  25.307  1.00 20.22 ?  348 GLU A C   1 
ATOM   2604 O  O   . GLU A 1 346 ? 32.540  -4.174  24.915  1.00 16.91 ?  348 GLU A O   1 
ATOM   2605 C  CB  . GLU A 1 346 ? 34.016  -6.494  26.846  1.00 17.69 ?  348 GLU A CB  1 
ATOM   2606 C  CG  . GLU A 1 346 ? 34.749  -7.009  28.078  1.00 30.73 ?  348 GLU A CG  1 
ATOM   2607 C  CD  . GLU A 1 346 ? 36.200  -6.577  28.134  1.00 39.36 ?  348 GLU A CD  1 
ATOM   2608 O  OE1 . GLU A 1 346 ? 36.489  -5.546  28.785  1.00 45.44 ?  348 GLU A OE1 1 
ATOM   2609 O  OE2 . GLU A 1 346 ? 37.050  -7.261  27.521  1.00 48.42 ?  348 GLU A OE2 1 
ATOM   2610 N  N   . GLU A 1 347 ? 34.717  -4.648  24.513  1.00 16.01 ?  349 GLU A N   1 
ATOM   2611 C  CA  . GLU A 1 347 ? 34.669  -4.351  23.078  1.00 18.68 ?  349 GLU A CA  1 
ATOM   2612 C  C   . GLU A 1 347 ? 34.062  -5.541  22.336  1.00 19.60 ?  349 GLU A C   1 
ATOM   2613 O  O   . GLU A 1 347 ? 34.740  -6.314  21.657  1.00 20.74 ?  349 GLU A O   1 
ATOM   2614 C  CB  . GLU A 1 347 ? 36.062  -4.015  22.554  1.00 20.46 ?  349 GLU A CB  1 
ATOM   2615 C  CG  . GLU A 1 347 ? 36.645  -2.744  23.146  1.00 21.01 ?  349 GLU A CG  1 
ATOM   2616 C  CD  . GLU A 1 347 ? 35.887  -1.503  22.712  1.00 25.93 ?  349 GLU A CD  1 
ATOM   2617 O  OE1 . GLU A 1 347 ? 35.010  -1.044  23.472  1.00 33.29 ?  349 GLU A OE1 1 
ATOM   2618 O  OE2 . GLU A 1 347 ? 36.170  -0.986  21.609  1.00 27.35 ?  349 GLU A OE2 1 
ATOM   2619 N  N   . SER A 1 348 ? 32.739  -5.658  22.433  1.00 14.93 ?  350 SER A N   1 
ATOM   2620 C  CA  . SER A 1 348 ? 31.984  -6.756  21.844  1.00 16.05 ?  350 SER A CA  1 
ATOM   2621 C  C   . SER A 1 348 ? 31.234  -6.227  20.627  1.00 14.40 ?  350 SER A C   1 
ATOM   2622 O  O   . SER A 1 348 ? 30.440  -5.294  20.761  1.00 14.83 ?  350 SER A O   1 
ATOM   2623 C  CB  . SER A 1 348 ? 31.003  -7.337  22.869  1.00 14.47 ?  350 SER A CB  1 
ATOM   2624 O  OG  . SER A 1 348 ? 30.204  -8.359  22.294  1.00 17.49 ?  350 SER A OG  1 
ATOM   2625 N  N   . PHE A 1 349 ? 31.488  -6.809  19.448  1.00 13.40 ?  351 PHE A N   1 
ATOM   2626 C  CA  . PHE A 1 349 ? 30.965  -6.276  18.190  1.00 11.33 ?  351 PHE A CA  1 
ATOM   2627 C  C   . PHE A 1 349 ? 30.362  -7.396  17.357  1.00 15.30 ?  351 PHE A C   1 
ATOM   2628 O  O   . PHE A 1 349 ? 31.073  -8.313  16.933  1.00 17.47 ?  351 PHE A O   1 
ATOM   2629 C  CB  . PHE A 1 349 ? 32.057  -5.568  17.381  1.00 13.12 ?  351 PHE A CB  1 
ATOM   2630 C  CG  . PHE A 1 349 ? 32.652  -4.374  18.086  1.00 12.90 ?  351 PHE A CG  1 
ATOM   2631 C  CD1 . PHE A 1 349 ? 31.859  -3.276  18.403  1.00 12.35 ?  351 PHE A CD1 1 
ATOM   2632 C  CD2 . PHE A 1 349 ? 33.982  -4.363  18.454  1.00 17.48 ?  351 PHE A CD2 1 
ATOM   2633 C  CE1 . PHE A 1 349 ? 32.388  -2.184  19.051  1.00 14.66 ?  351 PHE A CE1 1 
ATOM   2634 C  CE2 . PHE A 1 349 ? 34.524  -3.261  19.105  1.00 16.80 ?  351 PHE A CE2 1 
ATOM   2635 C  CZ  . PHE A 1 349 ? 33.723  -2.173  19.406  1.00 13.81 ?  351 PHE A CZ  1 
ATOM   2636 N  N   . THR A 1 350 ? 29.076  -7.279  17.078  1.00 12.18 ?  352 THR A N   1 
ATOM   2637 C  CA  . THR A 1 350 ? 28.316  -8.200  16.250  1.00 11.32 ?  352 THR A CA  1 
ATOM   2638 C  C   . THR A 1 350 ? 27.574  -7.364  15.225  1.00 10.23 ?  352 THR A C   1 
ATOM   2639 O  O   . THR A 1 350 ? 27.028  -6.311  15.571  1.00 11.09 ?  352 THR A O   1 
ATOM   2640 C  CB  . THR A 1 350 ? 27.295  -8.996  17.078  1.00 13.32 ?  352 THR A CB  1 
ATOM   2641 O  OG1 . THR A 1 350 ? 27.977  -9.835  18.013  1.00 19.10 ?  352 THR A OG1 1 
ATOM   2642 C  CG2 . THR A 1 350 ? 26.396  -9.854  16.182  1.00 15.74 ?  352 THR A CG2 1 
ATOM   2643 N  N   . VAL A 1 351 ? 27.526  -7.846  13.979  1.00 9.87  ?  353 VAL A N   1 
ATOM   2644 C  CA  . VAL A 1 351 ? 26.816  -7.123  12.929  1.00 9.71  ?  353 VAL A CA  1 
ATOM   2645 C  C   . VAL A 1 351 ? 25.388  -6.854  13.374  1.00 9.85  ?  353 VAL A C   1 
ATOM   2646 O  O   . VAL A 1 351 ? 24.717  -7.738  13.919  1.00 11.13 ?  353 VAL A O   1 
ATOM   2647 C  CB  . VAL A 1 351 ? 26.842  -7.921  11.610  1.00 11.03 ?  353 VAL A CB  1 
ATOM   2648 C  CG1 . VAL A 1 351 ? 25.860  -7.337  10.608  1.00 14.29 ?  353 VAL A CG1 1 
ATOM   2649 C  CG2 . VAL A 1 351 ? 28.250  -7.954  11.024  1.00 12.36 ?  353 VAL A CG2 1 
ATOM   2650 N  N   . ASP A 1 352 ? 24.943  -5.610  13.189  1.00 10.88 ?  354 ASP A N   1 
ATOM   2651 C  CA  . ASP A 1 352 ? 23.568  -5.153  13.402  1.00 9.98  ?  354 ASP A CA  1 
ATOM   2652 C  C   . ASP A 1 352 ? 23.183  -5.003  14.876  1.00 10.66 ?  354 ASP A C   1 
ATOM   2653 O  O   . ASP A 1 352 ? 22.022  -4.719  15.167  1.00 12.13 ?  354 ASP A O   1 
ATOM   2654 C  CB  . ASP A 1 352 ? 22.573  -6.065  12.661  1.00 10.51 ?  354 ASP A CB  1 
ATOM   2655 C  CG  . ASP A 1 352 ? 22.656  -5.892  11.152  1.00 11.19 ?  354 ASP A CG  1 
ATOM   2656 O  OD1 . ASP A 1 352 ? 23.417  -5.011  10.725  1.00 14.10 ?  354 ASP A OD1 1 
ATOM   2657 O  OD2 . ASP A 1 352 ? 21.992  -6.625  10.375  1.00 12.83 ?  354 ASP A OD2 1 
ATOM   2658 N  N   . GLN A 1 353 ? 24.134  -5.120  15.816  1.00 8.73  ?  355 GLN A N   1 
ATOM   2659 C  CA  . GLN A 1 353 ? 23.787  -5.018  17.234  1.00 9.24  ?  355 GLN A CA  1 
ATOM   2660 C  C   . GLN A 1 353 ? 23.328  -3.617  17.606  1.00 9.50  ?  355 GLN A C   1 
ATOM   2661 O  O   . GLN A 1 353 ? 22.621  -3.445  18.608  1.00 9.42  ?  355 GLN A O   1 
ATOM   2662 C  CB  . GLN A 1 353 ? 24.987  -5.389  18.123  1.00 10.02 ?  355 GLN A CB  1 
ATOM   2663 C  CG  . GLN A 1 353 ? 26.103  -4.322  18.153  1.00 9.75  ?  355 GLN A CG  1 
ATOM   2664 C  CD  . GLN A 1 353 ? 27.305  -4.742  19.027  1.00 11.29 ?  355 GLN A CD  1 
ATOM   2665 O  OE1 . GLN A 1 353 ? 27.593  -5.929  19.160  1.00 14.35 ?  355 GLN A OE1 1 
ATOM   2666 N  NE2 . GLN A 1 353 ? 27.995  -3.767  19.612  1.00 13.62 ?  355 GLN A NE2 1 
ATOM   2667 N  N   . TRP A 1 354 ? 23.717  -2.620  16.816  1.00 10.21 ?  356 TRP A N   1 
ATOM   2668 C  CA  . TRP A 1 354 ? 23.358  -1.239  17.114  1.00 12.45 ?  356 TRP A CA  1 
ATOM   2669 C  C   . TRP A 1 354 ? 21.846  -1.024  17.161  1.00 9.63  ?  356 TRP A C   1 
ATOM   2670 O  O   . TRP A 1 354 ? 21.375  -0.167  17.914  1.00 9.67  ?  356 TRP A O   1 
ATOM   2671 C  CB  . TRP A 1 354 ? 24.000  -0.311  16.084  1.00 10.57 ?  356 TRP A CB  1 
ATOM   2672 C  CG  . TRP A 1 354 ? 24.065  -0.877  14.701  1.00 10.60 ?  356 TRP A CG  1 
ATOM   2673 C  CD1 . TRP A 1 354 ? 23.077  -0.838  13.776  1.00 11.48 ?  356 TRP A CD1 1 
ATOM   2674 C  CD2 . TRP A 1 354 ? 25.180  -1.558  14.077  1.00 10.23 ?  356 TRP A CD2 1 
ATOM   2675 N  NE1 . TRP A 1 354 ? 23.486  -1.453  12.612  1.00 12.11 ?  356 TRP A NE1 1 
ATOM   2676 C  CE2 . TRP A 1 354 ? 24.774  -1.897  12.768  1.00 9.72  ?  356 TRP A CE2 1 
ATOM   2677 C  CE3 . TRP A 1 354 ? 26.474  -1.908  14.502  1.00 9.43  ?  356 TRP A CE3 1 
ATOM   2678 C  CZ2 . TRP A 1 354 ? 25.605  -2.575  11.874  1.00 9.76  ?  356 TRP A CZ2 1 
ATOM   2679 C  CZ3 . TRP A 1 354 ? 27.315  -2.574  13.607  1.00 10.03 ?  356 TRP A CZ3 1 
ATOM   2680 C  CH2 . TRP A 1 354 ? 26.876  -2.900  12.305  1.00 8.60  ?  356 TRP A CH2 1 
ATOM   2681 N  N   . GLN A 1 355 ? 21.062  -1.765  16.375  1.00 9.92  ?  357 GLN A N   1 
ATOM   2682 C  CA  A GLN A 1 355 ? 19.612  -1.571  16.439  0.50 8.81  ?  357 GLN A CA  1 
ATOM   2683 C  CA  B GLN A 1 355 ? 19.624  -1.555  16.449  0.50 8.80  ?  357 GLN A CA  1 
ATOM   2684 C  C   . GLN A 1 355 ? 19.003  -2.200  17.678  1.00 9.82  ?  357 GLN A C   1 
ATOM   2685 O  O   . GLN A 1 355 ? 17.962  -1.726  18.160  1.00 10.96 ?  357 GLN A O   1 
ATOM   2686 C  CB  A GLN A 1 355 ? 18.903  -2.121  15.191  0.50 10.91 ?  357 GLN A CB  1 
ATOM   2687 C  CB  B GLN A 1 355 ? 18.941  -2.048  15.174  0.50 10.94 ?  357 GLN A CB  1 
ATOM   2688 C  CG  A GLN A 1 355 ? 18.813  -1.136  14.041  0.50 7.00  ?  357 GLN A CG  1 
ATOM   2689 C  CG  B GLN A 1 355 ? 17.662  -1.309  14.919  0.50 8.40  ?  357 GLN A CG  1 
ATOM   2690 C  CD  A GLN A 1 355 ? 18.163  0.187   14.435  0.50 11.15 ?  357 GLN A CD  1 
ATOM   2691 C  CD  B GLN A 1 355 ? 17.853  0.140   14.470  0.50 11.14 ?  357 GLN A CD  1 
ATOM   2692 O  OE1 A GLN A 1 355 ? 18.787  1.027   15.090  0.50 11.03 ?  357 GLN A OE1 1 
ATOM   2693 O  OE1 B GLN A 1 355 ? 18.818  0.812   14.843  0.50 11.26 ?  357 GLN A OE1 1 
ATOM   2694 N  NE2 A GLN A 1 355 ? 16.912  0.386   14.019  0.50 8.94  ?  357 GLN A NE2 1 
ATOM   2695 N  NE2 B GLN A 1 355 ? 16.899  0.637   13.693  0.50 9.11  ?  357 GLN A NE2 1 
ATOM   2696 N  N   . LEU A 1 356 ? 19.624  -3.256  18.206  1.00 11.45 ?  358 LEU A N   1 
ATOM   2697 C  CA  . LEU A 1 356 ? 19.194  -3.766  19.497  1.00 11.00 ?  358 LEU A CA  1 
ATOM   2698 C  C   . LEU A 1 356 ? 19.510  -2.760  20.595  1.00 10.26 ?  358 LEU A C   1 
ATOM   2699 O  O   . LEU A 1 356 ? 18.743  -2.614  21.554  1.00 10.16 ?  358 LEU A O   1 
ATOM   2700 C  CB  . LEU A 1 356 ? 19.860  -5.109  19.787  1.00 10.85 ?  358 LEU A CB  1 
ATOM   2701 C  CG  . LEU A 1 356 ? 19.175  -5.986  20.825  1.00 20.55 ?  358 LEU A CG  1 
ATOM   2702 C  CD1 . LEU A 1 356 ? 17.666  -6.075  20.564  1.00 15.38 ?  358 LEU A CD1 1 
ATOM   2703 C  CD2 . LEU A 1 356 ? 19.818  -7.379  20.894  1.00 17.43 ?  358 LEU A CD2 1 
ATOM   2704 N  N   . GLU A 1 357 ? 20.643  -2.059  20.474  1.00 9.82  ?  359 GLU A N   1 
ATOM   2705 C  CA  . GLU A 1 357 ? 20.964  -1.006  21.433  1.00 8.62  ?  359 GLU A CA  1 
ATOM   2706 C  C   . GLU A 1 357 ? 19.947  0.126   21.338  1.00 11.32 ?  359 GLU A C   1 
ATOM   2707 O  O   . GLU A 1 357 ? 19.542  0.696   22.358  1.00 10.04 ?  359 GLU A O   1 
ATOM   2708 C  CB  . GLU A 1 357 ? 22.393  -0.494  21.186  1.00 9.49  ?  359 GLU A CB  1 
ATOM   2709 C  CG  . GLU A 1 357 ? 22.840  0.626   22.121  1.00 9.26  ?  359 GLU A CG  1 
ATOM   2710 C  CD  . GLU A 1 357 ? 24.315  1.052   21.902  1.00 14.82 ?  359 GLU A CD  1 
ATOM   2711 O  OE1 . GLU A 1 357 ? 25.003  0.475   21.031  1.00 13.02 ?  359 GLU A OE1 1 
ATOM   2712 O  OE2 . GLU A 1 357 ? 24.785  1.962   22.611  1.00 16.26 ?  359 GLU A OE2 1 
ATOM   2713 N  N   . GLU A 1 358 ? 19.501  0.451   20.120  1.00 8.94  ?  360 GLU A N   1 
ATOM   2714 C  CA  . GLU A 1 358 ? 18.467  1.476   19.977  1.00 8.79  ?  360 GLU A CA  1 
ATOM   2715 C  C   . GLU A 1 358 ? 17.143  1.011   20.558  1.00 8.73  ?  360 GLU A C   1 
ATOM   2716 O  O   . GLU A 1 358 ? 16.413  1.809   21.155  1.00 8.51  ?  360 GLU A O   1 
ATOM   2717 C  CB  . GLU A 1 358 ? 18.278  1.892   18.507  1.00 6.73  ?  360 GLU A CB  1 
ATOM   2718 C  CG  . GLU A 1 358 ? 19.504  2.563   17.878  1.00 9.36  ?  360 GLU A CG  1 
ATOM   2719 C  CD  . GLU A 1 358 ? 19.755  3.970   18.421  1.00 12.63 ?  360 GLU A CD  1 
ATOM   2720 O  OE1 . GLU A 1 358 ? 20.877  4.498   18.231  1.00 13.69 ?  360 GLU A OE1 1 
ATOM   2721 O  OE2 . GLU A 1 358 ? 18.849  4.550   19.066  1.00 14.28 ?  360 GLU A OE2 1 
ATOM   2722 N  N   . LEU A 1 359 ? 16.812  -0.272  20.393  1.00 9.25  ?  361 LEU A N   1 
ATOM   2723 C  CA  . LEU A 1 359 ? 15.588  -0.785  20.999  1.00 9.35  ?  361 LEU A CA  1 
ATOM   2724 C  C   . LEU A 1 359 ? 15.681  -0.749  22.526  1.00 8.78  ?  361 LEU A C   1 
ATOM   2725 O  O   . LEU A 1 359 ? 14.688  -0.478  23.214  1.00 10.10 ?  361 LEU A O   1 
ATOM   2726 C  CB  . LEU A 1 359 ? 15.321  -2.201  20.486  1.00 8.69  ?  361 LEU A CB  1 
ATOM   2727 C  CG  . LEU A 1 359 ? 14.100  -2.935  21.048  1.00 10.08 ?  361 LEU A CG  1 
ATOM   2728 C  CD1 . LEU A 1 359 ? 12.781  -2.187  20.767  1.00 9.75  ?  361 LEU A CD1 1 
ATOM   2729 C  CD2 . LEU A 1 359 ? 14.063  -4.355  20.487  1.00 14.08 ?  361 LEU A CD2 1 
ATOM   2730 N  N   . ALA A 1 360 ? 16.873  -0.995  23.077  1.00 8.67  ?  362 ALA A N   1 
ATOM   2731 C  CA  . ALA A 1 360 ? 17.037  -0.873  24.518  1.00 10.79 ?  362 ALA A CA  1 
ATOM   2732 C  C   . ALA A 1 360 ? 16.814  0.566   24.966  1.00 10.84 ?  362 ALA A C   1 
ATOM   2733 O  O   . ALA A 1 360 ? 16.202  0.813   26.013  1.00 10.46 ?  362 ALA A O   1 
ATOM   2734 C  CB  . ALA A 1 360 ? 18.427  -1.381  24.924  1.00 10.54 ?  362 ALA A CB  1 
ATOM   2735 N  N   . LYS A 1 361 ? 17.293  1.534   24.170  1.00 8.41  ?  363 LYS A N   1 
ATOM   2736 C  CA  . LYS A 1 361 ? 17.049  2.942   24.483  1.00 11.81 ?  363 LYS A CA  1 
ATOM   2737 C  C   . LYS A 1 361 ? 15.553  3.238   24.520  1.00 13.16 ?  363 LYS A C   1 
ATOM   2738 O  O   . LYS A 1 361 ? 15.071  3.951   25.413  1.00 11.11 ?  363 LYS A O   1 
ATOM   2739 C  CB  . LYS A 1 361 ? 17.763  3.820   23.453  1.00 10.67 ?  363 LYS A CB  1 
ATOM   2740 C  CG  . LYS A 1 361 ? 17.619  5.337   23.635  1.00 12.04 ?  363 LYS A CG  1 
ATOM   2741 C  CD  . LYS A 1 361 ? 18.426  6.040   22.536  1.00 14.46 ?  363 LYS A CD  1 
ATOM   2742 C  CE  . LYS A 1 361 ? 18.085  7.512   22.381  1.00 24.49 ?  363 LYS A CE  1 
ATOM   2743 N  NZ  . LYS A 1 361 ? 19.044  8.192   21.437  1.00 19.41 ?  363 LYS A NZ  1 
ATOM   2744 N  N   . VAL A 1 362 ? 14.799  2.674   23.573  1.00 11.05 ?  364 VAL A N   1 
ATOM   2745 C  CA  . VAL A 1 362 ? 13.346  2.829   23.589  1.00 8.89  ?  364 VAL A CA  1 
ATOM   2746 C  C   . VAL A 1 362 ? 12.754  2.234   24.862  1.00 9.21  ?  364 VAL A C   1 
ATOM   2747 O  O   . VAL A 1 362 ? 11.946  2.870   25.546  1.00 13.39 ?  364 VAL A O   1 
ATOM   2748 C  CB  . VAL A 1 362 ? 12.718  2.185   22.343  1.00 8.36  ?  364 VAL A CB  1 
ATOM   2749 C  CG1 . VAL A 1 362 ? 11.204  2.167   22.477  1.00 11.19 ?  364 VAL A CG1 1 
ATOM   2750 C  CG2 . VAL A 1 362 ? 13.127  2.968   21.108  1.00 9.75  ?  364 VAL A CG2 1 
ATOM   2751 N  N   . ARG A 1 363 ? 13.116  0.990   25.173  1.00 8.38  ?  365 ARG A N   1 
ATOM   2752 C  CA  . ARG A 1 363 ? 12.441  0.296   26.266  1.00 12.32 ?  365 ARG A CA  1 
ATOM   2753 C  C   . ARG A 1 363 ? 12.821  0.836   27.641  1.00 17.83 ?  365 ARG A C   1 
ATOM   2754 O  O   . ARG A 1 363 ? 12.092  0.582   28.605  1.00 14.96 ?  365 ARG A O   1 
ATOM   2755 C  CB  . ARG A 1 363 ? 12.709  -1.218  26.188  1.00 12.51 ?  365 ARG A CB  1 
ATOM   2756 C  CG  . ARG A 1 363 ? 12.123  -1.940  24.951  1.00 9.92  ?  365 ARG A CG  1 
ATOM   2757 C  CD  . ARG A 1 363 ? 10.647  -1.539  24.716  1.00 15.21 ?  365 ARG A CD  1 
ATOM   2758 N  NE  . ARG A 1 363 ? 9.883   -1.624  25.953  1.00 24.68 ?  365 ARG A NE  1 
ATOM   2759 C  CZ  . ARG A 1 363 ? 9.657   -2.733  26.646  1.00 23.30 ?  365 ARG A CZ  1 
ATOM   2760 N  NH1 . ARG A 1 363 ? 10.006  -3.918  26.166  1.00 19.77 ?  365 ARG A NH1 1 
ATOM   2761 N  NH2 . ARG A 1 363 ? 9.000   -2.651  27.795  1.00 23.80 ?  365 ARG A NH2 1 
ATOM   2762 N  N   . ARG A 1 364 ? 13.921  1.592   27.758  1.00 12.86 ?  366 ARG A N   1 
ATOM   2763 C  CA  . ARG A 1 364 ? 14.187  2.289   29.012  1.00 15.78 ?  366 ARG A CA  1 
ATOM   2764 C  C   . ARG A 1 364 ? 13.184  3.401   29.284  1.00 19.52 ?  366 ARG A C   1 
ATOM   2765 O  O   . ARG A 1 364 ? 13.040  3.829   30.437  1.00 16.55 ?  366 ARG A O   1 
ATOM   2766 C  CB  . ARG A 1 364 ? 15.597  2.887   29.020  1.00 14.52 ?  366 ARG A CB  1 
ATOM   2767 C  CG  . ARG A 1 364 ? 16.685  1.839   29.163  1.00 18.61 ?  366 ARG A CG  1 
ATOM   2768 C  CD  . ARG A 1 364 ? 18.041  2.444   29.546  1.00 16.53 ?  366 ARG A CD  1 
ATOM   2769 N  NE  . ARG A 1 364 ? 18.558  3.356   28.532  1.00 19.23 ?  366 ARG A NE  1 
ATOM   2770 C  CZ  . ARG A 1 364 ? 19.260  2.949   27.479  1.00 14.09 ?  366 ARG A CZ  1 
ATOM   2771 N  NH1 . ARG A 1 364 ? 19.497  1.654   27.311  1.00 15.50 ?  366 ARG A NH1 1 
ATOM   2772 N  NH2 . ARG A 1 364 ? 19.706  3.826   26.596  1.00 17.20 ?  366 ARG A NH2 1 
ATOM   2773 N  N   . LYS A 1 365 ? 12.508  3.902   28.258  1.00 14.85 ?  367 LYS A N   1 
ATOM   2774 C  CA  . LYS A 1 365 ? 11.546  4.981   28.428  1.00 10.32 ?  367 LYS A CA  1 
ATOM   2775 C  C   . LYS A 1 365 ? 10.100  4.540   28.256  1.00 17.17 ?  367 LYS A C   1 
ATOM   2776 O  O   . LYS A 1 365 ? 9.224   5.041   28.966  1.00 16.94 ?  367 LYS A O   1 
ATOM   2777 C  CB  . LYS A 1 365 ? 11.842  6.118   27.440  1.00 13.33 ?  367 LYS A CB  1 
ATOM   2778 C  CG  . LYS A 1 365 ? 10.850  7.297   27.549  1.00 14.35 ?  367 LYS A CG  1 
ATOM   2779 C  CD  . LYS A 1 365 ? 11.278  8.482   26.719  1.00 13.66 ?  367 LYS A CD  1 
ATOM   2780 C  CE  . LYS A 1 365 ? 10.669  9.773   27.233  1.00 16.89 ?  367 LYS A CE  1 
ATOM   2781 N  NZ  . LYS A 1 365 ? 10.828  10.848  26.218  1.00 17.06 ?  367 LYS A NZ  1 
ATOM   2782 N  N   . ALA A 1 366 ? 9.809   3.622   27.336  1.00 11.71 ?  368 ALA A N   1 
ATOM   2783 C  CA  . ALA A 1 366 ? 8.420   3.364   26.964  1.00 10.36 ?  368 ALA A CA  1 
ATOM   2784 C  C   . ALA A 1 366 ? 8.165   1.875   26.776  1.00 12.77 ?  368 ALA A C   1 
ATOM   2785 O  O   . ALA A 1 366 ? 9.070   1.112   26.422  1.00 11.80 ?  368 ALA A O   1 
ATOM   2786 C  CB  . ALA A 1 366 ? 8.038   4.104   25.670  1.00 10.26 ?  368 ALA A CB  1 
ATOM   2787 N  N   . ARG A 1 367 ? 6.917   1.478   27.041  1.00 11.29 ?  369 ARG A N   1 
ATOM   2788 C  CA  . ARG A 1 367 ? 6.383   0.210   26.576  1.00 11.91 ?  369 ARG A CA  1 
ATOM   2789 C  C   . ARG A 1 367 ? 6.100   0.294   25.082  1.00 10.32 ?  369 ARG A C   1 
ATOM   2790 O  O   . ARG A 1 367 ? 5.877   1.377   24.537  1.00 11.79 ?  369 ARG A O   1 
ATOM   2791 C  CB  . ARG A 1 367 ? 5.084   -0.138  27.316  1.00 11.76 ?  369 ARG A CB  1 
ATOM   2792 C  CG  . ARG A 1 367 ? 5.222   -0.132  28.842  1.00 18.28 ?  369 ARG A CG  1 
ATOM   2793 C  CD  . ARG A 1 367 ? 3.873   -0.375  29.522  1.00 27.02 ?  369 ARG A CD  1 
ATOM   2794 N  N   . VAL A 1 368 ? 6.110   -0.860  24.416  1.00 10.60 ?  370 VAL A N   1 
ATOM   2795 C  CA  . VAL A 1 368 ? 5.844   -0.925  22.983  1.00 11.93 ?  370 VAL A CA  1 
ATOM   2796 C  C   . VAL A 1 368 ? 4.787   -1.982  22.706  1.00 10.31 ?  370 VAL A C   1 
ATOM   2797 O  O   . VAL A 1 368 ? 4.934   -3.133  23.134  1.00 12.24 ?  370 VAL A O   1 
ATOM   2798 C  CB  . VAL A 1 368 ? 7.112   -1.251  22.175  1.00 11.74 ?  370 VAL A CB  1 
ATOM   2799 C  CG1 . VAL A 1 368 ? 6.751   -1.447  20.698  1.00 12.03 ?  370 VAL A CG1 1 
ATOM   2800 C  CG2 . VAL A 1 368 ? 8.181   -0.148  22.367  1.00 11.70 ?  370 VAL A CG2 1 
ATOM   2801 N  N   . LYS A 1 369 ? 3.750   -1.601  21.954  1.00 9.43  ?  371 LYS A N   1 
ATOM   2802 C  CA  . LYS A 1 369 ? 2.775   -2.528  21.390  1.00 8.51  ?  371 LYS A CA  1 
ATOM   2803 C  C   . LYS A 1 369 ? 2.993   -2.532  19.883  1.00 10.96 ?  371 LYS A C   1 
ATOM   2804 O  O   . LYS A 1 369 ? 3.026   -1.462  19.266  1.00 11.94 ?  371 LYS A O   1 
ATOM   2805 C  CB  . LYS A 1 369 ? 1.344   -2.092  21.728  1.00 11.64 ?  371 LYS A CB  1 
ATOM   2806 C  CG  . LYS A 1 369 ? 1.004   -2.207  23.228  1.00 11.65 ?  371 LYS A CG  1 
ATOM   2807 C  CD  . LYS A 1 369 ? -0.435  -1.710  23.502  1.00 11.57 ?  371 LYS A CD  1 
ATOM   2808 C  CE  . LYS A 1 369 ? -0.792  -1.783  25.004  1.00 14.96 ?  371 LYS A CE  1 
ATOM   2809 N  NZ  . LYS A 1 369 ? -0.979  -3.202  25.455  1.00 15.59 ?  371 LYS A NZ  1 
ATOM   2810 N  N   . PHE A 1 370 ? 3.171   -3.719  19.295  1.00 8.47  ?  372 PHE A N   1 
ATOM   2811 C  CA  A PHE A 1 370 ? 3.594   -3.861  17.905  0.50 9.20  ?  372 PHE A CA  1 
ATOM   2812 C  CA  B PHE A 1 370 ? 3.586   -3.851  17.902  0.50 9.20  ?  372 PHE A CA  1 
ATOM   2813 C  C   . PHE A 1 370 ? 2.500   -4.572  17.118  1.00 12.05 ?  372 PHE A C   1 
ATOM   2814 O  O   . PHE A 1 370 ? 2.092   -5.675  17.489  1.00 11.31 ?  372 PHE A O   1 
ATOM   2815 C  CB  A PHE A 1 370 ? 4.925   -4.626  17.824  0.50 9.20  ?  372 PHE A CB  1 
ATOM   2816 C  CB  B PHE A 1 370 ? 4.934   -4.580  17.796  0.50 9.23  ?  372 PHE A CB  1 
ATOM   2817 C  CG  A PHE A 1 370 ? 5.763   -4.258  16.635  0.50 11.29 ?  372 PHE A CG  1 
ATOM   2818 C  CG  B PHE A 1 370 ? 5.728   -4.204  16.573  0.50 11.28 ?  372 PHE A CG  1 
ATOM   2819 C  CD1 A PHE A 1 370 ? 6.988   -3.628  16.806  0.50 9.75  ?  372 PHE A CD1 1 
ATOM   2820 C  CD1 B PHE A 1 370 ? 7.013   -3.698  16.698  0.50 9.80  ?  372 PHE A CD1 1 
ATOM   2821 C  CD2 A PHE A 1 370 ? 5.339   -4.564  15.352  0.50 10.34 ?  372 PHE A CD2 1 
ATOM   2822 C  CD2 B PHE A 1 370 ? 5.208   -4.403  15.302  0.50 10.46 ?  372 PHE A CD2 1 
ATOM   2823 C  CE1 A PHE A 1 370 ? 7.764   -3.276  15.708  0.50 10.88 ?  372 PHE A CE1 1 
ATOM   2824 C  CE1 B PHE A 1 370 ? 7.750   -3.345  15.574  0.50 10.94 ?  372 PHE A CE1 1 
ATOM   2825 C  CE2 A PHE A 1 370 ? 6.104   -4.229  14.249  0.50 11.25 ?  372 PHE A CE2 1 
ATOM   2826 C  CE2 B PHE A 1 370 ? 5.935   -4.070  14.170  0.50 11.25 ?  372 PHE A CE2 1 
ATOM   2827 C  CZ  A PHE A 1 370 ? 7.325   -3.583  14.425  0.50 9.06  ?  372 PHE A CZ  1 
ATOM   2828 C  CZ  B PHE A 1 370 ? 7.216   -3.536  14.306  0.50 9.05  ?  372 PHE A CZ  1 
ATOM   2829 N  N   . VAL A 1 371 ? 2.030   -3.932  16.043  1.00 8.75  ?  373 VAL A N   1 
ATOM   2830 C  CA  . VAL A 1 371 ? 0.964   -4.445  15.183  1.00 9.76  ?  373 VAL A CA  1 
ATOM   2831 C  C   . VAL A 1 371 ? 1.550   -4.749  13.809  1.00 11.72 ?  373 VAL A C   1 
ATOM   2832 O  O   . VAL A 1 371 ? 2.019   -3.842  13.109  1.00 10.00 ?  373 VAL A O   1 
ATOM   2833 C  CB  . VAL A 1 371 ? -0.205  -3.448  15.079  1.00 11.59 ?  373 VAL A CB  1 
ATOM   2834 C  CG1 . VAL A 1 371 ? -1.337  -4.020  14.229  1.00 13.56 ?  373 VAL A CG1 1 
ATOM   2835 C  CG2 . VAL A 1 371 ? -0.728  -3.099  16.473  1.00 11.20 ?  373 VAL A CG2 1 
ATOM   2836 N  N   . SER A 1 372 ? 1.488   -6.016  13.400  1.00 12.15 ?  374 SER A N   1 
ATOM   2837 C  CA  . SER A 1 372 ? 2.057   -6.425  12.119  1.00 12.08 ?  374 SER A CA  1 
ATOM   2838 C  C   . SER A 1 372 ? 1.445   -7.750  11.695  1.00 13.75 ?  374 SER A C   1 
ATOM   2839 O  O   . SER A 1 372 ? 1.199   -8.608  12.544  1.00 15.68 ?  374 SER A O   1 
ATOM   2840 C  CB  . SER A 1 372 ? 3.577   -6.589  12.221  1.00 9.76  ?  374 SER A CB  1 
ATOM   2841 O  OG  . SER A 1 372 ? 4.122   -6.973  10.967  1.00 12.80 ?  374 SER A OG  1 
ATOM   2842 N  N   . ASP A 1 373 ? 1.253   -7.944  10.388  1.00 12.12 ?  375 ASP A N   1 
ATOM   2843 C  CA  . ASP A 1 373 ? 0.944   -9.285  9.906   1.00 13.24 ?  375 ASP A CA  1 
ATOM   2844 C  C   . ASP A 1 373 ? 2.112   -9.912  9.163   1.00 17.36 ?  375 ASP A C   1 
ATOM   2845 O  O   . ASP A 1 373 ? 1.932   -10.942 8.512   1.00 17.32 ?  375 ASP A O   1 
ATOM   2846 C  CB  . ASP A 1 373 ? -0.336  -9.317  9.044   1.00 18.36 ?  375 ASP A CB  1 
ATOM   2847 C  CG  . ASP A 1 373 ? -0.281  -8.424  7.803   1.00 18.92 ?  375 ASP A CG  1 
ATOM   2848 O  OD1 . ASP A 1 373 ? 0.677   -7.652  7.604   1.00 20.77 ?  375 ASP A OD1 1 
ATOM   2849 O  OD2 . ASP A 1 373 ? -1.243  -8.512  7.007   1.00 20.30 ?  375 ASP A OD2 1 
ATOM   2850 N  N   . GLY A 1 374 ? 3.316   -9.354  9.292   1.00 14.19 ?  376 GLY A N   1 
ATOM   2851 C  CA  . GLY A 1 374 ? 4.464   -9.867  8.559   1.00 13.72 ?  376 GLY A CA  1 
ATOM   2852 C  C   . GLY A 1 374 ? 5.339   -10.805 9.366   1.00 16.57 ?  376 GLY A C   1 
ATOM   2853 O  O   . GLY A 1 374 ? 6.143   -11.548 8.792   1.00 18.92 ?  376 GLY A O   1 
ATOM   2854 N  N   . VAL A 1 375 ? 5.222   -10.754 10.690  1.00 14.52 ?  377 VAL A N   1 
ATOM   2855 C  CA  . VAL A 1 375 ? 5.964   -11.621 11.610  1.00 15.26 ?  377 VAL A CA  1 
ATOM   2856 C  C   . VAL A 1 375 ? 4.950   -12.186 12.601  1.00 23.23 ?  377 VAL A C   1 
ATOM   2857 O  O   . VAL A 1 375 ? 4.126   -11.421 13.121  1.00 17.01 ?  377 VAL A O   1 
ATOM   2858 C  CB  . VAL A 1 375 ? 7.078   -10.846 12.343  1.00 14.35 ?  377 VAL A CB  1 
ATOM   2859 C  CG1 . VAL A 1 375 ? 7.644   -11.652 13.498  1.00 21.90 ?  377 VAL A CG1 1 
ATOM   2860 C  CG2 . VAL A 1 375 ? 8.205   -10.416 11.377  1.00 17.43 ?  377 VAL A CG2 1 
ATOM   2861 N  N   . PRO A 1 376 ? 4.965   -13.491 12.901  1.00 21.76 ?  378 PRO A N   1 
ATOM   2862 C  CA  . PRO A 1 376 ? 4.002   -14.036 13.871  1.00 23.23 ?  378 PRO A CA  1 
ATOM   2863 C  C   . PRO A 1 376 ? 4.132   -13.389 15.244  1.00 15.33 ?  378 PRO A C   1 
ATOM   2864 O  O   . PRO A 1 376 ? 5.211   -12.969 15.661  1.00 20.41 ?  378 PRO A O   1 
ATOM   2865 C  CB  . PRO A 1 376 ? 4.363   -15.529 13.932  1.00 19.89 ?  378 PRO A CB  1 
ATOM   2866 C  CG  . PRO A 1 376 ? 5.117   -15.805 12.656  1.00 25.60 ?  378 PRO A CG  1 
ATOM   2867 C  CD  . PRO A 1 376 ? 5.877   -14.533 12.385  1.00 21.02 ?  378 PRO A CD  1 
ATOM   2868 N  N   . ALA A 1 377 ? 3.006   -13.345 15.968  1.00 14.80 ?  379 ALA A N   1 
ATOM   2869 C  CA  . ALA A 1 377 ? 3.008   -12.760 17.303  1.00 16.46 ?  379 ALA A CA  1 
ATOM   2870 C  C   . ALA A 1 377 ? 4.030   -13.440 18.207  1.00 16.48 ?  379 ALA A C   1 
ATOM   2871 O  O   . ALA A 1 377 ? 4.702   -12.778 19.007  1.00 15.93 ?  379 ALA A O   1 
ATOM   2872 C  CB  . ALA A 1 377 ? 1.611   -12.853 17.921  1.00 17.52 ?  379 ALA A CB  1 
ATOM   2873 N  N   . ALA A 1 378 ? 4.156   -14.764 18.102  1.00 15.11 ?  380 ALA A N   1 
ATOM   2874 C  CA  . ALA A 1 378 ? 5.057   -15.481 18.999  1.00 21.14 ?  380 ALA A CA  1 
ATOM   2875 C  C   . ALA A 1 378 ? 6.499   -15.038 18.797  1.00 24.17 ?  380 ALA A C   1 
ATOM   2876 O  O   . ALA A 1 378 ? 7.275   -14.958 19.758  1.00 22.76 ?  380 ALA A O   1 
ATOM   2877 C  CB  . ALA A 1 378 ? 4.928   -16.986 18.777  1.00 22.11 ?  380 ALA A CB  1 
ATOM   2878 N  N   . VAL A 1 379 ? 6.871   -14.741 17.552  1.00 18.66 ?  381 VAL A N   1 
ATOM   2879 C  CA  . VAL A 1 379 ? 8.212   -14.243 17.263  1.00 19.19 ?  381 VAL A CA  1 
ATOM   2880 C  C   . VAL A 1 379 ? 8.395   -12.838 17.816  1.00 17.81 ?  381 VAL A C   1 
ATOM   2881 O  O   . VAL A 1 379 ? 9.377   -12.558 18.511  1.00 15.41 ?  381 VAL A O   1 
ATOM   2882 C  CB  . VAL A 1 379 ? 8.484   -14.285 15.752  1.00 23.06 ?  381 VAL A CB  1 
ATOM   2883 C  CG1 . VAL A 1 379 ? 9.892   -13.808 15.465  1.00 18.63 ?  381 VAL A CG1 1 
ATOM   2884 C  CG2 . VAL A 1 379 ? 8.290   -15.703 15.232  1.00 26.24 ?  381 VAL A CG2 1 
ATOM   2885 N  N   . LEU A 1 380 ? 7.451   -11.936 17.514  1.00 15.36 ?  382 LEU A N   1 
ATOM   2886 C  CA  . LEU A 1 380 ? 7.550   -10.558 17.994  1.00 16.08 ?  382 LEU A CA  1 
ATOM   2887 C  C   . LEU A 1 380 ? 7.647   -10.496 19.513  1.00 16.89 ?  382 LEU A C   1 
ATOM   2888 O  O   . LEU A 1 380 ? 8.321   -9.611  20.060  1.00 16.96 ?  382 LEU A O   1 
ATOM   2889 C  CB  . LEU A 1 380 ? 6.343   -9.745  17.518  1.00 15.12 ?  382 LEU A CB  1 
ATOM   2890 C  CG  . LEU A 1 380 ? 6.338   -9.279  16.065  1.00 14.67 ?  382 LEU A CG  1 
ATOM   2891 C  CD1 . LEU A 1 380 ? 5.003   -8.610  15.733  1.00 17.13 ?  382 LEU A CD1 1 
ATOM   2892 C  CD2 . LEU A 1 380 ? 7.495   -8.331  15.804  1.00 15.04 ?  382 LEU A CD2 1 
ATOM   2893 N  N   . SER A 1 381 ? 6.984   -11.418 20.213  1.00 13.23 ?  383 SER A N   1 
ATOM   2894 C  CA  . SER A 1 381 ? 7.049   -11.397 21.664  1.00 15.69 ?  383 SER A CA  1 
ATOM   2895 C  C   . SER A 1 381 ? 8.438   -11.740 22.186  1.00 14.69 ?  383 SER A C   1 
ATOM   2896 O  O   . SER A 1 381 ? 8.710   -11.448 23.352  1.00 17.69 ?  383 SER A O   1 
ATOM   2897 C  CB  . SER A 1 381 ? 6.014   -12.356 22.261  1.00 20.69 ?  383 SER A CB  1 
ATOM   2898 O  OG  . SER A 1 381 ? 6.387   -13.696 22.011  1.00 27.89 ?  383 SER A OG  1 
ATOM   2899 N  N   . ARG A 1 382 ? 9.323   -12.304 21.360  1.00 16.35 ?  384 ARG A N   1 
ATOM   2900 C  CA  . ARG A 1 382 ? 10.709  -12.537 21.761  1.00 18.20 ?  384 ARG A CA  1 
ATOM   2901 C  C   . ARG A 1 382 ? 11.601  -11.356 21.415  1.00 16.71 ?  384 ARG A C   1 
ATOM   2902 O  O   . ARG A 1 382 ? 12.812  -11.395 21.676  1.00 20.98 ?  384 ARG A O   1 
ATOM   2903 C  CB  . ARG A 1 382 ? 11.260  -13.807 21.114  1.00 19.59 ?  384 ARG A CB  1 
ATOM   2904 C  CG  . ARG A 1 382 ? 10.565  -15.009 21.703  1.00 20.19 ?  384 ARG A CG  1 
ATOM   2905 C  CD  . ARG A 1 382 ? 11.183  -16.385 21.422  1.00 30.38 ?  384 ARG A CD  1 
ATOM   2906 N  NE  . ARG A 1 382 ? 10.133  -17.313 21.007  1.00 44.77 ?  384 ARG A NE  1 
ATOM   2907 C  CZ  . ARG A 1 382 ? 9.652   -17.376 19.775  1.00 46.30 ?  384 ARG A CZ  1 
ATOM   2908 N  NH1 . ARG A 1 382 ? 8.669   -18.212 19.509  1.00 41.39 ?  384 ARG A NH1 1 
ATOM   2909 N  NH2 . ARG A 1 382 ? 10.283  -16.752 18.776  1.00 47.43 ?  384 ARG A NH2 1 
ATOM   2910 N  N   . CYS A 1 383 ? 11.016  -10.294 20.865  1.00 12.90 ?  385 CYS A N   1 
ATOM   2911 C  CA  . CYS A 1 383 ? 11.744  -9.125  20.405  1.00 14.34 ?  385 CYS A CA  1 
ATOM   2912 C  C   . CYS A 1 383 ? 11.526  -7.920  21.306  1.00 16.24 ?  385 CYS A C   1 
ATOM   2913 O  O   . CYS A 1 383 ? 11.724  -6.791  20.865  1.00 11.48 ?  385 CYS A O   1 
ATOM   2914 C  CB  . CYS A 1 383 ? 11.320  -8.797  18.981  1.00 15.54 ?  385 CYS A CB  1 
ATOM   2915 S  SG  . CYS A 1 383 ? 11.782  -10.045 17.792  1.00 19.65 ?  385 CYS A SG  1 
ATOM   2916 N  N   . HIS A 1 384 ? 11.087  -8.139  22.548  1.00 12.98 ?  386 HIS A N   1 
ATOM   2917 C  CA  . HIS A 1 384 ? 10.992  -7.095  23.565  1.00 12.85 ?  386 HIS A CA  1 
ATOM   2918 C  C   . HIS A 1 384 ? 9.940   -6.057  23.217  1.00 14.44 ?  386 HIS A C   1 
ATOM   2919 O  O   . HIS A 1 384 ? 10.044  -4.893  23.612  1.00 13.46 ?  386 HIS A O   1 
ATOM   2920 C  CB  . HIS A 1 384 ? 12.356  -6.453  23.808  1.00 15.09 ?  386 HIS A CB  1 
ATOM   2921 C  CG  . HIS A 1 384 ? 13.401  -7.467  24.126  1.00 18.67 ?  386 HIS A CG  1 
ATOM   2922 N  ND1 . HIS A 1 384 ? 14.456  -7.745  23.285  1.00 20.64 ?  386 HIS A ND1 1 
ATOM   2923 C  CD2 . HIS A 1 384 ? 13.493  -8.343  25.153  1.00 17.60 ?  386 HIS A CD2 1 
ATOM   2924 C  CE1 . HIS A 1 384 ? 15.181  -8.721  23.805  1.00 19.19 ?  386 HIS A CE1 1 
ATOM   2925 N  NE2 . HIS A 1 384 ? 14.614  -9.103  24.935  1.00 22.64 ?  386 HIS A NE2 1 
ATOM   2926 N  N   . VAL A 1 385 ? 8.925   -6.483  22.465  1.00 11.93 ?  387 VAL A N   1 
ATOM   2927 C  CA  . VAL A 1 385 ? 7.735   -5.687  22.212  1.00 10.42 ?  387 VAL A CA  1 
ATOM   2928 C  C   . VAL A 1 385 ? 6.536   -6.590  22.495  1.00 13.84 ?  387 VAL A C   1 
ATOM   2929 O  O   . VAL A 1 385 ? 6.662   -7.817  22.586  1.00 14.67 ?  387 VAL A O   1 
ATOM   2930 C  CB  . VAL A 1 385 ? 7.702   -5.143  20.765  1.00 10.80 ?  387 VAL A CB  1 
ATOM   2931 C  CG1 . VAL A 1 385 ? 8.961   -4.304  20.473  1.00 9.99  ?  387 VAL A CG1 1 
ATOM   2932 C  CG2 . VAL A 1 385 ? 7.567   -6.296  19.770  1.00 12.43 ?  387 VAL A CG2 1 
ATOM   2933 N  N   . GLU A 1 386 ? 5.364   -5.966  22.688  1.00 11.07 ?  388 GLU A N   1 
ATOM   2934 C  CA  . GLU A 1 386 ? 4.148   -6.732  22.913  1.00 11.63 ?  388 GLU A CA  1 
ATOM   2935 C  C   . GLU A 1 386 ? 3.339   -6.799  21.629  1.00 10.06 ?  388 GLU A C   1 
ATOM   2936 O  O   . GLU A 1 386 ? 2.800   -5.771  21.203  1.00 13.18 ?  388 GLU A O   1 
ATOM   2937 C  CB  . GLU A 1 386 ? 3.311   -6.101  24.024  1.00 13.51 ?  388 GLU A CB  1 
ATOM   2938 C  CG  . GLU A 1 386 ? 2.013   -6.863  24.296  1.00 15.81 ?  388 GLU A CG  1 
ATOM   2939 C  CD  . GLU A 1 386 ? 0.994   -6.057  25.102  1.00 16.83 ?  388 GLU A CD  1 
ATOM   2940 O  OE1 . GLU A 1 386 ? -0.132  -6.556  25.314  1.00 21.10 ?  388 GLU A OE1 1 
ATOM   2941 O  OE2 . GLU A 1 386 ? 1.298   -4.918  25.508  1.00 18.82 ?  388 GLU A OE2 1 
ATOM   2942 N  N   . PRO A 1 387 ? 3.199   -7.959  20.985  1.00 11.24 ?  389 PRO A N   1 
ATOM   2943 C  CA  . PRO A 1 387 ? 2.343   -8.019  19.796  1.00 10.73 ?  389 PRO A CA  1 
ATOM   2944 C  C   . PRO A 1 387 ? 0.883   -7.820  20.192  1.00 13.32 ?  389 PRO A C   1 
ATOM   2945 O  O   . PRO A 1 387 ? 0.402   -8.409  21.165  1.00 13.43 ?  389 PRO A O   1 
ATOM   2946 C  CB  . PRO A 1 387 ? 2.599   -9.427  19.240  1.00 11.96 ?  389 PRO A CB  1 
ATOM   2947 C  CG  . PRO A 1 387 ? 3.009   -10.218 20.438  1.00 16.43 ?  389 PRO A CG  1 
ATOM   2948 C  CD  . PRO A 1 387 ? 3.809   -9.267  21.286  1.00 15.79 ?  389 PRO A CD  1 
ATOM   2949 N  N   . VAL A 1 388 ? 0.191   -6.955  19.455  1.00 11.68 ?  390 VAL A N   1 
ATOM   2950 C  CA  . VAL A 1 388 ? -1.243  -6.749  19.623  1.00 12.34 ?  390 VAL A CA  1 
ATOM   2951 C  C   . VAL A 1 388 ? -1.896  -6.870  18.250  1.00 12.52 ?  390 VAL A C   1 
ATOM   2952 O  O   . VAL A 1 388 ? -1.314  -6.466  17.238  1.00 11.42 ?  390 VAL A O   1 
ATOM   2953 C  CB  . VAL A 1 388 ? -1.554  -5.391  20.297  1.00 10.58 ?  390 VAL A CB  1 
ATOM   2954 C  CG1 . VAL A 1 388 ? -3.033  -5.243  20.563  1.00 10.34 ?  390 VAL A CG1 1 
ATOM   2955 C  CG2 . VAL A 1 388 ? -0.783  -5.253  21.632  1.00 11.80 ?  390 VAL A CG2 1 
ATOM   2956 N  N   . ALA A 1 389 ? -3.098  -7.457  18.206  1.00 11.83 ?  391 ALA A N   1 
ATOM   2957 C  CA  . ALA A 1 389 ? -3.680  -7.831  16.918  1.00 12.27 ?  391 ALA A CA  1 
ATOM   2958 C  C   . ALA A 1 389 ? -4.018  -6.621  16.057  1.00 11.50 ?  391 ALA A C   1 
ATOM   2959 O  O   . ALA A 1 389 ? -3.962  -6.708  14.823  1.00 12.82 ?  391 ALA A O   1 
ATOM   2960 C  CB  . ALA A 1 389 ? -4.934  -8.686  17.139  1.00 15.03 ?  391 ALA A CB  1 
ATOM   2961 N  N   . THR A 1 390 ? -4.418  -5.505  16.666  1.00 10.94 ?  392 THR A N   1 
ATOM   2962 C  CA  . THR A 1 390 ? -4.807  -4.329  15.892  1.00 11.81 ?  392 THR A CA  1 
ATOM   2963 C  C   . THR A 1 390 ? -4.357  -3.076  16.627  1.00 12.83 ?  392 THR A C   1 
ATOM   2964 O  O   . THR A 1 390 ? -4.171  -3.081  17.846  1.00 11.48 ?  392 THR A O   1 
ATOM   2965 C  CB  . THR A 1 390 ? -6.323  -4.257  15.627  1.00 10.68 ?  392 THR A CB  1 
ATOM   2966 O  OG1 . THR A 1 390 ? -7.005  -3.771  16.792  1.00 13.23 ?  392 THR A OG1 1 
ATOM   2967 C  CG2 . THR A 1 390 ? -6.924  -5.610  15.192  1.00 13.21 ?  392 THR A CG2 1 
ATOM   2968 N  N   . VAL A 1 391 ? -4.172  -1.994  15.863  1.00 10.51 ?  393 VAL A N   1 
ATOM   2969 C  CA  . VAL A 1 391 ? -3.813  -0.718  16.486  1.00 10.74 ?  393 VAL A CA  1 
ATOM   2970 C  C   . VAL A 1 391 ? -4.944  -0.228  17.373  1.00 11.30 ?  393 VAL A C   1 
ATOM   2971 O  O   . VAL A 1 391 ? -4.714  0.303   18.472  1.00 12.13 ?  393 VAL A O   1 
ATOM   2972 C  CB  . VAL A 1 391 ? -3.471  0.329   15.408  1.00 11.66 ?  393 VAL A CB  1 
ATOM   2973 C  CG1 . VAL A 1 391 ? -3.252  1.707   16.055  1.00 9.96  ?  393 VAL A CG1 1 
ATOM   2974 C  CG2 . VAL A 1 391 ? -2.236  -0.105  14.623  1.00 10.58 ?  393 VAL A CG2 1 
ATOM   2975 N  N   . GLU A 1 392 ? -6.184  -0.384  16.902  1.00 10.75 ?  394 GLU A N   1 
ATOM   2976 C  CA  . GLU A 1 392 ? -7.330  0.059   17.686  1.00 11.16 ?  394 GLU A CA  1 
ATOM   2977 C  C   . GLU A 1 392 ? -7.391  -0.671  19.028  1.00 11.10 ?  394 GLU A C   1 
ATOM   2978 O  O   . GLU A 1 392 ? -7.624  -0.051  20.075  1.00 12.88 ?  394 GLU A O   1 
ATOM   2979 C  CB  . GLU A 1 392 ? -8.611  -0.153  16.870  1.00 10.95 ?  394 GLU A CB  1 
ATOM   2980 C  CG  . GLU A 1 392 ? -9.859  0.346   17.563  1.00 17.09 ?  394 GLU A CG  1 
ATOM   2981 C  CD  . GLU A 1 392 ? -11.070 0.408   16.651  1.00 18.04 ?  394 GLU A CD  1 
ATOM   2982 O  OE1 . GLU A 1 392 ? -10.935 0.175   15.419  1.00 14.04 ?  394 GLU A OE1 1 
ATOM   2983 O  OE2 . GLU A 1 392 ? -12.166 0.700   17.185  1.00 17.85 ?  394 GLU A OE2 1 
ATOM   2984 N  N   . LEU A 1 393 ? -7.146  -1.981  19.025  1.00 10.63 ?  395 LEU A N   1 
ATOM   2985 C  CA  . LEU A 1 393 ? -7.091  -2.727  20.283  1.00 14.69 ?  395 LEU A CA  1 
ATOM   2986 C  C   . LEU A 1 393 ? -5.930  -2.254  21.152  1.00 13.51 ?  395 LEU A C   1 
ATOM   2987 O  O   . LEU A 1 393 ? -6.081  -2.043  22.362  1.00 13.00 ?  395 LEU A O   1 
ATOM   2988 C  CB  . LEU A 1 393 ? -6.972  -4.227  19.994  1.00 13.82 ?  395 LEU A CB  1 
ATOM   2989 C  CG  . LEU A 1 393 ? -6.745  -5.149  21.194  1.00 21.00 ?  395 LEU A CG  1 
ATOM   2990 C  CD1 . LEU A 1 393 ? -7.912  -5.062  22.164  1.00 17.66 ?  395 LEU A CD1 1 
ATOM   2991 C  CD2 . LEU A 1 393 ? -6.555  -6.583  20.720  1.00 14.86 ?  395 LEU A CD2 1 
ATOM   2992 N  N   . ALA A 1 394 ? -4.752  -2.099  20.552  1.00 8.04  ?  396 ALA A N   1 
ATOM   2993 C  CA  . ALA A 1 394 ? -3.580  -1.644  21.301  1.00 11.14 ?  396 ALA A CA  1 
ATOM   2994 C  C   . ALA A 1 394 ? -3.837  -0.310  22.004  1.00 10.64 ?  396 ALA A C   1 
ATOM   2995 O  O   . ALA A 1 394 ? -3.457  -0.120  23.167  1.00 12.57 ?  396 ALA A O   1 
ATOM   2996 C  CB  . ALA A 1 394 ? -2.377  -1.536  20.349  1.00 10.03 ?  396 ALA A CB  1 
ATOM   2997 N  N   . VAL A 1 395 ? -4.456  0.638   21.295  1.00 10.02 ?  397 VAL A N   1 
ATOM   2998 C  CA  . VAL A 1 395 ? -4.768  1.941   21.883  1.00 9.67  ?  397 VAL A CA  1 
ATOM   2999 C  C   . VAL A 1 395 ? -5.775  1.788   23.020  1.00 11.95 ?  397 VAL A C   1 
ATOM   3000 O  O   . VAL A 1 395 ? -5.605  2.364   24.105  1.00 11.70 ?  397 VAL A O   1 
ATOM   3001 C  CB  . VAL A 1 395 ? -5.274  2.902   20.793  1.00 12.44 ?  397 VAL A CB  1 
ATOM   3002 C  CG1 . VAL A 1 395 ? -5.867  4.175   21.390  1.00 14.62 ?  397 VAL A CG1 1 
ATOM   3003 C  CG2 . VAL A 1 395 ? -4.114  3.242   19.825  1.00 11.29 ?  397 VAL A CG2 1 
ATOM   3004 N  N   . ALA A 1 396 ? -6.832  0.997   22.791  1.00 11.36 ?  398 ALA A N   1 
ATOM   3005 C  CA  . ALA A 1 396 ? -7.810  0.747   23.848  1.00 13.15 ?  398 ALA A CA  1 
ATOM   3006 C  C   . ALA A 1 396 ? -7.141  0.155   25.086  1.00 13.56 ?  398 ALA A C   1 
ATOM   3007 O  O   . ALA A 1 396 ? -7.435  0.570   26.214  1.00 16.14 ?  398 ALA A O   1 
ATOM   3008 C  CB  . ALA A 1 396 ? -8.919  -0.171  23.336  1.00 15.79 ?  398 ALA A CB  1 
ATOM   3009 N  N   . GLN A 1 397 ? -6.214  -0.793  24.893  1.00 12.70 ?  399 GLN A N   1 
ATOM   3010 C  CA  . GLN A 1 397 ? -5.494  -1.373  26.027  1.00 13.68 ?  399 GLN A CA  1 
ATOM   3011 C  C   . GLN A 1 397 ? -4.680  -0.317  26.760  1.00 15.11 ?  399 GLN A C   1 
ATOM   3012 O  O   . GLN A 1 397 ? -4.713  -0.239  27.993  1.00 16.72 ?  399 GLN A O   1 
ATOM   3013 C  CB  . GLN A 1 397 ? -4.580  -2.513  25.573  1.00 12.84 ?  399 GLN A CB  1 
ATOM   3014 C  CG  . GLN A 1 397 ? -5.293  -3.766  25.056  1.00 17.21 ?  399 GLN A CG  1 
ATOM   3015 C  CD  . GLN A 1 397 ? -4.338  -4.741  24.415  1.00 19.74 ?  399 GLN A CD  1 
ATOM   3016 O  OE1 . GLN A 1 397 ? -3.198  -4.390  24.110  1.00 17.43 ?  399 GLN A OE1 1 
ATOM   3017 N  NE2 . GLN A 1 397 ? -4.791  -5.974  24.209  1.00 18.36 ?  399 GLN A NE2 1 
ATOM   3018 N  N   . ALA A 1 398 ? -3.934  0.504   26.011  1.00 14.70 ?  400 ALA A N   1 
ATOM   3019 C  CA  . ALA A 1 398 ? -3.088  1.519   26.633  1.00 14.43 ?  400 ALA A CA  1 
ATOM   3020 C  C   . ALA A 1 398 ? -3.923  2.561   27.367  1.00 17.76 ?  400 ALA A C   1 
ATOM   3021 O  O   . ALA A 1 398 ? -3.554  3.009   28.457  1.00 18.89 ?  400 ALA A O   1 
ATOM   3022 C  CB  . ALA A 1 398 ? -2.211  2.179   25.569  1.00 15.52 ?  400 ALA A CB  1 
ATOM   3023 N  N   . LEU A 1 399 ? -5.052  2.962   26.783  1.00 14.27 ?  401 LEU A N   1 
ATOM   3024 C  CA  . LEU A 1 399 ? -5.884  3.985   27.407  1.00 16.47 ?  401 LEU A CA  1 
ATOM   3025 C  C   . LEU A 1 399 ? -6.486  3.499   28.718  1.00 21.53 ?  401 LEU A C   1 
ATOM   3026 O  O   . LEU A 1 399 ? -6.667  4.292   29.650  1.00 21.46 ?  401 LEU A O   1 
ATOM   3027 C  CB  . LEU A 1 399 ? -6.973  4.404   26.427  1.00 16.34 ?  401 LEU A CB  1 
ATOM   3028 C  CG  . LEU A 1 399 ? -6.460  5.327   25.314  1.00 18.55 ?  401 LEU A CG  1 
ATOM   3029 C  CD1 . LEU A 1 399 ? -7.600  5.832   24.427  1.00 18.80 ?  401 LEU A CD1 1 
ATOM   3030 C  CD2 . LEU A 1 399 ? -5.649  6.506   25.871  1.00 25.08 ?  401 LEU A CD2 1 
ATOM   3031 N  N   . GLU A 1 400 ? -6.806  2.210   28.812  1.00 19.04 ?  402 GLU A N   1 
ATOM   3032 C  CA  . GLU A 1 400 ? -7.269  1.671   30.087  1.00 19.45 ?  402 GLU A CA  1 
ATOM   3033 C  C   . GLU A 1 400 ? -6.163  1.731   31.130  1.00 25.97 ?  402 GLU A C   1 
ATOM   3034 O  O   . GLU A 1 400 ? -6.425  1.998   32.309  1.00 25.26 ?  402 GLU A O   1 
ATOM   3035 C  CB  . GLU A 1 400 ? -7.761  0.234   29.901  1.00 23.39 ?  402 GLU A CB  1 
ATOM   3036 N  N   . GLN A 1 401 ? -4.915  1.503   30.708  1.00 20.52 ?  403 GLN A N   1 
ATOM   3037 C  CA  . GLN A 1 401 ? -3.791  1.502   31.642  1.00 18.68 ?  403 GLN A CA  1 
ATOM   3038 C  C   . GLN A 1 401 ? -3.510  2.900   32.187  1.00 24.82 ?  403 GLN A C   1 
ATOM   3039 O  O   . GLN A 1 401 ? -3.197  3.055   33.372  1.00 29.29 ?  403 GLN A O   1 
ATOM   3040 C  CB  . GLN A 1 401 ? -2.562  0.909   30.946  1.00 22.05 ?  403 GLN A CB  1 
ATOM   3041 C  CG  . GLN A 1 401 ? -1.220  1.132   31.635  1.00 27.17 ?  403 GLN A CG  1 
ATOM   3042 C  CD  . GLN A 1 401 ? -0.073  0.475   30.859  1.00 32.66 ?  403 GLN A CD  1 
ATOM   3043 O  OE1 . GLN A 1 401 ? -0.270  -0.020  29.741  1.00 36.75 ?  403 GLN A OE1 1 
ATOM   3044 N  NE2 . GLN A 1 401 ? 1.123   0.474   31.444  1.00 33.18 ?  403 GLN A NE2 1 
ATOM   3045 N  N   . TYR A 1 402 ? -3.651  3.935   31.357  1.00 18.73 ?  404 TYR A N   1 
ATOM   3046 C  CA  . TYR A 1 402 ? -3.267  5.284   31.757  1.00 18.82 ?  404 TYR A CA  1 
ATOM   3047 C  C   . TYR A 1 402 ? -4.431  6.137   32.247  1.00 22.40 ?  404 TYR A C   1 
ATOM   3048 O  O   . TYR A 1 402 ? -4.193  7.176   32.874  1.00 23.23 ?  404 TYR A O   1 
ATOM   3049 C  CB  . TYR A 1 402 ? -2.549  5.981   30.592  1.00 17.83 ?  404 TYR A CB  1 
ATOM   3050 C  CG  . TYR A 1 402 ? -1.259  5.264   30.217  1.00 17.14 ?  404 TYR A CG  1 
ATOM   3051 C  CD1 . TYR A 1 402 ? -0.217  5.152   31.127  1.00 18.80 ?  404 TYR A CD1 1 
ATOM   3052 C  CD2 . TYR A 1 402 ? -1.117  4.636   28.988  1.00 18.54 ?  404 TYR A CD2 1 
ATOM   3053 C  CE1 . TYR A 1 402 ? 0.956   4.475   30.801  1.00 18.40 ?  404 TYR A CE1 1 
ATOM   3054 C  CE2 . TYR A 1 402 ? 0.047   3.955   28.655  1.00 15.01 ?  404 TYR A CE2 1 
ATOM   3055 C  CZ  . TYR A 1 402 ? 1.075   3.877   29.566  1.00 17.69 ?  404 TYR A CZ  1 
ATOM   3056 O  OH  . TYR A 1 402 ? 2.221   3.197   29.238  1.00 18.06 ?  404 TYR A OH  1 
ATOM   3057 N  N   . GLY A 1 403 ? -5.667  5.731   31.987  1.00 21.81 ?  405 GLY A N   1 
ATOM   3058 C  CA  . GLY A 1 403 ? -6.811  6.365   32.602  1.00 26.01 ?  405 GLY A CA  1 
ATOM   3059 C  C   . GLY A 1 403 ? -7.484  7.410   31.735  1.00 30.87 ?  405 GLY A C   1 
ATOM   3060 O  O   . GLY A 1 403 ? -7.119  7.633   30.573  1.00 23.38 ?  405 GLY A O   1 
ATOM   3061 N  N   . PRO A 1 404 ? -8.485  8.091   32.304  1.00 26.06 ?  406 PRO A N   1 
ATOM   3062 C  CA  . PRO A 1 404 ? -9.368  8.937   31.492  1.00 27.76 ?  406 PRO A CA  1 
ATOM   3063 C  C   . PRO A 1 404 ? -8.762  10.261  31.054  1.00 24.39 ?  406 PRO A C   1 
ATOM   3064 O  O   . PRO A 1 404 ? -9.337  10.914  30.174  1.00 25.26 ?  406 PRO A O   1 
ATOM   3065 C  CB  . PRO A 1 404 ? -10.562 9.154   32.430  1.00 26.72 ?  406 PRO A CB  1 
ATOM   3066 C  CG  . PRO A 1 404 ? -9.894  9.256   33.771  1.00 23.96 ?  406 PRO A CG  1 
ATOM   3067 C  CD  . PRO A 1 404 ? -8.880  8.116   33.726  1.00 28.26 ?  406 PRO A CD  1 
ATOM   3068 N  N   . GLU A 1 405 ? -7.632  10.680  31.629  1.00 20.79 ?  407 GLU A N   1 
ATOM   3069 C  CA  . GLU A 1 405 ? -6.951  11.891  31.195  1.00 23.00 ?  407 GLU A CA  1 
ATOM   3070 C  C   . GLU A 1 405 ? -5.951  11.637  30.068  1.00 24.50 ?  407 GLU A C   1 
ATOM   3071 O  O   . GLU A 1 405 ? -5.434  12.598  29.485  1.00 27.49 ?  407 GLU A O   1 
ATOM   3072 C  CB  . GLU A 1 405 ? -6.230  12.537  32.383  1.00 28.07 ?  407 GLU A CB  1 
ATOM   3073 N  N   . ALA A 1 406 ? -5.677  10.377  29.746  1.00 22.78 ?  408 ALA A N   1 
ATOM   3074 C  CA  . ALA A 1 406 ? -4.618  10.049  28.797  1.00 19.79 ?  408 ALA A CA  1 
ATOM   3075 C  C   . ALA A 1 406 ? -4.981  10.509  27.389  1.00 21.85 ?  408 ALA A C   1 
ATOM   3076 O  O   . ALA A 1 406 ? -6.146  10.453  26.982  1.00 21.57 ?  408 ALA A O   1 
ATOM   3077 C  CB  . ALA A 1 406 ? -4.354  8.545   28.808  1.00 14.74 ?  408 ALA A CB  1 
ATOM   3078 N  N   . ARG A 1 407 ? -3.969  10.952  26.642  1.00 17.25 ?  409 ARG A N   1 
ATOM   3079 C  CA  . ARG A 1 407 ? -4.143  11.464  25.291  1.00 17.19 ?  409 ARG A CA  1 
ATOM   3080 C  C   . ARG A 1 407 ? -3.335  10.614  24.312  1.00 13.60 ?  409 ARG A C   1 
ATOM   3081 O  O   . ARG A 1 407 ? -2.346  9.976   24.685  1.00 14.67 ?  409 ARG A O   1 
ATOM   3082 C  CB  . ARG A 1 407 ? -3.699  12.929  25.191  1.00 20.13 ?  409 ARG A CB  1 
ATOM   3083 C  CG  . ARG A 1 407 ? -4.594  13.916  25.959  1.00 29.82 ?  409 ARG A CG  1 
ATOM   3084 C  CD  . ARG A 1 407 ? -6.026  13.944  25.423  1.00 31.65 ?  409 ARG A CD  1 
ATOM   3085 N  NE  . ARG A 1 407 ? -6.990  14.375  26.444  1.00 44.69 ?  409 ARG A NE  1 
ATOM   3086 C  CZ  . ARG A 1 407 ? -7.883  13.577  27.027  1.00 40.06 ?  409 ARG A CZ  1 
ATOM   3087 N  NH1 . ARG A 1 407 ? -7.934  12.295  26.708  1.00 43.26 ?  409 ARG A NH1 1 
ATOM   3088 N  NH2 . ARG A 1 407 ? -8.722  14.055  27.938  1.00 39.41 ?  409 ARG A NH2 1 
ATOM   3089 N  N   . VAL A 1 408 ? -3.756  10.628  23.050  1.00 12.97 ?  410 VAL A N   1 
ATOM   3090 C  CA  . VAL A 1 408 ? -3.116  9.854   21.988  1.00 12.30 ?  410 VAL A CA  1 
ATOM   3091 C  C   . VAL A 1 408 ? -2.557  10.834  20.965  1.00 11.13 ?  410 VAL A C   1 
ATOM   3092 O  O   . VAL A 1 408 ? -3.273  11.731  20.514  1.00 12.99 ?  410 VAL A O   1 
ATOM   3093 C  CB  . VAL A 1 408 ? -4.113  8.884   21.319  1.00 15.94 ?  410 VAL A CB  1 
ATOM   3094 C  CG1 . VAL A 1 408 ? -3.420  8.103   20.191  1.00 14.90 ?  410 VAL A CG1 1 
ATOM   3095 C  CG2 . VAL A 1 408 ? -4.736  7.935   22.361  1.00 15.89 ?  410 VAL A CG2 1 
ATOM   3096 N  N   . ALA A 1 409 ? -1.289  10.670  20.591  1.00 12.42 ?  411 ALA A N   1 
ATOM   3097 C  CA  . ALA A 1 409 ? -0.757  11.364  19.424  1.00 10.21 ?  411 ALA A CA  1 
ATOM   3098 C  C   . ALA A 1 409 ? -0.533  10.329  18.331  1.00 10.49 ?  411 ALA A C   1 
ATOM   3099 O  O   . ALA A 1 409 ? -0.240  9.170   18.625  1.00 12.50 ?  411 ALA A O   1 
ATOM   3100 C  CB  . ALA A 1 409 ? 0.555   12.098  19.732  1.00 10.52 ?  411 ALA A CB  1 
ATOM   3101 N  N   . VAL A 1 410 ? -0.681  10.734  17.072  1.00 11.37 ?  412 VAL A N   1 
ATOM   3102 C  CA  . VAL A 1 410 ? -0.511  9.807   15.956  1.00 13.31 ?  412 VAL A CA  1 
ATOM   3103 C  C   . VAL A 1 410 ? 0.392   10.411  14.888  1.00 11.70 ?  412 VAL A C   1 
ATOM   3104 O  O   . VAL A 1 410 ? 0.285   11.601  14.561  1.00 10.99 ?  412 VAL A O   1 
ATOM   3105 C  CB  . VAL A 1 410 ? -1.874  9.367   15.376  1.00 12.20 ?  412 VAL A CB  1 
ATOM   3106 C  CG1 . VAL A 1 410 ? -2.652  10.556  14.833  1.00 13.97 ?  412 VAL A CG1 1 
ATOM   3107 C  CG2 . VAL A 1 410 ? -1.659  8.306   14.280  1.00 13.34 ?  412 VAL A CG2 1 
ATOM   3108 N  N   . ILE A 1 411 ? 1.300   9.585   14.361  1.00 10.36 ?  413 ILE A N   1 
ATOM   3109 C  CA  . ILE A 1 411 ? 2.348   10.027  13.441  1.00 9.07  ?  413 ILE A CA  1 
ATOM   3110 C  C   . ILE A 1 411 ? 2.254   9.128   12.210  1.00 8.17  ?  413 ILE A C   1 
ATOM   3111 O  O   . ILE A 1 411 ? 2.953   8.103   12.147  1.00 8.58  ?  413 ILE A O   1 
ATOM   3112 C  CB  . ILE A 1 411 ? 3.750   9.902   14.056  1.00 8.61  ?  413 ILE A CB  1 
ATOM   3113 C  CG1 . ILE A 1 411 ? 3.830   10.631  15.404  1.00 10.50 ?  413 ILE A CG1 1 
ATOM   3114 C  CG2 . ILE A 1 411 ? 4.727   10.642  13.137  1.00 9.41  ?  413 ILE A CG2 1 
ATOM   3115 C  CD1 . ILE A 1 411 ? 5.103   10.290  16.197  1.00 12.40 ?  413 ILE A CD1 1 
ATOM   3116 N  N   . PRO A 1 412 ? 1.377   9.431   11.247  1.00 9.69  ?  414 PRO A N   1 
ATOM   3117 C  CA  . PRO A 1 412 ? 1.155   8.485   10.134  1.00 9.09  ?  414 PRO A CA  1 
ATOM   3118 C  C   . PRO A 1 412 ? 2.411   8.125   9.354   1.00 10.38 ?  414 PRO A C   1 
ATOM   3119 O  O   . PRO A 1 412 ? 2.556   6.964   8.941   1.00 9.92  ?  414 PRO A O   1 
ATOM   3120 C  CB  . PRO A 1 412 ? 0.126   9.221   9.265   1.00 10.25 ?  414 PRO A CB  1 
ATOM   3121 C  CG  . PRO A 1 412 ? -0.640  10.050  10.260  1.00 11.01 ?  414 PRO A CG  1 
ATOM   3122 C  CD  . PRO A 1 412 ? 0.421   10.556  11.213  1.00 9.83  ?  414 PRO A CD  1 
ATOM   3123 N  N   . LYS A 1 413 ? 3.327   9.069   9.147   1.00 7.25  ?  415 LYS A N   1 
ATOM   3124 C  CA  A LYS A 1 413 ? 4.541   8.788   8.386   0.70 9.89  ?  415 LYS A CA  1 
ATOM   3125 C  CA  B LYS A 1 413 ? 4.555   8.840   8.394   0.30 9.98  ?  415 LYS A CA  1 
ATOM   3126 C  C   . LYS A 1 413 ? 5.723   8.407   9.280   1.00 9.99  ?  415 LYS A C   1 
ATOM   3127 O  O   . LYS A 1 413 ? 6.858   8.312   8.792   1.00 9.48  ?  415 LYS A O   1 
ATOM   3128 C  CB  A LYS A 1 413 ? 4.902   9.988   7.495   0.70 10.72 ?  415 LYS A CB  1 
ATOM   3129 C  CB  B LYS A 1 413 ? 4.946   10.106  7.617   0.30 10.81 ?  415 LYS A CB  1 
ATOM   3130 C  CG  A LYS A 1 413 ? 4.205   10.021  6.119   0.70 13.17 ?  415 LYS A CG  1 
ATOM   3131 C  CG  B LYS A 1 413 ? 4.379   10.222  6.199   0.30 13.26 ?  415 LYS A CG  1 
ATOM   3132 C  CD  A LYS A 1 413 ? 2.700   9.798   6.187   0.70 14.38 ?  415 LYS A CD  1 
ATOM   3133 C  CD  B LYS A 1 413 ? 2.932   9.768   6.103   0.30 14.20 ?  415 LYS A CD  1 
ATOM   3134 C  CE  A LYS A 1 413 ? 2.031   10.083  4.830   0.70 14.87 ?  415 LYS A CE  1 
ATOM   3135 C  CE  B LYS A 1 413 ? 2.266   10.308  4.840   0.30 15.26 ?  415 LYS A CE  1 
ATOM   3136 N  NZ  A LYS A 1 413 ? 2.350   9.049   3.792   0.70 11.25 ?  415 LYS A NZ  1 
ATOM   3137 N  NZ  B LYS A 1 413 ? 0.850   9.868   4.718   0.30 18.93 ?  415 LYS A NZ  1 
ATOM   3138 N  N   . GLY A 1 414 ? 5.482   8.176   10.566  1.00 9.07  ?  416 GLY A N   1 
ATOM   3139 C  CA  . GLY A 1 414 ? 6.470   7.614   11.457  1.00 9.77  ?  416 GLY A CA  1 
ATOM   3140 C  C   . GLY A 1 414 ? 7.794   8.351   11.460  1.00 8.17  ?  416 GLY A C   1 
ATOM   3141 O  O   . GLY A 1 414 ? 7.850   9.561   11.677  1.00 8.11  ?  416 GLY A O   1 
ATOM   3142 N  N   . PRO A 1 415 ? 8.893   7.636   11.191  1.00 7.86  ?  417 PRO A N   1 
ATOM   3143 C  CA  . PRO A 1 415 ? 10.224  8.245   11.334  1.00 8.74  ?  417 PRO A CA  1 
ATOM   3144 C  C   . PRO A 1 415 ? 10.553  9.275   10.265  1.00 8.66  ?  417 PRO A C   1 
ATOM   3145 O  O   . PRO A 1 415 ? 11.650  9.836   10.297  1.00 11.23 ?  417 PRO A O   1 
ATOM   3146 C  CB  . PRO A 1 415 ? 11.168  7.032   11.245  1.00 10.16 ?  417 PRO A CB  1 
ATOM   3147 C  CG  . PRO A 1 415 ? 10.423  6.086   10.328  1.00 7.97  ?  417 PRO A CG  1 
ATOM   3148 C  CD  . PRO A 1 415 ? 8.975   6.229   10.752  1.00 8.87  ?  417 PRO A CD  1 
ATOM   3149 N  N   . TYR A 1 416 ? 9.671   9.526   9.306   1.00 7.43  ?  418 TYR A N   1 
ATOM   3150 C  CA  . TYR A 1 416 ? 9.905   10.625  8.376   1.00 9.27  ?  418 TYR A CA  1 
ATOM   3151 C  C   . TYR A 1 416 ? 9.387   11.950  8.923   1.00 11.65 ?  418 TYR A C   1 
ATOM   3152 O  O   . TYR A 1 416 ? 9.527   12.982  8.256   1.00 11.64 ?  418 TYR A O   1 
ATOM   3153 C  CB  . TYR A 1 416 ? 9.282   10.317  7.012   1.00 8.86  ?  418 TYR A CB  1 
ATOM   3154 C  CG  . TYR A 1 416 ? 9.944   9.185   6.241   1.00 7.37  ?  418 TYR A CG  1 
ATOM   3155 C  CD1 . TYR A 1 416 ? 9.331   8.666   5.101   1.00 9.27  ?  418 TYR A CD1 1 
ATOM   3156 C  CD2 . TYR A 1 416 ? 11.160  8.634   6.638   1.00 10.33 ?  418 TYR A CD2 1 
ATOM   3157 C  CE1 . TYR A 1 416 ? 9.906   7.628   4.372   1.00 7.69  ?  418 TYR A CE1 1 
ATOM   3158 C  CE2 . TYR A 1 416 ? 11.751  7.582   5.898   1.00 10.83 ?  418 TYR A CE2 1 
ATOM   3159 C  CZ  . TYR A 1 416 ? 11.099  7.090   4.769   1.00 11.86 ?  418 TYR A CZ  1 
ATOM   3160 O  OH  . TYR A 1 416 ? 11.627  6.057   4.013   1.00 8.86  ?  418 TYR A OH  1 
ATOM   3161 N  N   . VAL A 1 417 ? 8.820   11.935  10.131  1.00 8.89  ?  419 VAL A N   1 
ATOM   3162 C  CA  . VAL A 1 417 ? 8.408   13.129  10.859  1.00 9.15  ?  419 VAL A CA  1 
ATOM   3163 C  C   . VAL A 1 417 ? 9.331   13.284  12.060  1.00 13.37 ?  419 VAL A C   1 
ATOM   3164 O  O   . VAL A 1 417 ? 9.848   12.297  12.598  1.00 12.73 ?  419 VAL A O   1 
ATOM   3165 C  CB  . VAL A 1 417 ? 6.933   13.012  11.302  1.00 10.54 ?  419 VAL A CB  1 
ATOM   3166 C  CG1 . VAL A 1 417 ? 6.509   14.217  12.143  1.00 11.57 ?  419 VAL A CG1 1 
ATOM   3167 C  CG2 . VAL A 1 417 ? 6.030   12.835  10.078  1.00 11.40 ?  419 VAL A CG2 1 
ATOM   3168 N  N   . LEU A 1 418 ? 9.557   14.532  12.474  1.00 11.08 ?  420 LEU A N   1 
ATOM   3169 C  CA  . LEU A 1 418 ? 10.392  14.828  13.639  1.00 10.51 ?  420 LEU A CA  1 
ATOM   3170 C  C   . LEU A 1 418 ? 9.490   15.391  14.731  1.00 11.22 ?  420 LEU A C   1 
ATOM   3171 O  O   . LEU A 1 418 ? 9.279   16.611  14.799  1.00 12.34 ?  420 LEU A O   1 
ATOM   3172 C  CB  . LEU A 1 418 ? 11.492  15.826  13.264  1.00 16.70 ?  420 LEU A CB  1 
ATOM   3173 C  CG  . LEU A 1 418 ? 12.640  16.143  14.220  1.00 23.00 ?  420 LEU A CG  1 
ATOM   3174 C  CD1 . LEU A 1 418 ? 13.407  14.884  14.547  1.00 19.86 ?  420 LEU A CD1 1 
ATOM   3175 C  CD2 . LEU A 1 418 ? 13.580  17.178  13.601  1.00 19.83 ?  420 LEU A CD2 1 
ATOM   3176 N  N   . PRO A 1 419 ? 8.926   14.552  15.605  1.00 10.92 ?  421 PRO A N   1 
ATOM   3177 C  CA  . PRO A 1 419 ? 7.968   15.050  16.599  1.00 14.53 ?  421 PRO A CA  1 
ATOM   3178 C  C   . PRO A 1 419 ? 8.708   15.789  17.697  1.00 11.79 ?  421 PRO A C   1 
ATOM   3179 O  O   . PRO A 1 419 ? 9.762   15.348  18.157  1.00 14.70 ?  421 PRO A O   1 
ATOM   3180 C  CB  . PRO A 1 419 ? 7.352   13.766  17.172  1.00 18.07 ?  421 PRO A CB  1 
ATOM   3181 C  CG  . PRO A 1 419 ? 7.670   12.708  16.196  1.00 21.25 ?  421 PRO A CG  1 
ATOM   3182 C  CD  . PRO A 1 419 ? 8.996   13.080  15.618  1.00 13.71 ?  421 PRO A CD  1 
ATOM   3183 N  N   . VAL A 1 420 ? 8.135   16.901  18.163  1.00 14.42 ?  422 VAL A N   1 
ATOM   3184 C  CA  . VAL A 1 420 ? 8.767   17.663  19.234  1.00 14.25 ?  422 VAL A CA  1 
ATOM   3185 C  C   . VAL A 1 420 ? 7.702   18.159  20.200  1.00 14.32 ?  422 VAL A C   1 
ATOM   3186 O  O   . VAL A 1 420 ? 6.522   18.294  19.864  1.00 16.64 ?  422 VAL A O   1 
ATOM   3187 C  CB  . VAL A 1 420 ? 9.600   18.863  18.725  1.00 19.44 ?  422 VAL A CB  1 
ATOM   3188 C  CG1 . VAL A 1 420 ? 10.775  18.396  17.853  1.00 23.35 ?  422 VAL A CG1 1 
ATOM   3189 C  CG2 . VAL A 1 420 ? 8.728   19.851  17.999  1.00 18.49 ?  422 VAL A CG2 1 
ATOM   3190 N  N   . VAL A 1 421 ? 8.141   18.412  21.422  1.00 16.74 ?  423 VAL A N   1 
ATOM   3191 C  CA  . VAL A 1 421 ? 7.307   19.048  22.432  1.00 18.94 ?  423 VAL A CA  1 
ATOM   3192 C  C   . VAL A 1 421 ? 7.605   20.540  22.381  1.00 20.57 ?  423 VAL A C   1 
ATOM   3193 O  O   . VAL A 1 421 ? 8.764   20.951  22.496  1.00 19.80 ?  423 VAL A O   1 
ATOM   3194 C  CB  . VAL A 1 421 ? 7.595   18.479  23.827  1.00 17.28 ?  423 VAL A CB  1 
ATOM   3195 C  CG1 . VAL A 1 421 ? 6.920   19.331  24.905  1.00 20.25 ?  423 VAL A CG1 1 
ATOM   3196 C  CG2 . VAL A 1 421 ? 7.172   17.016  23.916  1.00 16.52 ?  423 VAL A CG2 1 
ATOM   3197 N  N   . ASP A 1 422 ? 6.574   21.348  22.177  1.00 21.90 ?  424 ASP A N   1 
ATOM   3198 C  CA  . ASP A 1 422 ? 6.725   22.802  22.205  1.00 30.11 ?  424 ASP A CA  1 
ATOM   3199 C  C   . ASP A 1 422 ? 5.790   23.333  23.280  1.00 25.54 ?  424 ASP A C   1 
ATOM   3200 O  O   . ASP A 1 422 ? 4.582   23.496  23.029  1.00 28.25 ?  424 ASP A O   1 
ATOM   3201 C  CB  . ASP A 1 422 ? 6.414   23.428  20.846  1.00 26.46 ?  424 ASP A CB  1 
ATOM   3202 C  CG  . ASP A 1 422 ? 6.776   24.906  20.786  1.00 35.34 ?  424 ASP A CG  1 
ATOM   3203 O  OD1 . ASP A 1 422 ? 6.762   25.470  19.674  1.00 33.91 ?  424 ASP A OD1 1 
ATOM   3204 O  OD2 . ASP A 1 422 ? 7.083   25.504  21.843  1.00 34.00 ?  424 ASP A OD2 1 
ATOM   3205 N  N   . PRO A 1 423 ? 6.298   23.598  24.486  1.00 26.50 ?  425 PRO A N   1 
ATOM   3206 C  CA  . PRO A 1 423 ? 5.418   24.058  25.574  1.00 30.41 ?  425 PRO A CA  1 
ATOM   3207 C  C   . PRO A 1 423 ? 4.722   25.375  25.276  1.00 34.39 ?  425 PRO A C   1 
ATOM   3208 O  O   . PRO A 1 423 ? 3.613   25.604  25.779  1.00 41.61 ?  425 PRO A O   1 
ATOM   3209 C  CB  . PRO A 1 423 ? 6.381   24.177  26.768  1.00 30.54 ?  425 PRO A CB  1 
ATOM   3210 C  CG  . PRO A 1 423 ? 7.554   23.285  26.399  1.00 34.83 ?  425 PRO A CG  1 
ATOM   3211 C  CD  . PRO A 1 423 ? 7.700   23.479  24.922  1.00 27.69 ?  425 PRO A CD  1 
ATOM   3212 N  N   . THR A 1 424 ? 5.328   26.241  24.458  1.00 34.12 ?  426 THR A N   1 
ATOM   3213 C  CA  . THR A 1 424 ? 4.696   27.503  24.083  1.00 34.63 ?  426 THR A CA  1 
ATOM   3214 C  C   . THR A 1 424 ? 3.409   27.301  23.294  1.00 41.16 ?  426 THR A C   1 
ATOM   3215 O  O   . THR A 1 424 ? 2.673   28.270  23.081  1.00 42.79 ?  426 THR A O   1 
ATOM   3216 C  CB  . THR A 1 424 ? 5.669   28.352  23.262  1.00 30.70 ?  426 THR A CB  1 
ATOM   3217 N  N   . LEU A 1 425 ? 3.116   26.075  22.878  1.00 36.21 ?  427 LEU A N   1 
ATOM   3218 C  CA  . LEU A 1 425 ? 2.005   25.788  21.983  1.00 38.45 ?  427 LEU A CA  1 
ATOM   3219 C  C   . LEU A 1 425 ? 0.699   25.579  22.750  1.00 40.87 ?  427 LEU A C   1 
ATOM   3220 O  O   . LEU A 1 425 ? 0.667   25.661  23.983  1.00 42.71 ?  427 LEU A O   1 
ATOM   3221 C  CB  . LEU A 1 425 ? 2.348   24.556  21.139  1.00 30.55 ?  427 LEU A CB  1 
ATOM   3222 C  CG  . LEU A 1 425 ? 1.544   24.177  19.909  1.00 41.27 ?  427 LEU A CG  1 
ATOM   3223 C  CD1 . LEU A 1 425 ? 1.712   25.228  18.823  1.00 39.52 ?  427 LEU A CD1 1 
ATOM   3224 C  CD2 . LEU A 1 425 ? 2.018   22.817  19.438  1.00 28.93 ?  427 LEU A CD2 1 
ATOM   3225 N  N   . ARG B 1 1   ? 54.187  4.039   -51.033 1.00 26.62 ?  3   ARG B N   1 
ATOM   3226 C  CA  . ARG B 1 1   ? 53.353  4.772   -51.993 1.00 25.46 ?  3   ARG B CA  1 
ATOM   3227 C  C   . ARG B 1 1   ? 51.928  4.207   -52.071 1.00 22.01 ?  3   ARG B C   1 
ATOM   3228 O  O   . ARG B 1 1   ? 51.717  3.057   -52.452 1.00 22.10 ?  3   ARG B O   1 
ATOM   3229 C  CB  . ARG B 1 1   ? 53.988  4.759   -53.381 1.00 31.76 ?  3   ARG B CB  1 
ATOM   3230 N  N   . VAL B 1 2   ? 50.940  5.028   -51.730 1.00 15.15 ?  4   VAL B N   1 
ATOM   3231 C  CA  . VAL B 1 2   ? 49.547  4.602   -51.768 1.00 14.07 ?  4   VAL B CA  1 
ATOM   3232 C  C   . VAL B 1 2   ? 48.712  5.757   -52.305 1.00 15.15 ?  4   VAL B C   1 
ATOM   3233 O  O   . VAL B 1 2   ? 49.028  6.928   -52.081 1.00 16.62 ?  4   VAL B O   1 
ATOM   3234 C  CB  . VAL B 1 2   ? 49.054  4.137   -50.369 1.00 19.87 ?  4   VAL B CB  1 
ATOM   3235 C  CG1 . VAL B 1 2   ? 48.952  5.308   -49.407 1.00 18.17 ?  4   VAL B CG1 1 
ATOM   3236 C  CG2 . VAL B 1 2   ? 47.735  3.411   -50.476 1.00 21.79 ?  4   VAL B CG2 1 
ATOM   3237 N  N   . THR B 1 3   ? 47.647  5.428   -53.035 1.00 14.51 ?  5   THR B N   1 
ATOM   3238 C  CA  . THR B 1 3   ? 46.710  6.429   -53.532 1.00 11.93 ?  5   THR B CA  1 
ATOM   3239 C  C   . THR B 1 3   ? 45.462  6.388   -52.656 1.00 13.08 ?  5   THR B C   1 
ATOM   3240 O  O   . THR B 1 3   ? 44.683  5.432   -52.727 1.00 15.30 ?  5   THR B O   1 
ATOM   3241 C  CB  . THR B 1 3   ? 46.346  6.181   -54.995 1.00 14.94 ?  5   THR B CB  1 
ATOM   3242 O  OG1 . THR B 1 3   ? 47.536  6.141   -55.793 1.00 17.56 ?  5   THR B OG1 1 
ATOM   3243 C  CG2 . THR B 1 3   ? 45.456  7.315   -55.503 1.00 13.31 ?  5   THR B CG2 1 
ATOM   3244 N  N   . LEU B 1 4   ? 45.271  7.418   -51.835 1.00 10.93 ?  6   LEU B N   1 
ATOM   3245 C  CA  . LEU B 1 4   ? 44.027  7.576   -51.087 1.00 12.06 ?  6   LEU B CA  1 
ATOM   3246 C  C   . LEU B 1 4   ? 42.918  8.103   -51.989 1.00 11.85 ?  6   LEU B C   1 
ATOM   3247 O  O   . LEU B 1 4   ? 43.155  8.916   -52.884 1.00 13.82 ?  6   LEU B O   1 
ATOM   3248 C  CB  . LEU B 1 4   ? 44.206  8.576   -49.952 1.00 11.22 ?  6   LEU B CB  1 
ATOM   3249 C  CG  . LEU B 1 4   ? 45.350  8.282   -48.986 1.00 12.90 ?  6   LEU B CG  1 
ATOM   3250 C  CD1 . LEU B 1 4   ? 45.384  9.341   -47.883 1.00 13.60 ?  6   LEU B CD1 1 
ATOM   3251 C  CD2 . LEU B 1 4   ? 45.209  6.862   -48.410 1.00 12.40 ?  6   LEU B CD2 1 
ATOM   3252 N  N   . ASP B 1 5   ? 41.686  7.704   -51.692 1.00 11.38 ?  7   ASP B N   1 
ATOM   3253 C  CA  . ASP B 1 5   ? 40.551  8.293   -52.392 1.00 10.36 ?  7   ASP B CA  1 
ATOM   3254 C  C   . ASP B 1 5   ? 40.483  9.777   -52.006 1.00 12.05 ?  7   ASP B C   1 
ATOM   3255 O  O   . ASP B 1 5   ? 40.661  10.130  -50.838 1.00 11.34 ?  7   ASP B O   1 
ATOM   3256 C  CB  . ASP B 1 5   ? 39.258  7.585   -51.984 1.00 12.80 ?  7   ASP B CB  1 
ATOM   3257 C  CG  . ASP B 1 5   ? 39.012  6.299   -52.768 1.00 17.53 ?  7   ASP B CG  1 
ATOM   3258 O  OD1 . ASP B 1 5   ? 39.783  5.971   -53.699 1.00 17.13 ?  7   ASP B OD1 1 
ATOM   3259 O  OD2 . ASP B 1 5   ? 38.002  5.630   -52.472 1.00 16.48 ?  7   ASP B OD2 1 
ATOM   3260 N  N   . TYR B 1 6   ? 40.259  10.663  -52.982 1.00 9.99  ?  8   TYR B N   1 
ATOM   3261 C  CA  . TYR B 1 6   ? 40.313  12.107  -52.703 1.00 12.02 ?  8   TYR B CA  1 
ATOM   3262 C  C   . TYR B 1 6   ? 39.648  12.861  -53.847 1.00 11.81 ?  8   TYR B C   1 
ATOM   3263 O  O   . TYR B 1 6   ? 40.239  12.960  -54.919 1.00 11.19 ?  8   TYR B O   1 
ATOM   3264 C  CB  . TYR B 1 6   ? 41.771  12.553  -52.534 1.00 11.32 ?  8   TYR B CB  1 
ATOM   3265 C  CG  . TYR B 1 6   ? 41.940  13.975  -52.031 1.00 13.07 ?  8   TYR B CG  1 
ATOM   3266 C  CD1 . TYR B 1 6   ? 41.977  14.252  -50.662 1.00 12.36 ?  8   TYR B CD1 1 
ATOM   3267 C  CD2 . TYR B 1 6   ? 42.080  15.034  -52.920 1.00 12.87 ?  8   TYR B CD2 1 
ATOM   3268 C  CE1 . TYR B 1 6   ? 42.132  15.536  -50.197 1.00 12.92 ?  8   TYR B CE1 1 
ATOM   3269 C  CE2 . TYR B 1 6   ? 42.230  16.322  -52.465 1.00 16.26 ?  8   TYR B CE2 1 
ATOM   3270 C  CZ  . TYR B 1 6   ? 42.256  16.572  -51.100 1.00 14.81 ?  8   TYR B CZ  1 
ATOM   3271 O  OH  . TYR B 1 6   ? 42.414  17.863  -50.653 1.00 15.85 ?  8   TYR B OH  1 
ATOM   3272 N  N   . GLY B 1 7   ? 38.443  13.393  -53.623 1.00 13.24 ?  9   GLY B N   1 
ATOM   3273 C  CA  . GLY B 1 7   ? 37.700  14.024  -54.713 1.00 14.73 ?  9   GLY B CA  1 
ATOM   3274 C  C   . GLY B 1 7   ? 37.668  13.166  -55.968 1.00 13.31 ?  9   GLY B C   1 
ATOM   3275 O  O   . GLY B 1 7   ? 37.494  11.944  -55.912 1.00 13.36 ?  9   GLY B O   1 
ATOM   3276 N  N   . LYS B 1 8   ? 37.878  13.803  -57.124 1.00 12.50 ?  10  LYS B N   1 
ATOM   3277 C  CA  . LYS B 1 8   ? 37.858  13.095  -58.404 1.00 12.86 ?  10  LYS B CA  1 
ATOM   3278 C  C   . LYS B 1 8   ? 39.234  12.592  -58.834 1.00 16.24 ?  10  LYS B C   1 
ATOM   3279 O  O   . LYS B 1 8   ? 39.341  11.931  -59.876 1.00 14.99 ?  10  LYS B O   1 
ATOM   3280 C  CB  . LYS B 1 8   ? 37.277  14.004  -59.488 1.00 17.32 ?  10  LYS B CB  1 
ATOM   3281 C  CG  . LYS B 1 8   ? 35.938  14.607  -59.091 1.00 15.93 ?  10  LYS B CG  1 
ATOM   3282 C  CD  . LYS B 1 8   ? 35.354  15.488  -60.168 1.00 18.48 ?  10  LYS B CD  1 
ATOM   3283 C  CE  . LYS B 1 8   ? 33.932  15.902  -59.795 1.00 25.82 ?  10  LYS B CE  1 
ATOM   3284 N  NZ  . LYS B 1 8   ? 33.122  16.283  -60.986 1.00 36.49 ?  10  LYS B NZ  1 
ATOM   3285 N  N   . THR B 1 9   ? 40.280  12.854  -58.048 1.00 14.16 ?  11  THR B N   1 
ATOM   3286 C  CA  . THR B 1 9   ? 41.653  12.608  -58.470 1.00 12.60 ?  11  THR B CA  1 
ATOM   3287 C  C   . THR B 1 9   ? 42.359  11.503  -57.713 1.00 14.75 ?  11  THR B C   1 
ATOM   3288 O  O   . THR B 1 9   ? 43.273  10.884  -58.262 1.00 14.95 ?  11  THR B O   1 
ATOM   3289 C  CB  . THR B 1 9   ? 42.491  13.882  -58.299 1.00 15.00 ?  11  THR B CB  1 
ATOM   3290 O  OG1 . THR B 1 9   ? 42.467  14.272  -56.914 1.00 12.10 ?  11  THR B OG1 1 
ATOM   3291 C  CG2 . THR B 1 9   ? 41.941  15.015  -59.163 1.00 16.53 ?  11  THR B CG2 1 
ATOM   3292 N  N   . GLY B 1 10  ? 41.986  11.257  -56.462 1.00 13.30 ?  12  GLY B N   1 
ATOM   3293 C  CA  . GLY B 1 10  ? 42.851  10.531  -55.558 1.00 12.86 ?  12  GLY B CA  1 
ATOM   3294 C  C   . GLY B 1 10  ? 44.008  11.412  -55.102 1.00 12.08 ?  12  GLY B C   1 
ATOM   3295 O  O   . GLY B 1 10  ? 44.174  12.549  -55.533 1.00 13.16 ?  12  GLY B O   1 
ATOM   3296 N  N   . LEU B 1 11  ? 44.809  10.875  -54.180 1.00 11.20 ?  13  LEU B N   1 
ATOM   3297 C  CA  . LEU B 1 11  ? 45.914  11.613  -53.561 1.00 11.72 ?  13  LEU B CA  1 
ATOM   3298 C  C   . LEU B 1 11  ? 47.054  10.641  -53.323 1.00 14.01 ?  13  LEU B C   1 
ATOM   3299 O  O   . LEU B 1 11  ? 46.855  9.624   -52.654 1.00 13.67 ?  13  LEU B O   1 
ATOM   3300 C  CB  . LEU B 1 11  ? 45.471  12.258  -52.236 1.00 11.65 ?  13  LEU B CB  1 
ATOM   3301 C  CG  . LEU B 1 11  ? 46.476  13.146  -51.495 1.00 11.60 ?  13  LEU B CG  1 
ATOM   3302 C  CD1 . LEU B 1 11  ? 46.666  14.488  -52.209 1.00 12.46 ?  13  LEU B CD1 1 
ATOM   3303 C  CD2 . LEU B 1 11  ? 46.063  13.352  -50.021 1.00 14.65 ?  13  LEU B CD2 1 
ATOM   3304 N  N   . ASN B 1 12  ? 48.237  10.938  -53.876 1.00 11.56 ?  14  ASN B N   1 
ATOM   3305 C  CA  . ASN B 1 12  ? 49.365  10.013  -53.817 1.00 12.27 ?  14  ASN B CA  1 
ATOM   3306 C  C   . ASN B 1 12  ? 50.188  10.336  -52.578 1.00 14.54 ?  14  ASN B C   1 
ATOM   3307 O  O   . ASN B 1 12  ? 50.750  11.433  -52.472 1.00 14.38 ?  14  ASN B O   1 
ATOM   3308 C  CB  . ASN B 1 12  ? 50.227  10.097  -55.081 1.00 14.93 ?  14  ASN B CB  1 
ATOM   3309 C  CG  . ASN B 1 12  ? 49.711  9.190   -56.172 1.00 27.10 ?  14  ASN B CG  1 
ATOM   3310 O  OD1 . ASN B 1 12  ? 48.875  8.325   -55.909 1.00 25.50 ?  14  ASN B OD1 1 
ATOM   3311 N  ND2 . ASN B 1 12  ? 50.181  9.390   -57.404 1.00 20.26 ?  14  ASN B ND2 1 
ATOM   3312 N  N   . VAL B 1 13  ? 50.262  9.374   -51.658 1.00 13.28 ?  15  VAL B N   1 
ATOM   3313 C  CA  . VAL B 1 13  ? 50.880  9.540   -50.349 1.00 15.13 ?  15  VAL B CA  1 
ATOM   3314 C  C   . VAL B 1 13  ? 52.023  8.544   -50.234 1.00 15.14 ?  15  VAL B C   1 
ATOM   3315 O  O   . VAL B 1 13  ? 51.891  7.392   -50.664 1.00 16.10 ?  15  VAL B O   1 
ATOM   3316 C  CB  . VAL B 1 13  ? 49.849  9.306   -49.222 1.00 15.09 ?  15  VAL B CB  1 
ATOM   3317 C  CG1 . VAL B 1 13  ? 50.520  9.341   -47.846 1.00 18.34 ?  15  VAL B CG1 1 
ATOM   3318 C  CG2 . VAL B 1 13  ? 48.721  10.307  -49.312 1.00 13.06 ?  15  VAL B CG2 1 
ATOM   3319 N  N   . ASP B 1 14  ? 53.143  8.978   -49.661 1.00 13.33 ?  16  ASP B N   1 
ATOM   3320 C  CA  . ASP B 1 14  ? 54.230  8.065   -49.330 1.00 14.10 ?  16  ASP B CA  1 
ATOM   3321 C  C   . ASP B 1 14  ? 54.233  7.823   -47.820 1.00 16.70 ?  16  ASP B C   1 
ATOM   3322 O  O   . ASP B 1 14  ? 54.364  8.768   -47.037 1.00 21.90 ?  16  ASP B O   1 
ATOM   3323 C  CB  . ASP B 1 14  ? 55.582  8.617   -49.779 1.00 17.40 ?  16  ASP B CB  1 
ATOM   3324 C  CG  . ASP B 1 14  ? 56.573  7.512   -50.089 1.00 32.58 ?  16  ASP B CG  1 
ATOM   3325 O  OD1 . ASP B 1 14  ? 56.911  6.750   -49.163 1.00 34.65 ?  16  ASP B OD1 1 
ATOM   3326 O  OD2 . ASP B 1 14  ? 57.018  7.411   -51.254 1.00 42.45 ?  16  ASP B OD2 1 
ATOM   3327 N  N   . LEU B 1 15  ? 54.075  6.568   -47.424 1.00 15.08 ?  17  LEU B N   1 
ATOM   3328 C  CA  . LEU B 1 15  ? 54.015  6.176   -46.028 1.00 16.21 ?  17  LEU B CA  1 
ATOM   3329 C  C   . LEU B 1 15  ? 55.285  5.414   -45.656 1.00 17.34 ?  17  LEU B C   1 
ATOM   3330 O  O   . LEU B 1 15  ? 55.897  4.775   -46.518 1.00 18.91 ?  17  LEU B O   1 
ATOM   3331 C  CB  . LEU B 1 15  ? 52.789  5.291   -45.771 1.00 14.03 ?  17  LEU B CB  1 
ATOM   3332 C  CG  . LEU B 1 15  ? 51.445  6.023   -45.841 1.00 18.42 ?  17  LEU B CG  1 
ATOM   3333 C  CD1 . LEU B 1 15  ? 50.295  5.068   -45.568 1.00 15.85 ?  17  LEU B CD1 1 
ATOM   3334 C  CD2 . LEU B 1 15  ? 51.399  7.223   -44.888 1.00 15.28 ?  17  LEU B CD2 1 
ATOM   3335 N  N   . PRO B 1 16  ? 55.707  5.447   -44.393 1.00 16.07 ?  18  PRO B N   1 
ATOM   3336 C  CA  . PRO B 1 16  ? 56.999  4.823   -44.033 1.00 18.04 ?  18  PRO B CA  1 
ATOM   3337 C  C   . PRO B 1 16  ? 56.958  3.302   -44.147 1.00 20.79 ?  18  PRO B C   1 
ATOM   3338 O  O   . PRO B 1 16  ? 56.120  2.645   -43.530 1.00 19.24 ?  18  PRO B O   1 
ATOM   3339 C  CB  . PRO B 1 16  ? 57.212  5.274   -42.581 1.00 21.62 ?  18  PRO B CB  1 
ATOM   3340 C  CG  . PRO B 1 16  ? 56.315  6.482   -42.431 1.00 24.55 ?  18  PRO B CG  1 
ATOM   3341 C  CD  . PRO B 1 16  ? 55.103  6.112   -43.229 1.00 19.70 ?  18  PRO B CD  1 
ATOM   3342 N  N   . ASP B 1 17  ? 57.898  2.741   -44.924 1.00 20.47 ?  19  ASP B N   1 
ATOM   3343 C  CA  . ASP B 1 17  ? 57.931  1.290   -45.139 1.00 26.08 ?  19  ASP B CA  1 
ATOM   3344 C  C   . ASP B 1 17  ? 58.058  0.516   -43.834 1.00 21.04 ?  19  ASP B C   1 
ATOM   3345 O  O   . ASP B 1 17  ? 57.480  -0.566  -43.691 1.00 29.23 ?  19  ASP B O   1 
ATOM   3346 C  CB  . ASP B 1 17  ? 59.095  0.897   -46.054 1.00 29.81 ?  19  ASP B CB  1 
ATOM   3347 C  CG  . ASP B 1 17  ? 59.069  1.606   -47.386 1.00 40.57 ?  19  ASP B CG  1 
ATOM   3348 O  OD1 . ASP B 1 17  ? 60.164  1.867   -47.929 1.00 48.99 ?  19  ASP B OD1 1 
ATOM   3349 O  OD2 . ASP B 1 17  ? 57.966  1.871   -47.903 1.00 30.06 ?  19  ASP B OD2 1 
ATOM   3350 N  N   . ASP B 1 18  ? 58.832  1.033   -42.883 1.00 26.55 ?  20  ASP B N   1 
ATOM   3351 C  CA  . ASP B 1 18  ? 59.116  0.267   -41.675 1.00 28.40 ?  20  ASP B CA  1 
ATOM   3352 C  C   . ASP B 1 18  ? 57.952  0.240   -40.697 1.00 26.13 ?  20  ASP B C   1 
ATOM   3353 O  O   . ASP B 1 18  ? 57.975  -0.558  -39.750 1.00 23.15 ?  20  ASP B O   1 
ATOM   3354 C  CB  . ASP B 1 18  ? 60.368  0.825   -40.974 1.00 24.76 ?  20  ASP B CB  1 
ATOM   3355 C  CG  . ASP B 1 18  ? 60.245  2.308   -40.630 1.00 35.22 ?  20  ASP B CG  1 
ATOM   3356 O  OD1 . ASP B 1 18  ? 60.772  2.727   -39.575 1.00 41.44 ?  20  ASP B OD1 1 
ATOM   3357 O  OD2 . ASP B 1 18  ? 59.639  3.064   -41.421 1.00 38.50 ?  20  ASP B OD2 1 
ATOM   3358 N  N   . ARG B 1 19  ? 56.934  1.072   -40.898 1.00 18.61 ?  21  ARG B N   1 
ATOM   3359 C  CA  . ARG B 1 19  ? 55.873  1.226   -39.916 1.00 17.66 ?  21  ARG B CA  1 
ATOM   3360 C  C   . ARG B 1 19  ? 54.488  0.867   -40.429 1.00 15.00 ?  21  ARG B C   1 
ATOM   3361 O  O   . ARG B 1 19  ? 53.569  0.752   -39.614 1.00 16.60 ?  21  ARG B O   1 
ATOM   3362 C  CB  . ARG B 1 19  ? 55.803  2.676   -39.409 1.00 18.89 ?  21  ARG B CB  1 
ATOM   3363 C  CG  . ARG B 1 19  ? 57.119  3.321   -39.066 1.00 22.28 ?  21  ARG B CG  1 
ATOM   3364 C  CD  . ARG B 1 19  ? 57.620  2.864   -37.714 1.00 26.25 ?  21  ARG B CD  1 
ATOM   3365 N  NE  . ARG B 1 19  ? 58.550  3.835   -37.154 1.00 34.54 ?  21  ARG B NE  1 
ATOM   3366 C  CZ  . ARG B 1 19  ? 58.321  4.547   -36.055 1.00 29.17 ?  21  ARG B CZ  1 
ATOM   3367 N  NH1 . ARG B 1 19  ? 57.198  4.373   -35.362 1.00 22.22 ?  21  ARG B NH1 1 
ATOM   3368 N  NH2 . ARG B 1 19  ? 59.236  5.410   -35.630 1.00 32.23 ?  21  ARG B NH2 1 
ATOM   3369 N  N   . THR B 1 20  ? 54.304  0.714   -41.739 1.00 14.87 ?  22  THR B N   1 
ATOM   3370 C  CA  . THR B 1 20  ? 52.978  0.694   -42.343 1.00 14.94 ?  22  THR B CA  1 
ATOM   3371 C  C   . THR B 1 20  ? 52.595  -0.726  -42.726 1.00 19.80 ?  22  THR B C   1 
ATOM   3372 O  O   . THR B 1 20  ? 53.338  -1.400  -43.447 1.00 18.10 ?  22  THR B O   1 
ATOM   3373 C  CB  . THR B 1 20  ? 52.931  1.602   -43.579 1.00 15.24 ?  22  THR B CB  1 
ATOM   3374 O  OG1 . THR B 1 20  ? 53.420  2.906   -43.241 1.00 18.68 ?  22  THR B OG1 1 
ATOM   3375 C  CG2 . THR B 1 20  ? 51.495  1.708   -44.125 1.00 13.61 ?  22  THR B CG2 1 
ATOM   3376 N  N   . LEU B 1 21  ? 51.431  -1.163  -42.247 1.00 15.68 ?  23  LEU B N   1 
ATOM   3377 C  CA  . LEU B 1 21  ? 50.877  -2.459  -42.585 1.00 14.87 ?  23  LEU B CA  1 
ATOM   3378 C  C   . LEU B 1 21  ? 50.398  -2.465  -44.041 1.00 17.64 ?  23  LEU B C   1 
ATOM   3379 O  O   . LEU B 1 21  ? 50.179  -1.409  -44.643 1.00 15.97 ?  23  LEU B O   1 
ATOM   3380 C  CB  . LEU B 1 21  ? 49.719  -2.779  -41.641 1.00 15.20 ?  23  LEU B CB  1 
ATOM   3381 C  CG  . LEU B 1 21  ? 50.010  -3.345  -40.238 1.00 22.53 ?  23  LEU B CG  1 
ATOM   3382 C  CD1 . LEU B 1 21  ? 50.939  -2.452  -39.441 1.00 26.13 ?  23  LEU B CD1 1 
ATOM   3383 C  CD2 . LEU B 1 21  ? 48.723  -3.478  -39.486 1.00 21.80 ?  23  LEU B CD2 1 
ATOM   3384 N  N   . PRO B 1 22  ? 50.239  -3.639  -44.638 1.00 19.13 ?  24  PRO B N   1 
ATOM   3385 C  CA  . PRO B 1 22  ? 49.649  -3.703  -45.980 1.00 20.15 ?  24  PRO B CA  1 
ATOM   3386 C  C   . PRO B 1 22  ? 48.317  -2.970  -46.004 1.00 15.57 ?  24  PRO B C   1 
ATOM   3387 O  O   . PRO B 1 22  ? 47.551  -3.057  -45.037 1.00 17.79 ?  24  PRO B O   1 
ATOM   3388 C  CB  . PRO B 1 22  ? 49.471  -5.211  -46.200 1.00 23.91 ?  24  PRO B CB  1 
ATOM   3389 C  CG  . PRO B 1 22  ? 50.622  -5.791  -45.424 1.00 24.17 ?  24  PRO B CG  1 
ATOM   3390 C  CD  . PRO B 1 22  ? 50.628  -4.978  -44.154 1.00 22.27 ?  24  PRO B CD  1 
ATOM   3391 N  N   . PRO B 1 23  ? 48.024  -2.214  -47.065 1.00 15.48 ?  25  PRO B N   1 
ATOM   3392 C  CA  . PRO B 1 23  ? 46.787  -1.417  -47.086 1.00 13.98 ?  25  PRO B CA  1 
ATOM   3393 C  C   . PRO B 1 23  ? 45.555  -2.289  -46.910 1.00 15.47 ?  25  PRO B C   1 
ATOM   3394 O  O   . PRO B 1 23  ? 45.505  -3.431  -47.371 1.00 15.06 ?  25  PRO B O   1 
ATOM   3395 C  CB  . PRO B 1 23  ? 46.807  -0.760  -48.473 1.00 12.93 ?  25  PRO B CB  1 
ATOM   3396 C  CG  . PRO B 1 23  ? 48.265  -0.729  -48.841 1.00 19.51 ?  25  PRO B CG  1 
ATOM   3397 C  CD  . PRO B 1 23  ? 48.804  -2.032  -48.299 1.00 17.74 ?  25  PRO B CD  1 
ATOM   3398 N  N   . LEU B 1 24  ? 44.566  -1.740  -46.209 1.00 13.04 ?  26  LEU B N   1 
ATOM   3399 C  CA  . LEU B 1 24  ? 43.283  -2.399  -45.992 1.00 12.80 ?  26  LEU B CA  1 
ATOM   3400 C  C   . LEU B 1 24  ? 42.401  -2.100  -47.199 1.00 14.79 ?  26  LEU B C   1 
ATOM   3401 O  O   . LEU B 1 24  ? 42.021  -0.953  -47.429 1.00 14.13 ?  26  LEU B O   1 
ATOM   3402 C  CB  . LEU B 1 24  ? 42.636  -1.914  -44.697 1.00 13.94 ?  26  LEU B CB  1 
ATOM   3403 C  CG  . LEU B 1 24  ? 43.179  -2.557  -43.420 1.00 19.25 ?  26  LEU B CG  1 
ATOM   3404 C  CD1 . LEU B 1 24  ? 44.573  -2.106  -43.146 1.00 22.15 ?  26  LEU B CD1 1 
ATOM   3405 C  CD2 . LEU B 1 24  ? 42.298  -2.190  -42.245 1.00 23.94 ?  26  LEU B CD2 1 
ATOM   3406 N  N   . THR B 1 25  ? 42.108  -3.126  -47.990 1.00 15.09 ?  27  THR B N   1 
ATOM   3407 C  CA  . THR B 1 25  ? 41.371  -2.964  -49.230 1.00 14.86 ?  27  THR B CA  1 
ATOM   3408 C  C   . THR B 1 25  ? 40.260  -3.998  -49.268 1.00 16.60 ?  27  THR B C   1 
ATOM   3409 O  O   . THR B 1 25  ? 40.325  -5.019  -48.580 1.00 19.27 ?  27  THR B O   1 
ATOM   3410 C  CB  . THR B 1 25  ? 42.275  -3.137  -50.468 1.00 23.56 ?  27  THR B CB  1 
ATOM   3411 O  OG1 . THR B 1 25  ? 42.905  -4.421  -50.421 1.00 22.99 ?  27  THR B OG1 1 
ATOM   3412 C  CG2 . THR B 1 25  ? 43.358  -2.070  -50.521 1.00 22.34 ?  27  THR B CG2 1 
ATOM   3413 N  N   . ILE B 1 26  ? 39.236  -3.743  -50.088 1.00 17.83 ?  28  ILE B N   1 
ATOM   3414 C  CA  . ILE B 1 26  ? 38.157  -4.718  -50.144 1.00 16.95 ?  28  ILE B CA  1 
ATOM   3415 C  C   . ILE B 1 26  ? 38.643  -5.893  -50.981 1.00 16.18 ?  28  ILE B C   1 
ATOM   3416 O  O   . ILE B 1 26  ? 39.490  -5.739  -51.866 1.00 21.80 ?  28  ILE B O   1 
ATOM   3417 C  CB  . ILE B 1 26  ? 36.845  -4.136  -50.701 1.00 27.58 ?  28  ILE B CB  1 
ATOM   3418 C  CG1 . ILE B 1 26  ? 36.880  -4.018  -52.201 1.00 24.22 ?  28  ILE B CG1 1 
ATOM   3419 C  CG2 . ILE B 1 26  ? 36.611  -2.721  -50.170 1.00 24.65 ?  28  ILE B CG2 1 
ATOM   3420 C  CD1 . ILE B 1 26  ? 35.538  -3.615  -52.734 1.00 25.49 ?  28  ILE B CD1 1 
ATOM   3421 N  N   . ARG B 1 27  ? 38.137  -7.081  -50.667 1.00 20.28 ?  29  ARG B N   1 
ATOM   3422 C  CA  . ARG B 1 27  ? 38.586  -8.289  -51.341 1.00 16.22 ?  29  ARG B CA  1 
ATOM   3423 C  C   . ARG B 1 27  ? 38.266  -8.213  -52.838 1.00 17.44 ?  29  ARG B C   1 
ATOM   3424 O  O   . ARG B 1 27  ? 37.235  -7.666  -53.238 1.00 17.82 ?  29  ARG B O   1 
ATOM   3425 C  CB  . ARG B 1 27  ? 37.918  -9.516  -50.724 1.00 22.48 ?  29  ARG B CB  1 
ATOM   3426 N  N   . PRO B 1 28  ? 39.139  -8.749  -53.693 1.00 17.53 ?  30  PRO B N   1 
ATOM   3427 C  CA  . PRO B 1 28  ? 38.968  -8.568  -55.156 1.00 15.73 ?  30  PRO B CA  1 
ATOM   3428 C  C   . PRO B 1 28  ? 37.990  -9.519  -55.844 1.00 20.82 ?  30  PRO B C   1 
ATOM   3429 O  O   . PRO B 1 28  ? 38.356  -10.432 -56.584 1.00 28.81 ?  30  PRO B O   1 
ATOM   3430 C  CB  . PRO B 1 28  ? 40.393  -8.774  -55.680 1.00 20.57 ?  30  PRO B CB  1 
ATOM   3431 C  CG  . PRO B 1 28  ? 40.998  -9.742  -54.721 1.00 21.06 ?  30  PRO B CG  1 
ATOM   3432 C  CD  . PRO B 1 28  ? 40.412  -9.412  -53.360 1.00 18.62 ?  30  PRO B CD  1 
ATOM   3433 N  N   . ALA B 1 29  ? 36.697  -9.264  -55.656 1.00 17.26 ?  31  ALA B N   1 
ATOM   3434 C  CA  . ALA B 1 29  ? 35.652  -10.055 -56.290 1.00 13.15 ?  31  ALA B CA  1 
ATOM   3435 C  C   . ALA B 1 29  ? 35.518  -9.675  -57.764 1.00 11.29 ?  31  ALA B C   1 
ATOM   3436 O  O   . ALA B 1 29  ? 35.811  -8.544  -58.152 1.00 13.44 ?  31  ALA B O   1 
ATOM   3437 C  CB  . ALA B 1 29  ? 34.314  -9.838  -55.587 1.00 15.66 ?  31  ALA B CB  1 
ATOM   3438 N  N   . PRO B 1 30  ? 35.079  -10.594 -58.612 1.00 14.20 ?  32  PRO B N   1 
ATOM   3439 C  CA  . PRO B 1 30  ? 34.968  -10.268 -60.034 1.00 10.72 ?  32  PRO B CA  1 
ATOM   3440 C  C   . PRO B 1 30  ? 33.844  -9.281  -60.298 1.00 12.49 ?  32  PRO B C   1 
ATOM   3441 O  O   . PRO B 1 30  ? 32.696  -9.501  -59.879 1.00 14.91 ?  32  PRO B O   1 
ATOM   3442 C  CB  . PRO B 1 30  ? 34.688  -11.632 -60.685 1.00 17.43 ?  32  PRO B CB  1 
ATOM   3443 C  CG  . PRO B 1 30  ? 34.033  -12.422 -59.604 1.00 20.33 ?  32  PRO B CG  1 
ATOM   3444 C  CD  . PRO B 1 30  ? 34.771  -12.011 -58.350 1.00 12.81 ?  32  PRO B CD  1 
ATOM   3445 N  N   . PRO B 1 31  ? 34.136  -8.173  -60.980 1.00 12.25 ?  33  PRO B N   1 
ATOM   3446 C  CA  . PRO B 1 31  ? 33.057  -7.315  -61.472 1.00 14.87 ?  33  PRO B CA  1 
ATOM   3447 C  C   . PRO B 1 31  ? 32.146  -8.089  -62.400 1.00 13.70 ?  33  PRO B C   1 
ATOM   3448 O  O   . PRO B 1 31  ? 32.558  -9.066  -63.033 1.00 14.05 ?  33  PRO B O   1 
ATOM   3449 C  CB  . PRO B 1 31  ? 33.798  -6.209  -62.234 1.00 14.93 ?  33  PRO B CB  1 
ATOM   3450 C  CG  . PRO B 1 31  ? 35.133  -6.187  -61.625 1.00 17.37 ?  33  PRO B CG  1 
ATOM   3451 C  CD  . PRO B 1 31  ? 35.452  -7.630  -61.353 1.00 13.31 ?  33  PRO B CD  1 
ATOM   3452 N  N   . LEU B 1 32  ? 30.897  -7.644  -62.471 1.00 11.22 ?  34  LEU B N   1 
ATOM   3453 C  CA  . LEU B 1 32  ? 30.013  -8.113  -63.529 1.00 13.41 ?  34  LEU B CA  1 
ATOM   3454 C  C   . LEU B 1 32  ? 30.453  -7.507  -64.850 1.00 15.74 ?  34  LEU B C   1 
ATOM   3455 O  O   . LEU B 1 32  ? 30.695  -6.301  -64.951 1.00 16.35 ?  34  LEU B O   1 
ATOM   3456 C  CB  . LEU B 1 32  ? 28.558  -7.751  -63.238 1.00 10.94 ?  34  LEU B CB  1 
ATOM   3457 C  CG  . LEU B 1 32  ? 28.039  -8.135  -61.852 1.00 17.54 ?  34  LEU B CG  1 
ATOM   3458 C  CD1 . LEU B 1 32  ? 26.588  -7.738  -61.698 1.00 13.76 ?  34  LEU B CD1 1 
ATOM   3459 C  CD2 . LEU B 1 32  ? 28.216  -9.623  -61.627 1.00 22.49 ?  34  LEU B CD2 1 
ATOM   3460 N  N   . ASP B 1 33  ? 30.572  -8.355  -65.865 1.00 12.75 ?  35  ASP B N   1 
ATOM   3461 C  CA  . ASP B 1 33  ? 30.977  -7.870  -67.170 1.00 11.52 ?  35  ASP B CA  1 
ATOM   3462 C  C   . ASP B 1 33  ? 29.959  -6.891  -67.732 1.00 14.73 ?  35  ASP B C   1 
ATOM   3463 O  O   . ASP B 1 33  ? 30.322  -5.842  -68.275 1.00 15.01 ?  35  ASP B O   1 
ATOM   3464 C  CB  . ASP B 1 33  ? 31.145  -9.053  -68.112 1.00 13.68 ?  35  ASP B CB  1 
ATOM   3465 C  CG  . ASP B 1 33  ? 31.205  -8.625  -69.560 1.00 14.63 ?  35  ASP B CG  1 
ATOM   3466 O  OD1 . ASP B 1 33  ? 32.163  -7.930  -69.958 1.00 16.95 ?  35  ASP B OD1 1 
ATOM   3467 O  OD2 . ASP B 1 33  ? 30.287  -9.009  -70.292 1.00 17.87 ?  35  ASP B OD2 1 
ATOM   3468 N  N   . ASP B 1 34  ? 28.680  -7.216  -67.620 1.00 13.33 ?  36  ASP B N   1 
ATOM   3469 C  CA  . ASP B 1 34  ? 27.613  -6.412  -68.213 1.00 13.80 ?  36  ASP B CA  1 
ATOM   3470 C  C   . ASP B 1 34  ? 26.540  -6.247  -67.154 1.00 14.98 ?  36  ASP B C   1 
ATOM   3471 O  O   . ASP B 1 34  ? 25.564  -7.004  -67.122 1.00 13.68 ?  36  ASP B O   1 
ATOM   3472 C  CB  . ASP B 1 34  ? 27.056  -7.067  -69.476 1.00 16.93 ?  36  ASP B CB  1 
ATOM   3473 C  CG  . ASP B 1 34  ? 26.328  -6.082  -70.366 1.00 20.09 ?  36  ASP B CG  1 
ATOM   3474 O  OD1 . ASP B 1 34  ? 26.504  -6.137  -71.608 1.00 17.47 ?  36  ASP B OD1 1 
ATOM   3475 O  OD2 . ASP B 1 34  ? 25.581  -5.244  -69.820 1.00 19.08 ?  36  ASP B OD2 1 
ATOM   3476 N  N   . PRO B 1 35  ? 26.708  -5.286  -66.246 1.00 14.72 ?  37  PRO B N   1 
ATOM   3477 C  CA  . PRO B 1 35  ? 25.768  -5.193  -65.126 1.00 13.27 ?  37  PRO B CA  1 
ATOM   3478 C  C   . PRO B 1 35  ? 24.375  -4.793  -65.567 1.00 11.70 ?  37  PRO B C   1 
ATOM   3479 O  O   . PRO B 1 35  ? 23.408  -5.218  -64.927 1.00 14.36 ?  37  PRO B O   1 
ATOM   3480 C  CB  . PRO B 1 35  ? 26.399  -4.142  -64.201 1.00 14.08 ?  37  PRO B CB  1 
ATOM   3481 C  CG  . PRO B 1 35  ? 27.429  -3.436  -65.028 1.00 17.23 ?  37  PRO B CG  1 
ATOM   3482 C  CD  . PRO B 1 35  ? 27.840  -4.347  -66.137 1.00 12.47 ?  37  PRO B CD  1 
ATOM   3483 N  N   . GLU B 1 36  ? 24.234  -4.028  -66.658 1.00 13.57 ?  38  GLU B N   1 
ATOM   3484 C  CA  . GLU B 1 36  ? 22.884  -3.718  -67.133 1.00 13.90 ?  38  GLU B CA  1 
ATOM   3485 C  C   . GLU B 1 36  ? 22.157  -4.982  -67.575 1.00 19.55 ?  38  GLU B C   1 
ATOM   3486 O  O   . GLU B 1 36  ? 20.970  -5.170  -67.266 1.00 15.35 ?  38  GLU B O   1 
ATOM   3487 C  CB  . GLU B 1 36  ? 22.917  -2.707  -68.276 1.00 17.16 ?  38  GLU B CB  1 
ATOM   3488 C  CG  . GLU B 1 36  ? 21.565  -2.037  -68.476 1.00 20.31 ?  38  GLU B CG  1 
ATOM   3489 C  CD  . GLU B 1 36  ? 21.619  -0.801  -69.354 1.00 28.16 ?  38  GLU B CD  1 
ATOM   3490 O  OE1 . GLU B 1 36  ? 20.582  -0.485  -69.981 1.00 27.93 ?  38  GLU B OE1 1 
ATOM   3491 O  OE2 . GLU B 1 36  ? 22.691  -0.157  -69.427 1.00 30.50 ?  38  GLU B OE2 1 
ATOM   3492 N  N   . ALA B 1 37  ? 22.859  -5.867  -68.291 1.00 16.65 ?  39  ALA B N   1 
ATOM   3493 C  CA  . ALA B 1 37  ? 22.254  -7.136  -68.675 1.00 15.57 ?  39  ALA B CA  1 
ATOM   3494 C  C   . ALA B 1 37  ? 21.939  -7.987  -67.457 1.00 17.34 ?  39  ALA B C   1 
ATOM   3495 O  O   . ALA B 1 37  ? 20.949  -8.725  -67.455 1.00 15.61 ?  39  ALA B O   1 
ATOM   3496 C  CB  . ALA B 1 37  ? 23.173  -7.892  -69.639 1.00 16.91 ?  39  ALA B CB  1 
ATOM   3497 N  N   . GLU B 1 38  ? 22.756  -7.882  -66.404 1.00 12.82 ?  40  GLU B N   1 
ATOM   3498 C  CA  . GLU B 1 38  ? 22.461  -8.609  -65.179 1.00 15.39 ?  40  GLU B CA  1 
ATOM   3499 C  C   . GLU B 1 38  ? 21.214  -8.052  -64.501 1.00 14.06 ?  40  GLU B C   1 
ATOM   3500 O  O   . GLU B 1 38  ? 20.391  -8.818  -63.991 1.00 15.91 ?  40  GLU B O   1 
ATOM   3501 C  CB  . GLU B 1 38  ? 23.675  -8.561  -64.243 1.00 13.30 ?  40  GLU B CB  1 
ATOM   3502 C  CG  . GLU B 1 38  ? 23.563  -9.423  -62.994 1.00 14.96 ?  40  GLU B CG  1 
ATOM   3503 C  CD  . GLU B 1 38  ? 23.341  -10.901 -63.303 1.00 21.22 ?  40  GLU B CD  1 
ATOM   3504 O  OE1 . GLU B 1 38  ? 23.748  -11.364 -64.386 1.00 24.07 ?  40  GLU B OE1 1 
ATOM   3505 O  OE2 . GLU B 1 38  ? 22.771  -11.609 -62.448 1.00 32.16 ?  40  GLU B OE2 1 
ATOM   3506 N  N   . VAL B 1 39  ? 21.056  -6.725  -64.482 1.00 14.43 ?  41  VAL B N   1 
ATOM   3507 C  CA  . VAL B 1 39  ? 19.824  -6.154  -63.942 1.00 13.63 ?  41  VAL B CA  1 
ATOM   3508 C  C   . VAL B 1 39  ? 18.615  -6.708  -64.689 1.00 19.22 ?  41  VAL B C   1 
ATOM   3509 O  O   . VAL B 1 39  ? 17.624  -7.117  -64.068 1.00 16.49 ?  41  VAL B O   1 
ATOM   3510 C  CB  . VAL B 1 39  ? 19.865  -4.616  -63.987 1.00 17.16 ?  41  VAL B CB  1 
ATOM   3511 C  CG1 . VAL B 1 39  ? 18.477  -4.019  -63.620 1.00 18.92 ?  41  VAL B CG1 1 
ATOM   3512 C  CG2 . VAL B 1 39  ? 20.939  -4.098  -63.034 1.00 14.78 ?  41  VAL B CG2 1 
ATOM   3513 N  N   . VAL B 1 40  ? 18.693  -6.763  -66.024 1.00 17.47 ?  42  VAL B N   1 
ATOM   3514 C  CA  . VAL B 1 40  ? 17.584  -7.297  -66.824 1.00 16.25 ?  42  VAL B CA  1 
ATOM   3515 C  C   . VAL B 1 40  ? 17.258  -8.721  -66.391 1.00 18.20 ?  42  VAL B C   1 
ATOM   3516 O  O   . VAL B 1 40  ? 16.090  -9.083  -66.216 1.00 20.11 ?  42  VAL B O   1 
ATOM   3517 C  CB  . VAL B 1 40  ? 17.918  -7.229  -68.327 1.00 20.52 ?  42  VAL B CB  1 
ATOM   3518 C  CG1 . VAL B 1 40  ? 16.909  -8.063  -69.141 1.00 20.31 ?  42  VAL B CG1 1 
ATOM   3519 C  CG2 . VAL B 1 40  ? 17.978  -5.785  -68.806 1.00 16.62 ?  42  VAL B CG2 1 
ATOM   3520 N  N   . ARG B 1 41  ? 18.289  -9.550  -66.196 1.00 17.53 ?  43  ARG B N   1 
ATOM   3521 C  CA  . ARG B 1 41  ? 18.055  -10.930 -65.772 1.00 16.28 ?  43  ARG B CA  1 
ATOM   3522 C  C   . ARG B 1 41  ? 17.442  -10.979 -64.382 1.00 20.97 ?  43  ARG B C   1 
ATOM   3523 O  O   . ARG B 1 41  ? 16.559  -11.799 -64.112 1.00 18.07 ?  43  ARG B O   1 
ATOM   3524 C  CB  . ARG B 1 41  ? 19.366  -11.733 -65.796 1.00 16.26 ?  43  ARG B CB  1 
ATOM   3525 C  CG  . ARG B 1 41  ? 19.859  -12.102 -67.194 1.00 16.52 ?  43  ARG B CG  1 
ATOM   3526 C  CD  . ARG B 1 41  ? 21.126  -12.958 -67.131 1.00 19.36 ?  43  ARG B CD  1 
ATOM   3527 N  NE  . ARG B 1 41  ? 22.333  -12.153 -66.930 1.00 19.18 ?  43  ARG B NE  1 
ATOM   3528 C  CZ  . ARG B 1 41  ? 23.011  -11.585 -67.921 1.00 18.03 ?  43  ARG B CZ  1 
ATOM   3529 N  NH1 . ARG B 1 41  ? 22.573  -11.704 -69.168 1.00 20.81 ?  43  ARG B NH1 1 
ATOM   3530 N  NH2 . ARG B 1 41  ? 24.101  -10.870 -67.669 1.00 22.24 ?  43  ARG B NH2 1 
ATOM   3531 N  N   . CYS B 1 42  ? 17.910  -10.110 -63.483 1.00 19.30 ?  44  CYS B N   1 
ATOM   3532 C  CA  . CYS B 1 42  ? 17.420  -10.128 -62.109 1.00 18.40 ?  44  CYS B CA  1 
ATOM   3533 C  C   . CYS B 1 42  ? 15.994  -9.598  -62.003 1.00 17.33 ?  44  CYS B C   1 
ATOM   3534 O  O   . CYS B 1 42  ? 15.261  -10.013 -61.099 1.00 20.81 ?  44  CYS B O   1 
ATOM   3535 C  CB  . CYS B 1 42  ? 18.355  -9.324  -61.212 1.00 16.91 ?  44  CYS B CB  1 
ATOM   3536 S  SG  . CYS B 1 42  ? 19.957  -10.141 -60.961 1.00 22.84 ?  44  CYS B SG  1 
ATOM   3537 N  N   . LEU B 1 43  ? 15.587  -8.681  -62.894 1.00 16.80 ?  45  LEU B N   1 
ATOM   3538 C  CA  . LEU B 1 43  ? 14.189  -8.249  -62.934 1.00 23.69 ?  45  LEU B CA  1 
ATOM   3539 C  C   . LEU B 1 43  ? 13.273  -9.385  -63.354 1.00 27.15 ?  45  LEU B C   1 
ATOM   3540 O  O   . LEU B 1 43  ? 12.092  -9.403  -62.984 1.00 21.92 ?  45  LEU B O   1 
ATOM   3541 C  CB  . LEU B 1 43  ? 14.001  -7.071  -63.892 1.00 21.47 ?  45  LEU B CB  1 
ATOM   3542 C  CG  . LEU B 1 43  ? 14.701  -5.748  -63.590 1.00 20.51 ?  45  LEU B CG  1 
ATOM   3543 C  CD1 . LEU B 1 43  ? 14.207  -4.641  -64.497 1.00 20.41 ?  45  LEU B CD1 1 
ATOM   3544 C  CD2 . LEU B 1 43  ? 14.510  -5.381  -62.130 1.00 22.99 ?  45  LEU B CD2 1 
ATOM   3545 N  N   . ALA B 1 44  ? 13.798  -10.338 -64.122 1.00 23.08 ?  46  ALA B N   1 
ATOM   3546 C  CA  . ALA B 1 44  ? 13.004  -11.466 -64.580 1.00 20.02 ?  46  ALA B CA  1 
ATOM   3547 C  C   . ALA B 1 44  ? 13.022  -12.629 -63.607 1.00 23.29 ?  46  ALA B C   1 
ATOM   3548 O  O   . ALA B 1 44  ? 12.066  -13.409 -63.577 1.00 24.55 ?  46  ALA B O   1 
ATOM   3549 C  CB  . ALA B 1 44  ? 13.499  -11.930 -65.954 1.00 23.37 ?  46  ALA B CB  1 
ATOM   3550 N  N   . GLU B 1 45  ? 14.079  -12.775 -62.812 1.00 20.93 ?  47  GLU B N   1 
ATOM   3551 C  CA  . GLU B 1 45  ? 14.185  -13.849 -61.827 1.00 18.04 ?  47  GLU B CA  1 
ATOM   3552 C  C   . GLU B 1 45  ? 14.693  -13.258 -60.516 1.00 22.82 ?  47  GLU B C   1 
ATOM   3553 O  O   . GLU B 1 45  ? 15.883  -13.388 -60.188 1.00 27.34 ?  47  GLU B O   1 
ATOM   3554 C  CB  . GLU B 1 45  ? 15.102  -14.966 -62.328 1.00 21.34 ?  47  GLU B CB  1 
ATOM   3555 N  N   . PRO B 1 46  ? 13.818  -12.606 -59.739 1.00 24.49 ?  48  PRO B N   1 
ATOM   3556 C  CA  . PRO B 1 46  ? 14.262  -11.847 -58.562 1.00 18.34 ?  48  PRO B CA  1 
ATOM   3557 C  C   . PRO B 1 46  ? 14.432  -12.749 -57.343 1.00 21.71 ?  48  PRO B C   1 
ATOM   3558 O  O   . PRO B 1 46  ? 14.178  -13.950 -57.373 1.00 22.51 ?  48  PRO B O   1 
ATOM   3559 C  CB  . PRO B 1 46  ? 13.107  -10.877 -58.310 1.00 24.20 ?  48  PRO B CB  1 
ATOM   3560 C  CG  . PRO B 1 46  ? 12.392  -10.752 -59.597 1.00 29.17 ?  48  PRO B CG  1 
ATOM   3561 C  CD  . PRO B 1 46  ? 12.505  -12.129 -60.217 1.00 24.09 ?  48  PRO B CD  1 
ATOM   3562 N  N   . ILE B 1 47  ? 14.823  -12.121 -56.238 1.00 19.33 ?  49  ILE B N   1 
ATOM   3563 C  CA  . ILE B 1 47  ? 14.940  -12.775 -54.942 1.00 19.17 ?  49  ILE B CA  1 
ATOM   3564 C  C   . ILE B 1 47  ? 13.648  -12.537 -54.164 1.00 24.14 ?  49  ILE B C   1 
ATOM   3565 O  O   . ILE B 1 47  ? 13.282  -11.387 -53.896 1.00 19.83 ?  49  ILE B O   1 
ATOM   3566 C  CB  . ILE B 1 47  ? 16.153  -12.249 -54.154 1.00 15.30 ?  49  ILE B CB  1 
ATOM   3567 C  CG1 . ILE B 1 47  ? 17.449  -12.458 -54.950 1.00 17.56 ?  49  ILE B CG1 1 
ATOM   3568 C  CG2 . ILE B 1 47  ? 16.211  -12.930 -52.801 1.00 18.46 ?  49  ILE B CG2 1 
ATOM   3569 C  CD1 . ILE B 1 47  ? 18.615  -11.527 -54.541 1.00 18.14 ?  49  ILE B CD1 1 
ATOM   3570 N  N   . GLY B 1 48  ? 12.957  -13.619 -53.806 1.00 22.55 ?  50  GLY B N   1 
ATOM   3571 C  CA  . GLY B 1 48  ? 11.801  -13.524 -52.924 1.00 25.76 ?  50  GLY B CA  1 
ATOM   3572 C  C   . GLY B 1 48  ? 10.685  -12.656 -53.452 1.00 27.19 ?  50  GLY B C   1 
ATOM   3573 O  O   . GLY B 1 48  ? 9.960   -12.031 -52.665 1.00 25.72 ?  50  GLY B O   1 
ATOM   3574 N  N   . SER B 1 49  ? 10.509  -12.616 -54.770 1.00 24.54 ?  51  SER B N   1 
ATOM   3575 C  CA  . SER B 1 49  ? 9.579   -11.690 -55.395 1.00 26.27 ?  51  SER B CA  1 
ATOM   3576 C  C   . SER B 1 49  ? 9.161   -12.249 -56.742 1.00 29.92 ?  51  SER B C   1 
ATOM   3577 O  O   . SER B 1 49  ? 9.966   -12.907 -57.411 1.00 26.83 ?  51  SER B O   1 
ATOM   3578 C  CB  . SER B 1 49  ? 10.225  -10.314 -55.577 1.00 26.34 ?  51  SER B CB  1 
ATOM   3579 O  OG  . SER B 1 49  ? 9.361   -9.432  -56.252 1.00 32.51 ?  51  SER B OG  1 
ATOM   3580 N  N   . PRO B 1 50  ? 7.935   -11.986 -57.180 1.00 27.80 ?  52  PRO B N   1 
ATOM   3581 C  CA  . PRO B 1 50  ? 7.600   -12.195 -58.584 1.00 26.88 ?  52  PRO B CA  1 
ATOM   3582 C  C   . PRO B 1 50  ? 8.485   -11.328 -59.458 1.00 29.22 ?  52  PRO B C   1 
ATOM   3583 O  O   . PRO B 1 50  ? 9.071   -10.346 -58.973 1.00 25.50 ?  52  PRO B O   1 
ATOM   3584 C  CB  . PRO B 1 50  ? 6.130   -11.749 -58.671 1.00 26.27 ?  52  PRO B CB  1 
ATOM   3585 C  CG  . PRO B 1 50  ? 5.627   -11.823 -57.263 1.00 32.62 ?  52  PRO B CG  1 
ATOM   3586 C  CD  . PRO B 1 50  ? 6.808   -11.410 -56.430 1.00 28.54 ?  52  PRO B CD  1 
ATOM   3587 N  N   . PRO B 1 51  ? 8.613   -11.659 -60.741 1.00 27.51 ?  53  PRO B N   1 
ATOM   3588 C  CA  . PRO B 1 51  ? 9.271   -10.743 -61.675 1.00 26.01 ?  53  PRO B CA  1 
ATOM   3589 C  C   . PRO B 1 51  ? 8.667   -9.351  -61.577 1.00 25.31 ?  53  PRO B C   1 
ATOM   3590 O  O   . PRO B 1 51  ? 7.466   -9.194  -61.334 1.00 25.23 ?  53  PRO B O   1 
ATOM   3591 C  CB  . PRO B 1 51  ? 8.992   -11.379 -63.040 1.00 20.97 ?  53  PRO B CB  1 
ATOM   3592 C  CG  . PRO B 1 51  ? 8.915   -12.826 -62.747 1.00 24.06 ?  53  PRO B CG  1 
ATOM   3593 C  CD  . PRO B 1 51  ? 8.273   -12.943 -61.379 1.00 29.68 ?  53  PRO B CD  1 
ATOM   3594 N  N   . LEU B 1 52  ? 9.516   -8.334  -61.756 1.00 17.41 ?  54  LEU B N   1 
ATOM   3595 C  CA  . LEU B 1 52  ? 9.026   -6.958  -61.737 1.00 20.25 ?  54  LEU B CA  1 
ATOM   3596 C  C   . LEU B 1 52  ? 7.886   -6.771  -62.727 1.00 24.67 ?  54  LEU B C   1 
ATOM   3597 O  O   . LEU B 1 52  ? 6.881   -6.126  -62.407 1.00 26.29 ?  54  LEU B O   1 
ATOM   3598 C  CB  . LEU B 1 52  ? 10.147  -5.966  -62.047 1.00 23.55 ?  54  LEU B CB  1 
ATOM   3599 C  CG  . LEU B 1 52  ? 9.678   -4.507  -62.124 1.00 22.42 ?  54  LEU B CG  1 
ATOM   3600 C  CD1 . LEU B 1 52  ? 9.063   -4.029  -60.788 1.00 20.95 ?  54  LEU B CD1 1 
ATOM   3601 C  CD2 . LEU B 1 52  ? 10.794  -3.579  -62.553 1.00 21.58 ?  54  LEU B CD2 1 
ATOM   3602 N  N   . LEU B 1 53  ? 8.028   -7.326  -63.940 1.00 21.14 ?  55  LEU B N   1 
ATOM   3603 C  CA  . LEU B 1 53  ? 6.948   -7.255  -64.925 1.00 24.08 ?  55  LEU B CA  1 
ATOM   3604 C  C   . LEU B 1 53  ? 5.629   -7.756  -64.355 1.00 20.37 ?  55  LEU B C   1 
ATOM   3605 O  O   . LEU B 1 53  ? 4.583   -7.132  -64.560 1.00 25.92 ?  55  LEU B O   1 
ATOM   3606 C  CB  . LEU B 1 53  ? 7.314   -8.058  -66.173 1.00 23.67 ?  55  LEU B CB  1 
ATOM   3607 C  CG  . LEU B 1 53  ? 6.303   -7.958  -67.317 1.00 26.18 ?  55  LEU B CG  1 
ATOM   3608 C  CD1 . LEU B 1 53  ? 6.011   -6.504  -67.687 1.00 22.45 ?  55  LEU B CD1 1 
ATOM   3609 C  CD2 . LEU B 1 53  ? 6.803   -8.729  -68.511 1.00 25.41 ?  55  LEU B CD2 1 
ATOM   3610 N  N   . ASP B 1 54  ? 5.659   -8.876  -63.633 1.00 24.63 ?  56  ASP B N   1 
ATOM   3611 C  CA  . ASP B 1 54  ? 4.433   -9.427  -63.060 1.00 21.74 ?  56  ASP B CA  1 
ATOM   3612 C  C   . ASP B 1 54  ? 3.850   -8.504  -61.988 1.00 31.64 ?  56  ASP B C   1 
ATOM   3613 O  O   . ASP B 1 54  ? 2.625   -8.352  -61.892 1.00 26.08 ?  56  ASP B O   1 
ATOM   3614 C  CB  . ASP B 1 54  ? 4.705   -10.821 -62.496 1.00 24.14 ?  56  ASP B CB  1 
ATOM   3615 C  CG  . ASP B 1 54  ? 5.166   -11.808 -63.568 1.00 27.11 ?  56  ASP B CG  1 
ATOM   3616 O  OD1 . ASP B 1 54  ? 5.325   -13.009 -63.250 1.00 29.57 ?  56  ASP B OD1 1 
ATOM   3617 O  OD2 . ASP B 1 54  ? 5.339   -11.393 -64.732 1.00 31.59 ?  56  ASP B OD2 1 
ATOM   3618 N  N   . LEU B 1 55  ? 4.712   -7.868  -61.182 1.00 20.60 ?  57  LEU B N   1 
ATOM   3619 C  CA  . LEU B 1 55  ? 4.245   -6.936  -60.156 1.00 23.41 ?  57  LEU B CA  1 
ATOM   3620 C  C   . LEU B 1 55  ? 3.643   -5.674  -60.752 1.00 25.39 ?  57  LEU B C   1 
ATOM   3621 O  O   . LEU B 1 55  ? 2.794   -5.040  -60.115 1.00 27.46 ?  57  LEU B O   1 
ATOM   3622 C  CB  . LEU B 1 55  ? 5.400   -6.544  -59.221 1.00 17.22 ?  57  LEU B CB  1 
ATOM   3623 C  CG  . LEU B 1 55  ? 5.889   -7.622  -58.274 1.00 25.33 ?  57  LEU B CG  1 
ATOM   3624 C  CD1 . LEU B 1 55  ? 7.151   -7.152  -57.552 1.00 24.08 ?  57  LEU B CD1 1 
ATOM   3625 C  CD2 . LEU B 1 55  ? 4.793   -7.925  -57.283 1.00 24.68 ?  57  LEU B CD2 1 
ATOM   3626 N  N   . ALA B 1 56  ? 4.086   -5.270  -61.939 1.00 22.55 ?  58  ALA B N   1 
ATOM   3627 C  CA  . ALA B 1 56  ? 3.602   -4.032  -62.525 1.00 21.97 ?  58  ALA B CA  1 
ATOM   3628 C  C   . ALA B 1 56  ? 2.297   -4.207  -63.293 1.00 31.79 ?  58  ALA B C   1 
ATOM   3629 O  O   . ALA B 1 56  ? 1.720   -3.201  -63.720 1.00 31.60 ?  58  ALA B O   1 
ATOM   3630 C  CB  . ALA B 1 56  ? 4.657   -3.426  -63.458 1.00 22.84 ?  58  ALA B CB  1 
ATOM   3631 N  N   . ARG B 1 57  ? 1.831   -5.446  -63.483 1.00 27.36 ?  59  ARG B N   1 
ATOM   3632 C  CA  . ARG B 1 57  ? 0.566   -5.684  -64.177 1.00 34.57 ?  59  ARG B CA  1 
ATOM   3633 C  C   . ARG B 1 57  ? -0.592  -5.109  -63.370 1.00 36.72 ?  59  ARG B C   1 
ATOM   3634 O  O   . ARG B 1 57  ? -0.743  -5.402  -62.177 1.00 33.35 ?  59  ARG B O   1 
ATOM   3635 C  CB  . ARG B 1 57  ? 0.340   -7.186  -64.396 1.00 28.62 ?  59  ARG B CB  1 
ATOM   3636 C  CG  . ARG B 1 57  ? 1.391   -7.879  -65.253 1.00 31.21 ?  59  ARG B CG  1 
ATOM   3637 C  CD  . ARG B 1 57  ? 1.672   -7.161  -66.558 1.00 33.82 ?  59  ARG B CD  1 
ATOM   3638 N  NE  . ARG B 1 57  ? 2.393   -8.036  -67.479 1.00 30.45 ?  59  ARG B NE  1 
ATOM   3639 C  CZ  . ARG B 1 57  ? 2.490   -7.839  -68.789 1.00 25.99 ?  59  ARG B CZ  1 
ATOM   3640 N  NH1 . ARG B 1 57  ? 1.890   -6.801  -69.355 1.00 33.83 ?  59  ARG B NH1 1 
ATOM   3641 N  NH2 . ARG B 1 57  ? 3.185   -8.688  -69.536 1.00 27.58 ?  59  ARG B NH2 1 
ATOM   3642 N  N   . GLY B 1 58  ? -1.419  -4.298  -64.029 1.00 40.28 ?  60  GLY B N   1 
ATOM   3643 C  CA  . GLY B 1 58  ? -2.573  -3.722  -63.366 1.00 44.86 ?  60  GLY B CA  1 
ATOM   3644 C  C   . GLY B 1 58  ? -2.253  -2.619  -62.384 1.00 46.61 ?  60  GLY B C   1 
ATOM   3645 O  O   . GLY B 1 58  ? -3.060  -2.343  -61.492 1.00 46.43 ?  60  GLY B O   1 
ATOM   3646 N  N   . LYS B 1 59  ? -1.091  -1.987  -62.517 1.00 42.44 ?  61  LYS B N   1 
ATOM   3647 C  CA  . LYS B 1 59  ? -0.694  -0.857  -61.690 1.00 34.45 ?  61  LYS B CA  1 
ATOM   3648 C  C   . LYS B 1 59  ? -0.824  0.410   -62.521 1.00 26.57 ?  61  LYS B C   1 
ATOM   3649 O  O   . LYS B 1 59  ? -0.484  0.412   -63.706 1.00 25.56 ?  61  LYS B O   1 
ATOM   3650 C  CB  . LYS B 1 59  ? 0.748   -1.023  -61.199 1.00 26.71 ?  61  LYS B CB  1 
ATOM   3651 C  CG  . LYS B 1 59  ? 0.950   -2.272  -60.369 1.00 31.24 ?  61  LYS B CG  1 
ATOM   3652 C  CD  . LYS B 1 59  ? 0.233   -2.202  -59.041 1.00 33.74 ?  61  LYS B CD  1 
ATOM   3653 C  CE  . LYS B 1 59  ? 0.895   -3.116  -58.027 1.00 36.05 ?  61  LYS B CE  1 
ATOM   3654 N  NZ  . LYS B 1 59  ? 0.675   -4.545  -58.402 1.00 41.51 ?  61  LYS B NZ  1 
ATOM   3655 N  N   . ARG B 1 60  ? -1.323  1.484   -61.903 1.00 31.67 ?  62  ARG B N   1 
ATOM   3656 C  CA  . ARG B 1 60  ? -1.600  2.724   -62.621 1.00 32.36 ?  62  ARG B CA  1 
ATOM   3657 C  C   . ARG B 1 60  ? -0.511  3.780   -62.477 1.00 32.75 ?  62  ARG B C   1 
ATOM   3658 O  O   . ARG B 1 60  ? -0.417  4.673   -63.326 1.00 34.21 ?  62  ARG B O   1 
ATOM   3659 C  CB  . ARG B 1 60  ? -2.931  3.327   -62.149 1.00 38.88 ?  62  ARG B CB  1 
ATOM   3660 N  N   . SER B 1 61  ? 0.297   3.717   -61.425 1.00 30.32 ?  63  SER B N   1 
ATOM   3661 C  CA  . SER B 1 61  ? 1.355   4.693   -61.227 1.00 27.43 ?  63  SER B CA  1 
ATOM   3662 C  C   . SER B 1 61  ? 2.523   3.997   -60.548 1.00 20.15 ?  63  SER B C   1 
ATOM   3663 O  O   . SER B 1 61  ? 2.352   2.968   -59.888 1.00 21.72 ?  63  SER B O   1 
ATOM   3664 C  CB  . SER B 1 61  ? 0.876   5.891   -60.390 1.00 25.11 ?  63  SER B CB  1 
ATOM   3665 O  OG  . SER B 1 61  ? 0.472   5.460   -59.103 1.00 24.81 ?  63  SER B OG  1 
ATOM   3666 N  N   . ALA B 1 62  ? 3.711   4.559   -60.728 1.00 22.57 ?  64  ALA B N   1 
ATOM   3667 C  CA  . ALA B 1 62  ? 4.902   4.021   -60.088 1.00 26.21 ?  64  ALA B CA  1 
ATOM   3668 C  C   . ALA B 1 62  ? 5.749   5.155   -59.540 1.00 21.96 ?  64  ALA B C   1 
ATOM   3669 O  O   . ALA B 1 62  ? 5.826   6.237   -60.130 1.00 20.69 ?  64  ALA B O   1 
ATOM   3670 C  CB  . ALA B 1 62  ? 5.737   3.171   -61.057 1.00 26.80 ?  64  ALA B CB  1 
ATOM   3671 N  N   . CYS B 1 63  ? 6.377   4.899   -58.398 1.00 20.75 ?  65  CYS B N   1 
ATOM   3672 C  CA  . CYS B 1 63  ? 7.363   5.808   -57.838 1.00 18.47 ?  65  CYS B CA  1 
ATOM   3673 C  C   . CYS B 1 63  ? 8.654   5.028   -57.629 1.00 14.06 ?  65  CYS B C   1 
ATOM   3674 O  O   . CYS B 1 63  ? 8.638   3.970   -56.993 1.00 16.52 ?  65  CYS B O   1 
ATOM   3675 C  CB  . CYS B 1 63  ? 6.879   6.419   -56.524 1.00 19.90 ?  65  CYS B CB  1 
ATOM   3676 S  SG  . CYS B 1 63  ? 8.019   7.704   -55.879 1.00 22.39 ?  65  CYS B SG  1 
ATOM   3677 N  N   . ILE B 1 64  ? 9.748   5.539   -58.191 1.00 14.64 ?  66  ILE B N   1 
ATOM   3678 C  CA  . ILE B 1 64  ? 11.072  4.918   -58.114 1.00 17.55 ?  66  ILE B CA  1 
ATOM   3679 C  C   . ILE B 1 64  ? 11.975  5.823   -57.286 1.00 15.90 ?  66  ILE B C   1 
ATOM   3680 O  O   . ILE B 1 64  ? 12.260  6.959   -57.682 1.00 15.25 ?  66  ILE B O   1 
ATOM   3681 C  CB  . ILE B 1 64  ? 11.684  4.687   -59.505 1.00 20.61 ?  66  ILE B CB  1 
ATOM   3682 C  CG1 . ILE B 1 64  ? 10.722  3.911   -60.407 1.00 17.15 ?  66  ILE B CG1 1 
ATOM   3683 C  CG2 . ILE B 1 64  ? 13.054  3.979   -59.402 1.00 17.37 ?  66  ILE B CG2 1 
ATOM   3684 C  CD1 . ILE B 1 64  ? 11.079  4.014   -61.884 1.00 20.60 ?  66  ILE B CD1 1 
ATOM   3685 N  N   . LEU B 1 65  ? 12.445  5.305   -56.155 1.00 16.20 ?  67  LEU B N   1 
ATOM   3686 C  CA  . LEU B 1 65  ? 13.355  6.045   -55.289 1.00 15.86 ?  67  LEU B CA  1 
ATOM   3687 C  C   . LEU B 1 65  ? 14.777  5.879   -55.800 1.00 14.06 ?  67  LEU B C   1 
ATOM   3688 O  O   . LEU B 1 65  ? 15.204  4.753   -56.074 1.00 17.19 ?  67  LEU B O   1 
ATOM   3689 C  CB  . LEU B 1 65  ? 13.252  5.513   -53.863 1.00 14.98 ?  67  LEU B CB  1 
ATOM   3690 C  CG  . LEU B 1 65  ? 11.847  5.599   -53.262 1.00 17.29 ?  67  LEU B CG  1 
ATOM   3691 C  CD1 . LEU B 1 65  ? 11.888  5.175   -51.790 1.00 12.82 ?  67  LEU B CD1 1 
ATOM   3692 C  CD2 . LEU B 1 65  ? 11.271  7.013   -53.452 1.00 17.44 ?  67  LEU B CD2 1 
ATOM   3693 N  N   . VAL B 1 66  ? 15.510  6.986   -55.931 1.00 15.76 ?  68  VAL B N   1 
ATOM   3694 C  CA  . VAL B 1 66  ? 16.925  6.928   -56.283 1.00 12.93 ?  68  VAL B CA  1 
ATOM   3695 C  C   . VAL B 1 66  ? 17.722  7.718   -55.254 1.00 13.41 ?  68  VAL B C   1 
ATOM   3696 O  O   . VAL B 1 66  ? 17.219  8.659   -54.636 1.00 13.50 ?  68  VAL B O   1 
ATOM   3697 C  CB  . VAL B 1 66  ? 17.231  7.462   -57.700 1.00 14.51 ?  68  VAL B CB  1 
ATOM   3698 C  CG1 . VAL B 1 66  ? 16.498  6.643   -58.772 1.00 17.73 ?  68  VAL B CG1 1 
ATOM   3699 C  CG2 . VAL B 1 66  ? 16.952  8.964   -57.809 1.00 18.70 ?  68  VAL B CG2 1 
ATOM   3700 N  N   . CYS B 1 67  ? 18.992  7.343   -55.094 1.00 14.78 ?  69  CYS B N   1 
ATOM   3701 C  CA  . CYS B 1 67  ? 19.866  8.060   -54.177 1.00 13.89 ?  69  CYS B CA  1 
ATOM   3702 C  C   . CYS B 1 67  ? 20.249  9.422   -54.750 1.00 13.93 ?  69  CYS B C   1 
ATOM   3703 O  O   . CYS B 1 67  ? 20.215  9.641   -55.968 1.00 14.79 ?  69  CYS B O   1 
ATOM   3704 C  CB  . CYS B 1 67  ? 21.129  7.241   -53.909 1.00 11.17 ?  69  CYS B CB  1 
ATOM   3705 S  SG  . CYS B 1 67  ? 20.816  5.714   -53.023 1.00 15.86 ?  69  CYS B SG  1 
ATOM   3706 N  N   . ASP B 1 68  ? 20.663  10.341  -53.860 1.00 13.78 ?  70  ASP B N   1 
ATOM   3707 C  CA  . ASP B 1 68  ? 21.115  11.660  -54.285 1.00 12.53 ?  70  ASP B CA  1 
ATOM   3708 C  C   . ASP B 1 68  ? 22.597  11.613  -54.669 1.00 13.18 ?  70  ASP B C   1 
ATOM   3709 O  O   . ASP B 1 68  ? 23.177  10.537  -54.836 1.00 14.28 ?  70  ASP B O   1 
ATOM   3710 C  CB  . ASP B 1 68  ? 20.790  12.724  -53.223 1.00 12.69 ?  70  ASP B CB  1 
ATOM   3711 C  CG  . ASP B 1 68  ? 21.588  12.584  -51.927 1.00 15.22 ?  70  ASP B CG  1 
ATOM   3712 O  OD1 . ASP B 1 68  ? 22.412  11.651  -51.775 1.00 13.48 ?  70  ASP B OD1 1 
ATOM   3713 O  OD2 . ASP B 1 68  ? 21.351  13.435  -51.037 1.00 13.25 ?  70  ASP B OD2 1 
ATOM   3714 N  N   . ILE B 1 69  ? 23.216  12.786  -54.830 1.00 13.83 ?  71  ILE B N   1 
ATOM   3715 C  CA  . ILE B 1 69  ? 24.568  12.863  -55.387 1.00 16.32 ?  71  ILE B CA  1 
ATOM   3716 C  C   . ILE B 1 69  ? 25.585  12.154  -54.507 1.00 16.25 ?  71  ILE B C   1 
ATOM   3717 O  O   . ILE B 1 69  ? 26.627  11.699  -55.003 1.00 12.20 ?  71  ILE B O   1 
ATOM   3718 C  CB  . ILE B 1 69  ? 24.978  14.336  -55.631 1.00 15.12 ?  71  ILE B CB  1 
ATOM   3719 C  CG1 . ILE B 1 69  ? 26.126  14.425  -56.655 1.00 14.63 ?  71  ILE B CG1 1 
ATOM   3720 C  CG2 . ILE B 1 69  ? 25.301  15.056  -54.323 1.00 13.97 ?  71  ILE B CG2 1 
ATOM   3721 C  CD1 . ILE B 1 69  ? 25.784  13.807  -58.002 1.00 19.46 ?  71  ILE B CD1 1 
ATOM   3722 N  N   . THR B 1 70  ? 25.312  12.045  -53.205 1.00 12.78 ?  72  THR B N   1 
ATOM   3723 C  CA  . THR B 1 70  ? 26.339  11.565  -52.278 1.00 11.85 ?  72  THR B CA  1 
ATOM   3724 C  C   . THR B 1 70  ? 26.574  10.066  -52.388 1.00 14.47 ?  72  THR B C   1 
ATOM   3725 O  O   . THR B 1 70  ? 27.504  9.556   -51.742 1.00 13.76 ?  72  THR B O   1 
ATOM   3726 C  CB  . THR B 1 70  ? 25.966  11.891  -50.826 1.00 11.88 ?  72  THR B CB  1 
ATOM   3727 O  OG1 . THR B 1 70  ? 24.814  11.134  -50.436 1.00 13.27 ?  72  THR B OG1 1 
ATOM   3728 C  CG2 . THR B 1 70  ? 25.656  13.382  -50.680 1.00 13.03 ?  72  THR B CG2 1 
ATOM   3729 N  N   . ARG B 1 71  ? 25.730  9.345   -53.132 1.00 11.56 ?  73  ARG B N   1 
ATOM   3730 C  CA  . ARG B 1 71  ? 25.939  7.925   -53.370 1.00 11.54 ?  73  ARG B CA  1 
ATOM   3731 C  C   . ARG B 1 71  ? 26.275  7.715   -54.836 1.00 13.21 ?  73  ARG B C   1 
ATOM   3732 O  O   . ARG B 1 71  ? 25.485  8.111   -55.704 1.00 16.43 ?  73  ARG B O   1 
ATOM   3733 C  CB  . ARG B 1 71  ? 24.719  7.092   -52.977 1.00 11.06 ?  73  ARG B CB  1 
ATOM   3734 C  CG  . ARG B 1 71  ? 23.994  7.551   -51.710 1.00 16.00 ?  73  ARG B CG  1 
ATOM   3735 C  CD  . ARG B 1 71  ? 24.929  7.473   -50.537 1.00 18.45 ?  73  ARG B CD  1 
ATOM   3736 N  NE  . ARG B 1 71  ? 24.288  7.172   -49.266 1.00 13.32 ?  73  ARG B NE  1 
ATOM   3737 C  CZ  . ARG B 1 71  ? 24.379  7.934   -48.176 1.00 10.59 ?  73  ARG B CZ  1 
ATOM   3738 N  NH1 . ARG B 1 71  ? 25.030  9.098   -48.212 1.00 10.96 ?  73  ARG B NH1 1 
ATOM   3739 N  NH2 . ARG B 1 71  ? 23.799  7.528   -47.056 1.00 11.20 ?  73  ARG B NH2 1 
ATOM   3740 N  N   . PRO B 1 72  ? 27.424  7.120   -55.163 1.00 11.16 ?  74  PRO B N   1 
ATOM   3741 C  CA  . PRO B 1 72  ? 27.818  6.908   -56.563 1.00 12.73 ?  74  PRO B CA  1 
ATOM   3742 C  C   . PRO B 1 72  ? 27.121  5.715   -57.227 1.00 13.79 ?  74  PRO B C   1 
ATOM   3743 O  O   . PRO B 1 72  ? 27.763  4.868   -57.856 1.00 14.04 ?  74  PRO B O   1 
ATOM   3744 C  CB  . PRO B 1 72  ? 29.330  6.690   -56.457 1.00 12.91 ?  74  PRO B CB  1 
ATOM   3745 C  CG  . PRO B 1 72  ? 29.511  6.043   -55.090 1.00 13.45 ?  74  PRO B CG  1 
ATOM   3746 C  CD  . PRO B 1 72  ? 28.441  6.640   -54.203 1.00 12.30 ?  74  PRO B CD  1 
ATOM   3747 N  N   . VAL B 1 73  ? 25.799  5.647   -57.082 1.00 14.03 ?  75  VAL B N   1 
ATOM   3748 C  CA  . VAL B 1 73  ? 25.018  4.611   -57.775 1.00 15.12 ?  75  VAL B CA  1 
ATOM   3749 C  C   . VAL B 1 73  ? 25.084  4.852   -59.277 1.00 12.86 ?  75  VAL B C   1 
ATOM   3750 O  O   . VAL B 1 73  ? 24.787  5.969   -59.734 1.00 15.74 ?  75  VAL B O   1 
ATOM   3751 C  CB  . VAL B 1 73  ? 23.559  4.624   -57.306 1.00 17.90 ?  75  VAL B CB  1 
ATOM   3752 C  CG1 . VAL B 1 73  ? 22.824  3.394   -57.873 1.00 16.78 ?  75  VAL B CG1 1 
ATOM   3753 C  CG2 . VAL B 1 73  ? 23.460  4.682   -55.788 1.00 16.54 ?  75  VAL B CG2 1 
ATOM   3754 N  N   . PRO B 1 74  ? 25.443  3.863   -60.075 1.00 16.89 ?  76  PRO B N   1 
ATOM   3755 C  CA  . PRO B 1 74  ? 25.350  4.034   -61.538 1.00 17.96 ?  76  PRO B CA  1 
ATOM   3756 C  C   . PRO B 1 74  ? 23.902  3.872   -61.983 1.00 15.47 ?  76  PRO B C   1 
ATOM   3757 O  O   . PRO B 1 74  ? 23.500  2.866   -62.576 1.00 19.04 ?  76  PRO B O   1 
ATOM   3758 C  CB  . PRO B 1 74  ? 26.272  2.926   -62.058 1.00 18.36 ?  76  PRO B CB  1 
ATOM   3759 C  CG  . PRO B 1 74  ? 26.188  1.858   -61.017 1.00 22.97 ?  76  PRO B CG  1 
ATOM   3760 C  CD  . PRO B 1 74  ? 25.988  2.549   -59.687 1.00 16.24 ?  76  PRO B CD  1 
ATOM   3761 N  N   . ASN B 1 75  ? 23.090  4.873   -61.649 1.00 16.03 ?  77  ASN B N   1 
ATOM   3762 C  CA  . ASN B 1 75  ? 21.639  4.742   -61.778 1.00 16.37 ?  77  ASN B CA  1 
ATOM   3763 C  C   . ASN B 1 75  ? 21.149  4.345   -63.165 1.00 14.98 ?  77  ASN B C   1 
ATOM   3764 O  O   . ASN B 1 75  ? 20.198  3.547   -63.235 1.00 17.89 ?  77  ASN B O   1 
ATOM   3765 C  CB  . ASN B 1 75  ? 20.956  6.045   -61.343 1.00 16.60 ?  77  ASN B CB  1 
ATOM   3766 C  CG  . ASN B 1 75  ? 21.153  6.337   -59.870 1.00 17.79 ?  77  ASN B CG  1 
ATOM   3767 O  OD1 . ASN B 1 75  ? 20.666  5.598   -59.015 1.00 17.90 ?  77  ASN B OD1 1 
ATOM   3768 N  ND2 . ASN B 1 75  ? 21.852  7.423   -59.567 1.00 17.30 ?  77  ASN B ND2 1 
ATOM   3769 N  N   . PRO B 1 76  ? 21.708  4.849   -64.277 1.00 19.33 ?  78  PRO B N   1 
ATOM   3770 C  CA  . PRO B 1 76  ? 21.202  4.429   -65.601 1.00 17.01 ?  78  PRO B CA  1 
ATOM   3771 C  C   . PRO B 1 76  ? 21.237  2.927   -65.831 1.00 22.32 ?  78  PRO B C   1 
ATOM   3772 O  O   . PRO B 1 76  ? 20.342  2.391   -66.500 1.00 19.59 ?  78  PRO B O   1 
ATOM   3773 C  CB  . PRO B 1 76  ? 22.131  5.168   -66.576 1.00 22.45 ?  78  PRO B CB  1 
ATOM   3774 C  CG  . PRO B 1 76  ? 22.567  6.389   -65.816 1.00 25.23 ?  78  PRO B CG  1 
ATOM   3775 C  CD  . PRO B 1 76  ? 22.747  5.892   -64.406 1.00 17.81 ?  78  PRO B CD  1 
ATOM   3776 N  N   . VAL B 1 77  ? 22.243  2.236   -65.293 1.00 17.30 ?  79  VAL B N   1 
ATOM   3777 C  CA  . VAL B 1 77  ? 22.343  0.784   -65.405 1.00 18.92 ?  79  VAL B CA  1 
ATOM   3778 C  C   . VAL B 1 77  ? 21.151  0.112   -64.729 1.00 18.97 ?  79  VAL B C   1 
ATOM   3779 O  O   . VAL B 1 77  ? 20.681  -0.949  -65.166 1.00 17.55 ?  79  VAL B O   1 
ATOM   3780 C  CB  . VAL B 1 77  ? 23.691  0.344   -64.787 1.00 20.79 ?  79  VAL B CB  1 
ATOM   3781 C  CG1 . VAL B 1 77  ? 23.761  -1.146  -64.557 1.00 18.60 ?  79  VAL B CG1 1 
ATOM   3782 C  CG2 . VAL B 1 77  ? 24.859  0.871   -65.618 1.00 25.21 ?  79  VAL B CG2 1 
ATOM   3783 N  N   . LEU B 1 78  ? 20.645  0.717   -63.652 1.00 19.07 ?  80  LEU B N   1 
ATOM   3784 C  CA  A LEU B 1 78  ? 19.482  0.180   -62.954 0.50 17.53 ?  80  LEU B CA  1 
ATOM   3785 C  CA  B LEU B 1 78  ? 19.486  0.171   -62.960 0.50 17.53 ?  80  LEU B CA  1 
ATOM   3786 C  C   . LEU B 1 78  ? 18.184  0.650   -63.589 1.00 16.30 ?  80  LEU B C   1 
ATOM   3787 O  O   . LEU B 1 78  ? 17.240  -0.137  -63.741 1.00 17.36 ?  80  LEU B O   1 
ATOM   3788 C  CB  A LEU B 1 78  ? 19.505  0.604   -61.483 0.50 16.82 ?  80  LEU B CB  1 
ATOM   3789 C  CB  B LEU B 1 78  ? 19.542  0.566   -61.482 0.50 16.84 ?  80  LEU B CB  1 
ATOM   3790 C  CG  A LEU B 1 78  ? 20.772  0.371   -60.666 0.50 18.34 ?  80  LEU B CG  1 
ATOM   3791 C  CG  B LEU B 1 78  ? 20.587  -0.148  -60.623 0.50 18.81 ?  80  LEU B CG  1 
ATOM   3792 C  CD1 A LEU B 1 78  ? 20.473  0.550   -59.183 0.50 14.66 ?  80  LEU B CD1 1 
ATOM   3793 C  CD1 B LEU B 1 78  ? 21.956  0.498   -60.783 0.50 18.24 ?  80  LEU B CD1 1 
ATOM   3794 C  CD2 A LEU B 1 78  ? 21.327  -1.021  -60.936 0.50 18.25 ?  80  LEU B CD2 1 
ATOM   3795 C  CD2 B LEU B 1 78  ? 20.169  -0.109  -59.162 0.50 16.97 ?  80  LEU B CD2 1 
ATOM   3796 N  N   . LEU B 1 79  ? 18.120  1.931   -63.955 1.00 17.78 ?  81  LEU B N   1 
ATOM   3797 C  CA  . LEU B 1 79  ? 16.862  2.548   -64.367 1.00 16.78 ?  81  LEU B CA  1 
ATOM   3798 C  C   . LEU B 1 79  ? 16.438  2.167   -65.781 1.00 20.71 ?  81  LEU B C   1 
ATOM   3799 O  O   . LEU B 1 79  ? 15.243  1.991   -66.029 1.00 17.77 ?  81  LEU B O   1 
ATOM   3800 C  CB  . LEU B 1 79  ? 16.960  4.063   -64.243 1.00 17.87 ?  81  LEU B CB  1 
ATOM   3801 C  CG  . LEU B 1 79  ? 17.002  4.619   -62.822 1.00 16.72 ?  81  LEU B CG  1 
ATOM   3802 C  CD1 . LEU B 1 79  ? 17.254  6.115   -62.885 1.00 18.06 ?  81  LEU B CD1 1 
ATOM   3803 C  CD2 . LEU B 1 79  ? 15.720  4.318   -62.071 1.00 19.81 ?  81  LEU B CD2 1 
ATOM   3804 N  N   . ARG B 1 80  ? 17.364  2.068   -66.736 1.00 20.00 ?  82  ARG B N   1 
ATOM   3805 C  CA  . ARG B 1 80  ? 16.917  1.710   -68.085 1.00 21.98 ?  82  ARG B CA  1 
ATOM   3806 C  C   . ARG B 1 80  ? 16.173  0.382   -68.096 1.00 22.82 ?  82  ARG B C   1 
ATOM   3807 O  O   . ARG B 1 80  ? 15.078  0.322   -68.685 1.00 24.16 ?  82  ARG B O   1 
ATOM   3808 C  CB  . ARG B 1 80  ? 18.092  1.724   -69.073 1.00 20.75 ?  82  ARG B CB  1 
ATOM   3809 C  CG  . ARG B 1 80  ? 18.588  3.117   -69.439 1.00 20.19 ?  82  ARG B CG  1 
ATOM   3810 C  CD  . ARG B 1 80  ? 19.600  3.045   -70.570 1.00 25.03 ?  82  ARG B CD  1 
ATOM   3811 N  NE  . ARG B 1 80  ? 20.876  2.510   -70.101 1.00 25.67 ?  82  ARG B NE  1 
ATOM   3812 C  CZ  . ARG B 1 80  ? 21.923  3.258   -69.774 1.00 26.37 ?  82  ARG B CZ  1 
ATOM   3813 N  NH1 . ARG B 1 80  ? 21.856  4.580   -69.882 1.00 24.98 ?  82  ARG B NH1 1 
ATOM   3814 N  NH2 . ARG B 1 80  ? 23.036  2.686   -69.338 1.00 28.16 ?  82  ARG B NH2 1 
ATOM   3815 N  N   . PRO B 1 81  ? 16.660  -0.689  -67.451 1.00 23.48 ?  83  PRO B N   1 
ATOM   3816 C  CA  . PRO B 1 81  ? 15.850  -1.919  -67.389 1.00 19.51 ?  83  PRO B CA  1 
ATOM   3817 C  C   . PRO B 1 81  ? 14.553  -1.763  -66.609 1.00 24.79 ?  83  PRO B C   1 
ATOM   3818 O  O   . PRO B 1 81  ? 13.528  -2.328  -67.010 1.00 22.14 ?  83  PRO B O   1 
ATOM   3819 C  CB  . PRO B 1 81  ? 16.798  -2.925  -66.714 1.00 21.46 ?  83  PRO B CB  1 
ATOM   3820 C  CG  . PRO B 1 81  ? 18.170  -2.404  -67.020 1.00 19.44 ?  83  PRO B CG  1 
ATOM   3821 C  CD  . PRO B 1 81  ? 18.019  -0.917  -66.914 1.00 19.27 ?  83  PRO B CD  1 
ATOM   3822 N  N   . ILE B 1 82  ? 14.566  -1.030  -65.492 1.00 18.15 ?  84  ILE B N   1 
ATOM   3823 C  CA  . ILE B 1 82  ? 13.334  -0.823  -64.729 1.00 17.24 ?  84  ILE B CA  1 
ATOM   3824 C  C   . ILE B 1 82  ? 12.304  -0.086  -65.576 1.00 19.49 ?  84  ILE B C   1 
ATOM   3825 O  O   . ILE B 1 82  ? 11.134  -0.482  -65.649 1.00 23.75 ?  84  ILE B O   1 
ATOM   3826 C  CB  . ILE B 1 82  ? 13.629  -0.063  -63.423 1.00 17.00 ?  84  ILE B CB  1 
ATOM   3827 C  CG1 . ILE B 1 82  ? 14.423  -0.943  -62.460 1.00 17.99 ?  84  ILE B CG1 1 
ATOM   3828 C  CG2 . ILE B 1 82  ? 12.330  0.408   -62.758 1.00 20.48 ?  84  ILE B CG2 1 
ATOM   3829 C  CD1 . ILE B 1 82  ? 14.951  -0.143  -61.259 1.00 17.48 ?  84  ILE B CD1 1 
ATOM   3830 N  N   . LEU B 1 83  ? 12.725  0.996   -66.229 1.00 18.99 ?  85  LEU B N   1 
ATOM   3831 C  CA  . LEU B 1 83  ? 11.783  1.814   -66.985 1.00 20.30 ?  85  LEU B CA  1 
ATOM   3832 C  C   . LEU B 1 83  ? 11.232  1.051   -68.184 1.00 26.34 ?  85  LEU B C   1 
ATOM   3833 O  O   . LEU B 1 83  ? 10.044  1.168   -68.509 1.00 23.96 ?  85  LEU B O   1 
ATOM   3834 C  CB  . LEU B 1 83  ? 12.464  3.110   -67.422 1.00 20.86 ?  85  LEU B CB  1 
ATOM   3835 C  CG  . LEU B 1 83  ? 12.740  4.073   -66.258 1.00 21.74 ?  85  LEU B CG  1 
ATOM   3836 C  CD1 . LEU B 1 83  ? 13.701  5.183   -66.655 1.00 18.70 ?  85  LEU B CD1 1 
ATOM   3837 C  CD2 . LEU B 1 83  ? 11.445  4.657   -65.728 1.00 21.75 ?  85  LEU B CD2 1 
ATOM   3838 N  N   . ARG B 1 84  ? 12.077  0.259   -68.846 1.00 24.83 ?  86  ARG B N   1 
ATOM   3839 C  CA  . ARG B 1 84  ? 11.609  -0.552  -69.966 1.00 25.30 ?  86  ARG B CA  1 
ATOM   3840 C  C   . ARG B 1 84  ? 10.553  -1.552  -69.512 1.00 28.34 ?  86  ARG B C   1 
ATOM   3841 O  O   . ARG B 1 84  ? 9.573   -1.801  -70.225 1.00 29.61 ?  86  ARG B O   1 
ATOM   3842 C  CB  . ARG B 1 84  ? 12.795  -1.266  -70.621 1.00 24.31 ?  86  ARG B CB  1 
ATOM   3843 N  N   . THR B 1 85  ? 10.728  -2.124  -68.320 1.00 22.22 ?  87  THR B N   1 
ATOM   3844 C  CA  . THR B 1 85  ? 9.744   -3.057  -67.782 1.00 25.17 ?  87  THR B CA  1 
ATOM   3845 C  C   . THR B 1 85  ? 8.423   -2.356  -67.494 1.00 31.00 ?  87  THR B C   1 
ATOM   3846 O  O   . THR B 1 85  ? 7.352   -2.862  -67.851 1.00 26.79 ?  87  THR B O   1 
ATOM   3847 C  CB  . THR B 1 85  ? 10.285  -3.716  -66.513 1.00 25.06 ?  87  THR B CB  1 
ATOM   3848 O  OG1 . THR B 1 85  ? 11.482  -4.440  -66.818 1.00 25.64 ?  87  THR B OG1 1 
ATOM   3849 C  CG2 . THR B 1 85  ? 9.256   -4.661  -65.917 1.00 27.75 ?  87  THR B CG2 1 
ATOM   3850 N  N   . LEU B 1 86  ? 8.481   -1.185  -66.850 1.00 26.03 ?  88  LEU B N   1 
ATOM   3851 C  CA  . LEU B 1 86  ? 7.261   -0.443  -66.532 1.00 25.81 ?  88  LEU B CA  1 
ATOM   3852 C  C   . LEU B 1 86  ? 6.486   -0.082  -67.796 1.00 31.87 ?  88  LEU B C   1 
ATOM   3853 O  O   . LEU B 1 86  ? 5.253   -0.179  -67.828 1.00 29.06 ?  88  LEU B O   1 
ATOM   3854 C  CB  . LEU B 1 86  ? 7.616   0.811   -65.729 1.00 27.82 ?  88  LEU B CB  1 
ATOM   3855 C  CG  . LEU B 1 86  ? 8.182   0.534   -64.328 1.00 23.41 ?  88  LEU B CG  1 
ATOM   3856 C  CD1 . LEU B 1 86  ? 8.066   1.737   -63.402 1.00 24.15 ?  88  LEU B CD1 1 
ATOM   3857 C  CD2 . LEU B 1 86  ? 7.525   -0.673  -63.701 1.00 24.47 ?  88  LEU B CD2 1 
ATOM   3858 N  N   . HIS B 1 87  ? 7.193   0.316   -68.856 1.00 25.77 ?  89  HIS B N   1 
ATOM   3859 C  CA  . HIS B 1 87  ? 6.510   0.647   -70.103 1.00 33.61 ?  89  HIS B CA  1 
ATOM   3860 C  C   . HIS B 1 87  ? 5.859   -0.583  -70.717 1.00 36.39 ?  89  HIS B C   1 
ATOM   3861 O  O   . HIS B 1 87  ? 4.733   -0.505  -71.221 1.00 35.25 ?  89  HIS B O   1 
ATOM   3862 C  CB  . HIS B 1 87  ? 7.480   1.291   -71.092 1.00 28.43 ?  89  HIS B CB  1 
ATOM   3863 C  CG  . HIS B 1 87  ? 7.845   2.699   -70.737 1.00 36.15 ?  89  HIS B CG  1 
ATOM   3864 N  ND1 . HIS B 1 87  ? 6.900   3.666   -70.463 1.00 40.17 ?  89  HIS B ND1 1 
ATOM   3865 C  CD2 . HIS B 1 87  ? 9.051   3.304   -70.607 1.00 40.74 ?  89  HIS B CD2 1 
ATOM   3866 C  CE1 . HIS B 1 87  ? 7.508   4.805   -70.178 1.00 37.79 ?  89  HIS B CE1 1 
ATOM   3867 N  NE2 . HIS B 1 87  ? 8.813   4.613   -70.259 1.00 45.09 ?  89  HIS B NE2 1 
ATOM   3868 N  N   . ALA B 1 88  ? 6.543   -1.729  -70.672 1.00 29.82 ?  90  ALA B N   1 
ATOM   3869 C  CA  . ALA B 1 88  ? 5.960   -2.953  -71.206 1.00 35.05 ?  90  ALA B CA  1 
ATOM   3870 C  C   . ALA B 1 88  ? 4.690   -3.355  -70.465 1.00 39.68 ?  90  ALA B C   1 
ATOM   3871 O  O   . ALA B 1 88  ? 3.855   -4.068  -71.032 1.00 33.40 ?  90  ALA B O   1 
ATOM   3872 C  CB  . ALA B 1 88  ? 6.980   -4.089  -71.157 1.00 26.33 ?  90  ALA B CB  1 
ATOM   3873 N  N   . ALA B 1 89  ? 4.522   -2.920  -69.220 1.00 34.82 ?  91  ALA B N   1 
ATOM   3874 C  CA  . ALA B 1 89  ? 3.308   -3.201  -68.467 1.00 33.67 ?  91  ALA B CA  1 
ATOM   3875 C  C   . ALA B 1 89  ? 2.229   -2.148  -68.675 1.00 33.31 ?  91  ALA B C   1 
ATOM   3876 O  O   . ALA B 1 89  ? 1.172   -2.232  -68.044 1.00 31.55 ?  91  ALA B O   1 
ATOM   3877 C  CB  . ALA B 1 89  ? 3.624   -3.322  -66.972 1.00 34.93 ?  91  ALA B CB  1 
ATOM   3878 N  N   . GLY B 1 90  ? 2.475   -1.149  -69.516 1.00 30.77 ?  92  GLY B N   1 
ATOM   3879 C  CA  . GLY B 1 90  ? 1.464   -0.174  -69.851 1.00 31.05 ?  92  GLY B CA  1 
ATOM   3880 C  C   . GLY B 1 90  ? 1.595   1.179   -69.189 1.00 39.54 ?  92  GLY B C   1 
ATOM   3881 O  O   . GLY B 1 90  ? 0.788   2.065   -69.486 1.00 39.13 ?  92  GLY B O   1 
ATOM   3882 N  N   . LEU B 1 91  ? 2.574   1.382   -68.305 1.00 37.41 ?  93  LEU B N   1 
ATOM   3883 C  CA  . LEU B 1 91  ? 2.688   2.677   -67.650 1.00 36.77 ?  93  LEU B CA  1 
ATOM   3884 C  C   . LEU B 1 91  ? 3.311   3.685   -68.608 1.00 35.22 ?  93  LEU B C   1 
ATOM   3885 O  O   . LEU B 1 91  ? 4.368   3.430   -69.195 1.00 38.66 ?  93  LEU B O   1 
ATOM   3886 C  CB  . LEU B 1 91  ? 3.509   2.592   -66.360 1.00 30.01 ?  93  LEU B CB  1 
ATOM   3887 C  CG  . LEU B 1 91  ? 2.844   2.000   -65.113 1.00 32.08 ?  93  LEU B CG  1 
ATOM   3888 C  CD1 . LEU B 1 91  ? 2.730   0.482   -65.182 1.00 31.79 ?  93  LEU B CD1 1 
ATOM   3889 C  CD2 . LEU B 1 91  ? 3.536   2.459   -63.832 1.00 33.01 ?  93  LEU B CD2 1 
ATOM   3890 N  N   . ALA B 1 92  ? 2.651   4.829   -68.766 1.00 36.87 ?  94  ALA B N   1 
ATOM   3891 C  CA  . ALA B 1 92  ? 3.202   5.906   -69.572 1.00 33.61 ?  94  ALA B CA  1 
ATOM   3892 C  C   . ALA B 1 92  ? 4.157   6.757   -68.741 1.00 38.10 ?  94  ALA B C   1 
ATOM   3893 O  O   . ALA B 1 92  ? 4.181   6.689   -67.508 1.00 38.77 ?  94  ALA B O   1 
ATOM   3894 C  CB  . ALA B 1 92  ? 2.087   6.779   -70.146 1.00 38.81 ?  94  ALA B CB  1 
ATOM   3895 N  N   . THR B 1 93  ? 4.946   7.575   -69.443 1.00 35.55 ?  95  THR B N   1 
ATOM   3896 C  CA  . THR B 1 93  ? 5.925   8.431   -68.779 1.00 38.64 ?  95  THR B CA  1 
ATOM   3897 C  C   . THR B 1 93  ? 5.291   9.276   -67.681 1.00 41.56 ?  95  THR B C   1 
ATOM   3898 O  O   . THR B 1 93  ? 5.885   9.469   -66.612 1.00 42.11 ?  95  THR B O   1 
ATOM   3899 C  CB  . THR B 1 93  ? 6.616   9.318   -69.815 1.00 39.17 ?  95  THR B CB  1 
ATOM   3900 O  OG1 . THR B 1 93  ? 7.425   8.504   -70.676 1.00 44.15 ?  95  THR B OG1 1 
ATOM   3901 C  CG2 . THR B 1 93  ? 7.484   10.374  -69.145 1.00 43.96 ?  95  THR B CG2 1 
ATOM   3902 N  N   . GLN B 1 94  ? 4.075   9.775   -67.915 1.00 35.21 ?  96  GLN B N   1 
ATOM   3903 C  CA  . GLN B 1 94  ? 3.407   10.602  -66.916 1.00 33.10 ?  96  GLN B CA  1 
ATOM   3904 C  C   . GLN B 1 94  ? 3.019   9.819   -65.665 1.00 29.17 ?  96  GLN B C   1 
ATOM   3905 O  O   . GLN B 1 94  ? 2.774   10.430  -64.621 1.00 37.58 ?  96  GLN B O   1 
ATOM   3906 C  CB  . GLN B 1 94  ? 2.161   11.254  -67.529 1.00 37.73 ?  96  GLN B CB  1 
ATOM   3907 N  N   . ASP B 1 95  ? 2.938   8.492   -65.746 1.00 29.71 ?  97  ASP B N   1 
ATOM   3908 C  CA  . ASP B 1 95  ? 2.536   7.668   -64.613 1.00 32.78 ?  97  ASP B CA  1 
ATOM   3909 C  C   . ASP B 1 95  ? 3.710   7.310   -63.708 1.00 29.59 ?  97  ASP B C   1 
ATOM   3910 O  O   . ASP B 1 95  ? 3.511   6.644   -62.686 1.00 29.06 ?  97  ASP B O   1 
ATOM   3911 C  CB  . ASP B 1 95  ? 1.864   6.376   -65.105 1.00 30.52 ?  97  ASP B CB  1 
ATOM   3912 C  CG  . ASP B 1 95  ? 0.667   6.641   -66.022 1.00 44.95 ?  97  ASP B CG  1 
ATOM   3913 O  OD1 . ASP B 1 95  ? 0.409   5.807   -66.921 1.00 40.59 ?  97  ASP B OD1 1 
ATOM   3914 O  OD2 . ASP B 1 95  ? -0.012  7.678   -65.841 1.00 39.62 ?  97  ASP B OD2 1 
ATOM   3915 N  N   . ILE B 1 96  ? 4.919   7.728   -64.068 1.00 30.31 ?  98  ILE B N   1 
ATOM   3916 C  CA  . ILE B 1 96  ? 6.146   7.312   -63.395 1.00 26.22 ?  98  ILE B CA  1 
ATOM   3917 C  C   . ILE B 1 96  ? 6.828   8.541   -62.814 1.00 23.24 ?  98  ILE B C   1 
ATOM   3918 O  O   . ILE B 1 96  ? 6.992   9.555   -63.504 1.00 30.84 ?  98  ILE B O   1 
ATOM   3919 C  CB  . ILE B 1 96  ? 7.096   6.565   -64.350 1.00 29.78 ?  98  ILE B CB  1 
ATOM   3920 C  CG1 . ILE B 1 96  ? 6.431   5.299   -64.885 1.00 28.76 ?  98  ILE B CG1 1 
ATOM   3921 C  CG2 . ILE B 1 96  ? 8.431   6.236   -63.650 1.00 23.86 ?  98  ILE B CG2 1 
ATOM   3922 C  CD1 . ILE B 1 96  ? 7.096   4.738   -66.122 1.00 30.74 ?  98  ILE B CD1 1 
ATOM   3923 N  N   . LEU B 1 97  ? 7.228   8.448   -61.549 1.00 23.08 ?  99  LEU B N   1 
ATOM   3924 C  CA  . LEU B 1 97  ? 7.964   9.513   -60.886 1.00 22.73 ?  99  LEU B CA  1 
ATOM   3925 C  C   . LEU B 1 97  ? 9.273   8.940   -60.369 1.00 20.66 ?  99  LEU B C   1 
ATOM   3926 O  O   . LEU B 1 97  ? 9.275   7.903   -59.701 1.00 21.67 ?  99  LEU B O   1 
ATOM   3927 C  CB  . LEU B 1 97  ? 7.171   10.122  -59.724 1.00 23.01 ?  99  LEU B CB  1 
ATOM   3928 C  CG  . LEU B 1 97  ? 7.976   11.050  -58.798 1.00 20.85 ?  99  LEU B CG  1 
ATOM   3929 C  CD1 . LEU B 1 97  ? 8.286   12.367  -59.481 1.00 19.85 ?  99  LEU B CD1 1 
ATOM   3930 C  CD2 . LEU B 1 97  ? 7.245   11.295  -57.495 1.00 23.87 ?  99  LEU B CD2 1 
ATOM   3931 N  N   . ILE B 1 98  ? 10.372  9.606   -60.694 1.00 20.46 ?  100 ILE B N   1 
ATOM   3932 C  CA  . ILE B 1 98  ? 11.667  9.331   -60.082 1.00 16.92 ?  100 ILE B CA  1 
ATOM   3933 C  C   . ILE B 1 98  ? 11.822  10.342  -58.951 1.00 16.11 ?  100 ILE B C   1 
ATOM   3934 O  O   . ILE B 1 98  ? 11.895  11.553  -59.200 1.00 20.49 ?  100 ILE B O   1 
ATOM   3935 C  CB  . ILE B 1 98  ? 12.812  9.441   -61.101 1.00 20.98 ?  100 ILE B CB  1 
ATOM   3936 C  CG1 . ILE B 1 98  ? 12.673  8.364   -62.182 1.00 23.48 ?  100 ILE B CG1 1 
ATOM   3937 C  CG2 . ILE B 1 98  ? 14.176  9.259   -60.397 1.00 18.99 ?  100 ILE B CG2 1 
ATOM   3938 C  CD1 . ILE B 1 98  ? 13.644  8.535   -63.352 1.00 20.53 ?  100 ILE B CD1 1 
ATOM   3939 N  N   . LEU B 1 99  ? 11.854  9.851   -57.714 1.00 17.54 ?  101 LEU B N   1 
ATOM   3940 C  CA  . LEU B 1 99  ? 11.931  10.684  -56.517 1.00 18.12 ?  101 LEU B CA  1 
ATOM   3941 C  C   . LEU B 1 99  ? 13.332  10.563  -55.915 1.00 15.49 ?  101 LEU B C   1 
ATOM   3942 O  O   . LEU B 1 99  ? 13.739  9.464   -55.521 1.00 16.87 ?  101 LEU B O   1 
ATOM   3943 C  CB  . LEU B 1 99  ? 10.874  10.250  -55.499 1.00 15.90 ?  101 LEU B CB  1 
ATOM   3944 C  CG  . LEU B 1 99  ? 10.739  11.085  -54.219 1.00 18.42 ?  101 LEU B CG  1 
ATOM   3945 C  CD1 . LEU B 1 99  ? 10.475  12.538  -54.533 1.00 21.52 ?  101 LEU B CD1 1 
ATOM   3946 C  CD2 . LEU B 1 99  ? 9.687   10.524  -53.285 1.00 18.22 ?  101 LEU B CD2 1 
ATOM   3947 N  N   . VAL B 1 100 ? 14.057  11.676  -55.852 1.00 15.30 ?  102 VAL B N   1 
ATOM   3948 C  CA  . VAL B 1 100 ? 15.409  11.677  -55.291 1.00 16.29 ?  102 VAL B CA  1 
ATOM   3949 C  C   . VAL B 1 100 ? 15.293  11.623  -53.771 1.00 16.83 ?  102 VAL B C   1 
ATOM   3950 O  O   . VAL B 1 100 ? 14.801  12.566  -53.142 1.00 16.02 ?  102 VAL B O   1 
ATOM   3951 C  CB  . VAL B 1 100 ? 16.206  12.907  -55.743 1.00 16.23 ?  102 VAL B CB  1 
ATOM   3952 C  CG1 . VAL B 1 100 ? 17.640  12.882  -55.148 1.00 14.19 ?  102 VAL B CG1 1 
ATOM   3953 C  CG2 . VAL B 1 100 ? 16.260  12.981  -57.277 1.00 16.06 ?  102 VAL B CG2 1 
ATOM   3954 N  N   . ALA B 1 101 ? 15.752  10.518  -53.182 1.00 15.33 ?  103 ALA B N   1 
ATOM   3955 C  CA  . ALA B 1 101 ? 15.615  10.266  -51.750 1.00 11.62 ?  103 ALA B CA  1 
ATOM   3956 C  C   . ALA B 1 101 ? 16.762  10.961  -51.016 1.00 17.81 ?  103 ALA B C   1 
ATOM   3957 O  O   . ALA B 1 101 ? 17.754  10.356  -50.598 1.00 14.99 ?  103 ALA B O   1 
ATOM   3958 C  CB  . ALA B 1 101 ? 15.567  8.764   -51.483 1.00 11.89 ?  103 ALA B CB  1 
ATOM   3959 N  N   . THR B 1 102 ? 16.604  12.275  -50.848 1.00 13.87 ?  104 THR B N   1 
ATOM   3960 C  CA  . THR B 1 102 ? 17.596  13.124  -50.198 1.00 15.90 ?  104 THR B CA  1 
ATOM   3961 C  C   . THR B 1 102 ? 17.733  12.868  -48.699 1.00 14.39 ?  104 THR B C   1 
ATOM   3962 O  O   . THR B 1 102 ? 18.729  13.295  -48.108 1.00 15.34 ?  104 THR B O   1 
ATOM   3963 C  CB  . THR B 1 102 ? 17.222  14.596  -50.394 1.00 14.34 ?  104 THR B CB  1 
ATOM   3964 O  OG1 . THR B 1 102 ? 15.874  14.768  -49.944 1.00 16.11 ?  104 THR B OG1 1 
ATOM   3965 C  CG2 . THR B 1 102 ? 17.337  15.003  -51.868 1.00 14.49 ?  104 THR B CG2 1 
ATOM   3966 N  N   . GLY B 1 103 ? 16.763  12.220  -48.063 1.00 15.74 ?  105 GLY B N   1 
ATOM   3967 C  CA  . GLY B 1 103 ? 16.761  12.243  -46.611 1.00 14.51 ?  105 GLY B CA  1 
ATOM   3968 C  C   . GLY B 1 103 ? 16.546  13.675  -46.168 1.00 18.05 ?  105 GLY B C   1 
ATOM   3969 O  O   . GLY B 1 103 ? 15.587  14.333  -46.586 1.00 18.59 ?  105 GLY B O   1 
ATOM   3970 N  N   . LEU B 1 104 ? 17.447  14.185  -45.329 1.00 14.97 ?  106 LEU B N   1 
ATOM   3971 C  CA  . LEU B 1 104 ? 17.452  15.603  -44.987 1.00 15.33 ?  106 LEU B CA  1 
ATOM   3972 C  C   . LEU B 1 104 ? 18.529  16.397  -45.711 1.00 17.12 ?  106 LEU B C   1 
ATOM   3973 O  O   . LEU B 1 104 ? 18.752  17.565  -45.368 1.00 16.80 ?  106 LEU B O   1 
ATOM   3974 C  CB  . LEU B 1 104 ? 17.581  15.795  -43.470 1.00 18.45 ?  106 LEU B CB  1 
ATOM   3975 C  CG  . LEU B 1 104 ? 16.269  15.886  -42.688 1.00 18.79 ?  106 LEU B CG  1 
ATOM   3976 C  CD1 . LEU B 1 104 ? 15.575  17.184  -43.071 1.00 19.88 ?  106 LEU B CD1 1 
ATOM   3977 C  CD2 . LEU B 1 104 ? 15.336  14.716  -42.962 1.00 14.30 ?  106 LEU B CD2 1 
ATOM   3978 N  N   . HIS B 1 105 ? 19.181  15.815  -46.715 1.00 13.28 ?  107 HIS B N   1 
ATOM   3979 C  CA  . HIS B 1 105 ? 20.139  16.587  -47.484 1.00 14.56 ?  107 HIS B CA  1 
ATOM   3980 C  C   . HIS B 1 105 ? 19.400  17.648  -48.294 1.00 16.11 ?  107 HIS B C   1 
ATOM   3981 O  O   . HIS B 1 105 ? 18.180  17.573  -48.498 1.00 16.03 ?  107 HIS B O   1 
ATOM   3982 C  CB  . HIS B 1 105 ? 20.939  15.702  -48.453 1.00 13.92 ?  107 HIS B CB  1 
ATOM   3983 C  CG  . HIS B 1 105 ? 21.683  14.576  -47.796 1.00 13.83 ?  107 HIS B CG  1 
ATOM   3984 N  ND1 . HIS B 1 105 ? 22.098  13.458  -48.491 1.00 12.92 ?  107 HIS B ND1 1 
ATOM   3985 C  CD2 . HIS B 1 105 ? 22.095  14.399  -46.517 1.00 15.54 ?  107 HIS B CD2 1 
ATOM   3986 C  CE1 . HIS B 1 105 ? 22.727  12.638  -47.665 1.00 11.87 ?  107 HIS B CE1 1 
ATOM   3987 N  NE2 . HIS B 1 105 ? 22.741  13.185  -46.462 1.00 13.49 ?  107 HIS B NE2 1 
ATOM   3988 N  N   . ARG B 1 106 ? 20.164  18.629  -48.773 1.00 16.12 ?  108 ARG B N   1 
ATOM   3989 C  CA  . ARG B 1 106 ? 19.667  19.602  -49.737 1.00 20.01 ?  108 ARG B CA  1 
ATOM   3990 C  C   . ARG B 1 106 ? 19.174  18.890  -50.995 1.00 19.43 ?  108 ARG B C   1 
ATOM   3991 O  O   . ARG B 1 106 ? 19.588  17.766  -51.281 1.00 14.84 ?  108 ARG B O   1 
ATOM   3992 C  CB  . ARG B 1 106 ? 20.776  20.578  -50.121 1.00 17.19 ?  108 ARG B CB  1 
ATOM   3993 C  CG  . ARG B 1 106 ? 22.034  19.887  -50.643 1.00 16.17 ?  108 ARG B CG  1 
ATOM   3994 C  CD  . ARG B 1 106 ? 22.868  20.823  -51.492 1.00 18.29 ?  108 ARG B CD  1 
ATOM   3995 N  NE  . ARG B 1 106 ? 24.061  20.177  -52.042 1.00 18.03 ?  108 ARG B NE  1 
ATOM   3996 C  CZ  . ARG B 1 106 ? 24.080  19.493  -53.183 1.00 19.15 ?  108 ARG B CZ  1 
ATOM   3997 N  NH1 . ARG B 1 106 ? 22.968  19.326  -53.883 1.00 17.33 ?  108 ARG B NH1 1 
ATOM   3998 N  NH2 . ARG B 1 106 ? 25.209  18.955  -53.620 1.00 21.50 ?  108 ARG B NH2 1 
ATOM   3999 N  N   . PRO B 1 107 ? 18.302  19.530  -51.779 1.00 20.23 ?  109 PRO B N   1 
ATOM   4000 C  CA  . PRO B 1 107 ? 17.868  18.908  -53.037 1.00 18.81 ?  109 PRO B CA  1 
ATOM   4001 C  C   . PRO B 1 107 ? 19.016  18.821  -54.031 1.00 16.59 ?  109 PRO B C   1 
ATOM   4002 O  O   . PRO B 1 107 ? 19.986  19.584  -53.968 1.00 16.52 ?  109 PRO B O   1 
ATOM   4003 C  CB  . PRO B 1 107 ? 16.761  19.846  -53.542 1.00 18.99 ?  109 PRO B CB  1 
ATOM   4004 C  CG  . PRO B 1 107 ? 17.101  21.171  -52.944 1.00 19.71 ?  109 PRO B CG  1 
ATOM   4005 C  CD  . PRO B 1 107 ? 17.670  20.848  -51.570 1.00 21.35 ?  109 PRO B CD  1 
ATOM   4006 N  N   . SER B 1 108 ? 18.911  17.848  -54.929 1.00 16.71 ?  110 SER B N   1 
ATOM   4007 C  CA  . SER B 1 108 ? 19.852  17.742  -56.030 1.00 15.54 ?  110 SER B CA  1 
ATOM   4008 C  C   . SER B 1 108 ? 19.641  18.894  -57.005 1.00 23.20 ?  110 SER B C   1 
ATOM   4009 O  O   . SER B 1 108 ? 18.519  19.368  -57.207 1.00 26.27 ?  110 SER B O   1 
ATOM   4010 C  CB  . SER B 1 108 ? 19.692  16.404  -56.764 1.00 21.11 ?  110 SER B CB  1 
ATOM   4011 O  OG  . SER B 1 108 ? 18.377  16.244  -57.285 1.00 22.07 ?  110 SER B OG  1 
ATOM   4012 N  N   . THR B 1 109 ? 20.737  19.347  -57.604 1.00 22.22 ?  111 THR B N   1 
ATOM   4013 C  CA  . THR B 1 109 ? 20.677  20.384  -58.621 1.00 22.44 ?  111 THR B CA  1 
ATOM   4014 C  C   . THR B 1 109 ? 20.315  19.772  -59.972 1.00 27.73 ?  111 THR B C   1 
ATOM   4015 O  O   . THR B 1 109 ? 20.342  18.550  -60.135 1.00 21.86 ?  111 THR B O   1 
ATOM   4016 C  CB  . THR B 1 109 ? 22.017  21.117  -58.691 1.00 29.45 ?  111 THR B CB  1 
ATOM   4017 O  OG1 . THR B 1 109 ? 23.032  20.226  -59.169 1.00 24.56 ?  111 THR B OG1 1 
ATOM   4018 C  CG2 . THR B 1 109 ? 22.414  21.642  -57.319 1.00 28.80 ?  111 THR B CG2 1 
ATOM   4019 N  N   . PRO B 1 110 ? 19.912  20.597  -60.950 1.00 28.93 ?  112 PRO B N   1 
ATOM   4020 C  CA  . PRO B 1 110 ? 19.732  20.061  -62.315 1.00 28.22 ?  112 PRO B CA  1 
ATOM   4021 C  C   . PRO B 1 110 ? 20.969  19.362  -62.871 1.00 23.65 ?  112 PRO B C   1 
ATOM   4022 O  O   . PRO B 1 110 ? 20.849  18.271  -63.446 1.00 25.27 ?  112 PRO B O   1 
ATOM   4023 C  CB  . PRO B 1 110 ? 19.355  21.318  -63.116 1.00 30.47 ?  112 PRO B CB  1 
ATOM   4024 C  CG  . PRO B 1 110 ? 18.616  22.161  -62.097 1.00 27.43 ?  112 PRO B CG  1 
ATOM   4025 C  CD  . PRO B 1 110 ? 19.446  21.996  -60.849 1.00 30.40 ?  112 PRO B CD  1 
ATOM   4026 N  N   . ALA B 1 111 ? 22.156  19.957  -62.717 1.00 25.44 ?  113 ALA B N   1 
ATOM   4027 C  CA  . ALA B 1 111 ? 23.372  19.313  -63.207 1.00 24.58 ?  113 ALA B CA  1 
ATOM   4028 C  C   . ALA B 1 111 ? 23.623  17.988  -62.498 1.00 27.35 ?  113 ALA B C   1 
ATOM   4029 O  O   . ALA B 1 111 ? 24.113  17.033  -63.111 1.00 25.58 ?  113 ALA B O   1 
ATOM   4030 C  CB  . ALA B 1 111 ? 24.578  20.237  -63.039 1.00 25.49 ?  113 ALA B CB  1 
ATOM   4031 N  N   . GLU B 1 112 ? 23.303  17.911  -61.204 1.00 23.02 ?  114 GLU B N   1 
ATOM   4032 C  CA  . GLU B 1 112 ? 23.472  16.648  -60.491 1.00 20.75 ?  114 GLU B CA  1 
ATOM   4033 C  C   . GLU B 1 112 ? 22.494  15.594  -60.994 1.00 22.61 ?  114 GLU B C   1 
ATOM   4034 O  O   . GLU B 1 112 ? 22.846  14.414  -61.094 1.00 22.47 ?  114 GLU B O   1 
ATOM   4035 C  CB  . GLU B 1 112 ? 23.305  16.865  -58.985 1.00 23.99 ?  114 GLU B CB  1 
ATOM   4036 C  CG  . GLU B 1 112 ? 24.547  17.463  -58.336 1.00 22.50 ?  114 GLU B CG  1 
ATOM   4037 C  CD  . GLU B 1 112 ? 24.323  17.940  -56.911 1.00 23.35 ?  114 GLU B CD  1 
ATOM   4038 O  OE1 . GLU B 1 112 ? 23.173  17.945  -56.441 1.00 18.31 ?  114 GLU B OE1 1 
ATOM   4039 O  OE2 . GLU B 1 112 ? 25.314  18.331  -56.263 1.00 23.72 ?  114 GLU B OE2 1 
ATOM   4040 N  N   . LYS B 1 113 ? 21.263  15.992  -61.320 1.00 20.46 ?  115 LYS B N   1 
ATOM   4041 C  CA  . LYS B 1 113 ? 20.308  15.013  -61.824 1.00 19.07 ?  115 LYS B CA  1 
ATOM   4042 C  C   . LYS B 1 113 ? 20.825  14.375  -63.103 1.00 19.96 ?  115 LYS B C   1 
ATOM   4043 O  O   . LYS B 1 113 ? 20.661  13.168  -63.312 1.00 21.13 ?  115 LYS B O   1 
ATOM   4044 C  CB  . LYS B 1 113 ? 18.938  15.658  -62.048 1.00 21.89 ?  115 LYS B CB  1 
ATOM   4045 C  CG  . LYS B 1 113 ? 18.127  15.824  -60.774 1.00 19.51 ?  115 LYS B CG  1 
ATOM   4046 C  CD  . LYS B 1 113 ? 16.787  16.538  -61.027 1.00 19.40 ?  115 LYS B CD  1 
ATOM   4047 C  CE  . LYS B 1 113 ? 16.092  16.836  -59.700 1.00 19.64 ?  115 LYS B CE  1 
ATOM   4048 N  NZ  . LYS B 1 113 ? 16.733  18.017  -59.006 1.00 18.69 ?  115 LYS B NZ  1 
ATOM   4049 N  N   . VAL B 1 114 ? 21.496  15.163  -63.946 1.00 20.16 ?  116 VAL B N   1 
ATOM   4050 C  CA  . VAL B 1 114 ? 22.078  14.612  -65.163 1.00 24.63 ?  116 VAL B CA  1 
ATOM   4051 C  C   . VAL B 1 114 ? 23.251  13.703  -64.823 1.00 27.16 ?  116 VAL B C   1 
ATOM   4052 O  O   . VAL B 1 114 ? 23.384  12.610  -65.388 1.00 27.61 ?  116 VAL B O   1 
ATOM   4053 C  CB  . VAL B 1 114 ? 22.485  15.747  -66.123 1.00 30.91 ?  116 VAL B CB  1 
ATOM   4054 C  CG1 . VAL B 1 114 ? 23.418  15.227  -67.215 1.00 31.38 ?  116 VAL B CG1 1 
ATOM   4055 C  CG2 . VAL B 1 114 ? 21.242  16.369  -66.736 1.00 26.25 ?  116 VAL B CG2 1 
ATOM   4056 N  N   . GLU B 1 115 ? 24.111  14.134  -63.889 1.00 23.93 ?  117 GLU B N   1 
ATOM   4057 C  CA  . GLU B 1 115 ? 25.221  13.287  -63.458 1.00 24.55 ?  117 GLU B CA  1 
ATOM   4058 C  C   . GLU B 1 115 ? 24.701  11.992  -62.840 1.00 27.10 ?  117 GLU B C   1 
ATOM   4059 O  O   . GLU B 1 115 ? 25.250  10.914  -63.093 1.00 30.97 ?  117 GLU B O   1 
ATOM   4060 C  CB  . GLU B 1 115 ? 26.124  14.046  -62.467 1.00 25.53 ?  117 GLU B CB  1 
ATOM   4061 C  CG  . GLU B 1 115 ? 27.221  13.188  -61.806 1.00 29.86 ?  117 GLU B CG  1 
ATOM   4062 C  CD  . GLU B 1 115 ? 28.107  13.965  -60.821 1.00 35.65 ?  117 GLU B CD  1 
ATOM   4063 O  OE1 . GLU B 1 115 ? 28.018  15.215  -60.774 1.00 34.73 ?  117 GLU B OE1 1 
ATOM   4064 O  OE2 . GLU B 1 115 ? 28.901  13.324  -60.086 1.00 34.59 ?  117 GLU B OE2 1 
ATOM   4065 N  N   . MET B 1 116 ? 23.617  12.072  -62.054 1.00 19.82 ?  118 MET B N   1 
ATOM   4066 C  CA  . MET B 1 116 ? 23.092  10.868  -61.404 1.00 17.13 ?  118 MET B CA  1 
ATOM   4067 C  C   . MET B 1 116 ? 22.388  9.946   -62.392 1.00 22.69 ?  118 MET B C   1 
ATOM   4068 O  O   . MET B 1 116 ? 22.519  8.719   -62.306 1.00 19.98 ?  118 MET B O   1 
ATOM   4069 C  CB  . MET B 1 116 ? 22.095  11.200  -60.282 1.00 18.61 ?  118 MET B CB  1 
ATOM   4070 C  CG  . MET B 1 116 ? 22.643  11.716  -58.957 1.00 24.15 ?  118 MET B CG  1 
ATOM   4071 S  SD  . MET B 1 116 ? 21.591  13.001  -58.243 1.00 25.50 ?  118 MET B SD  1 
ATOM   4072 C  CE  . MET B 1 116 ? 19.997  12.200  -58.212 1.00 27.09 ?  118 MET B CE  1 
ATOM   4073 N  N   . LEU B 1 117 ? 21.593  10.508  -63.305 1.00 21.05 ?  119 LEU B N   1 
ATOM   4074 C  CA  . LEU B 1 117 ? 20.549  9.742   -63.962 1.00 17.58 ?  119 LEU B CA  1 
ATOM   4075 C  C   . LEU B 1 117 ? 20.740  9.567   -65.464 1.00 23.17 ?  119 LEU B C   1 
ATOM   4076 O  O   . LEU B 1 117 ? 20.020  8.753   -66.057 1.00 24.03 ?  119 LEU B O   1 
ATOM   4077 C  CB  . LEU B 1 117 ? 19.187  10.416  -63.732 1.00 21.12 ?  119 LEU B CB  1 
ATOM   4078 C  CG  . LEU B 1 117 ? 18.713  10.548  -62.276 1.00 19.81 ?  119 LEU B CG  1 
ATOM   4079 C  CD1 . LEU B 1 117 ? 17.410  11.338  -62.242 1.00 25.26 ?  119 LEU B CD1 1 
ATOM   4080 C  CD2 . LEU B 1 117 ? 18.573  9.211   -61.572 1.00 24.46 ?  119 LEU B CD2 1 
ATOM   4081 N  N   . SER B 1 118 ? 21.684  10.295  -66.075 1.00 22.17 ?  120 SER B N   1 
ATOM   4082 C  CA  . SER B 1 118 ? 21.914  10.454  -67.516 1.00 31.81 ?  120 SER B CA  1 
ATOM   4083 C  C   . SER B 1 118 ? 21.030  11.563  -68.074 1.00 30.11 ?  120 SER B C   1 
ATOM   4084 O  O   . SER B 1 118 ? 19.906  11.767  -67.601 1.00 28.56 ?  120 SER B O   1 
ATOM   4085 C  CB  . SER B 1 118 ? 21.707  9.146   -68.297 1.00 25.21 ?  120 SER B CB  1 
ATOM   4086 O  OG  . SER B 1 118 ? 20.339  8.908   -68.602 1.00 24.79 ?  120 SER B OG  1 
ATOM   4087 N  N   . GLU B 1 119 ? 21.551  12.307  -69.058 1.00 31.29 ?  121 GLU B N   1 
ATOM   4088 C  CA  . GLU B 1 119 ? 20.787  13.404  -69.644 1.00 24.39 ?  121 GLU B CA  1 
ATOM   4089 C  C   . GLU B 1 119 ? 19.479  12.904  -70.239 1.00 28.69 ?  121 GLU B C   1 
ATOM   4090 O  O   . GLU B 1 119 ? 18.448  13.578  -70.137 1.00 29.88 ?  121 GLU B O   1 
ATOM   4091 C  CB  . GLU B 1 119 ? 21.627  14.124  -70.701 1.00 32.57 ?  121 GLU B CB  1 
ATOM   4092 C  CG  . GLU B 1 119 ? 21.347  15.622  -70.822 1.00 31.90 ?  121 GLU B CG  1 
ATOM   4093 N  N   . GLU B 1 120 ? 19.494  11.709  -70.835 1.00 28.56 ?  122 GLU B N   1 
ATOM   4094 C  CA  . GLU B 1 120 ? 18.291  11.169  -71.462 1.00 30.76 ?  122 GLU B CA  1 
ATOM   4095 C  C   . GLU B 1 120 ? 17.187  10.945  -70.436 1.00 31.58 ?  122 GLU B C   1 
ATOM   4096 O  O   . GLU B 1 120 ? 16.038  11.351  -70.645 1.00 28.09 ?  122 GLU B O   1 
ATOM   4097 C  CB  . GLU B 1 120 ? 18.620  9.869   -72.200 1.00 32.39 ?  122 GLU B CB  1 
ATOM   4098 N  N   . ILE B 1 121 ? 17.514  10.312  -69.307 1.00 27.05 ?  123 ILE B N   1 
ATOM   4099 C  CA  . ILE B 1 121 ? 16.481  10.050  -68.311 1.00 26.18 ?  123 ILE B CA  1 
ATOM   4100 C  C   . ILE B 1 121 ? 16.062  11.341  -67.617 1.00 28.95 ?  123 ILE B C   1 
ATOM   4101 O  O   . ILE B 1 121 ? 14.870  11.568  -67.367 1.00 26.54 ?  123 ILE B O   1 
ATOM   4102 C  CB  . ILE B 1 121 ? 16.953  8.980   -67.311 1.00 26.45 ?  123 ILE B CB  1 
ATOM   4103 C  CG1 . ILE B 1 121 ? 17.059  7.622   -68.010 1.00 24.34 ?  123 ILE B CG1 1 
ATOM   4104 C  CG2 . ILE B 1 121 ? 16.007  8.904   -66.113 1.00 23.96 ?  123 ILE B CG2 1 
ATOM   4105 C  CD1 . ILE B 1 121 ? 17.448  6.476   -67.089 1.00 28.31 ?  123 ILE B CD1 1 
ATOM   4106 N  N   . ALA B 1 122 ? 17.026  12.215  -67.316 1.00 27.29 ?  124 ALA B N   1 
ATOM   4107 C  CA  . ALA B 1 122 ? 16.713  13.456  -66.615 1.00 27.76 ?  124 ALA B CA  1 
ATOM   4108 C  C   . ALA B 1 122 ? 15.768  14.334  -67.428 1.00 33.63 ?  124 ALA B C   1 
ATOM   4109 O  O   . ALA B 1 122 ? 14.885  14.991  -66.865 1.00 28.10 ?  124 ALA B O   1 
ATOM   4110 C  CB  . ALA B 1 122 ? 18.003  14.210  -66.294 1.00 24.10 ?  124 ALA B CB  1 
ATOM   4111 N  N   . ARG B 1 123 ? 15.937  14.356  -68.757 1.00 27.75 ?  125 ARG B N   1 
ATOM   4112 C  CA  . ARG B 1 123 ? 15.088  15.176  -69.622 1.00 30.51 ?  125 ARG B CA  1 
ATOM   4113 C  C   . ARG B 1 123 ? 13.755  14.509  -69.939 1.00 35.69 ?  125 ARG B C   1 
ATOM   4114 O  O   . ARG B 1 123 ? 12.758  15.208  -70.159 1.00 41.62 ?  125 ARG B O   1 
ATOM   4115 C  CB  . ARG B 1 123 ? 15.822  15.506  -70.925 1.00 26.27 ?  125 ARG B CB  1 
ATOM   4116 N  N   . THR B 1 124 ? 13.706  13.177  -69.964 1.00 27.52 ?  126 THR B N   1 
ATOM   4117 C  CA  . THR B 1 124 ? 12.493  12.485  -70.393 1.00 28.77 ?  126 THR B CA  1 
ATOM   4118 C  C   . THR B 1 124 ? 11.477  12.319  -69.270 1.00 29.93 ?  126 THR B C   1 
ATOM   4119 O  O   . THR B 1 124 ? 10.269  12.423  -69.508 1.00 31.07 ?  126 THR B O   1 
ATOM   4120 C  CB  . THR B 1 124 ? 12.854  11.115  -70.966 1.00 28.68 ?  126 THR B CB  1 
ATOM   4121 O  OG1 . THR B 1 124 ? 13.821  11.281  -72.006 1.00 37.88 ?  126 THR B OG1 1 
ATOM   4122 C  CG2 . THR B 1 124 ? 11.621  10.413  -71.517 1.00 33.85 ?  126 THR B CG2 1 
ATOM   4123 N  N   . TYR B 1 125 ? 11.929  12.040  -68.049 1.00 27.67 ?  127 TYR B N   1 
ATOM   4124 C  CA  . TYR B 1 125 ? 11.033  11.624  -66.980 1.00 25.27 ?  127 TYR B CA  1 
ATOM   4125 C  C   . TYR B 1 125 ? 10.903  12.705  -65.915 1.00 21.25 ?  127 TYR B C   1 
ATOM   4126 O  O   . TYR B 1 125 ? 11.758  13.584  -65.773 1.00 26.61 ?  127 TYR B O   1 
ATOM   4127 C  CB  . TYR B 1 125 ? 11.522  10.319  -66.342 1.00 28.69 ?  127 TYR B CB  1 
ATOM   4128 C  CG  . TYR B 1 125 ? 11.434  9.135   -67.271 1.00 24.92 ?  127 TYR B CG  1 
ATOM   4129 C  CD1 . TYR B 1 125 ? 12.474  8.837   -68.147 1.00 31.58 ?  127 TYR B CD1 1 
ATOM   4130 C  CD2 . TYR B 1 125 ? 10.319  8.310   -67.271 1.00 30.08 ?  127 TYR B CD2 1 
ATOM   4131 C  CE1 . TYR B 1 125 ? 12.398  7.755   -69.004 1.00 29.30 ?  127 TYR B CE1 1 
ATOM   4132 C  CE2 . TYR B 1 125 ? 10.236  7.223   -68.123 1.00 29.18 ?  127 TYR B CE2 1 
ATOM   4133 C  CZ  . TYR B 1 125 ? 11.278  6.951   -68.984 1.00 29.53 ?  127 TYR B CZ  1 
ATOM   4134 O  OH  . TYR B 1 125 ? 11.196  5.870   -69.827 1.00 32.00 ?  127 TYR B OH  1 
ATOM   4135 N  N   . ARG B 1 126 ? 9.807   12.626  -65.166 1.00 21.64 ?  128 ARG B N   1 
ATOM   4136 C  CA  . ARG B 1 126 ? 9.589   13.538  -64.051 1.00 23.65 ?  128 ARG B CA  1 
ATOM   4137 C  C   . ARG B 1 126 ? 10.520  13.155  -62.911 1.00 22.44 ?  128 ARG B C   1 
ATOM   4138 O  O   . ARG B 1 126 ? 10.429  12.043  -62.379 1.00 26.30 ?  128 ARG B O   1 
ATOM   4139 C  CB  . ARG B 1 126 ? 8.135   13.489  -63.592 1.00 27.81 ?  128 ARG B CB  1 
ATOM   4140 C  CG  . ARG B 1 126 ? 7.743   14.635  -62.655 1.00 35.99 ?  128 ARG B CG  1 
ATOM   4141 C  CD  . ARG B 1 126 ? 6.245   14.921  -62.689 1.00 37.78 ?  128 ARG B CD  1 
ATOM   4142 N  NE  . ARG B 1 126 ? 5.512   14.216  -61.640 1.00 41.26 ?  128 ARG B NE  1 
ATOM   4143 C  CZ  . ARG B 1 126 ? 4.831   13.087  -61.823 1.00 42.74 ?  128 ARG B CZ  1 
ATOM   4144 N  NH1 . ARG B 1 126 ? 4.781   12.524  -63.023 1.00 39.58 ?  128 ARG B NH1 1 
ATOM   4145 N  NH2 . ARG B 1 126 ? 4.197   12.521  -60.802 1.00 42.98 ?  128 ARG B NH2 1 
ATOM   4146 N  N   . VAL B 1 127 ? 11.421  14.062  -62.554 1.00 24.54 ?  129 VAL B N   1 
ATOM   4147 C  CA  . VAL B 1 127 ? 12.382  13.852  -61.471 1.00 22.73 ?  129 VAL B CA  1 
ATOM   4148 C  C   . VAL B 1 127 ? 12.152  14.932  -60.427 1.00 21.42 ?  129 VAL B C   1 
ATOM   4149 O  O   . VAL B 1 127 ? 12.305  16.125  -60.718 1.00 25.85 ?  129 VAL B O   1 
ATOM   4150 C  CB  . VAL B 1 127 ? 13.833  13.884  -61.975 1.00 24.42 ?  129 VAL B CB  1 
ATOM   4151 C  CG1 . VAL B 1 127 ? 14.790  13.500  -60.851 1.00 19.96 ?  129 VAL B CG1 1 
ATOM   4152 C  CG2 . VAL B 1 127 ? 14.006  12.940  -63.154 1.00 26.02 ?  129 VAL B CG2 1 
ATOM   4153 N  N   . GLU B 1 128 ? 11.797  14.521  -59.215 1.00 19.26 ?  130 GLU B N   1 
ATOM   4154 C  CA  . GLU B 1 128 ? 11.526  15.463  -58.145 1.00 19.11 ?  130 GLU B CA  1 
ATOM   4155 C  C   . GLU B 1 128 ? 12.397  15.111  -56.948 1.00 20.13 ?  130 GLU B C   1 
ATOM   4156 O  O   . GLU B 1 128 ? 12.889  13.986  -56.829 1.00 22.68 ?  130 GLU B O   1 
ATOM   4157 C  CB  . GLU B 1 128 ? 10.032  15.458  -57.785 1.00 25.94 ?  130 GLU B CB  1 
ATOM   4158 C  CG  . GLU B 1 128 ? 9.214   16.224  -58.829 1.00 23.70 ?  130 GLU B CG  1 
ATOM   4159 C  CD  . GLU B 1 128 ? 7.725   16.032  -58.698 1.00 33.36 ?  130 GLU B CD  1 
ATOM   4160 O  OE1 . GLU B 1 128 ? 7.008   16.461  -59.628 1.00 39.66 ?  130 GLU B OE1 1 
ATOM   4161 O  OE2 . GLU B 1 128 ? 7.268   15.477  -57.672 1.00 33.69 ?  130 GLU B OE2 1 
ATOM   4162 N  N   . ASP B 1 129 ? 12.586  16.097  -56.076 1.00 20.38 ?  131 ASP B N   1 
ATOM   4163 C  CA  . ASP B 1 129 ? 13.398  15.967  -54.869 1.00 20.81 ?  131 ASP B CA  1 
ATOM   4164 C  C   . ASP B 1 129 ? 12.520  15.811  -53.636 1.00 24.73 ?  131 ASP B C   1 
ATOM   4165 O  O   . ASP B 1 129 ? 11.438  16.405  -53.541 1.00 22.08 ?  131 ASP B O   1 
ATOM   4166 C  CB  . ASP B 1 129 ? 14.292  17.197  -54.711 1.00 23.06 ?  131 ASP B CB  1 
ATOM   4167 C  CG  . ASP B 1 129 ? 15.404  17.235  -55.724 1.00 28.18 ?  131 ASP B CG  1 
ATOM   4168 O  OD1 . ASP B 1 129 ? 16.302  16.361  -55.655 1.00 20.82 ?  131 ASP B OD1 1 
ATOM   4169 O  OD2 . ASP B 1 129 ? 15.327  18.083  -56.651 1.00 23.71 ?  131 ASP B OD2 1 
ATOM   4170 N  N   . HIS B 1 130 ? 12.990  15.000  -52.694 1.00 17.36 ?  132 HIS B N   1 
ATOM   4171 C  CA  . HIS B 1 130 ? 12.385  14.945  -51.375 1.00 20.22 ?  132 HIS B CA  1 
ATOM   4172 C  C   . HIS B 1 130 ? 12.826  16.157  -50.553 1.00 19.24 ?  132 HIS B C   1 
ATOM   4173 O  O   . HIS B 1 130 ? 13.987  16.568  -50.612 1.00 20.74 ?  132 HIS B O   1 
ATOM   4174 C  CB  . HIS B 1 130 ? 12.788  13.655  -50.661 1.00 16.62 ?  132 HIS B CB  1 
ATOM   4175 C  CG  . HIS B 1 130 ? 12.428  13.646  -49.213 1.00 18.38 ?  132 HIS B CG  1 
ATOM   4176 N  ND1 . HIS B 1 130 ? 13.364  13.731  -48.204 1.00 14.62 ?  132 HIS B ND1 1 
ATOM   4177 C  CD2 . HIS B 1 130 ? 11.222  13.568  -48.604 1.00 19.38 ?  132 HIS B CD2 1 
ATOM   4178 C  CE1 . HIS B 1 130 ? 12.749  13.704  -47.037 1.00 16.76 ?  132 HIS B CE1 1 
ATOM   4179 N  NE2 . HIS B 1 130 ? 11.449  13.617  -47.253 1.00 17.44 ?  132 HIS B NE2 1 
ATOM   4180 N  N   . TYR B 1 131 ? 11.882  16.748  -49.809 1.00 18.56 ?  133 TYR B N   1 
ATOM   4181 C  CA  . TYR B 1 131 ? 12.137  17.914  -48.956 1.00 23.31 ?  133 TYR B CA  1 
ATOM   4182 C  C   . TYR B 1 131 ? 11.744  17.543  -47.527 1.00 21.02 ?  133 TYR B C   1 
ATOM   4183 O  O   . TYR B 1 131 ? 10.569  17.613  -47.153 1.00 20.60 ?  133 TYR B O   1 
ATOM   4184 C  CB  . TYR B 1 131 ? 11.374  19.154  -49.445 1.00 19.45 ?  133 TYR B CB  1 
ATOM   4185 C  CG  . TYR B 1 131 ? 11.995  19.798  -50.664 1.00 21.59 ?  133 TYR B CG  1 
ATOM   4186 C  CD1 . TYR B 1 131 ? 11.620  19.401  -51.941 1.00 22.02 ?  133 TYR B CD1 1 
ATOM   4187 C  CD2 . TYR B 1 131 ? 12.955  20.793  -50.543 1.00 22.26 ?  133 TYR B CD2 1 
ATOM   4188 C  CE1 . TYR B 1 131 ? 12.182  19.974  -53.064 1.00 23.79 ?  133 TYR B CE1 1 
ATOM   4189 C  CE2 . TYR B 1 131 ? 13.535  21.376  -51.672 1.00 25.68 ?  133 TYR B CE2 1 
ATOM   4190 C  CZ  . TYR B 1 131 ? 13.132  20.959  -52.930 1.00 21.49 ?  133 TYR B CZ  1 
ATOM   4191 O  OH  . TYR B 1 131 ? 13.685  21.511  -54.057 1.00 26.16 ?  133 TYR B OH  1 
ATOM   4192 N  N   . GLY B 1 132 ? 12.737  17.169  -46.717 1.00 17.62 ?  134 GLY B N   1 
ATOM   4193 C  CA  . GLY B 1 132 ? 12.462  16.644  -45.392 1.00 15.93 ?  134 GLY B CA  1 
ATOM   4194 C  C   . GLY B 1 132 ? 11.866  17.639  -44.416 1.00 22.18 ?  134 GLY B C   1 
ATOM   4195 O  O   . GLY B 1 132 ? 11.217  17.226  -43.454 1.00 19.16 ?  134 GLY B O   1 
ATOM   4196 N  N   . THR B 1 133 ? 12.069  18.933  -44.627 1.00 21.78 ?  135 THR B N   1 
ATOM   4197 C  CA  . THR B 1 133 ? 11.497  19.904  -43.700 1.00 24.77 ?  135 THR B CA  1 
ATOM   4198 C  C   . THR B 1 133 ? 10.105  20.380  -44.110 1.00 29.77 ?  135 THR B C   1 
ATOM   4199 O  O   . THR B 1 133 ? 9.540   21.244  -43.434 1.00 27.70 ?  135 THR B O   1 
ATOM   4200 C  CB  . THR B 1 133 ? 12.432  21.102  -43.541 1.00 21.58 ?  135 THR B CB  1 
ATOM   4201 O  OG1 . THR B 1 133 ? 12.520  21.815  -44.775 1.00 24.82 ?  135 THR B OG1 1 
ATOM   4202 C  CG2 . THR B 1 133 ? 13.842  20.634  -43.125 1.00 21.89 ?  135 THR B CG2 1 
ATOM   4203 N  N   . ARG B 1 134 ? 9.542   19.852  -45.194 1.00 26.59 ?  136 ARG B N   1 
ATOM   4204 C  CA  . ARG B 1 134 ? 8.171   20.175  -45.597 1.00 28.87 ?  136 ARG B CA  1 
ATOM   4205 C  C   . ARG B 1 134 ? 7.272   19.023  -45.159 1.00 27.55 ?  136 ARG B C   1 
ATOM   4206 O  O   . ARG B 1 134 ? 7.020   18.082  -45.912 1.00 23.48 ?  136 ARG B O   1 
ATOM   4207 C  CB  . ARG B 1 134 ? 8.080   20.431  -47.096 1.00 27.26 ?  136 ARG B CB  1 
ATOM   4208 C  CG  . ARG B 1 134 ? 8.987   21.546  -47.613 1.00 27.30 ?  136 ARG B CG  1 
ATOM   4209 C  CD  . ARG B 1 134 ? 8.835   21.710  -49.123 1.00 33.56 ?  136 ARG B CD  1 
ATOM   4210 N  NE  . ARG B 1 134 ? 9.797   22.652  -49.693 1.00 34.39 ?  136 ARG B NE  1 
ATOM   4211 C  CZ  . ARG B 1 134 ? 9.935   22.891  -50.995 1.00 35.29 ?  136 ARG B CZ  1 
ATOM   4212 N  NH1 . ARG B 1 134 ? 10.834  23.775  -51.413 1.00 31.51 ?  136 ARG B NH1 1 
ATOM   4213 N  NH2 . ARG B 1 134 ? 9.183   22.247  -51.883 1.00 34.95 ?  136 ARG B NH2 1 
ATOM   4214 N  N   . LEU B 1 135 ? 6.778   19.104  -43.919 1.00 25.62 ?  137 LEU B N   1 
ATOM   4215 C  CA  . LEU B 1 135 ? 5.922   18.040  -43.405 1.00 23.44 ?  137 LEU B CA  1 
ATOM   4216 C  C   . LEU B 1 135 ? 4.701   17.834  -44.289 1.00 28.91 ?  137 LEU B C   1 
ATOM   4217 O  O   . LEU B 1 135 ? 4.182   16.716  -44.381 1.00 29.67 ?  137 LEU B O   1 
ATOM   4218 C  CB  . LEU B 1 135 ? 5.476   18.352  -41.978 1.00 31.87 ?  137 LEU B CB  1 
ATOM   4219 C  CG  . LEU B 1 135 ? 4.857   17.179  -41.218 1.00 28.29 ?  137 LEU B CG  1 
ATOM   4220 C  CD1 . LEU B 1 135 ? 5.843   16.025  -41.085 1.00 30.09 ?  137 LEU B CD1 1 
ATOM   4221 C  CD2 . LEU B 1 135 ? 4.359   17.628  -39.856 1.00 26.32 ?  137 LEU B CD2 1 
ATOM   4222 N  N   . GLU B 1 136 ? 4.242   18.898  -44.951 1.00 27.79 ?  138 GLU B N   1 
ATOM   4223 C  CA  . GLU B 1 136 ? 3.013   18.825  -45.734 1.00 32.75 ?  138 GLU B CA  1 
ATOM   4224 C  C   . GLU B 1 136 ? 3.160   17.871  -46.913 1.00 34.09 ?  138 GLU B C   1 
ATOM   4225 O  O   . GLU B 1 136 ? 2.164   17.313  -47.386 1.00 35.48 ?  138 GLU B O   1 
ATOM   4226 C  CB  . GLU B 1 136 ? 2.635   20.224  -46.225 1.00 32.12 ?  138 GLU B CB  1 
ATOM   4227 C  CG  . GLU B 1 136 ? 3.741   20.900  -47.041 1.00 37.57 ?  138 GLU B CG  1 
ATOM   4228 C  CD  . GLU B 1 136 ? 4.717   21.719  -46.207 1.00 38.38 ?  138 GLU B CD  1 
ATOM   4229 O  OE1 . GLU B 1 136 ? 5.379   22.610  -46.777 1.00 43.33 ?  138 GLU B OE1 1 
ATOM   4230 O  OE2 . GLU B 1 136 ? 4.837   21.464  -44.990 1.00 40.14 ?  138 GLU B OE2 1 
ATOM   4231 N  N   . GLU B 1 137 ? 4.387   17.668  -47.396 1.00 28.13 ?  139 GLU B N   1 
ATOM   4232 C  CA  . GLU B 1 137 ? 4.635   16.760  -48.506 1.00 26.02 ?  139 GLU B CA  1 
ATOM   4233 C  C   . GLU B 1 137 ? 4.696   15.299  -48.055 1.00 24.60 ?  139 GLU B C   1 
ATOM   4234 O  O   . GLU B 1 137 ? 4.989   14.419  -48.869 1.00 23.83 ?  139 GLU B O   1 
ATOM   4235 C  CB  . GLU B 1 137 ? 5.921   17.174  -49.240 1.00 24.20 ?  139 GLU B CB  1 
ATOM   4236 C  CG  . GLU B 1 137 ? 5.962   18.667  -49.622 1.00 26.33 ?  139 GLU B CG  1 
ATOM   4237 C  CD  . GLU B 1 137 ? 6.971   19.000  -50.711 1.00 37.28 ?  139 GLU B CD  1 
ATOM   4238 O  OE1 . GLU B 1 137 ? 7.843   18.152  -51.017 1.00 36.76 ?  139 GLU B OE1 1 
ATOM   4239 O  OE2 . GLU B 1 137 ? 6.910   20.127  -51.254 1.00 30.82 ?  139 GLU B OE2 1 
ATOM   4240 N  N   . HIS B 1 138 ? 4.382   15.020  -46.791 1.00 22.46 ?  140 HIS B N   1 
ATOM   4241 C  CA  . HIS B 1 138 ? 4.482   13.688  -46.213 1.00 22.98 ?  140 HIS B CA  1 
ATOM   4242 C  C   . HIS B 1 138 ? 3.141   13.211  -45.684 1.00 27.39 ?  140 HIS B C   1 
ATOM   4243 O  O   . HIS B 1 138 ? 2.286   14.010  -45.288 1.00 28.26 ?  140 HIS B O   1 
ATOM   4244 C  CB  . HIS B 1 138 ? 5.496   13.655  -45.065 1.00 28.56 ?  140 HIS B CB  1 
ATOM   4245 C  CG  . HIS B 1 138 ? 6.880   14.003  -45.493 1.00 17.00 ?  140 HIS B CG  1 
ATOM   4246 N  ND1 . HIS B 1 138 ? 7.269   15.296  -45.759 1.00 20.02 ?  140 HIS B ND1 1 
ATOM   4247 C  CD2 . HIS B 1 138 ? 7.974   13.229  -45.692 1.00 19.93 ?  140 HIS B CD2 1 
ATOM   4248 C  CE1 . HIS B 1 138 ? 8.536   15.305  -46.129 1.00 22.21 ?  140 HIS B CE1 1 
ATOM   4249 N  NE2 . HIS B 1 138 ? 8.986   14.063  -46.097 1.00 19.26 ?  140 HIS B NE2 1 
ATOM   4250 N  N   . THR B 1 139 ? 2.996   11.890  -45.649 1.00 23.99 ?  141 THR B N   1 
ATOM   4251 C  CA  . THR B 1 139 ? 1.813   11.215  -45.135 1.00 26.50 ?  141 THR B CA  1 
ATOM   4252 C  C   . THR B 1 139 ? 2.172   10.510  -43.835 1.00 28.68 ?  141 THR B C   1 
ATOM   4253 O  O   . THR B 1 139 ? 3.176   9.790   -43.772 1.00 24.27 ?  141 THR B O   1 
ATOM   4254 C  CB  . THR B 1 139 ? 1.282   10.202  -46.156 1.00 26.29 ?  141 THR B CB  1 
ATOM   4255 O  OG1 . THR B 1 139 ? 0.932   10.886  -47.368 1.00 24.71 ?  141 THR B OG1 1 
ATOM   4256 C  CG2 . THR B 1 139 ? 0.060   9.479   -45.608 1.00 30.90 ?  141 THR B CG2 1 
ATOM   4257 N  N   . TYR B 1 140 ? 1.351   10.709  -42.804 1.00 26.45 ?  142 TYR B N   1 
ATOM   4258 C  CA  . TYR B 1 140 ? 1.553   10.043  -41.520 1.00 25.55 ?  142 TYR B CA  1 
ATOM   4259 C  C   . TYR B 1 140 ? 1.034   8.611   -41.580 1.00 30.89 ?  142 TYR B C   1 
ATOM   4260 O  O   . TYR B 1 140 ? -0.146  8.382   -41.874 1.00 29.70 ?  142 TYR B O   1 
ATOM   4261 C  CB  . TYR B 1 140 ? 0.865   10.822  -40.399 1.00 23.33 ?  142 TYR B CB  1 
ATOM   4262 C  CG  . TYR B 1 140 ? 0.933   10.141  -39.055 1.00 31.81 ?  142 TYR B CG  1 
ATOM   4263 C  CD1 . TYR B 1 140 ? 2.143   9.970   -38.392 1.00 28.37 ?  142 TYR B CD1 1 
ATOM   4264 C  CD2 . TYR B 1 140 ? -0.217  9.659   -38.451 1.00 35.12 ?  142 TYR B CD2 1 
ATOM   4265 C  CE1 . TYR B 1 140 ? 2.196   9.341   -37.172 1.00 27.10 ?  142 TYR B CE1 1 
ATOM   4266 C  CE2 . TYR B 1 140 ? -0.173  9.033   -37.230 1.00 28.70 ?  142 TYR B CE2 1 
ATOM   4267 C  CZ  . TYR B 1 140 ? 1.031   8.877   -36.593 1.00 31.89 ?  142 TYR B CZ  1 
ATOM   4268 O  OH  . TYR B 1 140 ? 1.062   8.243   -35.377 1.00 31.11 ?  142 TYR B OH  1 
ATOM   4269 N  N   . LEU B 1 141 ? 1.911   7.649   -41.291 1.00 24.33 ?  143 LEU B N   1 
ATOM   4270 C  CA  . LEU B 1 141 ? 1.581   6.235   -41.385 1.00 24.03 ?  143 LEU B CA  1 
ATOM   4271 C  C   . LEU B 1 141 ? 1.384   5.575   -40.036 1.00 26.38 ?  143 LEU B C   1 
ATOM   4272 O  O   . LEU B 1 141 ? 1.091   4.375   -39.987 1.00 31.23 ?  143 LEU B O   1 
ATOM   4273 C  CB  . LEU B 1 141 ? 2.672   5.482   -42.159 1.00 24.57 ?  143 LEU B CB  1 
ATOM   4274 C  CG  . LEU B 1 141 ? 3.040   6.102   -43.504 1.00 24.59 ?  143 LEU B CG  1 
ATOM   4275 C  CD1 . LEU B 1 141 ? 4.161   5.321   -44.150 1.00 25.26 ?  143 LEU B CD1 1 
ATOM   4276 C  CD2 . LEU B 1 141 ? 1.832   6.163   -44.428 1.00 28.32 ?  143 LEU B CD2 1 
ATOM   4277 N  N   . GLY B 1 142 ? 1.537   6.311   -38.947 1.00 22.78 ?  144 GLY B N   1 
ATOM   4278 C  CA  . GLY B 1 142 ? 1.483   5.752   -37.615 1.00 28.32 ?  144 GLY B CA  1 
ATOM   4279 C  C   . GLY B 1 142 ? 2.785   5.974   -36.871 1.00 29.33 ?  144 GLY B C   1 
ATOM   4280 O  O   . GLY B 1 142 ? 3.751   6.521   -37.401 1.00 28.09 ?  144 GLY B O   1 
ATOM   4281 N  N   . THR B 1 143 ? 2.797   5.519   -35.622 1.00 29.37 ?  145 THR B N   1 
ATOM   4282 C  CA  . THR B 1 143 ? 3.951   5.664   -34.748 1.00 28.80 ?  145 THR B CA  1 
ATOM   4283 C  C   . THR B 1 143 ? 4.456   4.288   -34.334 1.00 32.58 ?  145 THR B C   1 
ATOM   4284 O  O   . THR B 1 143 ? 3.664   3.396   -34.010 1.00 34.31 ?  145 THR B O   1 
ATOM   4285 C  CB  . THR B 1 143 ? 3.598   6.516   -33.520 1.00 25.72 ?  145 THR B CB  1 
ATOM   4286 O  OG1 . THR B 1 143 ? 3.280   7.845   -33.953 1.00 28.04 ?  145 THR B OG1 1 
ATOM   4287 C  CG2 . THR B 1 143 ? 4.771   6.594   -32.553 1.00 27.74 ?  145 THR B CG2 1 
ATOM   4288 N  N   . THR B 1 144 ? 5.780   4.114   -34.371 1.00 26.69 ?  146 THR B N   1 
ATOM   4289 C  CA  . THR B 1 144 ? 6.391   2.848   -34.005 1.00 27.39 ?  146 THR B CA  1 
ATOM   4290 C  C   . THR B 1 144 ? 6.304   2.625   -32.496 1.00 28.26 ?  146 THR B C   1 
ATOM   4291 O  O   . THR B 1 144 ? 6.046   3.560   -31.734 1.00 28.40 ?  146 THR B O   1 
ATOM   4292 C  CB  . THR B 1 144 ? 7.860   2.814   -34.434 1.00 28.80 ?  146 THR B CB  1 
ATOM   4293 O  OG1 . THR B 1 144 ? 8.625   3.694   -33.596 1.00 27.84 ?  146 THR B OG1 1 
ATOM   4294 C  CG2 . THR B 1 144 ? 8.016   3.232   -35.892 1.00 27.63 ?  146 THR B CG2 1 
ATOM   4295 N  N   . PRO B 1 145 ? 6.518   1.384   -32.042 1.00 23.55 ?  147 PRO B N   1 
ATOM   4296 C  CA  . PRO B 1 145 ? 6.606   1.140   -30.593 1.00 32.65 ?  147 PRO B CA  1 
ATOM   4297 C  C   . PRO B 1 145 ? 7.679   1.959   -29.898 1.00 34.74 ?  147 PRO B C   1 
ATOM   4298 O  O   . PRO B 1 145 ? 7.495   2.340   -28.736 1.00 28.74 ?  147 PRO B O   1 
ATOM   4299 C  CB  . PRO B 1 145 ? 6.903   -0.363  -30.516 1.00 33.45 ?  147 PRO B CB  1 
ATOM   4300 C  CG  . PRO B 1 145 ? 6.278   -0.916  -31.753 1.00 34.27 ?  147 PRO B CG  1 
ATOM   4301 C  CD  . PRO B 1 145 ? 6.536   0.123   -32.807 1.00 31.02 ?  147 PRO B CD  1 
ATOM   4302 N  N   . ASN B 1 146 ? 8.794   2.248   -30.566 1.00 28.72 ?  148 ASN B N   1 
ATOM   4303 C  CA  . ASN B 1 146 ? 9.806   3.117   -29.978 1.00 29.24 ?  148 ASN B CA  1 
ATOM   4304 C  C   . ASN B 1 146 ? 9.408   4.583   -30.011 1.00 28.60 ?  148 ASN B C   1 
ATOM   4305 O  O   . ASN B 1 146 ? 10.213  5.432   -29.616 1.00 27.00 ?  148 ASN B O   1 
ATOM   4306 C  CB  . ASN B 1 146 ? 11.153  2.930   -30.689 1.00 25.60 ?  148 ASN B CB  1 
ATOM   4307 C  CG  . ASN B 1 146 ? 11.832  1.628   -30.321 1.00 33.10 ?  148 ASN B CG  1 
ATOM   4308 O  OD1 . ASN B 1 146 ? 11.688  1.135   -29.203 1.00 34.63 ?  148 ASN B OD1 1 
ATOM   4309 N  ND2 . ASN B 1 146 ? 12.574  1.060   -31.263 1.00 26.57 ?  148 ASN B ND2 1 
ATOM   4310 N  N   . GLY B 1 147 ? 8.203   4.898   -30.482 1.00 24.64 ?  149 GLY B N   1 
ATOM   4311 C  CA  . GLY B 1 147 ? 7.686   6.247   -30.409 1.00 25.97 ?  149 GLY B CA  1 
ATOM   4312 C  C   . GLY B 1 147 ? 8.100   7.163   -31.530 1.00 30.53 ?  149 GLY B C   1 
ATOM   4313 O  O   . GLY B 1 147 ? 8.022   8.386   -31.367 1.00 29.03 ?  149 GLY B O   1 
ATOM   4314 N  N   . VAL B 1 148 ? 8.535   6.624   -32.665 1.00 24.20 ?  150 VAL B N   1 
ATOM   4315 C  CA  . VAL B 1 148 ? 8.934   7.435   -33.810 1.00 24.40 ?  150 VAL B CA  1 
ATOM   4316 C  C   . VAL B 1 148 ? 7.732   7.569   -34.742 1.00 20.65 ?  150 VAL B C   1 
ATOM   4317 O  O   . VAL B 1 148 ? 7.236   6.546   -35.242 1.00 25.40 ?  150 VAL B O   1 
ATOM   4318 C  CB  . VAL B 1 148 ? 10.130  6.826   -34.550 1.00 19.65 ?  150 VAL B CB  1 
ATOM   4319 C  CG1 . VAL B 1 148 ? 10.422  7.651   -35.800 1.00 21.92 ?  150 VAL B CG1 1 
ATOM   4320 C  CG2 . VAL B 1 148 ? 11.349  6.772   -33.633 1.00 22.04 ?  150 VAL B CG2 1 
ATOM   4321 N  N   . PRO B 1 149 ? 7.244   8.782   -35.003 1.00 25.38 ?  151 PRO B N   1 
ATOM   4322 C  CA  . PRO B 1 149 ? 6.152   8.940   -35.971 1.00 26.29 ?  151 PRO B CA  1 
ATOM   4323 C  C   . PRO B 1 149 ? 6.703   8.745   -37.371 1.00 29.44 ?  151 PRO B C   1 
ATOM   4324 O  O   . PRO B 1 149 ? 7.754   9.292   -37.712 1.00 25.94 ?  151 PRO B O   1 
ATOM   4325 C  CB  . PRO B 1 149 ? 5.684   10.383  -35.754 1.00 25.19 ?  151 PRO B CB  1 
ATOM   4326 C  CG  . PRO B 1 149 ? 6.894   11.078  -35.223 1.00 24.60 ?  151 PRO B CG  1 
ATOM   4327 C  CD  . PRO B 1 149 ? 7.635   10.062  -34.395 1.00 21.85 ?  151 PRO B CD  1 
ATOM   4328 N  N   . ALA B 1 150 ? 5.990   7.961   -38.182 1.00 25.05 ?  152 ALA B N   1 
ATOM   4329 C  CA  . ALA B 1 150 ? 6.430   7.625   -39.533 1.00 18.88 ?  152 ALA B CA  1 
ATOM   4330 C  C   . ALA B 1 150 ? 5.768   8.574   -40.525 1.00 25.21 ?  152 ALA B C   1 
ATOM   4331 O  O   . ALA B 1 150 ? 4.571   8.454   -40.803 1.00 24.80 ?  152 ALA B O   1 
ATOM   4332 C  CB  . ALA B 1 150 ? 6.109   6.168   -39.860 1.00 21.21 ?  152 ALA B CB  1 
ATOM   4333 N  N   . TRP B 1 151 ? 6.552   9.510   -41.059 1.00 20.81 ?  153 TRP B N   1 
ATOM   4334 C  CA  . TRP B 1 151 ? 6.106   10.502  -42.034 1.00 20.95 ?  153 TRP B CA  1 
ATOM   4335 C  C   . TRP B 1 151 ? 6.901   10.284  -43.316 1.00 23.20 ?  153 TRP B C   1 
ATOM   4336 O  O   . TRP B 1 151 ? 8.098   10.598  -43.359 1.00 19.60 ?  153 TRP B O   1 
ATOM   4337 C  CB  . TRP B 1 151 ? 6.347   11.917  -41.513 1.00 20.48 ?  153 TRP B CB  1 
ATOM   4338 C  CG  . TRP B 1 151 ? 5.434   12.362  -40.419 1.00 23.45 ?  153 TRP B CG  1 
ATOM   4339 C  CD1 . TRP B 1 151 ? 5.666   12.296  -39.074 1.00 23.47 ?  153 TRP B CD1 1 
ATOM   4340 C  CD2 . TRP B 1 151 ? 4.161   12.998  -40.578 1.00 26.78 ?  153 TRP B CD2 1 
ATOM   4341 N  NE1 . TRP B 1 151 ? 4.604   12.830  -38.386 1.00 27.25 ?  153 TRP B NE1 1 
ATOM   4342 C  CE2 . TRP B 1 151 ? 3.664   13.264  -39.287 1.00 29.88 ?  153 TRP B CE2 1 
ATOM   4343 C  CE3 . TRP B 1 151 ? 3.389   13.353  -41.688 1.00 28.36 ?  153 TRP B CE3 1 
ATOM   4344 C  CZ2 . TRP B 1 151 ? 2.432   13.879  -39.074 1.00 29.28 ?  153 TRP B CZ2 1 
ATOM   4345 C  CZ3 . TRP B 1 151 ? 2.166   13.958  -41.475 1.00 34.40 ?  153 TRP B CZ3 1 
ATOM   4346 C  CH2 . TRP B 1 151 ? 1.700   14.216  -40.177 1.00 30.36 ?  153 TRP B CH2 1 
ATOM   4347 N  N   . ILE B 1 152 ? 6.240   9.783   -44.362 1.00 22.45 ?  154 ILE B N   1 
ATOM   4348 C  CA  . ILE B 1 152 ? 6.897   9.362   -45.597 1.00 16.86 ?  154 ILE B CA  1 
ATOM   4349 C  C   . ILE B 1 152 ? 6.313   10.152  -46.760 1.00 24.48 ?  154 ILE B C   1 
ATOM   4350 O  O   . ILE B 1 152 ? 5.100   10.390  -46.799 1.00 21.97 ?  154 ILE B O   1 
ATOM   4351 C  CB  . ILE B 1 152 ? 6.735   7.844   -45.809 1.00 18.98 ?  154 ILE B CB  1 
ATOM   4352 C  CG1 . ILE B 1 152 ? 7.335   7.074   -44.626 1.00 22.62 ?  154 ILE B CG1 1 
ATOM   4353 C  CG2 . ILE B 1 152 ? 7.367   7.399   -47.131 1.00 17.26 ?  154 ILE B CG2 1 
ATOM   4354 C  CD1 . ILE B 1 152 ? 8.877   7.268   -44.453 1.00 16.09 ?  154 ILE B CD1 1 
ATOM   4355 N  N   . ASP B 1 153 ? 7.178   10.556  -47.702 1.00 16.64 ?  155 ASP B N   1 
ATOM   4356 C  CA  . ASP B 1 153 ? 6.780   11.404  -48.823 1.00 20.12 ?  155 ASP B CA  1 
ATOM   4357 C  C   . ASP B 1 153 ? 5.527   10.855  -49.498 1.00 21.43 ?  155 ASP B C   1 
ATOM   4358 O  O   . ASP B 1 153 ? 5.459   9.675   -49.854 1.00 17.87 ?  155 ASP B O   1 
ATOM   4359 C  CB  . ASP B 1 153 ? 7.930   11.509  -49.831 1.00 17.00 ?  155 ASP B CB  1 
ATOM   4360 C  CG  . ASP B 1 153 ? 7.725   12.621  -50.862 1.00 22.18 ?  155 ASP B CG  1 
ATOM   4361 O  OD1 . ASP B 1 153 ? 6.752   12.559  -51.647 1.00 22.78 ?  155 ASP B OD1 1 
ATOM   4362 O  OD2 . ASP B 1 153 ? 8.541   13.566  -50.902 1.00 21.72 ?  155 ASP B OD2 1 
ATOM   4363 N  N   . SER B 1 154 ? 4.515   11.717  -49.633 1.00 25.43 ?  156 SER B N   1 
ATOM   4364 C  CA  . SER B 1 154 ? 3.208   11.258  -50.096 1.00 22.33 ?  156 SER B CA  1 
ATOM   4365 C  C   . SER B 1 154 ? 3.250   10.748  -51.530 1.00 21.96 ?  156 SER B C   1 
ATOM   4366 O  O   . SER B 1 154 ? 2.450   9.873   -51.894 1.00 29.65 ?  156 SER B O   1 
ATOM   4367 C  CB  . SER B 1 154 ? 2.185   12.388  -49.972 1.00 21.67 ?  156 SER B CB  1 
ATOM   4368 O  OG  . SER B 1 154 ? 2.074   12.827  -48.631 1.00 25.23 ?  156 SER B OG  1 
ATOM   4369 N  N   . ARG B 1 155 ? 4.149   11.283  -52.359 1.00 22.10 ?  157 ARG B N   1 
ATOM   4370 C  CA  . ARG B 1 155 ? 4.224   10.820  -53.745 1.00 22.63 ?  157 ARG B CA  1 
ATOM   4371 C  C   . ARG B 1 155 ? 4.598   9.349   -53.823 1.00 24.16 ?  157 ARG B C   1 
ATOM   4372 O  O   . ARG B 1 155 ? 4.123   8.625   -54.708 1.00 23.12 ?  157 ARG B O   1 
ATOM   4373 C  CB  . ARG B 1 155 ? 5.205   11.682  -54.524 1.00 22.73 ?  157 ARG B CB  1 
ATOM   4374 C  CG  . ARG B 1 155 ? 4.757   13.126  -54.589 1.00 22.12 ?  157 ARG B CG  1 
ATOM   4375 C  CD  . ARG B 1 155 ? 5.870   14.019  -55.045 1.00 24.72 ?  157 ARG B CD  1 
ATOM   4376 N  NE  . ARG B 1 155 ? 6.869   14.181  -53.991 1.00 26.17 ?  157 ARG B NE  1 
ATOM   4377 C  CZ  . ARG B 1 155 ? 7.763   15.165  -53.962 1.00 25.96 ?  157 ARG B CZ  1 
ATOM   4378 N  NH1 . ARG B 1 155 ? 7.785   16.068  -54.933 1.00 25.10 ?  157 ARG B NH1 1 
ATOM   4379 N  NH2 . ARG B 1 155 ? 8.635   15.247  -52.961 1.00 24.88 ?  157 ARG B NH2 1 
ATOM   4380 N  N   . TYR B 1 156 ? 5.413   8.875   -52.888 1.00 22.15 ?  158 TYR B N   1 
ATOM   4381 C  CA  . TYR B 1 156 ? 5.703   7.449   -52.844 1.00 19.60 ?  158 TYR B CA  1 
ATOM   4382 C  C   . TYR B 1 156 ? 4.563   6.662   -52.199 1.00 19.67 ?  158 TYR B C   1 
ATOM   4383 O  O   . TYR B 1 156 ? 4.191   5.590   -52.688 1.00 20.88 ?  158 TYR B O   1 
ATOM   4384 C  CB  . TYR B 1 156 ? 7.017   7.236   -52.092 1.00 17.48 ?  158 TYR B CB  1 
ATOM   4385 C  CG  . TYR B 1 156 ? 7.437   5.802   -51.905 1.00 16.66 ?  158 TYR B CG  1 
ATOM   4386 C  CD1 . TYR B 1 156 ? 8.161   5.135   -52.896 1.00 14.73 ?  158 TYR B CD1 1 
ATOM   4387 C  CD2 . TYR B 1 156 ? 7.143   5.120   -50.731 1.00 16.69 ?  158 TYR B CD2 1 
ATOM   4388 C  CE1 . TYR B 1 156 ? 8.572   3.811   -52.712 1.00 14.52 ?  158 TYR B CE1 1 
ATOM   4389 C  CE2 . TYR B 1 156 ? 7.543   3.810   -50.541 1.00 19.40 ?  158 TYR B CE2 1 
ATOM   4390 C  CZ  . TYR B 1 156 ? 8.266   3.161   -51.540 1.00 17.71 ?  158 TYR B CZ  1 
ATOM   4391 O  OH  . TYR B 1 156 ? 8.670   1.858   -51.356 1.00 16.54 ?  158 TYR B OH  1 
ATOM   4392 N  N   . VAL B 1 157 ? 4.007   7.168   -51.096 1.00 18.33 ?  159 VAL B N   1 
ATOM   4393 C  CA  . VAL B 1 157 ? 3.013   6.405   -50.345 1.00 21.49 ?  159 VAL B CA  1 
ATOM   4394 C  C   . VAL B 1 157 ? 1.815   6.054   -51.224 1.00 22.07 ?  159 VAL B C   1 
ATOM   4395 O  O   . VAL B 1 157 ? 1.254   4.956   -51.122 1.00 21.05 ?  159 VAL B O   1 
ATOM   4396 C  CB  . VAL B 1 157 ? 2.584   7.181   -49.084 1.00 24.68 ?  159 VAL B CB  1 
ATOM   4397 C  CG1 . VAL B 1 157 ? 1.407   6.484   -48.399 1.00 26.23 ?  159 VAL B CG1 1 
ATOM   4398 C  CG2 . VAL B 1 157 ? 3.765   7.314   -48.113 1.00 18.81 ?  159 VAL B CG2 1 
ATOM   4399 N  N   . GLN B 1 158 ? 1.427   6.956   -52.119 1.00 22.45 ?  160 GLN B N   1 
ATOM   4400 C  CA  . GLN B 1 158 ? 0.200   6.772   -52.883 1.00 25.75 ?  160 GLN B CA  1 
ATOM   4401 C  C   . GLN B 1 158 ? 0.415   6.107   -54.238 1.00 31.70 ?  160 GLN B C   1 
ATOM   4402 O  O   . GLN B 1 158 ? -0.546  5.966   -54.995 1.00 27.64 ?  160 GLN B O   1 
ATOM   4403 C  CB  . GLN B 1 158 ? -0.514  8.119   -53.060 1.00 30.06 ?  160 GLN B CB  1 
ATOM   4404 C  CG  . GLN B 1 158 ? -1.092  8.661   -51.739 1.00 34.10 ?  160 GLN B CG  1 
ATOM   4405 C  CD  . GLN B 1 158 ? -1.960  7.639   -50.984 1.00 35.08 ?  160 GLN B CD  1 
ATOM   4406 O  OE1 . GLN B 1 158 ? -1.943  7.592   -49.752 1.00 33.89 ?  160 GLN B OE1 1 
ATOM   4407 N  NE2 . GLN B 1 158 ? -2.754  6.859   -51.717 1.00 38.80 ?  160 GLN B NE2 1 
ATOM   4408 N  N   . ALA B 1 159 ? 1.630   5.674   -54.558 1.00 25.29 ?  161 ALA B N   1 
ATOM   4409 C  CA  . ALA B 1 159 ? 1.865   4.999   -55.832 1.00 25.77 ?  161 ALA B CA  1 
ATOM   4410 C  C   . ALA B 1 159 ? 1.384   3.548   -55.782 1.00 24.06 ?  161 ALA B C   1 
ATOM   4411 O  O   . ALA B 1 159 ? 1.570   2.864   -54.772 1.00 22.50 ?  161 ALA B O   1 
ATOM   4412 C  CB  . ALA B 1 159 ? 3.358   5.056   -56.180 1.00 24.74 ?  161 ALA B CB  1 
ATOM   4413 N  N   . ASP B 1 160 ? 0.732   3.078   -56.869 1.00 23.32 ?  162 ASP B N   1 
ATOM   4414 C  CA  A ASP B 1 160 ? 0.372   1.662   -56.937 0.50 32.92 ?  162 ASP B CA  1 
ATOM   4415 C  CA  B ASP B 1 160 ? 0.374   1.661   -56.960 0.50 32.93 ?  162 ASP B CA  1 
ATOM   4416 C  C   . ASP B 1 160 ? 1.595   0.770   -56.817 1.00 24.75 ?  162 ASP B C   1 
ATOM   4417 O  O   . ASP B 1 160 ? 1.540   -0.275  -56.156 1.00 26.94 ?  162 ASP B O   1 
ATOM   4418 C  CB  A ASP B 1 160 ? -0.372  1.325   -58.233 0.50 33.06 ?  162 ASP B CB  1 
ATOM   4419 C  CB  B ASP B 1 160 ? -0.314  1.342   -58.290 0.50 33.06 ?  162 ASP B CB  1 
ATOM   4420 C  CG  A ASP B 1 160 ? -1.785  1.848   -58.258 0.50 39.92 ?  162 ASP B CG  1 
ATOM   4421 C  CG  B ASP B 1 160 ? -1.787  1.648   -58.285 0.50 39.90 ?  162 ASP B CG  1 
ATOM   4422 O  OD1 A ASP B 1 160 ? -2.165  2.599   -57.337 0.50 43.62 ?  162 ASP B OD1 1 
ATOM   4423 O  OD1 B ASP B 1 160 ? -2.515  1.017   -57.489 0.50 45.61 ?  162 ASP B OD1 1 
ATOM   4424 O  OD2 A ASP B 1 160 ? -2.523  1.480   -59.200 0.50 41.24 ?  162 ASP B OD2 1 
ATOM   4425 O  OD2 B ASP B 1 160 ? -2.221  2.483   -59.107 0.50 42.36 ?  162 ASP B OD2 1 
ATOM   4426 N  N   . LEU B 1 161 ? 2.693   1.153   -57.460 1.00 27.78 ?  163 LEU B N   1 
ATOM   4427 C  CA  . LEU B 1 161 ? 3.911   0.357   -57.489 1.00 23.26 ?  163 LEU B CA  1 
ATOM   4428 C  C   . LEU B 1 161 ? 5.044   1.159   -56.864 1.00 17.22 ?  163 LEU B C   1 
ATOM   4429 O  O   . LEU B 1 161 ? 5.333   2.276   -57.304 1.00 19.77 ?  163 LEU B O   1 
ATOM   4430 C  CB  . LEU B 1 161 ? 4.244   -0.058  -58.921 1.00 21.81 ?  163 LEU B CB  1 
ATOM   4431 C  CG  . LEU B 1 161 ? 5.375   -1.071  -59.100 1.00 18.63 ?  163 LEU B CG  1 
ATOM   4432 C  CD1 . LEU B 1 161 ? 5.049   -2.413  -58.466 1.00 21.85 ?  163 LEU B CD1 1 
ATOM   4433 C  CD2 . LEU B 1 161 ? 5.630   -1.223  -60.594 1.00 24.83 ?  163 LEU B CD2 1 
ATOM   4434 N  N   . LYS B 1 162 ? 5.680   0.578   -55.851 1.00 20.21 ?  164 LYS B N   1 
ATOM   4435 C  CA  . LYS B 1 162 ? 6.731   1.240   -55.082 1.00 17.16 ?  164 LYS B CA  1 
ATOM   4436 C  C   . LYS B 1 162 ? 8.053   0.531   -55.351 1.00 14.42 ?  164 LYS B C   1 
ATOM   4437 O  O   . LYS B 1 162 ? 8.180   -0.663  -55.066 1.00 18.35 ?  164 LYS B O   1 
ATOM   4438 C  CB  . LYS B 1 162 ? 6.382   1.206   -53.597 1.00 17.31 ?  164 LYS B CB  1 
ATOM   4439 C  CG  . LYS B 1 162 ? 5.104   1.968   -53.255 1.00 22.40 ?  164 LYS B CG  1 
ATOM   4440 C  CD  . LYS B 1 162 ? 4.626   1.651   -51.842 1.00 23.07 ?  164 LYS B CD  1 
ATOM   4441 C  CE  . LYS B 1 162 ? 3.519   2.597   -51.374 1.00 27.12 ?  164 LYS B CE  1 
ATOM   4442 N  NZ  . LYS B 1 162 ? 2.379   2.609   -52.340 1.00 28.06 ?  164 LYS B NZ  1 
ATOM   4443 N  N   . ILE B 1 163 ? 9.023   1.255   -55.907 1.00 17.96 ?  165 ILE B N   1 
ATOM   4444 C  CA  . ILE B 1 163 ? 10.325  0.687   -56.242 1.00 18.34 ?  165 ILE B CA  1 
ATOM   4445 C  C   . ILE B 1 163 ? 11.417  1.538   -55.601 1.00 14.15 ?  165 ILE B C   1 
ATOM   4446 O  O   . ILE B 1 163 ? 11.325  2.770   -55.585 1.00 17.71 ?  165 ILE B O   1 
ATOM   4447 C  CB  . ILE B 1 163 ? 10.541  0.617   -57.768 1.00 19.98 ?  165 ILE B CB  1 
ATOM   4448 C  CG1 . ILE B 1 163 ? 9.440   -0.220  -58.445 1.00 20.51 ?  165 ILE B CG1 1 
ATOM   4449 C  CG2 . ILE B 1 163 ? 11.943  0.064   -58.088 1.00 17.13 ?  165 ILE B CG2 1 
ATOM   4450 C  CD1 . ILE B 1 163 ? 9.254   0.119   -59.911 1.00 17.40 ?  165 ILE B CD1 1 
ATOM   4451 N  N   . ALA B 1 164 ? 12.474  0.890   -55.104 1.00 17.94 ?  166 ALA B N   1 
ATOM   4452 C  CA  . ALA B 1 164 ? 13.606  1.617   -54.539 1.00 13.95 ?  166 ALA B CA  1 
ATOM   4453 C  C   . ALA B 1 164 ? 14.915  1.076   -55.107 1.00 16.72 ?  166 ALA B C   1 
ATOM   4454 O  O   . ALA B 1 164 ? 15.106  -0.139  -55.197 1.00 17.77 ?  166 ALA B O   1 
ATOM   4455 C  CB  . ALA B 1 164 ? 13.615  1.506   -52.995 1.00 14.79 ?  166 ALA B CB  1 
ATOM   4456 N  N   . THR B 1 165 ? 15.813  1.975   -55.491 1.00 13.52 ?  167 THR B N   1 
ATOM   4457 C  CA  . THR B 1 165 ? 17.128  1.583   -55.987 1.00 14.27 ?  167 THR B CA  1 
ATOM   4458 C  C   . THR B 1 165 ? 18.196  2.098   -55.037 1.00 15.61 ?  167 THR B C   1 
ATOM   4459 O  O   . THR B 1 165 ? 17.979  3.062   -54.300 1.00 21.21 ?  167 THR B O   1 
ATOM   4460 C  CB  . THR B 1 165 ? 17.399  2.143   -57.386 1.00 16.94 ?  167 THR B CB  1 
ATOM   4461 O  OG1 . THR B 1 165 ? 17.445  3.576   -57.326 1.00 18.17 ?  167 THR B OG1 1 
ATOM   4462 C  CG2 . THR B 1 165 ? 16.310  1.700   -58.372 1.00 15.75 ?  167 THR B CG2 1 
ATOM   4463 N  N   . GLY B 1 166 ? 19.373  1.487   -55.073 1.00 14.13 ?  168 GLY B N   1 
ATOM   4464 C  CA  . GLY B 1 166 ? 20.434  2.020   -54.240 1.00 13.99 ?  168 GLY B CA  1 
ATOM   4465 C  C   . GLY B 1 166 ? 21.654  1.122   -54.207 1.00 14.66 ?  168 GLY B C   1 
ATOM   4466 O  O   . GLY B 1 166 ? 21.849  0.262   -55.070 1.00 11.45 ?  168 GLY B O   1 
ATOM   4467 N  N   . LEU B 1 167 ? 22.444  1.320   -53.156 1.00 11.73 ?  169 LEU B N   1 
ATOM   4468 C  CA  . LEU B 1 167 ? 23.830  0.887   -53.114 1.00 11.73 ?  169 LEU B CA  1 
ATOM   4469 C  C   . LEU B 1 167 ? 24.158  0.413   -51.708 1.00 13.86 ?  169 LEU B C   1 
ATOM   4470 O  O   . LEU B 1 167 ? 23.965  1.158   -50.745 1.00 13.97 ?  169 LEU B O   1 
ATOM   4471 C  CB  . LEU B 1 167 ? 24.752  2.047   -53.515 1.00 12.47 ?  169 LEU B CB  1 
ATOM   4472 C  CG  . LEU B 1 167 ? 26.225  1.996   -53.108 1.00 11.77 ?  169 LEU B CG  1 
ATOM   4473 C  CD1 . LEU B 1 167 ? 26.935  0.837   -53.811 1.00 12.46 ?  169 LEU B CD1 1 
ATOM   4474 C  CD2 . LEU B 1 167 ? 26.924  3.343   -53.410 1.00 13.00 ?  169 LEU B CD2 1 
ATOM   4475 N  N   . ILE B 1 168 ? 24.677  -0.809  -51.590 1.00 11.18 ?  170 ILE B N   1 
ATOM   4476 C  CA  . ILE B 1 168 ? 24.962  -1.419  -50.295 1.00 9.83  ?  170 ILE B CA  1 
ATOM   4477 C  C   . ILE B 1 168 ? 26.432  -1.166  -49.972 1.00 14.29 ?  170 ILE B C   1 
ATOM   4478 O  O   . ILE B 1 168 ? 27.321  -1.737  -50.612 1.00 13.97 ?  170 ILE B O   1 
ATOM   4479 C  CB  . ILE B 1 168 ? 24.618  -2.912  -50.296 1.00 11.37 ?  170 ILE B CB  1 
ATOM   4480 C  CG1 . ILE B 1 168 ? 23.136  -3.086  -50.651 1.00 13.34 ?  170 ILE B CG1 1 
ATOM   4481 C  CG2 . ILE B 1 168 ? 24.939  -3.563  -48.941 1.00 14.46 ?  170 ILE B CG2 1 
ATOM   4482 C  CD1 . ILE B 1 168 ? 22.672  -4.535  -50.716 1.00 15.54 ?  170 ILE B CD1 1 
ATOM   4483 N  N   . GLU B 1 169 ? 26.671  -0.305  -48.984 1.00 11.35 ?  171 GLU B N   1 
ATOM   4484 C  CA  . GLU B 1 169 ? 27.980  0.072   -48.467 1.00 11.79 ?  171 GLU B CA  1 
ATOM   4485 C  C   . GLU B 1 169 ? 27.863  0.095   -46.953 1.00 12.14 ?  171 GLU B C   1 
ATOM   4486 O  O   . GLU B 1 169 ? 26.754  0.203   -46.423 1.00 11.81 ?  171 GLU B O   1 
ATOM   4487 C  CB  . GLU B 1 169 ? 28.426  1.461   -48.952 1.00 14.01 ?  171 GLU B CB  1 
ATOM   4488 C  CG  . GLU B 1 169 ? 28.681  1.551   -50.441 1.00 13.59 ?  171 GLU B CG  1 
ATOM   4489 C  CD  . GLU B 1 169 ? 30.044  1.037   -50.850 1.00 17.70 ?  171 GLU B CD  1 
ATOM   4490 O  OE1 . GLU B 1 169 ? 30.430  1.309   -52.005 1.00 13.52 ?  171 GLU B OE1 1 
ATOM   4491 O  OE2 . GLU B 1 169 ? 30.721  0.379   -50.022 1.00 14.18 ?  171 GLU B OE2 1 
ATOM   4492 N  N   . PRO B 1 170 ? 28.982  -0.013  -46.226 1.00 9.50  ?  172 PRO B N   1 
ATOM   4493 C  CA  . PRO B 1 170 ? 28.907  0.161   -44.766 1.00 9.30  ?  172 PRO B CA  1 
ATOM   4494 C  C   . PRO B 1 170 ? 28.348  1.535   -44.434 1.00 10.19 ?  172 PRO B C   1 
ATOM   4495 O  O   . PRO B 1 170 ? 28.517  2.492   -45.188 1.00 9.28  ?  172 PRO B O   1 
ATOM   4496 C  CB  . PRO B 1 170 ? 30.365  0.027   -44.307 1.00 12.01 ?  172 PRO B CB  1 
ATOM   4497 C  CG  . PRO B 1 170 ? 31.049  -0.733  -45.417 1.00 11.68 ?  172 PRO B CG  1 
ATOM   4498 C  CD  . PRO B 1 170 ? 30.356  -0.293  -46.683 1.00 11.55 ?  172 PRO B CD  1 
ATOM   4499 N  N   . HIS B 1 171 ? 27.638  1.616   -43.308 1.00 10.37 ?  173 HIS B N   1 
ATOM   4500 C  CA  . HIS B 1 171 ? 27.044  2.874   -42.861 1.00 10.04 ?  173 HIS B CA  1 
ATOM   4501 C  C   . HIS B 1 171 ? 27.206  3.022   -41.357 1.00 12.05 ?  173 HIS B C   1 
ATOM   4502 O  O   . HIS B 1 171 ? 26.892  2.098   -40.609 1.00 9.99  ?  173 HIS B O   1 
ATOM   4503 C  CB  . HIS B 1 171 ? 25.552  2.967   -43.215 1.00 9.85  ?  173 HIS B CB  1 
ATOM   4504 C  CG  . HIS B 1 171 ? 24.999  4.347   -43.031 1.00 10.62 ?  173 HIS B CG  1 
ATOM   4505 N  ND1 . HIS B 1 171 ? 24.417  4.765   -41.852 1.00 10.56 ?  173 HIS B ND1 1 
ATOM   4506 C  CD2 . HIS B 1 171 ? 24.975  5.412   -43.864 1.00 9.92  ?  173 HIS B CD2 1 
ATOM   4507 C  CE1 . HIS B 1 171 ? 24.048  6.027   -41.973 1.00 10.86 ?  173 HIS B CE1 1 
ATOM   4508 N  NE2 . HIS B 1 171 ? 24.379  6.445   -43.183 1.00 8.94  ?  173 HIS B NE2 1 
ATOM   4509 N  N   . LEU B 1 172 ? 27.611  4.221   -40.920 1.00 10.67 ?  174 LEU B N   1 
ATOM   4510 C  CA  . LEU B 1 172 ? 28.053  4.440   -39.547 1.00 9.01  ?  174 LEU B CA  1 
ATOM   4511 C  C   . LEU B 1 172 ? 26.915  4.419   -38.531 1.00 12.03 ?  174 LEU B C   1 
ATOM   4512 O  O   . LEU B 1 172 ? 27.189  4.338   -37.327 1.00 10.79 ?  174 LEU B O   1 
ATOM   4513 C  CB  . LEU B 1 172 ? 28.796  5.769   -39.463 1.00 10.46 ?  174 LEU B CB  1 
ATOM   4514 C  CG  . LEU B 1 172 ? 27.958  7.047   -39.379 1.00 12.47 ?  174 LEU B CG  1 
ATOM   4515 C  CD1 . LEU B 1 172 ? 28.902  8.205   -39.072 1.00 11.18 ?  174 LEU B CD1 1 
ATOM   4516 C  CD2 . LEU B 1 172 ? 27.095  7.322   -40.620 1.00 11.17 ?  174 LEU B CD2 1 
ATOM   4517 N  N   . MET B 1 173 ? 25.662  4.507   -38.966 1.00 11.88 ?  175 MET B N   1 
ATOM   4518 C  CA  . MET B 1 173 ? 24.524  4.341   -38.062 1.00 11.78 ?  175 MET B CA  1 
ATOM   4519 C  C   . MET B 1 173 ? 23.689  3.114   -38.359 1.00 12.30 ?  175 MET B C   1 
ATOM   4520 O  O   . MET B 1 173 ? 23.378  2.347   -37.443 1.00 11.89 ?  175 MET B O   1 
ATOM   4521 C  CB  . MET B 1 173 ? 23.623  5.583   -38.063 1.00 13.70 ?  175 MET B CB  1 
ATOM   4522 C  CG  . MET B 1 173 ? 24.389  6.893   -38.122 1.00 18.09 ?  175 MET B CG  1 
ATOM   4523 S  SD  . MET B 1 173 ? 23.373  8.313   -38.537 1.00 16.78 ?  175 MET B SD  1 
ATOM   4524 C  CE  . MET B 1 173 ? 24.528  9.615   -38.089 1.00 16.79 ?  175 MET B CE  1 
ATOM   4525 N  N   . ALA B 1 174 ? 23.336  2.900   -39.620 1.00 10.60 ?  176 ALA B N   1 
ATOM   4526 C  CA  . ALA B 1 174 ? 22.416  1.836   -39.986 1.00 10.56 ?  176 ALA B CA  1 
ATOM   4527 C  C   . ALA B 1 174 ? 23.112  0.525   -40.312 1.00 11.06 ?  176 ALA B C   1 
ATOM   4528 O  O   . ALA B 1 174 ? 22.435  -0.422  -40.720 1.00 13.27 ?  176 ALA B O   1 
ATOM   4529 C  CB  . ALA B 1 174 ? 21.558  2.282   -41.174 1.00 11.50 ?  176 ALA B CB  1 
ATOM   4530 N  N   . GLY B 1 175 ? 24.438  0.449   -40.148 1.00 10.56 ?  177 GLY B N   1 
ATOM   4531 C  CA  . GLY B 1 175 ? 25.176  -0.781  -40.389 1.00 10.34 ?  177 GLY B CA  1 
ATOM   4532 C  C   . GLY B 1 175 ? 25.585  -0.921  -41.842 1.00 11.49 ?  177 GLY B C   1 
ATOM   4533 O  O   . GLY B 1 175 ? 26.779  -0.985  -42.173 1.00 11.77 ?  177 GLY B O   1 
ATOM   4534 N  N   . TYR B 1 176 ? 24.582  -0.984  -42.717 1.00 12.84 ?  178 TYR B N   1 
ATOM   4535 C  CA  . TYR B 1 176 ? 24.763  -0.949  -44.164 1.00 12.41 ?  178 TYR B CA  1 
ATOM   4536 C  C   . TYR B 1 176 ? 23.703  -0.046  -44.776 1.00 12.18 ?  178 TYR B C   1 
ATOM   4537 O  O   . TYR B 1 176 ? 22.567  0.005   -44.293 1.00 13.79 ?  178 TYR B O   1 
ATOM   4538 C  CB  . TYR B 1 176 ? 24.651  -2.345  -44.789 1.00 13.17 ?  178 TYR B CB  1 
ATOM   4539 C  CG  . TYR B 1 176 ? 25.806  -3.218  -44.450 1.00 11.72 ?  178 TYR B CG  1 
ATOM   4540 C  CD1 . TYR B 1 176 ? 27.007  -3.109  -45.137 1.00 9.58  ?  178 TYR B CD1 1 
ATOM   4541 C  CD2 . TYR B 1 176 ? 25.715  -4.137  -43.414 1.00 13.72 ?  178 TYR B CD2 1 
ATOM   4542 C  CE1 . TYR B 1 176 ? 28.091  -3.904  -44.800 1.00 12.48 ?  178 TYR B CE1 1 
ATOM   4543 C  CE2 . TYR B 1 176 ? 26.784  -4.930  -43.073 1.00 13.91 ?  178 TYR B CE2 1 
ATOM   4544 C  CZ  . TYR B 1 176 ? 27.965  -4.816  -43.769 1.00 15.57 ?  178 TYR B CZ  1 
ATOM   4545 O  OH  . TYR B 1 176 ? 29.039  -5.607  -43.430 1.00 21.16 ?  178 TYR B OH  1 
ATOM   4546 N  N   . SER B 1 177 ? 24.085  0.671   -45.836 1.00 9.37  ?  179 SER B N   1 
ATOM   4547 C  CA  . SER B 1 177 ? 23.149  1.416   -46.658 1.00 11.49 ?  179 SER B CA  1 
ATOM   4548 C  C   . SER B 1 177 ? 22.400  0.467   -47.595 1.00 13.29 ?  179 SER B C   1 
ATOM   4549 O  O   . SER B 1 177 ? 22.788  -0.690  -47.790 1.00 11.47 ?  179 SER B O   1 
ATOM   4550 C  CB  . SER B 1 177 ? 23.900  2.476   -47.471 1.00 13.69 ?  179 SER B CB  1 
ATOM   4551 O  OG  . SER B 1 177 ? 24.306  3.570   -46.653 1.00 15.17 ?  179 SER B OG  1 
ATOM   4552 N  N   . GLY B 1 178 ? 21.296  0.964   -48.145 1.00 10.70 ?  180 GLY B N   1 
ATOM   4553 C  CA  . GLY B 1 178 ? 20.523  0.259   -49.152 1.00 12.76 ?  180 GLY B CA  1 
ATOM   4554 C  C   . GLY B 1 178 ? 19.190  -0.236  -48.611 1.00 15.10 ?  180 GLY B C   1 
ATOM   4555 O  O   . GLY B 1 178 ? 18.811  0.008   -47.465 1.00 12.45 ?  180 GLY B O   1 
ATOM   4556 N  N   . GLY B 1 179 ? 18.478  -0.938  -49.485 1.00 13.57 ?  181 GLY B N   1 
ATOM   4557 C  CA  . GLY B 1 179 ? 17.230  -1.559  -49.081 1.00 12.23 ?  181 GLY B CA  1 
ATOM   4558 C  C   . GLY B 1 179 ? 16.257  -0.542  -48.515 1.00 11.74 ?  181 GLY B C   1 
ATOM   4559 O  O   . GLY B 1 179 ? 16.035  0.535   -49.091 1.00 12.86 ?  181 GLY B O   1 
ATOM   4560 N  N   . ARG B 1 180 ? 15.678  -0.912  -47.369 1.00 12.43 ?  182 ARG B N   1 
ATOM   4561 C  CA  . ARG B 1 180 ? 14.840  -0.017  -46.568 1.00 13.86 ?  182 ARG B CA  1 
ATOM   4562 C  C   . ARG B 1 180 ? 15.300  1.420   -46.398 1.00 14.87 ?  182 ARG B C   1 
ATOM   4563 O  O   . ARG B 1 180 ? 14.454  2.303   -46.173 1.00 13.06 ?  182 ARG B O   1 
ATOM   4564 C  CB  . ARG B 1 180 ? 14.609  -0.610  -45.175 1.00 14.12 ?  182 ARG B CB  1 
ATOM   4565 C  CG  . ARG B 1 180 ? 15.782  -0.446  -44.141 1.00 12.13 ?  182 ARG B CG  1 
ATOM   4566 C  CD  . ARG B 1 180 ? 17.004  -1.366  -44.572 1.00 13.97 ?  182 ARG B CD  1 
ATOM   4567 N  NE  . ARG B 1 180 ? 18.184  -1.418  -43.686 1.00 15.17 ?  182 ARG B NE  1 
ATOM   4568 C  CZ  . ARG B 1 180 ? 19.255  -0.641  -43.609 1.00 15.56 ?  182 ARG B CZ  1 
ATOM   4569 N  NH1 . ARG B 1 180 ? 20.115  -0.821  -42.598 1.00 13.59 ?  182 ARG B NH1 1 
ATOM   4570 N  NH2 . ARG B 1 180 ? 19.663  0.018   -44.681 1.00 14.40 ?  182 ARG B NH2 1 
ATOM   4571 N  N   . LYS B 1 181 ? 16.610  1.682   -46.430 1.00 12.19 ?  183 LYS B N   1 
ATOM   4572 C  CA  . LYS B 1 181 ? 17.082  3.021   -46.079 1.00 12.95 ?  183 LYS B CA  1 
ATOM   4573 C  C   . LYS B 1 181 ? 16.643  4.076   -47.094 1.00 14.41 ?  183 LYS B C   1 
ATOM   4574 O  O   . LYS B 1 181 ? 16.608  5.268   -46.765 1.00 13.54 ?  183 LYS B O   1 
ATOM   4575 C  CB  . LYS B 1 181 ? 18.614  3.007   -45.932 1.00 11.57 ?  183 LYS B CB  1 
ATOM   4576 C  CG  . LYS B 1 181 ? 19.201  4.114   -45.060 1.00 11.78 ?  183 LYS B CG  1 
ATOM   4577 C  CD  . LYS B 1 181 ? 20.599  3.718   -44.560 1.00 12.25 ?  183 LYS B CD  1 
ATOM   4578 C  CE  . LYS B 1 181 ? 21.268  4.844   -43.788 1.00 9.82  ?  183 LYS B CE  1 
ATOM   4579 N  NZ  . LYS B 1 181 ? 21.219  6.135   -44.526 1.00 10.12 ?  183 LYS B NZ  1 
ATOM   4580 N  N   . LEU B 1 182 ? 16.305  3.660   -48.321 1.00 12.34 ?  184 LEU B N   1 
ATOM   4581 C  CA  . LEU B 1 182 ? 15.754  4.582   -49.305 1.00 13.72 ?  184 LEU B CA  1 
ATOM   4582 C  C   . LEU B 1 182 ? 14.443  5.194   -48.831 1.00 11.98 ?  184 LEU B C   1 
ATOM   4583 O  O   . LEU B 1 182 ? 14.125  6.333   -49.192 1.00 15.73 ?  184 LEU B O   1 
ATOM   4584 C  CB  . LEU B 1 182 ? 15.533  3.853   -50.632 1.00 13.82 ?  184 LEU B CB  1 
ATOM   4585 C  CG  . LEU B 1 182 ? 16.681  3.854   -51.629 1.00 10.57 ?  184 LEU B CG  1 
ATOM   4586 C  CD1 . LEU B 1 182 ? 17.035  5.270   -52.107 1.00 13.67 ?  184 LEU B CD1 1 
ATOM   4587 C  CD2 . LEU B 1 182 ? 17.915  3.166   -51.003 1.00 13.90 ?  184 LEU B CD2 1 
ATOM   4588 N  N   . ILE B 1 183 ? 13.665  4.451   -48.053 1.00 11.60 ?  185 ILE B N   1 
ATOM   4589 C  CA  . ILE B 1 183 ? 12.418  4.983   -47.496 1.00 15.27 ?  185 ILE B CA  1 
ATOM   4590 C  C   . ILE B 1 183 ? 12.683  5.733   -46.204 1.00 13.89 ?  185 ILE B C   1 
ATOM   4591 O  O   . ILE B 1 183 ? 12.354  6.915   -46.069 1.00 15.64 ?  185 ILE B O   1 
ATOM   4592 C  CB  . ILE B 1 183 ? 11.399  3.845   -47.282 1.00 16.80 ?  185 ILE B CB  1 
ATOM   4593 C  CG1 . ILE B 1 183 ? 10.993  3.234   -48.625 1.00 18.49 ?  185 ILE B CG1 1 
ATOM   4594 C  CG2 . ILE B 1 183 ? 10.152  4.364   -46.548 1.00 18.99 ?  185 ILE B CG2 1 
ATOM   4595 C  CD1 . ILE B 1 183 ? 10.507  1.814   -48.508 1.00 24.56 ?  185 ILE B CD1 1 
ATOM   4596 N  N   . CYS B 1 184 ? 13.317  5.072   -45.243 1.00 14.11 ?  186 CYS B N   1 
ATOM   4597 C  CA  . CYS B 1 184 ? 13.669  5.715   -43.979 1.00 13.44 ?  186 CYS B CA  1 
ATOM   4598 C  C   . CYS B 1 184 ? 15.184  5.733   -43.871 1.00 12.50 ?  186 CYS B C   1 
ATOM   4599 O  O   . CYS B 1 184 ? 15.784  4.682   -43.572 1.00 14.11 ?  186 CYS B O   1 
ATOM   4600 C  CB  . CYS B 1 184 ? 13.056  4.966   -42.797 1.00 13.66 ?  186 CYS B CB  1 
ATOM   4601 S  SG  . CYS B 1 184 ? 13.350  5.777   -41.204 1.00 18.11 ?  186 CYS B SG  1 
ATOM   4602 N  N   . PRO B 1 185 ? 15.851  6.886   -44.045 1.00 12.86 ?  187 PRO B N   1 
ATOM   4603 C  CA  . PRO B 1 185 ? 15.272  8.238   -44.019 1.00 14.13 ?  187 PRO B CA  1 
ATOM   4604 C  C   . PRO B 1 185 ? 15.107  8.868   -45.385 1.00 16.41 ?  187 PRO B C   1 
ATOM   4605 O  O   . PRO B 1 185 ? 14.780  10.051  -45.438 1.00 14.01 ?  187 PRO B O   1 
ATOM   4606 C  CB  . PRO B 1 185 ? 16.327  9.049   -43.280 1.00 13.02 ?  187 PRO B CB  1 
ATOM   4607 C  CG  . PRO B 1 185 ? 17.625  8.397   -43.762 1.00 12.58 ?  187 PRO B CG  1 
ATOM   4608 C  CD  . PRO B 1 185 ? 17.322  6.921   -43.902 1.00 13.90 ?  187 PRO B CD  1 
ATOM   4609 N  N   . GLY B 1 186 ? 15.418  8.123   -46.448 1.00 12.20 ?  188 GLY B N   1 
ATOM   4610 C  CA  . GLY B 1 186 ? 15.531  8.725   -47.769 1.00 12.83 ?  188 GLY B CA  1 
ATOM   4611 C  C   . GLY B 1 186 ? 14.362  9.621   -48.152 1.00 13.71 ?  188 GLY B C   1 
ATOM   4612 O  O   . GLY B 1 186 ? 14.552  10.661  -48.782 1.00 13.69 ?  188 GLY B O   1 
ATOM   4613 N  N   . ILE B 1 187 ? 13.144  9.235   -47.786 1.00 15.37 ?  189 ILE B N   1 
ATOM   4614 C  CA  . ILE B 1 187 ? 11.987  10.075  -48.094 1.00 15.07 ?  189 ILE B CA  1 
ATOM   4615 C  C   . ILE B 1 187 ? 11.155  10.277  -46.831 1.00 19.98 ?  189 ILE B C   1 
ATOM   4616 O  O   . ILE B 1 187 ? 9.919   10.369  -46.888 1.00 17.30 ?  189 ILE B O   1 
ATOM   4617 C  CB  . ILE B 1 187 ? 11.142  9.478   -49.239 1.00 12.45 ?  189 ILE B CB  1 
ATOM   4618 C  CG1 . ILE B 1 187 ? 10.738  8.039   -48.914 1.00 16.45 ?  189 ILE B CG1 1 
ATOM   4619 C  CG2 . ILE B 1 187 ? 11.905  9.579   -50.549 1.00 16.72 ?  189 ILE B CG2 1 
ATOM   4620 C  CD1 . ILE B 1 187 ? 9.696   7.441   -49.879 1.00 15.43 ?  189 ILE B CD1 1 
ATOM   4621 N  N   . ALA B 1 188 ? 11.832  10.365  -45.687 1.00 16.43 ?  190 ALA B N   1 
ATOM   4622 C  CA  . ALA B 1 188 ? 11.189  10.586  -44.398 1.00 15.63 ?  190 ALA B CA  1 
ATOM   4623 C  C   . ALA B 1 188 ? 11.287  12.052  -43.975 1.00 14.85 ?  190 ALA B C   1 
ATOM   4624 O  O   . ALA B 1 188 ? 12.272  12.743  -44.255 1.00 16.76 ?  190 ALA B O   1 
ATOM   4625 C  CB  . ALA B 1 188 ? 11.816  9.700   -43.319 1.00 16.27 ?  190 ALA B CB  1 
ATOM   4626 N  N   . ALA B 1 189 ? 10.244  12.527  -43.292 1.00 16.11 ?  191 ALA B N   1 
ATOM   4627 C  CA  . ALA B 1 189 ? 10.247  13.902  -42.825 1.00 18.37 ?  191 ALA B CA  1 
ATOM   4628 C  C   . ALA B 1 189 ? 11.190  14.076  -41.634 1.00 17.43 ?  191 ALA B C   1 
ATOM   4629 O  O   . ALA B 1 189 ? 11.507  13.135  -40.905 1.00 18.05 ?  191 ALA B O   1 
ATOM   4630 C  CB  . ALA B 1 189 ? 8.838   14.341  -42.424 1.00 19.57 ?  191 ALA B CB  1 
ATOM   4631 N  N   . PHE B 1 190 ? 11.612  15.323  -41.428 1.00 18.35 ?  192 PHE B N   1 
ATOM   4632 C  CA  . PHE B 1 190 ? 12.391  15.651  -40.237 1.00 18.00 ?  192 PHE B CA  1 
ATOM   4633 C  C   . PHE B 1 190 ? 11.689  15.204  -38.954 1.00 18.68 ?  192 PHE B C   1 
ATOM   4634 O  O   . PHE B 1 190 ? 12.349  14.826  -37.980 1.00 16.79 ?  192 PHE B O   1 
ATOM   4635 C  CB  . PHE B 1 190 ? 12.654  17.150  -40.202 1.00 16.70 ?  192 PHE B CB  1 
ATOM   4636 C  CG  . PHE B 1 190 ? 13.516  17.588  -39.052 1.00 19.66 ?  192 PHE B CG  1 
ATOM   4637 C  CD1 . PHE B 1 190 ? 14.829  17.144  -38.947 1.00 19.12 ?  192 PHE B CD1 1 
ATOM   4638 C  CD2 . PHE B 1 190 ? 13.009  18.422  -38.067 1.00 22.62 ?  192 PHE B CD2 1 
ATOM   4639 C  CE1 . PHE B 1 190 ? 15.628  17.554  -37.889 1.00 21.32 ?  192 PHE B CE1 1 
ATOM   4640 C  CE2 . PHE B 1 190 ? 13.799  18.829  -37.008 1.00 27.04 ?  192 PHE B CE2 1 
ATOM   4641 C  CZ  . PHE B 1 190 ? 15.109  18.398  -36.919 1.00 23.86 ?  192 PHE B CZ  1 
ATOM   4642 N  N   . GLU B 1 191 ? 10.351  15.246  -38.921 1.00 21.83 ?  193 GLU B N   1 
ATOM   4643 C  CA  . GLU B 1 191 ? 9.644   14.822  -37.717 1.00 20.13 ?  193 GLU B CA  1 
ATOM   4644 C  C   . GLU B 1 191 ? 9.922   13.359  -37.397 1.00 24.01 ?  193 GLU B C   1 
ATOM   4645 O  O   . GLU B 1 191 ? 9.897   12.958  -36.224 1.00 20.71 ?  193 GLU B O   1 
ATOM   4646 C  CB  . GLU B 1 191 ? 8.140   15.068  -37.878 1.00 24.82 ?  193 GLU B CB  1 
ATOM   4647 C  CG  . GLU B 1 191 ? 7.772   16.549  -37.871 1.00 20.17 ?  193 GLU B CG  1 
ATOM   4648 C  CD  . GLU B 1 191 ? 8.357   17.281  -36.680 1.00 34.81 ?  193 GLU B CD  1 
ATOM   4649 O  OE1 . GLU B 1 191 ? 8.168   16.795  -35.542 1.00 38.82 ?  193 GLU B OE1 1 
ATOM   4650 O  OE2 . GLU B 1 191 ? 8.997   18.341  -36.881 1.00 40.92 ?  193 GLU B OE2 1 
ATOM   4651 N  N   . THR B 1 192 ? 10.212  12.554  -38.424 1.00 17.95 ?  194 THR B N   1 
ATOM   4652 C  CA  . THR B 1 192 ? 10.628  11.175  -38.216 1.00 17.47 ?  194 THR B CA  1 
ATOM   4653 C  C   . THR B 1 192 ? 12.129  11.085  -37.944 1.00 17.21 ?  194 THR B C   1 
ATOM   4654 O  O   . THR B 1 192 ? 12.554  10.433  -36.987 1.00 17.12 ?  194 THR B O   1 
ATOM   4655 C  CB  . THR B 1 192 ? 10.265  10.344  -39.448 1.00 20.59 ?  194 THR B CB  1 
ATOM   4656 O  OG1 . THR B 1 192 ? 8.841   10.343  -39.614 1.00 19.87 ?  194 THR B OG1 1 
ATOM   4657 C  CG2 . THR B 1 192 ? 10.768  8.918   -39.311 1.00 19.63 ?  194 THR B CG2 1 
ATOM   4658 N  N   . VAL B 1 193 ? 12.931  11.766  -38.764 1.00 16.81 ?  195 VAL B N   1 
ATOM   4659 C  CA  . VAL B 1 193 ? 14.380  11.576  -38.745 1.00 14.59 ?  195 VAL B CA  1 
ATOM   4660 C  C   . VAL B 1 193 ? 15.013  12.136  -37.471 1.00 18.77 ?  195 VAL B C   1 
ATOM   4661 O  O   . VAL B 1 193 ? 15.996  11.579  -36.975 1.00 15.29 ?  195 VAL B O   1 
ATOM   4662 C  CB  . VAL B 1 193 ? 14.998  12.197  -40.010 1.00 15.81 ?  195 VAL B CB  1 
ATOM   4663 C  CG1 . VAL B 1 193 ? 16.527  12.034  -40.010 1.00 16.33 ?  195 VAL B CG1 1 
ATOM   4664 C  CG2 . VAL B 1 193 ? 14.399  11.539  -41.248 1.00 15.57 ?  195 VAL B CG2 1 
ATOM   4665 N  N   . LYS B 1 194 ? 14.491  13.243  -36.925 1.00 17.63 ?  196 LYS B N   1 
ATOM   4666 C  CA  . LYS B 1 194 ? 15.126  13.817  -35.736 1.00 18.18 ?  196 LYS B CA  1 
ATOM   4667 C  C   . LYS B 1 194 ? 15.067  12.857  -34.550 1.00 19.80 ?  196 LYS B C   1 
ATOM   4668 O  O   . LYS B 1 194 ? 15.957  12.874  -33.691 1.00 20.03 ?  196 LYS B O   1 
ATOM   4669 C  CB  . LYS B 1 194 ? 14.477  15.150  -35.342 1.00 16.13 ?  196 LYS B CB  1 
ATOM   4670 C  CG  . LYS B 1 194 ? 13.069  15.031  -34.767 1.00 22.93 ?  196 LYS B CG  1 
ATOM   4671 C  CD  . LYS B 1 194 ? 12.354  16.379  -34.776 1.00 22.98 ?  196 LYS B CD  1 
ATOM   4672 C  CE  . LYS B 1 194 ? 11.193  16.346  -33.793 1.00 28.71 ?  196 LYS B CE  1 
ATOM   4673 N  NZ  . LYS B 1 194 ? 10.585  17.680  -33.602 1.00 29.32 ?  196 LYS B NZ  1 
ATOM   4674 N  N   . LEU B 1 195 ? 14.032  12.017  -34.486 1.00 19.22 ?  197 LEU B N   1 
ATOM   4675 C  CA  . LEU B 1 195 ? 13.921  11.028  -33.416 1.00 17.58 ?  197 LEU B CA  1 
ATOM   4676 C  C   . LEU B 1 195 ? 14.701  9.760   -33.750 1.00 18.42 ?  197 LEU B C   1 
ATOM   4677 O  O   . LEU B 1 195 ? 15.359  9.179   -32.878 1.00 17.56 ?  197 LEU B O   1 
ATOM   4678 C  CB  . LEU B 1 195 ? 12.442  10.706  -33.175 1.00 16.16 ?  197 LEU B CB  1 
ATOM   4679 C  CG  . LEU B 1 195 ? 11.588  11.910  -32.760 1.00 20.50 ?  197 LEU B CG  1 
ATOM   4680 C  CD1 . LEU B 1 195 ? 10.202  11.430  -32.380 1.00 18.91 ?  197 LEU B CD1 1 
ATOM   4681 C  CD2 . LEU B 1 195 ? 12.224  12.602  -31.560 1.00 22.57 ?  197 LEU B CD2 1 
ATOM   4682 N  N   . TRP B 1 196 ? 14.622  9.306   -35.003 1.00 15.79 ?  198 TRP B N   1 
ATOM   4683 C  CA  . TRP B 1 196 ? 15.338  8.096   -35.388 1.00 13.49 ?  198 TRP B CA  1 
ATOM   4684 C  C   . TRP B 1 196 ? 16.850  8.329   -35.350 1.00 14.45 ?  198 TRP B C   1 
ATOM   4685 O  O   . TRP B 1 196 ? 17.603  7.474   -34.867 1.00 18.06 ?  198 TRP B O   1 
ATOM   4686 C  CB  . TRP B 1 196 ? 14.847  7.636   -36.761 1.00 18.30 ?  198 TRP B CB  1 
ATOM   4687 C  CG  . TRP B 1 196 ? 15.584  6.478   -37.344 1.00 16.59 ?  198 TRP B CG  1 
ATOM   4688 C  CD1 . TRP B 1 196 ? 15.618  5.196   -36.875 1.00 15.63 ?  198 TRP B CD1 1 
ATOM   4689 C  CD2 . TRP B 1 196 ? 16.386  6.499   -38.525 1.00 14.69 ?  198 TRP B CD2 1 
ATOM   4690 N  NE1 . TRP B 1 196 ? 16.397  4.409   -37.698 1.00 13.43 ?  198 TRP B NE1 1 
ATOM   4691 C  CE2 . TRP B 1 196 ? 16.892  5.191   -38.711 1.00 14.62 ?  198 TRP B CE2 1 
ATOM   4692 C  CE3 . TRP B 1 196 ? 16.733  7.499   -39.440 1.00 13.61 ?  198 TRP B CE3 1 
ATOM   4693 C  CZ2 . TRP B 1 196 ? 17.719  4.855   -39.777 1.00 12.24 ?  198 TRP B CZ2 1 
ATOM   4694 C  CZ3 . TRP B 1 196 ? 17.568  7.161   -40.508 1.00 14.77 ?  198 TRP B CZ3 1 
ATOM   4695 C  CH2 . TRP B 1 196 ? 18.055  5.850   -40.658 1.00 15.24 ?  198 TRP B CH2 1 
ATOM   4696 N  N   . HIS B 1 197 ? 17.309  9.494   -35.810 1.00 13.51 ?  199 HIS B N   1 
ATOM   4697 C  CA  A HIS B 1 197 ? 18.703  9.896   -35.640 0.50 14.76 ?  199 HIS B CA  1 
ATOM   4698 C  CA  B HIS B 1 197 ? 18.698  9.916   -35.652 0.50 14.77 ?  199 HIS B CA  1 
ATOM   4699 C  C   . HIS B 1 197 ? 18.958  10.578  -34.300 1.00 18.59 ?  199 HIS B C   1 
ATOM   4700 O  O   . HIS B 1 197 ? 19.881  11.394  -34.198 1.00 18.19 ?  199 HIS B O   1 
ATOM   4701 C  CB  A HIS B 1 197 ? 19.144  10.823  -36.777 0.50 13.17 ?  199 HIS B CB  1 
ATOM   4702 C  CB  B HIS B 1 197 ? 19.091  10.885  -36.775 0.50 13.19 ?  199 HIS B CB  1 
ATOM   4703 C  CG  A HIS B 1 197 ? 19.543  10.111  -38.035 0.50 12.61 ?  199 HIS B CG  1 
ATOM   4704 C  CG  B HIS B 1 197 ? 19.583  10.217  -38.025 0.50 12.65 ?  199 HIS B CG  1 
ATOM   4705 N  ND1 A HIS B 1 197 ? 19.909  8.783   -38.057 0.50 14.78 ?  199 HIS B ND1 1 
ATOM   4706 N  ND1 B HIS B 1 197 ? 19.707  8.851   -38.146 0.50 14.67 ?  199 HIS B ND1 1 
ATOM   4707 C  CD2 A HIS B 1 197 ? 19.660  10.554  -39.309 0.50 12.81 ?  199 HIS B CD2 1 
ATOM   4708 C  CD2 B HIS B 1 197 ? 19.976  10.736  -39.213 0.50 13.02 ?  199 HIS B CD2 1 
ATOM   4709 C  CE1 A HIS B 1 197 ? 20.217  8.433   -39.293 0.50 14.61 ?  199 HIS B CE1 1 
ATOM   4710 C  CE1 B HIS B 1 197 ? 20.164  8.556   -39.351 0.50 14.60 ?  199 HIS B CE1 1 
ATOM   4711 N  NE2 A HIS B 1 197 ? 20.082  9.490   -40.073 0.50 13.13 ?  199 HIS B NE2 1 
ATOM   4712 N  NE2 B HIS B 1 197 ? 20.341  9.682   -40.018 0.50 13.00 ?  199 HIS B NE2 1 
ATOM   4713 N  N   . GLY B 1 198 ? 18.146  10.291  -33.276 1.00 19.49 ?  200 GLY B N   1 
ATOM   4714 C  CA  . GLY B 1 198 ? 18.344  10.886  -31.967 1.00 17.87 ?  200 GLY B CA  1 
ATOM   4715 C  C   . GLY B 1 198 ? 19.362  10.123  -31.147 1.00 15.95 ?  200 GLY B C   1 
ATOM   4716 O  O   . GLY B 1 198 ? 19.694  8.976   -31.453 1.00 14.84 ?  200 GLY B O   1 
ATOM   4717 N  N   . PRO B 1 199 ? 19.888  10.752  -30.085 1.00 17.32 ?  201 PRO B N   1 
ATOM   4718 C  CA  . PRO B 1 199 ? 20.962  10.114  -29.306 1.00 18.36 ?  201 PRO B CA  1 
ATOM   4719 C  C   . PRO B 1 199 ? 20.609  8.748   -28.750 1.00 17.42 ?  201 PRO B C   1 
ATOM   4720 O  O   . PRO B 1 199 ? 21.505  7.915   -28.564 1.00 16.43 ?  201 PRO B O   1 
ATOM   4721 C  CB  . PRO B 1 199 ? 21.210  11.122  -28.174 1.00 23.59 ?  201 PRO B CB  1 
ATOM   4722 C  CG  . PRO B 1 199 ? 20.813  12.423  -28.749 1.00 23.09 ?  201 PRO B CG  1 
ATOM   4723 C  CD  . PRO B 1 199 ? 19.629  12.132  -29.637 1.00 20.64 ?  201 PRO B CD  1 
ATOM   4724 N  N   . ARG B 1 200 ? 19.333  8.487   -28.461 1.00 17.79 ?  202 ARG B N   1 
ATOM   4725 C  CA  . ARG B 1 200 ? 18.979  7.192   -27.896 1.00 15.71 ?  202 ARG B CA  1 
ATOM   4726 C  C   . ARG B 1 200 ? 19.187  6.067   -28.906 1.00 18.43 ?  202 ARG B C   1 
ATOM   4727 O  O   . ARG B 1 200 ? 19.447  4.924   -28.512 1.00 19.94 ?  202 ARG B O   1 
ATOM   4728 C  CB  . ARG B 1 200 ? 17.539  7.240   -27.389 1.00 23.59 ?  202 ARG B CB  1 
ATOM   4729 C  CG  . ARG B 1 200 ? 17.442  7.913   -26.021 1.00 28.85 ?  202 ARG B CG  1 
ATOM   4730 C  CD  . ARG B 1 200 ? 16.025  7.919   -25.452 1.00 29.38 ?  202 ARG B CD  1 
ATOM   4731 N  NE  . ARG B 1 200 ? 15.242  9.038   -25.977 1.00 38.81 ?  202 ARG B NE  1 
ATOM   4732 C  CZ  . ARG B 1 200 ? 14.047  8.915   -26.556 1.00 41.46 ?  202 ARG B CZ  1 
ATOM   4733 N  NH1 . ARG B 1 200 ? 13.476  7.722   -26.656 1.00 47.64 ?  202 ARG B NH1 1 
ATOM   4734 N  NH2 . ARG B 1 200 ? 13.413  9.986   -27.022 1.00 40.13 ?  202 ARG B NH2 1 
ATOM   4735 N  N   . PHE B 1 201 ? 19.106  6.368   -30.209 1.00 15.80 ?  203 PHE B N   1 
ATOM   4736 C  CA  . PHE B 1 201 ? 19.507  5.380   -31.206 1.00 13.78 ?  203 PHE B CA  1 
ATOM   4737 C  C   . PHE B 1 201 ? 21.017  5.405   -31.435 1.00 13.65 ?  203 PHE B C   1 
ATOM   4738 O  O   . PHE B 1 201 ? 21.668  4.356   -31.439 1.00 17.15 ?  203 PHE B O   1 
ATOM   4739 C  CB  . PHE B 1 201 ? 18.788  5.627   -32.538 1.00 12.40 ?  203 PHE B CB  1 
ATOM   4740 C  CG  . PHE B 1 201 ? 17.332  5.221   -32.540 1.00 15.42 ?  203 PHE B CG  1 
ATOM   4741 C  CD1 . PHE B 1 201 ? 16.339  6.120   -32.165 1.00 19.69 ?  203 PHE B CD1 1 
ATOM   4742 C  CD2 . PHE B 1 201 ? 16.958  3.944   -32.922 1.00 17.33 ?  203 PHE B CD2 1 
ATOM   4743 C  CE1 . PHE B 1 201 ? 14.983  5.742   -32.178 1.00 18.24 ?  203 PHE B CE1 1 
ATOM   4744 C  CE2 . PHE B 1 201 ? 15.619  3.564   -32.935 1.00 17.35 ?  203 PHE B CE2 1 
ATOM   4745 C  CZ  . PHE B 1 201 ? 14.635  4.461   -32.561 1.00 17.51 ?  203 PHE B CZ  1 
ATOM   4746 N  N   . LEU B 1 202 ? 21.581  6.601   -31.642 1.00 12.56 ?  204 LEU B N   1 
ATOM   4747 C  CA  . LEU B 1 202 ? 22.940  6.728   -32.162 1.00 14.08 ?  204 LEU B CA  1 
ATOM   4748 C  C   . LEU B 1 202 ? 24.002  6.399   -31.131 1.00 14.48 ?  204 LEU B C   1 
ATOM   4749 O  O   . LEU B 1 202 ? 25.136  6.101   -31.514 1.00 15.03 ?  204 LEU B O   1 
ATOM   4750 C  CB  . LEU B 1 202 ? 23.155  8.143   -32.694 1.00 16.12 ?  204 LEU B CB  1 
ATOM   4751 C  CG  . LEU B 1 202 ? 22.273  8.489   -33.903 1.00 17.04 ?  204 LEU B CG  1 
ATOM   4752 C  CD1 . LEU B 1 202 ? 22.795  9.745   -34.563 1.00 17.40 ?  204 LEU B CD1 1 
ATOM   4753 C  CD2 . LEU B 1 202 ? 22.225  7.339   -34.913 1.00 14.80 ?  204 LEU B CD2 1 
ATOM   4754 N  N   . GLU B 1 203 ? 23.678  6.471   -29.841 1.00 14.91 ?  205 GLU B N   1 
ATOM   4755 C  CA  . GLU B 1 203 ? 24.638  6.110   -28.807 1.00 16.66 ?  205 GLU B CA  1 
ATOM   4756 C  C   . GLU B 1 203 ? 24.611  4.625   -28.479 1.00 14.03 ?  205 GLU B C   1 
ATOM   4757 O  O   . GLU B 1 203 ? 25.428  4.172   -27.677 1.00 17.08 ?  205 GLU B O   1 
ATOM   4758 C  CB  . GLU B 1 203 ? 24.391  6.940   -27.542 1.00 16.77 ?  205 GLU B CB  1 
ATOM   4759 C  CG  . GLU B 1 203 ? 24.641  8.449   -27.727 1.00 15.42 ?  205 GLU B CG  1 
ATOM   4760 C  CD  . GLU B 1 203 ? 26.034  8.765   -28.255 1.00 17.97 ?  205 GLU B CD  1 
ATOM   4761 O  OE1 . GLU B 1 203 ? 27.005  8.137   -27.793 1.00 17.98 ?  205 GLU B OE1 1 
ATOM   4762 O  OE2 . GLU B 1 203 ? 26.167  9.666   -29.110 1.00 17.14 ?  205 GLU B OE2 1 
ATOM   4763 N  N   . HIS B 1 204 ? 23.705  3.859   -29.080 1.00 13.00 ?  206 HIS B N   1 
ATOM   4764 C  CA  . HIS B 1 204 ? 23.724  2.415   -28.902 1.00 16.00 ?  206 HIS B CA  1 
ATOM   4765 C  C   . HIS B 1 204 ? 25.027  1.843   -29.451 1.00 14.91 ?  206 HIS B C   1 
ATOM   4766 O  O   . HIS B 1 204 ? 25.475  2.256   -30.529 1.00 16.10 ?  206 HIS B O   1 
ATOM   4767 C  CB  . HIS B 1 204 ? 22.547  1.768   -29.630 1.00 15.37 ?  206 HIS B CB  1 
ATOM   4768 C  CG  . HIS B 1 204 ? 22.289  0.352   -29.217 1.00 19.25 ?  206 HIS B CG  1 
ATOM   4769 N  ND1 . HIS B 1 204 ? 23.010  -0.709  -29.724 1.00 17.56 ?  206 HIS B ND1 1 
ATOM   4770 C  CD2 . HIS B 1 204 ? 21.366  -0.185  -28.383 1.00 21.22 ?  206 HIS B CD2 1 
ATOM   4771 C  CE1 . HIS B 1 204 ? 22.557  -1.836  -29.202 1.00 19.92 ?  206 HIS B CE1 1 
ATOM   4772 N  NE2 . HIS B 1 204 ? 21.556  -1.547  -28.389 1.00 21.41 ?  206 HIS B NE2 1 
ATOM   4773 N  N   . PRO B 1 205 ? 25.656  0.886   -28.751 1.00 16.91 ?  207 PRO B N   1 
ATOM   4774 C  CA  . PRO B 1 205 ? 26.957  0.374   -29.212 1.00 16.75 ?  207 PRO B CA  1 
ATOM   4775 C  C   . PRO B 1 205 ? 26.888  -0.362  -30.534 1.00 19.64 ?  207 PRO B C   1 
ATOM   4776 O  O   . PRO B 1 205 ? 27.919  -0.473  -31.213 1.00 20.25 ?  207 PRO B O   1 
ATOM   4777 C  CB  . PRO B 1 205 ? 27.392  -0.566  -28.076 1.00 22.73 ?  207 PRO B CB  1 
ATOM   4778 C  CG  . PRO B 1 205 ? 26.133  -0.900  -27.356 1.00 27.88 ?  207 PRO B CG  1 
ATOM   4779 C  CD  . PRO B 1 205 ? 25.288  0.334   -27.437 1.00 19.01 ?  207 PRO B CD  1 
ATOM   4780 N  N   . LEU B 1 206 ? 25.719  -0.863  -30.929 1.00 15.81 ?  208 LEU B N   1 
ATOM   4781 C  CA  . LEU B 1 206 ? 25.578  -1.538  -32.212 1.00 17.06 ?  208 LEU B CA  1 
ATOM   4782 C  C   . LEU B 1 206 ? 25.063  -0.616  -33.310 1.00 15.90 ?  208 LEU B C   1 
ATOM   4783 O  O   . LEU B 1 206 ? 24.862  -1.080  -34.433 1.00 14.77 ?  208 LEU B O   1 
ATOM   4784 C  CB  . LEU B 1 206 ? 24.654  -2.755  -32.077 1.00 16.68 ?  208 LEU B CB  1 
ATOM   4785 C  CG  . LEU B 1 206 ? 25.124  -3.851  -31.116 1.00 20.12 ?  208 LEU B CG  1 
ATOM   4786 C  CD1 . LEU B 1 206 ? 24.238  -5.077  -31.224 1.00 21.17 ?  208 LEU B CD1 1 
ATOM   4787 C  CD2 . LEU B 1 206 ? 26.583  -4.222  -31.373 1.00 23.09 ?  208 LEU B CD2 1 
ATOM   4788 N  N   . ALA B 1 207 ? 24.866  0.678   -33.024 1.00 13.20 ?  209 ALA B N   1 
ATOM   4789 C  CA  . ALA B 1 207 ? 24.621  1.674   -34.074 1.00 11.87 ?  209 ALA B CA  1 
ATOM   4790 C  C   . ALA B 1 207 ? 25.970  2.045   -34.690 1.00 14.34 ?  209 ALA B C   1 
ATOM   4791 O  O   . ALA B 1 207 ? 26.590  3.060   -34.358 1.00 14.73 ?  209 ALA B O   1 
ATOM   4792 C  CB  . ALA B 1 207 ? 23.901  2.896   -33.516 1.00 13.94 ?  209 ALA B CB  1 
ATOM   4793 N  N   . ASP B 1 208 ? 26.442  1.184   -35.593 1.00 13.15 ?  210 ASP B N   1 
ATOM   4794 C  CA  . ASP B 1 208 ? 27.802  1.295   -36.105 1.00 12.15 ?  210 ASP B CA  1 
ATOM   4795 C  C   . ASP B 1 208 ? 27.928  0.459   -37.369 1.00 13.41 ?  210 ASP B C   1 
ATOM   4796 O  O   . ASP B 1 208 ? 27.099  -0.407  -37.650 1.00 12.08 ?  210 ASP B O   1 
ATOM   4797 C  CB  . ASP B 1 208 ? 28.828  0.834   -35.061 1.00 17.40 ?  210 ASP B CB  1 
ATOM   4798 C  CG  . ASP B 1 208 ? 30.148  1.594   -35.143 1.00 24.29 ?  210 ASP B CG  1 
ATOM   4799 O  OD1 . ASP B 1 208 ? 30.924  1.505   -34.167 1.00 29.56 ?  210 ASP B OD1 1 
ATOM   4800 O  OD2 . ASP B 1 208 ? 30.413  2.270   -36.166 1.00 22.59 ?  210 ASP B OD2 1 
ATOM   4801 N  N   . CYS B 1 209 ? 28.991  0.730   -38.119 1.00 11.71 ?  211 CYS B N   1 
ATOM   4802 C  CA  A CYS B 1 209 ? 29.248  0.036   -39.379 0.65 13.33 ?  211 CYS B CA  1 
ATOM   4803 C  CA  B CYS B 1 209 ? 29.216  0.029   -39.376 0.35 13.33 ?  211 CYS B CA  1 
ATOM   4804 C  C   . CYS B 1 209 ? 29.215  -1.479  -39.193 1.00 14.14 ?  211 CYS B C   1 
ATOM   4805 O  O   . CYS B 1 209 ? 29.847  -2.019  -38.275 1.00 13.60 ?  211 CYS B O   1 
ATOM   4806 C  CB  A CYS B 1 209 ? 30.618  0.460   -39.929 0.65 14.83 ?  211 CYS B CB  1 
ATOM   4807 C  CB  B CYS B 1 209 ? 30.537  0.471   -39.991 0.35 14.84 ?  211 CYS B CB  1 
ATOM   4808 S  SG  A CYS B 1 209 ? 31.048  2.244   -39.835 0.65 14.93 ?  211 CYS B SG  1 
ATOM   4809 S  SG  B CYS B 1 209 ? 30.367  1.980   -40.905 0.35 13.83 ?  211 CYS B SG  1 
ATOM   4810 N  N   . GLY B 1 210 ? 28.485  -2.162  -40.075 1.00 11.49 ?  212 GLY B N   1 
ATOM   4811 C  CA  . GLY B 1 210 ? 28.505  -3.604  -40.133 1.00 15.24 ?  212 GLY B CA  1 
ATOM   4812 C  C   . GLY B 1 210 ? 27.442  -4.324  -39.329 1.00 17.53 ?  212 GLY B C   1 
ATOM   4813 O  O   . GLY B 1 210 ? 27.293  -5.542  -39.500 1.00 18.60 ?  212 GLY B O   1 
ATOM   4814 N  N   . PHE B 1 211 ? 26.689  -3.628  -38.472 1.00 14.34 ?  213 PHE B N   1 
ATOM   4815 C  CA  . PHE B 1 211 ? 25.732  -4.271  -37.575 1.00 15.94 ?  213 PHE B CA  1 
ATOM   4816 C  C   . PHE B 1 211 ? 24.313  -4.068  -38.085 1.00 13.13 ?  213 PHE B C   1 
ATOM   4817 O  O   . PHE B 1 211 ? 23.875  -2.927  -38.270 1.00 13.97 ?  213 PHE B O   1 
ATOM   4818 C  CB  . PHE B 1 211 ? 25.846  -3.702  -36.161 1.00 15.02 ?  213 PHE B CB  1 
ATOM   4819 C  CG  . PHE B 1 211 ? 27.148  -4.027  -35.485 1.00 18.66 ?  213 PHE B CG  1 
ATOM   4820 C  CD1 . PHE B 1 211 ? 27.409  -5.311  -35.037 1.00 18.65 ?  213 PHE B CD1 1 
ATOM   4821 C  CD2 . PHE B 1 211 ? 28.113  -3.051  -35.307 1.00 17.36 ?  213 PHE B CD2 1 
ATOM   4822 C  CE1 . PHE B 1 211 ? 28.602  -5.617  -34.412 1.00 24.47 ?  213 PHE B CE1 1 
ATOM   4823 C  CE2 . PHE B 1 211 ? 29.314  -3.352  -34.691 1.00 18.53 ?  213 PHE B CE2 1 
ATOM   4824 C  CZ  . PHE B 1 211 ? 29.562  -4.638  -34.244 1.00 22.13 ?  213 PHE B CZ  1 
ATOM   4825 N  N   . LEU B 1 212 ? 23.590  -5.171  -38.277 1.00 16.34 ?  214 LEU B N   1 
ATOM   4826 C  CA  . LEU B 1 212 ? 22.172  -5.126  -38.623 1.00 14.15 ?  214 LEU B CA  1 
ATOM   4827 C  C   . LEU B 1 212 ? 21.354  -5.706  -37.476 1.00 19.29 ?  214 LEU B C   1 
ATOM   4828 O  O   . LEU B 1 212 ? 20.680  -4.959  -36.765 1.00 15.62 ?  214 LEU B O   1 
ATOM   4829 C  CB  . LEU B 1 212 ? 21.906  -5.874  -39.932 1.00 14.28 ?  214 LEU B CB  1 
ATOM   4830 C  CG  . LEU B 1 212 ? 22.496  -5.231  -41.190 1.00 14.72 ?  214 LEU B CG  1 
ATOM   4831 C  CD1 . LEU B 1 212 ? 22.200  -6.086  -42.415 1.00 17.90 ?  214 LEU B CD1 1 
ATOM   4832 C  CD2 . LEU B 1 212 ? 21.958  -3.822  -41.396 1.00 12.06 ?  214 LEU B CD2 1 
ATOM   4833 N  N   . GLU B 1 213 ? 21.427  -7.018  -37.248 1.00 20.87 ?  215 GLU B N   1 
ATOM   4834 C  CA  . GLU B 1 213 ? 20.703  -7.623  -36.139 1.00 23.87 ?  215 GLU B CA  1 
ATOM   4835 C  C   . GLU B 1 213 ? 21.198  -7.059  -34.808 1.00 18.91 ?  215 GLU B C   1 
ATOM   4836 O  O   . GLU B 1 213 ? 22.398  -7.054  -34.523 1.00 19.57 ?  215 GLU B O   1 
ATOM   4837 C  CB  . GLU B 1 213 ? 20.865  -9.145  -36.178 1.00 28.51 ?  215 GLU B CB  1 
ATOM   4838 N  N   . GLY B 1 214 ? 20.263  -6.580  -33.990 1.00 20.17 ?  216 GLY B N   1 
ATOM   4839 C  CA  . GLY B 1 214 ? 20.605  -5.972  -32.725 1.00 24.02 ?  216 GLY B CA  1 
ATOM   4840 C  C   . GLY B 1 214 ? 20.908  -4.495  -32.805 1.00 21.04 ?  216 GLY B C   1 
ATOM   4841 O  O   . GLY B 1 214 ? 21.049  -3.848  -31.758 1.00 21.18 ?  216 GLY B O   1 
ATOM   4842 N  N   . ASN B 1 215 ? 21.015  -3.943  -34.012 1.00 16.25 ?  217 ASN B N   1 
ATOM   4843 C  CA  . ASN B 1 215 ? 21.247  -2.516  -34.189 1.00 19.99 ?  217 ASN B CA  1 
ATOM   4844 C  C   . ASN B 1 215 ? 19.897  -1.809  -34.230 1.00 17.97 ?  217 ASN B C   1 
ATOM   4845 O  O   . ASN B 1 215 ? 19.170  -1.950  -35.221 1.00 16.55 ?  217 ASN B O   1 
ATOM   4846 C  CB  . ASN B 1 215 ? 22.040  -2.262  -35.473 1.00 15.92 ?  217 ASN B CB  1 
ATOM   4847 C  CG  . ASN B 1 215 ? 22.142  -0.779  -35.832 1.00 14.16 ?  217 ASN B CG  1 
ATOM   4848 O  OD1 . ASN B 1 215 ? 21.712  0.090   -35.074 1.00 14.04 ?  217 ASN B OD1 1 
ATOM   4849 N  ND2 . ASN B 1 215 ? 22.799  -0.487  -36.958 1.00 12.52 ?  217 ASN B ND2 1 
ATOM   4850 N  N   . PRO B 1 216 ? 19.526  -1.032  -33.208 1.00 15.00 ?  218 PRO B N   1 
ATOM   4851 C  CA  . PRO B 1 216 ? 18.187  -0.416  -33.212 1.00 15.64 ?  218 PRO B CA  1 
ATOM   4852 C  C   . PRO B 1 216 ? 17.937  0.505   -34.390 1.00 18.30 ?  218 PRO B C   1 
ATOM   4853 O  O   . PRO B 1 216 ? 16.782  0.686   -34.786 1.00 14.15 ?  218 PRO B O   1 
ATOM   4854 C  CB  . PRO B 1 216 ? 18.158  0.358   -31.885 1.00 18.54 ?  218 PRO B CB  1 
ATOM   4855 C  CG  . PRO B 1 216 ? 19.595  0.647   -31.599 1.00 18.62 ?  218 PRO B CG  1 
ATOM   4856 C  CD  . PRO B 1 216 ? 20.328  -0.589  -32.054 1.00 17.93 ?  218 PRO B CD  1 
ATOM   4857 N  N   . VAL B 1 217 ? 18.982  1.108   -34.952 1.00 15.99 ?  219 VAL B N   1 
ATOM   4858 C  CA  . VAL B 1 217 ? 18.802  1.953   -36.128 1.00 12.55 ?  219 VAL B CA  1 
ATOM   4859 C  C   . VAL B 1 217 ? 18.233  1.139   -37.274 1.00 14.56 ?  219 VAL B C   1 
ATOM   4860 O  O   . VAL B 1 217 ? 17.308  1.571   -37.974 1.00 14.68 ?  219 VAL B O   1 
ATOM   4861 C  CB  . VAL B 1 217 ? 20.137  2.612   -36.517 1.00 11.14 ?  219 VAL B CB  1 
ATOM   4862 C  CG1 . VAL B 1 217 ? 19.995  3.378   -37.809 1.00 12.79 ?  219 VAL B CG1 1 
ATOM   4863 C  CG2 . VAL B 1 217 ? 20.580  3.535   -35.399 1.00 12.83 ?  219 VAL B CG2 1 
ATOM   4864 N  N   . HIS B 1 218 ? 18.798  -0.046  -37.487 1.00 12.42 ?  220 HIS B N   1 
ATOM   4865 C  CA  . HIS B 1 218 ? 18.371  -0.910  -38.574 1.00 15.23 ?  220 HIS B CA  1 
ATOM   4866 C  C   . HIS B 1 218 ? 17.000  -1.509  -38.296 1.00 16.21 ?  220 HIS B C   1 
ATOM   4867 O  O   . HIS B 1 218 ? 16.156  -1.591  -39.195 1.00 16.66 ?  220 HIS B O   1 
ATOM   4868 C  CB  . HIS B 1 218 ? 19.399  -2.017  -38.780 1.00 15.23 ?  220 HIS B CB  1 
ATOM   4869 C  CG  . HIS B 1 218 ? 18.896  -3.130  -39.634 1.00 15.66 ?  220 HIS B CG  1 
ATOM   4870 N  ND1 . HIS B 1 218 ? 18.645  -2.974  -40.980 1.00 14.11 ?  220 HIS B ND1 1 
ATOM   4871 C  CD2 . HIS B 1 218 ? 18.558  -4.405  -39.329 1.00 17.06 ?  220 HIS B CD2 1 
ATOM   4872 C  CE1 . HIS B 1 218 ? 18.182  -4.111  -41.470 1.00 14.38 ?  220 HIS B CE1 1 
ATOM   4873 N  NE2 . HIS B 1 218 ? 18.123  -4.996  -40.489 1.00 15.05 ?  220 HIS B NE2 1 
ATOM   4874 N  N   . GLU B 1 219 ? 16.769  -1.951  -37.061 1.00 16.59 ?  221 GLU B N   1 
ATOM   4875 C  CA  . GLU B 1 219 ? 15.460  -2.500  -36.717 1.00 18.38 ?  221 GLU B CA  1 
ATOM   4876 C  C   . GLU B 1 219 ? 14.359  -1.479  -36.962 1.00 19.96 ?  221 GLU B C   1 
ATOM   4877 O  O   . GLU B 1 219 ? 13.289  -1.822  -37.480 1.00 20.05 ?  221 GLU B O   1 
ATOM   4878 C  CB  . GLU B 1 219 ? 15.471  -2.981  -35.267 1.00 18.30 ?  221 GLU B CB  1 
ATOM   4879 C  CG  . GLU B 1 219 ? 16.421  -4.166  -35.100 1.00 21.63 ?  221 GLU B CG  1 
ATOM   4880 C  CD  . GLU B 1 219 ? 16.746  -4.530  -33.662 1.00 27.36 ?  221 GLU B CD  1 
ATOM   4881 O  OE1 . GLU B 1 219 ? 16.627  -3.672  -32.761 1.00 33.67 ?  221 GLU B OE1 1 
ATOM   4882 O  OE2 . GLU B 1 219 ? 17.149  -5.690  -33.445 1.00 31.89 ?  221 GLU B OE2 1 
ATOM   4883 N  N   . GLU B 1 220 ? 14.624  -0.210  -36.647 1.00 17.73 ?  222 GLU B N   1 
ATOM   4884 C  CA  . GLU B 1 220 ? 13.608  0.828   -36.750 1.00 16.68 ?  222 GLU B CA  1 
ATOM   4885 C  C   . GLU B 1 220 ? 13.378  1.285   -38.188 1.00 19.68 ?  222 GLU B C   1 
ATOM   4886 O  O   . GLU B 1 220 ? 12.223  1.495   -38.588 1.00 17.82 ?  222 GLU B O   1 
ATOM   4887 C  CB  . GLU B 1 220 ? 13.989  2.018   -35.864 1.00 16.35 ?  222 GLU B CB  1 
ATOM   4888 C  CG  . GLU B 1 220 ? 12.887  3.066   -35.708 1.00 18.44 ?  222 GLU B CG  1 
ATOM   4889 C  CD  . GLU B 1 220 ? 11.819  2.684   -34.693 1.00 24.89 ?  222 GLU B CD  1 
ATOM   4890 O  OE1 . GLU B 1 220 ? 10.945  3.531   -34.444 1.00 25.79 ?  222 GLU B OE1 1 
ATOM   4891 O  OE2 . GLU B 1 220 ? 11.868  1.568   -34.131 1.00 23.83 ?  222 GLU B OE2 1 
ATOM   4892 N  N   . ASN B 1 221 ? 14.441  1.479   -38.985 1.00 16.62 ?  223 ASN B N   1 
ATOM   4893 C  CA  . ASN B 1 221 ? 14.156  1.926   -40.349 1.00 16.04 ?  223 ASN B CA  1 
ATOM   4894 C  C   . ASN B 1 221 ? 13.609  0.793   -41.201 1.00 16.92 ?  223 ASN B C   1 
ATOM   4895 O  O   . ASN B 1 221 ? 12.863  1.057   -42.143 1.00 18.18 ?  223 ASN B O   1 
ATOM   4896 C  CB  . ASN B 1 221 ? 15.373  2.632   -41.000 1.00 13.22 ?  223 ASN B CB  1 
ATOM   4897 C  CG  . ASN B 1 221 ? 16.517  1.701   -41.452 1.00 15.08 ?  223 ASN B CG  1 
ATOM   4898 O  OD1 . ASN B 1 221 ? 16.673  0.546   -41.029 1.00 15.42 ?  223 ASN B OD1 1 
ATOM   4899 N  ND2 . ASN B 1 221 ? 17.370  2.264   -42.313 1.00 12.68 ?  223 ASN B ND2 1 
ATOM   4900 N  N   . THR B 1 222 ? 13.881  -0.461  -40.844 1.00 15.72 ?  224 THR B N   1 
ATOM   4901 C  CA  . THR B 1 222 ? 13.183  -1.564  -41.507 1.00 18.57 ?  224 THR B CA  1 
ATOM   4902 C  C   . THR B 1 222 ? 11.704  -1.568  -41.141 1.00 20.48 ?  224 THR B C   1 
ATOM   4903 O  O   . THR B 1 222 ? 10.843  -1.763  -42.010 1.00 19.47 ?  224 THR B O   1 
ATOM   4904 C  CB  . THR B 1 222 ? 13.829  -2.899  -41.140 1.00 21.05 ?  224 THR B CB  1 
ATOM   4905 O  OG1 . THR B 1 222 ? 15.196  -2.905  -41.586 1.00 14.95 ?  224 THR B OG1 1 
ATOM   4906 C  CG2 . THR B 1 222 ? 13.078  -4.058  -41.786 1.00 19.92 ?  224 THR B CG2 1 
ATOM   4907 N  N   . ARG B 1 223 ? 11.395  -1.316  -39.868 1.00 20.45 ?  225 ARG B N   1 
ATOM   4908 C  CA  . ARG B 1 223 ? 10.002  -1.242  -39.434 1.00 23.07 ?  225 ARG B CA  1 
ATOM   4909 C  C   . ARG B 1 223 ? 9.253   -0.125  -40.158 1.00 21.06 ?  225 ARG B C   1 
ATOM   4910 O  O   . ARG B 1 223 ? 8.152   -0.336  -40.683 1.00 22.66 ?  225 ARG B O   1 
ATOM   4911 C  CB  . ARG B 1 223 ? 9.951   -1.052  -37.918 1.00 22.01 ?  225 ARG B CB  1 
ATOM   4912 C  CG  . ARG B 1 223 ? 8.556   -0.960  -37.342 1.00 30.66 ?  225 ARG B CG  1 
ATOM   4913 C  CD  . ARG B 1 223 ? 8.603   -0.843  -35.818 1.00 36.39 ?  225 ARG B CD  1 
ATOM   4914 N  NE  . ARG B 1 223 ? 8.825   -2.131  -35.166 1.00 38.07 ?  225 ARG B NE  1 
ATOM   4915 C  CZ  . ARG B 1 223 ? 7.847   -2.957  -34.803 1.00 43.18 ?  225 ARG B CZ  1 
ATOM   4916 N  NH1 . ARG B 1 223 ? 6.582   -2.624  -35.024 1.00 38.01 ?  225 ARG B NH1 1 
ATOM   4917 N  NH2 . ARG B 1 223 ? 8.132   -4.113  -34.217 1.00 40.17 ?  225 ARG B NH2 1 
ATOM   4918 N  N   . ILE B 1 224 ? 9.840   1.069   -40.211 1.00 17.84 ?  226 ILE B N   1 
ATOM   4919 C  CA  . ILE B 1 224 ? 9.167   2.210   -40.824 1.00 17.60 ?  226 ILE B CA  1 
ATOM   4920 C  C   . ILE B 1 224 ? 9.004   2.002   -42.327 1.00 22.08 ?  226 ILE B C   1 
ATOM   4921 O  O   . ILE B 1 224 ? 7.951   2.318   -42.899 1.00 19.19 ?  226 ILE B O   1 
ATOM   4922 C  CB  . ILE B 1 224 ? 9.941   3.499   -40.488 1.00 16.56 ?  226 ILE B CB  1 
ATOM   4923 C  CG1 . ILE B 1 224 ? 9.754   3.828   -38.998 1.00 19.47 ?  226 ILE B CG1 1 
ATOM   4924 C  CG2 . ILE B 1 224 ? 9.522   4.662   -41.372 1.00 18.18 ?  226 ILE B CG2 1 
ATOM   4925 C  CD1 . ILE B 1 224 ? 10.762  4.802   -38.429 1.00 20.51 ?  226 ILE B CD1 1 
ATOM   4926 N  N   . ALA B 1 225 ? 10.033  1.455   -42.991 1.00 15.23 ?  227 ALA B N   1 
ATOM   4927 C  CA  . ALA B 1 225 ? 9.902   1.096   -44.402 1.00 16.75 ?  227 ALA B CA  1 
ATOM   4928 C  C   . ALA B 1 225 ? 8.738   0.138   -44.630 1.00 17.28 ?  227 ALA B C   1 
ATOM   4929 O  O   . ALA B 1 225 ? 8.015   0.253   -45.625 1.00 23.90 ?  227 ALA B O   1 
ATOM   4930 C  CB  . ALA B 1 225 ? 11.198  0.461   -44.908 1.00 18.08 ?  227 ALA B CB  1 
ATOM   4931 N  N   . ARG B 1 226 ? 8.562   -0.833  -43.738 1.00 20.69 ?  228 ARG B N   1 
ATOM   4932 C  CA  . ARG B 1 226 ? 7.478   -1.794  -43.910 1.00 22.18 ?  228 ARG B CA  1 
ATOM   4933 C  C   . ARG B 1 226 ? 6.114   -1.139  -43.732 1.00 27.60 ?  228 ARG B C   1 
ATOM   4934 O  O   . ARG B 1 226 ? 5.130   -1.611  -44.315 1.00 23.64 ?  228 ARG B O   1 
ATOM   4935 C  CB  . ARG B 1 226 ? 7.658   -2.964  -42.941 1.00 24.07 ?  228 ARG B CB  1 
ATOM   4936 C  CG  . ARG B 1 226 ? 8.628   -4.066  -43.432 1.00 23.51 ?  228 ARG B CG  1 
ATOM   4937 C  CD  . ARG B 1 226 ? 8.472   -4.346  -44.957 1.00 34.40 ?  228 ARG B CD  1 
ATOM   4938 N  NE  . ARG B 1 226 ? 9.188   -5.548  -45.423 1.00 37.42 ?  228 ARG B NE  1 
ATOM   4939 C  CZ  . ARG B 1 226 ? 9.206   -5.976  -46.690 1.00 36.68 ?  228 ARG B CZ  1 
ATOM   4940 N  NH1 . ARG B 1 226 ? 8.548   -5.311  -47.633 1.00 38.81 ?  228 ARG B NH1 1 
ATOM   4941 N  NH2 . ARG B 1 226 ? 9.888   -7.068  -47.025 1.00 34.13 ?  228 ARG B NH2 1 
ATOM   4942 N  N   . MET B 1 227 ? 6.025   -0.055  -42.946 1.00 24.25 ?  229 MET B N   1 
ATOM   4943 C  CA  . MET B 1 227 ? 4.745   0.643   -42.823 1.00 24.14 ?  229 MET B CA  1 
ATOM   4944 C  C   . MET B 1 227 ? 4.412   1.426   -44.087 1.00 25.13 ?  229 MET B C   1 
ATOM   4945 O  O   . MET B 1 227 ? 3.230   1.570   -44.434 1.00 25.61 ?  229 MET B O   1 
ATOM   4946 C  CB  . MET B 1 227 ? 4.739   1.578   -41.600 1.00 24.27 ?  229 MET B CB  1 
ATOM   4947 C  CG  . MET B 1 227 ? 5.245   0.950   -40.308 1.00 24.54 ?  229 MET B CG  1 
ATOM   4948 S  SD  . MET B 1 227 ? 5.628   2.144   -38.989 1.00 27.96 ?  229 MET B SD  1 
ATOM   4949 C  CE  . MET B 1 227 ? 4.115   3.113   -38.954 1.00 26.31 ?  229 MET B CE  1 
ATOM   4950 N  N   . ALA B 1 228 ? 5.425   1.936   -44.787 1.00 19.28 ?  230 ALA B N   1 
ATOM   4951 C  CA  . ALA B 1 228 ? 5.181   2.579   -46.070 1.00 21.89 ?  230 ALA B CA  1 
ATOM   4952 C  C   . ALA B 1 228 ? 4.977   1.553   -47.171 1.00 23.29 ?  230 ALA B C   1 
ATOM   4953 O  O   . ALA B 1 228 ? 4.203   1.793   -48.105 1.00 23.32 ?  230 ALA B O   1 
ATOM   4954 C  CB  . ALA B 1 228 ? 6.339   3.514   -46.437 1.00 19.06 ?  230 ALA B CB  1 
ATOM   4955 N  N   . GLY B 1 229 ? 5.639   0.410   -47.060 1.00 19.95 ?  231 GLY B N   1 
ATOM   4956 C  CA  . GLY B 1 229 ? 5.609   -0.599  -48.092 1.00 22.63 ?  231 GLY B CA  1 
ATOM   4957 C  C   . GLY B 1 229 ? 6.645   -0.339  -49.171 1.00 19.52 ?  231 GLY B C   1 
ATOM   4958 O  O   . GLY B 1 229 ? 7.107   0.782   -49.381 1.00 23.28 ?  231 GLY B O   1 
ATOM   4959 N  N   . CYS B 1 230 ? 7.005   -1.416  -49.859 1.00 19.69 ?  232 CYS B N   1 
ATOM   4960 C  CA  . CYS B 1 230 ? 7.933   -1.367  -50.979 1.00 18.97 ?  232 CYS B CA  1 
ATOM   4961 C  C   . CYS B 1 230 ? 7.727   -2.643  -51.781 1.00 19.59 ?  232 CYS B C   1 
ATOM   4962 O  O   . CYS B 1 230 ? 7.782   -3.741  -51.218 1.00 24.08 ?  232 CYS B O   1 
ATOM   4963 C  CB  . CYS B 1 230 ? 9.384   -1.252  -50.486 1.00 21.63 ?  232 CYS B CB  1 
ATOM   4964 S  SG  . CYS B 1 230 ? 10.576  -1.093  -51.827 1.00 23.91 ?  232 CYS B SG  1 
ATOM   4965 N  N   . ASP B 1 231 ? 7.462   -2.503  -53.073 1.00 21.37 ?  233 ASP B N   1 
ATOM   4966 C  CA  . ASP B 1 231 ? 7.138   -3.690  -53.852 1.00 19.90 ?  233 ASP B CA  1 
ATOM   4967 C  C   . ASP B 1 231 ? 8.377   -4.366  -54.424 1.00 25.41 ?  233 ASP B C   1 
ATOM   4968 O  O   . ASP B 1 231 ? 8.368   -5.586  -54.634 1.00 22.87 ?  233 ASP B O   1 
ATOM   4969 C  CB  . ASP B 1 231 ? 6.167   -3.329  -54.973 1.00 20.70 ?  233 ASP B CB  1 
ATOM   4970 C  CG  . ASP B 1 231 ? 4.859   -2.742  -54.436 1.00 25.86 ?  233 ASP B CG  1 
ATOM   4971 O  OD1 . ASP B 1 231 ? 4.133   -3.469  -53.728 1.00 32.42 ?  233 ASP B OD1 1 
ATOM   4972 O  OD2 . ASP B 1 231 ? 4.563   -1.566  -54.725 1.00 22.28 ?  233 ASP B OD2 1 
ATOM   4973 N  N   . PHE B 1 232 ? 9.450   -3.612  -54.645 1.00 22.57 ?  234 PHE B N   1 
ATOM   4974 C  CA  . PHE B 1 232 ? 10.580  -4.138  -55.400 1.00 19.00 ?  234 PHE B CA  1 
ATOM   4975 C  C   . PHE B 1 232 ? 11.786  -3.232  -55.199 1.00 17.20 ?  234 PHE B C   1 
ATOM   4976 O  O   . PHE B 1 232 ? 11.669  -2.009  -55.276 1.00 17.85 ?  234 PHE B O   1 
ATOM   4977 C  CB  . PHE B 1 232 ? 10.233  -4.231  -56.892 1.00 20.68 ?  234 PHE B CB  1 
ATOM   4978 C  CG  . PHE B 1 232 ? 11.106  -5.175  -57.673 1.00 20.14 ?  234 PHE B CG  1 
ATOM   4979 C  CD1 . PHE B 1 232 ? 10.812  -6.530  -57.726 1.00 23.72 ?  234 PHE B CD1 1 
ATOM   4980 C  CD2 . PHE B 1 232 ? 12.198  -4.700  -58.390 1.00 22.10 ?  234 PHE B CD2 1 
ATOM   4981 C  CE1 . PHE B 1 232 ? 11.600  -7.398  -58.460 1.00 22.88 ?  234 PHE B CE1 1 
ATOM   4982 C  CE2 . PHE B 1 232 ? 12.994  -5.564  -59.123 1.00 18.92 ?  234 PHE B CE2 1 
ATOM   4983 C  CZ  . PHE B 1 232 ? 12.704  -6.910  -59.155 1.00 18.12 ?  234 PHE B CZ  1 
ATOM   4984 N  N   . ILE B 1 233 ? 12.943  -3.834  -54.962 1.00 17.71 ?  235 ILE B N   1 
ATOM   4985 C  CA  . ILE B 1 233 ? 14.171  -3.056  -54.906 1.00 14.92 ?  235 ILE B CA  1 
ATOM   4986 C  C   . ILE B 1 233 ? 15.156  -3.592  -55.938 1.00 15.84 ?  235 ILE B C   1 
ATOM   4987 O  O   . ILE B 1 233 ? 15.089  -4.745  -56.360 1.00 16.57 ?  235 ILE B O   1 
ATOM   4988 C  CB  . ILE B 1 233 ? 14.798  -3.055  -53.491 1.00 14.66 ?  235 ILE B CB  1 
ATOM   4989 C  CG1 . ILE B 1 233 ? 15.313  -4.438  -53.080 1.00 17.55 ?  235 ILE B CG1 1 
ATOM   4990 C  CG2 . ILE B 1 233 ? 13.842  -2.520  -52.459 1.00 17.58 ?  235 ILE B CG2 1 
ATOM   4991 C  CD1 . ILE B 1 233 ? 16.479  -4.367  -52.056 1.00 12.26 ?  235 ILE B CD1 1 
ATOM   4992 N  N   . VAL B 1 234 ? 16.084  -2.731  -56.339 1.00 14.13 ?  236 VAL B N   1 
ATOM   4993 C  CA  . VAL B 1 234 ? 17.293  -3.152  -57.040 1.00 12.72 ?  236 VAL B CA  1 
ATOM   4994 C  C   . VAL B 1 234 ? 18.450  -2.441  -56.358 1.00 10.36 ?  236 VAL B C   1 
ATOM   4995 O  O   . VAL B 1 234 ? 18.490  -1.206  -56.345 1.00 12.33 ?  236 VAL B O   1 
ATOM   4996 C  CB  . VAL B 1 234 ? 17.277  -2.809  -58.541 1.00 13.87 ?  236 VAL B CB  1 
ATOM   4997 C  CG1 . VAL B 1 234 ? 18.542  -3.356  -59.218 1.00 13.10 ?  236 VAL B CG1 1 
ATOM   4998 C  CG2 . VAL B 1 234 ? 16.011  -3.342  -59.228 1.00 15.23 ?  236 VAL B CG2 1 
ATOM   4999 N  N   . ASN B 1 235 ? 19.392  -3.214  -55.814 1.00 14.18 ?  237 ASN B N   1 
ATOM   5000 C  CA  . ASN B 1 235 ? 20.577  -2.683  -55.146 1.00 11.95 ?  237 ASN B CA  1 
ATOM   5001 C  C   . ASN B 1 235 ? 21.838  -3.273  -55.769 1.00 13.65 ?  237 ASN B C   1 
ATOM   5002 O  O   . ASN B 1 235 ? 21.847  -4.435  -56.192 1.00 13.69 ?  237 ASN B O   1 
ATOM   5003 C  CB  . ASN B 1 235 ? 20.596  -3.028  -53.641 1.00 11.65 ?  237 ASN B CB  1 
ATOM   5004 C  CG  . ASN B 1 235 ? 19.647  -2.172  -52.792 1.00 15.08 ?  237 ASN B CG  1 
ATOM   5005 O  OD1 . ASN B 1 235 ? 19.686  -2.273  -51.566 1.00 16.82 ?  237 ASN B OD1 1 
ATOM   5006 N  ND2 . ASN B 1 235 ? 18.808  -1.345  -53.420 1.00 16.24 ?  237 ASN B ND2 1 
ATOM   5007 N  N   . VAL B 1 236 ? 22.922  -2.494  -55.764 1.00 13.12 ?  238 VAL B N   1 
ATOM   5008 C  CA  . VAL B 1 236 ? 24.213  -2.976  -56.251 1.00 11.27 ?  238 VAL B CA  1 
ATOM   5009 C  C   . VAL B 1 236 ? 25.254  -2.862  -55.146 1.00 13.26 ?  238 VAL B C   1 
ATOM   5010 O  O   . VAL B 1 236 ? 25.076  -2.156  -54.149 1.00 11.36 ?  238 VAL B O   1 
ATOM   5011 C  CB  . VAL B 1 236 ? 24.698  -2.208  -57.497 1.00 11.80 ?  238 VAL B CB  1 
ATOM   5012 C  CG1 . VAL B 1 236 ? 23.755  -2.445  -58.673 1.00 14.67 ?  238 VAL B CG1 1 
ATOM   5013 C  CG2 . VAL B 1 236 ? 24.845  -0.717  -57.186 1.00 12.91 ?  238 VAL B CG2 1 
ATOM   5014 N  N   . THR B 1 237 ? 26.346  -3.593  -55.332 1.00 11.51 ?  239 THR B N   1 
ATOM   5015 C  CA  . THR B 1 237 ? 27.597  -3.339  -54.625 1.00 9.97  ?  239 THR B CA  1 
ATOM   5016 C  C   . THR B 1 237 ? 28.653  -2.895  -55.633 1.00 12.33 ?  239 THR B C   1 
ATOM   5017 O  O   . THR B 1 237 ? 28.584  -3.238  -56.817 1.00 13.60 ?  239 THR B O   1 
ATOM   5018 C  CB  . THR B 1 237 ? 28.089  -4.572  -53.865 1.00 9.92  ?  239 THR B CB  1 
ATOM   5019 O  OG1 . THR B 1 237 ? 28.256  -5.677  -54.761 1.00 11.43 ?  239 THR B OG1 1 
ATOM   5020 C  CG2 . THR B 1 237 ? 27.076  -4.960  -52.773 1.00 13.01 ?  239 THR B CG2 1 
ATOM   5021 N  N   . LEU B 1 238 ? 29.612  -2.099  -55.166 1.00 11.11 ?  240 LEU B N   1 
ATOM   5022 C  CA  . LEU B 1 238 ? 30.657  -1.524  -56.004 1.00 12.88 ?  240 LEU B CA  1 
ATOM   5023 C  C   . LEU B 1 238 ? 32.027  -1.897  -55.438 1.00 16.45 ?  240 LEU B C   1 
ATOM   5024 O  O   . LEU B 1 238 ? 32.228  -1.868  -54.217 1.00 17.39 ?  240 LEU B O   1 
ATOM   5025 C  CB  . LEU B 1 238 ? 30.534  -0.005  -56.041 1.00 11.00 ?  240 LEU B CB  1 
ATOM   5026 C  CG  . LEU B 1 238 ? 29.281  0.564   -56.707 1.00 13.90 ?  240 LEU B CG  1 
ATOM   5027 C  CD1 . LEU B 1 238 ? 29.292  2.069   -56.535 1.00 15.14 ?  240 LEU B CD1 1 
ATOM   5028 C  CD2 . LEU B 1 238 ? 29.249  0.157   -58.193 1.00 18.69 ?  240 LEU B CD2 1 
ATOM   5029 N  N   . ASP B 1 239 ? 32.988  -2.218  -56.301 1.00 11.57 ?  241 ASP B N   1 
ATOM   5030 C  CA  . ASP B 1 239 ? 34.329  -2.425  -55.762 1.00 13.83 ?  241 ASP B CA  1 
ATOM   5031 C  C   . ASP B 1 239 ? 35.051  -1.085  -55.662 1.00 14.34 ?  241 ASP B C   1 
ATOM   5032 O  O   . ASP B 1 239 ? 34.463  -0.017  -55.856 1.00 14.44 ?  241 ASP B O   1 
ATOM   5033 C  CB  . ASP B 1 239 ? 35.119  -3.461  -56.565 1.00 14.46 ?  241 ASP B CB  1 
ATOM   5034 C  CG  . ASP B 1 239 ? 35.414  -3.041  -57.995 1.00 13.96 ?  241 ASP B CG  1 
ATOM   5035 O  OD1 . ASP B 1 239 ? 35.270  -1.860  -58.369 1.00 15.00 ?  241 ASP B OD1 1 
ATOM   5036 O  OD2 . ASP B 1 239 ? 35.826  -3.940  -58.762 1.00 17.24 ?  241 ASP B OD2 1 
ATOM   5037 N  N   . GLY B 1 240 ? 36.350  -1.136  -55.344 1.00 14.54 ?  242 GLY B N   1 
ATOM   5038 C  CA  . GLY B 1 240 ? 37.103  0.092   -55.139 1.00 17.39 ?  242 GLY B CA  1 
ATOM   5039 C  C   . GLY B 1 240 ? 37.184  0.965   -56.375 1.00 20.26 ?  242 GLY B C   1 
ATOM   5040 O  O   . GLY B 1 240 ? 37.299  2.188   -56.273 1.00 17.66 ?  242 GLY B O   1 
ATOM   5041 N  N   . ALA B 1 241 ? 37.126  0.359   -57.556 1.00 14.69 ?  243 ALA B N   1 
ATOM   5042 C  CA  . ALA B 1 241 ? 37.165  1.103   -58.802 1.00 14.02 ?  243 ALA B CA  1 
ATOM   5043 C  C   . ALA B 1 241 ? 35.767  1.470   -59.307 1.00 17.32 ?  243 ALA B C   1 
ATOM   5044 O  O   . ALA B 1 241 ? 35.615  1.857   -60.474 1.00 17.03 ?  243 ALA B O   1 
ATOM   5045 C  CB  . ALA B 1 241 ? 37.938  0.303   -59.860 1.00 16.94 ?  243 ALA B CB  1 
ATOM   5046 N  N   . ARG B 1 242 ? 34.752  1.373   -58.441 1.00 14.34 ?  244 ARG B N   1 
ATOM   5047 C  CA  . ARG B 1 242 ? 33.374  1.739   -58.751 1.00 14.27 ?  244 ARG B CA  1 
ATOM   5048 C  C   . ARG B 1 242 ? 32.764  0.838   -59.822 1.00 16.32 ?  244 ARG B C   1 
ATOM   5049 O  O   . ARG B 1 242 ? 31.866  1.256   -60.560 1.00 19.46 ?  244 ARG B O   1 
ATOM   5050 C  CB  . ARG B 1 242 ? 33.249  3.212   -59.160 1.00 20.06 ?  244 ARG B CB  1 
ATOM   5051 C  CG  . ARG B 1 242 ? 33.880  4.159   -58.151 1.00 17.93 ?  244 ARG B CG  1 
ATOM   5052 C  CD  . ARG B 1 242 ? 32.992  4.292   -56.920 1.00 17.95 ?  244 ARG B CD  1 
ATOM   5053 N  NE  . ARG B 1 242 ? 33.658  5.080   -55.889 1.00 19.22 ?  244 ARG B NE  1 
ATOM   5054 C  CZ  . ARG B 1 242 ? 33.622  6.406   -55.816 1.00 17.25 ?  244 ARG B CZ  1 
ATOM   5055 N  NH1 . ARG B 1 242 ? 32.927  7.102   -56.703 1.00 12.88 ?  244 ARG B NH1 1 
ATOM   5056 N  NH2 . ARG B 1 242 ? 34.286  7.036   -54.854 1.00 14.93 ?  244 ARG B NH2 1 
ATOM   5057 N  N   . ARG B 1 243 ? 33.217  -0.405  -59.908 1.00 13.27 ?  245 ARG B N   1 
ATOM   5058 C  CA  . ARG B 1 243 ? 32.571  -1.377  -60.781 1.00 13.23 ?  245 ARG B CA  1 
ATOM   5059 C  C   . ARG B 1 243 ? 31.571  -2.211  -59.991 1.00 12.25 ?  245 ARG B C   1 
ATOM   5060 O  O   . ARG B 1 243 ? 31.821  -2.583  -58.842 1.00 12.86 ?  245 ARG B O   1 
ATOM   5061 C  CB  . ARG B 1 243 ? 33.624  -2.265  -61.435 1.00 15.41 ?  245 ARG B CB  1 
ATOM   5062 C  CG  . ARG B 1 243 ? 34.604  -1.388  -62.173 1.00 19.93 ?  245 ARG B CG  1 
ATOM   5063 C  CD  . ARG B 1 243 ? 35.819  -2.101  -62.591 1.00 23.79 ?  245 ARG B CD  1 
ATOM   5064 N  NE  . ARG B 1 243 ? 36.476  -2.777  -61.481 1.00 17.67 ?  245 ARG B NE  1 
ATOM   5065 C  CZ  . ARG B 1 243 ? 37.596  -3.468  -61.644 1.00 16.89 ?  245 ARG B CZ  1 
ATOM   5066 N  NH1 . ARG B 1 243 ? 38.145  -3.512  -62.854 1.00 17.17 ?  245 ARG B NH1 1 
ATOM   5067 N  NH2 . ARG B 1 243 ? 38.155  -4.107  -60.626 1.00 17.77 ?  245 ARG B NH2 1 
ATOM   5068 N  N   . ILE B 1 244 ? 30.448  -2.529  -60.631 1.00 12.56 ?  246 ILE B N   1 
ATOM   5069 C  CA  . ILE B 1 244 ? 29.407  -3.314  -59.979 1.00 12.92 ?  246 ILE B CA  1 
ATOM   5070 C  C   . ILE B 1 244 ? 29.883  -4.749  -59.807 1.00 12.61 ?  246 ILE B C   1 
ATOM   5071 O  O   . ILE B 1 244 ? 30.270  -5.411  -60.776 1.00 14.06 ?  246 ILE B O   1 
ATOM   5072 C  CB  . ILE B 1 244 ? 28.106  -3.254  -60.792 1.00 10.34 ?  246 ILE B CB  1 
ATOM   5073 C  CG1 . ILE B 1 244 ? 27.564  -1.825  -60.805 1.00 14.18 ?  246 ILE B CG1 1 
ATOM   5074 C  CG2 . ILE B 1 244 ? 27.087  -4.237  -60.235 1.00 11.31 ?  246 ILE B CG2 1 
ATOM   5075 C  CD1 . ILE B 1 244 ? 26.264  -1.679  -61.576 1.00 14.29 ?  246 ILE B CD1 1 
ATOM   5076 N  N   . THR B 1 245 ? 29.845  -5.244  -58.566 1.00 11.08 ?  247 THR B N   1 
ATOM   5077 C  CA  . THR B 1 245 ? 30.215  -6.619  -58.290 1.00 12.16 ?  247 THR B CA  1 
ATOM   5078 C  C   . THR B 1 245 ? 29.019  -7.511  -57.966 1.00 13.97 ?  247 THR B C   1 
ATOM   5079 O  O   . THR B 1 245 ? 29.188  -8.733  -57.873 1.00 14.91 ?  247 THR B O   1 
ATOM   5080 C  CB  . THR B 1 245 ? 31.220  -6.671  -57.132 1.00 17.13 ?  247 THR B CB  1 
ATOM   5081 O  OG1 . THR B 1 245 ? 30.731  -5.864  -56.057 1.00 14.07 ?  247 THR B OG1 1 
ATOM   5082 C  CG2 . THR B 1 245 ? 32.550  -6.080  -57.594 1.00 13.67 ?  247 THR B CG2 1 
ATOM   5083 N  N   . SER B 1 246 ? 27.820  -6.944  -57.804 1.00 14.52 ?  248 SER B N   1 
ATOM   5084 C  CA  . SER B 1 246 ? 26.641  -7.775  -57.603 1.00 15.29 ?  248 SER B CA  1 
ATOM   5085 C  C   . SER B 1 246 ? 25.402  -6.927  -57.816 1.00 14.76 ?  248 SER B C   1 
ATOM   5086 O  O   . SER B 1 246 ? 25.435  -5.700  -57.655 1.00 11.41 ?  248 SER B O   1 
ATOM   5087 C  CB  . SER B 1 246 ? 26.623  -8.427  -56.207 1.00 15.73 ?  248 SER B CB  1 
ATOM   5088 O  OG  . SER B 1 246 ? 26.152  -7.531  -55.211 1.00 15.98 ?  248 SER B OG  1 
ATOM   5089 N  N   . VAL B 1 247 ? 24.319  -7.597  -58.217 1.00 12.08 ?  249 VAL B N   1 
ATOM   5090 C  CA  . VAL B 1 247 ? 22.999  -6.987  -58.345 1.00 14.43 ?  249 VAL B CA  1 
ATOM   5091 C  C   . VAL B 1 247 ? 22.033  -7.855  -57.559 1.00 13.87 ?  249 VAL B C   1 
ATOM   5092 O  O   . VAL B 1 247 ? 21.954  -9.066  -57.802 1.00 16.26 ?  249 VAL B O   1 
ATOM   5093 C  CB  . VAL B 1 247 ? 22.529  -6.890  -59.808 1.00 15.32 ?  249 VAL B CB  1 
ATOM   5094 C  CG1 . VAL B 1 247 ? 21.088  -6.398  -59.863 1.00 14.70 ?  249 VAL B CG1 1 
ATOM   5095 C  CG2 . VAL B 1 247 ? 23.459  -6.018  -60.642 1.00 16.05 ?  249 VAL B CG2 1 
ATOM   5096 N  N   . VAL B 1 248 ? 21.303  -7.253  -56.622 1.00 14.35 ?  250 VAL B N   1 
ATOM   5097 C  CA  . VAL B 1 248 ? 20.205  -7.936  -55.943 1.00 16.52 ?  250 VAL B CA  1 
ATOM   5098 C  C   . VAL B 1 248 ? 18.901  -7.219  -56.271 1.00 16.76 ?  250 VAL B C   1 
ATOM   5099 O  O   . VAL B 1 248 ? 18.803  -5.990  -56.156 1.00 19.00 ?  250 VAL B O   1 
ATOM   5100 C  CB  . VAL B 1 248 ? 20.427  -8.034  -54.422 1.00 16.21 ?  250 VAL B CB  1 
ATOM   5101 C  CG1 . VAL B 1 248 ? 21.638  -8.905  -54.128 1.00 15.58 ?  250 VAL B CG1 1 
ATOM   5102 C  CG2 . VAL B 1 248 ? 20.629  -6.657  -53.812 1.00 19.69 ?  250 VAL B CG2 1 
ATOM   5103 N  N   . ALA B 1 249 ? 17.904  -7.985  -56.697 1.00 16.85 ?  251 ALA B N   1 
ATOM   5104 C  CA  . ALA B 1 249 ? 16.602  -7.427  -57.021 1.00 16.73 ?  251 ALA B CA  1 
ATOM   5105 C  C   . ALA B 1 249 ? 15.534  -8.294  -56.382 1.00 14.98 ?  251 ALA B C   1 
ATOM   5106 O  O   . ALA B 1 249 ? 15.722  -9.502  -56.210 1.00 17.68 ?  251 ALA B O   1 
ATOM   5107 C  CB  . ALA B 1 249 ? 16.371  -7.343  -58.535 1.00 17.00 ?  251 ALA B CB  1 
ATOM   5108 N  N   . GLY B 1 250 ? 14.425  -7.661  -56.002 1.00 17.41 ?  252 GLY B N   1 
ATOM   5109 C  CA  . GLY B 1 250 ? 13.329  -8.421  -55.432 1.00 17.59 ?  252 GLY B CA  1 
ATOM   5110 C  C   . GLY B 1 250 ? 12.803  -7.860  -54.131 1.00 15.67 ?  252 GLY B C   1 
ATOM   5111 O  O   . GLY B 1 250 ? 12.654  -6.643  -53.993 1.00 18.39 ?  252 GLY B O   1 
ATOM   5112 N  N   . ASP B 1 251 ? 12.533  -8.748  -53.173 1.00 17.25 ?  253 ASP B N   1 
ATOM   5113 C  CA  . ASP B 1 251 ? 11.925  -8.355  -51.907 1.00 20.46 ?  253 ASP B CA  1 
ATOM   5114 C  C   . ASP B 1 251 ? 12.804  -7.352  -51.161 1.00 18.78 ?  253 ASP B C   1 
ATOM   5115 O  O   . ASP B 1 251 ? 14.029  -7.466  -51.150 1.00 19.06 ?  253 ASP B O   1 
ATOM   5116 C  CB  . ASP B 1 251 ? 11.686  -9.590  -51.046 1.00 23.29 ?  253 ASP B CB  1 
ATOM   5117 C  CG  . ASP B 1 251 ? 11.023  -9.254  -49.740 1.00 25.35 ?  253 ASP B CG  1 
ATOM   5118 O  OD1 . ASP B 1 251 ? 9.813   -8.940  -49.753 1.00 27.55 ?  253 ASP B OD1 1 
ATOM   5119 O  OD2 . ASP B 1 251 ? 11.726  -9.276  -48.709 1.00 22.27 ?  253 ASP B OD2 1 
ATOM   5120 N  N   . MET B 1 252 ? 12.170  -6.350  -50.544 1.00 20.01 ?  254 MET B N   1 
ATOM   5121 C  CA  . MET B 1 252 ? 12.942  -5.266  -49.936 1.00 21.43 ?  254 MET B CA  1 
ATOM   5122 C  C   . MET B 1 252 ? 13.875  -5.792  -48.850 1.00 22.27 ?  254 MET B C   1 
ATOM   5123 O  O   . MET B 1 252 ? 15.007  -5.313  -48.708 1.00 18.72 ?  254 MET B O   1 
ATOM   5124 C  CB  . MET B 1 252 ? 12.008  -4.198  -49.363 1.00 22.79 ?  254 MET B CB  1 
ATOM   5125 C  CG  . MET B 1 252 ? 12.752  -3.084  -48.646 1.00 19.01 ?  254 MET B CG  1 
ATOM   5126 S  SD  . MET B 1 252 ? 11.688  -2.048  -47.630 1.00 21.83 ?  254 MET B SD  1 
ATOM   5127 C  CE  . MET B 1 252 ? 11.668  -3.016  -46.137 1.00 20.48 ?  254 MET B CE  1 
ATOM   5128 N  N   . GLU B 1 253 ? 13.429  -6.778  -48.075 1.00 18.08 ?  255 GLU B N   1 
ATOM   5129 C  CA  . GLU B 1 253 ? 14.316  -7.341  -47.065 1.00 20.22 ?  255 GLU B CA  1 
ATOM   5130 C  C   . GLU B 1 253 ? 15.181  -8.480  -47.600 1.00 19.42 ?  255 GLU B C   1 
ATOM   5131 O  O   . GLU B 1 253 ? 16.387  -8.509  -47.342 1.00 20.99 ?  255 GLU B O   1 
ATOM   5132 C  CB  . GLU B 1 253 ? 13.500  -7.799  -45.858 1.00 22.07 ?  255 GLU B CB  1 
ATOM   5133 C  CG  . GLU B 1 253 ? 12.789  -6.649  -45.160 1.00 23.35 ?  255 GLU B CG  1 
ATOM   5134 C  CD  . GLU B 1 253 ? 12.012  -7.102  -43.941 1.00 27.56 ?  255 GLU B CD  1 
ATOM   5135 O  OE1 . GLU B 1 253 ? 12.632  -7.555  -42.964 1.00 30.46 ?  255 GLU B OE1 1 
ATOM   5136 O  OE2 . GLU B 1 253 ? 10.772  -6.999  -43.962 1.00 33.28 ?  255 GLU B OE2 1 
ATOM   5137 N  N   . GLN B 1 254 ? 14.595  -9.422  -48.347 1.00 18.80 ?  256 GLN B N   1 
ATOM   5138 C  CA  . GLN B 1 254 ? 15.348  -10.603 -48.778 1.00 18.73 ?  256 GLN B CA  1 
ATOM   5139 C  C   . GLN B 1 254 ? 16.480  -10.235 -49.733 1.00 16.78 ?  256 GLN B C   1 
ATOM   5140 O  O   . GLN B 1 254 ? 17.611  -10.716 -49.588 1.00 19.28 ?  256 GLN B O   1 
ATOM   5141 C  CB  . GLN B 1 254 ? 14.399  -11.599 -49.436 1.00 22.08 ?  256 GLN B CB  1 
ATOM   5142 C  CG  . GLN B 1 254 ? 13.623  -12.454 -48.459 1.00 25.98 ?  256 GLN B CG  1 
ATOM   5143 C  CD  . GLN B 1 254 ? 12.925  -13.597 -49.174 1.00 33.40 ?  256 GLN B CD  1 
ATOM   5144 O  OE1 . GLN B 1 254 ? 13.566  -14.522 -49.673 1.00 36.47 ?  256 GLN B OE1 1 
ATOM   5145 N  NE2 . GLN B 1 254 ? 11.597  -13.520 -49.249 1.00 38.59 ?  256 GLN B NE2 1 
ATOM   5146 N  N   . ALA B 1 255 ? 16.193  -9.393  -50.723 1.00 17.05 ?  257 ALA B N   1 
ATOM   5147 C  CA  . ALA B 1 255 ? 17.239  -9.001  -51.658 1.00 17.53 ?  257 ALA B CA  1 
ATOM   5148 C  C   . ALA B 1 255 ? 18.320  -8.184  -50.958 1.00 17.32 ?  257 ALA B C   1 
ATOM   5149 O  O   . ALA B 1 255 ? 19.516  -8.382  -51.209 1.00 18.35 ?  257 ALA B O   1 
ATOM   5150 C  CB  . ALA B 1 255 ? 16.639  -8.220  -52.826 1.00 16.54 ?  257 ALA B CB  1 
ATOM   5151 N  N   . PHE B 1 256 ? 17.917  -7.274  -50.066 1.00 15.20 ?  258 PHE B N   1 
ATOM   5152 C  CA  . PHE B 1 256 ? 18.889  -6.476  -49.325 1.00 16.44 ?  258 PHE B CA  1 
ATOM   5153 C  C   . PHE B 1 256 ? 19.800  -7.375  -48.495 1.00 16.56 ?  258 PHE B C   1 
ATOM   5154 O  O   . PHE B 1 256 ? 21.029  -7.232  -48.514 1.00 15.53 ?  258 PHE B O   1 
ATOM   5155 C  CB  . PHE B 1 256 ? 18.155  -5.455  -48.444 1.00 17.00 ?  258 PHE B CB  1 
ATOM   5156 C  CG  . PHE B 1 256 ? 19.043  -4.750  -47.442 1.00 14.82 ?  258 PHE B CG  1 
ATOM   5157 C  CD1 . PHE B 1 256 ? 20.015  -3.846  -47.877 1.00 13.92 ?  258 PHE B CD1 1 
ATOM   5158 C  CD2 . PHE B 1 256 ? 18.895  -4.968  -46.075 1.00 14.01 ?  258 PHE B CD2 1 
ATOM   5159 C  CE1 . PHE B 1 256 ? 20.844  -3.195  -46.966 1.00 14.73 ?  258 PHE B CE1 1 
ATOM   5160 C  CE2 . PHE B 1 256 ? 19.730  -4.317  -45.151 1.00 17.73 ?  258 PHE B CE2 1 
ATOM   5161 C  CZ  . PHE B 1 256 ? 20.703  -3.428  -45.605 1.00 14.76 ?  258 PHE B CZ  1 
ATOM   5162 N  N   . LEU B 1 257 ? 19.214  -8.330  -47.773 1.00 14.68 ?  259 LEU B N   1 
ATOM   5163 C  CA  . LEU B 1 257 ? 20.026  -9.185  -46.921 1.00 14.68 ?  259 LEU B CA  1 
ATOM   5164 C  C   . LEU B 1 257 ? 20.930  -10.062 -47.754 1.00 19.56 ?  259 LEU B C   1 
ATOM   5165 O  O   . LEU B 1 257 ? 22.002  -10.464 -47.306 1.00 18.38 ?  259 LEU B O   1 
ATOM   5166 C  CB  . LEU B 1 257 ? 19.126  -10.034 -46.026 1.00 20.17 ?  259 LEU B CB  1 
ATOM   5167 C  CG  . LEU B 1 257 ? 18.372  -9.213  -44.976 1.00 22.81 ?  259 LEU B CG  1 
ATOM   5168 C  CD1 . LEU B 1 257 ? 17.456  -10.108 -44.162 1.00 23.19 ?  259 LEU B CD1 1 
ATOM   5169 C  CD2 . LEU B 1 257 ? 19.342  -8.490  -44.064 1.00 18.61 ?  259 LEU B CD2 1 
ATOM   5170 N  N   . LYS B 1 258 ? 20.519  -10.344 -48.977 1.00 18.17 ?  260 LYS B N   1 
ATOM   5171 C  CA  . LYS B 1 258 ? 21.335  -11.183 -49.833 1.00 15.90 ?  260 LYS B CA  1 
ATOM   5172 C  C   . LYS B 1 258 ? 22.561  -10.380 -50.281 1.00 14.87 ?  260 LYS B C   1 
ATOM   5173 O  O   . LYS B 1 258 ? 23.693  -10.896 -50.363 1.00 14.36 ?  260 LYS B O   1 
ATOM   5174 C  CB  . LYS B 1 258 ? 20.512  -11.573 -51.061 1.00 19.89 ?  260 LYS B CB  1 
ATOM   5175 C  CG  . LYS B 1 258 ? 21.213  -12.507 -51.988 1.00 24.96 ?  260 LYS B CG  1 
ATOM   5176 C  CD  . LYS B 1 258 ? 21.355  -13.722 -51.130 1.00 39.50 ?  260 LYS B CD  1 
ATOM   5177 C  CE  . LYS B 1 258 ? 19.937  -14.309 -50.935 1.00 37.29 ?  260 LYS B CE  1 
ATOM   5178 N  NZ  . LYS B 1 258 ? 19.749  -15.571 -50.162 1.00 44.55 ?  260 LYS B NZ  1 
ATOM   5179 N  N   . GLY B 1 259 ? 22.328  -9.117  -50.634 1.00 14.32 ?  261 GLY B N   1 
ATOM   5180 C  CA  . GLY B 1 259 ? 23.426  -8.246  -51.004 1.00 12.37 ?  261 GLY B CA  1 
ATOM   5181 C  C   . GLY B 1 259 ? 24.375  -7.983  -49.851 1.00 15.73 ?  261 GLY B C   1 
ATOM   5182 O  O   . GLY B 1 259 ? 25.585  -7.858  -50.053 1.00 14.96 ?  261 GLY B O   1 
ATOM   5183 N  N   . VAL B 1 260 ? 23.839  -7.880  -48.629 1.00 12.05 ?  262 VAL B N   1 
ATOM   5184 C  CA  . VAL B 1 260 ? 24.693  -7.668  -47.460 1.00 13.36 ?  262 VAL B CA  1 
ATOM   5185 C  C   . VAL B 1 260 ? 25.528  -8.908  -47.189 1.00 15.54 ?  262 VAL B C   1 
ATOM   5186 O  O   . VAL B 1 260 ? 26.711  -8.813  -46.837 1.00 17.00 ?  262 VAL B O   1 
ATOM   5187 C  CB  . VAL B 1 260 ? 23.849  -7.281  -46.228 1.00 14.34 ?  262 VAL B CB  1 
ATOM   5188 C  CG1 . VAL B 1 260 ? 24.691  -7.387  -44.950 1.00 17.84 ?  262 VAL B CG1 1 
ATOM   5189 C  CG2 . VAL B 1 260 ? 23.268  -5.880  -46.392 1.00 13.14 ?  262 VAL B CG2 1 
ATOM   5190 N  N   . ALA B 1 261 ? 24.919  -10.091 -47.336 1.00 16.10 ?  263 ALA B N   1 
ATOM   5191 C  CA  . ALA B 1 261 ? 25.673  -11.331 -47.204 1.00 16.88 ?  263 ALA B CA  1 
ATOM   5192 C  C   . ALA B 1 261 ? 26.848  -11.351 -48.168 1.00 16.79 ?  263 ALA B C   1 
ATOM   5193 O  O   . ALA B 1 261 ? 27.944  -11.792 -47.812 1.00 19.42 ?  263 ALA B O   1 
ATOM   5194 C  CB  . ALA B 1 261 ? 24.755  -12.533 -47.448 1.00 20.08 ?  263 ALA B CB  1 
ATOM   5195 N  N   . PHE B 1 262 ? 26.648  -10.863 -49.394 1.00 15.66 ?  264 PHE B N   1 
ATOM   5196 C  CA  . PHE B 1 262 ? 27.775  -10.799 -50.315 1.00 16.62 ?  264 PHE B CA  1 
ATOM   5197 C  C   . PHE B 1 262 ? 28.784  -9.741  -49.879 1.00 15.55 ?  264 PHE B C   1 
ATOM   5198 O  O   . PHE B 1 262 ? 29.990  -10.007 -49.830 1.00 16.42 ?  264 PHE B O   1 
ATOM   5199 C  CB  . PHE B 1 262 ? 27.312  -10.510 -51.743 1.00 16.29 ?  264 PHE B CB  1 
ATOM   5200 C  CG  . PHE B 1 262 ? 28.461  -10.254 -52.678 1.00 14.60 ?  264 PHE B CG  1 
ATOM   5201 C  CD1 . PHE B 1 262 ? 29.326  -11.283 -53.026 1.00 18.63 ?  264 PHE B CD1 1 
ATOM   5202 C  CD2 . PHE B 1 262 ? 28.722  -8.981  -53.138 1.00 16.14 ?  264 PHE B CD2 1 
ATOM   5203 C  CE1 . PHE B 1 262 ? 30.418  -11.053 -53.864 1.00 16.79 ?  264 PHE B CE1 1 
ATOM   5204 C  CE2 . PHE B 1 262 ? 29.804  -8.740  -53.972 1.00 17.15 ?  264 PHE B CE2 1 
ATOM   5205 C  CZ  . PHE B 1 262 ? 30.656  -9.780  -54.334 1.00 17.38 ?  264 PHE B CZ  1 
ATOM   5206 N  N   . VAL B 1 263 ? 28.315  -8.532  -49.555 1.00 16.28 ?  265 VAL B N   1 
ATOM   5207 C  CA  . VAL B 1 263 ? 29.288  -7.460  -49.383 1.00 15.81 ?  265 VAL B CA  1 
ATOM   5208 C  C   . VAL B 1 263 ? 30.100  -7.705  -48.113 1.00 18.46 ?  265 VAL B C   1 
ATOM   5209 O  O   . VAL B 1 263 ? 31.266  -7.300  -48.032 1.00 17.26 ?  265 VAL B O   1 
ATOM   5210 C  CB  . VAL B 1 263 ? 28.610  -6.075  -49.370 1.00 18.26 ?  265 VAL B CB  1 
ATOM   5211 C  CG1 . VAL B 1 263 ? 27.888  -5.806  -48.054 1.00 18.09 ?  265 VAL B CG1 1 
ATOM   5212 C  CG2 . VAL B 1 263 ? 29.580  -4.976  -49.791 1.00 18.25 ?  265 VAL B CG2 1 
ATOM   5213 N  N   . GLU B 1 264 ? 29.521  -8.410  -47.126 1.00 16.30 ?  266 GLU B N   1 
ATOM   5214 C  CA  . GLU B 1 264 ? 30.274  -8.800  -45.930 1.00 18.67 ?  266 GLU B CA  1 
ATOM   5215 C  C   . GLU B 1 264 ? 31.486  -9.653  -46.267 1.00 24.21 ?  266 GLU B C   1 
ATOM   5216 O  O   . GLU B 1 264 ? 32.481  -9.622  -45.538 1.00 27.51 ?  266 GLU B O   1 
ATOM   5217 C  CB  . GLU B 1 264 ? 29.401  -9.583  -44.944 1.00 20.14 ?  266 GLU B CB  1 
ATOM   5218 C  CG  . GLU B 1 264 ? 28.395  -8.767  -44.191 1.00 27.35 ?  266 GLU B CG  1 
ATOM   5219 C  CD  . GLU B 1 264 ? 27.580  -9.623  -43.239 1.00 31.42 ?  266 GLU B CD  1 
ATOM   5220 O  OE1 . GLU B 1 264 ? 27.243  -9.130  -42.141 1.00 30.83 ?  266 GLU B OE1 1 
ATOM   5221 O  OE2 . GLU B 1 264 ? 27.296  -10.795 -43.585 1.00 30.69 ?  266 GLU B OE2 1 
ATOM   5222 N  N   . THR B 1 265 ? 31.423  -10.427 -47.348 1.00 20.90 ?  267 THR B N   1 
ATOM   5223 C  CA  . THR B 1 265 ? 32.564  -11.244 -47.739 1.00 23.24 ?  267 THR B CA  1 
ATOM   5224 C  C   . THR B 1 265 ? 33.672  -10.447 -48.408 1.00 21.05 ?  267 THR B C   1 
ATOM   5225 O  O   . THR B 1 265 ? 34.773  -10.985 -48.592 1.00 25.36 ?  267 THR B O   1 
ATOM   5226 C  CB  . THR B 1 265 ? 32.119  -12.372 -48.669 1.00 22.26 ?  267 THR B CB  1 
ATOM   5227 O  OG1 . THR B 1 265 ? 31.890  -11.844 -49.979 1.00 22.95 ?  267 THR B OG1 1 
ATOM   5228 C  CG2 . THR B 1 265 ? 30.848  -13.029 -48.147 1.00 28.81 ?  267 THR B CG2 1 
ATOM   5229 N  N   . VAL B 1 266 ? 33.434  -9.194  -48.781 1.00 20.59 ?  268 VAL B N   1 
ATOM   5230 C  CA  . VAL B 1 266 ? 34.490  -8.461  -49.470 1.00 18.49 ?  268 VAL B CA  1 
ATOM   5231 C  C   . VAL B 1 266 ? 34.957  -7.225  -48.706 1.00 18.60 ?  268 VAL B C   1 
ATOM   5232 O  O   . VAL B 1 266 ? 36.119  -6.840  -48.841 1.00 16.26 ?  268 VAL B O   1 
ATOM   5233 C  CB  . VAL B 1 266 ? 34.078  -8.079  -50.907 1.00 21.59 ?  268 VAL B CB  1 
ATOM   5234 C  CG1 . VAL B 1 266 ? 33.803  -9.331  -51.729 1.00 26.74 ?  268 VAL B CG1 1 
ATOM   5235 C  CG2 . VAL B 1 266 ? 32.878  -7.172  -50.914 1.00 19.64 ?  268 VAL B CG2 1 
ATOM   5236 N  N   . VAL B 1 267 ? 34.093  -6.601  -47.894 1.00 16.04 ?  269 VAL B N   1 
ATOM   5237 C  CA  . VAL B 1 267 ? 34.476  -5.304  -47.317 1.00 16.51 ?  269 VAL B CA  1 
ATOM   5238 C  C   . VAL B 1 267 ? 35.302  -5.416  -46.045 1.00 15.56 ?  269 VAL B C   1 
ATOM   5239 O  O   . VAL B 1 267 ? 35.969  -4.445  -45.680 1.00 14.54 ?  269 VAL B O   1 
ATOM   5240 C  CB  . VAL B 1 267 ? 33.291  -4.382  -46.976 1.00 19.32 ?  269 VAL B CB  1 
ATOM   5241 C  CG1 . VAL B 1 267 ? 32.565  -3.962  -48.246 1.00 24.82 ?  269 VAL B CG1 1 
ATOM   5242 C  CG2 . VAL B 1 267 ? 32.362  -5.050  -45.972 1.00 16.84 ?  269 VAL B CG2 1 
ATOM   5243 N  N   . LYS B 1 268 ? 35.279  -6.552  -45.351 1.00 12.24 ?  270 LYS B N   1 
ATOM   5244 C  CA  . LYS B 1 268 ? 36.051  -6.673  -44.125 1.00 13.65 ?  270 LYS B CA  1 
ATOM   5245 C  C   . LYS B 1 268 ? 37.542  -6.821  -44.433 1.00 18.42 ?  270 LYS B C   1 
ATOM   5246 O  O   . LYS B 1 268 ? 37.945  -7.624  -45.285 1.00 19.24 ?  270 LYS B O   1 
ATOM   5247 C  CB  . LYS B 1 268 ? 35.535  -7.858  -43.303 1.00 16.14 ?  270 LYS B CB  1 
ATOM   5248 N  N   . ALA B 1 269 ? 38.363  -6.033  -43.744 1.00 16.32 ?  271 ALA B N   1 
ATOM   5249 C  CA  . ALA B 1 269 ? 39.810  -6.060  -43.910 1.00 14.69 ?  271 ALA B CA  1 
ATOM   5250 C  C   . ALA B 1 269 ? 40.428  -5.990  -42.520 1.00 18.31 ?  271 ALA B C   1 
ATOM   5251 O  O   . ALA B 1 269 ? 40.051  -5.130  -41.725 1.00 16.36 ?  271 ALA B O   1 
ATOM   5252 C  CB  . ALA B 1 269 ? 40.295  -4.893  -44.786 1.00 16.04 ?  271 ALA B CB  1 
ATOM   5253 N  N   . ALA B 1 270 ? 41.360  -6.889  -42.222 1.00 19.27 ?  272 ALA B N   1 
ATOM   5254 C  CA  . ALA B 1 270 ? 41.769  -7.132  -40.845 1.00 19.49 ?  272 ALA B CA  1 
ATOM   5255 C  C   . ALA B 1 270 ? 43.196  -6.679  -40.569 1.00 23.51 ?  272 ALA B C   1 
ATOM   5256 O  O   . ALA B 1 270 ? 44.065  -6.694  -41.449 1.00 22.35 ?  272 ALA B O   1 
ATOM   5257 C  CB  . ALA B 1 270 ? 41.645  -8.617  -40.489 1.00 18.68 ?  272 ALA B CB  1 
ATOM   5258 N  N   . VAL B 1 271 ? 43.417  -6.279  -39.323 1.00 18.05 ?  273 VAL B N   1 
ATOM   5259 C  CA  . VAL B 1 271 ? 44.756  -6.053  -38.785 1.00 13.50 ?  273 VAL B CA  1 
ATOM   5260 C  C   . VAL B 1 271 ? 44.913  -6.985  -37.593 1.00 14.20 ?  273 VAL B C   1 
ATOM   5261 O  O   . VAL B 1 271 ? 43.916  -7.418  -36.994 1.00 19.65 ?  273 VAL B O   1 
ATOM   5262 C  CB  . VAL B 1 271 ? 44.974  -4.576  -38.379 1.00 15.76 ?  273 VAL B CB  1 
ATOM   5263 C  CG1 . VAL B 1 271 ? 44.958  -3.658  -39.615 1.00 18.57 ?  273 VAL B CG1 1 
ATOM   5264 C  CG2 . VAL B 1 271 ? 43.936  -4.139  -37.342 1.00 15.26 ?  273 VAL B CG2 1 
ATOM   5265 N  N   . PRO B 1 272 ? 46.154  -7.308  -37.210 1.00 20.76 ?  274 PRO B N   1 
ATOM   5266 C  CA  . PRO B 1 272 ? 46.348  -8.202  -36.056 1.00 22.21 ?  274 PRO B CA  1 
ATOM   5267 C  C   . PRO B 1 272 ? 45.983  -7.558  -34.734 1.00 22.71 ?  274 PRO B C   1 
ATOM   5268 O  O   . PRO B 1 272 ? 45.547  -8.253  -33.808 1.00 27.03 ?  274 PRO B O   1 
ATOM   5269 C  CB  . PRO B 1 272 ? 47.849  -8.535  -36.124 1.00 19.68 ?  274 PRO B CB  1 
ATOM   5270 C  CG  . PRO B 1 272 ? 48.260  -8.172  -37.497 1.00 25.42 ?  274 PRO B CG  1 
ATOM   5271 C  CD  . PRO B 1 272 ? 47.437  -6.967  -37.831 1.00 20.29 ?  274 PRO B CD  1 
ATOM   5272 N  N   . ALA B 1 273 ? 46.124  -6.242  -34.625 1.00 18.57 ?  275 ALA B N   1 
ATOM   5273 C  CA  . ALA B 1 273 ? 45.976  -5.543  -33.358 1.00 17.80 ?  275 ALA B CA  1 
ATOM   5274 C  C   . ALA B 1 273 ? 45.689  -4.091  -33.682 1.00 16.76 ?  275 ALA B C   1 
ATOM   5275 O  O   . ALA B 1 273 ? 46.108  -3.618  -34.743 1.00 18.26 ?  275 ALA B O   1 
ATOM   5276 C  CB  . ALA B 1 273 ? 47.256  -5.671  -32.509 1.00 19.58 ?  275 ALA B CB  1 
ATOM   5277 N  N   . PRO B 1 274 ? 44.956  -3.373  -32.826 1.00 20.28 ?  276 PRO B N   1 
ATOM   5278 C  CA  . PRO B 1 274 ? 44.741  -1.944  -33.075 1.00 17.37 ?  276 PRO B CA  1 
ATOM   5279 C  C   . PRO B 1 274 ? 46.065  -1.213  -33.199 1.00 19.11 ?  276 PRO B C   1 
ATOM   5280 O  O   . PRO B 1 274 ? 47.067  -1.584  -32.579 1.00 15.27 ?  276 PRO B O   1 
ATOM   5281 C  CB  . PRO B 1 274 ? 43.942  -1.470  -31.854 1.00 16.45 ?  276 PRO B CB  1 
ATOM   5282 C  CG  . PRO B 1 274 ? 44.074  -2.543  -30.842 1.00 24.74 ?  276 PRO B CG  1 
ATOM   5283 C  CD  . PRO B 1 274 ? 44.317  -3.821  -31.578 1.00 23.34 ?  276 PRO B CD  1 
ATOM   5284 N  N   . VAL B 1 275 ? 46.063  -0.170  -34.027 1.00 15.96 ?  277 VAL B N   1 
ATOM   5285 C  CA  . VAL B 1 275 ? 47.279  0.552   -34.350 1.00 13.83 ?  277 VAL B CA  1 
ATOM   5286 C  C   . VAL B 1 275 ? 47.215  1.957   -33.769 1.00 13.99 ?  277 VAL B C   1 
ATOM   5287 O  O   . VAL B 1 275 ? 46.149  2.494   -33.452 1.00 11.65 ?  277 VAL B O   1 
ATOM   5288 C  CB  . VAL B 1 275 ? 47.541  0.611   -35.874 1.00 19.47 ?  277 VAL B CB  1 
ATOM   5289 C  CG1 . VAL B 1 275 ? 47.952  -0.774  -36.393 1.00 24.52 ?  277 VAL B CG1 1 
ATOM   5290 C  CG2 . VAL B 1 275 ? 46.315  1.130   -36.612 1.00 15.59 ?  277 VAL B CG2 1 
ATOM   5291 N  N   . ASP B 1 276 ? 48.404  2.555   -33.672 1.00 14.83 ?  278 ASP B N   1 
ATOM   5292 C  CA  . ASP B 1 276 ? 48.596  3.909   -33.167 1.00 15.22 ?  278 ASP B CA  1 
ATOM   5293 C  C   . ASP B 1 276 ? 48.078  4.956   -34.148 1.00 13.80 ?  278 ASP B C   1 
ATOM   5294 O  O   . ASP B 1 276 ? 47.562  6.002   -33.738 1.00 12.42 ?  278 ASP B O   1 
ATOM   5295 C  CB  . ASP B 1 276 ? 50.092  4.089   -32.953 1.00 20.24 ?  278 ASP B CB  1 
ATOM   5296 C  CG  . ASP B 1 276 ? 50.639  3.131   -31.926 1.00 24.66 ?  278 ASP B CG  1 
ATOM   5297 O  OD1 . ASP B 1 276 ? 50.211  3.166   -30.763 1.00 25.02 ?  278 ASP B OD1 1 
ATOM   5298 O  OD2 . ASP B 1 276 ? 51.317  2.179   -32.362 1.00 32.80 ?  278 ASP B OD2 1 
ATOM   5299 N  N   . VAL B 1 277 ? 48.247  4.715   -35.449 1.00 10.45 ?  279 VAL B N   1 
ATOM   5300 C  CA  . VAL B 1 277 ? 47.934  5.702   -36.478 1.00 9.66  ?  279 VAL B CA  1 
ATOM   5301 C  C   . VAL B 1 277 ? 47.153  5.020   -37.590 1.00 10.54 ?  279 VAL B C   1 
ATOM   5302 O  O   . VAL B 1 277 ? 47.628  4.034   -38.162 1.00 13.49 ?  279 VAL B O   1 
ATOM   5303 C  CB  . VAL B 1 277 ? 49.221  6.333   -37.041 1.00 11.64 ?  279 VAL B CB  1 
ATOM   5304 C  CG1 . VAL B 1 277 ? 48.884  7.393   -38.072 1.00 11.50 ?  279 VAL B CG1 1 
ATOM   5305 C  CG2 . VAL B 1 277 ? 50.082  6.904   -35.896 1.00 13.44 ?  279 VAL B CG2 1 
ATOM   5306 N  N   . VAL B 1 278 ? 45.968  5.550   -37.907 1.00 10.60 ?  280 VAL B N   1 
ATOM   5307 C  CA  . VAL B 1 278 ? 45.162  5.063   -39.022 1.00 9.78  ?  280 VAL B CA  1 
ATOM   5308 C  C   . VAL B 1 278 ? 45.061  6.187   -40.037 1.00 10.02 ?  280 VAL B C   1 
ATOM   5309 O  O   . VAL B 1 278 ? 44.597  7.282   -39.705 1.00 11.49 ?  280 VAL B O   1 
ATOM   5310 C  CB  . VAL B 1 278 ? 43.757  4.619   -38.582 1.00 11.50 ?  280 VAL B CB  1 
ATOM   5311 C  CG1 . VAL B 1 278 ? 42.944  4.163   -39.796 1.00 12.43 ?  280 VAL B CG1 1 
ATOM   5312 C  CG2 . VAL B 1 278 ? 43.851  3.507   -37.552 1.00 12.60 ?  280 VAL B CG2 1 
ATOM   5313 N  N   . VAL B 1 279 ? 45.507  5.921   -41.261 1.00 8.56  ?  281 VAL B N   1 
ATOM   5314 C  CA  . VAL B 1 279 ? 45.381  6.861   -42.370 1.00 9.74  ?  281 VAL B CA  1 
ATOM   5315 C  C   . VAL B 1 279 ? 44.182  6.438   -43.197 1.00 11.75 ?  281 VAL B C   1 
ATOM   5316 O  O   . VAL B 1 279 ? 44.083  5.275   -43.599 1.00 11.56 ?  281 VAL B O   1 
ATOM   5317 C  CB  . VAL B 1 279 ? 46.657  6.883   -43.228 1.00 9.12  ?  281 VAL B CB  1 
ATOM   5318 C  CG1 . VAL B 1 279 ? 46.466  7.763   -44.465 1.00 10.14 ?  281 VAL B CG1 1 
ATOM   5319 C  CG2 . VAL B 1 279 ? 47.826  7.370   -42.377 1.00 10.04 ?  281 VAL B CG2 1 
ATOM   5320 N  N   . THR B 1 280 ? 43.264  7.364   -43.446 1.00 7.01  ?  282 THR B N   1 
ATOM   5321 C  CA  . THR B 1 280 ? 42.064  6.976   -44.166 1.00 9.18  ?  282 THR B CA  1 
ATOM   5322 C  C   . THR B 1 280 ? 41.607  8.116   -45.061 1.00 8.18  ?  282 THR B C   1 
ATOM   5323 O  O   . THR B 1 280 ? 42.247  9.166   -45.157 1.00 10.26 ?  282 THR B O   1 
ATOM   5324 C  CB  . THR B 1 280 ? 40.962  6.535   -43.191 1.00 12.06 ?  282 THR B CB  1 
ATOM   5325 O  OG1 . THR B 1 280 ? 39.887  5.942   -43.931 1.00 12.07 ?  282 THR B OG1 1 
ATOM   5326 C  CG2 . THR B 1 280 ? 40.446  7.715   -42.361 1.00 9.46  ?  282 THR B CG2 1 
ATOM   5327 N  N   . SER B 1 281 ? 40.494  7.880   -45.743 1.00 9.48  ?  283 SER B N   1 
ATOM   5328 C  CA  . SER B 1 281 ? 39.911  8.818   -46.682 1.00 10.86 ?  283 SER B CA  1 
ATOM   5329 C  C   . SER B 1 281 ? 38.424  8.957   -46.369 1.00 11.40 ?  283 SER B C   1 
ATOM   5330 O  O   . SER B 1 281 ? 37.892  8.337   -45.441 1.00 9.93  ?  283 SER B O   1 
ATOM   5331 C  CB  . SER B 1 281 ? 40.135  8.341   -48.123 1.00 11.82 ?  283 SER B CB  1 
ATOM   5332 O  OG  . SER B 1 281 ? 39.205  7.311   -48.463 1.00 10.32 ?  283 SER B OG  1 
ATOM   5333 N  N   . SER B 1 282 ? 37.746  9.778   -47.158 1.00 8.76  ?  284 SER B N   1 
ATOM   5334 C  CA  . SER B 1 282 ? 36.293  9.822   -47.149 1.00 11.09 ?  284 SER B CA  1 
ATOM   5335 C  C   . SER B 1 282 ? 35.716  9.221   -48.432 1.00 9.28  ?  284 SER B C   1 
ATOM   5336 O  O   . SER B 1 282 ? 34.631  9.611   -48.873 1.00 10.77 ?  284 SER B O   1 
ATOM   5337 C  CB  . SER B 1 282 ? 35.824  11.261  -46.931 1.00 10.27 ?  284 SER B CB  1 
ATOM   5338 O  OG  . SER B 1 282 ? 34.404  11.369  -46.957 1.00 14.30 ?  284 SER B OG  1 
ATOM   5339 N  N   . ALA B 1 283 ? 36.437  8.266   -49.035 1.00 8.97  ?  285 ALA B N   1 
ATOM   5340 C  CA  . ALA B 1 283 ? 36.011  7.515   -50.222 1.00 8.95  ?  285 ALA B CA  1 
ATOM   5341 C  C   . ALA B 1 283 ? 35.879  8.389   -51.473 1.00 9.57  ?  285 ALA B C   1 
ATOM   5342 O  O   . ALA B 1 283 ? 35.200  8.002   -52.437 1.00 13.85 ?  285 ALA B O   1 
ATOM   5343 C  CB  . ALA B 1 283 ? 34.706  6.755   -49.959 1.00 11.45 ?  285 ALA B CB  1 
ATOM   5344 N  N   . GLY B 1 284 ? 36.526  9.549   -51.492 1.00 10.11 ?  286 GLY B N   1 
ATOM   5345 C  CA  . GLY B 1 284 ? 36.607  10.351  -52.703 1.00 9.64  ?  286 GLY B CA  1 
ATOM   5346 C  C   . GLY B 1 284 ? 35.254  10.907  -53.127 1.00 12.08 ?  286 GLY B C   1 
ATOM   5347 O  O   . GLY B 1 284 ? 34.257  10.834  -52.417 1.00 10.20 ?  286 GLY B O   1 
ATOM   5348 N  N   . HIS B 1 285 ? 35.252  11.475  -54.332 1.00 10.20 ?  287 HIS B N   1 
ATOM   5349 C  CA  . HIS B 1 285 ? 34.017  11.980  -54.910 1.00 10.65 ?  287 HIS B CA  1 
ATOM   5350 C  C   . HIS B 1 285 ? 33.093  10.806  -55.225 1.00 10.60 ?  287 HIS B C   1 
ATOM   5351 O  O   . HIS B 1 285 ? 33.535  9.793   -55.778 1.00 13.43 ?  287 HIS B O   1 
ATOM   5352 C  CB  . HIS B 1 285 ? 34.317  12.787  -56.183 1.00 12.02 ?  287 HIS B CB  1 
ATOM   5353 C  CG  . HIS B 1 285 ? 33.096  13.372  -56.827 1.00 13.43 ?  287 HIS B CG  1 
ATOM   5354 N  ND1 . HIS B 1 285 ? 32.629  14.636  -56.536 1.00 17.78 ?  287 HIS B ND1 1 
ATOM   5355 C  CD2 . HIS B 1 285 ? 32.227  12.848  -57.724 1.00 15.32 ?  287 HIS B CD2 1 
ATOM   5356 C  CE1 . HIS B 1 285 ? 31.532  14.870  -57.237 1.00 18.27 ?  287 HIS B CE1 1 
ATOM   5357 N  NE2 . HIS B 1 285 ? 31.264  13.800  -57.963 1.00 15.29 ?  287 HIS B NE2 1 
ATOM   5358 N  N   . PRO B 1 286 ? 31.803  10.910  -54.909 1.00 11.20 ?  288 PRO B N   1 
ATOM   5359 C  CA  . PRO B 1 286 ? 31.075  12.097  -54.446 1.00 10.28 ?  288 PRO B CA  1 
ATOM   5360 C  C   . PRO B 1 286 ? 30.866  12.194  -52.934 1.00 13.08 ?  288 PRO B C   1 
ATOM   5361 O  O   . PRO B 1 286 ? 30.340  13.203  -52.474 1.00 11.97 ?  288 PRO B O   1 
ATOM   5362 C  CB  . PRO B 1 286 ? 29.718  11.930  -55.119 1.00 10.62 ?  288 PRO B CB  1 
ATOM   5363 C  CG  . PRO B 1 286 ? 29.524  10.445  -55.088 1.00 11.73 ?  288 PRO B CG  1 
ATOM   5364 C  CD  . PRO B 1 286 ? 30.885  9.836   -55.319 1.00 13.19 ?  288 PRO B CD  1 
ATOM   5365 N  N   . LEU B 1 287 ? 31.249  11.167  -52.173 1.00 10.38 ?  289 LEU B N   1 
ATOM   5366 C  CA  . LEU B 1 287 ? 30.971  11.212  -50.741 1.00 9.61  ?  289 LEU B CA  1 
ATOM   5367 C  C   . LEU B 1 287 ? 31.751  12.328  -50.042 1.00 10.13 ?  289 LEU B C   1 
ATOM   5368 O  O   . LEU B 1 287 ? 31.231  12.955  -49.109 1.00 10.80 ?  289 LEU B O   1 
ATOM   5369 C  CB  . LEU B 1 287 ? 31.284  9.857   -50.101 1.00 13.31 ?  289 LEU B CB  1 
ATOM   5370 C  CG  . LEU B 1 287 ? 30.888  9.723   -48.633 1.00 11.09 ?  289 LEU B CG  1 
ATOM   5371 C  CD1 . LEU B 1 287 ? 29.380  9.826   -48.447 1.00 11.53 ?  289 LEU B CD1 1 
ATOM   5372 C  CD2 . LEU B 1 287 ? 31.387  8.382   -48.087 1.00 12.33 ?  289 LEU B CD2 1 
ATOM   5373 N  N   . ASP B 1 288 ? 32.994  12.599  -50.465 1.00 12.09 ?  290 ASP B N   1 
ATOM   5374 C  CA  . ASP B 1 288 ? 33.833  13.537  -49.723 1.00 11.04 ?  290 ASP B CA  1 
ATOM   5375 C  C   . ASP B 1 288 ? 33.586  15.001  -50.100 1.00 11.02 ?  290 ASP B C   1 
ATOM   5376 O  O   . ASP B 1 288 ? 34.438  15.850  -49.817 1.00 11.65 ?  290 ASP B O   1 
ATOM   5377 C  CB  . ASP B 1 288 ? 35.328  13.161  -49.832 1.00 9.46  ?  290 ASP B CB  1 
ATOM   5378 C  CG  . ASP B 1 288 ? 36.006  13.555  -51.149 1.00 9.90  ?  290 ASP B CG  1 
ATOM   5379 O  OD1 . ASP B 1 288 ? 35.366  14.038  -52.112 1.00 11.68 ?  290 ASP B OD1 1 
ATOM   5380 O  OD2 . ASP B 1 288 ? 37.248  13.363  -51.201 1.00 14.74 ?  290 ASP B OD2 1 
ATOM   5381 N  N   . LEU B 1 289 ? 32.414  15.314  -50.674 1.00 8.97  ?  291 LEU B N   1 
ATOM   5382 C  CA  . LEU B 1 289 ? 32.062  16.696  -50.988 1.00 12.31 ?  291 LEU B CA  1 
ATOM   5383 C  C   . LEU B 1 289 ? 31.994  17.598  -49.751 1.00 14.55 ?  291 LEU B C   1 
ATOM   5384 O  O   . LEU B 1 289 ? 32.286  18.794  -49.854 1.00 14.53 ?  291 LEU B O   1 
ATOM   5385 C  CB  . LEU B 1 289 ? 30.712  16.728  -51.715 1.00 11.92 ?  291 LEU B CB  1 
ATOM   5386 C  CG  . LEU B 1 289 ? 30.730  16.348  -53.199 1.00 13.39 ?  291 LEU B CG  1 
ATOM   5387 C  CD1 . LEU B 1 289 ? 29.274  16.126  -53.680 1.00 12.53 ?  291 LEU B CD1 1 
ATOM   5388 C  CD2 . LEU B 1 289 ? 31.458  17.393  -54.048 1.00 15.86 ?  291 LEU B CD2 1 
ATOM   5389 N  N   . THR B 1 290 ? 31.586  17.075  -48.584 1.00 11.77 ?  292 THR B N   1 
ATOM   5390 C  CA  . THR B 1 290 ? 31.407  17.913  -47.401 1.00 12.08 ?  292 THR B CA  1 
ATOM   5391 C  C   . THR B 1 290 ? 32.074  17.293  -46.178 1.00 12.72 ?  292 THR B C   1 
ATOM   5392 O  O   . THR B 1 290 ? 32.237  16.072  -46.082 1.00 11.23 ?  292 THR B O   1 
ATOM   5393 C  CB  . THR B 1 290 ? 29.917  18.170  -47.070 1.00 11.96 ?  292 THR B CB  1 
ATOM   5394 O  OG1 . THR B 1 290 ? 29.225  16.922  -46.897 1.00 11.71 ?  292 THR B OG1 1 
ATOM   5395 C  CG2 . THR B 1 290 ? 29.257  19.000  -48.185 1.00 14.41 ?  292 THR B CG2 1 
ATOM   5396 N  N   . PHE B 1 291 ? 32.452  18.163  -45.240 1.00 11.04 ?  293 PHE B N   1 
ATOM   5397 C  CA  . PHE B 1 291 ? 32.964  17.708  -43.950 1.00 11.12 ?  293 PHE B CA  1 
ATOM   5398 C  C   . PHE B 1 291 ? 31.922  16.857  -43.236 1.00 13.14 ?  293 PHE B C   1 
ATOM   5399 O  O   . PHE B 1 291 ? 32.247  15.842  -42.605 1.00 11.25 ?  293 PHE B O   1 
ATOM   5400 C  CB  . PHE B 1 291 ? 33.345  18.931  -43.109 1.00 11.77 ?  293 PHE B CB  1 
ATOM   5401 C  CG  . PHE B 1 291 ? 33.906  18.602  -41.762 1.00 13.78 ?  293 PHE B CG  1 
ATOM   5402 C  CD1 . PHE B 1 291 ? 35.250  18.314  -41.618 1.00 15.72 ?  293 PHE B CD1 1 
ATOM   5403 C  CD2 . PHE B 1 291 ? 33.085  18.566  -40.640 1.00 14.23 ?  293 PHE B CD2 1 
ATOM   5404 C  CE1 . PHE B 1 291 ? 35.780  18.007  -40.372 1.00 12.37 ?  293 PHE B CE1 1 
ATOM   5405 C  CE2 . PHE B 1 291 ? 33.603  18.261  -39.389 1.00 15.06 ?  293 PHE B CE2 1 
ATOM   5406 C  CZ  . PHE B 1 291 ? 34.945  17.982  -39.249 1.00 12.84 ?  293 PHE B CZ  1 
ATOM   5407 N  N   . TYR B 1 292 ? 30.656  17.267  -43.338 1.00 10.91 ?  294 TYR B N   1 
ATOM   5408 C  CA  . TYR B 1 292 ? 29.532  16.507  -42.806 1.00 10.18 ?  294 TYR B CA  1 
ATOM   5409 C  C   . TYR B 1 292 ? 29.608  15.031  -43.201 1.00 12.11 ?  294 TYR B C   1 
ATOM   5410 O  O   . TYR B 1 292 ? 29.530  14.146  -42.343 1.00 11.23 ?  294 TYR B O   1 
ATOM   5411 C  CB  . TYR B 1 292 ? 28.240  17.165  -43.309 1.00 10.45 ?  294 TYR B CB  1 
ATOM   5412 C  CG  . TYR B 1 292 ? 26.954  16.410  -43.072 1.00 12.72 ?  294 TYR B CG  1 
ATOM   5413 C  CD1 . TYR B 1 292 ? 26.376  15.635  -44.082 1.00 11.71 ?  294 TYR B CD1 1 
ATOM   5414 C  CD2 . TYR B 1 292 ? 26.299  16.481  -41.838 1.00 13.45 ?  294 TYR B CD2 1 
ATOM   5415 C  CE1 . TYR B 1 292 ? 25.190  14.962  -43.868 1.00 14.88 ?  294 TYR B CE1 1 
ATOM   5416 C  CE2 . TYR B 1 292 ? 25.110  15.810  -41.620 1.00 12.46 ?  294 TYR B CE2 1 
ATOM   5417 C  CZ  . TYR B 1 292 ? 24.560  15.050  -42.639 1.00 13.58 ?  294 TYR B CZ  1 
ATOM   5418 O  OH  . TYR B 1 292 ? 23.386  14.369  -42.436 1.00 14.30 ?  294 TYR B OH  1 
ATOM   5419 N  N   . GLN B 1 293 ? 29.801  14.741  -44.493 1.00 10.88 ?  295 GLN B N   1 
ATOM   5420 C  CA  . GLN B 1 293 ? 29.926  13.339  -44.902 1.00 13.05 ?  295 GLN B CA  1 
ATOM   5421 C  C   . GLN B 1 293 ? 31.288  12.732  -44.538 1.00 10.96 ?  295 GLN B C   1 
ATOM   5422 O  O   . GLN B 1 293 ? 31.363  11.529  -44.235 1.00 11.01 ?  295 GLN B O   1 
ATOM   5423 C  CB  . GLN B 1 293 ? 29.695  13.200  -46.415 1.00 12.00 ?  295 GLN B CB  1 
ATOM   5424 C  CG  . GLN B 1 293 ? 28.259  13.518  -46.846 1.00 11.40 ?  295 GLN B CG  1 
ATOM   5425 C  CD  . GLN B 1 293 ? 27.265  12.423  -46.486 1.00 11.40 ?  295 GLN B CD  1 
ATOM   5426 O  OE1 . GLN B 1 293 ? 27.643  11.339  -46.027 1.00 13.15 ?  295 GLN B OE1 1 
ATOM   5427 N  NE2 . GLN B 1 293 ? 25.977  12.716  -46.662 1.00 12.74 ?  295 GLN B NE2 1 
ATOM   5428 N  N   . ALA B 1 294 ? 32.358  13.536  -44.565 1.00 10.76 ?  296 ALA B N   1 
ATOM   5429 C  CA  . ALA B 1 294 ? 33.718  13.038  -44.344 1.00 8.48  ?  296 ALA B CA  1 
ATOM   5430 C  C   . ALA B 1 294 ? 33.919  12.478  -42.940 1.00 11.17 ?  296 ALA B C   1 
ATOM   5431 O  O   . ALA B 1 294 ? 34.837  11.675  -42.720 1.00 10.95 ?  296 ALA B O   1 
ATOM   5432 C  CB  . ALA B 1 294 ? 34.729  14.157  -44.619 1.00 11.91 ?  296 ALA B CB  1 
ATOM   5433 N  N   . VAL B 1 295 ? 33.065  12.853  -41.991 1.00 9.97  ?  297 VAL B N   1 
ATOM   5434 C  CA  . VAL B 1 295 ? 33.116  12.239  -40.667 1.00 8.82  ?  297 VAL B CA  1 
ATOM   5435 C  C   . VAL B 1 295 ? 32.973  10.713  -40.753 1.00 10.42 ?  297 VAL B C   1 
ATOM   5436 O  O   . VAL B 1 295 ? 33.479  9.985   -39.888 1.00 9.24  ?  297 VAL B O   1 
ATOM   5437 C  CB  . VAL B 1 295 ? 32.037  12.898  -39.778 1.00 10.70 ?  297 VAL B CB  1 
ATOM   5438 C  CG1 . VAL B 1 295 ? 31.845  12.152  -38.472 1.00 11.79 ?  297 VAL B CG1 1 
ATOM   5439 C  CG2 . VAL B 1 295 ? 32.423  14.359  -39.502 1.00 14.05 ?  297 VAL B CG2 1 
ATOM   5440 N  N   . LYS B 1 296 ? 32.306  10.201  -41.796 1.00 9.73  ?  298 LYS B N   1 
ATOM   5441 C  CA  . LYS B 1 296 ? 32.212  8.748   -41.980 1.00 8.40  ?  298 LYS B CA  1 
ATOM   5442 C  C   . LYS B 1 296 ? 33.579  8.083   -42.074 1.00 8.55  ?  298 LYS B C   1 
ATOM   5443 O  O   . LYS B 1 296 ? 33.725  6.913   -41.693 1.00 8.91  ?  298 LYS B O   1 
ATOM   5444 C  CB  . LYS B 1 296 ? 31.423  8.418   -43.246 1.00 10.71 ?  298 LYS B CB  1 
ATOM   5445 C  CG  . LYS B 1 296 ? 29.969  8.837   -43.178 1.00 8.84  ?  298 LYS B CG  1 
ATOM   5446 C  CD  . LYS B 1 296 ? 29.306  8.724   -44.566 1.00 7.99  ?  298 LYS B CD  1 
ATOM   5447 C  CE  . LYS B 1 296 ? 27.805  8.519   -44.380 1.00 12.05 ?  298 LYS B CE  1 
ATOM   5448 N  NZ  . LYS B 1 296 ? 27.102  8.644   -45.669 1.00 10.62 ?  298 LYS B NZ  1 
ATOM   5449 N  N   . GLY B 1 297 ? 34.571  8.764   -42.649 1.00 8.98  ?  299 GLY B N   1 
ATOM   5450 C  CA  . GLY B 1 297 ? 35.896  8.172   -42.684 1.00 9.03  ?  299 GLY B CA  1 
ATOM   5451 C  C   . GLY B 1 297 ? 36.479  8.043   -41.293 1.00 9.92  ?  299 GLY B C   1 
ATOM   5452 O  O   . GLY B 1 297 ? 37.219  7.096   -41.004 1.00 11.25 ?  299 GLY B O   1 
ATOM   5453 N  N   . LEU B 1 298 ? 36.145  8.988   -40.411 1.00 10.69 ?  300 LEU B N   1 
ATOM   5454 C  CA  . LEU B 1 298 ? 36.646  8.946   -39.039 1.00 8.95  ?  300 LEU B CA  1 
ATOM   5455 C  C   . LEU B 1 298 ? 35.977  7.836   -38.235 1.00 10.89 ?  300 LEU B C   1 
ATOM   5456 O  O   . LEU B 1 298 ? 36.657  7.055   -37.554 1.00 11.97 ?  300 LEU B O   1 
ATOM   5457 C  CB  . LEU B 1 298 ? 36.433  10.300  -38.370 1.00 10.22 ?  300 LEU B CB  1 
ATOM   5458 C  CG  . LEU B 1 298 ? 37.095  11.463  -39.108 1.00 8.74  ?  300 LEU B CG  1 
ATOM   5459 C  CD1 . LEU B 1 298 ? 36.705  12.799  -38.481 1.00 10.94 ?  300 LEU B CD1 1 
ATOM   5460 C  CD2 . LEU B 1 298 ? 38.616  11.270  -39.068 1.00 11.63 ?  300 LEU B CD2 1 
ATOM   5461 N  N   . THR B 1 299 ? 34.643  7.761   -38.276 1.00 9.58  ?  301 THR B N   1 
ATOM   5462 C  CA  . THR B 1 299 ? 33.973  6.682   -37.558 1.00 11.33 ?  301 THR B CA  1 
ATOM   5463 C  C   . THR B 1 299 ? 34.366  5.324   -38.111 1.00 10.93 ?  301 THR B C   1 
ATOM   5464 O  O   . THR B 1 299 ? 34.481  4.358   -37.347 1.00 14.27 ?  301 THR B O   1 
ATOM   5465 C  CB  . THR B 1 299 ? 32.443  6.840   -37.591 1.00 11.90 ?  301 THR B CB  1 
ATOM   5466 O  OG1 . THR B 1 299 ? 31.971  6.977   -38.939 1.00 11.52 ?  301 THR B OG1 1 
ATOM   5467 C  CG2 . THR B 1 299 ? 32.020  8.069   -36.813 1.00 13.90 ?  301 THR B CG2 1 
ATOM   5468 N  N   . GLY B 1 300 ? 34.592  5.234   -39.422 1.00 10.96 ?  302 GLY B N   1 
ATOM   5469 C  CA  . GLY B 1 300 ? 34.961  3.960   -40.019 1.00 12.11 ?  302 GLY B CA  1 
ATOM   5470 C  C   . GLY B 1 300 ? 36.300  3.445   -39.531 1.00 14.99 ?  302 GLY B C   1 
ATOM   5471 O  O   . GLY B 1 300 ? 36.520  2.234   -39.480 1.00 12.76 ?  302 GLY B O   1 
ATOM   5472 N  N   . ALA B 1 301 ? 37.207  4.350   -39.167 1.00 10.92 ?  303 ALA B N   1 
ATOM   5473 C  CA  . ALA B 1 301 ? 38.531  3.964   -38.690 1.00 11.30 ?  303 ALA B CA  1 
ATOM   5474 C  C   . ALA B 1 301 ? 38.537  3.519   -37.234 1.00 14.15 ?  303 ALA B C   1 
ATOM   5475 O  O   . ALA B 1 301 ? 39.478  2.834   -36.812 1.00 13.97 ?  303 ALA B O   1 
ATOM   5476 C  CB  . ALA B 1 301 ? 39.505  5.134   -38.867 1.00 13.65 ?  303 ALA B CB  1 
ATOM   5477 N  N   . LEU B 1 302 ? 37.525  3.897   -36.459 1.00 10.31 ?  304 LEU B N   1 
ATOM   5478 C  CA  . LEU B 1 302 ? 37.555  3.668   -35.016 1.00 16.06 ?  304 LEU B CA  1 
ATOM   5479 C  C   . LEU B 1 302 ? 37.839  2.236   -34.589 1.00 16.49 ?  304 LEU B C   1 
ATOM   5480 O  O   . LEU B 1 302 ? 38.557  2.063   -33.589 1.00 15.50 ?  304 LEU B O   1 
ATOM   5481 C  CB  . LEU B 1 302 ? 36.233  4.121   -34.381 1.00 16.16 ?  304 LEU B CB  1 
ATOM   5482 C  CG  . LEU B 1 302 ? 36.031  5.622   -34.254 1.00 16.96 ?  304 LEU B CG  1 
ATOM   5483 C  CD1 . LEU B 1 302 ? 34.632  5.914   -33.724 1.00 15.27 ?  304 LEU B CD1 1 
ATOM   5484 C  CD2 . LEU B 1 302 ? 37.098  6.228   -33.352 1.00 14.93 ?  304 LEU B CD2 1 
ATOM   5485 N  N   . PRO B 1 303 ? 37.317  1.190   -35.242 1.00 12.28 ?  305 PRO B N   1 
ATOM   5486 C  CA  . PRO B 1 303 ? 37.533  -0.166  -34.712 1.00 15.92 ?  305 PRO B CA  1 
ATOM   5487 C  C   . PRO B 1 303 ? 38.989  -0.589  -34.666 1.00 18.87 ?  305 PRO B C   1 
ATOM   5488 O  O   . PRO B 1 303 ? 39.314  -1.506  -33.905 1.00 16.91 ?  305 PRO B O   1 
ATOM   5489 C  CB  . PRO B 1 303 ? 36.733  -1.052  -35.680 1.00 18.27 ?  305 PRO B CB  1 
ATOM   5490 C  CG  . PRO B 1 303 ? 35.652  -0.152  -36.192 1.00 18.00 ?  305 PRO B CG  1 
ATOM   5491 C  CD  . PRO B 1 303 ? 36.335  1.176   -36.349 1.00 16.38 ?  305 PRO B CD  1 
ATOM   5492 N  N   . ILE B 1 304 ? 39.887  0.022   -35.442 1.00 11.28 ?  306 ILE B N   1 
ATOM   5493 C  CA  . ILE B 1 304 ? 41.263  -0.455  -35.464 1.00 11.92 ?  306 ILE B CA  1 
ATOM   5494 C  C   . ILE B 1 304 ? 42.249  0.547   -34.904 1.00 12.58 ?  306 ILE B C   1 
ATOM   5495 O  O   . ILE B 1 304 ? 43.457  0.274   -34.932 1.00 16.41 ?  306 ILE B O   1 
ATOM   5496 C  CB  . ILE B 1 304 ? 41.702  -0.893  -36.876 1.00 15.81 ?  306 ILE B CB  1 
ATOM   5497 C  CG1 . ILE B 1 304 ? 41.635  0.281   -37.860 1.00 14.08 ?  306 ILE B CG1 1 
ATOM   5498 C  CG2 . ILE B 1 304 ? 40.885  -2.091  -37.340 1.00 12.94 ?  306 ILE B CG2 1 
ATOM   5499 C  CD1 . ILE B 1 304 ? 42.494  0.082   -39.093 1.00 10.36 ?  306 ILE B CD1 1 
ATOM   5500 N  N   . VAL B 1 305 ? 41.792  1.707   -34.400 1.00 14.41 ?  307 VAL B N   1 
ATOM   5501 C  CA  . VAL B 1 305 ? 42.711  2.642   -33.750 1.00 12.76 ?  307 VAL B CA  1 
ATOM   5502 C  C   . VAL B 1 305 ? 42.746  2.373   -32.246 1.00 11.20 ?  307 VAL B C   1 
ATOM   5503 O  O   . VAL B 1 305 ? 41.726  2.062   -31.622 1.00 14.13 ?  307 VAL B O   1 
ATOM   5504 C  CB  . VAL B 1 305 ? 42.344  4.107   -34.067 1.00 10.48 ?  307 VAL B CB  1 
ATOM   5505 C  CG1 . VAL B 1 305 ? 41.090  4.567   -33.340 1.00 13.63 ?  307 VAL B CG1 1 
ATOM   5506 C  CG2 . VAL B 1 305 ? 43.540  5.022   -33.754 1.00 12.35 ?  307 VAL B CG2 1 
ATOM   5507 N  N   . LYS B 1 306 ? 43.945  2.441   -31.670 1.00 11.62 ?  308 LYS B N   1 
ATOM   5508 C  CA  . LYS B 1 306 ? 44.072  2.347   -30.231 1.00 13.32 ?  308 LYS B CA  1 
ATOM   5509 C  C   . LYS B 1 306 ? 43.418  3.557   -29.573 1.00 17.36 ?  308 LYS B C   1 
ATOM   5510 O  O   . LYS B 1 306 ? 43.466  4.665   -30.116 1.00 15.43 ?  308 LYS B O   1 
ATOM   5511 C  CB  . LYS B 1 306 ? 45.537  2.278   -29.822 1.00 16.31 ?  308 LYS B CB  1 
ATOM   5512 C  CG  . LYS B 1 306 ? 46.251  0.987   -30.193 1.00 19.31 ?  308 LYS B CG  1 
ATOM   5513 C  CD  . LYS B 1 306 ? 47.745  1.225   -30.273 1.00 26.43 ?  308 LYS B CD  1 
ATOM   5514 C  CE  . LYS B 1 306 ? 48.388  1.178   -28.907 1.00 31.59 ?  308 LYS B CE  1 
ATOM   5515 N  NZ  . LYS B 1 306 ? 49.837  0.830   -29.009 1.00 32.38 ?  308 LYS B NZ  1 
ATOM   5516 N  N   . PRO B 1 307 ? 42.801  3.376   -28.408 1.00 15.77 ?  309 PRO B N   1 
ATOM   5517 C  CA  . PRO B 1 307 ? 42.376  4.534   -27.618 1.00 16.65 ?  309 PRO B CA  1 
ATOM   5518 C  C   . PRO B 1 307 ? 43.550  5.474   -27.420 1.00 15.39 ?  309 PRO B C   1 
ATOM   5519 O  O   . PRO B 1 307 ? 44.658  5.044   -27.089 1.00 16.01 ?  309 PRO B O   1 
ATOM   5520 C  CB  . PRO B 1 307 ? 41.918  3.910   -26.293 1.00 19.90 ?  309 PRO B CB  1 
ATOM   5521 C  CG  . PRO B 1 307 ? 41.587  2.499   -26.644 1.00 25.11 ?  309 PRO B CG  1 
ATOM   5522 C  CD  . PRO B 1 307 ? 42.589  2.110   -27.683 1.00 21.32 ?  309 PRO B CD  1 
ATOM   5523 N  N   . GLY B 1 308 ? 43.323  6.758   -27.683 1.00 13.12 ?  310 GLY B N   1 
ATOM   5524 C  CA  . GLY B 1 308 ? 44.394  7.727   -27.643 1.00 12.72 ?  310 GLY B CA  1 
ATOM   5525 C  C   . GLY B 1 308 ? 45.225  7.816   -28.904 1.00 16.04 ?  310 GLY B C   1 
ATOM   5526 O  O   . GLY B 1 308 ? 46.105  8.687   -28.983 1.00 15.95 ?  310 GLY B O   1 
ATOM   5527 N  N   . GLY B 1 309 ? 44.989  6.938   -29.877 1.00 12.80 ?  311 GLY B N   1 
ATOM   5528 C  CA  . GLY B 1 309 ? 45.668  6.995   -31.158 1.00 9.58  ?  311 GLY B CA  1 
ATOM   5529 C  C   . GLY B 1 309 ? 45.179  8.161   -32.004 1.00 11.97 ?  311 GLY B C   1 
ATOM   5530 O  O   . GLY B 1 309 ? 44.400  9.014   -31.575 1.00 12.23 ?  311 GLY B O   1 
ATOM   5531 N  N   . THR B 1 310 ? 45.667  8.200   -33.242 1.00 9.33  ?  312 THR B N   1 
ATOM   5532 C  CA  . THR B 1 310 ? 45.375  9.314   -34.138 1.00 8.24  ?  312 THR B CA  1 
ATOM   5533 C  C   . THR B 1 310 ? 44.838  8.782   -35.451 1.00 10.00 ?  312 THR B C   1 
ATOM   5534 O  O   . THR B 1 310 ? 45.409  7.843   -36.011 1.00 9.54  ?  312 THR B O   1 
ATOM   5535 C  CB  . THR B 1 310 ? 46.639  10.156  -34.386 1.00 11.18 ?  312 THR B CB  1 
ATOM   5536 O  OG1 . THR B 1 310 ? 47.009  10.819  -33.162 1.00 11.91 ?  312 THR B OG1 1 
ATOM   5537 C  CG2 . THR B 1 310 ? 46.394  11.205  -35.466 1.00 11.75 ?  312 THR B CG2 1 
ATOM   5538 N  N   . ILE B 1 311 ? 43.751  9.389   -35.936 1.00 8.39  ?  313 ILE B N   1 
ATOM   5539 C  CA  . ILE B 1 311 ? 43.225  9.118   -37.269 1.00 8.58  ?  313 ILE B CA  1 
ATOM   5540 C  C   . ILE B 1 311 ? 43.636  10.284  -38.160 1.00 10.75 ?  313 ILE B C   1 
ATOM   5541 O  O   . ILE B 1 311 ? 43.358  11.446  -37.837 1.00 12.28 ?  313 ILE B O   1 
ATOM   5542 C  CB  . ILE B 1 311 ? 41.696  8.946   -37.245 1.00 8.87  ?  313 ILE B CB  1 
ATOM   5543 C  CG1 . ILE B 1 311 ? 41.309  7.798   -36.302 1.00 10.29 ?  313 ILE B CG1 1 
ATOM   5544 C  CG2 . ILE B 1 311 ? 41.154  8.705   -38.689 1.00 11.87 ?  313 ILE B CG2 1 
ATOM   5545 C  CD1 . ILE B 1 311 ? 39.806  7.737   -36.023 1.00 11.94 ?  313 ILE B CD1 1 
ATOM   5546 N  N   . VAL B 1 312 ? 44.321  9.981   -39.262 1.00 8.06  ?  314 VAL B N   1 
ATOM   5547 C  CA  . VAL B 1 312 ? 44.690  10.968  -40.270 1.00 10.05 ?  314 VAL B CA  1 
ATOM   5548 C  C   . VAL B 1 312 ? 43.776  10.740  -41.465 1.00 10.62 ?  314 VAL B C   1 
ATOM   5549 O  O   . VAL B 1 312 ? 43.792  9.654   -42.053 1.00 12.20 ?  314 VAL B O   1 
ATOM   5550 C  CB  . VAL B 1 312 ? 46.158  10.826  -40.690 1.00 10.22 ?  314 VAL B CB  1 
ATOM   5551 C  CG1 . VAL B 1 312 ? 46.500  11.872  -41.774 1.00 12.56 ?  314 VAL B CG1 1 
ATOM   5552 C  CG2 . VAL B 1 312 ? 47.098  10.935  -39.471 1.00 8.98  ?  314 VAL B CG2 1 
ATOM   5553 N  N   . ILE B 1 313 ? 42.986  11.747  -41.835 1.00 7.38  ?  315 ILE B N   1 
ATOM   5554 C  CA  . ILE B 1 313 ? 42.032  11.599  -42.929 1.00 7.58  ?  315 ILE B CA  1 
ATOM   5555 C  C   . ILE B 1 313 ? 42.330  12.636  -44.004 1.00 10.36 ?  315 ILE B C   1 
ATOM   5556 O  O   . ILE B 1 313 ? 42.651  13.784  -43.696 1.00 11.55 ?  315 ILE B O   1 
ATOM   5557 C  CB  . ILE B 1 313 ? 40.571  11.718  -42.439 1.00 9.47  ?  315 ILE B CB  1 
ATOM   5558 C  CG1 . ILE B 1 313 ? 39.584  11.379  -43.571 1.00 9.90  ?  315 ILE B CG1 1 
ATOM   5559 C  CG2 . ILE B 1 313 ? 40.305  13.087  -41.837 1.00 10.36 ?  315 ILE B CG2 1 
ATOM   5560 C  CD1 . ILE B 1 313 ? 38.106  11.203  -43.088 1.00 9.10  ?  315 ILE B CD1 1 
ATOM   5561 N  N   . ALA B 1 314 ? 42.275  12.212  -45.265 1.00 9.46  ?  316 ALA B N   1 
ATOM   5562 C  CA  . ALA B 1 314 ? 42.332  13.118  -46.405 1.00 8.86  ?  316 ALA B CA  1 
ATOM   5563 C  C   . ALA B 1 314 ? 40.978  13.107  -47.098 1.00 11.52 ?  316 ALA B C   1 
ATOM   5564 O  O   . ALA B 1 314 ? 40.402  12.040  -47.328 1.00 12.29 ?  316 ALA B O   1 
ATOM   5565 C  CB  . ALA B 1 314 ? 43.436  12.713  -47.382 1.00 12.60 ?  316 ALA B CB  1 
ATOM   5566 N  N   . ALA B 1 315 ? 40.464  14.294  -47.401 1.00 10.45 ?  317 ALA B N   1 
ATOM   5567 C  CA  . ALA B 1 315 ? 39.156  14.423  -48.029 1.00 10.35 ?  317 ALA B CA  1 
ATOM   5568 C  C   . ALA B 1 315 ? 39.134  15.747  -48.772 1.00 13.38 ?  317 ALA B C   1 
ATOM   5569 O  O   . ALA B 1 315 ? 39.620  16.751  -48.247 1.00 12.64 ?  317 ALA B O   1 
ATOM   5570 C  CB  . ALA B 1 315 ? 38.034  14.360  -46.986 1.00 11.79 ?  317 ALA B CB  1 
ATOM   5571 N  N   . ALA B 1 316 ? 38.582  15.747  -49.994 1.00 12.15 ?  318 ALA B N   1 
ATOM   5572 C  CA  . ALA B 1 316 ? 38.677  16.945  -50.830 1.00 13.05 ?  318 ALA B CA  1 
ATOM   5573 C  C   . ALA B 1 316 ? 37.772  18.069  -50.324 1.00 12.33 ?  318 ALA B C   1 
ATOM   5574 O  O   . ALA B 1 316 ? 38.150  19.246  -50.396 1.00 14.59 ?  318 ALA B O   1 
ATOM   5575 C  CB  . ALA B 1 316 ? 38.350  16.608  -52.284 1.00 12.49 ?  318 ALA B CB  1 
ATOM   5576 N  N   . LEU B 1 317 ? 36.583  17.734  -49.809 1.00 10.47 ?  319 LEU B N   1 
ATOM   5577 C  CA  . LEU B 1 317 ? 35.656  18.733  -49.268 1.00 12.04 ?  319 LEU B CA  1 
ATOM   5578 C  C   . LEU B 1 317 ? 35.338  19.813  -50.308 1.00 13.01 ?  319 LEU B C   1 
ATOM   5579 O  O   . LEU B 1 317 ? 35.289  21.005  -49.997 1.00 15.46 ?  319 LEU B O   1 
ATOM   5580 C  CB  . LEU B 1 317 ? 36.229  19.361  -47.992 1.00 11.42 ?  319 LEU B CB  1 
ATOM   5581 C  CG  . LEU B 1 317 ? 36.664  18.404  -46.883 1.00 11.08 ?  319 LEU B CG  1 
ATOM   5582 C  CD1 . LEU B 1 317 ? 36.952  19.196  -45.604 1.00 14.58 ?  319 LEU B CD1 1 
ATOM   5583 C  CD2 . LEU B 1 317 ? 35.574  17.378  -46.645 1.00 11.91 ?  319 LEU B CD2 1 
ATOM   5584 N  N   . ALA B 1 318 ? 35.139  19.390  -51.563 1.00 13.55 ?  320 ALA B N   1 
ATOM   5585 C  CA  . ALA B 1 318 ? 34.935  20.356  -52.640 1.00 17.55 ?  320 ALA B CA  1 
ATOM   5586 C  C   . ALA B 1 318 ? 33.768  21.300  -52.359 1.00 15.45 ?  320 ALA B C   1 
ATOM   5587 O  O   . ALA B 1 318 ? 33.812  22.475  -52.744 1.00 18.92 ?  320 ALA B O   1 
ATOM   5588 C  CB  . ALA B 1 318 ? 34.721  19.620  -53.963 1.00 16.58 ?  320 ALA B CB  1 
ATOM   5589 N  N   . GLU B 1 319 ? 32.725  20.820  -51.696 1.00 13.26 ?  321 GLU B N   1 
ATOM   5590 C  CA  . GLU B 1 319 ? 31.565  21.652  -51.402 1.00 13.29 ?  321 GLU B CA  1 
ATOM   5591 C  C   . GLU B 1 319 ? 31.647  22.336  -50.038 1.00 14.31 ?  321 GLU B C   1 
ATOM   5592 O  O   . GLU B 1 319 ? 30.759  23.121  -49.699 1.00 18.73 ?  321 GLU B O   1 
ATOM   5593 C  CB  . GLU B 1 319 ? 30.288  20.808  -51.512 1.00 14.42 ?  321 GLU B CB  1 
ATOM   5594 C  CG  . GLU B 1 319 ? 29.010  21.596  -51.736 1.00 21.97 ?  321 GLU B CG  1 
ATOM   5595 C  CD  . GLU B 1 319 ? 27.780  20.702  -51.737 1.00 24.96 ?  321 GLU B CD  1 
ATOM   5596 O  OE1 . GLU B 1 319 ? 26.781  21.030  -51.054 1.00 24.39 ?  321 GLU B OE1 1 
ATOM   5597 O  OE2 . GLU B 1 319 ? 27.825  19.654  -52.415 1.00 22.43 ?  321 GLU B OE2 1 
ATOM   5598 N  N   . GLY B 1 320 ? 32.693  22.085  -49.255 1.00 14.03 ?  322 GLY B N   1 
ATOM   5599 C  CA  . GLY B 1 320 ? 32.818  22.763  -47.981 1.00 17.66 ?  322 GLY B CA  1 
ATOM   5600 C  C   . GLY B 1 320 ? 32.339  21.969  -46.777 1.00 15.82 ?  322 GLY B C   1 
ATOM   5601 O  O   . GLY B 1 320 ? 32.476  20.743  -46.742 1.00 15.46 ?  322 GLY B O   1 
ATOM   5602 N  N   . LEU B 1 321 ? 31.787  22.659  -45.781 1.00 14.57 ?  323 LEU B N   1 
ATOM   5603 C  CA  . LEU B 1 321 ? 31.456  22.015  -44.507 1.00 12.74 ?  323 LEU B CA  1 
ATOM   5604 C  C   . LEU B 1 321 ? 30.157  21.224  -44.553 1.00 16.07 ?  323 LEU B C   1 
ATOM   5605 O  O   . LEU B 1 321 ? 30.047  20.179  -43.901 1.00 15.29 ?  323 LEU B O   1 
ATOM   5606 C  CB  . LEU B 1 321 ? 31.379  23.054  -43.387 1.00 16.17 ?  323 LEU B CB  1 
ATOM   5607 C  CG  . LEU B 1 321 ? 32.703  23.701  -42.981 1.00 15.96 ?  323 LEU B CG  1 
ATOM   5608 C  CD1 . LEU B 1 321 ? 32.484  24.600  -41.784 1.00 22.81 ?  323 LEU B CD1 1 
ATOM   5609 C  CD2 . LEU B 1 321 ? 33.710  22.617  -42.635 1.00 17.05 ?  323 LEU B CD2 1 
ATOM   5610 N  N   . GLY B 1 322 ? 29.159  21.696  -45.285 1.00 14.63 ?  324 GLY B N   1 
ATOM   5611 C  CA  . GLY B 1 322 ? 27.857  21.078  -45.215 1.00 15.87 ?  324 GLY B CA  1 
ATOM   5612 C  C   . GLY B 1 322 ? 26.774  22.132  -45.069 1.00 15.96 ?  324 GLY B C   1 
ATOM   5613 O  O   . GLY B 1 322 ? 26.969  23.306  -45.397 1.00 18.89 ?  324 GLY B O   1 
ATOM   5614 N  N   . SER B 1 323 ? 25.632  21.705  -44.553 1.00 12.85 ?  325 SER B N   1 
ATOM   5615 C  CA  . SER B 1 323 ? 24.448  22.543  -44.526 1.00 16.25 ?  325 SER B CA  1 
ATOM   5616 C  C   . SER B 1 323 ? 24.610  23.736  -43.582 1.00 16.87 ?  325 SER B C   1 
ATOM   5617 O  O   . SER B 1 323 ? 25.458  23.735  -42.684 1.00 16.68 ?  325 SER B O   1 
ATOM   5618 C  CB  . SER B 1 323 ? 23.240  21.703  -44.119 1.00 14.18 ?  325 SER B CB  1 
ATOM   5619 O  OG  . SER B 1 323 ? 23.252  21.500  -42.717 1.00 18.03 ?  325 SER B OG  1 
ATOM   5620 N  N   . PRO B 1 324 ? 23.808  24.785  -43.784 1.00 20.18 ?  326 PRO B N   1 
ATOM   5621 C  CA  . PRO B 1 324 ? 23.867  25.921  -42.851 1.00 19.17 ?  326 PRO B CA  1 
ATOM   5622 C  C   . PRO B 1 324 ? 23.529  25.515  -41.429 1.00 17.21 ?  326 PRO B C   1 
ATOM   5623 O  O   . PRO B 1 324 ? 24.165  26.002  -40.485 1.00 17.95 ?  326 PRO B O   1 
ATOM   5624 C  CB  . PRO B 1 324 ? 22.834  26.895  -43.437 1.00 23.60 ?  326 PRO B CB  1 
ATOM   5625 C  CG  . PRO B 1 324 ? 22.796  26.533  -44.907 1.00 24.54 ?  326 PRO B CG  1 
ATOM   5626 C  CD  . PRO B 1 324 ? 22.847  25.028  -44.875 1.00 19.68 ?  326 PRO B CD  1 
ATOM   5627 N  N   . GLU B 1 325 ? 22.566  24.603  -41.263 1.00 19.46 ?  327 GLU B N   1 
ATOM   5628 C  CA  . GLU B 1 325 ? 22.206  24.116  -39.935 1.00 19.25 ?  327 GLU B CA  1 
ATOM   5629 C  C   . GLU B 1 325 ? 23.375  23.382  -39.289 1.00 16.47 ?  327 GLU B C   1 
ATOM   5630 O  O   . GLU B 1 325 ? 23.658  23.566  -38.098 1.00 16.61 ?  327 GLU B O   1 
ATOM   5631 C  CB  . GLU B 1 325 ? 21.001  23.182  -40.023 1.00 19.43 ?  327 GLU B CB  1 
ATOM   5632 C  CG  . GLU B 1 325 ? 19.700  23.873  -40.440 1.00 19.40 ?  327 GLU B CG  1 
ATOM   5633 C  CD  . GLU B 1 325 ? 19.553  24.038  -41.950 1.00 32.57 ?  327 GLU B CD  1 
ATOM   5634 O  OE1 . GLU B 1 325 ? 18.459  24.475  -42.371 1.00 40.53 ?  327 GLU B OE1 1 
ATOM   5635 O  OE2 . GLU B 1 325 ? 20.483  23.680  -42.722 1.00 20.79 ?  327 GLU B OE2 1 
ATOM   5636 N  N   . PHE B 1 326 ? 24.048  22.524  -40.056 1.00 16.93 ?  328 PHE B N   1 
ATOM   5637 C  CA  . PHE B 1 326 ? 25.222  21.825  -39.538 1.00 15.21 ?  328 PHE B CA  1 
ATOM   5638 C  C   . PHE B 1 326 ? 26.301  22.817  -39.099 1.00 17.04 ?  328 PHE B C   1 
ATOM   5639 O  O   . PHE B 1 326 ? 26.847  22.716  -37.993 1.00 16.33 ?  328 PHE B O   1 
ATOM   5640 C  CB  . PHE B 1 326 ? 25.736  20.856  -40.611 1.00 14.26 ?  328 PHE B CB  1 
ATOM   5641 C  CG  . PHE B 1 326 ? 26.965  20.069  -40.220 1.00 15.96 ?  328 PHE B CG  1 
ATOM   5642 C  CD1 . PHE B 1 326 ? 26.923  19.163  -39.167 1.00 11.54 ?  328 PHE B CD1 1 
ATOM   5643 C  CD2 . PHE B 1 326 ? 28.134  20.181  -40.960 1.00 11.02 ?  328 PHE B CD2 1 
ATOM   5644 C  CE1 . PHE B 1 326 ? 28.051  18.405  -38.833 1.00 14.49 ?  328 PHE B CE1 1 
ATOM   5645 C  CE2 . PHE B 1 326 ? 29.271  19.441  -40.633 1.00 12.16 ?  328 PHE B CE2 1 
ATOM   5646 C  CZ  . PHE B 1 326 ? 29.229  18.552  -39.565 1.00 13.56 ?  328 PHE B CZ  1 
ATOM   5647 N  N   . GLN B 1 327 ? 26.612  23.798  -39.948 1.00 19.24 ?  329 GLN B N   1 
ATOM   5648 C  CA  . GLN B 1 327 ? 27.641  24.772  -39.589 1.00 18.40 ?  329 GLN B CA  1 
ATOM   5649 C  C   . GLN B 1 327 ? 27.251  25.563  -38.338 1.00 19.86 ?  329 GLN B C   1 
ATOM   5650 O  O   . GLN B 1 327 ? 28.112  25.894  -37.511 1.00 17.64 ?  329 GLN B O   1 
ATOM   5651 C  CB  . GLN B 1 327 ? 27.901  25.707  -40.769 1.00 21.29 ?  329 GLN B CB  1 
ATOM   5652 C  CG  . GLN B 1 327 ? 28.448  24.975  -41.996 1.00 16.98 ?  329 GLN B CG  1 
ATOM   5653 C  CD  . GLN B 1 327 ? 28.834  25.903  -43.116 1.00 26.23 ?  329 GLN B CD  1 
ATOM   5654 O  OE1 . GLN B 1 327 ? 29.392  26.977  -42.886 1.00 28.06 ?  329 GLN B OE1 1 
ATOM   5655 N  NE2 . GLN B 1 327 ? 28.530  25.498  -44.347 1.00 22.31 ?  329 GLN B NE2 1 
ATOM   5656 N  N   . SER B 1 328 ? 25.958  25.858  -38.174 1.00 20.84 ?  330 SER B N   1 
ATOM   5657 C  CA  . SER B 1 328 ? 25.504  26.671  -37.046 1.00 22.08 ?  330 SER B CA  1 
ATOM   5658 C  C   . SER B 1 328 ? 25.791  26.015  -35.699 1.00 25.15 ?  330 SER B C   1 
ATOM   5659 O  O   . SER B 1 328 ? 25.947  26.714  -34.690 1.00 21.84 ?  330 SER B O   1 
ATOM   5660 C  CB  . SER B 1 328 ? 24.010  26.961  -37.188 1.00 22.10 ?  330 SER B CB  1 
ATOM   5661 O  OG  . SER B 1 328 ? 23.215  25.835  -36.836 1.00 18.24 ?  330 SER B OG  1 
ATOM   5662 N  N   . LEU B 1 329 ? 25.873  24.685  -35.656 1.00 21.58 ?  331 LEU B N   1 
ATOM   5663 C  CA  . LEU B 1 329 ? 26.082  24.014  -34.377 1.00 23.09 ?  331 LEU B CA  1 
ATOM   5664 C  C   . LEU B 1 329 ? 27.494  24.226  -33.851 1.00 19.23 ?  331 LEU B C   1 
ATOM   5665 O  O   . LEU B 1 329 ? 27.707  24.219  -32.632 1.00 24.16 ?  331 LEU B O   1 
ATOM   5666 C  CB  . LEU B 1 329 ? 25.780  22.523  -34.511 1.00 20.15 ?  331 LEU B CB  1 
ATOM   5667 C  CG  . LEU B 1 329 ? 24.301  22.205  -34.755 1.00 21.49 ?  331 LEU B CG  1 
ATOM   5668 C  CD1 . LEU B 1 329 ? 24.196  20.853  -35.422 1.00 20.11 ?  331 LEU B CD1 1 
ATOM   5669 C  CD2 . LEU B 1 329 ? 23.449  22.265  -33.481 1.00 22.91 ?  331 LEU B CD2 1 
ATOM   5670 N  N   . PHE B 1 330 ? 28.469  24.405  -34.747 1.00 20.35 ?  332 PHE B N   1 
ATOM   5671 C  CA  . PHE B 1 330 ? 29.833  24.688  -34.313 1.00 20.77 ?  332 PHE B CA  1 
ATOM   5672 C  C   . PHE B 1 330 ? 29.932  26.074  -33.692 1.00 23.97 ?  332 PHE B C   1 
ATOM   5673 O  O   . PHE B 1 330 ? 30.684  26.277  -32.732 1.00 24.90 ?  332 PHE B O   1 
ATOM   5674 C  CB  . PHE B 1 330 ? 30.788  24.557  -35.496 1.00 24.65 ?  332 PHE B CB  1 
ATOM   5675 C  CG  . PHE B 1 330 ? 30.908  23.158  -36.023 1.00 21.29 ?  332 PHE B CG  1 
ATOM   5676 C  CD1 . PHE B 1 330 ? 30.074  22.714  -37.044 1.00 21.38 ?  332 PHE B CD1 1 
ATOM   5677 C  CD2 . PHE B 1 330 ? 31.861  22.291  -35.516 1.00 20.68 ?  332 PHE B CD2 1 
ATOM   5678 C  CE1 . PHE B 1 330 ? 30.183  21.437  -37.534 1.00 21.04 ?  332 PHE B CE1 1 
ATOM   5679 C  CE2 . PHE B 1 330 ? 31.982  21.004  -36.018 1.00 17.83 ?  332 PHE B CE2 1 
ATOM   5680 C  CZ  . PHE B 1 330 ? 31.138  20.578  -37.027 1.00 16.59 ?  332 PHE B CZ  1 
ATOM   5681 N  N   . GLU B 1 331 ? 29.180  27.038  -34.232 1.00 22.95 ?  333 GLU B N   1 
ATOM   5682 C  CA  . GLU B 1 331 ? 29.118  28.372  -33.644 1.00 26.67 ?  333 GLU B CA  1 
ATOM   5683 C  C   . GLU B 1 331 ? 28.372  28.346  -32.318 1.00 22.91 ?  333 GLU B C   1 
ATOM   5684 O  O   . GLU B 1 331 ? 28.766  29.026  -31.367 1.00 26.88 ?  333 GLU B O   1 
ATOM   5685 C  CB  . GLU B 1 331 ? 28.430  29.342  -34.613 1.00 24.01 ?  333 GLU B CB  1 
ATOM   5686 C  CG  . GLU B 1 331 ? 29.058  29.420  -36.006 1.00 38.28 ?  333 GLU B CG  1 
ATOM   5687 C  CD  . GLU B 1 331 ? 28.195  30.191  -37.011 1.00 48.86 ?  333 GLU B CD  1 
ATOM   5688 O  OE1 . GLU B 1 331 ? 27.400  31.053  -36.580 1.00 57.59 ?  333 GLU B OE1 1 
ATOM   5689 O  OE2 . GLU B 1 331 ? 28.313  29.937  -38.233 1.00 50.81 ?  333 GLU B OE2 1 
ATOM   5690 N  N   . GLU B 1 332 ? 27.289  27.568  -32.242 1.00 21.08 ?  334 GLU B N   1 
ATOM   5691 C  CA  . GLU B 1 332 ? 26.462  27.511  -31.037 1.00 24.37 ?  334 GLU B CA  1 
ATOM   5692 C  C   . GLU B 1 332 ? 27.153  26.795  -29.880 1.00 27.62 ?  334 GLU B C   1 
ATOM   5693 O  O   . GLU B 1 332 ? 26.931  27.147  -28.714 1.00 21.41 ?  334 GLU B O   1 
ATOM   5694 C  CB  . GLU B 1 332 ? 25.140  26.813  -31.347 1.00 23.59 ?  334 GLU B CB  1 
ATOM   5695 C  CG  . GLU B 1 332 ? 24.178  26.777  -30.182 1.00 35.18 ?  334 GLU B CG  1 
ATOM   5696 C  CD  . GLU B 1 332 ? 22.820  26.228  -30.559 1.00 39.27 ?  334 GLU B CD  1 
ATOM   5697 O  OE1 . GLU B 1 332 ? 22.583  25.999  -31.765 1.00 50.33 ?  334 GLU B OE1 1 
ATOM   5698 O  OE2 . GLU B 1 332 ? 21.988  26.030  -29.648 1.00 39.51 ?  334 GLU B OE2 1 
ATOM   5699 N  N   . HIS B 1 333 ? 27.962  25.779  -30.169 1.00 22.78 ?  335 HIS B N   1 
ATOM   5700 C  CA  . HIS B 1 333 ? 28.621  24.977  -29.137 1.00 23.13 ?  335 HIS B CA  1 
ATOM   5701 C  C   . HIS B 1 333 ? 30.120  24.924  -29.390 1.00 23.21 ?  335 HIS B C   1 
ATOM   5702 O  O   . HIS B 1 333 ? 30.581  24.121  -30.221 1.00 27.65 ?  335 HIS B O   1 
ATOM   5703 C  CB  . HIS B 1 333 ? 28.048  23.563  -29.074 1.00 24.57 ?  335 HIS B CB  1 
ATOM   5704 C  CG  . HIS B 1 333 ? 26.554  23.512  -29.025 1.00 20.97 ?  335 HIS B CG  1 
ATOM   5705 N  ND1 . HIS B 1 333 ? 25.847  23.699  -27.856 1.00 25.12 ?  335 HIS B ND1 1 
ATOM   5706 C  CD2 . HIS B 1 333 ? 25.632  23.294  -29.990 1.00 26.32 ?  335 HIS B CD2 1 
ATOM   5707 C  CE1 . HIS B 1 333 ? 24.555  23.596  -28.104 1.00 24.93 ?  335 HIS B CE1 1 
ATOM   5708 N  NE2 . HIS B 1 333 ? 24.397  23.348  -29.391 1.00 26.91 ?  335 HIS B NE2 1 
ATOM   5709 N  N   . PRO B 1 334 ? 30.915  25.733  -28.685 1.00 27.80 ?  336 PRO B N   1 
ATOM   5710 C  CA  . PRO B 1 334 ? 32.368  25.695  -28.896 1.00 28.51 ?  336 PRO B CA  1 
ATOM   5711 C  C   . PRO B 1 334 ? 33.009  24.400  -28.445 1.00 24.52 ?  336 PRO B C   1 
ATOM   5712 O  O   . PRO B 1 334 ? 34.092  24.064  -28.938 1.00 20.90 ?  336 PRO B O   1 
ATOM   5713 C  CB  . PRO B 1 334 ? 32.880  26.885  -28.070 1.00 27.41 ?  336 PRO B CB  1 
ATOM   5714 C  CG  . PRO B 1 334 ? 31.681  27.755  -27.870 1.00 31.11 ?  336 PRO B CG  1 
ATOM   5715 C  CD  . PRO B 1 334 ? 30.527  26.811  -27.760 1.00 30.35 ?  336 PRO B CD  1 
ATOM   5716 N  N   . THR B 1 335 ? 32.391  23.662  -27.529 1.00 18.67 ?  337 THR B N   1 
ATOM   5717 C  CA  . THR B 1 335 ? 32.934  22.388  -27.093 1.00 18.77 ?  337 THR B CA  1 
ATOM   5718 C  C   . THR B 1 335 ? 32.009  21.252  -27.508 1.00 15.12 ?  337 THR B C   1 
ATOM   5719 O  O   . THR B 1 335 ? 30.782  21.397  -27.536 1.00 16.75 ?  337 THR B O   1 
ATOM   5720 C  CB  . THR B 1 335 ? 33.143  22.349  -25.577 1.00 19.86 ?  337 THR B CB  1 
ATOM   5721 O  OG1 . THR B 1 335 ? 31.868  22.341  -24.929 1.00 19.74 ?  337 THR B OG1 1 
ATOM   5722 C  CG2 . THR B 1 335 ? 33.949  23.561  -25.101 1.00 24.74 ?  337 THR B CG2 1 
ATOM   5723 N  N   . LEU B 1 336 ? 32.622  20.114  -27.842 1.00 13.19 ?  338 LEU B N   1 
ATOM   5724 C  CA  . LEU B 1 336 ? 31.838  18.916  -28.126 1.00 16.33 ?  338 LEU B CA  1 
ATOM   5725 C  C   . LEU B 1 336 ? 31.064  18.466  -26.893 1.00 15.35 ?  338 LEU B C   1 
ATOM   5726 O  O   . LEU B 1 336 ? 29.940  17.959  -27.005 1.00 13.36 ?  338 LEU B O   1 
ATOM   5727 C  CB  . LEU B 1 336 ? 32.766  17.799  -28.612 1.00 16.07 ?  338 LEU B CB  1 
ATOM   5728 C  CG  . LEU B 1 336 ? 33.136  17.914  -30.093 1.00 20.70 ?  338 LEU B CG  1 
ATOM   5729 C  CD1 . LEU B 1 336 ? 34.172  16.875  -30.467 1.00 20.26 ?  338 LEU B CD1 1 
ATOM   5730 C  CD2 . LEU B 1 336 ? 31.881  17.746  -30.927 1.00 21.25 ?  338 LEU B CD2 1 
ATOM   5731 N  N   . GLU B 1 337 ? 31.668  18.623  -25.712 1.00 12.59 ?  339 GLU B N   1 
ATOM   5732 C  CA  . GLU B 1 337 ? 31.018  18.255  -24.456 1.00 13.45 ?  339 GLU B CA  1 
ATOM   5733 C  C   . GLU B 1 337 ? 29.745  19.062  -24.230 1.00 16.07 ?  339 GLU B C   1 
ATOM   5734 O  O   . GLU B 1 337 ? 28.708  18.514  -23.842 1.00 16.19 ?  339 GLU B O   1 
ATOM   5735 C  CB  . GLU B 1 337 ? 31.999  18.467  -23.300 1.00 16.27 ?  339 GLU B CB  1 
ATOM   5736 C  CG  . GLU B 1 337 ? 33.173  17.475  -23.301 1.00 20.31 ?  339 GLU B CG  1 
ATOM   5737 C  CD  . GLU B 1 337 ? 34.322  17.900  -24.224 1.00 27.62 ?  339 GLU B CD  1 
ATOM   5738 O  OE1 . GLU B 1 337 ? 34.314  19.045  -24.726 1.00 22.77 ?  339 GLU B OE1 1 
ATOM   5739 O  OE2 . GLU B 1 337 ? 35.244  17.084  -24.438 1.00 34.25 ?  339 GLU B OE2 1 
ATOM   5740 N  N   . GLY B 1 338 ? 29.810  20.377  -24.451 1.00 16.01 ?  340 GLY B N   1 
ATOM   5741 C  CA  . GLY B 1 338 ? 28.611  21.191  -24.336 1.00 16.03 ?  340 GLY B CA  1 
ATOM   5742 C  C   . GLY B 1 338 ? 27.570  20.863  -25.390 1.00 16.15 ?  340 GLY B C   1 
ATOM   5743 O  O   . GLY B 1 338 ? 26.372  20.894  -25.116 1.00 15.93 ?  340 GLY B O   1 
ATOM   5744 N  N   . PHE B 1 339 ? 28.014  20.568  -26.617 1.00 14.49 ?  341 PHE B N   1 
ATOM   5745 C  CA  . PHE B 1 339 ? 27.094  20.140  -27.659 1.00 14.83 ?  341 PHE B CA  1 
ATOM   5746 C  C   . PHE B 1 339 ? 26.375  18.867  -27.240 1.00 14.91 ?  341 PHE B C   1 
ATOM   5747 O  O   . PHE B 1 339 ? 25.145  18.769  -27.345 1.00 12.75 ?  341 PHE B O   1 
ATOM   5748 C  CB  . PHE B 1 339 ? 27.846  19.919  -28.975 1.00 14.45 ?  341 PHE B CB  1 
ATOM   5749 C  CG  . PHE B 1 339 ? 27.074  19.100  -29.967 1.00 14.77 ?  341 PHE B CG  1 
ATOM   5750 C  CD1 . PHE B 1 339 ? 26.064  19.682  -30.720 1.00 12.70 ?  341 PHE B CD1 1 
ATOM   5751 C  CD2 . PHE B 1 339 ? 27.341  17.742  -30.132 1.00 14.75 ?  341 PHE B CD2 1 
ATOM   5752 C  CE1 . PHE B 1 339 ? 25.336  18.932  -31.638 1.00 15.34 ?  341 PHE B CE1 1 
ATOM   5753 C  CE2 . PHE B 1 339 ? 26.610  16.983  -31.031 1.00 17.08 ?  341 PHE B CE2 1 
ATOM   5754 C  CZ  . PHE B 1 339 ? 25.609  17.575  -31.789 1.00 16.60 ?  341 PHE B CZ  1 
ATOM   5755 N  N   . MET B 1 340 ? 27.138  17.880  -26.748 1.00 13.57 ?  342 MET B N   1 
ATOM   5756 C  CA  . MET B 1 340 ? 26.529  16.616  -26.354 1.00 12.37 ?  342 MET B CA  1 
ATOM   5757 C  C   . MET B 1 340 ? 25.579  16.823  -25.193 1.00 13.70 ?  342 MET B C   1 
ATOM   5758 O  O   . MET B 1 340 ? 24.500  16.220  -25.156 1.00 12.69 ?  342 MET B O   1 
ATOM   5759 C  CB  . MET B 1 340 ? 27.601  15.587  -25.967 1.00 10.90 ?  342 MET B CB  1 
ATOM   5760 C  CG  . MET B 1 340 ? 28.374  15.040  -27.170 1.00 14.52 ?  342 MET B CG  1 
ATOM   5761 S  SD  . MET B 1 340 ? 27.322  14.057  -28.269 1.00 15.23 ?  342 MET B SD  1 
ATOM   5762 C  CE  . MET B 1 340 ? 26.830  12.752  -27.145 1.00 15.33 ?  342 MET B CE  1 
ATOM   5763 N  N   . GLU B 1 341 ? 25.968  17.659  -24.225 1.00 14.02 ?  343 GLU B N   1 
ATOM   5764 C  CA  A GLU B 1 341 ? 25.068  17.911  -23.113 0.60 16.87 ?  343 GLU B CA  1 
ATOM   5765 C  CA  B GLU B 1 341 ? 25.078  17.965  -23.109 0.40 16.90 ?  343 GLU B CA  1 
ATOM   5766 C  C   . GLU B 1 341 ? 23.746  18.490  -23.608 1.00 15.84 ?  343 GLU B C   1 
ATOM   5767 O  O   . GLU B 1 341 ? 22.690  18.059  -23.145 1.00 14.85 ?  343 GLU B O   1 
ATOM   5768 C  CB  A GLU B 1 341 ? 25.775  18.815  -22.086 0.60 16.56 ?  343 GLU B CB  1 
ATOM   5769 C  CB  B GLU B 1 341 ? 25.739  18.984  -22.158 0.40 16.69 ?  343 GLU B CB  1 
ATOM   5770 C  CG  A GLU B 1 341 ? 24.881  19.338  -20.977 0.60 23.41 ?  343 GLU B CG  1 
ATOM   5771 C  CG  B GLU B 1 341 ? 24.921  19.300  -20.919 0.40 23.45 ?  343 GLU B CG  1 
ATOM   5772 C  CD  A GLU B 1 341 ? 25.241  18.716  -19.636 0.60 28.54 ?  343 GLU B CD  1 
ATOM   5773 C  CD  B GLU B 1 341 ? 25.328  18.487  -19.697 0.40 28.63 ?  343 GLU B CD  1 
ATOM   5774 O  OE1 A GLU B 1 341 ? 25.888  19.393  -18.798 0.60 43.90 ?  343 GLU B OE1 1 
ATOM   5775 O  OE1 B GLU B 1 341 ? 24.885  17.327  -19.575 0.40 43.90 ?  343 GLU B OE1 1 
ATOM   5776 O  OE2 A GLU B 1 341 ? 24.905  17.536  -19.425 0.60 43.18 ?  343 GLU B OE2 1 
ATOM   5777 O  OE2 B GLU B 1 341 ? 26.087  19.009  -18.846 0.40 43.18 ?  343 GLU B OE2 1 
ATOM   5778 N  N   . ALA B 1 342 ? 23.781  19.404  -24.577 1.00 16.10 ?  344 ALA B N   1 
ATOM   5779 C  CA  . ALA B 1 342 ? 22.549  19.947  -25.136 1.00 15.76 ?  344 ALA B CA  1 
ATOM   5780 C  C   . ALA B 1 342 ? 21.717  18.876  -25.841 1.00 15.55 ?  344 ALA B C   1 
ATOM   5781 O  O   . ALA B 1 342 ? 20.512  18.763  -25.590 1.00 18.25 ?  344 ALA B O   1 
ATOM   5782 C  CB  . ALA B 1 342 ? 22.873  21.100  -26.089 1.00 17.35 ?  344 ALA B CB  1 
ATOM   5783 N  N   . ILE B 1 343 ? 22.316  18.091  -26.745 1.00 14.08 ?  345 ILE B N   1 
ATOM   5784 C  CA  . ILE B 1 343 ? 21.447  17.258  -27.568 1.00 12.52 ?  345 ILE B CA  1 
ATOM   5785 C  C   . ILE B 1 343 ? 20.905  16.072  -26.773 1.00 13.94 ?  345 ILE B C   1 
ATOM   5786 O  O   . ILE B 1 343 ? 19.828  15.557  -27.090 1.00 16.32 ?  345 ILE B O   1 
ATOM   5787 C  CB  . ILE B 1 343 ? 22.124  16.766  -28.861 1.00 15.58 ?  345 ILE B CB  1 
ATOM   5788 C  CG1 . ILE B 1 343 ? 23.292  15.826  -28.562 1.00 18.28 ?  345 ILE B CG1 1 
ATOM   5789 C  CG2 . ILE B 1 343 ? 22.540  17.968  -29.738 1.00 14.88 ?  345 ILE B CG2 1 
ATOM   5790 C  CD1 . ILE B 1 343 ? 23.777  15.070  -29.789 1.00 21.58 ?  345 ILE B CD1 1 
ATOM   5791 N  N   . LEU B 1 344 ? 21.629  15.614  -25.743 1.00 13.95 ?  346 LEU B N   1 
ATOM   5792 C  CA  . LEU B 1 344 ? 21.155  14.488  -24.951 1.00 14.76 ?  346 LEU B CA  1 
ATOM   5793 C  C   . LEU B 1 344 ? 19.866  14.824  -24.204 1.00 19.32 ?  346 LEU B C   1 
ATOM   5794 O  O   . LEU B 1 344 ? 19.117  13.910  -23.840 1.00 20.23 ?  346 LEU B O   1 
ATOM   5795 C  CB  . LEU B 1 344 ? 22.245  14.050  -23.968 1.00 15.16 ?  346 LEU B CB  1 
ATOM   5796 C  CG  . LEU B 1 344 ? 23.392  13.239  -24.584 1.00 17.86 ?  346 LEU B CG  1 
ATOM   5797 C  CD1 . LEU B 1 344 ? 24.525  13.003  -23.573 1.00 15.48 ?  346 LEU B CD1 1 
ATOM   5798 C  CD2 . LEU B 1 344 ? 22.889  11.918  -25.116 1.00 22.34 ?  346 LEU B CD2 1 
ATOM   5799 N  N   . LYS B 1 345 ? 19.589  16.114  -23.994 1.00 17.45 ?  347 LYS B N   1 
ATOM   5800 C  CA  . LYS B 1 345 ? 18.357  16.537  -23.334 1.00 21.47 ?  347 LYS B CA  1 
ATOM   5801 C  C   . LYS B 1 345 ? 17.130  16.385  -24.225 1.00 30.02 ?  347 LYS B C   1 
ATOM   5802 O  O   . LYS B 1 345 ? 16.009  16.320  -23.707 1.00 29.03 ?  347 LYS B O   1 
ATOM   5803 C  CB  . LYS B 1 345 ? 18.481  17.993  -22.898 1.00 19.54 ?  347 LYS B CB  1 
ATOM   5804 C  CG  . LYS B 1 345 ? 19.513  18.254  -21.816 1.00 22.87 ?  347 LYS B CG  1 
ATOM   5805 C  CD  . LYS B 1 345 ? 19.785  19.743  -21.750 1.00 25.30 ?  347 LYS B CD  1 
ATOM   5806 C  CE  . LYS B 1 345 ? 20.817  20.071  -20.707 1.00 26.23 ?  347 LYS B CE  1 
ATOM   5807 N  NZ  . LYS B 1 345 ? 20.864  21.532  -20.453 1.00 23.16 ?  347 LYS B NZ  1 
ATOM   5808 N  N   . GLU B 1 346 ? 17.313  16.360  -25.547 1.00 28.35 ?  348 GLU B N   1 
ATOM   5809 C  CA  . GLU B 1 346 ? 16.210  16.239  -26.503 1.00 25.46 ?  348 GLU B CA  1 
ATOM   5810 C  C   . GLU B 1 346 ? 15.159  17.323  -26.300 1.00 29.79 ?  348 GLU B C   1 
ATOM   5811 O  O   . GLU B 1 346 ? 13.969  17.101  -26.527 1.00 28.47 ?  348 GLU B O   1 
ATOM   5812 C  CB  . GLU B 1 346 ? 15.585  14.845  -26.433 1.00 23.73 ?  348 GLU B CB  1 
ATOM   5813 C  CG  . GLU B 1 346 ? 16.626  13.764  -26.664 1.00 24.05 ?  348 GLU B CG  1 
ATOM   5814 C  CD  . GLU B 1 346 ? 16.047  12.391  -26.856 1.00 35.14 ?  348 GLU B CD  1 
ATOM   5815 O  OE1 . GLU B 1 346 ? 14.859  12.292  -27.223 1.00 42.31 ?  348 GLU B OE1 1 
ATOM   5816 O  OE2 . GLU B 1 346 ? 16.788  11.403  -26.651 1.00 32.28 ?  348 GLU B OE2 1 
ATOM   5817 N  N   . GLU B 1 347 ? 15.597  18.503  -25.862 1.00 27.51 ?  349 GLU B N   1 
ATOM   5818 C  CA  . GLU B 1 347 ? 14.721  19.658  -25.721 1.00 33.35 ?  349 GLU B CA  1 
ATOM   5819 C  C   . GLU B 1 347 ? 14.583  20.416  -27.029 1.00 37.45 ?  349 GLU B C   1 
ATOM   5820 O  O   . GLU B 1 347 ? 13.688  21.255  -27.164 1.00 38.17 ?  349 GLU B O   1 
ATOM   5821 C  CB  . GLU B 1 347 ? 15.265  20.588  -24.635 1.00 35.70 ?  349 GLU B CB  1 
ATOM   5822 C  CG  . GLU B 1 347 ? 14.878  20.165  -23.233 1.00 40.21 ?  349 GLU B CG  1 
ATOM   5823 C  CD  . GLU B 1 347 ? 15.675  20.883  -22.156 1.00 47.81 ?  349 GLU B CD  1 
ATOM   5824 O  OE1 . GLU B 1 347 ? 16.346  21.894  -22.465 1.00 48.99 ?  349 GLU B OE1 1 
ATOM   5825 O  OE2 . GLU B 1 347 ? 15.648  20.412  -20.998 1.00 47.39 ?  349 GLU B OE2 1 
ATOM   5826 N  N   . SER B 1 348 ? 15.463  20.141  -27.983 1.00 28.52 ?  350 SER B N   1 
ATOM   5827 C  CA  . SER B 1 348 ? 15.426  20.754  -29.296 1.00 31.23 ?  350 SER B CA  1 
ATOM   5828 C  C   . SER B 1 348 ? 16.137  19.805  -30.243 1.00 28.95 ?  350 SER B C   1 
ATOM   5829 O  O   . SER B 1 348 ? 16.915  18.945  -29.822 1.00 27.60 ?  350 SER B O   1 
ATOM   5830 C  CB  . SER B 1 348 ? 16.083  22.142  -29.294 1.00 28.66 ?  350 SER B CB  1 
ATOM   5831 O  OG  . SER B 1 348 ? 17.491  22.036  -29.166 1.00 42.30 ?  350 SER B OG  1 
ATOM   5832 N  N   . PHE B 1 349 ? 15.854  19.959  -31.524 1.00 20.42 ?  351 PHE B N   1 
ATOM   5833 C  CA  . PHE B 1 349 ? 16.482  19.136  -32.541 1.00 20.25 ?  351 PHE B CA  1 
ATOM   5834 C  C   . PHE B 1 349 ? 16.900  20.061  -33.665 1.00 25.32 ?  351 PHE B C   1 
ATOM   5835 O  O   . PHE B 1 349 ? 16.120  20.922  -34.080 1.00 22.16 ?  351 PHE B O   1 
ATOM   5836 C  CB  . PHE B 1 349 ? 15.526  18.057  -33.050 1.00 20.68 ?  351 PHE B CB  1 
ATOM   5837 C  CG  . PHE B 1 349 ? 15.218  16.983  -32.038 1.00 20.44 ?  351 PHE B CG  1 
ATOM   5838 C  CD1 . PHE B 1 349 ? 14.087  17.063  -31.249 1.00 27.89 ?  351 PHE B CD1 1 
ATOM   5839 C  CD2 . PHE B 1 349 ? 16.044  15.877  -31.901 1.00 23.71 ?  351 PHE B CD2 1 
ATOM   5840 C  CE1 . PHE B 1 349 ? 13.793  16.073  -30.330 1.00 20.38 ?  351 PHE B CE1 1 
ATOM   5841 C  CE2 . PHE B 1 349 ? 15.755  14.884  -30.977 1.00 22.75 ?  351 PHE B CE2 1 
ATOM   5842 C  CZ  . PHE B 1 349 ? 14.628  14.984  -30.194 1.00 26.02 ?  351 PHE B CZ  1 
ATOM   5843 N  N   . THR B 1 350 ? 18.128  19.898  -34.140 1.00 17.42 ?  352 THR B N   1 
ATOM   5844 C  CA  . THR B 1 350 ? 18.663  20.697  -35.232 1.00 18.03 ?  352 THR B CA  1 
ATOM   5845 C  C   . THR B 1 350 ? 19.020  19.758  -36.370 1.00 17.04 ?  352 THR B C   1 
ATOM   5846 O  O   . THR B 1 350 ? 19.607  18.697  -36.133 1.00 18.35 ?  352 THR B O   1 
ATOM   5847 C  CB  . THR B 1 350 ? 19.889  21.492  -34.774 1.00 19.64 ?  352 THR B CB  1 
ATOM   5848 O  OG1 . THR B 1 350 ? 19.498  22.377  -33.716 1.00 21.83 ?  352 THR B OG1 1 
ATOM   5849 C  CG2 . THR B 1 350 ? 20.498  22.293  -35.921 1.00 19.06 ?  352 THR B CG2 1 
ATOM   5850 N  N   . VAL B 1 351 ? 18.631  20.131  -37.591 1.00 16.43 ?  353 VAL B N   1 
ATOM   5851 C  CA  . VAL B 1 351 ? 18.990  19.332  -38.755 1.00 17.32 ?  353 VAL B CA  1 
ATOM   5852 C  C   . VAL B 1 351 ? 20.492  19.089  -38.749 1.00 15.61 ?  353 VAL B C   1 
ATOM   5853 O  O   . VAL B 1 351 ? 21.280  20.002  -38.485 1.00 14.77 ?  353 VAL B O   1 
ATOM   5854 C  CB  . VAL B 1 351 ? 18.542  20.042  -40.044 1.00 14.47 ?  353 VAL B CB  1 
ATOM   5855 C  CG1 . VAL B 1 351 ? 19.173  19.397  -41.275 1.00 21.68 ?  353 VAL B CG1 1 
ATOM   5856 C  CG2 . VAL B 1 351 ? 17.020  20.049  -40.150 1.00 18.01 ?  353 VAL B CG2 1 
ATOM   5857 N  N   . ASP B 1 352 ? 20.888  17.843  -39.006 1.00 15.33 ?  354 ASP B N   1 
ATOM   5858 C  CA  . ASP B 1 352 ? 22.282  17.423  -39.184 1.00 12.46 ?  354 ASP B CA  1 
ATOM   5859 C  C   . ASP B 1 352 ? 23.071  17.374  -37.878 1.00 15.17 ?  354 ASP B C   1 
ATOM   5860 O  O   . ASP B 1 352 ? 24.291  17.134  -37.911 1.00 15.62 ?  354 ASP B O   1 
ATOM   5861 C  CB  . ASP B 1 352 ? 23.000  18.303  -40.220 1.00 14.80 ?  354 ASP B CB  1 
ATOM   5862 C  CG  . ASP B 1 352 ? 22.443  18.107  -41.625 1.00 14.04 ?  354 ASP B CG  1 
ATOM   5863 O  OD1 . ASP B 1 352 ? 21.633  17.174  -41.802 1.00 20.00 ?  354 ASP B OD1 1 
ATOM   5864 O  OD2 . ASP B 1 352 ? 22.795  18.881  -42.545 1.00 16.86 ?  354 ASP B OD2 1 
ATOM   5865 N  N   . GLN B 1 353 ? 22.413  17.557  -36.720 1.00 14.53 ?  355 GLN B N   1 
ATOM   5866 C  CA  . GLN B 1 353 ? 23.128  17.449  -35.449 1.00 15.08 ?  355 GLN B CA  1 
ATOM   5867 C  C   . GLN B 1 353 ? 23.712  16.061  -35.251 1.00 13.14 ?  355 GLN B C   1 
ATOM   5868 O  O   . GLN B 1 353 ? 24.688  15.912  -34.513 1.00 12.27 ?  355 GLN B O   1 
ATOM   5869 C  CB  . GLN B 1 353 ? 22.216  17.778  -34.258 1.00 16.33 ?  355 GLN B CB  1 
ATOM   5870 C  CG  . GLN B 1 353 ? 21.119  16.737  -33.983 1.00 14.18 ?  355 GLN B CG  1 
ATOM   5871 C  CD  . GLN B 1 353 ? 20.293  17.068  -32.742 1.00 19.54 ?  355 GLN B CD  1 
ATOM   5872 O  OE1 . GLN B 1 353 ? 19.924  18.224  -32.522 1.00 18.32 ?  355 GLN B OE1 1 
ATOM   5873 N  NE2 . GLN B 1 353 ? 20.005  16.052  -31.924 1.00 14.61 ?  355 GLN B NE2 1 
ATOM   5874 N  N   . TRP B 1 354 ? 23.138  15.053  -35.906 1.00 13.37 ?  356 TRP B N   1 
ATOM   5875 C  CA  . TRP B 1 354 ? 23.587  13.682  -35.709 1.00 15.22 ?  356 TRP B CA  1 
ATOM   5876 C  C   . TRP B 1 354 ? 25.040  13.469  -36.147 1.00 14.66 ?  356 TRP B C   1 
ATOM   5877 O  O   . TRP B 1 354 ? 25.738  12.639  -35.553 1.00 12.91 ?  356 TRP B O   1 
ATOM   5878 C  CB  . TRP B 1 354 ? 22.641  12.726  -36.437 1.00 11.77 ?  356 TRP B CB  1 
ATOM   5879 C  CG  . TRP B 1 354 ? 22.142  13.254  -37.750 1.00 13.29 ?  356 TRP B CG  1 
ATOM   5880 C  CD1 . TRP B 1 354 ? 22.776  13.185  -38.948 1.00 15.04 ?  356 TRP B CD1 1 
ATOM   5881 C  CD2 . TRP B 1 354 ? 20.885  13.904  -37.996 1.00 15.91 ?  356 TRP B CD2 1 
ATOM   5882 N  NE1 . TRP B 1 354 ? 22.019  13.774  -39.925 1.00 14.43 ?  356 TRP B NE1 1 
ATOM   5883 C  CE2 . TRP B 1 354 ? 20.841  14.210  -39.373 1.00 16.07 ?  356 TRP B CE2 1 
ATOM   5884 C  CE3 . TRP B 1 354 ? 19.797  14.261  -37.186 1.00 15.80 ?  356 TRP B CE3 1 
ATOM   5885 C  CZ2 . TRP B 1 354 ? 19.760  14.873  -39.962 1.00 15.97 ?  356 TRP B CZ2 1 
ATOM   5886 C  CZ3 . TRP B 1 354 ? 18.712  14.910  -37.775 1.00 17.68 ?  356 TRP B CZ3 1 
ATOM   5887 C  CH2 . TRP B 1 354 ? 18.700  15.198  -39.156 1.00 14.44 ?  356 TRP B CH2 1 
ATOM   5888 N  N   . GLN B 1 355 ? 25.532  14.199  -37.164 1.00 14.08 ?  357 GLN B N   1 
ATOM   5889 C  CA  A GLN B 1 355 ? 26.924  14.007  -37.571 0.50 12.41 ?  357 GLN B CA  1 
ATOM   5890 C  CA  B GLN B 1 355 ? 26.919  14.006  -37.568 0.50 12.41 ?  357 GLN B CA  1 
ATOM   5891 C  C   . GLN B 1 355 ? 27.913  14.672  -36.627 1.00 13.54 ?  357 GLN B C   1 
ATOM   5892 O  O   . GLN B 1 355 ? 29.036  14.180  -36.483 1.00 12.24 ?  357 GLN B O   1 
ATOM   5893 C  CB  A GLN B 1 355 ? 27.183  14.501  -38.994 0.50 14.82 ?  357 GLN B CB  1 
ATOM   5894 C  CB  B GLN B 1 355 ? 27.138  14.484  -38.999 0.50 14.82 ?  357 GLN B CB  1 
ATOM   5895 C  CG  A GLN B 1 355 ? 26.813  13.484  -40.032 0.50 13.50 ?  357 GLN B CG  1 
ATOM   5896 C  CG  B GLN B 1 355 ? 28.308  13.775  -39.650 0.50 13.40 ?  357 GLN B CG  1 
ATOM   5897 C  CD  A GLN B 1 355 ? 27.606  12.194  -39.874 0.50 15.40 ?  357 GLN B CD  1 
ATOM   5898 C  CD  B GLN B 1 355 ? 28.046  12.309  -39.986 0.50 15.96 ?  357 GLN B CD  1 
ATOM   5899 O  OE1 A GLN B 1 355 ? 27.167  11.278  -39.178 0.50 13.94 ?  357 GLN B OE1 1 
ATOM   5900 O  OE1 B GLN B 1 355 ? 27.270  11.626  -39.312 0.50 13.65 ?  357 GLN B OE1 1 
ATOM   5901 N  NE2 A GLN B 1 355 ? 28.763  12.104  -40.541 0.50 15.26 ?  357 GLN B NE2 1 
ATOM   5902 N  NE2 B GLN B 1 355 ? 28.738  11.808  -41.011 0.50 13.01 ?  357 GLN B NE2 1 
ATOM   5903 N  N   . LEU B 1 356 ? 27.538  15.776  -35.981 1.00 12.80 ?  358 LEU B N   1 
ATOM   5904 C  CA  . LEU B 1 356 ? 28.415  16.278  -34.932 1.00 12.28 ?  358 LEU B CA  1 
ATOM   5905 C  C   . LEU B 1 356 ? 28.435  15.307  -33.757 1.00 12.61 ?  358 LEU B C   1 
ATOM   5906 O  O   . LEU B 1 356 ? 29.469  15.147  -33.096 1.00 12.67 ?  358 LEU B O   1 
ATOM   5907 C  CB  . LEU B 1 356 ? 27.970  17.674  -34.491 1.00 12.93 ?  358 LEU B CB  1 
ATOM   5908 C  CG  . LEU B 1 356 ? 28.898  18.541  -33.639 1.00 18.38 ?  358 LEU B CG  1 
ATOM   5909 C  CD1 . LEU B 1 356 ? 30.353  18.455  -34.083 1.00 19.86 ?  358 LEU B CD1 1 
ATOM   5910 C  CD2 . LEU B 1 356 ? 28.417  19.994  -33.661 1.00 19.00 ?  358 LEU B CD2 1 
ATOM   5911 N  N   . GLU B 1 357 ? 27.317  14.615  -33.514 1.00 13.54 ?  359 GLU B N   1 
ATOM   5912 C  CA  . GLU B 1 357 ? 27.308  13.587  -32.480 1.00 11.93 ?  359 GLU B CA  1 
ATOM   5913 C  C   . GLU B 1 357 ? 28.247  12.442  -32.847 1.00 11.39 ?  359 GLU B C   1 
ATOM   5914 O  O   . GLU B 1 357 ? 28.955  11.905  -31.983 1.00 11.74 ?  359 GLU B O   1 
ATOM   5915 C  CB  . GLU B 1 357 ? 25.882  13.083  -32.263 1.00 12.86 ?  359 GLU B CB  1 
ATOM   5916 C  CG  . GLU B 1 357 ? 25.767  11.951  -31.277 1.00 9.96  ?  359 GLU B CG  1 
ATOM   5917 C  CD  . GLU B 1 357 ? 24.310  11.547  -31.037 1.00 17.31 ?  359 GLU B CD  1 
ATOM   5918 O  OE1 . GLU B 1 357 ? 24.068  10.638  -30.211 1.00 18.74 ?  359 GLU B OE1 1 
ATOM   5919 O  OE2 . GLU B 1 357 ? 23.408  12.129  -31.685 1.00 18.11 ?  359 GLU B OE2 1 
ATOM   5920 N  N   . GLU B 1 358 ? 28.291  12.072  -34.131 1.00 10.39 ?  360 GLU B N   1 
ATOM   5921 C  CA  . GLU B 1 358 ? 29.240  11.042  -34.557 1.00 10.30 ?  360 GLU B CA  1 
ATOM   5922 C  C   . GLU B 1 358 ? 30.679  11.529  -34.425 1.00 9.91  ?  360 GLU B C   1 
ATOM   5923 O  O   . GLU B 1 358 ? 31.568  10.752  -34.064 1.00 9.74  ?  360 GLU B O   1 
ATOM   5924 C  CB  . GLU B 1 358 ? 28.944  10.599  -35.995 1.00 11.47 ?  360 GLU B CB  1 
ATOM   5925 C  CG  . GLU B 1 358 ? 27.591  9.921   -36.165 1.00 9.52  ?  360 GLU B CG  1 
ATOM   5926 C  CD  . GLU B 1 358 ? 27.549  8.527   -35.566 1.00 15.17 ?  360 GLU B CD  1 
ATOM   5927 O  OE1 . GLU B 1 358 ? 26.421  7.992   -35.385 1.00 14.41 ?  360 GLU B OE1 1 
ATOM   5928 O  OE2 . GLU B 1 358 ? 28.637  7.971   -35.283 1.00 13.21 ?  360 GLU B OE2 1 
ATOM   5929 N  N   . LEU B 1 359 ? 30.932  12.809  -34.714 1.00 10.37 ?  361 LEU B N   1 
ATOM   5930 C  CA  . LEU B 1 359 ? 32.283  13.335  -34.538 1.00 10.44 ?  361 LEU B CA  1 
ATOM   5931 C  C   . LEU B 1 359 ? 32.680  13.315  -33.068 1.00 10.88 ?  361 LEU B C   1 
ATOM   5932 O  O   . LEU B 1 359 ? 33.838  13.054  -32.740 1.00 11.62 ?  361 LEU B O   1 
ATOM   5933 C  CB  . LEU B 1 359 ? 32.375  14.750  -35.112 1.00 9.86  ?  361 LEU B CB  1 
ATOM   5934 C  CG  . LEU B 1 359 ? 33.720  15.475  -34.980 1.00 13.38 ?  361 LEU B CG  1 
ATOM   5935 C  CD1 . LEU B 1 359 ? 34.830  14.730  -35.716 1.00 10.64 ?  361 LEU B CD1 1 
ATOM   5936 C  CD2 . LEU B 1 359 ? 33.604  16.900  -35.494 1.00 13.12 ?  361 LEU B CD2 1 
ATOM   5937 N  N   . ALA B 1 360 ? 31.722  13.553  -32.165 1.00 10.82 ?  362 ALA B N   1 
ATOM   5938 C  CA  . ALA B 1 360 ? 32.033  13.454  -30.742 1.00 12.16 ?  362 ALA B CA  1 
ATOM   5939 C  C   . ALA B 1 360 ? 32.409  12.028  -30.352 1.00 12.95 ?  362 ALA B C   1 
ATOM   5940 O  O   . ALA B 1 360 ? 33.336  11.822  -29.558 1.00 12.69 ?  362 ALA B O   1 
ATOM   5941 C  CB  . ALA B 1 360 ? 30.850  13.955  -29.902 1.00 13.73 ?  362 ALA B CB  1 
ATOM   5942 N  N   . LYS B 1 361 ? 31.707  11.033  -30.913 1.00 10.34 ?  363 LYS B N   1 
ATOM   5943 C  CA  . LYS B 1 361 ? 32.056  9.628   -30.692 1.00 12.74 ?  363 LYS B CA  1 
ATOM   5944 C  C   . LYS B 1 361 ? 33.489  9.325   -31.145 1.00 12.87 ?  363 LYS B C   1 
ATOM   5945 O  O   . LYS B 1 361 ? 34.211  8.580   -30.473 1.00 12.73 ?  363 LYS B O   1 
ATOM   5946 C  CB  . LYS B 1 361 ? 31.037  8.732   -31.418 1.00 13.30 ?  363 LYS B CB  1 
ATOM   5947 C  CG  . LYS B 1 361 ? 31.387  7.252   -31.510 1.00 14.98 ?  363 LYS B CG  1 
ATOM   5948 C  CD  . LYS B 1 361 ? 30.194  6.490   -32.135 1.00 15.51 ?  363 LYS B CD  1 
ATOM   5949 C  CE  . LYS B 1 361 ? 30.529  5.053   -32.527 1.00 18.82 ?  363 LYS B CE  1 
ATOM   5950 N  NZ  . LYS B 1 361 ? 29.301  4.278   -32.971 1.00 17.28 ?  363 LYS B NZ  1 
ATOM   5951 N  N   . VAL B 1 362 ? 33.930  9.916   -32.265 1.00 8.91  ?  364 VAL B N   1 
ATOM   5952 C  CA  . VAL B 1 362 ? 35.320  9.756   -32.710 1.00 7.68  ?  364 VAL B CA  1 
ATOM   5953 C  C   . VAL B 1 362 ? 36.287  10.364  -31.692 1.00 8.92  ?  364 VAL B C   1 
ATOM   5954 O  O   . VAL B 1 362 ? 37.292  9.747   -31.303 1.00 11.22 ?  364 VAL B O   1 
ATOM   5955 C  CB  . VAL B 1 362 ? 35.519  10.387  -34.106 1.00 10.34 ?  364 VAL B CB  1 
ATOM   5956 C  CG1 . VAL B 1 362 ? 37.017  10.377  -34.505 1.00 10.99 ?  364 VAL B CG1 1 
ATOM   5957 C  CG2 . VAL B 1 362 ? 34.691  9.659   -35.157 1.00 11.72 ?  364 VAL B CG2 1 
ATOM   5958 N  N   . ARG B 1 363 ? 36.014  11.606  -31.279 1.00 10.12 ?  365 ARG B N   1 
ATOM   5959 C  CA  . ARG B 1 363 ? 36.973  12.362  -30.475 1.00 14.38 ?  365 ARG B CA  1 
ATOM   5960 C  C   . ARG B 1 363 ? 37.068  11.863  -29.045 1.00 13.49 ?  365 ARG B C   1 
ATOM   5961 O  O   . ARG B 1 363 ? 38.057  12.175  -28.376 1.00 15.17 ?  365 ARG B O   1 
ATOM   5962 C  CB  . ARG B 1 363 ? 36.615  13.845  -30.493 1.00 11.41 ?  365 ARG B CB  1 
ATOM   5963 C  CG  . ARG B 1 363 ? 36.765  14.530  -31.862 1.00 13.55 ?  365 ARG B CG  1 
ATOM   5964 C  CD  . ARG B 1 363 ? 38.217  14.447  -32.410 1.00 18.72 ?  365 ARG B CD  1 
ATOM   5965 N  NE  . ARG B 1 363 ? 38.974  15.635  -31.984 1.00 25.20 ?  365 ARG B NE  1 
ATOM   5966 C  CZ  . ARG B 1 363 ? 39.856  15.650  -30.990 1.00 24.72 ?  365 ARG B CZ  1 
ATOM   5967 N  NH1 . ARG B 1 363 ? 40.167  14.547  -30.335 1.00 25.89 ?  365 ARG B NH1 1 
ATOM   5968 N  NH2 . ARG B 1 363 ? 40.476  16.770  -30.676 1.00 34.37 ?  365 ARG B NH2 1 
ATOM   5969 N  N   . ARG B 1 364 ? 36.075  11.105  -28.568 1.00 15.10 ?  366 ARG B N   1 
ATOM   5970 C  CA  . ARG B 1 364 ? 36.212  10.442  -27.272 1.00 16.56 ?  366 ARG B CA  1 
ATOM   5971 C  C   . ARG B 1 364 ? 37.315  9.405   -27.288 1.00 15.70 ?  366 ARG B C   1 
ATOM   5972 O  O   . ARG B 1 364 ? 37.879  9.081   -26.234 1.00 17.93 ?  366 ARG B O   1 
ATOM   5973 C  CB  . ARG B 1 364 ? 34.917  9.733   -26.862 1.00 17.92 ?  366 ARG B CB  1 
ATOM   5974 C  CG  . ARG B 1 364 ? 33.783  10.643  -26.562 1.00 23.67 ?  366 ARG B CG  1 
ATOM   5975 C  CD  . ARG B 1 364 ? 32.646  9.923   -25.848 1.00 22.47 ?  366 ARG B CD  1 
ATOM   5976 N  NE  . ARG B 1 364 ? 31.965  8.931   -26.673 1.00 26.09 ?  366 ARG B NE  1 
ATOM   5977 C  CZ  . ARG B 1 364 ? 30.834  9.182   -27.328 1.00 19.88 ?  366 ARG B CZ  1 
ATOM   5978 N  NH1 . ARG B 1 364 ? 30.330  10.402  -27.305 1.00 17.81 ?  366 ARG B NH1 1 
ATOM   5979 N  NH2 . ARG B 1 364 ? 30.246  8.236   -28.048 1.00 22.51 ?  366 ARG B NH2 1 
ATOM   5980 N  N   . LYS B 1 365 ? 37.607  8.844   -28.455 1.00 13.68 ?  367 LYS B N   1 
ATOM   5981 C  CA  . LYS B 1 365 ? 38.578  7.768   -28.579 1.00 12.87 ?  367 LYS B CA  1 
ATOM   5982 C  C   . LYS B 1 365 ? 39.898  8.203   -29.196 1.00 14.03 ?  367 LYS B C   1 
ATOM   5983 O  O   . LYS B 1 365 ? 40.947  7.715   -28.774 1.00 15.97 ?  367 LYS B O   1 
ATOM   5984 C  CB  . LYS B 1 365 ? 37.984  6.618   -29.409 1.00 13.86 ?  367 LYS B CB  1 
ATOM   5985 C  CG  . LYS B 1 365 ? 38.901  5.409   -29.495 1.00 12.07 ?  367 LYS B CG  1 
ATOM   5986 C  CD  . LYS B 1 365 ? 38.258  4.249   -30.238 1.00 18.01 ?  367 LYS B CD  1 
ATOM   5987 C  CE  . LYS B 1 365 ? 39.044  2.973   -30.009 1.00 18.03 ?  367 LYS B CE  1 
ATOM   5988 N  NZ  . LYS B 1 365 ? 38.433  1.856   -30.785 1.00 19.00 ?  367 LYS B NZ  1 
ATOM   5989 N  N   . ALA B 1 366 ? 39.897  9.130   -30.159 1.00 13.17 ?  368 ALA B N   1 
ATOM   5990 C  CA  . ALA B 1 366 ? 41.076  9.334   -30.994 1.00 12.24 ?  368 ALA B CA  1 
ATOM   5991 C  C   . ALA B 1 366 ? 41.288  10.810  -31.315 1.00 10.58 ?  368 ALA B C   1 
ATOM   5992 O  O   . ALA B 1 366 ? 40.331  11.587  -31.416 1.00 13.75 ?  368 ALA B O   1 
ATOM   5993 C  CB  . ALA B 1 366 ? 40.941  8.527   -32.304 1.00 10.57 ?  368 ALA B CB  1 
ATOM   5994 N  N   . ARG B 1 367 ? 42.559  11.179  -31.489 1.00 9.96  ?  369 ARG B N   1 
ATOM   5995 C  CA  . ARG B 1 367 ? 42.920  12.439  -32.131 1.00 9.83  ?  369 ARG B CA  1 
ATOM   5996 C  C   . ARG B 1 367 ? 42.633  12.351  -33.624 1.00 11.90 ?  369 ARG B C   1 
ATOM   5997 O  O   . ARG B 1 367 ? 42.693  11.272  -34.217 1.00 11.30 ?  369 ARG B O   1 
ATOM   5998 C  CB  . ARG B 1 367 ? 44.414  12.743  -31.941 1.00 10.57 ?  369 ARG B CB  1 
ATOM   5999 C  CG  . ARG B 1 367 ? 44.900  12.647  -30.499 1.00 11.02 ?  369 ARG B CG  1 
ATOM   6000 C  CD  . ARG B 1 367 ? 46.317  13.221  -30.324 1.00 12.85 ?  369 ARG B CD  1 
ATOM   6001 N  NE  . ARG B 1 367 ? 46.687  13.257  -28.909 1.00 14.66 ?  369 ARG B NE  1 
ATOM   6002 C  CZ  . ARG B 1 367 ? 47.573  14.100  -28.379 1.00 15.34 ?  369 ARG B CZ  1 
ATOM   6003 N  NH1 . ARG B 1 367 ? 48.202  14.971  -29.153 1.00 12.37 ?  369 ARG B NH1 1 
ATOM   6004 N  NH2 . ARG B 1 367 ? 47.826  14.073  -27.073 1.00 13.69 ?  369 ARG B NH2 1 
ATOM   6005 N  N   . VAL B 1 368 ? 42.357  13.501  -34.240 1.00 10.77 ?  370 VAL B N   1 
ATOM   6006 C  CA  . VAL B 1 368 ? 42.070  13.560  -35.673 1.00 10.27 ?  370 VAL B CA  1 
ATOM   6007 C  C   . VAL B 1 368 ? 42.937  14.643  -36.307 1.00 11.20 ?  370 VAL B C   1 
ATOM   6008 O  O   . VAL B 1 368 ? 42.851  15.819  -35.925 1.00 11.57 ?  370 VAL B O   1 
ATOM   6009 C  CB  . VAL B 1 368 ? 40.583  13.840  -35.959 1.00 11.05 ?  370 VAL B CB  1 
ATOM   6010 C  CG1 . VAL B 1 368 ? 40.369  14.049  -37.476 1.00 10.65 ?  370 VAL B CG1 1 
ATOM   6011 C  CG2 . VAL B 1 368 ? 39.711  12.708  -35.457 1.00 11.18 ?  370 VAL B CG2 1 
ATOM   6012 N  N   . LYS B 1 369 ? 43.732  14.254  -37.301 1.00 11.28 ?  371 LYS B N   1 
ATOM   6013 C  CA  . LYS B 1 369 ? 44.455  15.181  -38.159 1.00 7.16  ?  371 LYS B CA  1 
ATOM   6014 C  C   . LYS B 1 369 ? 43.758  15.160  -39.511 1.00 10.40 ?  371 LYS B C   1 
ATOM   6015 O  O   . LYS B 1 369 ? 43.535  14.082  -40.068 1.00 11.60 ?  371 LYS B O   1 
ATOM   6016 C  CB  . LYS B 1 369 ? 45.927  14.786  -38.287 1.00 9.17  ?  371 LYS B CB  1 
ATOM   6017 C  CG  . LYS B 1 369 ? 46.721  15.016  -37.001 1.00 10.17 ?  371 LYS B CG  1 
ATOM   6018 C  CD  . LYS B 1 369 ? 48.121  14.438  -37.085 1.00 9.62  ?  371 LYS B CD  1 
ATOM   6019 C  CE  . LYS B 1 369 ? 48.890  14.635  -35.769 1.00 13.57 ?  371 LYS B CE  1 
ATOM   6020 N  NZ  . LYS B 1 369 ? 49.322  16.062  -35.589 1.00 14.67 ?  371 LYS B NZ  1 
ATOM   6021 N  N   . PHE B 1 370 ? 43.369  16.334  -40.007 1.00 9.48  ?  372 PHE B N   1 
ATOM   6022 C  CA  A PHE B 1 370 ? 42.533  16.448  -41.196 0.50 10.40 ?  372 PHE B CA  1 
ATOM   6023 C  CA  B PHE B 1 370 ? 42.529  16.454  -41.194 0.50 10.40 ?  372 PHE B CA  1 
ATOM   6024 C  C   . PHE B 1 370 ? 43.293  17.160  -42.306 1.00 9.59  ?  372 PHE B C   1 
ATOM   6025 O  O   . PHE B 1 370 ? 43.805  18.269  -42.109 1.00 12.44 ?  372 PHE B O   1 
ATOM   6026 C  CB  A PHE B 1 370 ? 41.221  17.174  -40.873 0.50 10.07 ?  372 PHE B CB  1 
ATOM   6027 C  CB  B PHE B 1 370 ? 41.230  17.204  -40.874 0.50 10.06 ?  372 PHE B CB  1 
ATOM   6028 C  CG  A PHE B 1 370 ? 40.071  16.743  -41.737 0.50 10.44 ?  372 PHE B CG  1 
ATOM   6029 C  CG  B PHE B 1 370 ? 40.081  16.819  -41.762 0.50 10.44 ?  372 PHE B CG  1 
ATOM   6030 C  CD1 A PHE B 1 370 ? 38.945  16.161  -41.177 0.50 9.98  ?  372 PHE B CD1 1 
ATOM   6031 C  CD1 B PHE B 1 370 ? 38.993  16.131  -41.249 0.50 9.96  ?  372 PHE B CD1 1 
ATOM   6032 C  CD2 A PHE B 1 370 ? 40.107  16.947  -43.109 0.50 10.88 ?  372 PHE B CD2 1 
ATOM   6033 C  CD2 B PHE B 1 370 ? 40.091  17.149  -43.109 0.50 10.73 ?  372 PHE B CD2 1 
ATOM   6034 C  CE1 A PHE B 1 370 ? 37.876  15.762  -41.978 0.50 11.47 ?  372 PHE B CE1 1 
ATOM   6035 C  CE1 B PHE B 1 370 ? 37.928  15.767  -42.072 0.50 11.49 ?  372 PHE B CE1 1 
ATOM   6036 C  CE2 A PHE B 1 370 ? 39.052  16.554  -43.917 0.50 12.21 ?  372 PHE B CE2 1 
ATOM   6037 C  CE2 B PHE B 1 370 ? 39.040  16.791  -43.938 0.50 12.19 ?  372 PHE B CE2 1 
ATOM   6038 C  CZ  A PHE B 1 370 ? 37.929  15.961  -43.350 0.50 9.75  ?  372 PHE B CZ  1 
ATOM   6039 C  CZ  B PHE B 1 370 ? 37.951  16.099  -43.417 0.50 9.75  ?  372 PHE B CZ  1 
ATOM   6040 N  N   . VAL B 1 371 ? 43.369  16.514  -43.470 1.00 9.60  ?  373 VAL B N   1 
ATOM   6041 C  CA  . VAL B 1 371 ? 44.131  17.015  -44.613 1.00 9.45  ?  373 VAL B CA  1 
ATOM   6042 C  C   . VAL B 1 371 ? 43.168  17.291  -45.760 1.00 13.10 ?  373 VAL B C   1 
ATOM   6043 O  O   . VAL B 1 371 ? 42.545  16.365  -46.290 1.00 11.63 ?  373 VAL B O   1 
ATOM   6044 C  CB  . VAL B 1 371 ? 45.222  16.027  -45.047 1.00 12.10 ?  373 VAL B CB  1 
ATOM   6045 C  CG1 . VAL B 1 371 ? 46.011  16.597  -46.244 1.00 15.75 ?  373 VAL B CG1 1 
ATOM   6046 C  CG2 . VAL B 1 371 ? 46.151  15.718  -43.874 1.00 10.57 ?  373 VAL B CG2 1 
ATOM   6047 N  N   . SER B 1 372 ? 43.058  18.559  -46.153 1.00 13.75 ?  374 SER B N   1 
ATOM   6048 C  CA  . SER B 1 372 ? 42.123  18.949  -47.205 1.00 12.21 ?  374 SER B CA  1 
ATOM   6049 C  C   . SER B 1 372 ? 42.571  20.278  -47.795 1.00 16.55 ?  374 SER B C   1 
ATOM   6050 O  O   . SER B 1 372 ? 43.097  21.132  -47.082 1.00 15.85 ?  374 SER B O   1 
ATOM   6051 C  CB  . SER B 1 372 ? 40.695  19.092  -46.670 1.00 13.15 ?  374 SER B CB  1 
ATOM   6052 O  OG  . SER B 1 372 ? 39.789  19.438  -47.716 1.00 12.55 ?  374 SER B OG  1 
ATOM   6053 N  N   . ASP B 1 373 ? 42.330  20.468  -49.091 1.00 13.26 ?  375 ASP B N   1 
ATOM   6054 C  CA  . ASP B 1 373 ? 42.449  21.812  -49.644 1.00 18.33 ?  375 ASP B CA  1 
ATOM   6055 C  C   . ASP B 1 373 ? 41.091  22.384  -50.032 1.00 18.22 ?  375 ASP B C   1 
ATOM   6056 O  O   . ASP B 1 373 ? 41.028  23.373  -50.768 1.00 20.91 ?  375 ASP B O   1 
ATOM   6057 C  CB  . ASP B 1 373 ? 43.431  21.847  -50.825 1.00 17.78 ?  375 ASP B CB  1 
ATOM   6058 C  CG  . ASP B 1 373 ? 43.075  20.886  -51.942 1.00 22.03 ?  375 ASP B CG  1 
ATOM   6059 O  OD1 . ASP B 1 373 ? 42.090  20.134  -51.837 1.00 19.52 ?  375 ASP B OD1 1 
ATOM   6060 O  OD2 . ASP B 1 373 ? 43.816  20.880  -52.942 1.00 24.73 ?  375 ASP B OD2 1 
ATOM   6061 N  N   . GLY B 1 374 ? 40.000  21.796  -49.536 1.00 14.97 ?  376 GLY B N   1 
ATOM   6062 C  CA  . GLY B 1 374 ? 38.669  22.289  -49.856 1.00 15.11 ?  376 GLY B CA  1 
ATOM   6063 C  C   . GLY B 1 374 ? 38.112  23.293  -48.858 1.00 21.14 ?  376 GLY B C   1 
ATOM   6064 O  O   . GLY B 1 374 ? 37.150  24.013  -49.149 1.00 20.63 ?  376 GLY B O   1 
ATOM   6065 N  N   . VAL B 1 375 ? 38.712  23.346  -47.673 1.00 18.27 ?  377 VAL B N   1 
ATOM   6066 C  CA  . VAL B 1 375 ? 38.249  24.172  -46.560 1.00 18.06 ?  377 VAL B CA  1 
ATOM   6067 C  C   . VAL B 1 375 ? 39.497  24.765  -45.911 1.00 21.25 ?  377 VAL B C   1 
ATOM   6068 O  O   . VAL B 1 375 ? 40.476  24.034  -45.711 1.00 22.49 ?  377 VAL B O   1 
ATOM   6069 C  CB  . VAL B 1 375 ? 37.431  23.336  -45.560 1.00 19.93 ?  377 VAL B CB  1 
ATOM   6070 C  CG1 . VAL B 1 375 ? 37.245  24.078  -44.239 1.00 21.76 ?  377 VAL B CG1 1 
ATOM   6071 C  CG2 . VAL B 1 375 ? 36.071  22.919  -46.170 1.00 20.99 ?  377 VAL B CG2 1 
ATOM   6072 N  N   . PRO B 1 376 ? 39.528  26.060  -45.589 1.00 21.43 ?  378 PRO B N   1 
ATOM   6073 C  CA  . PRO B 1 376 ? 40.747  26.641  -45.009 1.00 17.27 ?  378 PRO B CA  1 
ATOM   6074 C  C   . PRO B 1 376 ? 41.062  26.041  -43.647 1.00 18.39 ?  378 PRO B C   1 
ATOM   6075 O  O   . PRO B 1 376 ? 40.165  25.676  -42.883 1.00 19.99 ?  378 PRO B O   1 
ATOM   6076 C  CB  . PRO B 1 376 ? 40.400  28.130  -44.878 1.00 23.42 ?  378 PRO B CB  1 
ATOM   6077 C  CG  . PRO B 1 376 ? 39.300  28.346  -45.864 1.00 24.05 ?  378 PRO B CG  1 
ATOM   6078 C  CD  . PRO B 1 376 ? 38.493  27.085  -45.792 1.00 23.47 ?  378 PRO B CD  1 
ATOM   6079 N  N   . ALA B 1 377 ? 42.363  25.989  -43.331 1.00 18.72 ?  379 ALA B N   1 
ATOM   6080 C  CA  . ALA B 1 377 ? 42.801  25.466  -42.039 1.00 21.91 ?  379 ALA B CA  1 
ATOM   6081 C  C   . ALA B 1 377 ? 42.084  26.148  -40.881 1.00 23.59 ?  379 ALA B C   1 
ATOM   6082 O  O   . ALA B 1 377 ? 41.681  25.489  -39.914 1.00 17.85 ?  379 ALA B O   1 
ATOM   6083 C  CB  . ALA B 1 377 ? 44.318  25.625  -41.894 1.00 17.79 ?  379 ALA B CB  1 
ATOM   6084 N  N   . ALA B 1 378 ? 41.895  27.472  -40.973 1.00 24.99 ?  380 ALA B N   1 
ATOM   6085 C  CA  . ALA B 1 378 ? 41.282  28.217  -39.876 1.00 24.57 ?  380 ALA B CA  1 
ATOM   6086 C  C   . ALA B 1 378 ? 39.841  27.791  -39.642 1.00 24.68 ?  380 ALA B C   1 
ATOM   6087 O  O   . ALA B 1 378 ? 39.346  27.881  -38.512 1.00 23.14 ?  380 ALA B O   1 
ATOM   6088 C  CB  . ALA B 1 378 ? 41.347  29.723  -40.148 1.00 25.91 ?  380 ALA B CB  1 
ATOM   6089 N  N   . VAL B 1 379 ? 39.156  27.330  -40.693 1.00 19.26 ?  381 VAL B N   1 
ATOM   6090 C  CA  . VAL B 1 379 ? 37.808  26.794  -40.535 1.00 20.80 ?  381 VAL B CA  1 
ATOM   6091 C  C   . VAL B 1 379 ? 37.855  25.402  -39.917 1.00 19.98 ?  381 VAL B C   1 
ATOM   6092 O  O   . VAL B 1 379 ? 37.133  25.108  -38.955 1.00 19.96 ?  381 VAL B O   1 
ATOM   6093 C  CB  . VAL B 1 379 ? 37.076  26.784  -41.888 1.00 24.14 ?  381 VAL B CB  1 
ATOM   6094 C  CG1 . VAL B 1 379 ? 35.659  26.249  -41.720 1.00 23.61 ?  381 VAL B CG1 1 
ATOM   6095 C  CG2 . VAL B 1 379 ? 37.047  28.187  -42.485 1.00 25.40 ?  381 VAL B CG2 1 
ATOM   6096 N  N   . LEU B 1 380 ? 38.716  24.526  -40.450 1.00 16.84 ?  382 LEU B N   1 
ATOM   6097 C  CA  . LEU B 1 380 ? 38.767  23.154  -39.940 1.00 14.88 ?  382 LEU B CA  1 
ATOM   6098 C  C   . LEU B 1 380 ? 39.153  23.127  -38.467 1.00 17.70 ?  382 LEU B C   1 
ATOM   6099 O  O   . LEU B 1 380 ? 38.658  22.294  -37.696 1.00 15.44 ?  382 LEU B O   1 
ATOM   6100 C  CB  . LEU B 1 380 ? 39.758  22.336  -40.761 1.00 16.05 ?  382 LEU B CB  1 
ATOM   6101 C  CG  . LEU B 1 380 ? 39.281  21.814  -42.115 1.00 18.51 ?  382 LEU B CG  1 
ATOM   6102 C  CD1 . LEU B 1 380 ? 40.427  21.119  -42.851 1.00 18.57 ?  382 LEU B CD1 1 
ATOM   6103 C  CD2 . LEU B 1 380 ? 38.073  20.893  -41.973 1.00 15.60 ?  382 LEU B CD2 1 
ATOM   6104 N  N   . SER B 1 381 ? 40.032  24.044  -38.055 1.00 16.59 ?  383 SER B N   1 
ATOM   6105 C  CA  . SER B 1 381 ? 40.486  24.053  -36.672 1.00 17.57 ?  383 SER B CA  1 
ATOM   6106 C  C   . SER B 1 381 ? 39.352  24.365  -35.711 1.00 17.50 ?  383 SER B C   1 
ATOM   6107 O  O   . SER B 1 381 ? 39.489  24.117  -34.508 1.00 20.94 ?  383 SER B O   1 
ATOM   6108 C  CB  . SER B 1 381 ? 41.621  25.062  -36.493 1.00 20.68 ?  383 SER B CB  1 
ATOM   6109 O  OG  . SER B 1 381 ? 41.110  26.374  -36.588 1.00 27.08 ?  383 SER B OG  1 
ATOM   6110 N  N   . ARG B 1 382 ? 38.230  24.878  -36.214 1.00 18.92 ?  384 ARG B N   1 
ATOM   6111 C  CA  . ARG B 1 382 ? 37.057  25.145  -35.400 1.00 16.75 ?  384 ARG B CA  1 
ATOM   6112 C  C   . ARG B 1 382 ? 36.034  24.021  -35.492 1.00 17.94 ?  384 ARG B C   1 
ATOM   6113 O  O   . ARG B 1 382 ? 34.941  24.125  -34.923 1.00 17.17 ?  384 ARG B O   1 
ATOM   6114 C  CB  . ARG B 1 382 ? 36.441  26.488  -35.809 1.00 26.94 ?  384 ARG B CB  1 
ATOM   6115 C  CG  . ARG B 1 382 ? 37.150  27.676  -35.139 1.00 28.07 ?  384 ARG B CG  1 
ATOM   6116 C  CD  . ARG B 1 382 ? 37.152  28.929  -36.005 1.00 39.13 ?  384 ARG B CD  1 
ATOM   6117 N  NE  . ARG B 1 382 ? 37.948  30.010  -35.413 1.00 45.04 ?  384 ARG B NE  1 
ATOM   6118 C  CZ  . ARG B 1 382 ? 39.202  30.306  -35.762 1.00 48.21 ?  384 ARG B CZ  1 
ATOM   6119 N  NH1 . ARG B 1 382 ? 39.821  29.605  -36.706 1.00 36.23 ?  384 ARG B NH1 1 
ATOM   6120 N  NH2 . ARG B 1 382 ? 39.842  31.311  -35.171 1.00 48.27 ?  384 ARG B NH2 1 
ATOM   6121 N  N   . CYS B 1 383 ? 36.373  22.939  -36.186 1.00 16.91 ?  385 CYS B N   1 
ATOM   6122 C  CA  . CYS B 1 383 ? 35.511  21.774  -36.311 1.00 15.86 ?  385 CYS B CA  1 
ATOM   6123 C  C   . CYS B 1 383 ? 36.045  20.589  -35.521 1.00 15.81 ?  385 CYS B C   1 
ATOM   6124 O  O   . CYS B 1 383 ? 35.763  19.447  -35.879 1.00 13.41 ?  385 CYS B O   1 
ATOM   6125 C  CB  . CYS B 1 383 ? 35.358  21.382  -37.776 1.00 15.43 ?  385 CYS B CB  1 
ATOM   6126 S  SG  . CYS B 1 383 ? 34.617  22.675  -38.785 1.00 22.48 ?  385 CYS B SG  1 
ATOM   6127 N  N   . HIS B 1 384 ? 36.854  20.841  -34.484 1.00 14.12 ?  386 HIS B N   1 
ATOM   6128 C  CA  . HIS B 1 384 ? 37.288  19.817  -33.534 1.00 13.78 ?  386 HIS B CA  1 
ATOM   6129 C  C   . HIS B 1 384 ? 38.172  18.764  -34.187 1.00 16.38 ?  386 HIS B C   1 
ATOM   6130 O  O   . HIS B 1 384 ? 38.166  17.596  -33.786 1.00 14.20 ?  386 HIS B O   1 
ATOM   6131 C  CB  . HIS B 1 384 ? 36.089  19.165  -32.842 1.00 16.35 ?  386 HIS B CB  1 
ATOM   6132 C  CG  . HIS B 1 384 ? 35.188  20.160  -32.198 1.00 15.64 ?  386 HIS B CG  1 
ATOM   6133 N  ND1 . HIS B 1 384 ? 35.538  20.846  -31.057 1.00 20.90 ?  386 HIS B ND1 1 
ATOM   6134 C  CD2 . HIS B 1 384 ? 33.981  20.640  -32.576 1.00 24.22 ?  386 HIS B CD2 1 
ATOM   6135 C  CE1 . HIS B 1 384 ? 34.572  21.690  -30.745 1.00 22.29 ?  386 HIS B CE1 1 
ATOM   6136 N  NE2 . HIS B 1 384 ? 33.614  21.580  -31.646 1.00 23.07 ?  386 HIS B NE2 1 
ATOM   6137 N  N   . VAL B 1 385 ? 38.924  19.179  -35.206 1.00 14.22 ?  387 VAL B N   1 
ATOM   6138 C  CA  . VAL B 1 385 ? 39.967  18.372  -35.816 1.00 11.40 ?  387 VAL B CA  1 
ATOM   6139 C  C   . VAL B 1 385 ? 41.186  19.270  -35.941 1.00 13.85 ?  387 VAL B C   1 
ATOM   6140 O  O   . VAL B 1 385 ? 41.082  20.497  -35.874 1.00 13.69 ?  387 VAL B O   1 
ATOM   6141 C  CB  . VAL B 1 385 ? 39.544  17.808  -37.191 1.00 13.96 ?  387 VAL B CB  1 
ATOM   6142 C  CG1 . VAL B 1 385 ? 38.257  16.980  -37.044 1.00 12.01 ?  387 VAL B CG1 1 
ATOM   6143 C  CG2 . VAL B 1 385 ? 39.351  18.937  -38.205 1.00 12.50 ?  387 VAL B CG2 1 
ATOM   6144 N  N   . GLU B 1 386 ? 42.360  18.651  -36.089 1.00 12.05 ?  388 GLU B N   1 
ATOM   6145 C  CA  . GLU B 1 386 ? 43.571  19.439  -36.294 1.00 9.39  ?  388 GLU B CA  1 
ATOM   6146 C  C   . GLU B 1 386 ? 43.887  19.477  -37.783 1.00 11.64 ?  388 GLU B C   1 
ATOM   6147 O  O   . GLU B 1 386 ? 44.236  18.435  -38.353 1.00 11.75 ?  388 GLU B O   1 
ATOM   6148 C  CB  . GLU B 1 386 ? 44.750  18.847  -35.521 1.00 9.54  ?  388 GLU B CB  1 
ATOM   6149 C  CG  . GLU B 1 386 ? 46.073  19.614  -35.807 1.00 13.63 ?  388 GLU B CG  1 
ATOM   6150 C  CD  . GLU B 1 386 ? 47.310  18.866  -35.361 1.00 17.37 ?  388 GLU B CD  1 
ATOM   6151 O  OE1 . GLU B 1 386 ? 48.434  19.428  -35.444 1.00 17.63 ?  388 GLU B OE1 1 
ATOM   6152 O  OE2 . GLU B 1 386 ? 47.166  17.716  -34.904 1.00 16.85 ?  388 GLU B OE2 1 
ATOM   6153 N  N   . PRO B 1 387 ? 43.809  20.628  -38.453 1.00 9.09  ?  389 PRO B N   1 
ATOM   6154 C  CA  . PRO B 1 387 ? 44.236  20.676  -39.862 1.00 11.27 ?  389 PRO B CA  1 
ATOM   6155 C  C   . PRO B 1 387 ? 45.744  20.504  -39.937 1.00 12.87 ?  389 PRO B C   1 
ATOM   6156 O  O   . PRO B 1 387 ? 46.498  21.125  -39.179 1.00 12.46 ?  389 PRO B O   1 
ATOM   6157 C  CB  . PRO B 1 387 ? 43.806  22.071  -40.334 1.00 16.00 ?  389 PRO B CB  1 
ATOM   6158 C  CG  . PRO B 1 387 ? 43.663  22.872  -39.065 1.00 23.24 ?  389 PRO B CG  1 
ATOM   6159 C  CD  . PRO B 1 387 ? 43.293  21.922  -37.971 1.00 12.68 ?  389 PRO B CD  1 
ATOM   6160 N  N   . VAL B 1 388 ? 46.180  19.644  -40.844 1.00 13.15 ?  390 VAL B N   1 
ATOM   6161 C  CA  . VAL B 1 388 ? 47.595  19.444  -41.116 1.00 10.58 ?  390 VAL B CA  1 
ATOM   6162 C  C   . VAL B 1 388 ? 47.797  19.535  -42.621 1.00 11.74 ?  390 VAL B C   1 
ATOM   6163 O  O   . VAL B 1 388 ? 46.941  19.090  -43.398 1.00 14.20 ?  390 VAL B O   1 
ATOM   6164 C  CB  . VAL B 1 388 ? 48.094  18.099  -40.547 1.00 12.62 ?  390 VAL B CB  1 
ATOM   6165 C  CG1 . VAL B 1 388 ? 49.605  17.918  -40.782 1.00 9.92  ?  390 VAL B CG1 1 
ATOM   6166 C  CG2 . VAL B 1 388 ? 47.793  18.026  -39.044 1.00 13.01 ?  390 VAL B CG2 1 
ATOM   6167 N  N   . ALA B 1 389 ? 48.924  20.125  -43.036 1.00 11.70 ?  391 ALA B N   1 
ATOM   6168 C  CA  . ALA B 1 389 ? 49.088  20.477  -44.445 1.00 15.93 ?  391 ALA B CA  1 
ATOM   6169 C  C   . ALA B 1 389 ? 49.175  19.245  -45.345 1.00 15.05 ?  391 ALA B C   1 
ATOM   6170 O  O   . ALA B 1 389 ? 48.716  19.283  -46.493 1.00 14.01 ?  391 ALA B O   1 
ATOM   6171 C  CB  . ALA B 1 389 ? 50.323  21.363  -44.628 1.00 16.02 ?  391 ALA B CB  1 
ATOM   6172 N  N   . THR B 1 390 ? 49.789  18.160  -44.876 1.00 11.85 ?  392 THR B N   1 
ATOM   6173 C  CA  . THR B 1 390 ? 49.932  16.962  -45.697 1.00 12.41 ?  392 THR B CA  1 
ATOM   6174 C  C   . THR B 1 390 ? 49.732  15.719  -44.842 1.00 13.21 ?  392 THR B C   1 
ATOM   6175 O  O   . THR B 1 390 ? 49.961  15.740  -43.631 1.00 11.14 ?  392 THR B O   1 
ATOM   6176 C  CB  . THR B 1 390 ? 51.309  16.870  -46.401 1.00 15.03 ?  392 THR B CB  1 
ATOM   6177 O  OG1 . THR B 1 390 ? 52.311  16.439  -45.473 1.00 16.23 ?  392 THR B OG1 1 
ATOM   6178 C  CG2 . THR B 1 390 ? 51.734  18.200  -47.028 1.00 16.60 ?  392 THR B CG2 1 
ATOM   6179 N  N   . VAL B 1 391 ? 49.314  14.630  -45.495 1.00 10.91 ?  393 VAL B N   1 
ATOM   6180 C  CA  . VAL B 1 391 ? 49.206  13.340  -44.810 1.00 10.35 ?  393 VAL B CA  1 
ATOM   6181 C  C   . VAL B 1 391 ? 50.572  12.888  -44.294 1.00 13.04 ?  393 VAL B C   1 
ATOM   6182 O  O   . VAL B 1 391 ? 50.694  12.400  -43.166 1.00 13.07 ?  393 VAL B O   1 
ATOM   6183 C  CB  . VAL B 1 391 ? 48.580  12.279  -45.738 1.00 12.62 ?  393 VAL B CB  1 
ATOM   6184 C  CG1 . VAL B 1 391 ? 48.630  10.901  -45.082 1.00 12.61 ?  393 VAL B CG1 1 
ATOM   6185 C  CG2 . VAL B 1 391 ? 47.131  12.654  -46.087 1.00 13.06 ?  393 VAL B CG2 1 
ATOM   6186 N  N   . GLU B 1 392 ? 51.618  13.012  -45.123 1.00 9.75  ?  394 GLU B N   1 
ATOM   6187 C  CA  A GLU B 1 392 ? 52.938  12.576  -44.680 0.46 13.29 ?  394 GLU B CA  1 
ATOM   6188 C  CA  B GLU B 1 392 ? 52.954  12.605  -44.699 0.54 13.30 ?  394 GLU B CA  1 
ATOM   6189 C  C   . GLU B 1 392 ? 53.378  13.338  -43.436 1.00 14.38 ?  394 GLU B C   1 
ATOM   6190 O  O   . GLU B 1 392 ? 53.967  12.743  -42.526 1.00 12.79 ?  394 GLU B O   1 
ATOM   6191 C  CB  A GLU B 1 392 ? 53.959  12.724  -45.813 0.46 14.85 ?  394 GLU B CB  1 
ATOM   6192 C  CB  B GLU B 1 392 ? 53.978  12.863  -45.808 0.54 14.82 ?  394 GLU B CB  1 
ATOM   6193 C  CG  A GLU B 1 392 ? 53.314  12.501  -47.128 0.46 15.28 ?  394 GLU B CG  1 
ATOM   6194 C  CG  B GLU B 1 392 ? 55.306  12.164  -45.538 0.54 12.41 ?  394 GLU B CG  1 
ATOM   6195 C  CD  A GLU B 1 392 ? 54.187  11.995  -48.235 0.46 17.76 ?  394 GLU B CD  1 
ATOM   6196 C  CD  B GLU B 1 392 ? 56.220  12.119  -46.750 0.54 14.21 ?  394 GLU B CD  1 
ATOM   6197 O  OE1 A GLU B 1 392 ? 55.426  11.948  -48.079 0.46 16.62 ?  394 GLU B OE1 1 
ATOM   6198 O  OE1 B GLU B 1 392 ? 55.730  12.240  -47.887 0.54 15.16 ?  394 GLU B OE1 1 
ATOM   6199 O  OE2 A GLU B 1 392 ? 53.593  11.680  -49.290 0.46 15.79 ?  394 GLU B OE2 1 
ATOM   6200 O  OE2 B GLU B 1 392 ? 57.440  11.976  -46.554 0.54 14.72 ?  394 GLU B OE2 1 
ATOM   6201 N  N   . LEU B 1 393 ? 53.088  14.644  -43.367 1.00 13.48 ?  395 LEU B N   1 
ATOM   6202 C  CA  . LEU B 1 393 ? 53.439  15.408  -42.171 1.00 14.97 ?  395 LEU B CA  1 
ATOM   6203 C  C   . LEU B 1 393 ? 52.592  14.983  -40.974 1.00 14.46 ?  395 LEU B C   1 
ATOM   6204 O  O   . LEU B 1 393 ? 53.116  14.802  -39.864 1.00 13.59 ?  395 LEU B O   1 
ATOM   6205 C  CB  . LEU B 1 393 ? 53.286  16.908  -42.440 1.00 13.83 ?  395 LEU B CB  1 
ATOM   6206 C  CG  . LEU B 1 393 ? 53.380  17.822  -41.215 1.00 14.79 ?  395 LEU B CG  1 
ATOM   6207 C  CD1 . LEU B 1 393 ? 54.768  17.762  -40.589 1.00 15.46 ?  395 LEU B CD1 1 
ATOM   6208 C  CD2 . LEU B 1 393 ? 53.009  19.256  -41.609 1.00 19.29 ?  395 LEU B CD2 1 
ATOM   6209 N  N   . ALA B 1 394 ? 51.278  14.819  -41.182 1.00 9.91  ?  396 ALA B N   1 
ATOM   6210 C  CA  . ALA B 1 394 ? 50.396  14.334  -40.124 1.00 12.08 ?  396 ALA B CA  1 
ATOM   6211 C  C   . ALA B 1 394 ? 50.905  13.017  -39.545 1.00 11.91 ?  396 ALA B C   1 
ATOM   6212 O  O   . ALA B 1 394 ? 50.928  12.825  -38.324 1.00 12.25 ?  396 ALA B O   1 
ATOM   6213 C  CB  . ALA B 1 394 ? 48.968  14.157  -40.668 1.00 9.43  ?  396 ALA B CB  1 
ATOM   6214 N  N   . VAL B 1 395 ? 51.297  12.090  -40.421 1.00 10.42 ?  397 VAL B N   1 
ATOM   6215 C  CA  . VAL B 1 395 ? 51.801  10.796  -39.978 1.00 10.91 ?  397 VAL B CA  1 
ATOM   6216 C  C   . VAL B 1 395 ? 53.112  10.958  -39.222 1.00 10.81 ?  397 VAL B C   1 
ATOM   6217 O  O   . VAL B 1 395 ? 53.326  10.315  -38.187 1.00 13.56 ?  397 VAL B O   1 
ATOM   6218 C  CB  . VAL B 1 395 ? 51.963  9.857   -41.185 1.00 12.27 ?  397 VAL B CB  1 
ATOM   6219 C  CG1 . VAL B 1 395 ? 52.701  8.598   -40.786 1.00 12.95 ?  397 VAL B CG1 1 
ATOM   6220 C  CG2 . VAL B 1 395 ? 50.592  9.508   -41.726 1.00 13.05 ?  397 VAL B CG2 1 
ATOM   6221 N  N   . ALA B 1 396 ? 54.019  11.799  -39.734 1.00 11.06 ?  398 ALA B N   1 
ATOM   6222 C  CA  . ALA B 1 396 ? 55.292  11.995  -39.050 1.00 13.30 ?  398 ALA B CA  1 
ATOM   6223 C  C   . ALA B 1 396 ? 55.068  12.560  -37.655 1.00 14.65 ?  398 ALA B C   1 
ATOM   6224 O  O   . ALA B 1 396 ? 55.721  12.131  -36.698 1.00 13.96 ?  398 ALA B O   1 
ATOM   6225 C  CB  . ALA B 1 396 ? 56.202  12.914  -39.865 1.00 14.31 ?  398 ALA B CB  1 
ATOM   6226 N  N   . GLN B 1 397 ? 54.147  13.518  -37.524 1.00 10.42 ?  399 GLN B N   1 
ATOM   6227 C  CA  . GLN B 1 397 ? 53.843  14.084  -36.208 1.00 10.66 ?  399 GLN B CA  1 
ATOM   6228 C  C   . GLN B 1 397 ? 53.315  13.018  -35.257 1.00 16.25 ?  399 GLN B C   1 
ATOM   6229 O  O   . GLN B 1 397 ? 53.715  12.953  -34.086 1.00 12.93 ?  399 GLN B O   1 
ATOM   6230 C  CB  . GLN B 1 397 ? 52.817  15.206  -36.342 1.00 13.64 ?  399 GLN B CB  1 
ATOM   6231 C  CG  . GLN B 1 397 ? 53.351  16.452  -37.021 1.00 15.92 ?  399 GLN B CG  1 
ATOM   6232 C  CD  . GLN B 1 397 ? 52.242  17.419  -37.383 1.00 15.43 ?  399 GLN B CD  1 
ATOM   6233 O  OE1 . GLN B 1 397 ? 51.069  17.036  -37.480 1.00 15.20 ?  399 GLN B OE1 1 
ATOM   6234 N  NE2 . GLN B 1 397 ? 52.612  18.671  -37.626 1.00 19.30 ?  399 GLN B NE2 1 
ATOM   6235 N  N   . ALA B 1 398 ? 52.385  12.194  -35.741 1.00 11.97 ?  400 ALA B N   1 
ATOM   6236 C  CA  . ALA B 1 398 ? 51.782  11.170  -34.897 1.00 13.31 ?  400 ALA B CA  1 
ATOM   6237 C  C   . ALA B 1 398 ? 52.798  10.108  -34.508 1.00 14.71 ?  400 ALA B C   1 
ATOM   6238 O  O   . ALA B 1 398 ? 52.843  9.677   -33.349 1.00 14.38 ?  400 ALA B O   1 
ATOM   6239 C  CB  . ALA B 1 398 ? 50.593  10.529  -35.619 1.00 11.95 ?  400 ALA B CB  1 
ATOM   6240 N  N   . LEU B 1 399 ? 53.605  9.653   -35.469 1.00 12.15 ?  401 LEU B N   1 
ATOM   6241 C  CA  . LEU B 1 399 ? 54.629  8.662   -35.151 1.00 10.41 ?  401 LEU B CA  1 
ATOM   6242 C  C   . LEU B 1 399 ? 55.649  9.205   -34.152 1.00 15.68 ?  401 LEU B C   1 
ATOM   6243 O  O   . LEU B 1 399 ? 56.161  8.454   -33.318 1.00 16.48 ?  401 LEU B O   1 
ATOM   6244 C  CB  . LEU B 1 399 ? 55.326  8.200   -36.430 1.00 12.39 ?  401 LEU B CB  1 
ATOM   6245 C  CG  . LEU B 1 399 ? 54.437  7.320   -37.325 1.00 15.45 ?  401 LEU B CG  1 
ATOM   6246 C  CD1 . LEU B 1 399 ? 55.164  6.929   -38.584 1.00 16.22 ?  401 LEU B CD1 1 
ATOM   6247 C  CD2 . LEU B 1 399 ? 53.944  6.072   -36.592 1.00 18.73 ?  401 LEU B CD2 1 
ATOM   6248 N  N   . GLU B 1 400 ? 55.946  10.499  -34.216 1.00 12.61 ?  402 GLU B N   1 
ATOM   6249 C  CA  . GLU B 1 400 ? 56.845  11.104  -33.235 1.00 16.81 ?  402 GLU B CA  1 
ATOM   6250 C  C   . GLU B 1 400 ? 56.247  11.026  -31.835 1.00 18.77 ?  402 GLU B C   1 
ATOM   6251 O  O   . GLU B 1 400 ? 56.956  10.746  -30.860 1.00 15.91 ?  402 GLU B O   1 
ATOM   6252 C  CB  . GLU B 1 400 ? 57.132  12.555  -33.630 1.00 17.48 ?  402 GLU B CB  1 
ATOM   6253 C  CG  . GLU B 1 400 ? 58.277  13.224  -32.881 1.00 21.12 ?  402 GLU B CG  1 
ATOM   6254 C  CD  . GLU B 1 400 ? 59.633  12.662  -33.282 1.00 23.70 ?  402 GLU B CD  1 
ATOM   6255 O  OE1 . GLU B 1 400 ? 59.820  12.324  -34.469 1.00 25.97 ?  402 GLU B OE1 1 
ATOM   6256 O  OE2 . GLU B 1 400 ? 60.526  12.582  -32.419 1.00 22.84 ?  402 GLU B OE2 1 
ATOM   6257 N  N   . GLN B 1 401 ? 54.939  11.253  -31.720 1.00 13.54 ?  403 GLN B N   1 
ATOM   6258 C  CA  . GLN B 1 401 ? 54.279  11.146  -30.427 1.00 12.46 ?  403 GLN B CA  1 
ATOM   6259 C  C   . GLN B 1 401 ? 54.298  9.713   -29.905 1.00 15.62 ?  403 GLN B C   1 
ATOM   6260 O  O   . GLN B 1 401 ? 54.601  9.477   -28.729 1.00 16.40 ?  403 GLN B O   1 
ATOM   6261 C  CB  . GLN B 1 401 ? 52.833  11.657  -30.513 1.00 14.12 ?  403 GLN B CB  1 
ATOM   6262 C  CG  . GLN B 1 401 ? 52.132  11.597  -29.157 1.00 14.61 ?  403 GLN B CG  1 
ATOM   6263 C  CD  . GLN B 1 401 ? 50.646  11.852  -29.210 1.00 18.43 ?  403 GLN B CD  1 
ATOM   6264 O  OE1 . GLN B 1 401 ? 50.116  12.384  -30.189 1.00 17.13 ?  403 GLN B OE1 1 
ATOM   6265 N  NE2 . GLN B 1 401 ? 49.959  11.488  -28.134 1.00 18.21 ?  403 GLN B NE2 1 
ATOM   6266 N  N   . TYR B 1 402 ? 53.959  8.739   -30.748 1.00 12.91 ?  404 TYR B N   1 
ATOM   6267 C  CA  . TYR B 1 402 ? 53.717  7.387   -30.258 1.00 12.53 ?  404 TYR B CA  1 
ATOM   6268 C  C   . TYR B 1 402 ? 54.970  6.515   -30.222 1.00 15.83 ?  404 TYR B C   1 
ATOM   6269 O  O   . TYR B 1 402 ? 54.932  5.433   -29.624 1.00 18.55 ?  404 TYR B O   1 
ATOM   6270 C  CB  . TYR B 1 402 ? 52.630  6.710   -31.099 1.00 16.03 ?  404 TYR B CB  1 
ATOM   6271 C  CG  . TYR B 1 402 ? 51.319  7.450   -31.041 1.00 14.52 ?  404 TYR B CG  1 
ATOM   6272 C  CD1 . TYR B 1 402 ? 50.700  7.732   -29.828 1.00 12.99 ?  404 TYR B CD1 1 
ATOM   6273 C  CD2 . TYR B 1 402 ? 50.698  7.881   -32.203 1.00 15.33 ?  404 TYR B CD2 1 
ATOM   6274 C  CE1 . TYR B 1 402 ? 49.488  8.419   -29.779 1.00 13.78 ?  404 TYR B CE1 1 
ATOM   6275 C  CE2 . TYR B 1 402 ? 49.508  8.571   -32.163 1.00 14.22 ?  404 TYR B CE2 1 
ATOM   6276 C  CZ  . TYR B 1 402 ? 48.902  8.836   -30.960 1.00 11.05 ?  404 TYR B CZ  1 
ATOM   6277 O  OH  . TYR B 1 402 ? 47.712  9.527   -30.952 1.00 12.42 ?  404 TYR B OH  1 
ATOM   6278 N  N   . GLY B 1 403 ? 56.069  6.948   -30.833 1.00 19.21 ?  405 GLY B N   1 
ATOM   6279 C  CA  . GLY B 1 403 ? 57.347  6.308   -30.609 1.00 18.89 ?  405 GLY B CA  1 
ATOM   6280 C  C   . GLY B 1 403 ? 57.751  5.267   -31.635 1.00 21.64 ?  405 GLY B C   1 
ATOM   6281 O  O   . GLY B 1 403 ? 57.031  4.970   -32.595 1.00 19.65 ?  405 GLY B O   1 
ATOM   6282 N  N   . PRO B 1 404 ? 58.929  4.671   -31.423 1.00 19.53 ?  406 PRO B N   1 
ATOM   6283 C  CA  . PRO B 1 404 ? 59.520  3.806   -32.459 1.00 22.67 ?  406 PRO B CA  1 
ATOM   6284 C  C   . PRO B 1 404 ? 58.766  2.515   -32.717 1.00 22.75 ?  406 PRO B C   1 
ATOM   6285 O  O   . PRO B 1 404 ? 58.996  1.894   -33.763 1.00 25.89 ?  406 PRO B O   1 
ATOM   6286 C  CB  . PRO B 1 404 ? 60.927  3.514   -31.914 1.00 26.37 ?  406 PRO B CB  1 
ATOM   6287 C  CG  . PRO B 1 404 ? 60.854  3.820   -30.463 1.00 28.77 ?  406 PRO B CG  1 
ATOM   6288 C  CD  . PRO B 1 404 ? 59.839  4.896   -30.289 1.00 23.10 ?  406 PRO B CD  1 
ATOM   6289 N  N   . GLU B 1 405 ? 57.914  2.064   -31.804 1.00 18.59 ?  407 GLU B N   1 
ATOM   6290 C  CA  . GLU B 1 405 ? 57.157  0.840   -32.029 1.00 22.52 ?  407 GLU B CA  1 
ATOM   6291 C  C   . GLU B 1 405 ? 55.775  1.109   -32.608 1.00 19.93 ?  407 GLU B C   1 
ATOM   6292 O  O   . GLU B 1 405 ? 55.018  0.163   -32.832 1.00 22.34 ?  407 GLU B O   1 
ATOM   6293 C  CB  . GLU B 1 405 ? 57.015  0.045   -30.727 1.00 26.46 ?  407 GLU B CB  1 
ATOM   6294 C  CG  . GLU B 1 405 ? 58.333  -0.165  -29.971 1.00 33.42 ?  407 GLU B CG  1 
ATOM   6295 C  CD  . GLU B 1 405 ? 59.369  -0.885  -30.810 1.00 42.29 ?  407 GLU B CD  1 
ATOM   6296 O  OE1 . GLU B 1 405 ? 59.002  -1.866  -31.491 1.00 45.26 ?  407 GLU B OE1 1 
ATOM   6297 O  OE2 . GLU B 1 405 ? 60.552  -0.479  -30.780 1.00 48.36 ?  407 GLU B OE2 1 
ATOM   6298 N  N   . ALA B 1 406 ? 55.434  2.373   -32.843 1.00 20.57 ?  408 ALA B N   1 
ATOM   6299 C  CA  . ALA B 1 406 ? 54.116  2.711   -33.361 1.00 19.06 ?  408 ALA B CA  1 
ATOM   6300 C  C   . ALA B 1 406 ? 53.960  2.237   -34.804 1.00 19.87 ?  408 ALA B C   1 
ATOM   6301 O  O   . ALA B 1 406 ? 54.909  2.285   -35.595 1.00 18.41 ?  408 ALA B O   1 
ATOM   6302 C  CB  . ALA B 1 406 ? 53.887  4.220   -33.260 1.00 15.22 ?  408 ALA B CB  1 
ATOM   6303 N  N   . ARG B 1 407 ? 52.752  1.774   -35.140 1.00 16.60 ?  409 ARG B N   1 
ATOM   6304 C  CA  . ARG B 1 407 ? 52.434  1.235   -36.456 1.00 15.28 ?  409 ARG B CA  1 
ATOM   6305 C  C   . ARG B 1 407 ? 51.348  2.067   -37.129 1.00 15.29 ?  409 ARG B C   1 
ATOM   6306 O  O   . ARG B 1 407 ? 50.518  2.694   -36.462 1.00 14.83 ?  409 ARG B O   1 
ATOM   6307 C  CB  . ARG B 1 407 ? 51.959  -0.218  -36.360 1.00 15.11 ?  409 ARG B CB  1 
ATOM   6308 C  CG  . ARG B 1 407 ? 53.044  -1.237  -35.944 1.00 22.88 ?  409 ARG B CG  1 
ATOM   6309 C  CD  . ARG B 1 407 ? 54.334  -1.037  -36.724 1.00 25.13 ?  409 ARG B CD  1 
ATOM   6310 N  NE  . ARG B 1 407 ? 55.474  -1.737  -36.121 1.00 45.62 ?  409 ARG B NE  1 
ATOM   6311 C  CZ  . ARG B 1 407 ? 56.645  -1.170  -35.827 1.00 43.07 ?  409 ARG B CZ  1 
ATOM   6312 N  NH1 . ARG B 1 407 ? 56.836  0.123   -36.047 1.00 33.16 ?  409 ARG B NH1 1 
ATOM   6313 N  NH2 . ARG B 1 407 ? 57.620  -1.892  -35.285 1.00 44.81 ?  409 ARG B NH2 1 
ATOM   6314 N  N   . VAL B 1 408 ? 51.342  2.033   -38.464 1.00 14.14 ?  410 VAL B N   1 
ATOM   6315 C  CA  . VAL B 1 408 ? 50.375  2.765   -39.275 1.00 14.18 ?  410 VAL B CA  1 
ATOM   6316 C  C   . VAL B 1 408 ? 49.543  1.762   -40.060 1.00 13.66 ?  410 VAL B C   1 
ATOM   6317 O  O   . VAL B 1 408 ? 50.100  0.877   -40.719 1.00 13.84 ?  410 VAL B O   1 
ATOM   6318 C  CB  . VAL B 1 408 ? 51.080  3.727   -40.248 1.00 15.31 ?  410 VAL B CB  1 
ATOM   6319 C  CG1 . VAL B 1 408 ? 50.049  4.509   -41.093 1.00 12.81 ?  410 VAL B CG1 1 
ATOM   6320 C  CG2 . VAL B 1 408 ? 52.026  4.643   -39.494 1.00 13.81 ?  410 VAL B CG2 1 
ATOM   6321 N  N   . ALA B 1 409 ? 48.221  1.917   -40.022 1.00 11.30 ?  411 ALA B N   1 
ATOM   6322 C  CA  . ALA B 1 409 ? 47.355  1.235   -40.977 1.00 11.19 ?  411 ALA B CA  1 
ATOM   6323 C  C   . ALA B 1 409 ? 46.798  2.269   -41.943 1.00 11.08 ?  411 ALA B C   1 
ATOM   6324 O  O   . ALA B 1 409 ? 46.586  3.428   -41.578 1.00 13.50 ?  411 ALA B O   1 
ATOM   6325 C  CB  . ALA B 1 409 ? 46.206  0.483   -40.289 1.00 12.62 ?  411 ALA B CB  1 
ATOM   6326 N  N   . VAL B 1 410 ? 46.589  1.861   -43.189 1.00 9.25  ?  412 VAL B N   1 
ATOM   6327 C  CA  . VAL B 1 410 ? 46.074  2.777   -44.206 1.00 10.00 ?  412 VAL B CA  1 
ATOM   6328 C  C   . VAL B 1 410 ? 44.872  2.143   -44.889 1.00 12.04 ?  412 VAL B C   1 
ATOM   6329 O  O   . VAL B 1 410 ? 44.875  0.945   -45.196 1.00 11.19 ?  412 VAL B O   1 
ATOM   6330 C  CB  . VAL B 1 410 ? 47.173  3.208   -45.210 1.00 11.32 ?  412 VAL B CB  1 
ATOM   6331 C  CG1 . VAL B 1 410 ? 47.755  2.024   -45.962 1.00 12.26 ?  412 VAL B CG1 1 
ATOM   6332 C  CG2 . VAL B 1 410 ? 46.606  4.249   -46.213 1.00 11.78 ?  412 VAL B CG2 1 
ATOM   6333 N  N   . ILE B 1 411 ? 43.817  2.943   -45.066 1.00 8.68  ?  413 ILE B N   1 
ATOM   6334 C  CA  . ILE B 1 411 ? 42.557  2.487   -45.666 1.00 8.87  ?  413 ILE B CA  1 
ATOM   6335 C  C   . ILE B 1 411 ? 42.228  3.365   -46.869 1.00 10.23 ?  413 ILE B C   1 
ATOM   6336 O  O   . ILE B 1 411 ? 41.491  4.348   -46.725 1.00 8.72  ?  413 ILE B O   1 
ATOM   6337 C  CB  . ILE B 1 411 ? 41.386  2.528   -44.667 1.00 8.99  ?  413 ILE B CB  1 
ATOM   6338 C  CG1 . ILE B 1 411 ? 41.793  1.984   -43.287 1.00 12.02 ?  413 ILE B CG1 1 
ATOM   6339 C  CG2 . ILE B 1 411 ? 40.148  1.822   -45.268 1.00 8.61  ?  413 ILE B CG2 1 
ATOM   6340 C  CD1 . ILE B 1 411 ? 40.735  2.236   -42.165 1.00 13.34 ?  413 ILE B CD1 1 
ATOM   6341 N  N   . PRO B 1 412 ? 42.743  3.059   -48.065 1.00 10.51 ?  414 PRO B N   1 
ATOM   6342 C  CA  . PRO B 1 412 ? 42.588  4.011   -49.183 1.00 9.05  ?  414 PRO B CA  1 
ATOM   6343 C  C   . PRO B 1 412 ? 41.145  4.344   -49.538 1.00 13.36 ?  414 PRO B C   1 
ATOM   6344 O  O   . PRO B 1 412 ? 40.870  5.498   -49.880 1.00 12.69 ?  414 PRO B O   1 
ATOM   6345 C  CB  . PRO B 1 412 ? 43.312  3.308   -50.335 1.00 9.89  ?  414 PRO B CB  1 
ATOM   6346 C  CG  . PRO B 1 412 ? 44.345  2.479   -49.652 1.00 13.17 ?  414 PRO B CG  1 
ATOM   6347 C  CD  . PRO B 1 412 ? 43.619  1.929   -48.429 1.00 9.75  ?  414 PRO B CD  1 
ATOM   6348 N  N   . LYS B 1 413 ? 40.216  3.388   -49.438 1.00 9.22  ?  415 LYS B N   1 
ATOM   6349 C  CA  A LYS B 1 413 ? 38.813  3.610   -49.758 0.30 10.68 ?  415 LYS B CA  1 
ATOM   6350 C  CA  B LYS B 1 413 ? 38.821  3.641   -49.767 0.70 10.62 ?  415 LYS B CA  1 
ATOM   6351 C  C   . LYS B 1 413 ? 37.979  4.016   -48.544 1.00 9.63  ?  415 LYS B C   1 
ATOM   6352 O  O   . LYS B 1 413 ? 36.747  4.084   -48.648 1.00 9.28  ?  415 LYS B O   1 
ATOM   6353 C  CB  A LYS B 1 413 ? 38.208  2.354   -50.396 0.30 10.55 ?  415 LYS B CB  1 
ATOM   6354 C  CB  B LYS B 1 413 ? 38.217  2.424   -50.480 0.70 10.52 ?  415 LYS B CB  1 
ATOM   6355 C  CG  A LYS B 1 413 ? 38.335  2.271   -51.922 0.30 10.52 ?  415 LYS B CG  1 
ATOM   6356 C  CG  B LYS B 1 413 ? 38.392  2.422   -52.023 0.70 10.24 ?  415 LYS B CG  1 
ATOM   6357 C  CD  A LYS B 1 413 ? 39.777  2.266   -52.385 0.30 13.96 ?  415 LYS B CD  1 
ATOM   6358 C  CD  B LYS B 1 413 ? 39.835  2.635   -52.451 0.70 14.25 ?  415 LYS B CD  1 
ATOM   6359 C  CE  A LYS B 1 413 ? 39.876  2.544   -53.879 0.30 13.81 ?  415 LYS B CE  1 
ATOM   6360 C  CE  B LYS B 1 413 ? 40.025  2.394   -53.956 0.70 13.43 ?  415 LYS B CE  1 
ATOM   6361 N  NZ  A LYS B 1 413 ? 41.271  2.413   -54.377 0.30 15.99 ?  415 LYS B NZ  1 
ATOM   6362 N  NZ  B LYS B 1 413 ? 39.465  3.498   -54.802 0.70 13.71 ?  415 LYS B NZ  1 
ATOM   6363 N  N   . GLY B 1 414 ? 38.616  4.272   -47.401 1.00 10.39 ?  416 GLY B N   1 
ATOM   6364 C  CA  . GLY B 1 414 ? 37.943  4.814   -46.241 1.00 11.44 ?  416 GLY B CA  1 
ATOM   6365 C  C   . GLY B 1 414 ? 36.692  4.073   -45.808 1.00 7.88  ?  416 GLY B C   1 
ATOM   6366 O  O   . GLY B 1 414 ? 36.714  2.877   -45.517 1.00 9.47  ?  416 GLY B O   1 
ATOM   6367 N  N   . PRO B 1 415 ? 35.567  4.785   -45.733 1.00 9.74  ?  417 PRO B N   1 
ATOM   6368 C  CA  . PRO B 1 415 ? 34.359  4.180   -45.155 1.00 8.40  ?  417 PRO B CA  1 
ATOM   6369 C  C   . PRO B 1 415 ? 33.708  3.134   -46.042 1.00 9.78  ?  417 PRO B C   1 
ATOM   6370 O  O   . PRO B 1 415 ? 32.709  2.527   -45.630 1.00 14.77 ?  417 PRO B O   1 
ATOM   6371 C  CB  . PRO B 1 415 ? 33.450  5.399   -44.932 1.00 8.21  ?  417 PRO B CB  1 
ATOM   6372 C  CG  . PRO B 1 415 ? 33.848  6.328   -46.040 1.00 11.44 ?  417 PRO B CG  1 
ATOM   6373 C  CD  . PRO B 1 415 ? 35.345  6.190   -46.129 1.00 8.73  ?  417 PRO B CD  1 
ATOM   6374 N  N   . TYR B 1 416 ? 34.221  2.905   -47.246 1.00 8.64  ?  418 TYR B N   1 
ATOM   6375 C  CA  . TYR B 1 416 ? 33.734  1.787   -48.046 1.00 10.90 ?  418 TYR B CA  1 
ATOM   6376 C  C   . TYR B 1 416 ? 34.430  0.485   -47.681 1.00 11.84 ?  418 TYR B C   1 
ATOM   6377 O  O   . TYR B 1 416 ? 34.132  -0.559  -48.274 1.00 14.11 ?  418 TYR B O   1 
ATOM   6378 C  CB  . TYR B 1 416 ? 33.915  2.089   -49.534 1.00 8.67  ?  418 TYR B CB  1 
ATOM   6379 C  CG  . TYR B 1 416 ? 33.021  3.182   -50.096 1.00 9.48  ?  418 TYR B CG  1 
ATOM   6380 C  CD1 . TYR B 1 416 ? 31.949  3.711   -49.365 1.00 10.40 ?  418 TYR B CD1 1 
ATOM   6381 C  CD2 . TYR B 1 416 ? 33.268  3.698   -51.363 1.00 9.74  ?  418 TYR B CD2 1 
ATOM   6382 C  CE1 . TYR B 1 416 ? 31.142  4.717   -49.901 1.00 10.47 ?  418 TYR B CE1 1 
ATOM   6383 C  CE2 . TYR B 1 416 ? 32.468  4.694   -51.908 1.00 10.32 ?  418 TYR B CE2 1 
ATOM   6384 C  CZ  . TYR B 1 416 ? 31.417  5.207   -51.181 1.00 12.73 ?  418 TYR B CZ  1 
ATOM   6385 O  OH  . TYR B 1 416 ? 30.651  6.223   -51.745 1.00 13.00 ?  418 TYR B OH  1 
ATOM   6386 N  N   . VAL B 1 417 ? 35.353  0.531   -46.726 1.00 11.12 ?  419 VAL B N   1 
ATOM   6387 C  CA  . VAL B 1 417 ? 35.980  -0.651  -46.150 1.00 10.27 ?  419 VAL B CA  1 
ATOM   6388 C  C   . VAL B 1 417 ? 35.473  -0.808  -44.722 1.00 13.05 ?  419 VAL B C   1 
ATOM   6389 O  O   . VAL B 1 417 ? 35.113  0.178   -44.068 1.00 12.74 ?  419 VAL B O   1 
ATOM   6390 C  CB  . VAL B 1 417 ? 37.514  -0.484  -46.178 1.00 10.31 ?  419 VAL B CB  1 
ATOM   6391 C  CG1 . VAL B 1 417 ? 38.223  -1.665  -45.520 1.00 11.21 ?  419 VAL B CG1 1 
ATOM   6392 C  CG2 . VAL B 1 417 ? 37.997  -0.244  -47.610 1.00 12.33 ?  419 VAL B CG2 1 
ATOM   6393 N  N   . LEU B 1 418 ? 35.458  -2.053  -44.235 1.00 10.28 ?  420 LEU B N   1 
ATOM   6394 C  CA  . LEU B 1 418 ? 35.096  -2.376  -42.854 1.00 12.33 ?  420 LEU B CA  1 
ATOM   6395 C  C   . LEU B 1 418 ? 36.322  -2.919  -42.132 1.00 15.89 ?  420 LEU B C   1 
ATOM   6396 O  O   . LEU B 1 418 ? 36.539  -4.141  -42.096 1.00 13.96 ?  420 LEU B O   1 
ATOM   6397 C  CB  . LEU B 1 418 ? 33.948  -3.390  -42.828 1.00 15.26 ?  420 LEU B CB  1 
ATOM   6398 C  CG  . LEU B 1 418 ? 33.086  -3.514  -41.575 1.00 24.99 ?  420 LEU B CG  1 
ATOM   6399 C  CD1 . LEU B 1 418 ? 32.168  -2.331  -41.498 1.00 22.70 ?  420 LEU B CD1 1 
ATOM   6400 C  CD2 . LEU B 1 418 ? 32.272  -4.814  -41.594 1.00 20.57 ?  420 LEU B CD2 1 
ATOM   6401 N  N   . PRO B 1 419 ? 37.164  -2.065  -41.545 1.00 11.84 ?  421 PRO B N   1 
ATOM   6402 C  CA  . PRO B 1 419 ? 38.377  -2.574  -40.889 1.00 13.71 ?  421 PRO B CA  1 
ATOM   6403 C  C   . PRO B 1 419 ? 38.045  -3.220  -39.551 1.00 18.19 ?  421 PRO B C   1 
ATOM   6404 O  O   . PRO B 1 419 ? 37.204  -2.732  -38.794 1.00 18.03 ?  421 PRO B O   1 
ATOM   6405 C  CB  . PRO B 1 419 ? 39.238  -1.315  -40.707 1.00 16.21 ?  421 PRO B CB  1 
ATOM   6406 C  CG  . PRO B 1 419 ? 38.238  -0.214  -40.553 1.00 17.78 ?  421 PRO B CG  1 
ATOM   6407 C  CD  . PRO B 1 419 ? 37.033  -0.602  -41.409 1.00 15.22 ?  421 PRO B CD  1 
ATOM   6408 N  N   . VAL B 1 420 ? 38.704  -4.345  -39.261 1.00 14.85 ?  422 VAL B N   1 
ATOM   6409 C  CA  . VAL B 1 420 ? 38.446  -5.077  -38.027 1.00 13.88 ?  422 VAL B CA  1 
ATOM   6410 C  C   . VAL B 1 420 ? 39.767  -5.593  -37.483 1.00 16.98 ?  422 VAL B C   1 
ATOM   6411 O  O   . VAL B 1 420 ? 40.751  -5.737  -38.212 1.00 13.70 ?  422 VAL B O   1 
ATOM   6412 C  CB  . VAL B 1 420 ? 37.486  -6.277  -38.223 1.00 18.74 ?  422 VAL B CB  1 
ATOM   6413 C  CG1 . VAL B 1 420 ? 36.093  -5.814  -38.679 1.00 24.70 ?  422 VAL B CG1 1 
ATOM   6414 C  CG2 . VAL B 1 420 ? 38.104  -7.288  -39.168 1.00 17.24 ?  422 VAL B CG2 1 
ATOM   6415 N  N   . VAL B 1 421 ? 39.769  -5.901  -36.184 1.00 17.12 ?  423 VAL B N   1 
ATOM   6416 C  CA  . VAL B 1 421 ? 40.913  -6.528  -35.532 1.00 17.27 ?  423 VAL B CA  1 
ATOM   6417 C  C   . VAL B 1 421 ? 40.672  -8.028  -35.520 1.00 18.52 ?  423 VAL B C   1 
ATOM   6418 O  O   . VAL B 1 421 ? 39.616  -8.486  -35.067 1.00 25.88 ?  423 VAL B O   1 
ATOM   6419 C  CB  . VAL B 1 421 ? 41.114  -6.008  -34.098 1.00 22.37 ?  423 VAL B CB  1 
ATOM   6420 C  CG1 . VAL B 1 421 ? 42.231  -6.815  -33.391 1.00 17.49 ?  423 VAL B CG1 1 
ATOM   6421 C  CG2 . VAL B 1 421 ? 41.406  -4.504  -34.094 1.00 21.44 ?  423 VAL B CG2 1 
ATOM   6422 N  N   . ASP B 1 422 ? 41.637  -8.787  -36.028 1.00 17.17 ?  424 ASP B N   1 
ATOM   6423 C  CA  . ASP B 1 422 ? 41.591  -10.250 -35.996 1.00 32.23 ?  424 ASP B CA  1 
ATOM   6424 C  C   . ASP B 1 422 ? 42.833  -10.749 -35.275 1.00 25.75 ?  424 ASP B C   1 
ATOM   6425 O  O   . ASP B 1 422 ? 43.909  -10.853 -35.891 1.00 27.28 ?  424 ASP B O   1 
ATOM   6426 C  CB  . ASP B 1 422 ? 41.517  -10.836 -37.404 1.00 27.48 ?  424 ASP B CB  1 
ATOM   6427 N  N   . PRO B 1 423 ? 42.738  -11.072 -33.983 1.00 26.38 ?  425 PRO B N   1 
ATOM   6428 C  CA  . PRO B 1 423 ? 43.951  -11.425 -33.220 1.00 33.09 ?  425 PRO B CA  1 
ATOM   6429 C  C   . PRO B 1 423 ? 44.702  -12.634 -33.761 1.00 39.95 ?  425 PRO B C   1 
ATOM   6430 O  O   . PRO B 1 423 ? 45.894  -12.779 -33.464 1.00 47.15 ?  425 PRO B O   1 
ATOM   6431 C  CB  . PRO B 1 423 ? 43.407  -11.688 -31.807 1.00 33.00 ?  425 PRO B CB  1 
ATOM   6432 C  CG  . PRO B 1 423 ? 42.144  -10.874 -31.747 1.00 33.81 ?  425 PRO B CG  1 
ATOM   6433 C  CD  . PRO B 1 423 ? 41.544  -11.030 -33.120 1.00 26.40 ?  425 PRO B CD  1 
ATOM   6434 N  N   . THR B 1 424 ? 44.060  -13.492 -34.552 1.00 45.62 ?  426 THR B N   1 
ATOM   6435 C  CA  . THR B 1 424 ? 44.721  -14.687 -35.075 1.00 45.93 ?  426 THR B CA  1 
ATOM   6436 C  C   . THR B 1 424 ? 45.759  -14.324 -36.136 1.00 40.03 ?  426 THR B C   1 
ATOM   6437 O  O   . THR B 1 424 ? 45.646  -13.296 -36.813 1.00 42.53 ?  426 THR B O   1 
ATOM   6438 C  CB  . THR B 1 424 ? 43.709  -15.679 -35.686 1.00 43.67 ?  426 THR B CB  1 
ATOM   6439 O  OG1 . THR B 1 424 ? 43.071  -15.078 -36.817 1.00 45.49 ?  426 THR B OG1 1 
ATOM   6440 C  CG2 . THR B 1 424 ? 42.643  -16.036 -34.659 1.00 40.98 ?  426 THR B CG2 1 
HETATM 6441 C  C2  . 4EY C 2 .   ? 22.966  3.702   6.268   1.00 7.32  ?  501 4EY A C2  1 
HETATM 6442 C  C3  . 4EY C 2 .   ? 23.237  3.692   7.637   1.00 9.64  ?  501 4EY A C3  1 
HETATM 6443 C  C1  . 4EY C 2 .   ? 24.009  0.124   8.180   1.00 10.46 ?  501 4EY A C1  1 
HETATM 6444 C  C4  . 4EY C 2 .   ? 23.572  2.481   8.234   1.00 9.49  ?  501 4EY A C4  1 
HETATM 6445 C  C5  . 4EY C 2 .   ? 23.602  1.329   7.479   1.00 7.34  ?  501 4EY A C5  1 
HETATM 6446 C  C6  . 4EY C 2 .   ? 23.335  1.402   6.107   1.00 8.82  ?  501 4EY A C6  1 
HETATM 6447 O  O2  . 4EY C 2 .   ? 24.022  -0.984  7.656   1.00 10.81 ?  501 4EY A O2  1 
HETATM 6448 O  O2P . 4EY C 2 .   ? 20.167  6.860   3.441   1.00 8.29  -1 501 4EY A O2P 1 
HETATM 6449 P  P   . 4EY C 2 .   ? 21.408  7.137   4.365   1.00 7.41  ?  501 4EY A P   1 
HETATM 6450 O  O3P . 4EY C 2 .   ? 21.018  7.056   5.801   1.00 7.71  ?  501 4EY A O3P 1 
HETATM 6451 O  O1P . 4EY C 2 .   ? 22.110  8.519   3.977   1.00 9.65  -1 501 4EY A O1P 1 
HETATM 6452 O  O5R . 4EY C 2 .   ? 22.475  5.924   4.152   1.00 6.86  ?  501 4EY A O5R 1 
HETATM 6453 C  C5R . 4EY C 2 .   ? 23.129  5.800   2.889   1.00 8.71  ?  501 4EY A C5R 1 
HETATM 6454 C  C4R . 4EY C 2 .   ? 23.111  4.310   2.516   1.00 8.49  ?  501 4EY A C4R 1 
HETATM 6455 O  O4R . 4EY C 2 .   ? 23.757  3.531   3.565   1.00 8.69  ?  501 4EY A O4R 1 
HETATM 6456 C  C3R . 4EY C 2 .   ? 21.683  3.739   2.347   1.00 7.93  ?  501 4EY A C3R 1 
HETATM 6457 O  O3R . 4EY C 2 .   ? 21.692  2.767   1.284   1.00 7.68  ?  501 4EY A O3R 1 
HETATM 6458 C  C2R . 4EY C 2 .   ? 21.382  3.107   3.708   1.00 7.90  ?  501 4EY A C2R 1 
HETATM 6459 O  O2R . 4EY C 2 .   ? 20.459  2.018   3.596   1.00 8.77  ?  501 4EY A O2R 1 
HETATM 6460 C  C1R . 4EY C 2 .   ? 22.778  2.598   4.125   1.00 8.57  ?  501 4EY A C1R 1 
HETATM 6461 N  N1  . 4EY C 2 .   ? 23.014  2.571   5.565   1.00 6.98  ?  501 4EY A N1  1 
HETATM 6462 C  C7  . 4EY C 2 .   ? 23.220  4.880   8.493   1.00 7.60  ?  501 4EY A C7  1 
HETATM 6463 S  S7  . 4EY C 2 .   ? 23.860  4.740   9.963   1.00 8.26  ?  501 4EY A S7  1 
HETATM 6464 S  S2  . 4EY C 2 .   ? 24.616  0.444   9.803   1.00 11.74 ?  501 4EY A S2  1 
HETATM 6465 C  C1  . PGE D 3 .   ? 12.738  23.940  -2.667  1.00 28.24 ?  502 PGE A C1  1 
HETATM 6466 O  O1  . PGE D 3 .   ? 12.848  24.884  -3.727  1.00 37.55 ?  502 PGE A O1  1 
HETATM 6467 C  C2  . PGE D 3 .   ? 13.727  24.297  -1.573  1.00 26.60 ?  502 PGE A C2  1 
HETATM 6468 O  O2  . PGE D 3 .   ? 15.064  24.040  -1.977  1.00 31.63 ?  502 PGE A O2  1 
HETATM 6469 C  C3  . PGE D 3 .   ? 15.909  23.727  -0.884  1.00 26.93 ?  502 PGE A C3  1 
HETATM 6470 C  C4  . PGE D 3 .   ? 17.358  24.060  -1.187  1.00 29.03 ?  502 PGE A C4  1 
HETATM 6471 O  O4  . PGE D 3 .   ? 19.904  26.343  -3.299  1.00 39.95 ?  502 PGE A O4  1 
HETATM 6472 C  C6  . PGE D 3 .   ? 19.237  25.316  -4.021  1.00 35.10 ?  502 PGE A C6  1 
HETATM 6473 C  C5  . PGE D 3 .   ? 18.754  24.249  -3.061  1.00 31.13 ?  502 PGE A C5  1 
HETATM 6474 O  O3  . PGE D 3 .   ? 17.510  24.601  -2.485  1.00 36.23 ?  502 PGE A O3  1 
HETATM 6475 C  C1  . PEG E 4 .   ? 20.076  7.631   -19.305 1.00 33.88 ?  503 PEG A C1  1 
HETATM 6476 O  O1  . PEG E 4 .   ? 19.566  6.330   -19.373 1.00 39.39 ?  503 PEG A O1  1 
HETATM 6477 C  C2  . PEG E 4 .   ? 21.562  7.577   -19.643 1.00 33.34 ?  503 PEG A C2  1 
HETATM 6478 O  O2  . PEG E 4 .   ? 21.748  8.136   -20.906 1.00 34.88 ?  503 PEG A O2  1 
HETATM 6479 C  C3  . PEG E 4 .   ? 23.074  8.485   -21.174 1.00 34.03 ?  503 PEG A C3  1 
HETATM 6480 C  C4  . PEG E 4 .   ? 23.269  8.532   -22.684 1.00 32.61 ?  503 PEG A C4  1 
HETATM 6481 O  O4  . PEG E 4 .   ? 23.759  7.289   -23.105 1.00 45.80 ?  503 PEG A O4  1 
HETATM 6482 C  CA  . VAD F 5 .   ? 20.785  1.391   9.649   1.00 10.93 ?  504 VAD A CA  1 
HETATM 6483 C  CB  . VAD F 5 .   ? 19.996  1.497   10.958  1.00 12.19 ?  504 VAD A CB  1 
HETATM 6484 C  CG1 . VAD F 5 .   ? 18.642  0.788   10.883  1.00 9.48  ?  504 VAD A CG1 1 
HETATM 6485 C  CG2 . VAD F 5 .   ? 20.819  1.010   12.148  1.00 14.23 ?  504 VAD A CG2 1 
HETATM 6486 C  C   . VAD F 5 .   ? 20.033  2.190   8.597   1.00 10.09 ?  504 VAD A C   1 
HETATM 6487 O  O   . VAD F 5 .   ? 19.819  3.412   8.777   1.00 10.49 -1 504 VAD A O   1 
HETATM 6488 O  OXT . VAD F 5 .   ? 19.621  1.630   7.556   1.00 8.57  ?  504 VAD A OXT 1 
HETATM 6489 O  OE  . VAD F 5 .   ? 20.908  0.066   9.199   1.00 11.24 ?  504 VAD A OE  1 
HETATM 6490 C  C1  . PEG G 4 .   ? 21.331  22.179  11.656  1.00 35.10 ?  505 PEG A C1  1 
HETATM 6491 O  O1  . PEG G 4 .   ? 22.371  22.172  10.706  1.00 42.93 ?  505 PEG A O1  1 
HETATM 6492 C  C2  . PEG G 4 .   ? 21.199  20.799  12.297  1.00 32.76 ?  505 PEG A C2  1 
HETATM 6493 O  O2  . PEG G 4 .   ? 20.499  20.887  13.509  1.00 43.25 ?  505 PEG A O2  1 
HETATM 6494 C  C3  . PEG G 4 .   ? 21.241  21.332  14.619  1.00 37.53 ?  505 PEG A C3  1 
HETATM 6495 C  C4  . PEG G 4 .   ? 22.046  20.158  15.169  1.00 26.36 ?  505 PEG A C4  1 
HETATM 6496 O  O4  . PEG G 4 .   ? 22.472  20.273  16.507  1.00 33.56 ?  505 PEG A O4  1 
HETATM 6497 NI NI  . NI  H 6 .   ? 24.283  2.597   9.991   1.00 10.28 ?  506 NI  A NI  1 
HETATM 6498 C  C2  . 4EY I 2 .   ? 20.591  8.481   -46.063 1.00 11.26 ?  501 4EY B C2  1 
HETATM 6499 C  C3  . 4EY I 2 .   ? 20.809  8.532   -44.669 1.00 12.78 ?  501 4EY B C3  1 
HETATM 6500 C  C1  . 4EY I 2 .   ? 20.139  12.111  -43.986 1.00 14.40 ?  501 4EY B C1  1 
HETATM 6501 C  C4  . 4EY I 2 .   ? 20.650  9.744   -44.027 1.00 11.75 ?  501 4EY B C4  1 
HETATM 6502 C  C5  . 4EY I 2 .   ? 20.312  10.872  -44.742 1.00 11.61 ?  501 4EY B C5  1 
HETATM 6503 C  C6  . 4EY I 2 .   ? 20.118  10.769  -46.112 1.00 11.07 ?  501 4EY B C6  1 
HETATM 6504 O  O2  . 4EY I 2 .   ? 19.974  13.197  -44.511 1.00 15.73 ?  501 4EY B O2  1 
HETATM 6505 O  O2P . 4EY I 2 .   ? 20.821  3.590   -48.374 1.00 14.34 -1 501 4EY B O2P 1 
HETATM 6506 P  P   . 4EY I 2 .   ? 21.517  5.021   -48.277 1.00 12.25 ?  501 4EY B P   1 
HETATM 6507 O  O3P . 4EY I 2 .   ? 22.331  5.293   -49.498 1.00 10.78 ?  501 4EY B O3P 1 
HETATM 6508 O  O1P . 4EY I 2 .   ? 22.398  5.160   -46.959 1.00 13.31 -1 501 4EY B O1P 1 
HETATM 6509 O  O5R . 4EY I 2 .   ? 20.415  6.188   -48.168 1.00 12.79 ?  501 4EY B O5R 1 
HETATM 6510 C  C5R . 4EY I 2 .   ? 19.403  6.299   -49.180 1.00 13.09 ?  501 4EY B C5R 1 
HETATM 6511 C  C4R . 4EY I 2 .   ? 19.249  7.783   -49.530 1.00 11.24 ?  501 4EY B C4R 1 
HETATM 6512 O  O4R . 4EY I 2 .   ? 18.972  8.570   -48.341 1.00 13.20 ?  501 4EY B O4R 1 
HETATM 6513 C  C3R . 4EY I 2 .   ? 20.540  8.364   -50.155 1.00 11.40 ?  501 4EY B C3R 1 
HETATM 6514 O  O3R . 4EY I 2 .   ? 20.209  9.314   -51.166 1.00 13.89 ?  501 4EY B O3R 1 
HETATM 6515 C  C2R . 4EY I 2 .   ? 21.217  9.080   -48.970 1.00 10.53 ?  501 4EY B C2R 1 
HETATM 6516 O  O2R . 4EY I 2 .   ? 21.998  10.173  -49.425 1.00 11.51 ?  501 4EY B O2R 1 
HETATM 6517 C  C1R . 4EY I 2 .   ? 20.010  9.570   -48.152 1.00 12.51 ?  501 4EY B C1R 1 
HETATM 6518 N  N1  . 4EY I 2 .   ? 20.273  9.605   -46.716 1.00 14.67 ?  501 4EY B N1  1 
HETATM 6519 C  C7  . 4EY I 2 .   ? 21.164  7.382   -43.829 1.00 14.66 ?  501 4EY B C7  1 
HETATM 6520 S  S7  . 4EY I 2 .   ? 20.979  7.513   -42.225 1.00 11.55 ?  501 4EY B S7  1 
HETATM 6521 S  S2  . 4EY I 2 .   ? 20.097  11.871  -42.249 1.00 15.44 ?  501 4EY B S2  1 
HETATM 6522 C  CA  . VAD J 5 .   ? 23.765  10.878  -43.582 1.00 14.53 ?  502 VAD B CA  1 
HETATM 6523 C  CB  . VAD J 5 .   ? 24.944  10.806  -42.605 1.00 16.55 ?  502 VAD B CB  1 
HETATM 6524 C  CG1 . VAD J 5 .   ? 26.126  11.645  -43.083 1.00 13.84 ?  502 VAD B CG1 1 
HETATM 6525 C  CG2 . VAD J 5 .   ? 24.467  11.287  -41.245 1.00 18.43 ?  502 VAD B CG2 1 
HETATM 6526 C  C   . VAD J 5 .   ? 24.149  10.075  -44.807 1.00 12.16 ?  502 VAD B C   1 
HETATM 6527 O  O   . VAD J 5 .   ? 24.403  8.857   -44.686 1.00 13.62 -1 502 VAD B O   1 
HETATM 6528 O  OXT . VAD J 5 .   ? 24.212  10.647  -45.925 1.00 12.97 ?  502 VAD B OXT 1 
HETATM 6529 O  OE  . VAD J 5 .   ? 23.472  12.181  -44.004 1.00 14.89 ?  502 VAD B OE  1 
HETATM 6530 NI NI  . NI  K 6 .   ? 20.522  9.676   -42.110 1.00 13.90 ?  503 NI  B NI  1 
HETATM 6531 O  O   . HOH L 7 .   ? 14.383  -12.889 22.686  1.00 29.63 ?  601 HOH A O   1 
HETATM 6532 O  O   . HOH L 7 .   ? 23.638  -4.172  -15.150 1.00 33.52 ?  602 HOH A O   1 
HETATM 6533 O  O   . HOH L 7 .   ? 40.217  -3.722  12.012  1.00 34.97 ?  603 HOH A O   1 
HETATM 6534 O  O   . HOH L 7 .   ? -15.545 6.147   13.862  1.00 38.81 ?  604 HOH A O   1 
HETATM 6535 O  O   . HOH L 7 .   ? 47.225  5.039   10.417  1.00 22.77 ?  605 HOH A O   1 
HETATM 6536 O  O   . HOH L 7 .   ? 11.882  14.558  17.167  1.00 24.41 ?  606 HOH A O   1 
HETATM 6537 O  O   . HOH L 7 .   ? 5.892   24.735  17.471  1.00 34.23 ?  607 HOH A O   1 
HETATM 6538 O  O   . HOH L 7 .   ? 1.699   -11.047 13.506  1.00 25.99 ?  608 HOH A O   1 
HETATM 6539 O  O   . HOH L 7 .   ? 28.938  0.395   -16.491 1.00 22.79 ?  609 HOH A O   1 
HETATM 6540 O  O   . HOH L 7 .   ? 27.194  5.878   14.714  1.00 18.63 ?  610 HOH A O   1 
HETATM 6541 O  O   . HOH L 7 .   ? 11.253  12.990  -15.096 1.00 24.52 ?  611 HOH A O   1 
HETATM 6542 O  O   . HOH L 7 .   ? 2.216   17.214  4.561   1.00 29.52 ?  612 HOH A O   1 
HETATM 6543 O  O   . HOH L 7 .   ? -14.456 7.897   18.977  1.00 38.06 ?  613 HOH A O   1 
HETATM 6544 O  O   . HOH L 7 .   ? -1.161  17.658  16.703  1.00 31.69 ?  614 HOH A O   1 
HETATM 6545 O  O   . HOH L 7 .   ? 16.217  -9.840  5.834   1.00 21.99 ?  615 HOH A O   1 
HETATM 6546 O  O   . HOH L 7 .   ? 22.227  24.869  -7.046  1.00 19.95 ?  616 HOH A O   1 
HETATM 6547 O  O   . HOH L 7 .   ? 33.488  14.551  17.444  1.00 36.87 ?  617 HOH A O   1 
HETATM 6548 O  O   . HOH L 7 .   ? 21.556  6.689   19.347  1.00 15.27 ?  618 HOH A O   1 
HETATM 6549 O  O   . HOH L 7 .   ? 32.416  17.560  -2.258  1.00 19.18 ?  619 HOH A O   1 
HETATM 6550 O  O   . HOH L 7 .   ? 25.850  -8.545  -5.315  1.00 19.40 ?  620 HOH A O   1 
HETATM 6551 O  O   . HOH L 7 .   ? 21.245  28.451  -2.737  1.00 44.62 ?  621 HOH A O   1 
HETATM 6552 O  O   . HOH L 7 .   ? 30.447  -7.664  32.074  1.00 13.70 ?  622 HOH A O   1 
HETATM 6553 O  O   . HOH L 7 .   ? 30.710  8.995   -23.461 1.00 21.56 ?  623 HOH A O   1 
HETATM 6554 O  O   . HOH L 7 .   ? 16.998  19.581  12.924  1.00 20.40 ?  624 HOH A O   1 
HETATM 6555 O  O   . HOH L 7 .   ? 16.836  8.098   7.274   1.00 11.55 ?  625 HOH A O   1 
HETATM 6556 O  O   . HOH L 7 .   ? 11.814  -5.360  -6.071  1.00 20.20 ?  626 HOH A O   1 
HETATM 6557 O  O   . HOH L 7 .   ? 37.093  -5.531  25.555  1.00 26.10 ?  627 HOH A O   1 
HETATM 6558 O  O   . HOH L 7 .   ? 7.762   7.525   14.823  1.00 13.90 ?  628 HOH A O   1 
HETATM 6559 O  O   . HOH L 7 .   ? -1.783  -5.741  27.184  1.00 31.19 ?  629 HOH A O   1 
HETATM 6560 O  O   . HOH L 7 .   ? 2.948   25.374  1.274   1.00 31.18 ?  630 HOH A O   1 
HETATM 6561 O  O   . HOH L 7 .   ? 41.595  7.624   -9.855  1.00 33.15 ?  631 HOH A O   1 
HETATM 6562 O  O   . HOH L 7 .   ? 23.095  -3.228  8.819   1.00 13.45 ?  632 HOH A O   1 
HETATM 6563 O  O   . HOH L 7 .   ? 12.422  -6.112  -1.784  1.00 19.14 ?  633 HOH A O   1 
HETATM 6564 O  O   . HOH L 7 .   ? 42.707  1.339   -3.409  1.00 22.69 ?  634 HOH A O   1 
HETATM 6565 O  O   . HOH L 7 .   ? 13.958  -9.211  -4.350  1.00 20.24 ?  635 HOH A O   1 
HETATM 6566 O  O   . HOH L 7 .   ? 10.098  13.701  5.785   1.00 15.81 ?  636 HOH A O   1 
HETATM 6567 O  O   . HOH L 7 .   ? 9.305   22.735  -1.689  1.00 15.74 ?  637 HOH A O   1 
HETATM 6568 O  O   . HOH L 7 .   ? 8.310   25.753  1.480   1.00 28.67 ?  638 HOH A O   1 
HETATM 6569 O  O   . HOH L 7 .   ? 29.638  26.416  -9.978  1.00 21.59 ?  639 HOH A O   1 
HETATM 6570 O  O   . HOH L 7 .   ? 22.305  -9.861  -4.920  1.00 21.01 ?  640 HOH A O   1 
HETATM 6571 O  O   . HOH L 7 .   ? 2.174   1.084   -3.195  1.00 25.18 ?  641 HOH A O   1 
HETATM 6572 O  O   . HOH L 7 .   ? 0.501   9.434   1.933   1.00 28.64 ?  642 HOH A O   1 
HETATM 6573 O  O   . HOH L 7 .   ? 9.326   11.963  3.631   1.00 12.71 ?  643 HOH A O   1 
HETATM 6574 O  O   . HOH L 7 .   ? 33.566  16.480  11.446  1.00 19.80 ?  644 HOH A O   1 
HETATM 6575 O  O   . HOH L 7 .   ? 26.343  7.538   -19.064 1.00 16.95 ?  645 HOH A O   1 
HETATM 6576 O  O   . HOH L 7 .   ? 18.977  11.003  22.667  1.00 20.54 ?  646 HOH A O   1 
HETATM 6577 O  O   . HOH L 7 .   ? 3.129   -3.102  26.155  1.00 24.55 ?  647 HOH A O   1 
HETATM 6578 O  O   . HOH L 7 .   ? 28.245  -8.276  20.496  1.00 14.64 ?  648 HOH A O   1 
HETATM 6579 O  O   . HOH L 7 .   ? 28.387  7.007   -20.740 1.00 19.63 ?  649 HOH A O   1 
HETATM 6580 O  O   . HOH L 7 .   ? 14.088  -13.847 8.533   1.00 34.33 ?  650 HOH A O   1 
HETATM 6581 O  O   . HOH L 7 .   ? 32.576  -0.678  22.452  1.00 17.93 ?  651 HOH A O   1 
HETATM 6582 O  O   . HOH L 7 .   ? -0.130  7.259   5.426   1.00 20.10 ?  652 HOH A O   1 
HETATM 6583 O  O   . HOH L 7 .   ? 5.267   9.846   33.033  1.00 29.93 ?  653 HOH A O   1 
HETATM 6584 O  O   . HOH L 7 .   ? 11.742  11.112  14.067  1.00 17.68 ?  654 HOH A O   1 
HETATM 6585 O  O   . HOH L 7 .   ? 29.378  -8.356  3.456   1.00 17.20 ?  655 HOH A O   1 
HETATM 6586 O  O   . HOH L 7 .   ? 14.290  -11.043 7.599   1.00 16.28 ?  656 HOH A O   1 
HETATM 6587 O  O   . HOH L 7 .   ? 4.551   18.626  0.514   1.00 15.95 ?  657 HOH A O   1 
HETATM 6588 O  O   . HOH L 7 .   ? 28.262  17.465  21.861  1.00 28.22 ?  658 HOH A O   1 
HETATM 6589 O  O   . HOH L 7 .   ? 22.888  -6.921  7.869   1.00 14.93 ?  659 HOH A O   1 
HETATM 6590 O  O   . HOH L 7 .   ? -9.042  0.499   13.549  1.00 14.30 ?  660 HOH A O   1 
HETATM 6591 O  O   . HOH L 7 .   ? 26.947  25.426  -16.153 1.00 17.32 ?  661 HOH A O   1 
HETATM 6592 O  O   . HOH L 7 .   ? 10.947  1.336   -3.592  1.00 22.28 ?  662 HOH A O   1 
HETATM 6593 O  O   . HOH L 7 .   ? 6.653   -11.355 6.162   1.00 30.14 ?  663 HOH A O   1 
HETATM 6594 O  O   . HOH L 7 .   ? 10.494  15.694  3.902   1.00 13.19 ?  664 HOH A O   1 
HETATM 6595 O  O   . HOH L 7 .   ? 9.406   9.558   -5.527  1.00 26.97 ?  665 HOH A O   1 
HETATM 6596 O  O   . HOH L 7 .   ? 21.684  8.183   22.663  1.00 16.83 ?  666 HOH A O   1 
HETATM 6597 O  O   . HOH L 7 .   ? 36.392  15.992  0.034   1.00 29.40 ?  667 HOH A O   1 
HETATM 6598 O  O   . HOH L 7 .   ? 28.954  -1.700  17.120  1.00 11.49 ?  668 HOH A O   1 
HETATM 6599 O  O   . HOH L 7 .   ? 33.488  24.329  -2.079  1.00 19.51 ?  669 HOH A O   1 
HETATM 6600 O  O   . HOH L 7 .   ? 34.516  13.455  14.792  1.00 21.83 ?  670 HOH A O   1 
HETATM 6601 O  O   . HOH L 7 .   ? 16.352  25.783  8.540   1.00 23.85 ?  671 HOH A O   1 
HETATM 6602 O  O   . HOH L 7 .   ? 10.662  15.383  -13.691 1.00 16.45 ?  672 HOH A O   1 
HETATM 6603 O  O   . HOH L 7 .   ? 27.169  27.121  -9.291  1.00 18.57 ?  673 HOH A O   1 
HETATM 6604 O  O   . HOH L 7 .   ? 8.105   16.623  -7.270  1.00 15.25 ?  674 HOH A O   1 
HETATM 6605 O  O   . HOH L 7 .   ? 38.223  -1.720  20.014  1.00 26.58 ?  675 HOH A O   1 
HETATM 6606 O  O   . HOH L 7 .   ? 20.724  1.876   24.689  1.00 11.52 ?  676 HOH A O   1 
HETATM 6607 O  O   . HOH L 7 .   ? -1.474  11.583  27.977  1.00 19.95 ?  677 HOH A O   1 
HETATM 6608 O  O   . HOH L 7 .   ? 1.462   -0.744  27.398  1.00 22.63 ?  678 HOH A O   1 
HETATM 6609 O  O   . HOH L 7 .   ? 15.633  6.301   26.626  1.00 20.66 ?  679 HOH A O   1 
HETATM 6610 O  O   . HOH L 7 .   ? 15.237  14.109  18.426  1.00 26.05 ?  680 HOH A O   1 
HETATM 6611 O  O   . HOH L 7 .   ? 35.670  15.200  13.834  1.00 30.22 ?  681 HOH A O   1 
HETATM 6612 O  O   . HOH L 7 .   ? 7.959   22.027  10.594  1.00 28.28 ?  682 HOH A O   1 
HETATM 6613 O  O   . HOH L 7 .   ? 10.990  15.965  24.162  1.00 27.09 ?  683 HOH A O   1 
HETATM 6614 O  O   . HOH L 7 .   ? 14.587  -3.234  28.906  1.00 32.92 ?  684 HOH A O   1 
HETATM 6615 O  O   . HOH L 7 .   ? -0.918  -8.550  23.657  1.00 22.36 ?  685 HOH A O   1 
HETATM 6616 O  O   . HOH L 7 .   ? 32.376  -4.172  -0.839  1.00 11.03 ?  686 HOH A O   1 
HETATM 6617 O  O   . HOH L 7 .   ? 14.596  9.543   19.987  1.00 27.64 ?  687 HOH A O   1 
HETATM 6618 O  O   . HOH L 7 .   ? 13.907  7.350   13.952  1.00 12.19 ?  688 HOH A O   1 
HETATM 6619 O  O   . HOH L 7 .   ? 17.871  8.267   3.116   1.00 14.28 ?  689 HOH A O   1 
HETATM 6620 O  O   . HOH L 7 .   ? 24.170  -9.327  7.489   1.00 22.15 ?  690 HOH A O   1 
HETATM 6621 O  O   . HOH L 7 .   ? 20.338  6.902   -4.040  1.00 11.52 ?  691 HOH A O   1 
HETATM 6622 O  O   . HOH L 7 .   ? 22.804  19.840  -16.466 1.00 15.86 ?  692 HOH A O   1 
HETATM 6623 O  O   . HOH L 7 .   ? 6.669   18.805  2.456   1.00 17.39 ?  693 HOH A O   1 
HETATM 6624 O  O   . HOH L 7 .   ? 9.619   -0.317  29.293  1.00 29.21 ?  694 HOH A O   1 
HETATM 6625 O  O   . HOH L 7 .   ? 33.708  -8.381  19.410  1.00 30.84 ?  695 HOH A O   1 
HETATM 6626 O  O   . HOH L 7 .   ? 25.998  -7.706  5.711   1.00 23.90 ?  696 HOH A O   1 
HETATM 6627 O  O   . HOH L 7 .   ? 15.152  -3.773  5.864   1.00 10.26 ?  697 HOH A O   1 
HETATM 6628 O  O   . HOH L 7 .   ? 12.686  14.120  2.964   1.00 10.08 ?  698 HOH A O   1 
HETATM 6629 O  O   . HOH L 7 .   ? 40.397  -3.783  -2.461  1.00 21.99 ?  699 HOH A O   1 
HETATM 6630 O  O   . HOH L 7 .   ? 10.165  7.516   -4.133  1.00 22.35 ?  700 HOH A O   1 
HETATM 6631 O  O   . HOH L 7 .   ? 28.077  27.854  -4.547  1.00 28.90 ?  701 HOH A O   1 
HETATM 6632 O  O   . HOH L 7 .   ? 4.622   20.011  10.623  1.00 32.68 ?  702 HOH A O   1 
HETATM 6633 O  O   . HOH L 7 .   ? 37.603  11.866  15.264  1.00 15.60 ?  703 HOH A O   1 
HETATM 6634 O  O   . HOH L 7 .   ? 27.209  -4.963  3.704   1.00 11.81 ?  704 HOH A O   1 
HETATM 6635 O  O   . HOH L 7 .   ? 33.193  17.999  -19.853 1.00 28.39 ?  705 HOH A O   1 
HETATM 6636 O  O   . HOH L 7 .   ? 17.611  -13.118 7.485   1.00 26.92 ?  706 HOH A O   1 
HETATM 6637 O  O   . HOH L 7 .   ? 13.719  -1.618  4.986   1.00 10.78 ?  707 HOH A O   1 
HETATM 6638 O  O   . HOH L 7 .   ? 16.910  23.303  -6.406  1.00 24.85 ?  708 HOH A O   1 
HETATM 6639 O  O   . HOH L 7 .   ? 18.169  7.377   18.762  1.00 17.04 ?  709 HOH A O   1 
HETATM 6640 O  O   . HOH L 7 .   ? 10.917  -10.258 24.467  1.00 20.51 ?  710 HOH A O   1 
HETATM 6641 O  O   . HOH L 7 .   ? 27.207  -12.111 19.339  1.00 29.69 ?  711 HOH A O   1 
HETATM 6642 O  O   . HOH L 7 .   ? 3.514   15.538  3.139   1.00 25.77 ?  712 HOH A O   1 
HETATM 6643 O  O   . HOH L 7 .   ? 37.718  18.164  -14.571 1.00 29.07 ?  713 HOH A O   1 
HETATM 6644 O  O   . HOH L 7 .   ? -5.784  9.357   33.401  1.00 32.10 ?  714 HOH A O   1 
HETATM 6645 O  O   . HOH L 7 .   ? 19.907  -3.982  1.245   1.00 10.56 ?  715 HOH A O   1 
HETATM 6646 O  O   . HOH L 7 .   ? 40.603  14.556  3.319   1.00 19.44 ?  716 HOH A O   1 
HETATM 6647 O  O   . HOH L 7 .   ? 30.122  -6.357  -5.437  1.00 22.77 ?  717 HOH A O   1 
HETATM 6648 O  O   . HOH L 7 .   ? 20.108  -10.250 -0.988  1.00 18.26 ?  718 HOH A O   1 
HETATM 6649 O  O   . HOH L 7 .   ? 43.523  2.244   13.557  1.00 17.29 ?  719 HOH A O   1 
HETATM 6650 O  O   . HOH L 7 .   ? 20.582  16.256  -19.169 1.00 22.15 ?  720 HOH A O   1 
HETATM 6651 O  O   . HOH L 7 .   ? 12.267  16.430  -17.127 1.00 28.73 ?  721 HOH A O   1 
HETATM 6652 O  O   . HOH L 7 .   ? 22.131  -8.423  -8.452  1.00 22.52 ?  722 HOH A O   1 
HETATM 6653 O  O   . HOH L 7 .   ? 2.963   -7.814  6.020   1.00 18.43 ?  723 HOH A O   1 
HETATM 6654 O  O   . HOH L 7 .   ? 20.246  8.153   -7.584  1.00 27.43 ?  724 HOH A O   1 
HETATM 6655 O  O   . HOH L 7 .   ? 27.652  15.702  3.917   1.00 9.68  ?  725 HOH A O   1 
HETATM 6656 O  O   . HOH L 7 .   ? -0.200  16.912  24.642  1.00 31.14 ?  726 HOH A O   1 
HETATM 6657 O  O   . HOH L 7 .   ? 40.041  8.406   -1.691  1.00 23.90 ?  727 HOH A O   1 
HETATM 6658 O  O   . HOH L 7 .   ? 0.706   -14.663 15.182  1.00 28.57 ?  728 HOH A O   1 
HETATM 6659 O  O   . HOH L 7 .   ? 26.544  -1.027  19.293  1.00 12.65 ?  729 HOH A O   1 
HETATM 6660 O  O   . HOH L 7 .   ? 8.219   -5.996  -2.534  1.00 27.45 ?  730 HOH A O   1 
HETATM 6661 O  O   . HOH L 7 .   ? 22.530  -3.801  31.626  1.00 20.66 ?  731 HOH A O   1 
HETATM 6662 O  O   . HOH L 7 .   ? 20.218  24.106  9.366   1.00 29.78 ?  732 HOH A O   1 
HETATM 6663 O  O   . HOH L 7 .   ? 26.685  1.071   -23.817 1.00 33.20 ?  733 HOH A O   1 
HETATM 6664 O  O   . HOH L 7 .   ? 5.801   7.925   3.530   1.00 19.28 ?  734 HOH A O   1 
HETATM 6665 O  O   . HOH L 7 .   ? 36.093  15.301  -2.183  1.00 26.46 ?  735 HOH A O   1 
HETATM 6666 O  O   . HOH L 7 .   ? 8.884   -10.745 1.579   1.00 34.04 ?  736 HOH A O   1 
HETATM 6667 O  O   . HOH L 7 .   ? 9.121   17.668  2.086   1.00 11.10 ?  737 HOH A O   1 
HETATM 6668 O  O   . HOH L 7 .   ? -1.809  13.272  16.972  1.00 12.05 ?  738 HOH A O   1 
HETATM 6669 O  O   . HOH L 7 .   ? 41.970  2.265   15.749  1.00 27.12 ?  739 HOH A O   1 
HETATM 6670 O  O   . HOH L 7 .   ? -4.930  9.667   7.173   1.00 29.84 ?  740 HOH A O   1 
HETATM 6671 O  O   . HOH L 7 .   ? 25.861  -6.556  1.214   1.00 13.06 ?  741 HOH A O   1 
HETATM 6672 O  O   . HOH L 7 .   ? 2.687   11.874  9.299   1.00 11.04 ?  742 HOH A O   1 
HETATM 6673 O  O   . HOH L 7 .   ? -3.036  4.224   1.450   1.00 32.86 ?  743 HOH A O   1 
HETATM 6674 O  O   . HOH L 7 .   ? -0.137  -7.704  15.036  1.00 22.24 ?  744 HOH A O   1 
HETATM 6675 O  O   . HOH L 7 .   ? 14.245  5.302   4.599   1.00 11.18 ?  745 HOH A O   1 
HETATM 6676 O  O   . HOH L 7 .   ? 14.759  3.449   -4.720  1.00 14.00 ?  746 HOH A O   1 
HETATM 6677 O  O   . HOH L 7 .   ? 0.263   -4.140  3.291   1.00 19.33 ?  747 HOH A O   1 
HETATM 6678 O  O   . HOH L 7 .   ? 2.283   2.661   3.131   1.00 13.97 ?  748 HOH A O   1 
HETATM 6679 O  O   . HOH L 7 .   ? 32.871  22.340  1.897   1.00 28.83 ?  749 HOH A O   1 
HETATM 6680 O  O   . HOH L 7 .   ? 13.497  1.769   -2.622  1.00 11.88 ?  750 HOH A O   1 
HETATM 6681 O  O   . HOH L 7 .   ? 2.604   15.505  29.724  1.00 30.31 ?  751 HOH A O   1 
HETATM 6682 O  O   . HOH L 7 .   ? 15.462  5.411   -16.769 1.00 21.04 ?  752 HOH A O   1 
HETATM 6683 O  O   . HOH L 7 .   ? 33.432  3.090   19.503  1.00 14.97 ?  753 HOH A O   1 
HETATM 6684 O  O   . HOH L 7 .   ? 5.008   1.293   8.359   1.00 8.07  ?  754 HOH A O   1 
HETATM 6685 O  O   . HOH L 7 .   ? 26.840  -10.384 21.523  1.00 21.75 ?  755 HOH A O   1 
HETATM 6686 O  O   . HOH L 7 .   ? 13.219  9.487   12.604  1.00 13.84 ?  756 HOH A O   1 
HETATM 6687 O  O   . HOH L 7 .   ? 7.256   -9.268  24.925  1.00 34.60 ?  757 HOH A O   1 
HETATM 6688 O  O   . HOH L 7 .   ? 11.703  -5.188  -10.070 1.00 24.04 ?  758 HOH A O   1 
HETATM 6689 O  O   . HOH L 7 .   ? 29.654  -10.464 24.088  1.00 33.65 ?  759 HOH A O   1 
HETATM 6690 O  O   . HOH L 7 .   ? 12.176  11.984  16.633  1.00 16.02 ?  760 HOH A O   1 
HETATM 6691 O  O   . HOH L 7 .   ? -9.170  5.606   29.739  1.00 27.79 ?  761 HOH A O   1 
HETATM 6692 O  O   . HOH L 7 .   ? 37.870  11.549  -7.084  1.00 20.90 ?  762 HOH A O   1 
HETATM 6693 O  O   . HOH L 7 .   ? 27.949  -0.332  -19.632 1.00 31.00 ?  763 HOH A O   1 
HETATM 6694 O  O   . HOH L 7 .   ? 38.524  -1.779  13.658  1.00 20.43 ?  764 HOH A O   1 
HETATM 6695 O  O   . HOH L 7 .   ? 37.585  14.038  -4.274  1.00 24.71 ?  765 HOH A O   1 
HETATM 6696 O  O   . HOH L 7 .   ? -9.950  1.795   26.675  1.00 25.73 ?  766 HOH A O   1 
HETATM 6697 O  O   . HOH L 7 .   ? 31.793  1.989   21.476  1.00 15.21 ?  767 HOH A O   1 
HETATM 6698 O  O   . HOH L 7 .   ? 12.120  -7.849  0.698   1.00 19.63 ?  768 HOH A O   1 
HETATM 6699 O  O   . HOH L 7 .   ? 10.698  -4.384  -2.566  1.00 20.43 ?  769 HOH A O   1 
HETATM 6700 O  O   . HOH L 7 .   ? 30.604  1.515   29.250  1.00 34.90 ?  770 HOH A O   1 
HETATM 6701 O  O   . HOH L 7 .   ? 16.352  21.667  -16.967 1.00 17.06 ?  771 HOH A O   1 
HETATM 6702 O  O   . HOH L 7 .   ? 15.910  -5.705  4.002   1.00 17.56 ?  772 HOH A O   1 
HETATM 6703 O  O   . HOH L 7 .   ? 19.174  -6.633  9.894   1.00 14.43 ?  773 HOH A O   1 
HETATM 6704 O  O   . HOH L 7 .   ? 11.687  -0.046  -14.773 1.00 27.01 ?  774 HOH A O   1 
HETATM 6705 O  O   . HOH L 7 .   ? 17.414  18.007  -0.955  1.00 18.26 ?  775 HOH A O   1 
HETATM 6706 O  O   . HOH L 7 .   ? 17.651  16.620  -19.556 1.00 30.25 ?  776 HOH A O   1 
HETATM 6707 O  O   . HOH L 7 .   ? 44.104  -0.684  2.253   1.00 19.48 ?  777 HOH A O   1 
HETATM 6708 O  O   . HOH L 7 .   ? 14.158  11.167  18.124  1.00 26.53 ?  778 HOH A O   1 
HETATM 6709 O  O   . HOH L 7 .   ? 31.707  -0.580  25.220  1.00 21.64 ?  779 HOH A O   1 
HETATM 6710 O  O   . HOH L 7 .   ? 30.790  -2.849  22.256  1.00 15.24 ?  780 HOH A O   1 
HETATM 6711 O  O   . HOH L 7 .   ? 14.646  -7.187  28.292  1.00 20.00 ?  781 HOH A O   1 
HETATM 6712 O  O   . HOH L 7 .   ? 18.541  9.996   -20.844 1.00 35.47 ?  782 HOH A O   1 
HETATM 6713 O  O   . HOH L 7 .   ? 35.054  5.176   20.056  1.00 24.78 ?  783 HOH A O   1 
HETATM 6714 O  O   . HOH L 7 .   ? 36.299  -10.047 -3.153  1.00 29.15 ?  784 HOH A O   1 
HETATM 6715 O  O   . HOH L 7 .   ? 20.095  -11.555 28.155  1.00 22.36 ?  785 HOH A O   1 
HETATM 6716 O  O   . HOH L 7 .   ? 14.891  22.495  -4.742  1.00 17.92 ?  786 HOH A O   1 
HETATM 6717 O  O   . HOH L 7 .   ? 20.664  9.023   1.544   1.00 10.31 ?  787 HOH A O   1 
HETATM 6718 O  O   . HOH L 7 .   ? 23.910  -6.076  -11.717 1.00 28.29 ?  788 HOH A O   1 
HETATM 6719 O  O   . HOH L 7 .   ? 36.011  -3.389  -3.959  1.00 21.32 ?  789 HOH A O   1 
HETATM 6720 O  O   . HOH L 7 .   ? 9.165   13.097  26.900  1.00 31.42 ?  790 HOH A O   1 
HETATM 6721 O  O   . HOH L 7 .   ? 26.345  -1.546  35.059  1.00 26.79 ?  791 HOH A O   1 
HETATM 6722 O  O   . HOH L 7 .   ? 37.893  14.136  -9.341  1.00 25.68 ?  792 HOH A O   1 
HETATM 6723 O  O   . HOH L 7 .   ? 24.729  -13.303 18.462  1.00 30.11 ?  793 HOH A O   1 
HETATM 6724 O  O   . HOH L 7 .   ? 28.794  -10.387 13.475  1.00 17.43 ?  794 HOH A O   1 
HETATM 6725 O  O   . HOH L 7 .   ? 7.060   -4.357  4.423   1.00 8.46  ?  795 HOH A O   1 
HETATM 6726 O  O   . HOH L 7 .   ? 35.507  -7.333  16.431  1.00 26.80 ?  796 HOH A O   1 
HETATM 6727 O  O   . HOH L 7 .   ? 25.781  -1.765  -21.786 1.00 32.55 ?  797 HOH A O   1 
HETATM 6728 O  O   . HOH L 7 .   ? 5.273   20.576  27.768  1.00 34.27 ?  798 HOH A O   1 
HETATM 6729 O  O   . HOH L 7 .   ? 24.657  -13.125 6.581   1.00 31.07 ?  799 HOH A O   1 
HETATM 6730 O  O   . HOH L 7 .   ? 21.480  22.593  -5.714  1.00 16.50 ?  800 HOH A O   1 
HETATM 6731 O  O   . HOH L 7 .   ? -9.119  2.397   20.477  1.00 19.62 ?  801 HOH A O   1 
HETATM 6732 O  O   . HOH L 7 .   ? 28.048  19.923  10.074  1.00 27.51 ?  802 HOH A O   1 
HETATM 6733 O  O   . HOH L 7 .   ? 20.742  -7.079  6.074   1.00 13.69 ?  803 HOH A O   1 
HETATM 6734 O  O   . HOH L 7 .   ? 14.443  2.992   32.832  1.00 32.05 ?  804 HOH A O   1 
HETATM 6735 O  O   . HOH L 7 .   ? 45.757  8.011   10.324  1.00 27.34 ?  805 HOH A O   1 
HETATM 6736 O  O   . HOH L 7 .   ? 41.250  -1.686  11.229  1.00 21.85 ?  806 HOH A O   1 
HETATM 6737 O  O   . HOH L 7 .   ? 8.824   9.847   14.397  1.00 11.02 ?  807 HOH A O   1 
HETATM 6738 O  O   . HOH L 7 .   ? 10.831  17.620  22.190  1.00 20.07 ?  808 HOH A O   1 
HETATM 6739 O  O   . HOH L 7 .   ? -1.558  -2.320  28.168  1.00 25.23 ?  809 HOH A O   1 
HETATM 6740 O  O   . HOH L 7 .   ? -0.498  2.962   -1.060  1.00 30.93 ?  810 HOH A O   1 
HETATM 6741 O  O   . HOH L 7 .   ? 21.036  26.100  -14.014 1.00 25.91 ?  811 HOH A O   1 
HETATM 6742 O  O   . HOH L 7 .   ? -3.578  -8.357  23.053  1.00 20.46 ?  812 HOH A O   1 
HETATM 6743 O  O   . HOH L 7 .   ? -3.783  -9.129  20.493  1.00 16.61 ?  813 HOH A O   1 
HETATM 6744 O  O   . HOH L 7 .   ? 27.155  20.621  -15.540 1.00 12.63 ?  814 HOH A O   1 
HETATM 6745 O  O   . HOH L 7 .   ? 9.632   3.900   3.524   1.00 9.57  ?  815 HOH A O   1 
HETATM 6746 O  O   . HOH L 7 .   ? 33.937  -3.250  -10.436 1.00 27.29 ?  816 HOH A O   1 
HETATM 6747 O  O   . HOH L 7 .   ? 29.561  4.261   -23.913 1.00 28.84 ?  817 HOH A O   1 
HETATM 6748 O  O   . HOH L 7 .   ? 20.120  -16.358 12.926  1.00 30.27 ?  818 HOH A O   1 
HETATM 6749 O  O   . HOH L 7 .   ? 31.963  -7.663  -4.807  1.00 28.14 ?  819 HOH A O   1 
HETATM 6750 O  O   . HOH L 7 .   ? 8.354   13.883  -7.411  1.00 14.93 ?  820 HOH A O   1 
HETATM 6751 O  O   . HOH L 7 .   ? 21.464  -4.548  -12.491 1.00 27.08 ?  821 HOH A O   1 
HETATM 6752 O  O   . HOH L 7 .   ? 25.873  -12.411 -2.543  1.00 34.52 ?  822 HOH A O   1 
HETATM 6753 O  O   . HOH L 7 .   ? 15.705  6.902   11.842  1.00 9.92  ?  823 HOH A O   1 
HETATM 6754 O  O   . HOH L 7 .   ? 22.032  23.112  7.883   1.00 25.42 ?  824 HOH A O   1 
HETATM 6755 O  O   . HOH L 7 .   ? 3.913   18.150  -11.918 1.00 33.96 ?  825 HOH A O   1 
HETATM 6756 O  O   . HOH L 7 .   ? 29.205  -6.840  -12.218 1.00 34.60 ?  826 HOH A O   1 
HETATM 6757 O  O   . HOH L 7 .   ? 35.888  17.089  -4.710  1.00 28.00 ?  827 HOH A O   1 
HETATM 6758 O  O   . HOH L 7 .   ? 13.322  1.521   -17.833 1.00 25.03 ?  828 HOH A O   1 
HETATM 6759 O  O   . HOH L 7 .   ? 24.976  11.891  -0.853  1.00 9.86  ?  829 HOH A O   1 
HETATM 6760 O  O   . HOH L 7 .   ? 13.046  4.164   -8.053  1.00 31.19 ?  830 HOH A O   1 
HETATM 6761 O  O   . HOH L 7 .   ? 2.285   -16.575 16.727  1.00 21.00 ?  831 HOH A O   1 
HETATM 6762 O  O   . HOH L 7 .   ? 7.287   9.942   2.698   1.00 20.10 ?  832 HOH A O   1 
HETATM 6763 O  O   . HOH L 7 .   ? 10.808  19.279  -19.139 1.00 24.86 ?  833 HOH A O   1 
HETATM 6764 O  O   . HOH L 7 .   ? 14.691  11.417  -19.200 1.00 32.12 ?  834 HOH A O   1 
HETATM 6765 O  O   . HOH L 7 .   ? 12.171  -13.177 9.954   1.00 21.14 ?  835 HOH A O   1 
HETATM 6766 O  O   . HOH L 7 .   ? 3.281   7.469   31.562  1.00 31.53 ?  836 HOH A O   1 
HETATM 6767 O  O   . HOH L 7 .   ? 44.347  8.736   15.481  1.00 32.20 ?  837 HOH A O   1 
HETATM 6768 O  O   . HOH L 7 .   ? 10.063  22.275  -11.249 1.00 16.83 ?  838 HOH A O   1 
HETATM 6769 O  O   . HOH L 7 .   ? 28.301  16.664  6.507   1.00 11.57 ?  839 HOH A O   1 
HETATM 6770 O  O   . HOH L 7 .   ? -8.807  4.722   2.451   1.00 25.52 ?  840 HOH A O   1 
HETATM 6771 O  O   . HOH L 7 .   ? 6.433   -4.218  1.773   1.00 18.39 ?  841 HOH A O   1 
HETATM 6772 O  O   . HOH L 7 .   ? 29.131  -4.291  16.136  1.00 13.20 ?  842 HOH A O   1 
HETATM 6773 O  O   . HOH L 7 .   ? -0.668  14.350  27.835  1.00 32.82 ?  843 HOH A O   1 
HETATM 6774 O  O   . HOH L 7 .   ? 17.327  3.577   -3.384  1.00 10.25 ?  844 HOH A O   1 
HETATM 6775 O  O   . HOH L 7 .   ? 40.788  8.907   -4.275  1.00 26.99 ?  845 HOH A O   1 
HETATM 6776 O  O   . HOH L 7 .   ? 2.116   14.503  0.770   1.00 31.22 ?  846 HOH A O   1 
HETATM 6777 O  O   . HOH L 7 .   ? 27.784  -7.034  -6.791  1.00 19.35 ?  847 HOH A O   1 
HETATM 6778 O  O   . HOH L 7 .   ? 40.618  12.039  10.342  1.00 21.19 ?  848 HOH A O   1 
HETATM 6779 O  O   . HOH L 7 .   ? 8.294   5.685   -2.968  1.00 15.30 ?  849 HOH A O   1 
HETATM 6780 O  O   . HOH L 7 .   ? 16.301  -1.564  27.818  1.00 22.25 ?  850 HOH A O   1 
HETATM 6781 O  O   . HOH L 7 .   ? 36.943  -9.694  5.698   1.00 24.91 ?  851 HOH A O   1 
HETATM 6782 O  O   . HOH L 7 .   ? 39.154  2.631   18.587  1.00 31.15 ?  852 HOH A O   1 
HETATM 6783 O  O   . HOH L 7 .   ? -7.330  -7.078  25.339  1.00 28.28 ?  853 HOH A O   1 
HETATM 6784 O  O   . HOH L 7 .   ? 40.126  -10.837 3.616   1.00 31.21 ?  854 HOH A O   1 
HETATM 6785 O  O   . HOH L 7 .   ? 15.482  5.747   7.163   1.00 9.77  ?  855 HOH A O   1 
HETATM 6786 O  O   . HOH L 7 .   ? 14.764  -9.097  -1.621  1.00 28.82 ?  856 HOH A O   1 
HETATM 6787 O  O   . HOH L 7 .   ? 17.693  25.711  2.212   1.00 27.14 ?  857 HOH A O   1 
HETATM 6788 O  O   . HOH L 7 .   ? 33.217  20.695  -3.914  1.00 26.31 ?  858 HOH A O   1 
HETATM 6789 O  O   . HOH L 7 .   ? 14.311  7.216   9.479   1.00 12.11 ?  859 HOH A O   1 
HETATM 6790 O  O   . HOH L 7 .   ? 41.902  -4.577  2.435   1.00 25.98 ?  860 HOH A O   1 
HETATM 6791 O  O   . HOH L 7 .   ? 16.270  25.282  -17.435 1.00 26.83 ?  861 HOH A O   1 
HETATM 6792 O  O   . HOH L 7 .   ? 36.358  12.281  -20.033 1.00 31.03 ?  862 HOH A O   1 
HETATM 6793 O  O   . HOH L 7 .   ? 18.852  -0.951  28.684  1.00 24.89 ?  863 HOH A O   1 
HETATM 6794 O  O   . HOH L 7 .   ? 15.517  -10.787 -7.706  1.00 19.49 ?  864 HOH A O   1 
HETATM 6795 O  O   . HOH L 7 .   ? 11.335  7.857   -13.598 1.00 32.99 ?  865 HOH A O   1 
HETATM 6796 O  O   . HOH L 7 .   ? 13.975  25.884  -6.350  1.00 40.90 ?  866 HOH A O   1 
HETATM 6797 O  O   . HOH L 7 .   ? 36.812  10.661  -23.470 1.00 34.05 ?  867 HOH A O   1 
HETATM 6798 O  O   . HOH L 7 .   ? 18.623  -3.566  -1.260  1.00 10.96 ?  868 HOH A O   1 
HETATM 6799 O  O   . HOH L 7 .   ? 4.697   10.495  -5.821  1.00 32.02 ?  869 HOH A O   1 
HETATM 6800 O  O   . HOH L 7 .   ? 22.109  16.962  -16.863 1.00 18.02 ?  870 HOH A O   1 
HETATM 6801 O  O   . HOH L 7 .   ? 29.019  19.160  7.318   1.00 22.69 ?  871 HOH A O   1 
HETATM 6802 O  O   . HOH L 7 .   ? 31.213  12.942  -25.555 1.00 24.33 ?  872 HOH A O   1 
HETATM 6803 O  O   . HOH L 7 .   ? 19.270  -6.291  -12.015 1.00 31.67 ?  873 HOH A O   1 
HETATM 6804 O  O   . HOH L 7 .   ? -4.043  15.317  29.349  1.00 36.97 ?  874 HOH A O   1 
HETATM 6805 O  O   . HOH L 7 .   ? 31.131  -10.272 14.582  1.00 35.31 ?  875 HOH A O   1 
HETATM 6806 O  O   . HOH L 7 .   ? 1.515   18.455  12.217  1.00 34.11 ?  876 HOH A O   1 
HETATM 6807 O  O   . HOH L 7 .   ? -1.997  9.854   6.208   1.00 33.49 ?  877 HOH A O   1 
HETATM 6808 O  O   . HOH L 7 .   ? 6.201   -3.509  25.986  1.00 23.07 ?  878 HOH A O   1 
HETATM 6809 O  O   . HOH L 7 .   ? 4.318   22.115  14.491  1.00 29.14 ?  879 HOH A O   1 
HETATM 6810 O  O   . HOH L 7 .   ? -1.842  -8.269  13.040  1.00 32.35 ?  880 HOH A O   1 
HETATM 6811 O  O   . HOH L 7 .   ? 17.940  -3.325  6.187   1.00 11.70 ?  881 HOH A O   1 
HETATM 6812 O  O   . HOH L 7 .   ? 30.171  -12.124 2.070   1.00 41.98 ?  882 HOH A O   1 
HETATM 6813 O  O   . HOH L 7 .   ? 29.818  23.680  -18.214 1.00 31.56 ?  883 HOH A O   1 
HETATM 6814 O  O   . HOH L 7 .   ? 12.037  5.370   -14.758 1.00 34.30 ?  884 HOH A O   1 
HETATM 6815 O  O   . HOH L 7 .   ? 16.257  -11.329 1.923   1.00 34.56 ?  885 HOH A O   1 
HETATM 6816 O  O   . HOH L 7 .   ? 24.999  25.504  2.853   1.00 31.45 ?  886 HOH A O   1 
HETATM 6817 O  O   . HOH L 7 .   ? 25.022  -2.912  31.819  1.00 28.55 ?  887 HOH A O   1 
HETATM 6818 O  O   . HOH L 7 .   ? 35.139  -5.530  7.615   1.00 17.10 ?  888 HOH A O   1 
HETATM 6819 O  O   . HOH L 7 .   ? 18.505  6.647   27.361  1.00 31.56 ?  889 HOH A O   1 
HETATM 6820 O  O   . HOH L 7 .   ? 37.181  4.062   18.811  1.00 32.65 ?  890 HOH A O   1 
HETATM 6821 O  O   . HOH L 7 .   ? 9.575   15.903  -17.721 1.00 31.38 ?  891 HOH A O   1 
HETATM 6822 O  O   . HOH L 7 .   ? 2.574   -4.620  1.523   1.00 18.28 ?  892 HOH A O   1 
HETATM 6823 O  O   . HOH L 7 .   ? 38.633  -1.622  -7.854  1.00 38.93 ?  893 HOH A O   1 
HETATM 6824 O  O   . HOH L 7 .   ? 3.129   13.554  6.721   1.00 14.21 ?  894 HOH A O   1 
HETATM 6825 O  O   . HOH L 7 .   ? 43.429  -1.749  -0.540  1.00 32.39 ?  895 HOH A O   1 
HETATM 6826 O  O   . HOH L 7 .   ? 41.169  9.311   -7.525  1.00 33.29 ?  896 HOH A O   1 
HETATM 6827 O  O   . HOH L 7 .   ? 17.443  -7.358  5.880   1.00 20.46 ?  897 HOH A O   1 
HETATM 6828 O  O   . HOH L 7 .   ? 29.112  4.046   26.330  1.00 34.60 ?  898 HOH A O   1 
HETATM 6829 O  O   . HOH L 7 .   ? 14.313  -0.909  30.746  1.00 37.70 ?  899 HOH A O   1 
HETATM 6830 O  O   . HOH L 7 .   ? 14.254  24.004  13.172  1.00 41.60 ?  900 HOH A O   1 
HETATM 6831 O  O   . HOH L 7 .   ? 38.938  -5.651  -4.152  1.00 30.31 ?  901 HOH A O   1 
HETATM 6832 O  O   . HOH L 7 .   ? 35.052  -5.457  -5.136  1.00 28.38 ?  902 HOH A O   1 
HETATM 6833 O  O   . HOH L 7 .   ? -1.655  -10.858 19.761  1.00 32.76 ?  903 HOH A O   1 
HETATM 6834 O  O   . HOH L 7 .   ? 3.955   6.712   1.735   1.00 29.28 ?  904 HOH A O   1 
HETATM 6835 O  O   . HOH L 7 .   ? 36.188  22.073  -12.994 1.00 19.36 ?  905 HOH A O   1 
HETATM 6836 O  O   . HOH L 7 .   ? 32.035  22.944  5.756   1.00 41.85 ?  906 HOH A O   1 
HETATM 6837 O  O   . HOH L 7 .   ? 2.251   17.432  1.250   1.00 27.75 ?  907 HOH A O   1 
HETATM 6838 O  O   . HOH L 7 .   ? 9.311   27.707  5.897   1.00 37.00 ?  908 HOH A O   1 
HETATM 6839 O  O   . HOH L 7 .   ? 43.130  11.340  5.800   1.00 35.73 ?  909 HOH A O   1 
HETATM 6840 O  O   . HOH L 7 .   ? 24.538  21.894  19.870  1.00 45.17 ?  910 HOH A O   1 
HETATM 6841 O  O   . HOH L 7 .   ? 8.859   2.923   -2.653  1.00 21.98 ?  911 HOH A O   1 
HETATM 6842 O  O   . HOH L 7 .   ? 0.799   12.808  2.393   1.00 28.58 ?  912 HOH A O   1 
HETATM 6843 O  O   . HOH L 7 .   ? 6.940   -5.819  26.227  1.00 33.13 ?  913 HOH A O   1 
HETATM 6844 O  O   . HOH L 7 .   ? 13.375  15.724  18.415  1.00 34.90 ?  914 HOH A O   1 
HETATM 6845 O  O   . HOH L 7 .   ? 10.248  -2.889  -10.174 1.00 35.63 ?  915 HOH A O   1 
HETATM 6846 O  O   . HOH L 7 .   ? 6.438   8.343   -6.013  1.00 37.29 ?  916 HOH A O   1 
HETATM 6847 O  O   . HOH L 7 .   ? 6.995   5.883   34.908  1.00 44.65 ?  917 HOH A O   1 
HETATM 6848 O  O   . HOH L 7 .   ? 24.443  -15.473 12.359  1.00 35.52 ?  918 HOH A O   1 
HETATM 6849 O  O   . HOH L 7 .   ? 37.574  14.076  16.546  1.00 30.28 ?  919 HOH A O   1 
HETATM 6850 O  O   . HOH L 7 .   ? 16.964  -10.944 -0.293  1.00 29.95 ?  920 HOH A O   1 
HETATM 6851 O  O   . HOH L 7 .   ? 14.741  6.983   29.423  1.00 33.29 ?  921 HOH A O   1 
HETATM 6852 O  O   . HOH L 7 .   ? 19.633  -9.589  5.795   1.00 23.78 ?  922 HOH A O   1 
HETATM 6853 O  O   . HOH L 7 .   ? 26.661  -8.400  3.059   1.00 15.86 ?  923 HOH A O   1 
HETATM 6854 O  O   . HOH L 7 .   ? 15.685  7.639   4.520   1.00 11.97 ?  924 HOH A O   1 
HETATM 6855 O  O   . HOH L 7 .   ? 31.929  -11.139 19.338  1.00 37.78 ?  925 HOH A O   1 
HETATM 6856 O  O   . HOH L 7 .   ? 29.351  19.217  12.787  1.00 37.27 ?  926 HOH A O   1 
HETATM 6857 O  O   . HOH L 7 .   ? 14.525  -15.355 20.181  1.00 37.51 ?  927 HOH A O   1 
HETATM 6858 O  O   . HOH L 7 .   ? 39.111  1.113   23.221  1.00 38.86 ?  928 HOH A O   1 
HETATM 6859 O  O   . HOH L 7 .   ? 45.317  0.452   -7.797  1.00 42.52 ?  929 HOH A O   1 
HETATM 6860 O  O   . HOH L 7 .   ? 18.290  -4.379  3.666   1.00 14.56 ?  930 HOH A O   1 
HETATM 6861 O  O   . HOH L 7 .   ? -9.513  2.737   0.836   1.00 18.96 ?  931 HOH A O   1 
HETATM 6862 O  O   . HOH L 7 .   ? 11.820  7.967   -10.635 1.00 27.19 ?  932 HOH A O   1 
HETATM 6863 O  O   . HOH L 7 .   ? 20.491  23.898  -17.134 1.00 24.26 ?  933 HOH A O   1 
HETATM 6864 O  O   . HOH L 7 .   ? 3.104   -9.951  4.661   1.00 35.69 ?  934 HOH A O   1 
HETATM 6865 O  O   . HOH L 7 .   ? 6.179   12.212  -7.828  1.00 34.30 ?  935 HOH A O   1 
HETATM 6866 O  O   . HOH L 7 .   ? 23.224  -10.952 5.368   1.00 23.87 ?  936 HOH A O   1 
HETATM 6867 O  O   . HOH L 7 .   ? 11.958  -7.246  -4.267  1.00 23.98 ?  937 HOH A O   1 
HETATM 6868 O  O   . HOH L 7 .   ? 20.889  -11.499 -3.339  1.00 34.02 ?  938 HOH A O   1 
HETATM 6869 O  O   . HOH L 7 .   ? 7.717   -6.562  -0.003  1.00 26.64 ?  939 HOH A O   1 
HETATM 6870 O  O   . HOH L 7 .   ? 13.235  14.673  24.399  1.00 34.77 ?  940 HOH A O   1 
HETATM 6871 O  O   . HOH L 7 .   ? 1.199   8.136   -0.945  1.00 37.99 ?  941 HOH A O   1 
HETATM 6872 O  O   . HOH L 7 .   ? 18.543  10.062  25.234  1.00 34.16 ?  942 HOH A O   1 
HETATM 6873 O  O   . HOH L 7 .   ? 39.436  -1.982  16.022  1.00 25.54 ?  943 HOH A O   1 
HETATM 6874 O  O   . HOH L 7 .   ? 18.501  -5.646  7.253   1.00 24.86 ?  944 HOH A O   1 
HETATM 6875 O  O   . HOH L 7 .   ? 4.866   2.187   -2.200  1.00 35.55 ?  945 HOH A O   1 
HETATM 6876 O  O   . HOH L 7 .   ? 24.149  24.978  7.929   1.00 35.60 ?  946 HOH A O   1 
HETATM 6877 O  O   . HOH L 7 .   ? 28.158  28.886  -12.937 1.00 36.12 ?  947 HOH A O   1 
HETATM 6878 O  O   . HOH L 7 .   ? 27.052  -12.135 4.962   1.00 35.63 ?  948 HOH A O   1 
HETATM 6879 O  O   . HOH L 7 .   ? 24.977  26.266  -17.809 1.00 35.77 ?  949 HOH A O   1 
HETATM 6880 O  O   . HOH L 7 .   ? 13.792  -13.957 18.136  1.00 33.21 ?  950 HOH A O   1 
HETATM 6881 O  O   . HOH L 7 .   ? 6.030   5.901   -4.096  1.00 30.82 ?  951 HOH A O   1 
HETATM 6882 O  O   . HOH L 7 .   ? 5.824   26.552  15.347  1.00 39.59 ?  952 HOH A O   1 
HETATM 6883 O  O   . HOH L 7 .   ? 21.899  -7.831  -11.234 1.00 33.38 ?  953 HOH A O   1 
HETATM 6884 O  O   . HOH L 7 .   ? 21.166  -11.782 1.109   1.00 24.31 ?  954 HOH A O   1 
HETATM 6885 O  O   . HOH L 7 .   ? 3.139   -18.740 15.772  1.00 39.63 ?  955 HOH A O   1 
HETATM 6886 O  O   . HOH L 7 .   ? -0.528  17.724  1.413   1.00 23.49 ?  956 HOH A O   1 
HETATM 6887 O  O   . HOH L 7 .   ? 4.373   15.627  31.270  1.00 41.21 ?  957 HOH A O   1 
HETATM 6888 O  O   . HOH L 7 .   ? 27.659  -12.905 14.307  1.00 40.46 ?  958 HOH A O   1 
HETATM 6889 O  O   . HOH L 7 .   ? 15.573  8.796   25.413  1.00 29.85 ?  959 HOH A O   1 
HETATM 6890 O  O   . HOH L 7 .   ? 35.218  -0.866  -10.598 1.00 27.36 ?  960 HOH A O   1 
HETATM 6891 O  O   . HOH L 7 .   ? 25.854  -10.963 2.501   1.00 33.83 ?  961 HOH A O   1 
HETATM 6892 O  O   . HOH L 7 .   ? 24.398  -12.411 1.078   1.00 36.20 ?  962 HOH A O   1 
HETATM 6893 O  O   . HOH L 7 .   ? 20.531  27.137  8.584   1.00 34.92 ?  963 HOH A O   1 
HETATM 6894 O  O   . HOH L 7 .   ? 22.835  27.317  8.690   1.00 31.23 ?  964 HOH A O   1 
HETATM 6895 O  O   . HOH M 7 .   ? 48.922  4.816   -30.016 1.00 28.33 ?  601 HOH B O   1 
HETATM 6896 O  O   . HOH M 7 .   ? 31.450  6.198   -27.699 1.00 30.48 ?  602 HOH B O   1 
HETATM 6897 O  O   . HOH M 7 .   ? 25.110  18.967  -16.525 1.00 19.82 ?  603 HOH B O   1 
HETATM 6898 O  O   . HOH M 7 .   ? 58.596  7.307   -34.208 1.00 24.25 ?  604 HOH B O   1 
HETATM 6899 O  O   . HOH M 7 .   ? 32.127  23.746  -32.099 1.00 27.96 ?  605 HOH B O   1 
HETATM 6900 O  O   . HOH M 7 .   ? 19.028  11.678  -24.882 1.00 27.30 ?  606 HOH B O   1 
HETATM 6901 O  O   . HOH M 7 .   ? 25.292  21.216  -59.133 1.00 34.67 ?  607 HOH B O   1 
HETATM 6902 O  O   . HOH M 7 .   ? 21.187  15.510  -43.585 1.00 21.27 ?  608 HOH B O   1 
HETATM 6903 O  O   . HOH M 7 .   ? 6.477   23.185  -44.199 1.00 36.37 ?  609 HOH B O   1 
HETATM 6904 O  O   . HOH M 7 .   ? 34.781  -2.152  -39.078 1.00 24.49 ?  610 HOH B O   1 
HETATM 6905 O  O   . HOH M 7 .   ? 33.848  1.339   -42.203 1.00 21.67 ?  611 HOH B O   1 
HETATM 6906 O  O   . HOH M 7 .   ? 27.761  18.412  -56.932 1.00 28.40 ?  612 HOH B O   1 
HETATM 6907 O  O   . HOH M 7 .   ? 28.670  -7.081  -41.388 1.00 21.01 ?  613 HOH B O   1 
HETATM 6908 O  O   . HOH M 7 .   ? 53.443  12.767  -51.588 1.00 18.63 ?  614 HOH B O   1 
HETATM 6909 O  O   . HOH M 7 .   ? 16.919  10.282  -28.935 1.00 28.29 ?  615 HOH B O   1 
HETATM 6910 O  O   . HOH M 7 .   ? 37.994  -12.811 -57.465 1.00 29.96 ?  616 HOH B O   1 
HETATM 6911 O  O   . HOH M 7 .   ? 12.069  22.098  -25.360 1.00 32.69 ?  617 HOH B O   1 
HETATM 6912 O  O   . HOH M 7 .   ? 7.138   -11.922 -66.489 1.00 34.92 ?  618 HOH B O   1 
HETATM 6913 O  O   . HOH M 7 .   ? 29.699  2.448   -61.283 1.00 29.40 ?  619 HOH B O   1 
HETATM 6914 O  O   . HOH M 7 .   ? 11.520  -7.020  -66.753 1.00 28.05 ?  620 HOH B O   1 
HETATM 6915 O  O   . HOH M 7 .   ? 37.954  5.000   -42.497 1.00 16.60 ?  621 HOH B O   1 
HETATM 6916 O  O   . HOH M 7 .   ? 26.910  17.506  -61.272 1.00 33.04 ?  622 HOH B O   1 
HETATM 6917 O  O   . HOH M 7 .   ? 13.829  20.276  -56.335 1.00 27.55 ?  623 HOH B O   1 
HETATM 6918 O  O   . HOH M 7 .   ? 31.783  -1.432  -36.646 1.00 25.40 ?  624 HOH B O   1 
HETATM 6919 O  O   . HOH M 7 .   ? 45.615  3.004   -25.792 1.00 29.44 ?  625 HOH B O   1 
HETATM 6920 O  O   . HOH M 7 .   ? 32.701  -1.264  -50.400 1.00 17.42 ?  626 HOH B O   1 
HETATM 6921 O  O   . HOH M 7 .   ? 26.116  5.766   -34.068 1.00 15.11 ?  627 HOH B O   1 
HETATM 6922 O  O   . HOH M 7 .   ? 9.159   18.244  -54.518 1.00 34.22 ?  628 HOH B O   1 
HETATM 6923 O  O   . HOH M 7 .   ? 25.242  -0.693  -69.635 1.00 29.57 ?  629 HOH B O   1 
HETATM 6924 O  O   . HOH M 7 .   ? 19.338  6.594   -36.618 1.00 18.97 ?  630 HOH B O   1 
HETATM 6925 O  O   . HOH M 7 .   ? 18.149  19.063  -26.693 1.00 30.04 ?  631 HOH B O   1 
HETATM 6926 O  O   . HOH M 7 .   ? 6.389   -3.917  -48.205 1.00 35.13 ?  632 HOH B O   1 
HETATM 6927 O  O   . HOH M 7 .   ? 30.733  -4.204  -63.355 1.00 18.01 ?  633 HOH B O   1 
HETATM 6928 O  O   . HOH M 7 .   ? 20.560  0.423   -72.460 1.00 35.33 ?  634 HOH B O   1 
HETATM 6929 O  O   . HOH M 7 .   ? 12.448  -4.325  -37.414 1.00 33.36 ?  635 HOH B O   1 
HETATM 6930 O  O   . HOH M 7 .   ? 16.261  20.118  -60.537 1.00 31.09 ?  636 HOH B O   1 
HETATM 6931 O  O   . HOH M 7 .   ? 56.309  11.093  -27.519 1.00 23.29 ?  637 HOH B O   1 
HETATM 6932 O  O   . HOH M 7 .   ? 13.896  -8.218  -67.420 1.00 20.97 ?  638 HOH B O   1 
HETATM 6933 O  O   . HOH M 7 .   ? 37.400  11.296  -61.562 1.00 28.64 ?  639 HOH B O   1 
HETATM 6934 O  O   . HOH M 7 .   ? 29.591  4.961   -59.770 1.00 22.67 ?  640 HOH B O   1 
HETATM 6935 O  O   . HOH M 7 .   ? 36.563  -6.191  -57.197 1.00 20.37 ?  641 HOH B O   1 
HETATM 6936 O  O   . HOH M 7 .   ? 13.245  20.445  -46.924 1.00 32.68 ?  642 HOH B O   1 
HETATM 6937 O  O   . HOH M 7 .   ? 32.955  3.165   -35.539 1.00 27.71 ?  643 HOH B O   1 
HETATM 6938 O  O   . HOH M 7 .   ? 32.799  0.388   -52.754 1.00 15.57 ?  644 HOH B O   1 
HETATM 6939 O  O   . HOH M 7 .   ? 4.934   -3.845  -45.728 1.00 35.63 ?  645 HOH B O   1 
HETATM 6940 O  O   . HOH M 7 .   ? 14.775  9.010   -30.298 1.00 31.68 ?  646 HOH B O   1 
HETATM 6941 O  O   . HOH M 7 .   ? 28.613  10.616  -29.517 1.00 15.72 ?  647 HOH B O   1 
HETATM 6942 O  O   . HOH M 7 .   ? 31.469  -10.449 -57.722 1.00 16.23 ?  648 HOH B O   1 
HETATM 6943 O  O   . HOH M 7 .   ? 26.892  4.140   -46.908 1.00 13.89 ?  649 HOH B O   1 
HETATM 6944 O  O   . HOH M 7 .   ? 42.304  5.239   -54.133 1.00 21.99 ?  650 HOH B O   1 
HETATM 6945 O  O   . HOH M 7 .   ? 31.880  -3.438  -52.096 1.00 15.98 ?  651 HOH B O   1 
HETATM 6946 O  O   . HOH M 7 .   ? 20.548  22.188  -53.949 1.00 26.97 ?  652 HOH B O   1 
HETATM 6947 O  O   . HOH M 7 .   ? 37.956  -3.476  -32.728 1.00 30.60 ?  653 HOH B O   1 
HETATM 6948 O  O   . HOH M 7 .   ? 20.907  -4.922  -29.320 1.00 28.48 ?  654 HOH B O   1 
HETATM 6949 O  O   . HOH M 7 .   ? 25.197  22.659  -23.487 1.00 23.59 ?  655 HOH B O   1 
HETATM 6950 O  O   . HOH M 7 .   ? 9.163   16.122  -49.880 1.00 21.35 ?  656 HOH B O   1 
HETATM 6951 O  O   . HOH M 7 .   ? 18.194  14.262  -34.176 1.00 22.14 ?  657 HOH B O   1 
HETATM 6952 O  O   . HOH M 7 .   ? 22.374  -10.816 -44.676 1.00 27.80 ?  658 HOH B O   1 
HETATM 6953 O  O   . HOH M 7 .   ? 9.275   -5.956  -50.989 1.00 23.20 ?  659 HOH B O   1 
HETATM 6954 O  O   . HOH M 7 .   ? 26.611  22.123  -48.606 1.00 21.22 ?  660 HOH B O   1 
HETATM 6955 O  O   . HOH M 7 .   ? 22.517  21.666  -18.338 1.00 23.66 ?  661 HOH B O   1 
HETATM 6956 O  O   . HOH M 7 .   ? 48.577  21.349  -37.325 1.00 19.85 ?  662 HOH B O   1 
HETATM 6957 O  O   . HOH M 7 .   ? 29.102  5.168   -35.506 1.00 16.99 ?  663 HOH B O   1 
HETATM 6958 O  O   . HOH M 7 .   ? 28.087  -13.279 -45.566 1.00 28.78 ?  664 HOH B O   1 
HETATM 6959 O  O   . HOH M 7 .   ? 39.517  20.129  -52.658 1.00 21.93 ?  665 HOH B O   1 
HETATM 6960 O  O   . HOH M 7 .   ? 31.721  5.105   -41.564 1.00 11.94 ?  666 HOH B O   1 
HETATM 6961 O  O   . HOH M 7 .   ? 17.277  21.768  -57.116 1.00 28.31 ?  667 HOH B O   1 
HETATM 6962 O  O   . HOH M 7 .   ? 42.157  -6.495  -51.987 1.00 27.76 ?  668 HOH B O   1 
HETATM 6963 O  O   . HOH M 7 .   ? 40.697  2.771   -57.097 1.00 27.95 ?  669 HOH B O   1 
HETATM 6964 O  O   . HOH M 7 .   ? 28.684  19.847  -54.972 1.00 24.70 ?  670 HOH B O   1 
HETATM 6965 O  O   . HOH M 7 .   ? 28.871  13.892  -50.306 1.00 12.57 ?  671 HOH B O   1 
HETATM 6966 O  O   . HOH M 7 .   ? 25.756  25.338  -46.721 1.00 29.28 ?  672 HOH B O   1 
HETATM 6967 O  O   . HOH M 7 .   ? 15.663  -3.702  -46.627 1.00 15.84 ?  673 HOH B O   1 
HETATM 6968 O  O   . HOH M 7 .   ? 33.914  6.326   -28.987 1.00 20.94 ?  674 HOH B O   1 
HETATM 6969 O  O   . HOH M 7 .   ? 18.059  -13.006 -58.608 1.00 26.46 ?  675 HOH B O   1 
HETATM 6970 O  O   . HOH M 7 .   ? 47.698  -0.702  -43.691 1.00 11.76 ?  676 HOH B O   1 
HETATM 6971 O  O   . HOH M 7 .   ? 16.464  -13.938 -65.786 1.00 28.35 ?  677 HOH B O   1 
HETATM 6972 O  O   . HOH M 7 .   ? 38.301  -3.003  -55.016 1.00 29.96 ?  678 HOH B O   1 
HETATM 6973 O  O   . HOH M 7 .   ? 3.515   -10.425 -66.509 1.00 30.94 ?  679 HOH B O   1 
HETATM 6974 O  O   . HOH M 7 .   ? 32.650  -5.321  -54.199 1.00 17.90 ?  680 HOH B O   1 
HETATM 6975 O  O   . HOH M 7 .   ? 15.465  16.973  -47.254 1.00 18.48 ?  681 HOH B O   1 
HETATM 6976 O  O   . HOH M 7 .   ? 46.121  15.765  -33.306 1.00 18.25 ?  682 HOH B O   1 
HETATM 6977 O  O   . HOH M 7 .   ? 36.012  4.552   -54.003 1.00 20.00 ?  683 HOH B O   1 
HETATM 6978 O  O   . HOH M 7 .   ? 40.832  0.599   -49.346 1.00 12.85 ?  684 HOH B O   1 
HETATM 6979 O  O   . HOH M 7 .   ? 22.811  -11.364 -59.721 1.00 25.85 ?  685 HOH B O   1 
HETATM 6980 O  O   . HOH M 7 .   ? 33.734  25.467  -32.863 1.00 32.79 ?  686 HOH B O   1 
HETATM 6981 O  O   . HOH M 7 .   ? 19.928  6.751   -70.241 1.00 25.60 ?  687 HOH B O   1 
HETATM 6982 O  O   . HOH M 7 .   ? 47.133  -4.525  -49.286 1.00 31.90 ?  688 HOH B O   1 
HETATM 6983 O  O   . HOH M 7 .   ? 21.185  13.343  -32.775 1.00 16.67 ?  689 HOH B O   1 
HETATM 6984 O  O   . HOH M 7 .   ? 10.327  -8.606  -64.931 1.00 22.55 ?  690 HOH B O   1 
HETATM 6985 O  O   . HOH M 7 .   ? 41.194  22.011  -33.585 1.00 32.16 ?  691 HOH B O   1 
HETATM 6986 O  O   . HOH M 7 .   ? 30.222  24.435  -25.610 1.00 23.48 ?  692 HOH B O   1 
HETATM 6987 O  O   . HOH M 7 .   ? 29.460  -1.842  -52.336 1.00 13.65 ?  693 HOH B O   1 
HETATM 6988 O  O   . HOH M 7 .   ? 28.695  10.742  -59.164 1.00 28.45 ?  694 HOH B O   1 
HETATM 6989 O  O   . HOH M 7 .   ? 35.165  -6.490  -54.616 1.00 18.39 ?  695 HOH B O   1 
HETATM 6990 O  O   . HOH M 7 .   ? 24.515  3.927   -50.463 1.00 14.71 ?  696 HOH B O   1 
HETATM 6991 O  O   . HOH M 7 .   ? 15.922  18.413  -49.942 1.00 21.16 ?  697 HOH B O   1 
HETATM 6992 O  O   . HOH M 7 .   ? 19.818  4.990   -56.463 1.00 16.03 ?  698 HOH B O   1 
HETATM 6993 O  O   . HOH M 7 .   ? 29.103  23.576  -47.542 1.00 19.69 ?  699 HOH B O   1 
HETATM 6994 O  O   . HOH M 7 .   ? 9.767   0.510   -32.687 1.00 25.95 ?  700 HOH B O   1 
HETATM 6995 O  O   . HOH M 7 .   ? 45.285  20.356  -45.211 1.00 22.56 ?  701 HOH B O   1 
HETATM 6996 O  O   . HOH M 7 .   ? 27.673  16.108  -49.036 1.00 13.55 ?  702 HOH B O   1 
HETATM 6997 O  O   . HOH M 7 .   ? 49.217  12.478  -32.803 1.00 16.11 ?  703 HOH B O   1 
HETATM 6998 O  O   . HOH M 7 .   ? 22.617  16.430  -20.910 1.00 19.79 ?  704 HOH B O   1 
HETATM 6999 O  O   . HOH M 7 .   ? 55.538  10.467  -42.611 1.00 21.31 ?  705 HOH B O   1 
HETATM 7000 O  O   . HOH M 7 .   ? 17.138  19.796  -45.646 1.00 27.69 ?  706 HOH B O   1 
HETATM 7001 O  O   . HOH M 7 .   ? 33.441  -5.682  -68.969 1.00 24.01 ?  707 HOH B O   1 
HETATM 7002 O  O   . HOH M 7 .   ? 24.673  -7.604  -37.520 1.00 31.96 ?  708 HOH B O   1 
HETATM 7003 O  O   . HOH M 7 .   ? 46.289  10.932  -27.372 1.00 25.71 ?  709 HOH B O   1 
HETATM 7004 O  O   . HOH M 7 .   ? 25.852  22.161  -18.997 1.00 29.95 ?  710 HOH B O   1 
HETATM 7005 O  O   . HOH M 7 .   ? 35.368  19.998  -27.419 1.00 28.62 ?  711 HOH B O   1 
HETATM 7006 O  O   . HOH M 7 .   ? 21.725  16.104  -51.919 1.00 17.28 ?  712 HOH B O   1 
HETATM 7007 O  O   . HOH M 7 .   ? 18.454  22.920  -20.406 1.00 36.17 ?  713 HOH B O   1 
HETATM 7008 O  O   . HOH M 7 .   ? 34.306  0.549   -39.598 1.00 16.77 ?  714 HOH B O   1 
HETATM 7009 O  O   . HOH M 7 .   ? 11.682  24.111  -48.251 1.00 43.17 ?  715 HOH B O   1 
HETATM 7010 O  O   . HOH M 7 .   ? 34.939  16.690  -52.851 1.00 13.33 ?  716 HOH B O   1 
HETATM 7011 O  O   . HOH M 7 .   ? 29.679  1.646   -31.648 1.00 22.87 ?  717 HOH B O   1 
HETATM 7012 O  O   . HOH M 7 .   ? 25.892  17.035  -65.259 1.00 36.22 ?  718 HOH B O   1 
HETATM 7013 O  O   . HOH M 7 .   ? 27.257  4.368   -30.911 1.00 17.19 ?  719 HOH B O   1 
HETATM 7014 O  O   . HOH M 7 .   ? 47.614  -2.886  -30.173 1.00 27.55 ?  720 HOH B O   1 
HETATM 7015 O  O   . HOH M 7 .   ? 21.785  23.035  -30.331 1.00 33.47 ?  721 HOH B O   1 
HETATM 7016 O  O   . HOH M 7 .   ? 17.856  16.787  -35.085 1.00 22.96 ?  722 HOH B O   1 
HETATM 7017 O  O   . HOH M 7 .   ? 41.323  16.642  -55.970 1.00 21.96 ?  723 HOH B O   1 
HETATM 7018 O  O   . HOH M 7 .   ? 28.311  7.034   -50.446 1.00 12.92 ?  724 HOH B O   1 
HETATM 7019 O  O   . HOH M 7 .   ? 25.235  18.983  -43.909 1.00 15.50 ?  725 HOH B O   1 
HETATM 7020 O  O   . HOH M 7 .   ? 37.690  23.010  -32.669 1.00 19.36 ?  726 HOH B O   1 
HETATM 7021 O  O   . HOH M 7 .   ? 39.245  9.760   -55.436 1.00 13.16 ?  727 HOH B O   1 
HETATM 7022 O  O   . HOH M 7 .   ? 19.996  -9.440  -70.000 1.00 20.52 ?  728 HOH B O   1 
HETATM 7023 O  O   . HOH M 7 .   ? 18.469  16.407  -29.399 1.00 18.01 ?  729 HOH B O   1 
HETATM 7024 O  O   . HOH M 7 .   ? 23.965  6.351   -69.316 1.00 40.04 ?  730 HOH B O   1 
HETATM 7025 O  O   . HOH M 7 .   ? 12.579  -1.154  -34.114 1.00 27.43 ?  731 HOH B O   1 
HETATM 7026 O  O   . HOH M 7 .   ? 58.271  10.983  -37.026 1.00 23.65 ?  732 HOH B O   1 
HETATM 7027 O  O   . HOH M 7 .   ? 21.920  10.777  -71.934 1.00 33.98 ?  733 HOH B O   1 
HETATM 7028 O  O   . HOH M 7 .   ? 21.044  19.179  -44.738 1.00 24.08 ?  734 HOH B O   1 
HETATM 7029 O  O   . HOH M 7 .   ? 17.121  -7.633  -40.629 1.00 31.63 ?  735 HOH B O   1 
HETATM 7030 O  O   . HOH M 7 .   ? 38.231  11.202  -49.670 1.00 10.93 ?  736 HOH B O   1 
HETATM 7031 O  O   . HOH M 7 .   ? 31.950  2.932   -42.939 1.00 15.66 ?  737 HOH B O   1 
HETATM 7032 O  O   . HOH M 7 .   ? 44.379  2.852   -53.838 1.00 33.05 ?  738 HOH B O   1 
HETATM 7033 O  O   . HOH M 7 .   ? 49.467  7.696   -59.551 1.00 24.70 ?  739 HOH B O   1 
HETATM 7034 O  O   . HOH M 7 .   ? 56.623  3.164   -29.517 1.00 22.25 ?  740 HOH B O   1 
HETATM 7035 O  O   . HOH M 7 .   ? 34.370  2.399   -54.375 1.00 20.44 ?  741 HOH B O   1 
HETATM 7036 O  O   . HOH M 7 .   ? 19.785  21.661  -44.588 1.00 29.53 ?  742 HOH B O   1 
HETATM 7037 O  O   . HOH M 7 .   ? 26.477  18.011  -50.534 1.00 20.12 ?  743 HOH B O   1 
HETATM 7038 O  O   . HOH M 7 .   ? 36.709  2.538   -42.698 1.00 12.70 ?  744 HOH B O   1 
HETATM 7039 O  O   . HOH M 7 .   ? 21.365  3.011   -51.102 1.00 14.66 ?  745 HOH B O   1 
HETATM 7040 O  O   . HOH M 7 .   ? -1.141  12.068  -43.014 1.00 28.00 ?  746 HOH B O   1 
HETATM 7041 O  O   . HOH M 7 .   ? 24.986  -10.342 -58.598 1.00 23.25 ?  747 HOH B O   1 
HETATM 7042 O  O   . HOH M 7 .   ? 22.418  19.187  -47.119 1.00 20.67 ?  748 HOH B O   1 
HETATM 7043 O  O   . HOH M 7 .   ? 26.214  -2.823  -68.447 1.00 20.07 ?  749 HOH B O   1 
HETATM 7044 O  O   . HOH M 7 .   ? 15.811  -4.525  -43.865 1.00 18.22 ?  750 HOH B O   1 
HETATM 7045 O  O   . HOH M 7 .   ? 29.216  16.443  -58.479 1.00 31.36 ?  751 HOH B O   1 
HETATM 7046 O  O   . HOH M 7 .   ? 8.269   14.175  -34.198 1.00 36.91 ?  752 HOH B O   1 
HETATM 7047 O  O   . HOH M 7 .   ? 22.733  22.655  -61.919 1.00 30.14 ?  753 HOH B O   1 
HETATM 7048 O  O   . HOH M 7 .   ? 19.864  20.797  -31.230 1.00 27.65 ?  754 HOH B O   1 
HETATM 7049 O  O   . HOH M 7 .   ? 24.936  8.756   -58.997 1.00 21.67 ?  755 HOH B O   1 
HETATM 7050 O  O   . HOH M 7 .   ? 33.929  14.090  -27.868 1.00 21.35 ?  756 HOH B O   1 
HETATM 7051 O  O   . HOH M 7 .   ? 22.860  8.577   -56.947 1.00 17.29 ?  757 HOH B O   1 
HETATM 7052 O  O   . HOH M 7 .   ? 31.610  25.534  -46.118 1.00 23.56 ?  758 HOH B O   1 
HETATM 7053 O  O   . HOH M 7 .   ? 27.533  24.437  -25.614 1.00 25.20 ?  759 HOH B O   1 
HETATM 7054 O  O   . HOH M 7 .   ? 28.075  6.563   -47.447 1.00 12.03 ?  760 HOH B O   1 
HETATM 7055 O  O   . HOH M 7 .   ? 24.456  -6.710  -73.590 1.00 29.55 ?  761 HOH B O   1 
HETATM 7056 O  O   . HOH M 7 .   ? 27.901  5.563   -26.778 1.00 34.73 ?  762 HOH B O   1 
HETATM 7057 O  O   . HOH M 7 .   ? 32.337  8.344   -52.823 1.00 12.71 ?  763 HOH B O   1 
HETATM 7058 O  O   . HOH M 7 .   ? 26.774  10.364  -57.588 1.00 20.31 ?  764 HOH B O   1 
HETATM 7059 O  O   . HOH M 7 .   ? 50.990  20.898  -38.590 1.00 21.61 ?  765 HOH B O   1 
HETATM 7060 O  O   . HOH M 7 .   ? 50.379  21.733  -41.080 1.00 19.78 ?  766 HOH B O   1 
HETATM 7061 O  O   . HOH M 7 .   ? 11.267  18.668  -56.519 1.00 35.09 ?  767 HOH B O   1 
HETATM 7062 O  O   . HOH M 7 .   ? 25.174  28.734  -40.825 1.00 35.80 ?  768 HOH B O   1 
HETATM 7063 O  O   . HOH M 7 .   ? 40.456  9.314   -60.609 1.00 38.92 ?  769 HOH B O   1 
HETATM 7064 O  O   . HOH M 7 .   ? 30.188  -1.418  -63.338 1.00 19.76 ?  770 HOH B O   1 
HETATM 7065 O  O   . HOH M 7 .   ? 6.695   21.604  -42.370 1.00 36.35 ?  771 HOH B O   1 
HETATM 7066 O  O   . HOH M 7 .   ? 17.275  22.739  -37.741 1.00 22.00 ?  772 HOH B O   1 
HETATM 7067 O  O   . HOH M 7 .   ? 18.887  -10.502 -57.868 1.00 22.13 ?  773 HOH B O   1 
HETATM 7068 O  O   . HOH M 7 .   ? 55.406  19.596  -37.511 1.00 28.70 ?  774 HOH B O   1 
HETATM 7069 O  O   . HOH M 7 .   ? 22.473  22.529  -22.712 1.00 29.26 ?  775 HOH B O   1 
HETATM 7070 O  O   . HOH M 7 .   ? 40.327  -0.503  -31.232 1.00 34.14 ?  776 HOH B O   1 
HETATM 7071 O  O   . HOH M 7 .   ? 59.296  5.553   -51.522 1.00 41.18 ?  777 HOH B O   1 
HETATM 7072 O  O   . HOH M 7 .   ? 42.396  16.276  -33.040 1.00 21.24 ?  778 HOH B O   1 
HETATM 7073 O  O   . HOH M 7 .   ? 43.515  29.088  -42.845 1.00 22.54 ?  779 HOH B O   1 
HETATM 7074 O  O   . HOH M 7 .   ? 15.552  -7.086  -43.100 1.00 31.78 ?  780 HOH B O   1 
HETATM 7075 O  O   . HOH M 7 .   ? 34.202  1.891   -63.076 1.00 31.41 ?  781 HOH B O   1 
HETATM 7076 O  O   . HOH M 7 .   ? 16.589  0.053   -51.961 1.00 14.95 ?  782 HOH B O   1 
HETATM 7077 O  O   . HOH M 7 .   ? 29.326  5.531   -42.954 1.00 11.45 ?  783 HOH B O   1 
HETATM 7078 O  O   . HOH M 7 .   ? 23.479  -4.176  -71.624 1.00 33.93 ?  784 HOH B O   1 
HETATM 7079 O  O   . HOH M 7 .   ? 31.678  6.665   -59.368 1.00 20.72 ?  785 HOH B O   1 
HETATM 7080 O  O   . HOH M 7 .   ? 32.444  -1.046  -33.969 1.00 32.76 ?  786 HOH B O   1 
HETATM 7081 O  O   . HOH M 7 .   ? 44.375  27.427  -44.989 1.00 31.87 ?  787 HOH B O   1 
HETATM 7082 O  O   . HOH M 7 .   ? 31.388  17.963  -59.240 1.00 33.75 ?  788 HOH B O   1 
HETATM 7083 O  O   . HOH M 7 .   ? 47.531  5.331   -27.867 1.00 29.30 ?  789 HOH B O   1 
HETATM 7084 O  O   . HOH M 7 .   ? 60.075  5.644   -39.637 1.00 39.40 ?  790 HOH B O   1 
HETATM 7085 O  O   . HOH M 7 .   ? 29.936  5.086   -45.713 1.00 13.94 ?  791 HOH B O   1 
HETATM 7086 O  O   . HOH M 7 .   ? 49.952  -1.905  -33.350 1.00 31.77 ?  792 HOH B O   1 
HETATM 7087 O  O   . HOH M 7 .   ? 37.358  -5.136  -34.564 1.00 23.14 ?  793 HOH B O   1 
HETATM 7088 O  O   . HOH M 7 .   ? 47.490  2.588   -54.018 1.00 30.05 ?  794 HOH B O   1 
HETATM 7089 O  O   . HOH M 7 .   ? 5.317   -0.298  -36.488 1.00 33.28 ?  795 HOH B O   1 
HETATM 7090 O  O   . HOH M 7 .   ? 34.681  16.690  -55.655 1.00 25.00 ?  796 HOH B O   1 
HETATM 7091 O  O   . HOH M 7 .   ? 38.111  19.574  -30.007 1.00 33.15 ?  797 HOH B O   1 
HETATM 7092 O  O   . HOH M 7 .   ? 59.838  4.890   -45.960 1.00 37.35 ?  798 HOH B O   1 
HETATM 7093 O  O   . HOH M 7 .   ? 41.531  18.978  -32.547 1.00 30.91 ?  799 HOH B O   1 
HETATM 7094 O  O   . HOH M 7 .   ? 12.103  20.346  -33.992 1.00 40.32 ?  800 HOH B O   1 
HETATM 7095 O  O   . HOH M 7 .   ? 0.359   11.190  -53.775 1.00 29.55 ?  801 HOH B O   1 
HETATM 7096 O  O   . HOH M 7 .   ? 22.064  15.665  -54.595 1.00 15.73 ?  802 HOH B O   1 
HETATM 7097 O  O   . HOH M 7 .   ? 20.225  -13.149 -70.650 1.00 34.16 ?  803 HOH B O   1 
HETATM 7098 O  O   . HOH M 7 .   ? 3.657   8.461   -59.694 1.00 32.57 ?  804 HOH B O   1 
HETATM 7099 O  O   . HOH M 7 .   ? 25.666  19.805  -48.380 1.00 25.32 ?  805 HOH B O   1 
HETATM 7100 O  O   . HOH M 7 .   ? 25.267  15.575  -47.800 1.00 14.14 ?  806 HOH B O   1 
HETATM 7101 O  O   . HOH M 7 .   ? 31.668  13.612  -61.849 1.00 41.76 ?  807 HOH B O   1 
HETATM 7102 O  O   . HOH M 7 .   ? 9.210   17.510  -41.011 1.00 24.12 ?  808 HOH B O   1 
HETATM 7103 O  O   . HOH M 7 .   ? 43.576  0.742   -52.963 1.00 35.31 ?  809 HOH B O   1 
HETATM 7104 O  O   . HOH M 7 .   ? 27.096  8.979   -61.302 1.00 37.10 ?  810 HOH B O   1 
HETATM 7105 O  O   . HOH M 7 .   ? 59.014  14.951  -36.222 1.00 43.36 ?  811 HOH B O   1 
HETATM 7106 O  O   . HOH M 7 .   ? 7.856   -8.147  -52.284 1.00 35.67 ?  812 HOH B O   1 
HETATM 7107 O  O   . HOH M 7 .   ? 48.094  23.550  -40.770 1.00 33.22 ?  813 HOH B O   1 
HETATM 7108 O  O   . HOH M 7 .   ? 35.484  1.136   -32.157 1.00 37.21 ?  814 HOH B O   1 
HETATM 7109 O  O   . HOH M 7 .   ? 39.744  -0.937  -51.825 1.00 14.69 ?  815 HOH B O   1 
HETATM 7110 O  O   . HOH M 7 .   ? 46.636  22.695  -42.994 1.00 31.40 ?  816 HOH B O   1 
HETATM 7111 O  O   . HOH M 7 .   ? 20.295  -13.991 -62.661 1.00 36.59 ?  817 HOH B O   1 
HETATM 7112 O  O   . HOH M 7 .   ? 22.820  0.794   -72.883 1.00 40.93 ?  818 HOH B O   1 
HETATM 7113 O  O   . HOH M 7 .   ? 40.567  -0.288  -56.633 1.00 36.42 ?  819 HOH B O   1 
HETATM 7114 O  O   . HOH M 7 .   ? 38.882  -5.121  -56.994 1.00 31.74 ?  820 HOH B O   1 
HETATM 7115 O  O   . HOH M 7 .   ? 15.807  20.453  -48.172 1.00 25.36 ?  821 HOH B O   1 
HETATM 7116 O  O   . HOH M 7 .   ? 40.055  8.235   -57.577 1.00 36.01 ?  822 HOH B O   1 
HETATM 7117 O  O   . HOH M 7 .   ? 31.055  9.404   -59.057 1.00 22.77 ?  823 HOH B O   1 
HETATM 7118 O  O   . HOH M 7 .   ? 26.995  4.569   -49.774 1.00 16.17 ?  824 HOH B O   1 
HETATM 7119 O  O   . HOH M 7 .   ? 37.515  6.042   -56.890 1.00 36.82 ?  825 HOH B O   1 
HETATM 7120 O  O   . HOH M 7 .   ? 33.803  -3.107  -37.050 1.00 32.04 ?  826 HOH B O   1 
HETATM 7121 O  O   . HOH M 7 .   ? 30.608  -3.202  -30.841 1.00 40.58 ?  827 HOH B O   1 
HETATM 7122 O  O   . HOH M 7 .   ? 23.825  23.228  -54.386 1.00 34.74 ?  828 HOH B O   1 
HETATM 7123 O  O   . HOH M 7 .   ? 48.349  7.205   -26.181 1.00 37.35 ?  829 HOH B O   1 
HETATM 7124 O  O   . HOH M 7 .   ? 23.197  21.982  -47.578 1.00 29.87 ?  830 HOH B O   1 
HETATM 7125 O  O   . HOH M 7 .   ? 25.691  4.330   -65.477 1.00 32.13 ?  831 HOH B O   1 
HETATM 7126 O  O   . HOH M 7 .   ? 42.309  11.171  -27.490 1.00 28.73 ?  832 HOH B O   1 
HETATM 7127 O  O   . HOH M 7 .   ? 24.084  16.451  -50.137 1.00 17.31 ?  833 HOH B O   1 
HETATM 7128 O  O   . HOH M 7 .   ? 27.482  22.765  -17.384 1.00 21.72 ?  834 HOH B O   1 
HETATM 7129 O  O   . HOH M 7 .   ? 20.877  -4.719  -71.558 1.00 35.29 ?  835 HOH B O   1 
HETATM 7130 O  O   . HOH M 7 .   ? 49.646  9.633   -61.410 1.00 20.07 ?  836 HOH B O   1 
HETATM 7131 O  O   . HOH M 7 .   ? 32.739  28.091  -35.903 1.00 40.56 ?  837 HOH B O   1 
HETATM 7132 O  O   . HOH M 7 .   ? 45.466  29.417  -41.163 1.00 37.60 ?  838 HOH B O   1 
HETATM 7133 O  O   . HOH M 7 .   ? 15.304  12.120  -22.904 1.00 40.43 ?  839 HOH B O   1 
HETATM 7134 O  O   . HOH M 7 .   ? 57.488  9.875   -40.849 1.00 31.73 ?  840 HOH B O   1 
HETATM 7135 O  O   . HOH M 7 .   ? 27.533  19.407  -59.592 1.00 31.02 ?  841 HOH B O   1 
HETATM 7136 O  O   . HOH M 7 .   ? 36.047  30.638  -39.051 1.00 43.06 ?  842 HOH B O   1 
HETATM 7137 O  O   . HOH M 7 .   ? 13.664  -9.993  -69.462 1.00 34.75 ?  843 HOH B O   1 
HETATM 7138 O  O   . HOH M 7 .   ? 38.160  22.359  -53.626 1.00 36.06 ?  844 HOH B O   1 
HETATM 7139 O  O   . HOH M 7 .   ? 30.992  2.504   -29.547 1.00 32.07 ?  845 HOH B O   1 
HETATM 7140 O  O   . HOH M 7 .   ? 35.748  -1.787  -31.675 1.00 37.53 ?  846 HOH B O   1 
HETATM 7141 O  O   . HOH M 7 .   ? 33.060  18.812  -56.963 1.00 36.28 ?  847 HOH B O   1 
HETATM 7142 O  O   . HOH M 7 .   ? 14.683  3.824   -71.085 1.00 42.02 ?  848 HOH B O   1 
HETATM 7143 O  O   . HOH M 7 .   ? 26.918  22.867  -21.363 1.00 29.36 ?  849 HOH B O   1 
HETATM 7144 O  O   . HOH M 7 .   ? 17.977  23.654  -17.982 1.00 24.66 ?  850 HOH B O   1 
HETATM 7145 O  O   . HOH M 7 .   ? 29.683  23.732  -21.409 1.00 29.67 ?  851 HOH B O   1 
HETATM 7146 O  O   . HOH M 7 .   ? 24.866  17.871  -46.513 1.00 25.78 ?  852 HOH B O   1 
HETATM 7147 O  O   . HOH M 7 .   ? -0.141  12.477  -35.703 1.00 44.09 ?  853 HOH B O   1 
HETATM 7148 O  O   . HOH M 7 .   ? 26.251  6.841   -64.520 1.00 36.24 ?  854 HOH B O   1 
HETATM 7149 O  O   . HOH M 7 .   ? 18.250  -11.281 -70.498 1.00 35.83 ?  855 HOH B O   1 
HETATM 7150 O  O   . HOH M 7 .   ? 18.679  25.367  -37.200 1.00 37.80 ?  856 HOH B O   1 
HETATM 7151 O  O   . HOH M 7 .   ? -3.732  9.106   -44.668 1.00 36.80 ?  857 HOH B O   1 
HETATM 7152 O  O   . HOH M 7 .   ? 20.186  -7.557  -71.851 1.00 35.09 ?  858 HOH B O   1 
HETATM 7153 O  O   . HOH M 7 .   ? 35.746  -12.754 -52.794 1.00 36.94 ?  859 HOH B O   1 
HETATM 7154 O  O   . HOH M 7 .   ? 9.597   -10.807 -66.652 1.00 29.93 ?  860 HOH B O   1 
HETATM 7155 O  O   . HOH M 7 .   ? 20.345  23.744  -51.543 1.00 34.57 ?  861 HOH B O   1 
HETATM 7156 O  O   . HOH M 7 .   ? 16.177  19.466  -63.596 1.00 38.20 ?  862 HOH B O   1 
HETATM 7157 O  O   . HOH M 7 .   ? 33.573  -13.429 -55.146 1.00 34.67 ?  863 HOH B O   1 
HETATM 7158 O  O   . HOH M 7 .   ? 29.122  2.349   -64.270 1.00 36.67 ?  864 HOH B O   1 
HETATM 7159 O  O   . HOH M 7 .   ? 33.543  6.213   -61.321 1.00 37.79 ?  865 HOH B O   1 
HETATM 7160 O  O   . HOH M 7 .   ? 57.334  16.465  -35.535 1.00 38.62 ?  866 HOH B O   1 
HETATM 7161 O  O   . HOH M 7 .   ? 33.587  3.687   -30.338 1.00 29.69 ?  867 HOH B O   1 
HETATM 7162 O  O   . HOH M 7 .   ? 16.072  23.043  -48.680 1.00 37.96 ?  868 HOH B O   1 
HETATM 7163 O  O   . HOH M 7 .   ? 40.655  -11.937 -40.846 1.00 40.37 ?  869 HOH B O   1 
HETATM 7164 O  O   . HOH M 7 .   ? 13.689  22.129  -39.356 1.00 44.18 ?  870 HOH B O   1 
HETATM 7165 O  O   . HOH M 7 .   ? 63.275  5.192   -27.981 1.00 35.68 ?  871 HOH B O   1 
# 
