data_8KG1
# 
_entry.id   8KG1 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.398 
_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   8KG1         pdb_00008kg1 10.2210/pdb8kg1/pdb 
WWPDB D_1300040350 ?            ?                   
# 
_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       2024-11-20 
# 
_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                        8KG1 
_pdbx_database_status.recvd_initial_deposition_date   2023-08-17 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBC 
_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 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.email              liux@nankai.edu.cn 
_pdbx_contact_author.name_first         Xiang 
_pdbx_contact_author.name_last          Liu 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-5498-6942 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Liu, X.'  1 0000-0001-5498-6942 
'Tang, Y.' 2 0000-0002-8656-3220 
'Liu, Y.'  3 0009-0008-8335-3923 
'Ma, M.'   4 0009-0002-7651-2304 
'Gao, Y.'  5 0000-0002-0364-6427 
# 
_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                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To be published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Crystal structure of the cargo cysteine desulfurase from Mycobacterium smegmatis' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Liu, X.'  1 0000-0001-5498-6942 
primary 'Tang, Y.' 2 0000-0002-8656-3220 
# 
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 'cysteine desulfurase' 46524.297 2   2.8.1.7 ? ? ? 
2 water   nat water                  18.015    529 ?       ? ? ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   yes 
_entity_poly.pdbx_seq_one_letter_code       
;AHQPVPQFPDRHEIFDVNAIRADFPILRETVNGKPLIWFDNAATTQKPQAVIDRLSHFYAHENSNIHRAAHELAARATDA
YEDAREAVRRFIGAAKAEEIIFLRGTTEAINLVAHAWGGKHLGPGDEIVITHLEHHANIVPWQLLSRQTGAVLKVAPVDD
AGNLLLGEFEDLLGPRTKLVAATQVSNALGTVTPVETIVELGHRYGARVLIDGAQSIPHMPIDVAALGADFFVFSGH
(LLP)IYGPTGIGVLYGREDALAETPPWQGGGNMIADVTLERSLYQGPPNKFEAGTGNIADAVGLGEAIRYVERVGIERI
AAYEHALLEYATPRLAAIPGVRIVGTAQEKASVLSFVLAGHEPLEVGKALNAEGIAVRAGHHCAQPILRRMGLEATVRPS
FAFYNTFDEIDVFIDAVRRIAEGSVDYKDDDDK
;
_entity_poly.pdbx_seq_one_letter_code_can   
;AHQPVPQFPDRHEIFDVNAIRADFPILRETVNGKPLIWFDNAATTQKPQAVIDRLSHFYAHENSNIHRAAHELAARATDA
YEDAREAVRRFIGAAKAEEIIFLRGTTEAINLVAHAWGGKHLGPGDEIVITHLEHHANIVPWQLLSRQTGAVLKVAPVDD
AGNLLLGEFEDLLGPRTKLVAATQVSNALGTVTPVETIVELGHRYGARVLIDGAQSIPHMPIDVAALGADFFVFSGHKIY
GPTGIGVLYGREDALAETPPWQGGGNMIADVTLERSLYQGPPNKFEAGTGNIADAVGLGEAIRYVERVGIERIAAYEHAL
LEYATPRLAAIPGVRIVGTAQEKASVLSFVLAGHEPLEVGKALNAEGIAVRAGHHCAQPILRRMGLEATVRPSFAFYNTF
DEIDVFIDAVRRIAEGSVDYKDDDDK
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
_pdbx_entity_nonpoly.entity_id   2 
_pdbx_entity_nonpoly.name        water 
_pdbx_entity_nonpoly.comp_id     HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   ALA n 
1 2   HIS n 
1 3   GLN n 
1 4   PRO n 
1 5   VAL n 
1 6   PRO n 
1 7   GLN n 
1 8   PHE n 
1 9   PRO n 
1 10  ASP n 
1 11  ARG n 
1 12  HIS n 
1 13  GLU n 
1 14  ILE n 
1 15  PHE n 
1 16  ASP n 
1 17  VAL n 
1 18  ASN n 
1 19  ALA n 
1 20  ILE n 
1 21  ARG n 
1 22  ALA n 
1 23  ASP n 
1 24  PHE n 
1 25  PRO n 
1 26  ILE n 
1 27  LEU n 
1 28  ARG n 
1 29  GLU n 
1 30  THR n 
1 31  VAL n 
1 32  ASN n 
1 33  GLY n 
1 34  LYS n 
1 35  PRO n 
1 36  LEU n 
1 37  ILE n 
1 38  TRP n 
1 39  PHE n 
1 40  ASP n 
1 41  ASN n 
1 42  ALA n 
1 43  ALA n 
1 44  THR n 
1 45  THR n 
1 46  GLN n 
1 47  LYS n 
1 48  PRO n 
1 49  GLN n 
1 50  ALA n 
1 51  VAL n 
1 52  ILE n 
1 53  ASP n 
1 54  ARG n 
1 55  LEU n 
1 56  SER n 
1 57  HIS n 
1 58  PHE n 
1 59  TYR n 
1 60  ALA n 
1 61  HIS n 
1 62  GLU n 
1 63  ASN n 
1 64  SER n 
1 65  ASN n 
1 66  ILE n 
1 67  HIS n 
1 68  ARG n 
1 69  ALA n 
1 70  ALA n 
1 71  HIS n 
1 72  GLU n 
1 73  LEU n 
1 74  ALA n 
1 75  ALA n 
1 76  ARG n 
1 77  ALA n 
1 78  THR n 
1 79  ASP n 
1 80  ALA n 
1 81  TYR n 
1 82  GLU n 
1 83  ASP n 
1 84  ALA n 
1 85  ARG n 
1 86  GLU n 
1 87  ALA n 
1 88  VAL n 
1 89  ARG n 
1 90  ARG n 
1 91  PHE n 
1 92  ILE n 
1 93  GLY n 
1 94  ALA n 
1 95  ALA n 
1 96  LYS n 
1 97  ALA n 
1 98  GLU n 
1 99  GLU n 
1 100 ILE n 
1 101 ILE n 
1 102 PHE n 
1 103 LEU n 
1 104 ARG n 
1 105 GLY n 
1 106 THR n 
1 107 THR n 
1 108 GLU n 
1 109 ALA n 
1 110 ILE n 
1 111 ASN n 
1 112 LEU n 
1 113 VAL n 
1 114 ALA n 
1 115 HIS n 
1 116 ALA n 
1 117 TRP n 
1 118 GLY n 
1 119 GLY n 
1 120 LYS n 
1 121 HIS n 
1 122 LEU n 
1 123 GLY n 
1 124 PRO n 
1 125 GLY n 
1 126 ASP n 
1 127 GLU n 
1 128 ILE n 
1 129 VAL n 
1 130 ILE n 
1 131 THR n 
1 132 HIS n 
1 133 LEU n 
1 134 GLU n 
1 135 HIS n 
1 136 HIS n 
1 137 ALA n 
1 138 ASN n 
1 139 ILE n 
1 140 VAL n 
1 141 PRO n 
1 142 TRP n 
1 143 GLN n 
1 144 LEU n 
1 145 LEU n 
1 146 SER n 
1 147 ARG n 
1 148 GLN n 
1 149 THR n 
1 150 GLY n 
1 151 ALA n 
1 152 VAL n 
1 153 LEU n 
1 154 LYS n 
1 155 VAL n 
1 156 ALA n 
1 157 PRO n 
1 158 VAL n 
1 159 ASP n 
1 160 ASP n 
1 161 ALA n 
1 162 GLY n 
1 163 ASN n 
1 164 LEU n 
1 165 LEU n 
1 166 LEU n 
1 167 GLY n 
1 168 GLU n 
1 169 PHE n 
1 170 GLU n 
1 171 ASP n 
1 172 LEU n 
1 173 LEU n 
1 174 GLY n 
1 175 PRO n 
1 176 ARG n 
1 177 THR n 
1 178 LYS n 
1 179 LEU n 
1 180 VAL n 
1 181 ALA n 
1 182 ALA n 
1 183 THR n 
1 184 GLN n 
1 185 VAL n 
1 186 SER n 
1 187 ASN n 
1 188 ALA n 
1 189 LEU n 
1 190 GLY n 
1 191 THR n 
1 192 VAL n 
1 193 THR n 
1 194 PRO n 
1 195 VAL n 
1 196 GLU n 
1 197 THR n 
1 198 ILE n 
1 199 VAL n 
1 200 GLU n 
1 201 LEU n 
1 202 GLY n 
1 203 HIS n 
1 204 ARG n 
1 205 TYR n 
1 206 GLY n 
1 207 ALA n 
1 208 ARG n 
1 209 VAL n 
1 210 LEU n 
1 211 ILE n 
1 212 ASP n 
1 213 GLY n 
1 214 ALA n 
1 215 GLN n 
1 216 SER n 
1 217 ILE n 
1 218 PRO n 
1 219 HIS n 
1 220 MET n 
1 221 PRO n 
1 222 ILE n 
1 223 ASP n 
1 224 VAL n 
1 225 ALA n 
1 226 ALA n 
1 227 LEU n 
1 228 GLY n 
1 229 ALA n 
1 230 ASP n 
1 231 PHE n 
1 232 PHE n 
1 233 VAL n 
1 234 PHE n 
1 235 SER n 
1 236 GLY n 
1 237 HIS n 
1 238 LLP n 
1 239 ILE n 
1 240 TYR n 
1 241 GLY n 
1 242 PRO n 
1 243 THR n 
1 244 GLY n 
1 245 ILE n 
1 246 GLY n 
1 247 VAL n 
1 248 LEU n 
1 249 TYR n 
1 250 GLY n 
1 251 ARG n 
1 252 GLU n 
1 253 ASP n 
1 254 ALA n 
1 255 LEU n 
1 256 ALA n 
1 257 GLU n 
1 258 THR n 
1 259 PRO n 
1 260 PRO n 
1 261 TRP n 
1 262 GLN n 
1 263 GLY n 
1 264 GLY n 
1 265 GLY n 
1 266 ASN n 
1 267 MET n 
1 268 ILE n 
1 269 ALA n 
1 270 ASP n 
1 271 VAL n 
1 272 THR n 
1 273 LEU n 
1 274 GLU n 
1 275 ARG n 
1 276 SER n 
1 277 LEU n 
1 278 TYR n 
1 279 GLN n 
1 280 GLY n 
1 281 PRO n 
1 282 PRO n 
1 283 ASN n 
1 284 LYS n 
1 285 PHE n 
1 286 GLU n 
1 287 ALA n 
1 288 GLY n 
1 289 THR n 
1 290 GLY n 
1 291 ASN n 
1 292 ILE n 
1 293 ALA n 
1 294 ASP n 
1 295 ALA n 
1 296 VAL n 
1 297 GLY n 
1 298 LEU n 
1 299 GLY n 
1 300 GLU n 
1 301 ALA n 
1 302 ILE n 
1 303 ARG n 
1 304 TYR n 
1 305 VAL n 
1 306 GLU n 
1 307 ARG n 
1 308 VAL n 
1 309 GLY n 
1 310 ILE n 
1 311 GLU n 
1 312 ARG n 
1 313 ILE n 
1 314 ALA n 
1 315 ALA n 
1 316 TYR n 
1 317 GLU n 
1 318 HIS n 
1 319 ALA n 
1 320 LEU n 
1 321 LEU n 
1 322 GLU n 
1 323 TYR n 
1 324 ALA n 
1 325 THR n 
1 326 PRO n 
1 327 ARG n 
1 328 LEU n 
1 329 ALA n 
1 330 ALA n 
1 331 ILE n 
1 332 PRO n 
1 333 GLY n 
1 334 VAL n 
1 335 ARG n 
1 336 ILE n 
1 337 VAL n 
1 338 GLY n 
1 339 THR n 
1 340 ALA n 
1 341 GLN n 
1 342 GLU n 
1 343 LYS n 
1 344 ALA n 
1 345 SER n 
1 346 VAL n 
1 347 LEU n 
1 348 SER n 
1 349 PHE n 
1 350 VAL n 
1 351 LEU n 
1 352 ALA n 
1 353 GLY n 
1 354 HIS n 
1 355 GLU n 
1 356 PRO n 
1 357 LEU n 
1 358 GLU n 
1 359 VAL n 
1 360 GLY n 
1 361 LYS n 
1 362 ALA n 
1 363 LEU n 
1 364 ASN n 
1 365 ALA n 
1 366 GLU n 
1 367 GLY n 
1 368 ILE n 
1 369 ALA n 
1 370 VAL n 
1 371 ARG n 
1 372 ALA n 
1 373 GLY n 
1 374 HIS n 
1 375 HIS n 
1 376 CYS n 
1 377 ALA n 
1 378 GLN n 
1 379 PRO n 
1 380 ILE n 
1 381 LEU n 
1 382 ARG n 
1 383 ARG n 
1 384 MET n 
1 385 GLY n 
1 386 LEU n 
1 387 GLU n 
1 388 ALA n 
1 389 THR n 
1 390 VAL n 
1 391 ARG n 
1 392 PRO n 
1 393 SER n 
1 394 PHE n 
1 395 ALA n 
1 396 PHE n 
1 397 TYR n 
1 398 ASN n 
1 399 THR n 
1 400 PHE n 
1 401 ASP n 
1 402 GLU n 
1 403 ILE n 
1 404 ASP n 
1 405 VAL n 
1 406 PHE n 
1 407 ILE n 
1 408 ASP n 
1 409 ALA n 
1 410 VAL n 
1 411 ARG n 
1 412 ARG n 
1 413 ILE n 
1 414 ALA n 
1 415 GLU n 
1 416 GLY n 
1 417 SER n 
1 418 VAL n 
1 419 ASP n 
1 420 TYR n 
1 421 LYS n 
1 422 ASP n 
1 423 ASP n 
1 424 ASP n 
1 425 ASP n 
1 426 LYS 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                   426 
_entity_src_gen.gene_src_common_name               'Mycobacterium smegmatis' 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 MSMEI_4425 
_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      'Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155)' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     246196 
_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               'Mycobacterium smegmatis' 
_entity_src_gen.pdbx_host_org_scientific_name      'Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     246196 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
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 
LLP 'L-peptide linking' n '(2S)-2-amino-6-[[3-hydroxy-2-methyl-5-(phosphonooxymethyl)pyridin-4-yl]methylideneamino]hexanoic acid' 
"N'-PYRIDOXYL-LYSINE-5'-MONOPHOSPHATE" 'C14 H22 N3 O7 P' 375.314 
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 
PHE 'L-peptide linking' y PHENYLALANINE                                                                                           
?                                      'C9 H11 N O2'     165.189 
PRO 'L-peptide linking' y PROLINE                                                                                                 
?                                      'C5 H9 N O2'      115.130 
SER 'L-peptide linking' y SERINE                                                                                                  
?                                      'C3 H7 N O3'      105.093 
THR 'L-peptide linking' y THREONINE                                                                                               
?                                      'C4 H9 N O3'      119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                                                                              
?                                      'C11 H12 N2 O2'   204.225 
TYR 'L-peptide linking' y TYROSINE                                                                                                
?                                      'C9 H11 N O3'     181.189 
VAL 'L-peptide linking' y VALINE                                                                                                  
?                                      'C5 H11 N O2'     117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   ALA 1   142 ?   ?   ?   A . n 
A 1 2   HIS 2   143 ?   ?   ?   A . n 
A 1 3   GLN 3   144 ?   ?   ?   A . n 
A 1 4   PRO 4   145 ?   ?   ?   A . n 
A 1 5   VAL 5   146 ?   ?   ?   A . n 
A 1 6   PRO 6   147 ?   ?   ?   A . n 
A 1 7   GLN 7   148 ?   ?   ?   A . n 
A 1 8   PHE 8   149 ?   ?   ?   A . n 
A 1 9   PRO 9   150 ?   ?   ?   A . n 
A 1 10  ASP 10  151 ?   ?   ?   A . n 
A 1 11  ARG 11  152 152 ARG ARG A . n 
A 1 12  HIS 12  153 153 HIS HIS A . n 
A 1 13  GLU 13  154 154 GLU GLU A . n 
A 1 14  ILE 14  155 155 ILE ILE A . n 
A 1 15  PHE 15  156 156 PHE PHE A . n 
A 1 16  ASP 16  157 157 ASP ASP A . n 
A 1 17  VAL 17  158 158 VAL VAL A . n 
A 1 18  ASN 18  159 159 ASN ASN A . n 
A 1 19  ALA 19  160 160 ALA ALA A . n 
A 1 20  ILE 20  161 161 ILE ILE A . n 
A 1 21  ARG 21  162 162 ARG ARG A . n 
A 1 22  ALA 22  163 163 ALA ALA A . n 
A 1 23  ASP 23  164 164 ASP ASP A . n 
A 1 24  PHE 24  165 165 PHE PHE A . n 
A 1 25  PRO 25  166 166 PRO PRO A . n 
A 1 26  ILE 26  167 167 ILE ILE A . n 
A 1 27  LEU 27  168 168 LEU LEU A . n 
A 1 28  ARG 28  169 169 ARG ARG A . n 
A 1 29  GLU 29  170 170 GLU GLU A . n 
A 1 30  THR 30  171 171 THR THR A . n 
A 1 31  VAL 31  172 172 VAL VAL A . n 
A 1 32  ASN 32  173 173 ASN ASN A . n 
A 1 33  GLY 33  174 174 GLY GLY A . n 
A 1 34  LYS 34  175 175 LYS LYS A . n 
A 1 35  PRO 35  176 176 PRO PRO A . n 
A 1 36  LEU 36  177 177 LEU LEU A . n 
A 1 37  ILE 37  178 178 ILE ILE A . n 
A 1 38  TRP 38  179 179 TRP TRP A . n 
A 1 39  PHE 39  180 180 PHE PHE A . n 
A 1 40  ASP 40  181 181 ASP ASP A . n 
A 1 41  ASN 41  182 182 ASN ASN A . n 
A 1 42  ALA 42  183 183 ALA ALA A . n 
A 1 43  ALA 43  184 184 ALA ALA A . n 
A 1 44  THR 44  185 185 THR THR A . n 
A 1 45  THR 45  186 186 THR THR A . n 
A 1 46  GLN 46  187 187 GLN GLN A . n 
A 1 47  LYS 47  188 188 LYS LYS A . n 
A 1 48  PRO 48  189 189 PRO PRO A . n 
A 1 49  GLN 49  190 190 GLN GLN A . n 
A 1 50  ALA 50  191 191 ALA ALA A . n 
A 1 51  VAL 51  192 192 VAL VAL A . n 
A 1 52  ILE 52  193 193 ILE ILE A . n 
A 1 53  ASP 53  194 194 ASP ASP A . n 
A 1 54  ARG 54  195 195 ARG ARG A . n 
A 1 55  LEU 55  196 196 LEU LEU A . n 
A 1 56  SER 56  197 197 SER SER A . n 
A 1 57  HIS 57  198 198 HIS HIS A . n 
A 1 58  PHE 58  199 199 PHE PHE A . n 
A 1 59  TYR 59  200 200 TYR TYR A . n 
A 1 60  ALA 60  201 201 ALA ALA A . n 
A 1 61  HIS 61  202 202 HIS HIS A . n 
A 1 62  GLU 62  203 203 GLU GLU A . n 
A 1 63  ASN 63  204 204 ASN ASN A . n 
A 1 64  SER 64  205 205 SER SER A . n 
A 1 65  ASN 65  206 206 ASN ASN A . n 
A 1 66  ILE 66  207 207 ILE ILE A . n 
A 1 67  HIS 67  208 208 HIS HIS A . n 
A 1 68  ARG 68  209 209 ARG ARG A . n 
A 1 69  ALA 69  210 210 ALA ALA A . n 
A 1 70  ALA 70  211 211 ALA ALA A . n 
A 1 71  HIS 71  212 212 HIS HIS A . n 
A 1 72  GLU 72  213 213 GLU GLU A . n 
A 1 73  LEU 73  214 214 LEU LEU A . n 
A 1 74  ALA 74  215 215 ALA ALA A . n 
A 1 75  ALA 75  216 216 ALA ALA A . n 
A 1 76  ARG 76  217 217 ARG ARG A . n 
A 1 77  ALA 77  218 218 ALA ALA A . n 
A 1 78  THR 78  219 219 THR THR A . n 
A 1 79  ASP 79  220 220 ASP ASP A . n 
A 1 80  ALA 80  221 221 ALA ALA A . n 
A 1 81  TYR 81  222 222 TYR TYR A . n 
A 1 82  GLU 82  223 223 GLU GLU A . n 
A 1 83  ASP 83  224 224 ASP ASP A . n 
A 1 84  ALA 84  225 225 ALA ALA A . n 
A 1 85  ARG 85  226 226 ARG ARG A . n 
A 1 86  GLU 86  227 227 GLU GLU A . n 
A 1 87  ALA 87  228 228 ALA ALA A . n 
A 1 88  VAL 88  229 229 VAL VAL A . n 
A 1 89  ARG 89  230 230 ARG ARG A . n 
A 1 90  ARG 90  231 231 ARG ARG A . n 
A 1 91  PHE 91  232 232 PHE PHE A . n 
A 1 92  ILE 92  233 233 ILE ILE A . n 
A 1 93  GLY 93  234 234 GLY GLY A . n 
A 1 94  ALA 94  235 235 ALA ALA A . n 
A 1 95  ALA 95  236 236 ALA ALA A . n 
A 1 96  LYS 96  237 237 LYS LYS A . n 
A 1 97  ALA 97  238 238 ALA ALA A . n 
A 1 98  GLU 98  239 239 GLU GLU A . n 
A 1 99  GLU 99  240 240 GLU GLU A . n 
A 1 100 ILE 100 241 241 ILE ILE A . n 
A 1 101 ILE 101 242 242 ILE ILE A . n 
A 1 102 PHE 102 243 243 PHE PHE A . n 
A 1 103 LEU 103 244 244 LEU LEU A . n 
A 1 104 ARG 104 245 245 ARG ARG A . n 
A 1 105 GLY 105 246 246 GLY GLY A . n 
A 1 106 THR 106 247 247 THR THR A . n 
A 1 107 THR 107 248 248 THR THR A . n 
A 1 108 GLU 108 249 249 GLU GLU A . n 
A 1 109 ALA 109 250 250 ALA ALA A . n 
A 1 110 ILE 110 251 251 ILE ILE A . n 
A 1 111 ASN 111 252 252 ASN ASN A . n 
A 1 112 LEU 112 253 253 LEU LEU A . n 
A 1 113 VAL 113 254 254 VAL VAL A . n 
A 1 114 ALA 114 255 255 ALA ALA A . n 
A 1 115 HIS 115 256 256 HIS HIS A . n 
A 1 116 ALA 116 257 257 ALA ALA A . n 
A 1 117 TRP 117 258 258 TRP TRP A . n 
A 1 118 GLY 118 259 259 GLY GLY A . n 
A 1 119 GLY 119 260 260 GLY GLY A . n 
A 1 120 LYS 120 261 261 LYS LYS A . n 
A 1 121 HIS 121 262 262 HIS HIS A . n 
A 1 122 LEU 122 263 263 LEU LEU A . n 
A 1 123 GLY 123 264 264 GLY GLY A . n 
A 1 124 PRO 124 265 265 PRO PRO A . n 
A 1 125 GLY 125 266 266 GLY GLY A . n 
A 1 126 ASP 126 267 267 ASP ASP A . n 
A 1 127 GLU 127 268 268 GLU GLU A . n 
A 1 128 ILE 128 269 269 ILE ILE A . n 
A 1 129 VAL 129 270 270 VAL VAL A . n 
A 1 130 ILE 130 271 271 ILE ILE A . n 
A 1 131 THR 131 272 272 THR THR A . n 
A 1 132 HIS 132 273 273 HIS HIS A . n 
A 1 133 LEU 133 274 274 LEU LEU A . n 
A 1 134 GLU 134 275 275 GLU GLU A . n 
A 1 135 HIS 135 276 276 HIS HIS A . n 
A 1 136 HIS 136 277 277 HIS HIS A . n 
A 1 137 ALA 137 278 278 ALA ALA A . n 
A 1 138 ASN 138 279 279 ASN ASN A . n 
A 1 139 ILE 139 280 280 ILE ILE A . n 
A 1 140 VAL 140 281 281 VAL VAL A . n 
A 1 141 PRO 141 282 282 PRO PRO A . n 
A 1 142 TRP 142 283 283 TRP TRP A . n 
A 1 143 GLN 143 284 284 GLN GLN A . n 
A 1 144 LEU 144 285 285 LEU LEU A . n 
A 1 145 LEU 145 286 286 LEU LEU A . n 
A 1 146 SER 146 287 287 SER SER A . n 
A 1 147 ARG 147 288 288 ARG ARG A . n 
A 1 148 GLN 148 289 289 GLN GLN A . n 
A 1 149 THR 149 290 290 THR THR A . n 
A 1 150 GLY 150 291 291 GLY GLY A . n 
A 1 151 ALA 151 292 292 ALA ALA A . n 
A 1 152 VAL 152 293 293 VAL VAL A . n 
A 1 153 LEU 153 294 294 LEU LEU A . n 
A 1 154 LYS 154 295 295 LYS LYS A . n 
A 1 155 VAL 155 296 296 VAL VAL A . n 
A 1 156 ALA 156 297 297 ALA ALA A . n 
A 1 157 PRO 157 298 298 PRO PRO A . n 
A 1 158 VAL 158 299 299 VAL VAL A . n 
A 1 159 ASP 159 300 300 ASP ASP A . n 
A 1 160 ASP 160 301 301 ASP ASP A . n 
A 1 161 ALA 161 302 302 ALA ALA A . n 
A 1 162 GLY 162 303 303 GLY GLY A . n 
A 1 163 ASN 163 304 304 ASN ASN A . n 
A 1 164 LEU 164 305 305 LEU LEU A . n 
A 1 165 LEU 165 306 306 LEU LEU A . n 
A 1 166 LEU 166 307 307 LEU LEU A . n 
A 1 167 GLY 167 308 308 GLY GLY A . n 
A 1 168 GLU 168 309 309 GLU GLU A . n 
A 1 169 PHE 169 310 310 PHE PHE A . n 
A 1 170 GLU 170 311 311 GLU GLU A . n 
A 1 171 ASP 171 312 312 ASP ASP A . n 
A 1 172 LEU 172 313 313 LEU LEU A . n 
A 1 173 LEU 173 314 314 LEU LEU A . n 
A 1 174 GLY 174 315 315 GLY GLY A . n 
A 1 175 PRO 175 316 316 PRO PRO A . n 
A 1 176 ARG 176 317 317 ARG ARG A . n 
A 1 177 THR 177 318 318 THR THR A . n 
A 1 178 LYS 178 319 319 LYS LYS A . n 
A 1 179 LEU 179 320 320 LEU LEU A . n 
A 1 180 VAL 180 321 321 VAL VAL A . n 
A 1 181 ALA 181 322 322 ALA ALA A . n 
A 1 182 ALA 182 323 323 ALA ALA A . n 
A 1 183 THR 183 324 324 THR THR A . n 
A 1 184 GLN 184 325 325 GLN GLN A . n 
A 1 185 VAL 185 326 326 VAL VAL A . n 
A 1 186 SER 186 327 327 SER SER A . n 
A 1 187 ASN 187 328 328 ASN ASN A . n 
A 1 188 ALA 188 329 329 ALA ALA A . n 
A 1 189 LEU 189 330 330 LEU LEU A . n 
A 1 190 GLY 190 331 331 GLY GLY A . n 
A 1 191 THR 191 332 332 THR THR A . n 
A 1 192 VAL 192 333 333 VAL VAL A . n 
A 1 193 THR 193 334 334 THR THR A . n 
A 1 194 PRO 194 335 335 PRO PRO A . n 
A 1 195 VAL 195 336 336 VAL VAL A . n 
A 1 196 GLU 196 337 337 GLU GLU A . n 
A 1 197 THR 197 338 338 THR THR A . n 
A 1 198 ILE 198 339 339 ILE ILE A . n 
A 1 199 VAL 199 340 340 VAL VAL A . n 
A 1 200 GLU 200 341 341 GLU GLU A . n 
A 1 201 LEU 201 342 342 LEU LEU A . n 
A 1 202 GLY 202 343 343 GLY GLY A . n 
A 1 203 HIS 203 344 344 HIS HIS A . n 
A 1 204 ARG 204 345 345 ARG ARG A . n 
A 1 205 TYR 205 346 346 TYR TYR A . n 
A 1 206 GLY 206 347 347 GLY GLY A . n 
A 1 207 ALA 207 348 348 ALA ALA A . n 
A 1 208 ARG 208 349 349 ARG ARG A . n 
A 1 209 VAL 209 350 350 VAL VAL A . n 
A 1 210 LEU 210 351 351 LEU LEU A . n 
A 1 211 ILE 211 352 352 ILE ILE A . n 
A 1 212 ASP 212 353 353 ASP ASP A . n 
A 1 213 GLY 213 354 354 GLY GLY A . n 
A 1 214 ALA 214 355 355 ALA ALA A . n 
A 1 215 GLN 215 356 356 GLN GLN A . n 
A 1 216 SER 216 357 357 SER SER A . n 
A 1 217 ILE 217 358 358 ILE ILE A . n 
A 1 218 PRO 218 359 359 PRO PRO A . n 
A 1 219 HIS 219 360 360 HIS HIS A . n 
A 1 220 MET 220 361 361 MET MET A . n 
A 1 221 PRO 221 362 362 PRO PRO A . n 
A 1 222 ILE 222 363 363 ILE ILE A . n 
A 1 223 ASP 223 364 364 ASP ASP A . n 
A 1 224 VAL 224 365 365 VAL VAL A . n 
A 1 225 ALA 225 366 366 ALA ALA A . n 
A 1 226 ALA 226 367 367 ALA ALA A . n 
A 1 227 LEU 227 368 368 LEU LEU A . n 
A 1 228 GLY 228 369 369 GLY GLY A . n 
A 1 229 ALA 229 370 370 ALA ALA A . n 
A 1 230 ASP 230 371 371 ASP ASP A . n 
A 1 231 PHE 231 372 372 PHE PHE A . n 
A 1 232 PHE 232 373 373 PHE PHE A . n 
A 1 233 VAL 233 374 374 VAL VAL A . n 
A 1 234 PHE 234 375 375 PHE PHE A . n 
A 1 235 SER 235 376 376 SER SER A . n 
A 1 236 GLY 236 377 377 GLY GLY A . n 
A 1 237 HIS 237 378 378 HIS HIS A . n 
A 1 238 LLP 238 379 379 LLP LLP A . n 
A 1 239 ILE 239 380 380 ILE ILE A . n 
A 1 240 TYR 240 381 381 TYR TYR A . n 
A 1 241 GLY 241 382 382 GLY GLY A . n 
A 1 242 PRO 242 383 383 PRO PRO A . n 
A 1 243 THR 243 384 384 THR THR A . n 
A 1 244 GLY 244 385 385 GLY GLY A . n 
A 1 245 ILE 245 386 386 ILE ILE A . n 
A 1 246 GLY 246 387 387 GLY GLY A . n 
A 1 247 VAL 247 388 388 VAL VAL A . n 
A 1 248 LEU 248 389 389 LEU LEU A . n 
A 1 249 TYR 249 390 390 TYR TYR A . n 
A 1 250 GLY 250 391 391 GLY GLY A . n 
A 1 251 ARG 251 392 392 ARG ARG A . n 
A 1 252 GLU 252 393 393 GLU GLU A . n 
A 1 253 ASP 253 394 394 ASP ASP A . n 
A 1 254 ALA 254 395 395 ALA ALA A . n 
A 1 255 LEU 255 396 396 LEU LEU A . n 
A 1 256 ALA 256 397 397 ALA ALA A . n 
A 1 257 GLU 257 398 398 GLU GLU A . n 
A 1 258 THR 258 399 399 THR THR A . n 
A 1 259 PRO 259 400 400 PRO PRO A . n 
A 1 260 PRO 260 401 401 PRO PRO A . n 
A 1 261 TRP 261 402 402 TRP TRP A . n 
A 1 262 GLN 262 403 403 GLN GLN A . n 
A 1 263 GLY 263 404 404 GLY GLY A . n 
A 1 264 GLY 264 405 405 GLY GLY A . n 
A 1 265 GLY 265 406 406 GLY GLY A . n 
A 1 266 ASN 266 407 407 ASN ASN A . n 
A 1 267 MET 267 408 408 MET MET A . n 
A 1 268 ILE 268 409 409 ILE ILE A . n 
A 1 269 ALA 269 410 410 ALA ALA A . n 
A 1 270 ASP 270 411 411 ASP ASP A . n 
A 1 271 VAL 271 412 412 VAL VAL A . n 
A 1 272 THR 272 413 413 THR THR A . n 
A 1 273 LEU 273 414 414 LEU LEU A . n 
A 1 274 GLU 274 415 415 GLU GLU A . n 
A 1 275 ARG 275 416 416 ARG ARG A . n 
A 1 276 SER 276 417 417 SER SER A . n 
A 1 277 LEU 277 418 418 LEU LEU A . n 
A 1 278 TYR 278 419 419 TYR TYR A . n 
A 1 279 GLN 279 420 420 GLN GLN A . n 
A 1 280 GLY 280 421 421 GLY GLY A . n 
A 1 281 PRO 281 422 422 PRO PRO A . n 
A 1 282 PRO 282 423 423 PRO PRO A . n 
A 1 283 ASN 283 424 424 ASN ASN A . n 
A 1 284 LYS 284 425 425 LYS LYS A . n 
A 1 285 PHE 285 426 426 PHE PHE A . n 
A 1 286 GLU 286 427 427 GLU GLU A . n 
A 1 287 ALA 287 428 428 ALA ALA A . n 
A 1 288 GLY 288 429 429 GLY GLY A . n 
A 1 289 THR 289 430 430 THR THR A . n 
A 1 290 GLY 290 431 431 GLY GLY A . n 
A 1 291 ASN 291 432 432 ASN ASN A . n 
A 1 292 ILE 292 433 433 ILE ILE A . n 
A 1 293 ALA 293 434 434 ALA ALA A . n 
A 1 294 ASP 294 435 435 ASP ASP A . n 
A 1 295 ALA 295 436 436 ALA ALA A . n 
A 1 296 VAL 296 437 437 VAL VAL A . n 
A 1 297 GLY 297 438 438 GLY GLY A . n 
A 1 298 LEU 298 439 439 LEU LEU A . n 
A 1 299 GLY 299 440 440 GLY GLY A . n 
A 1 300 GLU 300 441 441 GLU GLU A . n 
A 1 301 ALA 301 442 442 ALA ALA A . n 
A 1 302 ILE 302 443 443 ILE ILE A . n 
A 1 303 ARG 303 444 444 ARG ARG A . n 
A 1 304 TYR 304 445 445 TYR TYR A . n 
A 1 305 VAL 305 446 446 VAL VAL A . n 
A 1 306 GLU 306 447 447 GLU GLU A . n 
A 1 307 ARG 307 448 448 ARG ARG A . n 
A 1 308 VAL 308 449 449 VAL VAL A . n 
A 1 309 GLY 309 450 450 GLY GLY A . n 
A 1 310 ILE 310 451 451 ILE ILE A . n 
A 1 311 GLU 311 452 452 GLU GLU A . n 
A 1 312 ARG 312 453 453 ARG ARG A . n 
A 1 313 ILE 313 454 454 ILE ILE A . n 
A 1 314 ALA 314 455 455 ALA ALA A . n 
A 1 315 ALA 315 456 456 ALA ALA A . n 
A 1 316 TYR 316 457 457 TYR TYR A . n 
A 1 317 GLU 317 458 458 GLU GLU A . n 
A 1 318 HIS 318 459 459 HIS HIS A . n 
A 1 319 ALA 319 460 460 ALA ALA A . n 
A 1 320 LEU 320 461 461 LEU LEU A . n 
A 1 321 LEU 321 462 462 LEU LEU A . n 
A 1 322 GLU 322 463 463 GLU GLU A . n 
A 1 323 TYR 323 464 464 TYR TYR A . n 
A 1 324 ALA 324 465 465 ALA ALA A . n 
A 1 325 THR 325 466 466 THR THR A . n 
A 1 326 PRO 326 467 467 PRO PRO A . n 
A 1 327 ARG 327 468 468 ARG ARG A . n 
A 1 328 LEU 328 469 469 LEU LEU A . n 
A 1 329 ALA 329 470 470 ALA ALA A . n 
A 1 330 ALA 330 471 471 ALA ALA A . n 
A 1 331 ILE 331 472 472 ILE ILE A . n 
A 1 332 PRO 332 473 473 PRO PRO A . n 
A 1 333 GLY 333 474 474 GLY GLY A . n 
A 1 334 VAL 334 475 475 VAL VAL A . n 
A 1 335 ARG 335 476 476 ARG ARG A . n 
A 1 336 ILE 336 477 477 ILE ILE A . n 
A 1 337 VAL 337 478 478 VAL VAL A . n 
A 1 338 GLY 338 479 479 GLY GLY A . n 
A 1 339 THR 339 480 480 THR THR A . n 
A 1 340 ALA 340 481 481 ALA ALA A . n 
A 1 341 GLN 341 482 482 GLN GLN A . n 
A 1 342 GLU 342 483 483 GLU GLU A . n 
A 1 343 LYS 343 484 484 LYS LYS A . n 
A 1 344 ALA 344 485 485 ALA ALA A . n 
A 1 345 SER 345 486 486 SER SER A . n 
A 1 346 VAL 346 487 487 VAL VAL A . n 
A 1 347 LEU 347 488 488 LEU LEU A . n 
A 1 348 SER 348 489 489 SER SER A . n 
A 1 349 PHE 349 490 490 PHE PHE A . n 
A 1 350 VAL 350 491 491 VAL VAL A . n 
A 1 351 LEU 351 492 492 LEU LEU A . n 
A 1 352 ALA 352 493 493 ALA ALA A . n 
A 1 353 GLY 353 494 494 GLY GLY A . n 
A 1 354 HIS 354 495 495 HIS HIS A . n 
A 1 355 GLU 355 496 496 GLU GLU A . n 
A 1 356 PRO 356 497 497 PRO PRO A . n 
A 1 357 LEU 357 498 498 LEU LEU A . n 
A 1 358 GLU 358 499 499 GLU GLU A . n 
A 1 359 VAL 359 500 500 VAL VAL A . n 
A 1 360 GLY 360 501 501 GLY GLY A . n 
A 1 361 LYS 361 502 502 LYS LYS A . n 
A 1 362 ALA 362 503 503 ALA ALA A . n 
A 1 363 LEU 363 504 504 LEU LEU A . n 
A 1 364 ASN 364 505 505 ASN ASN A . n 
A 1 365 ALA 365 506 506 ALA ALA A . n 
A 1 366 GLU 366 507 507 GLU GLU A . n 
A 1 367 GLY 367 508 508 GLY GLY A . n 
A 1 368 ILE 368 509 509 ILE ILE A . n 
A 1 369 ALA 369 510 510 ALA ALA A . n 
A 1 370 VAL 370 511 511 VAL VAL A . n 
A 1 371 ARG 371 512 512 ARG ARG A . n 
A 1 372 ALA 372 513 513 ALA ALA A . n 
A 1 373 GLY 373 514 514 GLY GLY A . n 
A 1 374 HIS 374 515 515 HIS HIS A . n 
A 1 375 HIS 375 516 516 HIS HIS A . n 
A 1 376 CYS 376 517 517 CYS CYS A . n 
A 1 377 ALA 377 518 518 ALA ALA A . n 
A 1 378 GLN 378 519 519 GLN GLN A . n 
A 1 379 PRO 379 520 520 PRO PRO A . n 
A 1 380 ILE 380 521 521 ILE ILE A . n 
A 1 381 LEU 381 522 522 LEU LEU A . n 
A 1 382 ARG 382 523 523 ARG ARG A . n 
A 1 383 ARG 383 524 524 ARG ARG A . n 
A 1 384 MET 384 525 525 MET MET A . n 
A 1 385 GLY 385 526 526 GLY GLY A . n 
A 1 386 LEU 386 527 527 LEU LEU A . n 
A 1 387 GLU 387 528 528 GLU GLU A . n 
A 1 388 ALA 388 529 529 ALA ALA A . n 
A 1 389 THR 389 530 530 THR THR A . n 
A 1 390 VAL 390 531 531 VAL VAL A . n 
A 1 391 ARG 391 532 532 ARG ARG A . n 
A 1 392 PRO 392 533 533 PRO PRO A . n 
A 1 393 SER 393 534 534 SER SER A . n 
A 1 394 PHE 394 535 535 PHE PHE A . n 
A 1 395 ALA 395 536 536 ALA ALA A . n 
A 1 396 PHE 396 537 537 PHE PHE A . n 
A 1 397 TYR 397 538 538 TYR TYR A . n 
A 1 398 ASN 398 539 539 ASN ASN A . n 
A 1 399 THR 399 540 540 THR THR A . n 
A 1 400 PHE 400 541 541 PHE PHE A . n 
A 1 401 ASP 401 542 542 ASP ASP A . n 
A 1 402 GLU 402 543 543 GLU GLU A . n 
A 1 403 ILE 403 544 544 ILE ILE A . n 
A 1 404 ASP 404 545 545 ASP ASP A . n 
A 1 405 VAL 405 546 546 VAL VAL A . n 
A 1 406 PHE 406 547 547 PHE PHE A . n 
A 1 407 ILE 407 548 548 ILE ILE A . n 
A 1 408 ASP 408 549 549 ASP ASP A . n 
A 1 409 ALA 409 550 550 ALA ALA A . n 
A 1 410 VAL 410 551 551 VAL VAL A . n 
A 1 411 ARG 411 552 552 ARG ARG A . n 
A 1 412 ARG 412 553 553 ARG ARG A . n 
A 1 413 ILE 413 554 554 ILE ILE A . n 
A 1 414 ALA 414 555 555 ALA ALA A . n 
A 1 415 GLU 415 556 556 GLU GLU A . n 
A 1 416 GLY 416 557 ?   ?   ?   A . n 
A 1 417 SER 417 558 ?   ?   ?   A . n 
A 1 418 VAL 418 559 ?   ?   ?   A . n 
A 1 419 ASP 419 560 ?   ?   ?   A . n 
A 1 420 TYR 420 561 ?   ?   ?   A . n 
A 1 421 LYS 421 562 ?   ?   ?   A . n 
A 1 422 ASP 422 563 ?   ?   ?   A . n 
A 1 423 ASP 423 564 ?   ?   ?   A . n 
A 1 424 ASP 424 565 ?   ?   ?   A . n 
A 1 425 ASP 425 566 ?   ?   ?   A . n 
A 1 426 LYS 426 567 ?   ?   ?   A . n 
B 1 1   ALA 1   142 ?   ?   ?   B . n 
B 1 2   HIS 2   143 ?   ?   ?   B . n 
B 1 3   GLN 3   144 ?   ?   ?   B . n 
B 1 4   PRO 4   145 ?   ?   ?   B . n 
B 1 5   VAL 5   146 ?   ?   ?   B . n 
B 1 6   PRO 6   147 ?   ?   ?   B . n 
B 1 7   GLN 7   148 ?   ?   ?   B . n 
B 1 8   PHE 8   149 ?   ?   ?   B . n 
B 1 9   PRO 9   150 ?   ?   ?   B . n 
B 1 10  ASP 10  151 ?   ?   ?   B . n 
B 1 11  ARG 11  152 ?   ?   ?   B . n 
B 1 12  HIS 12  153 ?   ?   ?   B . n 
B 1 13  GLU 13  154 ?   ?   ?   B . n 
B 1 14  ILE 14  155 ?   ?   ?   B . n 
B 1 15  PHE 15  156 156 PHE PHE B . n 
B 1 16  ASP 16  157 157 ASP ASP B . n 
B 1 17  VAL 17  158 158 VAL VAL B . n 
B 1 18  ASN 18  159 159 ASN ASN B . n 
B 1 19  ALA 19  160 160 ALA ALA B . n 
B 1 20  ILE 20  161 161 ILE ILE B . n 
B 1 21  ARG 21  162 162 ARG ARG B . n 
B 1 22  ALA 22  163 163 ALA ALA B . n 
B 1 23  ASP 23  164 164 ASP ASP B . n 
B 1 24  PHE 24  165 165 PHE PHE B . n 
B 1 25  PRO 25  166 166 PRO PRO B . n 
B 1 26  ILE 26  167 167 ILE ILE B . n 
B 1 27  LEU 27  168 168 LEU LEU B . n 
B 1 28  ARG 28  169 169 ARG ARG B . n 
B 1 29  GLU 29  170 170 GLU GLU B . n 
B 1 30  THR 30  171 171 THR THR B . n 
B 1 31  VAL 31  172 172 VAL VAL B . n 
B 1 32  ASN 32  173 173 ASN ASN B . n 
B 1 33  GLY 33  174 174 GLY GLY B . n 
B 1 34  LYS 34  175 175 LYS LYS B . n 
B 1 35  PRO 35  176 176 PRO PRO B . n 
B 1 36  LEU 36  177 177 LEU LEU B . n 
B 1 37  ILE 37  178 178 ILE ILE B . n 
B 1 38  TRP 38  179 179 TRP TRP B . n 
B 1 39  PHE 39  180 180 PHE PHE B . n 
B 1 40  ASP 40  181 181 ASP ASP B . n 
B 1 41  ASN 41  182 182 ASN ASN B . n 
B 1 42  ALA 42  183 183 ALA ALA B . n 
B 1 43  ALA 43  184 184 ALA ALA B . n 
B 1 44  THR 44  185 185 THR THR B . n 
B 1 45  THR 45  186 186 THR THR B . n 
B 1 46  GLN 46  187 187 GLN GLN B . n 
B 1 47  LYS 47  188 188 LYS LYS B . n 
B 1 48  PRO 48  189 189 PRO PRO B . n 
B 1 49  GLN 49  190 190 GLN GLN B . n 
B 1 50  ALA 50  191 191 ALA ALA B . n 
B 1 51  VAL 51  192 192 VAL VAL B . n 
B 1 52  ILE 52  193 193 ILE ILE B . n 
B 1 53  ASP 53  194 194 ASP ASP B . n 
B 1 54  ARG 54  195 195 ARG ARG B . n 
B 1 55  LEU 55  196 196 LEU LEU B . n 
B 1 56  SER 56  197 197 SER SER B . n 
B 1 57  HIS 57  198 198 HIS HIS B . n 
B 1 58  PHE 58  199 199 PHE PHE B . n 
B 1 59  TYR 59  200 200 TYR TYR B . n 
B 1 60  ALA 60  201 201 ALA ALA B . n 
B 1 61  HIS 61  202 202 HIS HIS B . n 
B 1 62  GLU 62  203 203 GLU GLU B . n 
B 1 63  ASN 63  204 204 ASN ASN B . n 
B 1 64  SER 64  205 205 SER SER B . n 
B 1 65  ASN 65  206 206 ASN ASN B . n 
B 1 66  ILE 66  207 207 ILE ILE B . n 
B 1 67  HIS 67  208 208 HIS HIS B . n 
B 1 68  ARG 68  209 209 ARG ARG B . n 
B 1 69  ALA 69  210 210 ALA ALA B . n 
B 1 70  ALA 70  211 211 ALA ALA B . n 
B 1 71  HIS 71  212 212 HIS HIS B . n 
B 1 72  GLU 72  213 213 GLU GLU B . n 
B 1 73  LEU 73  214 214 LEU LEU B . n 
B 1 74  ALA 74  215 215 ALA ALA B . n 
B 1 75  ALA 75  216 216 ALA ALA B . n 
B 1 76  ARG 76  217 217 ARG ARG B . n 
B 1 77  ALA 77  218 218 ALA ALA B . n 
B 1 78  THR 78  219 219 THR THR B . n 
B 1 79  ASP 79  220 220 ASP ASP B . n 
B 1 80  ALA 80  221 221 ALA ALA B . n 
B 1 81  TYR 81  222 222 TYR TYR B . n 
B 1 82  GLU 82  223 223 GLU GLU B . n 
B 1 83  ASP 83  224 224 ASP ASP B . n 
B 1 84  ALA 84  225 225 ALA ALA B . n 
B 1 85  ARG 85  226 226 ARG ARG B . n 
B 1 86  GLU 86  227 227 GLU GLU B . n 
B 1 87  ALA 87  228 228 ALA ALA B . n 
B 1 88  VAL 88  229 229 VAL VAL B . n 
B 1 89  ARG 89  230 230 ARG ARG B . n 
B 1 90  ARG 90  231 231 ARG ARG B . n 
B 1 91  PHE 91  232 232 PHE PHE B . n 
B 1 92  ILE 92  233 233 ILE ILE B . n 
B 1 93  GLY 93  234 234 GLY GLY B . n 
B 1 94  ALA 94  235 235 ALA ALA B . n 
B 1 95  ALA 95  236 236 ALA ALA B . n 
B 1 96  LYS 96  237 237 LYS LYS B . n 
B 1 97  ALA 97  238 238 ALA ALA B . n 
B 1 98  GLU 98  239 239 GLU GLU B . n 
B 1 99  GLU 99  240 240 GLU GLU B . n 
B 1 100 ILE 100 241 241 ILE ILE B . n 
B 1 101 ILE 101 242 242 ILE ILE B . n 
B 1 102 PHE 102 243 243 PHE PHE B . n 
B 1 103 LEU 103 244 244 LEU LEU B . n 
B 1 104 ARG 104 245 245 ARG ARG B . n 
B 1 105 GLY 105 246 246 GLY GLY B . n 
B 1 106 THR 106 247 247 THR THR B . n 
B 1 107 THR 107 248 248 THR THR B . n 
B 1 108 GLU 108 249 249 GLU GLU B . n 
B 1 109 ALA 109 250 250 ALA ALA B . n 
B 1 110 ILE 110 251 251 ILE ILE B . n 
B 1 111 ASN 111 252 252 ASN ASN B . n 
B 1 112 LEU 112 253 253 LEU LEU B . n 
B 1 113 VAL 113 254 254 VAL VAL B . n 
B 1 114 ALA 114 255 255 ALA ALA B . n 
B 1 115 HIS 115 256 256 HIS HIS B . n 
B 1 116 ALA 116 257 257 ALA ALA B . n 
B 1 117 TRP 117 258 258 TRP TRP B . n 
B 1 118 GLY 118 259 259 GLY GLY B . n 
B 1 119 GLY 119 260 260 GLY GLY B . n 
B 1 120 LYS 120 261 261 LYS LYS B . n 
B 1 121 HIS 121 262 262 HIS HIS B . n 
B 1 122 LEU 122 263 263 LEU LEU B . n 
B 1 123 GLY 123 264 264 GLY GLY B . n 
B 1 124 PRO 124 265 265 PRO PRO B . n 
B 1 125 GLY 125 266 266 GLY GLY B . n 
B 1 126 ASP 126 267 267 ASP ASP B . n 
B 1 127 GLU 127 268 268 GLU GLU B . n 
B 1 128 ILE 128 269 269 ILE ILE B . n 
B 1 129 VAL 129 270 270 VAL VAL B . n 
B 1 130 ILE 130 271 271 ILE ILE B . n 
B 1 131 THR 131 272 272 THR THR B . n 
B 1 132 HIS 132 273 273 HIS HIS B . n 
B 1 133 LEU 133 274 274 LEU LEU B . n 
B 1 134 GLU 134 275 275 GLU GLU B . n 
B 1 135 HIS 135 276 276 HIS HIS B . n 
B 1 136 HIS 136 277 277 HIS HIS B . n 
B 1 137 ALA 137 278 278 ALA ALA B . n 
B 1 138 ASN 138 279 279 ASN ASN B . n 
B 1 139 ILE 139 280 280 ILE ILE B . n 
B 1 140 VAL 140 281 281 VAL VAL B . n 
B 1 141 PRO 141 282 282 PRO PRO B . n 
B 1 142 TRP 142 283 283 TRP TRP B . n 
B 1 143 GLN 143 284 284 GLN GLN B . n 
B 1 144 LEU 144 285 285 LEU LEU B . n 
B 1 145 LEU 145 286 286 LEU LEU B . n 
B 1 146 SER 146 287 287 SER SER B . n 
B 1 147 ARG 147 288 288 ARG ARG B . n 
B 1 148 GLN 148 289 289 GLN GLN B . n 
B 1 149 THR 149 290 290 THR THR B . n 
B 1 150 GLY 150 291 291 GLY GLY B . n 
B 1 151 ALA 151 292 292 ALA ALA B . n 
B 1 152 VAL 152 293 293 VAL VAL B . n 
B 1 153 LEU 153 294 294 LEU LEU B . n 
B 1 154 LYS 154 295 295 LYS LYS B . n 
B 1 155 VAL 155 296 296 VAL VAL B . n 
B 1 156 ALA 156 297 297 ALA ALA B . n 
B 1 157 PRO 157 298 298 PRO PRO B . n 
B 1 158 VAL 158 299 299 VAL VAL B . n 
B 1 159 ASP 159 300 300 ASP ASP B . n 
B 1 160 ASP 160 301 301 ASP ASP B . n 
B 1 161 ALA 161 302 302 ALA ALA B . n 
B 1 162 GLY 162 303 303 GLY GLY B . n 
B 1 163 ASN 163 304 304 ASN ASN B . n 
B 1 164 LEU 164 305 305 LEU LEU B . n 
B 1 165 LEU 165 306 306 LEU LEU B . n 
B 1 166 LEU 166 307 307 LEU LEU B . n 
B 1 167 GLY 167 308 308 GLY GLY B . n 
B 1 168 GLU 168 309 309 GLU GLU B . n 
B 1 169 PHE 169 310 310 PHE PHE B . n 
B 1 170 GLU 170 311 311 GLU GLU B . n 
B 1 171 ASP 171 312 312 ASP ASP B . n 
B 1 172 LEU 172 313 313 LEU LEU B . n 
B 1 173 LEU 173 314 314 LEU LEU B . n 
B 1 174 GLY 174 315 315 GLY GLY B . n 
B 1 175 PRO 175 316 316 PRO PRO B . n 
B 1 176 ARG 176 317 317 ARG ARG B . n 
B 1 177 THR 177 318 318 THR THR B . n 
B 1 178 LYS 178 319 319 LYS LYS B . n 
B 1 179 LEU 179 320 320 LEU LEU B . n 
B 1 180 VAL 180 321 321 VAL VAL B . n 
B 1 181 ALA 181 322 322 ALA ALA B . n 
B 1 182 ALA 182 323 323 ALA ALA B . n 
B 1 183 THR 183 324 324 THR THR B . n 
B 1 184 GLN 184 325 325 GLN GLN B . n 
B 1 185 VAL 185 326 326 VAL VAL B . n 
B 1 186 SER 186 327 327 SER SER B . n 
B 1 187 ASN 187 328 328 ASN ASN B . n 
B 1 188 ALA 188 329 329 ALA ALA B . n 
B 1 189 LEU 189 330 330 LEU LEU B . n 
B 1 190 GLY 190 331 331 GLY GLY B . n 
B 1 191 THR 191 332 332 THR THR B . n 
B 1 192 VAL 192 333 333 VAL VAL B . n 
B 1 193 THR 193 334 334 THR THR B . n 
B 1 194 PRO 194 335 335 PRO PRO B . n 
B 1 195 VAL 195 336 336 VAL VAL B . n 
B 1 196 GLU 196 337 337 GLU GLU B . n 
B 1 197 THR 197 338 338 THR THR B . n 
B 1 198 ILE 198 339 339 ILE ILE B . n 
B 1 199 VAL 199 340 340 VAL VAL B . n 
B 1 200 GLU 200 341 341 GLU GLU B . n 
B 1 201 LEU 201 342 342 LEU LEU B . n 
B 1 202 GLY 202 343 343 GLY GLY B . n 
B 1 203 HIS 203 344 344 HIS HIS B . n 
B 1 204 ARG 204 345 345 ARG ARG B . n 
B 1 205 TYR 205 346 346 TYR TYR B . n 
B 1 206 GLY 206 347 347 GLY GLY B . n 
B 1 207 ALA 207 348 348 ALA ALA B . n 
B 1 208 ARG 208 349 349 ARG ARG B . n 
B 1 209 VAL 209 350 350 VAL VAL B . n 
B 1 210 LEU 210 351 351 LEU LEU B . n 
B 1 211 ILE 211 352 352 ILE ILE B . n 
B 1 212 ASP 212 353 353 ASP ASP B . n 
B 1 213 GLY 213 354 354 GLY GLY B . n 
B 1 214 ALA 214 355 355 ALA ALA B . n 
B 1 215 GLN 215 356 356 GLN GLN B . n 
B 1 216 SER 216 357 357 SER SER B . n 
B 1 217 ILE 217 358 358 ILE ILE B . n 
B 1 218 PRO 218 359 359 PRO PRO B . n 
B 1 219 HIS 219 360 360 HIS HIS B . n 
B 1 220 MET 220 361 361 MET MET B . n 
B 1 221 PRO 221 362 362 PRO PRO B . n 
B 1 222 ILE 222 363 363 ILE ILE B . n 
B 1 223 ASP 223 364 364 ASP ASP B . n 
B 1 224 VAL 224 365 365 VAL VAL B . n 
B 1 225 ALA 225 366 366 ALA ALA B . n 
B 1 226 ALA 226 367 367 ALA ALA B . n 
B 1 227 LEU 227 368 368 LEU LEU B . n 
B 1 228 GLY 228 369 369 GLY GLY B . n 
B 1 229 ALA 229 370 370 ALA ALA B . n 
B 1 230 ASP 230 371 371 ASP ASP B . n 
B 1 231 PHE 231 372 372 PHE PHE B . n 
B 1 232 PHE 232 373 373 PHE PHE B . n 
B 1 233 VAL 233 374 374 VAL VAL B . n 
B 1 234 PHE 234 375 375 PHE PHE B . n 
B 1 235 SER 235 376 376 SER SER B . n 
B 1 236 GLY 236 377 377 GLY GLY B . n 
B 1 237 HIS 237 378 378 HIS HIS B . n 
B 1 238 LLP 238 379 379 LLP LLP B . n 
B 1 239 ILE 239 380 380 ILE ILE B . n 
B 1 240 TYR 240 381 381 TYR TYR B . n 
B 1 241 GLY 241 382 382 GLY GLY B . n 
B 1 242 PRO 242 383 383 PRO PRO B . n 
B 1 243 THR 243 384 384 THR THR B . n 
B 1 244 GLY 244 385 385 GLY GLY B . n 
B 1 245 ILE 245 386 386 ILE ILE B . n 
B 1 246 GLY 246 387 387 GLY GLY B . n 
B 1 247 VAL 247 388 388 VAL VAL B . n 
B 1 248 LEU 248 389 389 LEU LEU B . n 
B 1 249 TYR 249 390 390 TYR TYR B . n 
B 1 250 GLY 250 391 391 GLY GLY B . n 
B 1 251 ARG 251 392 392 ARG ARG B . n 
B 1 252 GLU 252 393 393 GLU GLU B . n 
B 1 253 ASP 253 394 394 ASP ASP B . n 
B 1 254 ALA 254 395 395 ALA ALA B . n 
B 1 255 LEU 255 396 396 LEU LEU B . n 
B 1 256 ALA 256 397 397 ALA ALA B . n 
B 1 257 GLU 257 398 398 GLU GLU B . n 
B 1 258 THR 258 399 399 THR THR B . n 
B 1 259 PRO 259 400 400 PRO PRO B . n 
B 1 260 PRO 260 401 401 PRO PRO B . n 
B 1 261 TRP 261 402 402 TRP TRP B . n 
B 1 262 GLN 262 403 403 GLN GLN B . n 
B 1 263 GLY 263 404 404 GLY GLY B . n 
B 1 264 GLY 264 405 405 GLY GLY B . n 
B 1 265 GLY 265 406 406 GLY GLY B . n 
B 1 266 ASN 266 407 407 ASN ASN B . n 
B 1 267 MET 267 408 408 MET MET B . n 
B 1 268 ILE 268 409 409 ILE ILE B . n 
B 1 269 ALA 269 410 410 ALA ALA B . n 
B 1 270 ASP 270 411 411 ASP ASP B . n 
B 1 271 VAL 271 412 412 VAL VAL B . n 
B 1 272 THR 272 413 413 THR THR B . n 
B 1 273 LEU 273 414 414 LEU LEU B . n 
B 1 274 GLU 274 415 415 GLU GLU B . n 
B 1 275 ARG 275 416 416 ARG ARG B . n 
B 1 276 SER 276 417 417 SER SER B . n 
B 1 277 LEU 277 418 418 LEU LEU B . n 
B 1 278 TYR 278 419 419 TYR TYR B . n 
B 1 279 GLN 279 420 420 GLN GLN B . n 
B 1 280 GLY 280 421 421 GLY GLY B . n 
B 1 281 PRO 281 422 422 PRO PRO B . n 
B 1 282 PRO 282 423 423 PRO PRO B . n 
B 1 283 ASN 283 424 424 ASN ASN B . n 
B 1 284 LYS 284 425 425 LYS LYS B . n 
B 1 285 PHE 285 426 426 PHE PHE B . n 
B 1 286 GLU 286 427 427 GLU GLU B . n 
B 1 287 ALA 287 428 428 ALA ALA B . n 
B 1 288 GLY 288 429 429 GLY GLY B . n 
B 1 289 THR 289 430 430 THR THR B . n 
B 1 290 GLY 290 431 431 GLY GLY B . n 
B 1 291 ASN 291 432 432 ASN ASN B . n 
B 1 292 ILE 292 433 433 ILE ILE B . n 
B 1 293 ALA 293 434 434 ALA ALA B . n 
B 1 294 ASP 294 435 435 ASP ASP B . n 
B 1 295 ALA 295 436 436 ALA ALA B . n 
B 1 296 VAL 296 437 437 VAL VAL B . n 
B 1 297 GLY 297 438 438 GLY GLY B . n 
B 1 298 LEU 298 439 439 LEU LEU B . n 
B 1 299 GLY 299 440 440 GLY GLY B . n 
B 1 300 GLU 300 441 441 GLU GLU B . n 
B 1 301 ALA 301 442 442 ALA ALA B . n 
B 1 302 ILE 302 443 443 ILE ILE B . n 
B 1 303 ARG 303 444 444 ARG ARG B . n 
B 1 304 TYR 304 445 445 TYR TYR B . n 
B 1 305 VAL 305 446 446 VAL VAL B . n 
B 1 306 GLU 306 447 447 GLU GLU B . n 
B 1 307 ARG 307 448 448 ARG ARG B . n 
B 1 308 VAL 308 449 449 VAL VAL B . n 
B 1 309 GLY 309 450 450 GLY GLY B . n 
B 1 310 ILE 310 451 451 ILE ILE B . n 
B 1 311 GLU 311 452 452 GLU GLU B . n 
B 1 312 ARG 312 453 453 ARG ARG B . n 
B 1 313 ILE 313 454 454 ILE ILE B . n 
B 1 314 ALA 314 455 455 ALA ALA B . n 
B 1 315 ALA 315 456 456 ALA ALA B . n 
B 1 316 TYR 316 457 457 TYR TYR B . n 
B 1 317 GLU 317 458 458 GLU GLU B . n 
B 1 318 HIS 318 459 459 HIS HIS B . n 
B 1 319 ALA 319 460 460 ALA ALA B . n 
B 1 320 LEU 320 461 461 LEU LEU B . n 
B 1 321 LEU 321 462 462 LEU LEU B . n 
B 1 322 GLU 322 463 463 GLU GLU B . n 
B 1 323 TYR 323 464 464 TYR TYR B . n 
B 1 324 ALA 324 465 465 ALA ALA B . n 
B 1 325 THR 325 466 466 THR THR B . n 
B 1 326 PRO 326 467 467 PRO PRO B . n 
B 1 327 ARG 327 468 468 ARG ARG B . n 
B 1 328 LEU 328 469 469 LEU LEU B . n 
B 1 329 ALA 329 470 470 ALA ALA B . n 
B 1 330 ALA 330 471 471 ALA ALA B . n 
B 1 331 ILE 331 472 472 ILE ILE B . n 
B 1 332 PRO 332 473 473 PRO PRO B . n 
B 1 333 GLY 333 474 474 GLY GLY B . n 
B 1 334 VAL 334 475 475 VAL VAL B . n 
B 1 335 ARG 335 476 476 ARG ARG B . n 
B 1 336 ILE 336 477 477 ILE ILE B . n 
B 1 337 VAL 337 478 478 VAL VAL B . n 
B 1 338 GLY 338 479 479 GLY GLY B . n 
B 1 339 THR 339 480 480 THR THR B . n 
B 1 340 ALA 340 481 481 ALA ALA B . n 
B 1 341 GLN 341 482 482 GLN GLN B . n 
B 1 342 GLU 342 483 483 GLU GLU B . n 
B 1 343 LYS 343 484 484 LYS LYS B . n 
B 1 344 ALA 344 485 485 ALA ALA B . n 
B 1 345 SER 345 486 486 SER SER B . n 
B 1 346 VAL 346 487 487 VAL VAL B . n 
B 1 347 LEU 347 488 488 LEU LEU B . n 
B 1 348 SER 348 489 489 SER SER B . n 
B 1 349 PHE 349 490 490 PHE PHE B . n 
B 1 350 VAL 350 491 491 VAL VAL B . n 
B 1 351 LEU 351 492 492 LEU LEU B . n 
B 1 352 ALA 352 493 493 ALA ALA B . n 
B 1 353 GLY 353 494 494 GLY GLY B . n 
B 1 354 HIS 354 495 495 HIS HIS B . n 
B 1 355 GLU 355 496 496 GLU GLU B . n 
B 1 356 PRO 356 497 497 PRO PRO B . n 
B 1 357 LEU 357 498 498 LEU LEU B . n 
B 1 358 GLU 358 499 499 GLU GLU B . n 
B 1 359 VAL 359 500 500 VAL VAL B . n 
B 1 360 GLY 360 501 501 GLY GLY B . n 
B 1 361 LYS 361 502 502 LYS LYS B . n 
B 1 362 ALA 362 503 503 ALA ALA B . n 
B 1 363 LEU 363 504 504 LEU LEU B . n 
B 1 364 ASN 364 505 505 ASN ASN B . n 
B 1 365 ALA 365 506 506 ALA ALA B . n 
B 1 366 GLU 366 507 507 GLU GLU B . n 
B 1 367 GLY 367 508 508 GLY GLY B . n 
B 1 368 ILE 368 509 509 ILE ILE B . n 
B 1 369 ALA 369 510 510 ALA ALA B . n 
B 1 370 VAL 370 511 511 VAL VAL B . n 
B 1 371 ARG 371 512 512 ARG ARG B . n 
B 1 372 ALA 372 513 513 ALA ALA B . n 
B 1 373 GLY 373 514 514 GLY GLY B . n 
B 1 374 HIS 374 515 515 HIS HIS B . n 
B 1 375 HIS 375 516 516 HIS HIS B . n 
B 1 376 CYS 376 517 517 CYS CYS B . n 
B 1 377 ALA 377 518 518 ALA ALA B . n 
B 1 378 GLN 378 519 519 GLN GLN B . n 
B 1 379 PRO 379 520 520 PRO PRO B . n 
B 1 380 ILE 380 521 521 ILE ILE B . n 
B 1 381 LEU 381 522 522 LEU LEU B . n 
B 1 382 ARG 382 523 523 ARG ARG B . n 
B 1 383 ARG 383 524 524 ARG ARG B . n 
B 1 384 MET 384 525 525 MET MET B . n 
B 1 385 GLY 385 526 526 GLY GLY B . n 
B 1 386 LEU 386 527 527 LEU LEU B . n 
B 1 387 GLU 387 528 528 GLU GLU B . n 
B 1 388 ALA 388 529 529 ALA ALA B . n 
B 1 389 THR 389 530 530 THR THR B . n 
B 1 390 VAL 390 531 531 VAL VAL B . n 
B 1 391 ARG 391 532 532 ARG ARG B . n 
B 1 392 PRO 392 533 533 PRO PRO B . n 
B 1 393 SER 393 534 534 SER SER B . n 
B 1 394 PHE 394 535 535 PHE PHE B . n 
B 1 395 ALA 395 536 536 ALA ALA B . n 
B 1 396 PHE 396 537 537 PHE PHE B . n 
B 1 397 TYR 397 538 538 TYR TYR B . n 
B 1 398 ASN 398 539 539 ASN ASN B . n 
B 1 399 THR 399 540 540 THR THR B . n 
B 1 400 PHE 400 541 541 PHE PHE B . n 
B 1 401 ASP 401 542 542 ASP ASP B . n 
B 1 402 GLU 402 543 543 GLU GLU B . n 
B 1 403 ILE 403 544 544 ILE ILE B . n 
B 1 404 ASP 404 545 545 ASP ASP B . n 
B 1 405 VAL 405 546 546 VAL VAL B . n 
B 1 406 PHE 406 547 547 PHE PHE B . n 
B 1 407 ILE 407 548 548 ILE ILE B . n 
B 1 408 ASP 408 549 549 ASP ASP B . n 
B 1 409 ALA 409 550 550 ALA ALA B . n 
B 1 410 VAL 410 551 551 VAL VAL B . n 
B 1 411 ARG 411 552 552 ARG ARG B . n 
B 1 412 ARG 412 553 553 ARG ARG B . n 
B 1 413 ILE 413 554 554 ILE ILE B . n 
B 1 414 ALA 414 555 555 ALA ALA B . n 
B 1 415 GLU 415 556 556 GLU GLU B . n 
B 1 416 GLY 416 557 557 GLY GLY B . n 
B 1 417 SER 417 558 558 SER SER B . n 
B 1 418 VAL 418 559 559 VAL VAL B . n 
B 1 419 ASP 419 560 560 ASP ASP B . n 
B 1 420 TYR 420 561 ?   ?   ?   B . n 
B 1 421 LYS 421 562 ?   ?   ?   B . n 
B 1 422 ASP 422 563 ?   ?   ?   B . n 
B 1 423 ASP 423 564 ?   ?   ?   B . n 
B 1 424 ASP 424 565 ?   ?   ?   B . n 
B 1 425 ASP 425 566 ?   ?   ?   B . n 
B 1 426 LYS 426 567 ?   ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        LLP 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   LLP 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 HOH 1   601 395 HOH HOH A . 
C 2 HOH 2   602 537 HOH HOH A . 
C 2 HOH 3   603 48  HOH HOH A . 
C 2 HOH 4   604 171 HOH HOH A . 
C 2 HOH 5   605 145 HOH HOH A . 
C 2 HOH 6   606 191 HOH HOH A . 
C 2 HOH 7   607 139 HOH HOH A . 
C 2 HOH 8   608 148 HOH HOH A . 
C 2 HOH 9   609 27  HOH HOH A . 
C 2 HOH 10  610 51  HOH HOH A . 
C 2 HOH 11  611 221 HOH HOH A . 
C 2 HOH 12  612 304 HOH HOH A . 
C 2 HOH 13  613 402 HOH HOH A . 
C 2 HOH 14  614 263 HOH HOH A . 
C 2 HOH 15  615 133 HOH HOH A . 
C 2 HOH 16  616 449 HOH HOH A . 
C 2 HOH 17  617 199 HOH HOH A . 
C 2 HOH 18  618 219 HOH HOH A . 
C 2 HOH 19  619 409 HOH HOH A . 
C 2 HOH 20  620 456 HOH HOH A . 
C 2 HOH 21  621 331 HOH HOH A . 
C 2 HOH 22  622 320 HOH HOH A . 
C 2 HOH 23  623 50  HOH HOH A . 
C 2 HOH 24  624 87  HOH HOH A . 
C 2 HOH 25  625 423 HOH HOH A . 
C 2 HOH 26  626 313 HOH HOH A . 
C 2 HOH 27  627 197 HOH HOH A . 
C 2 HOH 28  628 1   HOH HOH A . 
C 2 HOH 29  629 454 HOH HOH A . 
C 2 HOH 30  630 187 HOH HOH A . 
C 2 HOH 31  631 353 HOH HOH A . 
C 2 HOH 32  632 521 HOH HOH A . 
C 2 HOH 33  633 356 HOH HOH A . 
C 2 HOH 34  634 64  HOH HOH A . 
C 2 HOH 35  635 44  HOH HOH A . 
C 2 HOH 36  636 30  HOH HOH A . 
C 2 HOH 37  637 21  HOH HOH A . 
C 2 HOH 38  638 544 HOH HOH A . 
C 2 HOH 39  639 73  HOH HOH A . 
C 2 HOH 40  640 195 HOH HOH A . 
C 2 HOH 41  641 271 HOH HOH A . 
C 2 HOH 42  642 309 HOH HOH A . 
C 2 HOH 43  643 16  HOH HOH A . 
C 2 HOH 44  644 24  HOH HOH A . 
C 2 HOH 45  645 206 HOH HOH A . 
C 2 HOH 46  646 237 HOH HOH A . 
C 2 HOH 47  647 119 HOH HOH A . 
C 2 HOH 48  648 379 HOH HOH A . 
C 2 HOH 49  649 345 HOH HOH A . 
C 2 HOH 50  650 85  HOH HOH A . 
C 2 HOH 51  651 36  HOH HOH A . 
C 2 HOH 52  652 396 HOH HOH A . 
C 2 HOH 53  653 367 HOH HOH A . 
C 2 HOH 54  654 241 HOH HOH A . 
C 2 HOH 55  655 167 HOH HOH A . 
C 2 HOH 56  656 485 HOH HOH A . 
C 2 HOH 57  657 182 HOH HOH A . 
C 2 HOH 58  658 184 HOH HOH A . 
C 2 HOH 59  659 333 HOH HOH A . 
C 2 HOH 60  660 131 HOH HOH A . 
C 2 HOH 61  661 256 HOH HOH A . 
C 2 HOH 62  662 40  HOH HOH A . 
C 2 HOH 63  663 262 HOH HOH A . 
C 2 HOH 64  664 95  HOH HOH A . 
C 2 HOH 65  665 34  HOH HOH A . 
C 2 HOH 66  666 180 HOH HOH A . 
C 2 HOH 67  667 68  HOH HOH A . 
C 2 HOH 68  668 33  HOH HOH A . 
C 2 HOH 69  669 305 HOH HOH A . 
C 2 HOH 70  670 43  HOH HOH A . 
C 2 HOH 71  671 322 HOH HOH A . 
C 2 HOH 72  672 99  HOH HOH A . 
C 2 HOH 73  673 60  HOH HOH A . 
C 2 HOH 74  674 75  HOH HOH A . 
C 2 HOH 75  675 4   HOH HOH A . 
C 2 HOH 76  676 234 HOH HOH A . 
C 2 HOH 77  677 205 HOH HOH A . 
C 2 HOH 78  678 229 HOH HOH A . 
C 2 HOH 79  679 233 HOH HOH A . 
C 2 HOH 80  680 130 HOH HOH A . 
C 2 HOH 81  681 542 HOH HOH A . 
C 2 HOH 82  682 516 HOH HOH A . 
C 2 HOH 83  683 19  HOH HOH A . 
C 2 HOH 84  684 94  HOH HOH A . 
C 2 HOH 85  685 10  HOH HOH A . 
C 2 HOH 86  686 227 HOH HOH A . 
C 2 HOH 87  687 323 HOH HOH A . 
C 2 HOH 88  688 80  HOH HOH A . 
C 2 HOH 89  689 411 HOH HOH A . 
C 2 HOH 90  690 15  HOH HOH A . 
C 2 HOH 91  691 49  HOH HOH A . 
C 2 HOH 92  692 55  HOH HOH A . 
C 2 HOH 93  693 414 HOH HOH A . 
C 2 HOH 94  694 295 HOH HOH A . 
C 2 HOH 95  695 26  HOH HOH A . 
C 2 HOH 96  696 369 HOH HOH A . 
C 2 HOH 97  697 81  HOH HOH A . 
C 2 HOH 98  698 77  HOH HOH A . 
C 2 HOH 99  699 254 HOH HOH A . 
C 2 HOH 100 700 125 HOH HOH A . 
C 2 HOH 101 701 343 HOH HOH A . 
C 2 HOH 102 702 128 HOH HOH A . 
C 2 HOH 103 703 196 HOH HOH A . 
C 2 HOH 104 704 327 HOH HOH A . 
C 2 HOH 105 705 213 HOH HOH A . 
C 2 HOH 106 706 110 HOH HOH A . 
C 2 HOH 107 707 332 HOH HOH A . 
C 2 HOH 108 708 135 HOH HOH A . 
C 2 HOH 109 709 266 HOH HOH A . 
C 2 HOH 110 710 194 HOH HOH A . 
C 2 HOH 111 711 32  HOH HOH A . 
C 2 HOH 112 712 126 HOH HOH A . 
C 2 HOH 113 713 159 HOH HOH A . 
C 2 HOH 114 714 97  HOH HOH A . 
C 2 HOH 115 715 245 HOH HOH A . 
C 2 HOH 116 716 11  HOH HOH A . 
C 2 HOH 117 717 381 HOH HOH A . 
C 2 HOH 118 718 339 HOH HOH A . 
C 2 HOH 119 719 223 HOH HOH A . 
C 2 HOH 120 720 23  HOH HOH A . 
C 2 HOH 121 721 249 HOH HOH A . 
C 2 HOH 122 722 442 HOH HOH A . 
C 2 HOH 123 723 69  HOH HOH A . 
C 2 HOH 124 724 240 HOH HOH A . 
C 2 HOH 125 725 101 HOH HOH A . 
C 2 HOH 126 726 261 HOH HOH A . 
C 2 HOH 127 727 45  HOH HOH A . 
C 2 HOH 128 728 165 HOH HOH A . 
C 2 HOH 129 729 74  HOH HOH A . 
C 2 HOH 130 730 210 HOH HOH A . 
C 2 HOH 131 731 504 HOH HOH A . 
C 2 HOH 132 732 474 HOH HOH A . 
C 2 HOH 133 733 284 HOH HOH A . 
C 2 HOH 134 734 499 HOH HOH A . 
C 2 HOH 135 735 364 HOH HOH A . 
C 2 HOH 136 736 372 HOH HOH A . 
C 2 HOH 137 737 538 HOH HOH A . 
C 2 HOH 138 738 460 HOH HOH A . 
C 2 HOH 139 739 232 HOH HOH A . 
C 2 HOH 140 740 530 HOH HOH A . 
C 2 HOH 141 741 430 HOH HOH A . 
C 2 HOH 142 742 143 HOH HOH A . 
C 2 HOH 143 743 520 HOH HOH A . 
C 2 HOH 144 744 111 HOH HOH A . 
C 2 HOH 145 745 358 HOH HOH A . 
C 2 HOH 146 746 244 HOH HOH A . 
C 2 HOH 147 747 225 HOH HOH A . 
C 2 HOH 148 748 296 HOH HOH A . 
C 2 HOH 149 749 183 HOH HOH A . 
C 2 HOH 150 750 298 HOH HOH A . 
C 2 HOH 151 751 115 HOH HOH A . 
C 2 HOH 152 752 178 HOH HOH A . 
C 2 HOH 153 753 18  HOH HOH A . 
C 2 HOH 154 754 89  HOH HOH A . 
C 2 HOH 155 755 415 HOH HOH A . 
C 2 HOH 156 756 478 HOH HOH A . 
C 2 HOH 157 757 280 HOH HOH A . 
C 2 HOH 158 758 247 HOH HOH A . 
C 2 HOH 159 759 335 HOH HOH A . 
C 2 HOH 160 760 378 HOH HOH A . 
C 2 HOH 161 761 124 HOH HOH A . 
C 2 HOH 162 762 70  HOH HOH A . 
C 2 HOH 163 763 31  HOH HOH A . 
C 2 HOH 164 764 209 HOH HOH A . 
C 2 HOH 165 765 523 HOH HOH A . 
C 2 HOH 166 766 25  HOH HOH A . 
C 2 HOH 167 767 76  HOH HOH A . 
C 2 HOH 168 768 287 HOH HOH A . 
C 2 HOH 169 769 88  HOH HOH A . 
C 2 HOH 170 770 513 HOH HOH A . 
C 2 HOH 171 771 479 HOH HOH A . 
C 2 HOH 172 772 387 HOH HOH A . 
C 2 HOH 173 773 179 HOH HOH A . 
C 2 HOH 174 774 270 HOH HOH A . 
C 2 HOH 175 775 151 HOH HOH A . 
C 2 HOH 176 776 439 HOH HOH A . 
C 2 HOH 177 777 170 HOH HOH A . 
C 2 HOH 178 778 120 HOH HOH A . 
C 2 HOH 179 779 158 HOH HOH A . 
C 2 HOH 180 780 267 HOH HOH A . 
C 2 HOH 181 781 273 HOH HOH A . 
C 2 HOH 182 782 117 HOH HOH A . 
C 2 HOH 183 783 236 HOH HOH A . 
C 2 HOH 184 784 384 HOH HOH A . 
C 2 HOH 185 785 207 HOH HOH A . 
C 2 HOH 186 786 61  HOH HOH A . 
C 2 HOH 187 787 464 HOH HOH A . 
C 2 HOH 188 788 260 HOH HOH A . 
C 2 HOH 189 789 8   HOH HOH A . 
C 2 HOH 190 790 445 HOH HOH A . 
C 2 HOH 191 791 173 HOH HOH A . 
C 2 HOH 192 792 368 HOH HOH A . 
C 2 HOH 193 793 349 HOH HOH A . 
C 2 HOH 194 794 533 HOH HOH A . 
C 2 HOH 195 795 318 HOH HOH A . 
C 2 HOH 196 796 427 HOH HOH A . 
C 2 HOH 197 797 374 HOH HOH A . 
C 2 HOH 198 798 28  HOH HOH A . 
C 2 HOH 199 799 109 HOH HOH A . 
C 2 HOH 200 800 231 HOH HOH A . 
C 2 HOH 201 801 238 HOH HOH A . 
C 2 HOH 202 802 294 HOH HOH A . 
C 2 HOH 203 803 312 HOH HOH A . 
C 2 HOH 204 804 519 HOH HOH A . 
C 2 HOH 205 805 129 HOH HOH A . 
C 2 HOH 206 806 543 HOH HOH A . 
C 2 HOH 207 807 228 HOH HOH A . 
C 2 HOH 208 808 156 HOH HOH A . 
C 2 HOH 209 809 502 HOH HOH A . 
C 2 HOH 210 810 377 HOH HOH A . 
C 2 HOH 211 811 457 HOH HOH A . 
C 2 HOH 212 812 176 HOH HOH A . 
C 2 HOH 213 813 477 HOH HOH A . 
C 2 HOH 214 814 259 HOH HOH A . 
C 2 HOH 215 815 507 HOH HOH A . 
C 2 HOH 216 816 127 HOH HOH A . 
C 2 HOH 217 817 461 HOH HOH A . 
C 2 HOH 218 818 489 HOH HOH A . 
C 2 HOH 219 819 2   HOH HOH A . 
C 2 HOH 220 820 410 HOH HOH A . 
C 2 HOH 221 821 175 HOH HOH A . 
C 2 HOH 222 822 416 HOH HOH A . 
C 2 HOH 223 823 174 HOH HOH A . 
C 2 HOH 224 824 448 HOH HOH A . 
C 2 HOH 225 825 319 HOH HOH A . 
C 2 HOH 226 826 336 HOH HOH A . 
C 2 HOH 227 827 107 HOH HOH A . 
C 2 HOH 228 828 306 HOH HOH A . 
C 2 HOH 229 829 465 HOH HOH A . 
C 2 HOH 230 830 500 HOH HOH A . 
C 2 HOH 231 831 509 HOH HOH A . 
C 2 HOH 232 832 469 HOH HOH A . 
C 2 HOH 233 833 153 HOH HOH A . 
C 2 HOH 234 834 272 HOH HOH A . 
C 2 HOH 235 835 286 HOH HOH A . 
C 2 HOH 236 836 355 HOH HOH A . 
C 2 HOH 237 837 505 HOH HOH A . 
C 2 HOH 238 838 359 HOH HOH A . 
C 2 HOH 239 839 541 HOH HOH A . 
C 2 HOH 240 840 269 HOH HOH A . 
C 2 HOH 241 841 324 HOH HOH A . 
C 2 HOH 242 842 470 HOH HOH A . 
C 2 HOH 243 843 433 HOH HOH A . 
C 2 HOH 244 844 144 HOH HOH A . 
C 2 HOH 245 845 123 HOH HOH A . 
C 2 HOH 246 846 453 HOH HOH A . 
C 2 HOH 247 847 201 HOH HOH A . 
C 2 HOH 248 848 428 HOH HOH A . 
C 2 HOH 249 849 390 HOH HOH A . 
C 2 HOH 250 850 235 HOH HOH A . 
C 2 HOH 251 851 293 HOH HOH A . 
C 2 HOH 252 852 540 HOH HOH A . 
C 2 HOH 253 853 466 HOH HOH A . 
C 2 HOH 254 854 518 HOH HOH A . 
C 2 HOH 255 855 480 HOH HOH A . 
C 2 HOH 256 856 437 HOH HOH A . 
C 2 HOH 257 857 283 HOH HOH A . 
C 2 HOH 258 858 403 HOH HOH A . 
C 2 HOH 259 859 506 HOH HOH A . 
C 2 HOH 260 860 307 HOH HOH A . 
C 2 HOH 261 861 347 HOH HOH A . 
C 2 HOH 262 862 363 HOH HOH A . 
C 2 HOH 263 863 527 HOH HOH A . 
C 2 HOH 264 864 391 HOH HOH A . 
C 2 HOH 265 865 216 HOH HOH A . 
C 2 HOH 266 866 142 HOH HOH A . 
C 2 HOH 267 867 393 HOH HOH A . 
C 2 HOH 268 868 121 HOH HOH A . 
C 2 HOH 269 869 385 HOH HOH A . 
C 2 HOH 270 870 471 HOH HOH A . 
C 2 HOH 271 871 276 HOH HOH A . 
C 2 HOH 272 872 257 HOH HOH A . 
C 2 HOH 273 873 152 HOH HOH A . 
C 2 HOH 274 874 438 HOH HOH A . 
C 2 HOH 275 875 310 HOH HOH A . 
C 2 HOH 276 876 285 HOH HOH A . 
C 2 HOH 277 877 532 HOH HOH A . 
C 2 HOH 278 878 447 HOH HOH A . 
C 2 HOH 279 879 534 HOH HOH A . 
C 2 HOH 280 880 451 HOH HOH A . 
C 2 HOH 281 881 161 HOH HOH A . 
C 2 HOH 282 882 217 HOH HOH A . 
C 2 HOH 283 883 535 HOH HOH A . 
C 2 HOH 284 884 362 HOH HOH A . 
D 2 HOH 1   601 185 HOH HOH B . 
D 2 HOH 2   602 383 HOH HOH B . 
D 2 HOH 3   603 300 HOH HOH B . 
D 2 HOH 4   604 150 HOH HOH B . 
D 2 HOH 5   605 265 HOH HOH B . 
D 2 HOH 6   606 198 HOH HOH B . 
D 2 HOH 7   607 467 HOH HOH B . 
D 2 HOH 8   608 321 HOH HOH B . 
D 2 HOH 9   609 155 HOH HOH B . 
D 2 HOH 10  610 29  HOH HOH B . 
D 2 HOH 11  611 72  HOH HOH B . 
D 2 HOH 12  612 214 HOH HOH B . 
D 2 HOH 13  613 342 HOH HOH B . 
D 2 HOH 14  614 47  HOH HOH B . 
D 2 HOH 15  615 314 HOH HOH B . 
D 2 HOH 16  616 338 HOH HOH B . 
D 2 HOH 17  617 188 HOH HOH B . 
D 2 HOH 18  618 192 HOH HOH B . 
D 2 HOH 19  619 154 HOH HOH B . 
D 2 HOH 20  620 200 HOH HOH B . 
D 2 HOH 21  621 419 HOH HOH B . 
D 2 HOH 22  622 35  HOH HOH B . 
D 2 HOH 23  623 14  HOH HOH B . 
D 2 HOH 24  624 204 HOH HOH B . 
D 2 HOH 25  625 434 HOH HOH B . 
D 2 HOH 26  626 340 HOH HOH B . 
D 2 HOH 27  627 326 HOH HOH B . 
D 2 HOH 28  628 446 HOH HOH B . 
D 2 HOH 29  629 3   HOH HOH B . 
D 2 HOH 30  630 351 HOH HOH B . 
D 2 HOH 31  631 308 HOH HOH B . 
D 2 HOH 32  632 17  HOH HOH B . 
D 2 HOH 33  633 181 HOH HOH B . 
D 2 HOH 34  634 122 HOH HOH B . 
D 2 HOH 35  635 62  HOH HOH B . 
D 2 HOH 36  636 9   HOH HOH B . 
D 2 HOH 37  637 6   HOH HOH B . 
D 2 HOH 38  638 258 HOH HOH B . 
D 2 HOH 39  639 404 HOH HOH B . 
D 2 HOH 40  640 290 HOH HOH B . 
D 2 HOH 41  641 56  HOH HOH B . 
D 2 HOH 42  642 54  HOH HOH B . 
D 2 HOH 43  643 46  HOH HOH B . 
D 2 HOH 44  644 495 HOH HOH B . 
D 2 HOH 45  645 65  HOH HOH B . 
D 2 HOH 46  646 274 HOH HOH B . 
D 2 HOH 47  647 39  HOH HOH B . 
D 2 HOH 48  648 346 HOH HOH B . 
D 2 HOH 49  649 112 HOH HOH B . 
D 2 HOH 50  650 59  HOH HOH B . 
D 2 HOH 51  651 193 HOH HOH B . 
D 2 HOH 52  652 103 HOH HOH B . 
D 2 HOH 53  653 212 HOH HOH B . 
D 2 HOH 54  654 450 HOH HOH B . 
D 2 HOH 55  655 134 HOH HOH B . 
D 2 HOH 56  656 253 HOH HOH B . 
D 2 HOH 57  657 251 HOH HOH B . 
D 2 HOH 58  658 325 HOH HOH B . 
D 2 HOH 59  659 203 HOH HOH B . 
D 2 HOH 60  660 208 HOH HOH B . 
D 2 HOH 61  661 12  HOH HOH B . 
D 2 HOH 62  662 425 HOH HOH B . 
D 2 HOH 63  663 275 HOH HOH B . 
D 2 HOH 64  664 250 HOH HOH B . 
D 2 HOH 65  665 5   HOH HOH B . 
D 2 HOH 66  666 186 HOH HOH B . 
D 2 HOH 67  667 100 HOH HOH B . 
D 2 HOH 68  668 86  HOH HOH B . 
D 2 HOH 69  669 317 HOH HOH B . 
D 2 HOH 70  670 22  HOH HOH B . 
D 2 HOH 71  671 84  HOH HOH B . 
D 2 HOH 72  672 360 HOH HOH B . 
D 2 HOH 73  673 230 HOH HOH B . 
D 2 HOH 74  674 539 HOH HOH B . 
D 2 HOH 75  675 426 HOH HOH B . 
D 2 HOH 76  676 375 HOH HOH B . 
D 2 HOH 77  677 289 HOH HOH B . 
D 2 HOH 78  678 102 HOH HOH B . 
D 2 HOH 79  679 113 HOH HOH B . 
D 2 HOH 80  680 96  HOH HOH B . 
D 2 HOH 81  681 337 HOH HOH B . 
D 2 HOH 82  682 98  HOH HOH B . 
D 2 HOH 83  683 291 HOH HOH B . 
D 2 HOH 84  684 114 HOH HOH B . 
D 2 HOH 85  685 455 HOH HOH B . 
D 2 HOH 86  686 370 HOH HOH B . 
D 2 HOH 87  687 490 HOH HOH B . 
D 2 HOH 88  688 92  HOH HOH B . 
D 2 HOH 89  689 42  HOH HOH B . 
D 2 HOH 90  690 522 HOH HOH B . 
D 2 HOH 91  691 118 HOH HOH B . 
D 2 HOH 92  692 106 HOH HOH B . 
D 2 HOH 93  693 394 HOH HOH B . 
D 2 HOH 94  694 302 HOH HOH B . 
D 2 HOH 95  695 132 HOH HOH B . 
D 2 HOH 96  696 105 HOH HOH B . 
D 2 HOH 97  697 57  HOH HOH B . 
D 2 HOH 98  698 13  HOH HOH B . 
D 2 HOH 99  699 52  HOH HOH B . 
D 2 HOH 100 700 7   HOH HOH B . 
D 2 HOH 101 701 242 HOH HOH B . 
D 2 HOH 102 702 252 HOH HOH B . 
D 2 HOH 103 703 141 HOH HOH B . 
D 2 HOH 104 704 444 HOH HOH B . 
D 2 HOH 105 705 288 HOH HOH B . 
D 2 HOH 106 706 508 HOH HOH B . 
D 2 HOH 107 707 443 HOH HOH B . 
D 2 HOH 108 708 67  HOH HOH B . 
D 2 HOH 109 709 149 HOH HOH B . 
D 2 HOH 110 710 243 HOH HOH B . 
D 2 HOH 111 711 172 HOH HOH B . 
D 2 HOH 112 712 397 HOH HOH B . 
D 2 HOH 113 713 281 HOH HOH B . 
D 2 HOH 114 714 82  HOH HOH B . 
D 2 HOH 115 715 463 HOH HOH B . 
D 2 HOH 116 716 58  HOH HOH B . 
D 2 HOH 117 717 116 HOH HOH B . 
D 2 HOH 118 718 517 HOH HOH B . 
D 2 HOH 119 719 514 HOH HOH B . 
D 2 HOH 120 720 157 HOH HOH B . 
D 2 HOH 121 721 146 HOH HOH B . 
D 2 HOH 122 722 412 HOH HOH B . 
D 2 HOH 123 723 357 HOH HOH B . 
D 2 HOH 124 724 83  HOH HOH B . 
D 2 HOH 125 725 189 HOH HOH B . 
D 2 HOH 126 726 407 HOH HOH B . 
D 2 HOH 127 727 93  HOH HOH B . 
D 2 HOH 128 728 277 HOH HOH B . 
D 2 HOH 129 729 352 HOH HOH B . 
D 2 HOH 130 730 37  HOH HOH B . 
D 2 HOH 131 731 311 HOH HOH B . 
D 2 HOH 132 732 348 HOH HOH B . 
D 2 HOH 133 733 417 HOH HOH B . 
D 2 HOH 134 734 487 HOH HOH B . 
D 2 HOH 135 735 63  HOH HOH B . 
D 2 HOH 136 736 400 HOH HOH B . 
D 2 HOH 137 737 160 HOH HOH B . 
D 2 HOH 138 738 215 HOH HOH B . 
D 2 HOH 139 739 316 HOH HOH B . 
D 2 HOH 140 740 458 HOH HOH B . 
D 2 HOH 141 741 79  HOH HOH B . 
D 2 HOH 142 742 382 HOH HOH B . 
D 2 HOH 143 743 529 HOH HOH B . 
D 2 HOH 144 744 66  HOH HOH B . 
D 2 HOH 145 745 329 HOH HOH B . 
D 2 HOH 146 746 163 HOH HOH B . 
D 2 HOH 147 747 528 HOH HOH B . 
D 2 HOH 148 748 136 HOH HOH B . 
D 2 HOH 149 749 422 HOH HOH B . 
D 2 HOH 150 750 108 HOH HOH B . 
D 2 HOH 151 751 301 HOH HOH B . 
D 2 HOH 152 752 41  HOH HOH B . 
D 2 HOH 153 753 91  HOH HOH B . 
D 2 HOH 154 754 268 HOH HOH B . 
D 2 HOH 155 755 486 HOH HOH B . 
D 2 HOH 156 756 71  HOH HOH B . 
D 2 HOH 157 757 408 HOH HOH B . 
D 2 HOH 158 758 168 HOH HOH B . 
D 2 HOH 159 759 140 HOH HOH B . 
D 2 HOH 160 760 20  HOH HOH B . 
D 2 HOH 161 761 406 HOH HOH B . 
D 2 HOH 162 762 78  HOH HOH B . 
D 2 HOH 163 763 476 HOH HOH B . 
D 2 HOH 164 764 211 HOH HOH B . 
D 2 HOH 165 765 389 HOH HOH B . 
D 2 HOH 166 766 90  HOH HOH B . 
D 2 HOH 167 767 468 HOH HOH B . 
D 2 HOH 168 768 413 HOH HOH B . 
D 2 HOH 169 769 292 HOH HOH B . 
D 2 HOH 170 770 365 HOH HOH B . 
D 2 HOH 171 771 162 HOH HOH B . 
D 2 HOH 172 772 401 HOH HOH B . 
D 2 HOH 173 773 392 HOH HOH B . 
D 2 HOH 174 774 328 HOH HOH B . 
D 2 HOH 175 775 166 HOH HOH B . 
D 2 HOH 176 776 104 HOH HOH B . 
D 2 HOH 177 777 38  HOH HOH B . 
D 2 HOH 178 778 376 HOH HOH B . 
D 2 HOH 179 779 53  HOH HOH B . 
D 2 HOH 180 780 147 HOH HOH B . 
D 2 HOH 181 781 278 HOH HOH B . 
D 2 HOH 182 782 137 HOH HOH B . 
D 2 HOH 183 783 488 HOH HOH B . 
D 2 HOH 184 784 303 HOH HOH B . 
D 2 HOH 185 785 536 HOH HOH B . 
D 2 HOH 186 786 222 HOH HOH B . 
D 2 HOH 187 787 496 HOH HOH B . 
D 2 HOH 188 788 239 HOH HOH B . 
D 2 HOH 189 789 334 HOH HOH B . 
D 2 HOH 190 790 220 HOH HOH B . 
D 2 HOH 191 791 421 HOH HOH B . 
D 2 HOH 192 792 226 HOH HOH B . 
D 2 HOH 193 793 432 HOH HOH B . 
D 2 HOH 194 794 436 HOH HOH B . 
D 2 HOH 195 795 497 HOH HOH B . 
D 2 HOH 196 796 282 HOH HOH B . 
D 2 HOH 197 797 380 HOH HOH B . 
D 2 HOH 198 798 472 HOH HOH B . 
D 2 HOH 199 799 492 HOH HOH B . 
D 2 HOH 200 800 366 HOH HOH B . 
D 2 HOH 201 801 524 HOH HOH B . 
D 2 HOH 202 802 246 HOH HOH B . 
D 2 HOH 203 803 361 HOH HOH B . 
D 2 HOH 204 804 515 HOH HOH B . 
D 2 HOH 205 805 330 HOH HOH B . 
D 2 HOH 206 806 224 HOH HOH B . 
D 2 HOH 207 807 190 HOH HOH B . 
D 2 HOH 208 808 264 HOH HOH B . 
D 2 HOH 209 809 501 HOH HOH B . 
D 2 HOH 210 810 299 HOH HOH B . 
D 2 HOH 211 811 431 HOH HOH B . 
D 2 HOH 212 812 344 HOH HOH B . 
D 2 HOH 213 813 475 HOH HOH B . 
D 2 HOH 214 814 462 HOH HOH B . 
D 2 HOH 215 815 525 HOH HOH B . 
D 2 HOH 216 816 164 HOH HOH B . 
D 2 HOH 217 817 491 HOH HOH B . 
D 2 HOH 218 818 350 HOH HOH B . 
D 2 HOH 219 819 218 HOH HOH B . 
D 2 HOH 220 820 279 HOH HOH B . 
D 2 HOH 221 821 248 HOH HOH B . 
D 2 HOH 222 822 435 HOH HOH B . 
D 2 HOH 223 823 418 HOH HOH B . 
D 2 HOH 224 824 503 HOH HOH B . 
D 2 HOH 225 825 531 HOH HOH B . 
D 2 HOH 226 826 526 HOH HOH B . 
D 2 HOH 227 827 405 HOH HOH B . 
D 2 HOH 228 828 169 HOH HOH B . 
D 2 HOH 229 829 512 HOH HOH B . 
D 2 HOH 230 830 297 HOH HOH B . 
D 2 HOH 231 831 440 HOH HOH B . 
D 2 HOH 232 832 371 HOH HOH B . 
D 2 HOH 233 833 255 HOH HOH B . 
D 2 HOH 234 834 498 HOH HOH B . 
D 2 HOH 235 835 452 HOH HOH B . 
D 2 HOH 236 836 420 HOH HOH B . 
D 2 HOH 237 837 481 HOH HOH B . 
D 2 HOH 238 838 177 HOH HOH B . 
D 2 HOH 239 839 482 HOH HOH B . 
D 2 HOH 240 840 373 HOH HOH B . 
D 2 HOH 241 841 354 HOH HOH B . 
D 2 HOH 242 842 386 HOH HOH B . 
D 2 HOH 243 843 388 HOH HOH B . 
D 2 HOH 244 844 510 HOH HOH B . 
D 2 HOH 245 845 398 HOH HOH B . 
# 
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   ? ? ? '(1.20.1_4487: ???)' 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .                    2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? MOLREP   ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  120.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8KG1 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     112.092 
_cell.length_a_esd                 ? 
_cell.length_b                     112.092 
_cell.length_b_esd                 ? 
_cell.length_c                     120.813 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        12 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         8KG1 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                152 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 31 2 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                   8KG1 
_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             2.35 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          47.76 
_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    
;The reservoir solution consisted of 0.1mM Bis-Tris pH6.5 and 9-24%w/v PEG10000. Protein crystals grew by vapor diffusion at 16&#8451; in sitting drops. Yellow crystals with a hexagonal morphology appeared within 24 h and reached their full size after 5-7 days.
;
_exptl_crystal_grow.pdbx_pH_range   6.5-7.5 
_exptl_crystal_grow.temp            289 
# 
_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 PILATUS3 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-04-12 
_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                    'LN2-cooled DCM with Si(111) crystals' 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.03845 
_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                        'SSRF BEAMLINE BL18U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.03845 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL18U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8KG1 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.10 
_reflns.d_resolution_low                               50.00 
_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                                     51350 
_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                           100.0 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                18.6 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          7.8 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.943 
_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                                0.141 
_reflns.pdbx_Rpim_I_all                                0.032 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       957416 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.995 
_reflns.pdbx_CC_star                                   0.999 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.137 
_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                        ? 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_measured_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.number_unique_obs 
_reflns_shell.percent_possible_obs 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.meanI_over_sigI_gt 
_reflns_shell.meanI_over_uI_all 
_reflns_shell.meanI_over_uI_gt 
_reflns_shell.number_measured_gt 
_reflns_shell.number_unique_gt 
_reflns_shell.percent_possible_gt 
_reflns_shell.Rmerge_F_gt 
_reflns_shell.Rmerge_I_gt 
_reflns_shell.pdbx_redundancy 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_netI_over_sigmaI_all 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_rejects 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_CC_star 
_reflns_shell.pdbx_R_split 
_reflns_shell.percent_possible_all 
_reflns_shell.Rmerge_I_all 
_reflns_shell.Rmerge_I_obs 
_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 
2.10 2.14  ? ? ? ? ? ? 2550 ? ? ? ? ? ? ? ? ? ? ? 17.4 0.841 ? ? 1.793 0.429 ? 1  1 0.890 0.971 ? 100.0 ? 1.740 ? ? ? ? ? ? ? ? ? 
2.14 2.18  ? ? ? ? ? ? 2530 ? ? ? ? ? ? ? ? ? ? ? 18.4 0.856 ? ? 1.536 0.359 ? 2  1 0.916 0.978 ? 100.0 ? 1.493 ? ? ? ? ? ? ? ? ? 
2.18 2.22  ? ? ? ? ? ? 2532 ? ? ? ? ? ? ? ? ? ? ? 17.9 0.856 ? ? 1.218 0.287 ? 3  1 0.932 0.982 ? 100.0 ? 1.183 ? ? ? ? ? ? ? ? ? 
2.22 2.26  ? ? ? ? ? ? 2504 ? ? ? ? ? ? ? ? ? ? ? 17.7 0.898 ? ? 1.011 0.240 ? 4  1 0.954 0.988 ? 100.0 ? 0.982 ? ? ? ? ? ? ? ? ? 
2.26 2.31  ? ? ? ? ? ? 2571 ? ? ? ? ? ? ? ? ? ? ? 19.0 0.888 ? ? 0.813 0.187 ? 5  1 0.962 0.990 ? 100.0 ? 0.791 ? ? ? ? ? ? ? ? ? 
2.31 2.37  ? ? ? ? ? ? 2518 ? ? ? ? ? ? ? ? ? ? ? 18.9 0.937 ? ? 0.760 0.171 ? 6  1 0.973 0.993 ? 100.0 ? 0.740 ? ? ? ? ? ? ? ? ? 
2.37 2.42  ? ? ? ? ? ? 2548 ? ? ? ? ? ? ? ? ? ? ? 18.7 0.894 ? ? 0.557 0.129 ? 7  1 0.974 0.993 ? 100.0 ? 0.541 ? ? ? ? ? ? ? ? ? 
2.42 2.49  ? ? ? ? ? ? 2573 ? ? ? ? ? ? ? ? ? ? ? 18.4 0.907 ? ? 0.451 0.105 ? 8  1 0.983 0.996 ? 100.0 ? 0.438 ? ? ? ? ? ? ? ? ? 
2.49 2.56  ? ? ? ? ? ? 2520 ? ? ? ? ? ? ? ? ? ? ? 17.6 0.914 ? ? 0.361 0.086 ? 9  1 0.986 0.996 ? 100.0 ? 0.350 ? ? ? ? ? ? ? ? ? 
2.56 2.65  ? ? ? ? ? ? 2556 ? ? ? ? ? ? ? ? ? ? ? 19.0 0.933 ? ? 0.304 0.070 ? 10 1 0.984 0.996 ? 100.0 ? 0.295 ? ? ? ? ? ? ? ? ? 
2.65 2.74  ? ? ? ? ? ? 2558 ? ? ? ? ? ? ? ? ? ? ? 18.2 0.919 ? ? 0.244 0.057 ? 11 1 0.991 0.998 ? 100.0 ? 0.237 ? ? ? ? ? ? ? ? ? 
2.74 2.85  ? ? ? ? ? ? 2552 ? ? ? ? ? ? ? ? ? ? ? 19.2 0.941 ? ? 0.199 0.045 ? 12 1 0.993 0.998 ? 100.0 ? 0.194 ? ? ? ? ? ? ? ? ? 
2.85 2.98  ? ? ? ? ? ? 2544 ? ? ? ? ? ? ? ? ? ? ? 19.5 0.941 ? ? 0.169 0.038 ? 13 1 0.993 0.998 ? 100.0 ? 0.165 ? ? ? ? ? ? ? ? ? 
2.98 3.14  ? ? ? ? ? ? 2562 ? ? ? ? ? ? ? ? ? ? ? 19.4 1.002 ? ? 0.147 0.033 ? 14 1 0.995 0.999 ? 100.0 ? 0.143 ? ? ? ? ? ? ? ? ? 
3.14 3.33  ? ? ? ? ? ? 2578 ? ? ? ? ? ? ? ? ? ? ? 18.6 1.044 ? ? 0.132 0.030 ? 15 1 0.994 0.998 ? 100.0 ? 0.128 ? ? ? ? ? ? ? ? ? 
3.33 3.59  ? ? ? ? ? ? 2588 ? ? ? ? ? ? ? ? ? ? ? 19.2 1.088 ? ? 0.120 0.027 ? 16 1 0.996 0.999 ? 100.0 ? 0.117 ? ? ? ? ? ? ? ? ? 
3.59 3.95  ? ? ? ? ? ? 2577 ? ? ? ? ? ? ? ? ? ? ? 19.7 1.047 ? ? 0.107 0.024 ? 17 1 0.995 0.999 ? 100.0 ? 0.104 ? ? ? ? ? ? ? ? ? 
3.95 4.52  ? ? ? ? ? ? 2596 ? ? ? ? ? ? ? ? ? ? ? 19.4 0.983 ? ? 0.099 0.022 ? 18 1 0.996 0.999 ? 100.0 ? 0.097 ? ? ? ? ? ? ? ? ? 
4.52 5.70  ? ? ? ? ? ? 2645 ? ? ? ? ? ? ? ? ? ? ? 18.6 0.856 ? ? 0.090 0.021 ? 19 1 0.996 0.999 ? 100.0 ? 0.087 ? ? ? ? ? ? ? ? ? 
5.70 50.00 ? ? ? ? ? ? 2748 ? ? ? ? ? ? ? ? ? ? ? 18.1 1.078 ? ? 0.077 0.018 ? 20 1 0.996 0.999 ? 100.0 ? 0.075 ? ? ? ? ? ? ? ? ? 
# 
_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                                 8KG1 
_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                            2.10 
_refine.ls_d_res_low                             45.04 
_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                     51305 
_refine.ls_number_reflns_R_free                  2605 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.76 
_refine.ls_percent_reflns_R_free                 5.08 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1511 
_refine.ls_R_factor_R_free                       0.1855 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1492 
_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                          1.36 
_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             1.10 
_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                 17.23 
_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                            0.15 
_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                       2.10 
_refine_hist.d_res_low                        45.04 
_refine_hist.number_atoms_solvent             529 
_refine_hist.number_atoms_total               6754 
_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        6225 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         0 
_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 ? 6412 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.843 ? 8737 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 7.826 ? 906  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.053 ? 977  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.009 ? 1153 ? 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' 2.10 2.14  . . 95  2467 95.00  . . . . 0.1769 . . . . . . . . . . . 0.2164 
'X-RAY DIFFRACTION' 2.14 2.18  . . 164 2495 100.00 . . . . 0.1763 . . . . . . . . . . . 0.2052 
'X-RAY DIFFRACTION' 2.18 2.23  . . 160 2527 100.00 . . . . 0.1661 . . . . . . . . . . . 0.2219 
'X-RAY DIFFRACTION' 2.23 2.28  . . 150 2524 100.00 . . . . 0.1594 . . . . . . . . . . . 0.2163 
'X-RAY DIFFRACTION' 2.28 2.33  . . 127 2557 100.00 . . . . 0.1568 . . . . . . . . . . . 0.1977 
'X-RAY DIFFRACTION' 2.33 2.39  . . 161 2511 100.00 . . . . 0.1559 . . . . . . . . . . . 0.2040 
'X-RAY DIFFRACTION' 2.39 2.45  . . 136 2549 100.00 . . . . 0.1561 . . . . . . . . . . . 0.2059 
'X-RAY DIFFRACTION' 2.45 2.52  . . 140 2528 100.00 . . . . 0.1571 . . . . . . . . . . . 0.2101 
'X-RAY DIFFRACTION' 2.52 2.60  . . 125 2596 100.00 . . . . 0.1500 . . . . . . . . . . . 0.1714 
'X-RAY DIFFRACTION' 2.60 2.70  . . 123 2539 100.00 . . . . 0.1476 . . . . . . . . . . . 0.1988 
'X-RAY DIFFRACTION' 2.70 2.81  . . 151 2550 100.00 . . . . 0.1482 . . . . . . . . . . . 0.1864 
'X-RAY DIFFRACTION' 2.81 2.93  . . 114 2575 100.00 . . . . 0.1535 . . . . . . . . . . . 0.1916 
'X-RAY DIFFRACTION' 2.93 3.09  . . 135 2566 100.00 . . . . 0.1458 . . . . . . . . . . . 0.1881 
'X-RAY DIFFRACTION' 3.09 3.28  . . 150 2553 100.00 . . . . 0.1502 . . . . . . . . . . . 0.2164 
'X-RAY DIFFRACTION' 3.28 3.53  . . 112 2589 100.00 . . . . 0.1449 . . . . . . . . . . . 0.1755 
'X-RAY DIFFRACTION' 3.53 3.89  . . 156 2583 100.00 . . . . 0.1353 . . . . . . . . . . . 0.1691 
'X-RAY DIFFRACTION' 3.89 4.45  . . 136 2615 100.00 . . . . 0.1293 . . . . . . . . . . . 0.1458 
'X-RAY DIFFRACTION' 4.45 5.60  . . 114 2651 100.00 . . . . 0.1421 . . . . . . . . . . . 0.1491 
'X-RAY DIFFRACTION' 5.61 45.04 . . 156 2725 100.00 . . . . 0.1619 . . . . . . . . . . . 0.1956 
# 
_struct.entry_id                     8KG1 
_struct.title                        'Crystal structure of the cargo cysteine desulfurase from Mycobacterium smegmatis' 
_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        8KG1 
_struct_keywords.text            'cargo protein, cysteine desulfurase, TRANSFERASE' 
_struct_keywords.pdbx_keywords   TRANSFERASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 2 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    I7GDP6_MYCS2 
_struct_ref.pdbx_db_accession          I7GDP6 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;AHQPVPQFPDRHEIFDVNAIRADFPILRETVNGKPLIWFDNAATTQKPQAVIDRLSHFYAHENSNIHRAAHELAARATDA
YEDAREAVRRFIGAAKAEEIIFLRGTTEAINLVAHAWGGKHLGPGDEIVITHLEHHANIVPWQLLSRQTGAVLKVAPVDD
AGNLLLGEFEDLLGPRTKLVAATQVSNALGTVTPVETIVELGHRYGARVLIDGAQSIPHMPIDVAALGADFFVFSGHKIY
GPTGIGVLYGREDALAETPPWQGGGNMIADVTLERSLYQGPPNKFEAGTGNIADAVGLGEAIRYVERVGIERIAAYEHAL
LEYATPRLAAIPGVRIVGTAQEKASVLSFVLAGHEPLEVGKALNAEGIAVRAGHHCAQPILRRMGLEATVRPSFAFYNTF
DEIDVFIDAVRRIAEGSV
;
_struct_ref.pdbx_align_begin           142 
# 
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 8KG1 A 1 ? 418 ? I7GDP6 142 ? 559 ? 142 559 
2 1 8KG1 B 1 ? 418 ? I7GDP6 142 ? 559 ? 142 559 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 8KG1 ASP A 419 ? UNP I7GDP6 ? ? 'expression tag' 560 1  
1 8KG1 TYR A 420 ? UNP I7GDP6 ? ? 'expression tag' 561 2  
1 8KG1 LYS A 421 ? UNP I7GDP6 ? ? 'expression tag' 562 3  
1 8KG1 ASP A 422 ? UNP I7GDP6 ? ? 'expression tag' 563 4  
1 8KG1 ASP A 423 ? UNP I7GDP6 ? ? 'expression tag' 564 5  
1 8KG1 ASP A 424 ? UNP I7GDP6 ? ? 'expression tag' 565 6  
1 8KG1 ASP A 425 ? UNP I7GDP6 ? ? 'expression tag' 566 7  
1 8KG1 LYS A 426 ? UNP I7GDP6 ? ? 'expression tag' 567 8  
2 8KG1 ASP B 419 ? UNP I7GDP6 ? ? 'expression tag' 560 9  
2 8KG1 TYR B 420 ? UNP I7GDP6 ? ? 'expression tag' 561 10 
2 8KG1 LYS B 421 ? UNP I7GDP6 ? ? 'expression tag' 562 11 
2 8KG1 ASP B 422 ? UNP I7GDP6 ? ? 'expression tag' 563 12 
2 8KG1 ASP B 423 ? UNP I7GDP6 ? ? 'expression tag' 564 13 
2 8KG1 ASP B 424 ? UNP I7GDP6 ? ? 'expression tag' 565 14 
2 8KG1 ASP B 425 ? UNP I7GDP6 ? ? 'expression tag' 566 15 
2 8KG1 LYS B 426 ? UNP I7GDP6 ? ? 'expression tag' 567 16 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 6870  ? 
1 MORE         -29   ? 
1 'SSA (A^2)'  25700 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D 
# 
_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 16  ? ALA A 22  ? ASP A 157 ALA A 163 1 ? 7  
HELX_P HELX_P2  AA2 ASP A 23  ? ARG A 28  ? ASP A 164 ARG A 169 5 ? 6  
HELX_P HELX_P3  AA3 PRO A 48  ? GLU A 62  ? PRO A 189 GLU A 203 1 ? 15 
HELX_P HELX_P4  AA4 HIS A 71  ? GLY A 93  ? HIS A 212 GLY A 234 1 ? 23 
HELX_P HELX_P5  AA5 LYS A 96  ? GLU A 98  ? LYS A 237 GLU A 239 5 ? 3  
HELX_P HELX_P6  AA6 GLY A 105 ? LEU A 122 ? GLY A 246 LEU A 263 1 ? 18 
HELX_P HELX_P7  AA7 HIS A 135 ? ASN A 138 ? HIS A 276 ASN A 279 5 ? 4  
HELX_P HELX_P8  AA8 ILE A 139 ? GLY A 150 ? ILE A 280 GLY A 291 1 ? 12 
HELX_P HELX_P9  AA9 LEU A 165 ? LEU A 173 ? LEU A 306 LEU A 314 1 ? 9  
HELX_P HELX_P10 AB1 PRO A 194 ? TYR A 205 ? PRO A 335 TYR A 346 1 ? 12 
HELX_P HELX_P11 AB2 ASP A 223 ? GLY A 228 ? ASP A 364 GLY A 369 1 ? 6  
HELX_P HELX_P12 AB3 HIS A 237 ? TYR A 240 ? HIS A 378 TYR A 381 5 ? 4  
HELX_P HELX_P13 AB4 ARG A 251 ? GLU A 257 ? ARG A 392 GLU A 398 1 ? 7  
HELX_P HELX_P14 AB5 PRO A 282 ? GLU A 286 ? PRO A 423 GLU A 427 5 ? 5  
HELX_P HELX_P15 AB6 ASN A 291 ? GLY A 309 ? ASN A 432 GLY A 450 1 ? 19 
HELX_P HELX_P16 AB7 GLY A 309 ? ALA A 330 ? GLY A 450 ALA A 471 1 ? 22 
HELX_P HELX_P17 AB8 GLU A 355 ? GLU A 366 ? GLU A 496 GLU A 507 1 ? 12 
HELX_P HELX_P18 AB9 ALA A 377 ? MET A 384 ? ALA A 518 MET A 525 1 ? 8  
HELX_P HELX_P19 AC1 THR A 399 ? GLU A 415 ? THR A 540 GLU A 556 1 ? 17 
HELX_P HELX_P20 AC2 ASP B 16  ? ALA B 22  ? ASP B 157 ALA B 163 1 ? 7  
HELX_P HELX_P21 AC3 ASP B 23  ? ARG B 28  ? ASP B 164 ARG B 169 5 ? 6  
HELX_P HELX_P22 AC4 PRO B 48  ? GLU B 62  ? PRO B 189 GLU B 203 1 ? 15 
HELX_P HELX_P23 AC5 HIS B 71  ? GLY B 93  ? HIS B 212 GLY B 234 1 ? 23 
HELX_P HELX_P24 AC6 LYS B 96  ? GLU B 98  ? LYS B 237 GLU B 239 5 ? 3  
HELX_P HELX_P25 AC7 GLY B 105 ? ALA B 116 ? GLY B 246 ALA B 257 1 ? 12 
HELX_P HELX_P26 AC8 ALA B 116 ? LEU B 122 ? ALA B 257 LEU B 263 1 ? 7  
HELX_P HELX_P27 AC9 HIS B 135 ? ASN B 138 ? HIS B 276 ASN B 279 5 ? 4  
HELX_P HELX_P28 AD1 ILE B 139 ? GLY B 150 ? ILE B 280 GLY B 291 1 ? 12 
HELX_P HELX_P29 AD2 LEU B 165 ? LEU B 172 ? LEU B 306 LEU B 313 1 ? 8  
HELX_P HELX_P30 AD3 PRO B 194 ? TYR B 205 ? PRO B 335 TYR B 346 1 ? 12 
HELX_P HELX_P31 AD4 ASP B 223 ? GLY B 228 ? ASP B 364 GLY B 369 1 ? 6  
HELX_P HELX_P32 AD5 HIS B 237 ? TYR B 240 ? HIS B 378 TYR B 381 5 ? 4  
HELX_P HELX_P33 AD6 ARG B 251 ? GLU B 257 ? ARG B 392 GLU B 398 1 ? 7  
HELX_P HELX_P34 AD7 PRO B 282 ? GLU B 286 ? PRO B 423 GLU B 427 5 ? 5  
HELX_P HELX_P35 AD8 ASN B 291 ? GLY B 309 ? ASN B 432 GLY B 450 1 ? 19 
HELX_P HELX_P36 AD9 GLY B 309 ? ALA B 330 ? GLY B 450 ALA B 471 1 ? 22 
HELX_P HELX_P37 AE1 GLU B 355 ? GLU B 366 ? GLU B 496 GLU B 507 1 ? 12 
HELX_P HELX_P38 AE2 ALA B 377 ? MET B 384 ? ALA B 518 MET B 525 1 ? 8  
HELX_P HELX_P39 AE3 THR B 399 ? GLY B 416 ? THR B 540 GLY B 557 1 ? 18 
# 
_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 both ? A HIS 237 C ? ? ? 1_555 A LLP 238 N ? ? A HIS 378 A LLP 379 1_555 ? ? ? ? ? ? ? 1.326 ? ? 
covale2 covale both ? A LLP 238 C ? ? ? 1_555 A ILE 239 N ? ? A LLP 379 A ILE 380 1_555 ? ? ? ? ? ? ? 1.332 ? ? 
covale3 covale both ? B HIS 237 C ? ? ? 1_555 B LLP 238 N ? ? B HIS 378 B LLP 379 1_555 ? ? ? ? ? ? ? 1.333 ? ? 
covale4 covale both ? B LLP 238 C ? ? ? 1_555 B ILE 239 N ? ? B LLP 379 B ILE 380 1_555 ? ? ? ? ? ? ? 1.333 ? ? 
# 
_struct_conn_type.id          covale 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
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 LLP A 238 ? . . . . LLP A 379 ? 1_555 . . . . . . . LYS 1 LLP 'Pyridoxal phosphate' 'Named protein modification' 
2 LLP B 238 ? . . . . LLP B 379 ? 1_555 . . . . . . . LYS 1 LLP 'Pyridoxal phosphate' 'Named protein 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 PRO 281 A . ? PRO 422 A PRO 282 A ? PRO 423 A 1 2.29 
2 PRO 281 B . ? PRO 422 B PRO 282 B ? PRO 423 B 1 0.58 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2 ? 
AA2 ? 2 ? 
AA3 ? 7 ? 
AA4 ? 2 ? 
AA5 ? 2 ? 
AA6 ? 2 ? 
AA7 ? 2 ? 
AA8 ? 2 ? 
AA9 ? 7 ? 
AB1 ? 2 ? 
AB2 ? 2 ? 
AB3 ? 2 ? 
# 
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      
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? parallel      
AA3 4 5 ? parallel      
AA3 5 6 ? parallel      
AA3 6 7 ? parallel      
AA4 1 2 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA8 1 2 ? parallel      
AA9 1 2 ? anti-parallel 
AA9 2 3 ? anti-parallel 
AA9 3 4 ? parallel      
AA9 4 5 ? parallel      
AA9 5 6 ? parallel      
AA9 6 7 ? parallel      
AB1 1 2 ? anti-parallel 
AB2 1 2 ? anti-parallel 
AB3 1 2 ? anti-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 THR A 30  ? VAL A 31  ? THR A 171 VAL A 172 
AA1 2 LYS A 34  ? PRO A 35  ? LYS A 175 PRO A 176 
AA2 1 ILE A 37  ? TRP A 38  ? ILE A 178 TRP A 179 
AA2 2 ILE A 368 ? ALA A 369 ? ILE A 509 ALA A 510 
AA3 1 ILE A 100 ? LEU A 103 ? ILE A 241 LEU A 244 
AA3 2 GLY A 246 ? GLY A 250 ? GLY A 387 GLY A 391 
AA3 3 PHE A 231 ? SER A 235 ? PHE A 372 SER A 376 
AA3 4 ARG A 208 ? ASP A 212 ? ARG A 349 ASP A 353 
AA3 5 THR A 177 ? THR A 183 ? THR A 318 THR A 324 
AA3 6 GLU A 127 ? THR A 131 ? GLU A 268 THR A 272 
AA3 7 VAL A 152 ? ALA A 156 ? VAL A 293 ALA A 297 
AA4 1 ILE A 268 ? VAL A 271 ? ILE A 409 VAL A 412 
AA4 2 SER A 276 ? TYR A 278 ? SER A 417 TYR A 419 
AA5 1 VAL A 334 ? VAL A 337 ? VAL A 475 VAL A 478 
AA5 2 SER A 348 ? LEU A 351 ? SER A 489 LEU A 492 
AA6 1 ARG A 371 ? GLY A 373 ? ARG A 512 GLY A 514 
AA6 2 THR A 389 ? ARG A 391 ? THR A 530 ARG A 532 
AA7 1 THR B 30  ? VAL B 31  ? THR B 171 VAL B 172 
AA7 2 LYS B 34  ? PRO B 35  ? LYS B 175 PRO B 176 
AA8 1 ILE B 37  ? TRP B 38  ? ILE B 178 TRP B 179 
AA8 2 ILE B 368 ? ALA B 369 ? ILE B 509 ALA B 510 
AA9 1 ILE B 100 ? LEU B 103 ? ILE B 241 LEU B 244 
AA9 2 GLY B 246 ? GLY B 250 ? GLY B 387 GLY B 391 
AA9 3 PHE B 231 ? SER B 235 ? PHE B 372 SER B 376 
AA9 4 ARG B 208 ? ASP B 212 ? ARG B 349 ASP B 353 
AA9 5 THR B 177 ? THR B 183 ? THR B 318 THR B 324 
AA9 6 GLU B 127 ? THR B 131 ? GLU B 268 THR B 272 
AA9 7 VAL B 152 ? ALA B 156 ? VAL B 293 ALA B 297 
AB1 1 ILE B 268 ? VAL B 271 ? ILE B 409 VAL B 412 
AB1 2 SER B 276 ? TYR B 278 ? SER B 417 TYR B 419 
AB2 1 VAL B 334 ? VAL B 337 ? VAL B 475 VAL B 478 
AB2 2 SER B 348 ? LEU B 351 ? SER B 489 LEU B 492 
AB3 1 ARG B 371 ? GLY B 373 ? ARG B 512 GLY B 514 
AB3 2 THR B 389 ? ARG B 391 ? THR B 530 ARG B 532 
# 
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 31  ? N VAL A 172 O LYS A 34  ? O LYS A 175 
AA2 1 2 N ILE A 37  ? N ILE A 178 O ALA A 369 ? O ALA A 510 
AA3 1 2 N ILE A 101 ? N ILE A 242 O LEU A 248 ? O LEU A 389 
AA3 2 3 O TYR A 249 ? O TYR A 390 N PHE A 232 ? N PHE A 373 
AA3 3 4 O PHE A 231 ? O PHE A 372 N ILE A 211 ? N ILE A 352 
AA3 4 5 O LEU A 210 ? O LEU A 351 N VAL A 180 ? N VAL A 321 
AA3 5 6 O ALA A 181 ? O ALA A 322 N VAL A 129 ? N VAL A 270 
AA3 6 7 N ILE A 130 ? N ILE A 271 O ALA A 156 ? O ALA A 297 
AA4 1 2 N ALA A 269 ? N ALA A 410 O LEU A 277 ? O LEU A 418 
AA5 1 2 N VAL A 337 ? N VAL A 478 O SER A 348 ? O SER A 489 
AA6 1 2 N ARG A 371 ? N ARG A 512 O ARG A 391 ? O ARG A 532 
AA7 1 2 N VAL B 31  ? N VAL B 172 O LYS B 34  ? O LYS B 175 
AA8 1 2 N ILE B 37  ? N ILE B 178 O ALA B 369 ? O ALA B 510 
AA9 1 2 N ILE B 101 ? N ILE B 242 O LEU B 248 ? O LEU B 389 
AA9 2 3 O TYR B 249 ? O TYR B 390 N PHE B 232 ? N PHE B 373 
AA9 3 4 O PHE B 231 ? O PHE B 372 N ILE B 211 ? N ILE B 352 
AA9 4 5 O LEU B 210 ? O LEU B 351 N VAL B 180 ? N VAL B 321 
AA9 5 6 O ALA B 181 ? O ALA B 322 N VAL B 129 ? N VAL B 270 
AA9 6 7 N ILE B 128 ? N ILE B 269 O LYS B 154 ? O LYS B 295 
AB1 1 2 N ALA B 269 ? N ALA B 410 O LEU B 277 ? O LEU B 418 
AB2 1 2 N VAL B 337 ? N VAL B 478 O SER B 348 ? O SER B 489 
AB3 1 2 N ARG B 371 ? N ARG B 512 O ARG B 391 ? O ARG B 532 
# 
_pdbx_entry_details.entry_id                   8KG1 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 SER A 205 ? ? 179.89  159.78 
2  1 HIS A 208 ? ? 95.30   93.46  
3  1 ILE A 280 ? ? -127.29 -56.82 
4  1 TRP A 402 ? ? -110.14 -80.23 
5  1 ASN A 407 ? ? 75.87   -41.97 
6  1 SER A 486 ? ? 74.73   -42.89 
7  1 ALA A 518 ? ? -148.72 52.66  
8  1 HIS B 208 ? A 94.20   90.40  
9  1 HIS B 208 ? B 94.61   89.75  
10 1 ILE B 280 ? ? -126.49 -58.15 
11 1 TRP B 402 ? ? -102.93 -79.92 
12 1 ASN B 407 ? ? 73.25   -44.97 
13 1 SER B 486 ? ? 73.10   -52.90 
14 1 ALA B 518 ? ? -151.82 50.84  
# 
loop_
_pdbx_struct_mod_residue.id 
_pdbx_struct_mod_residue.label_asym_id 
_pdbx_struct_mod_residue.label_comp_id 
_pdbx_struct_mod_residue.label_seq_id 
_pdbx_struct_mod_residue.auth_asym_id 
_pdbx_struct_mod_residue.auth_comp_id 
_pdbx_struct_mod_residue.auth_seq_id 
_pdbx_struct_mod_residue.PDB_ins_code 
_pdbx_struct_mod_residue.parent_comp_id 
_pdbx_struct_mod_residue.details 
1 A LLP 238 A LLP 379 ? LYS 'modified residue' 
2 B LLP 238 B LLP 379 ? LYS 'modified residue' 
# 
loop_
_pdbx_struct_special_symmetry.id 
_pdbx_struct_special_symmetry.PDB_model_num 
_pdbx_struct_special_symmetry.auth_asym_id 
_pdbx_struct_special_symmetry.auth_comp_id 
_pdbx_struct_special_symmetry.auth_seq_id 
_pdbx_struct_special_symmetry.PDB_ins_code 
_pdbx_struct_special_symmetry.label_asym_id 
_pdbx_struct_special_symmetry.label_comp_id 
_pdbx_struct_special_symmetry.label_seq_id 
1 1 B HOH 702 ? D HOH . 
2 1 B HOH 808 ? D HOH . 
# 
_pdbx_refine_tls.id               1 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         -45.7343 
_pdbx_refine_tls.origin_y         60.2486 
_pdbx_refine_tls.origin_z         -18.4209 
_pdbx_refine_tls.T[1][1]          0.0912 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          0.0477 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          0.0229 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.1660 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          0.0062 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.1118 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          1.0103 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          0.3908 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          0.0264 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          0.5468 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          0.0124 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          0.7538 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          0.0539 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          -0.0636 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          -0.0785 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          0.0381 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          -0.0284 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          -0.0087 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          -0.1692 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          -0.0882 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          -0.0154 
_pdbx_refine_tls.S[3][3]_esd      ? 
# 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.refine_tls_id       1 
_pdbx_refine_tls_group.beg_label_asym_id   ? 
_pdbx_refine_tls_group.beg_label_seq_id    ? 
_pdbx_refine_tls_group.beg_auth_asym_id    ? 
_pdbx_refine_tls_group.beg_auth_seq_id     ? 
_pdbx_refine_tls_group.beg_PDB_ins_code    ? 
_pdbx_refine_tls_group.end_label_asym_id   ? 
_pdbx_refine_tls_group.end_label_seq_id    ? 
_pdbx_refine_tls_group.end_auth_asym_id    ? 
_pdbx_refine_tls_group.end_auth_seq_id     ? 
_pdbx_refine_tls_group.end_PDB_ins_code    ? 
_pdbx_refine_tls_group.selection           ? 
_pdbx_refine_tls_group.selection_details   all 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 883 ? 6.34 . 
2 1 O ? A HOH 884 ? 6.78 . 
3 1 O ? B HOH 845 ? 6.81 . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A ALA 142 ? A ALA 1   
2  1 Y 1 A HIS 143 ? A HIS 2   
3  1 Y 1 A GLN 144 ? A GLN 3   
4  1 Y 1 A PRO 145 ? A PRO 4   
5  1 Y 1 A VAL 146 ? A VAL 5   
6  1 Y 1 A PRO 147 ? A PRO 6   
7  1 Y 1 A GLN 148 ? A GLN 7   
8  1 Y 1 A PHE 149 ? A PHE 8   
9  1 Y 1 A PRO 150 ? A PRO 9   
10 1 Y 1 A ASP 151 ? A ASP 10  
11 1 Y 1 A GLY 557 ? A GLY 416 
12 1 Y 1 A SER 558 ? A SER 417 
13 1 Y 1 A VAL 559 ? A VAL 418 
14 1 Y 1 A ASP 560 ? A ASP 419 
15 1 Y 1 A TYR 561 ? A TYR 420 
16 1 Y 1 A LYS 562 ? A LYS 421 
17 1 Y 1 A ASP 563 ? A ASP 422 
18 1 Y 1 A ASP 564 ? A ASP 423 
19 1 Y 1 A ASP 565 ? A ASP 424 
20 1 Y 1 A ASP 566 ? A ASP 425 
21 1 Y 1 A LYS 567 ? A LYS 426 
22 1 Y 1 B ALA 142 ? B ALA 1   
23 1 Y 1 B HIS 143 ? B HIS 2   
24 1 Y 1 B GLN 144 ? B GLN 3   
25 1 Y 1 B PRO 145 ? B PRO 4   
26 1 Y 1 B VAL 146 ? B VAL 5   
27 1 Y 1 B PRO 147 ? B PRO 6   
28 1 Y 1 B GLN 148 ? B GLN 7   
29 1 Y 1 B PHE 149 ? B PHE 8   
30 1 Y 1 B PRO 150 ? B PRO 9   
31 1 Y 1 B ASP 151 ? B ASP 10  
32 1 Y 1 B ARG 152 ? B ARG 11  
33 1 Y 1 B HIS 153 ? B HIS 12  
34 1 Y 1 B GLU 154 ? B GLU 13  
35 1 Y 1 B ILE 155 ? B ILE 14  
36 1 Y 1 B TYR 561 ? B TYR 420 
37 1 Y 1 B LYS 562 ? B LYS 421 
38 1 Y 1 B ASP 563 ? B ASP 422 
39 1 Y 1 B ASP 564 ? B ASP 423 
40 1 Y 1 B ASP 565 ? B ASP 424 
41 1 Y 1 B ASP 566 ? B ASP 425 
42 1 Y 1 B LYS 567 ? B LYS 426 
# 
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 
ALA N      N N N 1   
ALA CA     C N S 2   
ALA C      C N N 3   
ALA O      O N N 4   
ALA CB     C N N 5   
ALA OXT    O N N 6   
ALA H      H N N 7   
ALA H2     H N N 8   
ALA HA     H N N 9   
ALA HB1    H N N 10  
ALA HB2    H N N 11  
ALA HB3    H N N 12  
ALA HXT    H N N 13  
ARG N      N N N 14  
ARG CA     C N S 15  
ARG C      C N N 16  
ARG O      O N N 17  
ARG CB     C N N 18  
ARG CG     C N N 19  
ARG CD     C N N 20  
ARG NE     N N N 21  
ARG CZ     C N N 22  
ARG NH1    N N N 23  
ARG NH2    N N N 24  
ARG OXT    O N N 25  
ARG H      H N N 26  
ARG H2     H N N 27  
ARG HA     H N N 28  
ARG HB2    H N N 29  
ARG HB3    H N N 30  
ARG HG2    H N N 31  
ARG HG3    H N N 32  
ARG HD2    H N N 33  
ARG HD3    H N N 34  
ARG HE     H N N 35  
ARG HH11   H N N 36  
ARG HH12   H N N 37  
ARG HH21   H N N 38  
ARG HH22   H N N 39  
ARG HXT    H N N 40  
ASN N      N N N 41  
ASN CA     C N S 42  
ASN C      C N N 43  
ASN O      O N N 44  
ASN CB     C N N 45  
ASN CG     C N N 46  
ASN OD1    O N N 47  
ASN ND2    N N N 48  
ASN OXT    O N N 49  
ASN H      H N N 50  
ASN H2     H N N 51  
ASN HA     H N N 52  
ASN HB2    H N N 53  
ASN HB3    H N N 54  
ASN HD21   H N N 55  
ASN HD22   H N N 56  
ASN HXT    H N N 57  
ASP N      N N N 58  
ASP CA     C N S 59  
ASP C      C N N 60  
ASP O      O N N 61  
ASP CB     C N N 62  
ASP CG     C N N 63  
ASP OD1    O N N 64  
ASP OD2    O N N 65  
ASP OXT    O N N 66  
ASP H      H N N 67  
ASP H2     H N N 68  
ASP HA     H N N 69  
ASP HB2    H N N 70  
ASP HB3    H N N 71  
ASP HD2    H N N 72  
ASP HXT    H N N 73  
CYS N      N N N 74  
CYS CA     C N R 75  
CYS C      C N N 76  
CYS O      O N N 77  
CYS CB     C N N 78  
CYS SG     S N N 79  
CYS OXT    O N N 80  
CYS H      H N N 81  
CYS H2     H N N 82  
CYS HA     H N N 83  
CYS HB2    H N N 84  
CYS HB3    H N N 85  
CYS HG     H N N 86  
CYS HXT    H N N 87  
GLN N      N N N 88  
GLN CA     C N S 89  
GLN C      C N N 90  
GLN O      O N N 91  
GLN CB     C N N 92  
GLN CG     C N N 93  
GLN CD     C N N 94  
GLN OE1    O N N 95  
GLN NE2    N N N 96  
GLN OXT    O N N 97  
GLN H      H N N 98  
GLN H2     H N N 99  
GLN HA     H N N 100 
GLN HB2    H N N 101 
GLN HB3    H N N 102 
GLN HG2    H N N 103 
GLN HG3    H N N 104 
GLN HE21   H N N 105 
GLN HE22   H N N 106 
GLN HXT    H N N 107 
GLU N      N N N 108 
GLU CA     C N S 109 
GLU C      C N N 110 
GLU O      O N N 111 
GLU CB     C N N 112 
GLU CG     C N N 113 
GLU CD     C N N 114 
GLU OE1    O N N 115 
GLU OE2    O N N 116 
GLU OXT    O N N 117 
GLU H      H N N 118 
GLU H2     H N N 119 
GLU HA     H N N 120 
GLU HB2    H N N 121 
GLU HB3    H N N 122 
GLU HG2    H N N 123 
GLU HG3    H N N 124 
GLU HE2    H N N 125 
GLU HXT    H N N 126 
GLY N      N N N 127 
GLY CA     C N N 128 
GLY C      C N N 129 
GLY O      O N N 130 
GLY OXT    O N N 131 
GLY H      H N N 132 
GLY H2     H N N 133 
GLY HA2    H N N 134 
GLY HA3    H N N 135 
GLY HXT    H N N 136 
HIS N      N N N 137 
HIS CA     C N S 138 
HIS C      C N N 139 
HIS O      O N N 140 
HIS CB     C N N 141 
HIS CG     C Y N 142 
HIS ND1    N Y N 143 
HIS CD2    C Y N 144 
HIS CE1    C Y N 145 
HIS NE2    N Y N 146 
HIS OXT    O N N 147 
HIS H      H N N 148 
HIS H2     H N N 149 
HIS HA     H N N 150 
HIS HB2    H N N 151 
HIS HB3    H N N 152 
HIS HD1    H N N 153 
HIS HD2    H N N 154 
HIS HE1    H N N 155 
HIS HE2    H N N 156 
HIS HXT    H N N 157 
HOH O      O N N 158 
HOH H1     H N N 159 
HOH H2     H N N 160 
ILE N      N N N 161 
ILE CA     C N S 162 
ILE C      C N N 163 
ILE O      O N N 164 
ILE CB     C N S 165 
ILE CG1    C N N 166 
ILE CG2    C N N 167 
ILE CD1    C N N 168 
ILE OXT    O N N 169 
ILE H      H N N 170 
ILE H2     H N N 171 
ILE HA     H N N 172 
ILE HB     H N N 173 
ILE HG12   H N N 174 
ILE HG13   H N N 175 
ILE HG21   H N N 176 
ILE HG22   H N N 177 
ILE HG23   H N N 178 
ILE HD11   H N N 179 
ILE HD12   H N N 180 
ILE HD13   H N N 181 
ILE HXT    H N N 182 
LEU N      N N N 183 
LEU CA     C N S 184 
LEU C      C N N 185 
LEU O      O N N 186 
LEU CB     C N N 187 
LEU CG     C N N 188 
LEU CD1    C N N 189 
LEU CD2    C N N 190 
LEU OXT    O N N 191 
LEU H      H N N 192 
LEU H2     H N N 193 
LEU HA     H N N 194 
LEU HB2    H N N 195 
LEU HB3    H N N 196 
LEU HG     H N N 197 
LEU HD11   H N N 198 
LEU HD12   H N N 199 
LEU HD13   H N N 200 
LEU HD21   H N N 201 
LEU HD22   H N N 202 
LEU HD23   H N N 203 
LEU HXT    H N N 204 
LLP N1     N Y N 205 
LLP C2     C Y N 206 
LLP "C2'"  C N N 207 
LLP C3     C Y N 208 
LLP O3     O N N 209 
LLP C4     C Y N 210 
LLP "C4'"  C N N 211 
LLP C5     C Y N 212 
LLP C6     C Y N 213 
LLP "C5'"  C N N 214 
LLP OP4    O N N 215 
LLP P      P N N 216 
LLP OP1    O N N 217 
LLP OP2    O N N 218 
LLP OP3    O N N 219 
LLP N      N N N 220 
LLP CA     C N S 221 
LLP CB     C N N 222 
LLP CG     C N N 223 
LLP CD     C N N 224 
LLP CE     C N N 225 
LLP NZ     N N N 226 
LLP C      C N N 227 
LLP O      O N N 228 
LLP OXT    O N N 229 
LLP "H2'1" H N N 230 
LLP "H2'2" H N N 231 
LLP "H2'3" H N N 232 
LLP HO3    H N N 233 
LLP "H4'1" H N N 234 
LLP H6     H N N 235 
LLP "H5'1" H N N 236 
LLP "H5'2" H N N 237 
LLP HOP2   H N N 238 
LLP HOP3   H N N 239 
LLP H      H N N 240 
LLP H2     H N N 241 
LLP HA     H N N 242 
LLP HB2    H N N 243 
LLP HB3    H N N 244 
LLP HG2    H N N 245 
LLP HG3    H N N 246 
LLP HD2    H N N 247 
LLP HD3    H N N 248 
LLP HE2    H N N 249 
LLP HE3    H N N 250 
LLP HXT    H N N 251 
LYS N      N N N 252 
LYS CA     C N S 253 
LYS C      C N N 254 
LYS O      O N N 255 
LYS CB     C N N 256 
LYS CG     C N N 257 
LYS CD     C N N 258 
LYS CE     C N N 259 
LYS NZ     N N N 260 
LYS OXT    O N N 261 
LYS H      H N N 262 
LYS H2     H N N 263 
LYS HA     H N N 264 
LYS HB2    H N N 265 
LYS HB3    H N N 266 
LYS HG2    H N N 267 
LYS HG3    H N N 268 
LYS HD2    H N N 269 
LYS HD3    H N N 270 
LYS HE2    H N N 271 
LYS HE3    H N N 272 
LYS HZ1    H N N 273 
LYS HZ2    H N N 274 
LYS HZ3    H N N 275 
LYS HXT    H N N 276 
MET N      N N N 277 
MET CA     C N S 278 
MET C      C N N 279 
MET O      O N N 280 
MET CB     C N N 281 
MET CG     C N N 282 
MET SD     S N N 283 
MET CE     C N N 284 
MET OXT    O N N 285 
MET H      H N N 286 
MET H2     H N N 287 
MET HA     H N N 288 
MET HB2    H N N 289 
MET HB3    H N N 290 
MET HG2    H N N 291 
MET HG3    H N N 292 
MET HE1    H N N 293 
MET HE2    H N N 294 
MET HE3    H N N 295 
MET HXT    H N N 296 
PHE N      N N N 297 
PHE CA     C N S 298 
PHE C      C N N 299 
PHE O      O N N 300 
PHE CB     C N N 301 
PHE CG     C Y N 302 
PHE CD1    C Y N 303 
PHE CD2    C Y N 304 
PHE CE1    C Y N 305 
PHE CE2    C Y N 306 
PHE CZ     C Y N 307 
PHE OXT    O N N 308 
PHE H      H N N 309 
PHE H2     H N N 310 
PHE HA     H N N 311 
PHE HB2    H N N 312 
PHE HB3    H N N 313 
PHE HD1    H N N 314 
PHE HD2    H N N 315 
PHE HE1    H N N 316 
PHE HE2    H N N 317 
PHE HZ     H N N 318 
PHE HXT    H N N 319 
PRO N      N N N 320 
PRO CA     C N S 321 
PRO C      C N N 322 
PRO O      O N N 323 
PRO CB     C N N 324 
PRO CG     C N N 325 
PRO CD     C N N 326 
PRO OXT    O N N 327 
PRO H      H N N 328 
PRO HA     H N N 329 
PRO HB2    H N N 330 
PRO HB3    H N N 331 
PRO HG2    H N N 332 
PRO HG3    H N N 333 
PRO HD2    H N N 334 
PRO HD3    H N N 335 
PRO HXT    H N N 336 
SER N      N N N 337 
SER CA     C N S 338 
SER C      C N N 339 
SER O      O N N 340 
SER CB     C N N 341 
SER OG     O N N 342 
SER OXT    O N N 343 
SER H      H N N 344 
SER H2     H N N 345 
SER HA     H N N 346 
SER HB2    H N N 347 
SER HB3    H N N 348 
SER HG     H N N 349 
SER HXT    H N N 350 
THR N      N N N 351 
THR CA     C N S 352 
THR C      C N N 353 
THR O      O N N 354 
THR CB     C N R 355 
THR OG1    O N N 356 
THR CG2    C N N 357 
THR OXT    O N N 358 
THR H      H N N 359 
THR H2     H N N 360 
THR HA     H N N 361 
THR HB     H N N 362 
THR HG1    H N N 363 
THR HG21   H N N 364 
THR HG22   H N N 365 
THR HG23   H N N 366 
THR HXT    H N N 367 
TRP N      N N N 368 
TRP CA     C N S 369 
TRP C      C N N 370 
TRP O      O N N 371 
TRP CB     C N N 372 
TRP CG     C Y N 373 
TRP CD1    C Y N 374 
TRP CD2    C Y N 375 
TRP NE1    N Y N 376 
TRP CE2    C Y N 377 
TRP CE3    C Y N 378 
TRP CZ2    C Y N 379 
TRP CZ3    C Y N 380 
TRP CH2    C Y N 381 
TRP OXT    O N N 382 
TRP H      H N N 383 
TRP H2     H N N 384 
TRP HA     H N N 385 
TRP HB2    H N N 386 
TRP HB3    H N N 387 
TRP HD1    H N N 388 
TRP HE1    H N N 389 
TRP HE3    H N N 390 
TRP HZ2    H N N 391 
TRP HZ3    H N N 392 
TRP HH2    H N N 393 
TRP HXT    H N N 394 
TYR N      N N N 395 
TYR CA     C N S 396 
TYR C      C N N 397 
TYR O      O N N 398 
TYR CB     C N N 399 
TYR CG     C Y N 400 
TYR CD1    C Y N 401 
TYR CD2    C Y N 402 
TYR CE1    C Y N 403 
TYR CE2    C Y N 404 
TYR CZ     C Y N 405 
TYR OH     O N N 406 
TYR OXT    O N N 407 
TYR H      H N N 408 
TYR H2     H N N 409 
TYR HA     H N N 410 
TYR HB2    H N N 411 
TYR HB3    H N N 412 
TYR HD1    H N N 413 
TYR HD2    H N N 414 
TYR HE1    H N N 415 
TYR HE2    H N N 416 
TYR HH     H N N 417 
TYR HXT    H N N 418 
VAL N      N N N 419 
VAL CA     C N S 420 
VAL C      C N N 421 
VAL O      O N N 422 
VAL CB     C N N 423 
VAL CG1    C N N 424 
VAL CG2    C N N 425 
VAL OXT    O N N 426 
VAL H      H N N 427 
VAL H2     H N N 428 
VAL HA     H N N 429 
VAL HB     H N N 430 
VAL HG11   H N N 431 
VAL HG12   H N N 432 
VAL HG13   H N N 433 
VAL HG21   H N N 434 
VAL HG22   H N N 435 
VAL HG23   H N N 436 
VAL HXT    H N N 437 
# 
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 
ALA N     CA     sing N N 1   
ALA N     H      sing N N 2   
ALA N     H2     sing N N 3   
ALA CA    C      sing N N 4   
ALA CA    CB     sing N N 5   
ALA CA    HA     sing N N 6   
ALA C     O      doub N N 7   
ALA C     OXT    sing N N 8   
ALA CB    HB1    sing N N 9   
ALA CB    HB2    sing N N 10  
ALA CB    HB3    sing N N 11  
ALA OXT   HXT    sing N N 12  
ARG N     CA     sing N N 13  
ARG N     H      sing N N 14  
ARG N     H2     sing N N 15  
ARG CA    C      sing N N 16  
ARG CA    CB     sing N N 17  
ARG CA    HA     sing N N 18  
ARG C     O      doub N N 19  
ARG C     OXT    sing N N 20  
ARG CB    CG     sing N N 21  
ARG CB    HB2    sing N N 22  
ARG CB    HB3    sing N N 23  
ARG CG    CD     sing N N 24  
ARG CG    HG2    sing N N 25  
ARG CG    HG3    sing N N 26  
ARG CD    NE     sing N N 27  
ARG CD    HD2    sing N N 28  
ARG CD    HD3    sing N N 29  
ARG NE    CZ     sing N N 30  
ARG NE    HE     sing N N 31  
ARG CZ    NH1    sing N N 32  
ARG CZ    NH2    doub N N 33  
ARG NH1   HH11   sing N N 34  
ARG NH1   HH12   sing N N 35  
ARG NH2   HH21   sing N N 36  
ARG NH2   HH22   sing N N 37  
ARG OXT   HXT    sing N N 38  
ASN N     CA     sing N N 39  
ASN N     H      sing N N 40  
ASN N     H2     sing N N 41  
ASN CA    C      sing N N 42  
ASN CA    CB     sing N N 43  
ASN CA    HA     sing N N 44  
ASN C     O      doub N N 45  
ASN C     OXT    sing N N 46  
ASN CB    CG     sing N N 47  
ASN CB    HB2    sing N N 48  
ASN CB    HB3    sing N N 49  
ASN CG    OD1    doub N N 50  
ASN CG    ND2    sing N N 51  
ASN ND2   HD21   sing N N 52  
ASN ND2   HD22   sing N N 53  
ASN OXT   HXT    sing N N 54  
ASP N     CA     sing N N 55  
ASP N     H      sing N N 56  
ASP N     H2     sing N N 57  
ASP CA    C      sing N N 58  
ASP CA    CB     sing N N 59  
ASP CA    HA     sing N N 60  
ASP C     O      doub N N 61  
ASP C     OXT    sing N N 62  
ASP CB    CG     sing N N 63  
ASP CB    HB2    sing N N 64  
ASP CB    HB3    sing N N 65  
ASP CG    OD1    doub N N 66  
ASP CG    OD2    sing N N 67  
ASP OD2   HD2    sing N N 68  
ASP OXT   HXT    sing N N 69  
CYS N     CA     sing N N 70  
CYS N     H      sing N N 71  
CYS N     H2     sing N N 72  
CYS CA    C      sing N N 73  
CYS CA    CB     sing N N 74  
CYS CA    HA     sing N N 75  
CYS C     O      doub N N 76  
CYS C     OXT    sing N N 77  
CYS CB    SG     sing N N 78  
CYS CB    HB2    sing N N 79  
CYS CB    HB3    sing N N 80  
CYS SG    HG     sing N N 81  
CYS OXT   HXT    sing N N 82  
GLN N     CA     sing N N 83  
GLN N     H      sing N N 84  
GLN N     H2     sing N N 85  
GLN CA    C      sing N N 86  
GLN CA    CB     sing N N 87  
GLN CA    HA     sing N N 88  
GLN C     O      doub N N 89  
GLN C     OXT    sing N N 90  
GLN CB    CG     sing N N 91  
GLN CB    HB2    sing N N 92  
GLN CB    HB3    sing N N 93  
GLN CG    CD     sing N N 94  
GLN CG    HG2    sing N N 95  
GLN CG    HG3    sing N N 96  
GLN CD    OE1    doub N N 97  
GLN CD    NE2    sing N N 98  
GLN NE2   HE21   sing N N 99  
GLN NE2   HE22   sing N N 100 
GLN OXT   HXT    sing N N 101 
GLU N     CA     sing N N 102 
GLU N     H      sing N N 103 
GLU N     H2     sing N N 104 
GLU CA    C      sing N N 105 
GLU CA    CB     sing N N 106 
GLU CA    HA     sing N N 107 
GLU C     O      doub N N 108 
GLU C     OXT    sing N N 109 
GLU CB    CG     sing N N 110 
GLU CB    HB2    sing N N 111 
GLU CB    HB3    sing N N 112 
GLU CG    CD     sing N N 113 
GLU CG    HG2    sing N N 114 
GLU CG    HG3    sing N N 115 
GLU CD    OE1    doub N N 116 
GLU CD    OE2    sing N N 117 
GLU OE2   HE2    sing N N 118 
GLU OXT   HXT    sing N N 119 
GLY N     CA     sing N N 120 
GLY N     H      sing N N 121 
GLY N     H2     sing N N 122 
GLY CA    C      sing N N 123 
GLY CA    HA2    sing N N 124 
GLY CA    HA3    sing N N 125 
GLY C     O      doub N N 126 
GLY C     OXT    sing N N 127 
GLY OXT   HXT    sing N N 128 
HIS N     CA     sing N N 129 
HIS N     H      sing N N 130 
HIS N     H2     sing N N 131 
HIS CA    C      sing N N 132 
HIS CA    CB     sing N N 133 
HIS CA    HA     sing N N 134 
HIS C     O      doub N N 135 
HIS C     OXT    sing N N 136 
HIS CB    CG     sing N N 137 
HIS CB    HB2    sing N N 138 
HIS CB    HB3    sing N N 139 
HIS CG    ND1    sing Y N 140 
HIS CG    CD2    doub Y N 141 
HIS ND1   CE1    doub Y N 142 
HIS ND1   HD1    sing N N 143 
HIS CD2   NE2    sing Y N 144 
HIS CD2   HD2    sing N N 145 
HIS CE1   NE2    sing Y N 146 
HIS CE1   HE1    sing N N 147 
HIS NE2   HE2    sing N N 148 
HIS OXT   HXT    sing N N 149 
HOH O     H1     sing N N 150 
HOH O     H2     sing N N 151 
ILE N     CA     sing N N 152 
ILE N     H      sing N N 153 
ILE N     H2     sing N N 154 
ILE CA    C      sing N N 155 
ILE CA    CB     sing N N 156 
ILE CA    HA     sing N N 157 
ILE C     O      doub N N 158 
ILE C     OXT    sing N N 159 
ILE CB    CG1    sing N N 160 
ILE CB    CG2    sing N N 161 
ILE CB    HB     sing N N 162 
ILE CG1   CD1    sing N N 163 
ILE CG1   HG12   sing N N 164 
ILE CG1   HG13   sing N N 165 
ILE CG2   HG21   sing N N 166 
ILE CG2   HG22   sing N N 167 
ILE CG2   HG23   sing N N 168 
ILE CD1   HD11   sing N N 169 
ILE CD1   HD12   sing N N 170 
ILE CD1   HD13   sing N N 171 
ILE OXT   HXT    sing N N 172 
LEU N     CA     sing N N 173 
LEU N     H      sing N N 174 
LEU N     H2     sing N N 175 
LEU CA    C      sing N N 176 
LEU CA    CB     sing N N 177 
LEU CA    HA     sing N N 178 
LEU C     O      doub N N 179 
LEU C     OXT    sing N N 180 
LEU CB    CG     sing N N 181 
LEU CB    HB2    sing N N 182 
LEU CB    HB3    sing N N 183 
LEU CG    CD1    sing N N 184 
LEU CG    CD2    sing N N 185 
LEU CG    HG     sing N N 186 
LEU CD1   HD11   sing N N 187 
LEU CD1   HD12   sing N N 188 
LEU CD1   HD13   sing N N 189 
LEU CD2   HD21   sing N N 190 
LEU CD2   HD22   sing N N 191 
LEU CD2   HD23   sing N N 192 
LEU OXT   HXT    sing N N 193 
LLP N1    C2     doub Y N 194 
LLP N1    C6     sing Y N 195 
LLP C2    "C2'"  sing N N 196 
LLP C2    C3     sing Y N 197 
LLP C3    O3     sing N N 198 
LLP C3    C4     doub Y N 199 
LLP C4    "C4'"  sing N N 200 
LLP C4    C5     sing Y N 201 
LLP "C4'" NZ     doub N N 202 
LLP C5    C6     doub Y N 203 
LLP C5    "C5'"  sing N N 204 
LLP "C5'" OP4    sing N N 205 
LLP OP4   P      sing N N 206 
LLP P     OP1    doub N N 207 
LLP P     OP2    sing N N 208 
LLP P     OP3    sing N N 209 
LLP N     CA     sing N N 210 
LLP CA    CB     sing N N 211 
LLP CA    C      sing N N 212 
LLP CB    CG     sing N N 213 
LLP CG    CD     sing N N 214 
LLP CD    CE     sing N N 215 
LLP CE    NZ     sing N N 216 
LLP C     O      doub N N 217 
LLP C     OXT    sing N N 218 
LLP "C2'" "H2'1" sing N N 219 
LLP "C2'" "H2'2" sing N N 220 
LLP "C2'" "H2'3" sing N N 221 
LLP O3    HO3    sing N N 222 
LLP "C4'" "H4'1" sing N N 223 
LLP C6    H6     sing N N 224 
LLP "C5'" "H5'1" sing N N 225 
LLP "C5'" "H5'2" sing N N 226 
LLP OP2   HOP2   sing N N 227 
LLP OP3   HOP3   sing N N 228 
LLP N     H      sing N N 229 
LLP N     H2     sing N N 230 
LLP CA    HA     sing N N 231 
LLP CB    HB2    sing N N 232 
LLP CB    HB3    sing N N 233 
LLP CG    HG2    sing N N 234 
LLP CG    HG3    sing N N 235 
LLP CD    HD2    sing N N 236 
LLP CD    HD3    sing N N 237 
LLP CE    HE2    sing N N 238 
LLP CE    HE3    sing N N 239 
LLP OXT   HXT    sing N N 240 
LYS N     CA     sing N N 241 
LYS N     H      sing N N 242 
LYS N     H2     sing N N 243 
LYS CA    C      sing N N 244 
LYS CA    CB     sing N N 245 
LYS CA    HA     sing N N 246 
LYS C     O      doub N N 247 
LYS C     OXT    sing N N 248 
LYS CB    CG     sing N N 249 
LYS CB    HB2    sing N N 250 
LYS CB    HB3    sing N N 251 
LYS CG    CD     sing N N 252 
LYS CG    HG2    sing N N 253 
LYS CG    HG3    sing N N 254 
LYS CD    CE     sing N N 255 
LYS CD    HD2    sing N N 256 
LYS CD    HD3    sing N N 257 
LYS CE    NZ     sing N N 258 
LYS CE    HE2    sing N N 259 
LYS CE    HE3    sing N N 260 
LYS NZ    HZ1    sing N N 261 
LYS NZ    HZ2    sing N N 262 
LYS NZ    HZ3    sing N N 263 
LYS OXT   HXT    sing N N 264 
MET N     CA     sing N N 265 
MET N     H      sing N N 266 
MET N     H2     sing N N 267 
MET CA    C      sing N N 268 
MET CA    CB     sing N N 269 
MET CA    HA     sing N N 270 
MET C     O      doub N N 271 
MET C     OXT    sing N N 272 
MET CB    CG     sing N N 273 
MET CB    HB2    sing N N 274 
MET CB    HB3    sing N N 275 
MET CG    SD     sing N N 276 
MET CG    HG2    sing N N 277 
MET CG    HG3    sing N N 278 
MET SD    CE     sing N N 279 
MET CE    HE1    sing N N 280 
MET CE    HE2    sing N N 281 
MET CE    HE3    sing N N 282 
MET OXT   HXT    sing N N 283 
PHE N     CA     sing N N 284 
PHE N     H      sing N N 285 
PHE N     H2     sing N N 286 
PHE CA    C      sing N N 287 
PHE CA    CB     sing N N 288 
PHE CA    HA     sing N N 289 
PHE C     O      doub N N 290 
PHE C     OXT    sing N N 291 
PHE CB    CG     sing N N 292 
PHE CB    HB2    sing N N 293 
PHE CB    HB3    sing N N 294 
PHE CG    CD1    doub Y N 295 
PHE CG    CD2    sing Y N 296 
PHE CD1   CE1    sing Y N 297 
PHE CD1   HD1    sing N N 298 
PHE CD2   CE2    doub Y N 299 
PHE CD2   HD2    sing N N 300 
PHE CE1   CZ     doub Y N 301 
PHE CE1   HE1    sing N N 302 
PHE CE2   CZ     sing Y N 303 
PHE CE2   HE2    sing N N 304 
PHE CZ    HZ     sing N N 305 
PHE OXT   HXT    sing N N 306 
PRO N     CA     sing N N 307 
PRO N     CD     sing N N 308 
PRO N     H      sing N N 309 
PRO CA    C      sing N N 310 
PRO CA    CB     sing N N 311 
PRO CA    HA     sing N N 312 
PRO C     O      doub N N 313 
PRO C     OXT    sing N N 314 
PRO CB    CG     sing N N 315 
PRO CB    HB2    sing N N 316 
PRO CB    HB3    sing N N 317 
PRO CG    CD     sing N N 318 
PRO CG    HG2    sing N N 319 
PRO CG    HG3    sing N N 320 
PRO CD    HD2    sing N N 321 
PRO CD    HD3    sing N N 322 
PRO OXT   HXT    sing N N 323 
SER N     CA     sing N N 324 
SER N     H      sing N N 325 
SER N     H2     sing N N 326 
SER CA    C      sing N N 327 
SER CA    CB     sing N N 328 
SER CA    HA     sing N N 329 
SER C     O      doub N N 330 
SER C     OXT    sing N N 331 
SER CB    OG     sing N N 332 
SER CB    HB2    sing N N 333 
SER CB    HB3    sing N N 334 
SER OG    HG     sing N N 335 
SER OXT   HXT    sing N N 336 
THR N     CA     sing N N 337 
THR N     H      sing N N 338 
THR N     H2     sing N N 339 
THR CA    C      sing N N 340 
THR CA    CB     sing N N 341 
THR CA    HA     sing N N 342 
THR C     O      doub N N 343 
THR C     OXT    sing N N 344 
THR CB    OG1    sing N N 345 
THR CB    CG2    sing N N 346 
THR CB    HB     sing N N 347 
THR OG1   HG1    sing N N 348 
THR CG2   HG21   sing N N 349 
THR CG2   HG22   sing N N 350 
THR CG2   HG23   sing N N 351 
THR OXT   HXT    sing N N 352 
TRP N     CA     sing N N 353 
TRP N     H      sing N N 354 
TRP N     H2     sing N N 355 
TRP CA    C      sing N N 356 
TRP CA    CB     sing N N 357 
TRP CA    HA     sing N N 358 
TRP C     O      doub N N 359 
TRP C     OXT    sing N N 360 
TRP CB    CG     sing N N 361 
TRP CB    HB2    sing N N 362 
TRP CB    HB3    sing N N 363 
TRP CG    CD1    doub Y N 364 
TRP CG    CD2    sing Y N 365 
TRP CD1   NE1    sing Y N 366 
TRP CD1   HD1    sing N N 367 
TRP CD2   CE2    doub Y N 368 
TRP CD2   CE3    sing Y N 369 
TRP NE1   CE2    sing Y N 370 
TRP NE1   HE1    sing N N 371 
TRP CE2   CZ2    sing Y N 372 
TRP CE3   CZ3    doub Y N 373 
TRP CE3   HE3    sing N N 374 
TRP CZ2   CH2    doub Y N 375 
TRP CZ2   HZ2    sing N N 376 
TRP CZ3   CH2    sing Y N 377 
TRP CZ3   HZ3    sing N N 378 
TRP CH2   HH2    sing N N 379 
TRP OXT   HXT    sing N N 380 
TYR N     CA     sing N N 381 
TYR N     H      sing N N 382 
TYR N     H2     sing N N 383 
TYR CA    C      sing N N 384 
TYR CA    CB     sing N N 385 
TYR CA    HA     sing N N 386 
TYR C     O      doub N N 387 
TYR C     OXT    sing N N 388 
TYR CB    CG     sing N N 389 
TYR CB    HB2    sing N N 390 
TYR CB    HB3    sing N N 391 
TYR CG    CD1    doub Y N 392 
TYR CG    CD2    sing Y N 393 
TYR CD1   CE1    sing Y N 394 
TYR CD1   HD1    sing N N 395 
TYR CD2   CE2    doub Y N 396 
TYR CD2   HD2    sing N N 397 
TYR CE1   CZ     doub Y N 398 
TYR CE1   HE1    sing N N 399 
TYR CE2   CZ     sing Y N 400 
TYR CE2   HE2    sing N N 401 
TYR CZ    OH     sing N N 402 
TYR OH    HH     sing N N 403 
TYR OXT   HXT    sing N N 404 
VAL N     CA     sing N N 405 
VAL N     H      sing N N 406 
VAL N     H2     sing N N 407 
VAL CA    C      sing N N 408 
VAL CA    CB     sing N N 409 
VAL CA    HA     sing N N 410 
VAL C     O      doub N N 411 
VAL C     OXT    sing N N 412 
VAL CB    CG1    sing N N 413 
VAL CB    CG2    sing N N 414 
VAL CB    HB     sing N N 415 
VAL CG1   HG11   sing N N 416 
VAL CG1   HG12   sing N N 417 
VAL CG1   HG13   sing N N 418 
VAL CG2   HG21   sing N N 419 
VAL CG2   HG22   sing N N 420 
VAL CG2   HG23   sing N N 421 
VAL OXT   HXT    sing N N 422 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'National Natural Science Foundation of China (NSFC)' China 32171259 1 
'National Natural Science Foundation of China (NSFC)' China 32201033 2 
# 
_atom_sites.entry_id                    8KG1 
_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]   0.008921 
_atom_sites.fract_transf_matrix[1][2]   0.005151 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.010301 
_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]   0.008277 
_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 
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 11  ? -74.644 47.650 -8.758  1.00 55.79 ? 152 ARG A N     1 
ATOM   2    C CA    . ARG A 1 11  ? -74.611 47.145 -10.128 1.00 49.06 ? 152 ARG A CA    1 
ATOM   3    C C     . ARG A 1 11  ? -73.461 46.171 -10.315 1.00 48.30 ? 152 ARG A C     1 
ATOM   4    O O     . ARG A 1 11  ? -72.541 46.114 -9.495  1.00 53.50 ? 152 ARG A O     1 
ATOM   5    C CB    . ARG A 1 11  ? -74.459 48.281 -11.148 1.00 44.10 ? 152 ARG A CB    1 
ATOM   6    C CG    . ARG A 1 11  ? -75.404 49.447 -10.991 1.00 37.60 ? 152 ARG A CG    1 
ATOM   7    C CD    . ARG A 1 11  ? -75.885 49.943 -12.344 1.00 31.69 ? 152 ARG A CD    1 
ATOM   8    N NE    . ARG A 1 11  ? -74.800 50.434 -13.190 1.00 30.93 ? 152 ARG A NE    1 
ATOM   9    C CZ    . ARG A 1 11  ? -74.824 50.417 -14.517 1.00 29.06 ? 152 ARG A CZ    1 
ATOM   10   N NH1   . ARG A 1 11  ? -75.849 49.912 -15.185 1.00 29.75 ? 152 ARG A NH1   1 
ATOM   11   N NH2   . ARG A 1 11  ? -73.804 50.935 -15.194 1.00 24.67 ? 152 ARG A NH2   1 
ATOM   12   N N     . HIS A 1 12  ? -73.523 45.427 -11.418 1.00 43.69 ? 153 HIS A N     1 
ATOM   13   C CA    . HIS A 1 12  ? -72.475 44.512 -11.866 1.00 40.78 ? 153 HIS A CA    1 
ATOM   14   C C     . HIS A 1 12  ? -72.261 43.338 -10.919 1.00 42.37 ? 153 HIS A C     1 
ATOM   15   O O     . HIS A 1 12  ? -71.242 42.650 -11.008 1.00 39.71 ? 153 HIS A O     1 
ATOM   16   C CB    . HIS A 1 12  ? -71.146 45.241 -12.109 1.00 42.69 ? 153 HIS A CB    1 
ATOM   17   C CG    . HIS A 1 12  ? -71.279 46.462 -12.964 1.00 42.44 ? 153 HIS A CG    1 
ATOM   18   N ND1   . HIS A 1 12  ? -72.200 46.556 -13.989 1.00 34.48 ? 153 HIS A ND1   1 
ATOM   19   C CD2   . HIS A 1 12  ? -70.591 47.630 -12.966 1.00 32.40 ? 153 HIS A CD2   1 
ATOM   20   C CE1   . HIS A 1 12  ? -72.088 47.738 -14.570 1.00 33.16 ? 153 HIS A CE1   1 
ATOM   21   N NE2   . HIS A 1 12  ? -71.118 48.408 -13.970 1.00 33.21 ? 153 HIS A NE2   1 
ATOM   22   N N     . GLU A 1 13  ? -73.204 43.080 -10.013 1.00 42.93 ? 154 GLU A N     1 
ATOM   23   C CA    . GLU A 1 13  ? -73.212 41.796 -9.321  1.00 43.97 ? 154 GLU A CA    1 
ATOM   24   C C     . GLU A 1 13  ? -73.272 40.653 -10.328 1.00 40.90 ? 154 GLU A C     1 
ATOM   25   O O     . GLU A 1 13  ? -72.472 39.711 -10.272 1.00 41.66 ? 154 GLU A O     1 
ATOM   26   C CB    . GLU A 1 13  ? -74.395 41.729 -8.357  1.00 48.43 ? 154 GLU A CB    1 
ATOM   27   C CG    . GLU A 1 13  ? -74.370 40.509 -7.465  1.00 59.13 ? 154 GLU A CG    1 
ATOM   28   C CD    . GLU A 1 13  ? -74.652 40.861 -6.024  1.00 65.62 ? 154 GLU A CD    1 
ATOM   29   O OE1   . GLU A 1 13  ? -75.797 40.644 -5.561  1.00 64.97 ? 154 GLU A OE1   1 
ATOM   30   O OE2   . GLU A 1 13  ? -73.735 41.395 -5.370  1.00 64.39 ? 154 GLU A OE2   1 
ATOM   31   N N     . ILE A 1 14  ? -74.224 40.727 -11.262 1.00 35.77 ? 155 ILE A N     1 
ATOM   32   C CA    . ILE A 1 14  ? -74.307 39.837 -12.414 1.00 38.21 ? 155 ILE A CA    1 
ATOM   33   C C     . ILE A 1 14  ? -73.756 40.579 -13.622 1.00 35.22 ? 155 ILE A C     1 
ATOM   34   O O     . ILE A 1 14  ? -73.886 41.805 -13.740 1.00 33.56 ? 155 ILE A O     1 
ATOM   35   C CB    . ILE A 1 14  ? -75.759 39.370 -12.668 1.00 39.54 ? 155 ILE A CB    1 
ATOM   36   C CG1   . ILE A 1 14  ? -76.649 40.573 -12.981 1.00 37.72 ? 155 ILE A CG1   1 
ATOM   37   C CG2   . ILE A 1 14  ? -76.312 38.636 -11.444 1.00 39.51 ? 155 ILE A CG2   1 
ATOM   38   C CD1   . ILE A 1 14  ? -77.626 40.345 -14.090 1.00 42.37 ? 155 ILE A CD1   1 
ATOM   39   N N     . PHE A 1 15  ? -73.148 39.833 -14.539 1.00 33.12 ? 156 PHE A N     1 
ATOM   40   C CA    . PHE A 1 15  ? -72.583 40.407 -15.759 1.00 27.47 ? 156 PHE A CA    1 
ATOM   41   C C     . PHE A 1 15  ? -73.689 40.639 -16.792 1.00 26.64 ? 156 PHE A C     1 
ATOM   42   O O     . PHE A 1 15  ? -74.410 39.707 -17.163 1.00 24.78 ? 156 PHE A O     1 
ATOM   43   C CB    . PHE A 1 15  ? -71.510 39.473 -16.317 1.00 25.86 ? 156 PHE A CB    1 
ATOM   44   C CG    . PHE A 1 15  ? -70.769 40.026 -17.496 1.00 25.26 ? 156 PHE A CG    1 
ATOM   45   C CD1   . PHE A 1 15  ? -71.322 39.982 -18.770 1.00 24.15 ? 156 PHE A CD1   1 
ATOM   46   C CD2   . PHE A 1 15  ? -69.509 40.575 -17.330 1.00 25.64 ? 156 PHE A CD2   1 
ATOM   47   C CE1   . PHE A 1 15  ? -70.634 40.491 -19.856 1.00 22.68 ? 156 PHE A CE1   1 
ATOM   48   C CE2   . PHE A 1 15  ? -68.806 41.076 -18.416 1.00 28.14 ? 156 PHE A CE2   1 
ATOM   49   C CZ    . PHE A 1 15  ? -69.377 41.034 -19.686 1.00 25.67 ? 156 PHE A CZ    1 
ATOM   50   N N     . ASP A 1 16  ? -73.823 41.875 -17.263 1.00 23.74 ? 157 ASP A N     1 
ATOM   51   C CA    . ASP A 1 16  ? -74.755 42.184 -18.346 1.00 23.88 ? 157 ASP A CA    1 
ATOM   52   C C     . ASP A 1 16  ? -74.113 43.247 -19.216 1.00 23.01 ? 157 ASP A C     1 
ATOM   53   O O     . ASP A 1 16  ? -73.798 44.337 -18.722 1.00 22.99 ? 157 ASP A O     1 
ATOM   54   C CB    . ASP A 1 16  ? -76.107 42.681 -17.824 1.00 23.40 ? 157 ASP A CB    1 
ATOM   55   C CG    . ASP A 1 16  ? -77.071 43.039 -18.966 1.00 31.80 ? 157 ASP A CG    1 
ATOM   56   O OD1   . ASP A 1 16  ? -76.860 44.073 -19.637 1.00 35.63 ? 157 ASP A OD1   1 
ATOM   57   O OD2   . ASP A 1 16  ? -78.034 42.283 -19.202 1.00 41.47 ? 157 ASP A OD2   1 
ATOM   58   N N     . VAL A 1 17  ? -73.929 42.945 -20.503 1.00 20.74 ? 158 VAL A N     1 
ATOM   59   C CA    . VAL A 1 17  ? -73.116 43.847 -21.313 1.00 20.69 ? 158 VAL A CA    1 
ATOM   60   C C     . VAL A 1 17  ? -73.781 45.218 -21.481 1.00 24.24 ? 158 VAL A C     1 
ATOM   61   O O     . VAL A 1 17  ? -73.078 46.229 -21.603 1.00 19.34 ? 158 VAL A O     1 
ATOM   62   C CB    . VAL A 1 17  ? -72.768 43.206 -22.675 1.00 26.11 ? 158 VAL A CB    1 
ATOM   63   C CG1   . VAL A 1 17  ? -73.975 43.164 -23.596 1.00 22.80 ? 158 VAL A CG1   1 
ATOM   64   C CG2   . VAL A 1 17  ? -71.624 43.982 -23.352 1.00 18.18 ? 158 VAL A CG2   1 
ATOM   65   N N     . ASN A 1 18  ? -75.120 45.304 -21.481 1.00 21.18 ? 159 ASN A N     1 
ATOM   66   C CA    . ASN A 1 18  ? -75.713 46.635 -21.634 1.00 24.67 ? 159 ASN A CA    1 
ATOM   67   C C     . ASN A 1 18  ? -75.546 47.479 -20.380 1.00 20.75 ? 159 ASN A C     1 
ATOM   68   O O     . ASN A 1 18  ? -75.281 48.687 -20.474 1.00 22.01 ? 159 ASN A O     1 
ATOM   69   C CB    . ASN A 1 18  ? -77.189 46.569 -22.040 1.00 29.65 ? 159 ASN A CB    1 
ATOM   70   C CG    . ASN A 1 18  ? -77.388 45.891 -23.381 1.00 34.94 ? 159 ASN A CG    1 
ATOM   71   O OD1   . ASN A 1 18  ? -76.971 46.411 -24.411 1.00 35.01 ? 159 ASN A OD1   1 
ATOM   72   N ND2   . ASN A 1 18  ? -78.126 44.807 -23.387 1.00 41.75 ? 159 ASN A ND2   1 
ATOM   73   N N     . ALA A 1 19  ? -75.687 46.867 -19.202 1.00 22.19 ? 160 ALA A N     1 
ATOM   74   C CA    . ALA A 1 19  ? -75.360 47.570 -17.964 1.00 24.60 ? 160 ALA A CA    1 
ATOM   75   C C     . ALA A 1 19  ? -73.920 48.082 -17.994 1.00 22.13 ? 160 ALA A C     1 
ATOM   76   O O     . ALA A 1 19  ? -73.655 49.247 -17.676 1.00 22.39 ? 160 ALA A O     1 
ATOM   77   C CB    . ALA A 1 19  ? -75.595 46.650 -16.760 1.00 22.39 ? 160 ALA A CB    1 
ATOM   78   N N     . ILE A 1 20  ? -72.978 47.233 -18.410 1.00 21.29 ? 161 ILE A N     1 
ATOM   79   C CA    . ILE A 1 20  ? -71.570 47.636 -18.459 1.00 19.36 ? 161 ILE A CA    1 
ATOM   80   C C     . ILE A 1 20  ? -71.378 48.792 -19.434 1.00 20.43 ? 161 ILE A C     1 
ATOM   81   O O     . ILE A 1 20  ? -70.765 49.815 -19.100 1.00 17.04 ? 161 ILE A O     1 
ATOM   82   C CB    . ILE A 1 20  ? -70.683 46.435 -18.829 1.00 21.93 ? 161 ILE A CB    1 
ATOM   83   C CG1   . ILE A 1 20  ? -70.503 45.529 -17.617 1.00 28.59 ? 161 ILE A CG1   1 
ATOM   84   C CG2   . ILE A 1 20  ? -69.329 46.900 -19.325 1.00 20.83 ? 161 ILE A CG2   1 
ATOM   85   C CD1   . ILE A 1 20  ? -70.319 44.092 -17.978 1.00 29.25 ? 161 ILE A CD1   1 
ATOM   86   N N     . ARG A 1 21  ? -71.927 48.655 -20.646 1.00 19.99 ? 162 ARG A N     1 
ATOM   87   C CA    . ARG A 1 21  ? -71.772 49.681 -21.677 1.00 18.79 ? 162 ARG A CA    1 
ATOM   88   C C     . ARG A 1 21  ? -72.271 51.031 -21.197 1.00 22.33 ? 162 ARG A C     1 
ATOM   89   O O     . ARG A 1 21  ? -71.716 52.077 -21.564 1.00 20.24 ? 162 ARG A O     1 
ATOM   90   C CB    . ARG A 1 21  ? -72.536 49.284 -22.944 1.00 20.15 ? 162 ARG A CB    1 
ATOM   91   C CG    . ARG A 1 21  ? -71.930 48.145 -23.734 1.00 21.24 ? 162 ARG A CG    1 
ATOM   92   C CD    . ARG A 1 21  ? -72.813 47.782 -24.956 1.00 19.93 ? 162 ARG A CD    1 
ATOM   93   N NE    . ARG A 1 21  ? -73.063 48.922 -25.834 1.00 20.47 ? 162 ARG A NE    1 
ATOM   94   C CZ    . ARG A 1 21  ? -72.281 49.285 -26.847 1.00 24.39 ? 162 ARG A CZ    1 
ATOM   95   N NH1   . ARG A 1 21  ? -71.162 48.636 -27.127 1.00 19.42 ? 162 ARG A NH1   1 
ATOM   96   N NH2   . ARG A 1 21  ? -72.637 50.321 -27.608 1.00 21.56 ? 162 ARG A NH2   1 
ATOM   97   N N     . ALA A 1 22  ? -73.331 51.028 -20.384 1.00 20.47 ? 163 ALA A N     1 
ATOM   98   C CA    . ALA A 1 22  ? -73.886 52.288 -19.902 1.00 25.25 ? 163 ALA A CA    1 
ATOM   99   C C     . ALA A 1 22  ? -72.890 53.093 -19.067 1.00 22.64 ? 163 ALA A C     1 
ATOM   100  O O     . ALA A 1 22  ? -73.078 54.305 -18.905 1.00 24.50 ? 163 ALA A O     1 
ATOM   101  C CB    . ALA A 1 22  ? -75.159 52.017 -19.085 1.00 25.50 ? 163 ALA A CB    1 
ATOM   102  N N     . ASP A 1 23  ? -71.850 52.454 -18.525 1.00 20.32 ? 164 ASP A N     1 
ATOM   103  C CA    . ASP A 1 23  ? -70.816 53.160 -17.775 1.00 22.51 ? 164 ASP A CA    1 
ATOM   104  C C     . ASP A 1 23  ? -69.845 53.933 -18.662 1.00 20.84 ? 164 ASP A C     1 
ATOM   105  O O     . ASP A 1 23  ? -69.077 54.756 -18.142 1.00 21.37 ? 164 ASP A O     1 
ATOM   106  C CB    . ASP A 1 23  ? -70.007 52.175 -16.926 1.00 19.29 ? 164 ASP A CB    1 
ATOM   107  C CG    . ASP A 1 23  ? -70.813 51.595 -15.773 1.00 22.23 ? 164 ASP A CG    1 
ATOM   108  O OD1   . ASP A 1 23  ? -71.652 52.327 -15.196 1.00 22.33 ? 164 ASP A OD1   1 
ATOM   109  O OD2   . ASP A 1 23  ? -70.583 50.418 -15.420 1.00 20.10 ? 164 ASP A OD2   1 
ATOM   110  N N     . PHE A 1 24  ? -69.845 53.684 -19.970 1.00 19.61 ? 165 PHE A N     1 
ATOM   111  C CA    . PHE A 1 24  ? -68.838 54.233 -20.875 1.00 20.14 ? 165 PHE A CA    1 
ATOM   112  C C     . PHE A 1 24  ? -69.482 55.305 -21.743 1.00 19.44 ? 165 PHE A C     1 
ATOM   113  O O     . PHE A 1 24  ? -70.086 54.982 -22.778 1.00 19.76 ? 165 PHE A O     1 
ATOM   114  C CB    . PHE A 1 24  ? -68.223 53.124 -21.747 1.00 17.57 ? 165 PHE A CB    1 
ATOM   115  C CG    . PHE A 1 24  ? -67.355 52.164 -20.982 1.00 17.84 ? 165 PHE A CG    1 
ATOM   116  C CD1   . PHE A 1 24  ? -67.921 51.125 -20.246 1.00 18.82 ? 165 PHE A CD1   1 
ATOM   117  C CD2   . PHE A 1 24  ? -65.969 52.322 -20.957 1.00 16.01 ? 165 PHE A CD2   1 
ATOM   118  C CE1   . PHE A 1 24  ? -67.118 50.251 -19.514 1.00 18.84 ? 165 PHE A CE1   1 
ATOM   119  C CE2   . PHE A 1 24  ? -65.165 51.461 -20.230 1.00 15.31 ? 165 PHE A CE2   1 
ATOM   120  C CZ    . PHE A 1 24  ? -65.736 50.422 -19.506 1.00 17.42 ? 165 PHE A CZ    1 
ATOM   121  N N     . PRO A 1 25  ? -69.361 56.589 -21.388 1.00 20.78 ? 166 PRO A N     1 
ATOM   122  C CA    . PRO A 1 25  ? -70.137 57.621 -22.110 1.00 20.00 ? 166 PRO A CA    1 
ATOM   123  C C     . PRO A 1 25  ? -69.831 57.703 -23.603 1.00 26.49 ? 166 PRO A C     1 
ATOM   124  O O     . PRO A 1 25  ? -70.755 57.910 -24.410 1.00 23.18 ? 166 PRO A O     1 
ATOM   125  C CB    . PRO A 1 25  ? -69.763 58.922 -21.377 1.00 21.73 ? 166 PRO A CB    1 
ATOM   126  C CG    . PRO A 1 25  ? -68.466 58.614 -20.634 1.00 20.98 ? 166 PRO A CG    1 
ATOM   127  C CD    . PRO A 1 25  ? -68.556 57.152 -20.283 1.00 19.22 ? 166 PRO A CD    1 
ATOM   128  N N     . ILE A 1 26  ? -68.572 57.502 -24.008 1.00 19.96 ? 167 ILE A N     1 
ATOM   129  C CA    . ILE A 1 26  ? -68.230 57.656 -25.424 1.00 20.72 ? 167 ILE A CA    1 
ATOM   130  C C     . ILE A 1 26  ? -68.934 56.628 -26.291 1.00 21.96 ? 167 ILE A C     1 
ATOM   131  O O     . ILE A 1 26  ? -69.025 56.808 -27.511 1.00 23.01 ? 167 ILE A O     1 
ATOM   132  C CB    . ILE A 1 26  ? -66.699 57.586 -25.646 1.00 22.47 ? 167 ILE A CB    1 
ATOM   133  C CG1   . ILE A 1 26  ? -66.287 58.413 -26.878 1.00 21.26 ? 167 ILE A CG1   1 
ATOM   134  C CG2   . ILE A 1 26  ? -66.239 56.140 -25.812 1.00 18.13 ? 167 ILE A CG2   1 
ATOM   135  C CD1   . ILE A 1 26  ? -64.860 58.865 -26.838 1.00 18.51 ? 167 ILE A CD1   1 
ATOM   136  N N     . LEU A 1 27  ? -69.445 55.547 -25.694 1.00 20.65 ? 168 LEU A N     1 
ATOM   137  C CA    . LEU A 1 27  ? -70.118 54.523 -26.484 1.00 21.86 ? 168 LEU A CA    1 
ATOM   138  C C     . LEU A 1 27  ? -71.474 54.979 -27.009 1.00 29.82 ? 168 LEU A C     1 
ATOM   139  O O     . LEU A 1 27  ? -72.071 54.270 -27.829 1.00 25.39 ? 168 LEU A O     1 
ATOM   140  C CB    . LEU A 1 27  ? -70.287 53.245 -25.661 1.00 21.06 ? 168 LEU A CB    1 
ATOM   141  C CG    . LEU A 1 27  ? -68.986 52.515 -25.313 1.00 24.29 ? 168 LEU A CG    1 
ATOM   142  C CD1   . LEU A 1 27  ? -69.307 51.180 -24.609 1.00 22.63 ? 168 LEU A CD1   1 
ATOM   143  C CD2   . LEU A 1 27  ? -68.133 52.290 -26.560 1.00 21.46 ? 168 LEU A CD2   1 
ATOM   144  N N     . ARG A 1 28  ? -71.980 56.131 -26.564 1.00 29.15 ? 169 ARG A N     1 
ATOM   145  C CA    . ARG A 1 28  ? -73.187 56.683 -27.161 1.00 31.13 ? 169 ARG A CA    1 
ATOM   146  C C     . ARG A 1 28  ? -72.864 57.712 -28.238 1.00 29.80 ? 169 ARG A C     1 
ATOM   147  O O     . ARG A 1 28  ? -73.777 58.319 -28.803 1.00 32.16 ? 169 ARG A O     1 
ATOM   148  C CB    . ARG A 1 28  ? -74.102 57.270 -26.073 1.00 29.28 ? 169 ARG A CB    1 
ATOM   149  C CG    . ARG A 1 28  ? -74.582 56.195 -25.061 1.00 32.61 ? 169 ARG A CG    1 
ATOM   150  C CD    . ARG A 1 28  ? -76.022 56.372 -24.565 1.00 37.81 ? 169 ARG A CD    1 
ATOM   151  N NE    . ARG A 1 28  ? -76.278 55.646 -23.321 1.00 38.95 ? 169 ARG A NE    1 
ATOM   152  C CZ    . ARG A 1 28  ? -77.042 54.563 -23.218 1.00 38.44 ? 169 ARG A CZ    1 
ATOM   153  N NH1   . ARG A 1 28  ? -77.670 54.057 -24.268 1.00 31.74 ? 169 ARG A NH1   1 
ATOM   154  N NH2   . ARG A 1 28  ? -77.173 53.967 -22.032 1.00 32.31 ? 169 ARG A NH2   1 
ATOM   155  N N     . GLU A 1 29  ? -71.590 57.890 -28.567 1.00 27.94 ? 170 GLU A N     1 
ATOM   156  C CA    . GLU A 1 29  ? -71.216 58.838 -29.604 1.00 29.70 ? 170 GLU A CA    1 
ATOM   157  C C     . GLU A 1 29  ? -71.621 58.324 -30.988 1.00 35.80 ? 170 GLU A C     1 
ATOM   158  O O     . GLU A 1 29  ? -71.802 57.119 -31.217 1.00 25.31 ? 170 GLU A O     1 
ATOM   159  C CB    . GLU A 1 29  ? -69.712 59.115 -29.551 1.00 31.06 ? 170 GLU A CB    1 
ATOM   160  C CG    . GLU A 1 29  ? -69.284 60.401 -30.221 1.00 34.84 ? 170 GLU A CG    1 
ATOM   161  C CD    . GLU A 1 29  ? -69.372 61.622 -29.315 1.00 36.37 ? 170 GLU A CD    1 
ATOM   162  O OE1   . GLU A 1 29  ? -69.728 61.488 -28.120 1.00 36.92 ? 170 GLU A OE1   1 
ATOM   163  O OE2   . GLU A 1 29  ? -69.081 62.729 -29.811 1.00 32.09 ? 170 GLU A OE2   1 
ATOM   164  N N     . THR A 1 30  ? -71.764 59.267 -31.920 1.00 35.53 ? 171 THR A N     1 
ATOM   165  C CA    . THR A 1 30  ? -72.220 58.989 -33.274 1.00 37.97 ? 171 THR A CA    1 
ATOM   166  C C     . THR A 1 30  ? -71.095 59.284 -34.263 1.00 33.84 ? 171 THR A C     1 
ATOM   167  O O     . THR A 1 30  ? -70.337 60.238 -34.088 1.00 37.33 ? 171 THR A O     1 
ATOM   168  C CB    . THR A 1 30  ? -73.482 59.819 -33.592 1.00 37.00 ? 171 THR A CB    1 
ATOM   169  O OG1   . THR A 1 30  ? -74.640 59.167 -33.053 1.00 38.22 ? 171 THR A OG1   1 
ATOM   170  C CG2   . THR A 1 30  ? -73.683 59.965 -35.062 1.00 40.39 ? 171 THR A CG2   1 
ATOM   171  N N     . VAL A 1 31  ? -70.977 58.449 -35.291 1.00 32.35 ? 172 VAL A N     1 
ATOM   172  C CA    . VAL A 1 31  ? -69.948 58.594 -36.314 1.00 40.08 ? 172 VAL A CA    1 
ATOM   173  C C     . VAL A 1 31  ? -70.640 58.589 -37.663 1.00 39.59 ? 172 VAL A C     1 
ATOM   174  O O     . VAL A 1 31  ? -71.272 57.591 -38.029 1.00 40.32 ? 172 VAL A O     1 
ATOM   175  C CB    . VAL A 1 31  ? -68.905 57.464 -36.248 1.00 36.90 ? 172 VAL A CB    1 
ATOM   176  C CG1   . VAL A 1 31  ? -67.971 57.524 -37.458 1.00 36.21 ? 172 VAL A CG1   1 
ATOM   177  C CG2   . VAL A 1 31  ? -68.132 57.528 -34.942 1.00 38.17 ? 172 VAL A CG2   1 
ATOM   178  N N     . ASN A 1 32  ? -70.529 59.696 -38.401 1.00 47.03 ? 173 ASN A N     1 
ATOM   179  C CA    . ASN A 1 32  ? -71.130 59.797 -39.733 1.00 47.03 ? 173 ASN A CA    1 
ATOM   180  C C     . ASN A 1 32  ? -72.631 59.518 -39.694 1.00 50.63 ? 173 ASN A C     1 
ATOM   181  O O     . ASN A 1 32  ? -73.196 58.962 -40.635 1.00 54.11 ? 173 ASN A O     1 
ATOM   182  C CB    . ASN A 1 32  ? -70.435 58.848 -40.720 1.00 50.25 ? 173 ASN A CB    1 
ATOM   183  C CG    . ASN A 1 32  ? -70.842 59.093 -42.162 1.00 59.09 ? 173 ASN A CG    1 
ATOM   184  O OD1   . ASN A 1 32  ? -71.020 60.235 -42.583 1.00 63.93 ? 173 ASN A OD1   1 
ATOM   185  N ND2   . ASN A 1 32  ? -71.009 58.013 -42.924 1.00 55.49 ? 173 ASN A ND2   1 
ATOM   186  N N     . GLY A 1 33  ? -73.295 59.881 -38.599 1.00 47.85 ? 174 GLY A N     1 
ATOM   187  C CA    . GLY A 1 33  ? -74.703 59.572 -38.453 1.00 40.85 ? 174 GLY A CA    1 
ATOM   188  C C     . GLY A 1 33  ? -75.016 58.166 -37.986 1.00 43.14 ? 174 GLY A C     1 
ATOM   189  O O     . GLY A 1 33  ? -76.198 57.843 -37.806 1.00 41.05 ? 174 GLY A O     1 
ATOM   190  N N     . LYS A 1 34  ? -74.003 57.325 -37.767 1.00 38.79 ? 175 LYS A N     1 
ATOM   191  C CA    . LYS A 1 34  ? -74.147 55.937 -37.350 1.00 35.52 ? 175 LYS A CA    1 
ATOM   192  C C     . LYS A 1 34  ? -73.639 55.750 -35.922 1.00 36.61 ? 175 LYS A C     1 
ATOM   193  O O     . LYS A 1 34  ? -72.797 56.517 -35.440 1.00 33.90 ? 175 LYS A O     1 
ATOM   194  C CB    . LYS A 1 34  ? -73.365 54.991 -38.282 1.00 37.32 ? 175 LYS A CB    1 
ATOM   195  C CG    . LYS A 1 34  ? -73.954 54.755 -39.681 1.00 44.64 ? 175 LYS A CG    1 
ATOM   196  C CD    . LYS A 1 34  ? -73.841 55.980 -40.568 1.00 49.13 ? 175 LYS A CD    1 
ATOM   197  C CE    . LYS A 1 34  ? -74.222 55.699 -42.020 1.00 55.23 ? 175 LYS A CE    1 
ATOM   198  N NZ    . LYS A 1 34  ? -73.231 54.820 -42.697 1.00 49.15 ? 175 LYS A NZ    1 
ATOM   199  N N     . PRO A 1 35  ? -74.105 54.720 -35.224 1.00 32.54 ? 176 PRO A N     1 
ATOM   200  C CA    . PRO A 1 35  ? -73.543 54.431 -33.902 1.00 32.16 ? 176 PRO A CA    1 
ATOM   201  C C     . PRO A 1 35  ? -72.062 54.091 -34.005 1.00 31.31 ? 176 PRO A C     1 
ATOM   202  O O     . PRO A 1 35  ? -71.620 53.412 -34.935 1.00 29.79 ? 176 PRO A O     1 
ATOM   203  C CB    . PRO A 1 35  ? -74.368 53.232 -33.417 1.00 33.42 ? 176 PRO A CB    1 
ATOM   204  C CG    . PRO A 1 35  ? -75.613 53.235 -34.276 1.00 35.26 ? 176 PRO A CG    1 
ATOM   205  C CD    . PRO A 1 35  ? -75.184 53.785 -35.590 1.00 36.52 ? 176 PRO A CD    1 
ATOM   206  N N     . LEU A 1 36  ? -71.292 54.592 -33.047 1.00 28.50 ? 177 LEU A N     1 
ATOM   207  C CA    . LEU A 1 36  ? -69.901 54.187 -32.934 1.00 26.85 ? 177 LEU A CA    1 
ATOM   208  C C     . LEU A 1 36  ? -69.816 52.719 -32.554 1.00 24.37 ? 177 LEU A C     1 
ATOM   209  O O     . LEU A 1 36  ? -70.549 52.245 -31.684 1.00 25.73 ? 177 LEU A O     1 
ATOM   210  C CB    . LEU A 1 36  ? -69.176 55.027 -31.882 1.00 24.18 ? 177 LEU A CB    1 
ATOM   211  C CG    . LEU A 1 36  ? -67.772 54.532 -31.497 1.00 20.88 ? 177 LEU A CG    1 
ATOM   212  C CD1   . LEU A 1 36  ? -66.805 54.766 -32.643 1.00 19.30 ? 177 LEU A CD1   1 
ATOM   213  C CD2   . LEU A 1 36  ? -67.281 55.205 -30.213 1.00 19.53 ? 177 LEU A CD2   1 
ATOM   214  N N     . ILE A 1 37  ? -68.906 52.001 -33.197 1.00 19.82 ? 178 ILE A N     1 
ATOM   215  C CA    . ILE A 1 37  ? -68.579 50.630 -32.820 1.00 22.25 ? 178 ILE A CA    1 
ATOM   216  C C     . ILE A 1 37  ? -67.069 50.589 -32.599 1.00 20.36 ? 178 ILE A C     1 
ATOM   217  O O     . ILE A 1 37  ? -66.289 50.622 -33.558 1.00 19.92 ? 178 ILE A O     1 
ATOM   218  C CB    . ILE A 1 37  ? -69.021 49.622 -33.883 1.00 23.89 ? 178 ILE A CB    1 
ATOM   219  C CG1   . ILE A 1 37  ? -70.549 49.629 -34.002 1.00 24.02 ? 178 ILE A CG1   1 
ATOM   220  C CG2   . ILE A 1 37  ? -68.489 48.232 -33.551 1.00 21.08 ? 178 ILE A CG2   1 
ATOM   221  C CD1   . ILE A 1 37  ? -71.083 48.707 -35.078 1.00 21.11 ? 178 ILE A CD1   1 
ATOM   222  N N     . TRP A 1 38  ? -66.648 50.524 -31.341 1.00 18.05 ? 179 TRP A N     1 
ATOM   223  C CA    . TRP A 1 38  ? -65.232 50.630 -30.991 1.00 17.85 ? 179 TRP A CA    1 
ATOM   224  C C     . TRP A 1 38  ? -64.609 49.242 -31.004 1.00 19.95 ? 179 TRP A C     1 
ATOM   225  O O     . TRP A 1 38  ? -64.649 48.514 -30.009 1.00 18.67 ? 179 TRP A O     1 
ATOM   226  C CB    . TRP A 1 38  ? -65.052 51.302 -29.634 1.00 19.52 ? 179 TRP A CB    1 
ATOM   227  C CG    . TRP A 1 38  ? -63.592 51.564 -29.331 1.00 18.03 ? 179 TRP A CG    1 
ATOM   228  C CD1   . TRP A 1 38  ? -62.781 50.848 -28.492 1.00 15.29 ? 179 TRP A CD1   1 
ATOM   229  C CD2   . TRP A 1 38  ? -62.773 52.587 -29.911 1.00 14.83 ? 179 TRP A CD2   1 
ATOM   230  N NE1   . TRP A 1 38  ? -61.512 51.380 -28.498 1.00 15.94 ? 179 TRP A NE1   1 
ATOM   231  C CE2   . TRP A 1 38  ? -61.479 52.446 -29.362 1.00 19.97 ? 179 TRP A CE2   1 
ATOM   232  C CE3   . TRP A 1 38  ? -63.013 53.619 -30.828 1.00 15.65 ? 179 TRP A CE3   1 
ATOM   233  C CZ2   . TRP A 1 38  ? -60.423 53.300 -29.706 1.00 18.82 ? 179 TRP A CZ2   1 
ATOM   234  C CZ3   . TRP A 1 38  ? -61.966 54.461 -31.176 1.00 19.68 ? 179 TRP A CZ3   1 
ATOM   235  C CH2   . TRP A 1 38  ? -60.688 54.302 -30.611 1.00 17.02 ? 179 TRP A CH2   1 
ATOM   236  N N     . PHE A 1 39  ? -63.998 48.880 -32.151 1.00 15.04 ? 180 PHE A N     1 
ATOM   237  C CA    . PHE A 1 39  ? -63.207 47.660 -32.286 1.00 16.92 ? 180 PHE A CA    1 
ATOM   238  C C     . PHE A 1 39  ? -61.707 47.956 -32.359 1.00 17.97 ? 180 PHE A C     1 
ATOM   239  O O     . PHE A 1 39  ? -60.964 47.242 -33.042 1.00 17.34 ? 180 PHE A O     1 
ATOM   240  C CB    . PHE A 1 39  ? -63.633 46.870 -33.534 1.00 15.95 ? 180 PHE A CB    1 
ATOM   241  C CG    . PHE A 1 39  ? -64.962 46.173 -33.406 1.00 18.27 ? 180 PHE A CG    1 
ATOM   242  C CD1   . PHE A 1 39  ? -65.614 46.104 -32.187 1.00 16.97 ? 180 PHE A CD1   1 
ATOM   243  C CD2   . PHE A 1 39  ? -65.544 45.564 -34.514 1.00 18.42 ? 180 PHE A CD2   1 
ATOM   244  C CE1   . PHE A 1 39  ? -66.828 45.451 -32.076 1.00 19.63 ? 180 PHE A CE1   1 
ATOM   245  C CE2   . PHE A 1 39  ? -66.756 44.919 -34.411 1.00 22.25 ? 180 PHE A CE2   1 
ATOM   246  C CZ    . PHE A 1 39  ? -67.402 44.856 -33.190 1.00 20.65 ? 180 PHE A CZ    1 
ATOM   247  N N     . ASP A 1 40  ? -61.240 49.014 -31.683 1.00 18.42 ? 181 ASP A N     1 
ATOM   248  C CA    . ASP A 1 40  ? -59.832 49.416 -31.735 1.00 16.91 ? 181 ASP A CA    1 
ATOM   249  C C     . ASP A 1 40  ? -59.184 49.311 -30.359 1.00 18.66 ? 181 ASP A C     1 
ATOM   250  O O     . ASP A 1 40  ? -58.286 50.092 -30.020 1.00 14.26 ? 181 ASP A O     1 
ATOM   251  C CB    . ASP A 1 40  ? -59.681 50.836 -32.281 1.00 15.56 ? 181 ASP A CB    1 
ATOM   252  C CG    . ASP A 1 40  ? -58.300 51.096 -32.852 1.00 23.03 ? 181 ASP A CG    1 
ATOM   253  O OD1   . ASP A 1 40  ? -57.569 50.102 -33.103 1.00 20.01 ? 181 ASP A OD1   1 
ATOM   254  O OD2   . ASP A 1 40  ? -57.936 52.288 -33.018 1.00 22.86 ? 181 ASP A OD2   1 
ATOM   255  N N     . ASN A 1 41  ? -59.646 48.339 -29.566 1.00 15.73 ? 182 ASN A N     1 
ATOM   256  C CA    . ASN A 1 41  ? -59.225 48.203 -28.176 1.00 16.16 ? 182 ASN A CA    1 
ATOM   257  C C     . ASN A 1 41  ? -57.755 47.858 -28.022 1.00 18.77 ? 182 ASN A C     1 
ATOM   258  O O     . ASN A 1 41  ? -57.146 48.227 -27.012 1.00 20.29 ? 182 ASN A O     1 
ATOM   259  C CB    . ASN A 1 41  ? -60.100 47.158 -27.516 1.00 16.31 ? 182 ASN A CB    1 
ATOM   260  C CG    . ASN A 1 41  ? -61.500 47.632 -27.419 1.00 19.59 ? 182 ASN A CG    1 
ATOM   261  O OD1   . ASN A 1 41  ? -61.763 48.591 -26.689 1.00 17.44 ? 182 ASN A OD1   1 
ATOM   262  N ND2   . ASN A 1 41  ? -62.408 47.046 -28.219 1.00 16.51 ? 182 ASN A ND2   1 
ATOM   263  N N     . ALA A 1 42  ? -57.174 47.136 -28.981 1.00 17.91 ? 183 ALA A N     1 
ATOM   264  C CA    . ALA A 1 42  ? -55.747 46.838 -28.921 1.00 21.82 ? 183 ALA A CA    1 
ATOM   265  C C     . ALA A 1 42  ? -54.884 48.083 -29.098 1.00 21.86 ? 183 ALA A C     1 
ATOM   266  O O     . ALA A 1 42  ? -53.694 48.045 -28.769 1.00 24.14 ? 183 ALA A O     1 
ATOM   267  C CB    . ALA A 1 42  ? -55.376 45.797 -29.988 1.00 19.61 ? 183 ALA A CB    1 
ATOM   268  N N     . ALA A 1 43  ? -55.443 49.172 -29.634 1.00 20.80 ? 184 ALA A N     1 
ATOM   269  C CA    . ALA A 1 43  ? -54.730 50.447 -29.703 1.00 17.92 ? 184 ALA A CA    1 
ATOM   270  C C     . ALA A 1 43  ? -54.963 51.272 -28.442 1.00 19.02 ? 184 ALA A C     1 
ATOM   271  O O     . ALA A 1 43  ? -54.007 51.731 -27.813 1.00 18.53 ? 184 ALA A O     1 
ATOM   272  C CB    . ALA A 1 43  ? -55.160 51.232 -30.952 1.00 16.59 ? 184 ALA A CB    1 
ATOM   273  N N     . THR A 1 44  ? -56.225 51.477 -28.064 1.00 17.60 ? 185 THR A N     1 
ATOM   274  C CA    . THR A 1 44  ? -56.536 52.031 -26.751 1.00 14.89 ? 185 THR A CA    1 
ATOM   275  C C     . THR A 1 44  ? -57.985 51.703 -26.418 1.00 15.17 ? 185 THR A C     1 
ATOM   276  O O     . THR A 1 44  ? -58.782 51.374 -27.300 1.00 14.21 ? 185 THR A O     1 
ATOM   277  C CB    . THR A 1 44  ? -56.264 53.539 -26.693 1.00 16.32 ? 185 THR A CB    1 
ATOM   278  O OG1   . THR A 1 44  ? -56.169 53.958 -25.319 1.00 18.42 ? 185 THR A OG1   1 
ATOM   279  C CG2   . THR A 1 44  ? -57.373 54.322 -27.376 1.00 16.17 ? 185 THR A CG2   1 
ATOM   280  N N     . THR A 1 45  ? -58.313 51.766 -25.130 1.00 13.89 ? 186 THR A N     1 
ATOM   281  C CA    . THR A 1 45  ? -59.659 51.459 -24.659 1.00 15.07 ? 186 THR A CA    1 
ATOM   282  C C     . THR A 1 45  ? -60.395 52.734 -24.262 1.00 16.00 ? 186 THR A C     1 
ATOM   283  O O     . THR A 1 45  ? -59.789 53.781 -24.016 1.00 16.62 ? 186 THR A O     1 
ATOM   284  C CB    . THR A 1 45  ? -59.629 50.502 -23.458 1.00 15.46 ? 186 THR A CB    1 
ATOM   285  O OG1   . THR A 1 45  ? -58.880 51.098 -22.382 1.00 16.24 ? 186 THR A OG1   1 
ATOM   286  C CG2   . THR A 1 45  ? -58.987 49.169 -23.849 1.00 14.87 ? 186 THR A CG2   1 
ATOM   287  N N     . GLN A 1 46  ? -61.719 52.619 -24.169 1.00 15.67 ? 187 GLN A N     1 
ATOM   288  C CA    . GLN A 1 46  ? -62.564 53.710 -23.724 1.00 14.72 ? 187 GLN A CA    1 
ATOM   289  C C     . GLN A 1 46  ? -62.758 53.648 -22.209 1.00 17.97 ? 187 GLN A C     1 
ATOM   290  O O     . GLN A 1 46  ? -62.494 52.625 -21.571 1.00 16.38 ? 187 GLN A O     1 
ATOM   291  C CB    . GLN A 1 46  ? -63.895 53.676 -24.479 1.00 15.99 ? 187 GLN A CB    1 
ATOM   292  C CG    . GLN A 1 46  ? -63.703 53.773 -25.994 1.00 15.59 ? 187 GLN A CG    1 
ATOM   293  C CD    . GLN A 1 46  ? -62.934 55.033 -26.427 1.00 16.90 ? 187 GLN A CD    1 
ATOM   294  O OE1   . GLN A 1 46  ? -62.674 55.940 -25.619 1.00 18.22 ? 187 GLN A OE1   1 
ATOM   295  N NE2   . GLN A 1 46  ? -62.563 55.089 -27.705 1.00 15.65 ? 187 GLN A NE2   1 
ATOM   296  N N     . LYS A 1 47  ? -63.184 54.800 -21.616 1.00 16.80 ? 188 LYS A N     1 
ATOM   297  C CA    . LYS A 1 47  ? -63.086 54.941 -20.154 1.00 14.57 ? 188 LYS A CA    1 
ATOM   298  C C     . LYS A 1 47  ? -64.449 54.904 -19.482 1.00 15.38 ? 188 LYS A C     1 
ATOM   299  O O     . LYS A 1 47  ? -65.399 55.508 -19.985 1.00 18.09 ? 188 LYS A O     1 
ATOM   300  C CB    . LYS A 1 47  ? -62.396 56.257 -19.763 1.00 15.42 ? 188 LYS A CB    1 
ATOM   301  C CG    . LYS A 1 47  ? -61.255 56.656 -20.699 1.00 15.50 ? 188 LYS A CG    1 
ATOM   302  C CD    . LYS A 1 47  ? -60.177 55.558 -20.739 1.00 13.34 ? 188 LYS A CD    1 
ATOM   303  C CE    . LYS A 1 47  ? -59.039 55.977 -21.667 1.00 15.75 ? 188 LYS A CE    1 
ATOM   304  N NZ    . LYS A 1 47  ? -58.124 54.838 -21.950 1.00 14.24 ? 188 LYS A NZ    1 
ATOM   305  N N     . PRO A 1 48  ? -64.571 54.237 -18.336 1.00 17.41 ? 189 PRO A N     1 
ATOM   306  C CA    . PRO A 1 48  ? -65.811 54.351 -17.550 1.00 17.05 ? 189 PRO A CA    1 
ATOM   307  C C     . PRO A 1 48  ? -65.924 55.720 -16.905 1.00 16.62 ? 189 PRO A C     1 
ATOM   308  O O     . PRO A 1 48  ? -64.921 56.361 -16.582 1.00 17.77 ? 189 PRO A O     1 
ATOM   309  C CB    . PRO A 1 48  ? -65.676 53.254 -16.487 1.00 16.85 ? 189 PRO A CB    1 
ATOM   310  C CG    . PRO A 1 48  ? -64.182 52.945 -16.424 1.00 16.52 ? 189 PRO A CG    1 
ATOM   311  C CD    . PRO A 1 48  ? -63.578 53.326 -17.735 1.00 13.74 ? 189 PRO A CD    1 
ATOM   312  N N     . GLN A 1 49  ? -67.171 56.166 -16.716 1.00 16.86 ? 190 GLN A N     1 
ATOM   313  C CA    . GLN A 1 49  ? -67.408 57.460 -16.086 1.00 19.83 ? 190 GLN A CA    1 
ATOM   314  C C     . GLN A 1 49  ? -66.675 57.578 -14.753 1.00 18.07 ? 190 GLN A C     1 
ATOM   315  O O     . GLN A 1 49  ? -66.204 58.659 -14.406 1.00 16.83 ? 190 GLN A O     1 
ATOM   316  C CB    . GLN A 1 49  ? -68.913 57.688 -15.877 1.00 19.44 ? 190 GLN A CB    1 
ATOM   317  C CG    . GLN A 1 49  ? -69.276 59.110 -15.418 1.00 18.21 ? 190 GLN A CG    1 
ATOM   318  C CD    . GLN A 1 49  ? -68.939 60.141 -16.477 1.00 21.44 ? 190 GLN A CD    1 
ATOM   319  O OE1   . GLN A 1 49  ? -69.302 59.987 -17.637 1.00 24.70 ? 190 GLN A OE1   1 
ATOM   320  N NE2   . GLN A 1 49  ? -68.225 61.185 -16.088 1.00 22.59 ? 190 GLN A NE2   1 
ATOM   321  N N     . ALA A 1 50  ? -66.557 56.480 -14.005 1.00 17.07 ? 191 ALA A N     1 
ATOM   322  C CA    . ALA A 1 50  ? -65.896 56.537 -12.707 1.00 17.14 ? 191 ALA A CA    1 
ATOM   323  C C     . ALA A 1 50  ? -64.433 56.973 -12.836 1.00 17.67 ? 191 ALA A C     1 
ATOM   324  O O     . ALA A 1 50  ? -63.924 57.701 -11.978 1.00 17.27 ? 191 ALA A O     1 
ATOM   325  C CB    . ALA A 1 50  ? -65.999 55.180 -12.011 1.00 15.95 ? 191 ALA A CB    1 
ATOM   326  N N     . VAL A 1 51  ? -63.744 56.559 -13.902 1.00 15.46 ? 192 VAL A N     1 
ATOM   327  C CA    . VAL A 1 51  ? -62.356 56.987 -14.095 1.00 15.26 ? 192 VAL A CA    1 
ATOM   328  C C     . VAL A 1 51  ? -62.296 58.491 -14.383 1.00 17.19 ? 192 VAL A C     1 
ATOM   329  O O     . VAL A 1 51  ? -61.515 59.239 -13.764 1.00 14.83 ? 192 VAL A O     1 
ATOM   330  C CB    . VAL A 1 51  ? -61.701 56.152 -15.215 1.00 15.40 ? 192 VAL A CB    1 
ATOM   331  C CG1   . VAL A 1 51  ? -60.319 56.691 -15.590 1.00 16.93 ? 192 VAL A CG1   1 
ATOM   332  C CG2   . VAL A 1 51  ? -61.559 54.693 -14.768 1.00 17.10 ? 192 VAL A CG2   1 
ATOM   333  N N     . ILE A 1 52  ? -63.118 58.946 -15.339 1.00 14.85 ? 193 ILE A N     1 
ATOM   334  C CA    . ILE A 1 52  ? -63.235 60.369 -15.676 1.00 18.15 ? 193 ILE A CA    1 
ATOM   335  C C     . ILE A 1 52  ? -63.527 61.198 -14.425 1.00 19.20 ? 193 ILE A C     1 
ATOM   336  O O     . ILE A 1 52  ? -62.873 62.222 -14.151 1.00 22.27 ? 193 ILE A O     1 
ATOM   337  C CB    . ILE A 1 52  ? -64.328 60.550 -16.756 1.00 20.67 ? 193 ILE A CB    1 
ATOM   338  C CG1   . ILE A 1 52  ? -63.961 59.724 -18.008 1.00 17.05 ? 193 ILE A CG1   1 
ATOM   339  C CG2   . ILE A 1 52  ? -64.584 62.025 -17.081 1.00 18.41 ? 193 ILE A CG2   1 
ATOM   340  C CD1   . ILE A 1 52  ? -64.962 59.814 -19.165 1.00 19.47 ? 193 ILE A CD1   1 
ATOM   341  N N     . ASP A 1 53  ? -64.502 60.746 -13.632 1.00 17.24 ? 194 ASP A N     1 
ATOM   342  C CA    . ASP A 1 53  ? -64.875 61.442 -12.410 1.00 19.94 ? 194 ASP A CA    1 
ATOM   343  C C     . ASP A 1 53  ? -63.783 61.361 -11.349 1.00 20.92 ? 194 ASP A C     1 
ATOM   344  O O     . ASP A 1 53  ? -63.658 62.280 -10.539 1.00 22.29 ? 194 ASP A O     1 
ATOM   345  C CB    . ASP A 1 53  ? -66.175 60.868 -11.848 1.00 20.06 ? 194 ASP A CB    1 
ATOM   346  C CG    . ASP A 1 53  ? -67.392 61.233 -12.691 1.00 27.37 ? 194 ASP A CG    1 
ATOM   347  O OD1   . ASP A 1 53  ? -67.259 62.083 -13.605 1.00 23.72 ? 194 ASP A OD1   1 
ATOM   348  O OD2   . ASP A 1 53  ? -68.487 60.680 -12.423 1.00 26.08 ? 194 ASP A OD2   1 
ATOM   349  N N     . ARG A 1 54  ? -62.990 60.283 -11.327 1.00 18.87 ? 195 ARG A N     1 
ATOM   350  C CA    . ARG A 1 54  ? -61.928 60.188 -10.329 1.00 18.59 ? 195 ARG A CA    1 
ATOM   351  C C     . ARG A 1 54  ? -60.866 61.241 -10.589 1.00 20.80 ? 195 ARG A C     1 
ATOM   352  O O     . ARG A 1 54  ? -60.352 61.862 -9.645  1.00 15.58 ? 195 ARG A O     1 
ATOM   353  C CB    . ARG A 1 54  ? -61.311 58.785 -10.323 1.00 17.40 ? 195 ARG A CB    1 
ATOM   354  C CG    . ARG A 1 54  ? -60.282 58.555 -9.208  1.00 19.15 ? 195 ARG A CG    1 
ATOM   355  C CD    . ARG A 1 54  ? -60.945 58.643 -7.833  1.00 19.88 ? 195 ARG A CD    1 
ATOM   356  N NE    . ARG A 1 54  ? -59.991 58.666 -6.729  1.00 19.36 ? 195 ARG A NE    1 
ATOM   357  C CZ    . ARG A 1 54  ? -59.517 59.772 -6.166  1.00 25.19 ? 195 ARG A CZ    1 
ATOM   358  N NH1   . ARG A 1 54  ? -59.751 60.972 -6.686  1.00 20.29 ? 195 ARG A NH1   1 
ATOM   359  N NH2   . ARG A 1 54  ? -58.804 59.676 -5.045  1.00 23.20 ? 195 ARG A NH2   1 
ATOM   360  N N     . LEU A 1 55  ? -60.552 61.463 -11.876 1.00 17.39 ? 196 LEU A N     1 
ATOM   361  C CA    . LEU A 1 55  ? -59.616 62.519 -12.264 1.00 17.61 ? 196 LEU A CA    1 
ATOM   362  C C     . LEU A 1 55  ? -60.152 63.899 -11.901 1.00 20.64 ? 196 LEU A C     1 
ATOM   363  O O     . LEU A 1 55  ? -59.421 64.743 -11.349 1.00 20.86 ? 196 LEU A O     1 
ATOM   364  C CB    . LEU A 1 55  ? -59.340 62.466 -13.771 1.00 15.39 ? 196 LEU A CB    1 
ATOM   365  C CG    . LEU A 1 55  ? -58.614 61.248 -14.343 1.00 22.23 ? 196 LEU A CG    1 
ATOM   366  C CD1   . LEU A 1 55  ? -58.534 61.333 -15.889 1.00 18.34 ? 196 LEU A CD1   1 
ATOM   367  C CD2   . LEU A 1 55  ? -57.221 61.110 -13.730 1.00 18.28 ? 196 LEU A CD2   1 
ATOM   368  N N     . SER A 1 56  ? -61.416 64.169 -12.265 1.00 20.29 ? 197 SER A N     1 
ATOM   369  C CA    . SER A 1 56  ? -62.027 65.453 -11.909 1.00 21.31 ? 197 SER A CA    1 
ATOM   370  C C     . SER A 1 56  ? -61.996 65.682 -10.404 1.00 20.15 ? 197 SER A C     1 
ATOM   371  O O     . SER A 1 56  ? -61.690 66.789 -9.937  1.00 22.27 ? 197 SER A O     1 
ATOM   372  C CB    . SER A 1 56  ? -63.473 65.515 -12.403 1.00 21.16 ? 197 SER A CB    1 
ATOM   373  O OG    . SER A 1 56  ? -63.530 65.335 -13.798 1.00 28.61 ? 197 SER A OG    1 
ATOM   374  N N     . HIS A 1 57  ? -62.330 64.649 -9.630  1.00 20.96 ? 198 HIS A N     1 
ATOM   375  C CA    . HIS A 1 57  ? -62.354 64.784 -8.179  1.00 21.18 ? 198 HIS A CA    1 
ATOM   376  C C     . HIS A 1 57  ? -60.960 65.051 -7.623  1.00 19.92 ? 198 HIS A C     1 
ATOM   377  O O     . HIS A 1 57  ? -60.794 65.901 -6.741  1.00 24.15 ? 198 HIS A O     1 
ATOM   378  C CB    . HIS A 1 57  ? -62.949 63.530 -7.550  1.00 20.14 ? 198 HIS A CB    1 
ATOM   379  C CG    . HIS A 1 57  ? -63.160 63.658 -6.075  1.00 27.31 ? 198 HIS A CG    1 
ATOM   380  N ND1   . HIS A 1 57  ? -62.150 63.460 -5.156  1.00 27.13 ? 198 HIS A ND1   1 
ATOM   381  C CD2   . HIS A 1 57  ? -64.256 64.010 -5.362  1.00 24.40 ? 198 HIS A CD2   1 
ATOM   382  C CE1   . HIS A 1 57  ? -62.623 63.660 -3.937  1.00 29.67 ? 198 HIS A CE1   1 
ATOM   383  N NE2   . HIS A 1 57  ? -63.896 63.995 -4.035  1.00 27.87 ? 198 HIS A NE2   1 
ATOM   384  N N     . PHE A 1 58  ? -59.939 64.348 -8.127  1.00 19.81 ? 199 PHE A N     1 
ATOM   385  C CA    . PHE A 1 58  ? -58.581 64.618 -7.667  1.00 17.87 ? 199 PHE A CA    1 
ATOM   386  C C     . PHE A 1 58  ? -58.208 66.076 -7.905  1.00 19.39 ? 199 PHE A C     1 
ATOM   387  O O     . PHE A 1 58  ? -57.696 66.749 -7.003  1.00 20.56 ? 199 PHE A O     1 
ATOM   388  C CB    . PHE A 1 58  ? -57.580 63.676 -8.340  1.00 21.88 ? 199 PHE A CB    1 
ATOM   389  C CG    . PHE A 1 58  ? -56.137 63.962 -7.980  1.00 19.02 ? 199 PHE A CG    1 
ATOM   390  C CD1   . PHE A 1 58  ? -55.554 63.372 -6.869  1.00 17.47 ? 199 PHE A CD1   1 
ATOM   391  C CD2   . PHE A 1 58  ? -55.375 64.837 -8.751  1.00 19.41 ? 199 PHE A CD2   1 
ATOM   392  C CE1   . PHE A 1 58  ? -54.230 63.652 -6.529  1.00 20.76 ? 199 PHE A CE1   1 
ATOM   393  C CE2   . PHE A 1 58  ? -54.049 65.118 -8.426  1.00 17.59 ? 199 PHE A CE2   1 
ATOM   394  C CZ    . PHE A 1 58  ? -53.476 64.528 -7.315  1.00 20.51 ? 199 PHE A CZ    1 
ATOM   395  N N     . TYR A 1 59  ? -58.465 66.591 -9.113  1.00 19.54 ? 200 TYR A N     1 
ATOM   396  C CA    . TYR A 1 59  ? -58.046 67.961 -9.391  1.00 18.47 ? 200 TYR A CA    1 
ATOM   397  C C     . TYR A 1 59  ? -58.853 68.978 -8.595  1.00 21.17 ? 200 TYR A C     1 
ATOM   398  O O     . TYR A 1 59  ? -58.337 70.052 -8.264  1.00 23.27 ? 200 TYR A O     1 
ATOM   399  C CB    . TYR A 1 59  ? -58.146 68.261 -10.892 1.00 18.48 ? 200 TYR A CB    1 
ATOM   400  C CG    . TYR A 1 59  ? -56.991 67.665 -11.669 1.00 18.88 ? 200 TYR A CG    1 
ATOM   401  C CD1   . TYR A 1 59  ? -55.681 67.978 -11.332 1.00 19.02 ? 200 TYR A CD1   1 
ATOM   402  C CD2   . TYR A 1 59  ? -57.206 66.777 -12.714 1.00 17.69 ? 200 TYR A CD2   1 
ATOM   403  C CE1   . TYR A 1 59  ? -54.605 67.423 -12.020 1.00 17.85 ? 200 TYR A CE1   1 
ATOM   404  C CE2   . TYR A 1 59  ? -56.137 66.215 -13.417 1.00 17.74 ? 200 TYR A CE2   1 
ATOM   405  C CZ    . TYR A 1 59  ? -54.847 66.552 -13.069 1.00 19.25 ? 200 TYR A CZ    1 
ATOM   406  O OH    . TYR A 1 59  ? -53.781 66.016 -13.746 1.00 21.35 ? 200 TYR A OH    1 
ATOM   407  N N     . ALA A 1 60  ? -60.106 68.666 -8.270  1.00 20.62 ? 201 ALA A N     1 
ATOM   408  C CA    . ALA A 1 60  ? -60.930 69.624 -7.544  1.00 23.40 ? 201 ALA A CA    1 
ATOM   409  C C     . ALA A 1 60  ? -60.752 69.552 -6.032  1.00 22.70 ? 201 ALA A C     1 
ATOM   410  O O     . ALA A 1 60  ? -61.082 70.519 -5.336  1.00 25.07 ? 201 ALA A O     1 
ATOM   411  C CB    . ALA A 1 60  ? -62.404 69.406 -7.882  1.00 23.53 ? 201 ALA A CB    1 
ATOM   412  N N     . HIS A 1 61  ? -60.251 68.443 -5.496  1.00 21.65 ? 202 HIS A N     1 
ATOM   413  C CA    . HIS A 1 61  ? -60.285 68.238 -4.054  1.00 23.28 ? 202 HIS A CA    1 
ATOM   414  C C     . HIS A 1 61  ? -58.993 67.724 -3.442  1.00 24.46 ? 202 HIS A C     1 
ATOM   415  O O     . HIS A 1 61  ? -58.823 67.863 -2.224  1.00 25.19 ? 202 HIS A O     1 
ATOM   416  C CB    . HIS A 1 61  ? -61.414 67.263 -3.687  1.00 27.99 ? 202 HIS A CB    1 
ATOM   417  C CG    . HIS A 1 61  ? -62.782 67.752 -4.059  1.00 29.31 ? 202 HIS A CG    1 
ATOM   418  N ND1   . HIS A 1 61  ? -63.450 68.718 -3.337  1.00 34.03 ? 202 HIS A ND1   1 
ATOM   419  C CD2   . HIS A 1 61  ? -63.598 67.421 -5.089  1.00 27.44 ? 202 HIS A CD2   1 
ATOM   420  C CE1   . HIS A 1 61  ? -64.626 68.948 -3.896  1.00 31.18 ? 202 HIS A CE1   1 
ATOM   421  N NE2   . HIS A 1 61  ? -64.740 68.175 -4.961  1.00 27.91 ? 202 HIS A NE2   1 
ATOM   422  N N     . GLU A 1 62  ? -58.082 67.137 -4.220  1.00 21.62 ? 203 GLU A N     1 
ATOM   423  C CA    . GLU A 1 62  ? -56.914 66.489 -3.645  1.00 21.84 ? 203 GLU A CA    1 
ATOM   424  C C     . GLU A 1 62  ? -55.585 66.965 -4.206  1.00 20.91 ? 203 GLU A C     1 
ATOM   425  O O     . GLU A 1 62  ? -54.543 66.479 -3.748  1.00 22.24 ? 203 GLU A O     1 
ATOM   426  C CB    . GLU A 1 62  ? -56.986 64.962 -3.834  1.00 22.77 ? 203 GLU A CB    1 
ATOM   427  C CG    . GLU A 1 62  ? -58.239 64.295 -3.278  1.00 21.73 ? 203 GLU A CG    1 
ATOM   428  C CD    . GLU A 1 62  ? -58.480 62.944 -3.940  1.00 27.08 ? 203 GLU A CD    1 
ATOM   429  O OE1   . GLU A 1 62  ? -58.997 62.935 -5.075  1.00 32.44 ? 203 GLU A OE1   1 
ATOM   430  O OE2   . GLU A 1 62  ? -58.143 61.895 -3.347  1.00 28.69 ? 203 GLU A OE2   1 
ATOM   431  N N     . ASN A 1 63  ? -55.578 67.905 -5.150  1.00 19.68 ? 204 ASN A N     1 
ATOM   432  C CA    . ASN A 1 63  ? -54.389 68.117 -5.970  1.00 21.44 ? 204 ASN A CA    1 
ATOM   433  C C     . ASN A 1 63  ? -53.247 68.766 -5.191  1.00 19.79 ? 204 ASN A C     1 
ATOM   434  O O     . ASN A 1 63  ? -53.408 69.833 -4.596  1.00 21.69 ? 204 ASN A O     1 
ATOM   435  C CB    . ASN A 1 63  ? -54.710 68.978 -7.185  1.00 17.88 ? 204 ASN A CB    1 
ATOM   436  C CG    . ASN A 1 63  ? -53.473 69.260 -8.015  1.00 21.93 ? 204 ASN A CG    1 
ATOM   437  O OD1   . ASN A 1 63  ? -52.912 68.353 -8.636  1.00 25.73 ? 204 ASN A OD1   1 
ATOM   438  N ND2   . ASN A 1 63  ? -53.030 70.515 -8.023  1.00 22.44 ? 204 ASN A ND2   1 
ATOM   439  N N     . SER A 1 64  ? -52.071 68.154 -5.274  1.00 22.11 ? 205 SER A N     1 
ATOM   440  C CA    . SER A 1 64  ? -50.860 68.624 -4.623  1.00 20.49 ? 205 SER A CA    1 
ATOM   441  C C     . SER A 1 64  ? -49.758 67.637 -4.974  1.00 23.77 ? 205 SER A C     1 
ATOM   442  O O     . SER A 1 64  ? -50.034 66.502 -5.373  1.00 20.38 ? 205 SER A O     1 
ATOM   443  C CB    . SER A 1 64  ? -51.043 68.718 -3.095  1.00 24.37 ? 205 SER A CB    1 
ATOM   444  O OG    . SER A 1 64  ? -49.801 68.862 -2.434  1.00 23.76 ? 205 SER A OG    1 
ATOM   445  N N     . ASN A 1 65  ? -48.508 68.081 -4.840  1.00 22.36 ? 206 ASN A N     1 
ATOM   446  C CA    . ASN A 1 65  ? -47.423 67.116 -4.768  1.00 24.00 ? 206 ASN A CA    1 
ATOM   447  C C     . ASN A 1 65  ? -47.478 66.365 -3.432  1.00 26.91 ? 206 ASN A C     1 
ATOM   448  O O     . ASN A 1 65  ? -48.123 66.799 -2.467  1.00 21.16 ? 206 ASN A O     1 
ATOM   449  C CB    . ASN A 1 65  ? -46.077 67.808 -4.935  1.00 26.20 ? 206 ASN A CB    1 
ATOM   450  C CG    . ASN A 1 65  ? -45.201 67.113 -5.933  1.00 32.13 ? 206 ASN A CG    1 
ATOM   451  O OD1   . ASN A 1 65  ? -45.010 65.887 -5.860  1.00 31.96 ? 206 ASN A OD1   1 
ATOM   452  N ND2   . ASN A 1 65  ? -44.658 67.881 -6.886  1.00 35.61 ? 206 ASN A ND2   1 
ATOM   453  N N     . ILE A 1 66  ? -46.785 65.228 -3.370  1.00 26.00 ? 207 ILE A N     1 
ATOM   454  C CA    . ILE A 1 66  ? -46.953 64.336 -2.225  1.00 30.59 ? 207 ILE A CA    1 
ATOM   455  C C     . ILE A 1 66  ? -46.055 64.734 -1.053  1.00 33.20 ? 207 ILE A C     1 
ATOM   456  O O     . ILE A 1 66  ? -45.490 65.837 -1.044  1.00 30.63 ? 207 ILE A O     1 
ATOM   457  C CB    . ILE A 1 66  ? -46.725 62.868 -2.632  1.00 32.70 ? 207 ILE A CB    1 
ATOM   458  C CG1   . ILE A 1 66  ? -45.268 62.615 -3.020  1.00 33.30 ? 207 ILE A CG1   1 
ATOM   459  C CG2   . ILE A 1 66  ? -47.666 62.490 -3.777  1.00 30.71 ? 207 ILE A CG2   1 
ATOM   460  C CD1   . ILE A 1 66  ? -45.029 61.205 -3.515  1.00 35.29 ? 207 ILE A CD1   1 
ATOM   461  N N     . HIS A 1 67  ? -45.962 63.833 -0.051  1.00 33.72 ? 208 HIS A N     1 
ATOM   462  C CA    . HIS A 1 67  ? -45.275 63.960 1.245   1.00 39.66 ? 208 HIS A CA    1 
ATOM   463  C C     . HIS A 1 67  ? -46.284 64.408 2.307   1.00 35.69 ? 208 HIS A C     1 
ATOM   464  O O     . HIS A 1 67  ? -46.531 65.604 2.490   1.00 33.44 ? 208 HIS A O     1 
ATOM   465  C CB    . HIS A 1 67  ? -44.053 64.901 1.173   1.00 39.90 ? 208 HIS A CB    1 
ATOM   466  C CG    . HIS A 1 67  ? -43.352 65.106 2.483   1.00 48.67 ? 208 HIS A CG    1 
ATOM   467  N ND1   . HIS A 1 67  ? -42.957 66.352 2.930   1.00 49.46 ? 208 HIS A ND1   1 
ATOM   468  C CD2   . HIS A 1 67  ? -42.975 64.227 3.443   1.00 51.02 ? 208 HIS A CD2   1 
ATOM   469  C CE1   . HIS A 1 67  ? -42.367 66.231 4.107   1.00 48.97 ? 208 HIS A CE1   1 
ATOM   470  N NE2   . HIS A 1 67  ? -42.365 64.952 4.442   1.00 52.99 ? 208 HIS A NE2   1 
ATOM   471  N N     . ARG A 1 68  ? -46.877 63.445 3.017   1.00 38.95 ? 209 ARG A N     1 
ATOM   472  C CA    . ARG A 1 68  ? -48.075 63.739 3.799   1.00 35.43 ? 209 ARG A CA    1 
ATOM   473  C C     . ARG A 1 68  ? -47.815 64.697 4.953   1.00 38.03 ? 209 ARG A C     1 
ATOM   474  O O     . ARG A 1 68  ? -48.744 65.391 5.375   1.00 41.89 ? 209 ARG A O     1 
ATOM   475  C CB    . ARG A 1 68  ? -48.703 62.443 4.312   1.00 35.14 ? 209 ARG A CB    1 
ATOM   476  C CG    . ARG A 1 68  ? -47.989 61.803 5.474   1.00 45.31 ? 209 ARG A CG    1 
ATOM   477  C CD    . ARG A 1 68  ? -48.800 60.629 6.039   1.00 49.65 ? 209 ARG A CD    1 
ATOM   478  N NE    . ARG A 1 68  ? -49.058 59.604 5.032   1.00 46.30 ? 209 ARG A NE    1 
ATOM   479  C CZ    . ARG A 1 68  ? -50.235 59.390 4.461   1.00 44.24 ? 209 ARG A CZ    1 
ATOM   480  N NH1   . ARG A 1 68  ? -51.300 60.113 4.780   1.00 42.81 ? 209 ARG A NH1   1 
ATOM   481  N NH2   . ARG A 1 68  ? -50.351 58.423 3.550   1.00 38.57 ? 209 ARG A NH2   1 
ATOM   482  N N     . ALA A 1 69  ? -46.579 64.782 5.453   1.00 40.28 ? 210 ALA A N     1 
ATOM   483  C CA    . ALA A 1 69  ? -46.287 65.704 6.545   1.00 43.62 ? 210 ALA A CA    1 
ATOM   484  C C     . ALA A 1 69  ? -46.355 67.172 6.126   1.00 41.59 ? 210 ALA A C     1 
ATOM   485  O O     . ALA A 1 69  ? -46.408 68.042 7.003   1.00 38.69 ? 210 ALA A O     1 
ATOM   486  C CB    . ALA A 1 69  ? -44.906 65.396 7.138   1.00 40.40 ? 210 ALA A CB    1 
ATOM   487  N N     . ALA A 1 70  ? -46.385 67.468 4.824   1.00 35.88 ? 211 ALA A N     1 
ATOM   488  C CA    . ALA A 1 70  ? -46.294 68.854 4.370   1.00 37.65 ? 211 ALA A CA    1 
ATOM   489  C C     . ALA A 1 70  ? -47.495 69.680 4.823   1.00 34.00 ? 211 ALA A C     1 
ATOM   490  O O     . ALA A 1 70  ? -47.340 70.696 5.512   1.00 33.28 ? 211 ALA A O     1 
ATOM   491  C CB    . ALA A 1 70  ? -46.153 68.898 2.845   1.00 33.99 ? 211 ALA A CB    1 
ATOM   492  N N     . HIS A 1 71  ? -48.696 69.277 4.416   1.00 30.43 ? 212 HIS A N     1 
ATOM   493  C CA    . HIS A 1 71  ? -49.937 70.014 4.659   1.00 29.06 ? 212 HIS A CA    1 
ATOM   494  C C     . HIS A 1 71  ? -51.091 69.125 4.195   1.00 27.96 ? 212 HIS A C     1 
ATOM   495  O O     . HIS A 1 71  ? -50.872 68.036 3.659   1.00 25.57 ? 212 HIS A O     1 
ATOM   496  C CB    . HIS A 1 71  ? -49.939 71.380 3.959   1.00 25.32 ? 212 HIS A CB    1 
ATOM   497  C CG    . HIS A 1 71  ? -49.479 71.338 2.532   1.00 27.87 ? 212 HIS A CG    1 
ATOM   498  N ND1   . HIS A 1 71  ? -50.241 70.799 1.517   1.00 27.04 ? 212 HIS A ND1   1 
ATOM   499  C CD2   . HIS A 1 71  ? -48.334 71.771 1.950   1.00 30.05 ? 212 HIS A CD2   1 
ATOM   500  C CE1   . HIS A 1 71  ? -49.591 70.907 0.370   1.00 27.35 ? 212 HIS A CE1   1 
ATOM   501  N NE2   . HIS A 1 71  ? -48.430 71.493 0.604   1.00 31.67 ? 212 HIS A NE2   1 
ATOM   502  N N     . GLU A 1 72  ? -52.325 69.611 4.382   1.00 29.68 ? 213 GLU A N     1 
ATOM   503  C CA    . GLU A 1 72  ? -53.521 68.771 4.228   1.00 26.07 ? 213 GLU A CA    1 
ATOM   504  C C     . GLU A 1 72  ? -53.653 68.191 2.813   1.00 27.95 ? 213 GLU A C     1 
ATOM   505  O O     . GLU A 1 72  ? -53.863 66.980 2.637   1.00 26.51 ? 213 GLU A O     1 
ATOM   506  C CB    . GLU A 1 72  ? -54.767 69.580 4.583   1.00 31.06 ? 213 GLU A CB    1 
ATOM   507  C CG    . GLU A 1 72  ? -56.074 68.922 4.146   1.00 31.38 ? 213 GLU A CG    1 
ATOM   508  C CD    . GLU A 1 72  ? -56.407 67.665 4.932   1.00 37.02 ? 213 GLU A CD    1 
ATOM   509  O OE1   . GLU A 1 72  ? -55.751 67.393 5.969   1.00 39.63 ? 213 GLU A OE1   1 
ATOM   510  O OE2   . GLU A 1 72  ? -57.275 66.894 4.459   1.00 38.26 ? 213 GLU A OE2   1 
ATOM   511  N N     . LEU A 1 73  ? -53.566 69.043 1.789   1.00 22.90 ? 214 LEU A N     1 
ATOM   512  C CA    . LEU A 1 73  ? -53.714 68.541 0.426   1.00 26.50 ? 214 LEU A CA    1 
ATOM   513  C C     . LEU A 1 73  ? -52.580 67.596 0.065   1.00 24.16 ? 214 LEU A C     1 
ATOM   514  O O     . LEU A 1 73  ? -52.793 66.613 -0.652  1.00 24.26 ? 214 LEU A O     1 
ATOM   515  C CB    . LEU A 1 73  ? -53.780 69.692 -0.579  1.00 22.65 ? 214 LEU A CB    1 
ATOM   516  C CG    . LEU A 1 73  ? -55.090 70.483 -0.561  1.00 24.69 ? 214 LEU A CG    1 
ATOM   517  C CD1   . LEU A 1 73  ? -55.170 71.447 -1.751  1.00 21.89 ? 214 LEU A CD1   1 
ATOM   518  C CD2   . LEU A 1 73  ? -56.267 69.531 -0.548  1.00 28.87 ? 214 LEU A CD2   1 
ATOM   519  N N     . ALA A 1 74  ? -51.363 67.879 0.537   1.00 20.95 ? 215 ALA A N     1 
ATOM   520  C CA    . ALA A 1 74  ? -50.269 66.947 0.293   1.00 24.52 ? 215 ALA A CA    1 
ATOM   521  C C     . ALA A 1 74  ? -50.583 65.582 0.897   1.00 27.23 ? 215 ALA A C     1 
ATOM   522  O O     . ALA A 1 74  ? -50.305 64.547 0.276   1.00 23.34 ? 215 ALA A O     1 
ATOM   523  C CB    . ALA A 1 74  ? -48.948 67.502 0.843   1.00 25.43 ? 215 ALA A CB    1 
ATOM   524  N N     . ALA A 1 75  ? -51.207 65.557 2.087   1.00 21.54 ? 216 ALA A N     1 
ATOM   525  C CA    . ALA A 1 75  ? -51.588 64.279 2.687   1.00 26.07 ? 216 ALA A CA    1 
ATOM   526  C C     . ALA A 1 75  ? -52.676 63.582 1.873   1.00 24.15 ? 216 ALA A C     1 
ATOM   527  O O     . ALA A 1 75  ? -52.660 62.354 1.737   1.00 25.78 ? 216 ALA A O     1 
ATOM   528  C CB    . ALA A 1 75  ? -52.045 64.474 4.134   1.00 24.05 ? 216 ALA A CB    1 
ATOM   529  N N     . ARG A 1 76  ? -53.624 64.343 1.318   1.00 22.68 ? 217 ARG A N     1 
ATOM   530  C CA    . ARG A 1 76  ? -54.662 63.736 0.481   1.00 23.22 ? 217 ARG A CA    1 
ATOM   531  C C     . ARG A 1 76  ? -54.060 63.118 -0.778  1.00 22.92 ? 217 ARG A C     1 
ATOM   532  O O     . ARG A 1 76  ? -54.356 61.968 -1.134  1.00 24.75 ? 217 ARG A O     1 
ATOM   533  C CB    . ARG A 1 76  ? -55.703 64.786 0.089   1.00 23.44 ? 217 ARG A CB    1 
ATOM   534  C CG    . ARG A 1 76  ? -56.588 65.274 1.226   1.00 25.50 ? 217 ARG A CG    1 
ATOM   535  C CD    . ARG A 1 76  ? -57.553 66.335 0.731   1.00 24.97 ? 217 ARG A CD    1 
ATOM   536  N NE    . ARG A 1 76  ? -58.086 67.105 1.849   1.00 29.04 ? 217 ARG A NE    1 
ATOM   537  C CZ    . ARG A 1 76  ? -58.976 68.077 1.733   1.00 32.38 ? 217 ARG A CZ    1 
ATOM   538  N NH1   . ARG A 1 76  ? -59.475 68.420 0.552   1.00 30.43 ? 217 ARG A NH1   1 
ATOM   539  N NH2   . ARG A 1 76  ? -59.374 68.723 2.828   1.00 28.91 ? 217 ARG A NH2   1 
ATOM   540  N N     . ALA A 1 77  ? -53.232 63.889 -1.484  1.00 19.56 ? 218 ALA A N     1 
ATOM   541  C CA    . ALA A 1 77  ? -52.585 63.379 -2.690  1.00 23.21 ? 218 ALA A CA    1 
ATOM   542  C C     . ALA A 1 77  ? -51.710 62.170 -2.381  1.00 24.76 ? 218 ALA A C     1 
ATOM   543  O O     . ALA A 1 77  ? -51.681 61.212 -3.158  1.00 21.80 ? 218 ALA A O     1 
ATOM   544  C CB    . ALA A 1 77  ? -51.757 64.478 -3.354  1.00 22.29 ? 218 ALA A CB    1 
ATOM   545  N N     . THR A 1 78  ? -50.985 62.202 -1.257  1.00 22.91 ? 219 THR A N     1 
ATOM   546  C CA    . THR A 1 78  ? -50.133 61.078 -0.873  1.00 28.47 ? 219 THR A CA    1 
ATOM   547  C C     . THR A 1 78  ? -50.965 59.831 -0.617  1.00 25.31 ? 219 THR A C     1 
ATOM   548  O O     . THR A 1 78  ? -50.614 58.736 -1.066  1.00 27.10 ? 219 THR A O     1 
ATOM   549  C CB    . THR A 1 78  ? -49.322 61.422 0.390   1.00 30.75 ? 219 THR A CB    1 
ATOM   550  O OG1   . THR A 1 78  ? -48.470 62.546 0.147   1.00 26.73 ? 219 THR A OG1   1 
ATOM   551  C CG2   . THR A 1 78  ? -48.466 60.215 0.837   1.00 28.86 ? 219 THR A CG2   1 
ATOM   552  N N     . ASP A 1 79  ? -52.056 59.976 0.141   1.00 24.25 ? 220 ASP A N     1 
ATOM   553  C CA    . ASP A 1 79  ? -52.958 58.857 0.380   1.00 25.55 ? 220 ASP A CA    1 
ATOM   554  C C     . ASP A 1 79  ? -53.429 58.268 -0.942  1.00 24.22 ? 220 ASP A C     1 
ATOM   555  O O     . ASP A 1 79  ? -53.435 57.046 -1.129  1.00 20.69 ? 220 ASP A O     1 
ATOM   556  C CB    . ASP A 1 79  ? -54.168 59.323 1.201   1.00 23.35 ? 220 ASP A CB    1 
ATOM   557  C CG    . ASP A 1 79  ? -53.903 59.381 2.717   1.00 36.98 ? 220 ASP A CG    1 
ATOM   558  O OD1   . ASP A 1 79  ? -52.851 58.905 3.196   1.00 37.94 ? 220 ASP A OD1   1 
ATOM   559  O OD2   . ASP A 1 79  ? -54.761 59.953 3.426   1.00 39.84 ? 220 ASP A OD2   1 
ATOM   560  N N     . ALA A 1 80  ? -53.844 59.133 -1.873  1.00 21.02 ? 221 ALA A N     1 
ATOM   561  C CA    . ALA A 1 80  ? -54.401 58.633 -3.129  1.00 22.43 ? 221 ALA A CA    1 
ATOM   562  C C     . ALA A 1 80  ? -53.336 57.940 -3.966  1.00 21.26 ? 221 ALA A C     1 
ATOM   563  O O     . ALA A 1 80  ? -53.587 56.877 -4.547  1.00 20.59 ? 221 ALA A O     1 
ATOM   564  C CB    . ALA A 1 80  ? -55.051 59.776 -3.911  1.00 19.49 ? 221 ALA A CB    1 
ATOM   565  N N     . TYR A 1 81  ? -52.133 58.518 -4.023  1.00 22.04 ? 222 TYR A N     1 
ATOM   566  C CA    . TYR A 1 81  ? -51.041 57.930 -4.795  1.00 21.67 ? 222 TYR A CA    1 
ATOM   567  C C     . TYR A 1 81  ? -50.637 56.571 -4.226  1.00 21.03 ? 222 TYR A C     1 
ATOM   568  O O     . TYR A 1 81  ? -50.466 55.599 -4.975  1.00 19.30 ? 222 TYR A O     1 
ATOM   569  C CB    . TYR A 1 81  ? -49.851 58.894 -4.805  1.00 19.55 ? 222 TYR A CB    1 
ATOM   570  C CG    . TYR A 1 81  ? -48.833 58.707 -5.915  1.00 19.47 ? 222 TYR A CG    1 
ATOM   571  C CD1   . TYR A 1 81  ? -49.219 58.473 -7.232  1.00 18.92 ? 222 TYR A CD1   1 
ATOM   572  C CD2   . TYR A 1 81  ? -47.476 58.794 -5.636  1.00 21.54 ? 222 TYR A CD2   1 
ATOM   573  C CE1   . TYR A 1 81  ? -48.264 58.322 -8.242  1.00 18.41 ? 222 TYR A CE1   1 
ATOM   574  C CE2   . TYR A 1 81  ? -46.521 58.647 -6.623  1.00 21.77 ? 222 TYR A CE2   1 
ATOM   575  C CZ    . TYR A 1 81  ? -46.914 58.421 -7.924  1.00 19.50 ? 222 TYR A CZ    1 
ATOM   576  O OH    . TYR A 1 81  ? -45.945 58.275 -8.893  1.00 19.86 ? 222 TYR A OH    1 
ATOM   577  N N     . GLU A 1 82  ? -50.475 56.487 -2.897  1.00 20.74 ? 223 GLU A N     1 
ATOM   578  C CA    . GLU A 1 82  ? -50.127 55.213 -2.260  1.00 22.45 ? 223 GLU A CA    1 
ATOM   579  C C     . GLU A 1 82  ? -51.220 54.172 -2.473  1.00 21.94 ? 223 GLU A C     1 
ATOM   580  O O     . GLU A 1 82  ? -50.929 52.999 -2.747  1.00 20.36 ? 223 GLU A O     1 
ATOM   581  C CB    . GLU A 1 82  ? -49.874 55.415 -0.755  1.00 23.12 ? 223 GLU A CB    1 
ATOM   582  C CG    . GLU A 1 82  ? -48.562 56.149 -0.428  1.00 33.19 ? 223 GLU A CG    1 
ATOM   583  C CD    . GLU A 1 82  ? -48.384 56.430 1.076   1.00 40.66 ? 223 GLU A CD    1 
ATOM   584  O OE1   . GLU A 1 82  ? -47.319 56.989 1.466   1.00 38.46 ? 223 GLU A OE1   1 
ATOM   585  O OE2   . GLU A 1 82  ? -49.315 56.117 1.859   1.00 36.66 ? 223 GLU A OE2   1 
ATOM   586  N N     . ASP A 1 83  ? -52.489 54.582 -2.346  1.00 22.26 ? 224 ASP A N     1 
ATOM   587  C CA    . ASP A 1 83  ? -53.607 53.678 -2.612  1.00 19.88 ? 224 ASP A CA    1 
ATOM   588  C C     . ASP A 1 83  ? -53.597 53.185 -4.062  1.00 20.81 ? 224 ASP A C     1 
ATOM   589  O O     . ASP A 1 83  ? -53.920 52.023 -4.335  1.00 19.36 ? 224 ASP A O     1 
ATOM   590  C CB    . ASP A 1 83  ? -54.903 54.404 -2.281  1.00 23.45 ? 224 ASP A CB    1 
ATOM   591  C CG    . ASP A 1 83  ? -55.231 54.369 -0.777  1.00 37.95 ? 224 ASP A CG    1 
ATOM   592  O OD1   . ASP A 1 83  ? -54.290 54.291 0.061   1.00 36.82 ? 224 ASP A OD1   1 
ATOM   593  O OD2   . ASP A 1 83  ? -56.422 54.500 -0.432  1.00 38.40 ? 224 ASP A OD2   1 
ATOM   594  N N     . ALA A 1 84  ? -53.220 54.046 -5.007  1.00 18.71 ? 225 ALA A N     1 
ATOM   595  C CA    . ALA A 1 84  ? -53.152 53.629 -6.412  1.00 18.86 ? 225 ALA A CA    1 
ATOM   596  C C     . ALA A 1 84  ? -52.038 52.610 -6.639  1.00 19.63 ? 225 ALA A C     1 
ATOM   597  O O     . ALA A 1 84  ? -52.227 51.605 -7.347  1.00 17.45 ? 225 ALA A O     1 
ATOM   598  C CB    . ALA A 1 84  ? -52.953 54.858 -7.300  1.00 14.39 ? 225 ALA A CB    1 
ATOM   599  N N     . ARG A 1 85  ? -50.866 52.841 -6.036  1.00 18.12 ? 226 ARG A N     1 
ATOM   600  C CA    . ARG A 1 85  ? -49.799 51.847 -6.137  1.00 18.64 ? 226 ARG A CA    1 
ATOM   601  C C     . ARG A 1 85  ? -50.244 50.511 -5.545  1.00 20.81 ? 226 ARG A C     1 
ATOM   602  O O     . ARG A 1 85  ? -49.947 49.440 -6.091  1.00 17.33 ? 226 ARG A O     1 
ATOM   603  C CB    . ARG A 1 85  ? -48.527 52.342 -5.441  1.00 15.84 ? 226 ARG A CB    1 
ATOM   604  C CG    . ARG A 1 85  ? -47.272 51.554 -5.856  1.00 17.87 ? 226 ARG A CG    1 
ATOM   605  C CD    . ARG A 1 85  ? -46.000 51.965 -5.096  1.00 19.12 ? 226 ARG A CD    1 
ATOM   606  N NE    . ARG A 1 85  ? -45.750 53.398 -5.193  1.00 19.57 ? 226 ARG A NE    1 
ATOM   607  C CZ    . ARG A 1 85  ? -45.046 53.985 -6.152  1.00 22.07 ? 226 ARG A CZ    1 
ATOM   608  N NH1   . ARG A 1 85  ? -44.465 53.282 -7.117  1.00 17.60 ? 226 ARG A NH1   1 
ATOM   609  N NH2   . ARG A 1 85  ? -44.906 55.309 -6.135  1.00 17.59 ? 226 ARG A NH2   1 
ATOM   610  N N     . GLU A 1 86  ? -50.955 50.558 -4.421  1.00 17.77 ? 227 GLU A N     1 
ATOM   611  C CA    . GLU A 1 86  ? -51.417 49.329 -3.792  1.00 22.68 ? 227 GLU A CA    1 
ATOM   612  C C     . GLU A 1 86  ? -52.474 48.632 -4.650  1.00 20.26 ? 227 GLU A C     1 
ATOM   613  O O     . GLU A 1 86  ? -52.510 47.398 -4.704  1.00 19.86 ? 227 GLU A O     1 
ATOM   614  C CB    . GLU A 1 86  ? -51.950 49.649 -2.391  1.00 20.54 ? 227 GLU A CB    1 
ATOM   615  C CG    . GLU A 1 86  ? -52.803 48.559 -1.747  1.00 24.71 ? 227 GLU A CG    1 
ATOM   616  C CD    . GLU A 1 86  ? -52.002 47.301 -1.467  1.00 26.51 ? 227 GLU A CD    1 
ATOM   617  O OE1   . GLU A 1 86  ? -50.747 47.378 -1.458  1.00 27.33 ? 227 GLU A OE1   1 
ATOM   618  O OE2   . GLU A 1 86  ? -52.632 46.238 -1.268  1.00 29.67 ? 227 GLU A OE2   1 
ATOM   619  N N     . ALA A 1 87  ? -53.331 49.400 -5.328  1.00 17.05 ? 228 ALA A N     1 
ATOM   620  C CA    . ALA A 1 87  ? -54.297 48.806 -6.250  1.00 19.27 ? 228 ALA A CA    1 
ATOM   621  C C     . ALA A 1 87  ? -53.589 48.035 -7.353  1.00 19.24 ? 228 ALA A C     1 
ATOM   622  O O     . ALA A 1 87  ? -53.999 46.922 -7.708  1.00 17.32 ? 228 ALA A O     1 
ATOM   623  C CB    . ALA A 1 87  ? -55.192 49.887 -6.860  1.00 16.97 ? 228 ALA A CB    1 
ATOM   624  N N     . VAL A 1 88  ? -52.511 48.611 -7.900  1.00 18.08 ? 229 VAL A N     1 
ATOM   625  C CA    . VAL A 1 88  ? -51.732 47.892 -8.910  1.00 18.25 ? 229 VAL A CA    1 
ATOM   626  C C     . VAL A 1 88  ? -51.116 46.628 -8.312  1.00 19.02 ? 229 VAL A C     1 
ATOM   627  O O     . VAL A 1 88  ? -51.183 45.540 -8.906  1.00 17.05 ? 229 VAL A O     1 
ATOM   628  C CB    . VAL A 1 88  ? -50.655 48.806 -9.517  1.00 18.45 ? 229 VAL A CB    1 
ATOM   629  C CG1   . VAL A 1 88  ? -49.774 48.009 -10.477 1.00 15.85 ? 229 VAL A CG1   1 
ATOM   630  C CG2   . VAL A 1 88  ? -51.317 49.979 -10.236 1.00 16.75 ? 229 VAL A CG2   1 
ATOM   631  N N     . ARG A 1 89  ? -50.487 46.759 -7.137  1.00 15.20 ? 230 ARG A N     1 
ATOM   632  C CA    . ARG A 1 89  ? -49.847 45.603 -6.507  1.00 20.37 ? 230 ARG A CA    1 
ATOM   633  C C     . ARG A 1 89  ? -50.835 44.459 -6.342  1.00 19.17 ? 230 ARG A C     1 
ATOM   634  O O     . ARG A 1 89  ? -50.538 43.303 -6.674  1.00 17.95 ? 230 ARG A O     1 
ATOM   635  C CB    . ARG A 1 89  ? -49.263 45.982 -5.139  1.00 18.62 ? 230 ARG A CB    1 
ATOM   636  C CG    . ARG A 1 89  ? -48.512 44.830 -4.455  1.00 19.32 ? 230 ARG A CG    1 
ATOM   637  C CD    . ARG A 1 89  ? -48.593 44.897 -2.925  1.00 19.95 ? 230 ARG A CD    1 
ATOM   638  N NE    . ARG A 1 89  ? -49.964 44.781 -2.431  1.00 21.93 ? 230 ARG A NE    1 
ATOM   639  C CZ    . ARG A 1 89  ? -50.685 43.664 -2.447  1.00 27.65 ? 230 ARG A CZ    1 
ATOM   640  N NH1   . ARG A 1 89  ? -50.191 42.525 -2.906  1.00 27.10 ? 230 ARG A NH1   1 
ATOM   641  N NH2   . ARG A 1 89  ? -51.930 43.688 -1.979  1.00 28.54 ? 230 ARG A NH2   1 
ATOM   642  N N     . ARG A 1 90  ? -52.014 44.772 -5.806  1.00 18.96 ? 231 ARG A N     1 
ATOM   643  C CA    . ARG A 1 90  ? -53.029 43.758 -5.555  1.00 19.35 ? 231 ARG A CA    1 
ATOM   644  C C     . ARG A 1 90  ? -53.516 43.145 -6.859  1.00 23.55 ? 231 ARG A C     1 
ATOM   645  O O     . ARG A 1 90  ? -53.635 41.917 -6.978  1.00 20.36 ? 231 ARG A O     1 
ATOM   646  C CB    . ARG A 1 90  ? -54.194 44.387 -4.785  1.00 23.31 ? 231 ARG A CB    1 
ATOM   647  C CG    . ARG A 1 90  ? -55.455 43.531 -4.685  1.00 26.09 ? 231 ARG A CG    1 
ATOM   648  C CD    . ARG A 1 90  ? -56.620 44.310 -4.041  1.00 27.85 ? 231 ARG A CD    1 
ATOM   649  N NE    . ARG A 1 90  ? -57.212 45.281 -4.959  1.00 26.17 ? 231 ARG A NE    1 
ATOM   650  C CZ    . ARG A 1 90  ? -57.183 46.598 -4.783  1.00 27.80 ? 231 ARG A CZ    1 
ATOM   651  N NH1   . ARG A 1 90  ? -56.595 47.143 -3.725  1.00 22.37 ? 231 ARG A NH1   1 
ATOM   652  N NH2   . ARG A 1 90  ? -57.737 47.390 -5.702  1.00 23.71 ? 231 ARG A NH2   1 
ATOM   653  N N     . PHE A 1 91  ? -53.790 43.989 -7.861  1.00 21.52 ? 232 PHE A N     1 
ATOM   654  C CA    . PHE A 1 91  ? -54.395 43.494 -9.091  1.00 19.60 ? 232 PHE A CA    1 
ATOM   655  C C     . PHE A 1 91  ? -53.464 42.554 -9.833  1.00 18.68 ? 232 PHE A C     1 
ATOM   656  O O     . PHE A 1 91  ? -53.926 41.603 -10.471 1.00 19.38 ? 232 PHE A O     1 
ATOM   657  C CB    . PHE A 1 91  ? -54.790 44.660 -10.000 1.00 19.85 ? 232 PHE A CB    1 
ATOM   658  C CG    . PHE A 1 91  ? -55.565 44.233 -11.226 1.00 20.42 ? 232 PHE A CG    1 
ATOM   659  C CD1   . PHE A 1 91  ? -56.822 43.657 -11.101 1.00 24.74 ? 232 PHE A CD1   1 
ATOM   660  C CD2   . PHE A 1 91  ? -55.031 44.389 -12.497 1.00 20.64 ? 232 PHE A CD2   1 
ATOM   661  C CE1   . PHE A 1 91  ? -57.555 43.259 -12.231 1.00 22.46 ? 232 PHE A CE1   1 
ATOM   662  C CE2   . PHE A 1 91  ? -55.756 43.992 -13.626 1.00 23.53 ? 232 PHE A CE2   1 
ATOM   663  C CZ    . PHE A 1 91  ? -57.020 43.427 -13.486 1.00 21.47 ? 232 PHE A CZ    1 
ATOM   664  N N     . ILE A 1 92  ? -52.149 42.803 -9.792  1.00 17.19 ? 233 ILE A N     1 
ATOM   665  C CA    . ILE A 1 92  ? -51.241 41.909 -10.508 1.00 17.08 ? 233 ILE A CA    1 
ATOM   666  C C     . ILE A 1 92  ? -50.586 40.883 -9.599  1.00 19.87 ? 233 ILE A C     1 
ATOM   667  O O     . ILE A 1 92  ? -49.775 40.078 -10.074 1.00 22.76 ? 233 ILE A O     1 
ATOM   668  C CB    . ILE A 1 92  ? -50.166 42.677 -11.304 1.00 19.26 ? 233 ILE A CB    1 
ATOM   669  C CG1   . ILE A 1 92  ? -49.168 43.378 -10.388 1.00 18.27 ? 233 ILE A CG1   1 
ATOM   670  C CG2   . ILE A 1 92  ? -50.814 43.667 -12.243 1.00 18.19 ? 233 ILE A CG2   1 
ATOM   671  C CD1   . ILE A 1 92  ? -48.010 44.016 -11.182 1.00 16.73 ? 233 ILE A CD1   1 
ATOM   672  N N     . GLY A 1 93  ? -50.923 40.869 -8.315  1.00 20.87 ? 234 GLY A N     1 
ATOM   673  C CA    . GLY A 1 93  ? -50.372 39.862 -7.421  1.00 22.90 ? 234 GLY A CA    1 
ATOM   674  C C     . GLY A 1 93  ? -48.896 40.020 -7.131  1.00 22.94 ? 234 GLY A C     1 
ATOM   675  O O     . GLY A 1 93  ? -48.187 39.016 -7.010  1.00 24.77 ? 234 GLY A O     1 
ATOM   676  N N     . ALA A 1 94  ? -48.410 41.254 -7.038  1.00 20.57 ? 235 ALA A N     1 
ATOM   677  C CA    . ALA A 1 94  ? -47.041 41.479 -6.607  1.00 20.73 ? 235 ALA A CA    1 
ATOM   678  C C     . ALA A 1 94  ? -46.948 41.325 -5.094  1.00 25.07 ? 235 ALA A C     1 
ATOM   679  O O     . ALA A 1 94  ? -47.887 41.638 -4.356  1.00 23.42 ? 235 ALA A O     1 
ATOM   680  C CB    . ALA A 1 94  ? -46.557 42.866 -7.021  1.00 19.22 ? 235 ALA A CB    1 
ATOM   681  N N     . ALA A 1 95  ? -45.798 40.832 -4.634  1.00 23.06 ? 236 ALA A N     1 
ATOM   682  C CA    . ALA A 1 95  ? -45.599 40.654 -3.201  1.00 23.57 ? 236 ALA A CA    1 
ATOM   683  C C     . ALA A 1 95  ? -45.560 41.993 -2.477  1.00 24.06 ? 236 ALA A C     1 
ATOM   684  O O     . ALA A 1 95  ? -46.095 42.120 -1.375  1.00 25.91 ? 236 ALA A O     1 
ATOM   685  C CB    . ALA A 1 95  ? -44.308 39.871 -2.943  1.00 25.72 ? 236 ALA A CB    1 
ATOM   686  N N     . LYS A 1 96  ? -44.930 43.005 -3.071  1.00 22.48 ? 237 LYS A N     1 
ATOM   687  C CA    . LYS A 1 96  ? -44.702 44.253 -2.356  1.00 22.92 ? 237 LYS A CA    1 
ATOM   688  C C     . LYS A 1 96  ? -44.993 45.442 -3.248  1.00 22.42 ? 237 LYS A C     1 
ATOM   689  O O     . LYS A 1 96  ? -44.720 45.403 -4.453  1.00 20.31 ? 237 LYS A O     1 
ATOM   690  C CB    . LYS A 1 96  ? -43.261 44.354 -1.842  1.00 27.43 ? 237 LYS A CB    1 
ATOM   691  C CG    . LYS A 1 96  ? -42.793 43.180 -0.992  1.00 29.90 ? 237 LYS A CG    1 
ATOM   692  C CD    . LYS A 1 96  ? -41.371 43.428 -0.500  1.00 31.19 ? 237 LYS A CD    1 
ATOM   693  C CE    . LYS A 1 96  ? -40.950 42.381 0.537   1.00 41.63 ? 237 LYS A CE    1 
ATOM   694  N NZ    . LYS A 1 96  ? -39.592 42.694 1.082   1.00 39.31 ? 237 LYS A NZ    1 
ATOM   695  N N     . ALA A 1 97  ? -45.535 46.507 -2.643  1.00 21.03 ? 238 ALA A N     1 
ATOM   696  C CA    . ALA A 1 97  ? -45.766 47.737 -3.400  1.00 21.36 ? 238 ALA A CA    1 
ATOM   697  C C     . ALA A 1 97  ? -44.456 48.348 -3.868  1.00 24.43 ? 238 ALA A C     1 
ATOM   698  O O     . ALA A 1 97  ? -44.427 49.065 -4.878  1.00 20.73 ? 238 ALA A O     1 
ATOM   699  C CB    . ALA A 1 97  ? -46.547 48.746 -2.562  1.00 24.04 ? 238 ALA A CB    1 
ATOM   700  N N     . GLU A 1 98  ? -43.359 48.074 -3.151  1.00 19.88 ? 239 GLU A N     1 
ATOM   701  C CA    . GLU A 1 98  ? -42.040 48.543 -3.560  1.00 23.52 ? 239 GLU A CA    1 
ATOM   702  C C     . GLU A 1 98  ? -41.568 47.916 -4.863  1.00 21.53 ? 239 GLU A C     1 
ATOM   703  O O     . GLU A 1 98  ? -40.545 48.356 -5.399  1.00 20.46 ? 239 GLU A O     1 
ATOM   704  C CB    . GLU A 1 98  ? -41.023 48.265 -2.448  1.00 21.62 ? 239 GLU A CB    1 
ATOM   705  C CG    . GLU A 1 98  ? -41.267 49.130 -1.207  1.00 30.56 ? 239 GLU A CG    1 
ATOM   706  C CD    . GLU A 1 98  ? -42.246 48.511 -0.199  1.00 40.82 ? 239 GLU A CD    1 
ATOM   707  O OE1   . GLU A 1 98  ? -42.975 47.539 -0.537  1.00 32.07 ? 239 GLU A OE1   1 
ATOM   708  O OE2   . GLU A 1 98  ? -42.271 48.998 0.953   1.00 49.84 ? 239 GLU A OE2   1 
ATOM   709  N N     . GLU A 1 99  ? -42.274 46.910 -5.377  1.00 19.13 ? 240 GLU A N     1 
ATOM   710  C CA    . GLU A 1 99  ? -41.949 46.307 -6.662  1.00 19.96 ? 240 GLU A CA    1 
ATOM   711  C C     . GLU A 1 99  ? -42.733 46.941 -7.814  1.00 16.99 ? 240 GLU A C     1 
ATOM   712  O O     . GLU A 1 99  ? -42.578 46.521 -8.963  1.00 17.25 ? 240 GLU A O     1 
ATOM   713  C CB    . GLU A 1 99  ? -42.218 44.798 -6.608  1.00 20.61 ? 240 GLU A CB    1 
ATOM   714  C CG    . GLU A 1 99  ? -41.432 44.073 -5.489  1.00 23.20 ? 240 GLU A CG    1 
ATOM   715  C CD    . GLU A 1 99  ? -41.714 42.558 -5.384  1.00 29.32 ? 240 GLU A CD    1 
ATOM   716  O OE1   . GLU A 1 99  ? -42.894 42.156 -5.234  1.00 24.67 ? 240 GLU A OE1   1 
ATOM   717  O OE2   . GLU A 1 99  ? -40.729 41.775 -5.317  1.00 27.56 ? 240 GLU A OE2   1 
ATOM   718  N N     . ILE A 1 100 ? -43.556 47.944 -7.528  1.00 17.11 ? 241 ILE A N     1 
ATOM   719  C CA    . ILE A 1 100 ? -44.394 48.622 -8.516  1.00 16.45 ? 241 ILE A CA    1 
ATOM   720  C C     . ILE A 1 100 ? -43.768 49.974 -8.828  1.00 16.96 ? 241 ILE A C     1 
ATOM   721  O O     . ILE A 1 100 ? -43.663 50.830 -7.941  1.00 17.91 ? 241 ILE A O     1 
ATOM   722  C CB    . ILE A 1 100 ? -45.828 48.812 -7.995  1.00 17.65 ? 241 ILE A CB    1 
ATOM   723  C CG1   . ILE A 1 100 ? -46.477 47.469 -7.607  1.00 19.47 ? 241 ILE A CG1   1 
ATOM   724  C CG2   . ILE A 1 100 ? -46.678 49.594 -9.032  1.00 14.80 ? 241 ILE A CG2   1 
ATOM   725  C CD1   . ILE A 1 100 ? -46.474 46.440 -8.729  1.00 18.79 ? 241 ILE A CD1   1 
ATOM   726  N N     . ILE A 1 101 ? -43.375 50.192 -10.081 1.00 16.24 ? 242 ILE A N     1 
ATOM   727  C CA    . ILE A 1 101 ? -42.787 51.451 -10.533 1.00 14.07 ? 242 ILE A CA    1 
ATOM   728  C C     . ILE A 1 101 ? -43.767 52.109 -11.491 1.00 18.12 ? 242 ILE A C     1 
ATOM   729  O O     . ILE A 1 101 ? -44.154 51.501 -12.498 1.00 14.46 ? 242 ILE A O     1 
ATOM   730  C CB    . ILE A 1 101 ? -41.438 51.240 -11.238 1.00 15.98 ? 242 ILE A CB    1 
ATOM   731  C CG1   . ILE A 1 101 ? -40.511 50.326 -10.428 1.00 16.44 ? 242 ILE A CG1   1 
ATOM   732  C CG2   . ILE A 1 101 ? -40.785 52.599 -11.544 1.00 14.78 ? 242 ILE A CG2   1 
ATOM   733  C CD1   . ILE A 1 101 ? -40.193 50.880 -9.042  1.00 19.81 ? 242 ILE A CD1   1 
ATOM   734  N N     . PHE A 1 102 ? -44.137 53.359 -11.199 1.00 14.10 ? 243 PHE A N     1 
ATOM   735  C CA    . PHE A 1 102 ? -44.969 54.147 -12.096 1.00 17.59 ? 243 PHE A CA    1 
ATOM   736  C C     . PHE A 1 102 ? -44.105 54.876 -13.114 1.00 16.49 ? 243 PHE A C     1 
ATOM   737  O O     . PHE A 1 102 ? -43.045 55.408 -12.770 1.00 15.15 ? 243 PHE A O     1 
ATOM   738  C CB    . PHE A 1 102 ? -45.796 55.161 -11.304 1.00 16.25 ? 243 PHE A CB    1 
ATOM   739  C CG    . PHE A 1 102 ? -47.021 54.574 -10.666 1.00 18.08 ? 243 PHE A CG    1 
ATOM   740  C CD1   . PHE A 1 102 ? -47.886 53.769 -11.397 1.00 15.61 ? 243 PHE A CD1   1 
ATOM   741  C CD2   . PHE A 1 102 ? -47.315 54.841 -9.328  1.00 16.55 ? 243 PHE A CD2   1 
ATOM   742  C CE1   . PHE A 1 102 ? -49.048 53.240 -10.809 1.00 17.38 ? 243 PHE A CE1   1 
ATOM   743  C CE2   . PHE A 1 102 ? -48.457 54.309 -8.734  1.00 18.65 ? 243 PHE A CE2   1 
ATOM   744  C CZ    . PHE A 1 102 ? -49.323 53.505 -9.472  1.00 17.75 ? 243 PHE A CZ    1 
ATOM   745  N N     . LEU A 1 103 ? -44.548 54.873 -14.370 1.00 13.70 ? 244 LEU A N     1 
ATOM   746  C CA    . LEU A 1 103 ? -43.898 55.625 -15.447 1.00 15.00 ? 244 LEU A CA    1 
ATOM   747  C C     . LEU A 1 103 ? -44.971 55.877 -16.506 1.00 16.27 ? 244 LEU A C     1 
ATOM   748  O O     . LEU A 1 103 ? -46.160 55.745 -16.212 1.00 13.93 ? 244 LEU A O     1 
ATOM   749  C CB    . LEU A 1 103 ? -42.655 54.881 -15.974 1.00 16.23 ? 244 LEU A CB    1 
ATOM   750  C CG    . LEU A 1 103 ? -42.557 53.390 -15.668 1.00 19.30 ? 244 LEU A CG    1 
ATOM   751  C CD1   . LEU A 1 103 ? -43.547 52.655 -16.570 1.00 17.46 ? 244 LEU A CD1   1 
ATOM   752  C CD2   . LEU A 1 103 ? -41.131 52.853 -15.865 1.00 16.27 ? 244 LEU A CD2   1 
ATOM   753  N N     . ARG A 1 104 ? -44.576 56.217 -17.742 1.00 13.15 ? 245 ARG A N     1 
ATOM   754  C CA    . ARG A 1 104 ? -45.605 56.642 -18.697 1.00 15.50 ? 245 ARG A CA    1 
ATOM   755  C C     . ARG A 1 104 ? -46.343 55.463 -19.346 1.00 15.40 ? 245 ARG A C     1 
ATOM   756  O O     . ARG A 1 104 ? -47.539 55.578 -19.655 1.00 17.44 ? 245 ARG A O     1 
ATOM   757  C CB    . ARG A 1 104 ? -44.997 57.547 -19.779 1.00 15.88 ? 245 ARG A CB    1 
ATOM   758  C CG    . ARG A 1 104 ? -45.934 57.757 -21.015 1.00 21.61 ? 245 ARG A CG    1 
ATOM   759  C CD    . ARG A 1 104 ? -45.576 58.964 -21.927 1.00 17.99 ? 245 ARG A CD    1 
ATOM   760  N NE    . ARG A 1 104 ? -44.188 58.888 -22.381 1.00 21.43 ? 245 ARG A NE    1 
ATOM   761  C CZ    . ARG A 1 104 ? -43.162 59.458 -21.754 1.00 25.00 ? 245 ARG A CZ    1 
ATOM   762  N NH1   . ARG A 1 104 ? -43.351 60.315 -20.760 1.00 21.50 ? 245 ARG A NH1   1 
ATOM   763  N NH2   . ARG A 1 104 ? -41.916 59.170 -22.137 1.00 18.93 ? 245 ARG A NH2   1 
ATOM   764  N N     . GLY A 1 105 ? -45.674 54.337 -19.564 1.00 13.00 ? 246 GLY A N     1 
ATOM   765  C CA    . GLY A 1 105 ? -46.350 53.198 -20.158 1.00 14.86 ? 246 GLY A CA    1 
ATOM   766  C C     . GLY A 1 105 ? -45.380 52.064 -20.418 1.00 16.07 ? 246 GLY A C     1 
ATOM   767  O O     . GLY A 1 105 ? -44.231 52.090 -19.977 1.00 14.45 ? 246 GLY A O     1 
ATOM   768  N N     . THR A 1 106 ? -45.876 51.062 -21.145 1.00 14.10 ? 247 THR A N     1 
ATOM   769  C CA    . THR A 1 106 ? -45.088 49.878 -21.468 1.00 14.98 ? 247 THR A CA    1 
ATOM   770  C C     . THR A 1 106 ? -43.757 50.245 -22.122 1.00 12.71 ? 247 THR A C     1 
ATOM   771  O O     . THR A 1 106 ? -42.710 49.683 -21.783 1.00 13.98 ? 247 THR A O     1 
ATOM   772  C CB    . THR A 1 106 ? -45.904 48.971 -22.400 1.00 15.17 ? 247 THR A CB    1 
ATOM   773  O OG1   . THR A 1 106 ? -47.113 48.544 -21.747 1.00 18.13 ? 247 THR A OG1   1 
ATOM   774  C CG2   . THR A 1 106 ? -45.090 47.762 -22.826 1.00 16.30 ? 247 THR A CG2   1 
ATOM   775  N N     . THR A 1 107 ? -43.783 51.186 -23.067 1.00 13.96 ? 248 THR A N     1 
ATOM   776  C CA    . THR A 1 107 ? -42.576 51.539 -23.818 1.00 12.26 ? 248 THR A CA    1 
ATOM   777  C C     . THR A 1 107 ? -41.502 52.130 -22.903 1.00 13.26 ? 248 THR A C     1 
ATOM   778  O O     . THR A 1 107 ? -40.322 51.746 -22.971 1.00 12.51 ? 248 THR A O     1 
ATOM   779  C CB    . THR A 1 107 ? -42.939 52.517 -24.947 1.00 14.73 ? 248 THR A CB    1 
ATOM   780  O OG1   . THR A 1 107 ? -43.931 51.926 -25.802 1.00 14.61 ? 248 THR A OG1   1 
ATOM   781  C CG2   . THR A 1 107 ? -41.712 52.867 -25.802 1.00 12.31 ? 248 THR A CG2   1 
ATOM   782  N N     . GLU A 1 108 ? -41.887 53.069 -22.033 1.00 10.93 ? 249 GLU A N     1 
ATOM   783  C CA    . GLU A 1 108 ? -40.905 53.604 -21.096 1.00 14.02 ? 249 GLU A CA    1 
ATOM   784  C C     . GLU A 1 108 ? -40.402 52.513 -20.157 1.00 10.60 ? 249 GLU A C     1 
ATOM   785  O O     . GLU A 1 108 ? -39.219 52.477 -19.831 1.00 14.04 ? 249 GLU A O     1 
ATOM   786  C CB    . GLU A 1 108 ? -41.476 54.780 -20.283 1.00 14.38 ? 249 GLU A CB    1 
ATOM   787  C CG    . GLU A 1 108 ? -40.472 55.287 -19.223 1.00 15.59 ? 249 GLU A CG    1 
ATOM   788  C CD    . GLU A 1 108 ? -40.849 56.616 -18.557 1.00 22.68 ? 249 GLU A CD    1 
ATOM   789  O OE1   . GLU A 1 108 ? -42.047 56.984 -18.531 1.00 19.54 ? 249 GLU A OE1   1 
ATOM   790  O OE2   . GLU A 1 108 ? -39.943 57.267 -17.978 1.00 21.93 ? 249 GLU A OE2   1 
ATOM   791  N N     . ALA A 1 109 ? -41.272 51.596 -19.735 1.00 13.81 ? 250 ALA A N     1 
ATOM   792  C CA    . ALA A 1 109 ? -40.835 50.536 -18.812 1.00 14.48 ? 250 ALA A CA    1 
ATOM   793  C C     . ALA A 1 109 ? -39.797 49.619 -19.454 1.00 15.07 ? 250 ALA A C     1 
ATOM   794  O O     . ALA A 1 109 ? -38.785 49.245 -18.825 1.00 13.99 ? 250 ALA A O     1 
ATOM   795  C CB    . ALA A 1 109 ? -42.041 49.716 -18.354 1.00 13.02 ? 250 ALA A CB    1 
ATOM   796  N N     . ILE A 1 110 ? -40.034 49.229 -20.707 1.00 13.53 ? 251 ILE A N     1 
ATOM   797  C CA    . ILE A 1 110 ? -39.065 48.374 -21.380 1.00 13.69 ? 251 ILE A CA    1 
ATOM   798  C C     . ILE A 1 110 ? -37.761 49.129 -21.614 1.00 15.74 ? 251 ILE A C     1 
ATOM   799  O O     . ILE A 1 110 ? -36.666 48.555 -21.503 1.00 13.47 ? 251 ILE A O     1 
ATOM   800  C CB    . ILE A 1 110 ? -39.641 47.835 -22.696 1.00 13.27 ? 251 ILE A CB    1 
ATOM   801  C CG1   . ILE A 1 110 ? -40.846 46.915 -22.418 1.00 13.41 ? 251 ILE A CG1   1 
ATOM   802  C CG2   . ILE A 1 110 ? -38.526 47.122 -23.485 1.00 14.64 ? 251 ILE A CG2   1 
ATOM   803  C CD1   . ILE A 1 110 ? -41.537 46.428 -23.677 1.00 12.56 ? 251 ILE A CD1   1 
ATOM   804  N N     . ASN A 1 111 ? -37.848 50.421 -21.959 1.00 13.41 ? 252 ASN A N     1 
ATOM   805  C CA    . ASN A 1 111 ? -36.617 51.190 -22.135 1.00 15.19 ? 252 ASN A CA    1 
ATOM   806  C C     . ASN A 1 111 ? -35.848 51.299 -20.826 1.00 13.40 ? 252 ASN A C     1 
ATOM   807  O O     . ASN A 1 111 ? -34.617 51.272 -20.827 1.00 15.02 ? 252 ASN A O     1 
ATOM   808  C CB    . ASN A 1 111 ? -36.923 52.575 -22.702 1.00 11.97 ? 252 ASN A CB    1 
ATOM   809  C CG    . ASN A 1 111 ? -37.091 52.545 -24.202 1.00 15.93 ? 252 ASN A CG    1 
ATOM   810  O OD1   . ASN A 1 111 ? -36.118 52.662 -24.946 1.00 15.52 ? 252 ASN A OD1   1 
ATOM   811  N ND2   . ASN A 1 111 ? -38.331 52.380 -24.662 1.00 11.44 ? 252 ASN A ND2   1 
ATOM   812  N N     . LEU A 1 112 ? -36.557 51.429 -19.699 1.00 14.10 ? 253 LEU A N     1 
ATOM   813  C CA    . LEU A 1 112 ? -35.877 51.458 -18.407 1.00 15.70 ? 253 LEU A CA    1 
ATOM   814  C C     . LEU A 1 112 ? -35.067 50.195 -18.219 1.00 15.31 ? 253 LEU A C     1 
ATOM   815  O O     . LEU A 1 112 ? -33.857 50.252 -17.959 1.00 14.62 ? 253 LEU A O     1 
ATOM   816  C CB    . LEU A 1 112 ? -36.883 51.616 -17.253 1.00 15.06 ? 253 LEU A CB    1 
ATOM   817  C CG    . LEU A 1 112 ? -36.294 51.888 -15.847 1.00 17.30 ? 253 LEU A CG    1 
ATOM   818  C CD1   . LEU A 1 112 ? -37.329 52.599 -14.952 1.00 16.87 ? 253 LEU A CD1   1 
ATOM   819  C CD2   . LEU A 1 112 ? -35.806 50.616 -15.148 1.00 13.95 ? 253 LEU A CD2   1 
ATOM   820  N N     . VAL A 1 113 ? -35.724 49.038 -18.351 1.00 17.22 ? 254 VAL A N     1 
ATOM   821  C CA    . VAL A 1 113 ? -35.019 47.763 -18.151 1.00 15.73 ? 254 VAL A CA    1 
ATOM   822  C C     . VAL A 1 113 ? -33.844 47.637 -19.119 1.00 18.74 ? 254 VAL A C     1 
ATOM   823  O O     . VAL A 1 113 ? -32.712 47.313 -18.715 1.00 16.63 ? 254 VAL A O     1 
ATOM   824  C CB    . VAL A 1 113 ? -35.993 46.578 -18.290 1.00 16.55 ? 254 VAL A CB    1 
ATOM   825  C CG1   . VAL A 1 113 ? -35.236 45.247 -18.172 1.00 16.53 ? 254 VAL A CG1   1 
ATOM   826  C CG2   . VAL A 1 113 ? -37.115 46.682 -17.229 1.00 16.39 ? 254 VAL A CG2   1 
ATOM   827  N N     . ALA A 1 114 ? -34.081 47.944 -20.400 1.00 17.41 ? 255 ALA A N     1 
ATOM   828  C CA    . ALA A 1 114 ? -33.034 47.814 -21.407 1.00 19.51 ? 255 ALA A CA    1 
ATOM   829  C C     . ALA A 1 114 ? -31.830 48.676 -21.053 1.00 20.56 ? 255 ALA A C     1 
ATOM   830  O O     . ALA A 1 114 ? -30.727 48.163 -20.854 1.00 20.01 ? 255 ALA A O     1 
ATOM   831  C CB    . ALA A 1 114 ? -33.576 48.171 -22.795 1.00 18.30 ? 255 ALA A CB    1 
ATOM   832  N N     A HIS A 1 115 ? -32.047 49.983 -20.907 0.52 19.28 ? 256 HIS A N     1 
ATOM   833  N N     B HIS A 1 115 ? -32.020 49.990 -20.919 0.48 18.75 ? 256 HIS A N     1 
ATOM   834  C CA    A HIS A 1 115 ? -30.945 50.910 -20.683 0.52 20.14 ? 256 HIS A CA    1 
ATOM   835  C CA    B HIS A 1 115 ? -30.853 50.837 -20.690 0.48 20.26 ? 256 HIS A CA    1 
ATOM   836  C C     A HIS A 1 115 ? -30.243 50.617 -19.359 0.52 21.29 ? 256 HIS A C     1 
ATOM   837  C C     B HIS A 1 115 ? -30.218 50.550 -19.336 0.48 21.14 ? 256 HIS A C     1 
ATOM   838  O O     A HIS A 1 115 ? -29.062 50.268 -19.343 0.52 22.26 ? 256 HIS A O     1 
ATOM   839  O O     B HIS A 1 115 ? -29.044 50.189 -19.269 0.48 22.03 ? 256 HIS A O     1 
ATOM   840  C CB    A HIS A 1 115 ? -31.473 52.347 -20.738 0.52 19.29 ? 256 HIS A CB    1 
ATOM   841  C CB    B HIS A 1 115 ? -31.183 52.323 -20.802 0.48 19.47 ? 256 HIS A CB    1 
ATOM   842  C CG    A HIS A 1 115 ? -32.015 52.749 -22.080 0.52 20.62 ? 256 HIS A CG    1 
ATOM   843  C CG    B HIS A 1 115 ? -29.978 53.198 -20.620 0.48 22.11 ? 256 HIS A CG    1 
ATOM   844  N ND1   A HIS A 1 115 ? -31.786 53.991 -22.632 0.52 22.42 ? 256 HIS A ND1   1 
ATOM   845  N ND1   B HIS A 1 115 ? -29.723 53.886 -19.451 0.48 22.78 ? 256 HIS A ND1   1 
ATOM   846  C CD2   A HIS A 1 115 ? -32.768 52.072 -22.983 0.52 20.81 ? 256 HIS A CD2   1 
ATOM   847  C CD2   B HIS A 1 115 ? -28.941 53.472 -21.448 0.48 21.32 ? 256 HIS A CD2   1 
ATOM   848  C CE1   A HIS A 1 115 ? -32.380 54.065 -23.811 0.52 22.29 ? 256 HIS A CE1   1 
ATOM   849  C CE1   B HIS A 1 115 ? -28.589 54.553 -19.571 0.48 21.82 ? 256 HIS A CE1   1 
ATOM   850  N NE2   A HIS A 1 115 ? -32.980 52.913 -24.049 0.52 20.97 ? 256 HIS A NE2   1 
ATOM   851  N NE2   B HIS A 1 115 ? -28.097 54.322 -20.776 0.48 22.41 ? 256 HIS A NE2   1 
ATOM   852  N N     . ALA A 1 116 ? -30.977 50.661 -18.242 1.00 18.37 ? 257 ALA A N     1 
ATOM   853  C CA    . ALA A 1 116 ? -30.345 50.535 -16.927 1.00 19.26 ? 257 ALA A CA    1 
ATOM   854  C C     . ALA A 1 116 ? -29.862 49.106 -16.669 1.00 20.56 ? 257 ALA A C     1 
ATOM   855  O O     . ALA A 1 116 ? -28.650 48.859 -16.520 1.00 19.93 ? 257 ALA A O     1 
ATOM   856  C CB    . ALA A 1 116 ? -31.304 51.019 -15.827 1.00 14.87 ? 257 ALA A CB    1 
ATOM   857  N N     . TRP A 1 117 ? -30.786 48.136 -16.631 1.00 17.82 ? 258 TRP A N     1 
ATOM   858  C CA    . TRP A 1 117 ? -30.363 46.772 -16.348 1.00 20.58 ? 258 TRP A CA    1 
ATOM   859  C C     . TRP A 1 117 ? -29.449 46.241 -17.458 1.00 20.59 ? 258 TRP A C     1 
ATOM   860  O O     . TRP A 1 117 ? -28.396 45.644 -17.182 1.00 20.98 ? 258 TRP A O     1 
ATOM   861  C CB    . TRP A 1 117 ? -31.590 45.871 -16.162 1.00 20.29 ? 258 TRP A CB    1 
ATOM   862  C CG    . TRP A 1 117 ? -31.215 44.469 -15.773 1.00 23.25 ? 258 TRP A CG    1 
ATOM   863  C CD1   . TRP A 1 117 ? -31.120 43.969 -14.503 1.00 23.56 ? 258 TRP A CD1   1 
ATOM   864  C CD2   . TRP A 1 117 ? -30.868 43.393 -16.655 1.00 23.77 ? 258 TRP A CD2   1 
ATOM   865  N NE1   . TRP A 1 117 ? -30.735 42.647 -14.542 1.00 25.18 ? 258 TRP A NE1   1 
ATOM   866  C CE2   . TRP A 1 117 ? -30.576 42.267 -15.848 1.00 25.65 ? 258 TRP A CE2   1 
ATOM   867  C CE3   . TRP A 1 117 ? -30.796 43.264 -18.050 1.00 24.46 ? 258 TRP A CE3   1 
ATOM   868  C CZ2   . TRP A 1 117 ? -30.200 41.031 -16.387 1.00 28.79 ? 258 TRP A CZ2   1 
ATOM   869  C CZ3   . TRP A 1 117 ? -30.426 42.035 -18.585 1.00 28.14 ? 258 TRP A CZ3   1 
ATOM   870  C CH2   . TRP A 1 117 ? -30.135 40.934 -17.753 1.00 28.29 ? 258 TRP A CH2   1 
ATOM   871  N N     . GLY A 1 118 ? -29.841 46.429 -18.725 1.00 19.01 ? 259 GLY A N     1 
ATOM   872  C CA    . GLY A 1 118 ? -29.054 45.897 -19.820 1.00 20.94 ? 259 GLY A CA    1 
ATOM   873  C C     . GLY A 1 118 ? -27.654 46.474 -19.889 1.00 25.72 ? 259 GLY A C     1 
ATOM   874  O O     . GLY A 1 118 ? -26.690 45.724 -20.069 1.00 26.85 ? 259 GLY A O     1 
ATOM   875  N N     . GLY A 1 119 ? -27.505 47.809 -19.768 1.00 24.26 ? 260 GLY A N     1 
ATOM   876  C CA    . GLY A 1 119 ? -26.177 48.380 -19.781 1.00 23.98 ? 260 GLY A CA    1 
ATOM   877  C C     . GLY A 1 119 ? -25.337 47.969 -18.600 1.00 28.56 ? 260 GLY A C     1 
ATOM   878  O O     . GLY A 1 119 ? -24.103 47.992 -18.694 1.00 30.13 ? 260 GLY A O     1 
ATOM   879  N N     . LYS A 1 120 ? -25.965 47.586 -17.485 1.00 26.81 ? 261 LYS A N     1 
ATOM   880  C CA    . LYS A 1 120 ? -25.126 47.083 -16.406 1.00 26.66 ? 261 LYS A CA    1 
ATOM   881  C C     . LYS A 1 120 ? -24.718 45.622 -16.601 1.00 31.59 ? 261 LYS A C     1 
ATOM   882  O O     . LYS A 1 120 ? -23.625 45.233 -16.169 1.00 30.72 ? 261 LYS A O     1 
ATOM   883  C CB    . LYS A 1 120 ? -25.824 47.243 -15.055 1.00 28.39 ? 261 LYS A CB    1 
ATOM   884  C CG    . LYS A 1 120 ? -24.866 47.152 -13.886 1.00 34.09 ? 261 LYS A CG    1 
ATOM   885  C CD    . LYS A 1 120 ? -25.422 46.326 -12.741 1.00 38.72 ? 261 LYS A CD    1 
ATOM   886  C CE    . LYS A 1 120 ? -24.837 46.765 -11.400 1.00 42.66 ? 261 LYS A CE    1 
ATOM   887  N NZ    . LYS A 1 120 ? -25.650 46.256 -10.257 1.00 46.66 ? 261 LYS A NZ    1 
ATOM   888  N N     . HIS A 1 121 ? -25.557 44.787 -17.228 1.00 26.50 ? 262 HIS A N     1 
ATOM   889  C CA    . HIS A 1 121 ? -25.306 43.349 -17.182 1.00 26.57 ? 262 HIS A CA    1 
ATOM   890  C C     . HIS A 1 121 ? -24.933 42.694 -18.510 1.00 32.10 ? 262 HIS A C     1 
ATOM   891  O O     . HIS A 1 121 ? -24.529 41.526 -18.499 1.00 33.08 ? 262 HIS A O     1 
ATOM   892  C CB    . HIS A 1 121 ? -26.525 42.617 -16.605 1.00 24.58 ? 262 HIS A CB    1 
ATOM   893  C CG    . HIS A 1 121 ? -26.839 43.010 -15.198 1.00 31.76 ? 262 HIS A CG    1 
ATOM   894  N ND1   . HIS A 1 121 ? -26.204 42.448 -14.109 1.00 32.71 ? 262 HIS A ND1   1 
ATOM   895  C CD2   . HIS A 1 121 ? -27.702 43.929 -14.701 1.00 25.51 ? 262 HIS A CD2   1 
ATOM   896  C CE1   . HIS A 1 121 ? -26.672 42.997 -13.000 1.00 33.24 ? 262 HIS A CE1   1 
ATOM   897  N NE2   . HIS A 1 121 ? -27.585 43.895 -13.332 1.00 30.66 ? 262 HIS A NE2   1 
ATOM   898  N N     . LEU A 1 122 ? -25.041 43.383 -19.642 1.00 26.25 ? 263 LEU A N     1 
ATOM   899  C CA    . LEU A 1 122 ? -24.809 42.745 -20.932 1.00 29.31 ? 263 LEU A CA    1 
ATOM   900  C C     . LEU A 1 122 ? -23.482 43.181 -21.543 1.00 31.79 ? 263 LEU A C     1 
ATOM   901  O O     . LEU A 1 122 ? -23.055 44.331 -21.406 1.00 31.07 ? 263 LEU A O     1 
ATOM   902  C CB    . LEU A 1 122 ? -25.943 43.044 -21.916 1.00 30.46 ? 263 LEU A CB    1 
ATOM   903  C CG    . LEU A 1 122 ? -27.316 42.482 -21.560 1.00 31.91 ? 263 LEU A CG    1 
ATOM   904  C CD1   . LEU A 1 122 ? -28.213 42.514 -22.767 1.00 38.20 ? 263 LEU A CD1   1 
ATOM   905  C CD2   . LEU A 1 122 ? -27.210 41.071 -21.048 1.00 36.70 ? 263 LEU A CD2   1 
ATOM   906  N N     . GLY A 1 123 ? -22.839 42.240 -22.229 1.00 30.08 ? 264 GLY A N     1 
ATOM   907  C CA    . GLY A 1 123 ? -21.618 42.507 -22.946 1.00 29.19 ? 264 GLY A CA    1 
ATOM   908  C C     . GLY A 1 123 ? -21.497 41.645 -24.189 1.00 32.70 ? 264 GLY A C     1 
ATOM   909  O O     . GLY A 1 123 ? -22.408 40.876 -24.524 1.00 29.93 ? 264 GLY A O     1 
ATOM   910  N N     . PRO A 1 124 ? -20.359 41.750 -24.885 1.00 29.06 ? 265 PRO A N     1 
ATOM   911  C CA    . PRO A 1 124 ? -20.224 41.114 -26.205 1.00 29.80 ? 265 PRO A CA    1 
ATOM   912  C C     . PRO A 1 124 ? -20.507 39.618 -26.178 1.00 31.36 ? 265 PRO A C     1 
ATOM   913  O O     . PRO A 1 124 ? -19.985 38.878 -25.344 1.00 30.49 ? 265 PRO A O     1 
ATOM   914  C CB    . PRO A 1 124 ? -18.769 41.412 -26.588 1.00 30.52 ? 265 PRO A CB    1 
ATOM   915  C CG    . PRO A 1 124 ? -18.505 42.747 -25.922 1.00 29.98 ? 265 PRO A CG    1 
ATOM   916  C CD    . PRO A 1 124 ? -19.237 42.664 -24.595 1.00 25.84 ? 265 PRO A CD    1 
ATOM   917  N N     . GLY A 1 125 ? -21.346 39.174 -27.115 1.00 34.90 ? 266 GLY A N     1 
ATOM   918  C CA    . GLY A 1 125 ? -21.676 37.773 -27.240 1.00 31.94 ? 266 GLY A CA    1 
ATOM   919  C C     . GLY A 1 125 ? -22.795 37.290 -26.344 1.00 35.18 ? 266 GLY A C     1 
ATOM   920  O O     . GLY A 1 125 ? -23.356 36.219 -26.613 1.00 36.80 ? 266 GLY A O     1 
ATOM   921  N N     . ASP A 1 126 ? -23.128 38.025 -25.280 1.00 31.97 ? 267 ASP A N     1 
ATOM   922  C CA    . ASP A 1 126 ? -24.316 37.714 -24.495 1.00 32.13 ? 267 ASP A CA    1 
ATOM   923  C C     . ASP A 1 126 ? -25.551 37.735 -25.388 1.00 33.39 ? 267 ASP A C     1 
ATOM   924  O O     . ASP A 1 126 ? -25.620 38.478 -26.367 1.00 29.98 ? 267 ASP A O     1 
ATOM   925  C CB    . ASP A 1 126 ? -24.498 38.727 -23.363 1.00 33.88 ? 267 ASP A CB    1 
ATOM   926  C CG    . ASP A 1 126 ? -23.433 38.612 -22.302 1.00 37.86 ? 267 ASP A CG    1 
ATOM   927  O OD1   . ASP A 1 126 ? -22.708 37.594 -22.317 1.00 36.44 ? 267 ASP A OD1   1 
ATOM   928  O OD2   . ASP A 1 126 ? -23.324 39.541 -21.467 1.00 34.17 ? 267 ASP A OD2   1 
ATOM   929  N N     . GLU A 1 127 ? -26.554 36.939 -25.024 1.00 28.30 ? 268 GLU A N     1 
ATOM   930  C CA    . GLU A 1 127 ? -27.702 36.728 -25.890 1.00 27.85 ? 268 GLU A CA    1 
ATOM   931  C C     . GLU A 1 127 ? -28.985 37.196 -25.217 1.00 21.46 ? 268 GLU A C     1 
ATOM   932  O O     . GLU A 1 127 ? -29.217 36.919 -24.034 1.00 24.91 ? 268 GLU A O     1 
ATOM   933  C CB    . GLU A 1 127 ? -27.789 35.252 -26.293 1.00 29.92 ? 268 GLU A CB    1 
ATOM   934  C CG    . GLU A 1 127 ? -26.482 34.770 -26.931 1.00 35.54 ? 268 GLU A CG    1 
ATOM   935  C CD    . GLU A 1 127 ? -26.598 33.431 -27.648 1.00 42.02 ? 268 GLU A CD    1 
ATOM   936  O OE1   . GLU A 1 127 ? -27.388 32.572 -27.198 1.00 36.16 ? 268 GLU A OE1   1 
ATOM   937  O OE2   . GLU A 1 127 ? -25.852 33.227 -28.638 1.00 43.92 ? 268 GLU A OE2   1 
ATOM   938  N N     . ILE A 1 128 ? -29.799 37.920 -25.981 1.00 22.23 ? 269 ILE A N     1 
ATOM   939  C CA    . ILE A 1 128 ? -31.163 38.292 -25.617 1.00 24.18 ? 269 ILE A CA    1 
ATOM   940  C C     . ILE A 1 128 ? -32.099 37.517 -26.534 1.00 21.47 ? 269 ILE A C     1 
ATOM   941  O O     . ILE A 1 128 ? -31.912 37.514 -27.755 1.00 26.41 ? 269 ILE A O     1 
ATOM   942  C CB    . ILE A 1 128 ? -31.400 39.807 -25.775 1.00 22.70 ? 269 ILE A CB    1 
ATOM   943  C CG1   . ILE A 1 128 ? -30.354 40.622 -25.031 1.00 24.43 ? 269 ILE A CG1   1 
ATOM   944  C CG2   . ILE A 1 128 ? -32.847 40.204 -25.362 1.00 20.27 ? 269 ILE A CG2   1 
ATOM   945  C CD1   . ILE A 1 128 ? -29.986 41.913 -25.760 1.00 25.87 ? 269 ILE A CD1   1 
ATOM   946  N N     . VAL A 1 129 ? -33.093 36.855 -25.960 1.00 23.64 ? 270 VAL A N     1 
ATOM   947  C CA    . VAL A 1 129 ? -34.073 36.111 -26.743 1.00 24.02 ? 270 VAL A CA    1 
ATOM   948  C C     . VAL A 1 129 ? -35.404 36.845 -26.659 1.00 24.47 ? 270 VAL A C     1 
ATOM   949  O O     . VAL A 1 129 ? -35.906 37.106 -25.558 1.00 21.07 ? 270 VAL A O     1 
ATOM   950  C CB    . VAL A 1 129 ? -34.211 34.658 -26.264 1.00 22.60 ? 270 VAL A CB    1 
ATOM   951  C CG1   . VAL A 1 129 ? -35.273 33.948 -27.082 1.00 25.78 ? 270 VAL A CG1   1 
ATOM   952  C CG2   . VAL A 1 129 ? -32.871 33.928 -26.405 1.00 21.75 ? 270 VAL A CG2   1 
ATOM   953  N N     . ILE A 1 130 ? -35.957 37.200 -27.819 1.00 22.94 ? 271 ILE A N     1 
ATOM   954  C CA    . ILE A 1 130 ? -37.320 37.713 -27.929 1.00 24.74 ? 271 ILE A CA    1 
ATOM   955  C C     . ILE A 1 130 ? -38.097 36.776 -28.849 1.00 26.51 ? 271 ILE A C     1 
ATOM   956  O O     . ILE A 1 130 ? -37.529 35.929 -29.536 1.00 22.66 ? 271 ILE A O     1 
ATOM   957  C CB    . ILE A 1 130 ? -37.374 39.161 -28.462 1.00 21.59 ? 271 ILE A CB    1 
ATOM   958  C CG1   . ILE A 1 130 ? -36.840 39.224 -29.894 1.00 22.78 ? 271 ILE A CG1   1 
ATOM   959  C CG2   . ILE A 1 130 ? -36.596 40.104 -27.565 1.00 23.01 ? 271 ILE A CG2   1 
ATOM   960  C CD1   . ILE A 1 130 ? -37.170 40.538 -30.619 1.00 25.89 ? 271 ILE A CD1   1 
ATOM   961  N N     . THR A 1 131 ? -39.410 36.925 -28.851 1.00 25.57 ? 272 THR A N     1 
ATOM   962  C CA    . THR A 1 131 ? -40.222 36.124 -29.750 1.00 23.65 ? 272 THR A CA    1 
ATOM   963  C C     . THR A 1 131 ? -40.525 36.928 -31.005 1.00 22.87 ? 272 THR A C     1 
ATOM   964  O O     . THR A 1 131 ? -40.441 38.156 -31.021 1.00 25.57 ? 272 THR A O     1 
ATOM   965  C CB    . THR A 1 131 ? -41.523 35.660 -29.078 1.00 27.00 ? 272 THR A CB    1 
ATOM   966  O OG1   . THR A 1 131 ? -42.444 36.751 -29.024 1.00 27.18 ? 272 THR A OG1   1 
ATOM   967  C CG2   . THR A 1 131 ? -41.260 35.166 -27.660 1.00 25.23 ? 272 THR A CG2   1 
ATOM   968  N N     . HIS A 1 132 ? -40.848 36.211 -32.079 1.00 22.52 ? 273 HIS A N     1 
ATOM   969  C CA    . HIS A 1 132 ? -41.208 36.865 -33.327 1.00 23.08 ? 273 HIS A CA    1 
ATOM   970  C C     . HIS A 1 132 ? -42.499 37.677 -33.208 1.00 23.82 ? 273 HIS A C     1 
ATOM   971  O O     . HIS A 1 132 ? -42.787 38.488 -34.099 1.00 23.70 ? 273 HIS A O     1 
ATOM   972  C CB    . HIS A 1 132 ? -41.335 35.805 -34.426 1.00 24.35 ? 273 HIS A CB    1 
ATOM   973  C CG    . HIS A 1 132 ? -40.907 36.282 -35.774 1.00 25.99 ? 273 HIS A CG    1 
ATOM   974  N ND1   . HIS A 1 132 ? -40.508 35.423 -36.776 1.00 30.35 ? 273 HIS A ND1   1 
ATOM   975  C CD2   . HIS A 1 132 ? -40.808 37.531 -36.287 1.00 26.51 ? 273 HIS A CD2   1 
ATOM   976  C CE1   . HIS A 1 132 ? -40.182 36.122 -37.849 1.00 28.18 ? 273 HIS A CE1   1 
ATOM   977  N NE2   . HIS A 1 132 ? -40.360 37.404 -37.580 1.00 27.76 ? 273 HIS A NE2   1 
ATOM   978  N N     . LEU A 1 133 ? -43.261 37.495 -32.121 1.00 22.27 ? 274 LEU A N     1 
ATOM   979  C CA    . LEU A 1 133 ? -44.570 38.119 -31.903 1.00 24.01 ? 274 LEU A CA    1 
ATOM   980  C C     . LEU A 1 133 ? -44.498 39.539 -31.352 1.00 22.64 ? 274 LEU A C     1 
ATOM   981  O O     . LEU A 1 133 ? -45.553 40.147 -31.134 1.00 22.18 ? 274 LEU A O     1 
ATOM   982  C CB    . LEU A 1 133 ? -45.380 37.256 -30.932 1.00 21.74 ? 274 LEU A CB    1 
ATOM   983  C CG    . LEU A 1 133 ? -45.736 35.884 -31.492 1.00 21.55 ? 274 LEU A CG    1 
ATOM   984  C CD1   . LEU A 1 133 ? -46.255 34.990 -30.385 1.00 24.94 ? 274 LEU A CD1   1 
ATOM   985  C CD2   . LEU A 1 133 ? -46.790 36.067 -32.552 1.00 25.40 ? 274 LEU A CD2   1 
ATOM   986  N N     . GLU A 1 134 ? -43.300 40.074 -31.121 1.00 20.44 ? 275 GLU A N     1 
ATOM   987  C CA    . GLU A 1 134 ? -43.148 41.295 -30.338 1.00 19.75 ? 275 GLU A CA    1 
ATOM   988  C C     . GLU A 1 134 ? -43.677 42.531 -31.060 1.00 19.93 ? 275 GLU A C     1 
ATOM   989  O O     . GLU A 1 134 ? -43.509 42.695 -32.271 1.00 18.19 ? 275 GLU A O     1 
ATOM   990  C CB    . GLU A 1 134 ? -41.671 41.514 -29.989 1.00 20.59 ? 275 GLU A CB    1 
ATOM   991  C CG    . GLU A 1 134 ? -41.023 40.463 -29.072 1.00 21.65 ? 275 GLU A CG    1 
ATOM   992  C CD    . GLU A 1 134 ? -41.923 39.957 -27.937 1.00 27.61 ? 275 GLU A CD    1 
ATOM   993  O OE1   . GLU A 1 134 ? -42.491 40.801 -27.198 1.00 27.04 ? 275 GLU A OE1   1 
ATOM   994  O OE2   . GLU A 1 134 ? -42.064 38.710 -27.786 1.00 26.75 ? 275 GLU A OE2   1 
ATOM   995  N N     . HIS A 1 135 ? -44.314 43.404 -30.283 1.00 19.06 ? 276 HIS A N     1 
ATOM   996  C CA    . HIS A 1 135 ? -44.541 44.803 -30.613 1.00 19.02 ? 276 HIS A CA    1 
ATOM   997  C C     . HIS A 1 135 ? -43.188 45.516 -30.718 1.00 19.09 ? 276 HIS A C     1 
ATOM   998  O O     . HIS A 1 135 ? -42.197 45.088 -30.127 1.00 17.04 ? 276 HIS A O     1 
ATOM   999  C CB    . HIS A 1 135 ? -45.432 45.401 -29.511 1.00 17.86 ? 276 HIS A CB    1 
ATOM   1000 C CG    . HIS A 1 135 ? -45.866 46.821 -29.718 1.00 19.76 ? 276 HIS A CG    1 
ATOM   1001 N ND1   . HIS A 1 135 ? -45.027 47.899 -29.514 1.00 19.66 ? 276 HIS A ND1   1 
ATOM   1002 C CD2   . HIS A 1 135 ? -47.086 47.344 -30.004 1.00 21.26 ? 276 HIS A CD2   1 
ATOM   1003 C CE1   . HIS A 1 135 ? -45.697 49.021 -29.726 1.00 20.67 ? 276 HIS A CE1   1 
ATOM   1004 N NE2   . HIS A 1 135 ? -46.951 48.713 -30.020 1.00 18.31 ? 276 HIS A NE2   1 
ATOM   1005 N N     . HIS A 1 136 ? -43.143 46.613 -31.484 1.00 15.94 ? 277 HIS A N     1 
ATOM   1006 C CA    . HIS A 1 136 ? -41.887 47.361 -31.633 1.00 16.67 ? 277 HIS A CA    1 
ATOM   1007 C C     . HIS A 1 136 ? -41.312 47.818 -30.294 1.00 17.78 ? 277 HIS A C     1 
ATOM   1008 O O     . HIS A 1 136 ? -40.093 47.971 -30.167 1.00 16.86 ? 277 HIS A O     1 
ATOM   1009 C CB    . HIS A 1 136 ? -42.091 48.585 -32.531 1.00 16.40 ? 277 HIS A CB    1 
ATOM   1010 C CG    . HIS A 1 136 ? -42.417 48.243 -33.953 1.00 16.29 ? 277 HIS A CG    1 
ATOM   1011 N ND1   . HIS A 1 136 ? -42.914 49.171 -34.846 1.00 16.06 ? 277 HIS A ND1   1 
ATOM   1012 C CD2   . HIS A 1 136 ? -42.324 47.076 -34.634 1.00 15.25 ? 277 HIS A CD2   1 
ATOM   1013 C CE1   . HIS A 1 136 ? -43.113 48.588 -36.016 1.00 17.40 ? 277 HIS A CE1   1 
ATOM   1014 N NE2   . HIS A 1 136 ? -42.764 47.317 -35.914 1.00 16.21 ? 277 HIS A NE2   1 
ATOM   1015 N N     . ALA A 1 137 ? -42.166 48.075 -29.300 1.00 13.95 ? 278 ALA A N     1 
ATOM   1016 C CA    . ALA A 1 137 ? -41.673 48.493 -27.987 1.00 16.89 ? 278 ALA A CA    1 
ATOM   1017 C C     . ALA A 1 137 ? -40.780 47.434 -27.354 1.00 17.55 ? 278 ALA A C     1 
ATOM   1018 O O     . ALA A 1 137 ? -39.936 47.755 -26.510 1.00 15.60 ? 278 ALA A O     1 
ATOM   1019 C CB    . ALA A 1 137 ? -42.847 48.793 -27.056 1.00 14.70 ? 278 ALA A CB    1 
ATOM   1020 N N     . ASN A 1 138 ? -40.975 46.168 -27.717 1.00 15.93 ? 279 ASN A N     1 
ATOM   1021 C CA    . ASN A 1 138 ? -40.173 45.061 -27.209 1.00 18.25 ? 279 ASN A CA    1 
ATOM   1022 C C     . ASN A 1 138 ? -39.221 44.535 -28.276 1.00 19.45 ? 279 ASN A C     1 
ATOM   1023 O O     . ASN A 1 138 ? -38.835 43.361 -28.254 1.00 20.02 ? 279 ASN A O     1 
ATOM   1024 C CB    . ASN A 1 138 ? -41.075 43.941 -26.688 1.00 17.05 ? 279 ASN A CB    1 
ATOM   1025 C CG    . ASN A 1 138 ? -40.449 43.167 -25.526 1.00 21.60 ? 279 ASN A CG    1 
ATOM   1026 O OD1   . ASN A 1 138 ? -39.499 43.628 -24.885 1.00 17.62 ? 279 ASN A OD1   1 
ATOM   1027 N ND2   . ASN A 1 138 ? -40.983 41.976 -25.256 1.00 22.92 ? 279 ASN A ND2   1 
ATOM   1028 N N     . ILE A 1 139 ? -38.860 45.388 -29.234 1.00 16.90 ? 280 ILE A N     1 
ATOM   1029 C CA    . ILE A 1 139 ? -37.836 45.059 -30.221 1.00 18.92 ? 280 ILE A CA    1 
ATOM   1030 C C     . ILE A 1 139 ? -36.787 46.160 -30.241 1.00 21.07 ? 280 ILE A C     1 
ATOM   1031 O O     . ILE A 1 139 ? -35.589 45.896 -30.052 1.00 20.53 ? 280 ILE A O     1 
ATOM   1032 C CB    . ILE A 1 139 ? -38.418 44.867 -31.637 1.00 21.23 ? 280 ILE A CB    1 
ATOM   1033 C CG1   . ILE A 1 139 ? -39.369 43.675 -31.703 1.00 21.32 ? 280 ILE A CG1   1 
ATOM   1034 C CG2   . ILE A 1 139 ? -37.287 44.643 -32.651 1.00 20.67 ? 280 ILE A CG2   1 
ATOM   1035 C CD1   . ILE A 1 139 ? -40.228 43.680 -32.962 1.00 19.56 ? 280 ILE A CD1   1 
ATOM   1036 N N     . VAL A 1 140 ? -37.229 47.400 -30.487 1.00 17.34 ? 281 VAL A N     1 
ATOM   1037 C CA    . VAL A 1 140 ? -36.278 48.493 -30.725 1.00 16.44 ? 281 VAL A CA    1 
ATOM   1038 C C     . VAL A 1 140 ? -35.341 48.703 -29.542 1.00 19.86 ? 281 VAL A C     1 
ATOM   1039 O O     . VAL A 1 140 ? -34.134 48.878 -29.767 1.00 20.10 ? 281 VAL A O     1 
ATOM   1040 C CB    . VAL A 1 140 ? -37.022 49.768 -31.140 1.00 19.11 ? 281 VAL A CB    1 
ATOM   1041 C CG1   . VAL A 1 140 ? -36.014 50.908 -31.379 1.00 22.11 ? 281 VAL A CG1   1 
ATOM   1042 C CG2   . VAL A 1 140 ? -37.829 49.524 -32.409 1.00 18.99 ? 281 VAL A CG2   1 
ATOM   1043 N N     . PRO A 1 141 ? -35.800 48.714 -28.281 1.00 17.06 ? 282 PRO A N     1 
ATOM   1044 C CA    . PRO A 1 141 ? -34.841 48.879 -27.175 1.00 18.11 ? 282 PRO A CA    1 
ATOM   1045 C C     . PRO A 1 141 ? -33.783 47.788 -27.129 1.00 20.46 ? 282 PRO A C     1 
ATOM   1046 O O     . PRO A 1 141 ? -32.630 48.074 -26.781 1.00 19.95 ? 282 PRO A O     1 
ATOM   1047 C CB    . PRO A 1 141 ? -35.736 48.850 -25.924 1.00 17.14 ? 282 PRO A CB    1 
ATOM   1048 C CG    . PRO A 1 141 ? -37.108 49.313 -26.433 1.00 16.43 ? 282 PRO A CG    1 
ATOM   1049 C CD    . PRO A 1 141 ? -37.195 48.685 -27.789 1.00 16.70 ? 282 PRO A CD    1 
ATOM   1050 N N     . TRP A 1 142 ? -34.132 46.540 -27.468 1.00 19.33 ? 283 TRP A N     1 
ATOM   1051 C CA    . TRP A 1 142 ? -33.113 45.492 -27.483 1.00 21.17 ? 283 TRP A CA    1 
ATOM   1052 C C     . TRP A 1 142 ? -32.141 45.669 -28.644 1.00 24.54 ? 283 TRP A C     1 
ATOM   1053 O O     . TRP A 1 142 ? -30.958 45.353 -28.496 1.00 22.09 ? 283 TRP A O     1 
ATOM   1054 C CB    . TRP A 1 142 ? -33.779 44.113 -27.499 1.00 16.73 ? 283 TRP A CB    1 
ATOM   1055 C CG    . TRP A 1 142 ? -34.827 44.030 -26.411 1.00 20.72 ? 283 TRP A CG    1 
ATOM   1056 C CD1   . TRP A 1 142 ? -36.177 43.824 -26.574 1.00 20.32 ? 283 TRP A CD1   1 
ATOM   1057 C CD2   . TRP A 1 142 ? -34.619 44.209 -25.003 1.00 17.98 ? 283 TRP A CD2   1 
ATOM   1058 N NE1   . TRP A 1 142 ? -36.810 43.855 -25.352 1.00 18.42 ? 283 TRP A NE1   1 
ATOM   1059 C CE2   . TRP A 1 142 ? -35.880 44.084 -24.373 1.00 19.67 ? 283 TRP A CE2   1 
ATOM   1060 C CE3   . TRP A 1 142 ? -33.488 44.440 -24.211 1.00 20.21 ? 283 TRP A CE3   1 
ATOM   1061 C CZ2   . TRP A 1 142 ? -36.040 44.184 -22.993 1.00 19.60 ? 283 TRP A CZ2   1 
ATOM   1062 C CZ3   . TRP A 1 142 ? -33.652 44.549 -22.834 1.00 22.17 ? 283 TRP A CZ3   1 
ATOM   1063 C CH2   . TRP A 1 142 ? -34.917 44.421 -22.241 1.00 18.10 ? 283 TRP A CH2   1 
ATOM   1064 N N     . GLN A 1 143 ? -32.594 46.208 -29.784 1.00 22.12 ? 284 GLN A N     1 
ATOM   1065 C CA    . GLN A 1 143 ? -31.660 46.504 -30.877 1.00 24.66 ? 284 GLN A CA    1 
ATOM   1066 C C     . GLN A 1 143 ? -30.686 47.614 -30.493 1.00 27.05 ? 284 GLN A C     1 
ATOM   1067 O O     . GLN A 1 143 ? -29.480 47.524 -30.777 1.00 29.94 ? 284 GLN A O     1 
ATOM   1068 C CB    . GLN A 1 143 ? -32.425 46.885 -32.148 1.00 22.56 ? 284 GLN A CB    1 
ATOM   1069 C CG    . GLN A 1 143 ? -33.216 45.737 -32.787 1.00 21.98 ? 284 GLN A CG    1 
ATOM   1070 C CD    . GLN A 1 143 ? -34.118 46.198 -33.932 1.00 25.72 ? 284 GLN A CD    1 
ATOM   1071 O OE1   . GLN A 1 143 ? -34.647 47.317 -33.923 1.00 24.47 ? 284 GLN A OE1   1 
ATOM   1072 N NE2   . GLN A 1 143 ? -34.297 45.337 -34.917 1.00 22.50 ? 284 GLN A NE2   1 
ATOM   1073 N N     . LEU A 1 144 ? -31.196 48.676 -29.866 1.00 22.18 ? 285 LEU A N     1 
ATOM   1074 C CA    . LEU A 1 144 ? -30.334 49.736 -29.354 1.00 24.89 ? 285 LEU A CA    1 
ATOM   1075 C C     . LEU A 1 144 ? -29.308 49.169 -28.379 1.00 30.22 ? 285 LEU A C     1 
ATOM   1076 O O     . LEU A 1 144 ? -28.095 49.363 -28.542 1.00 30.75 ? 285 LEU A O     1 
ATOM   1077 C CB    . LEU A 1 144 ? -31.193 50.795 -28.671 1.00 28.75 ? 285 LEU A CB    1 
ATOM   1078 C CG    . LEU A 1 144 ? -31.993 51.750 -29.563 1.00 33.40 ? 285 LEU A CG    1 
ATOM   1079 C CD1   . LEU A 1 144 ? -32.427 52.963 -28.777 1.00 36.92 ? 285 LEU A CD1   1 
ATOM   1080 C CD2   . LEU A 1 144 ? -31.159 52.185 -30.746 1.00 34.67 ? 285 LEU A CD2   1 
ATOM   1081 N N     . LEU A 1 145 ? -29.782 48.436 -27.368 1.00 25.89 ? 286 LEU A N     1 
ATOM   1082 C CA    . LEU A 1 145 ? -28.882 47.854 -26.382 1.00 26.97 ? 286 LEU A CA    1 
ATOM   1083 C C     . LEU A 1 145 ? -27.881 46.905 -27.031 1.00 29.16 ? 286 LEU A C     1 
ATOM   1084 O O     . LEU A 1 145 ? -26.711 46.844 -26.630 1.00 27.10 ? 286 LEU A O     1 
ATOM   1085 C CB    . LEU A 1 145 ? -29.702 47.136 -25.317 1.00 24.38 ? 286 LEU A CB    1 
ATOM   1086 C CG    . LEU A 1 145 ? -28.897 46.454 -24.224 1.00 29.25 ? 286 LEU A CG    1 
ATOM   1087 C CD1   . LEU A 1 145 ? -28.250 47.533 -23.348 1.00 21.94 ? 286 LEU A CD1   1 
ATOM   1088 C CD2   . LEU A 1 145 ? -29.841 45.552 -23.432 1.00 25.87 ? 286 LEU A CD2   1 
ATOM   1089 N N     . SER A 1 146 ? -28.316 46.160 -28.041 1.00 27.03 ? 287 SER A N     1 
ATOM   1090 C CA    . SER A 1 146 ? -27.432 45.202 -28.675 1.00 27.19 ? 287 SER A CA    1 
ATOM   1091 C C     . SER A 1 146 ? -26.326 45.906 -29.451 1.00 30.76 ? 287 SER A C     1 
ATOM   1092 O O     . SER A 1 146 ? -25.179 45.448 -29.454 1.00 28.83 ? 287 SER A O     1 
ATOM   1093 C CB    . SER A 1 146 ? -28.239 44.274 -29.577 1.00 26.61 ? 287 SER A CB    1 
ATOM   1094 O OG    . SER A 1 146 ? -27.376 43.474 -30.353 1.00 34.55 ? 287 SER A OG    1 
ATOM   1095 N N     . ARG A 1 147 ? -26.634 47.027 -30.103 1.00 28.58 ? 288 ARG A N     1 
ATOM   1096 C CA    . ARG A 1 147 ? -25.547 47.754 -30.753 1.00 33.82 ? 288 ARG A CA    1 
ATOM   1097 C C     . ARG A 1 147 ? -24.628 48.405 -29.726 1.00 33.65 ? 288 ARG A C     1 
ATOM   1098 O O     . ARG A 1 147 ? -23.425 48.554 -29.972 1.00 32.48 ? 288 ARG A O     1 
ATOM   1099 C CB    . ARG A 1 147 ? -26.093 48.793 -31.740 1.00 35.47 ? 288 ARG A CB    1 
ATOM   1100 C CG    . ARG A 1 147 ? -26.799 48.173 -32.947 1.00 45.15 ? 288 ARG A CG    1 
ATOM   1101 C CD    . ARG A 1 147 ? -26.127 48.514 -34.293 1.00 54.70 ? 288 ARG A CD    1 
ATOM   1102 N NE    . ARG A 1 147 ? -26.530 49.815 -34.826 1.00 65.94 ? 288 ARG A NE    1 
ATOM   1103 C CZ    . ARG A 1 147 ? -27.149 50.002 -35.990 1.00 68.17 ? 288 ARG A CZ    1 
ATOM   1104 N NH1   . ARG A 1 147 ? -27.464 48.984 -36.781 1.00 56.76 ? 288 ARG A NH1   1 
ATOM   1105 N NH2   . ARG A 1 147 ? -27.463 51.244 -36.368 1.00 55.91 ? 288 ARG A NH2   1 
ATOM   1106 N N     . GLN A 1 148 ? -25.166 48.776 -28.566 1.00 30.76 ? 289 GLN A N     1 
ATOM   1107 C CA    . GLN A 1 148 ? -24.347 49.451 -27.567 1.00 31.75 ? 289 GLN A CA    1 
ATOM   1108 C C     . GLN A 1 148 ? -23.416 48.487 -26.832 1.00 28.80 ? 289 GLN A C     1 
ATOM   1109 O O     . GLN A 1 148 ? -22.290 48.857 -26.481 1.00 27.32 ? 289 GLN A O     1 
ATOM   1110 C CB    . GLN A 1 148 ? -25.256 50.174 -26.577 1.00 32.11 ? 289 GLN A CB    1 
ATOM   1111 C CG    . GLN A 1 148 ? -25.667 51.576 -27.012 1.00 44.22 ? 289 GLN A CG    1 
ATOM   1112 C CD    . GLN A 1 148 ? -26.602 52.244 -26.005 1.00 55.58 ? 289 GLN A CD    1 
ATOM   1113 O OE1   . GLN A 1 148 ? -26.466 52.061 -24.791 1.00 60.07 ? 289 GLN A OE1   1 
ATOM   1114 N NE2   . GLN A 1 148 ? -27.564 53.013 -26.510 1.00 56.26 ? 289 GLN A NE2   1 
ATOM   1115 N N     . THR A 1 149 ? -23.868 47.257 -26.580 1.00 24.71 ? 290 THR A N     1 
ATOM   1116 C CA    . THR A 1 149 ? -23.170 46.321 -25.712 1.00 28.17 ? 290 THR A CA    1 
ATOM   1117 C C     . THR A 1 149 ? -22.503 45.175 -26.447 1.00 27.08 ? 290 THR A C     1 
ATOM   1118 O O     . THR A 1 149 ? -21.739 44.438 -25.824 1.00 23.80 ? 290 THR A O     1 
ATOM   1119 C CB    . THR A 1 149 ? -24.132 45.696 -24.693 1.00 29.50 ? 290 THR A CB    1 
ATOM   1120 O OG1   . THR A 1 149 ? -25.113 44.909 -25.396 1.00 29.42 ? 290 THR A OG1   1 
ATOM   1121 C CG2   . THR A 1 149 ? -24.796 46.766 -23.842 1.00 26.77 ? 290 THR A CG2   1 
ATOM   1122 N N     . GLY A 1 150 ? -22.802 44.975 -27.727 1.00 24.43 ? 291 GLY A N     1 
ATOM   1123 C CA    . GLY A 1 150 ? -22.350 43.796 -28.426 1.00 24.06 ? 291 GLY A CA    1 
ATOM   1124 C C     . GLY A 1 150 ? -23.169 42.546 -28.183 1.00 27.78 ? 291 GLY A C     1 
ATOM   1125 O O     . GLY A 1 150 ? -22.833 41.491 -28.740 1.00 25.44 ? 291 GLY A O     1 
ATOM   1126 N N     . ALA A 1 151 ? -24.221 42.618 -27.368 1.00 28.04 ? 292 ALA A N     1 
ATOM   1127 C CA    . ALA A 1 151 ? -25.079 41.459 -27.149 1.00 28.89 ? 292 ALA A CA    1 
ATOM   1128 C C     . ALA A 1 151 ? -25.726 41.018 -28.458 1.00 26.08 ? 292 ALA A C     1 
ATOM   1129 O O     . ALA A 1 151 ? -25.908 41.811 -29.382 1.00 25.22 ? 292 ALA A O     1 
ATOM   1130 C CB    . ALA A 1 151 ? -26.163 41.779 -26.119 1.00 30.52 ? 292 ALA A CB    1 
ATOM   1131 N N     . VAL A 1 152 ? -26.050 39.731 -28.542 1.00 29.68 ? 293 VAL A N     1 
ATOM   1132 C CA    . VAL A 1 152 ? -26.671 39.144 -29.726 1.00 28.36 ? 293 VAL A CA    1 
ATOM   1133 C C     . VAL A 1 152 ? -28.161 38.975 -29.461 1.00 29.82 ? 293 VAL A C     1 
ATOM   1134 O O     . VAL A 1 152 ? -28.557 38.448 -28.414 1.00 27.82 ? 293 VAL A O     1 
ATOM   1135 C CB    . VAL A 1 152 ? -26.018 37.799 -30.082 1.00 32.26 ? 293 VAL A CB    1 
ATOM   1136 C CG1   . VAL A 1 152 ? -26.629 37.232 -31.355 1.00 30.99 ? 293 VAL A CG1   1 
ATOM   1137 C CG2   . VAL A 1 152 ? -24.503 37.984 -30.252 1.00 32.15 ? 293 VAL A CG2   1 
ATOM   1138 N N     . LEU A 1 153 ? -28.986 39.426 -30.400 1.00 30.02 ? 294 LEU A N     1 
ATOM   1139 C CA    . LEU A 1 153 ? -30.436 39.316 -30.301 1.00 26.75 ? 294 LEU A CA    1 
ATOM   1140 C C     . LEU A 1 153 ? -30.909 38.104 -31.101 1.00 26.85 ? 294 LEU A C     1 
ATOM   1141 O O     . LEU A 1 153 ? -30.676 38.030 -32.310 1.00 28.18 ? 294 LEU A O     1 
ATOM   1142 C CB    . LEU A 1 153 ? -31.098 40.596 -30.805 1.00 29.67 ? 294 LEU A CB    1 
ATOM   1143 C CG    . LEU A 1 153 ? -32.618 40.665 -30.715 1.00 28.32 ? 294 LEU A CG    1 
ATOM   1144 C CD1   . LEU A 1 153 ? -33.093 40.586 -29.255 1.00 26.28 ? 294 LEU A CD1   1 
ATOM   1145 C CD2   . LEU A 1 153 ? -33.088 41.963 -31.367 1.00 28.29 ? 294 LEU A CD2   1 
ATOM   1146 N N     . LYS A 1 154 ? -31.536 37.145 -30.421 1.00 24.65 ? 295 LYS A N     1 
ATOM   1147 C CA    . LYS A 1 154 ? -32.126 35.970 -31.052 1.00 28.74 ? 295 LYS A CA    1 
ATOM   1148 C C     . LYS A 1 154 ? -33.645 36.080 -31.011 1.00 27.60 ? 295 LYS A C     1 
ATOM   1149 O O     . LYS A 1 154 ? -34.214 36.620 -30.056 1.00 24.06 ? 295 LYS A O     1 
ATOM   1150 C CB    . LYS A 1 154 ? -31.701 34.675 -30.350 1.00 26.36 ? 295 LYS A CB    1 
ATOM   1151 C CG    . LYS A 1 154 ? -30.194 34.508 -30.163 1.00 34.23 ? 295 LYS A CG    1 
ATOM   1152 C CD    . LYS A 1 154 ? -29.463 34.732 -31.476 1.00 35.23 ? 295 LYS A CD    1 
ATOM   1153 C CE    . LYS A 1 154 ? -28.557 33.558 -31.837 1.00 46.05 ? 295 LYS A CE    1 
ATOM   1154 N NZ    . LYS A 1 154 ? -27.526 33.260 -30.787 1.00 46.46 ? 295 LYS A NZ    1 
ATOM   1155 N N     . VAL A 1 155 ? -34.296 35.540 -32.042 1.00 27.55 ? 296 VAL A N     1 
ATOM   1156 C CA    . VAL A 1 155 ? -35.739 35.680 -32.233 1.00 25.84 ? 296 VAL A CA    1 
ATOM   1157 C C     . VAL A 1 155 ? -36.357 34.283 -32.284 1.00 27.77 ? 296 VAL A C     1 
ATOM   1158 O O     . VAL A 1 155 ? -36.110 33.523 -33.226 1.00 26.02 ? 296 VAL A O     1 
ATOM   1159 C CB    . VAL A 1 155 ? -36.068 36.470 -33.506 1.00 26.78 ? 296 VAL A CB    1 
ATOM   1160 C CG1   . VAL A 1 155 ? -37.584 36.652 -33.650 1.00 27.42 ? 296 VAL A CG1   1 
ATOM   1161 C CG2   . VAL A 1 155 ? -35.342 37.829 -33.500 1.00 27.39 ? 296 VAL A CG2   1 
ATOM   1162 N N     . ALA A 1 156 ? -37.164 33.951 -31.284 1.00 24.70 ? 297 ALA A N     1 
ATOM   1163 C CA    . ALA A 1 156 ? -37.839 32.651 -31.247 1.00 24.26 ? 297 ALA A CA    1 
ATOM   1164 C C     . ALA A 1 156 ? -38.945 32.600 -32.297 1.00 28.43 ? 297 ALA A C     1 
ATOM   1165 O O     . ALA A 1 156 ? -39.725 33.551 -32.408 1.00 24.65 ? 297 ALA A O     1 
ATOM   1166 C CB    . ALA A 1 156 ? -38.425 32.406 -29.860 1.00 24.01 ? 297 ALA A CB    1 
ATOM   1167 N N     . PRO A 1 157 ? -39.050 31.523 -33.077 1.00 31.19 ? 298 PRO A N     1 
ATOM   1168 C CA    . PRO A 1 157 ? -39.981 31.500 -34.214 1.00 28.57 ? 298 PRO A CA    1 
ATOM   1169 C C     . PRO A 1 157 ? -41.393 31.040 -33.863 1.00 28.96 ? 298 PRO A C     1 
ATOM   1170 O O     . PRO A 1 157 ? -41.654 30.473 -32.801 1.00 27.89 ? 298 PRO A O     1 
ATOM   1171 C CB    . PRO A 1 157 ? -39.315 30.505 -35.180 1.00 31.91 ? 298 PRO A CB    1 
ATOM   1172 C CG    . PRO A 1 157 ? -38.548 29.581 -34.296 1.00 27.85 ? 298 PRO A CG    1 
ATOM   1173 C CD    . PRO A 1 157 ? -38.128 30.368 -33.079 1.00 29.40 ? 298 PRO A CD    1 
ATOM   1174 N N     . VAL A 1 158 ? -42.313 31.312 -34.791 1.00 27.21 ? 299 VAL A N     1 
ATOM   1175 C CA    . VAL A 1 158 ? -43.708 30.902 -34.684 1.00 29.83 ? 299 VAL A CA    1 
ATOM   1176 C C     . VAL A 1 158 ? -44.034 30.027 -35.889 1.00 32.31 ? 299 VAL A C     1 
ATOM   1177 O O     . VAL A 1 158 ? -43.374 30.104 -36.929 1.00 29.82 ? 299 VAL A O     1 
ATOM   1178 C CB    . VAL A 1 158 ? -44.682 32.106 -34.628 1.00 29.33 ? 299 VAL A CB    1 
ATOM   1179 C CG1   . VAL A 1 158 ? -44.481 32.934 -33.355 1.00 23.30 ? 299 VAL A CG1   1 
ATOM   1180 C CG2   . VAL A 1 158 ? -44.518 32.980 -35.876 1.00 28.60 ? 299 VAL A CG2   1 
ATOM   1181 N N     . ASP A 1 159 ? -45.075 29.197 -35.747 1.00 29.81 ? 300 ASP A N     1 
ATOM   1182 C CA    . ASP A 1 159 ? -45.639 28.545 -36.924 1.00 33.20 ? 300 ASP A CA    1 
ATOM   1183 C C     . ASP A 1 159 ? -46.548 29.521 -37.668 1.00 35.55 ? 300 ASP A C     1 
ATOM   1184 O O     . ASP A 1 159 ? -46.729 30.674 -37.265 1.00 31.76 ? 300 ASP A O     1 
ATOM   1185 C CB    . ASP A 1 159 ? -46.397 27.260 -36.572 1.00 27.98 ? 300 ASP A CB    1 
ATOM   1186 C CG    . ASP A 1 159 ? -47.670 27.514 -35.750 1.00 39.86 ? 300 ASP A CG    1 
ATOM   1187 O OD1   . ASP A 1 159 ? -48.453 28.423 -36.092 1.00 37.20 ? 300 ASP A OD1   1 
ATOM   1188 O OD2   . ASP A 1 159 ? -47.845 26.863 -34.695 1.00 42.83 ? 300 ASP A OD2   1 
ATOM   1189 N N     . ASP A 1 160 ? -47.165 29.044 -38.756 1.00 34.45 ? 301 ASP A N     1 
ATOM   1190 C CA    . ASP A 1 160 ? -47.912 29.964 -39.608 1.00 33.60 ? 301 ASP A CA    1 
ATOM   1191 C C     . ASP A 1 160 ? -49.242 30.372 -39.000 1.00 31.08 ? 301 ASP A C     1 
ATOM   1192 O O     . ASP A 1 160 ? -49.817 31.378 -39.432 1.00 28.10 ? 301 ASP A O     1 
ATOM   1193 C CB    . ASP A 1 160 ? -48.154 29.360 -40.986 1.00 38.27 ? 301 ASP A CB    1 
ATOM   1194 C CG    . ASP A 1 160 ? -46.891 28.799 -41.588 1.00 42.23 ? 301 ASP A CG    1 
ATOM   1195 O OD1   . ASP A 1 160 ? -46.124 29.577 -42.201 1.00 40.36 ? 301 ASP A OD1   1 
ATOM   1196 O OD2   . ASP A 1 160 ? -46.633 27.594 -41.360 1.00 46.00 ? 301 ASP A OD2   1 
ATOM   1197 N N     . ALA A 1 161 ? -49.742 29.612 -38.022 1.00 30.56 ? 302 ALA A N     1 
ATOM   1198 C CA    . ALA A 1 161 ? -50.916 30.016 -37.256 1.00 34.05 ? 302 ALA A CA    1 
ATOM   1199 C C     . ALA A 1 161 ? -50.589 31.051 -36.186 1.00 29.38 ? 302 ALA A C     1 
ATOM   1200 O O     . ALA A 1 161 ? -51.510 31.679 -35.649 1.00 28.42 ? 302 ALA A O     1 
ATOM   1201 C CB    . ALA A 1 161 ? -51.574 28.792 -36.606 1.00 32.86 ? 302 ALA A CB    1 
ATOM   1202 N N     . GLY A 1 162 ? -49.311 31.252 -35.875 1.00 30.73 ? 303 GLY A N     1 
ATOM   1203 C CA    . GLY A 1 162 ? -48.903 32.229 -34.892 1.00 26.34 ? 303 GLY A CA    1 
ATOM   1204 C C     . GLY A 1 162 ? -48.622 31.684 -33.512 1.00 28.91 ? 303 GLY A C     1 
ATOM   1205 O O     . GLY A 1 162 ? -48.428 32.479 -32.582 1.00 23.96 ? 303 GLY A O     1 
ATOM   1206 N N     . ASN A 1 163 ? -48.606 30.363 -33.343 1.00 26.36 ? 304 ASN A N     1 
ATOM   1207 C CA    . ASN A 1 163 ? -48.205 29.774 -32.073 1.00 31.20 ? 304 ASN A CA    1 
ATOM   1208 C C     . ASN A 1 163 ? -46.699 29.896 -31.890 1.00 32.26 ? 304 ASN A C     1 
ATOM   1209 O O     . ASN A 1 163 ? -45.923 29.619 -32.811 1.00 30.71 ? 304 ASN A O     1 
ATOM   1210 C CB    . ASN A 1 163 ? -48.576 28.286 -31.998 1.00 30.69 ? 304 ASN A CB    1 
ATOM   1211 C CG    . ASN A 1 163 ? -50.047 28.023 -32.210 1.00 32.58 ? 304 ASN A CG    1 
ATOM   1212 O OD1   . ASN A 1 163 ? -50.853 28.157 -31.288 1.00 34.64 ? 304 ASN A OD1   1 
ATOM   1213 N ND2   . ASN A 1 163 ? -50.400 27.583 -33.408 1.00 30.81 ? 304 ASN A ND2   1 
ATOM   1214 N N     . LEU A 1 164 ? -46.282 30.264 -30.680 1.00 31.46 ? 305 LEU A N     1 
ATOM   1215 C CA    . LEU A 1 164 ? -44.872 30.148 -30.325 1.00 32.20 ? 305 LEU A CA    1 
ATOM   1216 C C     . LEU A 1 164 ? -44.466 28.679 -30.265 1.00 34.15 ? 305 LEU A C     1 
ATOM   1217 O O     . LEU A 1 164 ? -45.137 27.871 -29.620 1.00 34.22 ? 305 LEU A O     1 
ATOM   1218 C CB    . LEU A 1 164 ? -44.603 30.819 -28.980 1.00 30.76 ? 305 LEU A CB    1 
ATOM   1219 C CG    . LEU A 1 164 ? -43.129 30.877 -28.577 1.00 32.83 ? 305 LEU A CG    1 
ATOM   1220 C CD1   . LEU A 1 164 ? -42.348 31.798 -29.496 1.00 28.02 ? 305 LEU A CD1   1 
ATOM   1221 C CD2   . LEU A 1 164 ? -43.009 31.320 -27.137 1.00 33.28 ? 305 LEU A CD2   1 
ATOM   1222 N N     . LEU A 1 165 ? -43.358 28.335 -30.932 1.00 33.37 ? 306 LEU A N     1 
ATOM   1223 C CA    . LEU A 1 165 ? -42.831 26.968 -30.945 1.00 36.14 ? 306 LEU A CA    1 
ATOM   1224 C C     . LEU A 1 165 ? -41.896 26.790 -29.754 1.00 39.03 ? 306 LEU A C     1 
ATOM   1225 O O     . LEU A 1 165 ? -40.754 27.264 -29.765 1.00 37.13 ? 306 LEU A O     1 
ATOM   1226 C CB    . LEU A 1 165 ? -42.106 26.680 -32.255 1.00 37.13 ? 306 LEU A CB    1 
ATOM   1227 C CG    . LEU A 1 165 ? -42.915 26.864 -33.538 1.00 37.89 ? 306 LEU A CG    1 
ATOM   1228 C CD1   . LEU A 1 165 ? -42.006 26.880 -34.771 1.00 35.81 ? 306 LEU A CD1   1 
ATOM   1229 C CD2   . LEU A 1 165 ? -43.966 25.775 -33.645 1.00 36.53 ? 306 LEU A CD2   1 
ATOM   1230 N N     . LEU A 1 166 ? -42.373 26.078 -28.732 1.00 37.31 ? 307 LEU A N     1 
ATOM   1231 C CA    . LEU A 1 166 ? -41.624 25.971 -27.484 1.00 37.49 ? 307 LEU A CA    1 
ATOM   1232 C C     . LEU A 1 166 ? -40.321 25.200 -27.661 1.00 37.73 ? 307 LEU A C     1 
ATOM   1233 O O     . LEU A 1 166 ? -39.346 25.462 -26.946 1.00 37.24 ? 307 LEU A O     1 
ATOM   1234 C CB    . LEU A 1 166 ? -42.498 25.307 -26.426 1.00 40.34 ? 307 LEU A CB    1 
ATOM   1235 C CG    . LEU A 1 166 ? -43.284 26.247 -25.507 1.00 43.69 ? 307 LEU A CG    1 
ATOM   1236 C CD1   . LEU A 1 166 ? -43.872 25.448 -24.345 1.00 43.94 ? 307 LEU A CD1   1 
ATOM   1237 C CD2   . LEU A 1 166 ? -42.439 27.415 -25.001 1.00 37.77 ? 307 LEU A CD2   1 
ATOM   1238 N N     . GLY A 1 167 ? -40.274 24.261 -28.606 1.00 39.42 ? 308 GLY A N     1 
ATOM   1239 C CA    . GLY A 1 167 ? -39.051 23.496 -28.806 1.00 40.65 ? 308 GLY A CA    1 
ATOM   1240 C C     . GLY A 1 167 ? -37.942 24.326 -29.424 1.00 40.24 ? 308 GLY A C     1 
ATOM   1241 O O     . GLY A 1 167 ? -36.799 24.310 -28.954 1.00 38.54 ? 308 GLY A O     1 
ATOM   1242 N N     . GLU A 1 168 ? -38.262 25.064 -30.491 1.00 37.52 ? 309 GLU A N     1 
ATOM   1243 C CA    . GLU A 1 168 ? -37.281 25.972 -31.075 1.00 42.33 ? 309 GLU A CA    1 
ATOM   1244 C C     . GLU A 1 168 ? -36.871 27.059 -30.077 1.00 37.83 ? 309 GLU A C     1 
ATOM   1245 O O     . GLU A 1 168 ? -35.695 27.461 -30.023 1.00 37.72 ? 309 GLU A O     1 
ATOM   1246 C CB    . GLU A 1 168 ? -37.843 26.576 -32.362 1.00 38.07 ? 309 GLU A CB    1 
ATOM   1247 C CG    . GLU A 1 168 ? -37.686 25.661 -33.581 1.00 44.84 ? 309 GLU A CG    1 
ATOM   1248 C CD    . GLU A 1 168 ? -38.946 24.866 -33.895 1.00 55.96 ? 309 GLU A CD    1 
ATOM   1249 O OE1   . GLU A 1 168 ? -39.244 24.655 -35.098 1.00 58.39 ? 309 GLU A OE1   1 
ATOM   1250 O OE2   . GLU A 1 168 ? -39.653 24.464 -32.942 1.00 55.80 ? 309 GLU A OE2   1 
ATOM   1251 N N     . PHE A 1 169 ? -37.817 27.520 -29.251 1.00 35.35 ? 310 PHE A N     1 
ATOM   1252 C CA    . PHE A 1 169 ? -37.485 28.518 -28.237 1.00 35.88 ? 310 PHE A CA    1 
ATOM   1253 C C     . PHE A 1 169 ? -36.473 27.965 -27.241 1.00 35.90 ? 310 PHE A C     1 
ATOM   1254 O O     . PHE A 1 169 ? -35.475 28.622 -26.922 1.00 36.44 ? 310 PHE A O     1 
ATOM   1255 C CB    . PHE A 1 169 ? -38.746 29.000 -27.507 1.00 32.62 ? 310 PHE A CB    1 
ATOM   1256 C CG    . PHE A 1 169 ? -38.449 29.731 -26.219 1.00 31.82 ? 310 PHE A CG    1 
ATOM   1257 C CD1   . PHE A 1 169 ? -37.917 31.006 -26.241 1.00 30.55 ? 310 PHE A CD1   1 
ATOM   1258 C CD2   . PHE A 1 169 ? -38.668 29.129 -24.992 1.00 31.76 ? 310 PHE A CD2   1 
ATOM   1259 C CE1   . PHE A 1 169 ? -37.619 31.679 -25.064 1.00 30.02 ? 310 PHE A CE1   1 
ATOM   1260 C CE2   . PHE A 1 169 ? -38.365 29.792 -23.809 1.00 28.42 ? 310 PHE A CE2   1 
ATOM   1261 C CZ    . PHE A 1 169 ? -37.837 31.069 -23.846 1.00 28.04 ? 310 PHE A CZ    1 
ATOM   1262 N N     . GLU A 1 170 ? -36.717 26.754 -26.731 1.00 35.76 ? 311 GLU A N     1 
ATOM   1263 C CA    . GLU A 1 170 ? -35.751 26.138 -25.829 1.00 37.38 ? 311 GLU A CA    1 
ATOM   1264 C C     . GLU A 1 170 ? -34.409 25.916 -26.518 1.00 37.95 ? 311 GLU A C     1 
ATOM   1265 O O     . GLU A 1 170 ? -33.357 26.053 -25.882 1.00 35.35 ? 311 GLU A O     1 
ATOM   1266 C CB    . GLU A 1 170 ? -36.306 24.822 -25.279 1.00 40.78 ? 311 GLU A CB    1 
ATOM   1267 C CG    . GLU A 1 170 ? -35.432 24.163 -24.204 1.00 41.94 ? 311 GLU A CG    1 
ATOM   1268 C CD    . GLU A 1 170 ? -36.137 23.007 -23.487 1.00 48.79 ? 311 GLU A CD    1 
ATOM   1269 O OE1   . GLU A 1 170 ? -37.194 22.547 -23.973 1.00 47.74 ? 311 GLU A OE1   1 
ATOM   1270 O OE2   . GLU A 1 170 ? -35.625 22.548 -22.442 1.00 52.38 ? 311 GLU A OE2   1 
ATOM   1271 N N     . ASP A 1 171 ? -34.422 25.601 -27.817 1.00 36.17 ? 312 ASP A N     1 
ATOM   1272 C CA    . ASP A 1 171 ? -33.169 25.397 -28.542 1.00 38.97 ? 312 ASP A CA    1 
ATOM   1273 C C     . ASP A 1 171 ? -32.347 26.673 -28.623 1.00 35.90 ? 312 ASP A C     1 
ATOM   1274 O O     . ASP A 1 171 ? -31.120 26.610 -28.749 1.00 37.88 ? 312 ASP A O     1 
ATOM   1275 C CB    . ASP A 1 171 ? -33.443 24.891 -29.954 1.00 36.89 ? 312 ASP A CB    1 
ATOM   1276 C CG    . ASP A 1 171 ? -33.737 23.417 -29.993 1.00 47.18 ? 312 ASP A CG    1 
ATOM   1277 O OD1   . ASP A 1 171 ? -33.758 22.784 -28.911 1.00 50.31 ? 312 ASP A OD1   1 
ATOM   1278 O OD2   . ASP A 1 171 ? -33.959 22.899 -31.108 1.00 47.53 ? 312 ASP A OD2   1 
ATOM   1279 N N     . LEU A 1 172 ? -33.000 27.836 -28.604 1.00 34.96 ? 313 LEU A N     1 
ATOM   1280 C CA    . LEU A 1 172 ? -32.232 29.078 -28.603 1.00 34.97 ? 313 LEU A CA    1 
ATOM   1281 C C     . LEU A 1 172 ? -31.576 29.379 -27.260 1.00 30.05 ? 313 LEU A C     1 
ATOM   1282 O O     . LEU A 1 172 ? -30.705 30.249 -27.201 1.00 30.12 ? 313 LEU A O     1 
ATOM   1283 C CB    . LEU A 1 172 ? -33.120 30.262 -29.004 1.00 34.68 ? 313 LEU A CB    1 
ATOM   1284 C CG    . LEU A 1 172 ? -33.642 30.255 -30.440 1.00 34.19 ? 313 LEU A CG    1 
ATOM   1285 C CD1   . LEU A 1 172 ? -34.568 31.447 -30.667 1.00 29.21 ? 313 LEU A CD1   1 
ATOM   1286 C CD2   . LEU A 1 172 ? -32.489 30.235 -31.442 1.00 31.79 ? 313 LEU A CD2   1 
ATOM   1287 N N     . LEU A 1 173 ? -31.977 28.714 -26.183 1.00 31.35 ? 314 LEU A N     1 
ATOM   1288 C CA    . LEU A 1 173 ? -31.419 29.010 -24.873 1.00 32.99 ? 314 LEU A CA    1 
ATOM   1289 C C     . LEU A 1 173 ? -30.108 28.258 -24.662 1.00 36.94 ? 314 LEU A C     1 
ATOM   1290 O O     . LEU A 1 173 ? -29.982 27.091 -25.040 1.00 32.12 ? 314 LEU A O     1 
ATOM   1291 C CB    . LEU A 1 173 ? -32.420 28.643 -23.778 1.00 34.84 ? 314 LEU A CB    1 
ATOM   1292 C CG    . LEU A 1 173 ? -33.810 29.270 -23.901 1.00 30.37 ? 314 LEU A CG    1 
ATOM   1293 C CD1   . LEU A 1 173 ? -34.684 28.824 -22.745 1.00 29.58 ? 314 LEU A CD1   1 
ATOM   1294 C CD2   . LEU A 1 173 ? -33.687 30.782 -23.949 1.00 22.37 ? 314 LEU A CD2   1 
ATOM   1295 N N     . GLY A 1 174 ? -29.129 28.935 -24.057 1.00 36.67 ? 315 GLY A N     1 
ATOM   1296 C CA    . GLY A 1 174 ? -27.832 28.344 -23.801 1.00 33.53 ? 315 GLY A CA    1 
ATOM   1297 C C     . GLY A 1 174 ? -27.054 29.056 -22.712 1.00 35.76 ? 315 GLY A C     1 
ATOM   1298 O O     . GLY A 1 174 ? -27.601 29.853 -21.944 1.00 37.44 ? 315 GLY A O     1 
ATOM   1299 N N     . PRO A 1 175 ? -25.748 28.783 -22.631 1.00 36.69 ? 316 PRO A N     1 
ATOM   1300 C CA    . PRO A 1 175 ? -24.931 29.401 -21.573 1.00 39.04 ? 316 PRO A CA    1 
ATOM   1301 C C     . PRO A 1 175 ? -24.765 30.907 -21.717 1.00 38.70 ? 316 PRO A C     1 
ATOM   1302 O O     . PRO A 1 175 ? -24.494 31.577 -20.712 1.00 41.51 ? 316 PRO A O     1 
ATOM   1303 C CB    . PRO A 1 175 ? -23.582 28.673 -21.701 1.00 39.81 ? 316 PRO A CB    1 
ATOM   1304 C CG    . PRO A 1 175 ? -23.515 28.257 -23.135 1.00 42.56 ? 316 PRO A CG    1 
ATOM   1305 C CD    . PRO A 1 175 ? -24.945 27.948 -23.545 1.00 41.40 ? 316 PRO A CD    1 
ATOM   1306 N N     . ARG A 1 176 ? -24.931 31.461 -22.914 1.00 35.65 ? 317 ARG A N     1 
ATOM   1307 C CA    . ARG A 1 176 ? -24.790 32.891 -23.153 1.00 36.05 ? 317 ARG A CA    1 
ATOM   1308 C C     . ARG A 1 176 ? -26.105 33.660 -22.993 1.00 36.35 ? 317 ARG A C     1 
ATOM   1309 O O     . ARG A 1 176 ? -26.100 34.886 -23.115 1.00 33.09 ? 317 ARG A O     1 
ATOM   1310 C CB    . ARG A 1 176 ? -24.226 33.122 -24.563 1.00 37.11 ? 317 ARG A CB    1 
ATOM   1311 C CG    . ARG A 1 176 ? -22.769 32.673 -24.776 1.00 41.78 ? 317 ARG A CG    1 
ATOM   1312 C CD    . ARG A 1 176 ? -21.899 32.916 -23.527 1.00 43.72 ? 317 ARG A CD    1 
ATOM   1313 N NE    . ARG A 1 176 ? -21.599 34.336 -23.328 1.00 45.79 ? 317 ARG A NE    1 
ATOM   1314 C CZ    . ARG A 1 176 ? -20.868 35.080 -24.151 1.00 44.92 ? 317 ARG A CZ    1 
ATOM   1315 N NH1   . ARG A 1 176 ? -20.284 34.561 -25.222 1.00 44.17 ? 317 ARG A NH1   1 
ATOM   1316 N NH2   . ARG A 1 176 ? -20.713 36.378 -23.889 1.00 40.76 ? 317 ARG A NH2   1 
ATOM   1317 N N     . THR A 1 177 ? -27.223 32.980 -22.726 1.00 33.07 ? 318 THR A N     1 
ATOM   1318 C CA    . THR A 1 177 ? -28.517 33.648 -22.617 1.00 30.14 ? 318 THR A CA    1 
ATOM   1319 C C     . THR A 1 177 ? -28.592 34.420 -21.307 1.00 28.01 ? 318 THR A C     1 
ATOM   1320 O O     . THR A 1 177 ? -28.591 33.818 -20.231 1.00 32.95 ? 318 THR A O     1 
ATOM   1321 C CB    . THR A 1 177 ? -29.666 32.635 -22.669 1.00 32.09 ? 318 THR A CB    1 
ATOM   1322 O OG1   . THR A 1 177 ? -29.557 31.807 -23.835 1.00 28.15 ? 318 THR A OG1   1 
ATOM   1323 C CG2   . THR A 1 177 ? -31.021 33.370 -22.707 1.00 26.01 ? 318 THR A CG2   1 
ATOM   1324 N N     . LYS A 1 178 ? -28.699 35.749 -21.385 1.00 25.52 ? 319 LYS A N     1 
ATOM   1325 C CA    . LYS A 1 178 ? -28.855 36.547 -20.175 1.00 25.57 ? 319 LYS A CA    1 
ATOM   1326 C C     . LYS A 1 178 ? -30.262 37.098 -19.964 1.00 27.06 ? 319 LYS A C     1 
ATOM   1327 O O     . LYS A 1 178 ? -30.646 37.356 -18.815 1.00 28.68 ? 319 LYS A O     1 
ATOM   1328 C CB    . LYS A 1 178 ? -27.845 37.703 -20.178 1.00 26.35 ? 319 LYS A CB    1 
ATOM   1329 C CG    . LYS A 1 178 ? -26.485 37.314 -19.584 1.00 34.04 ? 319 LYS A CG    1 
ATOM   1330 C CD    . LYS A 1 178 ? -25.671 36.510 -20.569 1.00 41.27 ? 319 LYS A CD    1 
ATOM   1331 C CE    . LYS A 1 178 ? -24.245 36.239 -20.070 1.00 46.41 ? 319 LYS A CE    1 
ATOM   1332 N NZ    . LYS A 1 178 ? -23.532 35.298 -21.007 1.00 49.65 ? 319 LYS A NZ    1 
ATOM   1333 N N     . LEU A 1 179 ? -31.042 37.275 -21.026 1.00 26.15 ? 320 LEU A N     1 
ATOM   1334 C CA    . LEU A 1 179 ? -32.343 37.907 -20.892 1.00 22.24 ? 320 LEU A CA    1 
ATOM   1335 C C     . LEU A 1 179 ? -33.291 37.317 -21.920 1.00 26.20 ? 320 LEU A C     1 
ATOM   1336 O O     . LEU A 1 179 ? -32.920 37.132 -23.082 1.00 25.49 ? 320 LEU A O     1 
ATOM   1337 C CB    . LEU A 1 179 ? -32.243 39.423 -21.075 1.00 24.57 ? 320 LEU A CB    1 
ATOM   1338 C CG    . LEU A 1 179 ? -33.555 40.222 -21.006 1.00 28.64 ? 320 LEU A CG    1 
ATOM   1339 C CD1   . LEU A 1 179 ? -34.170 40.189 -19.616 1.00 23.70 ? 320 LEU A CD1   1 
ATOM   1340 C CD2   . LEU A 1 179 ? -33.251 41.627 -21.391 1.00 28.94 ? 320 LEU A CD2   1 
ATOM   1341 N N     . VAL A 1 180 ? -34.504 36.999 -21.473 1.00 21.59 ? 321 VAL A N     1 
ATOM   1342 C CA    . VAL A 1 180 ? -35.616 36.646 -22.349 1.00 21.35 ? 321 VAL A CA    1 
ATOM   1343 C C     . VAL A 1 180 ? -36.654 37.747 -22.198 1.00 24.44 ? 321 VAL A C     1 
ATOM   1344 O O     . VAL A 1 180 ? -37.009 38.107 -21.071 1.00 22.37 ? 321 VAL A O     1 
ATOM   1345 C CB    . VAL A 1 180 ? -36.217 35.273 -21.992 1.00 24.51 ? 321 VAL A CB    1 
ATOM   1346 C CG1   . VAL A 1 180 ? -37.445 34.986 -22.842 1.00 23.61 ? 321 VAL A CG1   1 
ATOM   1347 C CG2   . VAL A 1 180 ? -35.185 34.152 -22.159 1.00 23.94 ? 321 VAL A CG2   1 
ATOM   1348 N N     . ALA A 1 181 ? -37.109 38.310 -23.318 1.00 21.31 ? 322 ALA A N     1 
ATOM   1349 C CA    . ALA A 1 181 ? -38.180 39.305 -23.301 1.00 20.52 ? 322 ALA A CA    1 
ATOM   1350 C C     . ALA A 1 181 ? -39.292 38.808 -24.209 1.00 21.33 ? 322 ALA A C     1 
ATOM   1351 O O     . ALA A 1 181 ? -39.108 38.725 -25.424 1.00 22.12 ? 322 ALA A O     1 
ATOM   1352 C CB    . ALA A 1 181 ? -37.677 40.680 -23.752 1.00 19.48 ? 322 ALA A CB    1 
ATOM   1353 N N     . ALA A 1 182 ? -40.449 38.483 -23.635 1.00 22.13 ? 323 ALA A N     1 
ATOM   1354 C CA    . ALA A 1 182 ? -41.502 37.830 -24.402 1.00 23.18 ? 323 ALA A CA    1 
ATOM   1355 C C     . ALA A 1 182 ? -42.839 38.507 -24.168 1.00 24.63 ? 323 ALA A C     1 
ATOM   1356 O O     . ALA A 1 182 ? -43.155 38.902 -23.041 1.00 25.38 ? 323 ALA A O     1 
ATOM   1357 C CB    . ALA A 1 182 ? -41.612 36.352 -24.034 1.00 22.98 ? 323 ALA A CB    1 
ATOM   1358 N N     . THR A 1 183 ? -43.630 38.638 -25.232 1.00 22.42 ? 324 THR A N     1 
ATOM   1359 C CA    . THR A 1 183 ? -44.981 39.154 -25.074 1.00 21.60 ? 324 THR A CA    1 
ATOM   1360 C C     . THR A 1 183 ? -45.891 38.050 -24.548 1.00 18.86 ? 324 THR A C     1 
ATOM   1361 O O     . THR A 1 183 ? -45.719 36.877 -24.885 1.00 21.57 ? 324 THR A O     1 
ATOM   1362 C CB    . THR A 1 183 ? -45.529 39.703 -26.395 1.00 21.84 ? 324 THR A CB    1 
ATOM   1363 O OG1   . THR A 1 183 ? -46.804 40.308 -26.155 1.00 24.19 ? 324 THR A OG1   1 
ATOM   1364 C CG2   . THR A 1 183 ? -45.725 38.599 -27.417 1.00 23.80 ? 324 THR A CG2   1 
ATOM   1365 N N     . GLN A 1 184 ? -46.844 38.423 -23.685 1.00 19.20 ? 325 GLN A N     1 
ATOM   1366 C CA    . GLN A 1 184 ? -47.845 37.450 -23.251 1.00 19.45 ? 325 GLN A CA    1 
ATOM   1367 C C     . GLN A 1 184 ? -49.001 37.342 -24.243 1.00 20.83 ? 325 GLN A C     1 
ATOM   1368 O O     . GLN A 1 184 ? -49.568 36.257 -24.415 1.00 21.41 ? 325 GLN A O     1 
ATOM   1369 C CB    . GLN A 1 184 ? -48.379 37.805 -21.864 1.00 21.44 ? 325 GLN A CB    1 
ATOM   1370 C CG    . GLN A 1 184 ? -49.367 36.750 -21.307 1.00 22.42 ? 325 GLN A CG    1 
ATOM   1371 C CD    . GLN A 1 184 ? -49.586 36.882 -19.813 1.00 24.40 ? 325 GLN A CD    1 
ATOM   1372 O OE1   . GLN A 1 184 ? -49.302 37.928 -19.228 1.00 23.31 ? 325 GLN A OE1   1 
ATOM   1373 N NE2   . GLN A 1 184 ? -50.096 35.823 -19.188 1.00 22.95 ? 325 GLN A NE2   1 
ATOM   1374 N N     . VAL A 1 185 ? -49.391 38.451 -24.875 1.00 18.02 ? 326 VAL A N     1 
ATOM   1375 C CA    . VAL A 1 185 ? -50.437 38.455 -25.901 1.00 19.22 ? 326 VAL A CA    1 
ATOM   1376 C C     . VAL A 1 185 ? -49.951 39.321 -27.057 1.00 20.72 ? 326 VAL A C     1 
ATOM   1377 O O     . VAL A 1 185 ? -49.621 40.497 -26.857 1.00 17.86 ? 326 VAL A O     1 
ATOM   1378 C CB    . VAL A 1 185 ? -51.786 38.985 -25.383 1.00 17.12 ? 326 VAL A CB    1 
ATOM   1379 C CG1   . VAL A 1 185 ? -52.766 39.164 -26.551 1.00 17.37 ? 326 VAL A CG1   1 
ATOM   1380 C CG2   . VAL A 1 185 ? -52.380 38.044 -24.321 1.00 18.03 ? 326 VAL A CG2   1 
ATOM   1381 N N     . SER A 1 186 ? -49.909 38.746 -28.262 1.00 21.34 ? 327 SER A N     1 
ATOM   1382 C CA    . SER A 1 186 ? -49.517 39.493 -29.457 1.00 20.84 ? 327 SER A CA    1 
ATOM   1383 C C     . SER A 1 186 ? -50.576 40.539 -29.804 1.00 20.71 ? 327 SER A C     1 
ATOM   1384 O O     . SER A 1 186 ? -51.749 40.204 -29.984 1.00 19.42 ? 327 SER A O     1 
ATOM   1385 C CB    . SER A 1 186 ? -49.324 38.530 -30.622 1.00 22.36 ? 327 SER A CB    1 
ATOM   1386 O OG    . SER A 1 186 ? -49.335 39.220 -31.861 1.00 21.79 ? 327 SER A OG    1 
ATOM   1387 N N     . ASN A 1 187 ? -50.169 41.809 -29.915 1.00 19.56 ? 328 ASN A N     1 
ATOM   1388 C CA    . ASN A 1 187 ? -51.124 42.856 -30.268 1.00 20.80 ? 328 ASN A CA    1 
ATOM   1389 C C     . ASN A 1 187 ? -51.546 42.797 -31.730 1.00 20.13 ? 328 ASN A C     1 
ATOM   1390 O O     . ASN A 1 187 ? -52.561 43.403 -32.089 1.00 21.39 ? 328 ASN A O     1 
ATOM   1391 C CB    . ASN A 1 187 ? -50.539 44.242 -29.969 1.00 23.46 ? 328 ASN A CB    1 
ATOM   1392 C CG    . ASN A 1 187 ? -49.425 44.609 -30.923 1.00 21.73 ? 328 ASN A CG    1 
ATOM   1393 O OD1   . ASN A 1 187 ? -48.406 43.924 -30.977 1.00 24.46 ? 328 ASN A OD1   1 
ATOM   1394 N ND2   . ASN A 1 187 ? -49.625 45.668 -31.714 1.00 23.24 ? 328 ASN A ND2   1 
ATOM   1395 N N     . ALA A 1 188 ? -50.789 42.106 -32.585 1.00 18.93 ? 329 ALA A N     1 
ATOM   1396 C CA    . ALA A 1 188 ? -51.143 41.998 -33.998 1.00 22.08 ? 329 ALA A CA    1 
ATOM   1397 C C     . ALA A 1 188 ? -51.894 40.722 -34.340 1.00 19.45 ? 329 ALA A C     1 
ATOM   1398 O O     . ALA A 1 188 ? -52.734 40.740 -35.247 1.00 19.98 ? 329 ALA A O     1 
ATOM   1399 C CB    . ALA A 1 188 ? -49.885 42.079 -34.881 1.00 20.54 ? 329 ALA A CB    1 
ATOM   1400 N N     . LEU A 1 189 ? -51.607 39.612 -33.650 1.00 20.45 ? 330 LEU A N     1 
ATOM   1401 C CA    . LEU A 1 189 ? -52.211 38.322 -33.960 1.00 19.98 ? 330 LEU A CA    1 
ATOM   1402 C C     . LEU A 1 189 ? -53.156 37.811 -32.886 1.00 21.86 ? 330 LEU A C     1 
ATOM   1403 O O     . LEU A 1 189 ? -53.985 36.945 -33.184 1.00 22.16 ? 330 LEU A O     1 
ATOM   1404 C CB    . LEU A 1 189 ? -51.127 37.255 -34.174 1.00 21.90 ? 330 LEU A CB    1 
ATOM   1405 C CG    . LEU A 1 189 ? -50.212 37.411 -35.382 1.00 24.47 ? 330 LEU A CG    1 
ATOM   1406 C CD1   . LEU A 1 189 ? -49.521 36.081 -35.682 1.00 23.00 ? 330 LEU A CD1   1 
ATOM   1407 C CD2   . LEU A 1 189 ? -50.997 37.912 -36.576 1.00 23.43 ? 330 LEU A CD2   1 
ATOM   1408 N N     . GLY A 1 190 ? -53.055 38.316 -31.657 1.00 20.41 ? 331 GLY A N     1 
ATOM   1409 C CA    . GLY A 1 190 ? -53.879 37.832 -30.569 1.00 19.26 ? 331 GLY A CA    1 
ATOM   1410 C C     . GLY A 1 190 ? -53.357 36.587 -29.884 1.00 23.25 ? 331 GLY A C     1 
ATOM   1411 O O     . GLY A 1 190 ? -53.963 36.147 -28.898 1.00 19.68 ? 331 GLY A O     1 
ATOM   1412 N N     . THR A 1 191 ? -52.258 36.005 -30.377 1.00 22.49 ? 332 THR A N     1 
ATOM   1413 C CA    . THR A 1 191 ? -51.685 34.791 -29.793 1.00 23.12 ? 332 THR A CA    1 
ATOM   1414 C C     . THR A 1 191 ? -51.429 34.965 -28.304 1.00 24.79 ? 332 THR A C     1 
ATOM   1415 O O     . THR A 1 191 ? -50.805 35.945 -27.889 1.00 20.52 ? 332 THR A O     1 
ATOM   1416 C CB    . THR A 1 191 ? -50.357 34.461 -30.479 1.00 23.28 ? 332 THR A CB    1 
ATOM   1417 O OG1   . THR A 1 191 ? -50.576 34.191 -31.863 1.00 21.15 ? 332 THR A OG1   1 
ATOM   1418 C CG2   . THR A 1 191 ? -49.675 33.255 -29.801 1.00 21.72 ? 332 THR A CG2   1 
ATOM   1419 N N     . VAL A 1 192 ? -51.894 34.005 -27.503 1.00 21.93 ? 333 VAL A N     1 
ATOM   1420 C CA    . VAL A 1 192 ? -51.500 33.925 -26.100 1.00 23.69 ? 333 VAL A CA    1 
ATOM   1421 C C     . VAL A 1 192 ? -50.294 33.005 -25.990 1.00 26.84 ? 333 VAL A C     1 
ATOM   1422 O O     . VAL A 1 192 ? -50.300 31.895 -26.536 1.00 25.80 ? 333 VAL A O     1 
ATOM   1423 C CB    . VAL A 1 192 ? -52.656 33.418 -25.223 1.00 26.96 ? 333 VAL A CB    1 
ATOM   1424 C CG1   . VAL A 1 192 ? -52.212 33.381 -23.770 1.00 25.15 ? 333 VAL A CG1   1 
ATOM   1425 C CG2   . VAL A 1 192 ? -53.882 34.303 -25.383 1.00 22.29 ? 333 VAL A CG2   1 
ATOM   1426 N N     . THR A 1 193 ? -49.229 33.473 -25.280 1.00 28.26 ? 334 THR A N     1 
ATOM   1427 C CA    . THR A 1 193 ? -48.065 32.608 -25.195 1.00 24.23 ? 334 THR A CA    1 
ATOM   1428 C C     . THR A 1 193 ? -47.993 31.926 -23.831 1.00 27.25 ? 334 THR A C     1 
ATOM   1429 O O     . THR A 1 193 ? -48.522 32.441 -22.840 1.00 28.83 ? 334 THR A O     1 
ATOM   1430 C CB    . THR A 1 193 ? -46.771 33.404 -25.441 1.00 26.71 ? 334 THR A CB    1 
ATOM   1431 O OG1   . THR A 1 193 ? -46.584 34.370 -24.399 1.00 22.58 ? 334 THR A OG1   1 
ATOM   1432 C CG2   . THR A 1 193 ? -46.815 34.105 -26.802 1.00 25.42 ? 334 THR A CG2   1 
ATOM   1433 N N     . PRO A 1 194 ? -47.344 30.759 -23.735 1.00 28.19 ? 335 PRO A N     1 
ATOM   1434 C CA    . PRO A 1 194 ? -47.269 30.048 -22.434 1.00 30.17 ? 335 PRO A CA    1 
ATOM   1435 C C     . PRO A 1 194 ? -46.205 30.653 -21.521 1.00 30.32 ? 335 PRO A C     1 
ATOM   1436 O O     . PRO A 1 194 ? -45.084 30.161 -21.400 1.00 30.29 ? 335 PRO A O     1 
ATOM   1437 C CB    . PRO A 1 194 ? -46.904 28.623 -22.856 1.00 33.81 ? 335 PRO A CB    1 
ATOM   1438 C CG    . PRO A 1 194 ? -46.049 28.828 -24.058 1.00 32.97 ? 335 PRO A CG    1 
ATOM   1439 C CD    . PRO A 1 194 ? -46.672 30.000 -24.806 1.00 28.47 ? 335 PRO A CD    1 
ATOM   1440 N N     . VAL A 1 195 ? -46.557 31.759 -20.858 1.00 26.72 ? 336 VAL A N     1 
ATOM   1441 C CA    . VAL A 1 195 ? -45.532 32.540 -20.169 1.00 31.03 ? 336 VAL A CA    1 
ATOM   1442 C C     . VAL A 1 195 ? -44.944 31.779 -18.986 1.00 29.54 ? 336 VAL A C     1 
ATOM   1443 O O     . VAL A 1 195 ? -43.760 31.949 -18.675 1.00 29.59 ? 336 VAL A O     1 
ATOM   1444 C CB    . VAL A 1 195 ? -46.078 33.915 -19.741 1.00 29.32 ? 336 VAL A CB    1 
ATOM   1445 C CG1   . VAL A 1 195 ? -46.361 34.761 -20.974 1.00 27.47 ? 336 VAL A CG1   1 
ATOM   1446 C CG2   . VAL A 1 195 ? -47.337 33.755 -18.900 1.00 36.79 ? 336 VAL A CG2   1 
ATOM   1447 N N     . GLU A 1 196 ? -45.737 30.943 -18.308 1.00 28.44 ? 337 GLU A N     1 
ATOM   1448 C CA    . GLU A 1 196 ? -45.188 30.117 -17.230 1.00 34.53 ? 337 GLU A CA    1 
ATOM   1449 C C     . GLU A 1 196 ? -44.004 29.287 -17.722 1.00 30.14 ? 337 GLU A C     1 
ATOM   1450 O O     . GLU A 1 196 ? -42.938 29.252 -17.087 1.00 32.70 ? 337 GLU A O     1 
ATOM   1451 C CB    . GLU A 1 196 ? -46.274 29.200 -16.647 1.00 36.97 ? 337 GLU A CB    1 
ATOM   1452 C CG    . GLU A 1 196 ? -47.468 29.898 -16.004 1.00 41.66 ? 337 GLU A CG    1 
ATOM   1453 C CD    . GLU A 1 196 ? -48.472 30.459 -17.017 1.00 49.31 ? 337 GLU A CD    1 
ATOM   1454 O OE1   . GLU A 1 196 ? -48.470 30.028 -18.195 1.00 48.34 ? 337 GLU A OE1   1 
ATOM   1455 O OE2   . GLU A 1 196 ? -49.277 31.330 -16.625 1.00 48.50 ? 337 GLU A OE2   1 
ATOM   1456 N N     . THR A 1 197 ? -44.168 28.631 -18.875 1.00 31.84 ? 338 THR A N     1 
ATOM   1457 C CA    . THR A 1 197 ? -43.090 27.816 -19.430 1.00 31.91 ? 338 THR A CA    1 
ATOM   1458 C C     . THR A 1 197 ? -41.906 28.670 -19.854 1.00 33.06 ? 338 THR A C     1 
ATOM   1459 O O     . THR A 1 197 ? -40.751 28.283 -19.643 1.00 32.41 ? 338 THR A O     1 
ATOM   1460 C CB    . THR A 1 197 ? -43.602 27.008 -20.621 1.00 34.09 ? 338 THR A CB    1 
ATOM   1461 O OG1   . THR A 1 197 ? -44.877 26.441 -20.298 1.00 36.73 ? 338 THR A OG1   1 
ATOM   1462 C CG2   . THR A 1 197 ? -42.618 25.907 -20.982 1.00 33.10 ? 338 THR A CG2   1 
ATOM   1463 N N     . ILE A 1 198 ? -42.174 29.816 -20.481 1.00 30.34 ? 339 ILE A N     1 
ATOM   1464 C CA    . ILE A 1 198 ? -41.103 30.710 -20.909 1.00 28.71 ? 339 ILE A CA    1 
ATOM   1465 C C     . ILE A 1 198 ? -40.267 31.142 -19.712 1.00 27.84 ? 339 ILE A C     1 
ATOM   1466 O O     . ILE A 1 198 ? -39.029 31.138 -19.755 1.00 30.28 ? 339 ILE A O     1 
ATOM   1467 C CB    . ILE A 1 198 ? -41.697 31.921 -21.654 1.00 28.74 ? 339 ILE A CB    1 
ATOM   1468 C CG1   . ILE A 1 198 ? -42.481 31.443 -22.872 1.00 27.91 ? 339 ILE A CG1   1 
ATOM   1469 C CG2   . ILE A 1 198 ? -40.600 32.894 -22.045 1.00 26.59 ? 339 ILE A CG2   1 
ATOM   1470 C CD1   . ILE A 1 198 ? -43.228 32.532 -23.597 1.00 31.97 ? 339 ILE A CD1   1 
ATOM   1471 N N     . VAL A 1 199 ? -40.937 31.524 -18.622 1.00 26.41 ? 340 VAL A N     1 
ATOM   1472 C CA    . VAL A 1 199 ? -40.230 31.991 -17.435 1.00 30.04 ? 340 VAL A CA    1 
ATOM   1473 C C     . VAL A 1 199 ? -39.408 30.861 -16.824 1.00 31.37 ? 340 VAL A C     1 
ATOM   1474 O O     . VAL A 1 199 ? -38.249 31.059 -16.439 1.00 31.42 ? 340 VAL A O     1 
ATOM   1475 C CB    . VAL A 1 199 ? -41.223 32.581 -16.416 1.00 29.52 ? 340 VAL A CB    1 
ATOM   1476 C CG1   . VAL A 1 199 ? -40.546 32.757 -15.052 1.00 27.48 ? 340 VAL A CG1   1 
ATOM   1477 C CG2   . VAL A 1 199 ? -41.806 33.907 -16.928 1.00 27.62 ? 340 VAL A CG2   1 
ATOM   1478 N N     . GLU A 1 200 ? -39.993 29.660 -16.726 1.00 32.03 ? 341 GLU A N     1 
ATOM   1479 C CA    . GLU A 1 200 ? -39.276 28.529 -16.136 1.00 33.53 ? 341 GLU A CA    1 
ATOM   1480 C C     . GLU A 1 200 ? -38.056 28.148 -16.962 1.00 31.30 ? 341 GLU A C     1 
ATOM   1481 O O     . GLU A 1 200 ? -36.974 27.891 -16.412 1.00 34.54 ? 341 GLU A O     1 
ATOM   1482 C CB    . GLU A 1 200 ? -40.210 27.331 -16.000 1.00 34.64 ? 341 GLU A CB    1 
ATOM   1483 C CG    . GLU A 1 200 ? -40.015 26.570 -14.707 1.00 50.20 ? 341 GLU A CG    1 
ATOM   1484 C CD    . GLU A 1 200 ? -40.570 27.334 -13.518 1.00 61.19 ? 341 GLU A CD    1 
ATOM   1485 O OE1   . GLU A 1 200 ? -41.812 27.443 -13.412 1.00 63.25 ? 341 GLU A OE1   1 
ATOM   1486 O OE2   . GLU A 1 200 ? -39.763 27.833 -12.698 1.00 66.03 ? 341 GLU A OE2   1 
ATOM   1487 N N     . LEU A 1 201 ? -38.209 28.105 -18.286 1.00 29.78 ? 342 LEU A N     1 
ATOM   1488 C CA    . LEU A 1 201 ? -37.078 27.798 -19.150 1.00 32.90 ? 342 LEU A CA    1 
ATOM   1489 C C     . LEU A 1 201 ? -35.992 28.859 -19.023 1.00 32.97 ? 342 LEU A C     1 
ATOM   1490 O O     . LEU A 1 201 ? -34.809 28.536 -18.873 1.00 32.99 ? 342 LEU A O     1 
ATOM   1491 C CB    . LEU A 1 201 ? -37.554 27.674 -20.594 1.00 29.65 ? 342 LEU A CB    1 
ATOM   1492 C CG    . LEU A 1 201 ? -38.319 26.385 -20.887 1.00 36.84 ? 342 LEU A CG    1 
ATOM   1493 C CD1   . LEU A 1 201 ? -38.802 26.392 -22.328 1.00 37.91 ? 342 LEU A CD1   1 
ATOM   1494 C CD2   . LEU A 1 201 ? -37.425 25.187 -20.624 1.00 40.64 ? 342 LEU A CD2   1 
ATOM   1495 N N     . GLY A 1 202 ? -36.374 30.138 -19.089 1.00 29.23 ? 343 GLY A N     1 
ATOM   1496 C CA    . GLY A 1 202 ? -35.390 31.197 -18.940 1.00 27.08 ? 343 GLY A CA    1 
ATOM   1497 C C     . GLY A 1 202 ? -34.611 31.084 -17.646 1.00 28.40 ? 343 GLY A C     1 
ATOM   1498 O O     . GLY A 1 202 ? -33.385 31.187 -17.633 1.00 30.85 ? 343 GLY A O     1 
ATOM   1499 N N     . HIS A 1 203 ? -35.312 30.846 -16.539 1.00 29.56 ? 344 HIS A N     1 
ATOM   1500 C CA    . HIS A 1 203 ? -34.620 30.724 -15.265 1.00 27.63 ? 344 HIS A CA    1 
ATOM   1501 C C     . HIS A 1 203 ? -33.702 29.504 -15.241 1.00 35.65 ? 344 HIS A C     1 
ATOM   1502 O O     . HIS A 1 203 ? -32.611 29.562 -14.661 1.00 32.72 ? 344 HIS A O     1 
ATOM   1503 C CB    . HIS A 1 203 ? -35.653 30.680 -14.146 1.00 28.38 ? 344 HIS A CB    1 
ATOM   1504 C CG    . HIS A 1 203 ? -36.272 32.013 -13.868 1.00 31.16 ? 344 HIS A CG    1 
ATOM   1505 N ND1   . HIS A 1 203 ? -37.374 32.174 -13.057 1.00 29.75 ? 344 HIS A ND1   1 
ATOM   1506 C CD2   . HIS A 1 203 ? -35.929 33.253 -14.289 1.00 26.85 ? 344 HIS A CD2   1 
ATOM   1507 C CE1   . HIS A 1 203 ? -37.692 33.454 -13.000 1.00 29.97 ? 344 HIS A CE1   1 
ATOM   1508 N NE2   . HIS A 1 203 ? -36.828 34.132 -13.735 1.00 30.23 ? 344 HIS A NE2   1 
ATOM   1509 N N     . ARG A 1 204 ? -34.110 28.411 -15.895 1.00 32.18 ? 345 ARG A N     1 
ATOM   1510 C CA    . ARG A 1 204 ? -33.283 27.208 -15.945 1.00 34.42 ? 345 ARG A CA    1 
ATOM   1511 C C     . ARG A 1 204 ? -31.925 27.473 -16.585 1.00 39.32 ? 345 ARG A C     1 
ATOM   1512 O O     . ARG A 1 204 ? -30.922 26.862 -16.194 1.00 39.22 ? 345 ARG A O     1 
ATOM   1513 C CB    . ARG A 1 204 ? -34.020 26.107 -16.708 1.00 37.53 ? 345 ARG A CB    1 
ATOM   1514 C CG    . ARG A 1 204 ? -33.744 24.710 -16.190 1.00 45.26 ? 345 ARG A CG    1 
ATOM   1515 C CD    . ARG A 1 204 ? -34.230 23.654 -17.162 1.00 49.09 ? 345 ARG A CD    1 
ATOM   1516 N NE    . ARG A 1 204 ? -35.670 23.439 -17.080 1.00 53.36 ? 345 ARG A NE    1 
ATOM   1517 C CZ    . ARG A 1 204 ? -36.389 22.852 -18.029 1.00 59.68 ? 345 ARG A CZ    1 
ATOM   1518 N NH1   . ARG A 1 204 ? -35.822 22.372 -19.127 1.00 57.35 ? 345 ARG A NH1   1 
ATOM   1519 N NH2   . ARG A 1 204 ? -37.705 22.727 -17.866 1.00 52.25 ? 345 ARG A NH2   1 
ATOM   1520 N N     . TYR A 1 205 ? -31.861 28.378 -17.557 1.00 37.27 ? 346 TYR A N     1 
ATOM   1521 C CA    . TYR A 1 205 ? -30.595 28.724 -18.180 1.00 36.68 ? 346 TYR A CA    1 
ATOM   1522 C C     . TYR A 1 205 ? -29.963 29.971 -17.573 1.00 34.18 ? 346 TYR A C     1 
ATOM   1523 O O     . TYR A 1 205 ? -29.012 30.511 -18.146 1.00 39.22 ? 346 TYR A O     1 
ATOM   1524 C CB    . TYR A 1 205 ? -30.779 28.901 -19.687 1.00 37.74 ? 346 TYR A CB    1 
ATOM   1525 C CG    . TYR A 1 205 ? -31.073 27.607 -20.411 1.00 40.96 ? 346 TYR A CG    1 
ATOM   1526 C CD1   . TYR A 1 205 ? -32.311 26.990 -20.294 1.00 37.37 ? 346 TYR A CD1   1 
ATOM   1527 C CD2   . TYR A 1 205 ? -30.098 26.984 -21.194 1.00 40.50 ? 346 TYR A CD2   1 
ATOM   1528 C CE1   . TYR A 1 205 ? -32.583 25.807 -20.948 1.00 42.46 ? 346 TYR A CE1   1 
ATOM   1529 C CE2   . TYR A 1 205 ? -30.364 25.792 -21.852 1.00 37.60 ? 346 TYR A CE2   1 
ATOM   1530 C CZ    . TYR A 1 205 ? -31.601 25.211 -21.726 1.00 43.37 ? 346 TYR A CZ    1 
ATOM   1531 O OH    . TYR A 1 205 ? -31.873 24.034 -22.382 1.00 51.77 ? 346 TYR A OH    1 
ATOM   1532 N N     . GLY A 1 206 ? -30.467 30.444 -16.434 1.00 33.65 ? 347 GLY A N     1 
ATOM   1533 C CA    . GLY A 1 206 ? -29.849 31.560 -15.738 1.00 32.91 ? 347 GLY A CA    1 
ATOM   1534 C C     . GLY A 1 206 ? -30.212 32.948 -16.226 1.00 33.96 ? 347 GLY A C     1 
ATOM   1535 O O     . GLY A 1 206 ? -29.581 33.919 -15.796 1.00 35.81 ? 347 GLY A O     1 
ATOM   1536 N N     . ALA A 1 207 ? -31.202 33.089 -17.099 1.00 34.77 ? 348 ALA A N     1 
ATOM   1537 C CA    . ALA A 1 207 ? -31.558 34.402 -17.624 1.00 29.79 ? 348 ALA A CA    1 
ATOM   1538 C C     . ALA A 1 207 ? -32.632 35.064 -16.773 1.00 28.90 ? 348 ALA A C     1 
ATOM   1539 O O     . ALA A 1 207 ? -33.443 34.390 -16.132 1.00 30.89 ? 348 ALA A O     1 
ATOM   1540 C CB    . ALA A 1 207 ? -32.059 34.291 -19.063 1.00 25.36 ? 348 ALA A CB    1 
ATOM   1541 N N     . ARG A 1 208 ? -32.643 36.397 -16.783 1.00 26.92 ? 349 ARG A N     1 
ATOM   1542 C CA    . ARG A 1 208 ? -33.816 37.120 -16.296 1.00 28.13 ? 349 ARG A CA    1 
ATOM   1543 C C     . ARG A 1 208 ? -34.897 37.120 -17.373 1.00 25.01 ? 349 ARG A C     1 
ATOM   1544 O O     . ARG A 1 208 ? -34.602 37.012 -18.568 1.00 23.98 ? 349 ARG A O     1 
ATOM   1545 C CB    . ARG A 1 208 ? -33.456 38.561 -15.915 1.00 29.93 ? 349 ARG A CB    1 
ATOM   1546 C CG    . ARG A 1 208 ? -32.480 38.669 -14.759 1.00 30.79 ? 349 ARG A CG    1 
ATOM   1547 C CD    . ARG A 1 208 ? -33.203 38.623 -13.432 1.00 31.47 ? 349 ARG A CD    1 
ATOM   1548 N NE    . ARG A 1 208 ? -32.315 38.893 -12.307 1.00 29.77 ? 349 ARG A NE    1 
ATOM   1549 C CZ    . ARG A 1 208 ? -32.612 38.625 -11.042 1.00 36.33 ? 349 ARG A CZ    1 
ATOM   1550 N NH1   . ARG A 1 208 ? -33.786 38.107 -10.699 1.00 30.80 ? 349 ARG A NH1   1 
ATOM   1551 N NH2   . ARG A 1 208 ? -31.709 38.876 -10.097 1.00 38.14 ? 349 ARG A NH2   1 
ATOM   1552 N N     . VAL A 1 209 ? -36.161 37.226 -16.950 1.00 23.08 ? 350 VAL A N     1 
ATOM   1553 C CA    . VAL A 1 209 ? -37.279 37.174 -17.888 1.00 21.60 ? 350 VAL A CA    1 
ATOM   1554 C C     . VAL A 1 209 ? -38.177 38.399 -17.712 1.00 21.24 ? 350 VAL A C     1 
ATOM   1555 O O     . VAL A 1 209 ? -38.680 38.669 -16.608 1.00 22.14 ? 350 VAL A O     1 
ATOM   1556 C CB    . VAL A 1 209 ? -38.097 35.879 -17.751 1.00 25.02 ? 350 VAL A CB    1 
ATOM   1557 C CG1   . VAL A 1 209 ? -39.068 35.767 -18.925 1.00 22.95 ? 350 VAL A CG1   1 
ATOM   1558 C CG2   . VAL A 1 209 ? -37.171 34.658 -17.712 1.00 27.37 ? 350 VAL A CG2   1 
ATOM   1559 N N     . LEU A 1 210 ? -38.379 39.130 -18.806 1.00 19.52 ? 351 LEU A N     1 
ATOM   1560 C CA    . LEU A 1 210 ? -39.309 40.250 -18.886 1.00 20.61 ? 351 LEU A CA    1 
ATOM   1561 C C     . LEU A 1 210 ? -40.520 39.811 -19.693 1.00 21.80 ? 351 LEU A C     1 
ATOM   1562 O O     . LEU A 1 210 ? -40.371 39.217 -20.772 1.00 22.34 ? 351 LEU A O     1 
ATOM   1563 C CB    . LEU A 1 210 ? -38.674 41.476 -19.556 1.00 18.06 ? 351 LEU A CB    1 
ATOM   1564 C CG    . LEU A 1 210 ? -39.604 42.704 -19.715 1.00 19.63 ? 351 LEU A CG    1 
ATOM   1565 C CD1   . LEU A 1 210 ? -38.807 43.995 -19.618 1.00 16.79 ? 351 LEU A CD1   1 
ATOM   1566 C CD2   . LEU A 1 210 ? -40.422 42.699 -21.015 1.00 20.73 ? 351 LEU A CD2   1 
ATOM   1567 N N     . ILE A 1 211 ? -41.708 40.132 -19.190 1.00 17.72 ? 352 ILE A N     1 
ATOM   1568 C CA    . ILE A 1 211 ? -42.959 39.797 -19.851 1.00 19.07 ? 352 ILE A CA    1 
ATOM   1569 C C     . ILE A 1 211 ? -43.663 41.098 -20.234 1.00 17.55 ? 352 ILE A C     1 
ATOM   1570 O O     . ILE A 1 211 ? -43.917 41.961 -19.374 1.00 17.53 ? 352 ILE A O     1 
ATOM   1571 C CB    . ILE A 1 211 ? -43.843 38.906 -18.960 1.00 19.73 ? 352 ILE A CB    1 
ATOM   1572 C CG1   . ILE A 1 211 ? -43.086 37.630 -18.571 1.00 22.68 ? 352 ILE A CG1   1 
ATOM   1573 C CG2   . ILE A 1 211 ? -45.151 38.547 -19.675 1.00 20.88 ? 352 ILE A CG2   1 
ATOM   1574 C CD1   . ILE A 1 211 ? -42.736 36.713 -19.761 1.00 22.48 ? 352 ILE A CD1   1 
ATOM   1575 N N     . ASP A 1 212 ? -43.950 41.246 -21.529 1.00 17.34 ? 353 ASP A N     1 
ATOM   1576 C CA    . ASP A 1 212 ? -44.729 42.373 -22.047 1.00 18.55 ? 353 ASP A CA    1 
ATOM   1577 C C     . ASP A 1 212 ? -46.202 42.020 -21.871 1.00 17.68 ? 353 ASP A C     1 
ATOM   1578 O O     . ASP A 1 212 ? -46.755 41.193 -22.606 1.00 19.02 ? 353 ASP A O     1 
ATOM   1579 C CB    . ASP A 1 212 ? -44.362 42.652 -23.506 1.00 17.51 ? 353 ASP A CB    1 
ATOM   1580 C CG    . ASP A 1 212 ? -45.175 43.782 -24.125 1.00 20.33 ? 353 ASP A CG    1 
ATOM   1581 O OD1   . ASP A 1 212 ? -46.078 44.335 -23.466 1.00 18.16 ? 353 ASP A OD1   1 
ATOM   1582 O OD2   . ASP A 1 212 ? -44.894 44.141 -25.291 1.00 21.35 ? 353 ASP A OD2   1 
ATOM   1583 N N     . GLY A 1 213 ? -46.843 42.631 -20.879 1.00 18.72 ? 354 GLY A N     1 
ATOM   1584 C CA    . GLY A 1 213 ? -48.229 42.309 -20.575 1.00 17.24 ? 354 GLY A CA    1 
ATOM   1585 C C     . GLY A 1 213 ? -49.218 43.372 -21.003 1.00 19.28 ? 354 GLY A C     1 
ATOM   1586 O O     . GLY A 1 213 ? -50.324 43.424 -20.460 1.00 19.27 ? 354 GLY A O     1 
ATOM   1587 N N     . ALA A 1 214 ? -48.854 44.223 -21.976 1.00 15.62 ? 355 ALA A N     1 
ATOM   1588 C CA    . ALA A 1 214 ? -49.742 45.331 -22.337 1.00 17.98 ? 355 ALA A CA    1 
ATOM   1589 C C     . ALA A 1 214 ? -51.097 44.845 -22.863 1.00 18.01 ? 355 ALA A C     1 
ATOM   1590 O O     . ALA A 1 214 ? -52.124 45.503 -22.628 1.00 16.83 ? 355 ALA A O     1 
ATOM   1591 C CB    . ALA A 1 214 ? -49.062 46.247 -23.362 1.00 15.24 ? 355 ALA A CB    1 
ATOM   1592 N N     . GLN A 1 215 ? -51.130 43.711 -23.570 1.00 16.33 ? 356 GLN A N     1 
ATOM   1593 C CA    . GLN A 1 215 ? -52.381 43.130 -24.051 1.00 17.02 ? 356 GLN A CA    1 
ATOM   1594 C C     . GLN A 1 215 ? -52.829 41.901 -23.277 1.00 19.80 ? 356 GLN A C     1 
ATOM   1595 O O     . GLN A 1 215 ? -53.852 41.306 -23.639 1.00 19.83 ? 356 GLN A O     1 
ATOM   1596 C CB    . GLN A 1 215 ? -52.266 42.760 -25.529 1.00 19.98 ? 356 GLN A CB    1 
ATOM   1597 C CG    . GLN A 1 215 ? -51.873 43.933 -26.348 1.00 24.58 ? 356 GLN A CG    1 
ATOM   1598 C CD    . GLN A 1 215 ? -53.061 44.731 -26.848 1.00 30.61 ? 356 GLN A CD    1 
ATOM   1599 O OE1   . GLN A 1 215 ? -54.225 44.460 -26.508 1.00 28.31 ? 356 GLN A OE1   1 
ATOM   1600 N NE2   . GLN A 1 215 ? -52.764 45.767 -27.637 1.00 35.73 ? 356 GLN A NE2   1 
ATOM   1601 N N     . SER A 1 216 ? -52.095 41.481 -22.246 1.00 15.81 ? 357 SER A N     1 
ATOM   1602 C CA    . SER A 1 216 ? -52.640 40.412 -21.417 1.00 17.57 ? 357 SER A CA    1 
ATOM   1603 C C     . SER A 1 216 ? -53.393 40.943 -20.201 1.00 18.92 ? 357 SER A C     1 
ATOM   1604 O O     . SER A 1 216 ? -54.453 40.412 -19.852 1.00 22.21 ? 357 SER A O     1 
ATOM   1605 C CB    . SER A 1 216 ? -51.535 39.458 -20.967 1.00 17.46 ? 357 SER A CB    1 
ATOM   1606 O OG    . SER A 1 216 ? -50.581 40.104 -20.134 1.00 19.28 ? 357 SER A OG    1 
ATOM   1607 N N     . ILE A 1 217 ? -52.898 41.995 -19.561 1.00 15.28 ? 358 ILE A N     1 
ATOM   1608 C CA    . ILE A 1 217 ? -53.529 42.458 -18.327 1.00 18.56 ? 358 ILE A CA    1 
ATOM   1609 C C     . ILE A 1 217 ? -54.991 42.889 -18.507 1.00 18.83 ? 358 ILE A C     1 
ATOM   1610 O O     . ILE A 1 217 ? -55.766 42.721 -17.558 1.00 19.31 ? 358 ILE A O     1 
ATOM   1611 C CB    . ILE A 1 217 ? -52.685 43.555 -17.645 1.00 18.13 ? 358 ILE A CB    1 
ATOM   1612 C CG1   . ILE A 1 217 ? -53.182 43.757 -16.203 1.00 20.93 ? 358 ILE A CG1   1 
ATOM   1613 C CG2   . ILE A 1 217 ? -52.654 44.853 -18.443 1.00 17.77 ? 358 ILE A CG2   1 
ATOM   1614 C CD1   . ILE A 1 217 ? -52.263 44.523 -15.325 1.00 19.70 ? 358 ILE A CD1   1 
ATOM   1615 N N     . PRO A 1 218 ? -55.458 43.385 -19.664 1.00 18.60 ? 359 PRO A N     1 
ATOM   1616 C CA    . PRO A 1 218 ? -56.904 43.661 -19.781 1.00 20.07 ? 359 PRO A CA    1 
ATOM   1617 C C     . PRO A 1 218 ? -57.761 42.427 -20.033 1.00 21.60 ? 359 PRO A C     1 
ATOM   1618 O O     . PRO A 1 218 ? -58.993 42.530 -19.942 1.00 20.59 ? 359 PRO A O     1 
ATOM   1619 C CB    . PRO A 1 218 ? -56.994 44.623 -20.986 1.00 18.26 ? 359 PRO A CB    1 
ATOM   1620 C CG    . PRO A 1 218 ? -55.578 44.960 -21.358 1.00 20.84 ? 359 PRO A CG    1 
ATOM   1621 C CD    . PRO A 1 218 ? -54.757 43.800 -20.896 1.00 20.01 ? 359 PRO A CD    1 
ATOM   1622 N N     . HIS A 1 219 ? -57.160 41.267 -20.333 1.00 19.27 ? 360 HIS A N     1 
ATOM   1623 C CA    . HIS A 1 219 ? -57.899 40.150 -20.910 1.00 21.83 ? 360 HIS A CA    1 
ATOM   1624 C C     . HIS A 1 219 ? -57.783 38.833 -20.153 1.00 24.92 ? 360 HIS A C     1 
ATOM   1625 O O     . HIS A 1 219 ? -58.446 37.862 -20.536 1.00 25.05 ? 360 HIS A O     1 
ATOM   1626 C CB    . HIS A 1 219 ? -57.445 39.930 -22.362 1.00 21.22 ? 360 HIS A CB    1 
ATOM   1627 C CG    . HIS A 1 219 ? -57.697 41.111 -23.242 1.00 21.78 ? 360 HIS A CG    1 
ATOM   1628 N ND1   . HIS A 1 219 ? -58.945 41.676 -23.374 1.00 21.12 ? 360 HIS A ND1   1 
ATOM   1629 C CD2   . HIS A 1 219 ? -56.862 41.856 -24.007 1.00 21.91 ? 360 HIS A CD2   1 
ATOM   1630 C CE1   . HIS A 1 219 ? -58.874 42.711 -24.195 1.00 23.61 ? 360 HIS A CE1   1 
ATOM   1631 N NE2   . HIS A 1 219 ? -57.621 42.844 -24.591 1.00 20.98 ? 360 HIS A NE2   1 
ATOM   1632 N N     . MET A 1 220 ? -56.965 38.761 -19.111 1.00 20.64 ? 361 MET A N     1 
ATOM   1633 C CA    . MET A 1 220 ? -56.804 37.530 -18.348 1.00 24.77 ? 361 MET A CA    1 
ATOM   1634 C C     . MET A 1 220 ? -56.194 37.884 -17.006 1.00 23.73 ? 361 MET A C     1 
ATOM   1635 O O     . MET A 1 220 ? -55.481 38.893 -16.903 1.00 19.91 ? 361 MET A O     1 
ATOM   1636 C CB    . MET A 1 220 ? -55.930 36.521 -19.106 1.00 21.16 ? 361 MET A CB    1 
ATOM   1637 C CG    . MET A 1 220 ? -54.477 36.956 -19.228 1.00 25.51 ? 361 MET A CG    1 
ATOM   1638 S SD    . MET A 1 220 ? -53.577 36.015 -20.493 1.00 27.59 ? 361 MET A SD    1 
ATOM   1639 C CE    . MET A 1 220 ? -54.496 36.541 -21.940 1.00 26.86 ? 361 MET A CE    1 
ATOM   1640 N N     . PRO A 1 221 ? -56.484 37.112 -15.958 1.00 23.85 ? 362 PRO A N     1 
ATOM   1641 C CA    . PRO A 1 221 ? -55.917 37.421 -14.643 1.00 23.28 ? 362 PRO A CA    1 
ATOM   1642 C C     . PRO A 1 221 ? -54.405 37.305 -14.681 1.00 24.09 ? 362 PRO A C     1 
ATOM   1643 O O     . PRO A 1 221 ? -53.849 36.488 -15.415 1.00 24.76 ? 362 PRO A O     1 
ATOM   1644 C CB    . PRO A 1 221 ? -56.548 36.366 -13.718 1.00 25.35 ? 362 PRO A CB    1 
ATOM   1645 C CG    . PRO A 1 221 ? -57.059 35.304 -14.601 1.00 27.91 ? 362 PRO A CG    1 
ATOM   1646 C CD    . PRO A 1 221 ? -57.404 35.960 -15.911 1.00 26.11 ? 362 PRO A CD    1 
ATOM   1647 N N     . ILE A 1 222 ? -53.739 38.157 -13.900 1.00 24.23 ? 363 ILE A N     1 
ATOM   1648 C CA    . ILE A 1 222 ? -52.280 38.187 -13.819 1.00 23.41 ? 363 ILE A CA    1 
ATOM   1649 C C     . ILE A 1 222 ? -51.870 37.962 -12.368 1.00 21.79 ? 363 ILE A C     1 
ATOM   1650 O O     . ILE A 1 222 ? -52.418 38.593 -11.460 1.00 25.44 ? 363 ILE A O     1 
ATOM   1651 C CB    . ILE A 1 222 ? -51.703 39.522 -14.334 1.00 22.64 ? 363 ILE A CB    1 
ATOM   1652 C CG1   . ILE A 1 222 ? -52.080 39.777 -15.798 1.00 20.67 ? 363 ILE A CG1   1 
ATOM   1653 C CG2   . ILE A 1 222 ? -50.181 39.538 -14.185 1.00 23.02 ? 363 ILE A CG2   1 
ATOM   1654 C CD1   . ILE A 1 222 ? -51.608 38.707 -16.754 1.00 19.91 ? 363 ILE A CD1   1 
ATOM   1655 N N     . ASP A 1 223 ? -50.882 37.095 -12.156 1.00 25.50 ? 364 ASP A N     1 
ATOM   1656 C CA    . ASP A 1 223 ? -50.296 36.844 -10.833 1.00 25.95 ? 364 ASP A CA    1 
ATOM   1657 C C     . ASP A 1 223 ? -48.782 36.751 -11.027 1.00 23.93 ? 364 ASP A C     1 
ATOM   1658 O O     . ASP A 1 223 ? -48.249 35.668 -11.281 1.00 24.88 ? 364 ASP A O     1 
ATOM   1659 C CB    . ASP A 1 223 ? -50.872 35.574 -10.211 1.00 23.29 ? 364 ASP A CB    1 
ATOM   1660 C CG    . ASP A 1 223 ? -50.417 35.359 -8.764  1.00 31.09 ? 364 ASP A CG    1 
ATOM   1661 O OD1   . ASP A 1 223 ? -49.386 35.930 -8.335  1.00 30.46 ? 364 ASP A OD1   1 
ATOM   1662 O OD2   . ASP A 1 223 ? -51.114 34.617 -8.046  1.00 38.90 ? 364 ASP A OD2   1 
ATOM   1663 N N     . VAL A 1 224 ? -48.090 37.885 -10.900 1.00 22.74 ? 365 VAL A N     1 
ATOM   1664 C CA    . VAL A 1 224 ? -46.659 37.888 -11.223 1.00 24.88 ? 365 VAL A CA    1 
ATOM   1665 C C     . VAL A 1 224 ? -45.864 37.100 -10.193 1.00 25.93 ? 365 VAL A C     1 
ATOM   1666 O O     . VAL A 1 224 ? -44.804 36.545 -10.513 1.00 24.12 ? 365 VAL A O     1 
ATOM   1667 C CB    . VAL A 1 224 ? -46.113 39.321 -11.348 1.00 19.12 ? 365 VAL A CB    1 
ATOM   1668 C CG1   . VAL A 1 224 ? -46.727 40.016 -12.558 1.00 18.30 ? 365 VAL A CG1   1 
ATOM   1669 C CG2   . VAL A 1 224 ? -46.365 40.112 -10.070 1.00 19.27 ? 365 VAL A CG2   1 
ATOM   1670 N N     . ALA A 1 225 ? -46.340 37.041 -8.947  1.00 24.58 ? 366 ALA A N     1 
ATOM   1671 C CA    . ALA A 1 225 ? -45.631 36.265 -7.936  1.00 28.16 ? 366 ALA A CA    1 
ATOM   1672 C C     . ALA A 1 225 ? -45.680 34.783 -8.272  1.00 31.11 ? 366 ALA A C     1 
ATOM   1673 O O     . ALA A 1 225 ? -44.660 34.088 -8.201  1.00 30.11 ? 366 ALA A O     1 
ATOM   1674 C CB    . ALA A 1 225 ? -46.216 36.524 -6.544  1.00 27.37 ? 366 ALA A CB    1 
ATOM   1675 N N     . ALA A 1 226 ? -46.863 34.286 -8.647  1.00 31.12 ? 367 ALA A N     1 
ATOM   1676 C CA    . ALA A 1 226 ? -46.972 32.909 -9.124  1.00 31.70 ? 367 ALA A CA    1 
ATOM   1677 C C     . ALA A 1 226 ? -46.190 32.711 -10.413 1.00 30.56 ? 367 ALA A C     1 
ATOM   1678 O O     . ALA A 1 226 ? -45.527 31.686 -10.597 1.00 32.55 ? 367 ALA A O     1 
ATOM   1679 C CB    . ALA A 1 226 ? -48.441 32.545 -9.341  1.00 28.03 ? 367 ALA A CB    1 
ATOM   1680 N N     . LEU A 1 227 ? -46.266 33.679 -11.324 1.00 27.93 ? 368 LEU A N     1 
ATOM   1681 C CA    . LEU A 1 227 ? -45.586 33.553 -12.608 1.00 27.48 ? 368 LEU A CA    1 
ATOM   1682 C C     . LEU A 1 227 ? -44.073 33.506 -12.434 1.00 27.66 ? 368 LEU A C     1 
ATOM   1683 O O     . LEU A 1 227 ? -43.380 32.776 -13.153 1.00 31.47 ? 368 LEU A O     1 
ATOM   1684 C CB    . LEU A 1 227 ? -45.993 34.716 -13.506 1.00 28.13 ? 368 LEU A CB    1 
ATOM   1685 C CG    . LEU A 1 227 ? -45.340 34.882 -14.871 1.00 32.95 ? 368 LEU A CG    1 
ATOM   1686 C CD1   . LEU A 1 227 ? -45.347 33.568 -15.656 1.00 31.15 ? 368 LEU A CD1   1 
ATOM   1687 C CD2   . LEU A 1 227 ? -46.102 35.964 -15.613 1.00 33.81 ? 368 LEU A CD2   1 
ATOM   1688 N N     . GLY A 1 228 ? -43.540 34.275 -11.488 1.00 26.09 ? 369 GLY A N     1 
ATOM   1689 C CA    . GLY A 1 228 ? -42.113 34.312 -11.261 1.00 25.18 ? 369 GLY A CA    1 
ATOM   1690 C C     . GLY A 1 228 ? -41.319 35.175 -12.221 1.00 25.95 ? 369 GLY A C     1 
ATOM   1691 O O     . GLY A 1 228 ? -40.090 35.209 -12.113 1.00 23.53 ? 369 GLY A O     1 
ATOM   1692 N N     . ALA A 1 229 ? -41.970 35.861 -13.161 1.00 24.23 ? 370 ALA A N     1 
ATOM   1693 C CA    . ALA A 1 229 ? -41.246 36.717 -14.091 1.00 21.05 ? 370 ALA A CA    1 
ATOM   1694 C C     . ALA A 1 229 ? -40.473 37.781 -13.329 1.00 22.49 ? 370 ALA A C     1 
ATOM   1695 O O     . ALA A 1 229 ? -40.915 38.261 -12.279 1.00 22.07 ? 370 ALA A O     1 
ATOM   1696 C CB    . ALA A 1 229 ? -42.214 37.369 -15.076 1.00 23.39 ? 370 ALA A CB    1 
ATOM   1697 N N     . ASP A 1 230 ? -39.288 38.123 -13.840 1.00 18.89 ? 371 ASP A N     1 
ATOM   1698 C CA    . ASP A 1 230 ? -38.480 39.138 -13.182 1.00 20.60 ? 371 ASP A CA    1 
ATOM   1699 C C     . ASP A 1 230 ? -38.990 40.546 -13.453 1.00 22.13 ? 371 ASP A C     1 
ATOM   1700 O O     . ASP A 1 230 ? -38.852 41.424 -12.593 1.00 19.53 ? 371 ASP A O     1 
ATOM   1701 C CB    . ASP A 1 230 ? -37.026 39.022 -13.633 1.00 24.62 ? 371 ASP A CB    1 
ATOM   1702 C CG    . ASP A 1 230 ? -36.447 37.655 -13.348 1.00 27.55 ? 371 ASP A CG    1 
ATOM   1703 O OD1   . ASP A 1 230 ? -35.976 37.459 -12.208 1.00 27.52 ? 371 ASP A OD1   1 
ATOM   1704 O OD2   . ASP A 1 230 ? -36.478 36.786 -14.255 1.00 27.70 ? 371 ASP A OD2   1 
ATOM   1705 N N     . PHE A 1 231 ? -39.534 40.789 -14.645 1.00 18.90 ? 372 PHE A N     1 
ATOM   1706 C CA    . PHE A 1 231 ? -40.122 42.082 -14.971 1.00 18.33 ? 372 PHE A CA    1 
ATOM   1707 C C     . PHE A 1 231 ? -41.460 41.843 -15.655 1.00 19.01 ? 372 PHE A C     1 
ATOM   1708 O O     . PHE A 1 231 ? -41.594 40.898 -16.430 1.00 19.94 ? 372 PHE A O     1 
ATOM   1709 C CB    . PHE A 1 231 ? -39.220 42.913 -15.902 1.00 16.90 ? 372 PHE A CB    1 
ATOM   1710 C CG    . PHE A 1 231 ? -37.827 43.150 -15.369 1.00 21.03 ? 372 PHE A CG    1 
ATOM   1711 C CD1   . PHE A 1 231 ? -37.596 44.074 -14.368 1.00 18.35 ? 372 PHE A CD1   1 
ATOM   1712 C CD2   . PHE A 1 231 ? -36.748 42.447 -15.886 1.00 20.84 ? 372 PHE A CD2   1 
ATOM   1713 C CE1   . PHE A 1 231 ? -36.311 44.287 -13.884 1.00 21.26 ? 372 PHE A CE1   1 
ATOM   1714 C CE2   . PHE A 1 231 ? -35.458 42.655 -15.403 1.00 22.36 ? 372 PHE A CE2   1 
ATOM   1715 C CZ    . PHE A 1 231 ? -35.245 43.581 -14.403 1.00 20.72 ? 372 PHE A CZ    1 
ATOM   1716 N N     . PHE A 1 232 ? -42.439 42.706 -15.381 1.00 16.31 ? 373 PHE A N     1 
ATOM   1717 C CA    . PHE A 1 232 ? -43.743 42.649 -16.043 1.00 14.94 ? 373 PHE A CA    1 
ATOM   1718 C C     . PHE A 1 232 ? -44.161 44.079 -16.351 1.00 15.78 ? 373 PHE A C     1 
ATOM   1719 O O     . PHE A 1 232 ? -44.083 44.939 -15.467 1.00 16.01 ? 373 PHE A O     1 
ATOM   1720 C CB    . PHE A 1 232 ? -44.800 41.948 -15.158 1.00 14.26 ? 373 PHE A CB    1 
ATOM   1721 C CG    . PHE A 1 232 ? -46.164 41.791 -15.822 1.00 16.82 ? 373 PHE A CG    1 
ATOM   1722 C CD1   . PHE A 1 232 ? -46.467 40.667 -16.580 1.00 17.06 ? 373 PHE A CD1   1 
ATOM   1723 C CD2   . PHE A 1 232 ? -47.139 42.775 -15.676 1.00 16.46 ? 373 PHE A CD2   1 
ATOM   1724 C CE1   . PHE A 1 232 ? -47.713 40.523 -17.196 1.00 18.72 ? 373 PHE A CE1   1 
ATOM   1725 C CE2   . PHE A 1 232 ? -48.386 42.638 -16.288 1.00 19.92 ? 373 PHE A CE2   1 
ATOM   1726 C CZ    . PHE A 1 232 ? -48.675 41.509 -17.044 1.00 16.66 ? 373 PHE A CZ    1 
ATOM   1727 N N     . VAL A 1 233 ? -44.578 44.362 -17.590 1.00 14.53 ? 374 VAL A N     1 
ATOM   1728 C CA    . VAL A 1 233 ? -44.859 45.756 -17.953 1.00 12.66 ? 374 VAL A CA    1 
ATOM   1729 C C     . VAL A 1 233 ? -46.248 45.895 -18.563 1.00 14.09 ? 374 VAL A C     1 
ATOM   1730 O O     . VAL A 1 233 ? -46.711 45.000 -19.278 1.00 15.73 ? 374 VAL A O     1 
ATOM   1731 C CB    . VAL A 1 233 ? -43.784 46.320 -18.923 1.00 13.68 ? 374 VAL A CB    1 
ATOM   1732 C CG1   . VAL A 1 233 ? -42.420 46.260 -18.272 1.00 13.71 ? 374 VAL A CG1   1 
ATOM   1733 C CG2   . VAL A 1 233 ? -43.769 45.555 -20.255 1.00 12.62 ? 374 VAL A CG2   1 
ATOM   1734 N N     . PHE A 1 234 ? -46.913 47.034 -18.297 1.00 14.31 ? 375 PHE A N     1 
ATOM   1735 C CA    . PHE A 1 234 ? -48.181 47.305 -18.988 1.00 15.86 ? 375 PHE A CA    1 
ATOM   1736 C C     . PHE A 1 234 ? -48.540 48.799 -18.989 1.00 17.33 ? 375 PHE A C     1 
ATOM   1737 O O     . PHE A 1 234 ? -47.939 49.623 -18.283 1.00 13.33 ? 375 PHE A O     1 
ATOM   1738 C CB    . PHE A 1 234 ? -49.329 46.476 -18.394 1.00 16.37 ? 375 PHE A CB    1 
ATOM   1739 C CG    . PHE A 1 234 ? -49.769 46.916 -17.030 1.00 16.73 ? 375 PHE A CG    1 
ATOM   1740 C CD1   . PHE A 1 234 ? -49.165 46.402 -15.901 1.00 15.78 ? 375 PHE A CD1   1 
ATOM   1741 C CD2   . PHE A 1 234 ? -50.814 47.818 -16.876 1.00 19.46 ? 375 PHE A CD2   1 
ATOM   1742 C CE1   . PHE A 1 234 ? -49.573 46.802 -14.632 1.00 18.15 ? 375 PHE A CE1   1 
ATOM   1743 C CE2   . PHE A 1 234 ? -51.233 48.225 -15.611 1.00 16.62 ? 375 PHE A CE2   1 
ATOM   1744 C CZ    . PHE A 1 234 ? -50.606 47.714 -14.490 1.00 17.88 ? 375 PHE A CZ    1 
ATOM   1745 N N     . SER A 1 235 ? -49.548 49.136 -19.809 1.00 14.33 ? 376 SER A N     1 
ATOM   1746 C CA    . SER A 1 235 ? -49.981 50.516 -20.045 1.00 14.45 ? 376 SER A CA    1 
ATOM   1747 C C     . SER A 1 235 ? -51.391 50.749 -19.506 1.00 14.61 ? 376 SER A C     1 
ATOM   1748 O O     . SER A 1 235 ? -52.315 49.986 -19.816 1.00 11.93 ? 376 SER A O     1 
ATOM   1749 C CB    . SER A 1 235 ? -49.969 50.852 -21.545 1.00 16.79 ? 376 SER A CB    1 
ATOM   1750 O OG    . SER A 1 235 ? -48.646 50.864 -22.078 1.00 17.84 ? 376 SER A OG    1 
ATOM   1751 N N     . GLY A 1 236 ? -51.573 51.854 -18.778 1.00 11.74 ? 377 GLY A N     1 
ATOM   1752 C CA    . GLY A 1 236 ? -52.879 52.141 -18.202 1.00 12.23 ? 377 GLY A CA    1 
ATOM   1753 C C     . GLY A 1 236 ? -53.974 52.359 -19.233 1.00 14.44 ? 377 GLY A C     1 
ATOM   1754 O O     . GLY A 1 236 ? -55.131 51.989 -19.006 1.00 13.94 ? 377 GLY A O     1 
ATOM   1755 N N     . HIS A 1 237 ? -53.643 52.978 -20.364 1.00 12.81 ? 378 HIS A N     1 
ATOM   1756 C CA    . HIS A 1 237 ? -54.694 53.341 -21.321 1.00 13.93 ? 378 HIS A CA    1 
ATOM   1757 C C     . HIS A 1 237 ? -55.293 52.118 -22.051 1.00 14.44 ? 378 HIS A C     1 
ATOM   1758 O O     . HIS A 1 237 ? -56.359 52.210 -22.656 1.00 15.21 ? 378 HIS A O     1 
ATOM   1759 C CB    . HIS A 1 237 ? -54.170 54.375 -22.337 1.00 13.38 ? 378 HIS A CB    1 
ATOM   1760 C CG    . HIS A 1 237 ? -53.153 53.826 -23.290 1.00 17.10 ? 378 HIS A CG    1 
ATOM   1761 N ND1   . HIS A 1 237 ? -53.485 53.377 -24.549 1.00 14.48 ? 378 HIS A ND1   1 
ATOM   1762 C CD2   . HIS A 1 237 ? -51.811 53.653 -23.169 1.00 15.06 ? 378 HIS A CD2   1 
ATOM   1763 C CE1   . HIS A 1 237 ? -52.395 52.946 -25.164 1.00 17.28 ? 378 HIS A CE1   1 
ATOM   1764 N NE2   . HIS A 1 237 ? -51.365 53.105 -24.348 1.00 17.91 ? 378 HIS A NE2   1 
HETATM 1765 N N1    . LLP A 1 238 ? -46.530 46.002 -26.360 1.00 19.33 ? 379 LLP A N1    1 
HETATM 1766 C C2    . LLP A 1 238 ? -47.766 45.606 -26.683 1.00 20.75 ? 379 LLP A C2    1 
HETATM 1767 C "C2'" . LLP A 1 238 ? -48.068 44.079 -26.838 1.00 21.55 ? 379 LLP A "C2'" 1 
HETATM 1768 C C3    . LLP A 1 238 ? -48.783 46.596 -26.876 1.00 23.54 ? 379 LLP A C3    1 
HETATM 1769 O O3    . LLP A 1 238 ? -50.089 46.216 -27.213 1.00 25.64 ? 379 LLP A O3    1 
HETATM 1770 C C4    . LLP A 1 238 ? -48.488 47.940 -26.719 1.00 21.96 ? 379 LLP A C4    1 
HETATM 1771 C "C4'" . LLP A 1 238 ? -49.642 49.031 -26.946 1.00 22.44 ? 379 LLP A "C4'" 1 
HETATM 1772 C C5    . LLP A 1 238 ? -47.224 48.340 -26.383 1.00 19.05 ? 379 LLP A C5    1 
HETATM 1773 C C6    . LLP A 1 238 ? -46.231 47.365 -26.199 1.00 21.32 ? 379 LLP A C6    1 
HETATM 1774 C "C5'" . LLP A 1 238 ? -46.858 49.860 -26.213 1.00 23.66 ? 379 LLP A "C5'" 1 
HETATM 1775 O OP4   . LLP A 1 238 ? -47.605 50.512 -25.193 1.00 22.46 ? 379 LLP A OP4   1 
HETATM 1776 P P     . LLP A 1 238 ? -47.536 52.065 -25.032 1.00 24.72 ? 379 LLP A P     1 
HETATM 1777 O OP1   . LLP A 1 238 ? -46.203 52.507 -24.426 1.00 17.56 ? 379 LLP A OP1   1 
HETATM 1778 O OP2   . LLP A 1 238 ? -48.650 52.439 -24.132 1.00 20.30 ? 379 LLP A OP2   1 
HETATM 1779 O OP3   . LLP A 1 238 ? -47.715 52.729 -26.367 1.00 21.31 ? 379 LLP A OP3   1 
HETATM 1780 N N     . LLP A 1 238 ? -54.628 50.973 -21.979 1.00 12.81 ? 379 LLP A N     1 
HETATM 1781 C CA    . LLP A 1 238 ? -55.158 49.741 -22.594 1.00 14.35 ? 379 LLP A CA    1 
HETATM 1782 C CB    . LLP A 1 238 ? -54.038 48.871 -23.123 1.00 16.23 ? 379 LLP A CB    1 
HETATM 1783 C CG    . LLP A 1 238 ? -53.344 49.570 -24.299 1.00 19.68 ? 379 LLP A CG    1 
HETATM 1784 C CD    . LLP A 1 238 ? -52.320 48.621 -24.939 1.00 20.44 ? 379 LLP A CD    1 
HETATM 1785 C CE    . LLP A 1 238 ? -51.842 49.286 -26.248 1.00 26.42 ? 379 LLP A CE    1 
HETATM 1786 N NZ    . LLP A 1 238 ? -50.911 48.387 -26.935 1.00 27.30 ? 379 LLP A NZ    1 
HETATM 1787 C C     . LLP A 1 238 ? -55.956 48.954 -21.605 1.00 14.53 ? 379 LLP A C     1 
HETATM 1788 O O     . LLP A 1 238 ? -56.486 47.909 -21.954 1.00 12.31 ? 379 LLP A O     1 
ATOM   1789 N N     . ILE A 1 239 ? -56.045 49.429 -20.364 1.00 13.82 ? 380 ILE A N     1 
ATOM   1790 C CA    . ILE A 1 239 ? -56.956 48.800 -19.404 1.00 13.25 ? 380 ILE A CA    1 
ATOM   1791 C C     . ILE A 1 239 ? -57.859 49.874 -18.771 1.00 14.50 ? 380 ILE A C     1 
ATOM   1792 O O     . ILE A 1 239 ? -57.983 49.973 -17.555 1.00 14.82 ? 380 ILE A O     1 
ATOM   1793 C CB    . ILE A 1 239 ? -56.169 47.926 -18.349 1.00 11.93 ? 380 ILE A CB    1 
ATOM   1794 C CG1   . ILE A 1 239 ? -57.133 47.128 -17.461 1.00 17.36 ? 380 ILE A CG1   1 
ATOM   1795 C CG2   . ILE A 1 239 ? -55.165 48.754 -17.509 1.00 14.03 ? 380 ILE A CG2   1 
ATOM   1796 C CD1   . ILE A 1 239 ? -56.439 46.055 -16.633 1.00 15.32 ? 380 ILE A CD1   1 
ATOM   1797 N N     . TYR A 1 240 ? -58.513 50.661 -19.634 1.00 14.68 ? 381 TYR A N     1 
ATOM   1798 C CA    . TYR A 1 240 ? -59.633 51.529 -19.285 1.00 13.94 ? 381 TYR A CA    1 
ATOM   1799 C C     . TYR A 1 240 ? -59.203 52.675 -18.387 1.00 16.47 ? 381 TYR A C     1 
ATOM   1800 O O     . TYR A 1 240 ? -60.039 53.304 -17.725 1.00 12.45 ? 381 TYR A O     1 
ATOM   1801 C CB    . TYR A 1 240 ? -60.780 50.696 -18.666 1.00 17.44 ? 381 TYR A CB    1 
ATOM   1802 C CG    . TYR A 1 240 ? -60.960 49.442 -19.499 1.00 16.84 ? 381 TYR A CG    1 
ATOM   1803 C CD1   . TYR A 1 240 ? -61.576 49.511 -20.739 1.00 18.06 ? 381 TYR A CD1   1 
ATOM   1804 C CD2   . TYR A 1 240 ? -60.411 48.211 -19.098 1.00 18.02 ? 381 TYR A CD2   1 
ATOM   1805 C CE1   . TYR A 1 240 ? -61.685 48.385 -21.554 1.00 22.25 ? 381 TYR A CE1   1 
ATOM   1806 C CE2   . TYR A 1 240 ? -60.497 47.085 -19.911 1.00 16.95 ? 381 TYR A CE2   1 
ATOM   1807 C CZ    . TYR A 1 240 ? -61.140 47.183 -21.140 1.00 18.95 ? 381 TYR A CZ    1 
ATOM   1808 O OH    . TYR A 1 240 ? -61.246 46.086 -21.966 1.00 22.63 ? 381 TYR A OH    1 
ATOM   1809 N N     . GLY A 1 241 ? -57.903 52.956 -18.356 1.00 14.45 ? 382 GLY A N     1 
ATOM   1810 C CA    . GLY A 1 241 ? -57.383 54.007 -17.520 1.00 13.01 ? 382 GLY A CA    1 
ATOM   1811 C C     . GLY A 1 241 ? -56.902 55.192 -18.331 1.00 14.48 ? 382 GLY A C     1 
ATOM   1812 O O     . GLY A 1 241 ? -56.965 55.207 -19.570 1.00 14.78 ? 382 GLY A O     1 
ATOM   1813 N N     . PRO A 1 242 ? -56.403 56.213 -17.633 1.00 15.37 ? 383 PRO A N     1 
ATOM   1814 C CA    . PRO A 1 242 ? -55.912 57.415 -18.317 1.00 14.53 ? 383 PRO A CA    1 
ATOM   1815 C C     . PRO A 1 242 ? -54.697 57.125 -19.186 1.00 15.23 ? 383 PRO A C     1 
ATOM   1816 O O     . PRO A 1 242 ? -53.940 56.185 -18.938 1.00 16.09 ? 383 PRO A O     1 
ATOM   1817 C CB    . PRO A 1 242 ? -55.542 58.358 -17.164 1.00 17.12 ? 383 PRO A CB    1 
ATOM   1818 C CG    . PRO A 1 242 ? -56.197 57.744 -15.911 1.00 18.82 ? 383 PRO A CG    1 
ATOM   1819 C CD    . PRO A 1 242 ? -56.262 56.284 -16.165 1.00 16.02 ? 383 PRO A CD    1 
ATOM   1820 N N     . THR A 1 243 ? -54.516 57.958 -20.215 1.00 15.93 ? 384 THR A N     1 
ATOM   1821 C CA    . THR A 1 243 ? -53.246 57.983 -20.921 1.00 17.41 ? 384 THR A CA    1 
ATOM   1822 C C     . THR A 1 243 ? -52.156 58.488 -19.981 1.00 16.04 ? 384 THR A C     1 
ATOM   1823 O O     . THR A 1 243 ? -52.425 59.055 -18.918 1.00 14.96 ? 384 THR A O     1 
ATOM   1824 C CB    . THR A 1 243 ? -53.308 58.879 -22.175 1.00 18.11 ? 384 THR A CB    1 
ATOM   1825 O OG1   . THR A 1 243 ? -53.572 60.244 -21.803 1.00 16.69 ? 384 THR A OG1   1 
ATOM   1826 C CG2   . THR A 1 243 ? -54.388 58.414 -23.146 1.00 15.91 ? 384 THR A CG2   1 
ATOM   1827 N N     . GLY A 1 244 ? -50.913 58.251 -20.374 1.00 16.75 ? 385 GLY A N     1 
ATOM   1828 C CA    . GLY A 1 244 ? -49.792 58.839 -19.682 1.00 16.07 ? 385 GLY A CA    1 
ATOM   1829 C C     . GLY A 1 244 ? -49.323 58.103 -18.455 1.00 18.17 ? 385 GLY A C     1 
ATOM   1830 O O     . GLY A 1 244 ? -48.438 58.617 -17.758 1.00 17.77 ? 385 GLY A O     1 
ATOM   1831 N N     . ILE A 1 245 ? -49.880 56.925 -18.164 1.00 14.48 ? 386 ILE A N     1 
ATOM   1832 C CA    . ILE A 1 245 ? -49.518 56.167 -16.970 1.00 14.62 ? 386 ILE A CA    1 
ATOM   1833 C C     . ILE A 1 245 ? -49.365 54.692 -17.339 1.00 16.37 ? 386 ILE A C     1 
ATOM   1834 O O     . ILE A 1 245 ? -50.168 54.130 -18.094 1.00 14.77 ? 386 ILE A O     1 
ATOM   1835 C CB    . ILE A 1 245 ? -50.552 56.369 -15.834 1.00 17.46 ? 386 ILE A CB    1 
ATOM   1836 C CG1   . ILE A 1 245 ? -50.099 55.683 -14.534 1.00 16.19 ? 386 ILE A CG1   1 
ATOM   1837 C CG2   . ILE A 1 245 ? -51.949 55.891 -16.251 1.00 12.76 ? 386 ILE A CG2   1 
ATOM   1838 C CD1   . ILE A 1 245 ? -48.937 56.394 -13.840 1.00 16.17 ? 386 ILE A CD1   1 
ATOM   1839 N N     . GLY A 1 246 ? -48.322 54.071 -16.802 1.00 13.68 ? 387 GLY A N     1 
ATOM   1840 C CA    . GLY A 1 246 ? -48.060 52.661 -16.964 1.00 12.96 ? 387 GLY A CA    1 
ATOM   1841 C C     . GLY A 1 246 ? -47.194 52.185 -15.814 1.00 14.21 ? 387 GLY A C     1 
ATOM   1842 O O     . GLY A 1 246 ? -46.799 52.960 -14.935 1.00 13.50 ? 387 GLY A O     1 
ATOM   1843 N N     . VAL A 1 247 ? -46.861 50.897 -15.860 1.00 11.36 ? 388 VAL A N     1 
ATOM   1844 C CA    . VAL A 1 247 ? -46.230 50.219 -14.731 1.00 12.52 ? 388 VAL A CA    1 
ATOM   1845 C C     . VAL A 1 247 ? -45.104 49.310 -15.209 1.00 13.89 ? 388 VAL A C     1 
ATOM   1846 O O     . VAL A 1 247 ? -45.242 48.570 -16.197 1.00 11.31 ? 388 VAL A O     1 
ATOM   1847 C CB    . VAL A 1 247 ? -47.251 49.392 -13.920 1.00 13.95 ? 388 VAL A CB    1 
ATOM   1848 C CG1   . VAL A 1 247 ? -46.544 48.506 -12.894 1.00 14.32 ? 388 VAL A CG1   1 
ATOM   1849 C CG2   . VAL A 1 247 ? -48.262 50.305 -13.243 1.00 13.14 ? 388 VAL A CG2   1 
ATOM   1850 N N     . LEU A 1 248 ? -44.003 49.352 -14.464 1.00 13.14 ? 389 LEU A N     1 
ATOM   1851 C CA    . LEU A 1 248 ? -42.983 48.316 -14.470 1.00 13.74 ? 389 LEU A CA    1 
ATOM   1852 C C     . LEU A 1 248 ? -43.052 47.608 -13.126 1.00 15.55 ? 389 LEU A C     1 
ATOM   1853 O O     . LEU A 1 248 ? -42.860 48.234 -12.079 1.00 15.14 ? 389 LEU A O     1 
ATOM   1854 C CB    . LEU A 1 248 ? -41.591 48.908 -14.690 1.00 14.21 ? 389 LEU A CB    1 
ATOM   1855 C CG    . LEU A 1 248 ? -40.420 47.964 -14.381 1.00 18.08 ? 389 LEU A CG    1 
ATOM   1856 C CD1   . LEU A 1 248 ? -40.371 46.816 -15.393 1.00 12.47 ? 389 LEU A CD1   1 
ATOM   1857 C CD2   . LEU A 1 248 ? -39.119 48.733 -14.386 1.00 15.23 ? 389 LEU A CD2   1 
ATOM   1858 N N     . TYR A 1 249 ? -43.367 46.326 -13.145 1.00 12.84 ? 390 TYR A N     1 
ATOM   1859 C CA    . TYR A 1 249 ? -43.176 45.493 -11.981 1.00 14.67 ? 390 TYR A CA    1 
ATOM   1860 C C     . TYR A 1 249 ? -41.810 44.853 -12.107 1.00 17.43 ? 390 TYR A C     1 
ATOM   1861 O O     . TYR A 1 249 ? -41.419 44.418 -13.194 1.00 17.34 ? 390 TYR A O     1 
ATOM   1862 C CB    . TYR A 1 249 ? -44.261 44.413 -11.884 1.00 15.37 ? 390 TYR A CB    1 
ATOM   1863 C CG    . TYR A 1 249 ? -43.820 43.219 -11.053 1.00 16.04 ? 390 TYR A CG    1 
ATOM   1864 C CD1   . TYR A 1 249 ? -43.947 43.239 -9.667  1.00 16.86 ? 390 TYR A CD1   1 
ATOM   1865 C CD2   . TYR A 1 249 ? -43.270 42.081 -11.651 1.00 17.38 ? 390 TYR A CD2   1 
ATOM   1866 C CE1   . TYR A 1 249 ? -43.549 42.173 -8.889  1.00 16.90 ? 390 TYR A CE1   1 
ATOM   1867 C CE2   . TYR A 1 249 ? -42.851 41.003 -10.875 1.00 19.81 ? 390 TYR A CE2   1 
ATOM   1868 C CZ    . TYR A 1 249 ? -43.008 41.054 -9.496  1.00 18.28 ? 390 TYR A CZ    1 
ATOM   1869 O OH    . TYR A 1 249 ? -42.623 40.001 -8.712  1.00 21.03 ? 390 TYR A OH    1 
ATOM   1870 N N     . GLY A 1 250 ? -41.080 44.805 -11.001 1.00 17.70 ? 391 GLY A N     1 
ATOM   1871 C CA    . GLY A 1 250 ? -39.826 44.084 -11.006 1.00 15.62 ? 391 GLY A CA    1 
ATOM   1872 C C     . GLY A 1 250 ? -39.698 43.338 -9.705  1.00 19.58 ? 391 GLY A C     1 
ATOM   1873 O O     . GLY A 1 250 ? -40.013 43.909 -8.662  1.00 18.59 ? 391 GLY A O     1 
ATOM   1874 N N     . ARG A 1 251 ? -39.294 42.065 -9.739  1.00 19.36 ? 392 ARG A N     1 
ATOM   1875 C CA    . ARG A 1 251 ? -38.973 41.379 -8.498  1.00 23.28 ? 392 ARG A CA    1 
ATOM   1876 C C     . ARG A 1 251 ? -37.987 42.216 -7.698  1.00 22.29 ? 392 ARG A C     1 
ATOM   1877 O O     . ARG A 1 251 ? -37.129 42.896 -8.263  1.00 20.42 ? 392 ARG A O     1 
ATOM   1878 C CB    . ARG A 1 251 ? -38.379 40.000 -8.774  1.00 25.29 ? 392 ARG A CB    1 
ATOM   1879 C CG    . ARG A 1 251 ? -39.388 38.984 -9.293  1.00 27.88 ? 392 ARG A CG    1 
ATOM   1880 C CD    . ARG A 1 251 ? -38.707 37.646 -9.565  1.00 27.76 ? 392 ARG A CD    1 
ATOM   1881 N NE    . ARG A 1 251 ? -38.374 36.957 -8.327  1.00 31.17 ? 392 ARG A NE    1 
ATOM   1882 C CZ    . ARG A 1 251 ? -39.257 36.315 -7.573  1.00 38.83 ? 392 ARG A CZ    1 
ATOM   1883 N NH1   . ARG A 1 251 ? -40.538 36.235 -7.917  1.00 32.21 ? 392 ARG A NH1   1 
ATOM   1884 N NH2   . ARG A 1 251 ? -38.847 35.733 -6.448  1.00 32.50 ? 392 ARG A NH2   1 
ATOM   1885 N N     . GLU A 1 252 ? -38.138 42.181 -6.375  1.00 22.44 ? 393 GLU A N     1 
ATOM   1886 C CA    . GLU A 1 252 ? -37.239 42.914 -5.489  1.00 24.51 ? 393 GLU A CA    1 
ATOM   1887 C C     . GLU A 1 252 ? -35.772 42.675 -5.841  1.00 25.22 ? 393 GLU A C     1 
ATOM   1888 O O     . GLU A 1 252 ? -34.977 43.620 -5.913  1.00 23.41 ? 393 GLU A O     1 
ATOM   1889 C CB    . GLU A 1 252 ? -37.522 42.513 -4.038  1.00 31.33 ? 393 GLU A CB    1 
ATOM   1890 C CG    . GLU A 1 252 ? -36.863 43.386 -2.976  1.00 35.04 ? 393 GLU A CG    1 
ATOM   1891 C CD    . GLU A 1 252 ? -37.236 42.963 -1.557  1.00 43.42 ? 393 GLU A CD    1 
ATOM   1892 O OE1   . GLU A 1 252 ? -37.967 41.960 -1.403  1.00 47.59 ? 393 GLU A OE1   1 
ATOM   1893 O OE2   . GLU A 1 252 ? -36.790 43.624 -0.595  1.00 48.26 ? 393 GLU A OE2   1 
ATOM   1894 N N     . ASP A 1 253 ? -35.387 41.414 -6.070  1.00 26.58 ? 394 ASP A N     1 
ATOM   1895 C CA    . ASP A 1 253 ? -33.972 41.150 -6.342  1.00 27.46 ? 394 ASP A CA    1 
ATOM   1896 C C     . ASP A 1 253 ? -33.567 41.611 -7.741  1.00 27.55 ? 394 ASP A C     1 
ATOM   1897 O O     . ASP A 1 253 ? -32.409 41.981 -7.956  1.00 28.25 ? 394 ASP A O     1 
ATOM   1898 C CB    . ASP A 1 253 ? -33.651 39.666 -6.128  1.00 29.70 ? 394 ASP A CB    1 
ATOM   1899 C CG    . ASP A 1 253 ? -34.390 38.744 -7.097  1.00 40.29 ? 394 ASP A CG    1 
ATOM   1900 O OD1   . ASP A 1 253 ? -35.640 38.661 -7.033  1.00 36.87 ? 394 ASP A OD1   1 
ATOM   1901 O OD2   . ASP A 1 253 ? -33.706 38.070 -7.905  1.00 45.52 ? 394 ASP A OD2   1 
ATOM   1902 N N     . ALA A 1 254 ? -34.498 41.631 -8.700  1.00 24.45 ? 395 ALA A N     1 
ATOM   1903 C CA    . ALA A 1 254 ? -34.151 42.166 -10.016 1.00 23.93 ? 395 ALA A CA    1 
ATOM   1904 C C     . ALA A 1 254 ? -33.993 43.684 -9.973  1.00 22.75 ? 395 ALA A C     1 
ATOM   1905 O O     . ALA A 1 254 ? -33.088 44.236 -10.614 1.00 24.09 ? 395 ALA A O     1 
ATOM   1906 C CB    . ALA A 1 254 ? -35.203 41.757 -11.052 1.00 24.34 ? 395 ALA A CB    1 
ATOM   1907 N N     . LEU A 1 255 ? -34.861 44.382 -9.233  1.00 20.08 ? 396 LEU A N     1 
ATOM   1908 C CA    . LEU A 1 255 ? -34.732 45.834 -9.128  1.00 21.16 ? 396 LEU A CA    1 
ATOM   1909 C C     . LEU A 1 255 ? -33.495 46.230 -8.330  1.00 23.28 ? 396 LEU A C     1 
ATOM   1910 O O     . LEU A 1 255 ? -32.884 47.269 -8.615  1.00 22.78 ? 396 LEU A O     1 
ATOM   1911 C CB    . LEU A 1 255 ? -35.988 46.438 -8.494  1.00 22.18 ? 396 LEU A CB    1 
ATOM   1912 C CG    . LEU A 1 255 ? -37.293 46.379 -9.310  1.00 19.85 ? 396 LEU A CG    1 
ATOM   1913 C CD1   . LEU A 1 255 ? -38.457 46.932 -8.509  1.00 20.37 ? 396 LEU A CD1   1 
ATOM   1914 C CD2   . LEU A 1 255 ? -37.168 47.117 -10.638 1.00 20.05 ? 396 LEU A CD2   1 
ATOM   1915 N N     . ALA A 1 256 ? -33.112 45.419 -7.337  1.00 23.09 ? 397 ALA A N     1 
ATOM   1916 C CA    . ALA A 1 256 ? -31.908 45.705 -6.564  1.00 21.70 ? 397 ALA A CA    1 
ATOM   1917 C C     . ALA A 1 256 ? -30.661 45.692 -7.443  1.00 26.42 ? 397 ALA A C     1 
ATOM   1918 O O     . ALA A 1 256 ? -29.735 46.479 -7.220  1.00 27.22 ? 397 ALA A O     1 
ATOM   1919 C CB    . ALA A 1 256 ? -31.761 44.695 -5.427  1.00 20.58 ? 397 ALA A CB    1 
ATOM   1920 N N     . GLU A 1 257 ? -30.613 44.813 -8.447  1.00 23.18 ? 398 GLU A N     1 
ATOM   1921 C CA    . GLU A 1 257 ? -29.476 44.789 -9.361  1.00 24.47 ? 398 GLU A CA    1 
ATOM   1922 C C     . GLU A 1 257 ? -29.651 45.710 -10.570 1.00 26.94 ? 398 GLU A C     1 
ATOM   1923 O O     . GLU A 1 257 ? -28.787 45.715 -11.453 1.00 28.23 ? 398 GLU A O     1 
ATOM   1924 C CB    . GLU A 1 257 ? -29.179 43.356 -9.810  1.00 29.49 ? 398 GLU A CB    1 
ATOM   1925 C CG    . GLU A 1 257 ? -29.936 42.876 -11.039 1.00 33.63 ? 398 GLU A CG    1 
ATOM   1926 C CD    . GLU A 1 257 ? -29.767 41.379 -11.250 1.00 37.13 ? 398 GLU A CD    1 
ATOM   1927 O OE1   . GLU A 1 257 ? -29.136 40.722 -10.383 1.00 37.88 ? 398 GLU A OE1   1 
ATOM   1928 O OE2   . GLU A 1 257 ? -30.256 40.866 -12.280 1.00 32.00 ? 398 GLU A OE2   1 
ATOM   1929 N N     . THR A 1 258 ? -30.714 46.528 -10.606 1.00 22.60 ? 399 THR A N     1 
ATOM   1930 C CA    . THR A 1 258 ? -30.899 47.527 -11.663 1.00 23.46 ? 399 THR A CA    1 
ATOM   1931 C C     . THR A 1 258 ? -30.448 48.889 -11.154 1.00 20.06 ? 399 THR A C     1 
ATOM   1932 O O     . THR A 1 258 ? -30.943 49.341 -10.118 1.00 20.82 ? 399 THR A O     1 
ATOM   1933 C CB    . THR A 1 258 ? -32.360 47.579 -12.104 1.00 19.45 ? 399 THR A CB    1 
ATOM   1934 O OG1   . THR A 1 258 ? -32.765 46.269 -12.545 1.00 23.54 ? 399 THR A OG1   1 
ATOM   1935 C CG2   . THR A 1 258 ? -32.575 48.591 -13.246 1.00 16.78 ? 399 THR A CG2   1 
ATOM   1936 N N     . PRO A 1 259 ? -29.513 49.562 -11.811 1.00 21.70 ? 400 PRO A N     1 
ATOM   1937 C CA    . PRO A 1 259 ? -29.101 50.897 -11.364 1.00 21.18 ? 400 PRO A CA    1 
ATOM   1938 C C     . PRO A 1 259 ? -30.184 51.916 -11.665 1.00 21.52 ? 400 PRO A C     1 
ATOM   1939 O O     . PRO A 1 259 ? -31.098 51.636 -12.458 1.00 19.35 ? 400 PRO A O     1 
ATOM   1940 C CB    . PRO A 1 259 ? -27.837 51.169 -12.198 1.00 21.38 ? 400 PRO A CB    1 
ATOM   1941 C CG    . PRO A 1 259 ? -28.078 50.405 -13.468 1.00 25.04 ? 400 PRO A CG    1 
ATOM   1942 C CD    . PRO A 1 259 ? -28.808 49.144 -13.039 1.00 25.05 ? 400 PRO A CD    1 
ATOM   1943 N N     . PRO A 1 260 ? -30.118 53.110 -11.069 1.00 19.13 ? 401 PRO A N     1 
ATOM   1944 C CA    . PRO A 1 260 ? -31.085 54.153 -11.428 1.00 20.23 ? 401 PRO A CA    1 
ATOM   1945 C C     . PRO A 1 260 ? -30.959 54.504 -12.901 1.00 19.56 ? 401 PRO A C     1 
ATOM   1946 O O     . PRO A 1 260 ? -29.917 54.305 -13.535 1.00 17.45 ? 401 PRO A O     1 
ATOM   1947 C CB    . PRO A 1 260 ? -30.704 55.346 -10.531 1.00 17.71 ? 401 PRO A CB    1 
ATOM   1948 C CG    . PRO A 1 260 ? -29.720 54.804 -9.505  1.00 22.86 ? 401 PRO A CG    1 
ATOM   1949 C CD    . PRO A 1 260 ? -29.072 53.606 -10.148 1.00 19.26 ? 401 PRO A CD    1 
ATOM   1950 N N     . TRP A 1 261 ? -32.056 55.012 -13.459 1.00 15.74 ? 402 TRP A N     1 
ATOM   1951 C CA    . TRP A 1 261 ? -32.062 55.370 -14.871 1.00 15.66 ? 402 TRP A CA    1 
ATOM   1952 C C     . TRP A 1 261 ? -32.118 56.883 -15.000 1.00 18.42 ? 402 TRP A C     1 
ATOM   1953 O O     . TRP A 1 261 ? -31.088 57.531 -15.221 1.00 15.85 ? 402 TRP A O     1 
ATOM   1954 C CB    . TRP A 1 261 ? -33.242 54.707 -15.595 1.00 14.91 ? 402 TRP A CB    1 
ATOM   1955 C CG    . TRP A 1 261 ? -33.287 54.957 -17.075 1.00 17.17 ? 402 TRP A CG    1 
ATOM   1956 C CD1   . TRP A 1 261 ? -32.216 55.130 -17.924 1.00 18.40 ? 402 TRP A CD1   1 
ATOM   1957 C CD2   . TRP A 1 261 ? -34.467 55.082 -17.885 1.00 14.44 ? 402 TRP A CD2   1 
ATOM   1958 N NE1   . TRP A 1 261 ? -32.663 55.339 -19.216 1.00 17.45 ? 402 TRP A NE1   1 
ATOM   1959 C CE2   . TRP A 1 261 ? -34.039 55.309 -19.219 1.00 18.17 ? 402 TRP A CE2   1 
ATOM   1960 C CE3   . TRP A 1 261 ? -35.842 55.016 -17.612 1.00 14.11 ? 402 TRP A CE3   1 
ATOM   1961 C CZ2   . TRP A 1 261 ? -34.942 55.482 -20.277 1.00 16.30 ? 402 TRP A CZ2   1 
ATOM   1962 C CZ3   . TRP A 1 261 ? -36.748 55.172 -18.668 1.00 15.23 ? 402 TRP A CZ3   1 
ATOM   1963 C CH2   . TRP A 1 261 ? -36.288 55.404 -19.986 1.00 18.54 ? 402 TRP A CH2   1 
ATOM   1964 N N     . GLN A 1 262 ? -33.311 57.460 -14.857 1.00 12.68 ? 403 GLN A N     1 
ATOM   1965 C CA    . GLN A 1 262 ? -33.447 58.906 -14.867 1.00 11.97 ? 403 GLN A CA    1 
ATOM   1966 C C     . GLN A 1 262 ? -33.045 59.477 -13.513 1.00 15.34 ? 403 GLN A C     1 
ATOM   1967 O O     . GLN A 1 262 ? -33.323 58.880 -12.470 1.00 17.57 ? 403 GLN A O     1 
ATOM   1968 C CB    . GLN A 1 262 ? -34.889 59.293 -15.202 1.00 12.66 ? 403 GLN A CB    1 
ATOM   1969 C CG    . GLN A 1 262 ? -35.213 59.079 -16.667 1.00 15.74 ? 403 GLN A CG    1 
ATOM   1970 C CD    . GLN A 1 262 ? -36.659 59.368 -16.976 1.00 20.37 ? 403 GLN A CD    1 
ATOM   1971 O OE1   . GLN A 1 262 ? -37.193 60.402 -16.578 1.00 21.58 ? 403 GLN A OE1   1 
ATOM   1972 N NE2   . GLN A 1 262 ? -37.317 58.437 -17.664 1.00 20.23 ? 403 GLN A NE2   1 
ATOM   1973 N N     . GLY A 1 263 ? -32.392 60.642 -13.521 1.00 11.81 ? 404 GLY A N     1 
ATOM   1974 C CA    . GLY A 1 263 ? -31.946 61.282 -12.294 1.00 14.48 ? 404 GLY A CA    1 
ATOM   1975 C C     . GLY A 1 263 ? -32.722 62.551 -11.989 1.00 13.87 ? 404 GLY A C     1 
ATOM   1976 O O     . GLY A 1 263 ? -33.231 63.212 -12.893 1.00 13.53 ? 404 GLY A O     1 
ATOM   1977 N N     . GLY A 1 264 ? -32.820 62.885 -10.714 1.00 16.28 ? 405 GLY A N     1 
ATOM   1978 C CA    . GLY A 1 264 ? -33.410 64.162 -10.313 1.00 14.26 ? 405 GLY A CA    1 
ATOM   1979 C C     . GLY A 1 264 ? -34.013 64.056 -8.918  1.00 19.49 ? 405 GLY A C     1 
ATOM   1980 O O     . GLY A 1 264 ? -33.580 63.235 -8.104  1.00 16.05 ? 405 GLY A O     1 
ATOM   1981 N N     . GLY A 1 265 ? -35.023 64.892 -8.669  1.00 17.82 ? 406 GLY A N     1 
ATOM   1982 C CA    . GLY A 1 265 ? -35.727 64.830 -7.398  1.00 18.23 ? 406 GLY A CA    1 
ATOM   1983 C C     . GLY A 1 265 ? -36.422 63.495 -7.201  1.00 19.30 ? 406 GLY A C     1 
ATOM   1984 O O     . GLY A 1 265 ? -36.646 62.732 -8.145  1.00 17.37 ? 406 GLY A O     1 
ATOM   1985 N N     . ASN A 1 266 ? -36.749 63.210 -5.937  1.00 19.34 ? 407 ASN A N     1 
ATOM   1986 C CA    . ASN A 1 266 ? -37.516 62.030 -5.521  1.00 20.17 ? 407 ASN A CA    1 
ATOM   1987 C C     . ASN A 1 266 ? -36.682 60.750 -5.541  1.00 21.19 ? 407 ASN A C     1 
ATOM   1988 O O     . ASN A 1 266 ? -36.777 59.938 -4.621  1.00 19.59 ? 407 ASN A O     1 
ATOM   1989 C CB    . ASN A 1 266 ? -38.769 61.835 -6.382  1.00 18.39 ? 407 ASN A CB    1 
ATOM   1990 C CG    . ASN A 1 266 ? -39.732 60.805 -5.790  1.00 23.20 ? 407 ASN A CG    1 
ATOM   1991 O OD1   . ASN A 1 266 ? -40.346 61.048 -4.757  1.00 22.83 ? 407 ASN A OD1   1 
ATOM   1992 N ND2   . ASN A 1 266 ? -39.852 59.651 -6.439  1.00 19.41 ? 407 ASN A ND2   1 
ATOM   1993 N N     . MET A 1 267 ? -35.855 60.546 -6.564  1.00 16.84 ? 408 MET A N     1 
ATOM   1994 C CA    . MET A 1 267 ? -35.026 59.344 -6.554  1.00 18.37 ? 408 MET A CA    1 
ATOM   1995 C C     . MET A 1 267 ? -33.742 59.495 -5.735  1.00 16.62 ? 408 MET A C     1 
ATOM   1996 O O     . MET A 1 267 ? -33.098 58.485 -5.447  1.00 18.24 ? 408 MET A O     1 
ATOM   1997 C CB    . MET A 1 267 ? -34.719 58.911 -7.995  1.00 17.24 ? 408 MET A CB    1 
ATOM   1998 C CG    . MET A 1 267 ? -34.038 59.945 -8.882  1.00 17.09 ? 408 MET A CG    1 
ATOM   1999 S SD    . MET A 1 267 ? -32.246 60.093 -8.634  1.00 17.37 ? 408 MET A SD    1 
ATOM   2000 C CE    . MET A 1 267 ? -31.765 58.450 -9.244  1.00 16.51 ? 408 MET A CE    1 
ATOM   2001 N N     . ILE A 1 268 ? -33.352 60.702 -5.348  1.00 16.67 ? 409 ILE A N     1 
ATOM   2002 C CA    . ILE A 1 268 ? -32.169 60.903 -4.509  1.00 19.55 ? 409 ILE A CA    1 
ATOM   2003 C C     . ILE A 1 268 ? -32.544 60.817 -3.035  1.00 23.45 ? 409 ILE A C     1 
ATOM   2004 O O     . ILE A 1 268 ? -33.678 61.102 -2.639  1.00 24.28 ? 409 ILE A O     1 
ATOM   2005 C CB    . ILE A 1 268 ? -31.480 62.259 -4.802  1.00 23.78 ? 409 ILE A CB    1 
ATOM   2006 C CG1   . ILE A 1 268 ? -32.439 63.435 -4.582  1.00 23.14 ? 409 ILE A CG1   1 
ATOM   2007 C CG2   . ILE A 1 268 ? -30.917 62.276 -6.196  1.00 18.89 ? 409 ILE A CG2   1 
ATOM   2008 C CD1   . ILE A 1 268 ? -32.390 64.059 -3.144  1.00 26.62 ? 409 ILE A CD1   1 
ATOM   2009 N N     . ALA A 1 269 ? -31.569 60.421 -2.213  1.00 21.86 ? 410 ALA A N     1 
ATOM   2010 C CA    . ALA A 1 269 ? -31.621 60.561 -0.766  1.00 23.77 ? 410 ALA A CA    1 
ATOM   2011 C C     . ALA A 1 269 ? -30.874 61.789 -0.275  1.00 27.54 ? 410 ALA A C     1 
ATOM   2012 O O     . ALA A 1 269 ? -31.253 62.365 0.747   1.00 23.44 ? 410 ALA A O     1 
ATOM   2013 C CB    . ALA A 1 269 ? -31.032 59.319 -0.084  1.00 22.47 ? 410 ALA A CB    1 
ATOM   2014 N N     . ASP A 1 270 ? -29.820 62.197 -0.979  1.00 23.14 ? 411 ASP A N     1 
ATOM   2015 C CA    . ASP A 1 270 ? -29.008 63.341 -0.593  1.00 24.32 ? 411 ASP A CA    1 
ATOM   2016 C C     . ASP A 1 270 ? -28.228 63.796 -1.813  1.00 22.06 ? 411 ASP A C     1 
ATOM   2017 O O     . ASP A 1 270 ? -27.692 62.964 -2.550  1.00 22.18 ? 411 ASP A O     1 
ATOM   2018 C CB    . ASP A 1 270 ? -28.040 62.987 0.546   1.00 24.79 ? 411 ASP A CB    1 
ATOM   2019 C CG    . ASP A 1 270 ? -27.344 64.214 1.120   1.00 31.01 ? 411 ASP A CG    1 
ATOM   2020 O OD1   . ASP A 1 270 ? -28.029 65.051 1.739   1.00 32.96 ? 411 ASP A OD1   1 
ATOM   2021 O OD2   . ASP A 1 270 ? -26.115 64.353 0.945   1.00 34.31 ? 411 ASP A OD2   1 
ATOM   2022 N N     . VAL A 1 271 ? -28.167 65.105 -2.025  1.00 19.72 ? 412 VAL A N     1 
ATOM   2023 C CA    . VAL A 1 271 ? -27.459 65.673 -3.166  1.00 23.49 ? 412 VAL A CA    1 
ATOM   2024 C C     . VAL A 1 271 ? -26.400 66.646 -2.649  1.00 26.61 ? 412 VAL A C     1 
ATOM   2025 O O     . VAL A 1 271 ? -26.713 67.559 -1.878  1.00 23.65 ? 412 VAL A O     1 
ATOM   2026 C CB    . VAL A 1 271 ? -28.425 66.377 -4.145  1.00 22.88 ? 412 VAL A CB    1 
ATOM   2027 C CG1   . VAL A 1 271 ? -27.653 67.207 -5.173  1.00 19.50 ? 412 VAL A CG1   1 
ATOM   2028 C CG2   . VAL A 1 271 ? -29.338 65.366 -4.852  1.00 19.21 ? 412 VAL A CG2   1 
ATOM   2029 N N     . THR A 1 272 ? -25.147 66.433 -3.052  1.00 22.31 ? 413 THR A N     1 
ATOM   2030 C CA    . THR A 1 272 ? -24.121 67.469 -3.020  1.00 26.18 ? 413 THR A CA    1 
ATOM   2031 C C     . THR A 1 272 ? -23.625 67.662 -4.447  1.00 27.29 ? 413 THR A C     1 
ATOM   2032 O O     . THR A 1 272 ? -23.836 66.802 -5.311  1.00 23.71 ? 413 THR A O     1 
ATOM   2033 C CB    . THR A 1 272 ? -22.932 67.111 -2.098  1.00 26.38 ? 413 THR A CB    1 
ATOM   2034 O OG1   . THR A 1 272 ? -22.138 66.077 -2.706  1.00 27.83 ? 413 THR A OG1   1 
ATOM   2035 C CG2   . THR A 1 272 ? -23.411 66.648 -0.711  1.00 28.88 ? 413 THR A CG2   1 
ATOM   2036 N N     . LEU A 1 273 ? -22.960 68.795 -4.697  1.00 22.29 ? 414 LEU A N     1 
ATOM   2037 C CA    . LEU A 1 273 ? -22.507 69.072 -6.063  1.00 28.08 ? 414 LEU A CA    1 
ATOM   2038 C C     . LEU A 1 273 ? -21.554 67.995 -6.562  1.00 26.77 ? 414 LEU A C     1 
ATOM   2039 O O     . LEU A 1 273 ? -21.564 67.654 -7.749  1.00 24.49 ? 414 LEU A O     1 
ATOM   2040 C CB    . LEU A 1 273 ? -21.832 70.437 -6.134  1.00 26.88 ? 414 LEU A CB    1 
ATOM   2041 C CG    . LEU A 1 273 ? -22.778 71.602 -5.879  1.00 27.50 ? 414 LEU A CG    1 
ATOM   2042 C CD1   . LEU A 1 273 ? -21.991 72.895 -5.802  1.00 28.59 ? 414 LEU A CD1   1 
ATOM   2043 C CD2   . LEU A 1 273 ? -23.842 71.650 -6.972  1.00 23.12 ? 414 LEU A CD2   1 
ATOM   2044 N N     . GLU A 1 274 ? -20.752 67.425 -5.667  1.00 24.32 ? 415 GLU A N     1 
ATOM   2045 C CA    . GLU A 1 274 ? -19.774 66.426 -6.063  1.00 26.31 ? 415 GLU A CA    1 
ATOM   2046 C C     . GLU A 1 274 ? -20.350 65.010 -6.122  1.00 28.48 ? 415 GLU A C     1 
ATOM   2047 O O     . GLU A 1 274 ? -19.872 64.190 -6.916  1.00 22.00 ? 415 GLU A O     1 
ATOM   2048 C CB    . GLU A 1 274 ? -18.570 66.498 -5.116  1.00 29.61 ? 415 GLU A CB    1 
ATOM   2049 C CG    . GLU A 1 274 ? -18.905 66.436 -3.614  1.00 39.77 ? 415 GLU A CG    1 
ATOM   2050 C CD    . GLU A 1 274 ? -19.407 67.761 -2.969  1.00 46.94 ? 415 GLU A CD    1 
ATOM   2051 O OE1   . GLU A 1 274 ? -19.767 68.723 -3.689  1.00 42.08 ? 415 GLU A OE1   1 
ATOM   2052 O OE2   . GLU A 1 274 ? -19.418 67.839 -1.708  1.00 52.63 ? 415 GLU A OE2   1 
ATOM   2053 N N     . ARG A 1 275 ? -21.393 64.705 -5.345  1.00 24.21 ? 416 ARG A N     1 
ATOM   2054 C CA    . ARG A 1 275 ? -21.895 63.336 -5.289  1.00 24.55 ? 416 ARG A CA    1 
ATOM   2055 C C     . ARG A 1 275 ? -23.325 63.313 -4.761  1.00 25.46 ? 416 ARG A C     1 
ATOM   2056 O O     . ARG A 1 275 ? -23.660 64.052 -3.831  1.00 21.05 ? 416 ARG A O     1 
ATOM   2057 C CB    . ARG A 1 275 ? -21.001 62.468 -4.390  1.00 26.17 ? 416 ARG A CB    1 
ATOM   2058 C CG    . ARG A 1 275 ? -21.404 61.012 -4.373  1.00 26.58 ? 416 ARG A CG    1 
ATOM   2059 C CD    . ARG A 1 275 ? -20.679 60.264 -3.277  1.00 28.29 ? 416 ARG A CD    1 
ATOM   2060 N NE    . ARG A 1 275 ? -21.088 58.868 -3.251  1.00 27.67 ? 416 ARG A NE    1 
ATOM   2061 C CZ    . ARG A 1 275 ? -21.157 58.130 -2.151  1.00 32.02 ? 416 ARG A CZ    1 
ATOM   2062 N NH1   . ARG A 1 275 ? -20.784 58.608 -0.977  1.00 32.57 ? 416 ARG A NH1   1 
ATOM   2063 N NH2   . ARG A 1 275 ? -21.619 56.884 -2.233  1.00 30.73 ? 416 ARG A NH2   1 
ATOM   2064 N N     . SER A 1 276 ? -24.151 62.443 -5.340  1.00 22.36 ? 417 SER A N     1 
ATOM   2065 C CA    . SER A 1 276 ? -25.500 62.196 -4.850  1.00 22.61 ? 417 SER A CA    1 
ATOM   2066 C C     . SER A 1 276 ? -25.634 60.737 -4.440  1.00 25.14 ? 417 SER A C     1 
ATOM   2067 O O     . SER A 1 276 ? -25.001 59.859 -5.029  1.00 23.84 ? 417 SER A O     1 
ATOM   2068 C CB    . SER A 1 276 ? -26.555 62.527 -5.927  1.00 20.17 ? 417 SER A CB    1 
ATOM   2069 O OG    . SER A 1 276 ? -26.508 63.902 -6.263  1.00 21.01 ? 417 SER A OG    1 
ATOM   2070 N N     . LEU A 1 277 ? -26.462 60.490 -3.425  1.00 24.23 ? 418 LEU A N     1 
ATOM   2071 C CA    . LEU A 1 277 ? -26.851 59.155 -2.983  1.00 22.88 ? 418 LEU A CA    1 
ATOM   2072 C C     . LEU A 1 277 ? -28.310 58.914 -3.355  1.00 23.91 ? 418 LEU A C     1 
ATOM   2073 O O     . LEU A 1 277 ? -29.108 59.845 -3.381  1.00 19.43 ? 418 LEU A O     1 
ATOM   2074 C CB    . LEU A 1 277 ? -26.697 58.996 -1.470  1.00 25.60 ? 418 LEU A CB    1 
ATOM   2075 C CG    . LEU A 1 277 ? -25.434 59.598 -0.888  1.00 26.31 ? 418 LEU A CG    1 
ATOM   2076 C CD1   . LEU A 1 277 ? -25.568 59.771 0.624   1.00 33.29 ? 418 LEU A CD1   1 
ATOM   2077 C CD2   . LEU A 1 277 ? -24.316 58.671 -1.238  1.00 26.53 ? 418 LEU A CD2   1 
ATOM   2078 N N     . TYR A 1 278 ? -28.671 57.660 -3.611  1.00 21.30 ? 419 TYR A N     1 
ATOM   2079 C CA    . TYR A 1 278 ? -29.981 57.344 -4.164  1.00 20.61 ? 419 TYR A CA    1 
ATOM   2080 C C     . TYR A 1 278 ? -30.829 56.589 -3.150  1.00 24.08 ? 419 TYR A C     1 
ATOM   2081 O O     . TYR A 1 278 ? -30.311 55.867 -2.292  1.00 21.90 ? 419 TYR A O     1 
ATOM   2082 C CB    . TYR A 1 278 ? -29.812 56.531 -5.451  1.00 21.45 ? 419 TYR A CB    1 
ATOM   2083 C CG    . TYR A 1 278 ? -28.957 57.326 -6.400  1.00 26.45 ? 419 TYR A CG    1 
ATOM   2084 C CD1   . TYR A 1 278 ? -29.302 58.636 -6.718  1.00 26.18 ? 419 TYR A CD1   1 
ATOM   2085 C CD2   . TYR A 1 278 ? -27.746 56.836 -6.864  1.00 26.77 ? 419 TYR A CD2   1 
ATOM   2086 C CE1   . TYR A 1 278 ? -28.507 59.410 -7.546  1.00 29.49 ? 419 TYR A CE1   1 
ATOM   2087 C CE2   . TYR A 1 278 ? -26.935 57.608 -7.703  1.00 22.62 ? 419 TYR A CE2   1 
ATOM   2088 C CZ    . TYR A 1 278 ? -27.321 58.894 -8.028  1.00 26.82 ? 419 TYR A CZ    1 
ATOM   2089 O OH    . TYR A 1 278 ? -26.531 59.694 -8.839  1.00 29.25 ? 419 TYR A OH    1 
ATOM   2090 N N     . GLN A 1 279 ? -32.143 56.769 -3.254  1.00 18.45 ? 420 GLN A N     1 
ATOM   2091 C CA    . GLN A 1 279 ? -33.068 56.018 -2.422  1.00 24.31 ? 420 GLN A CA    1 
ATOM   2092 C C     . GLN A 1 279 ? -33.232 54.599 -2.951  1.00 22.10 ? 420 GLN A C     1 
ATOM   2093 O O     . GLN A 1 279 ? -32.819 54.267 -4.065  1.00 20.78 ? 420 GLN A O     1 
ATOM   2094 C CB    . GLN A 1 279 ? -34.427 56.719 -2.370  1.00 26.43 ? 420 GLN A CB    1 
ATOM   2095 C CG    . GLN A 1 279 ? -34.401 57.955 -1.501  1.00 29.03 ? 420 GLN A CG    1 
ATOM   2096 C CD    . GLN A 1 279 ? -35.764 58.368 -1.030  1.00 34.27 ? 420 GLN A CD    1 
ATOM   2097 O OE1   . GLN A 1 279 ? -36.575 57.534 -0.616  1.00 39.72 ? 420 GLN A OE1   1 
ATOM   2098 N NE2   . GLN A 1 279 ? -36.040 59.662 -1.102  1.00 34.42 ? 420 GLN A NE2   1 
ATOM   2099 N N     . GLY A 1 280 ? -33.857 53.756 -2.133  1.00 20.25 ? 421 GLY A N     1 
ATOM   2100 C CA    . GLY A 1 280 ? -34.304 52.462 -2.587  1.00 21.96 ? 421 GLY A CA    1 
ATOM   2101 C C     . GLY A 1 280 ? -35.584 52.564 -3.398  1.00 23.11 ? 421 GLY A C     1 
ATOM   2102 O O     . GLY A 1 280 ? -36.168 53.642 -3.587  1.00 17.47 ? 421 GLY A O     1 
ATOM   2103 N N     . PRO A 1 281 ? -36.040 51.419 -3.896  1.00 22.76 ? 422 PRO A N     1 
ATOM   2104 C CA    . PRO A 1 281 ? -37.270 51.396 -4.700  1.00 21.17 ? 422 PRO A CA    1 
ATOM   2105 C C     . PRO A 1 281 ? -38.504 51.580 -3.831  1.00 21.63 ? 422 PRO A C     1 
ATOM   2106 O O     . PRO A 1 281 ? -38.502 51.254 -2.635  1.00 21.14 ? 422 PRO A O     1 
ATOM   2107 C CB    . PRO A 1 281 ? -37.241 50.005 -5.353  1.00 23.56 ? 422 PRO A CB    1 
ATOM   2108 C CG    . PRO A 1 281 ? -36.407 49.174 -4.427  1.00 28.73 ? 422 PRO A CG    1 
ATOM   2109 C CD    . PRO A 1 281 ? -35.414 50.090 -3.767  1.00 24.70 ? 422 PRO A CD    1 
ATOM   2110 N N     . PRO A 1 282 ? -39.593 52.093 -4.400  1.00 21.79 ? 423 PRO A N     1 
ATOM   2111 C CA    . PRO A 1 282 ? -39.763 52.469 -5.810  1.00 19.30 ? 423 PRO A CA    1 
ATOM   2112 C C     . PRO A 1 282 ? -39.130 53.823 -6.151  1.00 20.16 ? 423 PRO A C     1 
ATOM   2113 O O     . PRO A 1 282 ? -38.877 54.079 -7.318  1.00 17.79 ? 423 PRO A O     1 
ATOM   2114 C CB    . PRO A 1 282 ? -41.292 52.492 -5.963  1.00 20.28 ? 423 PRO A CB    1 
ATOM   2115 C CG    . PRO A 1 282 ? -41.772 52.973 -4.612  1.00 22.46 ? 423 PRO A CG    1 
ATOM   2116 C CD    . PRO A 1 282 ? -40.824 52.323 -3.616  1.00 20.83 ? 423 PRO A CD    1 
ATOM   2117 N N     . ASN A 1 283 ? -38.874 54.691 -5.160  1.00 15.36 ? 424 ASN A N     1 
ATOM   2118 C CA    . ASN A 1 283 ? -38.355 56.030 -5.423  1.00 16.74 ? 424 ASN A CA    1 
ATOM   2119 C C     . ASN A 1 283 ? -37.135 56.009 -6.340  1.00 18.40 ? 424 ASN A C     1 
ATOM   2120 O O     . ASN A 1 283 ? -36.970 56.903 -7.173  1.00 14.85 ? 424 ASN A O     1 
ATOM   2121 C CB    . ASN A 1 283 ? -37.983 56.719 -4.106  1.00 21.23 ? 424 ASN A CB    1 
ATOM   2122 C CG    . ASN A 1 283 ? -39.146 56.796 -3.142  1.00 25.16 ? 424 ASN A CG    1 
ATOM   2123 O OD1   . ASN A 1 283 ? -39.740 55.782 -2.787  1.00 22.40 ? 424 ASN A OD1   1 
ATOM   2124 N ND2   . ASN A 1 283 ? -39.491 58.003 -2.736  1.00 27.63 ? 424 ASN A ND2   1 
ATOM   2125 N N     . LYS A 1 284 ? -36.268 55.004 -6.178  1.00 17.49 ? 425 LYS A N     1 
ATOM   2126 C CA    . LYS A 1 284 ? -35.034 54.873 -6.952  1.00 16.67 ? 425 LYS A CA    1 
ATOM   2127 C C     . LYS A 1 284 ? -35.259 55.063 -8.445  1.00 20.23 ? 425 LYS A C     1 
ATOM   2128 O O     . LYS A 1 284 ? -34.388 55.590 -9.150  1.00 15.33 ? 425 LYS A O     1 
ATOM   2129 C CB    . LYS A 1 284 ? -34.436 53.492 -6.692  1.00 17.96 ? 425 LYS A CB    1 
ATOM   2130 C CG    . LYS A 1 284 ? -33.207 53.111 -7.533  1.00 21.47 ? 425 LYS A CG    1 
ATOM   2131 C CD    . LYS A 1 284 ? -32.804 51.677 -7.170  1.00 22.74 ? 425 LYS A CD    1 
ATOM   2132 C CE    . LYS A 1 284 ? -31.442 51.263 -7.738  1.00 26.02 ? 425 LYS A CE    1 
ATOM   2133 N NZ    . LYS A 1 284 ? -31.269 49.771 -7.617  1.00 24.80 ? 425 LYS A NZ    1 
ATOM   2134 N N     . PHE A 1 285 ? -36.426 54.660 -8.943  1.00 18.21 ? 426 PHE A N     1 
ATOM   2135 C CA    . PHE A 1 285 ? -36.690 54.674 -10.375 1.00 19.54 ? 426 PHE A CA    1 
ATOM   2136 C C     . PHE A 1 285 ? -37.711 55.723 -10.780 1.00 19.01 ? 426 PHE A C     1 
ATOM   2137 O O     . PHE A 1 285 ? -38.093 55.763 -11.951 1.00 18.68 ? 426 PHE A O     1 
ATOM   2138 C CB    . PHE A 1 285 ? -37.141 53.284 -10.836 1.00 15.87 ? 426 PHE A CB    1 
ATOM   2139 C CG    . PHE A 1 285 ? -36.149 52.194 -10.510 1.00 19.50 ? 426 PHE A CG    1 
ATOM   2140 C CD1   . PHE A 1 285 ? -34.975 52.063 -11.246 1.00 19.63 ? 426 PHE A CD1   1 
ATOM   2141 C CD2   . PHE A 1 285 ? -36.380 51.314 -9.459  1.00 20.46 ? 426 PHE A CD2   1 
ATOM   2142 C CE1   . PHE A 1 285 ? -34.056 51.061 -10.945 1.00 19.19 ? 426 PHE A CE1   1 
ATOM   2143 C CE2   . PHE A 1 285 ? -35.461 50.320 -9.143  1.00 21.75 ? 426 PHE A CE2   1 
ATOM   2144 C CZ    . PHE A 1 285 ? -34.302 50.193 -9.893  1.00 21.90 ? 426 PHE A CZ    1 
ATOM   2145 N N     . GLU A 1 286 ? -38.152 56.585 -9.861  1.00 16.25 ? 427 GLU A N     1 
ATOM   2146 C CA    . GLU A 1 286 ? -39.182 57.570 -10.185 1.00 17.49 ? 427 GLU A CA    1 
ATOM   2147 C C     . GLU A 1 286 ? -38.581 58.957 -9.979  1.00 19.83 ? 427 GLU A C     1 
ATOM   2148 O O     . GLU A 1 286 ? -38.523 59.472 -8.855  1.00 19.09 ? 427 GLU A O     1 
ATOM   2149 C CB    . GLU A 1 286 ? -40.453 57.362 -9.351  1.00 15.36 ? 427 GLU A CB    1 
ATOM   2150 C CG    . GLU A 1 286 ? -41.012 55.938 -9.516  1.00 18.13 ? 427 GLU A CG    1 
ATOM   2151 C CD    . GLU A 1 286 ? -42.276 55.647 -8.710  1.00 22.65 ? 427 GLU A CD    1 
ATOM   2152 O OE1   . GLU A 1 286 ? -42.579 56.378 -7.733  1.00 21.62 ? 427 GLU A OE1   1 
ATOM   2153 O OE2   . GLU A 1 286 ? -42.945 54.634 -9.033  1.00 20.44 ? 427 GLU A OE2   1 
ATOM   2154 N N     . ALA A 1 287 ? -38.143 59.575 -11.066 1.00 17.22 ? 428 ALA A N     1 
ATOM   2155 C CA    . ALA A 1 287 ? -37.434 60.841 -10.980 1.00 17.70 ? 428 ALA A CA    1 
ATOM   2156 C C     . ALA A 1 287 ? -38.398 61.981 -11.294 1.00 18.80 ? 428 ALA A C     1 
ATOM   2157 O O     . ALA A 1 287 ? -39.129 61.929 -12.290 1.00 16.24 ? 428 ALA A O     1 
ATOM   2158 C CB    . ALA A 1 287 ? -36.235 60.843 -11.926 1.00 13.47 ? 428 ALA A CB    1 
ATOM   2159 N N     . GLY A 1 288 ? -38.407 62.998 -10.435 1.00 16.44 ? 429 GLY A N     1 
ATOM   2160 C CA    . GLY A 1 288 ? -39.271 64.143 -10.630 1.00 19.81 ? 429 GLY A CA    1 
ATOM   2161 C C     . GLY A 1 288 ? -40.688 63.895 -10.142 1.00 23.02 ? 429 GLY A C     1 
ATOM   2162 O O     . GLY A 1 288 ? -41.039 62.830 -9.635  1.00 19.02 ? 429 GLY A O     1 
ATOM   2163 N N     . THR A 1 289 ? -41.514 64.923 -10.290 1.00 20.16 ? 430 THR A N     1 
ATOM   2164 C CA    . THR A 1 289 ? -42.921 64.809 -9.928  1.00 21.63 ? 430 THR A CA    1 
ATOM   2165 C C     . THR A 1 289 ? -43.569 63.680 -10.717 1.00 22.45 ? 430 THR A C     1 
ATOM   2166 O O     . THR A 1 289 ? -43.519 63.668 -11.952 1.00 20.01 ? 430 THR A O     1 
ATOM   2167 C CB    . THR A 1 289 ? -43.628 66.131 -10.215 1.00 21.80 ? 430 THR A CB    1 
ATOM   2168 O OG1   . THR A 1 289 ? -42.995 67.172 -9.458  1.00 21.47 ? 430 THR A OG1   1 
ATOM   2169 C CG2   . THR A 1 289 ? -45.112 66.051 -9.865  1.00 22.55 ? 430 THR A CG2   1 
ATOM   2170 N N     . GLY A 1 290 ? -44.182 62.742 -10.009 1.00 21.08 ? 431 GLY A N     1 
ATOM   2171 C CA    . GLY A 1 290 ? -44.901 61.673 -10.669 1.00 21.80 ? 431 GLY A CA    1 
ATOM   2172 C C     . GLY A 1 290 ? -46.177 62.170 -11.326 1.00 21.04 ? 431 GLY A C     1 
ATOM   2173 O O     . GLY A 1 290 ? -46.671 63.275 -11.074 1.00 18.77 ? 431 GLY A O     1 
ATOM   2174 N N     . ASN A 1 291 ? -46.726 61.323 -12.196 1.00 17.00 ? 432 ASN A N     1 
ATOM   2175 C CA    . ASN A 1 291 ? -48.019 61.604 -12.813 1.00 17.54 ? 432 ASN A CA    1 
ATOM   2176 C C     . ASN A 1 291 ? -49.093 61.173 -11.819 1.00 17.13 ? 432 ASN A C     1 
ATOM   2177 O O     . ASN A 1 291 ? -49.732 60.128 -11.954 1.00 15.91 ? 432 ASN A O     1 
ATOM   2178 C CB    . ASN A 1 291 ? -48.151 60.889 -14.147 1.00 15.78 ? 432 ASN A CB    1 
ATOM   2179 C CG    . ASN A 1 291 ? -49.449 61.222 -14.850 1.00 19.26 ? 432 ASN A CG    1 
ATOM   2180 O OD1   . ASN A 1 291 ? -50.309 61.912 -14.284 1.00 18.16 ? 432 ASN A OD1   1 
ATOM   2181 N ND2   . ASN A 1 291 ? -49.591 60.769 -16.106 1.00 19.04 ? 432 ASN A ND2   1 
ATOM   2182 N N     . ILE A 1 292 ? -49.301 62.015 -10.801 1.00 17.16 ? 433 ILE A N     1 
ATOM   2183 C CA    . ILE A 1 292 ? -50.110 61.600 -9.654  1.00 17.20 ? 433 ILE A CA    1 
ATOM   2184 C C     . ILE A 1 292 ? -51.563 61.376 -10.069 1.00 18.78 ? 433 ILE A C     1 
ATOM   2185 O O     . ILE A 1 292 ? -52.158 60.331 -9.755  1.00 17.06 ? 433 ILE A O     1 
ATOM   2186 C CB    . ILE A 1 292 ? -49.980 62.621 -8.509  1.00 17.06 ? 433 ILE A CB    1 
ATOM   2187 C CG1   . ILE A 1 292 ? -48.526 62.677 -8.025  1.00 23.27 ? 433 ILE A CG1   1 
ATOM   2188 C CG2   . ILE A 1 292 ? -50.834 62.222 -7.318  1.00 16.51 ? 433 ILE A CG2   1 
ATOM   2189 C CD1   . ILE A 1 292 ? -48.112 64.051 -7.527  1.00 30.21 ? 433 ILE A CD1   1 
ATOM   2190 N N     . ALA A 1 293 ? -52.149 62.338 -10.800 1.00 17.48 ? 434 ALA A N     1 
ATOM   2191 C CA    . ALA A 1 293 ? -53.568 62.231 -11.143 1.00 17.37 ? 434 ALA A CA    1 
ATOM   2192 C C     . ALA A 1 293 ? -53.849 60.978 -11.956 1.00 14.76 ? 434 ALA A C     1 
ATOM   2193 O O     . ALA A 1 293 ? -54.841 60.284 -11.716 1.00 15.12 ? 434 ALA A O     1 
ATOM   2194 C CB    . ALA A 1 293 ? -54.038 63.467 -11.919 1.00 15.57 ? 434 ALA A CB    1 
ATOM   2195 N N     . ASP A 1 294 ? -52.994 60.659 -12.925 1.00 16.84 ? 435 ASP A N     1 
ATOM   2196 C CA    . ASP A 1 294 ? -53.351 59.528 -13.774 1.00 16.49 ? 435 ASP A CA    1 
ATOM   2197 C C     . ASP A 1 294 ? -53.084 58.199 -13.096 1.00 14.78 ? 435 ASP A C     1 
ATOM   2198 O O     . ASP A 1 294 ? -53.773 57.225 -13.392 1.00 14.10 ? 435 ASP A O     1 
ATOM   2199 C CB    . ASP A 1 294 ? -52.613 59.585 -15.102 1.00 14.52 ? 435 ASP A CB    1 
ATOM   2200 C CG    . ASP A 1 294 ? -53.027 60.779 -15.929 1.00 24.40 ? 435 ASP A CG    1 
ATOM   2201 O OD1   . ASP A 1 294 ? -54.205 61.235 -15.811 1.00 20.62 ? 435 ASP A OD1   1 
ATOM   2202 O OD2   . ASP A 1 294 ? -52.139 61.318 -16.621 1.00 23.47 ? 435 ASP A OD2   1 
ATOM   2203 N N     . ALA A 1 295 ? -52.101 58.127 -12.193 1.00 13.10 ? 436 ALA A N     1 
ATOM   2204 C CA    . ALA A 1 295 ? -51.981 56.936 -11.354 1.00 15.43 ? 436 ALA A CA    1 
ATOM   2205 C C     . ALA A 1 295 ? -53.247 56.726 -10.530 1.00 13.04 ? 436 ALA A C     1 
ATOM   2206 O O     . ALA A 1 295 ? -53.750 55.597 -10.410 1.00 15.14 ? 436 ALA A O     1 
ATOM   2207 C CB    . ALA A 1 295 ? -50.759 57.051 -10.434 1.00 14.39 ? 436 ALA A CB    1 
ATOM   2208 N N     . VAL A 1 296 ? -53.776 57.806 -9.945  1.00 14.94 ? 437 VAL A N     1 
ATOM   2209 C CA    . VAL A 1 296 ? -55.023 57.697 -9.184  1.00 14.18 ? 437 VAL A CA    1 
ATOM   2210 C C     . VAL A 1 296 ? -56.173 57.237 -10.091 1.00 16.10 ? 437 VAL A C     1 
ATOM   2211 O O     . VAL A 1 296 ? -56.997 56.383 -9.715  1.00 17.49 ? 437 VAL A O     1 
ATOM   2212 C CB    . VAL A 1 296 ? -55.321 59.045 -8.499  1.00 15.69 ? 437 VAL A CB    1 
ATOM   2213 C CG1   . VAL A 1 296 ? -56.727 59.057 -7.905  1.00 16.40 ? 437 VAL A CG1   1 
ATOM   2214 C CG2   . VAL A 1 296 ? -54.275 59.310 -7.414  1.00 15.17 ? 437 VAL A CG2   1 
ATOM   2215 N N     . GLY A 1 297 ? -56.232 57.772 -11.311 1.00 17.14 ? 438 GLY A N     1 
ATOM   2216 C CA    . GLY A 1 297 ? -57.253 57.327 -12.260 1.00 15.65 ? 438 GLY A CA    1 
ATOM   2217 C C     . GLY A 1 297 ? -57.080 55.870 -12.660 1.00 16.88 ? 438 GLY A C     1 
ATOM   2218 O O     . GLY A 1 297 ? -58.061 55.134 -12.819 1.00 17.52 ? 438 GLY A O     1 
ATOM   2219 N N     . LEU A 1 298 ? -55.831 55.425 -12.806 1.00 14.38 ? 439 LEU A N     1 
ATOM   2220 C CA    . LEU A 1 298 ? -55.566 54.014 -13.083 1.00 14.15 ? 439 LEU A CA    1 
ATOM   2221 C C     . LEU A 1 298 ? -56.040 53.130 -11.942 1.00 15.71 ? 439 LEU A C     1 
ATOM   2222 O O     . LEU A 1 298 ? -56.563 52.034 -12.175 1.00 16.01 ? 439 LEU A O     1 
ATOM   2223 C CB    . LEU A 1 298 ? -54.080 53.788 -13.329 1.00 12.94 ? 439 LEU A CB    1 
ATOM   2224 C CG    . LEU A 1 298 ? -53.659 52.322 -13.503 1.00 15.61 ? 439 LEU A CG    1 
ATOM   2225 C CD1   . LEU A 1 298 ? -54.471 51.655 -14.630 1.00 11.56 ? 439 LEU A CD1   1 
ATOM   2226 C CD2   . LEU A 1 298 ? -52.133 52.230 -13.766 1.00 14.92 ? 439 LEU A CD2   1 
ATOM   2227 N N     . GLY A 1 299 ? -55.828 53.570 -10.699 1.00 16.65 ? 440 GLY A N     1 
ATOM   2228 C CA    . GLY A 1 299 ? -56.381 52.834 -9.565  1.00 16.59 ? 440 GLY A CA    1 
ATOM   2229 C C     . GLY A 1 299 ? -57.891 52.698 -9.656  1.00 18.13 ? 440 GLY A C     1 
ATOM   2230 O O     . GLY A 1 299 ? -58.458 51.631 -9.378  1.00 19.44 ? 440 GLY A O     1 
ATOM   2231 N N     . GLU A 1 300 ? -58.567 53.777 -10.046 1.00 15.06 ? 441 GLU A N     1 
ATOM   2232 C CA    . GLU A 1 300 ? -60.011 53.669 -10.249 1.00 18.82 ? 441 GLU A CA    1 
ATOM   2233 C C     . GLU A 1 300 ? -60.346 52.669 -11.363 1.00 19.06 ? 441 GLU A C     1 
ATOM   2234 O O     . GLU A 1 300 ? -61.301 51.892 -11.246 1.00 16.96 ? 441 GLU A O     1 
ATOM   2235 C CB    . GLU A 1 300 ? -60.608 55.045 -10.556 1.00 19.42 ? 441 GLU A CB    1 
ATOM   2236 C CG    . GLU A 1 300 ? -62.145 55.129 -10.498 1.00 18.29 ? 441 GLU A CG    1 
ATOM   2237 C CD    . GLU A 1 300 ? -62.741 54.750 -9.130  1.00 25.59 ? 441 GLU A CD    1 
ATOM   2238 O OE1   . GLU A 1 300 ? -62.150 55.100 -8.086  1.00 30.98 ? 441 GLU A OE1   1 
ATOM   2239 O OE2   . GLU A 1 300 ? -63.825 54.121 -9.099  1.00 27.59 ? 441 GLU A OE2   1 
ATOM   2240 N N     . ALA A 1 301 ? -59.580 52.681 -12.456 1.00 15.17 ? 442 ALA A N     1 
ATOM   2241 C CA    . ALA A 1 301 ? -59.833 51.735 -13.550 1.00 16.88 ? 442 ALA A CA    1 
ATOM   2242 C C     . ALA A 1 301 ? -59.650 50.289 -13.088 1.00 18.57 ? 442 ALA A C     1 
ATOM   2243 O O     . ALA A 1 301 ? -60.420 49.392 -13.470 1.00 16.10 ? 442 ALA A O     1 
ATOM   2244 C CB    . ALA A 1 301 ? -58.906 52.037 -14.735 1.00 13.53 ? 442 ALA A CB    1 
ATOM   2245 N N     . ILE A 1 302 ? -58.634 50.049 -12.259 1.00 15.80 ? 443 ILE A N     1 
ATOM   2246 C CA    . ILE A 1 302 ? -58.407 48.713 -11.722 1.00 17.24 ? 443 ILE A CA    1 
ATOM   2247 C C     . ILE A 1 302 ? -59.578 48.285 -10.846 1.00 19.06 ? 443 ILE A C     1 
ATOM   2248 O O     . ILE A 1 302 ? -60.056 47.151 -10.941 1.00 19.30 ? 443 ILE A O     1 
ATOM   2249 C CB    . ILE A 1 302 ? -57.072 48.666 -10.961 1.00 18.00 ? 443 ILE A CB    1 
ATOM   2250 C CG1   . ILE A 1 302 ? -55.917 48.598 -11.960 1.00 15.69 ? 443 ILE A CG1   1 
ATOM   2251 C CG2   . ILE A 1 302 ? -57.033 47.457 -9.995  1.00 18.46 ? 443 ILE A CG2   1 
ATOM   2252 C CD1   . ILE A 1 302 ? -54.565 48.758 -11.303 1.00 21.22 ? 443 ILE A CD1   1 
ATOM   2253 N N     . ARG A 1 303 ? -60.067 49.184 -9.990  1.00 20.23 ? 444 ARG A N     1 
ATOM   2254 C CA    . ARG A 1 303 ? -61.231 48.842 -9.175  1.00 22.67 ? 444 ARG A CA    1 
ATOM   2255 C C     . ARG A 1 303 ? -62.457 48.554 -10.042 1.00 23.26 ? 444 ARG A C     1 
ATOM   2256 O O     . ARG A 1 303 ? -63.254 47.663 -9.725  1.00 20.36 ? 444 ARG A O     1 
ATOM   2257 C CB    . ARG A 1 303 ? -61.533 49.965 -8.185  1.00 22.48 ? 444 ARG A CB    1 
ATOM   2258 C CG    . ARG A 1 303 ? -60.575 49.970 -6.987  1.00 25.76 ? 444 ARG A CG    1 
ATOM   2259 C CD    . ARG A 1 303 ? -61.047 50.942 -5.911  1.00 29.01 ? 444 ARG A CD    1 
ATOM   2260 N NE    . ARG A 1 303 ? -60.939 52.324 -6.364  1.00 27.78 ? 444 ARG A NE    1 
ATOM   2261 C CZ    . ARG A 1 303 ? -59.800 53.004 -6.437  1.00 28.68 ? 444 ARG A CZ    1 
ATOM   2262 N NH1   . ARG A 1 303 ? -58.650 52.475 -6.038  1.00 24.34 ? 444 ARG A NH1   1 
ATOM   2263 N NH2   . ARG A 1 303 ? -59.817 54.245 -6.922  1.00 25.38 ? 444 ARG A NH2   1 
ATOM   2264 N N     . TYR A 1 304 ? -62.635 49.308 -11.132 1.00 19.25 ? 445 TYR A N     1 
ATOM   2265 C CA    . TYR A 1 304 ? -63.762 49.034 -12.026 1.00 23.57 ? 445 TYR A CA    1 
ATOM   2266 C C     . TYR A 1 304 ? -63.658 47.623 -12.601 1.00 21.43 ? 445 TYR A C     1 
ATOM   2267 O O     . TYR A 1 304 ? -64.637 46.853 -12.604 1.00 19.31 ? 445 TYR A O     1 
ATOM   2268 C CB    . TYR A 1 304 ? -63.815 50.066 -13.157 1.00 18.87 ? 445 TYR A CB    1 
ATOM   2269 C CG    . TYR A 1 304 ? -65.019 49.860 -14.050 1.00 21.16 ? 445 TYR A CG    1 
ATOM   2270 C CD1   . TYR A 1 304 ? -64.960 49.019 -15.156 1.00 19.45 ? 445 TYR A CD1   1 
ATOM   2271 C CD2   . TYR A 1 304 ? -66.221 50.498 -13.774 1.00 19.49 ? 445 TYR A CD2   1 
ATOM   2272 C CE1   . TYR A 1 304 ? -66.076 48.812 -15.963 1.00 22.84 ? 445 TYR A CE1   1 
ATOM   2273 C CE2   . TYR A 1 304 ? -67.338 50.304 -14.571 1.00 21.53 ? 445 TYR A CE2   1 
ATOM   2274 C CZ    . TYR A 1 304 ? -67.262 49.458 -15.660 1.00 21.71 ? 445 TYR A CZ    1 
ATOM   2275 O OH    . TYR A 1 304 ? -68.378 49.264 -16.445 1.00 23.04 ? 445 TYR A OH    1 
ATOM   2276 N N     . VAL A 1 305 ? -62.462 47.268 -13.084 1.00 20.63 ? 446 VAL A N     1 
ATOM   2277 C CA    . VAL A 1 305 ? -62.247 45.946 -13.669 1.00 19.37 ? 446 VAL A CA    1 
ATOM   2278 C C     . VAL A 1 305 ? -62.465 44.861 -12.623 1.00 22.36 ? 446 VAL A C     1 
ATOM   2279 O O     . VAL A 1 305 ? -63.022 43.800 -12.926 1.00 20.42 ? 446 VAL A O     1 
ATOM   2280 C CB    . VAL A 1 305 ? -60.844 45.855 -14.301 1.00 19.03 ? 446 VAL A CB    1 
ATOM   2281 C CG1   . VAL A 1 305 ? -60.451 44.392 -14.561 1.00 19.11 ? 446 VAL A CG1   1 
ATOM   2282 C CG2   . VAL A 1 305 ? -60.781 46.666 -15.598 1.00 20.35 ? 446 VAL A CG2   1 
ATOM   2283 N N     . GLU A 1 306 ? -62.038 45.108 -11.373 1.00 22.68 ? 447 GLU A N     1 
ATOM   2284 C CA    . GLU A 1 306 ? -62.254 44.121 -10.315 1.00 22.25 ? 447 GLU A CA    1 
ATOM   2285 C C     . GLU A 1 306 ? -63.733 43.958 -9.998  1.00 25.01 ? 447 GLU A C     1 
ATOM   2286 O O     . GLU A 1 306 ? -64.184 42.846 -9.708  1.00 26.38 ? 447 GLU A O     1 
ATOM   2287 C CB    . GLU A 1 306 ? -61.497 44.485 -9.031  1.00 22.87 ? 447 GLU A CB    1 
ATOM   2288 C CG    . GLU A 1 306 ? -59.983 44.468 -9.161  1.00 24.71 ? 447 GLU A CG    1 
ATOM   2289 C CD    . GLU A 1 306 ? -59.261 45.009 -7.926  1.00 31.66 ? 447 GLU A CD    1 
ATOM   2290 O OE1   . GLU A 1 306 ? -59.594 46.121 -7.431  1.00 28.19 ? 447 GLU A OE1   1 
ATOM   2291 O OE2   . GLU A 1 306 ? -58.319 44.316 -7.472  1.00 33.85 ? 447 GLU A OE2   1 
ATOM   2292 N N     . ARG A 1 307 ? -64.496 45.056 -10.013 1.00 23.64 ? 448 ARG A N     1 
ATOM   2293 C CA    . ARG A 1 307 ? -65.935 44.958 -9.781  1.00 23.69 ? 448 ARG A CA    1 
ATOM   2294 C C     . ARG A 1 307 ? -66.594 44.088 -10.840 1.00 24.41 ? 448 ARG A C     1 
ATOM   2295 O O     . ARG A 1 307 ? -67.438 43.242 -10.525 1.00 30.22 ? 448 ARG A O     1 
ATOM   2296 C CB    . ARG A 1 307 ? -66.595 46.341 -9.785  1.00 28.31 ? 448 ARG A CB    1 
ATOM   2297 C CG    . ARG A 1 307 ? -66.306 47.256 -8.599  1.00 37.87 ? 448 ARG A CG    1 
ATOM   2298 C CD    . ARG A 1 307 ? -66.937 48.669 -8.833  1.00 44.61 ? 448 ARG A CD    1 
ATOM   2299 N NE    . ARG A 1 307 ? -65.940 49.727 -9.030  1.00 38.62 ? 448 ARG A NE    1 
ATOM   2300 C CZ    . ARG A 1 307 ? -66.172 50.875 -9.663  1.00 38.30 ? 448 ARG A CZ    1 
ATOM   2301 N NH1   . ARG A 1 307 ? -67.373 51.176 -10.134 1.00 40.32 ? 448 ARG A NH1   1 
ATOM   2302 N NH2   . ARG A 1 307 ? -65.164 51.731 -9.854  1.00 39.34 ? 448 ARG A NH2   1 
ATOM   2303 N N     . VAL A 1 308 ? -66.248 44.311 -12.111 1.00 21.98 ? 449 VAL A N     1 
ATOM   2304 C CA    . VAL A 1 308 ? -66.810 43.474 -13.171 1.00 22.71 ? 449 VAL A CA    1 
ATOM   2305 C C     . VAL A 1 308 ? -66.287 42.046 -13.053 1.00 27.54 ? 449 VAL A C     1 
ATOM   2306 O O     . VAL A 1 308 ? -67.052 41.084 -13.184 1.00 25.77 ? 449 VAL A O     1 
ATOM   2307 C CB    . VAL A 1 308 ? -66.499 44.072 -14.555 1.00 25.60 ? 449 VAL A CB    1 
ATOM   2308 C CG1   . VAL A 1 308 ? -66.935 43.121 -15.661 1.00 22.10 ? 449 VAL A CG1   1 
ATOM   2309 C CG2   . VAL A 1 308 ? -67.180 45.425 -14.712 1.00 24.62 ? 449 VAL A CG2   1 
ATOM   2310 N N     . GLY A 1 309 ? -64.981 41.885 -12.799 1.00 21.53 ? 450 GLY A N     1 
ATOM   2311 C CA    . GLY A 1 309 ? -64.382 40.573 -12.617 1.00 24.71 ? 450 GLY A CA    1 
ATOM   2312 C C     . GLY A 1 309 ? -63.566 40.120 -13.812 1.00 22.15 ? 450 GLY A C     1 
ATOM   2313 O O     . GLY A 1 309 ? -64.117 39.914 -14.897 1.00 21.51 ? 450 GLY A O     1 
ATOM   2314 N N     . ILE A 1 310 ? -62.253 39.952 -13.627 1.00 21.25 ? 451 ILE A N     1 
ATOM   2315 C CA    . ILE A 1 310 ? -61.365 39.731 -14.766 1.00 23.19 ? 451 ILE A CA    1 
ATOM   2316 C C     . ILE A 1 310 ? -61.641 38.379 -15.419 1.00 23.62 ? 451 ILE A C     1 
ATOM   2317 O O     . ILE A 1 310 ? -61.542 38.256 -16.645 1.00 22.51 ? 451 ILE A O     1 
ATOM   2318 C CB    . ILE A 1 310 ? -59.880 39.879 -14.357 1.00 23.71 ? 451 ILE A CB    1 
ATOM   2319 C CG1   . ILE A 1 310 ? -58.960 39.780 -15.584 1.00 21.04 ? 451 ILE A CG1   1 
ATOM   2320 C CG2   . ILE A 1 310 ? -59.483 38.815 -13.334 1.00 22.34 ? 451 ILE A CG2   1 
ATOM   2321 C CD1   . ILE A 1 310 ? -59.201 40.856 -16.662 1.00 21.38 ? 451 ILE A CD1   1 
ATOM   2322 N N     . GLU A 1 311 ? -62.020 37.359 -14.637 1.00 22.72 ? 452 GLU A N     1 
ATOM   2323 C CA    . GLU A 1 311 ? -62.349 36.062 -15.228 1.00 28.41 ? 452 GLU A CA    1 
ATOM   2324 C C     . GLU A 1 311 ? -63.658 36.109 -16.005 1.00 23.39 ? 452 GLU A C     1 
ATOM   2325 O O     . GLU A 1 311 ? -63.790 35.434 -17.033 1.00 24.61 ? 452 GLU A O     1 
ATOM   2326 C CB    . GLU A 1 311 ? -62.423 34.985 -14.143 1.00 27.95 ? 452 GLU A CB    1 
ATOM   2327 C CG    . GLU A 1 311 ? -61.072 34.781 -13.474 1.00 29.92 ? 452 GLU A CG    1 
ATOM   2328 C CD    . GLU A 1 311 ? -60.964 35.559 -12.161 1.00 45.22 ? 452 GLU A CD    1 
ATOM   2329 O OE1   . GLU A 1 311 ? -61.674 36.602 -11.998 1.00 38.20 ? 452 GLU A OE1   1 
ATOM   2330 O OE2   . GLU A 1 311 ? -60.128 35.157 -11.318 1.00 50.21 ? 452 GLU A OE2   1 
ATOM   2331 N N     . ARG A 1 312 ? -64.622 36.914 -15.548 1.00 22.71 ? 453 ARG A N     1 
ATOM   2332 C CA    . ARG A 1 312 ? -65.860 37.085 -16.301 1.00 22.90 ? 453 ARG A CA    1 
ATOM   2333 C C     . ARG A 1 312 ? -65.611 37.861 -17.584 1.00 23.23 ? 453 ARG A C     1 
ATOM   2334 O O     . ARG A 1 312 ? -66.186 37.535 -18.635 1.00 19.99 ? 453 ARG A O     1 
ATOM   2335 C CB    . ARG A 1 312 ? -66.904 37.789 -15.436 1.00 21.18 ? 453 ARG A CB    1 
ATOM   2336 C CG    . ARG A 1 312 ? -67.313 36.964 -14.212 1.00 21.31 ? 453 ARG A CG    1 
ATOM   2337 C CD    . ARG A 1 312 ? -68.692 37.357 -13.724 1.00 26.88 ? 453 ARG A CD    1 
ATOM   2338 N NE    . ARG A 1 312 ? -68.736 38.761 -13.330 1.00 30.04 ? 453 ARG A NE    1 
ATOM   2339 C CZ    . ARG A 1 312 ? -69.657 39.286 -12.531 1.00 40.25 ? 453 ARG A CZ    1 
ATOM   2340 N NH1   . ARG A 1 312 ? -70.650 38.556 -12.043 1.00 34.45 ? 453 ARG A NH1   1 
ATOM   2341 N NH2   . ARG A 1 312 ? -69.582 40.577 -12.216 1.00 38.10 ? 453 ARG A NH2   1 
ATOM   2342 N N     . ILE A 1 313 ? -64.769 38.900 -17.507 1.00 21.80 ? 454 ILE A N     1 
ATOM   2343 C CA    . ILE A 1 313 ? -64.336 39.625 -18.700 1.00 20.53 ? 454 ILE A CA    1 
ATOM   2344 C C     . ILE A 1 313 ? -63.679 38.670 -19.686 1.00 20.92 ? 454 ILE A C     1 
ATOM   2345 O O     . ILE A 1 313 ? -63.961 38.701 -20.887 1.00 21.71 ? 454 ILE A O     1 
ATOM   2346 C CB    . ILE A 1 313 ? -63.381 40.773 -18.314 1.00 23.01 ? 454 ILE A CB    1 
ATOM   2347 C CG1   . ILE A 1 313 ? -64.166 41.966 -17.748 1.00 20.89 ? 454 ILE A CG1   1 
ATOM   2348 C CG2   . ILE A 1 313 ? -62.492 41.196 -19.521 1.00 18.88 ? 454 ILE A CG2   1 
ATOM   2349 C CD1   . ILE A 1 313 ? -63.337 42.871 -16.802 1.00 20.96 ? 454 ILE A CD1   1 
ATOM   2350 N N     . ALA A 1 314 ? -62.776 37.814 -19.189 1.00 20.65 ? 455 ALA A N     1 
ATOM   2351 C CA    . ALA A 1 314 ? -62.062 36.897 -20.066 1.00 22.01 ? 455 ALA A CA    1 
ATOM   2352 C C     . ALA A 1 314 ? -63.019 35.926 -20.758 1.00 21.35 ? 455 ALA A C     1 
ATOM   2353 O O     . ALA A 1 314 ? -62.909 35.691 -21.972 1.00 20.54 ? 455 ALA A O     1 
ATOM   2354 C CB    . ALA A 1 314 ? -60.995 36.145 -19.263 1.00 20.32 ? 455 ALA A CB    1 
ATOM   2355 N N     . ALA A 1 315 ? -63.992 35.379 -20.014 1.00 22.77 ? 456 ALA A N     1 
ATOM   2356 C CA    . ALA A 1 315 ? -64.929 34.437 -20.626 1.00 21.81 ? 456 ALA A CA    1 
ATOM   2357 C C     . ALA A 1 315 ? -65.853 35.131 -21.630 1.00 21.89 ? 456 ALA A C     1 
ATOM   2358 O O     . ALA A 1 315 ? -66.145 34.580 -22.705 1.00 23.52 ? 456 ALA A O     1 
ATOM   2359 C CB    . ALA A 1 315 ? -65.741 33.723 -19.538 1.00 21.63 ? 456 ALA A CB    1 
ATOM   2360 N N     . TYR A 1 316 ? -66.328 36.340 -21.306 1.00 20.13 ? 457 TYR A N     1 
ATOM   2361 C CA    . TYR A 1 316 ? -67.194 37.051 -22.241 1.00 21.36 ? 457 TYR A CA    1 
ATOM   2362 C C     . TYR A 1 316 ? -66.445 37.409 -23.525 1.00 21.46 ? 457 TYR A C     1 
ATOM   2363 O O     . TYR A 1 316 ? -66.954 37.208 -24.641 1.00 20.81 ? 457 TYR A O     1 
ATOM   2364 C CB    . TYR A 1 316 ? -67.766 38.309 -21.585 1.00 18.42 ? 457 TYR A CB    1 
ATOM   2365 C CG    . TYR A 1 316 ? -68.675 39.092 -22.521 1.00 20.63 ? 457 TYR A CG    1 
ATOM   2366 C CD1   . TYR A 1 316 ? -69.990 38.690 -22.751 1.00 20.48 ? 457 TYR A CD1   1 
ATOM   2367 C CD2   . TYR A 1 316 ? -68.202 40.214 -23.200 1.00 21.00 ? 457 TYR A CD2   1 
ATOM   2368 C CE1   . TYR A 1 316 ? -70.813 39.406 -23.624 1.00 22.21 ? 457 TYR A CE1   1 
ATOM   2369 C CE2   . TYR A 1 316 ? -69.010 40.934 -24.065 1.00 21.14 ? 457 TYR A CE2   1 
ATOM   2370 C CZ    . TYR A 1 316 ? -70.313 40.525 -24.277 1.00 20.63 ? 457 TYR A CZ    1 
ATOM   2371 O OH    . TYR A 1 316 ? -71.108 41.243 -25.143 1.00 23.39 ? 457 TYR A OH    1 
ATOM   2372 N N     . GLU A 1 317 ? -65.234 37.950 -23.390 1.00 20.37 ? 458 GLU A N     1 
ATOM   2373 C CA    . GLU A 1 317 ? -64.469 38.313 -24.577 1.00 19.69 ? 458 GLU A CA    1 
ATOM   2374 C C     . GLU A 1 317 ? -64.140 37.078 -25.414 1.00 20.34 ? 458 GLU A C     1 
ATOM   2375 O O     . GLU A 1 317 ? -64.144 37.134 -26.651 1.00 21.05 ? 458 GLU A O     1 
ATOM   2376 C CB    . GLU A 1 317 ? -63.199 39.063 -24.172 1.00 20.25 ? 458 GLU A CB    1 
ATOM   2377 C CG    . GLU A 1 317 ? -63.412 40.550 -23.835 1.00 18.01 ? 458 GLU A CG    1 
ATOM   2378 C CD    . GLU A 1 317 ? -62.205 41.153 -23.104 1.00 22.26 ? 458 GLU A CD    1 
ATOM   2379 O OE1   . GLU A 1 317 ? -62.245 42.350 -22.728 1.00 20.36 ? 458 GLU A OE1   1 
ATOM   2380 O OE2   . GLU A 1 317 ? -61.224 40.416 -22.872 1.00 20.30 ? 458 GLU A OE2   1 
ATOM   2381 N N     . HIS A 1 318 ? -63.877 35.944 -24.757 1.00 21.51 ? 459 HIS A N     1 
ATOM   2382 C CA    . HIS A 1 318 ? -63.669 34.699 -25.490 1.00 22.82 ? 459 HIS A CA    1 
ATOM   2383 C C     . HIS A 1 318 ? -64.909 34.317 -26.294 1.00 24.77 ? 459 HIS A C     1 
ATOM   2384 O O     . HIS A 1 318 ? -64.795 33.867 -27.440 1.00 23.88 ? 459 HIS A O     1 
ATOM   2385 C CB    . HIS A 1 318 ? -63.292 33.591 -24.509 1.00 23.93 ? 459 HIS A CB    1 
ATOM   2386 C CG    . HIS A 1 318 ? -63.004 32.273 -25.154 1.00 29.10 ? 459 HIS A CG    1 
ATOM   2387 N ND1   . HIS A 1 318 ? -63.940 31.262 -25.231 1.00 31.03 ? 459 HIS A ND1   1 
ATOM   2388 C CD2   . HIS A 1 318 ? -61.879 31.788 -25.728 1.00 30.96 ? 459 HIS A CD2   1 
ATOM   2389 C CE1   . HIS A 1 318 ? -63.405 30.215 -25.832 1.00 30.01 ? 459 HIS A CE1   1 
ATOM   2390 N NE2   . HIS A 1 318 ? -62.158 30.510 -26.149 1.00 32.21 ? 459 HIS A NE2   1 
ATOM   2391 N N     . ALA A 1 319 ? -66.107 34.483 -25.710 1.00 19.59 ? 460 ALA A N     1 
ATOM   2392 C CA    . ALA A 1 319 ? -67.324 34.204 -26.476 1.00 21.43 ? 460 ALA A CA    1 
ATOM   2393 C C     . ALA A 1 319 ? -67.433 35.125 -27.693 1.00 23.17 ? 460 ALA A C     1 
ATOM   2394 O O     . ALA A 1 319 ? -67.819 34.686 -28.783 1.00 21.17 ? 460 ALA A O     1 
ATOM   2395 C CB    . ALA A 1 319 ? -68.566 34.335 -25.588 1.00 25.12 ? 460 ALA A CB    1 
ATOM   2396 N N     . LEU A 1 320 ? -67.069 36.404 -27.531 1.00 22.47 ? 461 LEU A N     1 
ATOM   2397 C CA    . LEU A 1 320 ? -67.115 37.321 -28.673 1.00 22.28 ? 461 LEU A CA    1 
ATOM   2398 C C     . LEU A 1 320 ? -66.190 36.852 -29.794 1.00 23.83 ? 461 LEU A C     1 
ATOM   2399 O O     . LEU A 1 320 ? -66.584 36.818 -30.968 1.00 21.26 ? 461 LEU A O     1 
ATOM   2400 C CB    . LEU A 1 320 ? -66.726 38.732 -28.249 1.00 23.56 ? 461 LEU A CB    1 
ATOM   2401 C CG    . LEU A 1 320 ? -67.736 39.532 -27.432 1.00 24.50 ? 461 LEU A CG    1 
ATOM   2402 C CD1   . LEU A 1 320 ? -67.051 40.830 -27.039 1.00 18.37 ? 461 LEU A CD1   1 
ATOM   2403 C CD2   . LEU A 1 320 ? -69.037 39.776 -28.214 1.00 20.50 ? 461 LEU A CD2   1 
ATOM   2404 N N     . LEU A 1 321 ? -64.949 36.487 -29.444 1.00 19.29 ? 462 LEU A N     1 
ATOM   2405 C CA    . LEU A 1 321 ? -63.980 36.077 -30.462 1.00 20.09 ? 462 LEU A CA    1 
ATOM   2406 C C     . LEU A 1 321 ? -64.383 34.764 -31.127 1.00 22.00 ? 462 LEU A C     1 
ATOM   2407 O O     . LEU A 1 321 ? -64.238 34.612 -32.350 1.00 24.00 ? 462 LEU A O     1 
ATOM   2408 C CB    . LEU A 1 321 ? -62.580 35.970 -29.847 1.00 21.03 ? 462 LEU A CB    1 
ATOM   2409 C CG    . LEU A 1 321 ? -61.375 35.714 -30.764 1.00 25.75 ? 462 LEU A CG    1 
ATOM   2410 C CD1   . LEU A 1 321 ? -61.267 36.720 -31.917 1.00 18.92 ? 462 LEU A CD1   1 
ATOM   2411 C CD2   . LEU A 1 321 ? -60.082 35.708 -29.951 1.00 27.28 ? 462 LEU A CD2   1 
ATOM   2412 N N     . GLU A 1 322 ? -64.896 33.807 -30.340 1.00 22.04 ? 463 GLU A N     1 
ATOM   2413 C CA    . GLU A 1 322 ? -65.392 32.548 -30.886 1.00 24.55 ? 463 GLU A CA    1 
ATOM   2414 C C     . GLU A 1 322 ? -66.567 32.757 -31.830 1.00 26.04 ? 463 GLU A C     1 
ATOM   2415 O O     . GLU A 1 322 ? -66.739 31.990 -32.781 1.00 27.23 ? 463 GLU A O     1 
ATOM   2416 C CB    . GLU A 1 322 ? -65.833 31.607 -29.761 1.00 28.89 ? 463 GLU A CB    1 
ATOM   2417 C CG    . GLU A 1 322 ? -64.699 31.089 -28.908 1.00 32.00 ? 463 GLU A CG    1 
ATOM   2418 C CD    . GLU A 1 322 ? -63.805 30.131 -29.663 1.00 37.70 ? 463 GLU A CD    1 
ATOM   2419 O OE1   . GLU A 1 322 ? -64.326 29.130 -30.198 1.00 45.96 ? 463 GLU A OE1   1 
ATOM   2420 O OE2   . GLU A 1 322 ? -62.586 30.387 -29.725 1.00 45.99 ? 463 GLU A OE2   1 
ATOM   2421 N N     . TYR A 1 323 ? -67.413 33.749 -31.560 1.00 24.06 ? 464 TYR A N     1 
ATOM   2422 C CA    . TYR A 1 323 ? -68.532 34.012 -32.461 1.00 23.30 ? 464 TYR A CA    1 
ATOM   2423 C C     . TYR A 1 323 ? -68.047 34.683 -33.739 1.00 25.69 ? 464 TYR A C     1 
ATOM   2424 O O     . TYR A 1 323 ? -68.408 34.272 -34.849 1.00 26.65 ? 464 TYR A O     1 
ATOM   2425 C CB    . TYR A 1 323 ? -69.552 34.884 -31.743 1.00 22.43 ? 464 TYR A CB    1 
ATOM   2426 C CG    . TYR A 1 323 ? -70.761 35.346 -32.545 1.00 24.97 ? 464 TYR A CG    1 
ATOM   2427 C CD1   . TYR A 1 323 ? -71.918 34.565 -32.617 1.00 22.71 ? 464 TYR A CD1   1 
ATOM   2428 C CD2   . TYR A 1 323 ? -70.771 36.597 -33.164 1.00 22.14 ? 464 TYR A CD2   1 
ATOM   2429 C CE1   . TYR A 1 323 ? -73.044 35.008 -33.304 1.00 23.20 ? 464 TYR A CE1   1 
ATOM   2430 C CE2   . TYR A 1 323 ? -71.882 37.046 -33.860 1.00 24.97 ? 464 TYR A CE2   1 
ATOM   2431 C CZ    . TYR A 1 323 ? -73.016 36.250 -33.927 1.00 23.81 ? 464 TYR A CZ    1 
ATOM   2432 O OH    . TYR A 1 323 ? -74.117 36.714 -34.603 1.00 24.83 ? 464 TYR A OH    1 
ATOM   2433 N N     . ALA A 1 324 ? -67.196 35.699 -33.597 1.00 24.49 ? 465 ALA A N     1 
ATOM   2434 C CA    . ALA A 1 324 ? -66.813 36.519 -34.741 1.00 24.09 ? 465 ALA A CA    1 
ATOM   2435 C C     . ALA A 1 324 ? -65.961 35.741 -35.737 1.00 25.62 ? 465 ALA A C     1 
ATOM   2436 O O     . ALA A 1 324 ? -66.141 35.889 -36.952 1.00 24.99 ? 465 ALA A O     1 
ATOM   2437 C CB    . ALA A 1 324 ? -66.063 37.763 -34.260 1.00 19.53 ? 465 ALA A CB    1 
ATOM   2438 N N     . THR A 1 325 ? -65.031 34.907 -35.248 1.00 23.30 ? 466 THR A N     1 
ATOM   2439 C CA    . THR A 1 325 ? -64.021 34.326 -36.138 1.00 27.30 ? 466 THR A CA    1 
ATOM   2440 C C     . THR A 1 325 ? -64.606 33.475 -37.266 1.00 27.97 ? 466 THR A C     1 
ATOM   2441 O O     . THR A 1 325 ? -64.244 33.715 -38.432 1.00 28.26 ? 466 THR A O     1 
ATOM   2442 C CB    . THR A 1 325 ? -63.000 33.539 -35.306 1.00 24.46 ? 466 THR A CB    1 
ATOM   2443 O OG1   . THR A 1 325 ? -62.359 34.425 -34.382 1.00 25.49 ? 466 THR A OG1   1 
ATOM   2444 C CG2   . THR A 1 325 ? -61.942 32.902 -36.203 1.00 28.35 ? 466 THR A CG2   1 
ATOM   2445 N N     . PRO A 1 326 ? -65.489 32.496 -37.019 1.00 28.43 ? 467 PRO A N     1 
ATOM   2446 C CA    . PRO A 1 326 ? -66.027 31.704 -38.147 1.00 27.22 ? 467 PRO A CA    1 
ATOM   2447 C C     . PRO A 1 326 ? -66.866 32.507 -39.130 1.00 29.81 ? 467 PRO A C     1 
ATOM   2448 O O     . PRO A 1 326 ? -66.862 32.202 -40.331 1.00 29.60 ? 467 PRO A O     1 
ATOM   2449 C CB    . PRO A 1 326 ? -66.890 30.635 -37.453 1.00 30.05 ? 467 PRO A CB    1 
ATOM   2450 C CG    . PRO A 1 326 ? -66.512 30.661 -36.034 1.00 31.01 ? 467 PRO A CG    1 
ATOM   2451 C CD    . PRO A 1 326 ? -66.051 32.046 -35.734 1.00 31.50 ? 467 PRO A CD    1 
ATOM   2452 N N     . ARG A 1 327 ? -67.630 33.493 -38.646 1.00 26.36 ? 468 ARG A N     1 
ATOM   2453 C CA    . ARG A 1 327 ? -68.478 34.282 -39.535 1.00 26.65 ? 468 ARG A CA    1 
ATOM   2454 C C     . ARG A 1 327 ? -67.641 35.191 -40.419 1.00 28.03 ? 468 ARG A C     1 
ATOM   2455 O O     . ARG A 1 327 ? -67.952 35.376 -41.601 1.00 28.59 ? 468 ARG A O     1 
ATOM   2456 C CB    . ARG A 1 327 ? -69.473 35.102 -38.714 1.00 29.72 ? 468 ARG A CB    1 
ATOM   2457 C CG    . ARG A 1 327 ? -70.214 34.270 -37.679 1.00 31.13 ? 468 ARG A CG    1 
ATOM   2458 C CD    . ARG A 1 327 ? -71.227 35.102 -36.907 1.00 32.01 ? 468 ARG A CD    1 
ATOM   2459 N NE    . ARG A 1 327 ? -72.428 35.332 -37.691 1.00 30.48 ? 468 ARG A NE    1 
ATOM   2460 C CZ    . ARG A 1 327 ? -73.361 34.418 -37.898 1.00 29.37 ? 468 ARG A CZ    1 
ATOM   2461 N NH1   . ARG A 1 327 ? -73.285 33.216 -37.348 1.00 32.22 ? 468 ARG A NH1   1 
ATOM   2462 N NH2   . ARG A 1 327 ? -74.386 34.710 -38.685 1.00 31.67 ? 468 ARG A NH2   1 
ATOM   2463 N N     . LEU A 1 328 ? -66.565 35.753 -39.865 1.00 24.12 ? 469 LEU A N     1 
ATOM   2464 C CA    . LEU A 1 328 ? -65.616 36.511 -40.675 1.00 25.27 ? 469 LEU A CA    1 
ATOM   2465 C C     . LEU A 1 328 ? -64.917 35.613 -41.691 1.00 30.41 ? 469 LEU A C     1 
ATOM   2466 O O     . LEU A 1 328 ? -64.826 35.952 -42.877 1.00 27.36 ? 469 LEU A O     1 
ATOM   2467 C CB    . LEU A 1 328 ? -64.597 37.209 -39.773 1.00 22.28 ? 469 LEU A CB    1 
ATOM   2468 C CG    . LEU A 1 328 ? -63.508 38.037 -40.469 1.00 25.17 ? 469 LEU A CG    1 
ATOM   2469 C CD1   . LEU A 1 328 ? -64.136 39.083 -41.373 1.00 24.77 ? 469 LEU A CD1   1 
ATOM   2470 C CD2   . LEU A 1 328 ? -62.621 38.699 -39.433 1.00 20.08 ? 469 LEU A CD2   1 
ATOM   2471 N N     . ALA A 1 329 ? -64.419 34.454 -41.243 1.00 28.35 ? 470 ALA A N     1 
ATOM   2472 C CA    . ALA A 1 329 ? -63.694 33.553 -42.135 1.00 29.08 ? 470 ALA A CA    1 
ATOM   2473 C C     . ALA A 1 329 ? -64.562 33.009 -43.268 1.00 30.94 ? 470 ALA A C     1 
ATOM   2474 O O     . ALA A 1 329 ? -64.021 32.610 -44.306 1.00 31.53 ? 470 ALA A O     1 
ATOM   2475 C CB    . ALA A 1 329 ? -63.102 32.387 -41.342 1.00 26.45 ? 470 ALA A CB    1 
ATOM   2476 N N     . ALA A 1 330 ? -65.885 32.994 -43.109 1.00 27.99 ? 471 ALA A N     1 
ATOM   2477 C CA    . ALA A 1 330 ? -66.745 32.454 -44.157 1.00 32.96 ? 471 ALA A CA    1 
ATOM   2478 C C     . ALA A 1 330 ? -67.006 33.433 -45.293 1.00 34.59 ? 471 ALA A C     1 
ATOM   2479 O O     . ALA A 1 330 ? -67.610 33.036 -46.294 1.00 34.58 ? 471 ALA A O     1 
ATOM   2480 C CB    . ALA A 1 330 ? -68.086 32.000 -43.581 1.00 27.54 ? 471 ALA A CB    1 
ATOM   2481 N N     . ILE A 1 331 ? -66.592 34.688 -45.168 1.00 31.46 ? 472 ILE A N     1 
ATOM   2482 C CA    . ILE A 1 331 ? -66.773 35.627 -46.283 1.00 32.22 ? 472 ILE A CA    1 
ATOM   2483 C C     . ILE A 1 331 ? -65.766 35.297 -47.379 1.00 32.87 ? 472 ILE A C     1 
ATOM   2484 O O     . ILE A 1 331 ? -64.559 35.198 -47.091 1.00 28.25 ? 472 ILE A O     1 
ATOM   2485 C CB    . ILE A 1 331 ? -66.596 37.063 -45.804 1.00 31.20 ? 472 ILE A CB    1 
ATOM   2486 C CG1   . ILE A 1 331 ? -67.558 37.366 -44.657 1.00 33.44 ? 472 ILE A CG1   1 
ATOM   2487 C CG2   . ILE A 1 331 ? -66.788 38.028 -46.973 1.00 31.30 ? 472 ILE A CG2   1 
ATOM   2488 C CD1   . ILE A 1 331 ? -67.385 38.756 -44.116 1.00 29.95 ? 472 ILE A CD1   1 
ATOM   2489 N N     . PRO A 1 332 ? -66.192 35.111 -48.629 1.00 33.81 ? 473 PRO A N     1 
ATOM   2490 C CA    . PRO A 1 332 ? -65.228 34.757 -49.681 1.00 34.43 ? 473 PRO A CA    1 
ATOM   2491 C C     . PRO A 1 332 ? -64.172 35.840 -49.847 1.00 32.98 ? 473 PRO A C     1 
ATOM   2492 O O     . PRO A 1 332 ? -64.477 37.034 -49.882 1.00 33.10 ? 473 PRO A O     1 
ATOM   2493 C CB    . PRO A 1 332 ? -66.105 34.604 -50.932 1.00 35.72 ? 473 PRO A CB    1 
ATOM   2494 C CG    . PRO A 1 332 ? -67.460 34.208 -50.366 1.00 32.82 ? 473 PRO A CG    1 
ATOM   2495 C CD    . PRO A 1 332 ? -67.584 35.049 -49.113 1.00 28.93 ? 473 PRO A CD    1 
ATOM   2496 N N     . GLY A 1 333 ? -62.912 35.409 -49.909 1.00 32.81 ? 474 GLY A N     1 
ATOM   2497 C CA    . GLY A 1 333 ? -61.785 36.293 -50.037 1.00 31.32 ? 474 GLY A CA    1 
ATOM   2498 C C     . GLY A 1 333 ? -61.100 36.639 -48.730 1.00 31.50 ? 474 GLY A C     1 
ATOM   2499 O O     . GLY A 1 333 ? -59.967 37.130 -48.760 1.00 29.41 ? 474 GLY A O     1 
ATOM   2500 N N     . VAL A 1 334 ? -61.756 36.409 -47.587 1.00 30.05 ? 475 VAL A N     1 
ATOM   2501 C CA    . VAL A 1 334 ? -61.160 36.738 -46.295 1.00 27.80 ? 475 VAL A CA    1 
ATOM   2502 C C     . VAL A 1 334 ? -60.146 35.671 -45.911 1.00 29.08 ? 475 VAL A C     1 
ATOM   2503 O O     . VAL A 1 334 ? -60.388 34.469 -46.061 1.00 30.38 ? 475 VAL A O     1 
ATOM   2504 C CB    . VAL A 1 334 ? -62.238 36.875 -45.207 1.00 29.31 ? 475 VAL A CB    1 
ATOM   2505 C CG1   . VAL A 1 334 ? -61.587 36.832 -43.805 1.00 24.14 ? 475 VAL A CG1   1 
ATOM   2506 C CG2   . VAL A 1 334 ? -63.053 38.159 -45.401 1.00 28.51 ? 475 VAL A CG2   1 
ATOM   2507 N N     . ARG A 1 335 ? -59.009 36.105 -45.386 1.00 24.47 ? 476 ARG A N     1 
ATOM   2508 C CA    . ARG A 1 335 ? -58.054 35.212 -44.751 1.00 27.76 ? 476 ARG A CA    1 
ATOM   2509 C C     . ARG A 1 335 ? -57.820 35.723 -43.333 1.00 26.54 ? 476 ARG A C     1 
ATOM   2510 O O     . ARG A 1 335 ? -57.433 36.883 -43.146 1.00 25.32 ? 476 ARG A O     1 
ATOM   2511 C CB    . ARG A 1 335 ? -56.754 35.138 -45.565 1.00 30.77 ? 476 ARG A CB    1 
ATOM   2512 C CG    . ARG A 1 335 ? -55.522 34.612 -44.804 1.00 35.97 ? 476 ARG A CG    1 
ATOM   2513 C CD    . ARG A 1 335 ? -54.202 35.065 -45.466 1.00 42.05 ? 476 ARG A CD    1 
ATOM   2514 N NE    . ARG A 1 335 ? -53.016 34.637 -44.727 1.00 40.37 ? 476 ARG A NE    1 
ATOM   2515 C CZ    . ARG A 1 335 ? -51.785 35.086 -44.943 1.00 42.44 ? 476 ARG A CZ    1 
ATOM   2516 N NH1   . ARG A 1 335 ? -51.514 35.918 -45.938 1.00 41.88 ? 476 ARG A NH1   1 
ATOM   2517 N NH2   . ARG A 1 335 ? -50.799 34.685 -44.143 1.00 40.24 ? 476 ARG A NH2   1 
ATOM   2518 N N     . ILE A 1 336 ? -58.091 34.868 -42.338 1.00 26.05 ? 477 ILE A N     1 
ATOM   2519 C CA    . ILE A 1 336 ? -57.763 35.188 -40.950 1.00 23.33 ? 477 ILE A CA    1 
ATOM   2520 C C     . ILE A 1 336 ? -56.259 35.070 -40.750 1.00 24.80 ? 477 ILE A C     1 
ATOM   2521 O O     . ILE A 1 336 ? -55.630 34.105 -41.199 1.00 28.93 ? 477 ILE A O     1 
ATOM   2522 C CB    . ILE A 1 336 ? -58.500 34.262 -39.965 1.00 24.51 ? 477 ILE A CB    1 
ATOM   2523 C CG1   . ILE A 1 336 ? -60.005 34.225 -40.251 1.00 25.62 ? 477 ILE A CG1   1 
ATOM   2524 C CG2   . ILE A 1 336 ? -58.238 34.723 -38.524 1.00 24.66 ? 477 ILE A CG2   1 
ATOM   2525 C CD1   . ILE A 1 336 ? -60.675 35.559 -40.122 1.00 24.83 ? 477 ILE A CD1   1 
ATOM   2526 N N     . VAL A 1 337 ? -55.673 36.045 -40.061 1.00 24.04 ? 478 VAL A N     1 
ATOM   2527 C CA    . VAL A 1 337 ? -54.235 36.084 -39.813 1.00 24.51 ? 478 VAL A CA    1 
ATOM   2528 C C     . VAL A 1 337 ? -54.037 35.970 -38.313 1.00 23.56 ? 478 VAL A C     1 
ATOM   2529 O O     . VAL A 1 337 ? -54.389 36.891 -37.561 1.00 25.75 ? 478 VAL A O     1 
ATOM   2530 C CB    . VAL A 1 337 ? -53.585 37.361 -40.365 1.00 23.99 ? 478 VAL A CB    1 
ATOM   2531 C CG1   . VAL A 1 337 ? -52.076 37.360 -40.092 1.00 23.78 ? 478 VAL A CG1   1 
ATOM   2532 C CG2   . VAL A 1 337 ? -53.866 37.480 -41.855 1.00 25.07 ? 478 VAL A CG2   1 
ATOM   2533 N N     . GLY A 1 338 ? -53.463 34.853 -37.874 1.00 23.68 ? 479 GLY A N     1 
ATOM   2534 C CA    . GLY A 1 338 ? -53.339 34.592 -36.453 1.00 21.55 ? 479 GLY A CA    1 
ATOM   2535 C C     . GLY A 1 338 ? -54.448 33.680 -35.977 1.00 28.34 ? 479 GLY A C     1 
ATOM   2536 O O     . GLY A 1 338 ? -55.554 34.141 -35.665 1.00 26.83 ? 479 GLY A O     1 
ATOM   2537 N N     . THR A 1 339 ? -54.180 32.376 -35.947 1.00 25.14 ? 480 THR A N     1 
ATOM   2538 C CA    . THR A 1 339 ? -55.152 31.380 -35.505 1.00 27.48 ? 480 THR A CA    1 
ATOM   2539 C C     . THR A 1 339 ? -54.538 30.471 -34.450 1.00 30.59 ? 480 THR A C     1 
ATOM   2540 O O     . THR A 1 339 ? -54.668 29.243 -34.492 1.00 30.35 ? 480 THR A O     1 
ATOM   2541 C CB    . THR A 1 339 ? -55.666 30.564 -36.689 1.00 34.04 ? 480 THR A CB    1 
ATOM   2542 O OG1   . THR A 1 339 ? -54.554 29.937 -37.356 1.00 31.71 ? 480 THR A OG1   1 
ATOM   2543 C CG2   . THR A 1 339 ? -56.438 31.463 -37.668 1.00 29.97 ? 480 THR A CG2   1 
ATOM   2544 N N     . ALA A 1 340 ? -53.863 31.080 -33.477 1.00 25.08 ? 481 ALA A N     1 
ATOM   2545 C CA    . ALA A 1 340 ? -53.153 30.331 -32.450 1.00 29.69 ? 481 ALA A CA    1 
ATOM   2546 C C     . ALA A 1 340 ? -54.112 29.479 -31.617 1.00 30.68 ? 481 ALA A C     1 
ATOM   2547 O O     . ALA A 1 340 ? -55.320 29.734 -31.545 1.00 32.77 ? 481 ALA A O     1 
ATOM   2548 C CB    . ALA A 1 340 ? -52.381 31.286 -31.538 1.00 26.65 ? 481 ALA A CB    1 
ATOM   2549 N N     . GLN A 1 341 ? -53.542 28.459 -30.967 1.00 29.59 ? 482 GLN A N     1 
ATOM   2550 C CA    . GLN A 1 341 ? -54.311 27.589 -30.082 1.00 33.27 ? 482 GLN A CA    1 
ATOM   2551 C C     . GLN A 1 341 ? -55.091 28.396 -29.047 1.00 36.46 ? 482 GLN A C     1 
ATOM   2552 O O     . GLN A 1 341 ? -56.254 28.098 -28.759 1.00 34.66 ? 482 GLN A O     1 
ATOM   2553 C CB    . GLN A 1 341 ? -53.366 26.600 -29.390 1.00 39.51 ? 482 GLN A CB    1 
ATOM   2554 C CG    . GLN A 1 341 ? -53.005 25.323 -30.182 1.00 39.40 ? 482 GLN A CG    1 
ATOM   2555 C CD    . GLN A 1 341 ? -54.178 24.694 -30.933 1.00 51.04 ? 482 GLN A CD    1 
ATOM   2556 O OE1   . GLN A 1 341 ? -54.482 25.054 -32.076 1.00 49.81 ? 482 GLN A OE1   1 
ATOM   2557 N NE2   . GLN A 1 341 ? -54.832 23.728 -30.292 1.00 53.88 ? 482 GLN A NE2   1 
ATOM   2558 N N     . GLU A 1 342 ? -54.474 29.421 -28.474 1.00 31.69 ? 483 GLU A N     1 
ATOM   2559 C CA    . GLU A 1 342 ? -55.188 30.318 -27.576 1.00 35.40 ? 483 GLU A CA    1 
ATOM   2560 C C     . GLU A 1 342 ? -54.984 31.752 -28.025 1.00 27.63 ? 483 GLU A C     1 
ATOM   2561 O O     . GLU A 1 342 ? -53.875 32.142 -28.409 1.00 25.09 ? 483 GLU A O     1 
ATOM   2562 C CB    . GLU A 1 342 ? -54.736 30.152 -26.128 1.00 36.19 ? 483 GLU A CB    1 
ATOM   2563 C CG    . GLU A 1 342 ? -55.072 28.792 -25.559 1.00 45.93 ? 483 GLU A CG    1 
ATOM   2564 C CD    . GLU A 1 342 ? -53.985 28.272 -24.653 1.00 64.84 ? 483 GLU A CD    1 
ATOM   2565 O OE1   . GLU A 1 342 ? -53.903 28.757 -23.499 1.00 72.70 ? 483 GLU A OE1   1 
ATOM   2566 O OE2   . GLU A 1 342 ? -53.214 27.386 -25.098 1.00 64.03 ? 483 GLU A OE2   1 
ATOM   2567 N N     . LYS A 1 343 ? -56.063 32.526 -27.975 1.00 24.77 ? 484 LYS A N     1 
ATOM   2568 C CA    . LYS A 1 343 ? -56.048 33.906 -28.424 1.00 22.90 ? 484 LYS A CA    1 
ATOM   2569 C C     . LYS A 1 343 ? -56.816 34.762 -27.431 1.00 28.33 ? 484 LYS A C     1 
ATOM   2570 O O     . LYS A 1 343 ? -57.630 34.268 -26.647 1.00 25.90 ? 484 LYS A O     1 
ATOM   2571 C CB    . LYS A 1 343 ? -56.674 34.065 -29.820 1.00 27.42 ? 484 LYS A CB    1 
ATOM   2572 C CG    . LYS A 1 343 ? -55.887 33.461 -30.969 1.00 23.19 ? 484 LYS A CG    1 
ATOM   2573 C CD    . LYS A 1 343 ? -56.608 33.707 -32.293 1.00 24.59 ? 484 LYS A CD    1 
ATOM   2574 C CE    . LYS A 1 343 ? -56.725 35.204 -32.604 1.00 23.62 ? 484 LYS A CE    1 
ATOM   2575 N NZ    . LYS A 1 343 ? -57.408 35.453 -33.914 1.00 22.57 ? 484 LYS A NZ    1 
ATOM   2576 N N     . ALA A 1 344 ? -56.554 36.063 -27.485 1.00 21.95 ? 485 ALA A N     1 
ATOM   2577 C CA    . ALA A 1 344 ? -57.330 37.041 -26.738 1.00 25.86 ? 485 ALA A CA    1 
ATOM   2578 C C     . ALA A 1 344 ? -57.561 38.244 -27.638 1.00 24.82 ? 485 ALA A C     1 
ATOM   2579 O O     . ALA A 1 344 ? -56.599 38.803 -28.189 1.00 24.77 ? 485 ALA A O     1 
ATOM   2580 C CB    . ALA A 1 344 ? -56.615 37.454 -25.444 1.00 24.08 ? 485 ALA A CB    1 
ATOM   2581 N N     . SER A 1 345 ? -58.839 38.568 -27.851 1.00 20.65 ? 486 SER A N     1 
ATOM   2582 C CA    . SER A 1 345 ? -59.318 39.876 -28.296 1.00 24.30 ? 486 SER A CA    1 
ATOM   2583 C C     . SER A 1 345 ? -59.092 40.224 -29.769 1.00 22.12 ? 486 SER A C     1 
ATOM   2584 O O     . SER A 1 345 ? -59.992 40.779 -30.410 1.00 21.96 ? 486 SER A O     1 
ATOM   2585 C CB    . SER A 1 345 ? -58.696 40.969 -27.423 1.00 26.27 ? 486 SER A CB    1 
ATOM   2586 O OG    . SER A 1 345 ? -58.946 42.249 -27.985 1.00 25.64 ? 486 SER A OG    1 
ATOM   2587 N N     . VAL A 1 346 ? -57.913 39.925 -30.307 1.00 21.50 ? 487 VAL A N     1 
ATOM   2588 C CA    . VAL A 1 346 ? -57.480 40.436 -31.609 1.00 22.91 ? 487 VAL A CA    1 
ATOM   2589 C C     . VAL A 1 346 ? -57.915 39.488 -32.720 1.00 23.24 ? 487 VAL A C     1 
ATOM   2590 O O     . VAL A 1 346 ? -57.732 38.271 -32.609 1.00 20.75 ? 487 VAL A O     1 
ATOM   2591 C CB    . VAL A 1 346 ? -55.956 40.614 -31.626 1.00 21.23 ? 487 VAL A CB    1 
ATOM   2592 C CG1   . VAL A 1 346 ? -55.456 40.889 -33.043 1.00 21.70 ? 487 VAL A CG1   1 
ATOM   2593 C CG2   . VAL A 1 346 ? -55.539 41.698 -30.637 1.00 21.54 ? 487 VAL A CG2   1 
ATOM   2594 N N     . LEU A 1 347 ? -58.458 40.043 -33.824 1.00 19.40 ? 488 LEU A N     1 
ATOM   2595 C CA    . LEU A 1 347 ? -58.880 39.240 -34.974 1.00 22.24 ? 488 LEU A CA    1 
ATOM   2596 C C     . LEU A 1 347 ? -58.379 39.903 -36.266 1.00 22.43 ? 488 LEU A C     1 
ATOM   2597 O O     . LEU A 1 347 ? -59.144 40.524 -37.004 1.00 22.05 ? 488 LEU A O     1 
ATOM   2598 C CB    . LEU A 1 347 ? -60.422 39.056 -34.962 1.00 21.79 ? 488 LEU A CB    1 
ATOM   2599 C CG    . LEU A 1 347 ? -61.051 38.197 -36.068 1.00 20.32 ? 488 LEU A CG    1 
ATOM   2600 C CD1   . LEU A 1 347 ? -60.394 36.840 -36.144 1.00 20.75 ? 488 LEU A CD1   1 
ATOM   2601 C CD2   . LEU A 1 347 ? -62.560 38.037 -35.839 1.00 20.47 ? 488 LEU A CD2   1 
ATOM   2602 N N     . SER A 1 348 ? -57.090 39.748 -36.553 1.00 20.53 ? 489 SER A N     1 
ATOM   2603 C CA    . SER A 1 348 ? -56.541 40.268 -37.800 1.00 21.02 ? 489 SER A CA    1 
ATOM   2604 C C     . SER A 1 348 ? -57.043 39.468 -38.992 1.00 21.17 ? 489 SER A C     1 
ATOM   2605 O O     . SER A 1 348 ? -57.187 38.243 -38.929 1.00 21.57 ? 489 SER A O     1 
ATOM   2606 C CB    . SER A 1 348 ? -55.012 40.221 -37.783 1.00 18.09 ? 489 SER A CB    1 
ATOM   2607 O OG    . SER A 1 348 ? -54.491 41.404 -37.212 1.00 22.53 ? 489 SER A OG    1 
ATOM   2608 N N     . PHE A 1 349 ? -57.270 40.171 -40.102 1.00 22.57 ? 490 PHE A N     1 
ATOM   2609 C CA    . PHE A 1 349 ? -57.631 39.518 -41.352 1.00 20.99 ? 490 PHE A CA    1 
ATOM   2610 C C     . PHE A 1 349 ? -57.195 40.377 -42.538 1.00 23.67 ? 490 PHE A C     1 
ATOM   2611 O O     . PHE A 1 349 ? -56.823 41.549 -42.396 1.00 20.48 ? 490 PHE A O     1 
ATOM   2612 C CB    . PHE A 1 349 ? -59.132 39.214 -41.412 1.00 19.53 ? 490 PHE A CB    1 
ATOM   2613 C CG    . PHE A 1 349 ? -59.999 40.420 -41.624 1.00 23.79 ? 490 PHE A CG    1 
ATOM   2614 C CD1   . PHE A 1 349 ? -60.331 41.249 -40.562 1.00 21.05 ? 490 PHE A CD1   1 
ATOM   2615 C CD2   . PHE A 1 349 ? -60.531 40.699 -42.879 1.00 23.13 ? 490 PHE A CD2   1 
ATOM   2616 C CE1   . PHE A 1 349 ? -61.150 42.357 -40.756 1.00 22.50 ? 490 PHE A CE1   1 
ATOM   2617 C CE2   . PHE A 1 349 ? -61.359 41.807 -43.073 1.00 22.64 ? 490 PHE A CE2   1 
ATOM   2618 C CZ    . PHE A 1 349 ? -61.662 42.634 -42.015 1.00 19.19 ? 490 PHE A CZ    1 
ATOM   2619 N N     . VAL A 1 350 ? -57.198 39.750 -43.717 1.00 20.33 ? 491 VAL A N     1 
ATOM   2620 C CA    . VAL A 1 350 ? -57.038 40.453 -44.984 1.00 24.12 ? 491 VAL A CA    1 
ATOM   2621 C C     . VAL A 1 350 ? -58.160 40.010 -45.913 1.00 25.94 ? 491 VAL A C     1 
ATOM   2622 O O     . VAL A 1 350 ? -58.803 38.979 -45.704 1.00 26.50 ? 491 VAL A O     1 
ATOM   2623 C CB    . VAL A 1 350 ? -55.661 40.214 -45.661 1.00 27.27 ? 491 VAL A CB    1 
ATOM   2624 C CG1   . VAL A 1 350 ? -54.535 40.866 -44.858 1.00 30.08 ? 491 VAL A CG1   1 
ATOM   2625 C CG2   . VAL A 1 350 ? -55.410 38.734 -45.878 1.00 29.91 ? 491 VAL A CG2   1 
ATOM   2626 N N     . LEU A 1 351 ? -58.380 40.805 -46.959 1.00 26.56 ? 492 LEU A N     1 
ATOM   2627 C CA    . LEU A 1 351 ? -59.435 40.562 -47.936 1.00 27.47 ? 492 LEU A CA    1 
ATOM   2628 C C     . LEU A 1 351 ? -58.828 40.650 -49.329 1.00 31.88 ? 492 LEU A C     1 
ATOM   2629 O O     . LEU A 1 351 ? -58.284 41.697 -49.701 1.00 27.41 ? 492 LEU A O     1 
ATOM   2630 C CB    . LEU A 1 351 ? -60.575 41.575 -47.768 1.00 29.19 ? 492 LEU A CB    1 
ATOM   2631 C CG    . LEU A 1 351 ? -61.782 41.549 -48.712 1.00 30.35 ? 492 LEU A CG    1 
ATOM   2632 C CD1   . LEU A 1 351 ? -62.552 40.250 -48.566 1.00 31.12 ? 492 LEU A CD1   1 
ATOM   2633 C CD2   . LEU A 1 351 ? -62.689 42.741 -48.462 1.00 31.12 ? 492 LEU A CD2   1 
ATOM   2634 N N     . ALA A 1 352 ? -58.916 39.555 -50.090 1.00 29.86 ? 493 ALA A N     1 
ATOM   2635 C CA    . ALA A 1 352 ? -58.287 39.496 -51.406 1.00 32.49 ? 493 ALA A CA    1 
ATOM   2636 C C     . ALA A 1 352 ? -58.792 40.629 -52.294 1.00 34.03 ? 493 ALA A C     1 
ATOM   2637 O O     . ALA A 1 352 ? -59.997 40.889 -52.366 1.00 31.87 ? 493 ALA A O     1 
ATOM   2638 C CB    . ALA A 1 352 ? -58.562 38.140 -52.067 1.00 27.72 ? 493 ALA A CB    1 
ATOM   2639 N N     . GLY A 1 353 ? -57.863 41.312 -52.957 1.00 35.44 ? 494 GLY A N     1 
ATOM   2640 C CA    . GLY A 1 353 ? -58.208 42.334 -53.921 1.00 32.72 ? 494 GLY A CA    1 
ATOM   2641 C C     . GLY A 1 353 ? -58.524 43.696 -53.341 1.00 33.74 ? 494 GLY A C     1 
ATOM   2642 O O     . GLY A 1 353 ? -58.905 44.596 -54.102 1.00 32.87 ? 494 GLY A O     1 
ATOM   2643 N N     . HIS A 1 354 ? -58.383 43.881 -52.029 1.00 32.38 ? 495 HIS A N     1 
ATOM   2644 C CA    . HIS A 1 354 ? -58.663 45.152 -51.371 1.00 29.52 ? 495 HIS A CA    1 
ATOM   2645 C C     . HIS A 1 354 ? -57.513 45.507 -50.444 1.00 29.24 ? 495 HIS A C     1 
ATOM   2646 O O     . HIS A 1 354 ? -57.008 44.648 -49.722 1.00 31.42 ? 495 HIS A O     1 
ATOM   2647 C CB    . HIS A 1 354 ? -59.968 45.080 -50.577 1.00 28.95 ? 495 HIS A CB    1 
ATOM   2648 C CG    . HIS A 1 354 ? -61.180 44.906 -51.441 1.00 31.07 ? 495 HIS A CG    1 
ATOM   2649 N ND1   . HIS A 1 354 ? -61.963 45.964 -51.849 1.00 31.29 ? 495 HIS A ND1   1 
ATOM   2650 C CD2   . HIS A 1 354 ? -61.725 43.799 -51.998 1.00 33.14 ? 495 HIS A CD2   1 
ATOM   2651 C CE1   . HIS A 1 354 ? -62.948 45.517 -52.607 1.00 31.94 ? 495 HIS A CE1   1 
ATOM   2652 N NE2   . HIS A 1 354 ? -62.823 44.206 -52.719 1.00 36.13 ? 495 HIS A NE2   1 
ATOM   2653 N N     . GLU A 1 355 ? -57.108 46.771 -50.456 1.00 27.22 ? 496 GLU A N     1 
ATOM   2654 C CA    . GLU A 1 355 ? -56.067 47.217 -49.540 1.00 31.60 ? 496 GLU A CA    1 
ATOM   2655 C C     . GLU A 1 355 ? -56.623 47.280 -48.116 1.00 28.36 ? 496 GLU A C     1 
ATOM   2656 O O     . GLU A 1 355 ? -57.730 47.778 -47.911 1.00 25.14 ? 496 GLU A O     1 
ATOM   2657 C CB    . GLU A 1 355 ? -55.549 48.599 -49.943 1.00 30.08 ? 496 GLU A CB    1 
ATOM   2658 C CG    . GLU A 1 355 ? -54.665 48.641 -51.186 1.00 33.04 ? 496 GLU A CG    1 
ATOM   2659 C CD    . GLU A 1 355 ? -53.452 47.730 -51.087 1.00 41.20 ? 496 GLU A CD    1 
ATOM   2660 O OE1   . GLU A 1 355 ? -53.347 46.772 -51.888 1.00 40.67 ? 496 GLU A OE1   1 
ATOM   2661 O OE2   . GLU A 1 355 ? -52.601 47.977 -50.204 1.00 44.22 ? 496 GLU A OE2   1 
ATOM   2662 N N     . PRO A 1 356 ? -55.875 46.795 -47.115 1.00 28.36 ? 497 PRO A N     1 
ATOM   2663 C CA    . PRO A 1 356 ? -56.352 46.900 -45.721 1.00 24.53 ? 497 PRO A CA    1 
ATOM   2664 C C     . PRO A 1 356 ? -56.839 48.285 -45.327 1.00 27.75 ? 497 PRO A C     1 
ATOM   2665 O O     . PRO A 1 356 ? -57.875 48.407 -44.660 1.00 24.12 ? 497 PRO A O     1 
ATOM   2666 C CB    . PRO A 1 356 ? -55.115 46.498 -44.913 1.00 24.43 ? 497 PRO A CB    1 
ATOM   2667 C CG    . PRO A 1 356 ? -54.428 45.495 -45.790 1.00 28.24 ? 497 PRO A CG    1 
ATOM   2668 C CD    . PRO A 1 356 ? -54.664 45.961 -47.221 1.00 26.23 ? 497 PRO A CD    1 
ATOM   2669 N N     . LEU A 1 357 ? -56.122 49.338 -45.724 1.00 25.75 ? 498 LEU A N     1 
ATOM   2670 C CA    . LEU A 1 357 ? -56.507 50.686 -45.306 1.00 29.50 ? 498 LEU A CA    1 
ATOM   2671 C C     . LEU A 1 357 ? -57.856 51.101 -45.901 1.00 29.82 ? 498 LEU A C     1 
ATOM   2672 O O     . LEU A 1 357 ? -58.651 51.783 -45.242 1.00 29.37 ? 498 LEU A O     1 
ATOM   2673 C CB    . LEU A 1 357 ? -55.405 51.676 -45.690 1.00 34.24 ? 498 LEU A CB    1 
ATOM   2674 C CG    . LEU A 1 357 ? -55.645 53.166 -45.417 1.00 41.81 ? 498 LEU A CG    1 
ATOM   2675 C CD1   . LEU A 1 357 ? -56.063 53.443 -43.959 1.00 40.79 ? 498 LEU A CD1   1 
ATOM   2676 C CD2   . LEU A 1 357 ? -54.408 53.960 -45.795 1.00 40.00 ? 498 LEU A CD2   1 
ATOM   2677 N N     . GLU A 1 358 ? -58.148 50.694 -47.141 1.00 28.37 ? 499 GLU A N     1 
ATOM   2678 C CA    . GLU A 1 358 ? -59.453 51.033 -47.698 1.00 30.65 ? 499 GLU A CA    1 
ATOM   2679 C C     . GLU A 1 358 ? -60.576 50.277 -46.993 1.00 27.83 ? 499 GLU A C     1 
ATOM   2680 O O     . GLU A 1 358 ? -61.682 50.813 -46.833 1.00 27.83 ? 499 GLU A O     1 
ATOM   2681 C CB    . GLU A 1 358 ? -59.476 50.773 -49.206 1.00 33.59 ? 499 GLU A CB    1 
ATOM   2682 C CG    . GLU A 1 358 ? -58.621 51.778 -50.007 1.00 41.05 ? 499 GLU A CG    1 
ATOM   2683 C CD    . GLU A 1 358 ? -58.844 53.243 -49.578 1.00 40.84 ? 499 GLU A CD    1 
ATOM   2684 O OE1   . GLU A 1 358 ? -59.981 53.763 -49.749 1.00 39.34 ? 499 GLU A OE1   1 
ATOM   2685 O OE2   . GLU A 1 358 ? -57.878 53.869 -49.061 1.00 40.12 ? 499 GLU A OE2   1 
ATOM   2686 N N     . VAL A 1 359 ? -60.314 49.047 -46.549 1.00 26.46 ? 500 VAL A N     1 
ATOM   2687 C CA    . VAL A 1 359 ? -61.310 48.337 -45.751 1.00 26.88 ? 500 VAL A CA    1 
ATOM   2688 C C     . VAL A 1 359 ? -61.539 49.065 -44.431 1.00 24.39 ? 500 VAL A C     1 
ATOM   2689 O O     . VAL A 1 359 ? -62.681 49.226 -43.981 1.00 22.70 ? 500 VAL A O     1 
ATOM   2690 C CB    . VAL A 1 359 ? -60.874 46.876 -45.530 1.00 27.22 ? 500 VAL A CB    1 
ATOM   2691 C CG1   . VAL A 1 359 ? -61.880 46.135 -44.632 1.00 22.56 ? 500 VAL A CG1   1 
ATOM   2692 C CG2   . VAL A 1 359 ? -60.684 46.169 -46.875 1.00 22.18 ? 500 VAL A CG2   1 
ATOM   2693 N N     . GLY A 1 360 ? -60.457 49.517 -43.789 1.00 23.00 ? 501 GLY A N     1 
ATOM   2694 C CA    . GLY A 1 360 ? -60.612 50.259 -42.543 1.00 24.58 ? 501 GLY A CA    1 
ATOM   2695 C C     . GLY A 1 360 ? -61.426 51.529 -42.725 1.00 26.89 ? 501 GLY A C     1 
ATOM   2696 O O     . GLY A 1 360 ? -62.273 51.868 -41.891 1.00 24.19 ? 501 GLY A O     1 
ATOM   2697 N N     . LYS A 1 361 ? -61.202 52.236 -43.835 1.00 26.69 ? 502 LYS A N     1 
ATOM   2698 C CA    . LYS A 1 361 ? -61.946 53.473 -44.060 1.00 28.72 ? 502 LYS A CA    1 
ATOM   2699 C C     . LYS A 1 361 ? -63.405 53.199 -44.397 1.00 25.21 ? 502 LYS A C     1 
ATOM   2700 O O     . LYS A 1 361 ? -64.295 53.950 -43.977 1.00 28.42 ? 502 LYS A O     1 
ATOM   2701 C CB    . LYS A 1 361 ? -61.284 54.295 -45.161 1.00 32.88 ? 502 LYS A CB    1 
ATOM   2702 C CG    . LYS A 1 361 ? -59.886 54.745 -44.789 1.00 38.49 ? 502 LYS A CG    1 
ATOM   2703 C CD    . LYS A 1 361 ? -59.669 56.206 -45.117 1.00 44.08 ? 502 LYS A CD    1 
ATOM   2704 C CE    . LYS A 1 361 ? -58.658 56.347 -46.220 1.00 42.37 ? 502 LYS A CE    1 
ATOM   2705 N NZ    . LYS A 1 361 ? -57.299 56.059 -45.720 1.00 44.97 ? 502 LYS A NZ    1 
ATOM   2706 N N     . ALA A 1 362 ? -63.685 52.124 -45.138 1.00 24.26 ? 503 ALA A N     1 
ATOM   2707 C CA    . ALA A 1 362 ? -65.082 51.777 -45.388 1.00 25.02 ? 503 ALA A CA    1 
ATOM   2708 C C     . ALA A 1 362 ? -65.786 51.384 -44.092 1.00 24.81 ? 503 ALA A C     1 
ATOM   2709 O O     . ALA A 1 362 ? -66.952 51.760 -43.855 1.00 29.34 ? 503 ALA A O     1 
ATOM   2710 C CB    . ALA A 1 362 ? -65.163 50.647 -46.412 1.00 26.96 ? 503 ALA A CB    1 
ATOM   2711 N N     . LEU A 1 363 ? -65.082 50.647 -43.228 1.00 23.31 ? 504 LEU A N     1 
ATOM   2712 C CA    . LEU A 1 363 ? -65.661 50.277 -41.941 1.00 25.72 ? 504 LEU A CA    1 
ATOM   2713 C C     . LEU A 1 363 ? -65.949 51.516 -41.110 1.00 24.93 ? 504 LEU A C     1 
ATOM   2714 O O     . LEU A 1 363 ? -67.007 51.609 -40.479 1.00 28.34 ? 504 LEU A O     1 
ATOM   2715 C CB    . LEU A 1 363 ? -64.732 49.316 -41.189 1.00 23.93 ? 504 LEU A CB    1 
ATOM   2716 C CG    . LEU A 1 363 ? -64.663 47.932 -41.861 1.00 26.09 ? 504 LEU A CG    1 
ATOM   2717 C CD1   . LEU A 1 363 ? -63.715 46.982 -41.120 1.00 24.95 ? 504 LEU A CD1   1 
ATOM   2718 C CD2   . LEU A 1 363 ? -66.049 47.317 -42.010 1.00 23.05 ? 504 LEU A CD2   1 
ATOM   2719 N N     . ASN A 1 364 ? -65.035 52.496 -41.129 1.00 24.15 ? 505 ASN A N     1 
ATOM   2720 C CA    . ASN A 1 364 ? -65.289 53.741 -40.405 1.00 25.18 ? 505 ASN A CA    1 
ATOM   2721 C C     . ASN A 1 364 ? -66.504 54.457 -40.969 1.00 31.09 ? 505 ASN A C     1 
ATOM   2722 O O     . ASN A 1 364 ? -67.274 55.070 -40.219 1.00 26.43 ? 505 ASN A O     1 
ATOM   2723 C CB    . ASN A 1 364 ? -64.079 54.671 -40.452 1.00 24.11 ? 505 ASN A CB    1 
ATOM   2724 C CG    . ASN A 1 364 ? -64.362 56.022 -39.792 1.00 27.42 ? 505 ASN A CG    1 
ATOM   2725 O OD1   . ASN A 1 364 ? -64.601 56.102 -38.581 1.00 20.63 ? 505 ASN A OD1   1 
ATOM   2726 N ND2   . ASN A 1 364 ? -64.369 57.084 -40.594 1.00 24.29 ? 505 ASN A ND2   1 
ATOM   2727 N N     . ALA A 1 365 ? -66.691 54.397 -42.295 1.00 26.57 ? 506 ALA A N     1 
ATOM   2728 C CA    . ALA A 1 365 ? -67.910 54.952 -42.879 1.00 31.68 ? 506 ALA A CA    1 
ATOM   2729 C C     . ALA A 1 365 ? -69.152 54.280 -42.310 1.00 34.84 ? 506 ALA A C     1 
ATOM   2730 O O     . ALA A 1 365 ? -70.230 54.889 -42.282 1.00 32.75 ? 506 ALA A O     1 
ATOM   2731 C CB    . ALA A 1 365 ? -67.890 54.822 -44.406 1.00 29.24 ? 506 ALA A CB    1 
ATOM   2732 N N     . GLU A 1 366 ? -69.032 53.026 -41.872 1.00 32.46 ? 507 GLU A N     1 
ATOM   2733 C CA    . GLU A 1 366 ? -70.142 52.373 -41.171 1.00 31.06 ? 507 GLU A CA    1 
ATOM   2734 C C     . GLU A 1 366 ? -70.168 52.662 -39.661 1.00 33.23 ? 507 GLU A C     1 
ATOM   2735 O O     . GLU A 1 366 ? -70.969 52.058 -38.937 1.00 28.43 ? 507 GLU A O     1 
ATOM   2736 C CB    . GLU A 1 366 ? -70.089 50.859 -41.383 1.00 31.34 ? 507 GLU A CB    1 
ATOM   2737 C CG    . GLU A 1 366 ? -70.285 50.416 -42.807 1.00 35.44 ? 507 GLU A CG    1 
ATOM   2738 C CD    . GLU A 1 366 ? -71.625 50.838 -43.332 1.00 46.11 ? 507 GLU A CD    1 
ATOM   2739 O OE1   . GLU A 1 366 ? -71.651 51.678 -44.258 1.00 54.24 ? 507 GLU A OE1   1 
ATOM   2740 O OE2   . GLU A 1 366 ? -72.650 50.374 -42.780 1.00 50.88 ? 507 GLU A OE2   1 
ATOM   2741 N N     . GLY A 1 367 ? -69.304 53.546 -39.166 1.00 28.36 ? 508 GLY A N     1 
ATOM   2742 C CA    . GLY A 1 367 ? -69.185 53.785 -37.744 1.00 27.92 ? 508 GLY A CA    1 
ATOM   2743 C C     . GLY A 1 367 ? -68.224 52.872 -37.004 1.00 26.84 ? 508 GLY A C     1 
ATOM   2744 O O     . GLY A 1 367 ? -67.998 53.081 -35.801 1.00 25.65 ? 508 GLY A O     1 
ATOM   2745 N N     . ILE A 1 368 ? -67.637 51.881 -37.676 1.00 24.98 ? 509 ILE A N     1 
ATOM   2746 C CA    . ILE A 1 368 ? -66.796 50.887 -37.018 1.00 24.41 ? 509 ILE A CA    1 
ATOM   2747 C C     . ILE A 1 368 ? -65.355 51.376 -37.002 1.00 21.37 ? 509 ILE A C     1 
ATOM   2748 O O     . ILE A 1 368 ? -64.776 51.655 -38.054 1.00 19.86 ? 509 ILE A O     1 
ATOM   2749 C CB    . ILE A 1 368 ? -66.895 49.525 -37.731 1.00 25.61 ? 509 ILE A CB    1 
ATOM   2750 C CG1   . ILE A 1 368 ? -68.339 49.001 -37.720 1.00 26.05 ? 509 ILE A CG1   1 
ATOM   2751 C CG2   . ILE A 1 368 ? -65.924 48.528 -37.101 1.00 21.71 ? 509 ILE A CG2   1 
ATOM   2752 C CD1   . ILE A 1 368 ? -68.691 48.105 -38.916 1.00 26.49 ? 509 ILE A CD1   1 
ATOM   2753 N N     . ALA A 1 369 ? -64.753 51.421 -35.816 1.00 18.44 ? 510 ALA A N     1 
ATOM   2754 C CA    . ALA A 1 369 ? -63.364 51.830 -35.657 1.00 18.87 ? 510 ALA A CA    1 
ATOM   2755 C C     . ALA A 1 369 ? -62.469 50.593 -35.560 1.00 19.76 ? 510 ALA A C     1 
ATOM   2756 O O     . ALA A 1 369 ? -62.620 49.780 -34.640 1.00 18.68 ? 510 ALA A O     1 
ATOM   2757 C CB    . ALA A 1 369 ? -63.201 52.724 -34.427 1.00 18.09 ? 510 ALA A CB    1 
ATOM   2758 N N     . VAL A 1 370 ? -61.563 50.439 -36.532 1.00 15.30 ? 511 VAL A N     1 
ATOM   2759 C CA    . VAL A 1 370 ? -60.525 49.415 -36.531 1.00 16.59 ? 511 VAL A CA    1 
ATOM   2760 C C     . VAL A 1 370 ? -59.235 50.072 -37.009 1.00 22.51 ? 511 VAL A C     1 
ATOM   2761 O O     . VAL A 1 370 ? -59.240 51.184 -37.537 1.00 23.83 ? 511 VAL A O     1 
ATOM   2762 C CB    . VAL A 1 370 ? -60.864 48.211 -37.436 1.00 20.31 ? 511 VAL A CB    1 
ATOM   2763 C CG1   . VAL A 1 370 ? -62.211 47.614 -37.089 1.00 19.26 ? 511 VAL A CG1   1 
ATOM   2764 C CG2   . VAL A 1 370 ? -60.844 48.647 -38.906 1.00 22.63 ? 511 VAL A CG2   1 
ATOM   2765 N N     . ARG A 1 371 ? -58.115 49.382 -36.820 1.00 21.80 ? 512 ARG A N     1 
ATOM   2766 C CA    . ARG A 1 371 ? -56.856 49.810 -37.414 1.00 22.09 ? 512 ARG A CA    1 
ATOM   2767 C C     . ARG A 1 371 ? -56.526 48.903 -38.581 1.00 23.12 ? 512 ARG A C     1 
ATOM   2768 O O     . ARG A 1 371 ? -56.683 47.681 -38.496 1.00 21.66 ? 512 ARG A O     1 
ATOM   2769 C CB    . ARG A 1 371 ? -55.690 49.773 -36.423 1.00 21.83 ? 512 ARG A CB    1 
ATOM   2770 C CG    . ARG A 1 371 ? -55.796 50.751 -35.297 1.00 31.00 ? 512 ARG A CG    1 
ATOM   2771 C CD    . ARG A 1 371 ? -55.285 52.133 -35.616 1.00 30.22 ? 512 ARG A CD    1 
ATOM   2772 N NE    . ARG A 1 371 ? -55.691 53.048 -34.554 1.00 28.13 ? 512 ARG A NE    1 
ATOM   2773 C CZ    . ARG A 1 371 ? -55.295 54.308 -34.461 1.00 27.35 ? 512 ARG A CZ    1 
ATOM   2774 N NH1   . ARG A 1 371 ? -54.431 54.826 -35.319 1.00 29.90 ? 512 ARG A NH1   1 
ATOM   2775 N NH2   . ARG A 1 371 ? -55.767 55.063 -33.477 1.00 24.13 ? 512 ARG A NH2   1 
ATOM   2776 N N     . ALA A 1 372 ? -56.049 49.508 -39.659 1.00 19.90 ? 513 ALA A N     1 
ATOM   2777 C CA    . ALA A 1 372 ? -55.503 48.787 -40.793 1.00 24.19 ? 513 ALA A CA    1 
ATOM   2778 C C     . ALA A 1 372 ? -54.076 49.275 -40.965 1.00 32.03 ? 513 ALA A C     1 
ATOM   2779 O O     . ALA A 1 372 ? -53.845 50.483 -41.100 1.00 34.13 ? 513 ALA A O     1 
ATOM   2780 C CB    . ALA A 1 372 ? -56.330 49.029 -42.057 1.00 25.19 ? 513 ALA A CB    1 
ATOM   2781 N N     . GLY A 1 373 ? -53.126 48.355 -40.915 1.00 28.45 ? 514 GLY A N     1 
ATOM   2782 C CA    . GLY A 1 373 ? -51.730 48.765 -40.885 1.00 23.13 ? 514 GLY A CA    1 
ATOM   2783 C C     . GLY A 1 373 ? -50.871 47.637 -40.349 1.00 23.98 ? 514 GLY A C     1 
ATOM   2784 O O     . GLY A 1 373 ? -51.299 46.482 -40.318 1.00 22.00 ? 514 GLY A O     1 
ATOM   2785 N N     . HIS A 1 374 ? -49.660 47.995 -39.906 1.00 20.17 ? 515 HIS A N     1 
ATOM   2786 C CA    . HIS A 1 374 ? -48.774 46.974 -39.363 1.00 25.56 ? 515 HIS A CA    1 
ATOM   2787 C C     . HIS A 1 374 ? -48.816 46.896 -37.841 1.00 22.93 ? 515 HIS A C     1 
ATOM   2788 O O     . HIS A 1 374 ? -48.171 46.011 -37.269 1.00 21.38 ? 515 HIS A O     1 
ATOM   2789 C CB    . HIS A 1 374 ? -47.330 47.163 -39.856 1.00 22.86 ? 515 HIS A CB    1 
ATOM   2790 C CG    . HIS A 1 374 ? -46.747 48.505 -39.566 1.00 24.34 ? 515 HIS A CG    1 
ATOM   2791 N ND1   . HIS A 1 374 ? -46.689 49.032 -38.294 1.00 23.83 ? 515 HIS A ND1   1 
ATOM   2792 C CD2   . HIS A 1 374 ? -46.168 49.419 -40.383 1.00 24.67 ? 515 HIS A CD2   1 
ATOM   2793 C CE1   . HIS A 1 374 ? -46.113 50.221 -38.340 1.00 28.82 ? 515 HIS A CE1   1 
ATOM   2794 N NE2   . HIS A 1 374 ? -45.784 50.478 -39.595 1.00 28.50 ? 515 HIS A NE2   1 
ATOM   2795 N N     . HIS A 1 375 ? -49.561 47.787 -37.182 1.00 19.99 ? 516 HIS A N     1 
ATOM   2796 C CA    . HIS A 1 375 ? -49.877 47.663 -35.755 1.00 21.26 ? 516 HIS A CA    1 
ATOM   2797 C C     . HIS A 1 375 ? -48.626 47.720 -34.887 1.00 19.87 ? 516 HIS A C     1 
ATOM   2798 O O     . HIS A 1 375 ? -48.596 47.150 -33.793 1.00 20.43 ? 516 HIS A O     1 
ATOM   2799 C CB    . HIS A 1 375 ? -50.668 46.376 -35.478 1.00 17.83 ? 516 HIS A CB    1 
ATOM   2800 C CG    . HIS A 1 375 ? -51.773 46.133 -36.463 1.00 22.16 ? 516 HIS A CG    1 
ATOM   2801 N ND1   . HIS A 1 375 ? -52.821 47.016 -36.635 1.00 19.89 ? 516 HIS A ND1   1 
ATOM   2802 C CD2   . HIS A 1 375 ? -51.972 45.132 -37.358 1.00 18.68 ? 516 HIS A CD2   1 
ATOM   2803 C CE1   . HIS A 1 375 ? -53.625 46.565 -37.585 1.00 22.60 ? 516 HIS A CE1   1 
ATOM   2804 N NE2   . HIS A 1 375 ? -53.136 45.420 -38.038 1.00 21.14 ? 516 HIS A NE2   1 
ATOM   2805 N N     . CYS A 1 376 ? -47.593 48.413 -35.367 1.00 17.92 ? 517 CYS A N     1 
ATOM   2806 C CA    . CYS A 1 376 ? -46.303 48.468 -34.685 1.00 15.37 ? 517 CYS A CA    1 
ATOM   2807 C C     . CYS A 1 376 ? -45.790 47.059 -34.417 1.00 18.62 ? 517 CYS A C     1 
ATOM   2808 O O     . CYS A 1 376 ? -45.249 46.765 -33.349 1.00 19.45 ? 517 CYS A O     1 
ATOM   2809 C CB    . CYS A 1 376 ? -46.386 49.275 -33.382 1.00 19.51 ? 517 CYS A CB    1 
ATOM   2810 S SG    . CYS A 1 376 ? -46.739 51.050 -33.611 1.00 35.21 ? 517 CYS A SG    1 
ATOM   2811 N N     . ALA A 1 377 ? -45.962 46.179 -35.399 1.00 17.78 ? 518 ALA A N     1 
ATOM   2812 C CA    . ALA A 1 377 ? -45.465 44.814 -35.302 1.00 18.83 ? 518 ALA A CA    1 
ATOM   2813 C C     . ALA A 1 377 ? -45.094 44.318 -36.699 1.00 21.02 ? 518 ALA A C     1 
ATOM   2814 O O     . ALA A 1 377 ? -45.542 43.265 -37.150 1.00 19.52 ? 518 ALA A O     1 
ATOM   2815 C CB    . ALA A 1 377 ? -46.495 43.902 -34.633 1.00 20.09 ? 518 ALA A CB    1 
ATOM   2816 N N     . GLN A 1 378 ? -44.269 45.090 -37.405 1.00 18.27 ? 519 GLN A N     1 
ATOM   2817 C CA    . GLN A 1 378 ? -43.890 44.703 -38.761 1.00 24.13 ? 519 GLN A CA    1 
ATOM   2818 C C     . GLN A 1 378 ? -43.260 43.324 -38.855 1.00 18.46 ? 519 GLN A C     1 
ATOM   2819 O O     . GLN A 1 378 ? -43.575 42.614 -39.819 1.00 24.87 ? 519 GLN A O     1 
ATOM   2820 C CB    . GLN A 1 378 ? -42.945 45.744 -39.363 1.00 23.05 ? 519 GLN A CB    1 
ATOM   2821 C CG    . GLN A 1 378 ? -43.584 47.089 -39.573 1.00 25.72 ? 519 GLN A CG    1 
ATOM   2822 C CD    . GLN A 1 378 ? -42.597 48.098 -40.104 1.00 28.57 ? 519 GLN A CD    1 
ATOM   2823 O OE1   . GLN A 1 378 ? -42.022 48.859 -39.340 1.00 30.32 ? 519 GLN A OE1   1 
ATOM   2824 N NE2   . GLN A 1 378 ? -42.391 48.108 -41.409 1.00 30.10 ? 519 GLN A NE2   1 
ATOM   2825 N N     . PRO A 1 379 ? -42.367 42.888 -37.955 1.00 21.26 ? 520 PRO A N     1 
ATOM   2826 C CA    . PRO A 1 379 ? -41.725 41.582 -38.189 1.00 24.35 ? 520 PRO A CA    1 
ATOM   2827 C C     . PRO A 1 379 ? -42.704 40.421 -38.209 1.00 24.73 ? 520 PRO A C     1 
ATOM   2828 O O     . PRO A 1 379 ? -42.603 39.561 -39.094 1.00 23.10 ? 520 PRO A O     1 
ATOM   2829 C CB    . PRO A 1 379 ? -40.716 41.483 -37.036 1.00 23.12 ? 520 PRO A CB    1 
ATOM   2830 C CG    . PRO A 1 379 ? -40.322 42.913 -36.809 1.00 23.44 ? 520 PRO A CG    1 
ATOM   2831 C CD    . PRO A 1 379 ? -41.669 43.629 -36.889 1.00 22.21 ? 520 PRO A CD    1 
ATOM   2832 N N     . ILE A 1 380 ? -43.671 40.380 -37.286 1.00 23.05 ? 521 ILE A N     1 
ATOM   2833 C CA    . ILE A 1 380 ? -44.632 39.279 -37.296 1.00 24.03 ? 521 ILE A CA    1 
ATOM   2834 C C     . ILE A 1 380 ? -45.490 39.323 -38.555 1.00 23.44 ? 521 ILE A C     1 
ATOM   2835 O O     . ILE A 1 380 ? -45.820 38.278 -39.128 1.00 25.94 ? 521 ILE A O     1 
ATOM   2836 C CB    . ILE A 1 380 ? -45.487 39.271 -36.012 1.00 21.57 ? 521 ILE A CB    1 
ATOM   2837 C CG1   . ILE A 1 380 ? -46.317 37.979 -35.945 1.00 22.77 ? 521 ILE A CG1   1 
ATOM   2838 C CG2   . ILE A 1 380 ? -46.419 40.472 -35.943 1.00 18.87 ? 521 ILE A CG2   1 
ATOM   2839 C CD1   . ILE A 1 380 ? -45.510 36.691 -36.033 1.00 23.52 ? 521 ILE A CD1   1 
ATOM   2840 N N     . LEU A 1 381 ? -45.841 40.523 -39.030 1.00 21.03 ? 522 LEU A N     1 
ATOM   2841 C CA    . LEU A 1 381 ? -46.646 40.590 -40.249 1.00 25.52 ? 522 LEU A CA    1 
ATOM   2842 C C     . LEU A 1 381 ? -45.842 40.134 -41.459 1.00 27.39 ? 522 LEU A C     1 
ATOM   2843 O O     . LEU A 1 381 ? -46.367 39.439 -42.334 1.00 27.89 ? 522 LEU A O     1 
ATOM   2844 C CB    . LEU A 1 381 ? -47.188 42.002 -40.460 1.00 23.00 ? 522 LEU A CB    1 
ATOM   2845 C CG    . LEU A 1 381 ? -48.280 42.468 -39.482 1.00 27.67 ? 522 LEU A CG    1 
ATOM   2846 C CD1   . LEU A 1 381 ? -49.128 43.557 -40.111 1.00 25.20 ? 522 LEU A CD1   1 
ATOM   2847 C CD2   . LEU A 1 381 ? -49.163 41.311 -39.009 1.00 22.35 ? 522 LEU A CD2   1 
ATOM   2848 N N     . ARG A 1 382 ? -44.563 40.496 -41.520 1.00 27.15 ? 523 ARG A N     1 
ATOM   2849 C CA    . ARG A 1 382 ? -43.725 40.009 -42.613 1.00 27.01 ? 523 ARG A CA    1 
ATOM   2850 C C     . ARG A 1 382 ? -43.555 38.497 -42.545 1.00 28.41 ? 523 ARG A C     1 
ATOM   2851 O O     . ARG A 1 382 ? -43.531 37.824 -43.584 1.00 29.31 ? 523 ARG A O     1 
ATOM   2852 C CB    . ARG A 1 382 ? -42.367 40.694 -42.582 1.00 28.36 ? 523 ARG A CB    1 
ATOM   2853 C CG    . ARG A 1 382 ? -42.435 42.189 -42.789 1.00 31.94 ? 523 ARG A CG    1 
ATOM   2854 C CD    . ARG A 1 382 ? -41.099 42.665 -43.311 1.00 47.20 ? 523 ARG A CD    1 
ATOM   2855 N NE    . ARG A 1 382 ? -40.878 44.086 -43.086 1.00 41.15 ? 523 ARG A NE    1 
ATOM   2856 C CZ    . ARG A 1 382 ? -40.450 44.595 -41.940 1.00 39.56 ? 523 ARG A CZ    1 
ATOM   2857 N NH1   . ARG A 1 382 ? -40.199 43.820 -40.891 1.00 30.48 ? 523 ARG A NH1   1 
ATOM   2858 N NH2   . ARG A 1 382 ? -40.271 45.914 -41.840 1.00 38.03 ? 523 ARG A NH2   1 
ATOM   2859 N N     . ARG A 1 383 ? -43.446 37.947 -41.332 1.00 26.68 ? 524 ARG A N     1 
ATOM   2860 C CA    . ARG A 1 383 ? -43.400 36.497 -41.182 1.00 27.76 ? 524 ARG A CA    1 
ATOM   2861 C C     . ARG A 1 383 ? -44.656 35.851 -41.750 1.00 33.25 ? 524 ARG A C     1 
ATOM   2862 O O     . ARG A 1 383 ? -44.592 34.738 -42.290 1.00 34.47 ? 524 ARG A O     1 
ATOM   2863 C CB    . ARG A 1 383 ? -43.207 36.130 -39.704 1.00 27.52 ? 524 ARG A CB    1 
ATOM   2864 C CG    . ARG A 1 383 ? -43.618 34.703 -39.307 1.00 29.28 ? 524 ARG A CG    1 
ATOM   2865 C CD    . ARG A 1 383 ? -42.664 33.659 -39.892 1.00 28.45 ? 524 ARG A CD    1 
ATOM   2866 N NE    . ARG A 1 383 ? -42.965 32.319 -39.398 1.00 31.58 ? 524 ARG A NE    1 
ATOM   2867 C CZ    . ARG A 1 383 ? -43.825 31.491 -39.977 1.00 34.33 ? 524 ARG A CZ    1 
ATOM   2868 N NH1   . ARG A 1 383 ? -44.492 31.841 -41.066 1.00 32.78 ? 524 ARG A NH1   1 
ATOM   2869 N NH2   . ARG A 1 383 ? -44.027 30.287 -39.446 1.00 31.22 ? 524 ARG A NH2   1 
ATOM   2870 N N     . MET A 1 384 ? -45.801 36.538 -41.655 1.00 27.60 ? 525 MET A N     1 
ATOM   2871 C CA    . MET A 1 384 ? -47.035 36.062 -42.271 1.00 30.84 ? 525 MET A CA    1 
ATOM   2872 C C     . MET A 1 384 ? -47.138 36.432 -43.752 1.00 29.31 ? 525 MET A C     1 
ATOM   2873 O O     . MET A 1 384 ? -48.184 36.205 -44.358 1.00 31.76 ? 525 MET A O     1 
ATOM   2874 C CB    . MET A 1 384 ? -48.254 36.614 -41.517 1.00 30.53 ? 525 MET A CB    1 
ATOM   2875 C CG    . MET A 1 384 ? -48.398 36.097 -40.089 1.00 32.53 ? 525 MET A CG    1 
ATOM   2876 S SD    . MET A 1 384 ? -48.252 34.291 -40.053 1.00 46.99 ? 525 MET A SD    1 
ATOM   2877 C CE    . MET A 1 384 ? -47.545 33.974 -38.448 1.00 32.89 ? 525 MET A CE    1 
ATOM   2878 N N     . GLY A 1 385 ? -46.098 37.015 -44.339 1.00 30.54 ? 526 GLY A N     1 
ATOM   2879 C CA    . GLY A 1 385 ? -46.135 37.376 -45.744 1.00 27.53 ? 526 GLY A CA    1 
ATOM   2880 C C     . GLY A 1 385 ? -46.964 38.599 -46.066 1.00 33.41 ? 526 GLY A C     1 
ATOM   2881 O O     . GLY A 1 385 ? -47.500 38.693 -47.174 1.00 31.08 ? 526 GLY A O     1 
ATOM   2882 N N     . LEU A 1 386 ? -47.073 39.552 -45.137 1.00 29.15 ? 527 LEU A N     1 
ATOM   2883 C CA    . LEU A 1 386 ? -47.974 40.687 -45.290 1.00 29.04 ? 527 LEU A CA    1 
ATOM   2884 C C     . LEU A 1 386 ? -47.322 41.969 -44.799 1.00 31.21 ? 527 LEU A C     1 
ATOM   2885 O O     . LEU A 1 386 ? -46.456 41.956 -43.919 1.00 27.61 ? 527 LEU A O     1 
ATOM   2886 C CB    . LEU A 1 386 ? -49.282 40.497 -44.510 1.00 29.38 ? 527 LEU A CB    1 
ATOM   2887 C CG    . LEU A 1 386 ? -50.154 39.337 -44.970 1.00 31.88 ? 527 LEU A CG    1 
ATOM   2888 C CD1   . LEU A 1 386 ? -51.070 38.900 -43.836 1.00 28.28 ? 527 LEU A CD1   1 
ATOM   2889 C CD2   . LEU A 1 386 ? -50.940 39.718 -46.230 1.00 30.90 ? 527 LEU A CD2   1 
ATOM   2890 N N     . GLU A 1 387 ? -47.782 43.083 -45.363 1.00 30.04 ? 528 GLU A N     1 
ATOM   2891 C CA    . GLU A 1 387 ? -47.382 44.410 -44.927 1.00 31.35 ? 528 GLU A CA    1 
ATOM   2892 C C     . GLU A 1 387 ? -48.360 45.015 -43.924 1.00 27.28 ? 528 GLU A C     1 
ATOM   2893 O O     . GLU A 1 387 ? -47.979 45.909 -43.164 1.00 25.03 ? 528 GLU A O     1 
ATOM   2894 C CB    . GLU A 1 387 ? -47.264 45.344 -46.141 1.00 35.52 ? 528 GLU A CB    1 
ATOM   2895 C CG    . GLU A 1 387 ? -46.039 45.117 -47.047 1.00 36.30 ? 528 GLU A CG    1 
ATOM   2896 C CD    . GLU A 1 387 ? -44.718 45.117 -46.278 1.00 55.12 ? 528 GLU A CD    1 
ATOM   2897 O OE1   . GLU A 1 387 ? -44.065 44.051 -46.215 1.00 59.42 ? 528 GLU A OE1   1 
ATOM   2898 O OE2   . GLU A 1 387 ? -44.339 46.179 -45.718 1.00 58.82 ? 528 GLU A OE2   1 
ATOM   2899 N N     . ALA A 1 388 ? -49.605 44.549 -43.903 1.00 27.01 ? 529 ALA A N     1 
ATOM   2900 C CA    . ALA A 1 388 ? -50.628 45.147 -43.053 1.00 26.54 ? 529 ALA A CA    1 
ATOM   2901 C C     . ALA A 1 388 ? -51.771 44.159 -42.903 1.00 24.67 ? 529 ALA A C     1 
ATOM   2902 O O     . ALA A 1 388 ? -51.918 43.230 -43.699 1.00 25.02 ? 529 ALA A O     1 
ATOM   2903 C CB    . ALA A 1 388 ? -51.140 46.474 -43.632 1.00 22.40 ? 529 ALA A CB    1 
ATOM   2904 N N     . THR A 1 389 ? -52.568 44.356 -41.855 1.00 22.15 ? 530 THR A N     1 
ATOM   2905 C CA    . THR A 1 389 ? -53.832 43.646 -41.708 1.00 22.61 ? 530 THR A CA    1 
ATOM   2906 C C     . THR A 1 389 ? -54.894 44.629 -41.237 1.00 20.08 ? 530 THR A C     1 
ATOM   2907 O O     . THR A 1 389 ? -54.576 45.708 -40.713 1.00 22.56 ? 530 THR A O     1 
ATOM   2908 C CB    . THR A 1 389 ? -53.752 42.464 -40.711 1.00 21.85 ? 530 THR A CB    1 
ATOM   2909 O OG1   . THR A 1 389 ? -53.542 42.950 -39.378 1.00 20.51 ? 530 THR A OG1   1 
ATOM   2910 C CG2   . THR A 1 389 ? -52.640 41.509 -41.062 1.00 20.95 ? 530 THR A CG2   1 
ATOM   2911 N N     . VAL A 1 390 ? -56.163 44.260 -41.475 1.00 21.51 ? 531 VAL A N     1 
ATOM   2912 C CA    . VAL A 1 390 ? -57.305 44.878 -40.801 1.00 18.55 ? 531 VAL A CA    1 
ATOM   2913 C C     . VAL A 1 390 ? -57.482 44.173 -39.465 1.00 19.50 ? 531 VAL A C     1 
ATOM   2914 O O     . VAL A 1 390 ? -57.534 42.942 -39.415 1.00 19.69 ? 531 VAL A O     1 
ATOM   2915 C CB    . VAL A 1 390 ? -58.579 44.758 -41.658 1.00 21.17 ? 531 VAL A CB    1 
ATOM   2916 C CG1   . VAL A 1 390 ? -59.716 45.624 -41.090 1.00 19.00 ? 531 VAL A CG1   1 
ATOM   2917 C CG2   . VAL A 1 390 ? -58.292 45.100 -43.120 1.00 21.33 ? 531 VAL A CG2   1 
ATOM   2918 N N     . ARG A 1 391 ? -57.542 44.932 -38.371 1.00 18.28 ? 532 ARG A N     1 
ATOM   2919 C CA    . ARG A 1 391 ? -57.476 44.343 -37.030 1.00 19.29 ? 532 ARG A CA    1 
ATOM   2920 C C     . ARG A 1 391 ? -58.569 44.881 -36.119 1.00 19.76 ? 532 ARG A C     1 
ATOM   2921 O O     . ARG A 1 391 ? -58.323 45.765 -35.289 1.00 21.37 ? 532 ARG A O     1 
ATOM   2922 C CB    . ARG A 1 391 ? -56.109 44.578 -36.388 1.00 20.87 ? 532 ARG A CB    1 
ATOM   2923 C CG    . ARG A 1 391 ? -55.905 43.758 -35.112 1.00 23.23 ? 532 ARG A CG    1 
ATOM   2924 C CD    . ARG A 1 391 ? -54.892 44.374 -34.162 1.00 17.77 ? 532 ARG A CD    1 
ATOM   2925 N NE    . ARG A 1 391 ? -55.160 45.774 -33.859 1.00 20.20 ? 532 ARG A NE    1 
ATOM   2926 C CZ    . ARG A 1 391 ? -54.295 46.572 -33.242 1.00 20.89 ? 532 ARG A CZ    1 
ATOM   2927 N NH1   . ARG A 1 391 ? -53.106 46.137 -32.855 1.00 19.07 ? 532 ARG A NH1   1 
ATOM   2928 N NH2   . ARG A 1 391 ? -54.625 47.840 -33.013 1.00 22.72 ? 532 ARG A NH2   1 
ATOM   2929 N N     . PRO A 1 392 ? -59.783 44.349 -36.221 1.00 19.54 ? 533 PRO A N     1 
ATOM   2930 C CA    . PRO A 1 392 ? -60.730 44.507 -35.117 1.00 18.79 ? 533 PRO A CA    1 
ATOM   2931 C C     . PRO A 1 392 ? -60.170 43.825 -33.878 1.00 22.96 ? 533 PRO A C     1 
ATOM   2932 O O     . PRO A 1 392 ? -59.485 42.797 -33.966 1.00 18.90 ? 533 PRO A O     1 
ATOM   2933 C CB    . PRO A 1 392 ? -61.991 43.804 -35.630 1.00 22.24 ? 533 PRO A CB    1 
ATOM   2934 C CG    . PRO A 1 392 ? -61.445 42.755 -36.574 1.00 20.13 ? 533 PRO A CG    1 
ATOM   2935 C CD    . PRO A 1 392 ? -60.308 43.460 -37.270 1.00 18.49 ? 533 PRO A CD    1 
ATOM   2936 N N     . SER A 1 393 ? -60.430 44.429 -32.720 1.00 18.28 ? 534 SER A N     1 
ATOM   2937 C CA    . SER A 1 393 ? -60.030 43.847 -31.447 1.00 21.04 ? 534 SER A CA    1 
ATOM   2938 C C     . SER A 1 393 ? -61.118 44.156 -30.431 1.00 20.73 ? 534 SER A C     1 
ATOM   2939 O O     . SER A 1 393 ? -61.586 45.296 -30.348 1.00 21.53 ? 534 SER A O     1 
ATOM   2940 C CB    . SER A 1 393 ? -58.667 44.376 -30.969 1.00 20.29 ? 534 SER A CB    1 
ATOM   2941 O OG    . SER A 1 393 ? -58.582 45.800 -31.028 1.00 21.06 ? 534 SER A OG    1 
ATOM   2942 N N     . PHE A 1 394 ? -61.528 43.140 -29.684 1.00 20.24 ? 535 PHE A N     1 
ATOM   2943 C CA    . PHE A 1 394 ? -62.729 43.198 -28.862 1.00 21.49 ? 535 PHE A CA    1 
ATOM   2944 C C     . PHE A 1 394 ? -62.390 43.459 -27.399 1.00 21.51 ? 535 PHE A C     1 
ATOM   2945 O O     . PHE A 1 394 ? -61.332 43.059 -26.904 1.00 23.59 ? 535 PHE A O     1 
ATOM   2946 C CB    . PHE A 1 394 ? -63.533 41.892 -28.974 1.00 23.70 ? 535 PHE A CB    1 
ATOM   2947 C CG    . PHE A 1 394 ? -63.855 41.495 -30.396 1.00 24.17 ? 535 PHE A CG    1 
ATOM   2948 C CD1   . PHE A 1 394 ? -64.558 42.355 -31.228 1.00 22.72 ? 535 PHE A CD1   1 
ATOM   2949 C CD2   . PHE A 1 394 ? -63.435 40.273 -30.902 1.00 23.12 ? 535 PHE A CD2   1 
ATOM   2950 C CE1   . PHE A 1 394 ? -64.848 42.000 -32.548 1.00 24.44 ? 535 PHE A CE1   1 
ATOM   2951 C CE2   . PHE A 1 394 ? -63.705 39.913 -32.215 1.00 25.99 ? 535 PHE A CE2   1 
ATOM   2952 C CZ    . PHE A 1 394 ? -64.419 40.782 -33.046 1.00 25.22 ? 535 PHE A CZ    1 
ATOM   2953 N N     . ALA A 1 395 ? -63.302 44.155 -26.720 1.00 19.47 ? 536 ALA A N     1 
ATOM   2954 C CA    . ALA A 1 395 ? -63.293 44.321 -25.273 1.00 20.76 ? 536 ALA A CA    1 
ATOM   2955 C C     . ALA A 1 395 ? -64.667 43.936 -24.735 1.00 20.79 ? 536 ALA A C     1 
ATOM   2956 O O     . ALA A 1 395 ? -65.597 43.648 -25.500 1.00 17.72 ? 536 ALA A O     1 
ATOM   2957 C CB    . ALA A 1 395 ? -62.926 45.757 -24.871 1.00 18.14 ? 536 ALA A CB    1 
ATOM   2958 N N     . PHE A 1 396 ? -64.796 43.926 -23.402 1.00 16.14 ? 537 PHE A N     1 
ATOM   2959 C CA    . PHE A 1 396 ? -66.006 43.392 -22.784 1.00 18.70 ? 537 PHE A CA    1 
ATOM   2960 C C     . PHE A 1 396 ? -67.208 44.331 -22.856 1.00 18.71 ? 537 PHE A C     1 
ATOM   2961 O O     . PHE A 1 396 ? -68.303 43.915 -22.463 1.00 19.60 ? 537 PHE A O     1 
ATOM   2962 C CB    . PHE A 1 396 ? -65.746 42.994 -21.316 1.00 20.68 ? 537 PHE A CB    1 
ATOM   2963 C CG    . PHE A 1 396 ? -65.342 44.139 -20.416 1.00 19.68 ? 537 PHE A CG    1 
ATOM   2964 C CD1   . PHE A 1 396 ? -64.014 44.491 -20.273 1.00 19.47 ? 537 PHE A CD1   1 
ATOM   2965 C CD2   . PHE A 1 396 ? -66.290 44.831 -19.685 1.00 22.16 ? 537 PHE A CD2   1 
ATOM   2966 C CE1   . PHE A 1 396 ? -63.631 45.539 -19.443 1.00 21.79 ? 537 PHE A CE1   1 
ATOM   2967 C CE2   . PHE A 1 396 ? -65.920 45.877 -18.855 1.00 25.01 ? 537 PHE A CE2   1 
ATOM   2968 C CZ    . PHE A 1 396 ? -64.586 46.228 -18.727 1.00 21.34 ? 537 PHE A CZ    1 
ATOM   2969 N N     . TYR A 1 397 ? -67.057 45.562 -23.359 1.00 17.88 ? 538 TYR A N     1 
ATOM   2970 C CA    . TYR A 1 397 ? -68.233 46.372 -23.674 1.00 18.85 ? 538 TYR A CA    1 
ATOM   2971 C C     . TYR A 1 397 ? -68.696 46.210 -25.121 1.00 19.36 ? 538 TYR A C     1 
ATOM   2972 O O     . TYR A 1 397 ? -69.667 46.865 -25.515 1.00 19.35 ? 538 TYR A O     1 
ATOM   2973 C CB    . TYR A 1 397 ? -67.988 47.865 -23.361 1.00 15.70 ? 538 TYR A CB    1 
ATOM   2974 C CG    . TYR A 1 397 ? -66.652 48.438 -23.812 1.00 18.63 ? 538 TYR A CG    1 
ATOM   2975 C CD1   . TYR A 1 397 ? -66.217 48.323 -25.132 1.00 17.24 ? 538 TYR A CD1   1 
ATOM   2976 C CD2   . TYR A 1 397 ? -65.845 49.134 -22.921 1.00 18.75 ? 538 TYR A CD2   1 
ATOM   2977 C CE1   . TYR A 1 397 ? -65.001 48.862 -25.532 1.00 19.96 ? 538 TYR A CE1   1 
ATOM   2978 C CE2   . TYR A 1 397 ? -64.636 49.683 -23.320 1.00 15.90 ? 538 TYR A CE2   1 
ATOM   2979 C CZ    . TYR A 1 397 ? -64.215 49.541 -24.614 1.00 17.92 ? 538 TYR A CZ    1 
ATOM   2980 O OH    . TYR A 1 397 ? -63.000 50.074 -24.997 1.00 16.62 ? 538 TYR A OH    1 
ATOM   2981 N N     . ASN A 1 398 ? -68.032 45.369 -25.923 1.00 17.10 ? 539 ASN A N     1 
ATOM   2982 C CA    . ASN A 1 398 ? -68.505 45.092 -27.272 1.00 18.30 ? 539 ASN A CA    1 
ATOM   2983 C C     . ASN A 1 398 ? -69.598 44.024 -27.247 1.00 17.74 ? 539 ASN A C     1 
ATOM   2984 O O     . ASN A 1 398 ? -69.659 43.196 -26.335 1.00 20.13 ? 539 ASN A O     1 
ATOM   2985 C CB    . ASN A 1 398 ? -67.348 44.635 -28.173 1.00 18.58 ? 539 ASN A CB    1 
ATOM   2986 C CG    . ASN A 1 398 ? -66.343 45.743 -28.434 1.00 22.43 ? 539 ASN A CG    1 
ATOM   2987 O OD1   . ASN A 1 398 ? -65.144 45.582 -28.186 1.00 18.29 ? 539 ASN A OD1   1 
ATOM   2988 N ND2   . ASN A 1 398 ? -66.832 46.890 -28.902 1.00 17.47 ? 539 ASN A ND2   1 
ATOM   2989 N N     . THR A 1 399 ? -70.459 44.039 -28.268 1.00 18.13 ? 540 THR A N     1 
ATOM   2990 C CA    . THR A 1 399 ? -71.619 43.154 -28.321 1.00 20.60 ? 540 THR A CA    1 
ATOM   2991 C C     . THR A 1 399 ? -71.594 42.264 -29.559 1.00 25.62 ? 540 THR A C     1 
ATOM   2992 O O     . THR A 1 399 ? -70.923 42.553 -30.563 1.00 20.00 ? 540 THR A O     1 
ATOM   2993 C CB    . THR A 1 399 ? -72.946 43.937 -28.321 1.00 24.26 ? 540 THR A CB    1 
ATOM   2994 O OG1   . THR A 1 399 ? -73.090 44.656 -29.554 1.00 22.72 ? 540 THR A OG1   1 
ATOM   2995 C CG2   . THR A 1 399 ? -73.028 44.901 -27.137 1.00 20.51 ? 540 THR A CG2   1 
ATOM   2996 N N     . PHE A 1 400 ? -72.371 41.178 -29.485 1.00 19.76 ? 541 PHE A N     1 
ATOM   2997 C CA    . PHE A 1 400 ? -72.554 40.327 -30.655 1.00 21.93 ? 541 PHE A CA    1 
ATOM   2998 C C     . PHE A 1 400 ? -73.257 41.081 -31.788 1.00 23.57 ? 541 PHE A C     1 
ATOM   2999 O O     . PHE A 1 400 ? -72.951 40.867 -32.968 1.00 22.22 ? 541 PHE A O     1 
ATOM   3000 C CB    . PHE A 1 400 ? -73.319 39.058 -30.257 1.00 22.44 ? 541 PHE A CB    1 
ATOM   3001 C CG    . PHE A 1 400 ? -72.558 38.174 -29.278 1.00 22.63 ? 541 PHE A CG    1 
ATOM   3002 C CD1   . PHE A 1 400 ? -72.696 38.344 -27.907 1.00 22.07 ? 541 PHE A CD1   1 
ATOM   3003 C CD2   . PHE A 1 400 ? -71.682 37.198 -29.739 1.00 23.22 ? 541 PHE A CD2   1 
ATOM   3004 C CE1   . PHE A 1 400 ? -71.985 37.545 -27.016 1.00 22.95 ? 541 PHE A CE1   1 
ATOM   3005 C CE2   . PHE A 1 400 ? -70.963 36.388 -28.853 1.00 24.25 ? 541 PHE A CE2   1 
ATOM   3006 C CZ    . PHE A 1 400 ? -71.114 36.561 -27.492 1.00 25.23 ? 541 PHE A CZ    1 
ATOM   3007 N N     . ASP A 1 401 ? -74.197 41.972 -31.450 1.00 23.08 ? 542 ASP A N     1 
ATOM   3008 C CA    . ASP A 1 401 ? -74.871 42.787 -32.460 1.00 22.93 ? 542 ASP A CA    1 
ATOM   3009 C C     . ASP A 1 401 ? -73.873 43.643 -33.245 1.00 25.70 ? 542 ASP A C     1 
ATOM   3010 O O     . ASP A 1 401 ? -73.963 43.750 -34.480 1.00 24.16 ? 542 ASP A O     1 
ATOM   3011 C CB    . ASP A 1 401 ? -75.911 43.674 -31.778 1.00 25.39 ? 542 ASP A CB    1 
ATOM   3012 C CG    . ASP A 1 401 ? -77.218 42.939 -31.489 1.00 32.89 ? 542 ASP A CG    1 
ATOM   3013 O OD1   . ASP A 1 401 ? -77.258 41.689 -31.627 1.00 31.69 ? 542 ASP A OD1   1 
ATOM   3014 O OD2   . ASP A 1 401 ? -78.180 43.602 -31.054 1.00 33.16 ? 542 ASP A OD2   1 
ATOM   3015 N N     . GLU A 1 402 ? -72.934 44.285 -32.536 1.00 21.55 ? 543 GLU A N     1 
ATOM   3016 C CA    . GLU A 1 402 ? -71.883 45.057 -33.196 1.00 24.67 ? 543 GLU A CA    1 
ATOM   3017 C C     . GLU A 1 402 ? -71.067 44.180 -34.136 1.00 19.83 ? 543 GLU A C     1 
ATOM   3018 O O     . GLU A 1 402 ? -70.710 44.603 -35.246 1.00 22.49 ? 543 GLU A O     1 
ATOM   3019 C CB    . GLU A 1 402 ? -70.969 45.705 -32.148 1.00 20.53 ? 543 GLU A CB    1 
ATOM   3020 C CG    . GLU A 1 402 ? -71.614 46.804 -31.318 1.00 22.49 ? 543 GLU A CG    1 
ATOM   3021 C CD    . GLU A 1 402 ? -70.652 47.374 -30.282 1.00 23.78 ? 543 GLU A CD    1 
ATOM   3022 O OE1   . GLU A 1 402 ? -69.803 46.605 -29.788 1.00 20.33 ? 543 GLU A OE1   1 
ATOM   3023 O OE2   . GLU A 1 402 ? -70.736 48.588 -29.972 1.00 23.28 ? 543 GLU A OE2   1 
ATOM   3024 N N     . ILE A 1 403 ? -70.754 42.955 -33.702 1.00 19.65 ? 544 ILE A N     1 
ATOM   3025 C CA    . ILE A 1 403 ? -70.047 42.020 -34.567 1.00 20.05 ? 544 ILE A CA    1 
ATOM   3026 C C     . ILE A 1 403 ? -70.860 41.742 -35.828 1.00 22.53 ? 544 ILE A C     1 
ATOM   3027 O O     . ILE A 1 403 ? -70.307 41.659 -36.933 1.00 22.41 ? 544 ILE A O     1 
ATOM   3028 C CB    . ILE A 1 403 ? -69.716 40.730 -33.797 1.00 21.81 ? 544 ILE A CB    1 
ATOM   3029 C CG1   . ILE A 1 403 ? -68.632 41.007 -32.744 1.00 18.98 ? 544 ILE A CG1   1 
ATOM   3030 C CG2   . ILE A 1 403 ? -69.270 39.622 -34.773 1.00 23.92 ? 544 ILE A CG2   1 
ATOM   3031 C CD1   . ILE A 1 403 ? -68.391 39.854 -31.783 1.00 21.48 ? 544 ILE A CD1   1 
ATOM   3032 N N     . ASP A 1 404 ? -72.183 41.607 -35.687 1.00 22.33 ? 545 ASP A N     1 
ATOM   3033 C CA    . ASP A 1 404 ? -73.038 41.373 -36.848 1.00 24.28 ? 545 ASP A CA    1 
ATOM   3034 C C     . ASP A 1 404 ? -72.948 42.529 -37.835 1.00 22.86 ? 545 ASP A C     1 
ATOM   3035 O O     . ASP A 1 404 ? -72.846 42.322 -39.051 1.00 26.65 ? 545 ASP A O     1 
ATOM   3036 C CB    . ASP A 1 404 ? -74.488 41.170 -36.404 1.00 25.49 ? 545 ASP A CB    1 
ATOM   3037 C CG    . ASP A 1 404 ? -74.702 39.851 -35.696 1.00 26.13 ? 545 ASP A CG    1 
ATOM   3038 O OD1   . ASP A 1 404 ? -73.837 38.966 -35.846 1.00 24.30 ? 545 ASP A OD1   1 
ATOM   3039 O OD2   . ASP A 1 404 ? -75.737 39.698 -34.996 1.00 26.29 ? 545 ASP A OD2   1 
ATOM   3040 N N     . VAL A 1 405 ? -73.019 43.761 -37.325 1.00 24.58 ? 546 VAL A N     1 
ATOM   3041 C CA    . VAL A 1 405 ? -72.886 44.923 -38.203 1.00 24.72 ? 546 VAL A CA    1 
ATOM   3042 C C     . VAL A 1 405 ? -71.552 44.866 -38.948 1.00 25.66 ? 546 VAL A C     1 
ATOM   3043 O O     . VAL A 1 405 ? -71.484 45.100 -40.166 1.00 27.41 ? 546 VAL A O     1 
ATOM   3044 C CB    . VAL A 1 405 ? -73.037 46.228 -37.398 1.00 29.39 ? 546 VAL A CB    1 
ATOM   3045 C CG1   . VAL A 1 405 ? -72.804 47.438 -38.304 1.00 28.96 ? 546 VAL A CG1   1 
ATOM   3046 C CG2   . VAL A 1 405 ? -74.430 46.313 -36.769 1.00 25.57 ? 546 VAL A CG2   1 
ATOM   3047 N N     . PHE A 1 406 ? -70.481 44.512 -38.232 1.00 22.42 ? 547 PHE A N     1 
ATOM   3048 C CA    . PHE A 1 406 ? -69.150 44.449 -38.837 1.00 23.11 ? 547 PHE A CA    1 
ATOM   3049 C C     . PHE A 1 406 ? -69.067 43.361 -39.916 1.00 23.30 ? 547 PHE A C     1 
ATOM   3050 O O     . PHE A 1 406 ? -68.490 43.580 -40.993 1.00 24.55 ? 547 PHE A O     1 
ATOM   3051 C CB    . PHE A 1 406 ? -68.123 44.249 -37.721 1.00 19.22 ? 547 PHE A CB    1 
ATOM   3052 C CG    . PHE A 1 406 ? -66.830 43.645 -38.162 1.00 24.49 ? 547 PHE A CG    1 
ATOM   3053 C CD1   . PHE A 1 406 ? -65.840 44.429 -38.740 1.00 26.21 ? 547 PHE A CD1   1 
ATOM   3054 C CD2   . PHE A 1 406 ? -66.586 42.296 -37.975 1.00 21.93 ? 547 PHE A CD2   1 
ATOM   3055 C CE1   . PHE A 1 406 ? -64.640 43.875 -39.141 1.00 24.50 ? 547 PHE A CE1   1 
ATOM   3056 C CE2   . PHE A 1 406 ? -65.386 41.739 -38.373 1.00 23.56 ? 547 PHE A CE2   1 
ATOM   3057 C CZ    . PHE A 1 406 ? -64.415 42.528 -38.961 1.00 23.50 ? 547 PHE A CZ    1 
ATOM   3058 N N     . ILE A 1 407 ? -69.650 42.188 -39.653 1.00 23.94 ? 548 ILE A N     1 
ATOM   3059 C CA    . ILE A 1 407 ? -69.647 41.105 -40.638 1.00 24.13 ? 548 ILE A CA    1 
ATOM   3060 C C     . ILE A 1 407 ? -70.398 41.524 -41.898 1.00 31.10 ? 548 ILE A C     1 
ATOM   3061 O O     . ILE A 1 407 ? -69.930 41.295 -43.023 1.00 30.20 ? 548 ILE A O     1 
ATOM   3062 C CB    . ILE A 1 407 ? -70.244 39.817 -40.044 1.00 28.20 ? 548 ILE A CB    1 
ATOM   3063 C CG1   . ILE A 1 407 ? -69.432 39.343 -38.834 1.00 22.75 ? 548 ILE A CG1   1 
ATOM   3064 C CG2   . ILE A 1 407 ? -70.344 38.732 -41.117 1.00 30.47 ? 548 ILE A CG2   1 
ATOM   3065 C CD1   . ILE A 1 407 ? -68.092 38.758 -39.177 1.00 23.82 ? 548 ILE A CD1   1 
ATOM   3066 N N     . ASP A 1 408 ? -71.590 42.114 -41.731 1.00 28.69 ? 549 ASP A N     1 
ATOM   3067 C CA    . ASP A 1 408 ? -72.336 42.596 -42.893 1.00 32.96 ? 549 ASP A CA    1 
ATOM   3068 C C     . ASP A 1 408 ? -71.532 43.618 -43.684 1.00 33.16 ? 549 ASP A C     1 
ATOM   3069 O O     . ASP A 1 408 ? -71.546 43.602 -44.922 1.00 32.90 ? 549 ASP A O     1 
ATOM   3070 C CB    . ASP A 1 408 ? -73.672 43.209 -42.476 1.00 29.25 ? 549 ASP A CB    1 
ATOM   3071 C CG    . ASP A 1 408 ? -74.686 42.171 -42.042 1.00 40.97 ? 549 ASP A CG    1 
ATOM   3072 O OD1   . ASP A 1 408 ? -74.503 40.984 -42.403 1.00 47.84 ? 549 ASP A OD1   1 
ATOM   3073 O OD2   . ASP A 1 408 ? -75.674 42.546 -41.363 1.00 43.53 ? 549 ASP A OD2   1 
ATOM   3074 N N     . ALA A 1 409 ? -70.831 44.520 -42.986 1.00 27.36 ? 550 ALA A N     1 
ATOM   3075 C CA    . ALA A 1 409 ? -70.036 45.534 -43.673 1.00 28.54 ? 550 ALA A CA    1 
ATOM   3076 C C     . ALA A 1 409 ? -68.907 44.898 -44.488 1.00 30.36 ? 550 ALA A C     1 
ATOM   3077 O O     . ALA A 1 409 ? -68.684 45.260 -45.655 1.00 30.19 ? 550 ALA A O     1 
ATOM   3078 C CB    . ALA A 1 409 ? -69.477 46.531 -42.658 1.00 29.13 ? 550 ALA A CB    1 
ATOM   3079 N N     . VAL A 1 410 ? -68.170 43.961 -43.884 1.00 25.56 ? 551 VAL A N     1 
ATOM   3080 C CA    . VAL A 1 410 ? -67.085 43.304 -44.612 1.00 28.91 ? 551 VAL A CA    1 
ATOM   3081 C C     . VAL A 1 410 ? -67.639 42.551 -45.817 1.00 31.16 ? 551 VAL A C     1 
ATOM   3082 O O     . VAL A 1 410 ? -67.056 42.585 -46.905 1.00 28.62 ? 551 VAL A O     1 
ATOM   3083 C CB    . VAL A 1 410 ? -66.278 42.371 -43.689 1.00 27.76 ? 551 VAL A CB    1 
ATOM   3084 C CG1   . VAL A 1 410 ? -65.203 41.628 -44.500 1.00 23.72 ? 551 VAL A CG1   1 
ATOM   3085 C CG2   . VAL A 1 410 ? -65.636 43.159 -42.550 1.00 23.15 ? 551 VAL A CG2   1 
ATOM   3086 N N     . ARG A 1 411 ? -68.777 41.871 -45.642 1.00 29.22 ? 552 ARG A N     1 
ATOM   3087 C CA    . ARG A 1 411 ? -69.395 41.134 -46.742 1.00 34.40 ? 552 ARG A CA    1 
ATOM   3088 C C     . ARG A 1 411 ? -69.770 42.059 -47.893 1.00 35.55 ? 552 ARG A C     1 
ATOM   3089 O O     . ARG A 1 411 ? -69.539 41.735 -49.067 1.00 36.21 ? 552 ARG A O     1 
ATOM   3090 C CB    . ARG A 1 411 ? -70.639 40.394 -46.248 1.00 42.42 ? 552 ARG A CB    1 
ATOM   3091 C CG    . ARG A 1 411 ? -70.541 38.882 -46.372 1.00 44.42 ? 552 ARG A CG    1 
ATOM   3092 C CD    . ARG A 1 411 ? -71.837 38.174 -45.997 1.00 40.90 ? 552 ARG A CD    1 
ATOM   3093 N NE    . ARG A 1 411 ? -71.536 36.859 -45.446 1.00 41.26 ? 552 ARG A NE    1 
ATOM   3094 C CZ    . ARG A 1 411 ? -71.050 35.842 -46.146 1.00 45.69 ? 552 ARG A CZ    1 
ATOM   3095 N NH1   . ARG A 1 411 ? -70.895 35.915 -47.460 1.00 46.19 ? 552 ARG A NH1   1 
ATOM   3096 N NH2   . ARG A 1 411 ? -70.703 34.723 -45.510 1.00 40.24 ? 552 ARG A NH2   1 
ATOM   3097 N N     . ARG A 1 412 ? -70.362 43.209 -47.578 1.00 31.07 ? 553 ARG A N     1 
ATOM   3098 C CA    . ARG A 1 412 ? -70.696 44.170 -48.624 1.00 35.44 ? 553 ARG A CA    1 
ATOM   3099 C C     . ARG A 1 412 ? -69.444 44.694 -49.319 1.00 37.01 ? 553 ARG A C     1 
ATOM   3100 O O     . ARG A 1 412 ? -69.459 44.949 -50.529 1.00 34.70 ? 553 ARG A O     1 
ATOM   3101 C CB    . ARG A 1 412 ? -71.516 45.315 -48.034 1.00 35.33 ? 553 ARG A CB    1 
ATOM   3102 C CG    . ARG A 1 412 ? -72.964 44.918 -47.730 1.00 41.34 ? 553 ARG A CG    1 
ATOM   3103 C CD    . ARG A 1 412 ? -73.800 46.135 -47.385 1.00 46.60 ? 553 ARG A CD    1 
ATOM   3104 N NE    . ARG A 1 412 ? -73.188 46.919 -46.315 1.00 46.84 ? 553 ARG A NE    1 
ATOM   3105 C CZ    . ARG A 1 412 ? -73.414 46.737 -45.018 1.00 44.63 ? 553 ARG A CZ    1 
ATOM   3106 N NH1   . ARG A 1 412 ? -74.247 45.806 -44.583 1.00 45.98 ? 553 ARG A NH1   1 
ATOM   3107 N NH2   . ARG A 1 412 ? -72.800 47.520 -44.137 1.00 43.16 ? 553 ARG A NH2   1 
ATOM   3108 N N     . ILE A 1 413 ? -68.349 44.866 -48.578 1.00 33.29 ? 554 ILE A N     1 
ATOM   3109 C CA    . ILE A 1 413 ? -67.101 45.249 -49.234 1.00 35.03 ? 554 ILE A CA    1 
ATOM   3110 C C     . ILE A 1 413 ? -66.622 44.134 -50.158 1.00 37.61 ? 554 ILE A C     1 
ATOM   3111 O O     . ILE A 1 413 ? -66.187 44.388 -51.290 1.00 40.03 ? 554 ILE A O     1 
ATOM   3112 C CB    . ILE A 1 413 ? -66.032 45.626 -48.193 1.00 36.36 ? 554 ILE A CB    1 
ATOM   3113 C CG1   . ILE A 1 413 ? -66.426 46.905 -47.443 1.00 30.41 ? 554 ILE A CG1   1 
ATOM   3114 C CG2   . ILE A 1 413 ? -64.674 45.802 -48.857 1.00 32.24 ? 554 ILE A CG2   1 
ATOM   3115 C CD1   . ILE A 1 413 ? -65.678 47.084 -46.110 1.00 28.40 ? 554 ILE A CD1   1 
ATOM   3116 N N     . ALA A 1 414 ? -66.725 42.882 -49.711 1.00 36.11 ? 555 ALA A N     1 
ATOM   3117 C CA    . ALA A 1 414 ? -66.207 41.770 -50.501 1.00 35.61 ? 555 ALA A CA    1 
ATOM   3118 C C     . ALA A 1 414 ? -67.065 41.518 -51.730 1.00 45.17 ? 555 ALA A C     1 
ATOM   3119 O O     . ALA A 1 414 ? -66.551 41.105 -52.778 1.00 46.25 ? 555 ALA A O     1 
ATOM   3120 C CB    . ALA A 1 414 ? -66.116 40.508 -49.643 1.00 36.08 ? 555 ALA A CB    1 
ATOM   3121 N N     . GLU A 1 415 ? -68.372 41.745 -51.620 1.00 42.03 ? 556 GLU A N     1 
ATOM   3122 C CA    . GLU A 1 415 ? -69.255 41.639 -52.771 1.00 42.17 ? 556 GLU A CA    1 
ATOM   3123 C C     . GLU A 1 415 ? -69.209 42.950 -53.553 1.00 48.38 ? 556 GLU A C     1 
ATOM   3124 O O     . GLU A 1 415 ? -70.053 43.202 -54.414 1.00 56.91 ? 556 GLU A O     1 
ATOM   3125 C CB    . GLU A 1 415 ? -70.688 41.310 -52.336 1.00 42.81 ? 556 GLU A CB    1 
ATOM   3126 C CG    . GLU A 1 415 ? -70.858 39.887 -51.793 1.00 47.56 ? 556 GLU A CG    1 
ATOM   3127 C CD    . GLU A 1 415 ? -72.131 39.699 -50.959 1.00 60.76 ? 556 GLU A CD    1 
ATOM   3128 O OE1   . GLU A 1 415 ? -72.903 40.673 -50.791 1.00 58.41 ? 556 GLU A OE1   1 
ATOM   3129 O OE2   . GLU A 1 415 ? -72.355 38.569 -50.464 1.00 58.81 ? 556 GLU A OE2   1 
ATOM   3130 N N     . PHE B 1 15  ? -56.186 94.332 -12.177 1.00 41.34 ? 156 PHE B N     1 
ATOM   3131 C CA    . PHE B 1 15  ? -56.081 92.871 -12.191 1.00 45.53 ? 156 PHE B CA    1 
ATOM   3132 C C     . PHE B 1 15  ? -57.084 92.262 -11.231 1.00 43.23 ? 156 PHE B C     1 
ATOM   3133 O O     . PHE B 1 15  ? -56.954 92.384 -10.013 1.00 43.38 ? 156 PHE B O     1 
ATOM   3134 C CB    . PHE B 1 15  ? -54.670 92.400 -11.825 1.00 47.07 ? 156 PHE B CB    1 
ATOM   3135 C CG    . PHE B 1 15  ? -54.444 90.921 -12.051 1.00 39.69 ? 156 PHE B CG    1 
ATOM   3136 C CD1   . PHE B 1 15  ? -54.845 89.988 -11.101 1.00 36.32 ? 156 PHE B CD1   1 
ATOM   3137 C CD2   . PHE B 1 15  ? -53.835 90.471 -13.214 1.00 39.26 ? 156 PHE B CD2   1 
ATOM   3138 C CE1   . PHE B 1 15  ? -54.642 88.629 -11.301 1.00 39.22 ? 156 PHE B CE1   1 
ATOM   3139 C CE2   . PHE B 1 15  ? -53.619 89.113 -13.428 1.00 37.73 ? 156 PHE B CE2   1 
ATOM   3140 C CZ    . PHE B 1 15  ? -54.024 88.186 -12.469 1.00 36.75 ? 156 PHE B CZ    1 
ATOM   3141 N N     . ASP B 1 16  ? -58.072 91.575 -11.799 1.00 46.09 ? 157 ASP B N     1 
ATOM   3142 C CA    . ASP B 1 16  ? -59.237 91.125 -11.047 1.00 40.22 ? 157 ASP B CA    1 
ATOM   3143 C C     . ASP B 1 16  ? -58.991 89.718 -10.507 1.00 39.12 ? 157 ASP B C     1 
ATOM   3144 O O     . ASP B 1 16  ? -59.425 88.712 -11.072 1.00 38.32 ? 157 ASP B O     1 
ATOM   3145 C CB    . ASP B 1 16  ? -60.474 91.176 -11.928 1.00 40.32 ? 157 ASP B CB    1 
ATOM   3146 C CG    . ASP B 1 16  ? -61.738 90.945 -11.143 1.00 45.82 ? 157 ASP B CG    1 
ATOM   3147 O OD1   . ASP B 1 16  ? -61.653 90.941 -9.896  1.00 46.65 ? 157 ASP B OD1   1 
ATOM   3148 O OD2   . ASP B 1 16  ? -62.802 90.762 -11.766 1.00 50.36 ? 157 ASP B OD2   1 
ATOM   3149 N N     . VAL B 1 17  ? -58.313 89.660 -9.358  1.00 40.94 ? 158 VAL B N     1 
ATOM   3150 C CA    . VAL B 1 17  ? -57.972 88.374 -8.758  1.00 42.29 ? 158 VAL B CA    1 
ATOM   3151 C C     . VAL B 1 17  ? -59.217 87.615 -8.288  1.00 43.23 ? 158 VAL B C     1 
ATOM   3152 O O     . VAL B 1 17  ? -59.226 86.380 -8.295  1.00 37.66 ? 158 VAL B O     1 
ATOM   3153 C CB    . VAL B 1 17  ? -56.952 88.579 -7.618  1.00 41.59 ? 158 VAL B CB    1 
ATOM   3154 C CG1   . VAL B 1 17  ? -57.532 89.439 -6.510  1.00 40.49 ? 158 VAL B CG1   1 
ATOM   3155 C CG2   . VAL B 1 17  ? -56.459 87.229 -7.081  1.00 36.40 ? 158 VAL B CG2   1 
ATOM   3156 N N     . ASN B 1 18  ? -60.294 88.314 -7.909  1.00 42.91 ? 159 ASN B N     1 
ATOM   3157 C CA    . ASN B 1 18  ? -61.483 87.613 -7.419  1.00 42.22 ? 159 ASN B CA    1 
ATOM   3158 C C     . ASN B 1 18  ? -62.190 86.844 -8.538  1.00 41.94 ? 159 ASN B C     1 
ATOM   3159 O O     . ASN B 1 18  ? -62.589 85.677 -8.359  1.00 39.19 ? 159 ASN B O     1 
ATOM   3160 C CB    . ASN B 1 18  ? -62.434 88.603 -6.753  1.00 46.97 ? 159 ASN B CB    1 
ATOM   3161 C CG    . ASN B 1 18  ? -62.471 88.439 -5.248  1.00 57.21 ? 159 ASN B CG    1 
ATOM   3162 O OD1   . ASN B 1 18  ? -61.467 88.069 -4.627  1.00 52.66 ? 159 ASN B OD1   1 
ATOM   3163 N ND2   . ASN B 1 18  ? -63.625 88.726 -4.646  1.00 64.08 ? 159 ASN B ND2   1 
ATOM   3164 N N     . ALA B 1 19  ? -62.356 87.478 -9.703  1.00 40.65 ? 160 ALA B N     1 
ATOM   3165 C CA    . ALA B 1 19  ? -62.909 86.762 -10.848 1.00 39.82 ? 160 ALA B CA    1 
ATOM   3166 C C     . ALA B 1 19  ? -62.065 85.538 -11.199 1.00 36.05 ? 160 ALA B C     1 
ATOM   3167 O O     . ALA B 1 19  ? -62.606 84.474 -11.529 1.00 35.79 ? 160 ALA B O     1 
ATOM   3168 C CB    . ALA B 1 19  ? -63.020 87.696 -12.053 1.00 38.83 ? 160 ALA B CB    1 
ATOM   3169 N N     . ILE B 1 20  ? -60.739 85.663 -11.127 1.00 35.26 ? 161 ILE B N     1 
ATOM   3170 C CA    . ILE B 1 20  ? -59.872 84.541 -11.473 1.00 33.75 ? 161 ILE B CA    1 
ATOM   3171 C C     . ILE B 1 20  ? -60.027 83.413 -10.460 1.00 35.14 ? 161 ILE B C     1 
ATOM   3172 O O     . ILE B 1 20  ? -60.170 82.239 -10.831 1.00 30.88 ? 161 ILE B O     1 
ATOM   3173 C CB    . ILE B 1 20  ? -58.413 85.008 -11.584 1.00 36.34 ? 161 ILE B CB    1 
ATOM   3174 C CG1   . ILE B 1 20  ? -58.186 85.654 -12.943 1.00 34.28 ? 161 ILE B CG1   1 
ATOM   3175 C CG2   . ILE B 1 20  ? -57.445 83.834 -11.385 1.00 36.65 ? 161 ILE B CG2   1 
ATOM   3176 C CD1   . ILE B 1 20  ? -56.997 86.554 -12.970 1.00 42.49 ? 161 ILE B CD1   1 
ATOM   3177 N N     . ARG B 1 21  ? -60.002 83.760 -9.167  1.00 32.79 ? 162 ARG B N     1 
ATOM   3178 C CA    . ARG B 1 21  ? -60.162 82.775 -8.105  1.00 36.24 ? 162 ARG B CA    1 
ATOM   3179 C C     . ARG B 1 21  ? -61.453 81.999 -8.263  1.00 31.12 ? 162 ARG B C     1 
ATOM   3180 O O     . ARG B 1 21  ? -61.505 80.813 -7.923  1.00 31.65 ? 162 ARG B O     1 
ATOM   3181 C CB    . ARG B 1 21  ? -60.135 83.459 -6.734  1.00 32.20 ? 162 ARG B CB    1 
ATOM   3182 C CG    . ARG B 1 21  ? -58.761 83.891 -6.275  1.00 33.45 ? 162 ARG B CG    1 
ATOM   3183 C CD    . ARG B 1 21  ? -58.817 84.610 -4.910  1.00 33.57 ? 162 ARG B CD    1 
ATOM   3184 N NE    . ARG B 1 21  ? -59.276 83.758 -3.816  1.00 29.23 ? 162 ARG B NE    1 
ATOM   3185 C CZ    . ARG B 1 21  ? -58.484 82.990 -3.076  1.00 33.78 ? 162 ARG B CZ    1 
ATOM   3186 N NH1   . ARG B 1 21  ? -57.194 82.866 -3.341  1.00 32.37 ? 162 ARG B NH1   1 
ATOM   3187 N NH2   . ARG B 1 21  ? -58.999 82.330 -2.044  1.00 28.13 ? 162 ARG B NH2   1 
ATOM   3188 N N     . ALA B 1 22  ? -62.507 82.641 -8.772  1.00 34.39 ? 163 ALA B N     1 
ATOM   3189 C CA    . ALA B 1 22  ? -63.747 81.894 -8.972  1.00 34.30 ? 163 ALA B CA    1 
ATOM   3190 C C     . ALA B 1 22  ? -63.582 80.721 -9.943  1.00 29.89 ? 163 ALA B C     1 
ATOM   3191 O O     . ALA B 1 22  ? -64.393 79.794 -9.909  1.00 32.85 ? 163 ALA B O     1 
ATOM   3192 C CB    . ALA B 1 22  ? -64.864 82.820 -9.456  1.00 33.12 ? 163 ALA B CB    1 
ATOM   3193 N N     . ASP B 1 23  ? -62.548 80.716 -10.793 1.00 31.07 ? 164 ASP B N     1 
ATOM   3194 C CA    . ASP B 1 23  ? -62.381 79.609 -11.737 1.00 29.47 ? 164 ASP B CA    1 
ATOM   3195 C C     . ASP B 1 23  ? -61.753 78.366 -11.112 1.00 29.63 ? 164 ASP B C     1 
ATOM   3196 O O     . ASP B 1 23  ? -61.849 77.282 -11.697 1.00 29.73 ? 164 ASP B O     1 
ATOM   3197 C CB    . ASP B 1 23  ? -61.524 80.039 -12.932 1.00 28.47 ? 164 ASP B CB    1 
ATOM   3198 C CG    . ASP B 1 23  ? -62.199 81.106 -13.793 1.00 32.53 ? 164 ASP B CG    1 
ATOM   3199 O OD1   . ASP B 1 23  ? -63.431 81.048 -13.974 1.00 34.63 ? 164 ASP B OD1   1 
ATOM   3200 O OD2   . ASP B 1 23  ? -61.489 81.999 -14.299 1.00 29.30 ? 164 ASP B OD2   1 
ATOM   3201 N N     . PHE B 1 24  ? -61.122 78.486 -9.939  1.00 29.77 ? 165 PHE B N     1 
ATOM   3202 C CA    . PHE B 1 24  ? -60.353 77.389 -9.370  1.00 28.31 ? 165 PHE B CA    1 
ATOM   3203 C C     . PHE B 1 24  ? -61.141 76.739 -8.241  1.00 31.56 ? 165 PHE B C     1 
ATOM   3204 O O     . PHE B 1 24  ? -61.148 77.264 -7.115  1.00 31.05 ? 165 PHE B O     1 
ATOM   3205 C CB    . PHE B 1 24  ? -59.001 77.897 -8.864  1.00 24.59 ? 165 PHE B CB    1 
ATOM   3206 C CG    . PHE B 1 24  ? -58.079 78.351 -9.956  1.00 26.10 ? 165 PHE B CG    1 
ATOM   3207 C CD1   . PHE B 1 24  ? -58.301 79.551 -10.617 1.00 24.82 ? 165 PHE B CD1   1 
ATOM   3208 C CD2   . PHE B 1 24  ? -56.992 77.569 -10.330 1.00 25.51 ? 165 PHE B CD2   1 
ATOM   3209 C CE1   . PHE B 1 24  ? -57.458 79.963 -11.628 1.00 26.14 ? 165 PHE B CE1   1 
ATOM   3210 C CE2   . PHE B 1 24  ? -56.139 77.976 -11.333 1.00 22.69 ? 165 PHE B CE2   1 
ATOM   3211 C CZ    . PHE B 1 24  ? -56.371 79.174 -11.989 1.00 27.36 ? 165 PHE B CZ    1 
ATOM   3212 N N     . PRO B 1 25  ? -61.792 75.589 -8.474  1.00 28.70 ? 166 PRO B N     1 
ATOM   3213 C CA    . PRO B 1 25  ? -62.719 75.049 -7.459  1.00 30.29 ? 166 PRO B CA    1 
ATOM   3214 C C     . PRO B 1 25  ? -62.045 74.649 -6.159  1.00 29.19 ? 166 PRO B C     1 
ATOM   3215 O O     . PRO B 1 25  ? -62.626 74.839 -5.082  1.00 30.92 ? 166 PRO B O     1 
ATOM   3216 C CB    . PRO B 1 25  ? -63.340 73.837 -8.172  1.00 26.64 ? 166 PRO B CB    1 
ATOM   3217 C CG    . PRO B 1 25  ? -62.309 73.449 -9.216  1.00 27.79 ? 166 PRO B CG    1 
ATOM   3218 C CD    . PRO B 1 25  ? -61.762 74.765 -9.694  1.00 25.76 ? 166 PRO B CD    1 
ATOM   3219 N N     . ILE B 1 26  ? -60.822 74.120 -6.220  1.00 26.55 ? 167 ILE B N     1 
ATOM   3220 C CA    . ILE B 1 26  ? -60.151 73.670 -5.005  1.00 25.87 ? 167 ILE B CA    1 
ATOM   3221 C C     . ILE B 1 26  ? -59.938 74.813 -4.025  1.00 29.55 ? 167 ILE B C     1 
ATOM   3222 O O     . ILE B 1 26  ? -59.779 74.577 -2.819  1.00 30.09 ? 167 ILE B O     1 
ATOM   3223 C CB    . ILE B 1 26  ? -58.813 72.997 -5.353  1.00 24.86 ? 167 ILE B CB    1 
ATOM   3224 C CG1   . ILE B 1 26  ? -58.423 71.963 -4.286  1.00 25.73 ? 167 ILE B CG1   1 
ATOM   3225 C CG2   . ILE B 1 26  ? -57.736 74.049 -5.520  1.00 25.44 ? 167 ILE B CG2   1 
ATOM   3226 C CD1   . ILE B 1 26  ? -57.370 70.963 -4.776  1.00 22.30 ? 167 ILE B CD1   1 
ATOM   3227 N N     . LEU B 1 27  ? -59.942 76.056 -4.508  1.00 24.23 ? 168 LEU B N     1 
ATOM   3228 C CA    . LEU B 1 27  ? -59.727 77.185 -3.618  1.00 31.28 ? 168 LEU B CA    1 
ATOM   3229 C C     . LEU B 1 27  ? -60.870 77.361 -2.628  1.00 33.31 ? 168 LEU B C     1 
ATOM   3230 O O     . LEU B 1 27  ? -60.745 78.178 -1.713  1.00 30.19 ? 168 LEU B O     1 
ATOM   3231 C CB    . LEU B 1 27  ? -59.536 78.466 -4.426  1.00 29.80 ? 168 LEU B CB    1 
ATOM   3232 C CG    . LEU B 1 27  ? -58.317 78.517 -5.355  1.00 35.51 ? 168 LEU B CG    1 
ATOM   3233 C CD1   . LEU B 1 27  ? -58.191 79.902 -5.954  1.00 32.33 ? 168 LEU B CD1   1 
ATOM   3234 C CD2   . LEU B 1 27  ? -57.014 78.095 -4.655  1.00 29.32 ? 168 LEU B CD2   1 
ATOM   3235 N N     . ARG B 1 28  ? -61.961 76.608 -2.788  1.00 32.03 ? 169 ARG B N     1 
ATOM   3236 C CA    . ARG B 1 28  ? -63.078 76.622 -1.856  1.00 38.72 ? 169 ARG B CA    1 
ATOM   3237 C C     . ARG B 1 28  ? -62.899 75.619 -0.723  1.00 38.82 ? 169 ARG B C     1 
ATOM   3238 O O     . ARG B 1 28  ? -63.715 75.596 0.202   1.00 44.41 ? 169 ARG B O     1 
ATOM   3239 C CB    . ARG B 1 28  ? -64.383 76.320 -2.605  1.00 38.81 ? 169 ARG B CB    1 
ATOM   3240 C CG    . ARG B 1 28  ? -65.027 77.509 -3.323  1.00 44.44 ? 169 ARG B CG    1 
ATOM   3241 C CD    . ARG B 1 28  ? -66.507 77.641 -2.956  1.00 51.22 ? 169 ARG B CD    1 
ATOM   3242 N NE    . ARG B 1 28  ? -66.954 79.030 -2.914  1.00 62.97 ? 169 ARG B NE    1 
ATOM   3243 C CZ    . ARG B 1 28  ? -67.774 79.533 -1.999  1.00 61.90 ? 169 ARG B CZ    1 
ATOM   3244 N NH1   . ARG B 1 28  ? -68.257 78.786 -1.018  1.00 57.93 ? 169 ARG B NH1   1 
ATOM   3245 N NH2   . ARG B 1 28  ? -68.122 80.817 -2.073  1.00 57.30 ? 169 ARG B NH2   1 
ATOM   3246 N N     . GLU B 1 29  ? -61.861 74.792 -0.779  1.00 32.76 ? 170 GLU B N     1 
ATOM   3247 C CA    . GLU B 1 29  ? -61.642 73.764 0.226   1.00 35.87 ? 170 GLU B CA    1 
ATOM   3248 C C     . GLU B 1 29  ? -61.268 74.389 1.573   1.00 38.07 ? 170 GLU B C     1 
ATOM   3249 O O     . GLU B 1 29  ? -60.875 75.556 1.660   1.00 35.50 ? 170 GLU B O     1 
ATOM   3250 C CB    . GLU B 1 29  ? -60.545 72.807 -0.241  1.00 37.33 ? 170 GLU B CB    1 
ATOM   3251 C CG    . GLU B 1 29  ? -60.660 71.403 0.317   1.00 42.54 ? 170 GLU B CG    1 
ATOM   3252 C CD    . GLU B 1 29  ? -61.601 70.517 -0.477  1.00 37.97 ? 170 GLU B CD    1 
ATOM   3253 O OE1   . GLU B 1 29  ? -62.071 70.936 -1.557  1.00 37.76 ? 170 GLU B OE1   1 
ATOM   3254 O OE2   . GLU B 1 29  ? -61.869 69.391 -0.014  1.00 40.35 ? 170 GLU B OE2   1 
ATOM   3255 N N     . THR B 1 30  ? -61.390 73.593 2.636   1.00 39.40 ? 171 THR B N     1 
ATOM   3256 C CA    . THR B 1 30  ? -61.081 74.055 3.983   1.00 40.92 ? 171 THR B CA    1 
ATOM   3257 C C     . THR B 1 30  ? -60.132 73.089 4.677   1.00 41.16 ? 171 THR B C     1 
ATOM   3258 O O     . THR B 1 30  ? -60.180 71.876 4.459   1.00 37.83 ? 171 THR B O     1 
ATOM   3259 C CB    . THR B 1 30  ? -62.340 74.202 4.851   1.00 42.91 ? 171 THR B CB    1 
ATOM   3260 O OG1   . THR B 1 30  ? -63.069 72.972 4.820   1.00 41.78 ? 171 THR B OG1   1 
ATOM   3261 C CG2   . THR B 1 30  ? -63.220 75.339 4.354   1.00 43.58 ? 171 THR B CG2   1 
ATOM   3262 N N     . VAL B 1 31  ? -59.283 73.646 5.539   1.00 41.60 ? 172 VAL B N     1 
ATOM   3263 C CA    . VAL B 1 31  ? -58.346 72.878 6.354   1.00 46.65 ? 172 VAL B CA    1 
ATOM   3264 C C     . VAL B 1 31  ? -58.558 73.283 7.805   1.00 49.82 ? 172 VAL B C     1 
ATOM   3265 O O     . VAL B 1 31  ? -58.442 74.469 8.139   1.00 51.49 ? 172 VAL B O     1 
ATOM   3266 C CB    . VAL B 1 31  ? -56.886 73.124 5.943   1.00 42.81 ? 172 VAL B CB    1 
ATOM   3267 C CG1   . VAL B 1 31  ? -55.954 72.207 6.736   1.00 43.45 ? 172 VAL B CG1   1 
ATOM   3268 C CG2   . VAL B 1 31  ? -56.718 72.957 4.439   1.00 33.41 ? 172 VAL B CG2   1 
ATOM   3269 N N     . ASN B 1 32  ? -58.862 72.309 8.666   1.00 56.17 ? 173 ASN B N     1 
ATOM   3270 C CA    . ASN B 1 32  ? -59.147 72.583 10.078  1.00 56.61 ? 173 ASN B CA    1 
ATOM   3271 C C     . ASN B 1 32  ? -60.274 73.603 10.216  1.00 58.49 ? 173 ASN B C     1 
ATOM   3272 O O     . ASN B 1 32  ? -60.240 74.479 11.084  1.00 61.43 ? 173 ASN B O     1 
ATOM   3273 C CB    . ASN B 1 32  ? -57.896 73.065 10.820  1.00 57.14 ? 173 ASN B CB    1 
ATOM   3274 C CG    . ASN B 1 32  ? -56.975 71.930 11.211  1.00 66.69 ? 173 ASN B CG    1 
ATOM   3275 O OD1   . ASN B 1 32  ? -57.346 71.057 11.998  1.00 79.75 ? 173 ASN B OD1   1 
ATOM   3276 N ND2   . ASN B 1 32  ? -55.763 71.932 10.658  1.00 62.65 ? 173 ASN B ND2   1 
ATOM   3277 N N     . GLY B 1 33  ? -61.271 73.506 9.340   1.00 51.94 ? 174 GLY B N     1 
ATOM   3278 C CA    . GLY B 1 33  ? -62.346 74.473 9.319   1.00 48.40 ? 174 GLY B CA    1 
ATOM   3279 C C     . GLY B 1 33  ? -61.962 75.860 8.863   1.00 51.15 ? 174 GLY B C     1 
ATOM   3280 O O     . GLY B 1 33  ? -62.822 76.748 8.855   1.00 53.35 ? 174 GLY B O     1 
ATOM   3281 N N     . LYS B 1 34  ? -60.671 76.085 8.465   1.00 50.59 ? 175 LYS B N     1 
ATOM   3282 C CA    . LYS B 1 34  ? -60.144 77.345 7.964   1.00 46.08 ? 175 LYS B CA    1 
ATOM   3283 C C     . LYS B 1 34  ? -59.987 77.291 6.448   1.00 41.51 ? 175 LYS B C     1 
ATOM   3284 O O     . LYS B 1 34  ? -59.698 76.230 5.888   1.00 40.00 ? 175 LYS B O     1 
ATOM   3285 C CB    . LYS B 1 34  ? -58.789 77.652 8.608   1.00 46.51 ? 175 LYS B CB    1 
ATOM   3286 C CG    . LYS B 1 34  ? -58.850 77.715 10.135  1.00 48.39 ? 175 LYS B CG    1 
ATOM   3287 C CD    . LYS B 1 34  ? -57.805 78.651 10.709  1.00 52.46 ? 175 LYS B CD    1 
ATOM   3288 C CE    . LYS B 1 34  ? -57.837 78.636 12.231  1.00 53.83 ? 175 LYS B CE    1 
ATOM   3289 N NZ    . LYS B 1 34  ? -58.185 77.284 12.751  1.00 58.43 ? 175 LYS B NZ    1 
ATOM   3290 N N     . PRO B 1 35  ? -60.193 78.407 5.749   1.00 39.66 ? 176 PRO B N     1 
ATOM   3291 C CA    . PRO B 1 35  ? -59.991 78.405 4.295   1.00 38.77 ? 176 PRO B CA    1 
ATOM   3292 C C     . PRO B 1 35  ? -58.559 78.043 3.918   1.00 36.70 ? 176 PRO B C     1 
ATOM   3293 O O     . PRO B 1 35  ? -57.590 78.534 4.503   1.00 36.63 ? 176 PRO B O     1 
ATOM   3294 C CB    . PRO B 1 35  ? -60.341 79.840 3.883   1.00 36.13 ? 176 PRO B CB    1 
ATOM   3295 C CG    . PRO B 1 35  ? -60.272 80.647 5.155   1.00 40.04 ? 176 PRO B CG    1 
ATOM   3296 C CD    . PRO B 1 35  ? -60.698 79.704 6.234   1.00 39.28 ? 176 PRO B CD    1 
ATOM   3297 N N     . LEU B 1 36  ? -58.441 77.148 2.944   1.00 34.49 ? 177 LEU B N     1 
ATOM   3298 C CA    . LEU B 1 36  ? -57.140 76.842 2.365   1.00 32.72 ? 177 LEU B CA    1 
ATOM   3299 C C     . LEU B 1 36  ? -56.494 78.107 1.812   1.00 34.18 ? 177 LEU B C     1 
ATOM   3300 O O     . LEU B 1 36  ? -57.156 78.942 1.188   1.00 34.30 ? 177 LEU B O     1 
ATOM   3301 C CB    . LEU B 1 36  ? -57.295 75.801 1.260   1.00 30.55 ? 177 LEU B CB    1 
ATOM   3302 C CG    . LEU B 1 36  ? -56.099 75.608 0.332   1.00 26.71 ? 177 LEU B CG    1 
ATOM   3303 C CD1   . LEU B 1 36  ? -55.029 74.818 1.071   1.00 25.38 ? 177 LEU B CD1   1 
ATOM   3304 C CD2   . LEU B 1 36  ? -56.562 74.886 -0.915  1.00 25.65 ? 177 LEU B CD2   1 
ATOM   3305 N N     . ILE B 1 37  ? -55.200 78.262 2.072   1.00 30.64 ? 178 ILE B N     1 
ATOM   3306 C CA    . ILE B 1 37  ? -54.397 79.314 1.463   1.00 30.23 ? 178 ILE B CA    1 
ATOM   3307 C C     . ILE B 1 37  ? -53.235 78.619 0.772   1.00 29.30 ? 178 ILE B C     1 
ATOM   3308 O O     . ILE B 1 37  ? -52.355 78.057 1.439   1.00 27.49 ? 178 ILE B O     1 
ATOM   3309 C CB    . ILE B 1 37  ? -53.911 80.337 2.499   1.00 34.16 ? 178 ILE B CB    1 
ATOM   3310 C CG1   . ILE B 1 37  ? -55.103 81.097 3.087   1.00 31.87 ? 178 ILE B CG1   1 
ATOM   3311 C CG2   . ILE B 1 37  ? -52.903 81.289 1.869   1.00 30.66 ? 178 ILE B CG2   1 
ATOM   3312 C CD1   . ILE B 1 37  ? -54.730 82.143 4.130   1.00 33.47 ? 178 ILE B CD1   1 
ATOM   3313 N N     . TRP B 1 38  ? -53.231 78.628 -0.561  1.00 28.83 ? 179 TRP B N     1 
ATOM   3314 C CA    . TRP B 1 38  ? -52.279 77.811 -1.318  1.00 26.45 ? 179 TRP B CA    1 
ATOM   3315 C C     . TRP B 1 38  ? -51.042 78.646 -1.627  1.00 27.44 ? 179 TRP B C     1 
ATOM   3316 O O     . TRP B 1 38  ? -51.010 79.401 -2.604  1.00 24.50 ? 179 TRP B O     1 
ATOM   3317 C CB    . TRP B 1 38  ? -52.919 77.256 -2.589  1.00 23.12 ? 179 TRP B CB    1 
ATOM   3318 C CG    . TRP B 1 38  ? -52.013 76.311 -3.337  1.00 23.47 ? 179 TRP B CG    1 
ATOM   3319 C CD1   . TRP B 1 38  ? -51.312 76.574 -4.487  1.00 23.73 ? 179 TRP B CD1   1 
ATOM   3320 C CD2   . TRP B 1 38  ? -51.687 74.966 -2.967  1.00 21.69 ? 179 TRP B CD2   1 
ATOM   3321 N NE1   . TRP B 1 38  ? -50.577 75.470 -4.856  1.00 24.22 ? 179 TRP B NE1   1 
ATOM   3322 C CE2   . TRP B 1 38  ? -50.794 74.468 -3.942  1.00 25.13 ? 179 TRP B CE2   1 
ATOM   3323 C CE3   . TRP B 1 38  ? -52.064 74.129 -1.903  1.00 22.59 ? 179 TRP B CE3   1 
ATOM   3324 C CZ2   . TRP B 1 38  ? -50.277 73.171 -3.889  1.00 21.23 ? 179 TRP B CZ2   1 
ATOM   3325 C CZ3   . TRP B 1 38  ? -51.550 72.841 -1.854  1.00 22.70 ? 179 TRP B CZ3   1 
ATOM   3326 C CH2   . TRP B 1 38  ? -50.665 72.375 -2.842  1.00 21.37 ? 179 TRP B CH2   1 
ATOM   3327 N N     . PHE B 1 39  ? -50.012 78.503 -0.790  1.00 26.30 ? 180 PHE B N     1 
ATOM   3328 C CA    . PHE B 1 39  ? -48.724 79.151 -1.000  1.00 27.21 ? 180 PHE B CA    1 
ATOM   3329 C C     . PHE B 1 39  ? -47.658 78.125 -1.376  1.00 25.19 ? 180 PHE B C     1 
ATOM   3330 O O     . PHE B 1 39  ? -46.479 78.288 -1.047  1.00 23.98 ? 180 PHE B O     1 
ATOM   3331 C CB    . PHE B 1 39  ? -48.298 79.930 0.250   1.00 24.12 ? 180 PHE B CB    1 
ATOM   3332 C CG    . PHE B 1 39  ? -49.002 81.258 0.432   1.00 28.64 ? 180 PHE B CG    1 
ATOM   3333 C CD1   . PHE B 1 39  ? -49.838 81.776 -0.553  1.00 27.91 ? 180 PHE B CD1   1 
ATOM   3334 C CD2   . PHE B 1 39  ? -48.849 81.974 1.617   1.00 27.86 ? 180 PHE B CD2   1 
ATOM   3335 C CE1   . PHE B 1 39  ? -50.493 82.995 -0.371  1.00 28.67 ? 180 PHE B CE1   1 
ATOM   3336 C CE2   . PHE B 1 39  ? -49.499 83.195 1.805   1.00 32.62 ? 180 PHE B CE2   1 
ATOM   3337 C CZ    . PHE B 1 39  ? -50.317 83.705 0.804   1.00 30.15 ? 180 PHE B CZ    1 
ATOM   3338 N N     . ASP B 1 40  ? -48.068 77.048 -2.054  1.00 26.37 ? 181 ASP B N     1 
ATOM   3339 C CA    . ASP B 1 40  ? -47.171 75.975 -2.474  1.00 23.69 ? 181 ASP B CA    1 
ATOM   3340 C C     . ASP B 1 40  ? -47.040 75.882 -3.992  1.00 25.20 ? 181 ASP B C     1 
ATOM   3341 O O     . ASP B 1 40  ? -46.836 74.795 -4.533  1.00 22.04 ? 181 ASP B O     1 
ATOM   3342 C CB    . ASP B 1 40  ? -47.635 74.634 -1.898  1.00 24.15 ? 181 ASP B CB    1 
ATOM   3343 C CG    . ASP B 1 40  ? -46.500 73.653 -1.743  1.00 27.30 ? 181 ASP B CG    1 
ATOM   3344 O OD1   . ASP B 1 40  ? -45.331 74.108 -1.748  1.00 29.48 ? 181 ASP B OD1   1 
ATOM   3345 O OD2   . ASP B 1 40  ? -46.772 72.433 -1.620  1.00 28.18 ? 181 ASP B OD2   1 
ATOM   3346 N N     . ASN B 1 41  ? -47.116 77.023 -4.682  1.00 26.60 ? 182 ASN B N     1 
ATOM   3347 C CA    . ASN B 1 41  ? -47.144 77.021 -6.141  1.00 24.35 ? 182 ASN B CA    1 
ATOM   3348 C C     . ASN B 1 41  ? -45.819 76.610 -6.753  1.00 25.34 ? 182 ASN B C     1 
ATOM   3349 O O     . ASN B 1 41  ? -45.796 76.132 -7.892  1.00 25.98 ? 182 ASN B O     1 
ATOM   3350 C CB    . ASN B 1 41  ? -47.551 78.392 -6.645  1.00 22.78 ? 182 ASN B CB    1 
ATOM   3351 C CG    . ASN B 1 41  ? -48.923 78.767 -6.178  1.00 28.67 ? 182 ASN B CG    1 
ATOM   3352 O OD1   . ASN B 1 41  ? -49.910 78.240 -6.693  1.00 27.54 ? 182 ASN B OD1   1 
ATOM   3353 N ND2   . ASN B 1 41  ? -49.008 79.664 -5.179  1.00 24.96 ? 182 ASN B ND2   1 
ATOM   3354 N N     . ALA B 1 42  ? -44.708 76.780 -6.031  1.00 25.94 ? 183 ALA B N     1 
ATOM   3355 C CA    . ALA B 1 42  ? -43.434 76.324 -6.583  1.00 25.96 ? 183 ALA B CA    1 
ATOM   3356 C C     . ALA B 1 42  ? -43.332 74.809 -6.585  1.00 26.70 ? 183 ALA B C     1 
ATOM   3357 O O     . ALA B 1 42  ? -42.468 74.263 -7.279  1.00 30.80 ? 183 ALA B O     1 
ATOM   3358 C CB    . ALA B 1 42  ? -42.257 76.913 -5.807  1.00 25.90 ? 183 ALA B CB    1 
ATOM   3359 N N     . ALA B 1 43  ? -44.177 74.119 -5.816  1.00 22.78 ? 184 ALA B N     1 
ATOM   3360 C CA    . ALA B 1 43  ? -44.265 72.664 -5.894  1.00 24.49 ? 184 ALA B CA    1 
ATOM   3361 C C     . ALA B 1 43  ? -45.280 72.229 -6.952  1.00 22.47 ? 184 ALA B C     1 
ATOM   3362 O O     . ALA B 1 43  ? -44.962 71.408 -7.814  1.00 21.60 ? 184 ALA B O     1 
ATOM   3363 C CB    . ALA B 1 43  ? -44.611 72.075 -4.521  1.00 24.01 ? 184 ALA B CB    1 
ATOM   3364 N N     . THR B 1 44  ? -46.493 72.776 -6.914  1.00 22.40 ? 185 THR B N     1 
ATOM   3365 C CA    . THR B 1 44  ? -47.447 72.573 -8.000  1.00 21.53 ? 185 THR B CA    1 
ATOM   3366 C C     . THR B 1 44  ? -48.541 73.629 -7.895  1.00 26.38 ? 185 THR B C     1 
ATOM   3367 O O     . THR B 1 44  ? -48.688 74.315 -6.874  1.00 21.05 ? 185 THR B O     1 
ATOM   3368 C CB    . THR B 1 44  ? -48.038 71.152 -7.986  1.00 19.94 ? 185 THR B CB    1 
ATOM   3369 O OG1   . THR B 1 44  ? -48.529 70.826 -9.295  1.00 20.50 ? 185 THR B OG1   1 
ATOM   3370 C CG2   . THR B 1 44  ? -49.191 71.046 -6.983  1.00 22.68 ? 185 THR B CG2   1 
ATOM   3371 N N     . THR B 1 45  ? -49.301 73.768 -8.977  1.00 19.90 ? 186 THR B N     1 
ATOM   3372 C CA    . THR B 1 45  ? -50.372 74.747 -9.020  1.00 20.34 ? 186 THR B CA    1 
ATOM   3373 C C     . THR B 1 45  ? -51.729 74.067 -9.048  1.00 19.15 ? 186 THR B C     1 
ATOM   3374 O O     . THR B 1 45  ? -51.864 72.886 -9.382  1.00 19.61 ? 186 THR B O     1 
ATOM   3375 C CB    . THR B 1 45  ? -50.255 75.657 -10.249 1.00 18.15 ? 186 THR B CB    1 
ATOM   3376 O OG1   . THR B 1 45  ? -50.223 74.843 -11.421 1.00 19.60 ? 186 THR B OG1   1 
ATOM   3377 C CG2   . THR B 1 45  ? -48.998 76.516 -10.173 1.00 22.58 ? 186 THR B CG2   1 
ATOM   3378 N N     . GLN B 1 46  ? -52.746 74.853 -8.740  1.00 19.41 ? 187 GLN B N     1 
ATOM   3379 C CA    . GLN B 1 46  ? -54.121 74.385 -8.796  1.00 22.98 ? 187 GLN B CA    1 
ATOM   3380 C C     . GLN B 1 46  ? -54.715 74.687 -10.169 1.00 21.23 ? 187 GLN B C     1 
ATOM   3381 O O     . GLN B 1 46  ? -54.194 75.510 -10.927 1.00 20.07 ? 187 GLN B O     1 
ATOM   3382 C CB    . GLN B 1 46  ? -54.939 75.015 -7.663  1.00 18.90 ? 187 GLN B CB    1 
ATOM   3383 C CG    . GLN B 1 46  ? -54.327 74.730 -6.274  1.00 21.11 ? 187 GLN B CG    1 
ATOM   3384 C CD    . GLN B 1 46  ? -54.272 73.234 -5.955  1.00 22.92 ? 187 GLN B CD    1 
ATOM   3385 O OE1   . GLN B 1 46  ? -54.871 72.416 -6.654  1.00 21.10 ? 187 GLN B OE1   1 
ATOM   3386 N NE2   . GLN B 1 46  ? -53.555 72.876 -4.893  1.00 22.08 ? 187 GLN B NE2   1 
ATOM   3387 N N     . LYS B 1 47  ? -55.813 73.963 -10.508 1.00 23.29 ? 188 LYS B N     1 
ATOM   3388 C CA    . LYS B 1 47  ? -56.308 73.985 -11.887 1.00 23.41 ? 188 LYS B CA    1 
ATOM   3389 C C     . LYS B 1 47  ? -57.611 74.757 -12.017 1.00 24.85 ? 188 LYS B C     1 
ATOM   3390 O O     . LYS B 1 47  ? -58.512 74.607 -11.182 1.00 24.36 ? 188 LYS B O     1 
ATOM   3391 C CB    . LYS B 1 47  ? -56.545 72.567 -12.414 1.00 20.04 ? 188 LYS B CB    1 
ATOM   3392 C CG    . LYS B 1 47  ? -55.572 71.550 -11.866 1.00 21.89 ? 188 LYS B CG    1 
ATOM   3393 C CD    . LYS B 1 47  ? -54.137 71.908 -12.248 1.00 19.72 ? 188 LYS B CD    1 
ATOM   3394 C CE    . LYS B 1 47  ? -53.175 70.950 -11.586 1.00 19.95 ? 188 LYS B CE    1 
ATOM   3395 N NZ    . LYS B 1 47  ? -51.759 71.346 -11.814 1.00 18.67 ? 188 LYS B NZ    1 
ATOM   3396 N N     . PRO B 1 48  ? -57.757 75.552 -13.073 1.00 24.33 ? 189 PRO B N     1 
ATOM   3397 C CA    . PRO B 1 48  ? -59.074 76.117 -13.383 1.00 23.58 ? 189 PRO B CA    1 
ATOM   3398 C C     . PRO B 1 48  ? -60.025 75.042 -13.891 1.00 22.71 ? 189 PRO B C     1 
ATOM   3399 O O     . PRO B 1 48  ? -59.611 74.027 -14.466 1.00 22.71 ? 189 PRO B O     1 
ATOM   3400 C CB    . PRO B 1 48  ? -58.771 77.156 -14.470 1.00 23.50 ? 189 PRO B CB    1 
ATOM   3401 C CG    . PRO B 1 48  ? -57.509 76.679 -15.117 1.00 26.20 ? 189 PRO B CG    1 
ATOM   3402 C CD    . PRO B 1 48  ? -56.724 75.942 -14.049 1.00 23.57 ? 189 PRO B CD    1 
ATOM   3403 N N     . GLN B 1 49  ? -61.322 75.290 -13.687 1.00 22.82 ? 190 GLN B N     1 
ATOM   3404 C CA    . GLN B 1 49  ? -62.346 74.346 -14.131 1.00 25.79 ? 190 GLN B CA    1 
ATOM   3405 C C     . GLN B 1 49  ? -62.285 74.081 -15.635 1.00 25.67 ? 190 GLN B C     1 
ATOM   3406 O O     . GLN B 1 49  ? -62.634 72.983 -16.082 1.00 24.17 ? 190 GLN B O     1 
ATOM   3407 C CB    . GLN B 1 49  ? -63.735 74.858 -13.748 1.00 27.37 ? 190 GLN B CB    1 
ATOM   3408 C CG    . GLN B 1 49  ? -64.816 73.805 -13.927 1.00 27.44 ? 190 GLN B CG    1 
ATOM   3409 C CD    . GLN B 1 49  ? -64.730 72.720 -12.871 1.00 27.04 ? 190 GLN B CD    1 
ATOM   3410 O OE1   . GLN B 1 49  ? -64.588 73.004 -11.681 1.00 33.09 ? 190 GLN B OE1   1 
ATOM   3411 N NE2   . GLN B 1 49  ? -64.790 71.469 -13.301 1.00 26.50 ? 190 GLN B NE2   1 
ATOM   3412 N N     . ALA B 1 50  ? -61.843 75.058 -16.429 1.00 24.28 ? 191 ALA B N     1 
ATOM   3413 C CA    . ALA B 1 50  ? -61.696 74.832 -17.866 1.00 22.15 ? 191 ALA B CA    1 
ATOM   3414 C C     . ALA B 1 50  ? -60.712 73.698 -18.173 1.00 23.41 ? 191 ALA B C     1 
ATOM   3415 O O     . ALA B 1 50  ? -60.929 72.923 -19.111 1.00 19.75 ? 191 ALA B O     1 
ATOM   3416 C CB    . ALA B 1 50  ? -61.251 76.127 -18.556 1.00 22.26 ? 191 ALA B CB    1 
ATOM   3417 N N     . VAL B 1 51  ? -59.638 73.560 -17.385 1.00 20.56 ? 192 VAL B N     1 
ATOM   3418 C CA    . VAL B 1 51  ? -58.678 72.478 -17.630 1.00 20.94 ? 192 VAL B CA    1 
ATOM   3419 C C     . VAL B 1 51  ? -59.284 71.124 -17.251 1.00 19.87 ? 192 VAL B C     1 
ATOM   3420 O O     . VAL B 1 51  ? -59.192 70.133 -18.004 1.00 17.50 ? 192 VAL B O     1 
ATOM   3421 C CB    . VAL B 1 51  ? -57.362 72.749 -16.869 1.00 19.02 ? 192 VAL B CB    1 
ATOM   3422 C CG1   . VAL B 1 51  ? -56.433 71.543 -16.947 1.00 16.14 ? 192 VAL B CG1   1 
ATOM   3423 C CG2   . VAL B 1 51  ? -56.660 73.988 -17.425 1.00 18.94 ? 192 VAL B CG2   1 
ATOM   3424 N N     . ILE B 1 52  ? -59.915 71.071 -16.075 1.00 19.72 ? 193 ILE B N     1 
ATOM   3425 C CA    . ILE B 1 52  ? -60.580 69.861 -15.600 1.00 21.18 ? 193 ILE B CA    1 
ATOM   3426 C C     . ILE B 1 52  ? -61.613 69.390 -16.614 1.00 20.57 ? 193 ILE B C     1 
ATOM   3427 O O     . ILE B 1 52  ? -61.676 68.202 -16.975 1.00 24.71 ? 193 ILE B O     1 
ATOM   3428 C CB    . ILE B 1 52  ? -61.224 70.138 -14.225 1.00 21.37 ? 193 ILE B CB    1 
ATOM   3429 C CG1   . ILE B 1 52  ? -60.170 70.698 -13.251 1.00 22.23 ? 193 ILE B CG1   1 
ATOM   3430 C CG2   . ILE B 1 52  ? -61.934 68.890 -13.693 1.00 20.17 ? 193 ILE B CG2   1 
ATOM   3431 C CD1   . ILE B 1 52  ? -60.707 71.040 -11.847 1.00 21.84 ? 193 ILE B CD1   1 
ATOM   3432 N N     . ASP B 1 53  ? -62.427 70.333 -17.103 1.00 23.48 ? 194 ASP B N     1 
ATOM   3433 C CA    . ASP B 1 53  ? -63.461 70.033 -18.090 1.00 22.48 ? 194 ASP B CA    1 
ATOM   3434 C C     . ASP B 1 53  ? -62.862 69.624 -19.428 1.00 22.90 ? 194 ASP B C     1 
ATOM   3435 O O     . ASP B 1 53  ? -63.425 68.767 -20.120 1.00 21.41 ? 194 ASP B O     1 
ATOM   3436 C CB    . ASP B 1 53  ? -64.378 71.246 -18.273 1.00 22.34 ? 194 ASP B CB    1 
ATOM   3437 C CG    . ASP B 1 53  ? -65.334 71.443 -17.104 1.00 27.18 ? 194 ASP B CG    1 
ATOM   3438 O OD1   . ASP B 1 53  ? -65.436 70.530 -16.252 1.00 33.45 ? 194 ASP B OD1   1 
ATOM   3439 O OD2   . ASP B 1 53  ? -66.003 72.500 -17.047 1.00 31.41 ? 194 ASP B OD2   1 
ATOM   3440 N N     . ARG B 1 54  ? -61.746 70.243 -19.839 1.00 19.96 ? 195 ARG B N     1 
ATOM   3441 C CA    . ARG B 1 54  ? -61.124 69.826 -21.092 1.00 18.04 ? 195 ARG B CA    1 
ATOM   3442 C C     . ARG B 1 54  ? -60.708 68.359 -21.034 1.00 20.44 ? 195 ARG B C     1 
ATOM   3443 O O     . ARG B 1 54  ? -60.919 67.608 -21.994 1.00 18.17 ? 195 ARG B O     1 
ATOM   3444 C CB    . ARG B 1 54  ? -59.922 70.706 -21.408 1.00 18.36 ? 195 ARG B CB    1 
ATOM   3445 C CG    . ARG B 1 54  ? -59.405 70.546 -22.839 1.00 17.70 ? 195 ARG B CG    1 
ATOM   3446 C CD    . ARG B 1 54  ? -60.494 70.850 -23.851 1.00 17.90 ? 195 ARG B CD    1 
ATOM   3447 N NE    . ARG B 1 54  ? -60.091 70.563 -25.225 1.00 21.68 ? 195 ARG B NE    1 
ATOM   3448 C CZ    . ARG B 1 54  ? -60.332 69.410 -25.834 1.00 22.51 ? 195 ARG B CZ    1 
ATOM   3449 N NH1   . ARG B 1 54  ? -60.867 68.384 -25.182 1.00 19.13 ? 195 ARG B NH1   1 
ATOM   3450 N NH2   . ARG B 1 54  ? -60.035 69.283 -27.122 1.00 19.94 ? 195 ARG B NH2   1 
ATOM   3451 N N     . LEU B 1 55  ? -60.136 67.925 -19.902 1.00 18.22 ? 196 LEU B N     1 
ATOM   3452 C CA    . LEU B 1 55  ? -59.776 66.509 -19.768 1.00 19.69 ? 196 LEU B CA    1 
ATOM   3453 C C     . LEU B 1 55  ? -61.009 65.612 -19.850 1.00 22.09 ? 196 LEU B C     1 
ATOM   3454 O O     . LEU B 1 55  ? -61.006 64.578 -20.548 1.00 18.79 ? 196 LEU B O     1 
ATOM   3455 C CB    . LEU B 1 55  ? -59.035 66.265 -18.452 1.00 19.49 ? 196 LEU B CB    1 
ATOM   3456 C CG    . LEU B 1 55  ? -57.612 66.788 -18.260 1.00 22.71 ? 196 LEU B CG    1 
ATOM   3457 C CD1   . LEU B 1 55  ? -57.115 66.486 -16.832 1.00 19.71 ? 196 LEU B CD1   1 
ATOM   3458 C CD2   . LEU B 1 55  ? -56.680 66.180 -19.300 1.00 19.56 ? 196 LEU B CD2   1 
ATOM   3459 N N     . SER B 1 56  ? -62.068 65.982 -19.111 1.00 19.45 ? 197 SER B N     1 
ATOM   3460 C CA    . SER B 1 56  ? -63.311 65.206 -19.141 1.00 20.77 ? 197 SER B CA    1 
ATOM   3461 C C     . SER B 1 56  ? -63.895 65.134 -20.545 1.00 18.49 ? 197 SER B C     1 
ATOM   3462 O O     . SER B 1 56  ? -64.369 64.076 -20.986 1.00 18.90 ? 197 SER B O     1 
ATOM   3463 C CB    . SER B 1 56  ? -64.344 65.826 -18.189 1.00 19.22 ? 197 SER B CB    1 
ATOM   3464 O OG    . SER B 1 56  ? -63.914 65.680 -16.852 1.00 28.08 ? 197 SER B OG    1 
ATOM   3465 N N     . HIS B 1 57  ? -63.909 66.262 -21.245 1.00 19.40 ? 198 HIS B N     1 
ATOM   3466 C CA    . HIS B 1 57  ? -64.424 66.287 -22.605 1.00 21.09 ? 198 HIS B CA    1 
ATOM   3467 C C     . HIS B 1 57  ? -63.613 65.367 -23.501 1.00 19.48 ? 198 HIS B C     1 
ATOM   3468 O O     . HIS B 1 57  ? -64.177 64.635 -24.322 1.00 19.58 ? 198 HIS B O     1 
ATOM   3469 C CB    . HIS B 1 57  ? -64.407 67.718 -23.151 1.00 20.69 ? 198 HIS B CB    1 
ATOM   3470 C CG    . HIS B 1 57  ? -65.150 67.878 -24.440 1.00 24.31 ? 198 HIS B CG    1 
ATOM   3471 N ND1   . HIS B 1 57  ? -64.554 67.698 -25.673 1.00 28.38 ? 198 HIS B ND1   1 
ATOM   3472 C CD2   . HIS B 1 57  ? -66.445 68.187 -24.690 1.00 25.38 ? 198 HIS B CD2   1 
ATOM   3473 C CE1   . HIS B 1 57  ? -65.449 67.898 -26.627 1.00 24.00 ? 198 HIS B CE1   1 
ATOM   3474 N NE2   . HIS B 1 57  ? -66.603 68.197 -26.056 1.00 32.68 ? 198 HIS B NE2   1 
ATOM   3475 N N     . PHE B 1 58  ? -62.284 65.393 -23.366 1.00 20.21 ? 199 PHE B N     1 
ATOM   3476 C CA    . PHE B 1 58  ? -61.464 64.518 -24.196 1.00 19.75 ? 199 PHE B CA    1 
ATOM   3477 C C     . PHE B 1 58  ? -61.836 63.064 -23.960 1.00 17.52 ? 199 PHE B C     1 
ATOM   3478 O O     . PHE B 1 58  ? -62.054 62.296 -24.905 1.00 16.56 ? 199 PHE B O     1 
ATOM   3479 C CB    . PHE B 1 58  ? -59.971 64.724 -23.914 1.00 19.54 ? 199 PHE B CB    1 
ATOM   3480 C CG    . PHE B 1 58  ? -59.080 63.814 -24.730 1.00 21.22 ? 199 PHE B CG    1 
ATOM   3481 C CD1   . PHE B 1 58  ? -58.727 64.157 -26.032 1.00 18.24 ? 199 PHE B CD1   1 
ATOM   3482 C CD2   . PHE B 1 58  ? -58.636 62.596 -24.218 1.00 18.17 ? 199 PHE B CD2   1 
ATOM   3483 C CE1   . PHE B 1 58  ? -57.922 63.311 -26.803 1.00 19.99 ? 199 PHE B CE1   1 
ATOM   3484 C CE2   . PHE B 1 58  ? -57.836 61.736 -24.991 1.00 17.99 ? 199 PHE B CE2   1 
ATOM   3485 C CZ    . PHE B 1 58  ? -57.477 62.098 -26.278 1.00 16.69 ? 199 PHE B CZ    1 
ATOM   3486 N N     . TYR B 1 59  ? -61.914 62.664 -22.695 1.00 17.68 ? 200 TYR B N     1 
ATOM   3487 C CA    . TYR B 1 59  ? -62.170 61.255 -22.432 1.00 20.21 ? 200 TYR B CA    1 
ATOM   3488 C C     . TYR B 1 59  ? -63.576 60.849 -22.859 1.00 19.51 ? 200 TYR B C     1 
ATOM   3489 O O     . TYR B 1 59  ? -63.792 59.688 -23.241 1.00 18.09 ? 200 TYR B O     1 
ATOM   3490 C CB    . TYR B 1 59  ? -61.918 60.950 -20.952 1.00 16.91 ? 200 TYR B CB    1 
ATOM   3491 C CG    . TYR B 1 59  ? -60.430 60.807 -20.660 1.00 14.37 ? 200 TYR B CG    1 
ATOM   3492 C CD1   . TYR B 1 59  ? -59.651 59.913 -21.389 1.00 15.93 ? 200 TYR B CD1   1 
ATOM   3493 C CD2   . TYR B 1 59  ? -59.811 61.564 -19.674 1.00 15.13 ? 200 TYR B CD2   1 
ATOM   3494 C CE1   . TYR B 1 59  ? -58.281 59.757 -21.136 1.00 16.71 ? 200 TYR B CE1   1 
ATOM   3495 C CE2   . TYR B 1 59  ? -58.439 61.421 -19.401 1.00 16.69 ? 200 TYR B CE2   1 
ATOM   3496 C CZ    . TYR B 1 59  ? -57.683 60.511 -20.132 1.00 16.70 ? 200 TYR B CZ    1 
ATOM   3497 O OH    . TYR B 1 59  ? -56.328 60.352 -19.889 1.00 14.78 ? 200 TYR B OH    1 
ATOM   3498 N N     . ALA B 1 60  ? -64.536 61.784 -22.833 1.00 17.13 ? 201 ALA B N     1 
ATOM   3499 C CA    . ALA B 1 60  ? -65.917 61.436 -23.151 1.00 19.70 ? 201 ALA B CA    1 
ATOM   3500 C C     . ALA B 1 60  ? -66.249 61.549 -24.630 1.00 20.57 ? 201 ALA B C     1 
ATOM   3501 O O     . ALA B 1 60  ? -67.263 60.981 -25.057 1.00 23.19 ? 201 ALA B O     1 
ATOM   3502 C CB    . ALA B 1 60  ? -66.898 62.321 -22.369 1.00 21.04 ? 201 ALA B CB    1 
ATOM   3503 N N     . HIS B 1 61  ? -65.433 62.257 -25.421 1.00 19.21 ? 202 HIS B N     1 
ATOM   3504 C CA    . HIS B 1 61  ? -65.807 62.565 -26.802 1.00 21.40 ? 202 HIS B CA    1 
ATOM   3505 C C     . HIS B 1 61  ? -64.697 62.398 -27.830 1.00 21.55 ? 202 HIS B C     1 
ATOM   3506 O O     . HIS B 1 61  ? -65.015 62.271 -29.018 1.00 22.68 ? 202 HIS B O     1 
ATOM   3507 C CB    . HIS B 1 61  ? -66.337 64.008 -26.903 1.00 21.77 ? 202 HIS B CB    1 
ATOM   3508 C CG    . HIS B 1 61  ? -67.544 64.269 -26.055 1.00 27.36 ? 202 HIS B CG    1 
ATOM   3509 N ND1   . HIS B 1 61  ? -68.801 63.806 -26.384 1.00 28.95 ? 202 HIS B ND1   1 
ATOM   3510 C CD2   . HIS B 1 61  ? -67.679 64.925 -24.876 1.00 26.79 ? 202 HIS B CD2   1 
ATOM   3511 C CE1   . HIS B 1 61  ? -69.658 64.169 -25.445 1.00 29.75 ? 202 HIS B CE1   1 
ATOM   3512 N NE2   . HIS B 1 61  ? -69.003 64.847 -24.519 1.00 29.36 ? 202 HIS B NE2   1 
ATOM   3513 N N     . GLU B 1 62  ? -63.420 62.410 -27.449 1.00 18.25 ? 203 GLU B N     1 
ATOM   3514 C CA    . GLU B 1 62  ? -62.344 62.458 -28.423 1.00 20.08 ? 203 GLU B CA    1 
ATOM   3515 C C     . GLU B 1 62  ? -61.352 61.304 -28.289 1.00 21.93 ? 203 GLU B C     1 
ATOM   3516 O O     . GLU B 1 62  ? -60.435 61.207 -29.111 1.00 22.74 ? 203 GLU B O     1 
ATOM   3517 C CB    . GLU B 1 62  ? -61.581 63.793 -28.307 1.00 19.94 ? 203 GLU B CB    1 
ATOM   3518 C CG    . GLU B 1 62  ? -62.396 65.057 -28.667 1.00 22.90 ? 203 GLU B CG    1 
ATOM   3519 C CD    . GLU B 1 62  ? -61.782 66.331 -28.082 1.00 26.31 ? 203 GLU B CD    1 
ATOM   3520 O OE1   . GLU B 1 62  ? -61.780 66.476 -26.847 1.00 31.75 ? 203 GLU B OE1   1 
ATOM   3521 O OE2   . GLU B 1 62  ? -61.292 67.189 -28.854 1.00 30.41 ? 203 GLU B OE2   1 
ATOM   3522 N N     . ASN B 1 63  ? -61.524 60.415 -27.311 1.00 19.07 ? 204 ASN B N     1 
ATOM   3523 C CA    . ASN B 1 63  ? -60.433 59.548 -26.884 1.00 19.03 ? 204 ASN B CA    1 
ATOM   3524 C C     . ASN B 1 63  ? -60.126 58.453 -27.900 1.00 18.01 ? 204 ASN B C     1 
ATOM   3525 O O     . ASN B 1 63  ? -61.003 57.662 -28.268 1.00 17.73 ? 204 ASN B O     1 
ATOM   3526 C CB    . ASN B 1 63  ? -60.754 58.909 -25.539 1.00 16.73 ? 204 ASN B CB    1 
ATOM   3527 C CG    . ASN B 1 63  ? -59.710 57.889 -25.142 1.00 18.95 ? 204 ASN B CG    1 
ATOM   3528 O OD1   . ASN B 1 63  ? -58.562 58.243 -24.873 1.00 20.36 ? 204 ASN B OD1   1 
ATOM   3529 N ND2   . ASN B 1 63  ? -60.088 56.608 -25.142 1.00 17.47 ? 204 ASN B ND2   1 
ATOM   3530 N N     . SER B 1 64  ? -58.856 58.374 -28.297 1.00 16.89 ? 205 SER B N     1 
ATOM   3531 C CA    . SER B 1 64  ? -58.341 57.433 -29.288 1.00 17.37 ? 205 SER B CA    1 
ATOM   3532 C C     . SER B 1 64  ? -56.839 57.665 -29.370 1.00 18.54 ? 205 SER B C     1 
ATOM   3533 O O     . SER B 1 64  ? -56.350 58.739 -29.011 1.00 18.79 ? 205 SER B O     1 
ATOM   3534 C CB    . SER B 1 64  ? -59.000 57.646 -30.669 1.00 17.81 ? 205 SER B CB    1 
ATOM   3535 O OG    . SER B 1 64  ? -58.370 56.899 -31.693 1.00 18.70 ? 205 SER B OG    1 
ATOM   3536 N N     . ASN B 1 65  ? -56.106 56.651 -29.824 1.00 17.66 ? 206 ASN B N     1 
ATOM   3537 C CA    . ASN B 1 65  ? -54.770 56.943 -30.331 1.00 22.14 ? 206 ASN B CA    1 
ATOM   3538 C C     . ASN B 1 65  ? -54.864 57.769 -31.616 1.00 21.68 ? 206 ASN B C     1 
ATOM   3539 O O     . ASN B 1 65  ? -55.931 57.881 -32.237 1.00 23.22 ? 206 ASN B O     1 
ATOM   3540 C CB    . ASN B 1 65  ? -53.984 55.658 -30.582 1.00 23.45 ? 206 ASN B CB    1 
ATOM   3541 C CG    . ASN B 1 65  ? -52.598 55.716 -29.991 1.00 36.03 ? 206 ASN B CG    1 
ATOM   3542 O OD1   . ASN B 1 65  ? -51.821 56.655 -30.276 1.00 31.34 ? 206 ASN B OD1   1 
ATOM   3543 N ND2   . ASN B 1 65  ? -52.277 54.737 -29.142 1.00 33.24 ? 206 ASN B ND2   1 
ATOM   3544 N N     . ILE B 1 66  ? -53.737 58.363 -32.017 1.00 23.64 ? 207 ILE B N     1 
ATOM   3545 C CA    . ILE B 1 66  ? -53.764 59.311 -33.131 1.00 27.81 ? 207 ILE B CA    1 
ATOM   3546 C C     . ILE B 1 66  ? -53.679 58.581 -34.474 1.00 28.74 ? 207 ILE B C     1 
ATOM   3547 O O     . ILE B 1 66  ? -53.766 57.350 -34.511 1.00 27.52 ? 207 ILE B O     1 
ATOM   3548 C CB    . ILE B 1 66  ? -52.645 60.359 -32.995 1.00 30.44 ? 207 ILE B CB    1 
ATOM   3549 C CG1   . ILE B 1 66  ? -51.296 59.683 -32.766 1.00 34.17 ? 207 ILE B CG1   1 
ATOM   3550 C CG2   . ILE B 1 66  ? -52.958 61.316 -31.846 1.00 27.10 ? 207 ILE B CG2   1 
ATOM   3551 C CD1   . ILE B 1 66  ? -50.229 60.648 -32.273 1.00 42.84 ? 207 ILE B CD1   1 
ATOM   3552 N N     A HIS B 1 67  ? -53.509 59.361 -35.557 0.52 29.77 ? 208 HIS B N     1 
ATOM   3553 N N     B HIS B 1 67  ? -53.501 59.350 -35.564 0.48 29.70 ? 208 HIS B N     1 
ATOM   3554 C CA    A HIS B 1 67  ? -53.480 58.990 -36.977 0.52 32.41 ? 208 HIS B CA    1 
ATOM   3555 C CA    B HIS B 1 67  ? -53.493 58.957 -36.981 0.48 32.40 ? 208 HIS B CA    1 
ATOM   3556 C C     A HIS B 1 67  ? -54.868 59.156 -37.585 0.52 30.28 ? 208 HIS B C     1 
ATOM   3557 C C     B HIS B 1 67  ? -54.881 59.155 -37.579 0.48 30.28 ? 208 HIS B C     1 
ATOM   3558 O O     A HIS B 1 67  ? -55.678 58.223 -37.588 0.52 31.51 ? 208 HIS B O     1 
ATOM   3559 O O     B HIS B 1 67  ? -55.709 58.238 -37.572 0.48 31.49 ? 208 HIS B O     1 
ATOM   3560 C CB    A HIS B 1 67  ? -52.940 57.575 -37.209 0.52 31.85 ? 208 HIS B CB    1 
ATOM   3561 C CB    B HIS B 1 67  ? -53.019 57.513 -37.209 0.48 31.83 ? 208 HIS B CB    1 
ATOM   3562 C CG    A HIS B 1 67  ? -51.453 57.477 -37.074 0.52 33.08 ? 208 HIS B CG    1 
ATOM   3563 C CG    B HIS B 1 67  ? -52.936 57.122 -38.653 0.48 33.07 ? 208 HIS B CG    1 
ATOM   3564 N ND1   A HIS B 1 67  ? -50.779 57.917 -35.954 0.52 33.21 ? 208 HIS B ND1   1 
ATOM   3565 N ND1   B HIS B 1 67  ? -53.712 56.122 -39.200 0.48 34.81 ? 208 HIS B ND1   1 
ATOM   3566 C CD2   A HIS B 1 67  ? -50.509 57.001 -37.919 0.52 35.33 ? 208 HIS B CD2   1 
ATOM   3567 C CD2   B HIS B 1 67  ? -52.155 57.584 -39.659 0.48 35.08 ? 208 HIS B CD2   1 
ATOM   3568 C CE1   A HIS B 1 67  ? -49.484 57.711 -36.113 0.52 33.15 ? 208 HIS B CE1   1 
ATOM   3569 C CE1   B HIS B 1 67  ? -53.423 55.994 -40.483 0.48 34.90 ? 208 HIS B CE1   1 
ATOM   3570 N NE2   A HIS B 1 67  ? -49.293 57.154 -37.296 0.52 37.11 ? 208 HIS B NE2   1 
ATOM   3571 N NE2   B HIS B 1 67  ? -52.484 56.872 -40.788 0.48 33.18 ? 208 HIS B NE2   1 
ATOM   3572 N N     . ARG B 1 68  ? -55.140 60.349 -38.118 1.00 30.28 ? 209 ARG B N     1 
ATOM   3573 C CA    . ARG B 1 68  ? -56.502 60.729 -38.478 1.00 29.46 ? 209 ARG B CA    1 
ATOM   3574 C C     . ARG B 1 68  ? -57.075 59.916 -39.635 1.00 32.72 ? 209 ARG B C     1 
ATOM   3575 O O     . ARG B 1 68  ? -58.302 59.852 -39.777 1.00 33.30 ? 209 ARG B O     1 
ATOM   3576 C CB    . ARG B 1 68  ? -56.553 62.227 -38.810 1.00 32.01 ? 209 ARG B CB    1 
ATOM   3577 C CG    . ARG B 1 68  ? -55.623 62.644 -39.930 1.00 37.82 ? 209 ARG B CG    1 
ATOM   3578 C CD    . ARG B 1 68  ? -55.914 64.065 -40.372 1.00 40.15 ? 209 ARG B CD    1 
ATOM   3579 N NE    . ARG B 1 68  ? -55.251 65.036 -39.512 1.00 38.31 ? 209 ARG B NE    1 
ATOM   3580 C CZ    . ARG B 1 68  ? -55.888 65.803 -38.641 1.00 38.25 ? 209 ARG B CZ    1 
ATOM   3581 N NH1   . ARG B 1 68  ? -57.198 65.710 -38.475 1.00 40.04 ? 209 ARG B NH1   1 
ATOM   3582 N NH2   . ARG B 1 68  ? -55.194 66.684 -37.916 1.00 33.96 ? 209 ARG B NH2   1 
ATOM   3583 N N     . ALA B 1 69  ? -56.234 59.292 -40.463 1.00 32.43 ? 210 ALA B N     1 
ATOM   3584 C CA    . ALA B 1 69  ? -56.775 58.463 -41.536 1.00 34.22 ? 210 ALA B CA    1 
ATOM   3585 C C     . ALA B 1 69  ? -57.461 57.199 -41.017 1.00 32.39 ? 210 ALA B C     1 
ATOM   3586 O O     . ALA B 1 69  ? -58.229 56.582 -41.764 1.00 33.56 ? 210 ALA B O     1 
ATOM   3587 C CB    . ALA B 1 69  ? -55.664 58.080 -42.523 1.00 32.20 ? 210 ALA B CB    1 
ATOM   3588 N N     . ALA B 1 70  ? -57.205 56.801 -39.766 1.00 28.67 ? 211 ALA B N     1 
ATOM   3589 C CA    . ALA B 1 70  ? -57.707 55.521 -39.266 1.00 30.39 ? 211 ALA B CA    1 
ATOM   3590 C C     . ALA B 1 70  ? -59.228 55.535 -39.115 1.00 28.86 ? 211 ALA B C     1 
ATOM   3591 O O     . ALA B 1 70  ? -59.929 54.697 -39.696 1.00 24.05 ? 211 ALA B O     1 
ATOM   3592 C CB    . ALA B 1 70  ? -57.036 55.178 -37.931 1.00 28.48 ? 211 ALA B CB    1 
ATOM   3593 N N     . HIS B 1 71  ? -59.759 56.471 -38.334 1.00 26.60 ? 212 HIS B N     1 
ATOM   3594 C CA    . HIS B 1 71  ? -61.197 56.524 -38.082 1.00 21.61 ? 212 HIS B CA    1 
ATOM   3595 C C     . HIS B 1 71  ? -61.526 57.843 -37.384 1.00 22.67 ? 212 HIS B C     1 
ATOM   3596 O O     . HIS B 1 71  ? -60.643 58.653 -37.081 1.00 21.84 ? 212 HIS B O     1 
ATOM   3597 C CB    . HIS B 1 71  ? -61.672 55.309 -37.269 1.00 23.10 ? 212 HIS B CB    1 
ATOM   3598 C CG    . HIS B 1 71  ? -60.838 55.005 -36.057 1.00 21.03 ? 212 HIS B CG    1 
ATOM   3599 N ND1   . HIS B 1 71  ? -60.822 55.814 -34.939 1.00 19.71 ? 212 HIS B ND1   1 
ATOM   3600 C CD2   . HIS B 1 71  ? -60.006 53.970 -35.781 1.00 25.40 ? 212 HIS B CD2   1 
ATOM   3601 C CE1   . HIS B 1 71  ? -60.019 55.291 -34.028 1.00 19.10 ? 212 HIS B CE1   1 
ATOM   3602 N NE2   . HIS B 1 71  ? -59.510 54.171 -34.511 1.00 19.73 ? 212 HIS B NE2   1 
ATOM   3603 N N     . GLU B 1 72  ? -62.817 58.041 -37.124 1.00 24.12 ? 213 GLU B N     1 
ATOM   3604 C CA    . GLU B 1 72  ? -63.316 59.346 -36.704 1.00 22.38 ? 213 GLU B CA    1 
ATOM   3605 C C     . GLU B 1 72  ? -62.688 59.792 -35.386 1.00 23.15 ? 213 GLU B C     1 
ATOM   3606 O O     . GLU B 1 72  ? -62.095 60.878 -35.307 1.00 25.54 ? 213 GLU B O     1 
ATOM   3607 C CB    . GLU B 1 72  ? -64.848 59.292 -36.611 1.00 24.27 ? 213 GLU B CB    1 
ATOM   3608 C CG    . GLU B 1 72  ? -65.509 60.467 -35.907 1.00 25.40 ? 213 GLU B CG    1 
ATOM   3609 C CD    . GLU B 1 72  ? -65.253 61.787 -36.602 1.00 27.57 ? 213 GLU B CD    1 
ATOM   3610 O OE1   . GLU B 1 72  ? -64.891 61.781 -37.804 1.00 29.58 ? 213 GLU B OE1   1 
ATOM   3611 O OE2   . GLU B 1 72  ? -65.414 62.838 -35.944 1.00 30.60 ? 213 GLU B OE2   1 
ATOM   3612 N N     . LEU B 1 73  ? -62.785 58.961 -34.341 1.00 19.38 ? 214 LEU B N     1 
ATOM   3613 C CA    . LEU B 1 73  ? -62.201 59.342 -33.052 1.00 20.67 ? 214 LEU B CA    1 
ATOM   3614 C C     . LEU B 1 73  ? -60.691 59.531 -33.153 1.00 19.07 ? 214 LEU B C     1 
ATOM   3615 O O     . LEU B 1 73  ? -60.132 60.409 -32.489 1.00 19.78 ? 214 LEU B O     1 
ATOM   3616 C CB    . LEU B 1 73  ? -62.532 58.313 -31.966 1.00 15.47 ? 214 LEU B CB    1 
ATOM   3617 C CG    . LEU B 1 73  ? -64.003 58.162 -31.575 1.00 21.90 ? 214 LEU B CG    1 
ATOM   3618 C CD1   . LEU B 1 73  ? -64.149 57.261 -30.351 1.00 16.41 ? 214 LEU B CD1   1 
ATOM   3619 C CD2   . LEU B 1 73  ? -64.622 59.516 -31.316 1.00 22.12 ? 214 LEU B CD2   1 
ATOM   3620 N N     . ALA B 1 74  ? -60.006 58.710 -33.959 1.00 16.99 ? 215 ALA B N     1 
ATOM   3621 C CA    . ALA B 1 74  ? -58.576 58.933 -34.159 1.00 18.57 ? 215 ALA B CA    1 
ATOM   3622 C C     . ALA B 1 74  ? -58.318 60.314 -34.750 1.00 21.42 ? 215 ALA B C     1 
ATOM   3623 O O     . ALA B 1 74  ? -57.350 60.983 -34.376 1.00 20.20 ? 215 ALA B O     1 
ATOM   3624 C CB    . ALA B 1 74  ? -57.975 57.841 -35.051 1.00 21.90 ? 215 ALA B CB    1 
ATOM   3625 N N     . ALA B 1 75  ? -59.207 60.779 -35.640 1.00 20.46 ? 216 ALA B N     1 
ATOM   3626 C CA    . ALA B 1 75  ? -59.052 62.109 -36.229 1.00 21.58 ? 216 ALA B CA    1 
ATOM   3627 C C     . ALA B 1 75  ? -59.311 63.211 -35.203 1.00 21.32 ? 216 ALA B C     1 
ATOM   3628 O O     . ALA B 1 75  ? -58.591 64.215 -35.172 1.00 22.39 ? 216 ALA B O     1 
ATOM   3629 C CB    . ALA B 1 75  ? -59.985 62.271 -37.431 1.00 21.76 ? 216 ALA B CB    1 
ATOM   3630 N N     . ARG B 1 76  ? -60.338 63.048 -34.365 1.00 19.81 ? 217 ARG B N     1 
ATOM   3631 C CA    . ARG B 1 76  ? -60.560 63.987 -33.262 1.00 21.79 ? 217 ARG B CA    1 
ATOM   3632 C C     . ARG B 1 76  ? -59.341 64.067 -32.332 1.00 20.82 ? 217 ARG B C     1 
ATOM   3633 O O     . ARG B 1 76  ? -58.886 65.161 -31.963 1.00 21.14 ? 217 ARG B O     1 
ATOM   3634 C CB    . ARG B 1 76  ? -61.804 63.569 -32.481 1.00 20.44 ? 217 ARG B CB    1 
ATOM   3635 C CG    . ARG B 1 76  ? -63.083 63.553 -33.303 1.00 23.98 ? 217 ARG B CG    1 
ATOM   3636 C CD    . ARG B 1 76  ? -64.273 63.254 -32.408 1.00 23.87 ? 217 ARG B CD    1 
ATOM   3637 N NE    . ARG B 1 76  ? -65.494 63.056 -33.177 1.00 25.42 ? 217 ARG B NE    1 
ATOM   3638 C CZ    . ARG B 1 76  ? -66.659 62.703 -32.654 1.00 28.07 ? 217 ARG B CZ    1 
ATOM   3639 N NH1   . ARG B 1 76  ? -66.793 62.471 -31.358 1.00 21.65 ? 217 ARG B NH1   1 
ATOM   3640 N NH2   . ARG B 1 76  ? -67.718 62.583 -33.451 1.00 27.78 ? 217 ARG B NH2   1 
ATOM   3641 N N     . ALA B 1 77  ? -58.795 62.912 -31.946 1.00 18.78 ? 218 ALA B N     1 
ATOM   3642 C CA    . ALA B 1 77  ? -57.622 62.898 -31.072 1.00 19.79 ? 218 ALA B CA    1 
ATOM   3643 C C     . ALA B 1 77  ? -56.415 63.546 -31.746 1.00 18.22 ? 218 ALA B C     1 
ATOM   3644 O O     . ALA B 1 77  ? -55.655 64.281 -31.104 1.00 16.50 ? 218 ALA B O     1 
ATOM   3645 C CB    . ALA B 1 77  ? -57.298 61.462 -30.646 1.00 16.00 ? 218 ALA B CB    1 
ATOM   3646 N N     . THR B 1 78  ? -56.219 63.288 -33.038 1.00 19.51 ? 219 THR B N     1 
ATOM   3647 C CA    . THR B 1 78  ? -55.101 63.906 -33.745 1.00 21.74 ? 219 THR B CA    1 
ATOM   3648 C C     . THR B 1 78  ? -55.254 65.417 -33.804 1.00 20.30 ? 219 THR B C     1 
ATOM   3649 O O     . THR B 1 78  ? -54.289 66.154 -33.566 1.00 21.22 ? 219 THR B O     1 
ATOM   3650 C CB    . THR B 1 78  ? -54.973 63.331 -35.150 1.00 25.98 ? 219 THR B CB    1 
ATOM   3651 O OG1   . THR B 1 78  ? -54.848 61.908 -35.062 1.00 27.12 ? 219 THR B OG1   1 
ATOM   3652 C CG2   . THR B 1 78  ? -53.739 63.904 -35.852 1.00 28.27 ? 219 THR B CG2   1 
ATOM   3653 N N     . ASP B 1 79  ? -56.458 65.900 -34.141 1.00 22.31 ? 220 ASP B N     1 
ATOM   3654 C CA    . ASP B 1 79  ? -56.696 67.341 -34.139 1.00 25.05 ? 220 ASP B CA    1 
ATOM   3655 C C     . ASP B 1 79  ? -56.350 67.947 -32.785 1.00 23.36 ? 220 ASP B C     1 
ATOM   3656 O O     . ASP B 1 79  ? -55.642 68.960 -32.705 1.00 20.36 ? 220 ASP B O     1 
ATOM   3657 C CB    . ASP B 1 79  ? -58.153 67.656 -34.490 1.00 22.59 ? 220 ASP B CB    1 
ATOM   3658 C CG    . ASP B 1 79  ? -58.465 67.453 -35.967 1.00 33.07 ? 220 ASP B CG    1 
ATOM   3659 O OD1   . ASP B 1 79  ? -57.520 67.440 -36.779 1.00 31.97 ? 220 ASP B OD1   1 
ATOM   3660 O OD2   . ASP B 1 79  ? -59.664 67.335 -36.316 1.00 40.25 ? 220 ASP B OD2   1 
ATOM   3661 N N     . ALA B 1 80  ? -56.844 67.333 -31.706 1.00 17.22 ? 221 ALA B N     1 
ATOM   3662 C CA    . ALA B 1 80  ? -56.628 67.920 -30.387 1.00 21.10 ? 221 ALA B CA    1 
ATOM   3663 C C     . ALA B 1 80  ? -55.144 67.909 -30.000 1.00 17.85 ? 221 ALA B C     1 
ATOM   3664 O O     . ALA B 1 80  ? -54.637 68.896 -29.451 1.00 18.50 ? 221 ALA B O     1 
ATOM   3665 C CB    . ALA B 1 80  ? -57.484 67.188 -29.355 1.00 17.04 ? 221 ALA B CB    1 
ATOM   3666 N N     . TYR B 1 81  ? -54.430 66.814 -30.298 1.00 16.65 ? 222 TYR B N     1 
ATOM   3667 C CA    . TYR B 1 81  ? -53.003 66.703 -29.972 1.00 17.02 ? 222 TYR B CA    1 
ATOM   3668 C C     . TYR B 1 81  ? -52.169 67.711 -30.764 1.00 19.93 ? 222 TYR B C     1 
ATOM   3669 O O     . TYR B 1 81  ? -51.279 68.375 -30.211 1.00 16.88 ? 222 TYR B O     1 
ATOM   3670 C CB    . TYR B 1 81  ? -52.523 65.279 -30.265 1.00 18.64 ? 222 TYR B CB    1 
ATOM   3671 C CG    . TYR B 1 81  ? -51.244 64.813 -29.568 1.00 19.73 ? 222 TYR B CG    1 
ATOM   3672 C CD1   . TYR B 1 81  ? -51.030 65.061 -28.213 1.00 19.80 ? 222 TYR B CD1   1 
ATOM   3673 C CD2   . TYR B 1 81  ? -50.288 64.067 -30.256 1.00 23.86 ? 222 TYR B CD2   1 
ATOM   3674 C CE1   . TYR B 1 81  ? -49.889 64.604 -27.564 1.00 20.21 ? 222 TYR B CE1   1 
ATOM   3675 C CE2   . TYR B 1 81  ? -49.134 63.596 -29.616 1.00 22.21 ? 222 TYR B CE2   1 
ATOM   3676 C CZ    . TYR B 1 81  ? -48.948 63.871 -28.268 1.00 24.04 ? 222 TYR B CZ    1 
ATOM   3677 O OH    . TYR B 1 81  ? -47.829 63.423 -27.606 1.00 20.38 ? 222 TYR B OH    1 
ATOM   3678 N N     . GLU B 1 82  ? -52.433 67.829 -32.073 1.00 19.24 ? 223 GLU B N     1 
ATOM   3679 C CA    . GLU B 1 82  ? -51.742 68.840 -32.874 1.00 22.41 ? 223 GLU B CA    1 
ATOM   3680 C C     . GLU B 1 82  ? -52.013 70.251 -32.357 1.00 21.12 ? 223 GLU B C     1 
ATOM   3681 O O     . GLU B 1 82  ? -51.101 71.090 -32.297 1.00 21.12 ? 223 GLU B O     1 
ATOM   3682 C CB    . GLU B 1 82  ? -52.150 68.723 -34.349 1.00 22.30 ? 223 GLU B CB    1 
ATOM   3683 C CG    . GLU B 1 82  ? -51.753 67.371 -34.980 1.00 31.30 ? 223 GLU B CG    1 
ATOM   3684 C CD    . GLU B 1 82  ? -52.211 67.200 -36.447 1.00 37.18 ? 223 GLU B CD    1 
ATOM   3685 O OE1   . GLU B 1 82  ? -53.134 67.919 -36.909 1.00 35.29 ? 223 GLU B OE1   1 
ATOM   3686 O OE2   . GLU B 1 82  ? -51.616 66.347 -37.147 1.00 40.37 ? 223 GLU B OE2   1 
ATOM   3687 N N     . ASP B 1 83  ? -53.264 70.539 -32.000 1.00 20.57 ? 224 ASP B N     1 
ATOM   3688 C CA    . ASP B 1 83  ? -53.580 71.858 -31.466 1.00 21.03 ? 224 ASP B CA    1 
ATOM   3689 C C     . ASP B 1 83  ? -52.866 72.113 -30.137 1.00 22.12 ? 224 ASP B C     1 
ATOM   3690 O O     . ASP B 1 83  ? -52.446 73.242 -29.860 1.00 19.70 ? 224 ASP B O     1 
ATOM   3691 C CB    . ASP B 1 83  ? -55.087 71.995 -31.302 1.00 25.17 ? 224 ASP B CB    1 
ATOM   3692 C CG    . ASP B 1 83  ? -55.764 72.461 -32.571 1.00 38.93 ? 224 ASP B CG    1 
ATOM   3693 O OD1   . ASP B 1 83  ? -55.089 72.490 -33.633 1.00 41.87 ? 224 ASP B OD1   1 
ATOM   3694 O OD2   . ASP B 1 83  ? -56.960 72.824 -32.504 1.00 47.94 ? 224 ASP B OD2   1 
ATOM   3695 N N     . ALA B 1 84  ? -52.722 71.084 -29.298 1.00 16.31 ? 225 ALA B N     1 
ATOM   3696 C CA    . ALA B 1 84  ? -51.978 71.278 -28.056 1.00 17.34 ? 225 ALA B CA    1 
ATOM   3697 C C     . ALA B 1 84  ? -50.516 71.614 -28.341 1.00 16.80 ? 225 ALA B C     1 
ATOM   3698 O O     . ALA B 1 84  ? -49.939 72.527 -27.722 1.00 19.08 ? 225 ALA B O     1 
ATOM   3699 C CB    . ALA B 1 84  ? -52.081 70.031 -27.175 1.00 18.82 ? 225 ALA B CB    1 
ATOM   3700 N N     . ARG B 1 85  ? -49.899 70.886 -29.278 1.00 16.69 ? 226 ARG B N     1 
ATOM   3701 C CA    . ARG B 1 85  ? -48.496 71.162 -29.591 1.00 18.07 ? 226 ARG B CA    1 
ATOM   3702 C C     . ARG B 1 85  ? -48.338 72.576 -30.147 1.00 19.59 ? 226 ARG B C     1 
ATOM   3703 O O     . ARG B 1 85  ? -47.373 73.284 -29.818 1.00 19.08 ? 226 ARG B O     1 
ATOM   3704 C CB    . ARG B 1 85  ? -47.942 70.112 -30.568 1.00 15.77 ? 226 ARG B CB    1 
ATOM   3705 C CG    . ARG B 1 85  ? -46.398 70.072 -30.625 1.00 18.11 ? 226 ARG B CG    1 
ATOM   3706 C CD    . ARG B 1 85  ? -45.860 69.139 -31.738 1.00 19.34 ? 226 ARG B CD    1 
ATOM   3707 N NE    . ARG B 1 85  ? -46.342 67.772 -31.570 1.00 14.85 ? 226 ARG B NE    1 
ATOM   3708 C CZ    . ARG B 1 85  ? -45.779 66.860 -30.786 1.00 18.02 ? 226 ARG B CZ    1 
ATOM   3709 N NH1   . ARG B 1 85  ? -44.683 67.120 -30.087 1.00 15.28 ? 226 ARG B NH1   1 
ATOM   3710 N NH2   . ARG B 1 85  ? -46.324 65.654 -30.706 1.00 18.03 ? 226 ARG B NH2   1 
ATOM   3711 N N     . GLU B 1 86  ? -49.302 73.021 -30.962 1.00 21.07 ? 227 GLU B N     1 
ATOM   3712 C CA    . GLU B 1 86  ? -49.237 74.372 -31.515 1.00 20.22 ? 227 GLU B CA    1 
ATOM   3713 C C     . GLU B 1 86  ? -49.481 75.453 -30.458 1.00 21.55 ? 227 GLU B C     1 
ATOM   3714 O O     . GLU B 1 86  ? -48.878 76.531 -30.533 1.00 21.28 ? 227 GLU B O     1 
ATOM   3715 C CB    . GLU B 1 86  ? -50.225 74.494 -32.676 1.00 25.94 ? 227 GLU B CB    1 
ATOM   3716 C CG    . GLU B 1 86  ? -50.578 75.926 -33.096 1.00 26.62 ? 227 GLU B CG    1 
ATOM   3717 C CD    . GLU B 1 86  ? -49.376 76.681 -33.657 1.00 29.91 ? 227 GLU B CD    1 
ATOM   3718 O OE1   . GLU B 1 86  ? -48.382 76.022 -34.061 1.00 26.35 ? 227 GLU B OE1   1 
ATOM   3719 O OE2   . GLU B 1 86  ? -49.451 77.931 -33.748 1.00 29.31 ? 227 GLU B OE2   1 
ATOM   3720 N N     . ALA B 1 87  ? -50.331 75.186 -29.458 1.00 22.39 ? 228 ALA B N     1 
ATOM   3721 C CA    . ALA B 1 87  ? -50.482 76.130 -28.349 1.00 19.37 ? 228 ALA B CA    1 
ATOM   3722 C C     . ALA B 1 87  ? -49.175 76.282 -27.573 1.00 22.14 ? 228 ALA B C     1 
ATOM   3723 O O     . ALA B 1 87  ? -48.794 77.400 -27.194 1.00 18.25 ? 228 ALA B O     1 
ATOM   3724 C CB    . ALA B 1 87  ? -51.601 75.681 -27.411 1.00 17.27 ? 228 ALA B CB    1 
ATOM   3725 N N     . VAL B 1 88  ? -48.463 75.171 -27.334 1.00 19.18 ? 229 VAL B N     1 
ATOM   3726 C CA    . VAL B 1 88  ? -47.166 75.288 -26.660 1.00 18.70 ? 229 VAL B CA    1 
ATOM   3727 C C     . VAL B 1 88  ? -46.189 76.107 -27.502 1.00 19.35 ? 229 VAL B C     1 
ATOM   3728 O O     . VAL B 1 88  ? -45.502 77.006 -26.987 1.00 18.42 ? 229 VAL B O     1 
ATOM   3729 C CB    . VAL B 1 88  ? -46.581 73.905 -26.336 1.00 18.63 ? 229 VAL B CB    1 
ATOM   3730 C CG1   . VAL B 1 88  ? -45.139 74.074 -25.872 1.00 16.68 ? 229 VAL B CG1   1 
ATOM   3731 C CG2   . VAL B 1 88  ? -47.397 73.224 -25.256 1.00 17.18 ? 229 VAL B CG2   1 
ATOM   3732 N N     . ARG B 1 89  ? -46.092 75.784 -28.801 1.00 16.47 ? 230 ARG B N     1 
ATOM   3733 C CA    . ARG B 1 89  ? -45.182 76.505 -29.693 1.00 18.78 ? 230 ARG B CA    1 
ATOM   3734 C C     . ARG B 1 89  ? -45.450 78.001 -29.658 1.00 21.13 ? 230 ARG B C     1 
ATOM   3735 O O     . ARG B 1 89  ? -44.524 78.812 -29.496 1.00 19.72 ? 230 ARG B O     1 
ATOM   3736 C CB    . ARG B 1 89  ? -45.314 75.995 -31.131 1.00 18.48 ? 230 ARG B CB    1 
ATOM   3737 C CG    . ARG B 1 89  ? -44.347 76.677 -32.111 1.00 19.23 ? 230 ARG B CG    1 
ATOM   3738 C CD    . ARG B 1 89  ? -44.925 76.797 -33.533 1.00 24.84 ? 230 ARG B CD    1 
ATOM   3739 N NE    . ARG B 1 89  ? -46.117 77.642 -33.605 1.00 22.03 ? 230 ARG B NE    1 
ATOM   3740 C CZ    . ARG B 1 89  ? -46.124 78.962 -33.450 1.00 27.85 ? 230 ARG B CZ    1 
ATOM   3741 N NH1   . ARG B 1 89  ? -45.016 79.635 -33.177 1.00 26.29 ? 230 ARG B NH1   1 
ATOM   3742 N NH2   . ARG B 1 89  ? -47.274 79.623 -33.565 1.00 24.70 ? 230 ARG B NH2   1 
ATOM   3743 N N     . ARG B 1 90  ? -46.724 78.380 -29.798 1.00 21.96 ? 231 ARG B N     1 
ATOM   3744 C CA    . ARG B 1 90  ? -47.096 79.784 -29.742 1.00 22.43 ? 231 ARG B CA    1 
ATOM   3745 C C     . ARG B 1 90  ? -46.709 80.396 -28.407 1.00 23.73 ? 231 ARG B C     1 
ATOM   3746 O O     . ARG B 1 90  ? -46.108 81.479 -28.352 1.00 23.21 ? 231 ARG B O     1 
ATOM   3747 C CB    . ARG B 1 90  ? -48.599 79.933 -29.979 1.00 25.78 ? 231 ARG B CB    1 
ATOM   3748 C CG    . ARG B 1 90  ? -49.103 81.373 -29.921 1.00 23.48 ? 231 ARG B CG    1 
ATOM   3749 C CD    . ARG B 1 90  ? -50.618 81.402 -30.084 1.00 28.90 ? 231 ARG B CD    1 
ATOM   3750 N NE    . ARG B 1 90  ? -51.274 80.780 -28.936 1.00 28.00 ? 231 ARG B NE    1 
ATOM   3751 C CZ    . ARG B 1 90  ? -52.008 79.676 -28.987 1.00 26.11 ? 231 ARG B CZ    1 
ATOM   3752 N NH1   . ARG B 1 90  ? -52.214 79.034 -30.124 1.00 20.39 ? 231 ARG B NH1   1 
ATOM   3753 N NH2   . ARG B 1 90  ? -52.530 79.191 -27.860 1.00 28.10 ? 231 ARG B NH2   1 
ATOM   3754 N N     . PHE B 1 91  ? -47.046 79.711 -27.313 1.00 23.73 ? 232 PHE B N     1 
ATOM   3755 C CA    . PHE B 1 91  ? -46.894 80.322 -26.003 1.00 21.92 ? 232 PHE B CA    1 
ATOM   3756 C C     . PHE B 1 91  ? -45.431 80.585 -25.677 1.00 21.44 ? 232 PHE B C     1 
ATOM   3757 O O     . PHE B 1 91  ? -45.113 81.593 -25.041 1.00 22.72 ? 232 PHE B O     1 
ATOM   3758 C CB    . PHE B 1 91  ? -47.519 79.435 -24.930 1.00 21.49 ? 232 PHE B CB    1 
ATOM   3759 C CG    . PHE B 1 91  ? -47.580 80.093 -23.589 1.00 23.29 ? 232 PHE B CG    1 
ATOM   3760 C CD1   . PHE B 1 91  ? -48.409 81.186 -23.388 1.00 25.54 ? 232 PHE B CD1   1 
ATOM   3761 C CD2   . PHE B 1 91  ? -46.799 79.637 -22.542 1.00 23.84 ? 232 PHE B CD2   1 
ATOM   3762 C CE1   . PHE B 1 91  ? -48.468 81.818 -22.148 1.00 28.20 ? 232 PHE B CE1   1 
ATOM   3763 C CE2   . PHE B 1 91  ? -46.850 80.251 -21.306 1.00 23.84 ? 232 PHE B CE2   1 
ATOM   3764 C CZ    . PHE B 1 91  ? -47.682 81.353 -21.111 1.00 23.35 ? 232 PHE B CZ    1 
ATOM   3765 N N     . ILE B 1 92  ? -44.521 79.692 -26.085 1.00 22.97 ? 233 ILE B N     1 
ATOM   3766 C CA    . ILE B 1 92  ? -43.114 79.916 -25.765 1.00 23.23 ? 233 ILE B CA    1 
ATOM   3767 C C     . ILE B 1 92  ? -42.347 80.574 -26.904 1.00 23.46 ? 233 ILE B C     1 
ATOM   3768 O O     . ILE B 1 92  ? -41.143 80.828 -26.764 1.00 26.06 ? 233 ILE B O     1 
ATOM   3769 C CB    . ILE B 1 92  ? -42.417 78.618 -25.316 1.00 21.98 ? 233 ILE B CB    1 
ATOM   3770 C CG1   . ILE B 1 92  ? -42.326 77.597 -26.455 1.00 22.28 ? 233 ILE B CG1   1 
ATOM   3771 C CG2   . ILE B 1 92  ? -43.155 78.033 -24.142 1.00 22.62 ? 233 ILE B CG2   1 
ATOM   3772 C CD1   . ILE B 1 92  ? -41.370 76.448 -26.145 1.00 18.37 ? 233 ILE B CD1   1 
ATOM   3773 N N     . GLY B 1 93  ? -43.005 80.890 -28.013 1.00 21.89 ? 234 GLY B N     1 
ATOM   3774 C CA    . GLY B 1 93  ? -42.311 81.581 -29.080 1.00 19.78 ? 234 GLY B CA    1 
ATOM   3775 C C     . GLY B 1 93  ? -41.320 80.732 -29.841 1.00 24.18 ? 234 GLY B C     1 
ATOM   3776 O O     . GLY B 1 93  ? -40.322 81.260 -30.335 1.00 26.58 ? 234 GLY B O     1 
ATOM   3777 N N     . ALA B 1 94  ? -41.561 79.427 -29.950 1.00 20.67 ? 235 ALA B N     1 
ATOM   3778 C CA    . ALA B 1 94  ? -40.738 78.586 -30.809 1.00 19.78 ? 235 ALA B CA    1 
ATOM   3779 C C     . ALA B 1 94  ? -41.122 78.790 -32.272 1.00 22.37 ? 235 ALA B C     1 
ATOM   3780 O O     . ALA B 1 94  ? -42.282 79.049 -32.603 1.00 23.98 ? 235 ALA B O     1 
ATOM   3781 C CB    . ALA B 1 94  ? -40.890 77.110 -30.428 1.00 15.94 ? 235 ALA B CB    1 
ATOM   3782 N N     . ALA B 1 95  ? -40.133 78.661 -33.162 1.00 25.00 ? 236 ALA B N     1 
ATOM   3783 C CA    . ALA B 1 95  ? -40.408 78.876 -34.585 1.00 21.96 ? 236 ALA B CA    1 
ATOM   3784 C C     . ALA B 1 95  ? -41.234 77.746 -35.197 1.00 23.33 ? 236 ALA B C     1 
ATOM   3785 O O     . ALA B 1 95  ? -42.031 77.996 -36.101 1.00 21.86 ? 236 ALA B O     1 
ATOM   3786 C CB    . ALA B 1 95  ? -39.100 79.040 -35.365 1.00 21.44 ? 236 ALA B CB    1 
ATOM   3787 N N     . LYS B 1 96  ? -41.073 76.499 -34.733 1.00 23.28 ? 237 LYS B N     1 
ATOM   3788 C CA    . LYS B 1 96  ? -41.726 75.373 -35.393 1.00 19.92 ? 237 LYS B CA    1 
ATOM   3789 C C     . LYS B 1 96  ? -42.319 74.414 -34.375 1.00 22.11 ? 237 LYS B C     1 
ATOM   3790 O O     . LYS B 1 96  ? -41.744 74.192 -33.303 1.00 19.94 ? 237 LYS B O     1 
ATOM   3791 C CB    . LYS B 1 96  ? -40.743 74.604 -36.295 1.00 23.71 ? 237 LYS B CB    1 
ATOM   3792 C CG    . LYS B 1 96  ? -40.292 75.378 -37.534 1.00 24.44 ? 237 LYS B CG    1 
ATOM   3793 C CD    . LYS B 1 96  ? -39.310 74.558 -38.369 1.00 27.56 ? 237 LYS B CD    1 
ATOM   3794 C CE    . LYS B 1 96  ? -38.901 75.325 -39.623 1.00 30.23 ? 237 LYS B CE    1 
ATOM   3795 N NZ    . LYS B 1 96  ? -37.798 74.626 -40.325 1.00 30.55 ? 237 LYS B NZ    1 
ATOM   3796 N N     . ALA B 1 97  ? -43.462 73.823 -34.732 1.00 24.17 ? 238 ALA B N     1 
ATOM   3797 C CA    . ALA B 1 97  ? -44.057 72.790 -33.891 1.00 23.77 ? 238 ALA B CA    1 
ATOM   3798 C C     . ALA B 1 97  ? -43.133 71.583 -33.737 1.00 22.35 ? 238 ALA B C     1 
ATOM   3799 O O     . ALA B 1 97  ? -43.169 70.905 -32.703 1.00 21.83 ? 238 ALA B O     1 
ATOM   3800 C CB    . ALA B 1 97  ? -45.405 72.354 -34.470 1.00 24.67 ? 238 ALA B CB    1 
ATOM   3801 N N     . GLU B 1 98  ? -42.298 71.307 -34.743 1.00 18.57 ? 239 GLU B N     1 
ATOM   3802 C CA    . GLU B 1 98  ? -41.345 70.204 -34.704 1.00 21.61 ? 239 GLU B CA    1 
ATOM   3803 C C     . GLU B 1 98  ? -40.250 70.402 -33.670 1.00 20.92 ? 239 GLU B C     1 
ATOM   3804 O O     . GLU B 1 98  ? -39.453 69.481 -33.460 1.00 22.12 ? 239 GLU B O     1 
ATOM   3805 C CB    . GLU B 1 98  ? -40.689 70.022 -36.068 1.00 24.78 ? 239 GLU B CB    1 
ATOM   3806 C CG    . GLU B 1 98  ? -41.624 69.548 -37.186 1.00 31.63 ? 239 GLU B CG    1 
ATOM   3807 C CD    . GLU B 1 98  ? -42.502 70.675 -37.688 1.00 34.15 ? 239 GLU B CD    1 
ATOM   3808 O OE1   . GLU B 1 98  ? -42.103 71.851 -37.541 1.00 31.80 ? 239 GLU B OE1   1 
ATOM   3809 O OE2   . GLU B 1 98  ? -43.579 70.384 -38.250 1.00 48.62 ? 239 GLU B OE2   1 
ATOM   3810 N N     . GLU B 1 99  ? -40.150 71.585 -33.074 1.00 19.06 ? 240 GLU B N     1 
ATOM   3811 C CA    . GLU B 1 99  ? -39.189 71.840 -32.011 1.00 18.20 ? 240 GLU B CA    1 
ATOM   3812 C C     . GLU B 1 99  ? -39.765 71.567 -30.629 1.00 18.04 ? 240 GLU B C     1 
ATOM   3813 O O     . GLU B 1 99  ? -39.057 71.760 -29.631 1.00 16.13 ? 240 GLU B O     1 
ATOM   3814 C CB    . GLU B 1 99  ? -38.676 73.291 -32.110 1.00 18.26 ? 240 GLU B CB    1 
ATOM   3815 C CG    . GLU B 1 99  ? -37.848 73.534 -33.397 1.00 21.54 ? 240 GLU B CG    1 
ATOM   3816 C CD    . GLU B 1 99  ? -37.485 74.998 -33.621 1.00 24.49 ? 240 GLU B CD    1 
ATOM   3817 O OE1   . GLU B 1 99  ? -38.348 75.877 -33.394 1.00 20.97 ? 240 GLU B OE1   1 
ATOM   3818 O OE2   . GLU B 1 99  ? -36.334 75.272 -34.040 1.00 24.58 ? 240 GLU B OE2   1 
ATOM   3819 N N     . ILE B 1 100 ? -41.024 71.120 -30.551 1.00 18.87 ? 241 ILE B N     1 
ATOM   3820 C CA    . ILE B 1 100 ? -41.723 70.875 -29.286 1.00 16.93 ? 241 ILE B CA    1 
ATOM   3821 C C     . ILE B 1 100 ? -41.835 69.369 -29.077 1.00 16.89 ? 241 ILE B C     1 
ATOM   3822 O O     . ILE B 1 100 ? -42.484 68.672 -29.870 1.00 15.63 ? 241 ILE B O     1 
ATOM   3823 C CB    . ILE B 1 100 ? -43.120 71.515 -29.270 1.00 17.18 ? 241 ILE B CB    1 
ATOM   3824 C CG1   . ILE B 1 100 ? -43.038 73.027 -29.543 1.00 16.91 ? 241 ILE B CG1   1 
ATOM   3825 C CG2   . ILE B 1 100 ? -43.851 71.174 -27.953 1.00 13.02 ? 241 ILE B CG2   1 
ATOM   3826 C CD1   . ILE B 1 100 ? -42.142 73.817 -28.563 1.00 17.46 ? 241 ILE B CD1   1 
ATOM   3827 N N     . ILE B 1 101 ? -41.233 68.871 -27.998 1.00 15.10 ? 242 ILE B N     1 
ATOM   3828 C CA    . ILE B 1 101 ? -41.275 67.463 -27.621 1.00 14.12 ? 242 ILE B CA    1 
ATOM   3829 C C     . ILE B 1 101 ? -42.103 67.342 -26.348 1.00 15.44 ? 242 ILE B C     1 
ATOM   3830 O O     . ILE B 1 101 ? -41.817 68.019 -25.353 1.00 14.84 ? 242 ILE B O     1 
ATOM   3831 C CB    . ILE B 1 101 ? -39.852 66.903 -27.406 1.00 13.12 ? 242 ILE B CB    1 
ATOM   3832 C CG1   . ILE B 1 101 ? -38.906 67.279 -28.565 1.00 16.37 ? 242 ILE B CG1   1 
ATOM   3833 C CG2   . ILE B 1 101 ? -39.876 65.373 -27.186 1.00 14.44 ? 242 ILE B CG2   1 
ATOM   3834 C CD1   . ILE B 1 101 ? -39.352 66.757 -29.902 1.00 22.12 ? 242 ILE B CD1   1 
ATOM   3835 N N     . PHE B 1 102 ? -43.136 66.501 -26.382 1.00 14.70 ? 243 PHE B N     1 
ATOM   3836 C CA    . PHE B 1 102 ? -43.915 66.192 -25.189 1.00 14.30 ? 243 PHE B CA    1 
ATOM   3837 C C     . PHE B 1 102 ? -43.280 65.025 -24.438 1.00 14.99 ? 243 PHE B C     1 
ATOM   3838 O O     . PHE B 1 102 ? -42.843 64.040 -25.049 1.00 15.34 ? 243 PHE B O     1 
ATOM   3839 C CB    . PHE B 1 102 ? -45.360 65.828 -25.544 1.00 16.20 ? 243 PHE B CB    1 
ATOM   3840 C CG    . PHE B 1 102 ? -46.236 67.005 -25.875 1.00 15.52 ? 243 PHE B CG    1 
ATOM   3841 C CD1   . PHE B 1 102 ? -46.342 68.089 -25.002 1.00 17.99 ? 243 PHE B CD1   1 
ATOM   3842 C CD2   . PHE B 1 102 ? -46.969 67.020 -27.054 1.00 15.90 ? 243 PHE B CD2   1 
ATOM   3843 C CE1   . PHE B 1 102 ? -47.167 69.179 -25.303 1.00 16.91 ? 243 PHE B CE1   1 
ATOM   3844 C CE2   . PHE B 1 102 ? -47.802 68.118 -27.373 1.00 19.68 ? 243 PHE B CE2   1 
ATOM   3845 C CZ    . PHE B 1 102 ? -47.896 69.197 -26.488 1.00 18.73 ? 243 PHE B CZ    1 
ATOM   3846 N N     . LEU B 1 103 ? -43.221 65.148 -23.118 1.00 15.09 ? 244 LEU B N     1 
ATOM   3847 C CA    . LEU B 1 103 ? -42.808 64.046 -22.228 1.00 16.12 ? 244 LEU B CA    1 
ATOM   3848 C C     . LEU B 1 103 ? -43.467 64.286 -20.871 1.00 16.66 ? 244 LEU B C     1 
ATOM   3849 O O     . LEU B 1 103 ? -44.448 65.026 -20.779 1.00 15.82 ? 244 LEU B O     1 
ATOM   3850 C CB    . LEU B 1 103 ? -41.277 63.949 -22.152 1.00 15.87 ? 244 LEU B CB    1 
ATOM   3851 C CG    . LEU B 1 103 ? -40.542 65.217 -22.574 1.00 16.88 ? 244 LEU B CG    1 
ATOM   3852 C CD1   . LEU B 1 103 ? -40.699 66.290 -21.491 1.00 18.05 ? 244 LEU B CD1   1 
ATOM   3853 C CD2   . LEU B 1 103 ? -39.080 64.928 -22.880 1.00 16.30 ? 244 LEU B CD2   1 
ATOM   3854 N N     . ARG B 1 104 ? -42.943 63.669 -19.807 1.00 17.30 ? 245 ARG B N     1 
ATOM   3855 C CA    . ARG B 1 104 ? -43.655 63.719 -18.527 1.00 15.42 ? 245 ARG B CA    1 
ATOM   3856 C C     . ARG B 1 104 ? -43.479 65.051 -17.805 1.00 15.56 ? 245 ARG B C     1 
ATOM   3857 O O     . ARG B 1 104 ? -44.400 65.519 -17.116 1.00 14.00 ? 245 ARG B O     1 
ATOM   3858 C CB    . ARG B 1 104 ? -43.194 62.583 -17.604 1.00 15.27 ? 245 ARG B CB    1 
ATOM   3859 C CG    . ARG B 1 104 ? -43.891 62.610 -16.213 1.00 15.99 ? 245 ARG B CG    1 
ATOM   3860 C CD    . ARG B 1 104 ? -43.667 61.318 -15.403 1.00 19.63 ? 245 ARG B CD    1 
ATOM   3861 N NE    . ARG B 1 104 ? -42.312 60.790 -15.548 1.00 20.01 ? 245 ARG B NE    1 
ATOM   3862 C CZ    . ARG B 1 104 ? -41.991 59.740 -16.300 1.00 26.40 ? 245 ARG B CZ    1 
ATOM   3863 N NH1   . ARG B 1 104 ? -42.913 59.049 -16.962 1.00 22.45 ? 245 ARG B NH1   1 
ATOM   3864 N NH2   . ARG B 1 104 ? -40.713 59.382 -16.404 1.00 19.64 ? 245 ARG B NH2   1 
ATOM   3865 N N     . GLY B 1 105 ? -42.303 65.657 -17.895 1.00 16.57 ? 246 GLY B N     1 
ATOM   3866 C CA    . GLY B 1 105 ? -42.069 66.867 -17.123 1.00 15.10 ? 246 GLY B CA    1 
ATOM   3867 C C     . GLY B 1 105 ? -40.659 67.354 -17.333 1.00 14.51 ? 246 GLY B C     1 
ATOM   3868 O O     . GLY B 1 105 ? -39.899 66.797 -18.128 1.00 16.12 ? 246 GLY B O     1 
ATOM   3869 N N     . THR B 1 106 ? -40.321 68.421 -16.610 1.00 14.28 ? 247 THR B N     1 
ATOM   3870 C CA    . THR B 1 106 ? -38.981 68.997 -16.712 1.00 16.23 ? 247 THR B CA    1 
ATOM   3871 C C     . THR B 1 106 ? -37.899 67.950 -16.496 1.00 12.65 ? 247 THR B C     1 
ATOM   3872 O O     . THR B 1 106 ? -36.872 67.938 -17.191 1.00 13.61 ? 247 THR B O     1 
ATOM   3873 C CB    . THR B 1 106 ? -38.823 70.123 -15.678 1.00 16.80 ? 247 THR B CB    1 
ATOM   3874 O OG1   . THR B 1 106 ? -39.744 71.179 -15.982 1.00 15.72 ? 247 THR B OG1   1 
ATOM   3875 C CG2   . THR B 1 106 ? -37.387 70.672 -15.698 1.00 15.76 ? 247 THR B CG2   1 
ATOM   3876 N N     . THR B 1 107 ? -38.100 67.078 -15.509 1.00 14.10 ? 248 THR B N     1 
ATOM   3877 C CA    . THR B 1 107 ? -37.072 66.117 -15.143 1.00 11.54 ? 248 THR B CA    1 
ATOM   3878 C C     . THR B 1 107 ? -36.807 65.151 -16.294 1.00 12.86 ? 248 THR B C     1 
ATOM   3879 O O     . THR B 1 107 ? -35.646 64.868 -16.626 1.00 12.74 ? 248 THR B O     1 
ATOM   3880 C CB    . THR B 1 107 ? -37.494 65.372 -13.865 1.00 13.91 ? 248 THR B CB    1 
ATOM   3881 O OG1   . THR B 1 107 ? -37.652 66.316 -12.788 1.00 15.89 ? 248 THR B OG1   1 
ATOM   3882 C CG2   . THR B 1 107 ? -36.459 64.334 -13.466 1.00 13.11 ? 248 THR B CG2   1 
ATOM   3883 N N     . GLU B 1 108 ? -37.873 64.634 -16.923 1.00 11.47 ? 249 GLU B N     1 
ATOM   3884 C CA    . GLU B 1 108 ? -37.670 63.764 -18.082 1.00 15.28 ? 249 GLU B CA    1 
ATOM   3885 C C     . GLU B 1 108 ? -36.996 64.516 -19.223 1.00 12.55 ? 249 GLU B C     1 
ATOM   3886 O O     . GLU B 1 108 ? -36.135 63.964 -19.911 1.00 11.56 ? 249 GLU B O     1 
ATOM   3887 C CB    . GLU B 1 108 ? -38.988 63.145 -18.582 1.00 14.42 ? 249 GLU B CB    1 
ATOM   3888 C CG    . GLU B 1 108 ? -38.669 62.021 -19.606 1.00 15.11 ? 249 GLU B CG    1 
ATOM   3889 C CD    . GLU B 1 108 ? -39.882 61.302 -20.191 1.00 22.09 ? 249 GLU B CD    1 
ATOM   3890 O OE1   . GLU B 1 108 ? -39.679 60.385 -21.025 1.00 22.76 ? 249 GLU B OE1   1 
ATOM   3891 O OE2   . GLU B 1 108 ? -41.038 61.663 -19.875 1.00 19.02 ? 249 GLU B OE2   1 
ATOM   3892 N N     . ALA B 1 109 ? -37.388 65.777 -19.448 1.00 13.61 ? 250 ALA B N     1 
ATOM   3893 C CA    . ALA B 1 109 ? -36.803 66.569 -20.534 1.00 12.98 ? 250 ALA B CA    1 
ATOM   3894 C C     . ALA B 1 109 ? -35.296 66.729 -20.356 1.00 13.34 ? 250 ALA B C     1 
ATOM   3895 O O     . ALA B 1 109 ? -34.510 66.547 -21.302 1.00 13.59 ? 250 ALA B O     1 
ATOM   3896 C CB    . ALA B 1 109 ? -37.484 67.939 -20.581 1.00 12.68 ? 250 ALA B CB    1 
ATOM   3897 N N     . ILE B 1 110 ? -34.871 67.062 -19.133 1.00 12.19 ? 251 ILE B N     1 
ATOM   3898 C CA    . ILE B 1 110 ? -33.445 67.198 -18.870 1.00 11.69 ? 251 ILE B CA    1 
ATOM   3899 C C     . ILE B 1 110 ? -32.748 65.852 -19.012 1.00 12.60 ? 251 ILE B C     1 
ATOM   3900 O O     . ILE B 1 110 ? -31.629 65.780 -19.531 1.00 12.37 ? 251 ILE B O     1 
ATOM   3901 C CB    . ILE B 1 110 ? -33.207 67.834 -17.482 1.00 12.27 ? 251 ILE B CB    1 
ATOM   3902 C CG1   . ILE B 1 110 ? -33.741 69.279 -17.472 1.00 11.73 ? 251 ILE B CG1   1 
ATOM   3903 C CG2   . ILE B 1 110 ? -31.721 67.821 -17.127 1.00 11.65 ? 251 ILE B CG2   1 
ATOM   3904 C CD1   . ILE B 1 110 ? -33.744 69.964 -16.072 1.00 14.54 ? 251 ILE B CD1   1 
ATOM   3905 N N     . ASN B 1 111 ? -33.386 64.762 -18.560 1.00 12.51 ? 252 ASN B N     1 
ATOM   3906 C CA    . ASN B 1 111 ? -32.760 63.455 -18.737 1.00 11.33 ? 252 ASN B CA    1 
ATOM   3907 C C     . ASN B 1 111 ? -32.645 63.088 -20.209 1.00 13.34 ? 252 ASN B C     1 
ATOM   3908 O O     . ASN B 1 111 ? -31.681 62.432 -20.604 1.00 11.62 ? 252 ASN B O     1 
ATOM   3909 C CB    . ASN B 1 111 ? -33.529 62.372 -17.974 1.00 11.62 ? 252 ASN B CB    1 
ATOM   3910 C CG    . ASN B 1 111 ? -33.154 62.327 -16.490 1.00 14.84 ? 252 ASN B CG    1 
ATOM   3911 O OD1   . ASN B 1 111 ? -32.184 61.677 -16.108 1.00 14.77 ? 252 ASN B OD1   1 
ATOM   3912 N ND2   . ASN B 1 111 ? -33.909 63.050 -15.652 1.00 11.38 ? 252 ASN B ND2   1 
ATOM   3913 N N     . LEU B 1 112 ? -33.612 63.503 -21.031 1.00 13.38 ? 253 LEU B N     1 
ATOM   3914 C CA    . LEU B 1 112 ? -33.505 63.302 -22.471 1.00 13.12 ? 253 LEU B CA    1 
ATOM   3915 C C     . LEU B 1 112 ? -32.260 63.984 -23.005 1.00 12.40 ? 253 LEU B C     1 
ATOM   3916 O O     . LEU B 1 112 ? -31.455 63.356 -23.697 1.00 13.75 ? 253 LEU B O     1 
ATOM   3917 C CB    . LEU B 1 112 ? -34.756 63.824 -23.196 1.00 13.20 ? 253 LEU B CB    1 
ATOM   3918 C CG    . LEU B 1 112 ? -34.903 63.352 -24.668 1.00 17.35 ? 253 LEU B CG    1 
ATOM   3919 C CD1   . LEU B 1 112 ? -36.374 63.303 -25.104 1.00 16.32 ? 253 LEU B CD1   1 
ATOM   3920 C CD2   . LEU B 1 112 ? -34.139 64.243 -25.625 1.00 15.19 ? 253 LEU B CD2   1 
ATOM   3921 N N     . VAL B 1 113 ? -32.085 65.273 -22.695 1.00 11.79 ? 254 VAL B N     1 
ATOM   3922 C CA    . VAL B 1 113 ? -30.910 65.990 -23.208 1.00 11.95 ? 254 VAL B CA    1 
ATOM   3923 C C     . VAL B 1 113 ? -29.612 65.370 -22.685 1.00 13.47 ? 254 VAL B C     1 
ATOM   3924 O O     . VAL B 1 113 ? -28.635 65.225 -23.430 1.00 16.00 ? 254 VAL B O     1 
ATOM   3925 C CB    . VAL B 1 113 ? -30.974 67.491 -22.861 1.00 14.33 ? 254 VAL B CB    1 
ATOM   3926 C CG1   . VAL B 1 113 ? -29.734 68.213 -23.434 1.00 11.88 ? 254 VAL B CG1   1 
ATOM   3927 C CG2   . VAL B 1 113 ? -32.254 68.107 -23.386 1.00 12.71 ? 254 VAL B CG2   1 
ATOM   3928 N N     . ALA B 1 114 ? -29.578 64.999 -21.402 1.00 12.87 ? 255 ALA B N     1 
ATOM   3929 C CA    . ALA B 1 114 ? -28.359 64.443 -20.810 1.00 15.66 ? 255 ALA B CA    1 
ATOM   3930 C C     . ALA B 1 114 ? -28.013 63.082 -21.410 1.00 15.87 ? 255 ALA B C     1 
ATOM   3931 O O     . ALA B 1 114 ? -26.868 62.847 -21.809 1.00 17.68 ? 255 ALA B O     1 
ATOM   3932 C CB    . ALA B 1 114 ? -28.506 64.336 -19.285 1.00 13.84 ? 255 ALA B CB    1 
ATOM   3933 N N     . HIS B 1 115 ? -28.985 62.168 -21.491 1.00 15.63 ? 256 HIS B N     1 
ATOM   3934 C CA    . HIS B 1 115 ? -28.681 60.828 -21.995 1.00 19.13 ? 256 HIS B CA    1 
ATOM   3935 C C     . HIS B 1 115 ? -28.403 60.836 -23.498 1.00 19.22 ? 256 HIS B C     1 
ATOM   3936 O O     . HIS B 1 115 ? -27.479 60.163 -23.974 1.00 16.55 ? 256 HIS B O     1 
ATOM   3937 C CB    . HIS B 1 115 ? -29.835 59.865 -21.705 1.00 20.37 ? 256 HIS B CB    1 
ATOM   3938 C CG    . HIS B 1 115 ? -29.953 59.444 -20.270 1.00 25.93 ? 256 HIS B CG    1 
ATOM   3939 N ND1   . HIS B 1 115 ? -30.398 60.291 -19.276 1.00 24.18 ? 256 HIS B ND1   1 
ATOM   3940 C CD2   . HIS B 1 115 ? -29.742 58.247 -19.673 1.00 28.33 ? 256 HIS B CD2   1 
ATOM   3941 C CE1   . HIS B 1 115 ? -30.431 59.643 -18.124 1.00 25.14 ? 256 HIS B CE1   1 
ATOM   3942 N NE2   . HIS B 1 115 ? -30.037 58.401 -18.338 1.00 29.26 ? 256 HIS B NE2   1 
ATOM   3943 N N     . ALA B 1 116 ? -29.236 61.533 -24.274 1.00 15.54 ? 257 ALA B N     1 
ATOM   3944 C CA    . ALA B 1 116 ? -29.167 61.407 -25.732 1.00 14.84 ? 257 ALA B CA    1 
ATOM   3945 C C     . ALA B 1 116 ? -28.176 62.394 -26.333 1.00 14.16 ? 257 ALA B C     1 
ATOM   3946 O O     . ALA B 1 116 ? -27.198 61.983 -26.967 1.00 16.38 ? 257 ALA B O     1 
ATOM   3947 C CB    . ALA B 1 116 ? -30.562 61.594 -26.352 1.00 14.19 ? 257 ALA B CB    1 
ATOM   3948 N N     . TRP B 1 117 ? -28.433 63.698 -26.165 1.00 14.29 ? 258 TRP B N     1 
ATOM   3949 C CA    . TRP B 1 117 ? -27.490 64.709 -26.642 1.00 16.11 ? 258 TRP B CA    1 
ATOM   3950 C C     . TRP B 1 117 ? -26.162 64.600 -25.907 1.00 15.77 ? 258 TRP B C     1 
ATOM   3951 O O     . TRP B 1 117 ? -25.090 64.605 -26.530 1.00 15.51 ? 258 TRP B O     1 
ATOM   3952 C CB    . TRP B 1 117 ? -28.067 66.122 -26.479 1.00 15.31 ? 258 TRP B CB    1 
ATOM   3953 C CG    . TRP B 1 117 ? -27.152 67.173 -27.085 1.00 18.59 ? 258 TRP B CG    1 
ATOM   3954 C CD1   . TRP B 1 117 ? -27.150 67.604 -28.382 1.00 19.19 ? 258 TRP B CD1   1 
ATOM   3955 C CD2   . TRP B 1 117 ? -26.091 67.890 -26.424 1.00 18.98 ? 258 TRP B CD2   1 
ATOM   3956 N NE1   . TRP B 1 117 ? -26.160 68.553 -28.571 1.00 18.43 ? 258 TRP B NE1   1 
ATOM   3957 C CE2   . TRP B 1 117 ? -25.495 68.741 -27.389 1.00 20.89 ? 258 TRP B CE2   1 
ATOM   3958 C CE3   . TRP B 1 117 ? -25.585 67.891 -25.117 1.00 18.51 ? 258 TRP B CE3   1 
ATOM   3959 C CZ2   . TRP B 1 117 ? -24.421 69.584 -27.087 1.00 17.76 ? 258 TRP B CZ2   1 
ATOM   3960 C CZ3   . TRP B 1 117 ? -24.520 68.741 -24.818 1.00 20.02 ? 258 TRP B CZ3   1 
ATOM   3961 C CH2   . TRP B 1 117 ? -23.959 69.576 -25.801 1.00 17.75 ? 258 TRP B CH2   1 
ATOM   3962 N N     . GLY B 1 118 ? -26.213 64.505 -24.576 1.00 14.72 ? 259 GLY B N     1 
ATOM   3963 C CA    . GLY B 1 118 ? -24.985 64.419 -23.801 1.00 14.84 ? 259 GLY B CA    1 
ATOM   3964 C C     . GLY B 1 118 ? -24.213 63.141 -24.075 1.00 17.15 ? 259 GLY B C     1 
ATOM   3965 O O     . GLY B 1 118 ? -22.982 63.153 -24.155 1.00 20.26 ? 259 GLY B O     1 
ATOM   3966 N N     . GLY B 1 119 ? -24.920 62.023 -24.217 1.00 20.84 ? 260 GLY B N     1 
ATOM   3967 C CA    . GLY B 1 119 ? -24.245 60.780 -24.540 1.00 19.91 ? 260 GLY B CA    1 
ATOM   3968 C C     . GLY B 1 119 ? -23.466 60.872 -25.837 1.00 24.34 ? 260 GLY B C     1 
ATOM   3969 O O     . GLY B 1 119 ? -22.383 60.298 -25.965 1.00 20.43 ? 260 GLY B O     1 
ATOM   3970 N N     . LYS B 1 120 ? -23.989 61.628 -26.802 1.00 19.25 ? 261 LYS B N     1 
ATOM   3971 C CA    . LYS B 1 120 ? -23.308 61.781 -28.079 1.00 20.23 ? 261 LYS B CA    1 
ATOM   3972 C C     . LYS B 1 120 ? -22.211 62.834 -28.044 1.00 22.88 ? 261 LYS B C     1 
ATOM   3973 O O     . LYS B 1 120 ? -21.195 62.678 -28.738 1.00 23.23 ? 261 LYS B O     1 
ATOM   3974 C CB    . LYS B 1 120 ? -24.317 62.126 -29.177 1.00 22.70 ? 261 LYS B CB    1 
ATOM   3975 C CG    . LYS B 1 120 ? -23.729 62.023 -30.593 1.00 25.80 ? 261 LYS B CG    1 
ATOM   3976 C CD    . LYS B 1 120 ? -24.749 62.462 -31.639 1.00 30.47 ? 261 LYS B CD    1 
ATOM   3977 C CE    . LYS B 1 120 ? -24.152 62.509 -33.049 1.00 42.56 ? 261 LYS B CE    1 
ATOM   3978 N NZ    . LYS B 1 120 ? -24.419 63.833 -33.710 1.00 40.28 ? 261 LYS B NZ    1 
ATOM   3979 N N     . HIS B 1 121 ? -22.380 63.897 -27.252 1.00 19.50 ? 262 HIS B N     1 
ATOM   3980 C CA    . HIS B 1 121 ? -21.566 65.102 -27.386 1.00 21.38 ? 262 HIS B CA    1 
ATOM   3981 C C     . HIS B 1 121 ? -20.728 65.467 -26.167 1.00 19.99 ? 262 HIS B C     1 
ATOM   3982 O O     . HIS B 1 121 ? -19.908 66.383 -26.266 1.00 22.71 ? 262 HIS B O     1 
ATOM   3983 C CB    . HIS B 1 121 ? -22.463 66.308 -27.734 1.00 19.71 ? 262 HIS B CB    1 
ATOM   3984 C CG    . HIS B 1 121 ? -23.076 66.219 -29.097 1.00 20.11 ? 262 HIS B CG    1 
ATOM   3985 N ND1   . HIS B 1 121 ? -22.325 66.256 -30.253 1.00 22.80 ? 262 HIS B ND1   1 
ATOM   3986 C CD2   . HIS B 1 121 ? -24.360 66.046 -29.490 1.00 22.23 ? 262 HIS B CD2   1 
ATOM   3987 C CE1   . HIS B 1 121 ? -23.122 66.133 -31.300 1.00 24.87 ? 262 HIS B CE1   1 
ATOM   3988 N NE2   . HIS B 1 121 ? -24.363 66.006 -30.865 1.00 24.52 ? 262 HIS B NE2   1 
ATOM   3989 N N     . LEU B 1 122 ? -20.904 64.815 -25.030 1.00 17.73 ? 263 LEU B N     1 
ATOM   3990 C CA    . LEU B 1 122 ? -20.128 65.138 -23.830 1.00 20.66 ? 263 LEU B CA    1 
ATOM   3991 C C     . LEU B 1 122 ? -19.202 63.968 -23.507 1.00 22.38 ? 263 LEU B C     1 
ATOM   3992 O O     . LEU B 1 122 ? -19.638 62.960 -22.945 1.00 29.15 ? 263 LEU B O     1 
ATOM   3993 C CB    . LEU B 1 122 ? -21.063 65.457 -22.665 1.00 19.64 ? 263 LEU B CB    1 
ATOM   3994 C CG    . LEU B 1 122 ? -21.680 66.858 -22.732 1.00 23.35 ? 263 LEU B CG    1 
ATOM   3995 C CD1   . LEU B 1 122 ? -22.839 66.978 -21.741 1.00 25.72 ? 263 LEU B CD1   1 
ATOM   3996 C CD2   . LEU B 1 122 ? -20.626 67.901 -22.404 1.00 25.76 ? 263 LEU B CD2   1 
ATOM   3997 N N     . GLY B 1 123 ? -17.925 64.100 -23.860 1.00 23.63 ? 264 GLY B N     1 
ATOM   3998 C CA    . GLY B 1 123 ? -16.958 63.051 -23.635 1.00 21.67 ? 264 GLY B CA    1 
ATOM   3999 C C     . GLY B 1 123 ? -15.889 63.453 -22.640 1.00 24.48 ? 264 GLY B C     1 
ATOM   4000 O O     . GLY B 1 123 ? -15.960 64.520 -22.019 1.00 20.34 ? 264 GLY B O     1 
ATOM   4001 N N     . PRO B 1 124 ? -14.860 62.611 -22.499 1.00 21.80 ? 265 PRO B N     1 
ATOM   4002 C CA    . PRO B 1 124 ? -13.794 62.871 -21.524 1.00 18.68 ? 265 PRO B CA    1 
ATOM   4003 C C     . PRO B 1 124 ? -13.161 64.244 -21.680 1.00 22.96 ? 265 PRO B C     1 
ATOM   4004 O O     . PRO B 1 124 ? -12.688 64.620 -22.759 1.00 21.54 ? 265 PRO B O     1 
ATOM   4005 C CB    . PRO B 1 124 ? -12.780 61.756 -21.812 1.00 21.92 ? 265 PRO B CB    1 
ATOM   4006 C CG    . PRO B 1 124 ? -13.560 60.661 -22.404 1.00 20.83 ? 265 PRO B CG    1 
ATOM   4007 C CD    . PRO B 1 124 ? -14.673 61.319 -23.189 1.00 22.68 ? 265 PRO B CD    1 
ATOM   4008 N N     . GLY B 1 125 ? -13.125 64.990 -20.578 1.00 21.53 ? 266 GLY B N     1 
ATOM   4009 C CA    . GLY B 1 125 ? -12.556 66.319 -20.589 1.00 23.60 ? 266 GLY B CA    1 
ATOM   4010 C C     . GLY B 1 125 ? -13.475 67.421 -21.086 1.00 25.77 ? 266 GLY B C     1 
ATOM   4011 O O     . GLY B 1 125 ? -13.133 68.603 -20.922 1.00 25.38 ? 266 GLY B O     1 
ATOM   4012 N N     . ASP B 1 126 ? -14.619 67.088 -21.694 1.00 21.45 ? 267 ASP B N     1 
ATOM   4013 C CA    . ASP B 1 126 ? -15.582 68.113 -22.073 1.00 21.26 ? 267 ASP B CA    1 
ATOM   4014 C C     . ASP B 1 126 ? -16.240 68.668 -20.819 1.00 24.55 ? 267 ASP B C     1 
ATOM   4015 O O     . ASP B 1 126 ? -16.432 67.959 -19.827 1.00 22.98 ? 267 ASP B O     1 
ATOM   4016 C CB    . ASP B 1 126 ? -16.647 67.561 -23.023 1.00 20.82 ? 267 ASP B CB    1 
ATOM   4017 C CG    . ASP B 1 126 ? -16.071 67.108 -24.362 1.00 24.57 ? 267 ASP B CG    1 
ATOM   4018 O OD1   . ASP B 1 126 ? -15.053 67.691 -24.801 1.00 23.45 ? 267 ASP B OD1   1 
ATOM   4019 O OD2   . ASP B 1 126 ? -16.648 66.181 -24.980 1.00 22.20 ? 267 ASP B OD2   1 
ATOM   4020 N N     . GLU B 1 127 ? -16.558 69.958 -20.849 1.00 20.11 ? 268 GLU B N     1 
ATOM   4021 C CA    . GLU B 1 127 ? -17.014 70.648 -19.653 1.00 19.77 ? 268 GLU B CA    1 
ATOM   4022 C C     . GLU B 1 127 ? -18.489 71.016 -19.735 1.00 20.48 ? 268 GLU B C     1 
ATOM   4023 O O     . GLU B 1 127 ? -18.997 71.403 -20.796 1.00 18.38 ? 268 GLU B O     1 
ATOM   4024 C CB    . GLU B 1 127 ? -16.157 71.889 -19.382 1.00 22.70 ? 268 GLU B CB    1 
ATOM   4025 C CG    . GLU B 1 127 ? -14.918 71.550 -18.554 1.00 29.38 ? 268 GLU B CG    1 
ATOM   4026 C CD    . GLU B 1 127 ? -13.770 72.540 -18.703 1.00 33.24 ? 268 GLU B CD    1 
ATOM   4027 O OE1   . GLU B 1 127 ? -14.025 73.738 -18.970 1.00 33.74 ? 268 GLU B OE1   1 
ATOM   4028 O OE2   . GLU B 1 127 ? -12.605 72.115 -18.545 1.00 34.68 ? 268 GLU B OE2   1 
ATOM   4029 N N     . ILE B 1 128 ? -19.169 70.862 -18.597 1.00 18.34 ? 269 ILE B N     1 
ATOM   4030 C CA    . ILE B 1 128 ? -20.549 71.282 -18.397 1.00 19.20 ? 269 ILE B CA    1 
ATOM   4031 C C     . ILE B 1 128 ? -20.537 72.346 -17.315 1.00 22.72 ? 269 ILE B C     1 
ATOM   4032 O O     . ILE B 1 128 ? -19.894 72.161 -16.273 1.00 20.83 ? 269 ILE B O     1 
ATOM   4033 C CB    . ILE B 1 128 ? -21.459 70.106 -17.974 1.00 22.13 ? 269 ILE B CB    1 
ATOM   4034 C CG1   . ILE B 1 128 ? -21.294 68.903 -18.910 1.00 23.80 ? 269 ILE B CG1   1 
ATOM   4035 C CG2   . ILE B 1 128 ? -22.931 70.563 -17.838 1.00 19.47 ? 269 ILE B CG2   1 
ATOM   4036 C CD1   . ILE B 1 128 ? -21.695 67.555 -18.290 1.00 22.71 ? 269 ILE B CD1   1 
ATOM   4037 N N     . VAL B 1 129 ? -21.239 73.454 -17.551 1.00 18.95 ? 270 VAL B N     1 
ATOM   4038 C CA    . VAL B 1 129 ? -21.357 74.522 -16.558 1.00 21.12 ? 270 VAL B CA    1 
ATOM   4039 C C     . VAL B 1 129 ? -22.826 74.651 -16.176 1.00 19.45 ? 270 VAL B C     1 
ATOM   4040 O O     . VAL B 1 129 ? -23.689 74.854 -17.044 1.00 17.75 ? 270 VAL B O     1 
ATOM   4041 C CB    . VAL B 1 129 ? -20.782 75.856 -17.073 1.00 22.11 ? 270 VAL B CB    1 
ATOM   4042 C CG1   . VAL B 1 129 ? -20.924 76.952 -16.026 1.00 21.11 ? 270 VAL B CG1   1 
ATOM   4043 C CG2   . VAL B 1 129 ? -19.319 75.677 -17.469 1.00 21.08 ? 270 VAL B CG2   1 
ATOM   4044 N N     . ILE B 1 130 ? -23.115 74.469 -14.886 1.00 18.99 ? 271 ILE B N     1 
ATOM   4045 C CA    . ILE B 1 130 ? -24.422 74.739 -14.307 1.00 15.96 ? 271 ILE B CA    1 
ATOM   4046 C C     . ILE B 1 130 ? -24.233 75.853 -13.280 1.00 22.84 ? 271 ILE B C     1 
ATOM   4047 O O     . ILE B 1 130 ? -23.110 76.242 -12.966 1.00 22.92 ? 271 ILE B O     1 
ATOM   4048 C CB    . ILE B 1 130 ? -25.049 73.488 -13.649 1.00 19.11 ? 271 ILE B CB    1 
ATOM   4049 C CG1   . ILE B 1 130 ? -24.210 73.045 -12.447 1.00 20.66 ? 271 ILE B CG1   1 
ATOM   4050 C CG2   . ILE B 1 130 ? -25.162 72.329 -14.644 1.00 17.60 ? 271 ILE B CG2   1 
ATOM   4051 C CD1   . ILE B 1 130 ? -24.807 71.873 -11.679 1.00 24.42 ? 271 ILE B CD1   1 
ATOM   4052 N N     . THR B 1 131 ? -25.337 76.348 -12.730 1.00 21.10 ? 272 THR B N     1 
ATOM   4053 C CA    . THR B 1 131 ? -25.229 77.326 -11.650 1.00 21.46 ? 272 THR B CA    1 
ATOM   4054 C C     . THR B 1 131 ? -25.482 76.680 -10.290 1.00 22.33 ? 272 THR B C     1 
ATOM   4055 O O     . THR B 1 131 ? -26.024 75.576 -10.183 1.00 22.33 ? 272 THR B O     1 
ATOM   4056 C CB    . THR B 1 131 ? -26.205 78.483 -11.849 1.00 22.80 ? 272 THR B CB    1 
ATOM   4057 O OG1   . THR B 1 131 ? -27.481 78.120 -11.299 1.00 26.36 ? 272 THR B OG1   1 
ATOM   4058 C CG2   . THR B 1 131 ? -26.356 78.839 -13.328 1.00 19.58 ? 272 THR B CG2   1 
ATOM   4059 N N     . HIS B 1 132 ? -25.096 77.406 -9.237  1.00 22.58 ? 273 HIS B N     1 
ATOM   4060 C CA    . HIS B 1 132 ? -25.319 76.956 -7.870  1.00 21.85 ? 273 HIS B CA    1 
ATOM   4061 C C     . HIS B 1 132 ? -26.792 76.934 -7.485  1.00 22.65 ? 273 HIS B C     1 
ATOM   4062 O O     . HIS B 1 132 ? -27.142 76.328 -6.464  1.00 23.65 ? 273 HIS B O     1 
ATOM   4063 C CB    . HIS B 1 132 ? -24.543 77.853 -6.895  1.00 22.16 ? 273 HIS B CB    1 
ATOM   4064 C CG    . HIS B 1 132 ? -23.962 77.115 -5.735  1.00 24.75 ? 273 HIS B CG    1 
ATOM   4065 N ND1   . HIS B 1 132 ? -22.827 77.534 -5.079  1.00 26.52 ? 273 HIS B ND1   1 
ATOM   4066 C CD2   . HIS B 1 132 ? -24.361 75.981 -5.112  1.00 23.16 ? 273 HIS B CD2   1 
ATOM   4067 C CE1   . HIS B 1 132 ? -22.543 76.683 -4.109  1.00 25.02 ? 273 HIS B CE1   1 
ATOM   4068 N NE2   . HIS B 1 132 ? -23.460 75.732 -4.108  1.00 23.95 ? 273 HIS B NE2   1 
ATOM   4069 N N     . LEU B 1 133 ? -27.657 77.564 -8.275  1.00 20.99 ? 274 LEU B N     1 
ATOM   4070 C CA    . LEU B 1 133 ? -29.082 77.678 -7.979  1.00 20.18 ? 274 LEU B CA    1 
ATOM   4071 C C     . LEU B 1 133 ? -29.905 76.471 -8.424  1.00 21.34 ? 274 LEU B C     1 
ATOM   4072 O O     . LEU B 1 133 ? -31.116 76.462 -8.191  1.00 24.03 ? 274 LEU B O     1 
ATOM   4073 C CB    . LEU B 1 133 ? -29.643 78.939 -8.657  1.00 22.92 ? 274 LEU B CB    1 
ATOM   4074 C CG    . LEU B 1 133 ? -29.056 80.304 -8.278  1.00 28.96 ? 274 LEU B CG    1 
ATOM   4075 C CD1   . LEU B 1 133 ? -29.272 81.341 -9.397  1.00 25.76 ? 274 LEU B CD1   1 
ATOM   4076 C CD2   . LEU B 1 133 ? -29.661 80.791 -6.974  1.00 23.56 ? 274 LEU B CD2   1 
ATOM   4077 N N     . GLU B 1 134 ? -29.302 75.474 -9.071  1.00 24.83 ? 275 GLU B N     1 
ATOM   4078 C CA    . GLU B 1 134 ? -30.080 74.464 -9.782  1.00 17.76 ? 275 GLU B CA    1 
ATOM   4079 C C     . GLU B 1 134 ? -30.891 73.580 -8.842  1.00 22.53 ? 275 GLU B C     1 
ATOM   4080 O O     . GLU B 1 134 ? -30.467 73.241 -7.730  1.00 23.24 ? 275 GLU B O     1 
ATOM   4081 C CB    . GLU B 1 134 ? -29.177 73.580 -10.650 1.00 19.61 ? 275 GLU B CB    1 
ATOM   4082 C CG    . GLU B 1 134 ? -28.337 74.359 -11.662 1.00 20.04 ? 275 GLU B CG    1 
ATOM   4083 C CD    . GLU B 1 134 ? -29.173 75.249 -12.575 1.00 25.24 ? 275 GLU B CD    1 
ATOM   4084 O OE1   . GLU B 1 134 ? -30.294 74.827 -12.976 1.00 24.77 ? 275 GLU B OE1   1 
ATOM   4085 O OE2   . GLU B 1 134 ? -28.732 76.409 -12.826 1.00 26.03 ? 275 GLU B OE2   1 
ATOM   4086 N N     . HIS B 1 135 ? -32.091 73.257 -9.304  1.00 19.90 ? 276 HIS B N     1 
ATOM   4087 C CA    . HIS B 1 135 ? -32.889 72.149 -8.821  1.00 18.16 ? 276 HIS B CA    1 
ATOM   4088 C C     . HIS B 1 135 ? -32.155 70.830 -9.074  1.00 18.80 ? 276 HIS B C     1 
ATOM   4089 O O     . HIS B 1 135 ? -31.353 70.712 -10.007 1.00 17.19 ? 276 HIS B O     1 
ATOM   4090 C CB    . HIS B 1 135 ? -34.233 72.216 -9.559  1.00 20.69 ? 276 HIS B CB    1 
ATOM   4091 C CG    . HIS B 1 135 ? -35.302 71.309 -9.032  1.00 21.87 ? 276 HIS B CG    1 
ATOM   4092 N ND1   . HIS B 1 135 ? -35.327 69.957 -9.297  1.00 19.81 ? 276 HIS B ND1   1 
ATOM   4093 C CD2   . HIS B 1 135 ? -36.431 71.577 -8.333  1.00 22.28 ? 276 HIS B CD2   1 
ATOM   4094 C CE1   . HIS B 1 135 ? -36.406 69.423 -8.751  1.00 19.60 ? 276 HIS B CE1   1 
ATOM   4095 N NE2   . HIS B 1 135 ? -37.090 70.385 -8.156  1.00 23.09 ? 276 HIS B NE2   1 
ATOM   4096 N N     . HIS B 1 136 ? -32.434 69.827 -8.228  1.00 17.05 ? 277 HIS B N     1 
ATOM   4097 C CA    . HIS B 1 136 ? -31.810 68.515 -8.390  1.00 17.33 ? 277 HIS B CA    1 
ATOM   4098 C C     . HIS B 1 136 ? -32.025 67.950 -9.798  1.00 18.76 ? 277 HIS B C     1 
ATOM   4099 O O     . HIS B 1 136 ? -31.178 67.196 -10.303 1.00 16.07 ? 277 HIS B O     1 
ATOM   4100 C CB    . HIS B 1 136 ? -32.355 67.540 -7.340  1.00 15.65 ? 277 HIS B CB    1 
ATOM   4101 C CG    . HIS B 1 136 ? -31.944 67.866 -5.930  1.00 20.88 ? 277 HIS B CG    1 
ATOM   4102 N ND1   . HIS B 1 136 ? -32.510 67.254 -4.834  1.00 16.27 ? 277 HIS B ND1   1 
ATOM   4103 C CD2   . HIS B 1 136 ? -31.020 68.732 -5.440  1.00 20.39 ? 277 HIS B CD2   1 
ATOM   4104 C CE1   . HIS B 1 136 ? -31.954 67.724 -3.729  1.00 21.08 ? 277 HIS B CE1   1 
ATOM   4105 N NE2   . HIS B 1 136 ? -31.040 68.617 -4.068  1.00 20.81 ? 277 HIS B NE2   1 
ATOM   4106 N N     . ALA B 1 137 ? -33.146 68.300 -10.440 1.00 15.68 ? 278 ALA B N     1 
ATOM   4107 C CA    . ALA B 1 137 ? -33.421 67.846 -11.804 1.00 16.79 ? 278 ALA B CA    1 
ATOM   4108 C C     . ALA B 1 137 ? -32.366 68.321 -12.798 1.00 15.45 ? 278 ALA B C     1 
ATOM   4109 O O     . ALA B 1 137 ? -32.149 67.676 -13.829 1.00 17.18 ? 278 ALA B O     1 
ATOM   4110 C CB    . ALA B 1 137 ? -34.795 68.337 -12.252 1.00 15.73 ? 278 ALA B CB    1 
ATOM   4111 N N     . ASN B 1 138 ? -31.739 69.462 -12.538 1.00 15.53 ? 279 ASN B N     1 
ATOM   4112 C CA    . ASN B 1 138 ? -30.686 69.998 -13.394 1.00 13.76 ? 279 ASN B CA    1 
ATOM   4113 C C     . ASN B 1 138 ? -29.296 69.809 -12.776 1.00 19.18 ? 279 ASN B C     1 
ATOM   4114 O O     . ASN B 1 138 ? -28.367 70.571 -13.073 1.00 17.69 ? 279 ASN B O     1 
ATOM   4115 C CB    . ASN B 1 138 ? -30.969 71.474 -13.693 1.00 15.76 ? 279 ASN B CB    1 
ATOM   4116 C CG    . ASN B 1 138 ? -30.393 71.935 -15.033 1.00 21.18 ? 279 ASN B CG    1 
ATOM   4117 O OD1   . ASN B 1 138 ? -30.096 71.126 -15.915 1.00 15.18 ? 279 ASN B OD1   1 
ATOM   4118 N ND2   . ASN B 1 138 ? -30.226 73.251 -15.183 1.00 23.43 ? 279 ASN B ND2   1 
ATOM   4119 N N     . ILE B 1 139 ? -29.143 68.803 -11.908 1.00 17.77 ? 280 ILE B N     1 
ATOM   4120 C CA    . ILE B 1 139 ? -27.851 68.437 -11.333 1.00 17.00 ? 280 ILE B CA    1 
ATOM   4121 C C     . ILE B 1 139 ? -27.578 66.953 -11.560 1.00 16.20 ? 280 ILE B C     1 
ATOM   4122 O O     . ILE B 1 139 ? -26.572 66.578 -12.174 1.00 16.17 ? 280 ILE B O     1 
ATOM   4123 C CB    . ILE B 1 139 ? -27.795 68.756 -9.828  1.00 17.60 ? 280 ILE B CB    1 
ATOM   4124 C CG1   . ILE B 1 139 ? -27.958 70.254 -9.566  1.00 17.86 ? 280 ILE B CG1   1 
ATOM   4125 C CG2   . ILE B 1 139 ? -26.498 68.211 -9.215  1.00 18.92 ? 280 ILE B CG2   1 
ATOM   4126 C CD1   . ILE B 1 139 ? -27.962 70.600 -8.041  1.00 19.55 ? 280 ILE B CD1   1 
ATOM   4127 N N     . VAL B 1 140 ? -28.486 66.105 -11.061 1.00 14.28 ? 281 VAL B N     1 
ATOM   4128 C CA    . VAL B 1 140 ? -28.235 64.660 -11.057 1.00 14.12 ? 281 VAL B CA    1 
ATOM   4129 C C     . VAL B 1 140 ? -28.035 64.084 -12.452 1.00 17.05 ? 281 VAL B C     1 
ATOM   4130 O O     . VAL B 1 140 ? -27.162 63.217 -12.617 1.00 15.51 ? 281 VAL B O     1 
ATOM   4131 C CB    . VAL B 1 140 ? -29.345 63.942 -10.277 1.00 18.01 ? 281 VAL B CB    1 
ATOM   4132 C CG1   . VAL B 1 140 ? -29.072 62.438 -10.214 1.00 14.98 ? 281 VAL B CG1   1 
ATOM   4133 C CG2   . VAL B 1 140 ? -29.477 64.558 -8.889  1.00 15.35 ? 281 VAL B CG2   1 
ATOM   4134 N N     . PRO B 1 141 ? -28.808 64.464 -13.483 1.00 15.07 ? 282 PRO B N     1 
ATOM   4135 C CA    . PRO B 1 141 ? -28.544 63.904 -14.821 1.00 15.73 ? 282 PRO B CA    1 
ATOM   4136 C C     . PRO B 1 141 ? -27.149 64.224 -15.323 1.00 15.69 ? 282 PRO B C     1 
ATOM   4137 O O     . PRO B 1 141 ? -26.514 63.374 -15.966 1.00 17.80 ? 282 PRO B O     1 
ATOM   4138 C CB    . PRO B 1 141 ? -29.631 64.556 -15.693 1.00 14.13 ? 282 PRO B CB    1 
ATOM   4139 C CG    . PRO B 1 141 ? -30.736 64.905 -14.708 1.00 13.59 ? 282 PRO B CG    1 
ATOM   4140 C CD    . PRO B 1 141 ? -29.975 65.365 -13.497 1.00 15.10 ? 282 PRO B CD    1 
ATOM   4141 N N     . TRP B 1 142 ? -26.635 65.417 -15.000 1.00 16.33 ? 283 TRP B N     1 
ATOM   4142 C CA    . TRP B 1 142 ? -25.280 65.774 -15.415 1.00 15.46 ? 283 TRP B CA    1 
ATOM   4143 C C     . TRP B 1 142 ? -24.236 64.990 -14.625 1.00 17.64 ? 283 TRP B C     1 
ATOM   4144 O O     . TRP B 1 142 ? -23.215 64.584 -15.188 1.00 19.75 ? 283 TRP B O     1 
ATOM   4145 C CB    . TRP B 1 142 ? -25.077 67.289 -15.292 1.00 16.75 ? 283 TRP B CB    1 
ATOM   4146 C CG    . TRP B 1 142 ? -26.183 68.050 -15.994 1.00 16.83 ? 283 TRP B CG    1 
ATOM   4147 C CD1   . TRP B 1 142 ? -27.064 68.944 -15.434 1.00 15.67 ? 283 TRP B CD1   1 
ATOM   4148 C CD2   . TRP B 1 142 ? -26.537 67.956 -17.382 1.00 15.60 ? 283 TRP B CD2   1 
ATOM   4149 N NE1   . TRP B 1 142 ? -27.946 69.402 -16.393 1.00 14.83 ? 283 TRP B NE1   1 
ATOM   4150 C CE2   . TRP B 1 142 ? -27.652 68.800 -17.589 1.00 17.52 ? 283 TRP B CE2   1 
ATOM   4151 C CE3   . TRP B 1 142 ? -26.033 67.223 -18.465 1.00 19.70 ? 283 TRP B CE3   1 
ATOM   4152 C CZ2   . TRP B 1 142 ? -28.253 68.946 -18.831 1.00 16.82 ? 283 TRP B CZ2   1 
ATOM   4153 C CZ3   . TRP B 1 142 ? -26.636 67.366 -19.704 1.00 18.16 ? 283 TRP B CZ3   1 
ATOM   4154 C CH2   . TRP B 1 142 ? -27.736 68.216 -19.872 1.00 16.65 ? 283 TRP B CH2   1 
ATOM   4155 N N     . GLN B 1 143 ? -24.483 64.737 -13.332 1.00 16.18 ? 284 GLN B N     1 
ATOM   4156 C CA    . GLN B 1 143 ? -23.584 63.886 -12.549 1.00 18.12 ? 284 GLN B CA    1 
ATOM   4157 C C     . GLN B 1 143 ? -23.530 62.465 -13.101 1.00 20.35 ? 284 GLN B C     1 
ATOM   4158 O O     . GLN B 1 143 ? -22.441 61.879 -13.220 1.00 20.04 ? 284 GLN B O     1 
ATOM   4159 C CB    . GLN B 1 143 ? -24.011 63.846 -11.070 1.00 15.73 ? 284 GLN B CB    1 
ATOM   4160 C CG    . GLN B 1 143 ? -23.916 65.184 -10.340 1.00 16.49 ? 284 GLN B CG    1 
ATOM   4161 C CD    . GLN B 1 143 ? -24.379 65.065 -8.900  1.00 20.31 ? 284 GLN B CD    1 
ATOM   4162 O OE1   . GLN B 1 143 ? -25.236 64.236 -8.588  1.00 19.10 ? 284 GLN B OE1   1 
ATOM   4163 N NE2   . GLN B 1 143 ? -23.810 65.883 -8.010  1.00 20.04 ? 284 GLN B NE2   1 
ATOM   4164 N N     . LEU B 1 144 ? -24.690 61.889 -13.443 1.00 16.62 ? 285 LEU B N     1 
ATOM   4165 C CA    . LEU B 1 144 ? -24.715 60.527 -13.976 1.00 18.88 ? 285 LEU B CA    1 
ATOM   4166 C C     . LEU B 1 144 ? -23.975 60.449 -15.313 1.00 21.79 ? 285 LEU B C     1 
ATOM   4167 O O     . LEU B 1 144 ? -23.141 59.549 -15.538 1.00 23.15 ? 285 LEU B O     1 
ATOM   4168 C CB    . LEU B 1 144 ? -26.163 60.051 -14.131 1.00 18.80 ? 285 LEU B CB    1 
ATOM   4169 C CG    . LEU B 1 144 ? -26.950 59.844 -12.827 1.00 22.83 ? 285 LEU B CG    1 
ATOM   4170 C CD1   . LEU B 1 144 ? -28.413 59.633 -13.135 1.00 20.75 ? 285 LEU B CD1   1 
ATOM   4171 C CD2   . LEU B 1 144 ? -26.396 58.666 -12.015 1.00 21.92 ? 285 LEU B CD2   1 
ATOM   4172 N N     . LEU B 1 145 ? -24.262 61.394 -16.212 1.00 21.53 ? 286 LEU B N     1 
ATOM   4173 C CA    . LEU B 1 145 ? -23.529 61.457 -17.475 1.00 21.36 ? 286 LEU B CA    1 
ATOM   4174 C C     . LEU B 1 145 ? -22.028 61.595 -17.236 1.00 21.93 ? 286 LEU B C     1 
ATOM   4175 O O     . LEU B 1 145 ? -21.222 60.852 -17.814 1.00 24.56 ? 286 LEU B O     1 
ATOM   4176 C CB    . LEU B 1 145 ? -24.041 62.622 -18.312 1.00 20.17 ? 286 LEU B CB    1 
ATOM   4177 C CG    . LEU B 1 145 ? -23.382 62.691 -19.692 1.00 23.13 ? 286 LEU B CG    1 
ATOM   4178 C CD1   . LEU B 1 145 ? -23.720 61.433 -20.484 1.00 22.76 ? 286 LEU B CD1   1 
ATOM   4179 C CD2   . LEU B 1 145 ? -23.845 63.935 -20.414 1.00 23.71 ? 286 LEU B CD2   1 
ATOM   4180 N N     . SER B 1 146 ? -21.640 62.552 -16.378 1.00 22.18 ? 287 SER B N     1 
ATOM   4181 C CA    . SER B 1 146 ? -20.241 62.795 -16.050 1.00 22.91 ? 287 SER B CA    1 
ATOM   4182 C C     . SER B 1 146 ? -19.544 61.530 -15.581 1.00 23.51 ? 287 SER B C     1 
ATOM   4183 O O     . SER B 1 146 ? -18.395 61.269 -15.956 1.00 27.38 ? 287 SER B O     1 
ATOM   4184 C CB    . SER B 1 146 ? -20.149 63.861 -14.953 1.00 21.05 ? 287 SER B CB    1 
ATOM   4185 O OG    . SER B 1 146 ? -19.999 65.130 -15.540 1.00 35.35 ? 287 SER B OG    1 
ATOM   4186 N N     . ARG B 1 147 ? -20.207 60.752 -14.724 1.00 20.07 ? 288 ARG B N     1 
ATOM   4187 C CA    . ARG B 1 147 ? -19.582 59.531 -14.232 1.00 23.37 ? 288 ARG B CA    1 
ATOM   4188 C C     . ARG B 1 147 ? -19.469 58.482 -15.325 1.00 26.23 ? 288 ARG B C     1 
ATOM   4189 O O     . ARG B 1 147 ? -18.598 57.607 -15.252 1.00 26.82 ? 288 ARG B O     1 
ATOM   4190 C CB    . ARG B 1 147 ? -20.360 58.974 -13.048 1.00 22.50 ? 288 ARG B CB    1 
ATOM   4191 C CG    . ARG B 1 147 ? -20.447 59.926 -11.876 1.00 21.40 ? 288 ARG B CG    1 
ATOM   4192 C CD    . ARG B 1 147 ? -21.131 59.234 -10.687 1.00 21.91 ? 288 ARG B CD    1 
ATOM   4193 N NE    . ARG B 1 147 ? -20.762 59.968 -9.499  1.00 33.22 ? 288 ARG B NE    1 
ATOM   4194 C CZ    . ARG B 1 147 ? -20.214 59.443 -8.418  1.00 22.81 ? 288 ARG B CZ    1 
ATOM   4195 N NH1   . ARG B 1 147 ? -20.138 58.132 -8.242  1.00 22.96 ? 288 ARG B NH1   1 
ATOM   4196 N NH2   . ARG B 1 147 ? -19.742 60.256 -7.485  1.00 30.89 ? 288 ARG B NH2   1 
ATOM   4197 N N     . GLN B 1 148 ? -20.336 58.546 -16.336 1.00 23.34 ? 289 GLN B N     1 
ATOM   4198 C CA    . GLN B 1 148 ? -20.228 57.604 -17.453 1.00 23.61 ? 289 GLN B CA    1 
ATOM   4199 C C     . GLN B 1 148 ? -19.106 57.960 -18.430 1.00 26.02 ? 289 GLN B C     1 
ATOM   4200 O O     . GLN B 1 148 ? -18.471 57.061 -19.002 1.00 23.07 ? 289 GLN B O     1 
ATOM   4201 C CB    . GLN B 1 148 ? -21.560 57.535 -18.202 1.00 24.93 ? 289 GLN B CB    1 
ATOM   4202 C CG    . GLN B 1 148 ? -22.617 56.819 -17.388 1.00 34.13 ? 289 GLN B CG    1 
ATOM   4203 C CD    . GLN B 1 148 ? -22.076 55.490 -16.885 1.00 42.16 ? 289 GLN B CD    1 
ATOM   4204 O OE1   . GLN B 1 148 ? -21.994 55.238 -15.674 1.00 36.89 ? 289 GLN B OE1   1 
ATOM   4205 N NE2   . GLN B 1 148 ? -21.649 54.648 -17.826 1.00 40.04 ? 289 GLN B NE2   1 
ATOM   4206 N N     . THR B 1 149 ? -18.859 59.253 -18.655 1.00 23.29 ? 290 THR B N     1 
ATOM   4207 C CA    . THR B 1 149 ? -18.017 59.683 -19.763 1.00 23.49 ? 290 THR B CA    1 
ATOM   4208 C C     . THR B 1 149 ? -16.743 60.416 -19.364 1.00 24.36 ? 290 THR B C     1 
ATOM   4209 O O     . THR B 1 149 ? -15.919 60.696 -20.244 1.00 24.03 ? 290 THR B O     1 
ATOM   4210 C CB    . THR B 1 149 ? -18.801 60.612 -20.703 1.00 23.71 ? 290 THR B CB    1 
ATOM   4211 O OG1   . THR B 1 149 ? -19.019 61.857 -20.035 1.00 26.43 ? 290 THR B OG1   1 
ATOM   4212 C CG2   . THR B 1 149 ? -20.149 60.001 -21.088 1.00 23.36 ? 290 THR B CG2   1 
ATOM   4213 N N     . GLY B 1 150 ? -16.559 60.769 -18.096 1.00 20.59 ? 291 GLY B N     1 
ATOM   4214 C CA    . GLY B 1 150 ? -15.425 61.599 -17.741 1.00 17.17 ? 291 GLY B CA    1 
ATOM   4215 C C     . GLY B 1 150 ? -15.557 63.069 -18.084 1.00 23.44 ? 291 GLY B C     1 
ATOM   4216 O O     . GLY B 1 150 ? -14.558 63.794 -17.994 1.00 26.23 ? 291 GLY B O     1 
ATOM   4217 N N     . ALA B 1 151 ? -16.742 63.533 -18.495 1.00 24.48 ? 292 ALA B N     1 
ATOM   4218 C CA    . ALA B 1 151 ? -16.987 64.967 -18.619 1.00 23.36 ? 292 ALA B CA    1 
ATOM   4219 C C     . ALA B 1 151 ? -16.831 65.658 -17.264 1.00 23.66 ? 292 ALA B C     1 
ATOM   4220 O O     . ALA B 1 151 ? -16.961 65.045 -16.204 1.00 25.59 ? 292 ALA B O     1 
ATOM   4221 C CB    . ALA B 1 151 ? -18.390 65.226 -19.177 1.00 23.07 ? 292 ALA B CB    1 
ATOM   4222 N N     . VAL B 1 152 ? -16.560 66.957 -17.299 1.00 22.82 ? 293 VAL B N     1 
ATOM   4223 C CA    . VAL B 1 152 ? -16.233 67.727 -16.100 1.00 25.62 ? 293 VAL B CA    1 
ATOM   4224 C C     . VAL B 1 152 ? -17.384 68.683 -15.805 1.00 25.53 ? 293 VAL B C     1 
ATOM   4225 O O     . VAL B 1 152 ? -17.792 69.458 -16.680 1.00 23.45 ? 293 VAL B O     1 
ATOM   4226 C CB    . VAL B 1 152 ? -14.913 68.496 -16.282 1.00 26.68 ? 293 VAL B CB    1 
ATOM   4227 C CG1   . VAL B 1 152 ? -14.629 69.369 -15.070 1.00 31.78 ? 293 VAL B CG1   1 
ATOM   4228 C CG2   . VAL B 1 152 ? -13.762 67.519 -16.553 1.00 30.09 ? 293 VAL B CG2   1 
ATOM   4229 N N     . LEU B 1 153 ? -17.910 68.630 -14.585 1.00 22.37 ? 294 LEU B N     1 
ATOM   4230 C CA    . LEU B 1 153 ? -19.029 69.484 -14.185 1.00 21.37 ? 294 LEU B CA    1 
ATOM   4231 C C     . LEU B 1 153 ? -18.500 70.660 -13.369 1.00 25.45 ? 294 LEU B C     1 
ATOM   4232 O O     . LEU B 1 153 ? -17.855 70.461 -12.335 1.00 27.16 ? 294 LEU B O     1 
ATOM   4233 C CB    . LEU B 1 153 ? -20.063 68.685 -13.392 1.00 23.96 ? 294 LEU B CB    1 
ATOM   4234 C CG    . LEU B 1 153 ? -21.302 69.389 -12.829 1.00 26.92 ? 294 LEU B CG    1 
ATOM   4235 C CD1   . LEU B 1 153 ? -22.151 69.994 -13.947 1.00 21.86 ? 294 LEU B CD1   1 
ATOM   4236 C CD2   . LEU B 1 153 ? -22.144 68.415 -12.005 1.00 28.90 ? 294 LEU B CD2   1 
ATOM   4237 N N     . LYS B 1 154 ? -18.747 71.878 -13.844 1.00 21.24 ? 295 LYS B N     1 
ATOM   4238 C CA    . LYS B 1 154 ? -18.393 73.090 -13.121 1.00 25.38 ? 295 LYS B CA    1 
ATOM   4239 C C     . LYS B 1 154 ? -19.660 73.805 -12.669 1.00 24.63 ? 295 LYS B C     1 
ATOM   4240 O O     . LYS B 1 154 ? -20.711 73.692 -13.303 1.00 22.19 ? 295 LYS B O     1 
ATOM   4241 C CB    . LYS B 1 154 ? -17.534 74.040 -13.977 1.00 23.28 ? 295 LYS B CB    1 
ATOM   4242 C CG    . LYS B 1 154 ? -16.319 73.366 -14.617 1.00 29.52 ? 295 LYS B CG    1 
ATOM   4243 C CD    . LYS B 1 154 ? -15.074 74.237 -14.513 1.00 34.17 ? 295 LYS B CD    1 
ATOM   4244 C CE    . LYS B 1 154 ? -13.993 73.825 -15.504 1.00 36.89 ? 295 LYS B CE    1 
ATOM   4245 N NZ    . LYS B 1 154 ? -13.583 74.963 -16.404 1.00 45.32 ? 295 LYS B NZ    1 
ATOM   4246 N N     . VAL B 1 155 ? -19.549 74.554 -11.571 1.00 22.09 ? 296 VAL B N     1 
ATOM   4247 C CA    . VAL B 1 155 ? -20.699 75.200 -10.935 1.00 24.08 ? 296 VAL B CA    1 
ATOM   4248 C C     . VAL B 1 155 ? -20.407 76.685 -10.759 1.00 23.61 ? 296 VAL B C     1 
ATOM   4249 O O     . VAL B 1 155 ? -19.461 77.057 -10.058 1.00 24.14 ? 296 VAL B O     1 
ATOM   4250 C CB    . VAL B 1 155 ? -21.034 74.549 -9.584  1.00 29.26 ? 296 VAL B CB    1 
ATOM   4251 C CG1   . VAL B 1 155 ? -22.220 75.257 -8.917  1.00 23.51 ? 296 VAL B CG1   1 
ATOM   4252 C CG2   . VAL B 1 155 ? -21.337 73.066 -9.802  1.00 22.68 ? 296 VAL B CG2   1 
ATOM   4253 N N     . ALA B 1 156 ? -21.210 77.526 -11.390 1.00 22.60 ? 297 ALA B N     1 
ATOM   4254 C CA    . ALA B 1 156 ? -21.026 78.974 -11.289 1.00 25.86 ? 297 ALA B CA    1 
ATOM   4255 C C     . ALA B 1 156 ? -21.599 79.496 -9.971  1.00 22.44 ? 297 ALA B C     1 
ATOM   4256 O O     . ALA B 1 156 ? -22.727 79.142 -9.611  1.00 22.78 ? 297 ALA B O     1 
ATOM   4257 C CB    . ALA B 1 156 ? -21.683 79.672 -12.478 1.00 23.92 ? 297 ALA B CB    1 
ATOM   4258 N N     . PRO B 1 157 ? -20.865 80.336 -9.236  1.00 27.92 ? 298 PRO B N     1 
ATOM   4259 C CA    . PRO B 1 157 ? -21.280 80.715 -7.877  1.00 22.84 ? 298 PRO B CA    1 
ATOM   4260 C C     . PRO B 1 157 ? -22.294 81.852 -7.849  1.00 27.40 ? 298 PRO B C     1 
ATOM   4261 O O     . PRO B 1 157 ? -22.573 82.520 -8.850  1.00 29.03 ? 298 PRO B O     1 
ATOM   4262 C CB    . PRO B 1 157 ? -19.970 81.167 -7.228  1.00 25.22 ? 298 PRO B CB    1 
ATOM   4263 C CG    . PRO B 1 157 ? -19.201 81.793 -8.392  1.00 25.07 ? 298 PRO B CG    1 
ATOM   4264 C CD    . PRO B 1 157 ? -19.552 80.910 -9.595  1.00 24.45 ? 298 PRO B CD    1 
ATOM   4265 N N     . VAL B 1 158 ? -22.823 82.076 -6.642  1.00 25.21 ? 299 VAL B N     1 
ATOM   4266 C CA    . VAL B 1 158 ? -23.711 83.186 -6.329  1.00 29.28 ? 299 VAL B CA    1 
ATOM   4267 C C     . VAL B 1 158 ? -23.122 83.961 -5.151  1.00 30.16 ? 299 VAL B C     1 
ATOM   4268 O O     . VAL B 1 158 ? -22.241 83.478 -4.432  1.00 29.73 ? 299 VAL B O     1 
ATOM   4269 C CB    . VAL B 1 158 ? -25.144 82.718 -5.989  1.00 27.57 ? 299 VAL B CB    1 
ATOM   4270 C CG1   . VAL B 1 158 ? -25.770 82.007 -7.170  1.00 25.13 ? 299 VAL B CG1   1 
ATOM   4271 C CG2   . VAL B 1 158 ? -25.138 81.829 -4.741  1.00 26.21 ? 299 VAL B CG2   1 
ATOM   4272 N N     . ASP B 1 159 ? -23.629 85.174 -4.945  1.00 28.13 ? 300 ASP B N     1 
ATOM   4273 C CA    . ASP B 1 159 ? -23.272 85.907 -3.736  1.00 29.43 ? 300 ASP B CA    1 
ATOM   4274 C C     . ASP B 1 159 ? -24.218 85.525 -2.594  1.00 31.37 ? 300 ASP B C     1 
ATOM   4275 O O     . ASP B 1 159 ? -25.105 84.677 -2.747  1.00 30.70 ? 300 ASP B O     1 
ATOM   4276 C CB    . ASP B 1 159 ? -23.245 87.417 -3.998  1.00 29.28 ? 300 ASP B CB    1 
ATOM   4277 C CG    . ASP B 1 159 ? -24.610 87.998 -4.363  1.00 34.72 ? 300 ASP B CG    1 
ATOM   4278 O OD1   . ASP B 1 159 ? -25.659 87.412 -4.012  1.00 37.60 ? 300 ASP B OD1   1 
ATOM   4279 O OD2   . ASP B 1 159 ? -24.630 89.077 -4.998  1.00 35.48 ? 300 ASP B OD2   1 
ATOM   4280 N N     . ASP B 1 160 ? -24.032 86.163 -1.431  1.00 29.87 ? 301 ASP B N     1 
ATOM   4281 C CA    . ASP B 1 160 ? -24.792 85.784 -0.245  1.00 34.59 ? 301 ASP B CA    1 
ATOM   4282 C C     . ASP B 1 160 ? -26.277 86.060 -0.415  1.00 36.43 ? 301 ASP B C     1 
ATOM   4283 O O     . ASP B 1 160 ? -27.107 85.405 0.232   1.00 34.05 ? 301 ASP B O     1 
ATOM   4284 C CB    . ASP B 1 160 ? -24.256 86.521 0.991   1.00 33.91 ? 301 ASP B CB    1 
ATOM   4285 C CG    . ASP B 1 160 ? -22.924 85.974 1.463   1.00 40.02 ? 301 ASP B CG    1 
ATOM   4286 O OD1   . ASP B 1 160 ? -22.501 84.913 0.948   1.00 38.71 ? 301 ASP B OD1   1 
ATOM   4287 O OD2   . ASP B 1 160 ? -22.302 86.589 2.355   1.00 50.59 ? 301 ASP B OD2   1 
ATOM   4288 N N     . ALA B 1 161 ? -26.629 87.012 -1.282  1.00 30.11 ? 302 ALA B N     1 
ATOM   4289 C CA    . ALA B 1 161 ? -28.018 87.339 -1.564  1.00 31.34 ? 302 ALA B CA    1 
ATOM   4290 C C     . ALA B 1 161 ? -28.679 86.366 -2.535  1.00 33.99 ? 302 ALA B C     1 
ATOM   4291 O O     . ALA B 1 161 ? -29.908 86.404 -2.676  1.00 34.44 ? 302 ALA B O     1 
ATOM   4292 C CB    . ALA B 1 161 ? -28.115 88.761 -2.125  1.00 34.18 ? 302 ALA B CB    1 
ATOM   4293 N N     . GLY B 1 162 ? -27.912 85.501 -3.201  1.00 31.48 ? 303 GLY B N     1 
ATOM   4294 C CA    . GLY B 1 162 ? -28.464 84.603 -4.196  1.00 29.65 ? 303 GLY B CA    1 
ATOM   4295 C C     . GLY B 1 162 ? -28.408 85.096 -5.629  1.00 29.96 ? 303 GLY B C     1 
ATOM   4296 O O     . GLY B 1 162 ? -29.089 84.519 -6.486  1.00 28.93 ? 303 GLY B O     1 
ATOM   4297 N N     . ASN B 1 163 ? -27.634 86.145 -5.920  1.00 31.68 ? 304 ASN B N     1 
ATOM   4298 C CA    . ASN B 1 163 ? -27.450 86.616 -7.293  1.00 28.77 ? 304 ASN B CA    1 
ATOM   4299 C C     . ASN B 1 163 ? -26.394 85.785 -8.000  1.00 31.04 ? 304 ASN B C     1 
ATOM   4300 O O     . ASN B 1 163 ? -25.345 85.490 -7.427  1.00 30.82 ? 304 ASN B O     1 
ATOM   4301 C CB    . ASN B 1 163 ? -26.988 88.079 -7.330  1.00 29.75 ? 304 ASN B CB    1 
ATOM   4302 C CG    . ASN B 1 163 ? -27.995 89.042 -6.746  1.00 30.56 ? 304 ASN B CG    1 
ATOM   4303 O OD1   . ASN B 1 163 ? -29.038 89.301 -7.343  1.00 35.47 ? 304 ASN B OD1   1 
ATOM   4304 N ND2   . ASN B 1 163 ? -27.659 89.627 -5.603  1.00 32.52 ? 304 ASN B ND2   1 
ATOM   4305 N N     . LEU B 1 164 ? -26.644 85.455 -9.267  1.00 29.19 ? 305 LEU B N     1 
ATOM   4306 C CA    . LEU B 1 164 ? -25.610 84.819 -10.075 1.00 27.63 ? 305 LEU B CA    1 
ATOM   4307 C C     . LEU B 1 164 ? -24.490 85.815 -10.364 1.00 30.81 ? 305 LEU B C     1 
ATOM   4308 O O     . LEU B 1 164 ? -24.748 86.953 -10.767 1.00 32.62 ? 305 LEU B O     1 
ATOM   4309 C CB    . LEU B 1 164 ? -26.196 84.294 -11.378 1.00 28.17 ? 305 LEU B CB    1 
ATOM   4310 C CG    . LEU B 1 164 ? -25.266 83.445 -12.245 1.00 29.76 ? 305 LEU B CG    1 
ATOM   4311 C CD1   . LEU B 1 164 ? -25.024 82.106 -11.576 1.00 25.74 ? 305 LEU B CD1   1 
ATOM   4312 C CD2   . LEU B 1 164 ? -25.872 83.246 -13.622 1.00 25.96 ? 305 LEU B CD2   1 
ATOM   4313 N N     . LEU B 1 165 ? -23.244 85.386 -10.165 1.00 29.15 ? 306 LEU B N     1 
ATOM   4314 C CA    . LEU B 1 165 ? -22.073 86.238 -10.376 1.00 28.90 ? 306 LEU B CA    1 
ATOM   4315 C C     . LEU B 1 165 ? -21.607 86.086 -11.819 1.00 30.38 ? 306 LEU B C     1 
ATOM   4316 O O     . LEU B 1 165 ? -21.032 85.059 -12.187 1.00 27.90 ? 306 LEU B O     1 
ATOM   4317 C CB    . LEU B 1 165 ? -20.967 85.868 -9.395  1.00 29.32 ? 306 LEU B CB    1 
ATOM   4318 C CG    . LEU B 1 165 ? -21.298 86.140 -7.929  1.00 30.79 ? 306 LEU B CG    1 
ATOM   4319 C CD1   . LEU B 1 165 ? -20.241 85.550 -6.993  1.00 31.60 ? 306 LEU B CD1   1 
ATOM   4320 C CD2   . LEU B 1 165 ? -21.443 87.649 -7.708  1.00 33.20 ? 306 LEU B CD2   1 
ATOM   4321 N N     . LEU B 1 166 ? -21.849 87.108 -12.640 1.00 30.97 ? 307 LEU B N     1 
ATOM   4322 C CA    . LEU B 1 166 ? -21.643 86.948 -14.077 1.00 29.12 ? 307 LEU B CA    1 
ATOM   4323 C C     . LEU B 1 166 ? -20.164 86.865 -14.441 1.00 30.87 ? 307 LEU B C     1 
ATOM   4324 O O     . LEU B 1 166 ? -19.791 86.120 -15.357 1.00 31.68 ? 307 LEU B O     1 
ATOM   4325 C CB    . LEU B 1 166 ? -22.328 88.080 -14.838 1.00 32.10 ? 307 LEU B CB    1 
ATOM   4326 C CG    . LEU B 1 166 ? -23.834 87.927 -15.059 1.00 35.47 ? 307 LEU B CG    1 
ATOM   4327 C CD1   . LEU B 1 166 ? -24.357 89.110 -15.874 1.00 38.11 ? 307 LEU B CD1   1 
ATOM   4328 C CD2   . LEU B 1 166 ? -24.145 86.613 -15.763 1.00 31.90 ? 307 LEU B CD2   1 
ATOM   4329 N N     . GLY B 1 167 ? -19.306 87.623 -13.753 1.00 32.78 ? 308 GLY B N     1 
ATOM   4330 C CA    . GLY B 1 167 ? -17.880 87.552 -14.048 1.00 32.89 ? 308 GLY B CA    1 
ATOM   4331 C C     . GLY B 1 167 ? -17.297 86.179 -13.763 1.00 35.32 ? 308 GLY B C     1 
ATOM   4332 O O     . GLY B 1 167 ? -16.573 85.611 -14.588 1.00 32.20 ? 308 GLY B O     1 
ATOM   4333 N N     . GLU B 1 168 ? -17.608 85.628 -12.585 1.00 32.30 ? 309 GLU B N     1 
ATOM   4334 C CA    . GLU B 1 168 ? -17.156 84.280 -12.233 1.00 31.52 ? 309 GLU B CA    1 
ATOM   4335 C C     . GLU B 1 168 ? -17.758 83.220 -13.160 1.00 30.99 ? 309 GLU B C     1 
ATOM   4336 O O     . GLU B 1 168 ? -17.075 82.256 -13.562 1.00 32.68 ? 309 GLU B O     1 
ATOM   4337 C CB    . GLU B 1 168 ? -17.493 83.995 -10.768 1.00 31.37 ? 309 GLU B CB    1 
ATOM   4338 C CG    . GLU B 1 168 ? -16.783 84.901 -9.735  1.00 35.08 ? 309 GLU B CG    1 
ATOM   4339 C CD    . GLU B 1 168 ? -17.413 86.299 -9.551  1.00 43.07 ? 309 GLU B CD    1 
ATOM   4340 O OE1   . GLU B 1 168 ? -17.936 86.886 -10.526 1.00 42.02 ? 309 GLU B OE1   1 
ATOM   4341 O OE2   . GLU B 1 168 ? -17.357 86.832 -8.417  1.00 51.70 ? 309 GLU B OE2   1 
ATOM   4342 N N     . PHE B 1 169 ? -19.025 83.398 -13.542 1.00 27.22 ? 310 PHE B N     1 
ATOM   4343 C CA    . PHE B 1 169 ? -19.627 82.493 -14.516 1.00 29.72 ? 310 PHE B CA    1 
ATOM   4344 C C     . PHE B 1 169 ? -18.827 82.490 -15.816 1.00 28.76 ? 310 PHE B C     1 
ATOM   4345 O O     . PHE B 1 169 ? -18.437 81.425 -16.313 1.00 27.37 ? 310 PHE B O     1 
ATOM   4346 C CB    . PHE B 1 169 ? -21.082 82.879 -14.776 1.00 24.14 ? 310 PHE B CB    1 
ATOM   4347 C CG    . PHE B 1 169 ? -21.656 82.268 -16.036 1.00 26.59 ? 310 PHE B CG    1 
ATOM   4348 C CD1   . PHE B 1 169 ? -21.913 80.904 -16.108 1.00 27.24 ? 310 PHE B CD1   1 
ATOM   4349 C CD2   . PHE B 1 169 ? -21.925 83.056 -17.142 1.00 22.87 ? 310 PHE B CD2   1 
ATOM   4350 C CE1   . PHE B 1 169 ? -22.436 80.338 -17.271 1.00 28.96 ? 310 PHE B CE1   1 
ATOM   4351 C CE2   . PHE B 1 169 ? -22.451 82.505 -18.302 1.00 23.34 ? 310 PHE B CE2   1 
ATOM   4352 C CZ    . PHE B 1 169 ? -22.704 81.143 -18.372 1.00 24.42 ? 310 PHE B CZ    1 
ATOM   4353 N N     . GLU B 1 170 ? -18.553 83.682 -16.367 1.00 25.74 ? 311 GLU B N     1 
ATOM   4354 C CA    . GLU B 1 170 ? -17.817 83.772 -17.628 1.00 29.65 ? 311 GLU B CA    1 
ATOM   4355 C C     . GLU B 1 170 ? -16.407 83.205 -17.482 1.00 31.59 ? 311 GLU B C     1 
ATOM   4356 O O     . GLU B 1 170 ? -15.895 82.552 -18.403 1.00 26.38 ? 311 GLU B O     1 
ATOM   4357 C CB    . GLU B 1 170 ? -17.770 85.227 -18.119 1.00 28.61 ? 311 GLU B CB    1 
ATOM   4358 C CG    . GLU B 1 170 ? -16.820 85.441 -19.311 1.00 30.98 ? 311 GLU B CG    1 
ATOM   4359 C CD    . GLU B 1 170 ? -17.036 86.757 -20.059 1.00 33.62 ? 311 GLU B CD    1 
ATOM   4360 O OE1   . GLU B 1 170 ? -17.688 87.678 -19.520 1.00 33.82 ? 311 GLU B OE1   1 
ATOM   4361 O OE2   . GLU B 1 170 ? -16.535 86.875 -21.198 1.00 35.65 ? 311 GLU B OE2   1 
ATOM   4362 N N     . ASP B 1 171 ? -15.769 83.431 -16.321 1.00 30.64 ? 312 ASP B N     1 
ATOM   4363 C CA    . ASP B 1 171 ? -14.472 82.824 -16.030 1.00 30.47 ? 312 ASP B CA    1 
ATOM   4364 C C     . ASP B 1 171 ? -14.516 81.302 -16.063 1.00 30.99 ? 312 ASP B C     1 
ATOM   4365 O O     . ASP B 1 171 ? -13.463 80.670 -16.204 1.00 31.07 ? 312 ASP B O     1 
ATOM   4366 C CB    . ASP B 1 171 ? -13.956 83.245 -14.648 1.00 36.60 ? 312 ASP B CB    1 
ATOM   4367 C CG    . ASP B 1 171 ? -13.557 84.711 -14.579 1.00 40.30 ? 312 ASP B CG    1 
ATOM   4368 O OD1   . ASP B 1 171 ? -13.435 85.357 -15.643 1.00 39.98 ? 312 ASP B OD1   1 
ATOM   4369 O OD2   . ASP B 1 171 ? -13.371 85.212 -13.447 1.00 42.58 ? 312 ASP B OD2   1 
ATOM   4370 N N     . LEU B 1 172 ? -15.690 80.694 -15.874 1.00 27.33 ? 313 LEU B N     1 
ATOM   4371 C CA    . LEU B 1 172 ? -15.754 79.239 -15.980 1.00 26.42 ? 313 LEU B CA    1 
ATOM   4372 C C     . LEU B 1 172 ? -15.791 78.736 -17.425 1.00 28.95 ? 313 LEU B C     1 
ATOM   4373 O O     . LEU B 1 172 ? -15.576 77.537 -17.656 1.00 25.62 ? 313 LEU B O     1 
ATOM   4374 C CB    . LEU B 1 172 ? -16.975 78.711 -15.234 1.00 23.99 ? 313 LEU B CB    1 
ATOM   4375 C CG    . LEU B 1 172 ? -16.930 78.861 -13.704 1.00 29.05 ? 313 LEU B CG    1 
ATOM   4376 C CD1   . LEU B 1 172 ? -18.153 78.220 -13.118 1.00 27.27 ? 313 LEU B CD1   1 
ATOM   4377 C CD2   . LEU B 1 172 ? -15.689 78.224 -13.124 1.00 28.82 ? 313 LEU B CD2   1 
ATOM   4378 N N     . LEU B 1 173 ? -16.063 79.604 -18.397 1.00 26.16 ? 314 LEU B N     1 
ATOM   4379 C CA    . LEU B 1 173 ? -16.202 79.173 -19.783 1.00 28.12 ? 314 LEU B CA    1 
ATOM   4380 C C     . LEU B 1 173 ? -14.845 79.134 -20.478 1.00 26.33 ? 314 LEU B C     1 
ATOM   4381 O O     . LEU B 1 173 ? -13.948 79.926 -20.177 1.00 26.30 ? 314 LEU B O     1 
ATOM   4382 C CB    . LEU B 1 173 ? -17.152 80.099 -20.544 1.00 26.85 ? 314 LEU B CB    1 
ATOM   4383 C CG    . LEU B 1 173 ? -18.486 80.365 -19.846 1.00 27.04 ? 314 LEU B CG    1 
ATOM   4384 C CD1   . LEU B 1 173 ? -19.316 81.367 -20.629 1.00 25.85 ? 314 LEU B CD1   1 
ATOM   4385 C CD2   . LEU B 1 173 ? -19.242 79.058 -19.685 1.00 25.62 ? 314 LEU B CD2   1 
ATOM   4386 N N     . GLY B 1 174 ? -14.704 78.202 -21.423 1.00 24.29 ? 315 GLY B N     1 
ATOM   4387 C CA    . GLY B 1 174 ? -13.478 78.079 -22.178 1.00 24.38 ? 315 GLY B CA    1 
ATOM   4388 C C     . GLY B 1 174 ? -13.639 77.193 -23.398 1.00 26.70 ? 315 GLY B C     1 
ATOM   4389 O O     . GLY B 1 174 ? -14.751 76.806 -23.774 1.00 22.47 ? 315 GLY B O     1 
ATOM   4390 N N     . PRO B 1 175 ? -12.517 76.839 -24.032 1.00 24.48 ? 316 PRO B N     1 
ATOM   4391 C CA    . PRO B 1 175 ? -12.588 76.052 -25.278 1.00 23.85 ? 316 PRO B CA    1 
ATOM   4392 C C     . PRO B 1 175 ? -13.103 74.626 -25.093 1.00 27.23 ? 316 PRO B C     1 
ATOM   4393 O O     . PRO B 1 175 ? -13.427 73.980 -26.095 1.00 24.81 ? 316 PRO B O     1 
ATOM   4394 C CB    . PRO B 1 175 ? -11.143 76.074 -25.791 1.00 27.20 ? 316 PRO B CB    1 
ATOM   4395 C CG    . PRO B 1 175 ? -10.305 76.333 -24.585 1.00 29.49 ? 316 PRO B CG    1 
ATOM   4396 C CD    . PRO B 1 175 ? -11.136 77.193 -23.662 1.00 23.86 ? 316 PRO B CD    1 
ATOM   4397 N N     . ARG B 1 176 ? -13.232 74.119 -23.864 1.00 25.41 ? 317 ARG B N     1 
ATOM   4398 C CA    . ARG B 1 176 ? -13.777 72.781 -23.665 1.00 24.86 ? 317 ARG B CA    1 
ATOM   4399 C C     . ARG B 1 176 ? -15.216 72.800 -23.151 1.00 24.00 ? 317 ARG B C     1 
ATOM   4400 O O     . ARG B 1 176 ? -15.756 71.742 -22.808 1.00 22.10 ? 317 ARG B O     1 
ATOM   4401 C CB    . ARG B 1 176 ? -12.878 71.972 -22.724 1.00 22.81 ? 317 ARG B CB    1 
ATOM   4402 C CG    . ARG B 1 176 ? -11.426 71.840 -23.207 1.00 28.49 ? 317 ARG B CG    1 
ATOM   4403 C CD    . ARG B 1 176 ? -11.324 71.130 -24.569 1.00 29.27 ? 317 ARG B CD    1 
ATOM   4404 N NE    . ARG B 1 176 ? -12.026 69.849 -24.598 1.00 31.10 ? 317 ARG B NE    1 
ATOM   4405 C CZ    . ARG B 1 176 ? -11.553 68.716 -24.090 1.00 30.59 ? 317 ARG B CZ    1 
ATOM   4406 N NH1   . ARG B 1 176 ? -10.350 68.654 -23.542 1.00 30.99 ? 317 ARG B NH1   1 
ATOM   4407 N NH2   . ARG B 1 176 ? -12.312 67.620 -24.128 1.00 24.41 ? 317 ARG B NH2   1 
ATOM   4408 N N     . THR B 1 177 ? -15.864 73.965 -23.104 1.00 24.70 ? 318 THR B N     1 
ATOM   4409 C CA    . THR B 1 177 ? -17.248 74.039 -22.632 1.00 22.06 ? 318 THR B CA    1 
ATOM   4410 C C     . THR B 1 177 ? -18.181 73.592 -23.748 1.00 21.28 ? 318 THR B C     1 
ATOM   4411 O O     . THR B 1 177 ? -18.309 74.272 -24.773 1.00 23.89 ? 318 THR B O     1 
ATOM   4412 C CB    . THR B 1 177 ? -17.619 75.447 -22.174 1.00 24.78 ? 318 THR B CB    1 
ATOM   4413 O OG1   . THR B 1 177 ? -16.652 75.939 -21.235 1.00 23.27 ? 318 THR B OG1   1 
ATOM   4414 C CG2   . THR B 1 177 ? -19.001 75.438 -21.536 1.00 18.77 ? 318 THR B CG2   1 
ATOM   4415 N N     . LYS B 1 178 ? -18.852 72.461 -23.548 1.00 16.61 ? 319 LYS B N     1 
ATOM   4416 C CA    . LYS B 1 178 ? -19.824 71.977 -24.522 1.00 20.74 ? 319 LYS B CA    1 
ATOM   4417 C C     . LYS B 1 178 ? -21.254 72.383 -24.192 1.00 20.14 ? 319 LYS B C     1 
ATOM   4418 O O     . LYS B 1 178 ? -22.081 72.534 -25.101 1.00 17.20 ? 319 LYS B O     1 
ATOM   4419 C CB    . LYS B 1 178 ? -19.760 70.449 -24.621 1.00 18.61 ? 319 LYS B CB    1 
ATOM   4420 C CG    . LYS B 1 178 ? -18.524 69.906 -25.366 1.00 25.76 ? 319 LYS B CG    1 
ATOM   4421 C CD    . LYS B 1 178 ? -18.792 69.787 -26.852 1.00 29.14 ? 319 LYS B CD    1 
ATOM   4422 C CE    . LYS B 1 178 ? -17.753 68.945 -27.571 1.00 30.83 ? 319 LYS B CE    1 
ATOM   4423 N NZ    . LYS B 1 178 ? -18.163 67.521 -27.712 1.00 31.97 ? 319 LYS B NZ    1 
ATOM   4424 N N     . LEU B 1 179 ? -21.561 72.569 -22.914 1.00 17.58 ? 320 LEU B N     1 
ATOM   4425 C CA    . LEU B 1 179 ? -22.936 72.809 -22.509 1.00 18.39 ? 320 LEU B CA    1 
ATOM   4426 C C     . LEU B 1 179 ? -22.966 73.724 -21.299 1.00 18.77 ? 320 LEU B C     1 
ATOM   4427 O O     . LEU B 1 179 ? -22.194 73.548 -20.351 1.00 20.57 ? 320 LEU B O     1 
ATOM   4428 C CB    . LEU B 1 179 ? -23.643 71.495 -22.184 1.00 17.64 ? 320 LEU B CB    1 
ATOM   4429 C CG    . LEU B 1 179 ? -25.096 71.579 -21.716 1.00 19.23 ? 320 LEU B CG    1 
ATOM   4430 C CD1   . LEU B 1 179 ? -26.003 71.972 -22.878 1.00 19.35 ? 320 LEU B CD1   1 
ATOM   4431 C CD2   . LEU B 1 179 ? -25.466 70.222 -21.178 1.00 20.97 ? 320 LEU B CD2   1 
ATOM   4432 N N     . VAL B 1 180 ? -23.875 74.690 -21.334 1.00 17.56 ? 321 VAL B N     1 
ATOM   4433 C CA    . VAL B 1 180 ? -24.279 75.450 -20.156 1.00 17.38 ? 321 VAL B CA    1 
ATOM   4434 C C     . VAL B 1 180 ? -25.722 75.071 -19.865 1.00 18.31 ? 321 VAL B C     1 
ATOM   4435 O O     . VAL B 1 180 ? -26.558 75.085 -20.775 1.00 19.50 ? 321 VAL B O     1 
ATOM   4436 C CB    . VAL B 1 180 ? -24.141 76.967 -20.376 1.00 19.91 ? 321 VAL B CB    1 
ATOM   4437 C CG1   . VAL B 1 180 ? -24.718 77.745 -19.165 1.00 17.98 ? 321 VAL B CG1   1 
ATOM   4438 C CG2   . VAL B 1 180 ? -22.673 77.342 -20.665 1.00 16.55 ? 321 VAL B CG2   1 
ATOM   4439 N N     . ALA B 1 181 ? -26.003 74.665 -18.629 1.00 17.51 ? 322 ALA B N     1 
ATOM   4440 C CA    . ALA B 1 181 ? -27.364 74.341 -18.203 1.00 19.92 ? 322 ALA B CA    1 
ATOM   4441 C C     . ALA B 1 181 ? -27.689 75.213 -16.999 1.00 18.69 ? 322 ALA B C     1 
ATOM   4442 O O     . ALA B 1 181 ? -27.108 75.025 -15.927 1.00 22.18 ? 322 ALA B O     1 
ATOM   4443 C CB    . ALA B 1 181 ? -27.511 72.860 -17.864 1.00 15.72 ? 322 ALA B CB    1 
ATOM   4444 N N     . ALA B 1 182 ? -28.615 76.159 -17.168 1.00 20.62 ? 323 ALA B N     1 
ATOM   4445 C CA    . ALA B 1 182 ? -28.877 77.172 -16.148 1.00 22.97 ? 323 ALA B CA    1 
ATOM   4446 C C     . ALA B 1 182 ? -30.370 77.308 -15.873 1.00 20.59 ? 323 ALA B C     1 
ATOM   4447 O O     . ALA B 1 182 ? -31.183 77.262 -16.797 1.00 23.11 ? 323 ALA B O     1 
ATOM   4448 C CB    . ALA B 1 182 ? -28.322 78.537 -16.580 1.00 19.00 ? 323 ALA B CB    1 
ATOM   4449 N N     . THR B 1 183 ? -30.734 77.478 -14.603 1.00 22.91 ? 324 THR B N     1 
ATOM   4450 C CA    . THR B 1 183 ? -32.120 77.786 -14.283 1.00 20.59 ? 324 THR B CA    1 
ATOM   4451 C C     . THR B 1 183 ? -32.416 79.238 -14.620 1.00 22.37 ? 324 THR B C     1 
ATOM   4452 O O     . THR B 1 183 ? -31.558 80.109 -14.477 1.00 27.53 ? 324 THR B O     1 
ATOM   4453 C CB    . THR B 1 183 ? -32.428 77.533 -12.804 1.00 24.97 ? 324 THR B CB    1 
ATOM   4454 O OG1   . THR B 1 183 ? -33.847 77.595 -12.596 1.00 27.17 ? 324 THR B OG1   1 
ATOM   4455 C CG2   . THR B 1 183 ? -31.767 78.571 -11.911 1.00 24.48 ? 324 THR B CG2   1 
ATOM   4456 N N     . GLN B 1 184 ? -33.638 79.495 -15.094 1.00 22.84 ? 325 GLN B N     1 
ATOM   4457 C CA    . GLN B 1 184 ? -34.070 80.878 -15.268 1.00 23.58 ? 325 GLN B CA    1 
ATOM   4458 C C     . GLN B 1 184 ? -34.615 81.468 -13.974 1.00 22.88 ? 325 GLN B C     1 
ATOM   4459 O O     . GLN B 1 184 ? -34.407 82.656 -13.699 1.00 25.91 ? 325 GLN B O     1 
ATOM   4460 C CB    . GLN B 1 184 ? -35.136 80.995 -16.361 1.00 21.45 ? 325 GLN B CB    1 
ATOM   4461 C CG    . GLN B 1 184 ? -35.444 82.456 -16.715 1.00 23.15 ? 325 GLN B CG    1 
ATOM   4462 C CD    . GLN B 1 184 ? -36.240 82.579 -17.987 1.00 23.72 ? 325 GLN B CD    1 
ATOM   4463 O OE1   . GLN B 1 184 ? -36.739 81.583 -18.519 1.00 21.38 ? 325 GLN B OE1   1 
ATOM   4464 N NE2   . GLN B 1 184 ? -36.378 83.803 -18.483 1.00 25.44 ? 325 GLN B NE2   1 
ATOM   4465 N N     . VAL B 1 185 ? -35.314 80.667 -13.173 1.00 23.68 ? 326 VAL B N     1 
ATOM   4466 C CA    . VAL B 1 185 ? -35.811 81.103 -11.872 1.00 20.78 ? 326 VAL B CA    1 
ATOM   4467 C C     . VAL B 1 185 ? -35.534 80.002 -10.862 1.00 24.85 ? 326 VAL B C     1 
ATOM   4468 O O     . VAL B 1 185 ? -35.920 78.844 -11.071 1.00 19.14 ? 326 VAL B O     1 
ATOM   4469 C CB    . VAL B 1 185 ? -37.315 81.441 -11.894 1.00 19.99 ? 326 VAL B CB    1 
ATOM   4470 C CG1   . VAL B 1 185 ? -37.832 81.716 -10.468 1.00 24.50 ? 326 VAL B CG1   1 
ATOM   4471 C CG2   . VAL B 1 185 ? -37.579 82.621 -12.809 1.00 23.20 ? 326 VAL B CG2   1 
ATOM   4472 N N     . SER B 1 186 ? -34.875 80.366 -9.763  1.00 22.62 ? 327 SER B N     1 
ATOM   4473 C CA    . SER B 1 186 ? -34.546 79.405 -8.723  1.00 23.61 ? 327 SER B CA    1 
ATOM   4474 C C     . SER B 1 186 ? -35.803 79.048 -7.926  1.00 26.83 ? 327 SER B C     1 
ATOM   4475 O O     . SER B 1 186 ? -36.486 79.933 -7.383  1.00 25.30 ? 327 SER B O     1 
ATOM   4476 C CB    . SER B 1 186 ? -33.469 79.993 -7.813  1.00 24.00 ? 327 SER B CB    1 
ATOM   4477 O OG    . SER B 1 186 ? -33.417 79.277 -6.592  1.00 23.95 ? 327 SER B OG    1 
ATOM   4478 N N     . ASN B 1 187 ? -36.117 77.756 -7.851  1.00 22.29 ? 328 ASN B N     1 
ATOM   4479 C CA    . ASN B 1 187 ? -37.305 77.347 -7.103  1.00 25.16 ? 328 ASN B CA    1 
ATOM   4480 C C     . ASN B 1 187 ? -37.132 77.477 -5.594  1.00 24.75 ? 328 ASN B C     1 
ATOM   4481 O O     . ASN B 1 187 ? -38.132 77.484 -4.872  1.00 25.55 ? 328 ASN B O     1 
ATOM   4482 C CB    . ASN B 1 187 ? -37.671 75.905 -7.425  1.00 22.05 ? 328 ASN B CB    1 
ATOM   4483 C CG    . ASN B 1 187 ? -36.687 74.928 -6.845  1.00 27.91 ? 328 ASN B CG    1 
ATOM   4484 O OD1   . ASN B 1 187 ? -35.489 74.992 -7.150  1.00 27.31 ? 328 ASN B OD1   1 
ATOM   4485 N ND2   . ASN B 1 187 ? -37.175 74.011 -6.002  1.00 25.34 ? 328 ASN B ND2   1 
ATOM   4486 N N     . ALA B 1 188 ? -35.901 77.541 -5.092  1.00 23.52 ? 329 ALA B N     1 
ATOM   4487 C CA    . ALA B 1 188 ? -35.690 77.653 -3.654  1.00 26.23 ? 329 ALA B CA    1 
ATOM   4488 C C     . ALA B 1 188 ? -35.505 79.087 -3.189  1.00 30.49 ? 329 ALA B C     1 
ATOM   4489 O O     . ALA B 1 188 ? -35.865 79.405 -2.047  1.00 28.38 ? 329 ALA B O     1 
ATOM   4490 C CB    . ALA B 1 188 ? -34.469 76.832 -3.214  1.00 22.60 ? 329 ALA B CB    1 
ATOM   4491 N N     . LEU B 1 189 ? -34.941 79.952 -4.040  1.00 26.85 ? 330 LEU B N     1 
ATOM   4492 C CA    . LEU B 1 189 ? -34.651 81.332 -3.672  1.00 27.33 ? 330 LEU B CA    1 
ATOM   4493 C C     . LEU B 1 189 ? -35.471 82.361 -4.431  1.00 26.39 ? 330 LEU B C     1 
ATOM   4494 O O     . LEU B 1 189 ? -35.544 83.512 -3.988  1.00 28.17 ? 330 LEU B O     1 
ATOM   4495 C CB    . LEU B 1 189 ? -33.166 81.651 -3.911  1.00 26.99 ? 330 LEU B CB    1 
ATOM   4496 C CG    . LEU B 1 189 ? -32.119 80.889 -3.109  1.00 27.37 ? 330 LEU B CG    1 
ATOM   4497 C CD1   . LEU B 1 189 ? -30.747 81.527 -3.329  1.00 28.45 ? 330 LEU B CD1   1 
ATOM   4498 C CD2   . LEU B 1 189 ? -32.489 80.904 -1.635  1.00 30.54 ? 330 LEU B CD2   1 
ATOM   4499 N N     . GLY B 1 190 ? -36.059 81.990 -5.569  1.00 24.20 ? 331 GLY B N     1 
ATOM   4500 C CA    . GLY B 1 190 ? -36.751 82.941 -6.410  1.00 27.59 ? 331 GLY B CA    1 
ATOM   4501 C C     . GLY B 1 190 ? -35.873 83.793 -7.302  1.00 25.63 ? 331 GLY B C     1 
ATOM   4502 O O     . GLY B 1 190 ? -36.411 84.604 -8.068  1.00 27.23 ? 331 GLY B O     1 
ATOM   4503 N N     . THR B 1 191 ? -34.549 83.632 -7.248  1.00 24.08 ? 332 THR B N     1 
ATOM   4504 C CA    . THR B 1 191 ? -33.662 84.450 -8.072  1.00 28.83 ? 332 THR B CA    1 
ATOM   4505 C C     . THR B 1 191 ? -33.996 84.297 -9.548  1.00 27.14 ? 332 THR B C     1 
ATOM   4506 O O     . THR B 1 191 ? -34.156 83.179 -10.044 1.00 23.47 ? 332 THR B O     1 
ATOM   4507 C CB    . THR B 1 191 ? -32.204 84.061 -7.858  1.00 29.63 ? 332 THR B CB    1 
ATOM   4508 O OG1   . THR B 1 191 ? -31.865 84.153 -6.469  1.00 27.73 ? 332 THR B OG1   1 
ATOM   4509 C CG2   . THR B 1 191 ? -31.282 84.966 -8.699  1.00 28.57 ? 332 THR B CG2   1 
ATOM   4510 N N     . VAL B 1 192 ? -34.108 85.429 -10.238 1.00 27.58 ? 333 VAL B N     1 
ATOM   4511 C CA    . VAL B 1 192 ? -34.235 85.472 -11.689 1.00 26.70 ? 333 VAL B CA    1 
ATOM   4512 C C     . VAL B 1 192 ? -32.837 85.682 -12.256 1.00 28.31 ? 333 VAL B C     1 
ATOM   4513 O O     . VAL B 1 192 ? -32.162 86.658 -11.913 1.00 31.95 ? 333 VAL B O     1 
ATOM   4514 C CB    . VAL B 1 192 ? -35.195 86.586 -12.140 1.00 30.25 ? 333 VAL B CB    1 
ATOM   4515 C CG1   . VAL B 1 192 ? -35.317 86.613 -13.667 1.00 28.25 ? 333 VAL B CG1   1 
ATOM   4516 C CG2   . VAL B 1 192 ? -36.563 86.409 -11.487 1.00 27.11 ? 333 VAL B CG2   1 
ATOM   4517 N N     . THR B 1 193 ? -32.389 84.753 -13.104 1.00 26.09 ? 334 THR B N     1 
ATOM   4518 C CA    . THR B 1 193 ? -31.056 84.903 -13.658 1.00 26.50 ? 334 THR B CA    1 
ATOM   4519 C C     . THR B 1 193 ? -31.121 85.597 -15.017 1.00 27.47 ? 334 THR B C     1 
ATOM   4520 O O     . THR B 1 193 ? -32.154 85.550 -15.699 1.00 27.28 ? 334 THR B O     1 
ATOM   4521 C CB    . THR B 1 193 ? -30.391 83.539 -13.803 1.00 24.68 ? 334 THR B CB    1 
ATOM   4522 O OG1   . THR B 1 193 ? -31.060 82.794 -14.832 1.00 24.80 ? 334 THR B OG1   1 
ATOM   4523 C CG2   . THR B 1 193 ? -30.453 82.775 -12.483 1.00 25.74 ? 334 THR B CG2   1 
ATOM   4524 N N     . PRO B 1 194 ? -30.034 86.264 -15.430 1.00 28.07 ? 335 PRO B N     1 
ATOM   4525 C CA    . PRO B 1 194 ? -30.022 86.969 -16.734 1.00 27.08 ? 335 PRO B CA    1 
ATOM   4526 C C     . PRO B 1 194 ? -29.801 86.014 -17.905 1.00 29.84 ? 335 PRO B C     1 
ATOM   4527 O O     . PRO B 1 194 ? -28.698 85.869 -18.448 1.00 26.74 ? 335 PRO B O     1 
ATOM   4528 C CB    . PRO B 1 194 ? -28.857 87.949 -16.569 1.00 29.11 ? 335 PRO B CB    1 
ATOM   4529 C CG    . PRO B 1 194 ? -27.896 87.195 -15.716 1.00 27.85 ? 335 PRO B CG    1 
ATOM   4530 C CD    . PRO B 1 194 ? -28.752 86.431 -14.717 1.00 29.19 ? 335 PRO B CD    1 
ATOM   4531 N N     . VAL B 1 195 ? -30.887 85.353 -18.327 1.00 27.12 ? 336 VAL B N     1 
ATOM   4532 C CA    . VAL B 1 195 ? -30.747 84.249 -19.272 1.00 29.42 ? 336 VAL B CA    1 
ATOM   4533 C C     . VAL B 1 195 ? -30.251 84.729 -20.632 1.00 26.66 ? 336 VAL B C     1 
ATOM   4534 O O     . VAL B 1 195 ? -29.532 83.996 -21.314 1.00 25.26 ? 336 VAL B O     1 
ATOM   4535 C CB    . VAL B 1 195 ? -32.068 83.470 -19.408 1.00 28.29 ? 336 VAL B CB    1 
ATOM   4536 C CG1   . VAL B 1 195 ? -32.296 82.610 -18.168 1.00 25.05 ? 336 VAL B CG1   1 
ATOM   4537 C CG2   . VAL B 1 195 ? -33.223 84.431 -19.632 1.00 32.06 ? 336 VAL B CG2   1 
ATOM   4538 N N     . GLU B 1 196 ? -30.625 85.936 -21.069 1.00 28.72 ? 337 GLU B N     1 
ATOM   4539 C CA    . GLU B 1 196 ? -30.098 86.432 -22.341 1.00 28.00 ? 337 GLU B CA    1 
ATOM   4540 C C     . GLU B 1 196 ? -28.575 86.505 -22.312 1.00 29.56 ? 337 GLU B C     1 
ATOM   4541 O O     . GLU B 1 196 ? -27.902 86.054 -23.253 1.00 30.41 ? 337 GLU B O     1 
ATOM   4542 C CB    . GLU B 1 196 ? -30.694 87.800 -22.677 1.00 34.10 ? 337 GLU B CB    1 
ATOM   4543 C CG    . GLU B 1 196 ? -32.188 87.776 -22.953 1.00 36.31 ? 337 GLU B CG    1 
ATOM   4544 C CD    . GLU B 1 196 ? -33.017 87.920 -21.688 1.00 46.38 ? 337 GLU B CD    1 
ATOM   4545 O OE1   . GLU B 1 196 ? -32.426 87.946 -20.577 1.00 45.73 ? 337 GLU B OE1   1 
ATOM   4546 O OE2   . GLU B 1 196 ? -34.262 88.007 -21.805 1.00 48.11 ? 337 GLU B OE2   1 
ATOM   4547 N N     . THR B 1 197 ? -28.016 87.046 -21.226 1.00 28.25 ? 338 THR B N     1 
ATOM   4548 C CA    . THR B 1 197 ? -26.565 87.096 -21.083 1.00 28.72 ? 338 THR B CA    1 
ATOM   4549 C C     . THR B 1 197 ? -25.973 85.699 -21.039 1.00 28.51 ? 338 THR B C     1 
ATOM   4550 O O     . THR B 1 197 ? -24.945 85.437 -21.675 1.00 28.70 ? 338 THR B O     1 
ATOM   4551 C CB    . THR B 1 197 ? -26.183 87.868 -19.823 1.00 28.18 ? 338 THR B CB    1 
ATOM   4552 O OG1   . THR B 1 197 ? -26.870 89.122 -19.824 1.00 33.77 ? 338 THR B OG1   1 
ATOM   4553 C CG2   . THR B 1 197 ? -24.675 88.115 -19.783 1.00 28.24 ? 338 THR B CG2   1 
ATOM   4554 N N     . ILE B 1 198 ? -26.613 84.787 -20.298 1.00 26.48 ? 339 ILE B N     1 
ATOM   4555 C CA    . ILE B 1 198 ? -26.095 83.429 -20.159 1.00 24.16 ? 339 ILE B CA    1 
ATOM   4556 C C     . ILE B 1 198 ? -26.031 82.747 -21.518 1.00 23.21 ? 339 ILE B C     1 
ATOM   4557 O O     . ILE B 1 198 ? -25.010 82.153 -21.887 1.00 25.61 ? 339 ILE B O     1 
ATOM   4558 C CB    . ILE B 1 198 ? -26.950 82.630 -19.156 1.00 25.26 ? 339 ILE B CB    1 
ATOM   4559 C CG1   . ILE B 1 198 ? -26.829 83.241 -17.757 1.00 25.79 ? 339 ILE B CG1   1 
ATOM   4560 C CG2   . ILE B 1 198 ? -26.540 81.165 -19.129 1.00 20.17 ? 339 ILE B CG2   1 
ATOM   4561 C CD1   . ILE B 1 198 ? -27.828 82.647 -16.747 1.00 28.81 ? 339 ILE B CD1   1 
ATOM   4562 N N     . VAL B 1 199 ? -27.114 82.842 -22.291 1.00 22.89 ? 340 VAL B N     1 
ATOM   4563 C CA    . VAL B 1 199 ? -27.136 82.240 -23.620 1.00 22.80 ? 340 VAL B CA    1 
ATOM   4564 C C     . VAL B 1 199 ? -26.054 82.858 -24.502 1.00 23.72 ? 340 VAL B C     1 
ATOM   4565 O O     . VAL B 1 199 ? -25.296 82.144 -25.171 1.00 24.75 ? 340 VAL B O     1 
ATOM   4566 C CB    . VAL B 1 199 ? -28.529 82.382 -24.257 1.00 23.44 ? 340 VAL B CB    1 
ATOM   4567 C CG1   . VAL B 1 199 ? -28.482 81.962 -25.730 1.00 22.38 ? 340 VAL B CG1   1 
ATOM   4568 C CG2   . VAL B 1 199 ? -29.561 81.568 -23.492 1.00 21.55 ? 340 VAL B CG2   1 
ATOM   4569 N N     . GLU B 1 200 ? -25.979 84.195 -24.542 1.00 25.37 ? 341 GLU B N     1 
ATOM   4570 C CA    . GLU B 1 200 ? -25.010 84.838 -25.431 1.00 27.01 ? 341 GLU B CA    1 
ATOM   4571 C C     . GLU B 1 200 ? -23.584 84.446 -25.060 1.00 25.78 ? 341 GLU B C     1 
ATOM   4572 O O     . GLU B 1 200 ? -22.757 84.172 -25.938 1.00 27.92 ? 341 GLU B O     1 
ATOM   4573 C CB    . GLU B 1 200 ? -25.172 86.362 -25.390 1.00 27.03 ? 341 GLU B CB    1 
ATOM   4574 C CG    . GLU B 1 200 ? -24.390 87.135 -26.465 1.00 38.10 ? 341 GLU B CG    1 
ATOM   4575 C CD    . GLU B 1 200 ? -22.876 87.205 -26.216 1.00 48.17 ? 341 GLU B CD    1 
ATOM   4576 O OE1   . GLU B 1 200 ? -22.098 87.203 -27.202 1.00 48.62 ? 341 GLU B OE1   1 
ATOM   4577 O OE2   . GLU B 1 200 ? -22.459 87.256 -25.036 1.00 46.47 ? 341 GLU B OE2   1 
ATOM   4578 N N     . LEU B 1 201 ? -23.285 84.399 -23.762 1.00 26.24 ? 342 LEU B N     1 
ATOM   4579 C CA    . LEU B 1 201 ? -21.952 84.023 -23.309 1.00 24.43 ? 342 LEU B CA    1 
ATOM   4580 C C     . LEU B 1 201 ? -21.642 82.573 -23.664 1.00 25.22 ? 342 LEU B C     1 
ATOM   4581 O O     . LEU B 1 201 ? -20.571 82.271 -24.204 1.00 23.93 ? 342 LEU B O     1 
ATOM   4582 C CB    . LEU B 1 201 ? -21.835 84.246 -21.802 1.00 22.04 ? 342 LEU B CB    1 
ATOM   4583 C CG    . LEU B 1 201 ? -21.468 85.678 -21.381 1.00 31.47 ? 342 LEU B CG    1 
ATOM   4584 C CD1   . LEU B 1 201 ? -21.675 85.890 -19.886 1.00 28.35 ? 342 LEU B CD1   1 
ATOM   4585 C CD2   . LEU B 1 201 ? -20.048 86.068 -21.822 1.00 32.23 ? 342 LEU B CD2   1 
ATOM   4586 N N     . GLY B 1 202 ? -22.570 81.659 -23.371 1.00 24.82 ? 343 GLY B N     1 
ATOM   4587 C CA    . GLY B 1 202 ? -22.336 80.265 -23.709 1.00 22.89 ? 343 GLY B CA    1 
ATOM   4588 C C     . GLY B 1 202 ? -22.068 80.084 -25.189 1.00 23.56 ? 343 GLY B C     1 
ATOM   4589 O O     . GLY B 1 202 ? -21.135 79.378 -25.584 1.00 23.66 ? 343 GLY B O     1 
ATOM   4590 N N     . HIS B 1 203 ? -22.873 80.742 -26.028 1.00 22.55 ? 344 HIS B N     1 
ATOM   4591 C CA    . HIS B 1 203 ? -22.689 80.635 -27.472 1.00 26.73 ? 344 HIS B CA    1 
ATOM   4592 C C     . HIS B 1 203 ? -21.347 81.211 -27.896 1.00 26.13 ? 344 HIS B C     1 
ATOM   4593 O O     . HIS B 1 203 ? -20.667 80.645 -28.763 1.00 27.09 ? 344 HIS B O     1 
ATOM   4594 C CB    . HIS B 1 203 ? -23.831 81.345 -28.199 1.00 22.46 ? 344 HIS B CB    1 
ATOM   4595 C CG    . HIS B 1 203 ? -25.099 80.551 -28.226 1.00 26.14 ? 344 HIS B CG    1 
ATOM   4596 N ND1   . HIS B 1 203 ? -26.307 81.081 -28.621 1.00 24.62 ? 344 HIS B ND1   1 
ATOM   4597 C CD2   . HIS B 1 203 ? -25.343 79.258 -27.900 1.00 23.45 ? 344 HIS B CD2   1 
ATOM   4598 C CE1   . HIS B 1 203 ? -27.240 80.147 -28.550 1.00 25.32 ? 344 HIS B CE1   1 
ATOM   4599 N NE2   . HIS B 1 203 ? -26.681 79.031 -28.113 1.00 26.56 ? 344 HIS B NE2   1 
ATOM   4600 N N     . ARG B 1 204 ? -20.952 82.340 -27.301 1.00 24.19 ? 345 ARG B N     1 
ATOM   4601 C CA    . ARG B 1 204 ? -19.668 82.940 -27.645 1.00 28.93 ? 345 ARG B CA    1 
ATOM   4602 C C     . ARG B 1 204 ? -18.517 81.973 -27.386 1.00 28.60 ? 345 ARG B C     1 
ATOM   4603 O O     . ARG B 1 204 ? -17.552 81.922 -28.157 1.00 26.28 ? 345 ARG B O     1 
ATOM   4604 C CB    . ARG B 1 204 ? -19.466 84.236 -26.860 1.00 31.44 ? 345 ARG B CB    1 
ATOM   4605 C CG    . ARG B 1 204 ? -18.073 84.841 -27.027 1.00 39.49 ? 345 ARG B CG    1 
ATOM   4606 C CD    . ARG B 1 204 ? -17.860 86.036 -26.105 1.00 43.37 ? 345 ARG B CD    1 
ATOM   4607 N NE    . ARG B 1 204 ? -18.975 86.971 -26.175 1.00 45.79 ? 345 ARG B NE    1 
ATOM   4608 C CZ    . ARG B 1 204 ? -19.248 87.887 -25.255 1.00 50.79 ? 345 ARG B CZ    1 
ATOM   4609 N NH1   . ARG B 1 204 ? -18.487 88.041 -24.179 1.00 45.67 ? 345 ARG B NH1   1 
ATOM   4610 N NH2   . ARG B 1 204 ? -20.310 88.673 -25.419 1.00 54.73 ? 345 ARG B NH2   1 
ATOM   4611 N N     . TYR B 1 205 ? -18.614 81.169 -26.330 1.00 25.75 ? 346 TYR B N     1 
ATOM   4612 C CA    . TYR B 1 205 ? -17.548 80.240 -25.982 1.00 24.67 ? 346 TYR B CA    1 
ATOM   4613 C C     . TYR B 1 205 ? -17.724 78.862 -26.611 1.00 29.21 ? 346 TYR B C     1 
ATOM   4614 O O     . TYR B 1 205 ? -16.927 77.959 -26.326 1.00 29.23 ? 346 TYR B O     1 
ATOM   4615 C CB    . TYR B 1 205 ? -17.428 80.126 -24.459 1.00 26.58 ? 346 TYR B CB    1 
ATOM   4616 C CG    . TYR B 1 205 ? -16.771 81.335 -23.852 1.00 28.80 ? 346 TYR B CG    1 
ATOM   4617 C CD1   . TYR B 1 205 ? -17.513 82.469 -23.550 1.00 27.08 ? 346 TYR B CD1   1 
ATOM   4618 C CD2   . TYR B 1 205 ? -15.393 81.362 -23.616 1.00 30.79 ? 346 TYR B CD2   1 
ATOM   4619 C CE1   . TYR B 1 205 ? -16.914 83.588 -22.998 1.00 29.96 ? 346 TYR B CE1   1 
ATOM   4620 C CE2   . TYR B 1 205 ? -14.783 82.475 -23.072 1.00 28.87 ? 346 TYR B CE2   1 
ATOM   4621 C CZ    . TYR B 1 205 ? -15.551 83.583 -22.763 1.00 33.40 ? 346 TYR B CZ    1 
ATOM   4622 O OH    . TYR B 1 205 ? -14.961 84.693 -22.222 1.00 34.09 ? 346 TYR B OH    1 
ATOM   4623 N N     . GLY B 1 206 ? -18.731 78.684 -27.467 1.00 27.32 ? 347 GLY B N     1 
ATOM   4624 C CA    . GLY B 1 206 ? -18.886 77.460 -28.226 1.00 24.98 ? 347 GLY B CA    1 
ATOM   4625 C C     . GLY B 1 206 ? -19.791 76.406 -27.623 1.00 28.71 ? 347 GLY B C     1 
ATOM   4626 O O     . GLY B 1 206 ? -19.771 75.259 -28.089 1.00 25.65 ? 347 GLY B O     1 
ATOM   4627 N N     . ALA B 1 207 ? -20.582 76.739 -26.610 1.00 22.08 ? 348 ALA B N     1 
ATOM   4628 C CA    . ALA B 1 207 ? -21.430 75.750 -25.958 1.00 23.36 ? 348 ALA B CA    1 
ATOM   4629 C C     . ALA B 1 207 ? -22.881 75.879 -26.409 1.00 18.88 ? 348 ALA B C     1 
ATOM   4630 O O     . ALA B 1 207 ? -23.354 76.970 -26.733 1.00 22.51 ? 348 ALA B O     1 
ATOM   4631 C CB    . ALA B 1 207 ? -21.362 75.898 -24.431 1.00 19.89 ? 348 ALA B CB    1 
ATOM   4632 N N     . ARG B 1 208 ? -23.592 74.753 -26.405 1.00 18.24 ? 349 ARG B N     1 
ATOM   4633 C CA    . ARG B 1 208 ? -25.049 74.819 -26.374 1.00 18.31 ? 349 ARG B CA    1 
ATOM   4634 C C     . ARG B 1 208 ? -25.518 75.275 -24.992 1.00 18.59 ? 349 ARG B C     1 
ATOM   4635 O O     . ARG B 1 208 ? -24.798 75.148 -24.003 1.00 17.51 ? 349 ARG B O     1 
ATOM   4636 C CB    . ARG B 1 208 ? -25.666 73.458 -26.690 1.00 16.49 ? 349 ARG B CB    1 
ATOM   4637 C CG    . ARG B 1 208 ? -25.264 72.881 -28.037 1.00 25.76 ? 349 ARG B CG    1 
ATOM   4638 C CD    . ARG B 1 208 ? -26.217 73.337 -29.082 1.00 25.28 ? 349 ARG B CD    1 
ATOM   4639 N NE    . ARG B 1 208 ? -26.051 72.661 -30.363 1.00 26.41 ? 349 ARG B NE    1 
ATOM   4640 C CZ    . ARG B 1 208 ? -26.593 73.108 -31.487 1.00 27.85 ? 349 ARG B CZ    1 
ATOM   4641 N NH1   . ARG B 1 208 ? -27.368 74.179 -31.493 1.00 23.60 ? 349 ARG B NH1   1 
ATOM   4642 N NH2   . ARG B 1 208 ? -26.337 72.476 -32.633 1.00 26.55 ? 349 ARG B NH2   1 
ATOM   4643 N N     . VAL B 1 209 ? -26.739 75.813 -24.921 1.00 17.62 ? 350 VAL B N     1 
ATOM   4644 C CA    . VAL B 1 209 ? -27.285 76.319 -23.660 1.00 15.57 ? 350 VAL B CA    1 
ATOM   4645 C C     . VAL B 1 209 ? -28.692 75.758 -23.466 1.00 17.11 ? 350 VAL B C     1 
ATOM   4646 O O     . VAL B 1 209 ? -29.561 75.904 -24.342 1.00 16.93 ? 350 VAL B O     1 
ATOM   4647 C CB    . VAL B 1 209 ? -27.291 77.862 -23.599 1.00 19.26 ? 350 VAL B CB    1 
ATOM   4648 C CG1   . VAL B 1 209 ? -27.751 78.352 -22.211 1.00 18.48 ? 350 VAL B CG1   1 
ATOM   4649 C CG2   . VAL B 1 209 ? -25.901 78.429 -23.911 1.00 19.16 ? 350 VAL B CG2   1 
ATOM   4650 N N     . LEU B 1 210 ? -28.896 75.078 -22.337 1.00 15.69 ? 351 LEU B N     1 
ATOM   4651 C CA    . LEU B 1 210 ? -30.196 74.602 -21.884 1.00 18.98 ? 351 LEU B CA    1 
ATOM   4652 C C     . LEU B 1 210 ? -30.647 75.501 -20.744 1.00 17.85 ? 351 LEU B C     1 
ATOM   4653 O O     . LEU B 1 210 ? -29.855 75.813 -19.840 1.00 18.72 ? 351 LEU B O     1 
ATOM   4654 C CB    . LEU B 1 210 ? -30.149 73.135 -21.416 1.00 14.18 ? 351 LEU B CB    1 
ATOM   4655 C CG    . LEU B 1 210 ? -31.368 72.533 -20.707 1.00 16.53 ? 351 LEU B CG    1 
ATOM   4656 C CD1   . LEU B 1 210 ? -31.523 71.046 -21.027 1.00 14.74 ? 351 LEU B CD1   1 
ATOM   4657 C CD2   . LEU B 1 210 ? -31.301 72.725 -19.182 1.00 19.46 ? 351 LEU B CD2   1 
ATOM   4658 N N     . ILE B 1 211 ? -31.911 75.912 -20.799 1.00 17.81 ? 352 ILE B N     1 
ATOM   4659 C CA    . ILE B 1 211 ? -32.529 76.770 -19.797 1.00 18.78 ? 352 ILE B CA    1 
ATOM   4660 C C     . ILE B 1 211 ? -33.630 75.962 -19.113 1.00 18.14 ? 352 ILE B C     1 
ATOM   4661 O O     . ILE B 1 211 ? -34.519 75.412 -19.781 1.00 18.13 ? 352 ILE B O     1 
ATOM   4662 C CB    . ILE B 1 211 ? -33.081 78.066 -20.424 1.00 18.04 ? 352 ILE B CB    1 
ATOM   4663 C CG1   . ILE B 1 211 ? -31.948 78.871 -21.084 1.00 21.50 ? 352 ILE B CG1   1 
ATOM   4664 C CG2   . ILE B 1 211 ? -33.791 78.935 -19.376 1.00 16.01 ? 352 ILE B CG2   1 
ATOM   4665 C CD1   . ILE B 1 211 ? -30.822 79.260 -20.109 1.00 18.11 ? 352 ILE B CD1   1 
ATOM   4666 N N     . ASP B 1 212 ? -33.531 75.855 -17.792 1.00 18.60 ? 353 ASP B N     1 
ATOM   4667 C CA    . ASP B 1 212 ? -34.558 75.254 -16.944 1.00 19.77 ? 353 ASP B CA    1 
ATOM   4668 C C     . ASP B 1 212 ? -35.612 76.314 -16.672 1.00 19.38 ? 353 ASP B C     1 
ATOM   4669 O O     . ASP B 1 212 ? -35.413 77.199 -15.839 1.00 17.63 ? 353 ASP B O     1 
ATOM   4670 C CB    . ASP B 1 212 ? -33.949 74.756 -15.641 1.00 22.33 ? 353 ASP B CB    1 
ATOM   4671 C CG    . ASP B 1 212 ? -34.948 74.029 -14.749 1.00 23.89 ? 353 ASP B CG    1 
ATOM   4672 O OD1   . ASP B 1 212 ? -36.183 74.116 -14.986 1.00 23.17 ? 353 ASP B OD1   1 
ATOM   4673 O OD2   . ASP B 1 212 ? -34.483 73.375 -13.782 1.00 22.80 ? 353 ASP B OD2   1 
ATOM   4674 N N     . GLY B 1 213 ? -36.741 76.220 -17.366 1.00 20.52 ? 354 GLY B N     1 
ATOM   4675 C CA    . GLY B 1 213 ? -37.825 77.170 -17.239 1.00 19.07 ? 354 GLY B CA    1 
ATOM   4676 C C     . GLY B 1 213 ? -39.003 76.734 -16.392 1.00 17.88 ? 354 GLY B C     1 
ATOM   4677 O O     . GLY B 1 213 ? -40.062 77.363 -16.479 1.00 18.90 ? 354 GLY B O     1 
ATOM   4678 N N     . ALA B 1 214 ? -38.867 75.683 -15.576 1.00 17.16 ? 355 ALA B N     1 
ATOM   4679 C CA    . ALA B 1 214 ? -40.017 75.181 -14.818 1.00 20.96 ? 355 ALA B CA    1 
ATOM   4680 C C     . ALA B 1 214 ? -40.641 76.257 -13.928 1.00 21.84 ? 355 ALA B C     1 
ATOM   4681 O O     . ALA B 1 214 ? -41.852 76.227 -13.665 1.00 19.19 ? 355 ALA B O     1 
ATOM   4682 C CB    . ALA B 1 214 ? -39.611 73.970 -13.965 1.00 19.10 ? 355 ALA B CB    1 
ATOM   4683 N N     . GLN B 1 215 ? -39.845 77.207 -13.452 1.00 20.58 ? 356 GLN B N     1 
ATOM   4684 C CA    . GLN B 1 215 ? -40.343 78.269 -12.587 1.00 23.65 ? 356 GLN B CA    1 
ATOM   4685 C C     . GLN B 1 215 ? -40.377 79.630 -13.275 1.00 22.99 ? 356 GLN B C     1 
ATOM   4686 O O     . GLN B 1 215 ? -40.848 80.599 -12.674 1.00 25.81 ? 356 GLN B O     1 
ATOM   4687 C CB    . GLN B 1 215 ? -39.486 78.347 -11.320 1.00 21.10 ? 356 GLN B CB    1 
ATOM   4688 C CG    . GLN B 1 215 ? -40.227 78.727 -10.066 1.00 35.18 ? 356 GLN B CG    1 
ATOM   4689 C CD    . GLN B 1 215 ? -41.221 77.681 -9.659  1.00 33.87 ? 356 GLN B CD    1 
ATOM   4690 O OE1   . GLN B 1 215 ? -42.409 77.969 -9.508  1.00 36.81 ? 356 GLN B OE1   1 
ATOM   4691 N NE2   . GLN B 1 215 ? -40.755 76.439 -9.542  1.00 32.11 ? 356 GLN B NE2   1 
ATOM   4692 N N     . SER B 1 216 ? -39.879 79.738 -14.509 1.00 21.96 ? 357 SER B N     1 
ATOM   4693 C CA    . SER B 1 216 ? -39.985 81.005 -15.222 1.00 19.47 ? 357 SER B CA    1 
ATOM   4694 C C     . SER B 1 216 ? -41.237 81.068 -16.082 1.00 22.73 ? 357 SER B C     1 
ATOM   4695 O O     . SER B 1 216 ? -41.925 82.095 -16.092 1.00 26.79 ? 357 SER B O     1 
ATOM   4696 C CB    . SER B 1 216 ? -38.731 81.259 -16.070 1.00 22.65 ? 357 SER B CB    1 
ATOM   4697 O OG    . SER B 1 216 ? -38.539 80.289 -17.107 1.00 17.53 ? 357 SER B OG    1 
ATOM   4698 N N     . ILE B 1 217 ? -41.589 79.982 -16.762 1.00 21.42 ? 358 ILE B N     1 
ATOM   4699 C CA    . ILE B 1 217 ? -42.742 79.998 -17.667 1.00 21.93 ? 358 ILE B CA    1 
ATOM   4700 C C     . ILE B 1 217 ? -44.081 80.368 -17.010 1.00 22.84 ? 358 ILE B C     1 
ATOM   4701 O O     . ILE B 1 217 ? -44.893 81.026 -17.677 1.00 22.43 ? 358 ILE B O     1 
ATOM   4702 C CB    . ILE B 1 217 ? -42.842 78.671 -18.444 1.00 21.97 ? 358 ILE B CB    1 
ATOM   4703 C CG1   . ILE B 1 217 ? -43.585 78.915 -19.762 1.00 23.74 ? 358 ILE B CG1   1 
ATOM   4704 C CG2   . ILE B 1 217 ? -43.464 77.541 -17.623 1.00 22.00 ? 358 ILE B CG2   1 
ATOM   4705 C CD1   . ILE B 1 217 ? -43.912 77.680 -20.545 1.00 25.81 ? 358 ILE B CD1   1 
ATOM   4706 N N     . PRO B 1 218 ? -44.384 80.055 -15.740 1.00 24.12 ? 359 PRO B N     1 
ATOM   4707 C CA    . PRO B 1 218 ? -45.654 80.564 -15.184 1.00 25.19 ? 359 PRO B CA    1 
ATOM   4708 C C     . PRO B 1 218 ? -45.610 82.022 -14.741 1.00 25.99 ? 359 PRO B C     1 
ATOM   4709 O O     . PRO B 1 218 ? -46.664 82.580 -14.390 1.00 25.33 ? 359 PRO B O     1 
ATOM   4710 C CB    . PRO B 1 218 ? -45.922 79.641 -13.978 1.00 22.87 ? 359 PRO B CB    1 
ATOM   4711 C CG    . PRO B 1 218 ? -44.741 78.700 -13.864 1.00 25.51 ? 359 PRO B CG    1 
ATOM   4712 C CD    . PRO B 1 218 ? -43.642 79.287 -14.719 1.00 24.87 ? 359 PRO B CD    1 
ATOM   4713 N N     . HIS B 1 219 ? -44.437 82.660 -14.752 1.00 24.70 ? 360 HIS B N     1 
ATOM   4714 C CA    . HIS B 1 219 ? -44.246 83.936 -14.074 1.00 26.46 ? 360 HIS B CA    1 
ATOM   4715 C C     . HIS B 1 219 ? -43.717 85.065 -14.945 1.00 28.55 ? 360 HIS B C     1 
ATOM   4716 O O     . HIS B 1 219 ? -43.622 86.193 -14.451 1.00 29.67 ? 360 HIS B O     1 
ATOM   4717 C CB    . HIS B 1 219 ? -43.291 83.750 -12.885 1.00 24.96 ? 360 HIS B CB    1 
ATOM   4718 C CG    . HIS B 1 219 ? -43.811 82.803 -11.858 1.00 28.36 ? 360 HIS B CG    1 
ATOM   4719 N ND1   . HIS B 1 219 ? -45.059 82.941 -11.289 1.00 30.50 ? 360 HIS B ND1   1 
ATOM   4720 C CD2   . HIS B 1 219 ? -43.286 81.665 -11.347 1.00 26.53 ? 360 HIS B CD2   1 
ATOM   4721 C CE1   . HIS B 1 219 ? -45.262 81.953 -10.433 1.00 30.11 ? 360 HIS B CE1   1 
ATOM   4722 N NE2   . HIS B 1 219 ? -44.204 81.161 -10.455 1.00 30.72 ? 360 HIS B NE2   1 
ATOM   4723 N N     . MET B 1 220 ? -43.374 84.813 -16.205 1.00 26.13 ? 361 MET B N     1 
ATOM   4724 C CA    . MET B 1 220 ? -42.822 85.853 -17.064 1.00 25.69 ? 361 MET B CA    1 
ATOM   4725 C C     . MET B 1 220 ? -42.936 85.392 -18.509 1.00 27.82 ? 361 MET B C     1 
ATOM   4726 O O     . MET B 1 220 ? -43.007 84.184 -18.772 1.00 27.74 ? 361 MET B O     1 
ATOM   4727 C CB    . MET B 1 220 ? -41.360 86.143 -16.707 1.00 25.80 ? 361 MET B CB    1 
ATOM   4728 C CG    . MET B 1 220 ? -40.510 84.887 -16.657 1.00 32.56 ? 361 MET B CG    1 
ATOM   4729 S SD    . MET B 1 220 ? -38.831 85.215 -16.104 1.00 35.83 ? 361 MET B SD    1 
ATOM   4730 C CE    . MET B 1 220 ? -39.139 85.327 -14.342 1.00 31.54 ? 361 MET B CE    1 
ATOM   4731 N N     . PRO B 1 221 ? -42.975 86.325 -19.468 1.00 27.84 ? 362 PRO B N     1 
ATOM   4732 C CA    . PRO B 1 221 ? -43.089 85.917 -20.872 1.00 23.59 ? 362 PRO B CA    1 
ATOM   4733 C C     . PRO B 1 221 ? -41.826 85.212 -21.335 1.00 26.95 ? 362 PRO B C     1 
ATOM   4734 O O     . PRO B 1 221 ? -40.709 85.594 -20.980 1.00 26.98 ? 362 PRO B O     1 
ATOM   4735 C CB    . PRO B 1 221 ? -43.306 87.242 -21.625 1.00 26.02 ? 362 PRO B CB    1 
ATOM   4736 C CG    . PRO B 1 221 ? -42.793 88.291 -20.733 1.00 29.82 ? 362 PRO B CG    1 
ATOM   4737 C CD    . PRO B 1 221 ? -43.004 87.793 -19.316 1.00 29.02 ? 362 PRO B CD    1 
ATOM   4738 N N     . ILE B 1 222 ? -42.017 84.160 -22.123 1.00 25.96 ? 363 ILE B N     1 
ATOM   4739 C CA    . ILE B 1 222 ? -40.933 83.369 -22.692 1.00 25.42 ? 363 ILE B CA    1 
ATOM   4740 C C     . ILE B 1 222 ? -40.979 83.506 -24.211 1.00 25.54 ? 363 ILE B C     1 
ATOM   4741 O O     . ILE B 1 222 ? -42.031 83.312 -24.828 1.00 22.46 ? 363 ILE B O     1 
ATOM   4742 C CB    . ILE B 1 222 ? -41.040 81.888 -22.283 1.00 22.43 ? 363 ILE B CB    1 
ATOM   4743 C CG1   . ILE B 1 222 ? -41.048 81.741 -20.755 1.00 24.13 ? 363 ILE B CG1   1 
ATOM   4744 C CG2   . ILE B 1 222 ? -39.921 81.071 -22.923 1.00 23.58 ? 363 ILE B CG2   1 
ATOM   4745 C CD1   . ILE B 1 222 ? -39.737 82.120 -20.094 1.00 21.49 ? 363 ILE B CD1   1 
ATOM   4746 N N     . ASP B 1 223 ? -39.832 83.801 -24.812 1.00 27.18 ? 364 ASP B N     1 
ATOM   4747 C CA    . ASP B 1 223 ? -39.690 83.867 -26.262 1.00 23.99 ? 364 ASP B CA    1 
ATOM   4748 C C     . ASP B 1 223 ? -38.394 83.142 -26.603 1.00 24.72 ? 364 ASP B C     1 
ATOM   4749 O O     . ASP B 1 223 ? -37.325 83.761 -26.630 1.00 22.32 ? 364 ASP B O     1 
ATOM   4750 C CB    . ASP B 1 223 ? -39.686 85.309 -26.758 1.00 21.53 ? 364 ASP B CB    1 
ATOM   4751 C CG    . ASP B 1 223 ? -39.857 85.390 -28.271 1.00 27.43 ? 364 ASP B CG    1 
ATOM   4752 O OD1   . ASP B 1 223 ? -39.408 84.452 -28.966 1.00 26.42 ? 364 ASP B OD1   1 
ATOM   4753 O OD2   . ASP B 1 223 ? -40.410 86.393 -28.761 1.00 36.25 ? 364 ASP B OD2   1 
ATOM   4754 N N     . VAL B 1 224 ? -38.496 81.836 -26.872 1.00 18.93 ? 365 VAL B N     1 
ATOM   4755 C CA    . VAL B 1 224 ? -37.287 81.036 -26.997 1.00 21.80 ? 365 VAL B CA    1 
ATOM   4756 C C     . VAL B 1 224 ? -36.565 81.331 -28.298 1.00 25.43 ? 365 VAL B C     1 
ATOM   4757 O O     . VAL B 1 224 ? -35.335 81.216 -28.362 1.00 23.89 ? 365 VAL B O     1 
ATOM   4758 C CB    . VAL B 1 224 ? -37.597 79.530 -26.861 1.00 23.72 ? 365 VAL B CB    1 
ATOM   4759 C CG1   . VAL B 1 224 ? -38.204 79.225 -25.488 1.00 21.07 ? 365 VAL B CG1   1 
ATOM   4760 C CG2   . VAL B 1 224 ? -38.505 79.059 -27.984 1.00 21.73 ? 365 VAL B CG2   1 
ATOM   4761 N N     . ALA B 1 225 ? -37.293 81.715 -29.355 1.00 25.34 ? 366 ALA B N     1 
ATOM   4762 C CA    . ALA B 1 225 ? -36.608 82.057 -30.599 1.00 28.12 ? 366 ALA B CA    1 
ATOM   4763 C C     . ALA B 1 225 ? -35.782 83.322 -30.427 1.00 28.42 ? 366 ALA B C     1 
ATOM   4764 O O     . ALA B 1 225 ? -34.662 83.415 -30.941 1.00 31.86 ? 366 ALA B O     1 
ATOM   4765 C CB    . ALA B 1 225 ? -37.609 82.219 -31.747 1.00 26.16 ? 366 ALA B CB    1 
ATOM   4766 N N     . ALA B 1 226 ? -36.304 84.295 -29.681 1.00 26.50 ? 367 ALA B N     1 
ATOM   4767 C CA    . ALA B 1 226 ? -35.551 85.511 -29.412 1.00 29.23 ? 367 ALA B CA    1 
ATOM   4768 C C     . ALA B 1 226 ? -34.482 85.295 -28.347 1.00 30.55 ? 367 ALA B C     1 
ATOM   4769 O O     . ALA B 1 226 ? -33.420 85.928 -28.398 1.00 31.99 ? 367 ALA B O     1 
ATOM   4770 C CB    . ALA B 1 226 ? -36.504 86.630 -28.988 1.00 30.07 ? 367 ALA B CB    1 
ATOM   4771 N N     . LEU B 1 227 ? -34.739 84.416 -27.382 1.00 25.64 ? 368 LEU B N     1 
ATOM   4772 C CA    . LEU B 1 227 ? -33.720 84.080 -26.395 1.00 25.20 ? 368 LEU B CA    1 
ATOM   4773 C C     . LEU B 1 227 ? -32.543 83.361 -27.042 1.00 26.85 ? 368 LEU B C     1 
ATOM   4774 O O     . LEU B 1 227 ? -31.386 83.584 -26.669 1.00 31.18 ? 368 LEU B O     1 
ATOM   4775 C CB    . LEU B 1 227 ? -34.343 83.222 -25.301 1.00 25.56 ? 368 LEU B CB    1 
ATOM   4776 C CG    . LEU B 1 227 ? -33.449 82.731 -24.168 1.00 31.83 ? 368 LEU B CG    1 
ATOM   4777 C CD1   . LEU B 1 227 ? -32.575 83.861 -23.641 1.00 31.58 ? 368 LEU B CD1   1 
ATOM   4778 C CD2   . LEU B 1 227 ? -34.325 82.117 -23.063 1.00 28.48 ? 368 LEU B CD2   1 
ATOM   4779 N N     . GLY B 1 228 ? -32.812 82.511 -28.021 1.00 22.67 ? 369 GLY B N     1 
ATOM   4780 C CA    . GLY B 1 228 ? -31.762 81.771 -28.681 1.00 24.09 ? 369 GLY B CA    1 
ATOM   4781 C C     . GLY B 1 228 ? -31.288 80.536 -27.948 1.00 22.44 ? 369 GLY B C     1 
ATOM   4782 O O     . GLY B 1 228 ? -30.313 79.920 -28.386 1.00 21.55 ? 369 GLY B O     1 
ATOM   4783 N N     . ALA B 1 229 ? -31.932 80.160 -26.843 1.00 20.59 ? 370 ALA B N     1 
ATOM   4784 C CA    . ALA B 1 229 ? -31.513 78.972 -26.106 1.00 20.50 ? 370 ALA B CA    1 
ATOM   4785 C C     . ALA B 1 229 ? -31.613 77.739 -26.989 1.00 18.70 ? 370 ALA B C     1 
ATOM   4786 O O     . ALA B 1 229 ? -32.536 77.609 -27.797 1.00 19.45 ? 370 ALA B O     1 
ATOM   4787 C CB    . ALA B 1 229 ? -32.371 78.777 -24.850 1.00 19.42 ? 370 ALA B CB    1 
ATOM   4788 N N     . ASP B 1 230 ? -30.655 76.822 -26.827 1.00 16.22 ? 371 ASP B N     1 
ATOM   4789 C CA    . ASP B 1 230 ? -30.692 75.586 -27.602 1.00 18.00 ? 371 ASP B CA    1 
ATOM   4790 C C     . ASP B 1 230 ? -31.758 74.640 -27.085 1.00 20.58 ? 371 ASP B C     1 
ATOM   4791 O O     . ASP B 1 230 ? -32.398 73.927 -27.875 1.00 17.95 ? 371 ASP B O     1 
ATOM   4792 C CB    . ASP B 1 230 ? -29.324 74.914 -27.576 1.00 18.13 ? 371 ASP B CB    1 
ATOM   4793 C CG    . ASP B 1 230 ? -28.254 75.818 -28.119 1.00 22.52 ? 371 ASP B CG    1 
ATOM   4794 O OD1   . ASP B 1 230 ? -28.070 75.806 -29.352 1.00 24.23 ? 371 ASP B OD1   1 
ATOM   4795 O OD2   . ASP B 1 230 ? -27.643 76.566 -27.322 1.00 19.55 ? 371 ASP B OD2   1 
ATOM   4796 N N     . PHE B 1 231 ? -31.940 74.600 -25.765 1.00 15.94 ? 372 PHE B N     1 
ATOM   4797 C CA    . PHE B 1 231 ? -32.976 73.787 -25.147 1.00 17.93 ? 372 PHE B CA    1 
ATOM   4798 C C     . PHE B 1 231 ? -33.691 74.608 -24.080 1.00 17.93 ? 372 PHE B C     1 
ATOM   4799 O O     . PHE B 1 231 ? -33.079 75.433 -23.402 1.00 16.37 ? 372 PHE B O     1 
ATOM   4800 C CB    . PHE B 1 231 ? -32.417 72.508 -24.483 1.00 15.47 ? 372 PHE B CB    1 
ATOM   4801 C CG    . PHE B 1 231 ? -31.553 71.671 -25.378 1.00 15.10 ? 372 PHE B CG    1 
ATOM   4802 C CD1   . PHE B 1 231 ? -32.121 70.806 -26.293 1.00 15.44 ? 372 PHE B CD1   1 
ATOM   4803 C CD2   . PHE B 1 231 ? -30.171 71.739 -25.285 1.00 15.68 ? 372 PHE B CD2   1 
ATOM   4804 C CE1   . PHE B 1 231 ? -31.322 70.024 -27.131 1.00 16.33 ? 372 PHE B CE1   1 
ATOM   4805 C CE2   . PHE B 1 231 ? -29.363 70.964 -26.103 1.00 18.70 ? 372 PHE B CE2   1 
ATOM   4806 C CZ    . PHE B 1 231 ? -29.950 70.087 -27.020 1.00 19.66 ? 372 PHE B CZ    1 
ATOM   4807 N N     . PHE B 1 232 ? -34.986 74.345 -23.915 1.00 17.17 ? 373 PHE B N     1 
ATOM   4808 C CA    . PHE B 1 232 ? -35.788 75.012 -22.892 1.00 14.14 ? 373 PHE B CA    1 
ATOM   4809 C C     . PHE B 1 232 ? -36.772 73.995 -22.340 1.00 14.39 ? 373 PHE B C     1 
ATOM   4810 O O     . PHE B 1 232 ? -37.456 73.332 -23.116 1.00 16.92 ? 373 PHE B O     1 
ATOM   4811 C CB    . PHE B 1 232 ? -36.526 76.237 -23.467 1.00 16.20 ? 373 PHE B CB    1 
ATOM   4812 C CG    . PHE B 1 232 ? -37.324 77.017 -22.433 1.00 19.20 ? 373 PHE B CG    1 
ATOM   4813 C CD1   . PHE B 1 232 ? -36.741 78.049 -21.712 1.00 17.82 ? 373 PHE B CD1   1 
ATOM   4814 C CD2   . PHE B 1 232 ? -38.654 76.698 -22.183 1.00 18.40 ? 373 PHE B CD2   1 
ATOM   4815 C CE1   . PHE B 1 232 ? -37.474 78.758 -20.755 1.00 18.91 ? 373 PHE B CE1   1 
ATOM   4816 C CE2   . PHE B 1 232 ? -39.394 77.394 -21.231 1.00 20.84 ? 373 PHE B CE2   1 
ATOM   4817 C CZ    . PHE B 1 232 ? -38.801 78.431 -20.518 1.00 17.74 ? 373 PHE B CZ    1 
ATOM   4818 N N     . VAL B 1 233 ? -36.853 73.844 -21.019 1.00 14.63 ? 374 VAL B N     1 
ATOM   4819 C CA    . VAL B 1 233 ? -37.655 72.750 -20.470 1.00 14.91 ? 374 VAL B CA    1 
ATOM   4820 C C     . VAL B 1 233 ? -38.671 73.289 -19.465 1.00 15.30 ? 374 VAL B C     1 
ATOM   4821 O O     . VAL B 1 233 ? -38.375 74.237 -18.729 1.00 15.74 ? 374 VAL B O     1 
ATOM   4822 C CB    . VAL B 1 233 ? -36.763 71.659 -19.836 1.00 13.55 ? 374 VAL B CB    1 
ATOM   4823 C CG1   . VAL B 1 233 ? -35.888 70.990 -20.914 1.00 11.91 ? 374 VAL B CG1   1 
ATOM   4824 C CG2   . VAL B 1 233 ? -35.857 72.238 -18.726 1.00 13.92 ? 374 VAL B CG2   1 
ATOM   4825 N N     . PHE B 1 234 ? -39.872 72.692 -19.436 1.00 15.01 ? 375 PHE B N     1 
ATOM   4826 C CA    . PHE B 1 234 ? -40.822 73.056 -18.376 1.00 15.81 ? 375 PHE B CA    1 
ATOM   4827 C C     . PHE B 1 234 ? -41.835 71.941 -18.133 1.00 18.11 ? 375 PHE B C     1 
ATOM   4828 O O     . PHE B 1 234 ? -41.930 70.988 -18.907 1.00 17.95 ? 375 PHE B O     1 
ATOM   4829 C CB    . PHE B 1 234 ? -41.523 74.391 -18.674 1.00 15.95 ? 375 PHE B CB    1 
ATOM   4830 C CG    . PHE B 1 234 ? -42.557 74.331 -19.782 1.00 15.93 ? 375 PHE B CG    1 
ATOM   4831 C CD1   . PHE B 1 234 ? -42.190 74.573 -21.096 1.00 17.12 ? 375 PHE B CD1   1 
ATOM   4832 C CD2   . PHE B 1 234 ? -43.903 74.110 -19.492 1.00 17.74 ? 375 PHE B CD2   1 
ATOM   4833 C CE1   . PHE B 1 234 ? -43.156 74.557 -22.128 1.00 19.47 ? 375 PHE B CE1   1 
ATOM   4834 C CE2   . PHE B 1 234 ? -44.870 74.090 -20.505 1.00 16.17 ? 375 PHE B CE2   1 
ATOM   4835 C CZ    . PHE B 1 234 ? -44.497 74.320 -21.820 1.00 16.11 ? 375 PHE B CZ    1 
ATOM   4836 N N     . SER B 1 235 ? -42.589 72.081 -17.022 1.00 14.88 ? 376 SER B N     1 
ATOM   4837 C CA    . SER B 1 235 ? -43.548 71.093 -16.522 1.00 16.02 ? 376 SER B CA    1 
ATOM   4838 C C     . SER B 1 235 ? -44.952 71.675 -16.540 1.00 15.94 ? 376 SER B C     1 
ATOM   4839 O O     . SER B 1 235 ? -45.171 72.779 -16.026 1.00 16.13 ? 376 SER B O     1 
ATOM   4840 C CB    . SER B 1 235 ? -43.252 70.666 -15.066 1.00 18.28 ? 376 SER B CB    1 
ATOM   4841 O OG    . SER B 1 235 ? -42.100 69.855 -14.941 1.00 17.65 ? 376 SER B OG    1 
ATOM   4842 N N     . GLY B 1 236 ? -45.913 70.899 -17.061 1.00 15.87 ? 377 GLY B N     1 
ATOM   4843 C CA    . GLY B 1 236 ? -47.276 71.401 -17.193 1.00 15.01 ? 377 GLY B CA    1 
ATOM   4844 C C     . GLY B 1 236 ? -47.952 71.698 -15.861 1.00 15.47 ? 377 GLY B C     1 
ATOM   4845 O O     . GLY B 1 236 ? -48.743 72.639 -15.746 1.00 16.80 ? 377 GLY B O     1 
ATOM   4846 N N     . HIS B 1 237 ? -47.671 70.899 -14.845 1.00 14.38 ? 378 HIS B N     1 
ATOM   4847 C CA    . HIS B 1 237 ? -48.438 71.004 -13.605 1.00 16.52 ? 378 HIS B CA    1 
ATOM   4848 C C     . HIS B 1 237 ? -48.054 72.257 -12.796 1.00 20.26 ? 378 HIS B C     1 
ATOM   4849 O O     . HIS B 1 237 ? -48.777 72.656 -11.875 1.00 20.68 ? 378 HIS B O     1 
ATOM   4850 C CB    . HIS B 1 237 ? -48.264 69.734 -12.776 1.00 18.25 ? 378 HIS B CB    1 
ATOM   4851 C CG    . HIS B 1 237 ? -46.887 69.556 -12.233 1.00 18.29 ? 378 HIS B CG    1 
ATOM   4852 N ND1   . HIS B 1 237 ? -46.503 70.050 -11.003 1.00 17.71 ? 378 HIS B ND1   1 
ATOM   4853 C CD2   . HIS B 1 237 ? -45.794 68.944 -12.755 1.00 17.97 ? 378 HIS B CD2   1 
ATOM   4854 C CE1   . HIS B 1 237 ? -45.234 69.747 -10.788 1.00 17.67 ? 378 HIS B CE1   1 
ATOM   4855 N NE2   . HIS B 1 237 ? -44.777 69.086 -11.840 1.00 19.26 ? 378 HIS B NE2   1 
HETATM 4856 N N1    . LLP B 1 238 ? -36.533 72.642 -12.129 1.00 22.38 ? 379 LLP B N1    1 
HETATM 4857 C C2    . LLP B 1 238 ? -37.138 73.585 -11.408 1.00 24.63 ? 379 LLP B C2    1 
HETATM 4858 C "C2'" . LLP B 1 238 ? -36.541 75.019 -11.308 1.00 22.37 ? 379 LLP B "C2'" 1 
HETATM 4859 C C3    . LLP B 1 238 ? -38.342 73.265 -10.725 1.00 23.55 ? 379 LLP B C3    1 
HETATM 4860 O O3    . LLP B 1 238 ? -38.975 74.259 -9.978  1.00 27.76 ? 379 LLP B O3    1 
HETATM 4861 C C4    . LLP B 1 238 ? -38.882 71.997 -10.811 1.00 24.55 ? 379 LLP B C4    1 
HETATM 4862 C "C4'" . LLP B 1 238 ? -40.247 71.708 -10.013 1.00 28.77 ? 379 LLP B "C4'" 1 
HETATM 4863 C C5    . LLP B 1 238 ? -38.269 71.026 -11.561 1.00 24.67 ? 379 LLP B C5    1 
HETATM 4864 C C6    . LLP B 1 238 ? -37.075 71.351 -12.221 1.00 22.38 ? 379 LLP B C6    1 
HETATM 4865 C "C5'" . LLP B 1 238 ? -38.812 69.557 -11.684 1.00 19.81 ? 379 LLP B "C5'" 1 
HETATM 4866 O OP4   . LLP B 1 238 ? -40.036 69.446 -12.409 1.00 26.24 ? 379 LLP B OP4   1 
HETATM 4867 P P     . LLP B 1 238 ? -40.838 68.091 -12.376 1.00 22.87 ? 379 LLP B P     1 
HETATM 4868 O OP1   . LLP B 1 238 ? -42.255 68.392 -12.861 1.00 22.39 ? 379 LLP B OP1   1 
HETATM 4869 O OP2   . LLP B 1 238 ? -40.817 67.544 -10.990 1.00 24.80 ? 379 LLP B OP2   1 
HETATM 4870 O OP3   . LLP B 1 238 ? -40.235 67.093 -13.308 1.00 19.60 ? 379 LLP B OP3   1 
HETATM 4871 N N     . LLP B 1 238 ? -46.936 72.889 -13.153 1.00 17.82 ? 379 LLP B N     1 
HETATM 4872 C CA    . LLP B 1 238 ? -46.546 74.170 -12.524 1.00 18.34 ? 379 LLP B CA    1 
HETATM 4873 C CB    . LLP B 1 238 ? -45.049 74.312 -12.441 1.00 21.42 ? 379 LLP B CB    1 
HETATM 4874 C CG    . LLP B 1 238 ? -44.441 73.301 -11.457 1.00 23.71 ? 379 LLP B CG    1 
HETATM 4875 C CD    . LLP B 1 238 ? -43.014 73.751 -11.120 1.00 26.88 ? 379 LLP B CD    1 
HETATM 4876 C CE    . LLP B 1 238 ? -42.350 72.795 -10.109 1.00 26.62 ? 379 LLP B CE    1 
HETATM 4877 N NZ    . LLP B 1 238 ? -41.331 72.067 -10.863 1.00 33.06 ? 379 LLP B NZ    1 
HETATM 4878 C C     . LLP B 1 238 ? -47.082 75.327 -13.302 1.00 22.07 ? 379 LLP B C     1 
HETATM 4879 O O     . LLP B 1 238 ? -46.872 76.463 -12.905 1.00 21.91 ? 379 LLP B O     1 
ATOM   4880 N N     . ILE B 1 239 ? -47.752 75.076 -14.427 1.00 19.11 ? 380 ILE B N     1 
ATOM   4881 C CA    . ILE B 1 239 ? -48.433 76.176 -15.111 1.00 20.62 ? 380 ILE B CA    1 
ATOM   4882 C C     . ILE B 1 239 ? -49.932 75.841 -15.294 1.00 19.31 ? 380 ILE B C     1 
ATOM   4883 O O     . ILE B 1 239 ? -50.488 75.922 -16.395 1.00 16.73 ? 380 ILE B O     1 
ATOM   4884 C CB    . ILE B 1 239 ? -47.696 76.544 -16.433 1.00 19.50 ? 380 ILE B CB    1 
ATOM   4885 C CG1   . ILE B 1 239 ? -48.209 77.884 -16.985 1.00 20.25 ? 380 ILE B CG1   1 
ATOM   4886 C CG2   . ILE B 1 239 ? -47.712 75.395 -17.469 1.00 15.07 ? 380 ILE B CG2   1 
ATOM   4887 C CD1   . ILE B 1 239 ? -47.233 78.559 -17.929 1.00 23.56 ? 380 ILE B CD1   1 
ATOM   4888 N N     . TYR B 1 240 ? -50.580 75.484 -14.174 1.00 18.85 ? 381 TYR B N     1 
ATOM   4889 C CA    . TYR B 1 240 ? -52.037 75.314 -14.076 1.00 17.84 ? 381 TYR B CA    1 
ATOM   4890 C C     . TYR B 1 240 ? -52.564 74.173 -14.948 1.00 18.73 ? 381 TYR B C     1 
ATOM   4891 O O     . TYR B 1 240 ? -53.765 74.112 -15.234 1.00 20.08 ? 381 TYR B O     1 
ATOM   4892 C CB    . TYR B 1 240 ? -52.749 76.648 -14.381 1.00 20.15 ? 381 TYR B CB    1 
ATOM   4893 C CG    . TYR B 1 240 ? -52.018 77.754 -13.651 1.00 24.79 ? 381 TYR B CG    1 
ATOM   4894 C CD1   . TYR B 1 240 ? -52.163 77.906 -12.273 1.00 22.63 ? 381 TYR B CD1   1 
ATOM   4895 C CD2   . TYR B 1 240 ? -51.093 78.570 -14.312 1.00 19.89 ? 381 TYR B CD2   1 
ATOM   4896 C CE1   . TYR B 1 240 ? -51.449 78.853 -11.585 1.00 26.29 ? 381 TYR B CE1   1 
ATOM   4897 C CE2   . TYR B 1 240 ? -50.359 79.510 -13.628 1.00 20.82 ? 381 TYR B CE2   1 
ATOM   4898 C CZ    . TYR B 1 240 ? -50.545 79.650 -12.261 1.00 26.89 ? 381 TYR B CZ    1 
ATOM   4899 O OH    . TYR B 1 240 ? -49.829 80.595 -11.564 1.00 32.61 ? 381 TYR B OH    1 
ATOM   4900 N N     . GLY B 1 241 ? -51.694 73.245 -15.356 1.00 17.67 ? 382 GLY B N     1 
ATOM   4901 C CA    . GLY B 1 241 ? -52.077 72.145 -16.214 1.00 15.98 ? 382 GLY B CA    1 
ATOM   4902 C C     . GLY B 1 241 ? -52.059 70.800 -15.510 1.00 16.67 ? 382 GLY B C     1 
ATOM   4903 O O     . GLY B 1 241 ? -51.736 70.695 -14.326 1.00 16.27 ? 382 GLY B O     1 
ATOM   4904 N N     . PRO B 1 242 ? -52.414 69.740 -16.233 1.00 17.91 ? 383 PRO B N     1 
ATOM   4905 C CA    . PRO B 1 242 ? -52.435 68.391 -15.635 1.00 20.19 ? 383 PRO B CA    1 
ATOM   4906 C C     . PRO B 1 242 ? -51.057 67.919 -15.200 1.00 17.87 ? 383 PRO B C     1 
ATOM   4907 O O     . PRO B 1 242 ? -50.025 68.369 -15.710 1.00 16.41 ? 383 PRO B O     1 
ATOM   4908 C CB    . PRO B 1 242 ? -52.964 67.496 -16.773 1.00 19.35 ? 383 PRO B CB    1 
ATOM   4909 C CG    . PRO B 1 242 ? -53.564 68.441 -17.778 1.00 20.96 ? 383 PRO B CG    1 
ATOM   4910 C CD    . PRO B 1 242 ? -52.800 69.728 -17.652 1.00 17.84 ? 383 PRO B CD    1 
ATOM   4911 N N     . THR B 1 243 ? -51.048 66.959 -14.271 1.00 15.35 ? 384 THR B N     1 
ATOM   4912 C CA    . THR B 1 243 ? -49.811 66.247 -14.009 1.00 17.41 ? 384 THR B CA    1 
ATOM   4913 C C     . THR B 1 243 ? -49.469 65.357 -15.208 1.00 16.81 ? 384 THR B C     1 
ATOM   4914 O O     . THR B 1 243 ? -50.277 65.147 -16.121 1.00 16.97 ? 384 THR B O     1 
ATOM   4915 C CB    . THR B 1 243 ? -49.904 65.390 -12.738 1.00 19.66 ? 384 THR B CB    1 
ATOM   4916 O OG1   . THR B 1 243 ? -50.946 64.424 -12.891 1.00 19.48 ? 384 THR B OG1   1 
ATOM   4917 C CG2   . THR B 1 243 ? -50.219 66.245 -11.506 1.00 17.94 ? 384 THR B CG2   1 
ATOM   4918 N N     . GLY B 1 244 ? -48.250 64.841 -15.200 1.00 13.44 ? 385 GLY B N     1 
ATOM   4919 C CA    . GLY B 1 244 ? -47.826 63.886 -16.201 1.00 16.97 ? 385 GLY B CA    1 
ATOM   4920 C C     . GLY B 1 244 ? -47.476 64.453 -17.561 1.00 14.56 ? 385 GLY B C     1 
ATOM   4921 O O     . GLY B 1 244 ? -47.290 63.670 -18.498 1.00 15.29 ? 385 GLY B O     1 
ATOM   4922 N N     . ILE B 1 245 ? -47.375 65.776 -17.714 1.00 14.96 ? 386 ILE B N     1 
ATOM   4923 C CA    . ILE B 1 245 ? -47.058 66.367 -19.015 1.00 13.57 ? 386 ILE B CA    1 
ATOM   4924 C C     . ILE B 1 245 ? -46.062 67.502 -18.829 1.00 16.74 ? 386 ILE B C     1 
ATOM   4925 O O     . ILE B 1 245 ? -46.159 68.297 -17.889 1.00 13.44 ? 386 ILE B O     1 
ATOM   4926 C CB    . ILE B 1 245 ? -48.327 66.845 -19.770 1.00 13.27 ? 386 ILE B CB    1 
ATOM   4927 C CG1   . ILE B 1 245 ? -47.986 67.192 -21.226 1.00 13.34 ? 386 ILE B CG1   1 
ATOM   4928 C CG2   . ILE B 1 245 ? -49.036 68.016 -19.046 1.00 12.67 ? 386 ILE B CG2   1 
ATOM   4929 C CD1   . ILE B 1 245 ? -47.765 65.943 -22.095 1.00 15.95 ? 386 ILE B CD1   1 
ATOM   4930 N N     . GLY B 1 246 ? -45.081 67.555 -19.725 1.00 14.50 ? 387 GLY B N     1 
ATOM   4931 C CA    . GLY B 1 246 ? -44.108 68.622 -19.776 1.00 14.15 ? 387 GLY B CA    1 
ATOM   4932 C C     . GLY B 1 246 ? -43.545 68.678 -21.181 1.00 16.67 ? 387 GLY B C     1 
ATOM   4933 O O     . GLY B 1 246 ? -43.904 67.880 -22.056 1.00 14.07 ? 387 GLY B O     1 
ATOM   4934 N N     . VAL B 1 247 ? -42.610 69.612 -21.373 1.00 13.79 ? 388 VAL B N     1 
ATOM   4935 C CA    . VAL B 1 247 ? -42.129 69.961 -22.703 1.00 13.43 ? 388 VAL B CA    1 
ATOM   4936 C C     . VAL B 1 247 ? -40.614 70.118 -22.693 1.00 12.79 ? 388 VAL B C     1 
ATOM   4937 O O     . VAL B 1 247 ? -40.038 70.741 -21.788 1.00 14.92 ? 388 VAL B O     1 
ATOM   4938 C CB    . VAL B 1 247 ? -42.805 71.252 -23.209 1.00 16.46 ? 388 VAL B CB    1 
ATOM   4939 C CG1   . VAL B 1 247 ? -42.092 71.793 -24.427 1.00 16.79 ? 388 VAL B CG1   1 
ATOM   4940 C CG2   . VAL B 1 247 ? -44.265 70.995 -23.516 1.00 13.76 ? 388 VAL B CG2   1 
ATOM   4941 N N     . LEU B 1 248 ? -39.981 69.559 -23.719 1.00 13.44 ? 389 LEU B N     1 
ATOM   4942 C CA    . LEU B 1 248 ? -38.630 69.922 -24.120 1.00 13.47 ? 389 LEU B CA    1 
ATOM   4943 C C     . LEU B 1 248 ? -38.731 70.679 -25.436 1.00 15.99 ? 389 LEU B C     1 
ATOM   4944 O O     . LEU B 1 248 ? -39.190 70.124 -26.441 1.00 14.56 ? 389 LEU B O     1 
ATOM   4945 C CB    . LEU B 1 248 ? -37.736 68.694 -24.280 1.00 13.23 ? 389 LEU B CB    1 
ATOM   4946 C CG    . LEU B 1 248 ? -36.386 68.903 -25.007 1.00 16.16 ? 389 LEU B CG    1 
ATOM   4947 C CD1   . LEU B 1 248 ? -35.442 69.822 -24.230 1.00 12.63 ? 389 LEU B CD1   1 
ATOM   4948 C CD2   . LEU B 1 248 ? -35.705 67.565 -25.319 1.00 15.45 ? 389 LEU B CD2   1 
ATOM   4949 N N     . TYR B 1 249 ? -38.334 71.947 -25.430 1.00 14.48 ? 390 TYR B N     1 
ATOM   4950 C CA    . TYR B 1 249 ? -38.087 72.654 -26.671 1.00 16.24 ? 390 TYR B CA    1 
ATOM   4951 C C     . TYR B 1 249 ? -36.616 72.494 -27.017 1.00 17.26 ? 390 TYR B C     1 
ATOM   4952 O O     . TYR B 1 249 ? -35.749 72.585 -26.138 1.00 15.10 ? 390 TYR B O     1 
ATOM   4953 C CB    . TYR B 1 249 ? -38.437 74.136 -26.542 1.00 15.71 ? 390 TYR B CB    1 
ATOM   4954 C CG    . TYR B 1 249 ? -37.731 75.009 -27.573 1.00 17.97 ? 390 TYR B CG    1 
ATOM   4955 C CD1   . TYR B 1 249 ? -38.257 75.175 -28.860 1.00 13.90 ? 390 TYR B CD1   1 
ATOM   4956 C CD2   . TYR B 1 249 ? -36.539 75.660 -27.255 1.00 16.56 ? 390 TYR B CD2   1 
ATOM   4957 C CE1   . TYR B 1 249 ? -37.603 75.965 -29.807 1.00 17.50 ? 390 TYR B CE1   1 
ATOM   4958 C CE2   . TYR B 1 249 ? -35.884 76.453 -28.187 1.00 17.69 ? 390 TYR B CE2   1 
ATOM   4959 C CZ    . TYR B 1 249 ? -36.419 76.602 -29.453 1.00 18.84 ? 390 TYR B CZ    1 
ATOM   4960 O OH    . TYR B 1 249 ? -35.770 77.402 -30.351 1.00 19.53 ? 390 TYR B OH    1 
ATOM   4961 N N     . GLY B 1 250 ? -36.345 72.231 -28.290 1.00 15.68 ? 391 GLY B N     1 
ATOM   4962 C CA    . GLY B 1 250 ? -34.991 72.234 -28.794 1.00 18.03 ? 391 GLY B CA    1 
ATOM   4963 C C     . GLY B 1 250 ? -34.960 72.898 -30.154 1.00 21.36 ? 391 GLY B C     1 
ATOM   4964 O O     . GLY B 1 250 ? -35.826 72.615 -30.992 1.00 18.14 ? 391 GLY B O     1 
ATOM   4965 N N     . ARG B 1 251 ? -34.012 73.814 -30.367 1.00 18.55 ? 392 ARG B N     1 
ATOM   4966 C CA    . ARG B 1 251 ? -33.793 74.353 -31.699 1.00 21.89 ? 392 ARG B CA    1 
ATOM   4967 C C     . ARG B 1 251 ? -33.584 73.212 -32.675 1.00 20.46 ? 392 ARG B C     1 
ATOM   4968 O O     . ARG B 1 251 ? -32.993 72.182 -32.331 1.00 18.75 ? 392 ARG B O     1 
ATOM   4969 C CB    . ARG B 1 251 ? -32.576 75.274 -31.725 1.00 21.86 ? 392 ARG B CB    1 
ATOM   4970 C CG    . ARG B 1 251 ? -32.697 76.495 -30.861 1.00 27.54 ? 392 ARG B CG    1 
ATOM   4971 C CD    . ARG B 1 251 ? -31.401 77.286 -30.902 1.00 29.14 ? 392 ARG B CD    1 
ATOM   4972 N NE    . ARG B 1 251 ? -31.114 77.817 -32.231 1.00 28.27 ? 392 ARG B NE    1 
ATOM   4973 C CZ    . ARG B 1 251 ? -31.525 79.009 -32.651 1.00 37.86 ? 392 ARG B CZ    1 
ATOM   4974 N NH1   . ARG B 1 251 ? -32.258 79.801 -31.878 1.00 32.84 ? 392 ARG B NH1   1 
ATOM   4975 N NH2   . ARG B 1 251 ? -31.208 79.413 -33.880 1.00 33.54 ? 392 ARG B NH2   1 
ATOM   4976 N N     . GLU B 1 252 ? -34.074 73.391 -33.900 1.00 19.53 ? 393 GLU B N     1 
ATOM   4977 C CA    . GLU B 1 252 ? -34.079 72.256 -34.811 1.00 21.56 ? 393 GLU B CA    1 
ATOM   4978 C C     . GLU B 1 252 ? -32.665 71.773 -35.122 1.00 19.23 ? 393 GLU B C     1 
ATOM   4979 O O     . GLU B 1 252 ? -32.471 70.576 -35.309 1.00 19.77 ? 393 GLU B O     1 
ATOM   4980 C CB    . GLU B 1 252 ? -34.860 72.586 -36.093 1.00 26.57 ? 393 GLU B CB    1 
ATOM   4981 C CG    . GLU B 1 252 ? -34.249 73.613 -36.992 1.00 30.83 ? 393 GLU B CG    1 
ATOM   4982 C CD    . GLU B 1 252 ? -35.121 73.903 -38.215 1.00 36.20 ? 393 GLU B CD    1 
ATOM   4983 O OE1   . GLU B 1 252 ? -35.004 75.013 -38.767 1.00 41.37 ? 393 GLU B OE1   1 
ATOM   4984 O OE2   . GLU B 1 252 ? -35.925 73.032 -38.611 1.00 33.39 ? 393 GLU B OE2   1 
ATOM   4985 N N     . ASP B 1 253 ? -31.660 72.659 -35.140 1.00 19.71 ? 394 ASP B N     1 
ATOM   4986 C CA    . ASP B 1 253 ? -30.284 72.194 -35.369 1.00 23.90 ? 394 ASP B CA    1 
ATOM   4987 C C     . ASP B 1 253 ? -29.750 71.387 -34.173 1.00 24.90 ? 394 ASP B C     1 
ATOM   4988 O O     . ASP B 1 253 ? -29.084 70.346 -34.351 1.00 24.99 ? 394 ASP B O     1 
ATOM   4989 C CB    . ASP B 1 253 ? -29.390 73.394 -35.726 1.00 23.52 ? 394 ASP B CB    1 
ATOM   4990 C CG    . ASP B 1 253 ? -29.128 74.331 -34.540 1.00 34.07 ? 394 ASP B CG    1 
ATOM   4991 O OD1   . ASP B 1 253 ? -30.009 75.173 -34.236 1.00 36.05 ? 394 ASP B OD1   1 
ATOM   4992 O OD2   . ASP B 1 253 ? -28.017 74.290 -33.959 1.00 37.17 ? 394 ASP B OD2   1 
ATOM   4993 N N     . ALA B 1 254 ? -30.107 71.799 -32.950 1.00 19.78 ? 395 ALA B N     1 
ATOM   4994 C CA    . ALA B 1 254 ? -29.747 71.017 -31.764 1.00 23.60 ? 395 ALA B CA    1 
ATOM   4995 C C     . ALA B 1 254 ? -30.426 69.653 -31.775 1.00 21.24 ? 395 ALA B C     1 
ATOM   4996 O O     . ALA B 1 254 ? -29.791 68.628 -31.495 1.00 22.08 ? 395 ALA B O     1 
ATOM   4997 C CB    . ALA B 1 254 ? -30.117 71.779 -30.487 1.00 21.19 ? 395 ALA B CB    1 
ATOM   4998 N N     . LEU B 1 255 ? -31.728 69.622 -32.086 1.00 18.61 ? 396 LEU B N     1 
ATOM   4999 C CA    . LEU B 1 255 ? -32.435 68.348 -32.188 1.00 18.82 ? 396 LEU B CA    1 
ATOM   5000 C C     . LEU B 1 255 ? -31.856 67.488 -33.303 1.00 22.33 ? 396 LEU B C     1 
ATOM   5001 O O     . LEU B 1 255 ? -31.782 66.262 -33.178 1.00 21.80 ? 396 LEU B O     1 
ATOM   5002 C CB    . LEU B 1 255 ? -33.932 68.591 -32.421 1.00 18.07 ? 396 LEU B CB    1 
ATOM   5003 C CG    . LEU B 1 255 ? -34.698 69.232 -31.250 1.00 21.39 ? 396 LEU B CG    1 
ATOM   5004 C CD1   . LEU B 1 255 ? -36.219 69.255 -31.482 1.00 22.07 ? 396 LEU B CD1   1 
ATOM   5005 C CD2   . LEU B 1 255 ? -34.373 68.531 -29.928 1.00 18.05 ? 396 LEU B CD2   1 
ATOM   5006 N N     . ALA B 1 256 ? -31.443 68.117 -34.402 1.00 18.24 ? 397 ALA B N     1 
ATOM   5007 C CA    . ALA B 1 256 ? -30.890 67.380 -35.527 1.00 24.22 ? 397 ALA B CA    1 
ATOM   5008 C C     . ALA B 1 256 ? -29.626 66.642 -35.126 1.00 26.50 ? 397 ALA B C     1 
ATOM   5009 O O     . ALA B 1 256 ? -29.333 65.575 -35.678 1.00 26.29 ? 397 ALA B O     1 
ATOM   5010 C CB    . ALA B 1 256 ? -30.597 68.336 -36.693 1.00 20.97 ? 397 ALA B CB    1 
ATOM   5011 N N     . GLU B 1 257 ? -28.866 67.188 -34.177 1.00 23.20 ? 398 GLU B N     1 
ATOM   5012 C CA    . GLU B 1 257 ? -27.672 66.485 -33.707 1.00 24.96 ? 398 GLU B CA    1 
ATOM   5013 C C     . GLU B 1 257 ? -27.917 65.619 -32.463 1.00 24.25 ? 398 GLU B C     1 
ATOM   5014 O O     . GLU B 1 257 ? -26.951 65.136 -31.863 1.00 24.90 ? 398 GLU B O     1 
ATOM   5015 C CB    . GLU B 1 257 ? -26.534 67.492 -33.465 1.00 21.68 ? 398 GLU B CB    1 
ATOM   5016 C CG    . GLU B 1 257 ? -26.643 68.336 -32.208 1.00 27.89 ? 398 GLU B CG    1 
ATOM   5017 C CD    . GLU B 1 257 ? -25.452 69.302 -32.045 1.00 32.93 ? 398 GLU B CD    1 
ATOM   5018 O OE1   . GLU B 1 257 ? -25.134 69.714 -30.888 1.00 26.60 ? 398 GLU B OE1   1 
ATOM   5019 O OE2   . GLU B 1 257 ? -24.838 69.651 -33.086 1.00 30.58 ? 398 GLU B OE2   1 
ATOM   5020 N N     . THR B 1 258 ? -29.177 65.369 -32.096 1.00 17.81 ? 399 THR B N     1 
ATOM   5021 C CA    . THR B 1 258 ? -29.514 64.558 -30.929 1.00 20.69 ? 399 THR B CA    1 
ATOM   5022 C C     . THR B 1 258 ? -30.013 63.195 -31.384 1.00 21.66 ? 399 THR B C     1 
ATOM   5023 O O     . THR B 1 258 ? -31.026 63.129 -32.093 1.00 23.61 ? 399 THR B O     1 
ATOM   5024 C CB    . THR B 1 258 ? -30.579 65.246 -30.074 1.00 19.40 ? 399 THR B CB    1 
ATOM   5025 O OG1   . THR B 1 258 ? -30.099 66.525 -29.645 1.00 21.28 ? 399 THR B OG1   1 
ATOM   5026 C CG2   . THR B 1 258 ? -30.925 64.395 -28.833 1.00 19.88 ? 399 THR B CG2   1 
ATOM   5027 N N     . PRO B 1 259 ? -29.372 62.094 -31.011 1.00 22.25 ? 400 PRO B N     1 
ATOM   5028 C CA    . PRO B 1 259 ? -29.884 60.774 -31.403 1.00 20.15 ? 400 PRO B CA    1 
ATOM   5029 C C     . PRO B 1 259 ? -31.167 60.468 -30.651 1.00 20.12 ? 400 PRO B C     1 
ATOM   5030 O O     . PRO B 1 259 ? -31.548 61.207 -29.736 1.00 19.63 ? 400 PRO B O     1 
ATOM   5031 C CB    . PRO B 1 259 ? -28.742 59.813 -31.010 1.00 20.88 ? 400 PRO B CB    1 
ATOM   5032 C CG    . PRO B 1 259 ? -28.016 60.524 -29.902 1.00 26.68 ? 400 PRO B CG    1 
ATOM   5033 C CD    . PRO B 1 259 ? -28.178 62.009 -30.143 1.00 22.43 ? 400 PRO B CD    1 
ATOM   5034 N N     . PRO B 1 260 ? -31.905 59.431 -31.035 1.00 25.09 ? 401 PRO B N     1 
ATOM   5035 C CA    . PRO B 1 260 ? -33.101 59.073 -30.262 1.00 21.14 ? 401 PRO B CA    1 
ATOM   5036 C C     . PRO B 1 260 ? -32.712 58.589 -28.874 1.00 19.65 ? 401 PRO B C     1 
ATOM   5037 O O     . PRO B 1 260 ? -31.598 58.124 -28.628 1.00 19.39 ? 401 PRO B O     1 
ATOM   5038 C CB    . PRO B 1 260 ? -33.752 57.957 -31.081 1.00 21.64 ? 401 PRO B CB    1 
ATOM   5039 C CG    . PRO B 1 260 ? -33.117 58.068 -32.479 1.00 28.85 ? 401 PRO B CG    1 
ATOM   5040 C CD    . PRO B 1 260 ? -31.722 58.568 -32.219 1.00 26.26 ? 401 PRO B CD    1 
ATOM   5041 N N     . TRP B 1 261 ? -33.641 58.737 -27.945 1.00 16.25 ? 402 TRP B N     1 
ATOM   5042 C CA    . TRP B 1 261 ? -33.384 58.276 -26.590 1.00 15.56 ? 402 TRP B CA    1 
ATOM   5043 C C     . TRP B 1 261 ? -34.120 56.961 -26.373 1.00 19.61 ? 402 TRP B C     1 
ATOM   5044 O O     . TRP B 1 261 ? -33.514 55.890 -26.465 1.00 18.37 ? 402 TRP B O     1 
ATOM   5045 C CB    . TRP B 1 261 ? -33.816 59.350 -25.575 1.00 17.54 ? 402 TRP B CB    1 
ATOM   5046 C CG    . TRP B 1 261 ? -33.551 58.989 -24.132 1.00 18.83 ? 402 TRP B CG    1 
ATOM   5047 C CD1   . TRP B 1 261 ? -32.544 58.195 -23.654 1.00 18.12 ? 402 TRP B CD1   1 
ATOM   5048 C CD2   . TRP B 1 261 ? -34.297 59.430 -22.992 1.00 14.23 ? 402 TRP B CD2   1 
ATOM   5049 N NE1   . TRP B 1 261 ? -32.625 58.110 -22.280 1.00 20.64 ? 402 TRP B NE1   1 
ATOM   5050 C CE2   . TRP B 1 261 ? -33.693 58.858 -21.850 1.00 19.22 ? 402 TRP B CE2   1 
ATOM   5051 C CE3   . TRP B 1 261 ? -35.430 60.240 -22.829 1.00 16.42 ? 402 TRP B CE3   1 
ATOM   5052 C CZ2   . TRP B 1 261 ? -34.170 59.081 -20.554 1.00 16.70 ? 402 TRP B CZ2   1 
ATOM   5053 C CZ3   . TRP B 1 261 ? -35.917 60.454 -21.532 1.00 20.11 ? 402 TRP B CZ3   1 
ATOM   5054 C CH2   . TRP B 1 261 ? -35.280 59.874 -20.413 1.00 18.46 ? 402 TRP B CH2   1 
ATOM   5055 N N     . GLN B 1 262 ? -35.428 57.022 -26.102 1.00 14.80 ? 403 GLN B N     1 
ATOM   5056 C CA    . GLN B 1 262 ? -36.228 55.812 -25.953 1.00 15.73 ? 403 GLN B CA    1 
ATOM   5057 C C     . GLN B 1 262 ? -36.659 55.296 -27.326 1.00 14.89 ? 403 GLN B C     1 
ATOM   5058 O O     . GLN B 1 262 ? -36.927 56.082 -28.238 1.00 15.54 ? 403 GLN B O     1 
ATOM   5059 C CB    . GLN B 1 262 ? -37.451 56.101 -25.064 1.00 13.52 ? 403 GLN B CB    1 
ATOM   5060 C CG    . GLN B 1 262 ? -37.070 56.516 -23.624 1.00 14.94 ? 403 GLN B CG    1 
ATOM   5061 C CD    . GLN B 1 262 ? -38.291 56.890 -22.774 1.00 19.45 ? 403 GLN B CD    1 
ATOM   5062 O OE1   . GLN B 1 262 ? -39.350 56.259 -22.867 1.00 19.36 ? 403 GLN B OE1   1 
ATOM   5063 N NE2   . GLN B 1 262 ? -38.151 57.935 -21.965 1.00 17.28 ? 403 GLN B NE2   1 
ATOM   5064 N N     . GLY B 1 263 ? -36.694 53.972 -27.483 1.00 15.24 ? 404 GLY B N     1 
ATOM   5065 C CA    . GLY B 1 263 ? -37.086 53.344 -28.736 1.00 13.55 ? 404 GLY B CA    1 
ATOM   5066 C C     . GLY B 1 263 ? -38.415 52.617 -28.621 1.00 17.27 ? 404 GLY B C     1 
ATOM   5067 O O     . GLY B 1 263 ? -38.798 52.167 -27.538 1.00 13.86 ? 404 GLY B O     1 
ATOM   5068 N N     . GLY B 1 264 ? -39.119 52.497 -29.745 1.00 16.18 ? 405 GLY B N     1 
ATOM   5069 C CA    . GLY B 1 264 ? -40.392 51.801 -29.776 1.00 15.17 ? 405 GLY B CA    1 
ATOM   5070 C C     . GLY B 1 264 ? -41.268 52.330 -30.900 1.00 17.73 ? 405 GLY B C     1 
ATOM   5071 O O     . GLY B 1 264 ? -40.778 52.908 -31.860 1.00 17.66 ? 405 GLY B O     1 
ATOM   5072 N N     . GLY B 1 265 ? -42.575 52.098 -30.769 1.00 16.49 ? 406 GLY B N     1 
ATOM   5073 C CA    . GLY B 1 265 ? -43.520 52.655 -31.718 1.00 16.29 ? 406 GLY B CA    1 
ATOM   5074 C C     . GLY B 1 265 ? -43.482 54.171 -31.725 1.00 19.17 ? 406 GLY B C     1 
ATOM   5075 O O     . GLY B 1 265 ? -42.943 54.822 -30.815 1.00 16.11 ? 406 GLY B O     1 
ATOM   5076 N N     . ASN B 1 266 ? -44.062 54.730 -32.789 1.00 16.56 ? 407 ASN B N     1 
ATOM   5077 C CA    . ASN B 1 266 ? -44.168 56.168 -33.036 1.00 18.08 ? 407 ASN B CA    1 
ATOM   5078 C C     . ASN B 1 266 ? -42.836 56.788 -33.442 1.00 20.42 ? 407 ASN B C     1 
ATOM   5079 O O     . ASN B 1 266 ? -42.781 57.581 -34.389 1.00 18.06 ? 407 ASN B O     1 
ATOM   5080 C CB    . ASN B 1 266 ? -44.731 56.922 -31.828 1.00 18.14 ? 407 ASN B CB    1 
ATOM   5081 C CG    . ASN B 1 266 ? -45.152 58.347 -32.190 1.00 25.37 ? 407 ASN B CG    1 
ATOM   5082 O OD1   . ASN B 1 266 ? -46.020 58.530 -33.030 1.00 26.39 ? 407 ASN B OD1   1 
ATOM   5083 N ND2   . ASN B 1 266 ? -44.502 59.357 -31.590 1.00 19.46 ? 407 ASN B ND2   1 
ATOM   5084 N N     . MET B 1 267 ? -41.751 56.447 -32.749 1.00 15.44 ? 408 MET B N     1 
ATOM   5085 C CA    . MET B 1 267 ? -40.468 57.027 -33.126 1.00 17.78 ? 408 MET B CA    1 
ATOM   5086 C C     . MET B 1 267 ? -39.789 56.296 -34.279 1.00 19.04 ? 408 MET B C     1 
ATOM   5087 O O     . MET B 1 267 ? -38.852 56.850 -34.868 1.00 17.21 ? 408 MET B O     1 
ATOM   5088 C CB    . MET B 1 267 ? -39.555 57.098 -31.898 1.00 15.51 ? 408 MET B CB    1 
ATOM   5089 C CG    . MET B 1 267 ? -39.211 55.775 -31.232 1.00 14.84 ? 408 MET B CG    1 
ATOM   5090 S SD    . MET B 1 267 ? -37.920 54.834 -32.037 1.00 18.95 ? 408 MET B SD    1 
ATOM   5091 C CE    . MET B 1 267 ? -36.445 55.716 -31.536 1.00 19.40 ? 408 MET B CE    1 
ATOM   5092 N N     . ILE B 1 268 ? -40.244 55.074 -34.644 1.00 18.40 ? 409 ILE B N     1 
ATOM   5093 C CA    . ILE B 1 268 ? -39.644 54.358 -35.768 1.00 21.46 ? 409 ILE B CA    1 
ATOM   5094 C C     . ILE B 1 268 ? -40.373 54.728 -37.056 1.00 21.59 ? 409 ILE B C     1 
ATOM   5095 O O     . ILE B 1 268 ? -41.550 55.096 -37.053 1.00 21.99 ? 409 ILE B O     1 
ATOM   5096 C CB    . ILE B 1 268 ? -39.650 52.825 -35.561 1.00 22.30 ? 409 ILE B CB    1 
ATOM   5097 C CG1   . ILE B 1 268 ? -41.071 52.305 -35.307 1.00 19.52 ? 409 ILE B CG1   1 
ATOM   5098 C CG2   . ILE B 1 268 ? -38.711 52.421 -34.446 1.00 24.01 ? 409 ILE B CG2   1 
ATOM   5099 C CD1   . ILE B 1 268 ? -41.776 51.828 -36.583 1.00 27.55 ? 409 ILE B CD1   1 
ATOM   5100 N N     . ALA B 1 269 ? -39.663 54.609 -38.174 1.00 22.20 ? 410 ALA B N     1 
ATOM   5101 C CA    . ALA B 1 269 ? -40.259 54.615 -39.502 1.00 24.15 ? 410 ALA B CA    1 
ATOM   5102 C C     . ALA B 1 269 ? -40.405 53.216 -40.081 1.00 23.76 ? 410 ALA B C     1 
ATOM   5103 O O     . ALA B 1 269 ? -41.365 52.952 -40.812 1.00 30.21 ? 410 ALA B O     1 
ATOM   5104 C CB    . ALA B 1 269 ? -39.414 55.472 -40.453 1.00 25.84 ? 410 ALA B CB    1 
ATOM   5105 N N     . ASP B 1 270 ? -39.488 52.308 -39.747 1.00 24.21 ? 411 ASP B N     1 
ATOM   5106 C CA    . ASP B 1 270 ? -39.506 50.941 -40.250 1.00 25.17 ? 411 ASP B CA    1 
ATOM   5107 C C     . ASP B 1 270 ? -38.728 50.043 -39.300 1.00 26.74 ? 411 ASP B C     1 
ATOM   5108 O O     . ASP B 1 270 ? -37.649 50.417 -38.829 1.00 25.30 ? 411 ASP B O     1 
ATOM   5109 C CB    . ASP B 1 270 ? -38.899 50.857 -41.655 1.00 27.05 ? 411 ASP B CB    1 
ATOM   5110 C CG    . ASP B 1 270 ? -39.056 49.485 -42.264 1.00 31.61 ? 411 ASP B CG    1 
ATOM   5111 O OD1   . ASP B 1 270 ? -40.171 49.176 -42.734 1.00 32.54 ? 411 ASP B OD1   1 
ATOM   5112 O OD2   . ASP B 1 270 ? -38.065 48.721 -42.284 1.00 36.17 ? 411 ASP B OD2   1 
ATOM   5113 N N     . VAL B 1 271 ? -39.274 48.860 -39.031 1.00 21.45 ? 412 VAL B N     1 
ATOM   5114 C CA    . VAL B 1 271 ? -38.628 47.875 -38.173 1.00 23.44 ? 412 VAL B CA    1 
ATOM   5115 C C     . VAL B 1 271 ? -38.544 46.553 -38.922 1.00 28.18 ? 412 VAL B C     1 
ATOM   5116 O O     . VAL B 1 271 ? -39.554 46.058 -39.441 1.00 21.47 ? 412 VAL B O     1 
ATOM   5117 C CB    . VAL B 1 271 ? -39.381 47.689 -36.840 1.00 23.91 ? 412 VAL B CB    1 
ATOM   5118 C CG1   . VAL B 1 271 ? -38.758 46.555 -36.012 1.00 20.05 ? 412 VAL B CG1   1 
ATOM   5119 C CG2   . VAL B 1 271 ? -39.383 48.989 -36.049 1.00 19.85 ? 412 VAL B CG2   1 
ATOM   5120 N N     . THR B 1 272 ? -37.338 46.002 -39.004 1.00 22.67 ? 413 THR B N     1 
ATOM   5121 C CA    . THR B 1 272 ? -37.116 44.592 -39.284 1.00 25.04 ? 413 THR B CA    1 
ATOM   5122 C C     . THR B 1 272 ? -36.357 44.004 -38.104 1.00 25.08 ? 413 THR B C     1 
ATOM   5123 O O     . THR B 1 272 ? -35.867 44.733 -37.243 1.00 22.10 ? 413 THR B O     1 
ATOM   5124 C CB    . THR B 1 272 ? -36.336 44.384 -40.587 1.00 27.35 ? 413 THR B CB    1 
ATOM   5125 O OG1   . THR B 1 272 ? -34.956 44.687 -40.365 1.00 28.64 ? 413 THR B OG1   1 
ATOM   5126 C CG2   . THR B 1 272 ? -36.893 45.266 -41.704 1.00 26.33 ? 413 THR B CG2   1 
ATOM   5127 N N     . LEU B 1 273 ? -36.269 42.671 -38.049 1.00 23.80 ? 414 LEU B N     1 
ATOM   5128 C CA    . LEU B 1 273 ? -35.495 42.058 -36.975 1.00 25.96 ? 414 LEU B CA    1 
ATOM   5129 C C     . LEU B 1 273 ? -34.044 42.520 -37.009 1.00 28.29 ? 414 LEU B C     1 
ATOM   5130 O O     . LEU B 1 273 ? -33.382 42.573 -35.966 1.00 28.85 ? 414 LEU B O     1 
ATOM   5131 C CB    . LEU B 1 273 ? -35.568 40.533 -37.065 1.00 24.54 ? 414 LEU B CB    1 
ATOM   5132 C CG    . LEU B 1 273 ? -36.979 39.969 -36.859 1.00 30.98 ? 414 LEU B CG    1 
ATOM   5133 C CD1   . LEU B 1 273 ? -36.965 38.441 -36.859 1.00 28.99 ? 414 LEU B CD1   1 
ATOM   5134 C CD2   . LEU B 1 273 ? -37.582 40.508 -35.574 1.00 26.28 ? 414 LEU B CD2   1 
ATOM   5135 N N     . GLU B 1 274 ? -33.545 42.888 -38.190 1.00 25.94 ? 415 GLU B N     1 
ATOM   5136 C CA    . GLU B 1 274 ? -32.146 43.270 -38.326 1.00 31.71 ? 415 GLU B CA    1 
ATOM   5137 C C     . GLU B 1 274 ? -31.891 44.695 -37.829 1.00 32.82 ? 415 GLU B C     1 
ATOM   5138 O O     . GLU B 1 274 ? -30.920 44.932 -37.104 1.00 31.85 ? 415 GLU B O     1 
ATOM   5139 C CB    . GLU B 1 274 ? -31.694 43.104 -39.783 1.00 33.56 ? 415 GLU B CB    1 
ATOM   5140 C CG    . GLU B 1 274 ? -30.172 43.035 -39.929 1.00 48.33 ? 415 GLU B CG    1 
ATOM   5141 C CD    . GLU B 1 274 ? -29.664 43.527 -41.278 1.00 57.82 ? 415 GLU B CD    1 
ATOM   5142 O OE1   . GLU B 1 274 ? -30.270 44.458 -41.857 1.00 56.60 ? 415 GLU B OE1   1 
ATOM   5143 O OE2   . GLU B 1 274 ? -28.636 42.991 -41.748 1.00 65.08 ? 415 GLU B OE2   1 
ATOM   5144 N N     . ARG B 1 275 ? -32.749 45.653 -38.189 1.00 27.60 ? 416 ARG B N     1 
ATOM   5145 C CA    . ARG B 1 275 ? -32.484 47.047 -37.851 1.00 27.53 ? 416 ARG B CA    1 
ATOM   5146 C C     . ARG B 1 275 ? -33.777 47.844 -37.915 1.00 27.89 ? 416 ARG B C     1 
ATOM   5147 O O     . ARG B 1 275 ? -34.745 47.434 -38.555 1.00 26.87 ? 416 ARG B O     1 
ATOM   5148 C CB    . ARG B 1 275 ? -31.451 47.669 -38.795 1.00 28.19 ? 416 ARG B CB    1 
ATOM   5149 C CG    . ARG B 1 275 ? -31.843 47.577 -40.266 1.00 36.73 ? 416 ARG B CG    1 
ATOM   5150 C CD    . ARG B 1 275 ? -32.467 48.887 -40.724 1.00 38.90 ? 416 ARG B CD    1 
ATOM   5151 N NE    . ARG B 1 275 ? -33.204 48.782 -41.979 1.00 35.17 ? 416 ARG B NE    1 
ATOM   5152 C CZ    . ARG B 1 275 ? -34.527 48.760 -42.084 1.00 36.24 ? 416 ARG B CZ    1 
ATOM   5153 N NH1   . ARG B 1 275 ? -35.311 48.664 -41.016 1.00 30.52 ? 416 ARG B NH1   1 
ATOM   5154 N NH2   . ARG B 1 275 ? -35.079 48.826 -43.291 1.00 38.15 ? 416 ARG B NH2   1 
ATOM   5155 N N     . SER B 1 276 ? -33.773 49.004 -37.263 1.00 26.60 ? 417 SER B N     1 
ATOM   5156 C CA    . SER B 1 276 ? -34.894 49.933 -37.309 1.00 27.64 ? 417 SER B CA    1 
ATOM   5157 C C     . SER B 1 276 ? -34.420 51.293 -37.791 1.00 26.71 ? 417 SER B C     1 
ATOM   5158 O O     . SER B 1 276 ? -33.346 51.754 -37.399 1.00 27.55 ? 417 SER B O     1 
ATOM   5159 C CB    . SER B 1 276 ? -35.554 50.081 -35.937 1.00 23.58 ? 417 SER B CB    1 
ATOM   5160 O OG    . SER B 1 276 ? -36.026 48.830 -35.471 1.00 29.06 ? 417 SER B OG    1 
ATOM   5161 N N     . LEU B 1 277 ? -35.217 51.922 -38.649 1.00 22.08 ? 418 LEU B N     1 
ATOM   5162 C CA    . LEU B 1 277 ? -34.978 53.286 -39.107 1.00 24.30 ? 418 LEU B CA    1 
ATOM   5163 C C     . LEU B 1 277 ? -35.882 54.228 -38.327 1.00 22.58 ? 418 LEU B C     1 
ATOM   5164 O O     . LEU B 1 277 ? -36.994 53.866 -37.965 1.00 20.32 ? 418 LEU B O     1 
ATOM   5165 C CB    . LEU B 1 277 ? -35.254 53.425 -40.609 1.00 25.10 ? 418 LEU B CB    1 
ATOM   5166 C CG    . LEU B 1 277 ? -34.573 52.414 -41.535 1.00 30.71 ? 418 LEU B CG    1 
ATOM   5167 C CD1   . LEU B 1 277 ? -34.900 52.690 -43.011 1.00 32.30 ? 418 LEU B CD1   1 
ATOM   5168 C CD2   . LEU B 1 277 ? -33.081 52.459 -41.304 1.00 28.04 ? 418 LEU B CD2   1 
ATOM   5169 N N     . TYR B 1 278 ? -35.415 55.444 -38.081 1.00 23.83 ? 419 TYR B N     1 
ATOM   5170 C CA    . TYR B 1 278 ? -36.111 56.348 -37.175 1.00 23.88 ? 419 TYR B CA    1 
ATOM   5171 C C     . TYR B 1 278 ? -36.771 57.484 -37.941 1.00 24.29 ? 419 TYR B C     1 
ATOM   5172 O O     . TYR B 1 278 ? -36.330 57.868 -39.031 1.00 24.46 ? 419 TYR B O     1 
ATOM   5173 C CB    . TYR B 1 278 ? -35.141 56.896 -36.113 1.00 25.44 ? 419 TYR B CB    1 
ATOM   5174 C CG    . TYR B 1 278 ? -34.540 55.756 -35.325 1.00 27.87 ? 419 TYR B CG    1 
ATOM   5175 C CD1   . TYR B 1 278 ? -35.364 54.825 -34.700 1.00 28.95 ? 419 TYR B CD1   1 
ATOM   5176 C CD2   . TYR B 1 278 ? -33.165 55.543 -35.294 1.00 28.80 ? 419 TYR B CD2   1 
ATOM   5177 C CE1   . TYR B 1 278 ? -34.836 53.738 -34.005 1.00 33.09 ? 419 TYR B CE1   1 
ATOM   5178 C CE2   . TYR B 1 278 ? -32.620 54.447 -34.601 1.00 35.99 ? 419 TYR B CE2   1 
ATOM   5179 C CZ    . TYR B 1 278 ? -33.467 53.552 -33.957 1.00 34.25 ? 419 TYR B CZ    1 
ATOM   5180 O OH    . TYR B 1 278 ? -32.960 52.464 -33.272 1.00 33.30 ? 419 TYR B OH    1 
ATOM   5181 N N     . GLN B 1 279 ? -37.853 57.993 -37.365 1.00 22.33 ? 420 GLN B N     1 
ATOM   5182 C CA    . GLN B 1 279 ? -38.522 59.182 -37.866 1.00 23.94 ? 420 GLN B CA    1 
ATOM   5183 C C     . GLN B 1 279 ? -37.698 60.425 -37.567 1.00 23.27 ? 420 GLN B C     1 
ATOM   5184 O O     . GLN B 1 279 ? -36.754 60.402 -36.773 1.00 25.55 ? 420 GLN B O     1 
ATOM   5185 C CB    . GLN B 1 279 ? -39.882 59.348 -37.196 1.00 25.52 ? 420 GLN B CB    1 
ATOM   5186 C CG    . GLN B 1 279 ? -40.813 58.208 -37.400 1.00 26.48 ? 420 GLN B CG    1 
ATOM   5187 C CD    . GLN B 1 279 ? -42.008 58.636 -38.182 1.00 38.12 ? 420 GLN B CD    1 
ATOM   5188 O OE1   . GLN B 1 279 ? -41.952 58.732 -39.409 1.00 43.10 ? 420 GLN B OE1   1 
ATOM   5189 N NE2   . GLN B 1 279 ? -43.102 58.928 -37.481 1.00 40.80 ? 420 GLN B NE2   1 
ATOM   5190 N N     . GLY B 1 280 ? -38.107 61.536 -38.176 1.00 24.52 ? 421 GLY B N     1 
ATOM   5191 C CA    . GLY B 1 280 ? -37.627 62.841 -37.790 1.00 26.36 ? 421 GLY B CA    1 
ATOM   5192 C C     . GLY B 1 280 ? -38.424 63.398 -36.617 1.00 25.27 ? 421 GLY B C     1 
ATOM   5193 O O     . GLY B 1 280 ? -39.384 62.785 -36.135 1.00 24.28 ? 421 GLY B O     1 
ATOM   5194 N N     . PRO B 1 281 ? -38.032 64.572 -36.135 1.00 26.06 ? 422 PRO B N     1 
ATOM   5195 C CA    . PRO B 1 281 ? -38.703 65.167 -34.957 1.00 24.66 ? 422 PRO B CA    1 
ATOM   5196 C C     . PRO B 1 281 ? -40.070 65.733 -35.311 1.00 23.79 ? 422 PRO B C     1 
ATOM   5197 O O     . PRO B 1 281 ? -40.333 66.087 -36.468 1.00 25.58 ? 422 PRO B O     1 
ATOM   5198 C CB    . PRO B 1 281 ? -37.730 66.273 -34.520 1.00 26.06 ? 422 PRO B CB    1 
ATOM   5199 C CG    . PRO B 1 281 ? -36.940 66.597 -35.758 1.00 31.25 ? 422 PRO B CG    1 
ATOM   5200 C CD    . PRO B 1 281 ? -36.833 65.325 -36.548 1.00 25.67 ? 422 PRO B CD    1 
ATOM   5201 N N     . PRO B 1 282 ? -40.994 65.824 -34.338 1.00 22.93 ? 423 PRO B N     1 
ATOM   5202 C CA    . PRO B 1 282 ? -40.848 65.446 -32.927 1.00 22.01 ? 423 PRO B CA    1 
ATOM   5203 C C     . PRO B 1 282 ? -40.954 63.939 -32.668 1.00 21.57 ? 423 PRO B C     1 
ATOM   5204 O O     . PRO B 1 282 ? -40.531 63.477 -31.602 1.00 19.91 ? 423 PRO B O     1 
ATOM   5205 C CB    . PRO B 1 282 ? -41.992 66.215 -32.254 1.00 20.40 ? 423 PRO B CB    1 
ATOM   5206 C CG    . PRO B 1 282 ? -43.071 66.302 -33.313 1.00 25.38 ? 423 PRO B CG    1 
ATOM   5207 C CD    . PRO B 1 282 ? -42.371 66.251 -34.659 1.00 19.45 ? 423 PRO B CD    1 
ATOM   5208 N N     . ASN B 1 283 ? -41.502 63.172 -33.622 1.00 18.82 ? 424 ASN B N     1 
ATOM   5209 C CA    . ASN B 1 283 ? -41.765 61.746 -33.410 1.00 20.81 ? 424 ASN B CA    1 
ATOM   5210 C C     . ASN B 1 283 ? -40.521 61.002 -32.949 1.00 18.66 ? 424 ASN B C     1 
ATOM   5211 O O     . ASN B 1 283 ? -40.608 60.091 -32.119 1.00 16.22 ? 424 ASN B O     1 
ATOM   5212 C CB    . ASN B 1 283 ? -42.297 61.104 -34.703 1.00 22.11 ? 424 ASN B CB    1 
ATOM   5213 C CG    . ASN B 1 283 ? -43.515 61.835 -35.266 1.00 27.24 ? 424 ASN B CG    1 
ATOM   5214 O OD1   . ASN B 1 283 ? -43.436 63.003 -35.655 1.00 26.75 ? 424 ASN B OD1   1 
ATOM   5215 N ND2   . ASN B 1 283 ? -44.643 61.149 -35.304 1.00 28.87 ? 424 ASN B ND2   1 
ATOM   5216 N N     . LYS B 1 284 ? -39.359 61.377 -33.500 1.00 16.97 ? 425 LYS B N     1 
ATOM   5217 C CA    . LYS B 1 284 ? -38.072 60.782 -33.156 1.00 17.83 ? 425 LYS B CA    1 
ATOM   5218 C C     . LYS B 1 284 ? -37.872 60.652 -31.656 1.00 16.63 ? 425 LYS B C     1 
ATOM   5219 O O     . LYS B 1 284 ? -37.241 59.695 -31.190 1.00 14.82 ? 425 LYS B O     1 
ATOM   5220 C CB    . LYS B 1 284 ? -36.958 61.654 -33.741 1.00 18.76 ? 425 LYS B CB    1 
ATOM   5221 C CG    . LYS B 1 284 ? -35.532 61.145 -33.535 1.00 25.14 ? 425 LYS B CG    1 
ATOM   5222 C CD    . LYS B 1 284 ? -34.572 62.143 -34.205 1.00 25.22 ? 425 LYS B CD    1 
ATOM   5223 C CE    . LYS B 1 284 ? -33.104 61.749 -34.129 1.00 28.39 ? 425 LYS B CE    1 
ATOM   5224 N NZ    . LYS B 1 284 ? -32.260 62.954 -34.490 1.00 30.68 ? 425 LYS B NZ    1 
ATOM   5225 N N     . PHE B 1 285 ? -38.373 61.613 -30.888 1.00 14.28 ? 426 PHE B N     1 
ATOM   5226 C CA    . PHE B 1 285 ? -38.143 61.650 -29.448 1.00 14.08 ? 426 PHE B CA    1 
ATOM   5227 C C     . PHE B 1 285 ? -39.354 61.237 -28.625 1.00 16.13 ? 426 PHE B C     1 
ATOM   5228 O O     . PHE B 1 285 ? -39.310 61.331 -27.391 1.00 18.01 ? 426 PHE B O     1 
ATOM   5229 C CB    . PHE B 1 285 ? -37.687 63.063 -29.049 1.00 16.31 ? 426 PHE B CB    1 
ATOM   5230 C CG    . PHE B 1 285 ? -36.484 63.524 -29.825 1.00 15.72 ? 426 PHE B CG    1 
ATOM   5231 C CD1   . PHE B 1 285 ? -35.254 62.898 -29.639 1.00 22.43 ? 426 PHE B CD1   1 
ATOM   5232 C CD2   . PHE B 1 285 ? -36.591 64.516 -30.787 1.00 18.91 ? 426 PHE B CD2   1 
ATOM   5233 C CE1   . PHE B 1 285 ? -34.148 63.276 -30.380 1.00 18.98 ? 426 PHE B CE1   1 
ATOM   5234 C CE2   . PHE B 1 285 ? -35.483 64.902 -31.527 1.00 23.33 ? 426 PHE B CE2   1 
ATOM   5235 C CZ    . PHE B 1 285 ? -34.265 64.284 -31.313 1.00 20.36 ? 426 PHE B CZ    1 
ATOM   5236 N N     . GLU B 1 286 ? -40.443 60.806 -29.255 1.00 15.47 ? 427 GLU B N     1 
ATOM   5237 C CA    . GLU B 1 286 ? -41.638 60.404 -28.512 1.00 17.26 ? 427 GLU B CA    1 
ATOM   5238 C C     . GLU B 1 286 ? -41.888 58.929 -28.819 1.00 16.09 ? 427 GLU B C     1 
ATOM   5239 O O     . GLU B 1 286 ? -42.447 58.590 -29.862 1.00 16.34 ? 427 GLU B O     1 
ATOM   5240 C CB    . GLU B 1 286 ? -42.839 61.289 -28.858 1.00 16.33 ? 427 GLU B CB    1 
ATOM   5241 C CG    . GLU B 1 286 ? -42.536 62.789 -28.675 1.00 17.69 ? 427 GLU B CG    1 
ATOM   5242 C CD    . GLU B 1 286 ? -43.682 63.733 -29.108 1.00 21.98 ? 427 GLU B CD    1 
ATOM   5243 O OE1   . GLU B 1 286 ? -44.552 63.351 -29.930 1.00 21.93 ? 427 GLU B OE1   1 
ATOM   5244 O OE2   . GLU B 1 286 ? -43.657 64.906 -28.683 1.00 20.20 ? 427 GLU B OE2   1 
ATOM   5245 N N     . ALA B 1 287 ? -41.447 58.058 -27.918 1.00 15.87 ? 428 ALA B N     1 
ATOM   5246 C CA    . ALA B 1 287 ? -41.565 56.618 -28.082 1.00 18.02 ? 428 ALA B CA    1 
ATOM   5247 C C     . ALA B 1 287 ? -42.832 56.151 -27.382 1.00 17.23 ? 428 ALA B C     1 
ATOM   5248 O O     . ALA B 1 287 ? -43.063 56.499 -26.216 1.00 16.19 ? 428 ALA B O     1 
ATOM   5249 C CB    . ALA B 1 287 ? -40.336 55.903 -27.501 1.00 14.91 ? 428 ALA B CB    1 
ATOM   5250 N N     . GLY B 1 288 ? -43.648 55.368 -28.088 1.00 14.40 ? 429 GLY B N     1 
ATOM   5251 C CA    . GLY B 1 288 ? -44.869 54.841 -27.506 1.00 15.18 ? 429 GLY B CA    1 
ATOM   5252 C C     . GLY B 1 288 ? -46.050 55.808 -27.574 1.00 21.81 ? 429 GLY B C     1 
ATOM   5253 O O     . GLY B 1 288 ? -45.961 56.924 -28.092 1.00 19.76 ? 429 GLY B O     1 
ATOM   5254 N N     . THR B 1 289 ? -47.188 55.350 -27.035 1.00 16.63 ? 430 THR B N     1 
ATOM   5255 C CA    . THR B 1 289 ? -48.387 56.177 -26.967 1.00 19.37 ? 430 THR B CA    1 
ATOM   5256 C C     . THR B 1 289 ? -48.099 57.424 -26.144 1.00 17.89 ? 430 THR B C     1 
ATOM   5257 O O     . THR B 1 289 ? -47.635 57.340 -25.003 1.00 20.60 ? 430 THR B O     1 
ATOM   5258 C CB    . THR B 1 289 ? -49.547 55.386 -26.349 1.00 22.63 ? 430 THR B CB    1 
ATOM   5259 O OG1   . THR B 1 289 ? -49.792 54.214 -27.133 1.00 19.78 ? 430 THR B OG1   1 
ATOM   5260 C CG2   . THR B 1 289 ? -50.846 56.226 -26.271 1.00 20.16 ? 430 THR B CG2   1 
ATOM   5261 N N     . GLY B 1 290 ? -48.341 58.581 -26.726 1.00 19.44 ? 431 GLY B N     1 
ATOM   5262 C CA    . GLY B 1 290 ? -48.161 59.801 -25.980 1.00 22.98 ? 431 GLY B CA    1 
ATOM   5263 C C     . GLY B 1 290 ? -49.254 59.996 -24.950 1.00 22.21 ? 431 GLY B C     1 
ATOM   5264 O O     . GLY B 1 290 ? -50.322 59.377 -24.993 1.00 23.32 ? 431 GLY B O     1 
ATOM   5265 N N     . ASN B 1 291 ? -48.970 60.878 -23.994 1.00 18.26 ? 432 ASN B N     1 
ATOM   5266 C CA    . ASN B 1 291 ? -49.968 61.301 -23.023 1.00 20.88 ? 432 ASN B CA    1 
ATOM   5267 C C     . ASN B 1 291 ? -50.885 62.330 -23.686 1.00 17.81 ? 432 ASN B C     1 
ATOM   5268 O O     . ASN B 1 291 ? -50.842 63.530 -23.406 1.00 17.35 ? 432 ASN B O     1 
ATOM   5269 C CB    . ASN B 1 291 ? -49.299 61.862 -21.779 1.00 16.29 ? 432 ASN B CB    1 
ATOM   5270 C CG    . ASN B 1 291 ? -50.281 62.101 -20.673 1.00 17.59 ? 432 ASN B CG    1 
ATOM   5271 O OD1   . ASN B 1 291 ? -51.502 61.938 -20.862 1.00 17.76 ? 432 ASN B OD1   1 
ATOM   5272 N ND2   . ASN B 1 291 ? -49.771 62.486 -19.496 1.00 18.10 ? 432 ASN B ND2   1 
ATOM   5273 N N     . ILE B 1 292 ? -51.744 61.827 -24.577 1.00 15.07 ? 433 ILE B N     1 
ATOM   5274 C CA    . ILE B 1 292 ? -52.565 62.714 -25.401 1.00 17.25 ? 433 ILE B CA    1 
ATOM   5275 C C     . ILE B 1 292 ? -53.445 63.600 -24.527 1.00 17.73 ? 433 ILE B C     1 
ATOM   5276 O O     . ILE B 1 292 ? -53.546 64.814 -24.743 1.00 17.02 ? 433 ILE B O     1 
ATOM   5277 C CB    . ILE B 1 292 ? -53.423 61.902 -26.392 1.00 21.61 ? 433 ILE B CB    1 
ATOM   5278 C CG1   . ILE B 1 292 ? -52.571 60.894 -27.167 1.00 25.27 ? 433 ILE B CG1   1 
ATOM   5279 C CG2   . ILE B 1 292 ? -54.099 62.830 -27.382 1.00 17.91 ? 433 ILE B CG2   1 
ATOM   5280 C CD1   . ILE B 1 292 ? -51.617 61.545 -28.109 1.00 29.88 ? 433 ILE B CD1   1 
ATOM   5281 N N     . ALA B 1 293 ? -54.127 62.996 -23.543 1.00 17.92 ? 434 ALA B N     1 
ATOM   5282 C CA    . ALA B 1 293 ? -55.128 63.743 -22.785 1.00 16.05 ? 434 ALA B CA    1 
ATOM   5283 C C     . ALA B 1 293 ? -54.498 64.887 -22.005 1.00 16.14 ? 434 ALA B C     1 
ATOM   5284 O O     . ALA B 1 293 ? -55.046 65.997 -21.958 1.00 16.61 ? 434 ALA B O     1 
ATOM   5285 C CB    . ALA B 1 293 ? -55.878 62.807 -21.834 1.00 15.75 ? 434 ALA B CB    1 
ATOM   5286 N N     . ASP B 1 294 ? -53.356 64.640 -21.367 1.00 15.69 ? 435 ASP B N     1 
ATOM   5287 C CA    . ASP B 1 294 ? -52.774 65.698 -20.547 1.00 17.04 ? 435 ASP B CA    1 
ATOM   5288 C C     . ASP B 1 294 ? -52.137 66.783 -21.395 1.00 18.08 ? 435 ASP B C     1 
ATOM   5289 O O     . ASP B 1 294 ? -52.107 67.946 -20.983 1.00 14.95 ? 435 ASP B O     1 
ATOM   5290 C CB    . ASP B 1 294 ? -51.749 65.125 -19.582 1.00 15.34 ? 435 ASP B CB    1 
ATOM   5291 C CG    . ASP B 1 294 ? -52.389 64.229 -18.551 1.00 24.49 ? 435 ASP B CG    1 
ATOM   5292 O OD1   . ASP B 1 294 ? -53.577 64.472 -18.194 1.00 23.46 ? 435 ASP B OD1   1 
ATOM   5293 O OD2   . ASP B 1 294 ? -51.696 63.301 -18.094 1.00 22.91 ? 435 ASP B OD2   1 
ATOM   5294 N N     . ALA B 1 295 ? -51.631 66.429 -22.576 1.00 14.63 ? 436 ALA B N     1 
ATOM   5295 C CA    . ALA B 1 295 ? -51.202 67.458 -23.515 1.00 14.96 ? 436 ALA B CA    1 
ATOM   5296 C C     . ALA B 1 295 ? -52.379 68.337 -23.931 1.00 16.37 ? 436 ALA B C     1 
ATOM   5297 O O     . ALA B 1 295 ? -52.257 69.567 -23.989 1.00 18.26 ? 436 ALA B O     1 
ATOM   5298 C CB    . ALA B 1 295 ? -50.551 66.802 -24.733 1.00 14.02 ? 436 ALA B CB    1 
ATOM   5299 N N     . VAL B 1 296 ? -53.540 67.726 -24.197 1.00 19.33 ? 437 VAL B N     1 
ATOM   5300 C CA    . VAL B 1 296 ? -54.743 68.513 -24.505 1.00 19.33 ? 437 VAL B CA    1 
ATOM   5301 C C     . VAL B 1 296 ? -55.099 69.435 -23.333 1.00 18.02 ? 437 VAL B C     1 
ATOM   5302 O O     . VAL B 1 296 ? -55.399 70.631 -23.516 1.00 17.69 ? 437 VAL B O     1 
ATOM   5303 C CB    . VAL B 1 296 ? -55.909 67.570 -24.878 1.00 16.76 ? 437 VAL B CB    1 
ATOM   5304 C CG1   . VAL B 1 296 ? -57.206 68.323 -24.944 1.00 19.10 ? 437 VAL B CG1   1 
ATOM   5305 C CG2   . VAL B 1 296 ? -55.634 66.865 -26.239 1.00 17.42 ? 437 VAL B CG2   1 
ATOM   5306 N N     . GLY B 1 297 ? -55.036 68.903 -22.106 1.00 17.72 ? 438 GLY B N     1 
ATOM   5307 C CA    . GLY B 1 297 ? -55.310 69.729 -20.934 1.00 14.90 ? 438 GLY B CA    1 
ATOM   5308 C C     . GLY B 1 297 ? -54.300 70.850 -20.743 1.00 18.41 ? 438 GLY B C     1 
ATOM   5309 O O     . GLY B 1 297 ? -54.647 71.947 -20.291 1.00 18.28 ? 438 GLY B O     1 
ATOM   5310 N N     . LEU B 1 298 ? -53.032 70.591 -21.075 1.00 17.02 ? 439 LEU B N     1 
ATOM   5311 C CA    . LEU B 1 298 ? -52.021 71.641 -20.993 1.00 15.58 ? 439 LEU B CA    1 
ATOM   5312 C C     . LEU B 1 298 ? -52.298 72.740 -22.011 1.00 18.16 ? 439 LEU B C     1 
ATOM   5313 O O     . LEU B 1 298 ? -52.095 73.928 -21.726 1.00 18.59 ? 439 LEU B O     1 
ATOM   5314 C CB    . LEU B 1 298 ? -50.617 71.051 -21.202 1.00 16.32 ? 439 LEU B CB    1 
ATOM   5315 C CG    . LEU B 1 298 ? -49.481 72.082 -21.320 1.00 19.09 ? 439 LEU B CG    1 
ATOM   5316 C CD1   . LEU B 1 298 ? -49.383 72.901 -20.035 1.00 17.43 ? 439 LEU B CD1   1 
ATOM   5317 C CD2   . LEU B 1 298 ? -48.121 71.442 -21.642 1.00 20.08 ? 439 LEU B CD2   1 
ATOM   5318 N N     . GLY B 1 299 ? -52.751 72.370 -23.209 1.00 15.69 ? 440 GLY B N     1 
ATOM   5319 C CA    . GLY B 1 299 ? -53.148 73.393 -24.166 1.00 18.86 ? 440 GLY B CA    1 
ATOM   5320 C C     . GLY B 1 299 ? -54.270 74.275 -23.634 1.00 19.71 ? 440 GLY B C     1 
ATOM   5321 O O     . GLY B 1 299 ? -54.264 75.499 -23.825 1.00 20.89 ? 440 GLY B O     1 
ATOM   5322 N N     . GLU B 1 300 ? -55.244 73.661 -22.951 1.00 18.72 ? 441 GLU B N     1 
ATOM   5323 C CA    . GLU B 1 300 ? -56.305 74.445 -22.311 1.00 21.83 ? 441 GLU B CA    1 
ATOM   5324 C C     . GLU B 1 300 ? -55.748 75.368 -21.227 1.00 22.84 ? 441 GLU B C     1 
ATOM   5325 O O     . GLU B 1 300 ? -56.191 76.520 -21.082 1.00 23.02 ? 441 GLU B O     1 
ATOM   5326 C CB    . GLU B 1 300 ? -57.352 73.501 -21.731 1.00 20.13 ? 441 GLU B CB    1 
ATOM   5327 C CG    . GLU B 1 300 ? -58.605 74.141 -21.181 1.00 23.66 ? 441 GLU B CG    1 
ATOM   5328 C CD    . GLU B 1 300 ? -59.442 74.818 -22.265 1.00 30.74 ? 441 GLU B CD    1 
ATOM   5329 O OE1   . GLU B 1 300 ? -59.674 74.194 -23.332 1.00 30.04 ? 441 GLU B OE1   1 
ATOM   5330 O OE2   . GLU B 1 300 ? -59.964 75.921 -22.005 1.00 29.81 ? 441 GLU B OE2   1 
ATOM   5331 N N     . ALA B 1 301 ? -54.774 74.877 -20.455 1.00 19.18 ? 442 ALA B N     1 
ATOM   5332 C CA    . ALA B 1 301 ? -54.141 75.707 -19.434 1.00 19.06 ? 442 ALA B CA    1 
ATOM   5333 C C     . ALA B 1 301 ? -53.410 76.888 -20.059 1.00 20.02 ? 442 ALA B C     1 
ATOM   5334 O O     . ALA B 1 301 ? -53.434 78.007 -19.526 1.00 19.40 ? 442 ALA B O     1 
ATOM   5335 C CB    . ALA B 1 301 ? -53.175 74.857 -18.601 1.00 16.27 ? 442 ALA B CB    1 
ATOM   5336 N N     . ILE B 1 302 ? -52.739 76.650 -21.185 1.00 18.66 ? 443 ILE B N     1 
ATOM   5337 C CA    . ILE B 1 302 ? -52.029 77.719 -21.869 1.00 19.42 ? 443 ILE B CA    1 
ATOM   5338 C C     . ILE B 1 302 ? -53.014 78.778 -22.345 1.00 23.39 ? 443 ILE B C     1 
ATOM   5339 O O     . ILE B 1 302 ? -52.778 79.977 -22.180 1.00 24.29 ? 443 ILE B O     1 
ATOM   5340 C CB    . ILE B 1 302 ? -51.190 77.147 -23.029 1.00 21.32 ? 443 ILE B CB    1 
ATOM   5341 C CG1   . ILE B 1 302 ? -49.945 76.431 -22.492 1.00 19.99 ? 443 ILE B CG1   1 
ATOM   5342 C CG2   . ILE B 1 302 ? -50.785 78.252 -23.986 1.00 22.14 ? 443 ILE B CG2   1 
ATOM   5343 C CD1   . ILE B 1 302 ? -49.139 75.736 -23.581 1.00 21.48 ? 443 ILE B CD1   1 
ATOM   5344 N N     . ARG B 1 303 ? -54.141 78.353 -22.926 1.00 21.08 ? 444 ARG B N     1 
ATOM   5345 C CA    . ARG B 1 303 ? -55.164 79.315 -23.340 1.00 26.05 ? 444 ARG B CA    1 
ATOM   5346 C C     . ARG B 1 303 ? -55.695 80.120 -22.153 1.00 25.33 ? 444 ARG B C     1 
ATOM   5347 O O     . ARG B 1 303 ? -55.942 81.322 -22.279 1.00 23.59 ? 444 ARG B O     1 
ATOM   5348 C CB    . ARG B 1 303 ? -56.309 78.603 -24.060 1.00 25.77 ? 444 ARG B CB    1 
ATOM   5349 C CG    . ARG B 1 303 ? -55.969 78.238 -25.504 1.00 23.76 ? 444 ARG B CG    1 
ATOM   5350 C CD    . ARG B 1 303 ? -57.174 77.643 -26.225 1.00 27.70 ? 444 ARG B CD    1 
ATOM   5351 N NE    . ARG B 1 303 ? -57.542 76.323 -25.723 1.00 27.47 ? 444 ARG B NE    1 
ATOM   5352 C CZ    . ARG B 1 303 ? -56.898 75.200 -26.026 1.00 26.81 ? 444 ARG B CZ    1 
ATOM   5353 N NH1   . ARG B 1 303 ? -55.845 75.199 -26.829 1.00 26.86 ? 444 ARG B NH1   1 
ATOM   5354 N NH2   . ARG B 1 303 ? -57.319 74.050 -25.507 1.00 26.25 ? 444 ARG B NH2   1 
ATOM   5355 N N     . TYR B 1 304 ? -55.874 79.478 -20.992 1.00 25.32 ? 445 TYR B N     1 
ATOM   5356 C CA    . TYR B 1 304 ? -56.303 80.223 -19.806 1.00 24.82 ? 445 TYR B CA    1 
ATOM   5357 C C     . TYR B 1 304 ? -55.285 81.303 -19.433 1.00 25.14 ? 445 TYR B C     1 
ATOM   5358 O O     . TYR B 1 304 ? -55.634 82.480 -19.224 1.00 27.41 ? 445 TYR B O     1 
ATOM   5359 C CB    . TYR B 1 304 ? -56.520 79.261 -18.636 1.00 24.82 ? 445 TYR B CB    1 
ATOM   5360 C CG    . TYR B 1 304 ? -57.188 79.925 -17.451 1.00 26.52 ? 445 TYR B CG    1 
ATOM   5361 C CD1   . TYR B 1 304 ? -56.439 80.610 -16.510 1.00 23.69 ? 445 TYR B CD1   1 
ATOM   5362 C CD2   . TYR B 1 304 ? -58.571 79.891 -17.295 1.00 26.85 ? 445 TYR B CD2   1 
ATOM   5363 C CE1   . TYR B 1 304 ? -57.037 81.228 -15.435 1.00 27.59 ? 445 TYR B CE1   1 
ATOM   5364 C CE2   . TYR B 1 304 ? -59.181 80.499 -16.215 1.00 27.26 ? 445 TYR B CE2   1 
ATOM   5365 C CZ    . TYR B 1 304 ? -58.404 81.173 -15.288 1.00 30.39 ? 445 TYR B CZ    1 
ATOM   5366 O OH    . TYR B 1 304 ? -58.986 81.804 -14.204 1.00 32.97 ? 445 TYR B OH    1 
ATOM   5367 N N     . VAL B 1 305 ? -54.009 80.922 -19.360 1.00 21.90 ? 446 VAL B N     1 
ATOM   5368 C CA    . VAL B 1 305 ? -52.977 81.902 -19.038 1.00 24.55 ? 446 VAL B CA    1 
ATOM   5369 C C     . VAL B 1 305 ? -52.957 83.015 -20.083 1.00 28.21 ? 446 VAL B C     1 
ATOM   5370 O O     . VAL B 1 305 ? -52.808 84.199 -19.752 1.00 27.45 ? 446 VAL B O     1 
ATOM   5371 C CB    . VAL B 1 305 ? -51.607 81.213 -18.905 1.00 25.61 ? 446 VAL B CB    1 
ATOM   5372 C CG1   . VAL B 1 305 ? -50.493 82.252 -18.752 1.00 24.38 ? 446 VAL B CG1   1 
ATOM   5373 C CG2   . VAL B 1 305 ? -51.622 80.249 -17.723 1.00 21.95 ? 446 VAL B CG2   1 
ATOM   5374 N N     . GLU B 1 306 ? -53.158 82.662 -21.354 1.00 25.13 ? 447 GLU B N     1 
ATOM   5375 C CA    . GLU B 1 306 ? -53.069 83.656 -22.422 1.00 28.06 ? 447 GLU B CA    1 
ATOM   5376 C C     . GLU B 1 306 ? -54.218 84.645 -22.337 1.00 29.62 ? 447 GLU B C     1 
ATOM   5377 O O     . GLU B 1 306 ? -54.043 85.842 -22.602 1.00 29.79 ? 447 GLU B O     1 
ATOM   5378 C CB    . GLU B 1 306 ? -53.073 82.967 -23.788 1.00 26.31 ? 447 GLU B CB    1 
ATOM   5379 C CG    . GLU B 1 306 ? -51.711 82.400 -24.202 1.00 27.49 ? 447 GLU B CG    1 
ATOM   5380 C CD    . GLU B 1 306 ? -51.760 81.633 -25.537 1.00 34.70 ? 447 GLU B CD    1 
ATOM   5381 O OE1   . GLU B 1 306 ? -52.780 80.957 -25.808 1.00 30.12 ? 447 GLU B OE1   1 
ATOM   5382 O OE2   . GLU B 1 306 ? -50.753 81.675 -26.291 1.00 30.84 ? 447 GLU B OE2   1 
ATOM   5383 N N     . ARG B 1 307 ? -55.409 84.157 -21.988 1.00 31.58 ? 448 ARG B N     1 
ATOM   5384 C CA    . ARG B 1 307 ? -56.535 85.059 -21.790 1.00 30.11 ? 448 ARG B CA    1 
ATOM   5385 C C     . ARG B 1 307 ? -56.254 86.032 -20.654 1.00 32.49 ? 448 ARG B C     1 
ATOM   5386 O O     . ARG B 1 307 ? -56.591 87.217 -20.750 1.00 32.67 ? 448 ARG B O     1 
ATOM   5387 C CB    . ARG B 1 307 ? -57.822 84.271 -21.528 1.00 36.21 ? 448 ARG B CB    1 
ATOM   5388 C CG    . ARG B 1 307 ? -58.452 83.667 -22.781 1.00 39.12 ? 448 ARG B CG    1 
ATOM   5389 C CD    . ARG B 1 307 ? -59.875 83.172 -22.534 1.00 44.19 ? 448 ARG B CD    1 
ATOM   5390 N NE    . ARG B 1 307 ? -59.954 82.267 -21.394 1.00 42.40 ? 448 ARG B NE    1 
ATOM   5391 C CZ    . ARG B 1 307 ? -59.781 80.952 -21.470 1.00 40.50 ? 448 ARG B CZ    1 
ATOM   5392 N NH1   . ARG B 1 307 ? -59.537 80.352 -22.626 1.00 35.84 ? 448 ARG B NH1   1 
ATOM   5393 N NH2   . ARG B 1 307 ? -59.843 80.221 -20.357 1.00 34.90 ? 448 ARG B NH2   1 
ATOM   5394 N N     . VAL B 1 308 ? -55.614 85.563 -19.574 1.00 30.85 ? 449 VAL B N     1 
ATOM   5395 C CA    . VAL B 1 308 ? -55.340 86.500 -18.480 1.00 33.97 ? 449 VAL B CA    1 
ATOM   5396 C C     . VAL B 1 308 ? -54.230 87.474 -18.867 1.00 30.84 ? 449 VAL B C     1 
ATOM   5397 O O     . VAL B 1 308 ? -54.295 88.670 -18.546 1.00 36.27 ? 449 VAL B O     1 
ATOM   5398 C CB    . VAL B 1 308 ? -55.003 85.750 -17.179 1.00 29.90 ? 449 VAL B CB    1 
ATOM   5399 C CG1   . VAL B 1 308 ? -54.674 86.742 -16.076 1.00 29.27 ? 449 VAL B CG1   1 
ATOM   5400 C CG2   . VAL B 1 308 ? -56.154 84.855 -16.769 1.00 28.25 ? 449 VAL B CG2   1 
ATOM   5401 N N     . GLY B 1 309 ? -53.195 86.986 -19.548 1.00 29.14 ? 450 GLY B N     1 
ATOM   5402 C CA    . GLY B 1 309 ? -52.080 87.813 -19.979 1.00 32.18 ? 450 GLY B CA    1 
ATOM   5403 C C     . GLY B 1 309 ? -50.847 87.639 -19.116 1.00 31.75 ? 450 GLY B C     1 
ATOM   5404 O O     . GLY B 1 309 ? -50.867 88.005 -17.938 1.00 29.45 ? 450 GLY B O     1 
ATOM   5405 N N     . ILE B 1 310 ? -49.762 87.093 -19.684 1.00 28.93 ? 451 ILE B N     1 
ATOM   5406 C CA    . ILE B 1 310 ? -48.609 86.733 -18.860 1.00 27.45 ? 451 ILE B CA    1 
ATOM   5407 C C     . ILE B 1 310 ? -47.906 87.971 -18.305 1.00 32.65 ? 451 ILE B C     1 
ATOM   5408 O O     . ILE B 1 310 ? -47.332 87.916 -17.209 1.00 29.76 ? 451 ILE B O     1 
ATOM   5409 C CB    . ILE B 1 310 ? -47.634 85.825 -19.644 1.00 30.48 ? 451 ILE B CB    1 
ATOM   5410 C CG1   . ILE B 1 310 ? -46.582 85.223 -18.709 1.00 30.37 ? 451 ILE B CG1   1 
ATOM   5411 C CG2   . ILE B 1 310 ? -46.950 86.591 -20.770 1.00 29.36 ? 451 ILE B CG2   1 
ATOM   5412 C CD1   . ILE B 1 310 ? -47.153 84.307 -17.615 1.00 28.57 ? 451 ILE B CD1   1 
ATOM   5413 N N     . GLU B 1 311 ? -47.945 89.108 -19.016 1.00 31.63 ? 452 GLU B N     1 
ATOM   5414 C CA    . GLU B 1 311 ? -47.370 90.336 -18.450 1.00 35.21 ? 452 GLU B CA    1 
ATOM   5415 C C     . GLU B 1 311 ? -48.213 90.875 -17.295 1.00 28.70 ? 452 GLU B C     1 
ATOM   5416 O O     . GLU B 1 311 ? -47.667 91.407 -16.316 1.00 32.32 ? 452 GLU B O     1 
ATOM   5417 C CB    . GLU B 1 311 ? -47.192 91.425 -19.521 1.00 32.88 ? 452 GLU B CB    1 
ATOM   5418 C CG    . GLU B 1 311 ? -46.417 91.003 -20.781 1.00 38.96 ? 452 GLU B CG    1 
ATOM   5419 C CD    . GLU B 1 311 ? -47.213 90.100 -21.722 1.00 45.65 ? 452 GLU B CD    1 
ATOM   5420 O OE1   . GLU B 1 311 ? -48.279 89.569 -21.322 1.00 41.51 ? 452 GLU B OE1   1 
ATOM   5421 O OE2   . GLU B 1 311 ? -46.735 89.874 -22.854 1.00 48.51 ? 452 GLU B OE2   1 
ATOM   5422 N N     . ARG B 1 312 ? -49.541 90.753 -17.384 1.00 28.63 ? 453 ARG B N     1 
ATOM   5423 C CA    . ARG B 1 312 ? -50.383 91.155 -16.254 1.00 30.57 ? 453 ARG B CA    1 
ATOM   5424 C C     . ARG B 1 312 ? -50.174 90.238 -15.057 1.00 32.59 ? 453 ARG B C     1 
ATOM   5425 O O     . ARG B 1 312 ? -50.116 90.707 -13.911 1.00 33.38 ? 453 ARG B O     1 
ATOM   5426 C CB    . ARG B 1 312 ? -51.855 91.169 -16.659 1.00 33.04 ? 453 ARG B CB    1 
ATOM   5427 C CG    . ARG B 1 312 ? -52.158 91.956 -17.925 1.00 40.21 ? 453 ARG B CG    1 
ATOM   5428 C CD    . ARG B 1 312 ? -53.652 91.978 -18.212 1.00 39.98 ? 453 ARG B CD    1 
ATOM   5429 N NE    . ARG B 1 312 ? -54.450 92.515 -17.118 1.00 44.62 ? 453 ARG B NE    1 
ATOM   5430 C CZ    . ARG B 1 312 ? -55.488 91.895 -16.567 1.00 51.72 ? 453 ARG B CZ    1 
ATOM   5431 N NH1   . ARG B 1 312 ? -55.803 90.647 -16.893 1.00 44.00 ? 453 ARG B NH1   1 
ATOM   5432 N NH2   . ARG B 1 312 ? -56.224 92.541 -15.662 1.00 39.44 ? 453 ARG B NH2   1 
ATOM   5433 N N     . ILE B 1 313 ? -50.060 88.926 -15.305 1.00 29.82 ? 454 ILE B N     1 
ATOM   5434 C CA    . ILE B 1 313 ? -49.745 87.985 -14.233 1.00 32.65 ? 454 ILE B CA    1 
ATOM   5435 C C     . ILE B 1 313 ? -48.424 88.365 -13.579 1.00 31.11 ? 454 ILE B C     1 
ATOM   5436 O O     . ILE B 1 313 ? -48.308 88.400 -12.345 1.00 30.17 ? 454 ILE B O     1 
ATOM   5437 C CB    . ILE B 1 313 ? -49.714 86.540 -14.773 1.00 30.26 ? 454 ILE B CB    1 
ATOM   5438 C CG1   . ILE B 1 313 ? -51.132 85.964 -14.872 1.00 32.32 ? 454 ILE B CG1   1 
ATOM   5439 C CG2   . ILE B 1 313 ? -48.830 85.660 -13.898 1.00 30.65 ? 454 ILE B CG2   1 
ATOM   5440 C CD1   . ILE B 1 313 ? -51.313 84.905 -15.975 1.00 29.62 ? 454 ILE B CD1   1 
ATOM   5441 N N     . ALA B 1 314 ? -47.407 88.658 -14.402 1.00 28.77 ? 455 ALA B N     1 
ATOM   5442 C CA    . ALA B 1 314 ? -46.090 88.982 -13.867 1.00 28.26 ? 455 ALA B CA    1 
ATOM   5443 C C     . ALA B 1 314 ? -46.148 90.233 -13.002 1.00 30.12 ? 455 ALA B C     1 
ATOM   5444 O O     . ALA B 1 314 ? -45.584 90.257 -11.902 1.00 33.99 ? 455 ALA B O     1 
ATOM   5445 C CB    . ALA B 1 314 ? -45.076 89.154 -15.002 1.00 28.76 ? 455 ALA B CB    1 
ATOM   5446 N N     . ALA B 1 315 ? -46.853 91.269 -13.468 1.00 31.27 ? 456 ALA B N     1 
ATOM   5447 C CA    . ALA B 1 315 ? -46.972 92.499 -12.683 1.00 35.60 ? 456 ALA B CA    1 
ATOM   5448 C C     . ALA B 1 315 ? -47.692 92.250 -11.357 1.00 33.47 ? 456 ALA B C     1 
ATOM   5449 O O     . ALA B 1 315 ? -47.254 92.724 -10.295 1.00 36.31 ? 456 ALA B O     1 
ATOM   5450 C CB    . ALA B 1 315 ? -47.693 93.572 -13.503 1.00 33.40 ? 456 ALA B CB    1 
ATOM   5451 N N     . TYR B 1 316 ? -48.799 91.498 -11.393 1.00 33.85 ? 457 TYR B N     1 
ATOM   5452 C CA    . TYR B 1 316 ? -49.563 91.263 -10.171 1.00 31.40 ? 457 TYR B CA    1 
ATOM   5453 C C     . TYR B 1 316 ? -48.748 90.462 -9.158  1.00 34.77 ? 457 TYR B C     1 
ATOM   5454 O O     . TYR B 1 316 ? -48.680 90.815 -7.973  1.00 32.44 ? 457 TYR B O     1 
ATOM   5455 C CB    . TYR B 1 316 ? -50.879 90.553 -10.495 1.00 33.66 ? 457 TYR B CB    1 
ATOM   5456 C CG    . TYR B 1 316 ? -51.708 90.226 -9.271  1.00 34.54 ? 457 TYR B CG    1 
ATOM   5457 C CD1   . TYR B 1 316 ? -52.274 91.241 -8.500  1.00 37.94 ? 457 TYR B CD1   1 
ATOM   5458 C CD2   . TYR B 1 316 ? -51.923 88.911 -8.879  1.00 33.19 ? 457 TYR B CD2   1 
ATOM   5459 C CE1   . TYR B 1 316 ? -53.037 90.951 -7.379  1.00 34.54 ? 457 TYR B CE1   1 
ATOM   5460 C CE2   . TYR B 1 316 ? -52.684 88.609 -7.752  1.00 33.99 ? 457 TYR B CE2   1 
ATOM   5461 C CZ    . TYR B 1 316 ? -53.236 89.637 -7.005  1.00 36.71 ? 457 TYR B CZ    1 
ATOM   5462 O OH    . TYR B 1 316 ? -53.993 89.353 -5.887  1.00 30.45 ? 457 TYR B OH    1 
ATOM   5463 N N     . GLU B 1 317 ? -48.104 89.387 -9.618  1.00 29.84 ? 458 GLU B N     1 
ATOM   5464 C CA    . GLU B 1 317 ? -47.301 88.555 -8.730  1.00 31.27 ? 458 GLU B CA    1 
ATOM   5465 C C     . GLU B 1 317 ? -46.119 89.341 -8.167  1.00 33.67 ? 458 GLU B C     1 
ATOM   5466 O O     . GLU B 1 317 ? -45.736 89.151 -7.005  1.00 33.16 ? 458 GLU B O     1 
ATOM   5467 C CB    . GLU B 1 317 ? -46.829 87.309 -9.490  1.00 29.12 ? 458 GLU B CB    1 
ATOM   5468 C CG    . GLU B 1 317 ? -47.960 86.319 -9.821  1.00 30.04 ? 458 GLU B CG    1 
ATOM   5469 C CD    . GLU B 1 317 ? -47.486 85.112 -10.633 1.00 32.66 ? 458 GLU B CD    1 
ATOM   5470 O OE1   . GLU B 1 317 ? -46.345 85.153 -11.159 1.00 28.92 ? 458 GLU B OE1   1 
ATOM   5471 O OE2   . GLU B 1 317 ? -48.260 84.129 -10.768 1.00 27.92 ? 458 GLU B OE2   1 
ATOM   5472 N N     . HIS B 1 318 ? -45.518 90.220 -8.976  1.00 30.86 ? 459 HIS B N     1 
ATOM   5473 C CA    . HIS B 1 318 ? -44.471 91.087 -8.456  1.00 33.73 ? 459 HIS B CA    1 
ATOM   5474 C C     . HIS B 1 318 ? -45.007 91.956 -7.324  1.00 35.79 ? 459 HIS B C     1 
ATOM   5475 O O     . HIS B 1 318 ? -44.337 92.142 -6.297  1.00 35.43 ? 459 HIS B O     1 
ATOM   5476 C CB    . HIS B 1 318 ? -43.899 91.952 -9.582  1.00 35.83 ? 459 HIS B CB    1 
ATOM   5477 C CG    . HIS B 1 318 ? -42.835 92.906 -9.129  1.00 44.38 ? 459 HIS B CG    1 
ATOM   5478 N ND1   . HIS B 1 318 ? -41.524 92.524 -8.927  1.00 42.85 ? 459 HIS B ND1   1 
ATOM   5479 C CD2   . HIS B 1 318 ? -42.896 94.223 -8.813  1.00 44.91 ? 459 HIS B CD2   1 
ATOM   5480 C CE1   . HIS B 1 318 ? -40.821 93.568 -8.524  1.00 49.07 ? 459 HIS B CE1   1 
ATOM   5481 N NE2   . HIS B 1 318 ? -41.629 94.612 -8.447  1.00 45.31 ? 459 HIS B NE2   1 
ATOM   5482 N N     . ALA B 1 319 ? -46.221 92.487 -7.489  1.00 35.85 ? 460 ALA B N     1 
ATOM   5483 C CA    . ALA B 1 319 ? -46.837 93.244 -6.400  1.00 33.86 ? 460 ALA B CA    1 
ATOM   5484 C C     . ALA B 1 319 ? -47.002 92.378 -5.153  1.00 36.82 ? 460 ALA B C     1 
ATOM   5485 O O     . ALA B 1 319 ? -46.708 92.814 -4.037  1.00 36.16 ? 460 ALA B O     1 
ATOM   5486 C CB    . ALA B 1 319 ? -48.177 93.810 -6.847  1.00 31.88 ? 460 ALA B CB    1 
ATOM   5487 N N     . LEU B 1 320 ? -47.478 91.145 -5.324  1.00 36.48 ? 461 LEU B N     1 
ATOM   5488 C CA    . LEU B 1 320 ? -47.651 90.262 -4.170  1.00 37.79 ? 461 LEU B CA    1 
ATOM   5489 C C     . LEU B 1 320 ? -46.335 90.066 -3.423  1.00 36.44 ? 461 LEU B C     1 
ATOM   5490 O O     . LEU B 1 320 ? -46.270 90.215 -2.194  1.00 37.51 ? 461 LEU B O     1 
ATOM   5491 C CB    . LEU B 1 320 ? -48.206 88.910 -4.620  1.00 33.53 ? 461 LEU B CB    1 
ATOM   5492 C CG    . LEU B 1 320 ? -49.671 88.826 -5.033  1.00 33.81 ? 461 LEU B CG    1 
ATOM   5493 C CD1   . LEU B 1 320 ? -49.946 87.428 -5.565  1.00 33.78 ? 461 LEU B CD1   1 
ATOM   5494 C CD2   . LEU B 1 320 ? -50.613 89.162 -3.878  1.00 29.49 ? 461 LEU B CD2   1 
ATOM   5495 N N     . LEU B 1 321 ? -45.275 89.707 -4.156  1.00 34.94 ? 462 LEU B N     1 
ATOM   5496 C CA    . LEU B 1 321 ? -43.983 89.455 -3.525  1.00 34.21 ? 462 LEU B CA    1 
ATOM   5497 C C     . LEU B 1 321 ? -43.457 90.704 -2.828  1.00 36.08 ? 462 LEU B C     1 
ATOM   5498 O O     . LEU B 1 321 ? -42.917 90.624 -1.712  1.00 38.17 ? 462 LEU B O     1 
ATOM   5499 C CB    . LEU B 1 321 ? -42.981 88.959 -4.568  1.00 34.87 ? 462 LEU B CB    1 
ATOM   5500 C CG    . LEU B 1 321 ? -41.592 88.603 -4.044  1.00 34.50 ? 462 LEU B CG    1 
ATOM   5501 C CD1   . LEU B 1 321 ? -41.709 87.505 -2.995  1.00 33.18 ? 462 LEU B CD1   1 
ATOM   5502 C CD2   . LEU B 1 321 ? -40.669 88.168 -5.177  1.00 33.03 ? 462 LEU B CD2   1 
ATOM   5503 N N     . GLU B 1 322 ? -43.606 91.868 -3.478  1.00 31.38 ? 463 GLU B N     1 
ATOM   5504 C CA    . GLU B 1 322 ? -43.158 93.129 -2.893  1.00 39.27 ? 463 GLU B CA    1 
ATOM   5505 C C     . GLU B 1 322 ? -43.916 93.448 -1.615  1.00 40.01 ? 463 GLU B C     1 
ATOM   5506 O O     . GLU B 1 322 ? -43.338 93.973 -0.658  1.00 40.47 ? 463 GLU B O     1 
ATOM   5507 C CB    . GLU B 1 322 ? -43.345 94.269 -3.891  1.00 38.44 ? 463 GLU B CB    1 
ATOM   5508 C CG    . GLU B 1 322 ? -42.315 94.267 -4.970  1.00 45.67 ? 463 GLU B CG    1 
ATOM   5509 C CD    . GLU B 1 322 ? -41.053 94.959 -4.530  1.00 59.25 ? 463 GLU B CD    1 
ATOM   5510 O OE1   . GLU B 1 322 ? -41.135 96.139 -4.112  1.00 62.23 ? 463 GLU B OE1   1 
ATOM   5511 O OE2   . GLU B 1 322 ? -39.984 94.300 -4.581  1.00 56.57 ? 463 GLU B OE2   1 
ATOM   5512 N N     . TYR B 1 323 ? -45.223 93.179 -1.600  1.00 38.44 ? 464 TYR B N     1 
ATOM   5513 C CA    . TYR B 1 323 ? -46.019 93.397 -0.397  1.00 37.35 ? 464 TYR B CA    1 
ATOM   5514 C C     . TYR B 1 323 ? -45.553 92.485 0.731   1.00 41.39 ? 464 TYR B C     1 
ATOM   5515 O O     . TYR B 1 323 ? -45.382 92.931 1.873   1.00 39.08 ? 464 TYR B O     1 
ATOM   5516 C CB    . TYR B 1 323 ? -47.500 93.165 -0.714  1.00 39.05 ? 464 TYR B CB    1 
ATOM   5517 C CG    . TYR B 1 323 ? -48.471 93.387 0.446   1.00 42.50 ? 464 TYR B CG    1 
ATOM   5518 C CD1   . TYR B 1 323 ? -48.864 94.669 0.823   1.00 45.57 ? 464 TYR B CD1   1 
ATOM   5519 C CD2   . TYR B 1 323 ? -49.014 92.309 1.142   1.00 39.83 ? 464 TYR B CD2   1 
ATOM   5520 C CE1   . TYR B 1 323 ? -49.762 94.874 1.877   1.00 41.93 ? 464 TYR B CE1   1 
ATOM   5521 C CE2   . TYR B 1 323 ? -49.908 92.502 2.194   1.00 39.36 ? 464 TYR B CE2   1 
ATOM   5522 C CZ    . TYR B 1 323 ? -50.276 93.786 2.555   1.00 44.27 ? 464 TYR B CZ    1 
ATOM   5523 O OH    . TYR B 1 323 ? -51.162 93.977 3.594   1.00 40.33 ? 464 TYR B OH    1 
ATOM   5524 N N     . ALA B 1 324 ? -45.289 91.214 0.413   1.00 38.71 ? 465 ALA B N     1 
ATOM   5525 C CA    . ALA B 1 324 ? -45.034 90.226 1.459   1.00 37.73 ? 465 ALA B CA    1 
ATOM   5526 C C     . ALA B 1 324 ? -43.643 90.380 2.067   1.00 37.38 ? 465 ALA B C     1 
ATOM   5527 O O     . ALA B 1 324 ? -43.471 90.211 3.282   1.00 36.46 ? 465 ALA B O     1 
ATOM   5528 C CB    . ALA B 1 324 ? -45.221 88.812 0.898   1.00 37.62 ? 465 ALA B CB    1 
ATOM   5529 N N     . THR B 1 325 ? -42.640 90.712 1.250   1.00 37.35 ? 466 THR B N     1 
ATOM   5530 C CA    . THR B 1 325 ? -41.256 90.601 1.712   1.00 35.03 ? 466 THR B CA    1 
ATOM   5531 C C     . THR B 1 325 ? -40.916 91.502 2.900   1.00 37.39 ? 466 THR B C     1 
ATOM   5532 O O     . THR B 1 325 ? -40.341 90.992 3.883   1.00 37.55 ? 466 THR B O     1 
ATOM   5533 C CB    . THR B 1 325 ? -40.311 90.848 0.533   1.00 34.71 ? 466 THR B CB    1 
ATOM   5534 O OG1   . THR B 1 325 ? -40.532 89.845 -0.469  1.00 37.49 ? 466 THR B OG1   1 
ATOM   5535 C CG2   . THR B 1 325 ? -38.874 90.779 0.994   1.00 35.06 ? 466 THR B CG2   1 
ATOM   5536 N N     . PRO B 1 326 ? -41.211 92.813 2.895   1.00 36.36 ? 467 PRO B N     1 
ATOM   5537 C CA    . PRO B 1 326 ? -40.884 93.607 4.093   1.00 37.75 ? 467 PRO B CA    1 
ATOM   5538 C C     . PRO B 1 326 ? -41.712 93.231 5.308   1.00 40.63 ? 467 PRO B C     1 
ATOM   5539 O O     . PRO B 1 326 ? -41.210 93.315 6.439   1.00 37.78 ? 467 PRO B O     1 
ATOM   5540 C CB    . PRO B 1 326 ? -41.160 95.053 3.646   1.00 36.58 ? 467 PRO B CB    1 
ATOM   5541 C CG    . PRO B 1 326 ? -42.146 94.920 2.548   1.00 39.61 ? 467 PRO B CG    1 
ATOM   5542 C CD    . PRO B 1 326 ? -41.719 93.681 1.815   1.00 35.46 ? 467 PRO B CD    1 
ATOM   5543 N N     . ARG B 1 327 ? -42.973 92.832 5.113   1.00 39.26 ? 468 ARG B N     1 
ATOM   5544 C CA    . ARG B 1 327 ? -43.817 92.517 6.262   1.00 39.69 ? 468 ARG B CA    1 
ATOM   5545 C C     . ARG B 1 327 ? -43.353 91.241 6.947   1.00 40.80 ? 468 ARG B C     1 
ATOM   5546 O O     . ARG B 1 327 ? -43.348 91.156 8.180   1.00 40.54 ? 468 ARG B O     1 
ATOM   5547 C CB    . ARG B 1 327 ? -45.278 92.402 5.836   1.00 36.75 ? 468 ARG B CB    1 
ATOM   5548 C CG    . ARG B 1 327 ? -45.872 93.723 5.444   1.00 39.99 ? 468 ARG B CG    1 
ATOM   5549 C CD    . ARG B 1 327 ? -47.105 93.589 4.582   1.00 41.69 ? 468 ARG B CD    1 
ATOM   5550 N NE    . ARG B 1 327 ? -47.698 94.905 4.375   1.00 43.49 ? 468 ARG B NE    1 
ATOM   5551 C CZ    . ARG B 1 327 ? -47.240 95.815 3.524   1.00 45.37 ? 468 ARG B CZ    1 
ATOM   5552 N NH1   . ARG B 1 327 ? -46.251 95.544 2.682   1.00 37.82 ? 468 ARG B NH1   1 
ATOM   5553 N NH2   . ARG B 1 327 ? -47.797 97.023 3.508   1.00 44.86 ? 468 ARG B NH2   1 
ATOM   5554 N N     . LEU B 1 328 ? -42.963 90.239 6.162   1.00 38.75 ? 469 LEU B N     1 
ATOM   5555 C CA    . LEU B 1 328 ? -42.374 89.040 6.739   1.00 36.09 ? 469 LEU B CA    1 
ATOM   5556 C C     . LEU B 1 328 ? -41.025 89.346 7.373   1.00 35.42 ? 469 LEU B C     1 
ATOM   5557 O O     . LEU B 1 328 ? -40.722 88.852 8.466   1.00 39.24 ? 469 LEU B O     1 
ATOM   5558 C CB    . LEU B 1 328 ? -42.225 87.961 5.664   1.00 32.64 ? 469 LEU B CB    1 
ATOM   5559 C CG    . LEU B 1 328 ? -41.500 86.691 6.110   1.00 35.49 ? 469 LEU B CG    1 
ATOM   5560 C CD1   . LEU B 1 328 ? -42.336 85.948 7.143   1.00 34.07 ? 469 LEU B CD1   1 
ATOM   5561 C CD2   . LEU B 1 328 ? -41.189 85.787 4.906   1.00 36.23 ? 469 LEU B CD2   1 
ATOM   5562 N N     . ALA B 1 329 ? -40.201 90.161 6.706   1.00 34.87 ? 470 ALA B N     1 
ATOM   5563 C CA    . ALA B 1 329 ? -38.854 90.433 7.199   1.00 37.01 ? 470 ALA B CA    1 
ATOM   5564 C C     . ALA B 1 329 ? -38.857 91.200 8.515   1.00 43.43 ? 470 ALA B C     1 
ATOM   5565 O O     . ALA B 1 329 ? -37.873 91.136 9.264   1.00 39.39 ? 470 ALA B O     1 
ATOM   5566 C CB    . ALA B 1 329 ? -38.062 91.215 6.150   1.00 34.02 ? 470 ALA B CB    1 
ATOM   5567 N N     . ALA B 1 330 ? -39.938 91.916 8.810   1.00 42.57 ? 471 ALA B N     1 
ATOM   5568 C CA    . ALA B 1 330 ? -40.029 92.736 10.009  1.00 40.92 ? 471 ALA B CA    1 
ATOM   5569 C C     . ALA B 1 330 ? -40.354 91.928 11.258  1.00 45.04 ? 471 ALA B C     1 
ATOM   5570 O O     . ALA B 1 330 ? -40.291 92.475 12.368  1.00 43.94 ? 471 ALA B O     1 
ATOM   5571 C CB    . ALA B 1 330 ? -41.080 93.826 9.805   1.00 39.71 ? 471 ALA B CB    1 
ATOM   5572 N N     . ILE B 1 331 ? -40.693 90.656 11.111  1.00 39.02 ? 472 ILE B N     1 
ATOM   5573 C CA    . ILE B 1 331 ? -41.009 89.839 12.286  1.00 45.21 ? 472 ILE B CA    1 
ATOM   5574 C C     . ILE B 1 331 ? -39.714 89.484 13.008  1.00 44.95 ? 472 ILE B C     1 
ATOM   5575 O O     . ILE B 1 331 ? -38.789 88.935 12.380  1.00 40.29 ? 472 ILE B O     1 
ATOM   5576 C CB    . ILE B 1 331 ? -41.767 88.580 11.874  1.00 42.92 ? 472 ILE B CB    1 
ATOM   5577 C CG1   . ILE B 1 331 ? -43.112 88.961 11.251  1.00 42.58 ? 472 ILE B CG1   1 
ATOM   5578 C CG2   . ILE B 1 331 ? -41.958 87.676 13.091  1.00 39.57 ? 472 ILE B CG2   1 
ATOM   5579 C CD1   . ILE B 1 331 ? -43.926 87.790 10.769  1.00 35.71 ? 472 ILE B CD1   1 
ATOM   5580 N N     . PRO B 1 332 ? -39.591 89.780 14.301  1.00 45.14 ? 473 PRO B N     1 
ATOM   5581 C CA    . PRO B 1 332 ? -38.384 89.380 15.036  1.00 46.78 ? 473 PRO B CA    1 
ATOM   5582 C C     . PRO B 1 332 ? -38.184 87.872 14.971  1.00 43.11 ? 473 PRO B C     1 
ATOM   5583 O O     . PRO B 1 332 ? -39.120 87.095 15.164  1.00 44.70 ? 473 PRO B O     1 
ATOM   5584 C CB    . PRO B 1 332 ? -38.666 89.862 16.467  1.00 47.05 ? 473 PRO B CB    1 
ATOM   5585 C CG    . PRO B 1 332 ? -40.159 90.016 16.528  1.00 50.21 ? 473 PRO B CG    1 
ATOM   5586 C CD    . PRO B 1 332 ? -40.554 90.481 15.165  1.00 47.19 ? 473 PRO B CD    1 
ATOM   5587 N N     . GLY B 1 333 ? -36.948 87.464 14.676  1.00 38.23 ? 474 GLY B N     1 
ATOM   5588 C CA    . GLY B 1 333 ? -36.602 86.080 14.472  1.00 38.70 ? 474 GLY B CA    1 
ATOM   5589 C C     . GLY B 1 333 ? -36.485 85.673 13.012  1.00 38.15 ? 474 GLY B C     1 
ATOM   5590 O O     . GLY B 1 333 ? -35.748 84.728 12.701  1.00 35.66 ? 474 GLY B O     1 
ATOM   5591 N N     . VAL B 1 334 ? -37.178 86.362 12.112  1.00 35.12 ? 475 VAL B N     1 
ATOM   5592 C CA    . VAL B 1 334 ? -37.257 85.920 10.723  1.00 36.63 ? 475 VAL B CA    1 
ATOM   5593 C C     . VAL B 1 334 ? -36.033 86.410 9.960   1.00 39.88 ? 475 VAL B C     1 
ATOM   5594 O O     . VAL B 1 334 ? -35.636 87.577 10.076  1.00 37.98 ? 475 VAL B O     1 
ATOM   5595 C CB    . VAL B 1 334 ? -38.551 86.415 10.057  1.00 40.16 ? 475 VAL B CB    1 
ATOM   5596 C CG1   . VAL B 1 334 ? -38.396 86.439 8.524   1.00 36.31 ? 475 VAL B CG1   1 
ATOM   5597 C CG2   . VAL B 1 334 ? -39.731 85.547 10.461  1.00 39.74 ? 475 VAL B CG2   1 
ATOM   5598 N N     . ARG B 1 335 ? -35.440 85.517 9.166   1.00 39.12 ? 476 ARG B N     1 
ATOM   5599 C CA    . ARG B 1 335 ? -34.410 85.868 8.195   1.00 35.78 ? 476 ARG B CA    1 
ATOM   5600 C C     . ARG B 1 335 ? -34.885 85.468 6.801   1.00 39.03 ? 476 ARG B C     1 
ATOM   5601 O O     . ARG B 1 335 ? -35.333 84.332 6.601   1.00 33.34 ? 476 ARG B O     1 
ATOM   5602 C CB    . ARG B 1 335 ? -33.081 85.174 8.521   1.00 38.24 ? 476 ARG B CB    1 
ATOM   5603 C CG    . ARG B 1 335 ? -31.989 85.406 7.476   1.00 42.14 ? 476 ARG B CG    1 
ATOM   5604 C CD    . ARG B 1 335 ? -31.013 84.231 7.378   1.00 44.65 ? 476 ARG B CD    1 
ATOM   5605 N NE    . ARG B 1 335 ? -30.325 84.220 6.089   1.00 49.14 ? 476 ARG B NE    1 
ATOM   5606 C CZ    . ARG B 1 335 ? -29.380 83.354 5.747   1.00 51.61 ? 476 ARG B CZ    1 
ATOM   5607 N NH1   . ARG B 1 335 ? -28.975 82.409 6.582   1.00 50.55 ? 476 ARG B NH1   1 
ATOM   5608 N NH2   . ARG B 1 335 ? -28.822 83.445 4.539   1.00 45.41 ? 476 ARG B NH2   1 
ATOM   5609 N N     . ILE B 1 336 ? -34.803 86.400 5.846   1.00 35.26 ? 477 ILE B N     1 
ATOM   5610 C CA    . ILE B 1 336 ? -35.156 86.105 4.457   1.00 36.11 ? 477 ILE B CA    1 
ATOM   5611 C C     . ILE B 1 336 ? -33.981 85.412 3.783   1.00 35.61 ? 477 ILE B C     1 
ATOM   5612 O O     . ILE B 1 336 ? -32.830 85.850 3.918   1.00 35.70 ? 477 ILE B O     1 
ATOM   5613 C CB    . ILE B 1 336 ? -35.538 87.386 3.697   1.00 36.41 ? 477 ILE B CB    1 
ATOM   5614 C CG1   . ILE B 1 336 ? -36.653 88.145 4.429   1.00 37.53 ? 477 ILE B CG1   1 
ATOM   5615 C CG2   . ILE B 1 336 ? -35.921 87.046 2.261   1.00 34.41 ? 477 ILE B CG2   1 
ATOM   5616 C CD1   . ILE B 1 336 ? -37.911 87.343 4.643   1.00 34.06 ? 477 ILE B CD1   1 
ATOM   5617 N N     . VAL B 1 337 ? -34.264 84.335 3.046   1.00 34.18 ? 478 VAL B N     1 
ATOM   5618 C CA    . VAL B 1 337 ? -33.244 83.555 2.352   1.00 32.40 ? 478 VAL B CA    1 
ATOM   5619 C C     . VAL B 1 337 ? -33.447 83.736 0.850   1.00 31.29 ? 478 VAL B C     1 
ATOM   5620 O O     . VAL B 1 337 ? -34.395 83.199 0.263   1.00 28.46 ? 478 VAL B O     1 
ATOM   5621 C CB    . VAL B 1 337 ? -33.293 82.076 2.751   1.00 34.28 ? 478 VAL B CB    1 
ATOM   5622 C CG1   . VAL B 1 337 ? -32.163 81.308 2.084   1.00 32.94 ? 478 VAL B CG1   1 
ATOM   5623 C CG2   . VAL B 1 337 ? -33.216 81.946 4.263   1.00 36.78 ? 478 VAL B CG2   1 
ATOM   5624 N N     . GLY B 1 338 ? -32.547 84.480 0.222   1.00 32.52 ? 479 GLY B N     1 
ATOM   5625 C CA    . GLY B 1 338 ? -32.710 84.823 -1.176  1.00 30.91 ? 479 GLY B CA    1 
ATOM   5626 C C     . GLY B 1 338 ? -33.249 86.228 -1.344  1.00 32.36 ? 479 GLY B C     1 
ATOM   5627 O O     . GLY B 1 338 ? -34.466 86.448 -1.284  1.00 29.04 ? 479 GLY B O     1 
ATOM   5628 N N     . THR B 1 339 ? -32.348 87.193 -1.528  1.00 31.71 ? 480 THR B N     1 
ATOM   5629 C CA    . THR B 1 339 ? -32.712 88.595 -1.703  1.00 34.93 ? 480 THR B CA    1 
ATOM   5630 C C     . THR B 1 339 ? -32.058 89.140 -2.966  1.00 33.63 ? 480 THR B C     1 
ATOM   5631 O O     . THR B 1 339 ? -31.414 90.193 -2.971  1.00 34.41 ? 480 THR B O     1 
ATOM   5632 C CB    . THR B 1 339 ? -32.306 89.420 -0.484  1.00 36.91 ? 480 THR B CB    1 
ATOM   5633 O OG1   . THR B 1 339 ? -30.966 89.092 -0.101  1.00 38.07 ? 480 THR B OG1   1 
ATOM   5634 C CG2   . THR B 1 339 ? -33.215 89.072 0.690   1.00 38.91 ? 480 THR B CG2   1 
ATOM   5635 N N     . ALA B 1 340 ? -32.191 88.388 -4.055  1.00 31.78 ? 481 ALA B N     1 
ATOM   5636 C CA    . ALA B 1 340 ? -31.554 88.739 -5.313  1.00 36.75 ? 481 ALA B CA    1 
ATOM   5637 C C     . ALA B 1 340 ? -32.156 90.018 -5.889  1.00 36.79 ? 481 ALA B C     1 
ATOM   5638 O O     . ALA B 1 340 ? -33.256 90.441 -5.525  1.00 33.46 ? 481 ALA B O     1 
ATOM   5639 C CB    . ALA B 1 340 ? -31.694 87.595 -6.322  1.00 29.95 ? 481 ALA B CB    1 
ATOM   5640 N N     . GLN B 1 341 ? -31.415 90.626 -6.817  1.00 32.73 ? 482 GLN B N     1 
ATOM   5641 C CA    . GLN B 1 341 ? -31.855 91.879 -7.415  1.00 37.45 ? 482 GLN B CA    1 
ATOM   5642 C C     . GLN B 1 341 ? -33.186 91.726 -8.143  1.00 37.73 ? 482 GLN B C     1 
ATOM   5643 O O     . GLN B 1 341 ? -33.977 92.673 -8.191  1.00 37.56 ? 482 GLN B O     1 
ATOM   5644 C CB    . GLN B 1 341 ? -30.776 92.401 -8.367  1.00 38.47 ? 482 GLN B CB    1 
ATOM   5645 C CG    . GLN B 1 341 ? -29.801 93.352 -7.689  1.00 48.70 ? 482 GLN B CG    1 
ATOM   5646 C CD    . GLN B 1 341 ? -30.479 94.248 -6.666  1.00 51.15 ? 482 GLN B CD    1 
ATOM   5647 O OE1   . GLN B 1 341 ? -30.055 94.317 -5.510  1.00 52.54 ? 482 GLN B OE1   1 
ATOM   5648 N NE2   . GLN B 1 341 ? -31.511 94.978 -7.101  1.00 56.97 ? 482 GLN B NE2   1 
ATOM   5649 N N     . GLU B 1 342 ? -33.444 90.557 -8.724  1.00 34.32 ? 483 GLU B N     1 
ATOM   5650 C CA    . GLU B 1 342 ? -34.685 90.279 -9.433  1.00 36.03 ? 483 GLU B CA    1 
ATOM   5651 C C     . GLU B 1 342 ? -35.206 88.927 -8.968  1.00 34.03 ? 483 GLU B C     1 
ATOM   5652 O O     . GLU B 1 342 ? -34.471 87.936 -9.016  1.00 32.18 ? 483 GLU B O     1 
ATOM   5653 C CB    . GLU B 1 342 ? -34.456 90.278 -10.952 1.00 40.13 ? 483 GLU B CB    1 
ATOM   5654 C CG    . GLU B 1 342 ? -34.731 91.626 -11.635 1.00 49.41 ? 483 GLU B CG    1 
ATOM   5655 C CD    . GLU B 1 342 ? -36.187 92.070 -11.525 1.00 64.11 ? 483 GLU B CD    1 
ATOM   5656 O OE1   . GLU B 1 342 ? -36.517 92.843 -10.594 1.00 64.77 ? 483 GLU B OE1   1 
ATOM   5657 O OE2   . GLU B 1 342 ? -37.000 91.646 -12.382 1.00 70.17 ? 483 GLU B OE2   1 
ATOM   5658 N N     . LYS B 1 343 ? -36.460 88.886 -8.511  1.00 28.70 ? 484 LYS B N     1 
ATOM   5659 C CA    . LYS B 1 343 ? -37.051 87.674 -7.972  1.00 30.67 ? 484 LYS B CA    1 
ATOM   5660 C C     . LYS B 1 343 ? -38.409 87.432 -8.610  1.00 34.09 ? 484 LYS B C     1 
ATOM   5661 O O     . LYS B 1 343 ? -39.057 88.357 -9.104  1.00 31.88 ? 484 LYS B O     1 
ATOM   5662 C CB    . LYS B 1 343 ? -37.213 87.753 -6.448  1.00 30.59 ? 484 LYS B CB    1 
ATOM   5663 C CG    . LYS B 1 343 ? -35.910 87.724 -5.678  1.00 31.37 ? 484 LYS B CG    1 
ATOM   5664 C CD    . LYS B 1 343 ? -36.140 87.650 -4.176  1.00 33.24 ? 484 LYS B CD    1 
ATOM   5665 C CE    . LYS B 1 343 ? -37.292 86.704 -3.830  1.00 34.37 ? 484 LYS B CE    1 
ATOM   5666 N NZ    . LYS B 1 343 ? -37.245 86.292 -2.394  1.00 35.15 ? 484 LYS B NZ    1 
ATOM   5667 N N     . ALA B 1 344 ? -38.840 86.169 -8.584  1.00 31.65 ? 485 ALA B N     1 
ATOM   5668 C CA    . ALA B 1 344 ? -40.201 85.806 -8.962  1.00 31.11 ? 485 ALA B CA    1 
ATOM   5669 C C     . ALA B 1 344 ? -40.751 84.772 -7.987  1.00 34.15 ? 485 ALA B C     1 
ATOM   5670 O O     . ALA B 1 344 ? -40.091 83.765 -7.711  1.00 29.53 ? 485 ALA B O     1 
ATOM   5671 C CB    . ALA B 1 344 ? -40.254 85.254 -10.388 1.00 28.55 ? 485 ALA B CB    1 
ATOM   5672 N N     . SER B 1 345 ? -41.941 85.051 -7.443  1.00 34.76 ? 486 SER B N     1 
ATOM   5673 C CA    . SER B 1 345 ? -42.807 84.080 -6.769  1.00 33.08 ? 486 SER B CA    1 
ATOM   5674 C C     . SER B 1 345 ? -42.345 83.620 -5.383  1.00 31.72 ? 486 SER B C     1 
ATOM   5675 O O     . SER B 1 345 ? -43.122 83.689 -4.428  1.00 32.41 ? 486 SER B O     1 
ATOM   5676 C CB    . SER B 1 345 ? -43.010 82.851 -7.667  1.00 33.16 ? 486 SER B CB    1 
ATOM   5677 O OG    . SER B 1 345 ? -44.018 81.996 -7.137  1.00 34.54 ? 486 SER B OG    1 
ATOM   5678 N N     . VAL B 1 346 ? -41.103 83.148 -5.261  1.00 30.97 ? 487 VAL B N     1 
ATOM   5679 C CA    . VAL B 1 346 ? -40.643 82.401 -4.092  1.00 28.78 ? 487 VAL B CA    1 
ATOM   5680 C C     . VAL B 1 346 ? -40.186 83.354 -2.992  1.00 30.86 ? 487 VAL B C     1 
ATOM   5681 O O     . VAL B 1 346 ? -39.536 84.369 -3.259  1.00 32.41 ? 487 VAL B O     1 
ATOM   5682 C CB    . VAL B 1 346 ? -39.509 81.445 -4.507  1.00 32.77 ? 487 VAL B CB    1 
ATOM   5683 C CG1   . VAL B 1 346 ? -38.742 80.924 -3.293  1.00 27.38 ? 487 VAL B CG1   1 
ATOM   5684 C CG2   . VAL B 1 346 ? -40.063 80.294 -5.339  1.00 29.91 ? 487 VAL B CG2   1 
ATOM   5685 N N     . LEU B 1 347 ? -40.505 83.017 -1.721  1.00 30.13 ? 488 LEU B N     1 
ATOM   5686 C CA    . LEU B 1 347 ? -40.067 83.813 -0.566  1.00 29.69 ? 488 LEU B CA    1 
ATOM   5687 C C     . LEU B 1 347 ? -39.624 82.855 0.549   1.00 33.01 ? 488 LEU B C     1 
ATOM   5688 O O     . LEU B 1 347 ? -40.366 82.588 1.501   1.00 34.25 ? 488 LEU B O     1 
ATOM   5689 C CB    . LEU B 1 347 ? -41.176 84.745 -0.093  1.00 29.86 ? 488 LEU B CB    1 
ATOM   5690 C CG    . LEU B 1 347 ? -40.850 85.713 1.048   1.00 32.08 ? 488 LEU B CG    1 
ATOM   5691 C CD1   . LEU B 1 347 ? -39.633 86.567 0.702   1.00 31.17 ? 488 LEU B CD1   1 
ATOM   5692 C CD2   . LEU B 1 347 ? -42.049 86.584 1.326   1.00 31.59 ? 488 LEU B CD2   1 
ATOM   5693 N N     . SER B 1 348 ? -38.401 82.343 0.435   1.00 29.91 ? 489 SER B N     1 
ATOM   5694 C CA    . SER B 1 348 ? -37.833 81.504 1.484   1.00 29.01 ? 489 SER B CA    1 
ATOM   5695 C C     . SER B 1 348 ? -37.460 82.325 2.714   1.00 30.86 ? 489 SER B C     1 
ATOM   5696 O O     . SER B 1 348 ? -36.996 83.463 2.611   1.00 30.41 ? 489 SER B O     1 
ATOM   5697 C CB    . SER B 1 348 ? -36.586 80.778 0.981   1.00 29.66 ? 489 SER B CB    1 
ATOM   5698 O OG    . SER B 1 348 ? -36.885 79.478 0.520   1.00 30.53 ? 489 SER B OG    1 
ATOM   5699 N N     . PHE B 1 349 ? -37.621 81.710 3.888   1.00 28.65 ? 490 PHE B N     1 
ATOM   5700 C CA    . PHE B 1 349 ? -37.184 82.318 5.137   1.00 30.01 ? 490 PHE B CA    1 
ATOM   5701 C C     . PHE B 1 349 ? -36.933 81.231 6.178   1.00 31.97 ? 490 PHE B C     1 
ATOM   5702 O O     . PHE B 1 349 ? -37.295 80.064 6.001   1.00 29.66 ? 490 PHE B O     1 
ATOM   5703 C CB    . PHE B 1 349 ? -38.207 83.345 5.644   1.00 29.15 ? 490 PHE B CB    1 
ATOM   5704 C CG    . PHE B 1 349 ? -39.475 82.735 6.204   1.00 31.80 ? 490 PHE B CG    1 
ATOM   5705 C CD1   . PHE B 1 349 ? -40.485 82.288 5.362   1.00 27.46 ? 490 PHE B CD1   1 
ATOM   5706 C CD2   . PHE B 1 349 ? -39.664 82.632 7.579   1.00 31.93 ? 490 PHE B CD2   1 
ATOM   5707 C CE1   . PHE B 1 349 ? -41.651 81.749 5.871   1.00 30.02 ? 490 PHE B CE1   1 
ATOM   5708 C CE2   . PHE B 1 349 ? -40.836 82.083 8.102   1.00 29.38 ? 490 PHE B CE2   1 
ATOM   5709 C CZ    . PHE B 1 349 ? -41.831 81.638 7.247   1.00 31.44 ? 490 PHE B CZ    1 
ATOM   5710 N N     . VAL B 1 350 ? -36.274 81.635 7.263   1.00 27.36 ? 491 VAL B N     1 
ATOM   5711 C CA    . VAL B 1 350 ? -36.116 80.801 8.448   1.00 31.46 ? 491 VAL B CA    1 
ATOM   5712 C C     . VAL B 1 350 ? -36.526 81.631 9.658   1.00 34.01 ? 491 VAL B C     1 
ATOM   5713 O O     . VAL B 1 350 ? -36.585 82.863 9.603   1.00 36.55 ? 491 VAL B O     1 
ATOM   5714 C CB    . VAL B 1 350 ? -34.677 80.254 8.629   1.00 33.89 ? 491 VAL B CB    1 
ATOM   5715 C CG1   . VAL B 1 350 ? -34.384 79.145 7.622   1.00 34.78 ? 491 VAL B CG1   1 
ATOM   5716 C CG2   . VAL B 1 350 ? -33.643 81.378 8.527   1.00 37.75 ? 491 VAL B CG2   1 
ATOM   5717 N N     . LEU B 1 351 ? -36.806 80.941 10.763  1.00 34.76 ? 492 LEU B N     1 
ATOM   5718 C CA    . LEU B 1 351 ? -37.267 81.584 11.992  1.00 34.81 ? 492 LEU B CA    1 
ATOM   5719 C C     . LEU B 1 351 ? -36.458 81.064 13.173  1.00 34.27 ? 492 LEU B C     1 
ATOM   5720 O O     . LEU B 1 351 ? -36.473 79.860 13.453  1.00 34.58 ? 492 LEU B O     1 
ATOM   5721 C CB    . LEU B 1 351 ? -38.763 81.331 12.201  1.00 37.30 ? 492 LEU B CB    1 
ATOM   5722 C CG    . LEU B 1 351 ? -39.418 81.827 13.496  1.00 39.33 ? 492 LEU B CG    1 
ATOM   5723 C CD1   . LEU B 1 351 ? -39.254 83.329 13.660  1.00 36.42 ? 492 LEU B CD1   1 
ATOM   5724 C CD2   . LEU B 1 351 ? -40.880 81.443 13.479  1.00 35.37 ? 492 LEU B CD2   1 
ATOM   5725 N N     . ALA B 1 352 ? -35.759 81.969 13.861  1.00 32.90 ? 493 ALA B N     1 
ATOM   5726 C CA    . ALA B 1 352 ? -34.922 81.593 14.995  1.00 36.65 ? 493 ALA B CA    1 
ATOM   5727 C C     . ALA B 1 352 ? -35.711 80.801 16.035  1.00 38.48 ? 493 ALA B C     1 
ATOM   5728 O O     . ALA B 1 352 ? -36.852 81.134 16.363  1.00 39.90 ? 493 ALA B O     1 
ATOM   5729 C CB    . ALA B 1 352 ? -34.330 82.845 15.642  1.00 40.80 ? 493 ALA B CB    1 
ATOM   5730 N N     . GLY B 1 353 ? -35.102 79.728 16.537  1.00 41.71 ? 494 GLY B N     1 
ATOM   5731 C CA    . GLY B 1 353 ? -35.721 78.917 17.567  1.00 39.27 ? 494 GLY B CA    1 
ATOM   5732 C C     . GLY B 1 353 ? -36.774 77.945 17.085  1.00 44.73 ? 494 GLY B C     1 
ATOM   5733 O O     . GLY B 1 353 ? -37.452 77.328 17.919  1.00 41.73 ? 494 GLY B O     1 
ATOM   5734 N N     . HIS B 1 354 ? -36.930 77.780 15.772  1.00 37.33 ? 495 HIS B N     1 
ATOM   5735 C CA    . HIS B 1 354 ? -37.934 76.888 15.206  1.00 39.58 ? 495 HIS B CA    1 
ATOM   5736 C C     . HIS B 1 354 ? -37.355 76.167 14.004  1.00 40.01 ? 495 HIS B C     1 
ATOM   5737 O O     . HIS B 1 354 ? -36.718 76.791 13.151  1.00 38.11 ? 495 HIS B O     1 
ATOM   5738 C CB    . HIS B 1 354 ? -39.189 77.653 14.770  1.00 38.16 ? 495 HIS B CB    1 
ATOM   5739 C CG    . HIS B 1 354 ? -39.910 78.322 15.896  1.00 44.08 ? 495 HIS B CG    1 
ATOM   5740 N ND1   . HIS B 1 354 ? -40.949 77.721 16.571  1.00 44.33 ? 495 HIS B ND1   1 
ATOM   5741 C CD2   . HIS B 1 354 ? -39.737 79.537 16.471  1.00 38.62 ? 495 HIS B CD2   1 
ATOM   5742 C CE1   . HIS B 1 354 ? -41.394 78.540 17.507  1.00 44.59 ? 495 HIS B CE1   1 
ATOM   5743 N NE2   . HIS B 1 354 ? -40.677 79.648 17.467  1.00 45.55 ? 495 HIS B NE2   1 
ATOM   5744 N N     . GLU B 1 355 ? -37.593 74.852 13.930  1.00 38.66 ? 496 GLU B N     1 
ATOM   5745 C CA    . GLU B 1 355 ? -37.186 74.108 12.743  1.00 40.68 ? 496 GLU B CA    1 
ATOM   5746 C C     . GLU B 1 355 ? -38.213 74.321 11.629  1.00 38.14 ? 496 GLU B C     1 
ATOM   5747 O O     . GLU B 1 355 ? -39.421 74.331 11.892  1.00 35.04 ? 496 GLU B O     1 
ATOM   5748 C CB    . GLU B 1 355 ? -37.044 72.617 13.062  1.00 43.38 ? 496 GLU B CB    1 
ATOM   5749 C CG    . GLU B 1 355 ? -36.192 71.799 12.062  1.00 50.66 ? 496 GLU B CG    1 
ATOM   5750 C CD    . GLU B 1 355 ? -37.017 71.043 10.995  1.00 56.50 ? 496 GLU B CD    1 
ATOM   5751 O OE1   . GLU B 1 355 ? -37.611 69.988 11.351  1.00 56.80 ? 496 GLU B OE1   1 
ATOM   5752 O OE2   . GLU B 1 355 ? -37.045 71.474 9.806   1.00 47.28 ? 496 GLU B OE2   1 
ATOM   5753 N N     . PRO B 1 356 ? -37.758 74.513 10.387  1.00 41.55 ? 497 PRO B N     1 
ATOM   5754 C CA    . PRO B 1 356 ? -38.698 74.794 9.285   1.00 37.75 ? 497 PRO B CA    1 
ATOM   5755 C C     . PRO B 1 356 ? -39.902 73.859 9.187   1.00 33.25 ? 497 PRO B C     1 
ATOM   5756 O O     . PRO B 1 356 ? -41.015 74.347 8.963   1.00 32.69 ? 497 PRO B O     1 
ATOM   5757 C CB    . PRO B 1 356 ? -37.790 74.690 8.056   1.00 34.44 ? 497 PRO B CB    1 
ATOM   5758 C CG    . PRO B 1 356 ? -36.491 75.211 8.551   1.00 35.37 ? 497 PRO B CG    1 
ATOM   5759 C CD    . PRO B 1 356 ? -36.360 74.731 9.973   1.00 38.37 ? 497 PRO B CD    1 
ATOM   5760 N N     . LEU B 1 357 ? -39.727 72.541 9.343   1.00 36.93 ? 498 LEU B N     1 
ATOM   5761 C CA    . LEU B 1 357 ? -40.853 71.623 9.152   1.00 33.18 ? 498 LEU B CA    1 
ATOM   5762 C C     . LEU B 1 357 ? -41.952 71.868 10.180  1.00 39.89 ? 498 LEU B C     1 
ATOM   5763 O O     . LEU B 1 357 ? -43.147 71.825 9.845   1.00 35.78 ? 498 LEU B O     1 
ATOM   5764 C CB    . LEU B 1 357 ? -40.375 70.171 9.223   1.00 38.36 ? 498 LEU B CB    1 
ATOM   5765 C CG    . LEU B 1 357 ? -41.466 69.096 9.347   1.00 49.36 ? 498 LEU B CG    1 
ATOM   5766 C CD1   . LEU B 1 357 ? -42.439 69.086 8.139   1.00 41.97 ? 498 LEU B CD1   1 
ATOM   5767 C CD2   . LEU B 1 357 ? -40.856 67.715 9.572   1.00 53.21 ? 498 LEU B CD2   1 
ATOM   5768 N N     . GLU B 1 358 ? -41.567 72.123 11.443  1.00 35.47 ? 499 GLU B N     1 
ATOM   5769 C CA    . GLU B 1 358 ? -42.555 72.451 12.469  1.00 35.04 ? 499 GLU B CA    1 
ATOM   5770 C C     . GLU B 1 358 ? -43.277 73.752 12.133  1.00 32.36 ? 499 GLU B C     1 
ATOM   5771 O O     . GLU B 1 358 ? -44.487 73.881 12.374  1.00 31.71 ? 499 GLU B O     1 
ATOM   5772 C CB    . GLU B 1 358 ? -41.889 72.518 13.860  1.00 36.47 ? 499 GLU B CB    1 
ATOM   5773 C CG    . GLU B 1 358 ? -41.359 73.908 14.268  1.00 44.14 ? 499 GLU B CG    1 
ATOM   5774 C CD    . GLU B 1 358 ? -40.986 74.060 15.751  1.00 51.41 ? 499 GLU B CD    1 
ATOM   5775 O OE1   . GLU B 1 358 ? -41.903 74.153 16.595  1.00 56.25 ? 499 GLU B OE1   1 
ATOM   5776 O OE2   . GLU B 1 358 ? -39.769 74.107 16.069  1.00 49.03 ? 499 GLU B OE2   1 
ATOM   5777 N N     . VAL B 1 359 ? -42.562 74.720 11.550  1.00 33.43 ? 500 VAL B N     1 
ATOM   5778 C CA    . VAL B 1 359 ? -43.214 75.950 11.110  1.00 33.82 ? 500 VAL B CA    1 
ATOM   5779 C C     . VAL B 1 359 ? -44.228 75.644 10.017  1.00 32.02 ? 500 VAL B C     1 
ATOM   5780 O O     . VAL B 1 359 ? -45.345 76.172 10.023  1.00 29.75 ? 500 VAL B O     1 
ATOM   5781 C CB    . VAL B 1 359 ? -42.171 76.980 10.643  1.00 33.13 ? 500 VAL B CB    1 
ATOM   5782 C CG1   . VAL B 1 359 ? -42.871 78.258 10.167  1.00 29.88 ? 500 VAL B CG1   1 
ATOM   5783 C CG2   . VAL B 1 359 ? -41.201 77.295 11.779  1.00 31.86 ? 500 VAL B CG2   1 
ATOM   5784 N N     . GLY B 1 360 ? -43.864 74.767 9.081   1.00 31.55 ? 501 GLY B N     1 
ATOM   5785 C CA    . GLY B 1 360 ? -44.786 74.418 8.011   1.00 33.57 ? 501 GLY B CA    1 
ATOM   5786 C C     . GLY B 1 360 ? -46.040 73.749 8.535   1.00 30.84 ? 501 GLY B C     1 
ATOM   5787 O O     . GLY B 1 360 ? -47.151 74.039 8.082   1.00 30.44 ? 501 GLY B O     1 
ATOM   5788 N N     . LYS B 1 361 ? -45.881 72.861 9.518   1.00 34.09 ? 502 LYS B N     1 
ATOM   5789 C CA    . LYS B 1 361 ? -47.046 72.192 10.091  1.00 31.75 ? 502 LYS B CA    1 
ATOM   5790 C C     . LYS B 1 361 ? -47.927 73.172 10.849  1.00 29.67 ? 502 LYS B C     1 
ATOM   5791 O O     . LYS B 1 361 ? -49.165 73.102 10.760  1.00 31.60 ? 502 LYS B O     1 
ATOM   5792 C CB    . LYS B 1 361 ? -46.607 71.035 10.985  1.00 37.94 ? 502 LYS B CB    1 
ATOM   5793 C CG    . LYS B 1 361 ? -46.063 69.871 10.165  1.00 42.20 ? 502 LYS B CG    1 
ATOM   5794 C CD    . LYS B 1 361 ? -45.033 69.044 10.907  1.00 53.93 ? 502 LYS B CD    1 
ATOM   5795 C CE    . LYS B 1 361 ? -45.512 67.614 11.052  1.00 54.20 ? 502 LYS B CE    1 
ATOM   5796 N NZ    . LYS B 1 361 ? -44.463 66.738 11.614  1.00 64.21 ? 502 LYS B NZ    1 
ATOM   5797 N N     . ALA B 1 362 ? -47.314 74.103 11.589  1.00 33.83 ? 503 ALA B N     1 
ATOM   5798 C CA    . ALA B 1 362 ? -48.098 75.118 12.286  1.00 32.46 ? 503 ALA B CA    1 
ATOM   5799 C C     . ALA B 1 362 ? -48.852 75.996 11.297  1.00 32.40 ? 503 ALA B C     1 
ATOM   5800 O O     . ALA B 1 362 ? -50.009 76.358 11.528  1.00 30.07 ? 503 ALA B O     1 
ATOM   5801 C CB    . ALA B 1 362 ? -47.193 75.970 13.176  1.00 31.62 ? 503 ALA B CB    1 
ATOM   5802 N N     . LEU B 1 363 ? -48.215 76.338 10.178  1.00 31.11 ? 504 LEU B N     1 
ATOM   5803 C CA    . LEU B 1 363 ? -48.900 77.144 9.175   1.00 31.10 ? 504 LEU B CA    1 
ATOM   5804 C C     . LEU B 1 363 ? -50.057 76.373 8.560   1.00 33.29 ? 504 LEU B C     1 
ATOM   5805 O O     . LEU B 1 363 ? -51.108 76.955 8.262   1.00 36.15 ? 504 LEU B O     1 
ATOM   5806 C CB    . LEU B 1 363 ? -47.918 77.594 8.089   1.00 29.92 ? 504 LEU B CB    1 
ATOM   5807 C CG    . LEU B 1 363 ? -47.003 78.732 8.542   1.00 33.24 ? 504 LEU B CG    1 
ATOM   5808 C CD1   . LEU B 1 363 ? -45.796 78.888 7.595   1.00 30.10 ? 504 LEU B CD1   1 
ATOM   5809 C CD2   . LEU B 1 363 ? -47.803 80.028 8.688   1.00 31.11 ? 504 LEU B CD2   1 
ATOM   5810 N N     . ASN B 1 364 ? -49.880 75.063 8.363   1.00 30.30 ? 505 ASN B N     1 
ATOM   5811 C CA    . ASN B 1 364 ? -50.959 74.244 7.824   1.00 29.90 ? 505 ASN B CA    1 
ATOM   5812 C C     . ASN B 1 364 ? -52.141 74.193 8.777   1.00 35.17 ? 505 ASN B C     1 
ATOM   5813 O O     . ASN B 1 364 ? -53.298 74.171 8.338   1.00 34.89 ? 505 ASN B O     1 
ATOM   5814 C CB    . ASN B 1 364 ? -50.468 72.828 7.531   1.00 30.47 ? 505 ASN B CB    1 
ATOM   5815 C CG    . ASN B 1 364 ? -51.599 71.914 7.104   1.00 32.97 ? 505 ASN B CG    1 
ATOM   5816 O OD1   . ASN B 1 364 ? -52.218 72.135 6.069   1.00 28.60 ? 505 ASN B OD1   1 
ATOM   5817 N ND2   . ASN B 1 364 ? -51.915 70.918 7.930   1.00 32.65 ? 505 ASN B ND2   1 
ATOM   5818 N N     . ALA B 1 365 ? -51.874 74.162 10.088  1.00 33.20 ? 506 ALA B N     1 
ATOM   5819 C CA    . ALA B 1 365 ? -52.971 74.210 11.055  1.00 39.68 ? 506 ALA B CA    1 
ATOM   5820 C C     . ALA B 1 365 ? -53.822 75.467 10.888  1.00 42.10 ? 506 ALA B C     1 
ATOM   5821 O O     . ALA B 1 365 ? -55.004 75.471 11.250  1.00 49.89 ? 506 ALA B O     1 
ATOM   5822 C CB    . ALA B 1 365 ? -52.425 74.125 12.482  1.00 34.68 ? 506 ALA B CB    1 
ATOM   5823 N N     . GLU B 1 366 ? -53.241 76.539 10.352  1.00 40.40 ? 507 GLU B N     1 
ATOM   5824 C CA    . GLU B 1 366 ? -53.954 77.773 10.042  1.00 40.59 ? 507 GLU B CA    1 
ATOM   5825 C C     . GLU B 1 366 ? -54.579 77.753 8.650   1.00 41.24 ? 507 GLU B C     1 
ATOM   5826 O O     . GLU B 1 366 ? -55.180 78.753 8.240   1.00 41.56 ? 507 GLU B O     1 
ATOM   5827 C CB    . GLU B 1 366 ? -52.998 78.970 10.155  1.00 41.84 ? 507 GLU B CB    1 
ATOM   5828 C CG    . GLU B 1 366 ? -52.848 79.547 11.556  1.00 55.15 ? 507 GLU B CG    1 
ATOM   5829 C CD    . GLU B 1 366 ? -54.097 79.368 12.400  1.00 60.52 ? 507 GLU B CD    1 
ATOM   5830 O OE1   . GLU B 1 366 ? -55.086 80.096 12.150  1.00 59.83 ? 507 GLU B OE1   1 
ATOM   5831 O OE2   . GLU B 1 366 ? -54.096 78.489 13.294  1.00 58.35 ? 507 GLU B OE2   1 
ATOM   5832 N N     . GLY B 1 367 ? -54.452 76.647 7.916   1.00 35.61 ? 508 GLY B N     1 
ATOM   5833 C CA    . GLY B 1 367 ? -54.978 76.541 6.573   1.00 36.16 ? 508 GLY B CA    1 
ATOM   5834 C C     . GLY B 1 367 ? -53.983 76.839 5.470   1.00 37.13 ? 508 GLY B C     1 
ATOM   5835 O O     . GLY B 1 367 ? -54.323 76.655 4.292   1.00 31.35 ? 508 GLY B O     1 
ATOM   5836 N N     . ILE B 1 368 ? -52.767 77.259 5.816   1.00 30.13 ? 509 ILE B N     1 
ATOM   5837 C CA    . ILE B 1 368 ? -51.780 77.744 4.853   1.00 35.18 ? 509 ILE B CA    1 
ATOM   5838 C C     . ILE B 1 368 ? -50.878 76.593 4.427   1.00 30.54 ? 509 ILE B C     1 
ATOM   5839 O O     . ILE B 1 368 ? -50.221 75.968 5.267   1.00 29.99 ? 509 ILE B O     1 
ATOM   5840 C CB    . ILE B 1 368 ? -50.947 78.886 5.455   1.00 32.31 ? 509 ILE B CB    1 
ATOM   5841 C CG1   . ILE B 1 368 ? -51.856 79.994 5.989   1.00 31.63 ? 509 ILE B CG1   1 
ATOM   5842 C CG2   . ILE B 1 368 ? -49.951 79.419 4.444   1.00 30.30 ? 509 ILE B CG2   1 
ATOM   5843 C CD1   . ILE B 1 368 ? -51.157 80.925 6.956   1.00 35.14 ? 509 ILE B CD1   1 
ATOM   5844 N N     . ALA B 1 369 ? -50.815 76.338 3.122   1.00 27.11 ? 510 ALA B N     1 
ATOM   5845 C CA    . ALA B 1 369 ? -49.961 75.299 2.551   1.00 26.37 ? 510 ALA B CA    1 
ATOM   5846 C C     . ALA B 1 369 ? -48.654 75.920 2.058   1.00 28.06 ? 510 ALA B C     1 
ATOM   5847 O O     . ALA B 1 369 ? -48.656 76.715 1.109   1.00 25.68 ? 510 ALA B O     1 
ATOM   5848 C CB    . ALA B 1 369 ? -50.683 74.582 1.408   1.00 23.65 ? 510 ALA B CB    1 
ATOM   5849 N N     . VAL B 1 370 ? -47.536 75.555 2.696   1.00 23.64 ? 511 VAL B N     1 
ATOM   5850 C CA    . VAL B 1 370 ? -46.199 75.908 2.225   1.00 25.80 ? 511 VAL B CA    1 
ATOM   5851 C C     . VAL B 1 370 ? -45.321 74.662 2.282   1.00 28.54 ? 511 VAL B C     1 
ATOM   5852 O O     . VAL B 1 370 ? -45.659 73.666 2.925   1.00 31.75 ? 511 VAL B O     1 
ATOM   5853 C CB    . VAL B 1 370 ? -45.545 77.048 3.042   1.00 28.60 ? 511 VAL B CB    1 
ATOM   5854 C CG1   . VAL B 1 370 ? -46.376 78.332 2.984   1.00 25.77 ? 511 VAL B CG1   1 
ATOM   5855 C CG2   . VAL B 1 370 ? -45.349 76.598 4.497   1.00 30.20 ? 511 VAL B CG2   1 
ATOM   5856 N N     . ARG B 1 371 ? -44.171 74.728 1.606   1.00 29.51 ? 512 ARG B N     1 
ATOM   5857 C CA    . ARG B 1 371 ? -43.163 73.680 1.716   1.00 26.99 ? 512 ARG B CA    1 
ATOM   5858 C C     . ARG B 1 371 ? -42.135 74.077 2.763   1.00 27.04 ? 512 ARG B C     1 
ATOM   5859 O O     . ARG B 1 371 ? -41.716 75.236 2.845   1.00 25.65 ? 512 ARG B O     1 
ATOM   5860 C CB    . ARG B 1 371 ? -42.447 73.417 0.382   1.00 33.57 ? 512 ARG B CB    1 
ATOM   5861 C CG    . ARG B 1 371 ? -43.153 72.484 -0.620  1.00 37.14 ? 512 ARG B CG    1 
ATOM   5862 C CD    . ARG B 1 371 ? -43.627 71.151 -0.043  1.00 34.90 ? 512 ARG B CD    1 
ATOM   5863 N NE    . ARG B 1 371 ? -44.707 70.576 -0.846  1.00 34.73 ? 512 ARG B NE    1 
ATOM   5864 C CZ    . ARG B 1 371 ? -45.011 69.283 -0.906  1.00 33.22 ? 512 ARG B CZ    1 
ATOM   5865 N NH1   . ARG B 1 371 ? -44.288 68.369 -0.278  1.00 33.39 ? 512 ARG B NH1   1 
ATOM   5866 N NH2   . ARG B 1 371 ? -46.072 68.897 -1.611  1.00 30.71 ? 512 ARG B NH2   1 
ATOM   5867 N N     . ALA B 1 372 ? -41.728 73.109 3.571   1.00 29.15 ? 513 ALA B N     1 
ATOM   5868 C CA    . ALA B 1 372 ? -40.647 73.302 4.529   1.00 31.19 ? 513 ALA B CA    1 
ATOM   5869 C C     . ALA B 1 372 ? -39.666 72.165 4.326   1.00 32.21 ? 513 ALA B C     1 
ATOM   5870 O O     . ALA B 1 372 ? -40.008 70.998 4.547   1.00 38.02 ? 513 ALA B O     1 
ATOM   5871 C CB    . ALA B 1 372 ? -41.160 73.328 5.973   1.00 29.58 ? 513 ALA B CB    1 
ATOM   5872 N N     . GLY B 1 373 ? -38.467 72.497 3.900   1.00 30.80 ? 514 GLY B N     1 
ATOM   5873 C CA    . GLY B 1 373 ? -37.523 71.438 3.577   1.00 26.91 ? 514 GLY B CA    1 
ATOM   5874 C C     . GLY B 1 373 ? -36.425 71.996 2.699   1.00 26.56 ? 514 GLY B C     1 
ATOM   5875 O O     . GLY B 1 373 ? -36.162 73.198 2.708   1.00 26.28 ? 514 GLY B O     1 
ATOM   5876 N N     . HIS B 1 374 ? -35.809 71.105 1.926   1.00 25.28 ? 515 HIS B N     1 
ATOM   5877 C CA    . HIS B 1 374 ? -34.702 71.513 1.074   1.00 28.52 ? 515 HIS B CA    1 
ATOM   5878 C C     . HIS B 1 374 ? -35.140 71.823 -0.353  1.00 23.10 ? 515 HIS B C     1 
ATOM   5879 O O     . HIS B 1 374 ? -34.321 72.306 -1.141  1.00 24.36 ? 515 HIS B O     1 
ATOM   5880 C CB    . HIS B 1 374 ? -33.601 70.435 1.103   1.00 28.31 ? 515 HIS B CB    1 
ATOM   5881 C CG    . HIS B 1 374 ? -34.010 69.110 0.530   1.00 28.84 ? 515 HIS B CG    1 
ATOM   5882 N ND1   . HIS B 1 374 ? -33.597 67.909 1.071   1.00 33.08 ? 515 HIS B ND1   1 
ATOM   5883 C CD2   . HIS B 1 374 ? -34.690 68.796 -0.597  1.00 22.82 ? 515 HIS B CD2   1 
ATOM   5884 C CE1   . HIS B 1 374 ? -34.073 66.913 0.346   1.00 26.17 ? 515 HIS B CE1   1 
ATOM   5885 N NE2   . HIS B 1 374 ? -34.729 67.424 -0.680  1.00 31.88 ? 515 HIS B NE2   1 
ATOM   5886 N N     . HIS B 1 375 ? -36.404 71.550 -0.699  1.00 24.96 ? 516 HIS B N     1 
ATOM   5887 C CA    . HIS B 1 375 ? -36.998 71.958 -1.982  1.00 25.61 ? 516 HIS B CA    1 
ATOM   5888 C C     . HIS B 1 375 ? -36.266 71.374 -3.186  1.00 23.37 ? 516 HIS B C     1 
ATOM   5889 O O     . HIS B 1 375 ? -36.268 71.967 -4.270  1.00 20.84 ? 516 HIS B O     1 
ATOM   5890 C CB    . HIS B 1 375 ? -37.059 73.483 -2.090  1.00 23.10 ? 516 HIS B CB    1 
ATOM   5891 C CG    . HIS B 1 375 ? -37.504 74.144 -0.824  1.00 27.15 ? 516 HIS B CG    1 
ATOM   5892 N ND1   . HIS B 1 375 ? -38.744 73.913 -0.266  1.00 25.97 ? 516 HIS B ND1   1 
ATOM   5893 C CD2   . HIS B 1 375 ? -36.868 74.998 0.011   1.00 25.17 ? 516 HIS B CD2   1 
ATOM   5894 C CE1   . HIS B 1 375 ? -38.857 74.606 0.853   1.00 29.00 ? 516 HIS B CE1   1 
ATOM   5895 N NE2   . HIS B 1 375 ? -37.732 75.272 1.045   1.00 27.84 ? 516 HIS B NE2   1 
ATOM   5896 N N     . CYS B 1 376 ? -35.645 70.206 -3.012  1.00 21.34 ? 517 CYS B N     1 
ATOM   5897 C CA    . CYS B 1 376 ? -34.894 69.565 -4.091  1.00 22.50 ? 517 CYS B CA    1 
ATOM   5898 C C     . CYS B 1 376 ? -33.831 70.521 -4.625  1.00 22.34 ? 517 CYS B C     1 
ATOM   5899 O O     . CYS B 1 376 ? -33.633 70.647 -5.835  1.00 23.24 ? 517 CYS B O     1 
ATOM   5900 C CB    . CYS B 1 376 ? -35.821 69.088 -5.219  1.00 23.64 ? 517 CYS B CB    1 
ATOM   5901 S SG    . CYS B 1 376 ? -36.994 67.812 -4.694  1.00 34.93 ? 517 CYS B SG    1 
ATOM   5902 N N     . ALA B 1 377 ? -33.176 71.229 -3.705  1.00 19.45 ? 518 ALA B N     1 
ATOM   5903 C CA    . ALA B 1 377 ? -32.113 72.171 -4.039  1.00 18.95 ? 518 ALA B CA    1 
ATOM   5904 C C     . ALA B 1 377 ? -31.150 72.261 -2.859  1.00 18.74 ? 518 ALA B C     1 
ATOM   5905 O O     . ALA B 1 377 ? -30.832 73.342 -2.364  1.00 21.79 ? 518 ALA B O     1 
ATOM   5906 C CB    . ALA B 1 377 ? -32.682 73.542 -4.405  1.00 21.11 ? 518 ALA B CB    1 
ATOM   5907 N N     . GLN B 1 378 ? -30.695 71.107 -2.379  1.00 21.19 ? 519 GLN B N     1 
ATOM   5908 C CA    . GLN B 1 378 ? -29.771 71.094 -1.248  1.00 25.32 ? 519 GLN B CA    1 
ATOM   5909 C C     . GLN B 1 378 ? -28.520 71.933 -1.480  1.00 24.23 ? 519 GLN B C     1 
ATOM   5910 O O     . GLN B 1 378 ? -28.094 72.611 -0.531  1.00 23.75 ? 519 GLN B O     1 
ATOM   5911 C CB    . GLN B 1 378 ? -29.397 69.645 -0.901  1.00 25.63 ? 519 GLN B CB    1 
ATOM   5912 C CG    . GLN B 1 378 ? -30.573 68.823 -0.388  1.00 23.41 ? 519 GLN B CG    1 
ATOM   5913 C CD    . GLN B 1 378 ? -30.165 67.440 0.036   1.00 31.17 ? 519 GLN B CD    1 
ATOM   5914 O OE1   . GLN B 1 378 ? -30.082 66.542 -0.796  1.00 28.83 ? 519 GLN B OE1   1 
ATOM   5915 N NE2   . GLN B 1 378 ? -29.918 67.249 1.341   1.00 29.10 ? 519 GLN B NE2   1 
ATOM   5916 N N     . PRO B 1 379 ? -27.881 71.938 -2.661  1.00 21.70 ? 520 PRO B N     1 
ATOM   5917 C CA    . PRO B 1 379 ? -26.623 72.698 -2.772  1.00 22.07 ? 520 PRO B CA    1 
ATOM   5918 C C     . PRO B 1 379 ? -26.782 74.191 -2.538  1.00 26.08 ? 520 PRO B C     1 
ATOM   5919 O O     . PRO B 1 379 ? -25.952 74.774 -1.826  1.00 24.38 ? 520 PRO B O     1 
ATOM   5920 C CB    . PRO B 1 379 ? -26.141 72.383 -4.197  1.00 22.67 ? 520 PRO B CB    1 
ATOM   5921 C CG    . PRO B 1 379 ? -26.719 71.032 -4.491  1.00 25.02 ? 520 PRO B CG    1 
ATOM   5922 C CD    . PRO B 1 379 ? -28.095 71.078 -3.845  1.00 20.82 ? 520 PRO B CD    1 
ATOM   5923 N N     . ILE B 1 380 ? -27.818 74.832 -3.097  1.00 22.29 ? 521 ILE B N     1 
ATOM   5924 C CA    . ILE B 1 380 ? -27.962 76.274 -2.880  1.00 24.38 ? 521 ILE B CA    1 
ATOM   5925 C C     . ILE B 1 380 ? -28.266 76.570 -1.412  1.00 26.88 ? 521 ILE B C     1 
ATOM   5926 O O     . ILE B 1 380 ? -27.814 77.588 -0.873  1.00 28.96 ? 521 ILE B O     1 
ATOM   5927 C CB    . ILE B 1 380 ? -29.026 76.887 -3.820  1.00 23.14 ? 521 ILE B CB    1 
ATOM   5928 C CG1   . ILE B 1 380 ? -29.010 78.419 -3.745  1.00 22.44 ? 521 ILE B CG1   1 
ATOM   5929 C CG2   . ILE B 1 380 ? -30.430 76.382 -3.502  1.00 19.32 ? 521 ILE B CG2   1 
ATOM   5930 C CD1   . ILE B 1 380 ? -27.676 79.057 -4.033  1.00 25.78 ? 521 ILE B CD1   1 
ATOM   5931 N N     . LEU B 1 381 ? -29.000 75.690 -0.729  1.00 25.47 ? 522 LEU B N     1 
ATOM   5932 C CA    . LEU B 1 381 ? -29.299 75.946 0.680   1.00 28.85 ? 522 LEU B CA    1 
ATOM   5933 C C     . LEU B 1 381 ? -28.061 75.769 1.552   1.00 29.00 ? 522 LEU B C     1 
ATOM   5934 O O     . LEU B 1 381 ? -27.854 76.538 2.498   1.00 32.61 ? 522 LEU B O     1 
ATOM   5935 C CB    . LEU B 1 381 ? -30.429 75.044 1.162   1.00 22.26 ? 522 LEU B CB    1 
ATOM   5936 C CG    . LEU B 1 381 ? -31.821 75.321 0.589   1.00 30.17 ? 522 LEU B CG    1 
ATOM   5937 C CD1   . LEU B 1 381 ? -32.882 74.645 1.448   1.00 28.92 ? 522 LEU B CD1   1 
ATOM   5938 C CD2   . LEU B 1 381 ? -32.088 76.821 0.476   1.00 28.84 ? 522 LEU B CD2   1 
ATOM   5939 N N     . ARG B 1 382 ? -27.226 74.764 1.256   1.00 25.61 ? 523 ARG B N     1 
ATOM   5940 C CA    . ARG B 1 382 ? -25.941 74.663 1.947   1.00 30.16 ? 523 ARG B CA    1 
ATOM   5941 C C     . ARG B 1 382 ? -25.090 75.900 1.697   1.00 32.55 ? 523 ARG B C     1 
ATOM   5942 O O     . ARG B 1 382 ? -24.385 76.366 2.597   1.00 30.84 ? 523 ARG B O     1 
ATOM   5943 C CB    . ARG B 1 382 ? -25.183 73.413 1.505   1.00 28.90 ? 523 ARG B CB    1 
ATOM   5944 C CG    . ARG B 1 382 ? -25.890 72.116 1.819   1.00 38.96 ? 523 ARG B CG    1 
ATOM   5945 C CD    . ARG B 1 382 ? -24.928 70.965 1.990   1.00 37.99 ? 523 ARG B CD    1 
ATOM   5946 N NE    . ARG B 1 382 ? -25.656 69.700 2.010   1.00 37.64 ? 523 ARG B NE    1 
ATOM   5947 C CZ    . ARG B 1 382 ? -25.939 68.981 0.930   1.00 42.25 ? 523 ARG B CZ    1 
ATOM   5948 N NH1   . ARG B 1 382 ? -25.602 69.393 -0.295  1.00 28.19 ? 523 ARG B NH1   1 
ATOM   5949 N NH2   . ARG B 1 382 ? -26.589 67.829 1.077   1.00 36.50 ? 523 ARG B NH2   1 
ATOM   5950 N N     . ARG B 1 383 ? -25.130 76.437 0.471   1.00 29.08 ? 524 ARG B N     1 
ATOM   5951 C CA    . ARG B 1 383 ? -24.417 77.682 0.189   1.00 30.13 ? 524 ARG B CA    1 
ATOM   5952 C C     . ARG B 1 383 ? -24.906 78.819 1.087   1.00 31.43 ? 524 ARG B C     1 
ATOM   5953 O O     . ARG B 1 383 ? -24.131 79.719 1.437   1.00 32.81 ? 524 ARG B O     1 
ATOM   5954 C CB    . ARG B 1 383 ? -24.577 78.037 -1.297  1.00 26.00 ? 524 ARG B CB    1 
ATOM   5955 C CG    . ARG B 1 383 ? -24.225 79.472 -1.673  1.00 28.59 ? 524 ARG B CG    1 
ATOM   5956 C CD    . ARG B 1 383 ? -22.715 79.713 -1.661  1.00 28.14 ? 524 ARG B CD    1 
ATOM   5957 N NE    . ARG B 1 383 ? -22.407 81.102 -1.983  1.00 26.91 ? 524 ARG B NE    1 
ATOM   5958 C CZ    . ARG B 1 383 ? -22.544 82.115 -1.140  1.00 32.92 ? 524 ARG B CZ    1 
ATOM   5959 N NH1   . ARG B 1 383 ? -22.947 81.926 0.108   1.00 29.70 ? 524 ARG B NH1   1 
ATOM   5960 N NH2   . ARG B 1 383 ? -22.261 83.346 -1.555  1.00 30.21 ? 524 ARG B NH2   1 
ATOM   5961 N N     . MET B 1 384 ? -26.176 78.785 1.485   1.00 29.41 ? 525 MET B N     1 
ATOM   5962 C CA    . MET B 1 384 ? -26.765 79.774 2.380   1.00 32.26 ? 525 MET B CA    1 
ATOM   5963 C C     . MET B 1 384 ? -26.583 79.414 3.859   1.00 34.80 ? 525 MET B C     1 
ATOM   5964 O O     . MET B 1 384 ? -27.039 80.163 4.729   1.00 34.27 ? 525 MET B O     1 
ATOM   5965 C CB    . MET B 1 384 ? -28.259 79.931 2.055   1.00 33.50 ? 525 MET B CB    1 
ATOM   5966 C CG    . MET B 1 384 ? -28.574 80.788 0.797   1.00 32.89 ? 525 MET B CG    1 
ATOM   5967 S SD    . MET B 1 384 ? -27.336 82.051 0.404   1.00 42.43 ? 525 MET B SD    1 
ATOM   5968 C CE    . MET B 1 384 ? -27.792 82.529 -1.270  1.00 38.63 ? 525 MET B CE    1 
ATOM   5969 N N     . GLY B 1 385 ? -25.919 78.299 4.163   1.00 31.58 ? 526 GLY B N     1 
ATOM   5970 C CA    . GLY B 1 385 ? -25.717 77.894 5.541   1.00 34.73 ? 526 GLY B CA    1 
ATOM   5971 C C     . GLY B 1 385 ? -26.866 77.130 6.157   1.00 35.41 ? 526 GLY B C     1 
ATOM   5972 O O     . GLY B 1 385 ? -26.950 77.044 7.385   1.00 39.01 ? 526 GLY B O     1 
ATOM   5973 N N     . LEU B 1 386 ? -27.741 76.543 5.344   1.00 32.70 ? 527 LEU B N     1 
ATOM   5974 C CA    . LEU B 1 386 ? -29.016 76.009 5.805   1.00 34.66 ? 527 LEU B CA    1 
ATOM   5975 C C     . LEU B 1 386 ? -29.225 74.597 5.281   1.00 37.22 ? 527 LEU B C     1 
ATOM   5976 O O     . LEU B 1 386 ? -28.687 74.209 4.239   1.00 31.11 ? 527 LEU B O     1 
ATOM   5977 C CB    . LEU B 1 386 ? -30.181 76.898 5.346   1.00 32.96 ? 527 LEU B CB    1 
ATOM   5978 C CG    . LEU B 1 386 ? -30.168 78.318 5.917   1.00 36.44 ? 527 LEU B CG    1 
ATOM   5979 C CD1   . LEU B 1 386 ? -31.315 79.119 5.358   1.00 36.40 ? 527 LEU B CD1   1 
ATOM   5980 C CD2   . LEU B 1 386 ? -30.245 78.261 7.443   1.00 33.05 ? 527 LEU B CD2   1 
ATOM   5981 N N     . GLU B 1 387 ? -30.036 73.835 6.014   1.00 34.05 ? 528 GLU B N     1 
ATOM   5982 C CA    . GLU B 1 387 ? -30.466 72.514 5.570   1.00 35.68 ? 528 GLU B CA    1 
ATOM   5983 C C     . GLU B 1 387 ? -31.872 72.527 4.991   1.00 33.08 ? 528 GLU B C     1 
ATOM   5984 O O     . GLU B 1 387 ? -32.272 71.557 4.333   1.00 31.42 ? 528 GLU B O     1 
ATOM   5985 C CB    . GLU B 1 387 ? -30.414 71.514 6.736   1.00 36.16 ? 528 GLU B CB    1 
ATOM   5986 C CG    . GLU B 1 387 ? -29.006 71.062 7.094   1.00 44.31 ? 528 GLU B CG    1 
ATOM   5987 C CD    . GLU B 1 387 ? -28.349 70.235 5.995   1.00 54.85 ? 528 GLU B CD    1 
ATOM   5988 O OE1   . GLU B 1 387 ? -28.965 69.243 5.536   1.00 53.72 ? 528 GLU B OE1   1 
ATOM   5989 O OE2   . GLU B 1 387 ? -27.214 70.585 5.590   1.00 52.38 ? 528 GLU B OE2   1 
ATOM   5990 N N     . ALA B 1 388 ? -32.613 73.606 5.207   1.00 29.94 ? 529 ALA B N     1 
ATOM   5991 C CA    . ALA B 1 388 ? -34.035 73.685 4.926   1.00 33.01 ? 529 ALA B CA    1 
ATOM   5992 C C     . ALA B 1 388 ? -34.460 75.131 5.097   1.00 31.68 ? 529 ALA B C     1 
ATOM   5993 O O     . ALA B 1 388 ? -33.826 75.891 5.835   1.00 32.57 ? 529 ALA B O     1 
ATOM   5994 C CB    . ALA B 1 388 ? -34.846 72.781 5.869   1.00 30.35 ? 529 ALA B CB    1 
ATOM   5995 N N     . THR B 1 389 ? -35.527 75.506 4.401   1.00 28.96 ? 530 THR B N     1 
ATOM   5996 C CA    . THR B 1 389 ? -36.192 76.776 4.651   1.00 29.15 ? 530 THR B CA    1 
ATOM   5997 C C     . THR B 1 389 ? -37.695 76.543 4.618   1.00 30.11 ? 530 THR B C     1 
ATOM   5998 O O     . THR B 1 389 ? -38.175 75.495 4.159   1.00 24.17 ? 530 THR B O     1 
ATOM   5999 C CB    . THR B 1 389 ? -35.809 77.864 3.627   1.00 27.02 ? 530 THR B CB    1 
ATOM   6000 O OG1   . THR B 1 389 ? -36.416 77.565 2.362   1.00 29.96 ? 530 THR B OG1   1 
ATOM   6001 C CG2   . THR B 1 389 ? -34.303 77.978 3.459   1.00 29.98 ? 530 THR B CG2   1 
ATOM   6002 N N     . VAL B 1 390 ? -38.430 77.524 5.153   1.00 26.59 ? 531 VAL B N     1 
ATOM   6003 C CA    . VAL B 1 390 ? -39.872 77.623 4.966   1.00 26.58 ? 531 VAL B CA    1 
ATOM   6004 C C     . VAL B 1 390 ? -40.085 78.470 3.725   1.00 27.29 ? 531 VAL B C     1 
ATOM   6005 O O     . VAL B 1 390 ? -39.482 79.542 3.600   1.00 26.81 ? 531 VAL B O     1 
ATOM   6006 C CB    . VAL B 1 390 ? -40.546 78.265 6.192   1.00 28.79 ? 531 VAL B CB    1 
ATOM   6007 C CG1   . VAL B 1 390 ? -42.065 78.232 6.051   1.00 27.72 ? 531 VAL B CG1   1 
ATOM   6008 C CG2   . VAL B 1 390 ? -40.097 77.571 7.476   1.00 28.21 ? 531 VAL B CG2   1 
ATOM   6009 N N     . ARG B 1 391 ? -40.911 77.995 2.792   1.00 24.31 ? 532 ARG B N     1 
ATOM   6010 C CA    . ARG B 1 391 ? -40.976 78.585 1.452   1.00 27.43 ? 532 ARG B CA    1 
ATOM   6011 C C     . ARG B 1 391 ? -42.410 78.728 0.974   1.00 27.96 ? 532 ARG B C     1 
ATOM   6012 O O     . ARG B 1 391 ? -42.929 77.873 0.245   1.00 30.91 ? 532 ARG B O     1 
ATOM   6013 C CB    . ARG B 1 391 ? -40.169 77.753 0.447   1.00 27.06 ? 532 ARG B CB    1 
ATOM   6014 C CG    . ARG B 1 391 ? -40.012 78.409 -0.925  1.00 27.77 ? 532 ARG B CG    1 
ATOM   6015 C CD    . ARG B 1 391 ? -39.737 77.385 -2.042  1.00 25.35 ? 532 ARG B CD    1 
ATOM   6016 N NE    . ARG B 1 391 ? -40.861 76.482 -2.259  1.00 25.41 ? 532 ARG B NE    1 
ATOM   6017 C CZ    . ARG B 1 391 ? -40.818 75.391 -3.016  1.00 27.83 ? 532 ARG B CZ    1 
ATOM   6018 N NH1   . ARG B 1 391 ? -39.735 75.064 -3.704  1.00 25.39 ? 532 ARG B NH1   1 
ATOM   6019 N NH2   . ARG B 1 391 ? -41.892 74.614 -3.094  1.00 30.97 ? 532 ARG B NH2   1 
ATOM   6020 N N     . PRO B 1 392 ? -43.079 79.818 1.339   1.00 27.11 ? 533 PRO B N     1 
ATOM   6021 C CA    . PRO B 1 392 ? -44.254 80.234 0.569   1.00 27.93 ? 533 PRO B CA    1 
ATOM   6022 C C     . PRO B 1 392 ? -43.841 80.684 -0.828  1.00 26.93 ? 533 PRO B C     1 
ATOM   6023 O O     . PRO B 1 392 ? -42.741 81.205 -1.043  1.00 27.58 ? 533 PRO B O     1 
ATOM   6024 C CB    . PRO B 1 392 ? -44.821 81.401 1.382   1.00 27.63 ? 533 PRO B CB    1 
ATOM   6025 C CG    . PRO B 1 392 ? -43.615 81.969 2.071   1.00 27.48 ? 533 PRO B CG    1 
ATOM   6026 C CD    . PRO B 1 392 ? -42.754 80.774 2.408   1.00 25.99 ? 533 PRO B CD    1 
ATOM   6027 N N     . SER B 1 393 ? -44.737 80.454 -1.789  1.00 27.63 ? 534 SER B N     1 
ATOM   6028 C CA    . SER B 1 393 ? -44.549 80.888 -3.164  1.00 27.93 ? 534 SER B CA    1 
ATOM   6029 C C     . SER B 1 393 ? -45.906 81.277 -3.726  1.00 29.74 ? 534 SER B C     1 
ATOM   6030 O O     . SER B 1 393 ? -46.899 80.568 -3.520  1.00 30.38 ? 534 SER B O     1 
ATOM   6031 C CB    . SER B 1 393 ? -43.872 79.794 -4.019  1.00 28.68 ? 534 SER B CB    1 
ATOM   6032 O OG    . SER B 1 393 ? -44.574 78.560 -3.959  1.00 27.56 ? 534 SER B OG    1 
ATOM   6033 N N     . PHE B 1 394 ? -45.945 82.415 -4.419  1.00 27.33 ? 535 PHE B N     1 
ATOM   6034 C CA    . PHE B 1 394 ? -47.191 83.065 -4.794  1.00 32.38 ? 535 PHE B CA    1 
ATOM   6035 C C     . PHE B 1 394 ? -47.525 82.855 -6.262  1.00 31.41 ? 535 PHE B C     1 
ATOM   6036 O O     . PHE B 1 394 ? -46.646 82.739 -7.120  1.00 34.24 ? 535 PHE B O     1 
ATOM   6037 C CB    . PHE B 1 394 ? -47.134 84.564 -4.501  1.00 31.56 ? 535 PHE B CB    1 
ATOM   6038 C CG    . PHE B 1 394 ? -46.725 84.879 -3.105  1.00 32.44 ? 535 PHE B CG    1 
ATOM   6039 C CD1   . PHE B 1 394 ? -47.587 84.631 -2.047  1.00 34.32 ? 535 PHE B CD1   1 
ATOM   6040 C CD2   . PHE B 1 394 ? -45.467 85.388 -2.836  1.00 34.60 ? 535 PHE B CD2   1 
ATOM   6041 C CE1   . PHE B 1 394 ? -47.212 84.912 -0.740  1.00 34.68 ? 535 PHE B CE1   1 
ATOM   6042 C CE2   . PHE B 1 394 ? -45.083 85.673 -1.523  1.00 36.73 ? 535 PHE B CE2   1 
ATOM   6043 C CZ    . PHE B 1 394 ? -45.957 85.431 -0.478  1.00 34.03 ? 535 PHE B CZ    1 
ATOM   6044 N N     . ALA B 1 395 ? -48.821 82.819 -6.537  1.00 32.17 ? 536 ALA B N     1 
ATOM   6045 C CA    . ALA B 1 395 ? -49.356 82.713 -7.882  1.00 30.91 ? 536 ALA B CA    1 
ATOM   6046 C C     . ALA B 1 395 ? -50.465 83.745 -8.017  1.00 31.36 ? 536 ALA B C     1 
ATOM   6047 O O     . ALA B 1 395 ? -50.934 84.312 -7.022  1.00 30.18 ? 536 ALA B O     1 
ATOM   6048 C CB    . ALA B 1 395 ? -49.873 81.294 -8.171  1.00 28.88 ? 536 ALA B CB    1 
ATOM   6049 N N     . PHE B 1 396 ? -50.904 83.973 -9.258  1.00 27.89 ? 537 PHE B N     1 
ATOM   6050 C CA    . PHE B 1 396 ? -51.843 85.055 -9.534  1.00 31.59 ? 537 PHE B CA    1 
ATOM   6051 C C     . PHE B 1 396 ? -53.253 84.795 -9.016  1.00 30.34 ? 537 PHE B C     1 
ATOM   6052 O O     . PHE B 1 396 ? -54.096 85.683 -9.152  1.00 35.41 ? 537 PHE B O     1 
ATOM   6053 C CB    . PHE B 1 396 ? -51.884 85.362 -11.041 1.00 31.60 ? 537 PHE B CB    1 
ATOM   6054 C CG    . PHE B 1 396 ? -52.440 84.247 -11.892 1.00 29.74 ? 537 PHE B CG    1 
ATOM   6055 C CD1   . PHE B 1 396 ? -53.804 84.116 -12.092 1.00 36.21 ? 537 PHE B CD1   1 
ATOM   6056 C CD2   . PHE B 1 396 ? -51.595 83.358 -12.524 1.00 29.11 ? 537 PHE B CD2   1 
ATOM   6057 C CE1   . PHE B 1 396 ? -54.319 83.096 -12.892 1.00 35.01 ? 537 PHE B CE1   1 
ATOM   6058 C CE2   . PHE B 1 396 ? -52.100 82.347 -13.321 1.00 32.50 ? 537 PHE B CE2   1 
ATOM   6059 C CZ    . PHE B 1 396 ? -53.469 82.212 -13.498 1.00 33.18 ? 537 PHE B CZ    1 
ATOM   6060 N N     . TYR B 1 397 ? -53.571 83.637 -8.445  1.00 27.86 ? 538 TYR B N     1 
ATOM   6061 C CA    . TYR B 1 397 ? -54.833 83.567 -7.716  1.00 30.75 ? 538 TYR B CA    1 
ATOM   6062 C C     . TYR B 1 397 ? -54.671 83.864 -6.227  1.00 29.03 ? 538 TYR B C     1 
ATOM   6063 O O     . TYR B 1 397 ? -55.654 83.780 -5.486  1.00 31.77 ? 538 TYR B O     1 
ATOM   6064 C CB    . TYR B 1 397 ? -55.519 82.204 -7.899  1.00 29.98 ? 538 TYR B CB    1 
ATOM   6065 C CG    . TYR B 1 397 ? -54.612 80.997 -7.857  1.00 28.98 ? 538 TYR B CG    1 
ATOM   6066 C CD1   . TYR B 1 397 ? -53.764 80.765 -6.777  1.00 32.40 ? 538 TYR B CD1   1 
ATOM   6067 C CD2   . TYR B 1 397 ? -54.637 80.063 -8.879  1.00 26.85 ? 538 TYR B CD2   1 
ATOM   6068 C CE1   . TYR B 1 397 ? -52.941 79.650 -6.741  1.00 26.88 ? 538 TYR B CE1   1 
ATOM   6069 C CE2   . TYR B 1 397 ? -53.818 78.952 -8.855  1.00 29.43 ? 538 TYR B CE2   1 
ATOM   6070 C CZ    . TYR B 1 397 ? -52.976 78.746 -7.785  1.00 27.97 ? 538 TYR B CZ    1 
ATOM   6071 O OH    . TYR B 1 397 ? -52.172 77.633 -7.779  1.00 22.09 ? 538 TYR B OH    1 
ATOM   6072 N N     . ASN B 1 398 ? -53.464 84.195 -5.768  1.00 29.54 ? 539 ASN B N     1 
ATOM   6073 C CA    . ASN B 1 398 ? -53.273 84.578 -4.375  1.00 31.79 ? 539 ASN B CA    1 
ATOM   6074 C C     . ASN B 1 398 ? -53.594 86.060 -4.183  1.00 36.83 ? 539 ASN B C     1 
ATOM   6075 O O     . ASN B 1 398 ? -53.608 86.840 -5.144  1.00 31.17 ? 539 ASN B O     1 
ATOM   6076 C CB    . ASN B 1 398 ? -51.840 84.296 -3.926  1.00 26.50 ? 539 ASN B CB    1 
ATOM   6077 C CG    . ASN B 1 398 ? -51.530 82.823 -3.860  1.00 29.85 ? 539 ASN B CG    1 
ATOM   6078 O OD1   . ASN B 1 398 ? -50.465 82.383 -4.305  1.00 28.24 ? 539 ASN B OD1   1 
ATOM   6079 N ND2   . ASN B 1 398 ? -52.458 82.044 -3.304  1.00 26.17 ? 539 ASN B ND2   1 
ATOM   6080 N N     . THR B 1 399 ? -53.840 86.448 -2.920  1.00 30.42 ? 540 THR B N     1 
ATOM   6081 C CA    . THR B 1 399 ? -54.270 87.802 -2.583  1.00 33.73 ? 540 THR B CA    1 
ATOM   6082 C C     . THR B 1 399 ? -53.426 88.411 -1.465  1.00 34.55 ? 540 THR B C     1 
ATOM   6083 O O     . THR B 1 399 ? -52.751 87.713 -0.700  1.00 33.83 ? 540 THR B O     1 
ATOM   6084 C CB    . THR B 1 399 ? -55.735 87.845 -2.132  1.00 35.81 ? 540 THR B CB    1 
ATOM   6085 O OG1   . THR B 1 399 ? -55.853 87.206 -0.854  1.00 39.71 ? 540 THR B OG1   1 
ATOM   6086 C CG2   . THR B 1 399 ? -56.633 87.155 -3.133  1.00 32.51 ? 540 THR B CG2   1 
ATOM   6087 N N     . PHE B 1 400 ? -53.516 89.743 -1.352  1.00 38.78 ? 541 PHE B N     1 
ATOM   6088 C CA    . PHE B 1 400 ? -52.890 90.438 -0.226  1.00 38.28 ? 541 PHE B CA    1 
ATOM   6089 C C     . PHE B 1 400 ? -53.491 90.006 1.112   1.00 35.40 ? 541 PHE B C     1 
ATOM   6090 O O     . PHE B 1 400 ? -52.776 89.920 2.119   1.00 36.30 ? 541 PHE B O     1 
ATOM   6091 C CB    . PHE B 1 400 ? -52.999 91.953 -0.415  1.00 39.42 ? 541 PHE B CB    1 
ATOM   6092 C CG    . PHE B 1 400 ? -52.405 92.436 -1.714  1.00 42.41 ? 541 PHE B CG    1 
ATOM   6093 C CD1   . PHE B 1 400 ? -51.033 92.630 -1.833  1.00 41.80 ? 541 PHE B CD1   1 
ATOM   6094 C CD2   . PHE B 1 400 ? -53.210 92.687 -2.812  1.00 41.21 ? 541 PHE B CD2   1 
ATOM   6095 C CE1   . PHE B 1 400 ? -50.476 93.063 -3.028  1.00 42.40 ? 541 PHE B CE1   1 
ATOM   6096 C CE2   . PHE B 1 400 ? -52.660 93.122 -4.015  1.00 43.55 ? 541 PHE B CE2   1 
ATOM   6097 C CZ    . PHE B 1 400 ? -51.290 93.308 -4.123  1.00 37.03 ? 541 PHE B CZ    1 
ATOM   6098 N N     . ASP B 1 401 ? -54.799 89.720 1.141   1.00 38.95 ? 542 ASP B N     1 
ATOM   6099 C CA    . ASP B 1 401 ? -55.439 89.247 2.374   1.00 38.84 ? 542 ASP B CA    1 
ATOM   6100 C C     . ASP B 1 401 ? -54.826 87.932 2.862   1.00 41.22 ? 542 ASP B C     1 
ATOM   6101 O O     . ASP B 1 401 ? -54.575 87.756 4.068   1.00 34.86 ? 542 ASP B O     1 
ATOM   6102 C CB    . ASP B 1 401 ? -56.941 89.070 2.144   1.00 40.22 ? 542 ASP B CB    1 
ATOM   6103 C CG    . ASP B 1 401 ? -57.717 90.368 2.259   1.00 50.16 ? 542 ASP B CG    1 
ATOM   6104 O OD1   . ASP B 1 401 ? -57.108 91.423 2.562   1.00 52.47 ? 542 ASP B OD1   1 
ATOM   6105 O OD2   . ASP B 1 401 ? -58.950 90.326 2.052   1.00 55.55 ? 542 ASP B OD2   1 
ATOM   6106 N N     . GLU B 1 402 ? -54.605 86.982 1.941   1.00 34.96 ? 543 GLU B N     1 
ATOM   6107 C CA    . GLU B 1 402 ? -53.964 85.728 2.324   1.00 34.88 ? 543 GLU B CA    1 
ATOM   6108 C C     . GLU B 1 402 ? -52.576 85.987 2.885   1.00 32.74 ? 543 GLU B C     1 
ATOM   6109 O O     . GLU B 1 402 ? -52.166 85.366 3.877   1.00 36.99 ? 543 GLU B O     1 
ATOM   6110 C CB    . GLU B 1 402 ? -53.896 84.777 1.123   1.00 31.80 ? 543 GLU B CB    1 
ATOM   6111 C CG    . GLU B 1 402 ? -55.256 84.323 0.591   1.00 36.14 ? 543 GLU B CG    1 
ATOM   6112 C CD    . GLU B 1 402 ? -55.129 83.348 -0.579  1.00 35.80 ? 543 GLU B CD    1 
ATOM   6113 O OE1   . GLU B 1 402 ? -54.176 83.498 -1.375  1.00 36.39 ? 543 GLU B OE1   1 
ATOM   6114 O OE2   . GLU B 1 402 ? -55.964 82.422 -0.699  1.00 36.38 ? 543 GLU B OE2   1 
ATOM   6115 N N     . ILE B 1 403 ? -51.836 86.904 2.260   1.00 33.34 ? 544 ILE B N     1 
ATOM   6116 C CA    . ILE B 1 403 ? -50.521 87.274 2.767   1.00 34.39 ? 544 ILE B CA    1 
ATOM   6117 C C     . ILE B 1 403 ? -50.632 87.833 4.181   1.00 34.10 ? 544 ILE B C     1 
ATOM   6118 O O     . ILE B 1 403 ? -49.769 87.577 5.028   1.00 36.03 ? 544 ILE B O     1 
ATOM   6119 C CB    . ILE B 1 403 ? -49.851 88.271 1.800   1.00 35.12 ? 544 ILE B CB    1 
ATOM   6120 C CG1   . ILE B 1 403 ? -49.487 87.573 0.479   1.00 33.49 ? 544 ILE B CG1   1 
ATOM   6121 C CG2   . ILE B 1 403 ? -48.615 88.894 2.437   1.00 36.06 ? 544 ILE B CG2   1 
ATOM   6122 C CD1   . ILE B 1 403 ? -49.026 88.521 -0.610  1.00 34.51 ? 544 ILE B CD1   1 
ATOM   6123 N N     . ASP B 1 404 ? -51.706 88.568 4.476   1.00 37.21 ? 545 ASP B N     1 
ATOM   6124 C CA    . ASP B 1 404 ? -51.860 89.111 5.826   1.00 35.38 ? 545 ASP B CA    1 
ATOM   6125 C C     . ASP B 1 404 ? -52.098 88.000 6.841   1.00 38.80 ? 545 ASP B C     1 
ATOM   6126 O O     . ASP B 1 404 ? -51.536 88.023 7.948   1.00 37.60 ? 545 ASP B O     1 
ATOM   6127 C CB    . ASP B 1 404 ? -53.002 90.117 5.855   1.00 37.16 ? 545 ASP B CB    1 
ATOM   6128 C CG    . ASP B 1 404 ? -52.628 91.434 5.205   1.00 40.58 ? 545 ASP B CG    1 
ATOM   6129 O OD1   . ASP B 1 404 ? -51.421 91.767 5.172   1.00 38.51 ? 545 ASP B OD1   1 
ATOM   6130 O OD2   . ASP B 1 404 ? -53.544 92.142 4.737   1.00 46.23 ? 545 ASP B OD2   1 
ATOM   6131 N N     . VAL B 1 405 ? -52.930 87.021 6.475   1.00 37.23 ? 546 VAL B N     1 
ATOM   6132 C CA    . VAL B 1 405 ? -53.127 85.850 7.334   1.00 38.26 ? 546 VAL B CA    1 
ATOM   6133 C C     . VAL B 1 405 ? -51.794 85.159 7.607   1.00 37.74 ? 546 VAL B C     1 
ATOM   6134 O O     . VAL B 1 405 ? -51.475 84.799 8.750   1.00 35.61 ? 546 VAL B O     1 
ATOM   6135 C CB    . VAL B 1 405 ? -54.140 84.880 6.701   1.00 40.04 ? 546 VAL B CB    1 
ATOM   6136 C CG1   . VAL B 1 405 ? -54.297 83.647 7.575   1.00 41.11 ? 546 VAL B CG1   1 
ATOM   6137 C CG2   . VAL B 1 405 ? -55.485 85.563 6.519   1.00 40.66 ? 546 VAL B CG2   1 
ATOM   6138 N N     . PHE B 1 406 ? -51.005 84.954 6.546   1.00 36.83 ? 547 PHE B N     1 
ATOM   6139 C CA    . PHE B 1 406 ? -49.709 84.293 6.662   1.00 31.70 ? 547 PHE B CA    1 
ATOM   6140 C C     . PHE B 1 406 ? -48.769 85.057 7.593   1.00 34.89 ? 547 PHE B C     1 
ATOM   6141 O O     . PHE B 1 406 ? -48.078 84.453 8.425   1.00 32.86 ? 547 PHE B O     1 
ATOM   6142 C CB    . PHE B 1 406 ? -49.106 84.159 5.265   1.00 31.46 ? 547 PHE B CB    1 
ATOM   6143 C CG    . PHE B 1 406 ? -47.638 83.907 5.249   1.00 31.96 ? 547 PHE B CG    1 
ATOM   6144 C CD1   . PHE B 1 406 ? -47.135 82.646 5.540   1.00 32.23 ? 547 PHE B CD1   1 
ATOM   6145 C CD2   . PHE B 1 406 ? -46.755 84.920 4.911   1.00 34.63 ? 547 PHE B CD2   1 
ATOM   6146 C CE1   . PHE B 1 406 ? -45.783 82.399 5.513   1.00 28.89 ? 547 PHE B CE1   1 
ATOM   6147 C CE2   . PHE B 1 406 ? -45.387 84.686 4.874   1.00 30.96 ? 547 PHE B CE2   1 
ATOM   6148 C CZ    . PHE B 1 406 ? -44.898 83.423 5.181   1.00 32.12 ? 547 PHE B CZ    1 
ATOM   6149 N N     . ILE B 1 407 ? -48.720 86.386 7.451   1.00 33.67 ? 548 ILE B N     1 
ATOM   6150 C CA    . ILE B 1 407 ? -47.844 87.209 8.287   1.00 35.91 ? 548 ILE B CA    1 
ATOM   6151 C C     . ILE B 1 407 ? -48.265 87.119 9.750   1.00 39.28 ? 548 ILE B C     1 
ATOM   6152 O O     . ILE B 1 407 ? -47.423 87.008 10.657  1.00 36.59 ? 548 ILE B O     1 
ATOM   6153 C CB    . ILE B 1 407 ? -47.847 88.668 7.787   1.00 34.98 ? 548 ILE B CB    1 
ATOM   6154 C CG1   . ILE B 1 407 ? -47.324 88.757 6.341   1.00 37.34 ? 548 ILE B CG1   1 
ATOM   6155 C CG2   . ILE B 1 407 ? -47.061 89.572 8.733   1.00 39.27 ? 548 ILE B CG2   1 
ATOM   6156 C CD1   . ILE B 1 407 ? -45.880 88.393 6.172   1.00 35.02 ? 548 ILE B CD1   1 
ATOM   6157 N N     . ASP B 1 408 ? -49.574 87.145 10.003  1.00 37.66 ? 549 ASP B N     1 
ATOM   6158 C CA    . ASP B 1 408 ? -50.044 87.045 11.383  1.00 40.54 ? 549 ASP B CA    1 
ATOM   6159 C C     . ASP B 1 408 ? -49.748 85.670 11.982  1.00 41.61 ? 549 ASP B C     1 
ATOM   6160 O O     . ASP B 1 408 ? -49.387 85.566 13.162  1.00 37.98 ? 549 ASP B O     1 
ATOM   6161 C CB    . ASP B 1 408 ? -51.532 87.369 11.444  1.00 42.95 ? 549 ASP B CB    1 
ATOM   6162 C CG    . ASP B 1 408 ? -51.811 88.848 11.184  1.00 58.74 ? 549 ASP B CG    1 
ATOM   6163 O OD1   . ASP B 1 408 ? -50.964 89.685 11.579  1.00 62.95 ? 549 ASP B OD1   1 
ATOM   6164 O OD2   . ASP B 1 408 ? -52.872 89.177 10.599  1.00 63.05 ? 549 ASP B OD2   1 
ATOM   6165 N N     . ALA B 1 409 ? -49.856 84.605 11.175  1.00 38.01 ? 550 ALA B N     1 
ATOM   6166 C CA    . ALA B 1 409 ? -49.552 83.265 11.676  1.00 38.23 ? 550 ALA B CA    1 
ATOM   6167 C C     . ALA B 1 409 ? -48.067 83.113 11.987  1.00 35.43 ? 550 ALA B C     1 
ATOM   6168 O O     . ALA B 1 409 ? -47.691 82.515 13.010  1.00 38.86 ? 550 ALA B O     1 
ATOM   6169 C CB    . ALA B 1 409 ? -50.001 82.207 10.667  1.00 38.78 ? 550 ALA B CB    1 
ATOM   6170 N N     . VAL B 1 410 ? -47.206 83.662 11.131  1.00 33.71 ? 551 VAL B N     1 
ATOM   6171 C CA    . VAL B 1 410 ? -45.777 83.620 11.424  1.00 35.65 ? 551 VAL B CA    1 
ATOM   6172 C C     . VAL B 1 410 ? -45.472 84.388 12.701  1.00 38.39 ? 551 VAL B C     1 
ATOM   6173 O O     . VAL B 1 410 ? -44.680 83.934 13.536  1.00 38.59 ? 551 VAL B O     1 
ATOM   6174 C CB    . VAL B 1 410 ? -44.951 84.149 10.241  1.00 32.41 ? 551 VAL B CB    1 
ATOM   6175 C CG1   . VAL B 1 410 ? -43.471 84.117 10.595  1.00 32.37 ? 551 VAL B CG1   1 
ATOM   6176 C CG2   . VAL B 1 410 ? -45.204 83.298 9.003   1.00 33.92 ? 551 VAL B CG2   1 
ATOM   6177 N N     . ARG B 1 411 ? -46.082 85.563 12.881  1.00 38.32 ? 552 ARG B N     1 
ATOM   6178 C CA    . ARG B 1 411 ? -45.768 86.311 14.094  1.00 39.48 ? 552 ARG B CA    1 
ATOM   6179 C C     . ARG B 1 411 ? -46.293 85.606 15.344  1.00 40.73 ? 552 ARG B C     1 
ATOM   6180 O O     . ARG B 1 411 ? -45.644 85.664 16.393  1.00 44.40 ? 552 ARG B O     1 
ATOM   6181 C CB    . ARG B 1 411 ? -46.298 87.740 13.998  1.00 45.59 ? 552 ARG B CB    1 
ATOM   6182 C CG    . ARG B 1 411 ? -45.830 88.629 15.155  1.00 56.84 ? 552 ARG B CG    1 
ATOM   6183 C CD    . ARG B 1 411 ? -46.350 90.067 15.054  1.00 66.41 ? 552 ARG B CD    1 
ATOM   6184 N NE    . ARG B 1 411 ? -47.478 90.202 14.138  1.00 68.00 ? 552 ARG B NE    1 
ATOM   6185 C CZ    . ARG B 1 411 ? -47.424 90.811 12.960  1.00 66.01 ? 552 ARG B CZ    1 
ATOM   6186 N NH1   . ARG B 1 411 ? -46.301 91.353 12.511  1.00 62.86 ? 552 ARG B NH1   1 
ATOM   6187 N NH2   . ARG B 1 411 ? -48.523 90.875 12.212  1.00 63.19 ? 552 ARG B NH2   1 
ATOM   6188 N N     . ARG B 1 412 ? -47.439 84.917 15.255  1.00 37.96 ? 553 ARG B N     1 
ATOM   6189 C CA    . ARG B 1 412 ? -47.893 84.111 16.389  1.00 42.18 ? 553 ARG B CA    1 
ATOM   6190 C C     . ARG B 1 412 ? -46.904 82.994 16.701  1.00 43.31 ? 553 ARG B C     1 
ATOM   6191 O O     . ARG B 1 412 ? -46.674 82.670 17.872  1.00 39.82 ? 553 ARG B O     1 
ATOM   6192 C CB    . ARG B 1 412 ? -49.273 83.509 16.121  1.00 43.49 ? 553 ARG B CB    1 
ATOM   6193 C CG    . ARG B 1 412 ? -50.427 84.476 16.224  1.00 42.04 ? 553 ARG B CG    1 
ATOM   6194 C CD    . ARG B 1 412 ? -51.751 83.743 16.394  1.00 49.17 ? 553 ARG B CD    1 
ATOM   6195 N NE    . ARG B 1 412 ? -52.216 83.144 15.145  1.00 50.86 ? 553 ARG B NE    1 
ATOM   6196 C CZ    . ARG B 1 412 ? -52.641 83.824 14.085  1.00 53.89 ? 553 ARG B CZ    1 
ATOM   6197 N NH1   . ARG B 1 412 ? -52.679 85.148 14.077  1.00 56.55 ? 553 ARG B NH1   1 
ATOM   6198 N NH2   . ARG B 1 412 ? -53.046 83.159 13.007  1.00 49.65 ? 553 ARG B NH2   1 
ATOM   6199 N N     . ILE B 1 413 ? -46.323 82.375 15.667  1.00 39.38 ? 554 ILE B N     1 
ATOM   6200 C CA    . ILE B 1 413 ? -45.344 81.323 15.927  1.00 38.34 ? 554 ILE B CA    1 
ATOM   6201 C C     . ILE B 1 413 ? -44.098 81.918 16.566  1.00 39.56 ? 554 ILE B C     1 
ATOM   6202 O O     . ILE B 1 413 ? -43.534 81.352 17.510  1.00 44.29 ? 554 ILE B O     1 
ATOM   6203 C CB    . ILE B 1 413 ? -44.994 80.552 14.641  1.00 37.23 ? 554 ILE B CB    1 
ATOM   6204 C CG1   . ILE B 1 413 ? -46.096 79.568 14.272  1.00 37.19 ? 554 ILE B CG1   1 
ATOM   6205 C CG2   . ILE B 1 413 ? -43.727 79.746 14.835  1.00 36.73 ? 554 ILE B CG2   1 
ATOM   6206 C CD1   . ILE B 1 413 ? -46.400 79.566 12.784  1.00 37.95 ? 554 ILE B CD1   1 
ATOM   6207 N N     . ALA B 1 414 ? -43.666 83.087 16.082  1.00 36.70 ? 555 ALA B N     1 
ATOM   6208 C CA    . ALA B 1 414 ? -42.467 83.727 16.618  1.00 40.38 ? 555 ALA B CA    1 
ATOM   6209 C C     . ALA B 1 414 ? -42.672 84.192 18.059  1.00 44.09 ? 555 ALA B C     1 
ATOM   6210 O O     . ALA B 1 414 ? -41.756 84.091 18.881  1.00 43.33 ? 555 ALA B O     1 
ATOM   6211 C CB    . ALA B 1 414 ? -42.057 84.904 15.733  1.00 37.20 ? 555 ALA B CB    1 
ATOM   6212 N N     . GLU B 1 415 ? -43.856 84.720 18.377  1.00 40.30 ? 556 GLU B N     1 
ATOM   6213 C CA    . GLU B 1 415 ? -44.158 85.142 19.739  1.00 44.50 ? 556 GLU B CA    1 
ATOM   6214 C C     . GLU B 1 415 ? -44.480 83.979 20.665  1.00 44.08 ? 556 GLU B C     1 
ATOM   6215 O O     . GLU B 1 415 ? -44.566 84.186 21.878  1.00 45.99 ? 556 GLU B O     1 
ATOM   6216 C CB    . GLU B 1 415 ? -45.330 86.126 19.751  1.00 45.64 ? 556 GLU B CB    1 
ATOM   6217 C CG    . GLU B 1 415 ? -45.030 87.478 19.142  1.00 46.71 ? 556 GLU B CG    1 
ATOM   6218 C CD    . GLU B 1 415 ? -46.260 88.368 19.102  1.00 61.15 ? 556 GLU B CD    1 
ATOM   6219 O OE1   . GLU B 1 415 ? -47.175 88.146 19.929  1.00 64.26 ? 556 GLU B OE1   1 
ATOM   6220 O OE2   . GLU B 1 415 ? -46.300 89.301 18.268  1.00 62.40 ? 556 GLU B OE2   1 
ATOM   6221 N N     . GLY B 1 416 ? -44.677 82.778 20.128  1.00 47.33 ? 557 GLY B N     1 
ATOM   6222 C CA    . GLY B 1 416 ? -44.908 81.608 20.941  1.00 46.33 ? 557 GLY B CA    1 
ATOM   6223 C C     . GLY B 1 416 ? -43.622 81.067 21.536  1.00 44.37 ? 557 GLY B C     1 
ATOM   6224 O O     . GLY B 1 416 ? -42.583 81.725 21.579  1.00 45.32 ? 557 GLY B O     1 
ATOM   6225 N N     . SER B 1 417 ? -43.705 79.827 22.001  1.00 46.78 ? 558 SER B N     1 
ATOM   6226 C CA    . SER B 1 417 ? -42.557 79.172 22.607  1.00 51.50 ? 558 SER B CA    1 
ATOM   6227 C C     . SER B 1 417 ? -41.592 78.679 21.531  1.00 48.88 ? 558 SER B C     1 
ATOM   6228 O O     . SER B 1 417 ? -42.008 78.146 20.499  1.00 46.53 ? 558 SER B O     1 
ATOM   6229 C CB    . SER B 1 417 ? -43.030 78.011 23.486  1.00 50.55 ? 558 SER B CB    1 
ATOM   6230 O OG    . SER B 1 417 ? -42.071 76.973 23.553  1.00 56.16 ? 558 SER B OG    1 
ATOM   6231 N N     . VAL B 1 418 ? -40.292 78.873 21.771  1.00 50.22 ? 559 VAL B N     1 
ATOM   6232 C CA    . VAL B 1 418 ? -39.263 78.328 20.889  1.00 53.22 ? 559 VAL B CA    1 
ATOM   6233 C C     . VAL B 1 418 ? -39.227 76.815 21.059  1.00 59.17 ? 559 VAL B C     1 
ATOM   6234 O O     . VAL B 1 418 ? -39.948 76.254 21.893  1.00 56.61 ? 559 VAL B O     1 
ATOM   6235 C CB    . VAL B 1 418 ? -37.883 78.949 21.169  1.00 52.28 ? 559 VAL B CB    1 
ATOM   6236 C CG1   . VAL B 1 418 ? -37.947 80.464 21.051  1.00 49.85 ? 559 VAL B CG1   1 
ATOM   6237 C CG2   . VAL B 1 418 ? -37.389 78.535 22.552  1.00 51.79 ? 559 VAL B CG2   1 
ATOM   6238 N N     . ASP B 1 419 ? -38.389 76.141 20.275  1.00 61.06 ? 560 ASP B N     1 
ATOM   6239 C CA    . ASP B 1 419 ? -38.346 74.686 20.312  1.00 71.89 ? 560 ASP B CA    1 
ATOM   6240 C C     . ASP B 1 419 ? -37.442 74.211 21.446  1.00 79.62 ? 560 ASP B C     1 
ATOM   6241 O O     . ASP B 1 419 ? -36.349 74.749 21.647  1.00 79.26 ? 560 ASP B O     1 
ATOM   6242 C CB    . ASP B 1 419 ? -37.877 74.133 18.967  1.00 70.61 ? 560 ASP B CB    1 
ATOM   6243 C CG    . ASP B 1 419 ? -38.223 72.667 18.793  1.00 78.88 ? 560 ASP B CG    1 
ATOM   6244 O OD1   . ASP B 1 419 ? -38.852 72.095 19.708  1.00 81.76 ? 560 ASP B OD1   1 
ATOM   6245 O OD2   . ASP B 1 419 ? -37.879 72.091 17.737  1.00 77.98 ? 560 ASP B OD2   1 
HETATM 6246 O O     . HOH C 2 .   ? -23.362 34.691 -28.320 1.00 41.73 ? 601 HOH A O     1 
HETATM 6247 O O     . HOH C 2 .   ? -39.033 30.003 -12.562 1.00 50.48 ? 602 HOH A O     1 
HETATM 6248 O O     . HOH C 2 .   ? -20.725 63.032 -8.775  1.00 28.29 ? 603 HOH A O     1 
HETATM 6249 O O     . HOH C 2 .   ? -46.572 54.728 -23.682 1.00 24.85 ? 604 HOH A O     1 
HETATM 6250 O O     . HOH C 2 .   ? -29.743 32.627 -26.074 1.00 30.22 ? 605 HOH A O     1 
HETATM 6251 O O     . HOH C 2 .   ? -37.226 39.063 -5.284  1.00 31.33 ? 606 HOH A O     1 
HETATM 6252 O O     . HOH C 2 .   ? -73.987 39.706 -40.443 1.00 33.96 ? 607 HOH A O     1 
HETATM 6253 O O     . HOH C 2 .   ? -73.262 47.007 -41.820 1.00 35.58 ? 608 HOH A O     1 
HETATM 6254 O O     . HOH C 2 .   ? -60.654 43.772 -21.545 1.00 21.56 ? 609 HOH A O     1 
HETATM 6255 O O     . HOH C 2 .   ? -57.737 47.391 -33.574 1.00 24.43 ? 610 HOH A O     1 
HETATM 6256 O O     . HOH C 2 .   ? -24.117 59.292 -8.881  1.00 35.14 ? 611 HOH A O     1 
HETATM 6257 O O     . HOH C 2 .   ? -60.839 32.019 -29.117 1.00 42.12 ? 612 HOH A O     1 
HETATM 6258 O O     . HOH C 2 .   ? -70.735 61.441 -13.101 1.00 33.75 ? 613 HOH A O     1 
HETATM 6259 O O     . HOH C 2 .   ? -61.387 46.676 -5.828  1.00 32.03 ? 614 HOH A O     1 
HETATM 6260 O O     . HOH C 2 .   ? -53.218 33.295 -42.659 1.00 36.02 ? 615 HOH A O     1 
HETATM 6261 O O     . HOH C 2 .   ? -74.033 50.362 -40.701 1.00 52.26 ? 616 HOH A O     1 
HETATM 6262 O O     . HOH C 2 .   ? -24.190 65.228 2.277   1.00 36.87 ? 617 HOH A O     1 
HETATM 6263 O O     . HOH C 2 .   ? -46.999 28.072 -27.959 1.00 37.36 ? 618 HOH A O     1 
HETATM 6264 O O     . HOH C 2 .   ? -77.650 41.267 -35.383 1.00 30.73 ? 619 HOH A O     1 
HETATM 6265 O O     . HOH C 2 .   ? -41.528 57.178 -5.603  1.00 21.54 ? 620 HOH A O     1 
HETATM 6266 O O     . HOH C 2 .   ? -28.811 56.781 -16.023 1.00 25.78 ? 621 HOH A O     1 
HETATM 6267 O O     . HOH C 2 .   ? -38.984 61.454 -15.137 1.00 17.02 ? 622 HOH A O     1 
HETATM 6268 O O     . HOH C 2 .   ? -43.569 39.732 -6.383  1.00 21.35 ? 623 HOH A O     1 
HETATM 6269 O O     . HOH C 2 .   ? -30.783 55.999 -21.467 1.00 28.89 ? 624 HOH A O     1 
HETATM 6270 O O     . HOH C 2 .   ? -41.460 23.483 -31.463 1.00 52.94 ? 625 HOH A O     1 
HETATM 6271 O O     . HOH C 2 .   ? -47.088 28.390 -19.578 1.00 45.23 ? 626 HOH A O     1 
HETATM 6272 O O     . HOH C 2 .   ? -35.512 62.864 -2.965  1.00 30.02 ? 627 HOH A O     1 
HETATM 6273 O O     . HOH C 2 .   ? -56.807 56.103 -24.061 1.00 15.48 ? 628 HOH A O     1 
HETATM 6274 O O     . HOH C 2 .   ? -52.937 52.165 0.559   1.00 42.05 ? 629 HOH A O     1 
HETATM 6275 O O     . HOH C 2 .   ? -57.069 61.402 -1.064  1.00 26.63 ? 630 HOH A O     1 
HETATM 6276 O O     . HOH C 2 .   ? -19.879 60.779 0.067   1.00 51.97 ? 631 HOH A O     1 
HETATM 6277 O O     . HOH C 2 .   ? -47.214 58.269 3.696   1.00 43.56 ? 632 HOH A O     1 
HETATM 6278 O O     . HOH C 2 .   ? -49.753 27.801 -28.965 1.00 45.55 ? 633 HOH A O     1 
HETATM 6279 O O     . HOH C 2 .   ? -46.445 58.428 -11.435 1.00 26.36 ? 634 HOH A O     1 
HETATM 6280 O O     . HOH C 2 .   ? -39.917 38.911 -39.646 1.00 24.76 ? 635 HOH A O     1 
HETATM 6281 O O     . HOH C 2 .   ? -51.709 54.960 -20.011 1.00 16.06 ? 636 HOH A O     1 
HETATM 6282 O O     . HOH C 2 .   ? -44.374 42.834 -27.474 1.00 21.19 ? 637 HOH A O     1 
HETATM 6283 O O     . HOH C 2 .   ? -40.163 55.701 -13.521 1.00 24.09 ? 638 HOH A O     1 
HETATM 6284 O O     . HOH C 2 .   ? -55.201 45.875 -1.421  1.00 28.63 ? 639 HOH A O     1 
HETATM 6285 O O     . HOH C 2 .   ? -59.879 38.454 -23.922 1.00 27.99 ? 640 HOH A O     1 
HETATM 6286 O O     . HOH C 2 .   ? -63.304 55.874 -5.888  1.00 35.62 ? 641 HOH A O     1 
HETATM 6287 O O     . HOH C 2 .   ? -72.137 37.261 -13.739 1.00 38.99 ? 642 HOH A O     1 
HETATM 6288 O O     . HOH C 2 .   ? -26.766 55.896 -3.365  1.00 28.38 ? 643 HOH A O     1 
HETATM 6289 O O     . HOH C 2 .   ? -42.224 37.567 -10.131 1.00 21.83 ? 644 HOH A O     1 
HETATM 6290 O O     . HOH C 2 .   ? -61.319 32.441 -44.669 1.00 35.49 ? 645 HOH A O     1 
HETATM 6291 O O     . HOH C 2 .   ? -63.859 52.903 -6.768  1.00 33.29 ? 646 HOH A O     1 
HETATM 6292 O O     . HOH C 2 .   ? -66.049 64.334 -14.246 1.00 29.49 ? 647 HOH A O     1 
HETATM 6293 O O     . HOH C 2 .   ? -37.042 50.249 -0.677  1.00 39.09 ? 648 HOH A O     1 
HETATM 6294 O O     . HOH C 2 .   ? -18.905 66.640 0.599   1.00 51.77 ? 649 HOH A O     1 
HETATM 6295 O O     . HOH C 2 .   ? -41.565 62.391 -13.237 1.00 24.90 ? 650 HOH A O     1 
HETATM 6296 O O     . HOH C 2 .   ? -57.163 54.261 -31.364 1.00 19.82 ? 651 HOH A O     1 
HETATM 6297 O O     . HOH C 2 .   ? -35.203 35.205 -11.031 1.00 36.54 ? 652 HOH A O     1 
HETATM 6298 O O     . HOH C 2 .   ? -66.057 29.857 -41.299 1.00 38.31 ? 653 HOH A O     1 
HETATM 6299 O O     . HOH C 2 .   ? -55.967 31.482 -41.524 1.00 33.75 ? 654 HOH A O     1 
HETATM 6300 O O     . HOH C 2 .   ? -40.129 29.745 -30.739 1.00 32.99 ? 655 HOH A O     1 
HETATM 6301 O O     . HOH C 2 .   ? -43.451 58.984 -8.264  1.00 20.85 ? 656 HOH A O     1 
HETATM 6302 O O     . HOH C 2 .   ? -62.416 33.167 -17.353 1.00 27.05 ? 657 HOH A O     1 
HETATM 6303 O O     . HOH C 2 .   ? -58.240 35.442 -21.646 1.00 30.83 ? 658 HOH A O     1 
HETATM 6304 O O     . HOH C 2 .   ? -45.699 61.047 3.006   1.00 38.63 ? 659 HOH A O     1 
HETATM 6305 O O     . HOH C 2 .   ? -53.714 30.545 -39.819 1.00 33.52 ? 660 HOH A O     1 
HETATM 6306 O O     . HOH C 2 .   ? -72.594 51.726 -36.767 1.00 31.21 ? 661 HOH A O     1 
HETATM 6307 O O     . HOH C 2 .   ? -70.723 52.211 -29.013 1.00 23.03 ? 662 HOH A O     1 
HETATM 6308 O O     . HOH C 2 .   ? -60.534 35.651 -23.211 1.00 29.03 ? 663 HOH A O     1 
HETATM 6309 O O     . HOH C 2 .   ? -72.572 50.155 -31.138 1.00 25.09 ? 664 HOH A O     1 
HETATM 6310 O O     . HOH C 2 .   ? -58.314 48.626 -51.973 1.00 26.06 ? 665 HOH A O     1 
HETATM 6311 O O     . HOH C 2 .   ? -68.790 52.668 -11.863 1.00 28.73 ? 666 HOH A O     1 
HETATM 6312 O O     . HOH C 2 .   ? -56.183 56.387 -5.042  1.00 24.20 ? 667 HOH A O     1 
HETATM 6313 O O     . HOH C 2 .   ? -47.766 41.390 -32.119 1.00 24.31 ? 668 HOH A O     1 
HETATM 6314 O O     . HOH C 2 .   ? -73.319 43.923 -15.300 1.00 32.45 ? 669 HOH A O     1 
HETATM 6315 O O     . HOH C 2 .   ? -50.334 57.004 -22.690 1.00 21.69 ? 670 HOH A O     1 
HETATM 6316 O O     . HOH C 2 .   ? -59.673 34.002 -33.776 1.00 26.70 ? 671 HOH A O     1 
HETATM 6317 O O     . HOH C 2 .   ? -64.282 37.233 -12.247 1.00 32.16 ? 672 HOH A O     1 
HETATM 6318 O O     . HOH C 2 .   ? -41.242 32.467 -36.978 1.00 28.77 ? 673 HOH A O     1 
HETATM 6319 O O     . HOH C 2 .   ? -76.199 50.318 -22.416 1.00 26.95 ? 674 HOH A O     1 
HETATM 6320 O O     . HOH C 2 .   ? -48.999 41.521 -24.066 1.00 18.75 ? 675 HOH A O     1 
HETATM 6321 O O     . HOH C 2 .   ? -50.223 35.213 -13.976 1.00 31.62 ? 676 HOH A O     1 
HETATM 6322 O O     . HOH C 2 .   ? -35.470 46.056 -4.848  1.00 27.24 ? 677 HOH A O     1 
HETATM 6323 O O     . HOH C 2 .   ? -53.347 40.128 -4.971  1.00 32.57 ? 678 HOH A O     1 
HETATM 6324 O O     . HOH C 2 .   ? -74.067 37.357 -15.856 1.00 32.07 ? 679 HOH A O     1 
HETATM 6325 O O     . HOH C 2 .   ? -55.249 62.164 -18.135 1.00 22.50 ? 680 HOH A O     1 
HETATM 6326 O O     . HOH C 2 .   ? -56.797 46.769 -24.406 1.00 21.49 ? 681 HOH A O     1 
HETATM 6327 O O     . HOH C 2 .   ? -39.820 39.209 -5.330  1.00 37.43 ? 682 HOH A O     1 
HETATM 6328 O O     . HOH C 2 .   ? -55.528 41.173 -15.330 1.00 19.42 ? 683 HOH A O     1 
HETATM 6329 O O     . HOH C 2 .   ? -43.143 41.312 -34.593 1.00 20.09 ? 684 HOH A O     1 
HETATM 6330 O O     . HOH C 2 .   ? -62.240 52.088 -38.964 1.00 21.15 ? 685 HOH A O     1 
HETATM 6331 O O     . HOH C 2 .   ? -67.788 32.399 -22.622 1.00 29.37 ? 686 HOH A O     1 
HETATM 6332 O O     . HOH C 2 .   ? -51.690 47.520 -20.829 1.00 19.93 ? 687 HOH A O     1 
HETATM 6333 O O     . HOH C 2 .   ? -73.069 37.836 -38.595 1.00 31.56 ? 688 HOH A O     1 
HETATM 6334 O O     . HOH C 2 .   ? -34.368 27.507 -32.423 1.00 45.43 ? 689 HOH A O     1 
HETATM 6335 O O     . HOH C 2 .   ? -66.195 56.458 -22.432 1.00 16.84 ? 690 HOH A O     1 
HETATM 6336 O O     . HOH C 2 .   ? -55.871 37.509 -35.336 1.00 22.50 ? 691 HOH A O     1 
HETATM 6337 O O     . HOH C 2 .   ? -48.582 51.917 -1.823  1.00 27.31 ? 692 HOH A O     1 
HETATM 6338 O O     . HOH C 2 .   ? -74.945 60.767 -29.237 1.00 43.50 ? 693 HOH A O     1 
HETATM 6339 O O     . HOH C 2 .   ? -54.354 34.026 -16.533 1.00 37.64 ? 694 HOH A O     1 
HETATM 6340 O O     . HOH C 2 .   ? -50.768 69.384 -10.017 1.00 18.47 ? 695 HOH A O     1 
HETATM 6341 O O     . HOH C 2 .   ? -48.924 68.539 7.999   1.00 57.29 ? 696 HOH A O     1 
HETATM 6342 O O     . HOH C 2 .   ? -75.032 46.602 -29.686 1.00 22.23 ? 697 HOH A O     1 
HETATM 6343 O O     . HOH C 2 .   ? -58.175 50.252 -4.486  1.00 28.64 ? 698 HOH A O     1 
HETATM 6344 O O     . HOH C 2 .   ? -38.728 58.627 -13.584 1.00 24.03 ? 699 HOH A O     1 
HETATM 6345 O O     . HOH C 2 .   ? -55.977 52.262 -39.739 1.00 30.69 ? 700 HOH A O     1 
HETATM 6346 O O     . HOH C 2 .   ? -75.992 48.977 -24.644 1.00 36.23 ? 701 HOH A O     1 
HETATM 6347 O O     . HOH C 2 .   ? -42.513 35.056 -6.391  1.00 35.10 ? 702 HOH A O     1 
HETATM 6348 O O     . HOH C 2 .   ? -59.119 43.865 -56.760 1.00 35.90 ? 703 HOH A O     1 
HETATM 6349 O O     . HOH C 2 .   ? -52.317 32.954 -39.530 1.00 29.71 ? 704 HOH A O     1 
HETATM 6350 O O     . HOH C 2 .   ? -60.832 37.230 -26.466 1.00 24.27 ? 705 HOH A O     1 
HETATM 6351 O O     . HOH C 2 .   ? -53.286 26.883 -33.998 1.00 32.34 ? 706 HOH A O     1 
HETATM 6352 O O     . HOH C 2 .   ? -49.376 42.858 -47.629 1.00 36.45 ? 707 HOH A O     1 
HETATM 6353 O O     . HOH C 2 .   ? -42.047 60.256 -9.945  1.00 26.32 ? 708 HOH A O     1 
HETATM 6354 O O     . HOH C 2 .   ? -60.281 34.572 -25.861 1.00 30.20 ? 709 HOH A O     1 
HETATM 6355 O O     . HOH C 2 .   ? -56.852 43.139 -47.387 1.00 30.94 ? 710 HOH A O     1 
HETATM 6356 O O     . HOH C 2 .   ? -68.528 50.158 -29.318 1.00 20.66 ? 711 HOH A O     1 
HETATM 6357 O O     . HOH C 2 .   ? -70.531 35.252 -42.651 1.00 32.93 ? 712 HOH A O     1 
HETATM 6358 O O     . HOH C 2 .   ? -55.765 50.268 -3.201  1.00 25.83 ? 713 HOH A O     1 
HETATM 6359 O O     . HOH C 2 .   ? -69.334 62.183 -19.354 1.00 32.73 ? 714 HOH A O     1 
HETATM 6360 O O     . HOH C 2 .   ? -40.302 40.872 -2.472  1.00 49.41 ? 715 HOH A O     1 
HETATM 6361 O O     . HOH C 2 .   ? -34.093 56.217 -11.855 1.00 16.32 ? 716 HOH A O     1 
HETATM 6362 O O     . HOH C 2 .   ? -38.490 21.206 -21.885 1.00 54.27 ? 717 HOH A O     1 
HETATM 6363 O O     . HOH C 2 .   ? -44.189 52.731 -40.062 1.00 38.67 ? 718 HOH A O     1 
HETATM 6364 O O     . HOH C 2 .   ? -54.042 68.738 7.733   1.00 34.85 ? 719 HOH A O     1 
HETATM 6365 O O     . HOH C 2 .   ? -71.175 55.070 -14.887 1.00 22.78 ? 720 HOH A O     1 
HETATM 6366 O O     . HOH C 2 .   ? -64.095 56.682 -43.359 1.00 30.75 ? 721 HOH A O     1 
HETATM 6367 O O     . HOH C 2 .   ? -63.596 47.000 -7.016  1.00 28.95 ? 722 HOH A O     1 
HETATM 6368 O O     . HOH C 2 .   ? -46.702 52.189 -28.932 1.00 22.79 ? 723 HOH A O     1 
HETATM 6369 O O     . HOH C 2 .   ? -42.118 55.481 -1.309  1.00 39.83 ? 724 HOH A O     1 
HETATM 6370 O O     . HOH C 2 .   ? -69.519 32.442 -28.858 1.00 29.83 ? 725 HOH A O     1 
HETATM 6371 O O     . HOH C 2 .   ? -51.850 43.203 -46.515 1.00 31.56 ? 726 HOH A O     1 
HETATM 6372 O O     . HOH C 2 .   ? -65.408 54.914 -36.157 1.00 23.97 ? 727 HOH A O     1 
HETATM 6373 O O     . HOH C 2 .   ? -72.836 54.380 -22.915 1.00 27.43 ? 728 HOH A O     1 
HETATM 6374 O O     . HOH C 2 .   ? -57.829 41.583 -7.957  1.00 33.04 ? 729 HOH A O     1 
HETATM 6375 O O     . HOH C 2 .   ? -50.003 33.239 -20.576 1.00 31.14 ? 730 HOH A O     1 
HETATM 6376 O O     . HOH C 2 .   ? -43.137 29.798 -14.229 1.00 40.08 ? 731 HOH A O     1 
HETATM 6377 O O     . HOH C 2 .   ? -38.670 56.280 -15.657 1.00 23.61 ? 732 HOH A O     1 
HETATM 6378 O O     . HOH C 2 .   ? -49.056 49.274 -0.210  1.00 34.89 ? 733 HOH A O     1 
HETATM 6379 O O     . HOH C 2 .   ? -62.404 32.735 -49.122 1.00 46.09 ? 734 HOH A O     1 
HETATM 6380 O O     . HOH C 2 .   ? -28.019 55.851 -0.624  1.00 40.07 ? 735 HOH A O     1 
HETATM 6381 O O     . HOH C 2 .   ? -20.096 32.075 -26.572 1.00 51.03 ? 736 HOH A O     1 
HETATM 6382 O O     . HOH C 2 .   ? -71.129 53.946 -45.880 1.00 45.66 ? 737 HOH A O     1 
HETATM 6383 O O     . HOH C 2 .   ? -71.637 58.443 -18.138 1.00 30.84 ? 738 HOH A O     1 
HETATM 6384 O O     . HOH C 2 .   ? -55.088 27.149 -37.535 1.00 39.02 ? 739 HOH A O     1 
HETATM 6385 O O     . HOH C 2 .   ? -41.854 68.745 1.855   1.00 44.32 ? 740 HOH A O     1 
HETATM 6386 O O     . HOH C 2 .   ? -72.034 51.647 -12.455 1.00 34.08 ? 741 HOH A O     1 
HETATM 6387 O O     . HOH C 2 .   ? -19.515 67.127 -9.661  1.00 35.12 ? 742 HOH A O     1 
HETATM 6388 O O     . HOH C 2 .   ? -37.211 54.866 0.167   1.00 39.42 ? 743 HOH A O     1 
HETATM 6389 O O     . HOH C 2 .   ? -72.259 61.880 -36.846 1.00 42.68 ? 744 HOH A O     1 
HETATM 6390 O O     . HOH C 2 .   ? -43.291 58.231 -12.391 1.00 31.96 ? 745 HOH A O     1 
HETATM 6391 O O     . HOH C 2 .   ? -60.937 40.618 -11.177 1.00 29.90 ? 746 HOH A O     1 
HETATM 6392 O O     . HOH C 2 .   ? -73.578 55.035 -30.385 1.00 36.79 ? 747 HOH A O     1 
HETATM 6393 O O     . HOH C 2 .   ? -63.921 41.662 -53.760 1.00 43.61 ? 748 HOH A O     1 
HETATM 6394 O O     . HOH C 2 .   ? -45.256 47.014 -43.129 1.00 35.50 ? 749 HOH A O     1 
HETATM 6395 O O     . HOH C 2 .   ? -49.485 36.648 -5.557  1.00 39.92 ? 750 HOH A O     1 
HETATM 6396 O O     . HOH C 2 .   ? -53.495 49.216 -46.884 1.00 31.88 ? 751 HOH A O     1 
HETATM 6397 O O     . HOH C 2 .   ? -57.283 44.584 -26.855 1.00 29.52 ? 752 HOH A O     1 
HETATM 6398 O O     . HOH C 2 .   ? -48.935 54.866 -22.071 1.00 20.08 ? 753 HOH A O     1 
HETATM 6399 O O     . HOH C 2 .   ? -55.306 40.312 -12.802 1.00 23.38 ? 754 HOH A O     1 
HETATM 6400 O O     . HOH C 2 .   ? -57.723 26.454 -30.620 1.00 51.05 ? 755 HOH A O     1 
HETATM 6401 O O     . HOH C 2 .   ? -26.084 30.554 -25.599 1.00 37.78 ? 756 HOH A O     1 
HETATM 6402 O O     . HOH C 2 .   ? -46.297 60.550 -18.172 1.00 31.74 ? 757 HOH A O     1 
HETATM 6403 O O     . HOH C 2 .   ? -68.687 51.901 -46.196 1.00 36.16 ? 758 HOH A O     1 
HETATM 6404 O O     . HOH C 2 .   ? -51.557 39.987 -3.373  1.00 42.42 ? 759 HOH A O     1 
HETATM 6405 O O     . HOH C 2 .   ? -62.477 40.533 -9.178  1.00 44.23 ? 760 HOH A O     1 
HETATM 6406 O O     . HOH C 2 .   ? -51.444 29.811 -28.237 1.00 32.58 ? 761 HOH A O     1 
HETATM 6407 O O     . HOH C 2 .   ? -46.938 41.543 -28.970 1.00 28.41 ? 762 HOH A O     1 
HETATM 6408 O O     . HOH C 2 .   ? -53.005 71.911 1.681   1.00 27.05 ? 763 HOH A O     1 
HETATM 6409 O O     . HOH C 2 .   ? -58.610 31.114 -27.704 1.00 36.21 ? 764 HOH A O     1 
HETATM 6410 O O     . HOH C 2 .   ? -49.403 36.413 -47.901 1.00 40.30 ? 765 HOH A O     1 
HETATM 6411 O O     . HOH C 2 .   ? -68.299 54.135 -14.180 1.00 21.35 ? 766 HOH A O     1 
HETATM 6412 O O     . HOH C 2 .   ? -52.682 49.703 -35.477 1.00 30.21 ? 767 HOH A O     1 
HETATM 6413 O O     . HOH C 2 .   ? -64.956 58.069 -9.249  1.00 29.85 ? 768 HOH A O     1 
HETATM 6414 O O     . HOH C 2 .   ? -32.514 34.666 -34.215 1.00 32.42 ? 769 HOH A O     1 
HETATM 6415 O O     . HOH C 2 .   ? -74.859 51.930 -26.536 1.00 33.01 ? 770 HOH A O     1 
HETATM 6416 O O     . HOH C 2 .   ? -64.098 32.280 -47.289 1.00 49.91 ? 771 HOH A O     1 
HETATM 6417 O O     . HOH C 2 .   ? -75.922 43.339 -11.159 1.00 44.46 ? 772 HOH A O     1 
HETATM 6418 O O     . HOH C 2 .   ? -44.813 24.518 -29.354 1.00 39.49 ? 773 HOH A O     1 
HETATM 6419 O O     . HOH C 2 .   ? -72.614 61.963 -31.031 1.00 43.16 ? 774 HOH A O     1 
HETATM 6420 O O     . HOH C 2 .   ? -51.672 48.011 -31.061 1.00 30.25 ? 775 HOH A O     1 
HETATM 6421 O O     . HOH C 2 .   ? -62.632 53.071 -48.615 1.00 38.46 ? 776 HOH A O     1 
HETATM 6422 O O     . HOH C 2 .   ? -76.755 43.899 -35.483 1.00 33.15 ? 777 HOH A O     1 
HETATM 6423 O O     . HOH C 2 .   ? -59.063 32.115 -42.888 1.00 35.27 ? 778 HOH A O     1 
HETATM 6424 O O     . HOH C 2 .   ? -28.879 53.704 -16.260 1.00 25.58 ? 779 HOH A O     1 
HETATM 6425 O O     . HOH C 2 .   ? -29.059 37.267 -16.295 1.00 33.73 ? 780 HOH A O     1 
HETATM 6426 O O     . HOH C 2 .   ? -75.677 55.560 -19.650 1.00 38.13 ? 781 HOH A O     1 
HETATM 6427 O O     . HOH C 2 .   ? -72.231 56.251 -16.805 1.00 28.53 ? 782 HOH A O     1 
HETATM 6428 O O     . HOH C 2 .   ? -45.958 58.930 -16.118 1.00 29.37 ? 783 HOH A O     1 
HETATM 6429 O O     . HOH C 2 .   ? -53.284 56.931 5.409   1.00 50.69 ? 784 HOH A O     1 
HETATM 6430 O O     . HOH C 2 .   ? -65.762 64.246 -9.689  1.00 38.24 ? 785 HOH A O     1 
HETATM 6431 O O     . HOH C 2 .   ? -23.315 61.425 -8.048  1.00 21.99 ? 786 HOH A O     1 
HETATM 6432 O O     . HOH C 2 .   ? -30.383 52.480 -4.231  1.00 32.30 ? 787 HOH A O     1 
HETATM 6433 O O     . HOH C 2 .   ? -45.879 61.983 -20.645 1.00 24.62 ? 788 HOH A O     1 
HETATM 6434 O O     . HOH C 2 .   ? -44.395 54.722 -22.490 1.00 17.47 ? 789 HOH A O     1 
HETATM 6435 O O     . HOH C 2 .   ? -64.335 37.900 -52.795 1.00 53.97 ? 790 HOH A O     1 
HETATM 6436 O O     . HOH C 2 .   ? -44.036 62.753 -6.970  1.00 28.50 ? 791 HOH A O     1 
HETATM 6437 O O     . HOH C 2 .   ? -69.469 43.825 -8.334  1.00 49.27 ? 792 HOH A O     1 
HETATM 6438 O O     . HOH C 2 .   ? -17.740 65.269 -8.808  1.00 31.45 ? 793 HOH A O     1 
HETATM 6439 O O     . HOH C 2 .   ? -46.301 46.363 0.309   1.00 34.15 ? 794 HOH A O     1 
HETATM 6440 O O     . HOH C 2 .   ? -27.261 51.077 -21.674 1.00 42.39 ? 795 HOH A O     1 
HETATM 6441 O O     . HOH C 2 .   ? -29.558 53.392 -35.791 1.00 38.11 ? 796 HOH A O     1 
HETATM 6442 O O     . HOH C 2 .   ? -62.928 40.057 -52.085 1.00 48.25 ? 797 HOH A O     1 
HETATM 6443 O O     . HOH C 2 .   ? -36.011 56.131 -14.289 1.00 16.98 ? 798 HOH A O     1 
HETATM 6444 O O     . HOH C 2 .   ? -48.348 30.427 -28.420 1.00 30.45 ? 799 HOH A O     1 
HETATM 6445 O O     . HOH C 2 .   ? -57.910 30.191 -33.144 1.00 38.19 ? 800 HOH A O     1 
HETATM 6446 O O     . HOH C 2 .   ? -76.116 32.173 -38.970 1.00 38.24 ? 801 HOH A O     1 
HETATM 6447 O O     . HOH C 2 .   ? -38.228 46.453 -4.676  1.00 28.09 ? 802 HOH A O     1 
HETATM 6448 O O     . HOH C 2 .   ? -28.891 45.977 -33.386 1.00 38.09 ? 803 HOH A O     1 
HETATM 6449 O O     . HOH C 2 .   ? -28.225 50.306 -7.594  1.00 35.77 ? 804 HOH A O     1 
HETATM 6450 O O     . HOH C 2 .   ? -74.060 56.927 -21.577 1.00 33.29 ? 805 HOH A O     1 
HETATM 6451 O O     . HOH C 2 .   ? -59.415 45.747 -24.444 1.00 24.27 ? 806 HOH A O     1 
HETATM 6452 O O     . HOH C 2 .   ? -67.018 31.029 -24.939 1.00 37.16 ? 807 HOH A O     1 
HETATM 6453 O O     . HOH C 2 .   ? -51.188 34.988 -16.402 1.00 31.20 ? 808 HOH A O     1 
HETATM 6454 O O     . HOH C 2 .   ? -57.637 36.468 -10.003 1.00 46.40 ? 809 HOH A O     1 
HETATM 6455 O O     . HOH C 2 .   ? -29.692 47.476 -35.226 1.00 49.50 ? 810 HOH A O     1 
HETATM 6456 O O     . HOH C 2 .   ? -78.414 51.203 -21.311 1.00 30.60 ? 811 HOH A O     1 
HETATM 6457 O O     . HOH C 2 .   ? -21.551 46.713 -22.736 1.00 26.58 ? 812 HOH A O     1 
HETATM 6458 O O     . HOH C 2 .   ? -54.283 43.803 -51.732 1.00 50.23 ? 813 HOH A O     1 
HETATM 6459 O O     . HOH C 2 .   ? -51.608 50.087 -37.730 1.00 31.01 ? 814 HOH A O     1 
HETATM 6460 O O     . HOH C 2 .   ? -80.773 42.206 -29.987 1.00 46.15 ? 815 HOH A O     1 
HETATM 6461 O O     . HOH C 2 .   ? -52.275 49.896 -32.760 1.00 26.20 ? 816 HOH A O     1 
HETATM 6462 O O     . HOH C 2 .   ? -53.725 38.596 -8.598  1.00 34.51 ? 817 HOH A O     1 
HETATM 6463 O O     . HOH C 2 .   ? -46.318 53.399 -2.095  1.00 34.70 ? 818 HOH A O     1 
HETATM 6464 O O     . HOH C 2 .   ? -38.336 41.401 -40.084 1.00 17.89 ? 819 HOH A O     1 
HETATM 6465 O O     . HOH C 2 .   ? -58.101 57.403 -2.965  1.00 32.62 ? 820 HOH A O     1 
HETATM 6466 O O     . HOH C 2 .   ? -75.794 41.747 -28.702 1.00 29.69 ? 821 HOH A O     1 
HETATM 6467 O O     . HOH C 2 .   ? -73.957 40.624 -45.532 1.00 50.72 ? 822 HOH A O     1 
HETATM 6468 O O     . HOH C 2 .   ? -46.644 55.902 -3.408  1.00 32.69 ? 823 HOH A O     1 
HETATM 6469 O O     . HOH C 2 .   ? -77.310 56.834 -34.965 1.00 52.38 ? 824 HOH A O     1 
HETATM 6470 O O     . HOH C 2 .   ? -57.435 27.621 -34.209 1.00 45.70 ? 825 HOH A O     1 
HETATM 6471 O O     . HOH C 2 .   ? -74.458 51.993 -29.691 1.00 35.84 ? 826 HOH A O     1 
HETATM 6472 O O     . HOH C 2 .   ? -22.827 48.880 -21.538 1.00 32.99 ? 827 HOH A O     1 
HETATM 6473 O O     . HOH C 2 .   ? -36.986 33.740 -36.381 1.00 44.18 ? 828 HOH A O     1 
HETATM 6474 O O     . HOH C 2 .   ? -73.221 59.431 -22.854 1.00 37.82 ? 829 HOH A O     1 
HETATM 6475 O O     . HOH C 2 .   ? -50.720 67.282 7.220   1.00 39.41 ? 830 HOH A O     1 
HETATM 6476 O O     . HOH C 2 .   ? -61.997 30.499 -32.971 1.00 47.54 ? 831 HOH A O     1 
HETATM 6477 O O     . HOH C 2 .   ? -40.447 31.450 -41.403 1.00 46.83 ? 832 HOH A O     1 
HETATM 6478 O O     . HOH C 2 .   ? -41.915 64.569 -5.959  1.00 36.29 ? 833 HOH A O     1 
HETATM 6479 O O     . HOH C 2 .   ? -60.208 32.044 -31.513 1.00 36.91 ? 834 HOH A O     1 
HETATM 6480 O O     . HOH C 2 .   ? -74.727 52.324 -24.170 1.00 35.25 ? 835 HOH A O     1 
HETATM 6481 O O     . HOH C 2 .   ? -49.243 38.692 -3.248  1.00 49.85 ? 836 HOH A O     1 
HETATM 6482 O O     . HOH C 2 .   ? -55.392 37.432 -10.084 1.00 48.56 ? 837 HOH A O     1 
HETATM 6483 O O     . HOH C 2 .   ? -42.625 37.335 -5.345  1.00 40.44 ? 838 HOH A O     1 
HETATM 6484 O O     . HOH C 2 .   ? -75.898 49.288 -43.456 1.00 53.77 ? 839 HOH A O     1 
HETATM 6485 O O     . HOH C 2 .   ? -64.397 60.222 -7.745  1.00 30.96 ? 840 HOH A O     1 
HETATM 6486 O O     . HOH C 2 .   ? -75.194 47.038 -32.657 1.00 33.54 ? 841 HOH A O     1 
HETATM 6487 O O     . HOH C 2 .   ? -30.117 52.364 -1.430  1.00 45.13 ? 842 HOH A O     1 
HETATM 6488 O O     . HOH C 2 .   ? -49.659 51.517 -39.092 1.00 44.43 ? 843 HOH A O     1 
HETATM 6489 O O     . HOH C 2 .   ? -49.646 25.827 -42.410 1.00 38.98 ? 844 HOH A O     1 
HETATM 6490 O O     . HOH C 2 .   ? -39.530 65.300 -7.059  1.00 27.90 ? 845 HOH A O     1 
HETATM 6491 O O     . HOH C 2 .   ? -39.393 31.452 -38.940 1.00 38.92 ? 846 HOH A O     1 
HETATM 6492 O O     . HOH C 2 .   ? -67.666 63.829 -18.631 1.00 38.86 ? 847 HOH A O     1 
HETATM 6493 O O     . HOH C 2 .   ? -57.368 58.285 -1.037  1.00 32.70 ? 848 HOH A O     1 
HETATM 6494 O O     . HOH C 2 .   ? -61.431 60.391 -2.472  1.00 41.33 ? 849 HOH A O     1 
HETATM 6495 O O     . HOH C 2 .   ? -57.359 40.115 -10.433 1.00 32.91 ? 850 HOH A O     1 
HETATM 6496 O O     . HOH C 2 .   ? -54.552 41.053 -49.697 1.00 46.82 ? 851 HOH A O     1 
HETATM 6497 O O     . HOH C 2 .   ? -76.771 48.603 -45.367 1.00 55.88 ? 852 HOH A O     1 
HETATM 6498 O O     . HOH C 2 .   ? -55.900 39.073 -8.272  1.00 42.46 ? 853 HOH A O     1 
HETATM 6499 O O     . HOH C 2 .   ? -79.594 39.608 -35.115 1.00 36.22 ? 854 HOH A O     1 
HETATM 6500 O O     . HOH C 2 .   ? -55.625 56.999 5.756   1.00 51.99 ? 855 HOH A O     1 
HETATM 6501 O O     . HOH C 2 .   ? -66.523 58.503 -43.466 1.00 47.34 ? 856 HOH A O     1 
HETATM 6502 O O     . HOH C 2 .   ? -76.425 42.969 -26.344 1.00 39.90 ? 857 HOH A O     1 
HETATM 6503 O O     . HOH C 2 .   ? -61.640 32.296 -20.064 1.00 45.06 ? 858 HOH A O     1 
HETATM 6504 O O     . HOH C 2 .   ? -52.058 28.647 -41.038 1.00 39.11 ? 859 HOH A O     1 
HETATM 6505 O O     . HOH C 2 .   ? -58.583 31.793 -35.003 1.00 33.69 ? 860 HOH A O     1 
HETATM 6506 O O     . HOH C 2 .   ? -60.088 49.109 -3.122  1.00 38.00 ? 861 HOH A O     1 
HETATM 6507 O O     . HOH C 2 .   ? -61.391 62.396 -1.240  1.00 44.56 ? 862 HOH A O     1 
HETATM 6508 O O     . HOH C 2 .   ? -44.031 53.013 -1.674  1.00 52.86 ? 863 HOH A O     1 
HETATM 6509 O O     . HOH C 2 .   ? -29.178 60.399 3.452   1.00 46.04 ? 864 HOH A O     1 
HETATM 6510 O O     . HOH C 2 .   ? -20.322 64.604 -10.870 1.00 36.87 ? 865 HOH A O     1 
HETATM 6511 O O     . HOH C 2 .   ? -53.907 42.572 -47.974 1.00 35.55 ? 866 HOH A O     1 
HETATM 6512 O O     . HOH C 2 .   ? -26.380 61.361 3.880   1.00 50.90 ? 867 HOH A O     1 
HETATM 6513 O O     . HOH C 2 .   ? -59.982 33.666 -16.758 1.00 32.79 ? 868 HOH A O     1 
HETATM 6514 O O     . HOH C 2 .   ? -75.839 55.444 -31.145 1.00 42.80 ? 869 HOH A O     1 
HETATM 6515 O O     . HOH C 2 .   ? -57.748 27.146 -36.636 1.00 53.88 ? 870 HOH A O     1 
HETATM 6516 O O     . HOH C 2 .   ? -51.293 26.164 -40.082 1.00 48.12 ? 871 HOH A O     1 
HETATM 6517 O O     . HOH C 2 .   ? -74.510 50.209 -35.768 1.00 35.29 ? 872 HOH A O     1 
HETATM 6518 O O     . HOH C 2 .   ? -58.173 33.524 -19.616 1.00 36.65 ? 873 HOH A O     1 
HETATM 6519 O O     . HOH C 2 .   ? -68.338 30.533 -27.276 1.00 44.77 ? 874 HOH A O     1 
HETATM 6520 O O     . HOH C 2 .   ? -77.456 46.532 -34.448 1.00 37.57 ? 875 HOH A O     1 
HETATM 6521 O O     . HOH C 2 .   ? -57.217 42.497 -57.786 1.00 35.93 ? 876 HOH A O     1 
HETATM 6522 O O     . HOH C 2 .   ? -53.272 25.473 -36.723 1.00 48.14 ? 877 HOH A O     1 
HETATM 6523 O O     . HOH C 2 .   ? -51.112 51.258 1.505   1.00 42.68 ? 878 HOH A O     1 
HETATM 6524 O O     . HOH C 2 .   ? -58.800 31.961 -14.421 1.00 50.92 ? 879 HOH A O     1 
HETATM 6525 O O     . HOH C 2 .   ? -78.901 54.255 -35.578 1.00 46.85 ? 880 HOH A O     1 
HETATM 6526 O O     . HOH C 2 .   ? -74.201 49.472 -33.228 1.00 28.71 ? 881 HOH A O     1 
HETATM 6527 O O     . HOH C 2 .   ? -58.537 30.244 -40.857 1.00 47.69 ? 882 HOH A O     1 
HETATM 6528 O O     . HOH C 2 .   ? -77.067 49.400 -36.993 1.00 48.29 ? 883 HOH A O     1 
HETATM 6529 O O     . HOH C 2 .   ? -56.309 42.652 -60.058 1.00 40.04 ? 884 HOH A O     1 
HETATM 6530 O O     . HOH D 2 .   ? -67.866 73.101 -15.898 1.00 37.93 ? 601 HOH B O     1 
HETATM 6531 O O     . HOH D 2 .   ? -63.565 67.891 -0.194  1.00 41.26 ? 602 HOH B O     1 
HETATM 6532 O O     . HOH D 2 .   ? -19.026 88.142 -17.736 1.00 38.68 ? 603 HOH B O     1 
HETATM 6533 O O     . HOH D 2 .   ? -57.585 81.965 0.850   1.00 34.22 ? 604 HOH B O     1 
HETATM 6534 O O     . HOH D 2 .   ? -55.575 70.702 -34.999 1.00 47.70 ? 605 HOH B O     1 
HETATM 6535 O O     . HOH D 2 .   ? -30.599 88.648 -19.341 1.00 47.06 ? 606 HOH B O     1 
HETATM 6536 O O     . HOH D 2 .   ? -53.392 84.158 10.913  1.00 44.91 ? 607 HOH B O     1 
HETATM 6537 O O     . HOH D 2 .   ? -41.920 65.491 -13.703 1.00 30.45 ? 608 HOH B O     1 
HETATM 6538 O O     . HOH D 2 .   ? -50.229 90.635 -20.491 1.00 34.89 ? 609 HOH B O     1 
HETATM 6539 O O     . HOH D 2 .   ? -48.318 82.207 -12.447 1.00 24.70 ? 610 HOH B O     1 
HETATM 6540 O O     . HOH D 2 .   ? -16.884 75.410 -26.309 1.00 30.47 ? 611 HOH B O     1 
HETATM 6541 O O     . HOH D 2 .   ? -19.168 88.789 -11.300 1.00 46.88 ? 612 HOH B O     1 
HETATM 6542 O O     . HOH D 2 .   ? -35.689 89.643 8.812   1.00 41.06 ? 613 HOH B O     1 
HETATM 6543 O O     . HOH D 2 .   ? -60.756 67.100 -31.215 1.00 23.86 ? 614 HOH B O     1 
HETATM 6544 O O     . HOH D 2 .   ? -61.246 74.690 -25.122 1.00 33.88 ? 615 HOH B O     1 
HETATM 6545 O O     . HOH D 2 .   ? -33.572 81.682 -32.700 1.00 33.22 ? 616 HOH B O     1 
HETATM 6546 O O     . HOH D 2 .   ? -58.897 77.889 -21.034 1.00 30.29 ? 617 HOH B O     1 
HETATM 6547 O O     . HOH D 2 .   ? -61.682 71.633 7.771   1.00 51.20 ? 618 HOH B O     1 
HETATM 6548 O O     . HOH D 2 .   ? -56.575 79.991 6.606   1.00 35.22 ? 619 HOH B O     1 
HETATM 6549 O O     . HOH D 2 .   ? -44.213 79.196 -8.317  1.00 35.77 ? 620 HOH B O     1 
HETATM 6550 O O     . HOH D 2 .   ? -28.799 43.604 -36.809 1.00 42.37 ? 621 HOH B O     1 
HETATM 6551 O O     . HOH D 2 .   ? -16.166 75.111 -18.903 1.00 24.54 ? 622 HOH B O     1 
HETATM 6552 O O     . HOH D 2 .   ? -63.659 57.167 -23.332 1.00 16.71 ? 623 HOH B O     1 
HETATM 6553 O O     . HOH D 2 .   ? -33.200 76.482 -6.751  1.00 27.61 ? 624 HOH B O     1 
HETATM 6554 O O     . HOH D 2 .   ? -13.434 83.941 -11.245 1.00 41.40 ? 625 HOH B O     1 
HETATM 6555 O O     . HOH D 2 .   ? -18.249 73.213 -28.174 1.00 31.38 ? 626 HOH B O     1 
HETATM 6556 O O     . HOH D 2 .   ? -59.056 52.380 -40.344 1.00 28.16 ? 627 HOH B O     1 
HETATM 6557 O O     . HOH D 2 .   ? -9.471  66.947 -21.849 1.00 41.38 ? 628 HOH B O     1 
HETATM 6558 O O     . HOH D 2 .   ? -33.871 79.083 -29.410 1.00 21.03 ? 629 HOH B O     1 
HETATM 6559 O O     . HOH D 2 .   ? -33.454 44.395 -42.421 1.00 37.31 ? 630 HOH B O     1 
HETATM 6560 O O     . HOH D 2 .   ? -31.031 55.220 -26.521 1.00 32.78 ? 631 HOH B O     1 
HETATM 6561 O O     . HOH D 2 .   ? -56.653 72.314 -8.514  1.00 20.82 ? 632 HOH B O     1 
HETATM 6562 O O     . HOH D 2 .   ? -44.885 57.206 -24.520 1.00 23.96 ? 633 HOH B O     1 
HETATM 6563 O O     . HOH D 2 .   ? -44.907 62.209 -32.230 1.00 22.85 ? 634 HOH B O     1 
HETATM 6564 O O     . HOH D 2 .   ? -34.457 68.978 -35.785 1.00 23.49 ? 635 HOH B O     1 
HETATM 6565 O O     . HOH D 2 .   ? -47.202 68.064 -15.526 1.00 15.59 ? 636 HOH B O     1 
HETATM 6566 O O     . HOH D 2 .   ? -44.650 82.314 -19.918 1.00 22.41 ? 637 HOH B O     1 
HETATM 6567 O O     . HOH D 2 .   ? -21.488 82.608 -11.461 1.00 30.47 ? 638 HOH B O     1 
HETATM 6568 O O     . HOH D 2 .   ? -60.017 77.380 -24.158 1.00 34.78 ? 639 HOH B O     1 
HETATM 6569 O O     . HOH D 2 .   ? -55.073 81.580 -26.875 1.00 32.89 ? 640 HOH B O     1 
HETATM 6570 O O     . HOH D 2 .   ? -20.320 60.942 -24.504 1.00 29.10 ? 641 HOH B O     1 
HETATM 6571 O O     . HOH D 2 .   ? -32.909 74.188 -11.867 1.00 23.37 ? 642 HOH B O     1 
HETATM 6572 O O     . HOH D 2 .   ? -43.827 76.386 -1.704  1.00 31.72 ? 643 HOH B O     1 
HETATM 6573 O O     . HOH D 2 .   ? -28.546 78.027 -31.805 1.00 49.86 ? 644 HOH B O     1 
HETATM 6574 O O     . HOH D 2 .   ? -29.419 91.338 -4.228  1.00 35.21 ? 645 HOH B O     1 
HETATM 6575 O O     . HOH D 2 .   ? -36.670 77.936 10.791  1.00 32.98 ? 646 HOH B O     1 
HETATM 6576 O O     . HOH D 2 .   ? -47.671 70.475 -3.135  1.00 22.96 ? 647 HOH B O     1 
HETATM 6577 O O     . HOH D 2 .   ? -26.637 77.453 -30.826 1.00 46.08 ? 648 HOH B O     1 
HETATM 6578 O O     . HOH D 2 .   ? -47.588 63.382 -24.980 1.00 27.48 ? 649 HOH B O     1 
HETATM 6579 O O     . HOH D 2 .   ? -51.534 79.305 -32.892 1.00 30.17 ? 650 HOH B O     1 
HETATM 6580 O O     . HOH D 2 .   ? -58.140 79.640 -1.159  1.00 39.14 ? 651 HOH B O     1 
HETATM 6581 O O     . HOH D 2 .   ? -37.338 78.176 -32.578 1.00 23.01 ? 652 HOH B O     1 
HETATM 6582 O O     . HOH D 2 .   ? -11.395 69.898 -19.396 1.00 32.35 ? 653 HOH B O     1 
HETATM 6583 O O     . HOH D 2 .   ? -54.072 93.421 2.472   1.00 45.09 ? 654 HOH B O     1 
HETATM 6584 O O     . HOH D 2 .   ? -45.394 59.491 -27.719 1.00 28.03 ? 655 HOH B O     1 
HETATM 6585 O O     . HOH D 2 .   ? -31.411 53.563 -37.658 1.00 28.48 ? 656 HOH B O     1 
HETATM 6586 O O     . HOH D 2 .   ? -26.736 84.324 2.636   1.00 42.45 ? 657 HOH B O     1 
HETATM 6587 O O     . HOH D 2 .   ? -45.294 72.523 5.310   1.00 29.95 ? 658 HOH B O     1 
HETATM 6588 O O     . HOH D 2 .   ? -55.760 71.912 -25.889 1.00 27.64 ? 659 HOH B O     1 
HETATM 6589 O O     . HOH D 2 .   ? -39.423 70.353 -6.847  1.00 45.26 ? 660 HOH B O     1 
HETATM 6590 O O     . HOH D 2 .   ? -36.695 66.345 -10.289 1.00 16.22 ? 661 HOH B O     1 
HETATM 6591 O O     . HOH D 2 .   ? -40.607 62.223 -25.225 1.00 24.45 ? 662 HOH B O     1 
HETATM 6592 O O     . HOH D 2 .   ? -59.063 81.239 -25.108 1.00 38.12 ? 663 HOH B O     1 
HETATM 6593 O O     . HOH D 2 .   ? -14.565 70.111 -25.853 1.00 29.39 ? 664 HOH B O     1 
HETATM 6594 O O     . HOH D 2 .   ? -44.072 51.679 -28.581 1.00 16.17 ? 665 HOH B O     1 
HETATM 6595 O O     . HOH D 2 .   ? -55.131 79.989 -1.883  1.00 31.85 ? 666 HOH B O     1 
HETATM 6596 O O     . HOH D 2 .   ? -56.275 70.591 -28.163 1.00 21.64 ? 667 HOH B O     1 
HETATM 6597 O O     . HOH D 2 .   ? -46.393 61.589 -28.948 1.00 25.35 ? 668 HOH B O     1 
HETATM 6598 O O     . HOH D 2 .   ? -41.525 89.432 -9.074  1.00 35.16 ? 669 HOH B O     1 
HETATM 6599 O O     . HOH D 2 .   ? -48.104 74.301 5.200   1.00 28.73 ? 670 HOH B O     1 
HETATM 6600 O O     . HOH D 2 .   ? -17.779 55.615 -13.629 1.00 33.93 ? 671 HOH B O     1 
HETATM 6601 O O     . HOH D 2 .   ? -45.664 83.148 -30.429 1.00 33.20 ? 672 HOH B O     1 
HETATM 6602 O O     . HOH D 2 .   ? -46.613 95.397 -3.248  1.00 40.79 ? 673 HOH B O     1 
HETATM 6603 O O     . HOH D 2 .   ? -65.598 63.782 -39.478 1.00 45.25 ? 674 HOH B O     1 
HETATM 6604 O O     . HOH D 2 .   ? -38.933 60.749 -23.606 1.00 23.69 ? 675 HOH B O     1 
HETATM 6605 O O     . HOH D 2 .   ? -29.650 87.876 1.939   1.00 47.64 ? 676 HOH B O     1 
HETATM 6606 O O     . HOH D 2 .   ? -30.750 74.423 8.567   1.00 38.52 ? 677 HOH B O     1 
HETATM 6607 O O     . HOH D 2 .   ? -52.950 73.775 4.031   1.00 31.04 ? 678 HOH B O     1 
HETATM 6608 O O     . HOH D 2 .   ? -29.734 56.284 -29.369 1.00 32.67 ? 679 HOH B O     1 
HETATM 6609 O O     . HOH D 2 .   ? -65.189 67.915 -15.537 1.00 31.21 ? 680 HOH B O     1 
HETATM 6610 O O     . HOH D 2 .   ? -42.949 70.679 3.724   1.00 36.26 ? 681 HOH B O     1 
HETATM 6611 O O     . HOH D 2 .   ? -54.577 64.107 -15.686 1.00 23.09 ? 682 HOH B O     1 
HETATM 6612 O O     . HOH D 2 .   ? -30.653 69.571 3.401   1.00 32.12 ? 683 HOH B O     1 
HETATM 6613 O O     . HOH D 2 .   ? -36.671 83.642 -1.229  1.00 30.37 ? 684 HOH B O     1 
HETATM 6614 O O     . HOH D 2 .   ? -58.903 73.938 -8.556  1.00 25.31 ? 685 HOH B O     1 
HETATM 6615 O O     . HOH D 2 .   ? -16.106 62.811 -14.863 1.00 37.97 ? 686 HOH B O     1 
HETATM 6616 O O     . HOH D 2 .   ? -59.022 70.936 -29.063 1.00 32.37 ? 687 HOH B O     1 
HETATM 6617 O O     . HOH D 2 .   ? -23.233 57.033 -14.008 1.00 25.57 ? 688 HOH B O     1 
HETATM 6618 O O     . HOH D 2 .   ? -42.991 74.545 -15.517 1.00 20.06 ? 689 HOH B O     1 
HETATM 6619 O O     . HOH D 2 .   ? -69.966 61.254 -24.634 1.00 38.73 ? 690 HOH B O     1 
HETATM 6620 O O     . HOH D 2 .   ? -50.323 70.620 10.510  1.00 34.58 ? 691 HOH B O     1 
HETATM 6621 O O     . HOH D 2 .   ? -39.050 67.147 -8.918  1.00 27.07 ? 692 HOH B O     1 
HETATM 6622 O O     . HOH D 2 .   ? -38.373 88.944 -1.921  1.00 33.12 ? 693 HOH B O     1 
HETATM 6623 O O     . HOH D 2 .   ? -32.352 75.903 -35.489 1.00 33.14 ? 694 HOH B O     1 
HETATM 6624 O O     . HOH D 2 .   ? -19.782 67.312 -30.085 1.00 35.25 ? 695 HOH B O     1 
HETATM 6625 O O     . HOH D 2 .   ? -46.445 65.378 -13.163 1.00 25.34 ? 696 HOH B O     1 
HETATM 6626 O O     . HOH D 2 .   ? -28.672 73.941 -5.733  1.00 21.29 ? 697 HOH B O     1 
HETATM 6627 O O     . HOH D 2 .   ? -36.507 58.837 -28.654 1.00 17.89 ? 698 HOH B O     1 
HETATM 6628 O O     . HOH D 2 .   ? -23.156 73.982 -1.972  1.00 27.42 ? 699 HOH B O     1 
HETATM 6629 O O     . HOH D 2 .   ? -42.020 56.566 -23.585 1.00 18.31 ? 700 HOH B O     1 
HETATM 6630 O O     . HOH D 2 .   ? -32.982 75.644 8.475   1.00 36.39 ? 701 HOH B O     1 
HETATM 6631 O O     . HOH D 2 .   ? -48.136 83.374 20.136  0.50 41.81 ? 702 HOH B O     1 
HETATM 6632 O O     . HOH D 2 .   ? -64.570 59.938 -39.869 1.00 33.23 ? 703 HOH B O     1 
HETATM 6633 O O     . HOH D 2 .   ? -43.161 89.007 -11.325 1.00 34.71 ? 704 HOH B O     1 
HETATM 6634 O O     . HOH D 2 .   ? -40.161 71.811 -1.428  1.00 35.19 ? 705 HOH B O     1 
HETATM 6635 O O     . HOH D 2 .   ? -43.993 92.922 12.708  1.00 56.45 ? 706 HOH B O     1 
HETATM 6636 O O     . HOH D 2 .   ? -53.441 53.521 -38.205 1.00 35.13 ? 707 HOH B O     1 
HETATM 6637 O O     . HOH D 2 .   ? -33.304 85.314 -4.359  1.00 28.54 ? 708 HOH B O     1 
HETATM 6638 O O     . HOH D 2 .   ? -48.955 71.177 -34.102 1.00 24.60 ? 709 HOH B O     1 
HETATM 6639 O O     . HOH D 2 .   ? -63.125 79.014 -6.163  1.00 35.23 ? 710 HOH B O     1 
HETATM 6640 O O     . HOH D 2 .   ? -34.308 77.188 -34.360 1.00 38.92 ? 711 HOH B O     1 
HETATM 6641 O O     . HOH D 2 .   ? -45.048 92.775 9.719   1.00 41.91 ? 712 HOH B O     1 
HETATM 6642 O O     . HOH D 2 .   ? -37.658 70.987 -37.761 1.00 32.15 ? 713 HOH B O     1 
HETATM 6643 O O     . HOH D 2 .   ? -54.672 76.972 -28.674 1.00 25.18 ? 714 HOH B O     1 
HETATM 6644 O O     . HOH D 2 .   ? -26.434 83.890 -28.813 1.00 32.11 ? 715 HOH B O     1 
HETATM 6645 O O     . HOH D 2 .   ? -45.608 77.418 -10.569 1.00 24.13 ? 716 HOH B O     1 
HETATM 6646 O O     . HOH D 2 .   ? -49.856 86.041 -22.304 1.00 35.82 ? 717 HOH B O     1 
HETATM 6647 O O     . HOH D 2 .   ? -17.151 74.307 -10.097 1.00 29.78 ? 718 HOH B O     1 
HETATM 6648 O O     . HOH D 2 .   ? -37.810 85.009 -20.606 1.00 28.29 ? 719 HOH B O     1 
HETATM 6649 O O     . HOH D 2 .   ? -26.512 57.931 -22.524 1.00 40.27 ? 720 HOH B O     1 
HETATM 6650 O O     . HOH D 2 .   ? -15.773 72.430 -26.450 1.00 30.98 ? 721 HOH B O     1 
HETATM 6651 O O     . HOH D 2 .   ? -19.078 80.378 -31.096 1.00 32.69 ? 722 HOH B O     1 
HETATM 6652 O O     . HOH D 2 .   ? -64.710 77.039 -9.302  1.00 40.28 ? 723 HOH B O     1 
HETATM 6653 O O     . HOH D 2 .   ? -63.641 56.254 -34.321 1.00 22.13 ? 724 HOH B O     1 
HETATM 6654 O O     . HOH D 2 .   ? -44.109 54.450 -36.000 1.00 29.46 ? 725 HOH B O     1 
HETATM 6655 O O     . HOH D 2 .   ? -61.028 59.655 -40.581 1.00 38.87 ? 726 HOH B O     1 
HETATM 6656 O O     . HOH D 2 .   ? -37.045 78.024 -13.654 1.00 21.89 ? 727 HOH B O     1 
HETATM 6657 O O     . HOH D 2 .   ? -65.690 71.003 -9.976  1.00 46.17 ? 728 HOH B O     1 
HETATM 6658 O O     . HOH D 2 .   ? -31.277 88.618 -10.026 1.00 35.56 ? 729 HOH B O     1 
HETATM 6659 O O     . HOH D 2 .   ? -44.433 66.675 -14.497 1.00 20.45 ? 730 HOH B O     1 
HETATM 6660 O O     . HOH D 2 .   ? -43.292 87.411 -8.341  1.00 34.42 ? 731 HOH B O     1 
HETATM 6661 O O     . HOH D 2 .   ? -48.472 73.443 -35.330 1.00 34.12 ? 732 HOH B O     1 
HETATM 6662 O O     . HOH D 2 .   ? -53.464 59.868 -40.981 1.00 48.81 ? 733 HOH B O     1 
HETATM 6663 O O     . HOH D 2 .   ? -28.968 86.387 -10.692 1.00 29.19 ? 734 HOH B O     1 
HETATM 6664 O O     . HOH D 2 .   ? -34.707 85.916 -16.995 1.00 30.44 ? 735 HOH B O     1 
HETATM 6665 O O     . HOH D 2 .   ? -27.009 70.562 -36.349 1.00 39.49 ? 736 HOH B O     1 
HETATM 6666 O O     . HOH D 2 .   ? -12.782 75.121 -21.184 1.00 28.25 ? 737 HOH B O     1 
HETATM 6667 O O     . HOH D 2 .   ? -48.937 83.926 -26.321 1.00 33.83 ? 738 HOH B O     1 
HETATM 6668 O O     . HOH D 2 .   ? -29.936 85.015 1.348   1.00 37.11 ? 739 HOH B O     1 
HETATM 6669 O O     . HOH D 2 .   ? -32.735 56.036 -38.998 1.00 25.41 ? 740 HOH B O     1 
HETATM 6670 O O     . HOH D 2 .   ? -53.378 75.885 -30.596 1.00 24.51 ? 741 HOH B O     1 
HETATM 6671 O O     . HOH D 2 .   ? -51.065 93.369 -13.230 1.00 40.10 ? 742 HOH B O     1 
HETATM 6672 O O     . HOH D 2 .   ? -52.851 73.293 -35.314 1.00 47.84 ? 743 HOH B O     1 
HETATM 6673 O O     . HOH D 2 .   ? -40.549 58.850 -25.262 1.00 24.14 ? 744 HOH B O     1 
HETATM 6674 O O     . HOH D 2 .   ? -30.521 51.034 -33.987 1.00 40.63 ? 745 HOH B O     1 
HETATM 6675 O O     . HOH D 2 .   ? -62.897 73.455 -21.200 1.00 30.39 ? 746 HOH B O     1 
HETATM 6676 O O     . HOH D 2 .   ? -15.299 71.468 -11.343 1.00 42.77 ? 747 HOH B O     1 
HETATM 6677 O O     . HOH D 2 .   ? -45.837 95.267 -10.545 1.00 42.83 ? 748 HOH B O     1 
HETATM 6678 O O     . HOH D 2 .   ? -44.986 74.809 -37.032 1.00 30.40 ? 749 HOH B O     1 
HETATM 6679 O O     . HOH D 2 .   ? -56.375 82.162 -25.053 1.00 34.04 ? 750 HOH B O     1 
HETATM 6680 O O     . HOH D 2 .   ? -19.338 83.428 -4.031  1.00 50.03 ? 751 HOH B O     1 
HETATM 6681 O O     . HOH D 2 .   ? -60.868 66.036 -15.159 1.00 21.11 ? 752 HOH B O     1 
HETATM 6682 O O     . HOH D 2 .   ? -21.478 71.886 -27.906 1.00 23.89 ? 753 HOH B O     1 
HETATM 6683 O O     . HOH D 2 .   ? -27.302 88.010 -11.775 1.00 35.06 ? 754 HOH B O     1 
HETATM 6684 O O     . HOH D 2 .   ? -27.721 61.121 -17.429 1.00 27.69 ? 755 HOH B O     1 
HETATM 6685 O O     . HOH D 2 .   ? -40.010 73.211 -6.042  1.00 31.29 ? 756 HOH B O     1 
HETATM 6686 O O     . HOH D 2 .   ? -61.148 56.976 -41.845 1.00 42.33 ? 757 HOH B O     1 
HETATM 6687 O O     . HOH D 2 .   ? -33.842 60.215 -37.194 1.00 33.10 ? 758 HOH B O     1 
HETATM 6688 O O     . HOH D 2 .   ? -34.331 89.232 6.526   1.00 39.03 ? 759 HOH B O     1 
HETATM 6689 O O     . HOH D 2 .   ? -40.545 64.332 -15.685 1.00 16.79 ? 760 HOH B O     1 
HETATM 6690 O O     . HOH D 2 .   ? -43.904 86.871 -11.581 1.00 33.23 ? 761 HOH B O     1 
HETATM 6691 O O     . HOH D 2 .   ? -61.600 63.903 -16.334 1.00 23.86 ? 762 HOH B O     1 
HETATM 6692 O O     . HOH D 2 .   ? -38.889 70.469 0.510   1.00 37.10 ? 763 HOH B O     1 
HETATM 6693 O O     . HOH D 2 .   ? -16.776 66.828 -12.516 1.00 31.28 ? 764 HOH B O     1 
HETATM 6694 O O     . HOH D 2 .   ? -12.963 82.635 -19.462 1.00 36.00 ? 765 HOH B O     1 
HETATM 6695 O O     . HOH D 2 .   ? -44.881 83.115 -22.491 1.00 26.83 ? 766 HOH B O     1 
HETATM 6696 O O     . HOH D 2 .   ? -58.547 86.198 -0.051  1.00 42.52 ? 767 HOH B O     1 
HETATM 6697 O O     . HOH D 2 .   ? -29.610 91.717 -0.578  1.00 45.83 ? 768 HOH B O     1 
HETATM 6698 O O     . HOH D 2 .   ? -64.750 78.487 -14.794 1.00 41.70 ? 769 HOH B O     1 
HETATM 6699 O O     . HOH D 2 .   ? -29.663 85.976 -26.130 1.00 35.25 ? 770 HOH B O     1 
HETATM 6700 O O     . HOH D 2 .   ? -33.548 76.106 -10.012 1.00 26.89 ? 771 HOH B O     1 
HETATM 6701 O O     . HOH D 2 .   ? -65.747 75.659 -10.886 1.00 34.37 ? 772 HOH B O     1 
HETATM 6702 O O     . HOH D 2 .   ? -40.820 58.917 -42.186 1.00 34.86 ? 773 HOH B O     1 
HETATM 6703 O O     . HOH D 2 .   ? -52.544 61.740 -38.724 1.00 34.10 ? 774 HOH B O     1 
HETATM 6704 O O     . HOH D 2 .   ? -26.516 59.049 -27.214 1.00 29.31 ? 775 HOH B O     1 
HETATM 6705 O O     . HOH D 2 .   ? -31.389 49.431 -35.446 1.00 35.96 ? 776 HOH B O     1 
HETATM 6706 O O     . HOH D 2 .   ? -49.229 58.672 -29.624 1.00 30.89 ? 777 HOH B O     1 
HETATM 6707 O O     . HOH D 2 .   ? -21.759 88.169 -1.143  1.00 39.59 ? 778 HOH B O     1 
HETATM 6708 O O     . HOH D 2 .   ? -37.327 59.605 -25.845 1.00 19.09 ? 779 HOH B O     1 
HETATM 6709 O O     . HOH D 2 .   ? -61.948 78.046 -15.809 1.00 25.88 ? 780 HOH B O     1 
HETATM 6710 O O     . HOH D 2 .   ? -18.540 62.689 -27.206 1.00 38.38 ? 781 HOH B O     1 
HETATM 6711 O O     . HOH D 2 .   ? -40.952 71.849 -4.037  1.00 33.55 ? 782 HOH B O     1 
HETATM 6712 O O     . HOH D 2 .   ? -69.118 62.826 -36.182 1.00 42.46 ? 783 HOH B O     1 
HETATM 6713 O O     . HOH D 2 .   ? -40.932 62.126 -39.251 1.00 38.06 ? 784 HOH B O     1 
HETATM 6714 O O     . HOH D 2 .   ? -48.815 82.277 -33.223 1.00 42.41 ? 785 HOH B O     1 
HETATM 6715 O O     . HOH D 2 .   ? -29.421 57.952 -26.444 1.00 31.11 ? 786 HOH B O     1 
HETATM 6716 O O     . HOH D 2 .   ? -18.484 69.637 -9.425  1.00 46.83 ? 787 HOH B O     1 
HETATM 6717 O O     . HOH D 2 .   ? -37.025 70.181 -35.253 1.00 28.87 ? 788 HOH B O     1 
HETATM 6718 O O     . HOH D 2 .   ? -49.137 66.693 -32.361 1.00 31.75 ? 789 HOH B O     1 
HETATM 6719 O O     . HOH D 2 .   ? -60.278 91.294 -6.997  1.00 45.09 ? 790 HOH B O     1 
HETATM 6720 O O     . HOH D 2 .   ? -18.606 90.098 -21.304 1.00 44.66 ? 791 HOH B O     1 
HETATM 6721 O O     . HOH D 2 .   ? -66.526 68.180 -19.918 1.00 30.52 ? 792 HOH B O     1 
HETATM 6722 O O     . HOH D 2 .   ? -9.408  65.642 -23.766 1.00 43.60 ? 793 HOH B O     1 
HETATM 6723 O O     . HOH D 2 .   ? -38.258 63.176 -40.895 1.00 47.22 ? 794 HOH B O     1 
HETATM 6724 O O     . HOH D 2 .   ? -48.727 56.766 -31.003 1.00 33.35 ? 795 HOH B O     1 
HETATM 6725 O O     . HOH D 2 .   ? -47.298 79.570 -9.858  1.00 32.71 ? 796 HOH B O     1 
HETATM 6726 O O     . HOH D 2 .   ? -17.160 64.434 -27.650 1.00 41.80 ? 797 HOH B O     1 
HETATM 6727 O O     . HOH D 2 .   ? -31.535 88.985 -14.533 1.00 42.68 ? 798 HOH B O     1 
HETATM 6728 O O     . HOH D 2 .   ? -59.863 72.579 -27.748 1.00 36.54 ? 799 HOH B O     1 
HETATM 6729 O O     . HOH D 2 .   ? -51.240 61.459 -36.623 1.00 36.82 ? 800 HOH B O     1 
HETATM 6730 O O     . HOH D 2 .   ? -39.339 86.069 -31.850 1.00 55.37 ? 801 HOH B O     1 
HETATM 6731 O O     . HOH D 2 .   ? -57.077 90.739 -1.010  1.00 38.26 ? 802 HOH B O     1 
HETATM 6732 O O     . HOH D 2 .   ? -59.968 71.650 -33.285 1.00 56.36 ? 803 HOH B O     1 
HETATM 6733 O O     . HOH D 2 .   ? -44.343 84.570 -26.892 1.00 41.69 ? 804 HOH B O     1 
HETATM 6734 O O     . HOH D 2 .   ? -42.005 64.010 -38.539 1.00 48.08 ? 805 HOH B O     1 
HETATM 6735 O O     . HOH D 2 .   ? -64.902 69.087 -10.914 1.00 40.50 ? 806 HOH B O     1 
HETATM 6736 O O     . HOH D 2 .   ? -62.239 79.621 -18.038 1.00 29.95 ? 807 HOH B O     1 
HETATM 6737 O O     . HOH D 2 .   ? -49.370 85.511 20.136  0.50 49.14 ? 808 HOH B O     1 
HETATM 6738 O O     . HOH D 2 .   ? -54.092 75.730 -32.894 1.00 41.83 ? 809 HOH B O     1 
HETATM 6739 O O     . HOH D 2 .   ? -59.341 69.773 -31.265 1.00 35.20 ? 810 HOH B O     1 
HETATM 6740 O O     . HOH D 2 .   ? -62.409 61.379 -40.296 1.00 47.02 ? 811 HOH B O     1 
HETATM 6741 O O     . HOH D 2 .   ? -31.571 75.937 -38.389 1.00 50.16 ? 812 HOH B O     1 
HETATM 6742 O O     . HOH D 2 .   ? -21.723 70.163 -29.815 1.00 31.83 ? 813 HOH B O     1 
HETATM 6743 O O     . HOH D 2 .   ? -21.814 75.276 -0.336  1.00 42.41 ? 814 HOH B O     1 
HETATM 6744 O O     . HOH D 2 .   ? -50.936 94.496 -10.907 1.00 43.32 ? 815 HOH B O     1 
HETATM 6745 O O     . HOH D 2 .   ? -16.418 64.104 -12.567 1.00 50.49 ? 816 HOH B O     1 
HETATM 6746 O O     . HOH D 2 .   ? -63.890 71.457 -22.786 1.00 31.63 ? 817 HOH B O     1 
HETATM 6747 O O     . HOH D 2 .   ? -28.349 85.422 -28.109 1.00 34.77 ? 818 HOH B O     1 
HETATM 6748 O O     . HOH D 2 .   ? -35.410 79.741 -34.083 1.00 28.56 ? 819 HOH B O     1 
HETATM 6749 O O     . HOH D 2 .   ? -66.424 70.673 -21.653 1.00 40.52 ? 820 HOH B O     1 
HETATM 6750 O O     . HOH D 2 .   ? -33.840 77.214 10.588  1.00 38.36 ? 821 HOH B O     1 
HETATM 6751 O O     . HOH D 2 .   ? -65.558 78.132 -6.598  1.00 48.69 ? 822 HOH B O     1 
HETATM 6752 O O     . HOH D 2 .   ? -36.024 90.015 -1.374  1.00 36.87 ? 823 HOH B O     1 
HETATM 6753 O O     . HOH D 2 .   ? -53.398 95.196 -9.595  1.00 48.59 ? 824 HOH B O     1 
HETATM 6754 O O     . HOH D 2 .   ? -51.004 81.567 -33.746 1.00 40.45 ? 825 HOH B O     1 
HETATM 6755 O O     . HOH D 2 .   ? -47.037 84.932 -24.037 1.00 48.90 ? 826 HOH B O     1 
HETATM 6756 O O     . HOH D 2 .   ? -37.900 90.940 -4.071  1.00 42.24 ? 827 HOH B O     1 
HETATM 6757 O O     . HOH D 2 .   ? -47.600 62.719 -33.110 1.00 33.21 ? 828 HOH B O     1 
HETATM 6758 O O     . HOH D 2 .   ? -37.357 85.863 -33.265 1.00 41.76 ? 829 HOH B O     1 
HETATM 6759 O O     . HOH D 2 .   ? -70.667 62.632 -21.562 1.00 35.71 ? 830 HOH B O     1 
HETATM 6760 O O     . HOH D 2 .   ? -49.134 64.768 -33.543 1.00 31.37 ? 831 HOH B O     1 
HETATM 6761 O O     . HOH D 2 .   ? -66.051 77.296 -12.774 1.00 35.58 ? 832 HOH B O     1 
HETATM 6762 O O     . HOH D 2 .   ? -22.592 56.615 -11.413 1.00 29.71 ? 833 HOH B O     1 
HETATM 6763 O O     . HOH D 2 .   ? -54.367 77.845 -33.642 1.00 44.97 ? 834 HOH B O     1 
HETATM 6764 O O     . HOH D 2 .   ? -41.606 89.652 -16.339 1.00 41.53 ? 835 HOH B O     1 
HETATM 6765 O O     . HOH D 2 .   ? -31.981 58.766 -38.561 1.00 45.89 ? 836 HOH B O     1 
HETATM 6766 O O     . HOH D 2 .   ? -18.154 71.195 -7.866  1.00 48.90 ? 837 HOH B O     1 
HETATM 6767 O O     . HOH D 2 .   ? -43.491 91.063 -18.093 1.00 36.21 ? 838 HOH B O     1 
HETATM 6768 O O     . HOH D 2 .   ? -34.078 90.695 4.476   1.00 41.62 ? 839 HOH B O     1 
HETATM 6769 O O     . HOH D 2 .   ? -58.200 83.933 3.218   1.00 42.62 ? 840 HOH B O     1 
HETATM 6770 O O     . HOH D 2 .   ? -16.795 82.827 -5.880  1.00 45.92 ? 841 HOH B O     1 
HETATM 6771 O O     . HOH D 2 .   ? -42.844 92.138 -20.137 1.00 49.07 ? 842 HOH B O     1 
HETATM 6772 O O     . HOH D 2 .   ? -34.091 53.136 -46.409 1.00 43.72 ? 843 HOH B O     1 
HETATM 6773 O O     . HOH D 2 .   ? -51.708 95.551 -7.481  1.00 62.24 ? 844 HOH B O     1 
HETATM 6774 O O     . HOH D 2 .   ? -35.282 55.513 -45.334 1.00 37.81 ? 845 HOH B O     1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N     . ARG A 11  ? 0.5597 0.8854 0.6749 0.0027  0.0408  0.0288  152 ARG A N     
2    C CA    . ARG A 11  ? 0.4742 0.7943 0.5956 0.0034  0.0368  0.0283  152 ARG A CA    
3    C C     . ARG A 11  ? 0.4675 0.7777 0.5901 -0.0021 0.0335  0.0324  152 ARG A C     
4    O O     . ARG A 11  ? 0.5363 0.8421 0.6542 -0.0046 0.0340  0.0357  152 ARG A O     
5    C CB    . ARG A 11  ? 0.4147 0.7268 0.5341 0.0132  0.0359  0.0234  152 ARG A CB    
6    C CG    . ARG A 11  ? 0.3304 0.6494 0.4488 0.0201  0.0389  0.0193  152 ARG A CG    
7    C CD    . ARG A 11  ? 0.2551 0.5721 0.3770 0.0264  0.0365  0.0163  152 ARG A CD    
8    N NE    . ARG A 11  ? 0.2518 0.5537 0.3695 0.0309  0.0340  0.0153  152 ARG A NE    
9    C CZ    . ARG A 11  ? 0.2288 0.5264 0.3491 0.0332  0.0305  0.0142  152 ARG A CZ    
10   N NH1   . ARG A 11  ? 0.2320 0.5390 0.3591 0.0315  0.0289  0.0140  152 ARG A NH1   
11   N NH2   . ARG A 11  ? 0.1792 0.4633 0.2947 0.0371  0.0287  0.0133  152 ARG A NH2   
12   N N     . HIS A 12  ? 0.4079 0.7149 0.5373 -0.0038 0.0302  0.0322  153 HIS A N     
13   C CA    . HIS A 12  ? 0.3734 0.6700 0.5062 -0.0080 0.0268  0.0348  153 HIS A CA    
14   C C     . HIS A 12  ? 0.3918 0.6908 0.5274 -0.0178 0.0264  0.0413  153 HIS A C     
15   O O     . HIS A 12  ? 0.3603 0.6501 0.4985 -0.0213 0.0238  0.0445  153 HIS A O     
16   C CB    . HIS A 12  ? 0.4038 0.6872 0.5310 -0.0024 0.0261  0.0336  153 HIS A CB    
17   C CG    . HIS A 12  ? 0.4033 0.6828 0.5266 0.0069  0.0264  0.0280  153 HIS A CG    
18   N ND1   . HIS A 12  ? 0.2997 0.5833 0.4269 0.0094  0.0253  0.0247  153 HIS A ND1   
19   C CD2   . HIS A 12  ? 0.2812 0.5528 0.3971 0.0138  0.0274  0.0257  153 HIS A CD2   
20   C CE1   . HIS A 12  ? 0.2864 0.5647 0.4087 0.0175  0.0255  0.0211  153 HIS A CE1   
21   N NE2   . HIS A 12  ? 0.2920 0.5625 0.4074 0.0203  0.0268  0.0215  153 HIS A NE2   
22   N N     . GLU A 13  ? 0.3948 0.7059 0.5303 -0.0226 0.0286  0.0437  154 GLU A N     
23   C CA    . GLU A 13  ? 0.4059 0.7194 0.5453 -0.0332 0.0274  0.0503  154 GLU A CA    
24   C C     . GLU A 13  ? 0.3652 0.6744 0.5145 -0.0377 0.0238  0.0505  154 GLU A C     
25   O O     . GLU A 13  ? 0.3763 0.6771 0.5297 -0.0434 0.0211  0.0550  154 GLU A O     
26   C CB    . GLU A 13  ? 0.4580 0.7863 0.5958 -0.0375 0.0306  0.0518  154 GLU A CB    
27   C CG    . GLU A 13  ? 0.5922 0.9225 0.7317 -0.0488 0.0294  0.0596  154 GLU A CG    
28   C CD    . GLU A 13  ? 0.6741 1.0137 0.8055 -0.0518 0.0328  0.0626  154 GLU A CD    
29   O OE1   . GLU A 13  ? 0.6613 1.0136 0.7936 -0.0557 0.0350  0.0627  154 GLU A OE1   
30   O OE2   . GLU A 13  ? 0.6626 0.9972 0.7866 -0.0500 0.0333  0.0643  154 GLU A OE2   
31   N N     . ILE A 14  ? 0.2968 0.6116 0.4506 -0.0353 0.0237  0.0456  155 ILE A N     
32   C CA    . ILE A 14  ? 0.3260 0.6371 0.4887 -0.0384 0.0205  0.0438  155 ILE A CA    
33   C C     . ILE A 14  ? 0.2913 0.5942 0.4529 -0.0299 0.0191  0.0381  155 ILE A C     
34   O O     . ILE A 14  ? 0.2719 0.5760 0.4271 -0.0216 0.0208  0.0347  155 ILE A O     
35   C CB    . ILE A 14  ? 0.3368 0.6606 0.5050 -0.0423 0.0209  0.0426  155 ILE A CB    
36   C CG1   . ILE A 14  ? 0.3119 0.6447 0.4765 -0.0340 0.0230  0.0376  155 ILE A CG1   
37   C CG2   . ILE A 14  ? 0.3335 0.6655 0.5022 -0.0513 0.0224  0.0485  155 ILE A CG2   
38   C CD1   . ILE A 14  ? 0.3664 0.7060 0.5374 -0.0340 0.0214  0.0338  155 ILE A CD1   
39   N N     . PHE A 15  ? 0.2654 0.5598 0.4334 -0.0322 0.0160  0.0369  156 PHE A N     
40   C CA    . PHE A 15  ? 0.1967 0.4833 0.3637 -0.0253 0.0144  0.0315  156 PHE A CA    
41   C C     . PHE A 15  ? 0.1828 0.4774 0.3519 -0.0230 0.0138  0.0269  156 PHE A C     
42   O O     . PHE A 15  ? 0.1547 0.4553 0.3313 -0.0293 0.0125  0.0266  156 PHE A O     
43   C CB    . PHE A 15  ? 0.1778 0.4533 0.3515 -0.0292 0.0115  0.0316  156 PHE A CB    
44   C CG    . PHE A 15  ? 0.1735 0.4407 0.3457 -0.0228 0.0101  0.0264  156 PHE A CG    
45   C CD1   . PHE A 15  ? 0.1574 0.4277 0.3326 -0.0218 0.0086  0.0213  156 PHE A CD1   
46   C CD2   . PHE A 15  ? 0.1832 0.4401 0.3507 -0.0183 0.0103  0.0268  156 PHE A CD2   
47   C CE1   . PHE A 15  ? 0.1419 0.4051 0.3148 -0.0165 0.0074  0.0170  156 PHE A CE1   
48   C CE2   . PHE A 15  ? 0.2180 0.4673 0.3837 -0.0129 0.0092  0.0221  156 PHE A CE2   
49   C CZ    . PHE A 15  ? 0.1849 0.4374 0.3531 -0.0121 0.0078  0.0172  156 PHE A CZ    
50   N N     . ASP A 16  ? 0.1482 0.4429 0.3108 -0.0144 0.0145  0.0236  157 ASP A N     
51   C CA    . ASP A 16  ? 0.1472 0.4488 0.3114 -0.0116 0.0132  0.0198  157 ASP A CA    
52   C C     . ASP A 16  ? 0.1411 0.4343 0.2989 -0.0032 0.0123  0.0166  157 ASP A C     
53   O O     . ASP A 16  ? 0.1445 0.4341 0.2949 0.0031  0.0142  0.0168  157 ASP A O     
54   C CB    . ASP A 16  ? 0.1368 0.4522 0.3002 -0.0101 0.0154  0.0203  157 ASP A CB    
55   C CG    . ASP A 16  ? 0.2398 0.5631 0.4052 -0.0069 0.0136  0.0170  157 ASP A CG    
56   O OD1   . ASP A 16  ? 0.2913 0.6106 0.4517 0.0008  0.0129  0.0147  157 ASP A OD1   
57   O OD2   . ASP A 16  ? 0.3566 0.6903 0.5287 -0.0124 0.0126  0.0170  157 ASP A OD2   
58   N N     . VAL A 17  ? 0.1123 0.4028 0.2729 -0.0036 0.0095  0.0135  158 VAL A N     
59   C CA    . VAL A 17  ? 0.1168 0.3981 0.2710 0.0031  0.0086  0.0110  158 VAL A CA    
60   C C     . VAL A 17  ? 0.1626 0.4481 0.3103 0.0111  0.0093  0.0103  158 VAL A C     
61   O O     . VAL A 17  ? 0.1058 0.3828 0.2463 0.0173  0.0098  0.0097  158 VAL A O     
62   C CB    . VAL A 17  ? 0.1850 0.4638 0.3433 0.0004  0.0055  0.0077  158 VAL A CB    
63   C CG1   . VAL A 17  ? 0.1383 0.4290 0.2991 -0.0004 0.0036  0.0057  158 VAL A CG1   
64   C CG2   . VAL A 17  ? 0.0905 0.3580 0.2421 0.0061  0.0049  0.0057  158 VAL A CG2   
65   N N     . ASN A 18  ? 0.1186 0.4171 0.2692 0.0110  0.0095  0.0104  159 ASN A N     
66   C CA    . ASN A 18  ? 0.1632 0.4653 0.3090 0.0190  0.0101  0.0098  159 ASN A CA    
67   C C     . ASN A 18  ? 0.1161 0.4155 0.2569 0.0232  0.0136  0.0113  159 ASN A C     
68   O O     . ASN A 18  ? 0.1358 0.4299 0.2706 0.0305  0.0142  0.0105  159 ASN A O     
69   C CB    . ASN A 18  ? 0.2193 0.5369 0.3705 0.0185  0.0091  0.0095  159 ASN A CB    
70   C CG    . ASN A 18  ? 0.2838 0.6050 0.4388 0.0148  0.0053  0.0076  159 ASN A CG    
71   O OD1   . ASN A 18  ? 0.2875 0.6043 0.4386 0.0185  0.0031  0.0061  159 ASN A OD1   
72   N ND2   . ASN A 18  ? 0.3644 0.6952 0.5269 0.0075  0.0045  0.0077  159 ASN A ND2   
73   N N     . ALA A 19  ? 0.1322 0.4356 0.2754 0.0183  0.0160  0.0134  160 ALA A N     
74   C CA    . ALA A 19  ? 0.1654 0.4661 0.3032 0.0213  0.0194  0.0145  160 ALA A CA    
75   C C     . ALA A 19  ? 0.1416 0.4270 0.2725 0.0245  0.0193  0.0142  160 ALA A C     
76   O O     . ALA A 19  ? 0.1484 0.4291 0.2730 0.0308  0.0209  0.0134  160 ALA A O     
77   C CB    . ALA A 19  ? 0.1341 0.4416 0.2752 0.0140  0.0215  0.0174  160 ALA A CB    
78   N N     . ILE A 20  ? 0.1329 0.4103 0.2656 0.0202  0.0173  0.0147  161 ILE A N     
79   C CA    . ILE A 20  ? 0.1151 0.3785 0.2420 0.0228  0.0170  0.0145  161 ILE A CA    
80   C C     . ILE A 20  ? 0.1325 0.3899 0.2538 0.0301  0.0160  0.0119  161 ILE A C     
81   O O     . ILE A 20  ? 0.0945 0.3442 0.2088 0.0352  0.0173  0.0116  161 ILE A O     
82   C CB    . ILE A 20  ? 0.1479 0.4053 0.2799 0.0168  0.0149  0.0151  161 ILE A CB    
83   C CG1   . ILE A 20  ? 0.2302 0.4901 0.3659 0.0103  0.0162  0.0189  161 ILE A CG1   
84   C CG2   . ILE A 20  ? 0.1401 0.3840 0.2673 0.0202  0.0141  0.0137  161 ILE A CG2   
85   C CD1   . ILE A 20  ? 0.2355 0.4953 0.3804 0.0027  0.0140  0.0197  161 ILE A CD1   
86   N N     . ARG A 21  ? 0.1247 0.3861 0.2489 0.0304  0.0134  0.0102  162 ARG A N     
87   C CA    . ARG A 21  ? 0.1126 0.3694 0.2317 0.0366  0.0119  0.0085  162 ARG A CA    
88   C C     . ARG A 21  ? 0.1585 0.4166 0.2731 0.0436  0.0139  0.0087  162 ARG A C     
89   O O     . ARG A 21  ? 0.1369 0.3867 0.2453 0.0492  0.0137  0.0081  162 ARG A O     
90   C CB    . ARG A 21  ? 0.1256 0.3908 0.2492 0.0353  0.0089  0.0072  162 ARG A CB    
91   C CG    . ARG A 21  ? 0.1389 0.4015 0.2664 0.0294  0.0067  0.0058  162 ARG A CG    
92   C CD    . ARG A 21  ? 0.1175 0.3906 0.2491 0.0276  0.0037  0.0042  162 ARG A CD    
93   N NE    . ARG A 21  ? 0.1257 0.4001 0.2520 0.0340  0.0022  0.0039  162 ARG A NE    
94   C CZ    . ARG A 21  ? 0.1790 0.4474 0.3005 0.0360  0.0004  0.0025  162 ARG A CZ    
95   N NH1   . ARG A 21  ? 0.1187 0.3790 0.2401 0.0324  0.0002  0.0007  162 ARG A NH1   
96   N NH2   . ARG A 21  ? 0.1436 0.4148 0.2608 0.0417  -0.0011 0.0030  162 ARG A NH2   
97   N N     . ALA A 22  ? 0.1302 0.3990 0.2483 0.0434  0.0159  0.0094  163 ALA A N     
98   C CA    . ALA A 22  ? 0.1910 0.4620 0.3064 0.0502  0.0180  0.0089  163 ALA A CA    
99   C C     . ALA A 22  ? 0.1640 0.4239 0.2722 0.0533  0.0205  0.0087  163 ALA A C     
100  O O     . ALA A 22  ? 0.1892 0.4472 0.2943 0.0598  0.0219  0.0077  163 ALA A O     
101  C CB    . ALA A 22  ? 0.1873 0.4729 0.3086 0.0486  0.0202  0.0093  163 ALA A CB    
102  N N     . ASP A 23  ? 0.1377 0.3907 0.2437 0.0488  0.0210  0.0097  164 ASP A N     
103  C CA    . ASP A 23  ? 0.1712 0.4140 0.2702 0.0512  0.0230  0.0096  164 ASP A CA    
104  C C     . ASP A 23  ? 0.1562 0.3862 0.2494 0.0554  0.0213  0.0086  164 ASP A C     
105  O O     . ASP A 23  ? 0.1678 0.3893 0.2548 0.0584  0.0230  0.0082  164 ASP A O     
106  C CB    . ASP A 23  ? 0.1308 0.3717 0.2302 0.0448  0.0238  0.0116  164 ASP A CB    
107  C CG    . ASP A 23  ? 0.1628 0.4159 0.2660 0.0406  0.0262  0.0132  164 ASP A CG    
108  O OD1   . ASP A 23  ? 0.1620 0.4220 0.2645 0.0440  0.0288  0.0120  164 ASP A OD1   
109  O OD2   . ASP A 23  ? 0.1337 0.3893 0.2407 0.0338  0.0257  0.0157  164 ASP A OD2   
110  N N     . PHE A 24  ? 0.1405 0.3694 0.2353 0.0552  0.0182  0.0082  165 PHE A N     
111  C CA    . PHE A 24  ? 0.1528 0.3704 0.2421 0.0578  0.0165  0.0076  165 PHE A CA    
112  C C     . PHE A 24  ? 0.1439 0.3631 0.2316 0.0641  0.0152  0.0072  165 PHE A C     
113  O O     . PHE A 24  ? 0.1446 0.3704 0.2358 0.0636  0.0126  0.0072  165 PHE A O     
114  C CB    . PHE A 24  ? 0.1199 0.3355 0.2122 0.0526  0.0139  0.0073  165 PHE A CB    
115  C CG    . PHE A 24  ? 0.1240 0.3357 0.2183 0.0472  0.0148  0.0081  165 PHE A CG    
116  C CD1   . PHE A 24  ? 0.1313 0.3514 0.2322 0.0420  0.0155  0.0094  165 PHE A CD1   
117  C CD2   . PHE A 24  ? 0.1060 0.3062 0.1961 0.0473  0.0149  0.0080  165 PHE A CD2   
118  C CE1   . PHE A 24  ? 0.1318 0.3489 0.2352 0.0371  0.0160  0.0110  165 PHE A CE1   
119  C CE2   . PHE A 24  ? 0.0971 0.2945 0.1900 0.0427  0.0155  0.0092  165 PHE A CE2   
120  C CZ    . PHE A 24  ? 0.1188 0.3246 0.2185 0.0377  0.0159  0.0110  165 PHE A CZ    
121  N N     . PRO A 25  ? 0.1643 0.3780 0.2472 0.0700  0.0168  0.0069  166 PRO A N     
122  C CA    . PRO A 25  ? 0.1535 0.3701 0.2365 0.0765  0.0157  0.0070  166 PRO A CA    
123  C C     . PRO A 25  ? 0.2370 0.4514 0.3182 0.0774  0.0122  0.0078  166 PRO A C     
124  O O     . PRO A 25  ? 0.1910 0.4139 0.2757 0.0799  0.0100  0.0085  166 PRO A O     
125  C CB    . PRO A 25  ? 0.1799 0.3880 0.2578 0.0821  0.0184  0.0063  166 PRO A CB    
126  C CG    . PRO A 25  ? 0.1753 0.3738 0.2482 0.0783  0.0200  0.0059  166 PRO A CG    
127  C CD    . PRO A 25  ? 0.1492 0.3544 0.2268 0.0712  0.0198  0.0064  166 PRO A CD    
128  N N     . ILE A 26  ? 0.1592 0.3639 0.2355 0.0751  0.0114  0.0075  167 ILE A N     
129  C CA    . ILE A 26  ? 0.1699 0.3735 0.2438 0.0761  0.0083  0.0080  167 ILE A CA    
130  C C     . ILE A 26  ? 0.1798 0.3949 0.2595 0.0721  0.0057  0.0078  167 ILE A C     
131  O O     . ILE A 26  ? 0.1923 0.4110 0.2710 0.0734  0.0029  0.0083  167 ILE A O     
132  C CB    . ILE A 26  ? 0.1980 0.3898 0.2661 0.0740  0.0085  0.0074  167 ILE A CB    
133  C CG1   . ILE A 26  ? 0.1855 0.3740 0.2484 0.0780  0.0064  0.0083  167 ILE A CG1   
134  C CG2   . ILE A 26  ? 0.1410 0.3347 0.2131 0.0668  0.0078  0.0060  167 ILE A CG2   
135  C CD1   . ILE A 26  ? 0.1571 0.3330 0.2132 0.0783  0.0074  0.0080  167 ILE A CD1   
136  N N     . LEU A 27  ? 0.1589 0.3809 0.2448 0.0670  0.0065  0.0071  168 LEU A N     
137  C CA    . LEU A 27  ? 0.1686 0.4017 0.2604 0.0626  0.0040  0.0065  168 LEU A CA    
138  C C     . LEU A 27  ? 0.2642 0.5094 0.3594 0.0662  0.0022  0.0077  168 LEU A C     
139  O O     . LEU A 27  ? 0.2033 0.4586 0.3027 0.0629  -0.0003 0.0072  168 LEU A O     
140  C CB    . LEU A 27  ? 0.1552 0.3919 0.2530 0.0561  0.0054  0.0058  168 LEU A CB    
141  C CG    . LEU A 27  ? 0.1998 0.4266 0.2967 0.0516  0.0063  0.0048  168 LEU A CG    
142  C CD1   . LEU A 27  ? 0.1744 0.4066 0.2790 0.0450  0.0071  0.0048  168 LEU A CD1   
143  C CD2   . LEU A 27  ? 0.1658 0.3888 0.2607 0.0503  0.0042  0.0032  168 LEU A CD2   
144  N N     . ARG A 28  ? 0.2562 0.5009 0.3503 0.0727  0.0034  0.0089  169 ARG A N     
145  C CA    . ARG A 28  ? 0.2764 0.5320 0.3744 0.0770  0.0014  0.0104  169 ARG A CA    
146  C C     . ARG A 28  ? 0.2624 0.5143 0.3556 0.0825  -0.0012 0.0122  169 ARG A C     
147  O O     . ARG A 28  ? 0.2886 0.5485 0.3848 0.0870  -0.0033 0.0140  169 ARG A O     
148  C CB    . ARG A 28  ? 0.2501 0.5100 0.3523 0.0811  0.0041  0.0106  169 ARG A CB    
149  C CG    . ARG A 28  ? 0.2882 0.5549 0.3958 0.0753  0.0064  0.0093  169 ARG A CG    
150  C CD    . ARG A 28  ? 0.3470 0.6272 0.4623 0.0776  0.0075  0.0095  169 ARG A CD    
151  N NE    . ARG A 28  ? 0.3591 0.6433 0.4775 0.0732  0.0108  0.0086  169 ARG A NE    
152  C CZ    . ARG A 28  ? 0.3466 0.6425 0.4714 0.0674  0.0105  0.0086  169 ARG A CZ    
153  N NH1   . ARG A 28  ? 0.2572 0.5625 0.3863 0.0653  0.0070  0.0090  169 ARG A NH1   
154  N NH2   . ARG A 28  ? 0.2673 0.5662 0.3942 0.0634  0.0136  0.0082  169 ARG A NH2   
155  N N     . GLU A 29  ? 0.2451 0.4855 0.3311 0.0821  -0.0012 0.0119  170 GLU A N     
156  C CA    . GLU A 29  ? 0.2702 0.5072 0.3510 0.0869  -0.0036 0.0140  170 GLU A CA    
157  C C     . GLU A 29  ? 0.3431 0.5917 0.4255 0.0844  -0.0078 0.0147  170 GLU A C     
158  O O     . GLU A 29  ? 0.2065 0.4627 0.2925 0.0779  -0.0086 0.0126  170 GLU A O     
159  C CB    . GLU A 29  ? 0.2949 0.5175 0.3677 0.0865  -0.0022 0.0133  170 GLU A CB    
160  C CG    . GLU A 29  ? 0.3470 0.5631 0.4138 0.0928  -0.0036 0.0159  170 GLU A CG    
161  C CD    . GLU A 29  ? 0.3697 0.5770 0.4352 0.0993  -0.0011 0.0168  170 GLU A CD    
162  O OE1   . GLU A 29  ? 0.3758 0.5826 0.4446 0.0987  0.0019  0.0151  170 GLU A OE1   
163  O OE2   . GLU A 29  ? 0.3191 0.5201 0.3803 0.1048  -0.0022 0.0193  170 GLU A OE2   
164  N N     . THR A 30  ? 0.3400 0.5901 0.4197 0.0896  -0.0107 0.0178  171 THR A N     
165  C CA    . THR A 30  ? 0.3666 0.6289 0.4471 0.0880  -0.0153 0.0192  171 THR A CA    
166  C C     . THR A 30  ? 0.3189 0.5758 0.3911 0.0879  -0.0171 0.0200  171 THR A C     
167  O O     . THR A 30  ? 0.3690 0.6139 0.4356 0.0925  -0.0159 0.0217  171 THR A O     
168  C CB    . THR A 30  ? 0.3498 0.6209 0.4351 0.0941  -0.0180 0.0230  171 THR A CB    
169  O OG1   . THR A 30  ? 0.3586 0.6408 0.4527 0.0919  -0.0174 0.0217  171 THR A OG1   
170  C CG2   . THR A 30  ? 0.3904 0.6705 0.4738 0.0940  -0.0233 0.0259  171 THR A CG2   
171  N N     . VAL A 31  ? 0.2971 0.5633 0.3687 0.0822  -0.0198 0.0186  172 VAL A N     
172  C CA    . VAL A 31  ? 0.3981 0.6624 0.4622 0.0810  -0.0217 0.0188  172 VAL A CA    
173  C C     . VAL A 31  ? 0.3873 0.6659 0.4511 0.0797  -0.0270 0.0212  172 VAL A C     
174  O O     . VAL A 31  ? 0.3910 0.6818 0.4593 0.0739  -0.0286 0.0186  172 VAL A O     
175  C CB    . VAL A 31  ? 0.3591 0.6207 0.4223 0.0739  -0.0196 0.0134  172 VAL A CB    
176  C CG1   . VAL A 31  ? 0.3519 0.6157 0.4082 0.0718  -0.0219 0.0129  172 VAL A CG1   
177  C CG2   . VAL A 31  ? 0.3803 0.6270 0.4432 0.0750  -0.0148 0.0118  172 VAL A CG2   
178  N N     . ASN A 32  ? 0.4841 0.7608 0.5422 0.0846  -0.0301 0.0263  173 ASN A N     
179  C CA    . ASN A 32  ? 0.4803 0.7699 0.5368 0.0831  -0.0358 0.0295  173 ASN A CA    
180  C C     . ASN A 32  ? 0.5187 0.8211 0.5840 0.0832  -0.0378 0.0305  173 ASN A C     
181  O O     . ASN A 32  ? 0.5578 0.8741 0.6239 0.0782  -0.0416 0.0304  173 ASN A O     
182  C CB    . ASN A 32  ? 0.5203 0.8174 0.5717 0.0745  -0.0373 0.0255  173 ASN A CB    
183  C CG    . ASN A 32  ? 0.6301 0.9385 0.6766 0.0722  -0.0433 0.0292  173 ASN A CG    
184  O OD1   . ASN A 32  ? 0.6937 0.9988 0.7364 0.0777  -0.0464 0.0359  173 ASN A OD1   
185  N ND2   . ASN A 32  ? 0.5802 0.9015 0.6268 0.0635  -0.0450 0.0247  173 ASN A ND2   
186  N N     . GLY A 33  ? 0.4825 0.7810 0.5546 0.0882  -0.0352 0.0311  174 GLY A N     
187  C CA    . GLY A 33  ? 0.3865 0.6977 0.4678 0.0882  -0.0366 0.0316  174 GLY A CA    
188  C C     . GLY A 33  ? 0.4114 0.7297 0.4980 0.0807  -0.0344 0.0261  174 GLY A C     
189  O O     . GLY A 33  ? 0.3786 0.7080 0.4731 0.0802  -0.0353 0.0262  174 GLY A O     
190  N N     . LYS A 34  ? 0.3594 0.6717 0.4427 0.0750  -0.0316 0.0213  175 LYS A N     
191  C CA    . LYS A 34  ? 0.3148 0.6316 0.4031 0.0674  -0.0296 0.0161  175 LYS A CA    
192  C C     . LYS A 34  ? 0.3324 0.6364 0.4223 0.0680  -0.0243 0.0139  175 LYS A C     
193  O O     . LYS A 34  ? 0.3041 0.5948 0.3891 0.0725  -0.0220 0.0149  175 LYS A O     
194  C CB    . LYS A 34  ? 0.3378 0.6581 0.4220 0.0594  -0.0309 0.0118  175 LYS A CB    
195  C CG    . LYS A 34  ? 0.4257 0.7616 0.5087 0.0553  -0.0362 0.0123  175 LYS A CG    
196  C CD    . LYS A 34  ? 0.4848 0.8209 0.5610 0.0607  -0.0399 0.0180  175 LYS A CD    
197  C CE    . LYS A 34  ? 0.5584 0.9089 0.6312 0.0551  -0.0452 0.0183  175 LYS A CE    
198  N NZ    . LYS A 34  ? 0.4830 0.8345 0.5501 0.0467  -0.0448 0.0122  175 LYS A NZ    
199  N N     . PRO A 35  ? 0.2774 0.5850 0.3738 0.0630  -0.0224 0.0110  176 PRO A N     
200  C CA    . PRO A 35  ? 0.2763 0.5720 0.3735 0.0623  -0.0178 0.0092  176 PRO A CA    
201  C C     . PRO A 35  ? 0.2711 0.5556 0.3629 0.0594  -0.0163 0.0064  176 PRO A C     
202  O O     . PRO A 35  ? 0.2508 0.5396 0.3414 0.0542  -0.0181 0.0036  176 PRO A O     
203  C CB    . PRO A 35  ? 0.2867 0.5911 0.3921 0.0561  -0.0171 0.0070  176 PRO A CB    
204  C CG    . PRO A 35  ? 0.3031 0.6239 0.4125 0.0559  -0.0211 0.0085  176 PRO A CG    
205  C CD    . PRO A 35  ? 0.3206 0.6433 0.4236 0.0574  -0.0246 0.0097  176 PRO A CD    
206  N N     . LEU A 36  ? 0.2411 0.5118 0.3299 0.0625  -0.0129 0.0069  177 LEU A N     
207  C CA    . LEU A 36  ? 0.2251 0.4849 0.3103 0.0595  -0.0110 0.0042  177 LEU A CA    
208  C C     . LEU A 36  ? 0.1911 0.4524 0.2825 0.0518  -0.0099 0.0006  177 LEU A C     
209  O O     . LEU A 36  ? 0.2055 0.4695 0.3027 0.0501  -0.0086 0.0009  177 LEU A O     
210  C CB    . LEU A 36  ? 0.1975 0.4426 0.2785 0.0642  -0.0077 0.0057  177 LEU A CB    
211  C CG    . LEU A 36  ? 0.1604 0.3939 0.2392 0.0608  -0.0054 0.0031  177 LEU A CG    
212  C CD1   . LEU A 36  ? 0.1427 0.3749 0.2159 0.0609  -0.0069 0.0020  177 LEU A CD1   
213  C CD2   . LEU A 36  ? 0.1484 0.3692 0.2243 0.0641  -0.0021 0.0045  177 LEU A CD2   
214  N N     . ILE A 37  ? 0.1341 0.3940 0.2250 0.0470  -0.0102 -0.0031 178 ILE A N     
215  C CA    . ILE A 37  ? 0.1632 0.4217 0.2605 0.0399  -0.0089 -0.0067 178 ILE A CA    
216  C C     . ILE A 37  ? 0.1445 0.3900 0.2390 0.0396  -0.0066 -0.0086 178 ILE A C     
217  O O     . ILE A 37  ? 0.1400 0.3857 0.2311 0.0387  -0.0074 -0.0114 178 ILE A O     
218  C CB    . ILE A 37  ? 0.1785 0.4493 0.2800 0.0333  -0.0115 -0.0107 178 ILE A CB    
219  C CG1   . ILE A 37  ? 0.1746 0.4585 0.2796 0.0333  -0.0137 -0.0085 178 ILE A CG1   
220  C CG2   . ILE A 37  ? 0.1417 0.4089 0.2504 0.0261  -0.0099 -0.0149 178 ILE A CG2   
221  C CD1   . ILE A 37  ? 0.1322 0.4291 0.2406 0.0264  -0.0167 -0.0123 178 ILE A CD1   
222  N N     . TRP A 38  ? 0.1183 0.3534 0.2142 0.0402  -0.0038 -0.0071 179 TRP A N     
223  C CA    . TRP A 38  ? 0.1210 0.3431 0.2141 0.0406  -0.0017 -0.0080 179 TRP A CA    
224  C C     . TRP A 38  ? 0.1456 0.3663 0.2463 0.0340  -0.0010 -0.0119 179 TRP A C     
225  O O     . TRP A 38  ? 0.1283 0.3459 0.2353 0.0312  0.0004  -0.0110 179 TRP A O     
226  C CB    . TRP A 38  ? 0.1463 0.3586 0.2368 0.0442  0.0007  -0.0045 179 TRP A CB    
227  C CG    . TRP A 38  ? 0.1329 0.3324 0.2196 0.0450  0.0026  -0.0050 179 TRP A CG    
228  C CD1   . TRP A 38  ? 0.0993 0.2914 0.1902 0.0418  0.0044  -0.0055 179 TRP A CD1   
229  C CD2   . TRP A 38  ? 0.0970 0.2909 0.1756 0.0490  0.0026  -0.0049 179 TRP A CD2   
230  N NE1   . TRP A 38  ? 0.1126 0.2947 0.1985 0.0435  0.0056  -0.0059 179 TRP A NE1   
231  C CE2   . TRP A 38  ? 0.1659 0.3487 0.2441 0.0478  0.0047  -0.0057 179 TRP A CE2   
232  C CE3   . TRP A 38  ? 0.1083 0.3059 0.1804 0.0535  0.0010  -0.0038 179 TRP A CE3   
233  C CZ2   . TRP A 38  ? 0.1561 0.3316 0.2273 0.0506  0.0054  -0.0058 179 TRP A CZ2   
234  C CZ3   . TRP A 38  ? 0.1641 0.3544 0.2292 0.0565  0.0016  -0.0036 179 TRP A CZ3   
235  C CH2   . TRP A 38  ? 0.1343 0.3136 0.1989 0.0549  0.0039  -0.0048 179 TRP A CH2   
236  N N     . PHE A 39  ? 0.0824 0.3059 0.1830 0.0313  -0.0018 -0.0166 180 PHE A N     
237  C CA    . PHE A 39  ? 0.1047 0.3255 0.2127 0.0255  -0.0007 -0.0215 180 PHE A CA    
238  C C     . PHE A 39  ? 0.1225 0.3327 0.2274 0.0270  0.0013  -0.0233 180 PHE A C     
239  O O     . PHE A 39  ? 0.1133 0.3236 0.2220 0.0232  0.0020  -0.0292 180 PHE A O     
240  C CB    . PHE A 39  ? 0.0872 0.3199 0.1988 0.0200  -0.0026 -0.0273 180 PHE A CB    
241  C CG    . PHE A 39  ? 0.1115 0.3538 0.2290 0.0163  -0.0044 -0.0266 180 PHE A CG    
242  C CD1   . PHE A 39  ? 0.0945 0.3348 0.2155 0.0173  -0.0037 -0.0216 180 PHE A CD1   
243  C CD2   . PHE A 39  ? 0.1087 0.3628 0.2283 0.0110  -0.0066 -0.0315 180 PHE A CD2   
244  C CE1   . PHE A 39  ? 0.1231 0.3730 0.2499 0.0135  -0.0051 -0.0210 180 PHE A CE1   
245  C CE2   . PHE A 39  ? 0.1523 0.4154 0.2775 0.0071  -0.0082 -0.0309 180 PHE A CE2   
246  C CZ    . PHE A 39  ? 0.1315 0.3925 0.2605 0.0085  -0.0074 -0.0255 180 PHE A CZ    
247  N N     . ASP A 40  ? 0.1335 0.3347 0.2316 0.0323  0.0025  -0.0190 181 ASP A N     
248  C CA    . ASP A 40  ? 0.1189 0.3103 0.2133 0.0338  0.0043  -0.0203 181 ASP A CA    
249  C C     . ASP A 40  ? 0.1441 0.3240 0.2410 0.0343  0.0062  -0.0171 181 ASP A C     
250  O O     . ASP A 40  ? 0.0932 0.2642 0.1844 0.0372  0.0075  -0.0155 181 ASP A O     
251  C CB    . ASP A 40  ? 0.1055 0.2967 0.1890 0.0392  0.0039  -0.0183 181 ASP A CB    
252  C CG    . ASP A 40  ? 0.2031 0.3889 0.2831 0.0392  0.0055  -0.0215 181 ASP A CG    
253  O OD1   . ASP A 40  ? 0.1631 0.3475 0.2496 0.0347  0.0069  -0.0266 181 ASP A OD1   
254  O OD2   . ASP A 40  ? 0.2049 0.3875 0.2763 0.0436  0.0057  -0.0189 181 ASP A OD2   
255  N N     . ASN A 41  ? 0.1036 0.2848 0.2091 0.0311  0.0062  -0.0160 182 ASN A N     
256  C CA    . ASN A 41  ? 0.1107 0.2842 0.2191 0.0312  0.0074  -0.0122 182 ASN A CA    
257  C C     . ASN A 41  ? 0.1457 0.3103 0.2573 0.0302  0.0088  -0.0137 182 ASN A C     
258  O O     . ASN A 41  ? 0.1678 0.3252 0.2778 0.0318  0.0097  -0.0103 182 ASN A O     
259  C CB    . ASN A 41  ? 0.1075 0.2870 0.2252 0.0274  0.0068  -0.0107 182 ASN A CB    
260  C CG    . ASN A 41  ? 0.1477 0.3350 0.2617 0.0289  0.0059  -0.0086 182 ASN A CG    
261  O OD1   . ASN A 41  ? 0.1235 0.3083 0.2309 0.0327  0.0066  -0.0053 182 ASN A OD1   
262  N ND2   . ASN A 41  ? 0.1040 0.3014 0.2221 0.0260  0.0043  -0.0109 182 ASN A ND2   
263  N N     . ALA A 42  ? 0.1327 0.2985 0.2493 0.0275  0.0090  -0.0191 183 ALA A N     
264  C CA    . ALA A 42  ? 0.1838 0.3413 0.3039 0.0269  0.0104  -0.0210 183 ALA A CA    
265  C C     . ALA A 42  ? 0.1900 0.3410 0.2996 0.0307  0.0116  -0.0204 183 ALA A C     
266  O O     . ALA A 42  ? 0.2208 0.3643 0.3322 0.0308  0.0127  -0.0204 183 ALA A O     
267  C CB    . ALA A 42  ? 0.1524 0.3124 0.2802 0.0229  0.0108  -0.0286 183 ALA A CB    
268  N N     . ALA A 43  ? 0.1790 0.3333 0.2783 0.0337  0.0110  -0.0197 184 ALA A N     
269  C CA    . ALA A 43  ? 0.1477 0.2961 0.2369 0.0374  0.0119  -0.0183 184 ALA A CA    
270  C C     . ALA A 43  ? 0.1651 0.3081 0.2493 0.0404  0.0119  -0.0126 184 ALA A C     
271  O O     . ALA A 43  ? 0.1625 0.2976 0.2441 0.0413  0.0130  -0.0111 184 ALA A O     
272  C CB    . ALA A 43  ? 0.1314 0.2866 0.2125 0.0394  0.0111  -0.0201 184 ALA A CB    
273  N N     . THR A 44  ? 0.1460 0.2939 0.2288 0.0417  0.0108  -0.0100 185 THR A N     
274  C CA    . THR A 44  ? 0.1139 0.2582 0.1937 0.0436  0.0112  -0.0058 185 THR A CA    
275  C C     . THR A 44  ? 0.1138 0.2661 0.1966 0.0432  0.0103  -0.0043 185 THR A C     
276  O O     . THR A 44  ? 0.0982 0.2586 0.1830 0.0425  0.0090  -0.0059 185 THR A O     
277  C CB    . THR A 44  ? 0.1375 0.2764 0.2064 0.0483  0.0119  -0.0041 185 THR A CB    
278  O OG1   . THR A 44  ? 0.1663 0.3005 0.2330 0.0493  0.0129  -0.0013 185 THR A OG1   
279  C CG2   . THR A 44  ? 0.1353 0.2801 0.1989 0.0519  0.0107  -0.0034 185 THR A CG2   
280  N N     . THR A 45  ? 0.0978 0.2492 0.1809 0.0434  0.0110  -0.0013 186 THR A N     
281  C CA    . THR A 45  ? 0.1089 0.2685 0.1952 0.0427  0.0107  0.0002  186 THR A CA    
282  C C     . THR A 45  ? 0.1231 0.2834 0.2015 0.0476  0.0113  0.0020  186 THR A C     
283  O O     . THR A 45  ? 0.1358 0.2890 0.2068 0.0509  0.0123  0.0026  186 THR A O     
284  C CB    . THR A 45  ? 0.1110 0.2720 0.2045 0.0390  0.0112  0.0022  186 THR A CB    
285  O OG1   . THR A 45  ? 0.1245 0.2792 0.2133 0.0404  0.0126  0.0043  186 THR A OG1   
286  C CG2   . THR A 45  ? 0.1001 0.2610 0.2038 0.0345  0.0104  0.0005  186 THR A CG2   
287  N N     . GLN A 46  ? 0.1152 0.2842 0.1959 0.0478  0.0109  0.0027  187 GLN A N     
288  C CA    . GLN A 46  ? 0.1041 0.2752 0.1797 0.0525  0.0117  0.0041  187 GLN A CA    
289  C C     . GLN A 46  ? 0.1447 0.3168 0.2211 0.0517  0.0139  0.0058  187 GLN A C     
290  O O     . GLN A 46  ? 0.1223 0.2959 0.2042 0.0471  0.0142  0.0066  187 GLN A O     
291  C CB    . GLN A 46  ? 0.1159 0.2974 0.1941 0.0535  0.0102  0.0039  187 GLN A CB    
292  C CG    . GLN A 46  ? 0.1109 0.2936 0.1876 0.0543  0.0079  0.0024  187 GLN A CG    
293  C CD    . GLN A 46  ? 0.1331 0.3076 0.2012 0.0591  0.0081  0.0028  187 GLN A CD    
294  O OE1   . GLN A 46  ? 0.1537 0.3215 0.2170 0.0624  0.0098  0.0040  187 GLN A OE1   
295  N NE2   . GLN A 46  ? 0.1176 0.2934 0.1838 0.0594  0.0064  0.0016  187 GLN A NE2   
296  N N     . LYS A 47  ? 0.1320 0.3034 0.2030 0.0563  0.0154  0.0064  188 LYS A N     
297  C CA    . LYS A 47  ? 0.1041 0.2756 0.1738 0.0560  0.0179  0.0075  188 LYS A CA    
298  C C     . LYS A 47  ? 0.1098 0.2920 0.1827 0.0565  0.0192  0.0080  188 LYS A C     
299  O O     . LYS A 47  ? 0.1427 0.3291 0.2155 0.0602  0.0189  0.0074  188 LYS A O     
300  C CB    . LYS A 47  ? 0.1205 0.2833 0.1820 0.0605  0.0195  0.0071  188 LYS A CB    
301  C CG    . LYS A 47  ? 0.1263 0.2792 0.1835 0.0615  0.0182  0.0064  188 LYS A CG    
302  C CD    . LYS A 47  ? 0.0986 0.2486 0.1596 0.0563  0.0174  0.0066  188 LYS A CD    
303  C CE    . LYS A 47  ? 0.1334 0.2747 0.1905 0.0572  0.0165  0.0055  188 LYS A CE    
304  N NZ    . LYS A 47  ? 0.1129 0.2526 0.1757 0.0525  0.0155  0.0050  188 LYS A NZ    
305  N N     . PRO A 48  ? 0.1327 0.3204 0.2085 0.0529  0.0208  0.0095  189 PRO A N     
306  C CA    . PRO A 48  ? 0.1239 0.3221 0.2018 0.0535  0.0228  0.0097  189 PRO A CA    
307  C C     . PRO A 48  ? 0.1214 0.3171 0.1931 0.0591  0.0255  0.0083  189 PRO A C     
308  O O     . PRO A 48  ? 0.1408 0.3276 0.2066 0.0607  0.0264  0.0079  189 PRO A O     
309  C CB    . PRO A 48  ? 0.1181 0.3221 0.1999 0.0474  0.0238  0.0121  189 PRO A CB    
310  C CG    . PRO A 48  ? 0.1177 0.3123 0.1977 0.0452  0.0229  0.0133  189 PRO A CG    
311  C CD    . PRO A 48  ? 0.0863 0.2715 0.1642 0.0479  0.0208  0.0113  189 PRO A CD    
312  N N     . GLN A 49  ? 0.1209 0.3249 0.1948 0.0621  0.0268  0.0074  190 GLN A N     
313  C CA    . GLN A 49  ? 0.1605 0.3628 0.2302 0.0676  0.0297  0.0054  190 GLN A CA    
314  C C     . GLN A 49  ? 0.1404 0.3406 0.2054 0.0658  0.0328  0.0053  190 GLN A C     
315  O O     . GLN A 49  ? 0.1290 0.3219 0.1883 0.0698  0.0347  0.0034  190 GLN A O     
316  C CB    . GLN A 49  ? 0.1499 0.3639 0.2248 0.0701  0.0312  0.0043  190 GLN A CB    
317  C CG    . GLN A 49  ? 0.1358 0.3478 0.2081 0.0769  0.0343  0.0016  190 GLN A CG    
318  C CD    . GLN A 49  ? 0.1813 0.3829 0.2506 0.0828  0.0323  0.0011  190 GLN A CD    
319  O OE1   . GLN A 49  ? 0.2211 0.4242 0.2933 0.0837  0.0291  0.0024  190 GLN A OE1   
320  N NE2   . GLN A 49  ? 0.2013 0.3927 0.2645 0.0863  0.0342  -0.0006 190 GLN A NE2   
321  N N     . ALA A 50  ? 0.1247 0.3317 0.1923 0.0596  0.0332  0.0075  191 ALA A N     
322  C CA    . ALA A 50  ? 0.1270 0.3342 0.1900 0.0572  0.0360  0.0080  191 ALA A CA    
323  C C     . ALA A 50  ? 0.1399 0.3345 0.1968 0.0581  0.0352  0.0080  191 ALA A C     
324  O O     . ALA A 50  ? 0.1380 0.3296 0.1887 0.0594  0.0380  0.0067  191 ALA A O     
325  C CB    . ALA A 50  ? 0.1071 0.3242 0.1746 0.0497  0.0359  0.0116  191 ALA A CB    
326  N N     . VAL A 51  ? 0.1138 0.3013 0.1722 0.0574  0.0318  0.0092  192 VAL A N     
327  C CA    . VAL A 51  ? 0.1169 0.2928 0.1699 0.0582  0.0312  0.0091  192 VAL A CA    
328  C C     . VAL A 51  ? 0.1463 0.3137 0.1930 0.0647  0.0324  0.0059  192 VAL A C     
329  O O     . VAL A 51  ? 0.1206 0.2819 0.1609 0.0661  0.0344  0.0048  192 VAL A O     
330  C CB    . VAL A 51  ? 0.1190 0.2902 0.1761 0.0557  0.0275  0.0105  192 VAL A CB    
331  C CG1   . VAL A 51  ? 0.1440 0.3034 0.1960 0.0571  0.0268  0.0099  192 VAL A CG1   
332  C CG2   . VAL A 51  ? 0.1359 0.3139 0.1998 0.0491  0.0265  0.0138  192 VAL A CG2   
333  N N     . ILE A 52  ? 0.1163 0.2832 0.1648 0.0686  0.0312  0.0048  193 ILE A N     
334  C CA    . ILE A 52  ? 0.1620 0.3216 0.2060 0.0751  0.0321  0.0024  193 ILE A CA    
335  C C     . ILE A 52  ? 0.1759 0.3369 0.2166 0.0775  0.0364  -0.0001 193 ILE A C     
336  O O     . ILE A 52  ? 0.2200 0.3717 0.2544 0.0805  0.0382  -0.0021 193 ILE A O     
337  C CB    . ILE A 52  ? 0.1912 0.3546 0.2396 0.0785  0.0301  0.0025  193 ILE A CB    
338  C CG1   . ILE A 52  ? 0.1450 0.3070 0.1957 0.0755  0.0263  0.0043  193 ILE A CG1   
339  C CG2   . ILE A 52  ? 0.1658 0.3227 0.2110 0.0856  0.0310  0.0007  193 ILE A CG2   
340  C CD1   . ILE A 52  ? 0.1727 0.3397 0.2272 0.0781  0.0239  0.0046  193 ILE A CD1   
341  N N     . ASP A 53  ? 0.1458 0.3185 0.1907 0.0759  0.0384  -0.0004 194 ASP A N     
342  C CA    . ASP A 53  ? 0.1799 0.3557 0.2221 0.0775  0.0431  -0.0035 194 ASP A CA    
343  C C     . ASP A 53  ? 0.1954 0.3684 0.2311 0.0736  0.0452  -0.0036 194 ASP A C     
344  O O     . ASP A 53  ? 0.2157 0.3853 0.2459 0.0756  0.0489  -0.0071 194 ASP A O     
345  C CB    . ASP A 53  ? 0.1744 0.3649 0.2229 0.0758  0.0448  -0.0036 194 ASP A CB    
346  C CG    . ASP A 53  ? 0.2636 0.4580 0.3184 0.0806  0.0438  -0.0044 194 ASP A CG    
347  O OD1   . ASP A 53  ? 0.2207 0.4063 0.2744 0.0858  0.0421  -0.0050 194 ASP A OD1   
348  O OD2   . ASP A 53  ? 0.2410 0.4480 0.3018 0.0791  0.0446  -0.0041 194 ASP A OD2   
349  N N     . ARG A 54  ? 0.1687 0.3432 0.2050 0.0680  0.0429  0.0001  195 ARG A N     
350  C CA    . ARG A 54  ? 0.1676 0.3408 0.1978 0.0642  0.0446  0.0007  195 ARG A CA    
351  C C     . ARG A 54  ? 0.2026 0.3619 0.2256 0.0675  0.0449  -0.0015 195 ARG A C     
352  O O     . ARG A 54  ? 0.1399 0.2964 0.1555 0.0669  0.0481  -0.0038 195 ARG A O     
353  C CB    . ARG A 54  ? 0.1495 0.3278 0.1838 0.0578  0.0418  0.0059  195 ARG A CB    
354  C CG    . ARG A 54  ? 0.1728 0.3528 0.2019 0.0529  0.0433  0.0079  195 ARG A CG    
355  C CD    . ARG A 54  ? 0.1800 0.3699 0.2055 0.0498  0.0472  0.0069  195 ARG A CD    
356  N NE    . ARG A 54  ? 0.1756 0.3664 0.1935 0.0448  0.0488  0.0082  195 ARG A NE    
357  C CZ    . ARG A 54  ? 0.2551 0.4388 0.2632 0.0464  0.0518  0.0038  195 ARG A CZ    
358  N NH1   . ARG A 54  ? 0.1972 0.3709 0.2029 0.0534  0.0534  -0.0018 195 ARG A NH1   
359  N NH2   . ARG A 54  ? 0.2316 0.4180 0.2320 0.0402  0.0530  0.0053  195 ARG A NH2   
360  N N     . LEU A 55  ? 0.1620 0.3126 0.1863 0.0706  0.0418  -0.0009 196 LEU A N     
361  C CA    . LEU A 55  ? 0.1715 0.3085 0.1890 0.0739  0.0419  -0.0028 196 LEU A CA    
362  C C     . LEU A 55  ? 0.2130 0.3449 0.2262 0.0792  0.0454  -0.0074 196 LEU A C     
363  O O     . LEU A 55  ? 0.2211 0.3447 0.2267 0.0799  0.0479  -0.0101 196 LEU A O     
364  C CB    . LEU A 55  ? 0.1448 0.2751 0.1647 0.0757  0.0380  -0.0011 196 LEU A CB    
365  C CG    . LEU A 55  ? 0.2296 0.3615 0.2536 0.0710  0.0346  0.0023  196 LEU A CG    
366  C CD1   . LEU A 55  ? 0.1818 0.3077 0.2074 0.0729  0.0313  0.0028  196 LEU A CD1   
367  C CD2   . LEU A 55  ? 0.1821 0.3103 0.2020 0.0679  0.0353  0.0032  196 LEU A CD2   
368  N N     . SER A 56  ? 0.2054 0.3417 0.2239 0.0831  0.0455  -0.0084 197 SER A N     
369  C CA    . SER A 56  ? 0.2203 0.3526 0.2369 0.0886  0.0491  -0.0128 197 SER A CA    
370  C C     . SER A 56  ? 0.2061 0.3416 0.2180 0.0862  0.0541  -0.0165 197 SER A C     
371  O O     . SER A 56  ? 0.2378 0.3645 0.2437 0.0887  0.0574  -0.0209 197 SER A O     
372  C CB    . SER A 56  ? 0.2130 0.3530 0.2378 0.0925  0.0486  -0.0129 197 SER A CB    
373  O OG    . SER A 56  ? 0.3071 0.4447 0.3351 0.0942  0.0440  -0.0096 197 SER A OG    
374  N N     . HIS A 57  ? 0.2113 0.3595 0.2256 0.0809  0.0549  -0.0150 198 HIS A N     
375  C CA    . HIS A 57  ? 0.2141 0.3673 0.2233 0.0775  0.0597  -0.0181 198 HIS A CA    
376  C C     . HIS A 57  ? 0.2044 0.3491 0.2035 0.0741  0.0605  -0.0189 198 HIS A C     
377  O O     . HIS A 57  ? 0.2618 0.4022 0.2535 0.0740  0.0648  -0.0238 198 HIS A O     
378  C CB    . HIS A 57  ? 0.1943 0.3632 0.2078 0.0718  0.0596  -0.0150 198 HIS A CB    
379  C CG    . HIS A 57  ? 0.2846 0.4603 0.2929 0.0678  0.0647  -0.0181 198 HIS A CG    
380  N ND1   . HIS A 57  ? 0.2854 0.4604 0.2849 0.0617  0.0656  -0.0174 198 HIS A ND1   
381  C CD2   . HIS A 57  ? 0.2447 0.4279 0.2546 0.0689  0.0691  -0.0220 198 HIS A CD2   
382  C CE1   . HIS A 57  ? 0.3168 0.4985 0.3120 0.0586  0.0703  -0.0208 198 HIS A CE1   
383  N NE2   . HIS A 57  ? 0.2901 0.4769 0.2918 0.0631  0.0727  -0.0238 198 HIS A NE2   
384  N N     . PHE A 58  ? 0.2039 0.3462 0.2025 0.0711  0.0566  -0.0143 199 PHE A N     
385  C CA    . PHE A 58  ? 0.1851 0.3197 0.1743 0.0679  0.0572  -0.0148 199 PHE A CA    
386  C C     . PHE A 58  ? 0.2115 0.3310 0.1941 0.0729  0.0592  -0.0199 199 PHE A C     
387  O O     . PHE A 58  ? 0.2311 0.3456 0.2044 0.0708  0.0625  -0.0239 199 PHE A O     
388  C CB    . PHE A 58  ? 0.2350 0.3694 0.2267 0.0650  0.0527  -0.0091 199 PHE A CB    
389  C CG    . PHE A 58  ? 0.2044 0.3314 0.1871 0.0619  0.0530  -0.0092 199 PHE A CG    
390  C CD1   . PHE A 58  ? 0.1838 0.3183 0.1617 0.0547  0.0536  -0.0070 199 PHE A CD1   
391  C CD2   . PHE A 58  ? 0.2155 0.3282 0.1939 0.0656  0.0523  -0.0111 199 PHE A CD2   
392  C CE1   . PHE A 58  ? 0.2307 0.3579 0.2000 0.0507  0.0529  -0.0068 199 PHE A CE1   
393  C CE2   . PHE A 58  ? 0.1975 0.3035 0.1672 0.0624  0.0526  -0.0113 199 PHE A CE2   
394  C CZ    . PHE A 58  ? 0.2339 0.3458 0.1994 0.0542  0.0520  -0.0091 199 PHE A CZ    
395  N N     . TYR A 59  ? 0.2146 0.3264 0.2014 0.0789  0.0570  -0.0196 200 TYR A N     
396  C CA    . TYR A 59  ? 0.2082 0.3047 0.1888 0.0834  0.0586  -0.0236 200 TYR A CA    
397  C C     . TYR A 59  ? 0.2435 0.3386 0.2223 0.0864  0.0637  -0.0300 200 TYR A C     
398  O O     . TYR A 59  ? 0.2767 0.3599 0.2477 0.0876  0.0664  -0.0346 200 TYR A O     
399  C CB    . TYR A 59  ? 0.2091 0.2986 0.1943 0.0886  0.0548  -0.0210 200 TYR A CB    
400  C CG    . TYR A 59  ? 0.2160 0.3015 0.1998 0.0859  0.0509  -0.0167 200 TYR A CG    
401  C CD1   . TYR A 59  ? 0.2236 0.3003 0.1986 0.0831  0.0518  -0.0178 200 TYR A CD1   
402  C CD2   . TYR A 59  ? 0.1966 0.2875 0.1880 0.0856  0.0467  -0.0121 200 TYR A CD2   
403  C CE1   . TYR A 59  ? 0.2099 0.2839 0.1844 0.0806  0.0488  -0.0141 200 TYR A CE1   
404  C CE2   . TYR A 59  ? 0.1985 0.2862 0.1894 0.0829  0.0437  -0.0089 200 TYR A CE2   
405  C CZ    . TYR A 59  ? 0.2229 0.3025 0.2059 0.0807  0.0448  -0.0099 200 TYR A CZ    
406  O OH    . TYR A 59  ? 0.2502 0.3274 0.2336 0.0782  0.0423  -0.0071 200 TYR A OH    
407  N N     . ALA A 60  ? 0.2303 0.3370 0.2161 0.0874  0.0652  -0.0306 201 ALA A N     
408  C CA    . ALA A 60  ? 0.2658 0.3719 0.2513 0.0907  0.0706  -0.0370 201 ALA A CA    
409  C C     . ALA A 60  ? 0.2579 0.3689 0.2358 0.0847  0.0755  -0.0411 201 ALA A C     
410  O O     . ALA A 60  ? 0.2905 0.3972 0.2650 0.0865  0.0808  -0.0478 201 ALA A O     
411  C CB    . ALA A 60  ? 0.2601 0.3769 0.2569 0.0947  0.0705  -0.0363 201 ALA A CB    
412  N N     . HIS A 61  ? 0.2425 0.3624 0.2176 0.0773  0.0740  -0.0372 202 HIS A N     
413  C CA    . HIS A 61  ? 0.2629 0.3904 0.2313 0.0709  0.0781  -0.0398 202 HIS A CA    
414  C C     . HIS A 61  ? 0.2812 0.4083 0.2398 0.0629  0.0765  -0.0372 202 HIS A C     
415  O O     . HIS A 61  ? 0.2925 0.4223 0.2424 0.0573  0.0799  -0.0403 202 HIS A O     
416  C CB    . HIS A 61  ? 0.3142 0.4590 0.2904 0.0688  0.0785  -0.0372 202 HIS A CB    
417  C CG    . HIS A 61  ? 0.3268 0.4746 0.3123 0.0758  0.0807  -0.0401 202 HIS A CG    
418  N ND1   . HIS A 61  ? 0.3876 0.5341 0.3714 0.0784  0.0870  -0.0473 202 HIS A ND1   
419  C CD2   . HIS A 61  ? 0.2979 0.4502 0.2944 0.0805  0.0775  -0.0369 202 HIS A CD2   
420  C CE1   . HIS A 61  ? 0.3465 0.4972 0.3409 0.0848  0.0875  -0.0481 202 HIS A CE1   
421  N NE2   . HIS A 61  ? 0.3014 0.4558 0.3033 0.0859  0.0815  -0.0417 202 HIS A NE2   
422  N N     . GLU A 62  ? 0.2458 0.3702 0.2055 0.0619  0.0714  -0.0316 203 GLU A N     
423  C CA    . GLU A 62  ? 0.2502 0.3770 0.2026 0.0539  0.0693  -0.0280 203 GLU A CA    
424  C C     . GLU A 62  ? 0.2448 0.3585 0.1911 0.0543  0.0672  -0.0278 203 GLU A C     
425  O O     . GLU A 62  ? 0.2630 0.3787 0.2033 0.0476  0.0651  -0.0246 203 GLU A O     
426  C CB    . GLU A 62  ? 0.2547 0.3951 0.2152 0.0500  0.0652  -0.0199 203 GLU A CB    
427  C CG    . GLU A 62  ? 0.2347 0.3895 0.2013 0.0482  0.0667  -0.0188 203 GLU A CG    
428  C CD    . GLU A 62  ? 0.2957 0.4603 0.2731 0.0470  0.0623  -0.0114 203 GLU A CD    
429  O OE1   . GLU A 62  ? 0.3615 0.5236 0.3474 0.0530  0.0605  -0.0111 203 GLU A OE1   
430  O OE2   . GLU A 62  ? 0.3129 0.4871 0.2902 0.0395  0.0604  -0.0058 203 GLU A OE2   
431  N N     . ASN A 63  ? 0.2333 0.3338 0.1807 0.0614  0.0673  -0.0307 204 ASN A N     
432  C CA    . ASN A 63  ? 0.2604 0.3498 0.2045 0.0622  0.0643  -0.0288 204 ASN A CA    
433  C C     . ASN A 63  ? 0.2469 0.3279 0.1772 0.0571  0.0658  -0.0323 204 ASN A C     
434  O O     . ASN A 63  ? 0.2759 0.3491 0.1990 0.0577  0.0699  -0.0392 204 ASN A O     
435  C CB    . ASN A 63  ? 0.2180 0.2953 0.1663 0.0705  0.0637  -0.0303 204 ASN A CB    
436  C CG    . ASN A 63  ? 0.2748 0.3398 0.2186 0.0708  0.0611  -0.0286 204 ASN A CG    
437  O OD1   . ASN A 63  ? 0.3202 0.3893 0.2681 0.0691  0.0574  -0.0231 204 ASN A OD1   
438  N ND2   . ASN A 63  ? 0.2892 0.3389 0.2246 0.0728  0.0631  -0.0334 204 ASN A ND2   
439  N N     . SER A 64  ? 0.2770 0.3577 0.2053 0.0512  0.0616  -0.0274 205 SER A N     
440  C CA    . SER A 64  ? 0.2629 0.3351 0.1804 0.0438  0.0606  -0.0289 205 SER A CA    
441  C C     . SER A 64  ? 0.3024 0.3762 0.2246 0.0375  0.0541  -0.0211 205 SER A C     
442  O O     . SER A 64  ? 0.2528 0.3363 0.1854 0.0376  0.0511  -0.0152 205 SER A O     
443  C CB    . SER A 64  ? 0.3125 0.3927 0.2207 0.0375  0.0641  -0.0326 205 SER A CB    
444  O OG    . SER A 64  ? 0.3094 0.3850 0.2084 0.0285  0.0616  -0.0322 205 SER A OG    
445  N N     . ASN A 65  ? 0.2900 0.3543 0.2053 0.0322  0.0519  -0.0215 206 ASN A N     
446  C CA    . ASN A 65  ? 0.3080 0.3768 0.2271 0.0248  0.0461  -0.0145 206 ASN A CA    
447  C C     . ASN A 65  ? 0.3412 0.4235 0.2577 0.0171  0.0452  -0.0116 206 ASN A C     
448  O O     . ASN A 65  ? 0.2697 0.3562 0.1781 0.0159  0.0495  -0.0162 206 ASN A O     
449  C CB    . ASN A 65  ? 0.3420 0.3986 0.2548 0.0207  0.0440  -0.0157 206 ASN A CB    
450  C CG    . ASN A 65  ? 0.4143 0.4699 0.3367 0.0201  0.0389  -0.0099 206 ASN A CG    
451  O OD1   . ASN A 65  ? 0.4057 0.4716 0.3369 0.0171  0.0350  -0.0035 206 ASN A OD1   
452  N ND2   . ASN A 65  ? 0.4632 0.5060 0.3840 0.0227  0.0390  -0.0120 206 ASN A ND2   
453  N N     . ILE A 66  ? 0.3250 0.4144 0.2484 0.0116  0.0396  -0.0038 207 ILE A N     
454  C CA    . ILE A 66  ? 0.3788 0.4820 0.3016 0.0047  0.0379  0.0010  207 ILE A CA    
455  C C     . ILE A 66  ? 0.4157 0.5191 0.3266 -0.0044 0.0367  0.0003  207 ILE A C     
456  O O     . ILE A 66  ? 0.3898 0.4825 0.2916 -0.0048 0.0385  -0.0056 207 ILE A O     
457  C CB    . ILE A 66  ? 0.3983 0.5091 0.3350 0.0032  0.0323  0.0102  207 ILE A CB    
458  C CG1   . ILE A 66  ? 0.4064 0.5119 0.3471 -0.0003 0.0266  0.0143  207 ILE A CG1   
459  C CG2   . ILE A 66  ? 0.3692 0.4805 0.3170 0.0114  0.0336  0.0101  207 ILE A CG2   
460  C CD1   . ILE A 66  ? 0.4245 0.5360 0.3803 -0.0008 0.0214  0.0224  207 ILE A CD1   
461  N N     . HIS A 67  ? 0.4182 0.5341 0.3287 -0.0120 0.0337  0.0066  208 HIS A N     
462  C CA    . HIS A 67  ? 0.4955 0.6164 0.3948 -0.0220 0.0318  0.0076  208 HIS A CA    
463  C C     . HIS A 67  ? 0.4467 0.5746 0.3346 -0.0240 0.0379  0.0020  208 HIS A C     
464  O O     . HIS A 67  ? 0.4241 0.5448 0.3017 -0.0220 0.0435  -0.0076 208 HIS A O     
465  C CB    . HIS A 67  ? 0.5049 0.6145 0.3967 -0.0249 0.0305  0.0039  208 HIS A CB    
466  C CG    . HIS A 67  ? 0.6182 0.7331 0.4977 -0.0356 0.0285  0.0043  208 HIS A CG    
467  N ND1   . HIS A 67  ? 0.6357 0.7425 0.5012 -0.0387 0.0317  -0.0041 208 HIS A ND1   
468  C CD2   . HIS A 67  ? 0.6440 0.7716 0.5229 -0.0442 0.0235  0.0123  208 HIS A CD2   
469  C CE1   . HIS A 67  ? 0.6298 0.7447 0.4860 -0.0491 0.0287  -0.0018 208 HIS A CE1   
470  N NE2   . HIS A 67  ? 0.6738 0.8017 0.5379 -0.0526 0.0236  0.0086  208 HIS A NE2   
471  N N     . ARG A 68  ? 0.4825 0.6248 0.3725 -0.0282 0.0370  0.0079  209 ARG A N     
472  C CA    . ARG A 68  ? 0.4378 0.5868 0.3216 -0.0281 0.0431  0.0024  209 ARG A CA    
473  C C     . ARG A 68  ? 0.4768 0.6216 0.3467 -0.0337 0.0453  -0.0045 209 ARG A C     
474  O O     . ARG A 68  ? 0.5276 0.6709 0.3930 -0.0307 0.0516  -0.0126 209 ARG A O     
475  C CB    . ARG A 68  ? 0.4271 0.5900 0.3181 -0.0320 0.0405  0.0110  209 ARG A CB    
476  C CG    . ARG A 68  ? 0.5547 0.7248 0.4418 -0.0431 0.0346  0.0184  209 ARG A CG    
477  C CD    . ARG A 68  ? 0.6033 0.7863 0.4967 -0.0467 0.0329  0.0257  209 ARG A CD    
478  N NE    . ARG A 68  ? 0.5552 0.7415 0.4624 -0.0424 0.0305  0.0331  209 ARG A NE    
479  C CZ    . ARG A 68  ? 0.5257 0.7153 0.4401 -0.0361 0.0348  0.0311  209 ARG A CZ    
480  N NH1   . ARG A 68  ? 0.5088 0.6991 0.4188 -0.0327 0.0415  0.0221  209 ARG A NH1   
481  N NH2   . ARG A 68  ? 0.4486 0.6411 0.3758 -0.0330 0.0321  0.0382  209 ARG A NH2   
482  N N     . ALA A 69  ? 0.5078 0.6510 0.3715 -0.0416 0.0405  -0.0019 210 ALA A N     
483  C CA    . ALA A 69  ? 0.5557 0.6953 0.4063 -0.0474 0.0424  -0.0087 210 ALA A CA    
484  C C     . ALA A 69  ? 0.5375 0.6620 0.3809 -0.0415 0.0485  -0.0206 210 ALA A C     
485  O O     . ALA A 69  ? 0.5054 0.6262 0.3385 -0.0446 0.0518  -0.0281 210 ALA A O     
486  C CB    . ALA A 69  ? 0.5151 0.6574 0.3623 -0.0574 0.0349  -0.0023 210 ALA A CB    
487  N N     . ALA A 70  ? 0.4662 0.5819 0.3150 -0.0331 0.0501  -0.0226 211 ALA A N     
488  C CA    . ALA A 70  ? 0.4962 0.5959 0.3384 -0.0280 0.0549  -0.0328 211 ALA A CA    
489  C C     . ALA A 70  ? 0.4524 0.5486 0.2909 -0.0226 0.0625  -0.0422 211 ALA A C     
490  O O     . ALA A 70  ? 0.4493 0.5378 0.2775 -0.0249 0.0655  -0.0500 211 ALA A O     
491  C CB    . ALA A 70  ? 0.4497 0.5418 0.2998 -0.0199 0.0547  -0.0320 211 ALA A CB    
492  N N     . HIS A 71  ? 0.4023 0.5040 0.2498 -0.0152 0.0656  -0.0416 212 HIS A N     
493  C CA    . HIS A 71  ? 0.3862 0.4850 0.2331 -0.0085 0.0728  -0.0498 212 HIS A CA    
494  C C     . HIS A 71  ? 0.3645 0.4741 0.2239 -0.0029 0.0737  -0.0453 212 HIS A C     
495  O O     . HIS A 71  ? 0.3286 0.4463 0.1965 -0.0040 0.0688  -0.0366 212 HIS A O     
496  C CB    . HIS A 71  ? 0.3459 0.4266 0.1896 -0.0004 0.0772  -0.0588 212 HIS A CB    
497  C CG    . HIS A 71  ? 0.3785 0.4517 0.2289 0.0052  0.0747  -0.0560 212 HIS A CG    
498  N ND1   . HIS A 71  ? 0.3623 0.4397 0.2254 0.0134  0.0747  -0.0524 212 HIS A ND1   
499  C CD2   . HIS A 71  ? 0.4110 0.4736 0.2573 0.0034  0.0720  -0.0563 212 HIS A CD2   
500  C CE1   . HIS A 71  ? 0.3677 0.4374 0.2341 0.0172  0.0721  -0.0506 212 HIS A CE1   
501  N NE2   . HIS A 71  ? 0.4288 0.4886 0.2857 0.0110  0.0703  -0.0526 212 HIS A NE2   
502  N N     . GLU A 72  ? 0.3854 0.4952 0.2469 0.0032  0.0798  -0.0514 213 GLU A N     
503  C CA    . GLU A 72  ? 0.3318 0.4543 0.2045 0.0065  0.0808  -0.0477 213 GLU A CA    
504  C C     . GLU A 72  ? 0.3513 0.4740 0.2369 0.0134  0.0778  -0.0424 213 GLU A C     
505  O O     . GLU A 72  ? 0.3261 0.4610 0.2200 0.0113  0.0741  -0.0344 213 GLU A O     
506  C CB    . GLU A 72  ? 0.3955 0.5164 0.2684 0.0125  0.0882  -0.0561 213 GLU A CB    
507  C CG    . GLU A 72  ? 0.3915 0.5232 0.2777 0.0179  0.0896  -0.0534 213 GLU A CG    
508  C CD    . GLU A 72  ? 0.4563 0.6060 0.3445 0.0100  0.0872  -0.0466 213 GLU A CD    
509  O OE1   . GLU A 72  ? 0.4908 0.6450 0.3698 0.0004  0.0851  -0.0446 213 GLU A OE1   
510  O OE2   . GLU A 72  ? 0.4649 0.6242 0.3646 0.0130  0.0865  -0.0425 213 GLU A OE2   
511  N N     . LEU A 73  ? 0.2911 0.4003 0.1788 0.0216  0.0793  -0.0466 214 LEU A N     
512  C CA    . LEU A 73  ? 0.3325 0.4419 0.2324 0.0284  0.0762  -0.0417 214 LEU A CA    
513  C C     . LEU A 73  ? 0.3012 0.4146 0.2023 0.0233  0.0697  -0.0333 214 LEU A C     
514  O O     . LEU A 73  ? 0.2964 0.4173 0.2082 0.0253  0.0664  -0.0266 214 LEU A O     
515  C CB    . LEU A 73  ? 0.2886 0.3821 0.1901 0.0377  0.0783  -0.0473 214 LEU A CB    
516  C CG    . LEU A 73  ? 0.3138 0.4045 0.2197 0.0449  0.0840  -0.0538 214 LEU A CG    
517  C CD1   . LEU A 73  ? 0.2816 0.3577 0.1922 0.0542  0.0843  -0.0569 214 LEU A CD1   
518  C CD2   . LEU A 73  ? 0.3578 0.4642 0.2748 0.0462  0.0838  -0.0498 214 LEU A CD2   
519  N N     . ALA A 74  ? 0.2657 0.3739 0.1562 0.0163  0.0677  -0.0336 215 ALA A N     
520  C CA    . ALA A 74  ? 0.3088 0.4208 0.2020 0.0105  0.0609  -0.0249 215 ALA A CA    
521  C C     . ALA A 74  ? 0.3357 0.4649 0.2339 0.0045  0.0581  -0.0167 215 ALA A C     
522  O O     . ALA A 74  ? 0.2819 0.4139 0.1910 0.0042  0.0526  -0.0084 215 ALA A O     
523  C CB    . ALA A 74  ? 0.3268 0.4305 0.2087 0.0027  0.0586  -0.0263 215 ALA A CB    
524  N N     . ALA A 75  ? 0.2629 0.3993 0.1562 -0.0003 0.0606  -0.0186 216 ALA A N     
525  C CA    . ALA A 75  ? 0.3136 0.4650 0.2120 -0.0063 0.0577  -0.0105 216 ALA A CA    
526  C C     . ALA A 75  ? 0.2825 0.4407 0.1943 0.0005  0.0585  -0.0078 216 ALA A C     
527  O O     . ALA A 75  ? 0.2973 0.4651 0.2171 -0.0027 0.0543  0.0011  216 ALA A O     
528  C CB    . ALA A 75  ? 0.2890 0.4462 0.1787 -0.0127 0.0604  -0.0136 216 ALA A CB    
529  N N     . ARG A 76  ? 0.2645 0.4176 0.1797 0.0096  0.0635  -0.0149 217 ARG A N     
530  C CA    . ARG A 76  ? 0.2648 0.4242 0.1933 0.0160  0.0636  -0.0126 217 ARG A CA    
531  C C     . ARG A 76  ? 0.2588 0.4160 0.1960 0.0193  0.0591  -0.0067 217 ARG A C     
532  O O     . ARG A 76  ? 0.2756 0.4421 0.2227 0.0184  0.0563  0.0002  217 ARG A O     
533  C CB    . ARG A 76  ? 0.2690 0.4218 0.1997 0.0251  0.0690  -0.0211 217 ARG A CB    
534  C CG    . ARG A 76  ? 0.2954 0.4525 0.2208 0.0232  0.0744  -0.0269 217 ARG A CG    
535  C CD    . ARG A 76  ? 0.2899 0.4397 0.2191 0.0329  0.0794  -0.0347 217 ARG A CD    
536  N NE    . ARG A 76  ? 0.3439 0.4939 0.2654 0.0314  0.0853  -0.0419 217 ARG A NE    
537  C CZ    . ARG A 76  ? 0.3871 0.5319 0.3111 0.0386  0.0907  -0.0492 217 ARG A CZ    
538  N NH1   . ARG A 76  ? 0.3610 0.5003 0.2950 0.0476  0.0903  -0.0498 217 ARG A NH1   
539  N NH2   . ARG A 76  ? 0.3457 0.4908 0.2620 0.0366  0.0963  -0.0557 217 ARG A NH2   
540  N N     . ALA A 77  ? 0.2217 0.3660 0.1555 0.0233  0.0587  -0.0096 218 ALA A N     
541  C CA    . ALA A 77  ? 0.2672 0.4042 0.2106 0.0256  0.0531  -0.0045 218 ALA A CA    
542  C C     . ALA A 77  ? 0.2840 0.4256 0.2312 0.0172  0.0467  0.0046  218 ALA A C     
543  O O     . ALA A 77  ? 0.2421 0.3855 0.2009 0.0182  0.0427  0.0102  218 ALA A O     
544  C CB    . ALA A 77  ? 0.2629 0.3828 0.2012 0.0294  0.0530  -0.0090 218 ALA A CB    
545  N N     . THR A 78  ? 0.2630 0.4065 0.2008 0.0088  0.0454  0.0060  219 THR A N     
546  C CA    . THR A 78  ? 0.3306 0.4787 0.2723 0.0008  0.0389  0.0153  219 THR A CA    
547  C C     . THR A 78  ? 0.2833 0.4450 0.2334 -0.0017 0.0377  0.0219  219 THR A C     
548  O O     . THR A 78  ? 0.3019 0.4647 0.2630 -0.0032 0.0324  0.0293  219 THR A O     
549  C CB    . THR A 78  ? 0.3634 0.5129 0.2922 -0.0082 0.0379  0.0155  219 THR A CB    
550  O OG1   . THR A 78  ? 0.3193 0.4558 0.2405 -0.0068 0.0386  0.0097  219 THR A OG1   
551  C CG2   . THR A 78  ? 0.3358 0.4913 0.2697 -0.0163 0.0304  0.0264  219 THR A CG2   
552  N N     . ASP A 79  ? 0.2681 0.4401 0.2132 -0.0026 0.0429  0.0190  220 ASP A N     
553  C CA    . ASP A 79  ? 0.2776 0.4630 0.2303 -0.0052 0.0425  0.0249  220 ASP A CA    
554  C C     . ASP A 79  ? 0.2564 0.4399 0.2239 0.0016  0.0409  0.0265  220 ASP A C     
555  O O     . ASP A 79  ? 0.2069 0.3949 0.1844 -0.0015 0.0366  0.0342  220 ASP A O     
556  C CB    . ASP A 79  ? 0.2488 0.4431 0.1954 -0.0053 0.0489  0.0191  220 ASP A CB    
557  C CG    . ASP A 79  ? 0.4238 0.6220 0.3591 -0.0150 0.0483  0.0198  220 ASP A CG    
558  O OD1   . ASP A 79  ? 0.4370 0.6354 0.3690 -0.0224 0.0431  0.0266  220 ASP A OD1   
559  O OD2   . ASP A 79  ? 0.4609 0.6618 0.3910 -0.0148 0.0531  0.0133  220 ASP A OD2   
560  N N     . ALA A 80  ? 0.2177 0.3943 0.1866 0.0108  0.0444  0.0192  221 ALA A N     
561  C CA    . ALA A 80  ? 0.2314 0.4076 0.2132 0.0171  0.0433  0.0201  221 ALA A CA    
562  C C     . ALA A 80  ? 0.2167 0.3845 0.2065 0.0163  0.0369  0.0252  221 ALA A C     
563  O O     . ALA A 80  ? 0.2033 0.3746 0.2046 0.0160  0.0340  0.0299  221 ALA A O     
564  C CB    . ALA A 80  ? 0.1963 0.3672 0.1771 0.0270  0.0480  0.0118  221 ALA A CB    
565  N N     . TYR A 81  ? 0.2321 0.3889 0.2163 0.0155  0.0350  0.0241  222 TYR A N     
566  C CA    . TYR A 81  ? 0.2274 0.3767 0.2193 0.0148  0.0295  0.0282  222 TYR A CA    
567  C C     . TYR A 81  ? 0.2148 0.3706 0.2136 0.0073  0.0243  0.0373  222 TYR A C     
568  O O     . TYR A 81  ? 0.1891 0.3441 0.2002 0.0079  0.0206  0.0413  222 TYR A O     
569  C CB    . TYR A 81  ? 0.2071 0.3451 0.1907 0.0145  0.0289  0.0251  222 TYR A CB    
570  C CG    . TYR A 81  ? 0.2067 0.3355 0.1975 0.0165  0.0251  0.0262  222 TYR A CG    
571  C CD1   . TYR A 81  ? 0.1976 0.3238 0.1974 0.0226  0.0252  0.0248  222 TYR A CD1   
572  C CD2   . TYR A 81  ? 0.2355 0.3591 0.2238 0.0120  0.0216  0.0283  222 TYR A CD2   
573  C CE1   . TYR A 81  ? 0.1918 0.3103 0.1975 0.0239  0.0223  0.0251  222 TYR A CE1   
574  C CE2   . TYR A 81  ? 0.2385 0.3549 0.2337 0.0136  0.0187  0.0288  222 TYR A CE2   
575  C CZ    . TYR A 81  ? 0.2079 0.3216 0.2114 0.0195  0.0193  0.0270  222 TYR A CZ    
576  O OH    . TYR A 81  ? 0.2125 0.3199 0.2224 0.0205  0.0169  0.0270  222 TYR A OH    
577  N N     . GLU A 82  ? 0.2116 0.3737 0.2026 0.0001  0.0238  0.0406  223 GLU A N     
578  C CA    . GLU A 82  ? 0.2292 0.3976 0.2263 -0.0074 0.0184  0.0504  223 GLU A CA    
579  C C     . GLU A 82  ? 0.2165 0.3933 0.2236 -0.0074 0.0186  0.0540  223 GLU A C     
580  O O     . GLU A 82  ? 0.1927 0.3695 0.2114 -0.0097 0.0137  0.0609  223 GLU A O     
581  C CB    . GLU A 82  ? 0.2395 0.4144 0.2244 -0.0156 0.0182  0.0532  223 GLU A CB    
582  C CG    . GLU A 82  ? 0.3723 0.5400 0.3489 -0.0181 0.0160  0.0519  223 GLU A CG    
583  C CD    . GLU A 82  ? 0.4690 0.6440 0.4319 -0.0267 0.0161  0.0538  223 GLU A CD    
584  O OE1   . GLU A 82  ? 0.4450 0.6156 0.4005 -0.0301 0.0139  0.0532  223 GLU A OE1   
585  O OE2   . GLU A 82  ? 0.4159 0.6018 0.3750 -0.0305 0.0185  0.0556  223 GLU A OE2   
586  N N     . ASP A 83  ? 0.2195 0.4035 0.2229 -0.0048 0.0243  0.0494  224 ASP A N     
587  C CA    . ASP A 83  ? 0.1832 0.3759 0.1961 -0.0048 0.0249  0.0520  224 ASP A CA    
588  C C     . ASP A 83  ? 0.1928 0.3792 0.2188 0.0009  0.0227  0.0513  224 ASP A C     
589  O O     . ASP A 83  ? 0.1696 0.3596 0.2066 -0.0015 0.0200  0.0564  224 ASP A O     
590  C CB    . ASP A 83  ? 0.2275 0.4294 0.2342 -0.0020 0.0318  0.0458  224 ASP A CB    
591  C CG    . ASP A 83  ? 0.4106 0.6237 0.4075 -0.0100 0.0339  0.0485  224 ASP A CG    
592  O OD1   . ASP A 83  ? 0.3992 0.6106 0.3893 -0.0166 0.0307  0.0529  224 ASP A OD1   
593  O OD2   . ASP A 83  ? 0.4131 0.6374 0.4085 -0.0096 0.0390  0.0456  224 ASP A OD2   
594  N N     . ALA A 84  ? 0.1697 0.3466 0.1945 0.0079  0.0240  0.0449  225 ALA A N     
595  C CA    . ALA A 84  ? 0.1698 0.3410 0.2057 0.0128  0.0221  0.0436  225 ALA A CA    
596  C C     . ALA A 84  ? 0.1784 0.3441 0.2234 0.0091  0.0161  0.0495  225 ALA A C     
597  O O     . ALA A 84  ? 0.1467 0.3127 0.2037 0.0092  0.0138  0.0518  225 ALA A O     
598  C CB    . ALA A 84  ? 0.1179 0.2802 0.1487 0.0203  0.0247  0.0360  225 ALA A CB    
599  N N     . ARG A 85  ? 0.1625 0.3233 0.2025 0.0057  0.0136  0.0520  226 ARG A N     
600  C CA    . ARG A 85  ? 0.1672 0.3240 0.2171 0.0023  0.0077  0.0581  226 ARG A CA    
601  C C     . ARG A 85  ? 0.1895 0.3535 0.2476 -0.0035 0.0046  0.0663  226 ARG A C     
602  O O     . ARG A 85  ? 0.1420 0.3031 0.2133 -0.0040 0.0009  0.0700  226 ARG A O     
603  C CB    . ARG A 85  ? 0.1354 0.2880 0.1783 -0.0009 0.0053  0.0600  226 ARG A CB    
604  C CG    . ARG A 85  ? 0.1590 0.3061 0.2137 -0.0020 -0.0004 0.0644  226 ARG A CG    
605  C CD    . ARG A 85  ? 0.1775 0.3225 0.2264 -0.0059 -0.0035 0.0672  226 ARG A CD    
606  N NE    . ARG A 85  ? 0.1891 0.3295 0.2252 -0.0034 0.0003  0.0598  226 ARG A NE    
607  C CZ    . ARG A 85  ? 0.2230 0.3552 0.2602 0.0009  0.0010  0.0546  226 ARG A CZ    
608  N NH1   . ARG A 85  ? 0.1633 0.2918 0.2138 0.0032  -0.0015 0.0553  226 ARG A NH1   
609  N NH2   . ARG A 85  ? 0.1720 0.2997 0.1967 0.0025  0.0045  0.0484  226 ARG A NH2   
610  N N     . GLU A 86  ? 0.1506 0.3237 0.2010 -0.0082 0.0063  0.0692  227 GLU A N     
611  C CA    . GLU A 86  ? 0.2082 0.3883 0.2651 -0.0146 0.0035  0.0777  227 GLU A CA    
612  C C     . GLU A 86  ? 0.1731 0.3561 0.2405 -0.0122 0.0049  0.0762  227 GLU A C     
613  O O     . GLU A 86  ? 0.1643 0.3474 0.2428 -0.0159 0.0010  0.0826  227 GLU A O     
614  C CB    . GLU A 86  ? 0.1819 0.3723 0.2263 -0.0207 0.0057  0.0804  227 GLU A CB    
615  C CG    . GLU A 86  ? 0.2300 0.4302 0.2789 -0.0274 0.0045  0.0881  227 GLU A CG    
616  C CD    . GLU A 86  ? 0.2506 0.4474 0.3095 -0.0331 -0.0029 0.0989  227 GLU A CD    
617  O OE1   . GLU A 86  ? 0.2630 0.4525 0.3230 -0.0328 -0.0071 0.1009  227 GLU A OE1   
618  O OE2   . GLU A 86  ? 0.2865 0.4881 0.3528 -0.0377 -0.0046 0.1053  227 GLU A OE2   
619  N N     . ALA A 87  ? 0.1328 0.3177 0.1971 -0.0062 0.0100  0.0681  228 ALA A N     
620  C CA    . ALA A 87  ? 0.1566 0.3445 0.2308 -0.0037 0.0110  0.0661  228 ALA A CA    
621  C C     . ALA A 87  ? 0.1552 0.3338 0.2420 -0.0018 0.0071  0.0663  228 ALA A C     
622  O O     . ALA A 87  ? 0.1267 0.3067 0.2246 -0.0042 0.0051  0.0692  228 ALA A O     
623  C CB    . ALA A 87  ? 0.1284 0.3194 0.1971 0.0033  0.0166  0.0573  228 ALA A CB    
624  N N     . VAL A 88  ? 0.1442 0.3132 0.2295 0.0022  0.0062  0.0628  229 VAL A N     
625  C CA    . VAL A 88  ? 0.1451 0.3058 0.2424 0.0038  0.0029  0.0624  229 VAL A CA    
626  C C     . VAL A 88  ? 0.1521 0.3112 0.2592 -0.0022 -0.0024 0.0712  229 VAL A C     
627  O O     . VAL A 88  ? 0.1236 0.2803 0.2438 -0.0030 -0.0047 0.0727  229 VAL A O     
628  C CB    . VAL A 88  ? 0.1520 0.3041 0.2451 0.0085  0.0033  0.0573  229 VAL A CB    
629  C CG1   . VAL A 88  ? 0.1172 0.2618 0.2233 0.0096  0.0002  0.0569  229 VAL A CG1   
630  C CG2   . VAL A 88  ? 0.1330 0.2855 0.2178 0.0146  0.0081  0.0493  229 VAL A CG2   
631  N N     . ARG A 89  ? 0.1054 0.2657 0.2066 -0.0065 -0.0047 0.0772  230 ARG A N     
632  C CA    . ARG A 89  ? 0.1683 0.3270 0.2787 -0.0121 -0.0105 0.0868  230 ARG A CA    
633  C C     . ARG A 89  ? 0.1488 0.3122 0.2673 -0.0165 -0.0115 0.0919  230 ARG A C     
634  O O     . ARG A 89  ? 0.1304 0.2888 0.2629 -0.0180 -0.0154 0.0959  230 ARG A O     
635  C CB    . ARG A 89  ? 0.1483 0.3104 0.2487 -0.0172 -0.0127 0.0931  230 ARG A CB    
636  C CG    . ARG A 89  ? 0.1545 0.3151 0.2645 -0.0228 -0.0196 0.1042  230 ARG A CG    
637  C CD    . ARG A 89  ? 0.1633 0.3320 0.2627 -0.0305 -0.0215 0.1125  230 ARG A CD    
638  N NE    . ARG A 89  ? 0.1873 0.3652 0.2808 -0.0343 -0.0180 0.1135  230 ARG A NE    
639  C CZ    . ARG A 89  ? 0.2559 0.4359 0.3587 -0.0378 -0.0194 0.1189  230 ARG A CZ    
640  N NH1   . ARG A 89  ? 0.2462 0.4186 0.3649 -0.0380 -0.0245 0.1238  230 ARG A NH1   
641  N NH2   . ARG A 89  ? 0.2661 0.4560 0.3625 -0.0414 -0.0157 0.1191  230 ARG A NH2   
642  N N     . ARG A 90  ? 0.1458 0.3189 0.2557 -0.0188 -0.0079 0.0916  231 ARG A N     
643  C CA    . ARG A 90  ? 0.1466 0.3258 0.2628 -0.0240 -0.0084 0.0966  231 ARG A CA    
644  C C     . ARG A 90  ? 0.1969 0.3726 0.3252 -0.0206 -0.0077 0.0916  231 ARG A C     
645  O O     . ARG A 90  ? 0.1534 0.3265 0.2937 -0.0245 -0.0110 0.0965  231 ARG A O     
646  C CB    . ARG A 90  ? 0.1966 0.3884 0.3006 -0.0264 -0.0035 0.0957  231 ARG A CB    
647  C CG    . ARG A 90  ? 0.2271 0.4274 0.3368 -0.0312 -0.0026 0.0988  231 ARG A CG    
648  C CD    . ARG A 90  ? 0.2487 0.4628 0.3468 -0.0322 0.0033  0.0958  231 ARG A CD    
649  N NE    . ARG A 90  ? 0.2277 0.4436 0.3232 -0.0240 0.0084  0.0851  231 ARG A NE    
650  C CZ    . ARG A 90  ? 0.2516 0.4691 0.3355 -0.0192 0.0125  0.0789  231 ARG A CZ    
651  N NH1   . ARG A 90  ? 0.1863 0.4043 0.2592 -0.0220 0.0126  0.0813  231 ARG A NH1   
652  N NH2   . ARG A 90  ? 0.1998 0.4180 0.2830 -0.0115 0.0164  0.0701  231 ARG A NH2   
653  N N     . PHE A 91  ? 0.1725 0.3476 0.2976 -0.0137 -0.0037 0.0818  232 PHE A N     
654  C CA    . PHE A 91  ? 0.1454 0.3193 0.2800 -0.0111 -0.0028 0.0765  232 PHE A CA    
655  C C     . PHE A 91  ? 0.1329 0.2958 0.2811 -0.0107 -0.0068 0.0769  232 PHE A C     
656  O O     . PHE A 91  ? 0.1385 0.3002 0.2976 -0.0122 -0.0077 0.0762  232 PHE A O     
657  C CB    . PHE A 91  ? 0.1504 0.3259 0.2781 -0.0038 0.0017  0.0667  232 PHE A CB    
658  C CG    . PHE A 91  ? 0.1544 0.3314 0.2901 -0.0017 0.0028  0.0612  232 PHE A CG    
659  C CD1   . PHE A 91  ? 0.2054 0.3907 0.3438 -0.0055 0.0037  0.0624  232 PHE A CD1   
660  C CD2   . PHE A 91  ? 0.1589 0.3277 0.2977 0.0032  0.0028  0.0544  232 PHE A CD2   
661  C CE1   . PHE A 91  ? 0.1752 0.3597 0.3184 -0.0041 0.0043  0.0564  232 PHE A CE1   
662  C CE2   . PHE A 91  ? 0.1943 0.3626 0.3373 0.0044  0.0035  0.0484  232 PHE A CE2   
663  C CZ    . PHE A 91  ? 0.1646 0.3410 0.3101 0.0007  0.0041  0.0495  232 PHE A CZ    
664  N N     . ILE A 92  ? 0.1165 0.2716 0.2650 -0.0086 -0.0090 0.0775  233 ILE A N     
665  C CA    . ILE A 92  ? 0.1136 0.2590 0.2764 -0.0076 -0.0124 0.0772  233 ILE A CA    
666  C C     . ILE A 92  ? 0.1473 0.2890 0.3188 -0.0128 -0.0179 0.0876  233 ILE A C     
667  O O     . ILE A 92  ? 0.1821 0.3154 0.3671 -0.0119 -0.0210 0.0882  233 ILE A O     
668  C CB    . ILE A 92  ? 0.1438 0.2827 0.3051 -0.0015 -0.0114 0.0705  233 ILE A CB    
669  C CG1   . ILE A 92  ? 0.1342 0.2723 0.2876 -0.0018 -0.0130 0.0746  233 ILE A CG1   
670  C CG2   . ILE A 92  ? 0.1322 0.2740 0.2851 0.0035  -0.0065 0.0611  233 ILE A CG2   
671  C CD1   . ILE A 92  ? 0.1168 0.2484 0.2705 0.0033  -0.0124 0.0685  233 ILE A CD1   
672  N N     . GLY A 93  ? 0.1601 0.3081 0.3247 -0.0183 -0.0192 0.0960  234 GLY A N     
673  C CA    . GLY A 93  ? 0.1842 0.3292 0.3568 -0.0239 -0.0251 0.1072  234 GLY A CA    
674  C C     . GLY A 93  ? 0.1858 0.3251 0.3608 -0.0221 -0.0290 0.1104  234 GLY A C     
675  O O     . GLY A 93  ? 0.2065 0.3393 0.3952 -0.0236 -0.0342 0.1169  234 GLY A O     
676  N N     . ALA A 94  ? 0.1591 0.3004 0.3220 -0.0189 -0.0267 0.1060  235 ALA A N     
677  C CA    . ALA A 94  ? 0.1619 0.2999 0.3258 -0.0184 -0.0306 0.1097  235 ALA A CA    
678  C C     . ALA A 94  ? 0.2171 0.3608 0.3745 -0.0255 -0.0346 0.1212  235 ALA A C     
679  O O     . ALA A 94  ? 0.1975 0.3493 0.3430 -0.0297 -0.0323 0.1232  235 ALA A O     
680  C CB    . ALA A 94  ? 0.1466 0.2845 0.2993 -0.0134 -0.0267 0.1010  235 ALA A CB    
681  N N     . ALA A 95  ? 0.1901 0.3303 0.3557 -0.0269 -0.0408 0.1289  236 ALA A N     
682  C CA    . ALA A 95  ? 0.1966 0.3426 0.3563 -0.0341 -0.0456 0.1408  236 ALA A CA    
683  C C     . ALA A 95  ? 0.2070 0.3604 0.3466 -0.0357 -0.0427 0.1382  236 ALA A C     
684  O O     . ALA A 95  ? 0.2316 0.3931 0.3596 -0.0422 -0.0429 0.1441  236 ALA A O     
685  C CB    . ALA A 95  ? 0.2208 0.3616 0.3949 -0.0344 -0.0533 0.1495  236 ALA A CB    
686  N N     . LYS A 96  ? 0.1895 0.3403 0.3245 -0.0302 -0.0398 0.1292  237 LYS A N     
687  C CA    . LYS A 96  ? 0.1992 0.3554 0.3163 -0.0320 -0.0378 0.1269  237 LYS A CA    
688  C C     . LYS A 96  ? 0.1964 0.3503 0.3049 -0.0257 -0.0308 0.1138  237 LYS A C     
689  O O     . LYS A 96  ? 0.1690 0.3162 0.2866 -0.0196 -0.0293 0.1072  237 LYS A O     
690  C CB    . LYS A 96  ? 0.2560 0.4114 0.3751 -0.0335 -0.0436 0.1323  237 LYS A CB    
691  C CG    . LYS A 96  ? 0.2833 0.4403 0.4125 -0.0391 -0.0518 0.1464  237 LYS A CG    
692  C CD    . LYS A 96  ? 0.2998 0.4561 0.4293 -0.0404 -0.0565 0.1500  237 LYS A CD    
693  C CE    . LYS A 96  ? 0.4303 0.5863 0.5651 -0.0473 -0.0624 0.1621  237 LYS A CE    
694  N NZ    . LYS A 96  ? 0.4015 0.5572 0.5348 -0.0492 -0.0657 0.1639  237 LYS A NZ    
695  N N     . ALA A 97  ? 0.1828 0.3424 0.2737 -0.0274 -0.0265 0.1101  238 ALA A N     
696  C CA    . ALA A 97  ? 0.1910 0.3477 0.2729 -0.0215 -0.0202 0.0984  238 ALA A CA    
697  C C     . ALA A 97  ? 0.2317 0.3819 0.3146 -0.0183 -0.0215 0.0948  238 ALA A C     
698  O O     . ALA A 97  ? 0.1870 0.3320 0.2685 -0.0124 -0.0175 0.0858  238 ALA A O     
699  C CB    . ALA A 97  ? 0.2287 0.3922 0.2924 -0.0240 -0.0155 0.0953  238 ALA A CB    
700  N N     . GLU A 98  ? 0.1730 0.3242 0.2584 -0.0225 -0.0273 0.1020  239 GLU A N     
701  C CA    . GLU A 98  ? 0.2196 0.3661 0.3080 -0.0201 -0.0291 0.0994  239 GLU A CA    
702  C C     . GLU A 98  ? 0.1909 0.3306 0.2965 -0.0143 -0.0297 0.0964  239 GLU A C     
703  O O     . GLU A 98  ? 0.1776 0.3137 0.2861 -0.0116 -0.0300 0.0926  239 GLU A O     
704  C CB    . GLU A 98  ? 0.1939 0.3447 0.2828 -0.0263 -0.0359 0.1089  239 GLU A CB    
705  C CG    . GLU A 98  ? 0.3115 0.4689 0.3807 -0.0324 -0.0348 0.1099  239 GLU A CG    
706  C CD    . GLU A 98  ? 0.4405 0.6055 0.5050 -0.0384 -0.0357 0.1174  239 GLU A CD    
707  O OE1   . GLU A 98  ? 0.3264 0.4910 0.4012 -0.0374 -0.0360 0.1204  239 GLU A OE1   
708  O OE2   . GLU A 98  ? 0.5572 0.7290 0.6074 -0.0449 -0.0362 0.1201  239 GLU A OE2   
709  N N     . GLU A 99  ? 0.1571 0.2956 0.2740 -0.0127 -0.0297 0.0975  240 GLU A N     
710  C CA    . GLU A 99  ? 0.1645 0.2967 0.2971 -0.0073 -0.0294 0.0932  240 GLU A CA    
711  C C     . GLU A 99  ? 0.1295 0.2589 0.2571 -0.0021 -0.0228 0.0825  240 GLU A C     
712  O O     . GLU A 99  ? 0.1307 0.2555 0.2693 0.0020  -0.0217 0.0777  240 GLU A O     
713  C CB    . GLU A 99  ? 0.1677 0.2991 0.3163 -0.0089 -0.0334 0.1003  240 GLU A CB    
714  C CG    . GLU A 99  ? 0.1985 0.3309 0.3522 -0.0139 -0.0403 0.1117  240 GLU A CG    
715  C CD    . GLU A 99  ? 0.2732 0.4007 0.4401 -0.0159 -0.0436 0.1185  240 GLU A CD    
716  O OE1   . GLU A 99  ? 0.2130 0.3447 0.3799 -0.0182 -0.0429 0.1211  240 GLU A OE1   
717  O OE2   . GLU A 99  ? 0.2498 0.3704 0.4272 -0.0160 -0.0474 0.1222  240 GLU A OE2   
718  N N     . ILE A 100 ? 0.1355 0.2677 0.2469 -0.0023 -0.0185 0.0787  241 ILE A N     
719  C CA    . ILE A 100 ? 0.1296 0.2599 0.2354 0.0027  -0.0126 0.0696  241 ILE A CA    
720  C C     . ILE A 100 ? 0.1409 0.2675 0.2359 0.0053  -0.0099 0.0632  241 ILE A C     
721  O O     . ILE A 100 ? 0.1567 0.2852 0.2387 0.0027  -0.0092 0.0639  241 ILE A O     
722  C CB    . ILE A 100 ? 0.1460 0.2823 0.2425 0.0013  -0.0095 0.0697  241 ILE A CB    
723  C CG1   . ILE A 100 ? 0.1642 0.3046 0.2708 -0.0025 -0.0123 0.0768  241 ILE A CG1   
724  C CG2   . ILE A 100 ? 0.1121 0.2471 0.2033 0.0070  -0.0039 0.0606  241 ILE A CG2   
725  C CD1   . ILE A 100 ? 0.1517 0.2877 0.2745 0.0001  -0.0134 0.0751  241 ILE A CD1   
726  N N     . ILE A 101 ? 0.1320 0.2533 0.2315 0.0099  -0.0080 0.0568  242 ILE A N     
727  C CA    . ILE A 101 ? 0.1093 0.2261 0.1991 0.0122  -0.0053 0.0508  242 ILE A CA    
728  C C     . ILE A 101 ? 0.1633 0.2781 0.2469 0.0170  -0.0003 0.0436  242 ILE A C     
729  O O     . ILE A 101 ? 0.1142 0.2285 0.2065 0.0197  0.0005  0.0410  242 ILE A O     
730  C CB    . ILE A 101 ? 0.1314 0.2445 0.2312 0.0132  -0.0071 0.0494  242 ILE A CB    
731  C CG1   . ILE A 101 ? 0.1327 0.2486 0.2435 0.0093  -0.0129 0.0573  242 ILE A CG1   
732  C CG2   . ILE A 101 ? 0.1214 0.2302 0.2100 0.0142  -0.0046 0.0442  242 ILE A CG2   
733  C CD1   . ILE A 101 ? 0.1779 0.2971 0.2777 0.0044  -0.0152 0.0624  242 ILE A CD1   
734  N N     . PHE A 102 ? 0.1179 0.2314 0.1866 0.0180  0.0029  0.0404  243 PHE A N     
735  C CA    . PHE A 102 ? 0.1650 0.2760 0.2274 0.0230  0.0073  0.0341  243 PHE A CA    
736  C C     . PHE A 102 ? 0.1541 0.2580 0.2145 0.0255  0.0085  0.0292  243 PHE A C     
737  O O     . PHE A 102 ? 0.1396 0.2401 0.1960 0.0232  0.0075  0.0295  243 PHE A O     
738  C CB    . PHE A 102 ? 0.1522 0.2645 0.2006 0.0234  0.0104  0.0327  243 PHE A CB    
739  C CG    . PHE A 102 ? 0.1723 0.2928 0.2220 0.0224  0.0109  0.0354  243 PHE A CG    
740  C CD1   . PHE A 102 ? 0.1366 0.2609 0.1955 0.0245  0.0111  0.0352  243 PHE A CD1   
741  C CD2   . PHE A 102 ? 0.1542 0.2793 0.1955 0.0187  0.0114  0.0380  243 PHE A CD2   
742  C CE1   . PHE A 102 ? 0.1558 0.2885 0.2160 0.0230  0.0118  0.0378  243 PHE A CE1   
743  C CE2   . PHE A 102 ? 0.1775 0.3112 0.2198 0.0172  0.0124  0.0406  243 PHE A CE2   
744  C CZ    . PHE A 102 ? 0.1616 0.2991 0.2136 0.0194  0.0125  0.0406  243 PHE A CZ    
745  N N     . LEU A 103 ? 0.1184 0.2207 0.1816 0.0295  0.0104  0.0250  244 LEU A N     
746  C CA    . LEU A 103 ? 0.1380 0.2341 0.1979 0.0317  0.0121  0.0203  244 LEU A CA    
747  C C     . LEU A 103 ? 0.1547 0.2509 0.2126 0.0362  0.0147  0.0164  244 LEU A C     
748  O O     . LEU A 103 ? 0.1239 0.2246 0.1807 0.0378  0.0155  0.0171  244 LEU A O     
749  C CB    . LEU A 103 ? 0.1499 0.2454 0.2213 0.0298  0.0100  0.0204  244 LEU A CB    
750  C CG    . LEU A 103 ? 0.1822 0.2825 0.2686 0.0278  0.0067  0.0243  244 LEU A CG    
751  C CD1   . LEU A 103 ? 0.1558 0.2586 0.2489 0.0302  0.0078  0.0219  244 LEU A CD1   
752  C CD2   . LEU A 103 ? 0.1405 0.2400 0.2378 0.0260  0.0044  0.0250  244 LEU A CD2   
753  N N     . ARG A 104 ? 0.1166 0.2089 0.1741 0.0381  0.0159  0.0125  245 ARG A N     
754  C CA    . ARG A 104 ? 0.1477 0.2402 0.2010 0.0423  0.0179  0.0095  245 ARG A CA    
755  C C     . ARG A 104 ? 0.1406 0.2398 0.2047 0.0427  0.0171  0.0089  245 ARG A C     
756  O O     . ARG A 104 ? 0.1660 0.2686 0.2280 0.0455  0.0180  0.0081  245 ARG A O     
757  C CB    . ARG A 104 ? 0.1569 0.2429 0.2037 0.0436  0.0194  0.0061  245 ARG A CB    
758  C CG    . ARG A 104 ? 0.2296 0.3170 0.2744 0.0473  0.0206  0.0034  245 ARG A CG    
759  C CD    . ARG A 104 ? 0.1895 0.2698 0.2241 0.0489  0.0222  0.0013  245 ARG A CD    
760  N NE    . ARG A 104 ? 0.2336 0.3106 0.2702 0.0454  0.0223  -0.0001 245 ARG A NE    
761  C CZ    . ARG A 104 ? 0.2819 0.3536 0.3144 0.0428  0.0224  0.0007  245 ARG A CZ    
762  N NH1   . ARG A 104 ? 0.2420 0.3092 0.2659 0.0434  0.0227  0.0024  245 ARG A NH1   
763  N NH2   . ARG A 104 ? 0.2035 0.2749 0.2408 0.0394  0.0223  -0.0006 245 ARG A NH2   
764  N N     . GLY A 105 ? 0.1058 0.2066 0.1817 0.0401  0.0154  0.0091  246 GLY A N     
765  C CA    . GLY A 105 ? 0.1250 0.2295 0.2103 0.0394  0.0145  0.0077  246 GLY A CA    
766  C C     . GLY A 105 ? 0.1361 0.2401 0.2345 0.0367  0.0129  0.0070  246 GLY A C     
767  O O     . GLY A 105 ? 0.1149 0.2176 0.2168 0.0356  0.0122  0.0089  246 GLY A O     
768  N N     . THR A 106 ? 0.1082 0.2134 0.2143 0.0356  0.0124  0.0040  247 THR A N     
769  C CA    . THR A 106 ? 0.1154 0.2202 0.2334 0.0336  0.0109  0.0021  247 THR A CA    
770  C C     . THR A 106 ? 0.0878 0.1896 0.2057 0.0339  0.0122  -0.0009 247 THR A C     
771  O O     . THR A 106 ? 0.1023 0.2017 0.2271 0.0322  0.0108  0.0003  247 THR A O     
772  C CB    . THR A 106 ? 0.1155 0.2232 0.2376 0.0332  0.0112  -0.0014 247 THR A CB    
773  O OG1   . THR A 106 ? 0.1512 0.2624 0.2751 0.0323  0.0099  0.0014  247 THR A OG1   
774  C CG2   . THR A 106 ? 0.1278 0.2318 0.2599 0.0311  0.0105  -0.0030 247 THR A CG2   
775  N N     . THR A 107 ? 0.1060 0.2076 0.2167 0.0356  0.0149  -0.0049 248 THR A N     
776  C CA    . THR A 107 ? 0.0856 0.1847 0.1956 0.0352  0.0170  -0.0071 248 THR A CA    
777  C C     . THR A 107 ? 0.0983 0.1963 0.2093 0.0348  0.0163  -0.0046 248 THR A C     
778  O O     . THR A 107 ? 0.0872 0.1839 0.2042 0.0330  0.0158  -0.0055 248 THR A O     
779  C CB    . THR A 107 ? 0.1208 0.2187 0.2203 0.0362  0.0197  -0.0111 248 THR A CB    
780  O OG1   . THR A 107 ? 0.1186 0.2181 0.2184 0.0359  0.0199  -0.0134 248 THR A OG1   
781  C CG2   . THR A 107 ? 0.0908 0.1875 0.1895 0.0350  0.0218  -0.0151 248 THR A CG2   
782  N N     . GLU A 108 ? 0.0731 0.1691 0.1729 0.0354  0.0159  -0.0005 249 GLU A N     
783  C CA    . GLU A 108 ? 0.1141 0.2075 0.2111 0.0337  0.0147  0.0028  249 GLU A CA    
784  C C     . GLU A 108 ? 0.0654 0.1615 0.1757 0.0317  0.0114  0.0070  249 GLU A C     
785  O O     . GLU A 108 ? 0.1075 0.2033 0.2228 0.0300  0.0102  0.0082  249 GLU A O     
786  C CB    . GLU A 108 ? 0.1246 0.2149 0.2067 0.0344  0.0150  0.0056  249 GLU A CB    
787  C CG    . GLU A 108 ? 0.1418 0.2299 0.2207 0.0316  0.0136  0.0088  249 GLU A CG    
788  C CD    . GLU A 108 ? 0.2384 0.3220 0.3013 0.0320  0.0147  0.0098  249 GLU A CD    
789  O OE1   . GLU A 108 ? 0.2010 0.2843 0.2571 0.0347  0.0159  0.0095  249 GLU A OE1   
790  O OE2   . GLU A 108 ? 0.2315 0.3121 0.2894 0.0293  0.0142  0.0108  249 GLU A OE2   
791  N N     . ALA A 109 ? 0.1030 0.2018 0.2197 0.0318  0.0098  0.0096  250 ALA A N     
792  C CA    . ALA A 109 ? 0.1077 0.2072 0.2351 0.0294  0.0059  0.0143  250 ALA A CA    
793  C C     . ALA A 109 ? 0.1130 0.2096 0.2500 0.0284  0.0051  0.0108  250 ALA A C     
794  O O     . ALA A 109 ? 0.0973 0.1933 0.2410 0.0269  0.0025  0.0141  250 ALA A O     
795  C CB    . ALA A 109 ? 0.0881 0.1891 0.2174 0.0287  0.0045  0.0171  250 ALA A CB    
796  N N     . ILE A 110 ? 0.0937 0.1890 0.2312 0.0294  0.0074  0.0046  251 ILE A N     
797  C CA    . ILE A 110 ? 0.0938 0.1866 0.2397 0.0287  0.0075  0.0012  251 ILE A CA    
798  C C     . ILE A 110 ? 0.1199 0.2133 0.2651 0.0285  0.0087  -0.0005 251 ILE A C     
799  O O     . ILE A 110 ? 0.0885 0.1810 0.2422 0.0277  0.0075  -0.0003 251 ILE A O     
800  C CB    . ILE A 110 ? 0.0887 0.1807 0.2349 0.0291  0.0100  -0.0049 251 ILE A CB    
801  C CG1   . ILE A 110 ? 0.0891 0.1812 0.2390 0.0286  0.0084  -0.0031 251 ILE A CG1   
802  C CG2   . ILE A 110 ? 0.1041 0.1936 0.2585 0.0284  0.0110  -0.0094 251 ILE A CG2   
803  C CD1   . ILE A 110 ? 0.0781 0.1704 0.2285 0.0286  0.0107  -0.0090 251 ILE A CD1   
804  N N     . ASN A 111 ? 0.0929 0.1879 0.2288 0.0293  0.0114  -0.0022 252 ASN A N     
805  C CA    . ASN A 111 ? 0.1150 0.2111 0.2510 0.0285  0.0128  -0.0035 252 ASN A CA    
806  C C     . ASN A 111 ? 0.0901 0.1878 0.2310 0.0271  0.0094  0.0025  252 ASN A C     
807  O O     . ASN A 111 ? 0.1083 0.2073 0.2549 0.0258  0.0089  0.0020  252 ASN A O     
808  C CB    . ASN A 111 ? 0.0774 0.1742 0.2032 0.0294  0.0165  -0.0061 252 ASN A CB    
809  C CG    . ASN A 111 ? 0.1291 0.2252 0.2508 0.0296  0.0198  -0.0125 252 ASN A CG    
810  O OD1   . ASN A 111 ? 0.1232 0.2200 0.2464 0.0282  0.0219  -0.0163 252 ASN A OD1   
811  N ND2   . ASN A 111 ? 0.0742 0.1698 0.1908 0.0310  0.0203  -0.0135 252 ASN A ND2   
812  N N     . LEU A 112 ? 0.0997 0.1981 0.2381 0.0270  0.0070  0.0086  253 LEU A N     
813  C CA    . LEU A 112 ? 0.1178 0.2187 0.2601 0.0249  0.0032  0.0154  253 LEU A CA    
814  C C     . LEU A 112 ? 0.1096 0.2091 0.2631 0.0239  0.0000  0.0163  253 LEU A C     
815  O O     . LEU A 112 ? 0.0984 0.1998 0.2573 0.0226  -0.0016 0.0175  253 LEU A O     
816  C CB    . LEU A 112 ? 0.1129 0.2133 0.2461 0.0239  0.0011  0.0212  253 LEU A CB    
817  C CG    . LEU A 112 ? 0.1417 0.2439 0.2719 0.0205  -0.0028 0.0280  253 LEU A CG    
818  C CD1   . LEU A 112 ? 0.1419 0.2429 0.2561 0.0194  -0.0025 0.0307  253 LEU A CD1   
819  C CD2   . LEU A 112 ? 0.0923 0.1984 0.2393 0.0194  -0.0078 0.0343  253 LEU A CD2   
820  N N     . VAL A 113 ? 0.1334 0.2298 0.2912 0.0245  -0.0009 0.0161  254 VAL A N     
821  C CA    . VAL A 113 ? 0.1113 0.2053 0.2810 0.0240  -0.0037 0.0178  254 VAL A CA    
822  C C     . VAL A 113 ? 0.1477 0.2416 0.3229 0.0248  -0.0016 0.0120  254 VAL A C     
823  O O     . VAL A 113 ? 0.1179 0.2128 0.3013 0.0242  -0.0038 0.0142  254 VAL A O     
824  C CB    . VAL A 113 ? 0.1214 0.2117 0.2956 0.0245  -0.0043 0.0180  254 VAL A CB    
825  C CG1   . VAL A 113 ? 0.1176 0.2045 0.3060 0.0243  -0.0068 0.0196  254 VAL A CG1   
826  C CG2   . VAL A 113 ? 0.1204 0.2124 0.2898 0.0232  -0.0065 0.0246  254 VAL A CG2   
827  N N     . ALA A 114 ? 0.1324 0.2259 0.3032 0.0259  0.0028  0.0047  255 ALA A N     
828  C CA    . ALA A 114 ? 0.1573 0.2513 0.3328 0.0262  0.0055  -0.0011 255 ALA A CA    
829  C C     . ALA A 114 ? 0.1689 0.2675 0.3449 0.0251  0.0051  0.0003  255 ALA A C     
830  O O     . ALA A 114 ? 0.1583 0.2581 0.3438 0.0249  0.0035  0.0010  255 ALA A O     
831  C CB    . ALA A 114 ? 0.1444 0.2380 0.3127 0.0267  0.0102  -0.0082 255 ALA A CB    
832  N N     A HIS A 115 ? 0.1550 0.2562 0.3215 0.0242  0.0064  0.0009  256 HIS A N     
833  N N     B HIS A 115 ? 0.1482 0.2494 0.3148 0.0242  0.0065  0.0008  256 HIS A N     
834  C CA    A HIS A 115 ? 0.1641 0.2700 0.3312 0.0223  0.0067  0.0015  256 HIS A CA    
835  C CA    B HIS A 115 ? 0.1652 0.2712 0.3332 0.0223  0.0065  0.0014  256 HIS A CA    
836  C C     A HIS A 115 ? 0.1755 0.2839 0.3496 0.0209  0.0014  0.0085  256 HIS A C     
837  C C     B HIS A 115 ? 0.1734 0.2818 0.3480 0.0210  0.0012  0.0086  256 HIS A C     
838  O O     A HIS A 115 ? 0.1840 0.2952 0.3666 0.0204  0.0003  0.0083  256 HIS A O     
839  O O     B HIS A 115 ? 0.1809 0.2921 0.3641 0.0204  -0.0001 0.0088  256 HIS A O     
840  C CB    A HIS A 115 ? 0.1563 0.2635 0.3131 0.0216  0.0093  0.0012  256 HIS A CB    
841  C CB    B HIS A 115 ? 0.1578 0.2657 0.3161 0.0213  0.0094  0.0007  256 HIS A CB    
842  C CG    A HIS A 115 ? 0.1763 0.2816 0.3257 0.0226  0.0144  -0.0056 256 HIS A CG    
843  C CG    B HIS A 115 ? 0.1890 0.3020 0.3493 0.0184  0.0098  0.0011  256 HIS A CG    
844  N ND1   A HIS A 115 ? 0.2031 0.3075 0.3412 0.0209  0.0179  -0.0085 256 HIS A ND1   
845  N ND1   B HIS A 115 ? 0.2004 0.3127 0.3523 0.0154  0.0064  0.0069  256 HIS A ND1   
846  C CD2   A HIS A 115 ? 0.1805 0.2825 0.3277 0.0243  0.0161  -0.0095 256 HIS A CD2   
847  C CD2   B HIS A 115 ? 0.1767 0.2931 0.3403 0.0170  0.0129  -0.0039 256 HIS A CD2   
848  C CE1   A HIS A 115 ? 0.2036 0.3067 0.3367 0.0220  0.0216  -0.0138 256 HIS A CE1   
849  C CE1   B HIS A 115 ? 0.1875 0.3028 0.3388 0.0122  0.0072  0.0055  256 HIS A CE1   
850  N NE2   A HIS A 115 ? 0.1853 0.2874 0.3241 0.0241  0.0205  -0.0145 256 HIS A NE2   
851  N NE2   B HIS A 115 ? 0.1913 0.3097 0.3503 0.0132  0.0112  -0.0008 256 HIS A NE2   
852  N N     . ALA A 116 ? 0.1398 0.2476 0.3105 0.0202  -0.0020 0.0150  257 ALA A N     
853  C CA    . ALA A 116 ? 0.1487 0.2595 0.3236 0.0180  -0.0073 0.0226  257 ALA A CA    
854  C C     . ALA A 116 ? 0.1621 0.2706 0.3484 0.0190  -0.0105 0.0248  257 ALA A C     
855  O O     . ALA A 116 ? 0.1504 0.2619 0.3450 0.0185  -0.0123 0.0256  257 ALA A O     
856  C CB    . ALA A 116 ? 0.0955 0.2072 0.2621 0.0163  -0.0098 0.0293  257 ALA A CB    
857  N N     . TRP A 117 ? 0.1287 0.2320 0.3166 0.0203  -0.0112 0.0259  258 TRP A N     
858  C CA    . TRP A 117 ? 0.1605 0.2609 0.3606 0.0211  -0.0142 0.0288  258 TRP A CA    
859  C C     . TRP A 117 ? 0.1578 0.2576 0.3671 0.0233  -0.0114 0.0219  258 TRP A C     
860  O O     . TRP A 117 ? 0.1587 0.2597 0.3789 0.0236  -0.0138 0.0240  258 TRP A O     
861  C CB    . TRP A 117 ? 0.1583 0.2535 0.3591 0.0216  -0.0151 0.0312  258 TRP A CB    
862  C CG    . TRP A 117 ? 0.1924 0.2839 0.4069 0.0219  -0.0185 0.0354  258 TRP A CG    
863  C CD1   . TRP A 117 ? 0.1949 0.2866 0.4137 0.0199  -0.0239 0.0450  258 TRP A CD1   
864  C CD2   . TRP A 117 ? 0.1965 0.2837 0.4228 0.0242  -0.0169 0.0304  258 TRP A CD2   
865  N NE1   . TRP A 117 ? 0.2120 0.2993 0.4454 0.0211  -0.0259 0.0467  258 TRP A NE1   
866  C CE2   . TRP A 117 ? 0.2172 0.3015 0.4559 0.0238  -0.0216 0.0375  258 TRP A CE2   
867  C CE3   . TRP A 117 ? 0.2054 0.2910 0.4332 0.0262  -0.0120 0.0208  258 TRP A CE3   
868  C CZ2   . TRP A 117 ? 0.2536 0.3331 0.5072 0.0257  -0.0214 0.0349  258 TRP A CZ2   
869  C CZ3   . TRP A 117 ? 0.2486 0.3299 0.4905 0.0278  -0.0116 0.0179  258 TRP A CZ3   
870  C CH2   . TRP A 117 ? 0.2473 0.3253 0.5024 0.0277  -0.0163 0.0248  258 TRP A CH2   
871  N N     . GLY A 118 ? 0.1397 0.2379 0.3448 0.0246  -0.0063 0.0139  259 GLY A N     
872  C CA    . GLY A 118 ? 0.1614 0.2595 0.3746 0.0261  -0.0032 0.0072  259 GLY A CA    
873  C C     . GLY A 118 ? 0.2186 0.3230 0.4354 0.0256  -0.0028 0.0061  259 GLY A C     
874  O O     . GLY A 118 ? 0.2287 0.3340 0.4575 0.0268  -0.0033 0.0049  259 GLY A O     
875  N N     . GLY A 119 ? 0.2017 0.3110 0.4092 0.0236  -0.0018 0.0063  260 GLY A N     
876  C CA    . GLY A 119 ? 0.1944 0.3107 0.4059 0.0222  -0.0016 0.0055  260 GLY A CA    
877  C C     . GLY A 119 ? 0.2484 0.3678 0.4688 0.0216  -0.0072 0.0125  260 GLY A C     
878  O O     . GLY A 119 ? 0.2638 0.3889 0.4920 0.0214  -0.0074 0.0116  260 GLY A O     
879  N N     . LYS A 120 ? 0.2277 0.3439 0.4472 0.0211  -0.0119 0.0199  261 LYS A N     
880  C CA    . LYS A 120 ? 0.2218 0.3407 0.4503 0.0204  -0.0175 0.0270  261 LYS A CA    
881  C C     . LYS A 120 ? 0.2806 0.3958 0.5238 0.0235  -0.0186 0.0270  261 LYS A C     
882  O O     . LYS A 120 ? 0.2647 0.3839 0.5185 0.0238  -0.0216 0.0301  261 LYS A O     
883  C CB    . LYS A 120 ? 0.2462 0.3642 0.4683 0.0178  -0.0224 0.0360  261 LYS A CB    
884  C CG    . LYS A 120 ? 0.3148 0.4380 0.5425 0.0156  -0.0283 0.0438  261 LYS A CG    
885  C CD    . LYS A 120 ? 0.3741 0.4937 0.6033 0.0146  -0.0336 0.0531  261 LYS A CD    
886  C CE    . LYS A 120 ? 0.4228 0.5487 0.6494 0.0103  -0.0394 0.0620  261 LYS A CE    
887  N NZ    . LYS A 120 ? 0.4755 0.5988 0.6986 0.0079  -0.0439 0.0713  261 LYS A NZ    
888  N N     . HIS A 121 ? 0.2179 0.3259 0.4630 0.0256  -0.0163 0.0237  262 HIS A N     
889  C CA    . HIS A 121 ? 0.2154 0.3187 0.4754 0.0278  -0.0183 0.0253  262 HIS A CA    
890  C C     . HIS A 121 ? 0.2831 0.3845 0.5519 0.0306  -0.0137 0.0162  262 HIS A C     
891  O O     . HIS A 121 ? 0.2917 0.3899 0.5753 0.0326  -0.0152 0.0169  262 HIS A O     
892  C CB    . HIS A 121 ? 0.1929 0.2890 0.4521 0.0273  -0.0209 0.0305  262 HIS A CB    
893  C CG    . HIS A 121 ? 0.2852 0.3833 0.5380 0.0243  -0.0260 0.0404  262 HIS A CG    
894  N ND1   . HIS A 121 ? 0.2940 0.3934 0.5555 0.0233  -0.0318 0.0493  262 HIS A ND1   
895  C CD2   . HIS A 121 ? 0.2104 0.3099 0.4489 0.0218  -0.0262 0.0430  262 HIS A CD2   
896  C CE1   . HIS A 121 ? 0.3031 0.4048 0.5550 0.0199  -0.0353 0.0570  262 HIS A CE1   
897  N NE2   . HIS A 121 ? 0.2750 0.3768 0.5132 0.0190  -0.0319 0.0531  262 HIS A NE2   
898  N N     . LEU A 122 ? 0.2111 0.3144 0.4721 0.0305  -0.0081 0.0080  263 LEU A N     
899  C CA    . LEU A 122 ? 0.2481 0.3494 0.5162 0.0325  -0.0035 -0.0009 263 LEU A CA    
900  C C     . LEU A 122 ? 0.2754 0.3845 0.5479 0.0329  -0.0007 -0.0057 263 LEU A C     
901  O O     . LEU A 122 ? 0.2667 0.3825 0.5312 0.0309  -0.0002 -0.0049 263 LEU A O     
902  C CB    . LEU A 122 ? 0.2676 0.3653 0.5243 0.0318  0.0010  -0.0072 263 LEU A CB    
903  C CG    . LEU A 122 ? 0.2894 0.3799 0.5432 0.0315  -0.0008 -0.0042 263 LEU A CG    
904  C CD1   . LEU A 122 ? 0.3723 0.4601 0.6191 0.0312  0.0040  -0.0120 263 LEU A CD1   
905  C CD2   . LEU A 122 ? 0.3466 0.4318 0.6162 0.0328  -0.0043 -0.0006 263 LEU A CD2   
906  N N     . GLY A 123 ? 0.2496 0.3579 0.5356 0.0351  0.0012  -0.0108 264 GLY A N     
907  C CA    . GLY A 123 ? 0.2338 0.3497 0.5255 0.0357  0.0046  -0.0164 264 GLY A CA    
908  C C     . GLY A 123 ? 0.2763 0.3895 0.5767 0.0374  0.0093  -0.0258 264 GLY A C     
909  O O     . GLY A 123 ? 0.2435 0.3488 0.5450 0.0378  0.0099  -0.0283 264 GLY A O     
910  N N     . PRO A 124 ? 0.2255 0.3458 0.5327 0.0380  0.0127  -0.0314 265 PRO A N     
911  C CA    . PRO A 124 ? 0.2333 0.3524 0.5467 0.0388  0.0181  -0.0418 265 PRO A CA    
912  C C     . PRO A 124 ? 0.2508 0.3618 0.5791 0.0414  0.0167  -0.0431 265 PRO A C     
913  O O     . PRO A 124 ? 0.2352 0.3454 0.5777 0.0439  0.0123  -0.0377 265 PRO A O     
914  C CB    . PRO A 124 ? 0.2362 0.3657 0.5576 0.0393  0.0206  -0.0452 265 PRO A CB    
915  C CG    . PRO A 124 ? 0.2309 0.3674 0.5410 0.0368  0.0188  -0.0390 265 PRO A CG    
916  C CD    . PRO A 124 ? 0.1813 0.3123 0.4882 0.0370  0.0124  -0.0292 265 PRO A CD    
917  N N     . GLY A 125 ? 0.2983 0.4037 0.6241 0.0406  0.0202  -0.0504 266 GLY A N     
918  C CA    . GLY A 125 ? 0.2586 0.3563 0.5987 0.0423  0.0195  -0.0531 266 GLY A CA    
919  C C     . GLY A 125 ? 0.3028 0.3919 0.6418 0.0421  0.0148  -0.0458 266 GLY A C     
920  O O     . GLY A 125 ? 0.3226 0.4047 0.6710 0.0425  0.0149  -0.0490 266 GLY A O     
921  N N     . ASP A 126 ? 0.2654 0.3552 0.5941 0.0411  0.0106  -0.0361 267 ASP A N     
922  C CA    . ASP A 126 ? 0.2710 0.3536 0.5960 0.0402  0.0067  -0.0295 267 ASP A CA    
923  C C     . ASP A 126 ? 0.2916 0.3702 0.6069 0.0382  0.0103  -0.0359 267 ASP A C     
924  O O     . ASP A 126 ? 0.2508 0.3332 0.5552 0.0369  0.0149  -0.0427 267 ASP A O     
925  C CB    . ASP A 126 ? 0.2964 0.3822 0.6089 0.0388  0.0027  -0.0197 267 ASP A CB    
926  C CG    . ASP A 126 ? 0.3422 0.4317 0.6644 0.0402  -0.0020 -0.0120 267 ASP A CG    
927  O OD1   . ASP A 126 ? 0.3188 0.4070 0.6587 0.0426  -0.0030 -0.0127 267 ASP A OD1   
928  O OD2   . ASP A 126 ? 0.2971 0.3912 0.6098 0.0387  -0.0048 -0.0054 267 ASP A OD2   
929  N N     . GLU A 127 ? 0.2283 0.2995 0.5475 0.0378  0.0079  -0.0331 268 GLU A N     
930  C CA    . GLU A 127 ? 0.2257 0.2932 0.5394 0.0361  0.0110  -0.0397 268 GLU A CA    
931  C C     . GLU A 127 ? 0.1497 0.2150 0.4506 0.0345  0.0084  -0.0331 268 GLU A C     
932  O O     . GLU A 127 ? 0.1932 0.2558 0.4976 0.0346  0.0035  -0.0237 268 GLU A O     
933  C CB    . GLU A 127 ? 0.2478 0.3091 0.5801 0.0368  0.0114  -0.0448 268 GLU A CB    
934  C CG    . GLU A 127 ? 0.3134 0.3774 0.6596 0.0388  0.0141  -0.0517 268 GLU A CG    
935  C CD    . GLU A 127 ? 0.3915 0.4503 0.7547 0.0391  0.0162  -0.0599 268 GLU A CD    
936  O OE1   . GLU A 127 ? 0.3170 0.3687 0.6883 0.0387  0.0133  -0.0566 268 GLU A OE1   
937  O OE2   . GLU A 127 ? 0.4124 0.4746 0.7818 0.0397  0.0207  -0.0695 268 GLU A OE2   
938  N N     . ILE A 128 ? 0.1637 0.2309 0.4500 0.0328  0.0118  -0.0379 269 ILE A N     
939  C CA    . ILE A 128 ? 0.1927 0.2584 0.4675 0.0314  0.0105  -0.0338 269 ILE A CA    
940  C C     . ILE A 128 ? 0.1583 0.2204 0.4370 0.0302  0.0130  -0.0414 269 ILE A C     
941  O O     . ILE A 128 ? 0.2205 0.2846 0.4985 0.0295  0.0174  -0.0511 269 ILE A O     
942  C CB    . ILE A 128 ? 0.1787 0.2501 0.4337 0.0304  0.0122  -0.0332 269 ILE A CB    
943  C CG1   . ILE A 128 ? 0.2000 0.2760 0.4522 0.0311  0.0104  -0.0276 269 ILE A CG1   
944  C CG2   . ILE A 128 ? 0.1520 0.2226 0.3958 0.0293  0.0108  -0.0289 269 ILE A CG2   
945  C CD1   . ILE A 128 ? 0.2205 0.3026 0.4597 0.0302  0.0141  -0.0316 269 ILE A CD1   
946  N N     . VAL A 129 ? 0.1859 0.2432 0.4692 0.0296  0.0102  -0.0372 270 VAL A N     
947  C CA    . VAL A 129 ? 0.1901 0.2445 0.4781 0.0282  0.0122  -0.0441 270 VAL A CA    
948  C C     . VAL A 129 ? 0.2001 0.2569 0.4728 0.0268  0.0121  -0.0416 270 VAL A C     
949  O O     . VAL A 129 ? 0.1584 0.2150 0.4271 0.0269  0.0084  -0.0322 270 VAL A O     
950  C CB    . VAL A 129 ? 0.1678 0.2150 0.4760 0.0283  0.0093  -0.0420 270 VAL A CB    
951  C CG1   . VAL A 129 ? 0.2073 0.2519 0.5204 0.0264  0.0116  -0.0497 270 VAL A CG1   
952  C CG2   . VAL A 129 ? 0.1523 0.1976 0.4765 0.0300  0.0096  -0.0449 270 VAL A CG2   
953  N N     . ILE A 130 ? 0.1825 0.2425 0.4468 0.0255  0.0161  -0.0500 271 ILE A N     
954  C CA    . ILE A 130 ? 0.2083 0.2711 0.4607 0.0243  0.0163  -0.0492 271 ILE A CA    
955  C C     . ILE A 130 ? 0.2283 0.2896 0.4892 0.0224  0.0184  -0.0580 271 ILE A C     
956  O O     . ILE A 130 ? 0.1764 0.2351 0.4496 0.0220  0.0205  -0.0659 271 ILE A O     
957  C CB    . ILE A 130 ? 0.1726 0.2420 0.4057 0.0241  0.0187  -0.0503 271 ILE A CB    
958  C CG1   . ILE A 130 ? 0.1873 0.2592 0.4192 0.0230  0.0233  -0.0610 271 ILE A CG1   
959  C CG2   . ILE A 130 ? 0.1925 0.2635 0.4183 0.0256  0.0168  -0.0425 271 ILE A CG2   
960  C CD1   . ILE A 130 ? 0.2306 0.3088 0.4443 0.0221  0.0257  -0.0628 271 ILE A CD1   
961  N N     . THR A 131 ? 0.2177 0.2814 0.4726 0.0212  0.0180  -0.0571 272 THR A N     
962  C CA    . THR A 131 ? 0.1909 0.2547 0.4531 0.0190  0.0202  -0.0661 272 THR A CA    
963  C C     . THR A 131 ? 0.1834 0.2542 0.4314 0.0175  0.0241  -0.0740 272 THR A C     
964  O O     . THR A 131 ? 0.2214 0.2968 0.4532 0.0183  0.0244  -0.0705 272 THR A O     
965  C CB    . THR A 131 ? 0.2320 0.2953 0.4987 0.0180  0.0174  -0.0611 272 THR A CB    
966  O OG1   . THR A 131 ? 0.2376 0.3082 0.4869 0.0177  0.0172  -0.0574 272 THR A OG1   
967  C CG2   . THR A 131 ? 0.2081 0.2657 0.4848 0.0192  0.0128  -0.0502 272 THR A CG2   
968  N N     . HIS A 132 ? 0.1764 0.2481 0.4311 0.0150  0.0271  -0.0850 273 HIS A N     
969  C CA    . HIS A 132 ? 0.1852 0.2645 0.4271 0.0128  0.0306  -0.0930 273 HIS A CA    
970  C C     . HIS A 132 ? 0.1970 0.2827 0.4253 0.0124  0.0292  -0.0884 273 HIS A C     
971  O O     . HIS A 132 ? 0.1976 0.2903 0.4126 0.0110  0.0313  -0.0922 273 HIS A O     
972  C CB    . HIS A 132 ? 0.1976 0.2770 0.4508 0.0096  0.0340  -0.1062 273 HIS A CB    
973  C CG    . HIS A 132 ? 0.2194 0.3051 0.4631 0.0071  0.0382  -0.1156 273 HIS A CG    
974  N ND1   . HIS A 132 ? 0.2713 0.3572 0.5246 0.0042  0.0418  -0.1278 273 HIS A ND1   
975  C CD2   . HIS A 132 ? 0.2298 0.3221 0.4555 0.0068  0.0393  -0.1144 273 HIS A CD2   
976  C CE1   . HIS A 132 ? 0.2456 0.3386 0.4865 0.0019  0.0450  -0.1335 273 HIS A CE1   
977  N NE2   . HIS A 132 ? 0.2446 0.3412 0.4689 0.0035  0.0435  -0.1254 273 HIS A NE2   
978  N N     . LEU A 133 ? 0.1768 0.2610 0.4084 0.0133  0.0257  -0.0799 274 LEU A N     
979  C CA    . LEU A 133 ? 0.2000 0.2909 0.4212 0.0128  0.0241  -0.0752 274 LEU A CA    
980  C C     . LEU A 133 ? 0.1873 0.2810 0.3918 0.0153  0.0228  -0.0663 274 LEU A C     
981  O O     . LEU A 133 ? 0.1826 0.2820 0.3782 0.0154  0.0215  -0.0620 274 LEU A O     
982  C CB    . LEU A 133 ? 0.1681 0.2567 0.4013 0.0122  0.0209  -0.0697 274 LEU A CB    
983  C CG    . LEU A 133 ? 0.1605 0.2473 0.4111 0.0092  0.0222  -0.0788 274 LEU A CG    
984  C CD1   . LEU A 133 ? 0.2002 0.2826 0.4649 0.0085  0.0186  -0.0716 274 LEU A CD1   
985  C CD2   . LEU A 133 ? 0.2083 0.3048 0.4520 0.0058  0.0242  -0.0864 274 LEU A CD2   
986  N N     . GLU A 134 ? 0.1618 0.2520 0.3627 0.0172  0.0231  -0.0638 275 GLU A N     
987  C CA    . GLU A 134 ? 0.1568 0.2482 0.3452 0.0196  0.0216  -0.0548 275 GLU A CA    
988  C C     . GLU A 134 ? 0.1623 0.2603 0.3347 0.0196  0.0232  -0.0558 275 GLU A C     
989  O O     . GLU A 134 ? 0.1405 0.2415 0.3091 0.0180  0.0260  -0.0634 275 GLU A O     
990  C CB    . GLU A 134 ? 0.1685 0.2554 0.3584 0.0210  0.0217  -0.0529 275 GLU A CB    
991  C CG    . GLU A 134 ? 0.1790 0.2594 0.3843 0.0216  0.0194  -0.0496 275 GLU A CG    
992  C CD    . GLU A 134 ? 0.2531 0.3322 0.4637 0.0216  0.0158  -0.0422 275 GLU A CD    
993  O OE1   . GLU A 134 ? 0.2483 0.3307 0.4485 0.0223  0.0141  -0.0351 275 GLU A OE1   
994  O OE2   . GLU A 134 ? 0.2385 0.3134 0.4645 0.0206  0.0147  -0.0435 275 GLU A OE2   
995  N N     . HIS A 135 ? 0.1535 0.2538 0.3168 0.0214  0.0213  -0.0479 276 HIS A N     
996  C CA    . HIS A 135 ? 0.1566 0.2609 0.3051 0.0227  0.0222  -0.0461 276 HIS A CA    
997  C C     . HIS A 135 ? 0.1599 0.2612 0.3042 0.0234  0.0237  -0.0461 276 HIS A C     
998  O O     . HIS A 135 ? 0.1331 0.2298 0.2847 0.0237  0.0231  -0.0445 276 HIS A O     
999  C CB    . HIS A 135 ? 0.1431 0.2492 0.2862 0.0247  0.0198  -0.0376 276 HIS A CB    
1000 C CG    . HIS A 135 ? 0.1705 0.2801 0.3000 0.0266  0.0205  -0.0352 276 HIS A CG    
1001 N ND1   . HIS A 135 ? 0.1726 0.2796 0.2946 0.0282  0.0214  -0.0328 276 HIS A ND1   
1002 C CD2   . HIS A 135 ? 0.1900 0.3053 0.3126 0.0274  0.0200  -0.0345 276 HIS A CD2   
1003 C CE1   . HIS A 135 ? 0.1880 0.2979 0.2993 0.0299  0.0217  -0.0311 276 HIS A CE1   
1004 N NE2   . HIS A 135 ? 0.1565 0.2715 0.2677 0.0297  0.0207  -0.0319 276 HIS A NE2   
1005 N N     . HIS A 136 ? 0.1227 0.2272 0.2556 0.0235  0.0257  -0.0478 277 HIS A N     
1006 C CA    . HIS A 136 ? 0.1339 0.2365 0.2628 0.0236  0.0274  -0.0479 277 HIS A CA    
1007 C C     . HIS A 136 ? 0.1491 0.2481 0.2783 0.0257  0.0255  -0.0403 277 HIS A C     
1008 O O     . HIS A 136 ? 0.1374 0.2344 0.2689 0.0254  0.0263  -0.0405 277 HIS A O     
1009 C CB    . HIS A 136 ? 0.1335 0.2403 0.2494 0.0234  0.0294  -0.0496 277 HIS A CB    
1010 C CG    . HIS A 136 ? 0.1310 0.2429 0.2452 0.0206  0.0315  -0.0578 277 HIS A CG    
1011 N ND1   . HIS A 136 ? 0.1301 0.2477 0.2325 0.0199  0.0327  -0.0593 277 HIS A ND1   
1012 C CD2   . HIS A 136 ? 0.1146 0.2275 0.2373 0.0180  0.0326  -0.0651 277 HIS A CD2   
1013 C CE1   . HIS A 136 ? 0.1450 0.2678 0.2482 0.0167  0.0344  -0.0671 277 HIS A CE1   
1014 N NE2   . HIS A 136 ? 0.1268 0.2465 0.2424 0.0154  0.0346  -0.0712 277 HIS A NE2   
1015 N N     . ALA A 137 ? 0.1013 0.2005 0.2282 0.0275  0.0232  -0.0340 278 ALA A N     
1016 C CA    . ALA A 137 ? 0.1393 0.2362 0.2664 0.0290  0.0213  -0.0273 278 ALA A CA    
1017 C C     . ALA A 137 ? 0.1446 0.2384 0.2837 0.0282  0.0196  -0.0265 278 ALA A C     
1018 O O     . ALA A 137 ? 0.1200 0.2125 0.2602 0.0286  0.0184  -0.0226 278 ALA A O     
1019 C CB    . ALA A 137 ? 0.1122 0.2109 0.2356 0.0306  0.0194  -0.0216 278 ALA A CB    
1020 N N     . ASN A 138 ? 0.1213 0.2138 0.2701 0.0269  0.0193  -0.0300 279 ASN A N     
1021 C CA    . ASN A 138 ? 0.1476 0.2362 0.3095 0.0264  0.0177  -0.0296 279 ASN A CA    
1022 C C     . ASN A 138 ? 0.1613 0.2485 0.3294 0.0254  0.0203  -0.0373 279 ASN A C     
1023 O O     . ASN A 138 ? 0.1652 0.2491 0.3463 0.0249  0.0197  -0.0396 279 ASN A O     
1024 C CB    . ASN A 138 ? 0.1299 0.2171 0.3007 0.0258  0.0154  -0.0277 279 ASN A CB    
1025 C CG    . ASN A 138 ? 0.1853 0.2683 0.3671 0.0259  0.0122  -0.0223 279 ASN A CG    
1026 O OD1   . ASN A 138 ? 0.1354 0.2178 0.3162 0.0266  0.0111  -0.0186 279 ASN A OD1   
1027 N ND2   . ASN A 138 ? 0.1991 0.2796 0.3923 0.0249  0.0105  -0.0216 279 ASN A ND2   
1028 N N     . ILE A 139 ? 0.1308 0.2208 0.2905 0.0248  0.0233  -0.0415 280 ILE A N     
1029 C CA    . ILE A 139 ? 0.1549 0.2449 0.3193 0.0235  0.0262  -0.0488 280 ILE A CA    
1030 C C     . ILE A 139 ? 0.1836 0.2754 0.3416 0.0236  0.0276  -0.0475 280 ILE A C     
1031 O O     . ILE A 139 ? 0.1746 0.2656 0.3400 0.0237  0.0277  -0.0480 280 ILE A O     
1032 C CB    . ILE A 139 ? 0.1841 0.2771 0.3456 0.0214  0.0292  -0.0572 280 ILE A CB    
1033 C CG1   . ILE A 139 ? 0.1828 0.2745 0.3529 0.0208  0.0282  -0.0600 280 ILE A CG1   
1034 C CG2   . ILE A 139 ? 0.1753 0.2695 0.3405 0.0197  0.0325  -0.0650 280 ILE A CG2   
1035 C CD1   . ILE A 139 ? 0.1606 0.2572 0.3254 0.0185  0.0305  -0.0674 280 ILE A CD1   
1036 N N     . VAL A 140 ? 0.1397 0.2343 0.2847 0.0236  0.0287  -0.0460 281 VAL A N     
1037 C CA    . VAL A 140 ? 0.1297 0.2263 0.2686 0.0229  0.0307  -0.0461 281 VAL A CA    
1038 C C     . VAL A 140 ? 0.1719 0.2673 0.3155 0.0240  0.0286  -0.0405 281 VAL A C     
1039 O O     . VAL A 140 ? 0.1732 0.2703 0.3201 0.0230  0.0302  -0.0426 281 VAL A O     
1040 C CB    . VAL A 140 ? 0.1675 0.2663 0.2923 0.0229  0.0321  -0.0452 281 VAL A CB    
1041 C CG1   . VAL A 140 ? 0.2069 0.3076 0.3258 0.0216  0.0345  -0.0456 281 VAL A CG1   
1042 C CG2   . VAL A 140 ? 0.1665 0.2680 0.2870 0.0213  0.0340  -0.0512 281 VAL A CG2   
1043 N N     . PRO A 141 ? 0.1366 0.2304 0.2810 0.0256  0.0252  -0.0337 282 PRO A N     
1044 C CA    . PRO A 141 ? 0.1482 0.2422 0.2977 0.0260  0.0230  -0.0289 282 PRO A CA    
1045 C C     . PRO A 141 ? 0.1738 0.2669 0.3367 0.0258  0.0222  -0.0306 282 PRO A C     
1046 O O     . PRO A 141 ? 0.1653 0.2605 0.3321 0.0255  0.0220  -0.0294 282 PRO A O     
1047 C CB    . PRO A 141 ? 0.1367 0.2295 0.2849 0.0272  0.0194  -0.0221 282 PRO A CB    
1048 C CG    . PRO A 141 ? 0.1310 0.2241 0.2693 0.0279  0.0207  -0.0231 282 PRO A CG    
1049 C CD    . PRO A 141 ? 0.1338 0.2269 0.2740 0.0268  0.0233  -0.0301 282 PRO A CD    
1050 N N     . TRP A 142 ? 0.1578 0.2481 0.3287 0.0260  0.0219  -0.0336 283 TRP A N     
1051 C CA    . TRP A 142 ? 0.1769 0.2658 0.3618 0.0262  0.0215  -0.0358 283 TRP A CA    
1052 C C     . TRP A 142 ? 0.2182 0.3102 0.4042 0.0251  0.0256  -0.0431 283 TRP A C     
1053 O O     . TRP A 142 ? 0.1836 0.2768 0.3789 0.0255  0.0255  -0.0437 283 TRP A O     
1054 C CB    . TRP A 142 ? 0.1189 0.2034 0.3136 0.0266  0.0203  -0.0374 283 TRP A CB    
1055 C CG    . TRP A 142 ? 0.1707 0.2533 0.3632 0.0271  0.0166  -0.0302 283 TRP A CG    
1056 C CD1   . TRP A 142 ? 0.1672 0.2490 0.3558 0.0268  0.0165  -0.0305 283 TRP A CD1   
1057 C CD2   . TRP A 142 ? 0.1357 0.2181 0.3294 0.0277  0.0127  -0.0217 283 TRP A CD2   
1058 N NE1   . TRP A 142 ? 0.1438 0.2249 0.3313 0.0272  0.0130  -0.0228 283 TRP A NE1   
1059 C CE2   . TRP A 142 ? 0.1586 0.2399 0.3488 0.0276  0.0106  -0.0173 283 TRP A CE2   
1060 C CE3   . TRP A 142 ? 0.1621 0.2459 0.3599 0.0280  0.0106  -0.0175 283 TRP A CE3   
1061 C CZ2   . TRP A 142 ? 0.1577 0.2391 0.3481 0.0275  0.0067  -0.0090 283 TRP A CZ2   
1062 C CZ3   . TRP A 142 ? 0.1869 0.2707 0.3846 0.0279  0.0065  -0.0091 283 TRP A CZ3   
1063 C CH2   . TRP A 142 ? 0.1372 0.2196 0.3309 0.0275  0.0046  -0.0050 283 TRP A CH2   
1064 N N     . GLN A 143 ? 0.1900 0.2840 0.3666 0.0236  0.0291  -0.0485 284 GLN A N     
1065 C CA    . GLN A 143 ? 0.2210 0.3189 0.3971 0.0218  0.0332  -0.0552 284 GLN A CA    
1066 C C     . GLN A 143 ? 0.2513 0.3528 0.4236 0.0212  0.0336  -0.0519 284 GLN A C     
1067 O O     . GLN A 143 ? 0.2846 0.3893 0.4635 0.0206  0.0353  -0.0548 284 GLN A O     
1068 C CB    . GLN A 143 ? 0.1972 0.2970 0.3630 0.0196  0.0365  -0.0610 284 GLN A CB    
1069 C CG    . GLN A 143 ? 0.1888 0.2867 0.3598 0.0192  0.0369  -0.0667 284 GLN A CG    
1070 C CD    . GLN A 143 ? 0.2388 0.3398 0.3984 0.0168  0.0394  -0.0715 284 GLN A CD    
1071 O OE1   . GLN A 143 ? 0.2267 0.3293 0.3738 0.0167  0.0394  -0.0679 284 GLN A OE1   
1072 N NE2   . GLN A 143 ? 0.1961 0.2982 0.3604 0.0149  0.0416  -0.0798 284 GLN A NE2   
1073 N N     . LEU A 144 ? 0.1929 0.2945 0.3553 0.0214  0.0323  -0.0463 285 LEU A N     
1074 C CA    . LEU A 144 ? 0.2270 0.3320 0.3869 0.0205  0.0324  -0.0430 285 LEU A CA    
1075 C C     . LEU A 144 ? 0.2900 0.3960 0.4623 0.0216  0.0295  -0.0394 285 LEU A C     
1076 O O     . LEU A 144 ? 0.2936 0.4039 0.4709 0.0206  0.0309  -0.0411 285 LEU A O     
1077 C CB    . LEU A 144 ? 0.2797 0.3838 0.4290 0.0209  0.0311  -0.0377 285 LEU A CB    
1078 C CG    . LEU A 144 ? 0.3431 0.4474 0.4787 0.0197  0.0342  -0.0403 285 LEU A CG    
1079 C CD1   . LEU A 144 ? 0.3906 0.4945 0.5178 0.0201  0.0334  -0.0355 285 LEU A CD1   
1080 C CD2   . LEU A 144 ? 0.3588 0.4669 0.4915 0.0167  0.0385  -0.0462 285 LEU A CD2   
1081 N N     . LEU A 145 ? 0.2345 0.3371 0.4123 0.0236  0.0253  -0.0344 286 LEU A N     
1082 C CA    . LEU A 145 ? 0.2440 0.3474 0.4335 0.0246  0.0218  -0.0302 286 LEU A CA    
1083 C C     . LEU A 145 ? 0.2672 0.3717 0.4691 0.0252  0.0235  -0.0355 286 LEU A C     
1084 O O     . LEU A 145 ? 0.2371 0.3453 0.4474 0.0254  0.0225  -0.0341 286 LEU A O     
1085 C CB    . LEU A 145 ? 0.2117 0.3106 0.4041 0.0261  0.0173  -0.0243 286 LEU A CB    
1086 C CG    . LEU A 145 ? 0.2692 0.3684 0.4737 0.0270  0.0131  -0.0190 286 LEU A CG    
1087 C CD1   . LEU A 145 ? 0.1760 0.2805 0.3770 0.0257  0.0112  -0.0139 286 LEU A CD1   
1088 C CD2   . LEU A 145 ? 0.2270 0.3209 0.4349 0.0279  0.0094  -0.0143 286 LEU A CD2   
1089 N N     . SER A 146 ? 0.2406 0.3423 0.4443 0.0253  0.0261  -0.0420 287 SER A N     
1090 C CA    . SER A 146 ? 0.2381 0.3406 0.4546 0.0259  0.0279  -0.0480 287 SER A CA    
1091 C C     . SER A 146 ? 0.2815 0.3906 0.4967 0.0242  0.0319  -0.0526 287 SER A C     
1092 O O     . SER A 146 ? 0.2520 0.3644 0.4789 0.0250  0.0323  -0.0544 287 SER A O     
1093 C CB    . SER A 146 ? 0.2314 0.3297 0.4501 0.0257  0.0299  -0.0545 287 SER A CB    
1094 O OG    . SER A 146 ? 0.3275 0.4272 0.5578 0.0259  0.0326  -0.0619 287 SER A OG    
1095 N N     . ARG A 147 ? 0.2576 0.3692 0.4592 0.0217  0.0348  -0.0545 288 ARG A N     
1096 C CA    . ARG A 147 ? 0.3220 0.4404 0.5224 0.0194  0.0385  -0.0582 288 ARG A CA    
1097 C C     . ARG A 147 ? 0.3174 0.4402 0.5210 0.0194  0.0361  -0.0520 288 ARG A C     
1098 O O     . ARG A 147 ? 0.2985 0.4275 0.5082 0.0184  0.0380  -0.0542 288 ARG A O     
1099 C CB    . ARG A 147 ? 0.3475 0.4674 0.5327 0.0161  0.0423  -0.0616 288 ARG A CB    
1100 C CG    . ARG A 147 ? 0.4716 0.5897 0.6542 0.0152  0.0450  -0.0690 288 ARG A CG    
1101 C CD    . ARG A 147 ? 0.5917 0.7157 0.7709 0.0116  0.0503  -0.0769 288 ARG A CD    
1102 N NE    . ARG A 147 ? 0.7387 0.8648 0.9019 0.0083  0.0525  -0.0764 288 ARG A NE    
1103 C CZ    . ARG A 147 ? 0.7698 0.8971 0.9233 0.0055  0.0554  -0.0815 288 ARG A CZ    
1104 N NH1   . ARG A 147 ? 0.6239 0.7509 0.7818 0.0052  0.0566  -0.0882 288 ARG A NH1   
1105 N NH2   . ARG A 147 ? 0.6187 0.7478 0.7576 0.0025  0.0570  -0.0799 288 ARG A NH2   
1106 N N     . GLN A 148 ? 0.2827 0.4032 0.4827 0.0202  0.0320  -0.0443 289 GLN A N     
1107 C CA    . GLN A 148 ? 0.2928 0.4182 0.4953 0.0194  0.0295  -0.0387 289 GLN A CA    
1108 C C     . GLN A 148 ? 0.2495 0.3770 0.4676 0.0217  0.0261  -0.0360 289 GLN A C     
1109 O O     . GLN A 148 ? 0.2267 0.3611 0.4504 0.0206  0.0255  -0.0343 289 GLN A O     
1110 C CB    . GLN A 148 ? 0.3013 0.4240 0.4949 0.0191  0.0264  -0.0321 289 GLN A CB    
1111 C CG    . GLN A 148 ? 0.4589 0.5826 0.6387 0.0161  0.0296  -0.0333 289 GLN A CG    
1112 C CD    . GLN A 148 ? 0.6060 0.7270 0.7785 0.0163  0.0267  -0.0274 289 GLN A CD    
1113 O OE1   . GLN A 148 ? 0.6610 0.7827 0.8387 0.0169  0.0222  -0.0215 289 GLN A OE1   
1114 N NE2   . GLN A 148 ? 0.6196 0.7379 0.7799 0.0156  0.0293  -0.0292 289 GLN A NE2   
1115 N N     . THR A 149 ? 0.1972 0.3189 0.4229 0.0245  0.0237  -0.0353 290 THR A N     
1116 C CA    . THR A 149 ? 0.2360 0.3582 0.4762 0.0269  0.0196  -0.0314 290 THR A CA    
1117 C C     . THR A 149 ? 0.2176 0.3396 0.4716 0.0289  0.0218  -0.0375 290 THR A C     
1118 O O     . THR A 149 ? 0.1710 0.2944 0.4388 0.0311  0.0188  -0.0346 290 THR A O     
1119 C CB    . THR A 149 ? 0.2550 0.3702 0.4956 0.0283  0.0147  -0.0250 290 THR A CB    
1120 O OG1   . THR A 149 ? 0.2565 0.3648 0.4965 0.0292  0.0166  -0.0294 290 THR A OG1   
1121 C CG2   . THR A 149 ? 0.2245 0.3402 0.4526 0.0265  0.0124  -0.0188 290 THR A CG2   
1122 N N     . GLY A 150 ? 0.1855 0.3059 0.4369 0.0283  0.0266  -0.0458 291 GLY A N     
1123 C CA    . GLY A 150 ? 0.1767 0.2960 0.4416 0.0301  0.0288  -0.0525 291 GLY A CA    
1124 C C     . GLY A 150 ? 0.2241 0.3348 0.4965 0.0321  0.0264  -0.0521 291 GLY A C     
1125 O O     . GLY A 150 ? 0.1909 0.2998 0.4761 0.0336  0.0281  -0.0580 291 GLY A O     
1126 N N     . ALA A 151 ? 0.2315 0.3368 0.4970 0.0320  0.0227  -0.0456 292 ALA A N     
1127 C CA    . ALA A 151 ? 0.2426 0.3398 0.5151 0.0332  0.0205  -0.0450 292 ALA A CA    
1128 C C     . ALA A 151 ? 0.2086 0.3031 0.4794 0.0321  0.0250  -0.0546 292 ALA A C     
1129 O O     . ALA A 151 ? 0.2004 0.2983 0.4596 0.0299  0.0290  -0.0596 292 ALA A O     
1130 C CB    . ALA A 151 ? 0.2677 0.3610 0.5310 0.0327  0.0164  -0.0366 292 ALA A CB    
1131 N N     . VAL A 152 ? 0.2520 0.3405 0.5352 0.0332  0.0243  -0.0572 293 VAL A N     
1132 C CA    . VAL A 152 ? 0.2358 0.3219 0.5200 0.0318  0.0282  -0.0667 293 VAL A CA    
1133 C C     . VAL A 152 ? 0.2584 0.3389 0.5359 0.0308  0.0263  -0.0640 293 VAL A C     
1134 O O     . VAL A 152 ? 0.2326 0.3083 0.5160 0.0320  0.0218  -0.0567 293 VAL A O     
1135 C CB    . VAL A 152 ? 0.2793 0.3630 0.5836 0.0334  0.0293  -0.0728 293 VAL A CB    
1136 C CG1   . VAL A 152 ? 0.2634 0.3457 0.5685 0.0313  0.0337  -0.0838 293 VAL A CG1   
1137 C CG2   . VAL A 152 ? 0.2731 0.3636 0.5850 0.0349  0.0311  -0.0749 293 VAL A CG2   
1138 N N     . LEU A 153 ? 0.2644 0.3462 0.5299 0.0284  0.0295  -0.0695 294 LEU A N     
1139 C CA    . LEU A 153 ? 0.2265 0.3045 0.4855 0.0274  0.0282  -0.0679 294 LEU A CA    
1140 C C     . LEU A 153 ? 0.2253 0.2998 0.4952 0.0264  0.0302  -0.0765 294 LEU A C     
1141 O O     . LEU A 153 ? 0.2412 0.3189 0.5107 0.0246  0.0346  -0.0863 294 LEU A O     
1142 C CB    . LEU A 153 ? 0.2685 0.3507 0.5079 0.0255  0.0301  -0.0682 294 LEU A CB    
1143 C CG    . LEU A 153 ? 0.2549 0.3350 0.4861 0.0246  0.0288  -0.0662 294 LEU A CG    
1144 C CD1   . LEU A 153 ? 0.2298 0.3063 0.4623 0.0262  0.0238  -0.0557 294 LEU A CD1   
1145 C CD2   . LEU A 153 ? 0.2589 0.3440 0.4720 0.0230  0.0311  -0.0672 294 LEU A CD2   
1146 N N     . LYS A 154 ? 0.1960 0.2642 0.4762 0.0271  0.0270  -0.0731 295 LYS A N     
1147 C CA    . LYS A 154 ? 0.2453 0.3097 0.5371 0.0258  0.0284  -0.0808 295 LYS A CA    
1148 C C     . LYS A 154 ? 0.2341 0.2972 0.5174 0.0241  0.0275  -0.0794 295 LYS A C     
1149 O O     . LYS A 154 ? 0.1920 0.2545 0.4674 0.0248  0.0241  -0.0700 295 LYS A O     
1150 C CB    . LYS A 154 ? 0.2102 0.2681 0.5231 0.0277  0.0255  -0.0782 295 LYS A CB    
1151 C CG    . LYS A 154 ? 0.3059 0.3653 0.6292 0.0301  0.0255  -0.0778 295 LYS A CG    
1152 C CD    . LYS A 154 ? 0.3173 0.3825 0.6389 0.0291  0.0312  -0.0889 295 LYS A CD    
1153 C CE    . LYS A 154 ? 0.4479 0.5114 0.7904 0.0305  0.0328  -0.0955 295 LYS A CE    
1154 N NZ    . LYS A 154 ? 0.4494 0.5115 0.8043 0.0340  0.0290  -0.0876 295 LYS A NZ    
1155 N N     . VAL A 155 ? 0.2326 0.2960 0.5184 0.0217  0.0306  -0.0891 296 VAL A N     
1156 C CA    . VAL A 155 ? 0.2133 0.2775 0.4911 0.0198  0.0304  -0.0897 296 VAL A CA    
1157 C C     . VAL A 155 ? 0.2338 0.2925 0.5288 0.0187  0.0300  -0.0941 296 VAL A C     
1158 O O     . VAL A 155 ? 0.2084 0.2672 0.5132 0.0170  0.0333  -0.1048 296 VAL A O     
1159 C CB    . VAL A 155 ? 0.2278 0.2992 0.4906 0.0172  0.0345  -0.0975 296 VAL A CB    
1160 C CG1   . VAL A 155 ? 0.2380 0.3113 0.4925 0.0155  0.0340  -0.0975 296 VAL A CG1   
1161 C CG2   . VAL A 155 ? 0.2389 0.3152 0.4867 0.0181  0.0351  -0.0933 296 VAL A CG2   
1162 N N     . ALA A 156 ? 0.1949 0.2494 0.4941 0.0193  0.0260  -0.0862 297 ALA A N     
1163 C CA    . ALA A 156 ? 0.1854 0.2344 0.5021 0.0181  0.0253  -0.0894 297 ALA A CA    
1164 C C     . ALA A 156 ? 0.2384 0.2916 0.5502 0.0148  0.0285  -0.0992 297 ALA A C     
1165 O O     . ALA A 156 ? 0.1941 0.2531 0.4893 0.0141  0.0286  -0.0971 297 ALA A O     
1166 C CB    . ALA A 156 ? 0.1822 0.2265 0.5037 0.0192  0.0199  -0.0772 297 ALA A CB    
1167 N N     . PRO A 157 ? 0.2694 0.3205 0.5954 0.0125  0.0312  -0.1099 298 PRO A N     
1168 C CA    . PRO A 157 ? 0.2361 0.2928 0.5568 0.0088  0.0348  -0.1209 298 PRO A CA    
1169 C C     . PRO A 157 ? 0.2396 0.2952 0.5656 0.0072  0.0331  -0.1197 298 PRO A C     
1170 O O     . PRO A 157 ? 0.2242 0.2733 0.5620 0.0087  0.0292  -0.1114 298 PRO A O     
1171 C CB    . PRO A 157 ? 0.2741 0.3298 0.6088 0.0068  0.0388  -0.1333 298 PRO A CB    
1172 C CG    . PRO A 157 ? 0.2190 0.2660 0.5731 0.0096  0.0360  -0.1277 298 PRO A CG    
1173 C CD    . PRO A 157 ? 0.2417 0.2869 0.5882 0.0133  0.0315  -0.1134 298 PRO A CD    
1174 N N     . VAL A 158 ? 0.2180 0.2811 0.5348 0.0039  0.0359  -0.1280 299 VAL A N     
1175 C CA    . VAL A 158 ? 0.2489 0.3140 0.5705 0.0017  0.0351  -0.1293 299 VAL A CA    
1176 C C     . VAL A 158 ? 0.2770 0.3437 0.6071 -0.0029 0.0396  -0.1453 299 VAL A C     
1177 O O     . VAL A 158 ? 0.2460 0.3160 0.5712 -0.0048 0.0434  -0.1545 299 VAL A O     
1178 C CB    . VAL A 158 ? 0.2458 0.3214 0.5471 0.0012  0.0339  -0.1236 299 VAL A CB    
1179 C CG1   . VAL A 158 ? 0.1729 0.2468 0.4655 0.0051  0.0294  -0.1077 299 VAL A CG1   
1180 C CG2   . VAL A 158 ? 0.2395 0.3241 0.5230 -0.0007 0.0376  -0.1315 299 VAL A CG2   
1181 N N     . ASP A 159 ? 0.2417 0.3066 0.5845 -0.0051 0.0393  -0.1486 300 ASP A N     
1182 C CA    . ASP A 159 ? 0.2829 0.3502 0.6282 -0.0104 0.0435  -0.1643 300 ASP A CA    
1183 C C     . ASP A 159 ? 0.3156 0.3971 0.6380 -0.0145 0.0442  -0.1661 300 ASP A C     
1184 O O     . ASP A 159 ? 0.2699 0.3591 0.5776 -0.0123 0.0418  -0.1560 300 ASP A O     
1185 C CB    . ASP A 159 ? 0.2157 0.2723 0.5751 -0.0144 0.0411  -0.1648 300 ASP A CB    
1186 C CG    . ASP A 159 ? 0.3684 0.4281 0.7181 -0.0177 0.0351  -0.1515 300 ASP A CG    
1187 O OD1   . ASP A 159 ? 0.3369 0.4091 0.6675 -0.0202 0.0345  -0.1496 300 ASP A OD1   
1188 O OD2   . ASP A 159 ? 0.4052 0.4553 0.7666 -0.0173 0.0309  -0.1418 300 ASP A OD2   
1189 N N     . ASP A 160 ? 0.3017 0.3868 0.6206 -0.0211 0.0468  -0.1786 301 ASP A N     
1190 C CA    . ASP A 160 ? 0.2934 0.3929 0.5902 -0.0253 0.0472  -0.1809 301 ASP A CA    
1191 C C     . ASP A 160 ? 0.2632 0.3681 0.5495 -0.0276 0.0414  -0.1689 301 ASP A C     
1192 O O     . ASP A 160 ? 0.2275 0.3447 0.4954 -0.0289 0.0405  -0.1664 301 ASP A O     
1193 C CB    . ASP A 160 ? 0.3519 0.4551 0.6471 -0.0322 0.0517  -0.1980 301 ASP A CB    
1194 C CG    . ASP A 160 ? 0.3997 0.4995 0.7052 -0.0307 0.0568  -0.2064 301 ASP A CG    
1195 O OD1   . ASP A 160 ? 0.3771 0.4846 0.6717 -0.0301 0.0590  -0.2069 301 ASP A OD1   
1196 O OD2   . ASP A 160 ? 0.4450 0.5349 0.7681 -0.0305 0.0573  -0.2081 301 ASP A OD2   
1197 N N     . ALA A 161 ? 0.2557 0.3521 0.5534 -0.0282 0.0375  -0.1615 302 ALA A N     
1198 C CA    . ALA A 161 ? 0.3009 0.4026 0.5902 -0.0297 0.0322  -0.1488 302 ALA A CA    
1199 C C     . ALA A 161 ? 0.2432 0.3464 0.5267 -0.0230 0.0295  -0.1344 302 ALA A C     
1200 O O     . ALA A 161 ? 0.2321 0.3424 0.5053 -0.0233 0.0259  -0.1245 302 ALA A O     
1201 C CB    . ALA A 161 ? 0.2843 0.3766 0.5878 -0.0339 0.0292  -0.1462 302 ALA A CB    
1202 N N     . GLY A 162 ? 0.2602 0.3575 0.5499 -0.0170 0.0313  -0.1333 303 GLY A N     
1203 C CA    . GLY A 162 ? 0.2061 0.3045 0.4902 -0.0112 0.0290  -0.1206 303 GLY A CA    
1204 C C     . GLY A 162 ? 0.2375 0.3258 0.5352 -0.0085 0.0254  -0.1098 303 GLY A C     
1205 O O     . GLY A 162 ? 0.1762 0.2660 0.4683 -0.0045 0.0230  -0.0985 303 GLY A O     
1206 N N     . ASN A 163 ? 0.2029 0.2807 0.5179 -0.0108 0.0248  -0.1128 304 ASN A N     
1207 C CA    . ASN A 163 ? 0.2629 0.3302 0.5922 -0.0083 0.0212  -0.1023 304 ASN A CA    
1208 C C     . ASN A 163 ? 0.2748 0.3371 0.6136 -0.0018 0.0228  -0.1027 304 ASN A C     
1209 O O     . ASN A 163 ? 0.2536 0.3143 0.5990 -0.0006 0.0273  -0.1149 304 ASN A O     
1210 C CB    . ASN A 163 ? 0.2545 0.3108 0.6009 -0.0127 0.0200  -0.1054 304 ASN A CB    
1211 C CG    . ASN A 163 ? 0.2791 0.3404 0.6183 -0.0201 0.0184  -0.1058 304 ASN A CG    
1212 O OD1   . ASN A 163 ? 0.3059 0.3695 0.6408 -0.0219 0.0144  -0.0941 304 ASN A OD1   
1213 N ND2   . ASN A 163 ? 0.2563 0.3194 0.5950 -0.0248 0.0217  -0.1196 304 ASN A ND2   
1214 N N     . LEU A 164 ? 0.2650 0.3252 0.6052 0.0021  0.0191  -0.0896 305 LEU A N     
1215 C CA    . LEU A 164 ? 0.2755 0.3265 0.6216 0.0068  0.0188  -0.0872 305 LEU A CA    
1216 C C     . LEU A 164 ? 0.2953 0.3347 0.6675 0.0068  0.0186  -0.0913 305 LEU A C     
1217 O O     . LEU A 164 ? 0.2939 0.3281 0.6780 0.0046  0.0152  -0.0858 305 LEU A O     
1218 C CB    . LEU A 164 ? 0.2604 0.3104 0.5979 0.0094  0.0141  -0.0714 305 LEU A CB    
1219 C CG    . LEU A 164 ? 0.2883 0.3314 0.6276 0.0128  0.0132  -0.0676 305 LEU A CG    
1220 C CD1   . LEU A 164 ? 0.2311 0.2788 0.5546 0.0138  0.0172  -0.0747 305 LEU A CD1   
1221 C CD2   . LEU A 164 ? 0.2960 0.3382 0.6303 0.0144  0.0082  -0.0521 305 LEU A CD2   
1222 N N     . LEU A 165 ? 0.2856 0.3201 0.6621 0.0077  0.0214  -0.0995 306 LEU A N     
1223 C CA    . LEU A 165 ? 0.3168 0.3411 0.7154 0.0074  0.0211  -0.1030 306 LEU A CA    
1224 C C     . LEU A 165 ? 0.3531 0.3711 0.7588 0.0106  0.0162  -0.0897 306 LEU A C     
1225 O O     . LEU A 165 ? 0.3305 0.3503 0.7299 0.0128  0.0167  -0.0883 306 LEU A O     
1226 C CB    . LEU A 165 ? 0.3283 0.3550 0.7276 0.0060  0.0266  -0.1174 306 LEU A CB    
1227 C CG    . LEU A 165 ? 0.3383 0.3725 0.7288 0.0020  0.0317  -0.1314 306 LEU A CG    
1228 C CD1   . LEU A 165 ? 0.3116 0.3508 0.6981 0.0009  0.0369  -0.1431 306 LEU A CD1   
1229 C CD2   . LEU A 165 ? 0.3186 0.3471 0.7222 -0.0014 0.0317  -0.1365 306 LEU A CD2   
1230 N N     . LEU A 166 ? 0.3291 0.3402 0.7482 0.0104  0.0113  -0.0797 307 LEU A N     
1231 C CA    . LEU A 166 ? 0.3312 0.3378 0.7553 0.0127  0.0059  -0.0653 307 LEU A CA    
1232 C C     . LEU A 166 ? 0.3314 0.3338 0.7685 0.0145  0.0063  -0.0681 307 LEU A C     
1233 O O     . LEU A 166 ? 0.3256 0.3278 0.7615 0.0169  0.0034  -0.0597 307 LEU A O     
1234 C CB    . LEU A 166 ? 0.3656 0.3660 0.8011 0.0112  0.0004  -0.0539 307 LEU A CB    
1235 C CG    . LEU A 166 ? 0.4103 0.4167 0.8330 0.0112  -0.0029 -0.0420 307 LEU A CG    
1236 C CD1   . LEU A 166 ? 0.4115 0.4102 0.8477 0.0094  -0.0092 -0.0285 307 LEU A CD1   
1237 C CD2   . LEU A 166 ? 0.3396 0.3520 0.7437 0.0136  -0.0037 -0.0351 307 LEU A CD2   
1238 N N     . GLY A 167 ? 0.3494 0.3495 0.7987 0.0134  0.0099  -0.0801 308 GLY A N     
1239 C CA    . GLY A 167 ? 0.3616 0.3587 0.8244 0.0156  0.0106  -0.0832 308 GLY A CA    
1240 C C     . GLY A 167 ? 0.3579 0.3615 0.8095 0.0174  0.0143  -0.0889 308 GLY A C     
1241 O O     . GLY A 167 ? 0.3351 0.3379 0.7911 0.0203  0.0124  -0.0837 308 GLY A O     
1242 N N     . GLU A 168 ? 0.3260 0.3367 0.7629 0.0155  0.0194  -0.0996 309 GLU A N     
1243 C CA    . GLU A 168 ? 0.3891 0.4064 0.8128 0.0168  0.0227  -0.1040 309 GLU A CA    
1244 C C     . GLU A 168 ? 0.3360 0.3552 0.7460 0.0192  0.0189  -0.0912 309 GLU A C     
1245 O O     . GLU A 168 ? 0.3348 0.3563 0.7420 0.0216  0.0193  -0.0899 309 GLU A O     
1246 C CB    . GLU A 168 ? 0.3375 0.3624 0.7466 0.0138  0.0282  -0.1163 309 GLU A CB    
1247 C CG    . GLU A 168 ? 0.4193 0.4451 0.8395 0.0116  0.0335  -0.1311 309 GLU A CG    
1248 C CD    . GLU A 168 ? 0.5584 0.5818 0.9860 0.0083  0.0343  -0.1368 309 GLU A CD    
1249 O OE1   . GLU A 168 ? 0.5884 0.6166 1.0137 0.0050  0.0395  -0.1501 309 GLU A OE1   
1250 O OE2   . GLU A 168 ? 0.5560 0.5731 0.9910 0.0086  0.0298  -0.1279 309 GLU A OE2   
1251 N N     . PHE A 169 ? 0.3076 0.3262 0.7095 0.0186  0.0154  -0.0817 310 PHE A N     
1252 C CA    . PHE A 169 ? 0.3179 0.3387 0.7065 0.0206  0.0118  -0.0694 310 PHE A CA    
1253 C C     . PHE A 169 ? 0.3155 0.3315 0.7172 0.0230  0.0074  -0.0600 310 PHE A C     
1254 O O     . PHE A 169 ? 0.3236 0.3427 0.7182 0.0251  0.0068  -0.0561 310 PHE A O     
1255 C CB    . PHE A 169 ? 0.2795 0.3013 0.6586 0.0194  0.0089  -0.0609 310 PHE A CB    
1256 C CG    . PHE A 169 ? 0.2722 0.2951 0.6419 0.0210  0.0043  -0.0467 310 PHE A CG    
1257 C CD1   . PHE A 169 ? 0.2603 0.2895 0.6108 0.0224  0.0056  -0.0453 310 PHE A CD1   
1258 C CD2   . PHE A 169 ? 0.2695 0.2873 0.6498 0.0207  -0.0013 -0.0346 310 PHE A CD2   
1259 C CE1   . PHE A 169 ? 0.2559 0.2867 0.5980 0.0235  0.0017  -0.0332 310 PHE A CE1   
1260 C CE2   . PHE A 169 ? 0.2295 0.2494 0.6008 0.0216  -0.0054 -0.0219 310 PHE A CE2   
1261 C CZ    . PHE A 169 ? 0.2289 0.2554 0.5811 0.0230  -0.0038 -0.0217 310 PHE A CZ    
1262 N N     . GLU A 170 ? 0.3095 0.3185 0.7308 0.0225  0.0041  -0.0562 311 GLU A N     
1263 C CA    . GLU A 170 ? 0.3268 0.3317 0.7618 0.0246  -0.0003 -0.0473 311 GLU A CA    
1264 C C     . GLU A 170 ? 0.3311 0.3375 0.7732 0.0271  0.0029  -0.0554 311 GLU A C     
1265 O O     . GLU A 170 ? 0.2972 0.3043 0.7416 0.0296  0.0003  -0.0488 311 GLU A O     
1266 C CB    . GLU A 170 ? 0.3658 0.3629 0.8207 0.0234  -0.0043 -0.0421 311 GLU A CB    
1267 C CG    . GLU A 170 ? 0.3772 0.3703 0.8460 0.0253  -0.0100 -0.0308 311 GLU A CG    
1268 C CD    . GLU A 170 ? 0.4610 0.4468 0.9460 0.0236  -0.0150 -0.0227 311 GLU A CD    
1269 O OE1   . GLU A 170 ? 0.4474 0.4306 0.9360 0.0213  -0.0133 -0.0280 311 GLU A OE1   
1270 O OE2   . GLU A 170 ? 0.5044 0.4875 0.9985 0.0244  -0.0207 -0.0108 311 GLU A OE2   
1271 N N     . ASP A 171 ? 0.3071 0.3149 0.7523 0.0263  0.0087  -0.0698 312 ASP A N     
1272 C CA    . ASP A 171 ? 0.3396 0.3497 0.7916 0.0285  0.0123  -0.0782 312 ASP A CA    
1273 C C     . ASP A 171 ? 0.3040 0.3213 0.7388 0.0300  0.0137  -0.0774 312 ASP A C     
1274 O O     . ASP A 171 ? 0.3263 0.3456 0.7674 0.0326  0.0147  -0.0792 312 ASP A O     
1275 C CB    . ASP A 171 ? 0.3113 0.3227 0.7677 0.0266  0.0185  -0.0941 312 ASP A CB    
1276 C CG    . ASP A 171 ? 0.4367 0.4408 0.9152 0.0264  0.0178  -0.0970 312 ASP A CG    
1277 O OD1   . ASP A 171 ? 0.4744 0.4722 0.9649 0.0277  0.0121  -0.0859 312 ASP A OD1   
1278 O OD2   . ASP A 171 ? 0.4392 0.4442 0.9225 0.0247  0.0229  -0.1101 312 ASP A OD2   
1279 N N     . LEU A 172 ? 0.2977 0.3194 0.7112 0.0284  0.0142  -0.0751 313 LEU A N     
1280 C CA    . LEU A 172 ? 0.3010 0.3294 0.6982 0.0298  0.0153  -0.0732 313 LEU A CA    
1281 C C     . LEU A 172 ? 0.2388 0.2666 0.6362 0.0321  0.0099  -0.0597 313 LEU A C     
1282 O O     . LEU A 172 ? 0.2411 0.2743 0.6291 0.0336  0.0105  -0.0583 313 LEU A O     
1283 C CB    . LEU A 172 ? 0.3033 0.3369 0.6776 0.0277  0.0174  -0.0748 313 LEU A CB    
1284 C CG    . LEU A 172 ? 0.2976 0.3344 0.6672 0.0250  0.0231  -0.0884 313 LEU A CG    
1285 C CD1   . LEU A 172 ? 0.2402 0.2822 0.5874 0.0232  0.0241  -0.0876 313 LEU A CD1   
1286 C CD2   . LEU A 172 ? 0.2647 0.3058 0.6374 0.0255  0.0277  -0.0984 313 LEU A CD2   
1287 N N     . LEU A 173 ? 0.2540 0.2760 0.6613 0.0321  0.0045  -0.0497 314 LEU A N     
1288 C CA    . LEU A 173 ? 0.2749 0.2973 0.6814 0.0335  -0.0010 -0.0364 314 LEU A CA    
1289 C C     . LEU A 173 ? 0.3193 0.3403 0.7440 0.0364  -0.0025 -0.0355 314 LEU A C     
1290 O O     . LEU A 173 ? 0.2536 0.2699 0.6970 0.0371  -0.0019 -0.0404 314 LEU A O     
1291 C CB    . LEU A 173 ? 0.2992 0.3168 0.7079 0.0316  -0.0064 -0.0251 314 LEU A CB    
1292 C CG    . LEU A 173 ? 0.2472 0.2662 0.6404 0.0290  -0.0052 -0.0253 314 LEU A CG    
1293 C CD1   . LEU A 173 ? 0.2371 0.2520 0.6349 0.0271  -0.0108 -0.0133 314 LEU A CD1   
1294 C CD2   . LEU A 173 ? 0.1512 0.1777 0.5213 0.0294  -0.0033 -0.0249 314 LEU A CD2   
1295 N N     . GLY A 174 ? 0.3161 0.3417 0.7356 0.0383  -0.0044 -0.0294 315 GLY A N     
1296 C CA    . GLY A 174 ? 0.2707 0.2966 0.7068 0.0415  -0.0062 -0.0278 315 GLY A CA    
1297 C C     . GLY A 174 ? 0.2994 0.3299 0.7296 0.0427  -0.0105 -0.0169 315 GLY A C     
1298 O O     . GLY A 174 ? 0.3251 0.3574 0.7402 0.0407  -0.0131 -0.0087 315 GLY A O     
1299 N N     . PRO A 175 ? 0.3062 0.3394 0.7486 0.0459  -0.0112 -0.0168 316 PRO A N     
1300 C CA    . PRO A 175 ? 0.3353 0.3738 0.7740 0.0469  -0.0156 -0.0065 316 PRO A CA    
1301 C C     . PRO A 175 ? 0.3355 0.3822 0.7527 0.0461  -0.0131 -0.0078 316 PRO A C     
1302 O O     . PRO A 175 ? 0.3723 0.4230 0.7817 0.0455  -0.0171 0.0018  316 PRO A O     
1303 C CB    . PRO A 175 ? 0.3378 0.3778 0.7968 0.0510  -0.0160 -0.0086 316 PRO A CB    
1304 C CG    . PRO A 175 ? 0.3709 0.4100 0.8361 0.0520  -0.0092 -0.0234 316 PRO A CG    
1305 C CD    . PRO A 175 ? 0.3601 0.3926 0.8202 0.0487  -0.0076 -0.0270 316 PRO A CD    
1306 N N     . ARG A 176 ? 0.2993 0.3488 0.7065 0.0456  -0.0067 -0.0190 317 ARG A N     
1307 C CA    . ARG A 176 ? 0.3085 0.3656 0.6958 0.0446  -0.0041 -0.0207 317 ARG A CA    
1308 C C     . ARG A 176 ? 0.3191 0.3751 0.6871 0.0415  -0.0040 -0.0182 317 ARG A C     
1309 O O     . ARG A 176 ? 0.2814 0.3433 0.6324 0.0405  -0.0022 -0.0188 317 ARG A O     
1310 C CB    . ARG A 176 ? 0.3205 0.3822 0.7073 0.0454  0.0027  -0.0338 317 ARG A CB    
1311 C CG    . ARG A 176 ? 0.3727 0.4386 0.7760 0.0487  0.0035  -0.0369 317 ARG A CG    
1312 C CD    . ARG A 176 ? 0.3945 0.4645 0.8020 0.0504  -0.0021 -0.0257 317 ARG A CD    
1313 N NE    . ARG A 176 ? 0.4238 0.5022 0.8139 0.0491  -0.0016 -0.0233 317 ARG A NE    
1314 C CZ    . ARG A 176 ? 0.4117 0.4981 0.7967 0.0493  0.0031  -0.0305 317 ARG A CZ    
1315 N NH1   . ARG A 176 ? 0.3983 0.4861 0.7939 0.0509  0.0079  -0.0407 317 ARG A NH1   
1316 N NH2   . ARG A 176 ? 0.3621 0.4554 0.7314 0.0476  0.0031  -0.0274 317 ARG A NH2   
1317 N N     . THR A 177 ? 0.2789 0.3279 0.6496 0.0399  -0.0059 -0.0155 318 THR A N     
1318 C CA    . THR A 177 ? 0.2476 0.2961 0.6014 0.0373  -0.0057 -0.0136 318 THR A CA    
1319 C C     . THR A 177 ? 0.2231 0.2746 0.5664 0.0363  -0.0104 -0.0018 318 THR A C     
1320 O O     . THR A 177 ? 0.2839 0.3323 0.6358 0.0359  -0.0157 0.0079  318 THR A O     
1321 C CB    . THR A 177 ? 0.2722 0.3131 0.6341 0.0358  -0.0065 -0.0139 318 THR A CB    
1322 O OG1   . THR A 177 ? 0.2193 0.2574 0.5931 0.0364  -0.0024 -0.0252 318 THR A OG1   
1323 C CG2   . THR A 177 ? 0.2008 0.2424 0.5451 0.0334  -0.0055 -0.0132 318 THR A CG2   
1324 N N     . LYS A 178 ? 0.1959 0.2533 0.5206 0.0355  -0.0085 -0.0024 319 LYS A N     
1325 C CA    . LYS A 178 ? 0.1990 0.2597 0.5128 0.0341  -0.0125 0.0078  319 LYS A CA    
1326 C C     . LYS A 178 ? 0.2230 0.2830 0.5220 0.0318  -0.0124 0.0100  319 LYS A C     
1327 O O     . LYS A 178 ? 0.2449 0.3057 0.5389 0.0302  -0.0165 0.0195  319 LYS A O     
1328 C CB    . LYS A 178 ? 0.2091 0.2778 0.5143 0.0346  -0.0114 0.0070  319 LYS A CB    
1329 C CG    . LYS A 178 ? 0.3012 0.3725 0.6199 0.0362  -0.0147 0.0114  319 LYS A CG    
1330 C CD    . LYS A 178 ? 0.3879 0.4583 0.7218 0.0388  -0.0116 0.0031  319 LYS A CD    
1331 C CE    . LYS A 178 ? 0.4472 0.5218 0.7944 0.0409  -0.0145 0.0067  319 LYS A CE    
1332 N NZ    . LYS A 178 ? 0.4831 0.5562 0.8473 0.0438  -0.0114 -0.0016 319 LYS A NZ    
1333 N N     . LEU A 179 ? 0.2141 0.2733 0.5063 0.0316  -0.0078 0.0017  320 LEU A N     
1334 C CA    . LEU A 179 ? 0.1691 0.2292 0.4469 0.0299  -0.0073 0.0033  320 LEU A CA    
1335 C C     . LEU A 179 ? 0.2196 0.2761 0.4998 0.0295  -0.0041 -0.0044 320 LEU A C     
1336 O O     . LEU A 179 ? 0.2096 0.2660 0.4930 0.0302  0.0000  -0.0140 320 LEU A O     
1337 C CB    . LEU A 179 ? 0.2023 0.2690 0.4622 0.0296  -0.0050 0.0016  320 LEU A CB    
1338 C CG    . LEU A 179 ? 0.2585 0.3270 0.5028 0.0283  -0.0040 0.0026  320 LEU A CG    
1339 C CD1   . LEU A 179 ? 0.1964 0.2648 0.4391 0.0268  -0.0087 0.0130  320 LEU A CD1   
1340 C CD2   . LEU A 179 ? 0.2651 0.3394 0.4952 0.0284  -0.0013 -0.0004 320 LEU A CD2   
1341 N N     . VAL A 180 ? 0.1624 0.2165 0.4416 0.0280  -0.0059 -0.0003 321 VAL A N     
1342 C CA    . VAL A 180 ? 0.1600 0.2124 0.4388 0.0271  -0.0031 -0.0069 321 VAL A CA    
1343 C C     . VAL A 180 ? 0.2035 0.2610 0.4641 0.0262  -0.0023 -0.0049 321 VAL A C     
1344 O O     . VAL A 180 ? 0.1784 0.2377 0.4338 0.0253  -0.0056 0.0041  321 VAL A O     
1345 C CB    . VAL A 180 ? 0.1966 0.2426 0.4922 0.0261  -0.0059 -0.0038 321 VAL A CB    
1346 C CG1   . VAL A 180 ? 0.1856 0.2310 0.4805 0.0248  -0.0031 -0.0106 321 VAL A CG1   
1347 C CG2   . VAL A 180 ? 0.1846 0.2253 0.4998 0.0272  -0.0067 -0.0060 321 VAL A CG2   
1348 N N     . ALA A 181 ? 0.1661 0.2266 0.4169 0.0262  0.0020  -0.0131 322 ALA A N     
1349 C CA    . ALA A 181 ? 0.1598 0.2253 0.3946 0.0255  0.0029  -0.0120 322 ALA A CA    
1350 C C     . ALA A 181 ? 0.1696 0.2349 0.4061 0.0244  0.0052  -0.0184 322 ALA A C     
1351 O O     . ALA A 181 ? 0.1793 0.2450 0.4162 0.0244  0.0088  -0.0276 322 ALA A O     
1352 C CB    . ALA A 181 ? 0.1499 0.2204 0.3698 0.0263  0.0056  -0.0147 322 ALA A CB    
1353 N N     . ALA A 182 ? 0.1791 0.2449 0.4168 0.0232  0.0031  -0.0137 323 ALA A N     
1354 C CA    . ALA A 182 ? 0.1907 0.2567 0.4334 0.0218  0.0047  -0.0195 323 ALA A CA    
1355 C C     . ALA A 182 ? 0.2108 0.2833 0.4416 0.0208  0.0045  -0.0164 323 ALA A C     
1356 O O     . ALA A 182 ? 0.2212 0.2958 0.4471 0.0206  0.0019  -0.0077 323 ALA A O     
1357 C CB    . ALA A 182 ? 0.1835 0.2432 0.4464 0.0206  0.0022  -0.0177 323 ALA A CB    
1358 N N     . THR A 183 ? 0.1830 0.2595 0.4093 0.0200  0.0074  -0.0237 324 THR A N     
1359 C CA    . THR A 183 ? 0.1734 0.2568 0.3904 0.0190  0.0071  -0.0211 324 THR A CA    
1360 C C     . THR A 183 ? 0.1346 0.2175 0.3644 0.0164  0.0048  -0.0178 324 THR A C     
1361 O O     . THR A 183 ? 0.1653 0.2431 0.4110 0.0151  0.0046  -0.0217 324 THR A O     
1362 C CB    . THR A 183 ? 0.1777 0.2666 0.3856 0.0188  0.0105  -0.0294 324 THR A CB    
1363 O OG1   . THR A 183 ? 0.2081 0.3044 0.4067 0.0184  0.0099  -0.0260 324 THR A OG1   
1364 C CG2   . THR A 183 ? 0.1989 0.2863 0.4191 0.0167  0.0122  -0.0386 324 THR A CG2   
1365 N N     . GLN A 184 ? 0.1391 0.2274 0.3628 0.0153  0.0029  -0.0105 325 GLN A N     
1366 C CA    . GLN A 184 ? 0.1383 0.2279 0.3729 0.0119  0.0008  -0.0072 325 GLN A CA    
1367 C C     . GLN A 184 ? 0.1540 0.2502 0.3872 0.0098  0.0029  -0.0141 325 GLN A C     
1368 O O     . GLN A 184 ? 0.1573 0.2527 0.4036 0.0063  0.0021  -0.0160 325 GLN A O     
1369 C CB    . GLN A 184 ? 0.1639 0.2575 0.3932 0.0107  -0.0019 0.0038  325 GLN A CB    
1370 C CG    . GLN A 184 ? 0.1720 0.2671 0.4129 0.0061  -0.0044 0.0088  325 GLN A CG    
1371 C CD    . GLN A 184 ? 0.1971 0.2946 0.4355 0.0043  -0.0074 0.0207  325 GLN A CD    
1372 O OE1   . GLN A 184 ? 0.1865 0.2869 0.4122 0.0065  -0.0072 0.0241  325 GLN A OE1   
1373 N NE2   . GLN A 184 ? 0.1750 0.2715 0.4254 -0.0003 -0.0104 0.0269  325 GLN A NE2   
1374 N N     . VAL A 185 ? 0.1213 0.2242 0.3391 0.0114  0.0051  -0.0176 326 VAL A N     
1375 C CA    . VAL A 185 ? 0.1349 0.2452 0.3501 0.0096  0.0068  -0.0242 326 VAL A CA    
1376 C C     . VAL A 185 ? 0.1571 0.2686 0.3614 0.0121  0.0097  -0.0314 326 VAL A C     
1377 O O     . VAL A 185 ? 0.1249 0.2376 0.3162 0.0152  0.0102  -0.0282 326 VAL A O     
1378 C CB    . VAL A 185 ? 0.1077 0.2279 0.3149 0.0086  0.0058  -0.0189 326 VAL A CB    
1379 C CG1   . VAL A 185 ? 0.1095 0.2383 0.3121 0.0072  0.0073  -0.0258 326 VAL A CG1   
1380 C CG2   . VAL A 185 ? 0.1156 0.2358 0.3336 0.0047  0.0031  -0.0119 326 VAL A CG2   
1381 N N     . SER A 186 ? 0.1631 0.2747 0.3730 0.0102  0.0117  -0.0412 327 SER A N     
1382 C CA    . SER A 186 ? 0.1593 0.2734 0.3592 0.0114  0.0146  -0.0484 327 SER A CA    
1383 C C     . SER A 186 ? 0.1591 0.2831 0.3447 0.0120  0.0145  -0.0470 327 SER A C     
1384 O O     . SER A 186 ? 0.1397 0.2710 0.3273 0.0094  0.0136  -0.0479 327 SER A O     
1385 C CB    . SER A 186 ? 0.1754 0.2886 0.3855 0.0084  0.0169  -0.0599 327 SER A CB    
1386 O OG    . SER A 186 ? 0.1698 0.2889 0.3691 0.0082  0.0194  -0.0670 327 SER A OG    
1387 N N     . ASN A 187 ? 0.1489 0.2734 0.3209 0.0153  0.0154  -0.0447 328 ASN A N     
1388 C CA    . ASN A 187 ? 0.1660 0.2990 0.3254 0.0166  0.0152  -0.0431 328 ASN A CA    
1389 C C     . ASN A 187 ? 0.1560 0.2960 0.3129 0.0142  0.0165  -0.0518 328 ASN A C     
1390 O O     . ASN A 187 ? 0.1716 0.3204 0.3206 0.0145  0.0156  -0.0509 328 ASN A O     
1391 C CB    . ASN A 187 ? 0.2048 0.3352 0.3516 0.0207  0.0157  -0.0382 328 ASN A CB    
1392 C CG    . ASN A 187 ? 0.1853 0.3123 0.3281 0.0208  0.0181  -0.0439 328 ASN A CG    
1393 O OD1   . ASN A 187 ? 0.2193 0.3402 0.3698 0.0198  0.0191  -0.0472 328 ASN A OD1   
1394 N ND2   . ASN A 187 ? 0.2068 0.3383 0.3379 0.0220  0.0190  -0.0453 328 ASN A ND2   
1395 N N     . ALA A 188 ? 0.1396 0.2769 0.3028 0.0118  0.0187  -0.0606 329 ALA A N     
1396 C CA    . ALA A 188 ? 0.1776 0.3229 0.3384 0.0086  0.0203  -0.0699 329 ALA A CA    
1397 C C     . ALA A 188 ? 0.1389 0.2884 0.3118 0.0037  0.0200  -0.0763 329 ALA A C     
1398 O O     . ALA A 188 ? 0.1434 0.3033 0.3125 0.0005  0.0199  -0.0813 329 ALA A O     
1399 C CB    . ALA A 188 ? 0.1599 0.3013 0.3192 0.0082  0.0237  -0.0773 329 ALA A CB    
1400 N N     . LEU A 189 ? 0.1493 0.2911 0.3367 0.0025  0.0197  -0.0761 330 LEU A N     
1401 C CA    . LEU A 189 ? 0.1382 0.2819 0.3390 -0.0028 0.0196  -0.0827 330 LEU A CA    
1402 C C     . LEU A 189 ? 0.1597 0.3038 0.3672 -0.0042 0.0163  -0.0750 330 LEU A C     
1403 O O     . LEU A 189 ? 0.1605 0.3075 0.3740 -0.0094 0.0154  -0.0787 330 LEU A O     
1404 C CB    . LEU A 189 ? 0.1608 0.2948 0.3764 -0.0039 0.0221  -0.0903 330 LEU A CB    
1405 C CG    . LEU A 189 ? 0.1945 0.3286 0.4067 -0.0042 0.0263  -0.1008 330 LEU A CG    
1406 C CD1   . LEU A 189 ? 0.1724 0.2989 0.4026 -0.0064 0.0289  -0.1105 330 LEU A CD1   
1407 C CD2   . LEU A 189 ? 0.1811 0.3278 0.3812 -0.0076 0.0271  -0.1068 330 LEU A CD2   
1408 N N     . GLY A 190 ? 0.1436 0.2840 0.3479 -0.0004 0.0144  -0.0640 331 GLY A N     
1409 C CA    . GLY A 190 ? 0.1267 0.2680 0.3372 -0.0022 0.0116  -0.0564 331 GLY A CA    
1410 C C     . GLY A 190 ? 0.1748 0.3059 0.4026 -0.0042 0.0108  -0.0553 331 GLY A C     
1411 O O     . GLY A 190 ? 0.1278 0.2590 0.3610 -0.0063 0.0084  -0.0479 331 GLY A O     
1412 N N     . THR A 191 ? 0.1650 0.2878 0.4019 -0.0038 0.0129  -0.0623 332 THR A N     
1413 C CA    . THR A 191 ? 0.1703 0.2824 0.4255 -0.0051 0.0119  -0.0614 332 THR A CA    
1414 C C     . THR A 191 ? 0.1928 0.3003 0.4487 -0.0026 0.0089  -0.0486 332 THR A C     
1415 O O     . THR A 191 ? 0.1428 0.2495 0.3875 0.0019  0.0090  -0.0436 332 THR A O     
1416 C CB    . THR A 191 ? 0.1725 0.2769 0.4353 -0.0030 0.0149  -0.0700 332 THR A CB    
1417 O OG1   . THR A 191 ? 0.1444 0.2527 0.4063 -0.0062 0.0180  -0.0827 332 THR A OG1   
1418 C CG2   . THR A 191 ? 0.1500 0.2424 0.4329 -0.0030 0.0136  -0.0681 332 THR A CG2   
1419 N N     . VAL A 192 ? 0.1540 0.2578 0.4215 -0.0062 0.0062  -0.0430 333 VAL A N     
1420 C CA    . VAL A 192 ? 0.1764 0.2753 0.4484 -0.0048 0.0032  -0.0313 333 VAL A CA    
1421 C C     . VAL A 192 ? 0.2149 0.3013 0.5037 -0.0034 0.0027  -0.0327 333 VAL A C     
1422 O O     . VAL A 192 ? 0.1997 0.2795 0.5012 -0.0064 0.0032  -0.0392 333 VAL A O     
1423 C CB    . VAL A 192 ? 0.2166 0.3180 0.4899 -0.0099 0.0002  -0.0230 333 VAL A CB    
1424 C CG1   . VAL A 192 ? 0.1941 0.2912 0.4705 -0.0089 -0.0030 -0.0106 333 VAL A CG1   
1425 C CG2   . VAL A 192 ? 0.1578 0.2727 0.4162 -0.0108 0.0009  -0.0224 333 VAL A CG2   
1426 N N     . THR A 193 ? 0.2353 0.3171 0.5216 0.0011  0.0017  -0.0265 334 THR A N     
1427 C CA    . THR A 193 ? 0.1822 0.2530 0.4856 0.0030  0.0010  -0.0276 334 THR A CA    
1428 C C     . THR A 193 ? 0.2182 0.2838 0.5333 0.0017  -0.0039 -0.0151 334 THR A C     
1429 O O     . THR A 193 ? 0.2399 0.3104 0.5450 0.0004  -0.0064 -0.0049 334 THR A O     
1430 C CB    . THR A 193 ? 0.2176 0.2856 0.5118 0.0082  0.0029  -0.0299 334 THR A CB    
1431 O OG1   . THR A 193 ? 0.1690 0.2396 0.4495 0.0100  0.0008  -0.0195 334 THR A OG1   
1432 C CG2   . THR A 193 ? 0.2033 0.2769 0.4854 0.0088  0.0075  -0.0413 334 THR A CG2   
1433 N N     . PRO A 194 ? 0.2268 0.2819 0.5626 0.0018  -0.0056 -0.0153 335 PRO A N     
1434 C CA    . PRO A 194 ? 0.2507 0.2993 0.5962 0.0000  -0.0110 -0.0021 335 PRO A CA    
1435 C C     . PRO A 194 ? 0.2540 0.3020 0.5962 0.0043  -0.0135 0.0067  335 PRO A C     
1436 O O     . PRO A 194 ? 0.2526 0.2920 0.6065 0.0074  -0.0148 0.0074  335 PRO A O     
1437 C CB    . PRO A 194 ? 0.2939 0.3296 0.6610 -0.0008 -0.0115 -0.0071 335 PRO A CB    
1438 C CG    . PRO A 194 ? 0.2822 0.3177 0.6528 0.0038  -0.0066 -0.0209 335 PRO A CG    
1439 C CD    . PRO A 194 ? 0.2280 0.2759 0.5780 0.0033  -0.0026 -0.0276 335 PRO A CD    
1440 N N     . VAL A 195 ? 0.2124 0.2684 0.5346 0.0041  -0.0139 0.0133  336 VAL A N     
1441 C CA    . VAL A 195 ? 0.2705 0.3257 0.5828 0.0075  -0.0151 0.0191  336 VAL A CA    
1442 C C     . VAL A 195 ? 0.2493 0.2982 0.5748 0.0067  -0.0208 0.0311  336 VAL A C     
1443 O O     . VAL A 195 ? 0.2514 0.2961 0.5768 0.0095  -0.0219 0.0334  336 VAL A O     
1444 C CB    . VAL A 195 ? 0.2533 0.3184 0.5424 0.0073  -0.0139 0.0223  336 VAL A CB    
1445 C CG1   . VAL A 195 ? 0.2325 0.3027 0.5085 0.0091  -0.0088 0.0108  336 VAL A CG1   
1446 C CG2   . VAL A 195 ? 0.3463 0.4177 0.6337 0.0025  -0.0163 0.0308  336 VAL A CG2   
1447 N N     . GLU A 196 ? 0.2318 0.2804 0.5684 0.0022  -0.0246 0.0395  337 GLU A N     
1448 C CA    . GLU A 196 ? 0.3063 0.3484 0.6574 0.0011  -0.0308 0.0520  337 GLU A CA    
1449 C C     . GLU A 196 ? 0.2486 0.2789 0.6175 0.0050  -0.0312 0.0473  337 GLU A C     
1450 O O     . GLU A 196 ? 0.2821 0.3082 0.6523 0.0065  -0.0340 0.0534  337 GLU A O     
1451 C CB    . GLU A 196 ? 0.3358 0.3760 0.6929 -0.0057 -0.0341 0.0600  337 GLU A CB    
1452 C CG    . GLU A 196 ? 0.3979 0.4490 0.7357 -0.0107 -0.0336 0.0656  337 GLU A CG    
1453 C CD    . GLU A 196 ? 0.4964 0.5548 0.8225 -0.0114 -0.0279 0.0540  337 GLU A CD    
1454 O OE1   . GLU A 196 ? 0.4830 0.5369 0.8167 -0.0101 -0.0249 0.0425  337 GLU A OE1   
1455 O OE2   . GLU A 196 ? 0.4880 0.5572 0.7974 -0.0133 -0.0265 0.0565  337 GLU A OE2   
1456 N N     . THR A 197 ? 0.2675 0.2933 0.6491 0.0060  -0.0279 0.0355  338 THR A N     
1457 C CA    . THR A 197 ? 0.2668 0.2816 0.6641 0.0090  -0.0272 0.0292  338 THR A CA    
1458 C C     . THR A 197 ? 0.2851 0.3020 0.6693 0.0125  -0.0237 0.0226  338 THR A C     
1459 O O     . THR A 197 ? 0.2758 0.2880 0.6677 0.0139  -0.0252 0.0241  338 THR A O     
1460 C CB    . THR A 197 ? 0.2910 0.3013 0.7029 0.0088  -0.0236 0.0164  338 THR A CB    
1461 O OG1   . THR A 197 ? 0.3248 0.3338 0.7368 0.0026  -0.0256 0.0212  338 THR A OG1   
1462 C CG2   . THR A 197 ? 0.2762 0.2752 0.7060 0.0101  -0.0237 0.0115  338 THR A CG2   
1463 N N     . ILE A 198 ? 0.2543 0.2792 0.6191 0.0135  -0.0191 0.0153  339 ILE A N     
1464 C CA    . ILE A 198 ? 0.2373 0.2647 0.5890 0.0164  -0.0159 0.0097  339 ILE A CA    
1465 C C     . ILE A 198 ? 0.2277 0.2562 0.5739 0.0169  -0.0199 0.0211  339 ILE A C     
1466 O O     . ILE A 198 ? 0.2583 0.2848 0.6074 0.0189  -0.0199 0.0198  339 ILE A O     
1467 C CB    . ILE A 198 ? 0.2417 0.2779 0.5726 0.0168  -0.0112 0.0024  339 ILE A CB    
1468 C CG1   . ILE A 198 ? 0.2291 0.2653 0.5660 0.0157  -0.0073 -0.0094 339 ILE A CG1   
1469 C CG2   . ILE A 198 ? 0.2178 0.2567 0.5356 0.0194  -0.0084 -0.0021 339 ILE A CG2   
1470 C CD1   . ILE A 198 ? 0.2840 0.3295 0.6013 0.0153  -0.0034 -0.0156 339 ILE A CD1   
1471 N N     . VAL A 199 ? 0.2109 0.2436 0.5491 0.0146  -0.0234 0.0323  340 VAL A N     
1472 C CA    . VAL A 199 ? 0.2584 0.2932 0.5899 0.0143  -0.0273 0.0431  340 VAL A CA    
1473 C C     . VAL A 199 ? 0.2712 0.2989 0.6217 0.0138  -0.0321 0.0501  340 VAL A C     
1474 O O     . VAL A 199 ? 0.2719 0.2999 0.6220 0.0151  -0.0335 0.0527  340 VAL A O     
1475 C CB    . VAL A 199 ? 0.2535 0.2954 0.5727 0.0112  -0.0297 0.0530  340 VAL A CB    
1476 C CG1   . VAL A 199 ? 0.2281 0.2714 0.5446 0.0097  -0.0348 0.0655  340 VAL A CG1   
1477 C CG2   . VAL A 199 ? 0.2336 0.2838 0.5319 0.0122  -0.0249 0.0462  340 VAL A CG2   
1478 N N     . GLU A 200 ? 0.2757 0.2975 0.6438 0.0117  -0.0349 0.0535  341 GLU A N     
1479 C CA    . GLU A 200 ? 0.2907 0.3059 0.6774 0.0108  -0.0398 0.0607  341 GLU A CA    
1480 C C     . GLU A 200 ? 0.2604 0.2719 0.6571 0.0144  -0.0371 0.0508  341 GLU A C     
1481 O O     . GLU A 200 ? 0.2995 0.3103 0.7024 0.0152  -0.0402 0.0559  341 GLU A O     
1482 C CB    . GLU A 200 ? 0.3011 0.3106 0.7046 0.0077  -0.0429 0.0651  341 GLU A CB    
1483 C CG    . GLU A 200 ? 0.4956 0.5033 0.9085 0.0043  -0.0503 0.0804  341 GLU A CG    
1484 C CD    . GLU A 200 ? 0.6376 0.6528 1.0346 0.0007  -0.0537 0.0933  341 GLU A CD    
1485 O OE1   . GLU A 200 ? 0.6643 0.6820 1.0570 -0.0020 -0.0539 0.0964  341 GLU A OE1   
1486 O OE2   . GLU A 200 ? 0.7002 0.7195 1.0890 0.0004  -0.0562 0.0999  341 GLU A OE2   
1487 N N     . LEU A 201 ? 0.2410 0.2510 0.6394 0.0163  -0.0314 0.0367  342 LEU A N     
1488 C CA    . LEU A 201 ? 0.2785 0.2863 0.6852 0.0194  -0.0282 0.0265  342 LEU A CA    
1489 C C     . LEU A 201 ? 0.2820 0.2957 0.6750 0.0218  -0.0270 0.0263  342 LEU A C     
1490 O O     . LEU A 201 ? 0.2796 0.2925 0.6815 0.0237  -0.0283 0.0272  342 LEU A O     
1491 C CB    . LEU A 201 ? 0.2373 0.2441 0.6454 0.0201  -0.0220 0.0113  342 LEU A CB    
1492 C CG    . LEU A 201 ? 0.3242 0.3242 0.7513 0.0182  -0.0228 0.0089  342 LEU A CG    
1493 C CD1   . LEU A 201 ? 0.3379 0.3385 0.7640 0.0184  -0.0163 -0.0070 342 LEU A CD1   
1494 C CD2   . LEU A 201 ? 0.3672 0.3615 0.8152 0.0192  -0.0258 0.0114  342 LEU A CD2   
1495 N N     . GLY A 202 ? 0.2396 0.2598 0.6114 0.0218  -0.0245 0.0251  343 GLY A N     
1496 C CA    . GLY A 202 ? 0.2148 0.2407 0.5735 0.0236  -0.0236 0.0252  343 GLY A CA    
1497 C C     . GLY A 202 ? 0.2300 0.2565 0.5926 0.0231  -0.0294 0.0375  343 GLY A C     
1498 O O     . GLY A 202 ? 0.2594 0.2874 0.6253 0.0252  -0.0296 0.0367  343 GLY A O     
1499 N N     . HIS A 203 ? 0.2447 0.2708 0.6075 0.0200  -0.0343 0.0494  344 HIS A N     
1500 C CA    . HIS A 203 ? 0.2188 0.2464 0.5847 0.0187  -0.0402 0.0618  344 HIS A CA    
1501 C C     . HIS A 203 ? 0.3148 0.3370 0.7027 0.0200  -0.0430 0.0630  344 HIS A C     
1502 O O     . HIS A 203 ? 0.2759 0.3004 0.6669 0.0210  -0.0459 0.0680  344 HIS A O     
1503 C CB    . HIS A 203 ? 0.2294 0.2583 0.5905 0.0143  -0.0447 0.0741  344 HIS A CB    
1504 C CG    . HIS A 203 ? 0.2697 0.3060 0.6084 0.0133  -0.0428 0.0749  344 HIS A CG    
1505 N ND1   . HIS A 203 ? 0.2533 0.2926 0.5843 0.0095  -0.0453 0.0835  344 HIS A ND1   
1506 C CD2   . HIS A 203 ? 0.2186 0.2603 0.5412 0.0155  -0.0388 0.0680  344 HIS A CD2   
1507 C CE1   . HIS A 203 ? 0.2603 0.3068 0.5718 0.0097  -0.0425 0.0814  344 HIS A CE1   
1508 N NE2   . HIS A 203 ? 0.2650 0.3126 0.5712 0.0132  -0.0387 0.0722  344 HIS A NE2   
1509 N N     . ARG A 204 ? 0.2678 0.2833 0.6716 0.0202  -0.0420 0.0580  345 ARG A N     
1510 C CA    . ARG A 204 ? 0.2905 0.3009 0.7164 0.0218  -0.0444 0.0582  345 ARG A CA    
1511 C C     . ARG A 204 ? 0.3510 0.3637 0.7793 0.0261  -0.0412 0.0500  345 ARG A C     
1512 O O     . ARG A 204 ? 0.3455 0.3572 0.7876 0.0278  -0.0445 0.0541  345 ARG A O     
1513 C CB    . ARG A 204 ? 0.3272 0.3306 0.7683 0.0214  -0.0427 0.0518  345 ARG A CB    
1514 C CG    . ARG A 204 ? 0.4196 0.4172 0.8830 0.0210  -0.0480 0.0586  345 ARG A CG    
1515 C CD    . ARG A 204 ? 0.4651 0.4559 0.9442 0.0217  -0.0452 0.0490  345 ARG A CD    
1516 N NE    . ARG A 204 ? 0.5206 0.5093 0.9976 0.0180  -0.0459 0.0515  345 ARG A NE    
1517 C CZ    . ARG A 204 ? 0.5996 0.5839 1.0842 0.0178  -0.0423 0.0415  345 ARG A CZ    
1518 N NH1   . ARG A 204 ? 0.5675 0.5490 1.0624 0.0208  -0.0376 0.0283  345 ARG A NH1   
1519 N NH2   . ARG A 204 ? 0.5067 0.4897 0.9887 0.0144  -0.0434 0.0448  345 ARG A NH2   
1520 N N     . TYR A 205 ? 0.3282 0.3445 0.7436 0.0278  -0.0351 0.0389  346 TYR A N     
1521 C CA    . TYR A 205 ? 0.3192 0.3389 0.7355 0.0314  -0.0319 0.0313  346 TYR A CA    
1522 C C     . TYR A 205 ? 0.2904 0.3178 0.6906 0.0317  -0.0329 0.0362  346 TYR A C     
1523 O O     . TYR A 205 ? 0.3537 0.3856 0.7511 0.0343  -0.0296 0.0295  346 TYR A O     
1524 C CB    . TYR A 205 ? 0.3337 0.3534 0.7468 0.0327  -0.0246 0.0159  346 TYR A CB    
1525 C CG    . TYR A 205 ? 0.3704 0.3834 0.8025 0.0329  -0.0231 0.0089  346 TYR A CG    
1526 C CD1   . TYR A 205 ? 0.3252 0.3331 0.7615 0.0302  -0.0245 0.0110  346 TYR A CD1   
1527 C CD2   . TYR A 205 ? 0.3601 0.3721 0.8066 0.0359  -0.0204 0.0001  346 TYR A CD2   
1528 C CE1   . TYR A 205 ? 0.3859 0.3878 0.8399 0.0302  -0.0232 0.0043  346 TYR A CE1   
1529 C CE2   . TYR A 205 ? 0.3196 0.3255 0.7836 0.0361  -0.0188 -0.0069 346 TYR A CE2   
1530 C CZ    . TYR A 205 ? 0.3931 0.3940 0.8608 0.0332  -0.0203 -0.0048 346 TYR A CZ    
1531 O OH    . TYR A 205 ? 0.4957 0.4907 0.9808 0.0332  -0.0186 -0.0121 346 TYR A OH    
1532 N N     . GLY A 206 ? 0.2864 0.3161 0.6761 0.0288  -0.0371 0.0474  347 GLY A N     
1533 C CA    . GLY A 206 ? 0.2791 0.3162 0.6550 0.0286  -0.0386 0.0526  347 GLY A CA    
1534 C C     . GLY A 206 ? 0.2977 0.3403 0.6522 0.0285  -0.0339 0.0464  347 GLY A C     
1535 O O     . GLY A 206 ? 0.3225 0.3716 0.6665 0.0286  -0.0345 0.0489  347 GLY A O     
1536 N N     . ALA A 207 ? 0.3108 0.3516 0.6588 0.0283  -0.0295 0.0386  348 ALA A N     
1537 C CA    . ALA A 207 ? 0.2526 0.2987 0.5806 0.0283  -0.0251 0.0326  348 ALA A CA    
1538 C C     . ALA A 207 ? 0.2454 0.2940 0.5589 0.0255  -0.0271 0.0401  348 ALA A C     
1539 O O     . ALA A 207 ? 0.2699 0.3151 0.5885 0.0232  -0.0304 0.0472  348 ALA A O     
1540 C CB    . ALA A 207 ? 0.1974 0.2414 0.5247 0.0293  -0.0192 0.0200  348 ALA A CB    
1541 N N     . ARG A 208 ? 0.2240 0.2789 0.5199 0.0254  -0.0250 0.0384  349 ARG A N     
1542 C CA    . ARG A 208 ? 0.2433 0.3011 0.5243 0.0232  -0.0252 0.0422  349 ARG A CA    
1543 C C     . ARG A 208 ? 0.2057 0.2620 0.4825 0.0236  -0.0206 0.0336  349 ARG A C     
1544 O O     . ARG A 208 ? 0.1922 0.2471 0.4717 0.0255  -0.0165 0.0236  349 ARG A O     
1545 C CB    . ARG A 208 ? 0.2691 0.3341 0.5340 0.0228  -0.0246 0.0431  349 ARG A CB    
1546 C CG    . ARG A 208 ? 0.2781 0.3461 0.5456 0.0217  -0.0295 0.0520  349 ARG A CG    
1547 C CD    . ARG A 208 ? 0.2877 0.3571 0.5511 0.0181  -0.0341 0.0633  349 ARG A CD    
1548 N NE    . ARG A 208 ? 0.2648 0.3384 0.5278 0.0162  -0.0388 0.0719  349 ARG A NE    
1549 C CZ    . ARG A 208 ? 0.3476 0.4227 0.6101 0.0124  -0.0439 0.0833  349 ARG A CZ    
1550 N NH1   . ARG A 208 ? 0.2783 0.3514 0.5407 0.0101  -0.0450 0.0880  349 ARG A NH1   
1551 N NH2   . ARG A 208 ? 0.3691 0.4487 0.6313 0.0105  -0.0481 0.0904  349 ARG A NH2   
1552 N N     . VAL A 209 ? 0.1831 0.2404 0.4534 0.0216  -0.0214 0.0376  350 VAL A N     
1553 C CA    . VAL A 209 ? 0.1656 0.2224 0.4326 0.0217  -0.0177 0.0304  350 VAL A CA    
1554 C C     . VAL A 209 ? 0.1651 0.2284 0.4135 0.0209  -0.0160 0.0309  350 VAL A C     
1555 O O     . VAL A 209 ? 0.1772 0.2437 0.4203 0.0188  -0.0190 0.0395  350 VAL A O     
1556 C CB    . VAL A 209 ? 0.2060 0.2575 0.4873 0.0200  -0.0199 0.0336  350 VAL A CB    
1557 C CG1   . VAL A 209 ? 0.1801 0.2316 0.4601 0.0203  -0.0156 0.0240  350 VAL A CG1   
1558 C CG2   . VAL A 209 ? 0.2314 0.2760 0.5326 0.0207  -0.0223 0.0348  350 VAL A CG2   
1559 N N     . LEU A 210 ? 0.1457 0.2115 0.3845 0.0224  -0.0113 0.0216  351 LEU A N     
1560 C CA    . LEU A 210 ? 0.1631 0.2346 0.3856 0.0221  -0.0091 0.0204  351 LEU A CA    
1561 C C     . LEU A 210 ? 0.1777 0.2493 0.4014 0.0217  -0.0068 0.0154  351 LEU A C     
1562 O O     . LEU A 210 ? 0.1833 0.2517 0.4140 0.0224  -0.0045 0.0077  351 LEU A O     
1563 C CB    . LEU A 210 ? 0.1336 0.2084 0.3444 0.0238  -0.0057 0.0145  351 LEU A CB    
1564 C CG    . LEU A 210 ? 0.1570 0.2372 0.3517 0.0241  -0.0034 0.0129  351 LEU A CG    
1565 C CD1   . LEU A 210 ? 0.1233 0.2065 0.3081 0.0249  -0.0024 0.0125  351 LEU A CD1   
1566 C CD2   . LEU A 210 ? 0.1718 0.2527 0.3630 0.0247  0.0003  0.0049  351 LEU A CD2   
1567 N N     . ILE A 211 ? 0.1269 0.2029 0.3436 0.0203  -0.0074 0.0193  352 ILE A N     
1568 C CA    . ILE A 211 ? 0.1431 0.2211 0.3602 0.0195  -0.0056 0.0153  352 ILE A CA    
1569 C C     . ILE A 211 ? 0.1274 0.2120 0.3276 0.0206  -0.0026 0.0120  352 ILE A C     
1570 O O     . ILE A 211 ? 0.1288 0.2176 0.3195 0.0205  -0.0035 0.0172  352 ILE A O     
1571 C CB    . ILE A 211 ? 0.1485 0.2268 0.3744 0.0166  -0.0089 0.0230  352 ILE A CB    
1572 C CG1   . ILE A 211 ? 0.1824 0.2530 0.4263 0.0158  -0.0123 0.0271  352 ILE A CG1   
1573 C CG2   . ILE A 211 ? 0.1616 0.2430 0.3888 0.0152  -0.0070 0.0185  352 ILE A CG2   
1574 C CD1   . ILE A 211 ? 0.1775 0.2420 0.4345 0.0169  -0.0103 0.0181  352 ILE A CD1   
1575 N N     . ASP A 212 ? 0.1253 0.2109 0.3225 0.0215  0.0007  0.0035  353 ASP A N     
1576 C CA    . ASP A 212 ? 0.1434 0.2351 0.3263 0.0227  0.0033  0.0005  353 ASP A CA    
1577 C C     . ASP A 212 ? 0.1303 0.2271 0.3142 0.0210  0.0028  0.0022  353 ASP A C     
1578 O O     . ASP A 212 ? 0.1448 0.2416 0.3362 0.0195  0.0034  -0.0021 353 ASP A O     
1579 C CB    . ASP A 212 ? 0.1315 0.2228 0.3110 0.0238  0.0067  -0.0084 353 ASP A CB    
1580 C CG    . ASP A 212 ? 0.1697 0.2670 0.3355 0.0251  0.0089  -0.0108 353 ASP A CG    
1581 O OD1   . ASP A 212 ? 0.1429 0.2449 0.3023 0.0255  0.0082  -0.0064 353 ASP A OD1   
1582 O OD2   . ASP A 212 ? 0.1841 0.2815 0.3457 0.0256  0.0116  -0.0170 353 ASP A OD2   
1583 N N     . GLY A 213 ? 0.1442 0.2458 0.3211 0.0208  0.0017  0.0084  354 GLY A N     
1584 C CA    . GLY A 213 ? 0.1232 0.2307 0.3012 0.0188  0.0012  0.0109  354 GLY A CA    
1585 C C     . GLY A 213 ? 0.1505 0.2657 0.3163 0.0207  0.0035  0.0082  354 GLY A C     
1586 O O     . GLY A 213 ? 0.1489 0.2704 0.3128 0.0195  0.0032  0.0115  354 GLY A O     
1587 N N     . ALA A 214 ? 0.1070 0.2218 0.2646 0.0236  0.0059  0.0025  355 ALA A N     
1588 C CA    . ALA A 214 ? 0.1385 0.2599 0.2847 0.0260  0.0076  0.0009  355 ALA A CA    
1589 C C     . ALA A 214 ? 0.1355 0.2642 0.2846 0.0246  0.0079  -0.0009 355 ALA A C     
1590 O O     . ALA A 214 ? 0.1203 0.2558 0.2633 0.0259  0.0082  -0.0001 355 ALA A O     
1591 C CB    . ALA A 214 ? 0.1073 0.2265 0.2455 0.0288  0.0099  -0.0035 355 ALA A CB    
1592 N N     . GLN A 215 ? 0.1114 0.2384 0.2705 0.0218  0.0076  -0.0044 356 GLN A N     
1593 C CA    . GLN A 215 ? 0.1164 0.2505 0.2798 0.0194  0.0075  -0.0064 356 GLN A CA    
1594 C C     . GLN A 215 ? 0.1475 0.2818 0.3231 0.0151  0.0054  -0.0027 356 GLN A C     
1595 O O     . GLN A 215 ? 0.1441 0.2844 0.3248 0.0121  0.0051  -0.0044 356 GLN A O     
1596 C CB    . GLN A 215 ? 0.1534 0.2864 0.3192 0.0185  0.0088  -0.0147 356 GLN A CB    
1597 C CG    . GLN A 215 ? 0.2159 0.3484 0.3697 0.0218  0.0107  -0.0176 356 GLN A CG    
1598 C CD    . GLN A 215 ? 0.2927 0.4329 0.4375 0.0231  0.0110  -0.0177 356 GLN A CD    
1599 O OE1   . GLN A 215 ? 0.2606 0.4077 0.4076 0.0218  0.0100  -0.0153 356 GLN A OE1   
1600 N NE2   . GLN A 215 ? 0.3615 0.5004 0.4959 0.0256  0.0123  -0.0201 356 GLN A NE2   
1601 N N     . SER A 216 ? 0.0973 0.2253 0.2783 0.0141  0.0037  0.0028  357 SER A N     
1602 C CA    . SER A 216 ? 0.1157 0.2445 0.3073 0.0096  0.0014  0.0083  357 SER A CA    
1603 C C     . SER A 216 ? 0.1328 0.2685 0.3176 0.0089  0.0009  0.0159  357 SER A C     
1604 O O     . SER A 216 ? 0.1711 0.3131 0.3596 0.0052  0.0002  0.0188  357 SER A O     
1605 C CB    . SER A 216 ? 0.1137 0.2323 0.3174 0.0082  -0.0008 0.0112  357 SER A CB    
1606 O OG    . SER A 216 ? 0.1399 0.2547 0.3378 0.0106  -0.0016 0.0161  357 SER A OG    
1607 N N     . ILE A 217 ? 0.0904 0.2255 0.2648 0.0121  0.0014  0.0186  358 ILE A N     
1608 C CA    . ILE A 217 ? 0.1321 0.2731 0.3000 0.0110  0.0013  0.0254  358 ILE A CA    
1609 C C     . ILE A 217 ? 0.1343 0.2854 0.2960 0.0112  0.0031  0.0236  358 ILE A C     
1610 O O     . ILE A 217 ? 0.1385 0.2957 0.2994 0.0082  0.0029  0.0290  358 ILE A O     
1611 C CB    . ILE A 217 ? 0.1309 0.2689 0.2889 0.0141  0.0017  0.0278  358 ILE A CB    
1612 C CG1   . ILE A 217 ? 0.1658 0.3099 0.3196 0.0117  0.0013  0.0358  358 ILE A CG1   
1613 C CG2   . ILE A 217 ? 0.1302 0.2682 0.2767 0.0192  0.0044  0.0214  358 ILE A CG2   
1614 C CD1   . ILE A 217 ? 0.1531 0.2950 0.3005 0.0129  0.0010  0.0397  358 ILE A CD1   
1615 N N     . PRO A 218 ? 0.1318 0.2856 0.2893 0.0141  0.0047  0.0165  359 PRO A N     
1616 C CA    . PRO A 218 ? 0.1489 0.3116 0.3021 0.0138  0.0058  0.0154  359 PRO A CA    
1617 C C     . PRO A 218 ? 0.1625 0.3314 0.3268 0.0085  0.0047  0.0154  359 PRO A C     
1618 O O     . PRO A 218 ? 0.1479 0.3248 0.3095 0.0074  0.0053  0.0156  359 PRO A O     
1619 C CB    . PRO A 218 ? 0.1290 0.2902 0.2745 0.0184  0.0072  0.0090  359 PRO A CB    
1620 C CG    . PRO A 218 ? 0.1648 0.3175 0.3093 0.0209  0.0074  0.0068  359 PRO A CG    
1621 C CD    . PRO A 218 ? 0.1517 0.3011 0.3073 0.0175  0.0056  0.0096  359 PRO A CD    
1622 N N     . HIS A 219 ? 0.1304 0.2945 0.3071 0.0050  0.0030  0.0153  360 HIS A N     
1623 C CA    . HIS A 219 ? 0.1579 0.3261 0.3454 -0.0001 0.0021  0.0132  360 HIS A CA    
1624 C C     . HIS A 219 ? 0.1945 0.3579 0.3943 -0.0063 -0.0002 0.0189  360 HIS A C     
1625 O O     . HIS A 219 ? 0.1924 0.3580 0.4013 -0.0115 -0.0011 0.0174  360 HIS A O     
1626 C CB    . HIS A 219 ? 0.1500 0.3146 0.3416 0.0010  0.0026  0.0047  360 HIS A CB    
1627 C CG    . HIS A 219 ? 0.1588 0.3294 0.3393 0.0061  0.0043  -0.0001 360 HIS A CG    
1628 N ND1   . HIS A 219 ? 0.1494 0.3285 0.3246 0.0068  0.0049  0.0000  360 HIS A ND1   
1629 C CD2   . HIS A 219 ? 0.1647 0.3298 0.3381 0.0105  0.0056  -0.0039 360 HIS A CD2   
1630 C CE1   . HIS A 219 ? 0.1856 0.3623 0.3493 0.0114  0.0059  -0.0030 360 HIS A CE1   
1631 N NE2   . HIS A 219 ? 0.1548 0.3241 0.3181 0.0135  0.0065  -0.0051 360 HIS A NE2   
1632 N N     . MET A 220 ? 0.1424 0.2991 0.3428 -0.0064 -0.0015 0.0256  361 MET A N     
1633 C CA    . MET A 220 ? 0.1926 0.3439 0.4048 -0.0123 -0.0044 0.0324  361 MET A CA    
1634 C C     . MET A 220 ? 0.1816 0.3309 0.3891 -0.0120 -0.0057 0.0413  361 MET A C     
1635 O O     . MET A 220 ? 0.1368 0.2844 0.3354 -0.0068 -0.0046 0.0402  361 MET A O     
1636 C CB    . MET A 220 ? 0.1460 0.2857 0.3722 -0.0131 -0.0058 0.0282  361 MET A CB    
1637 C CG    . MET A 220 ? 0.2045 0.3351 0.4296 -0.0077 -0.0059 0.0266  361 MET A CG    
1638 S SD    . MET A 220 ? 0.2299 0.3493 0.4693 -0.0071 -0.0058 0.0175  361 MET A SD    
1639 C CE    . MET A 220 ? 0.2201 0.3484 0.4519 -0.0062 -0.0025 0.0065  361 MET A CE    
1640 N N     . PRO A 221 ? 0.1812 0.3311 0.3938 -0.0179 -0.0080 0.0501  362 PRO A N     
1641 C CA    . PRO A 221 ? 0.1758 0.3251 0.3837 -0.0185 -0.0096 0.0591  362 PRO A CA    
1642 C C     . PRO A 221 ? 0.1880 0.3258 0.4016 -0.0154 -0.0119 0.0599  362 PRO A C     
1643 O O     . PRO A 221 ? 0.1953 0.3242 0.4212 -0.0152 -0.0132 0.0564  362 PRO A O     
1644 C CB    . PRO A 221 ? 0.1993 0.3504 0.4133 -0.0267 -0.0121 0.0683  362 PRO A CB    
1645 C CG    . PRO A 221 ? 0.2289 0.3768 0.4547 -0.0300 -0.0127 0.0640  362 PRO A CG    
1646 C CD    . PRO A 221 ? 0.2062 0.3581 0.4279 -0.0250 -0.0093 0.0525  362 PRO A CD    
1647 N N     . ILE A 222 ? 0.1924 0.3311 0.3972 -0.0131 -0.0121 0.0638  363 ILE A N     
1648 C CA    . ILE A 222 ? 0.1839 0.3132 0.3925 -0.0101 -0.0143 0.0650  363 ILE A CA    
1649 C C     . ILE A 222 ? 0.1630 0.2931 0.3719 -0.0141 -0.0181 0.0769  363 ILE A C     
1650 O O     . ILE A 222 ? 0.2103 0.3488 0.4073 -0.0163 -0.0171 0.0812  363 ILE A O     
1651 C CB    . ILE A 222 ? 0.1781 0.3072 0.3748 -0.0036 -0.0113 0.0579  363 ILE A CB    
1652 C CG1   . ILE A 222 ? 0.1537 0.2826 0.3491 0.0000  -0.0079 0.0467  363 ILE A CG1   
1653 C CG2   . ILE A 222 ? 0.1848 0.3050 0.3850 -0.0012 -0.0136 0.0593  363 ILE A CG2   
1654 C CD1   . ILE A 222 ? 0.1422 0.2626 0.3516 -0.0002 -0.0089 0.0420  363 ILE A CD1   
1655 N N     . ASP A 223 ? 0.2090 0.3299 0.4301 -0.0150 -0.0224 0.0818  364 ASP A N     
1656 C CA    . ASP A 223 ? 0.2147 0.3349 0.4362 -0.0187 -0.0270 0.0936  364 ASP A CA    
1657 C C     . ASP A 223 ? 0.1897 0.3007 0.4190 -0.0145 -0.0297 0.0933  364 ASP A C     
1658 O O     . ASP A 223 ? 0.1994 0.3014 0.4446 -0.0146 -0.0329 0.0951  364 ASP A O     
1659 C CB    . ASP A 223 ? 0.1785 0.2971 0.4091 -0.0258 -0.0306 0.1028  364 ASP A CB    
1660 C CG    . ASP A 223 ? 0.2777 0.3974 0.5062 -0.0306 -0.0355 0.1162  364 ASP A CG    
1661 O OD1   . ASP A 223 ? 0.2711 0.3902 0.4960 -0.0280 -0.0373 0.1185  364 ASP A OD1   
1662 O OD2   . ASP A 223 ? 0.3752 0.4971 0.6055 -0.0376 -0.0377 0.1247  364 ASP A OD2   
1663 N N     . VAL A 224 ? 0.1779 0.2906 0.3957 -0.0107 -0.0282 0.0907  365 VAL A N     
1664 C CA    . VAL A 224 ? 0.2062 0.3100 0.4290 -0.0066 -0.0297 0.0883  365 VAL A CA    
1665 C C     . VAL A 224 ? 0.2177 0.3178 0.4497 -0.0097 -0.0360 0.1001  365 VAL A C     
1666 O O     . VAL A 224 ? 0.1942 0.2852 0.4371 -0.0072 -0.0381 0.0993  365 VAL A O     
1667 C CB    . VAL A 224 ? 0.1374 0.2439 0.3454 -0.0027 -0.0266 0.0826  365 VAL A CB    
1668 C CG1   . VAL A 224 ? 0.1287 0.2367 0.3298 0.0012  -0.0209 0.0708  365 VAL A CG1   
1669 C CG2   . VAL A 224 ? 0.1401 0.2562 0.3359 -0.0061 -0.0276 0.0901  365 VAL A CG2   
1670 N N     . ALA A 225 ? 0.1996 0.3070 0.4272 -0.0155 -0.0392 0.1111  366 ALA A N     
1671 C CA    . ALA A 225 ? 0.2432 0.3476 0.4791 -0.0191 -0.0459 0.1237  366 ALA A CA    
1672 C C     . ALA A 225 ? 0.2768 0.3724 0.5329 -0.0202 -0.0493 0.1271  366 ALA A C     
1673 O O     . ALA A 225 ? 0.2630 0.3496 0.5314 -0.0188 -0.0533 0.1309  366 ALA A O     
1674 C CB    . ALA A 225 ? 0.2330 0.3486 0.4584 -0.0261 -0.0485 0.1348  366 ALA A CB    
1675 N N     . ALA A 226 ? 0.2750 0.3726 0.5349 -0.0231 -0.0474 0.1253  367 ALA A N     
1676 C CA    . ALA A 226 ? 0.2794 0.3670 0.5580 -0.0242 -0.0497 0.1263  367 ALA A CA    
1677 C C     . ALA A 226 ? 0.2639 0.3425 0.5547 -0.0171 -0.0476 0.1150  367 ALA A C     
1678 O O     . ALA A 226 ? 0.2863 0.3549 0.5955 -0.0158 -0.0511 0.1172  367 ALA A O     
1679 C CB    . ALA A 226 ? 0.2332 0.3237 0.5082 -0.0291 -0.0468 0.1243  367 ALA A CB    
1680 N N     . LEU A 227 ? 0.2336 0.3148 0.5128 -0.0126 -0.0415 0.1023  368 LEU A N     
1681 C CA    . LEU A 227 ? 0.2282 0.3012 0.5147 -0.0067 -0.0383 0.0903  368 LEU A CA    
1682 C C     . LEU A 227 ? 0.2312 0.2971 0.5225 -0.0034 -0.0406 0.0917  368 LEU A C     
1683 O O     . LEU A 227 ? 0.2777 0.3345 0.5833 -0.0005 -0.0405 0.0865  368 LEU A O     
1684 C CB    . LEU A 227 ? 0.2398 0.3184 0.5105 -0.0035 -0.0318 0.0782  368 LEU A CB    
1685 C CG    . LEU A 227 ? 0.3022 0.3752 0.5747 0.0018  -0.0277 0.0650  368 LEU A CG    
1686 C CD1   . LEU A 227 ? 0.2753 0.3401 0.5681 0.0018  -0.0282 0.0608  368 LEU A CD1   
1687 C CD2   . LEU A 227 ? 0.3160 0.3962 0.5724 0.0032  -0.0223 0.0560  368 LEU A CD2   
1688 N N     . GLY A 228 ? 0.2138 0.2843 0.4932 -0.0041 -0.0423 0.0980  369 GLY A N     
1689 C CA    . GLY A 228 ? 0.2029 0.2685 0.4851 -0.0020 -0.0443 0.0992  369 GLY A CA    
1690 C C     . GLY A 228 ? 0.2155 0.2803 0.4903 0.0032  -0.0393 0.0869  369 GLY A C     
1691 O O     . GLY A 228 ? 0.1848 0.2466 0.4626 0.0048  -0.0405 0.0870  369 GLY A O     
1692 N N     . ALA A 229 ? 0.1957 0.2636 0.4612 0.0053  -0.0338 0.0767  370 ALA A N     
1693 C CA    . ALA A 229 ? 0.1581 0.2257 0.4158 0.0095  -0.0293 0.0657  370 ALA A CA    
1694 C C     . ALA A 229 ? 0.1790 0.2512 0.4245 0.0095  -0.0303 0.0693  370 ALA A C     
1695 O O     . ALA A 229 ? 0.1746 0.2528 0.4112 0.0065  -0.0324 0.0772  370 ALA A O     
1696 C CB    . ALA A 229 ? 0.1898 0.2614 0.4375 0.0108  -0.0241 0.0562  370 ALA A CB    
1697 N N     . ASP A 230 ? 0.1341 0.2040 0.3798 0.0124  -0.0288 0.0636  371 ASP A N     
1698 C CA    . ASP A 230 ? 0.1575 0.2320 0.3931 0.0122  -0.0298 0.0664  371 ASP A CA    
1699 C C     . ASP A 230 ? 0.1807 0.2612 0.3990 0.0131  -0.0258 0.0611  371 ASP A C     
1700 O O     . ASP A 230 ? 0.1493 0.2352 0.3577 0.0115  -0.0271 0.0657  371 ASP A O     
1701 C CB    . ASP A 230 ? 0.2072 0.2784 0.4499 0.0147  -0.0296 0.0623  371 ASP A CB    
1702 C CG    . ASP A 230 ? 0.2402 0.3054 0.5011 0.0142  -0.0336 0.0675  371 ASP A CG    
1703 O OD1   . ASP A 230 ? 0.2385 0.3051 0.5020 0.0118  -0.0386 0.0776  371 ASP A OD1   
1704 O OD2   . ASP A 230 ? 0.2402 0.2995 0.5129 0.0160  -0.0318 0.0616  371 ASP A OD2   
1705 N N     . PHE A 231 ? 0.1411 0.2210 0.3561 0.0154  -0.0211 0.0514  372 PHE A N     
1706 C CA    . PHE A 231 ? 0.1372 0.2223 0.3369 0.0164  -0.0174 0.0467  372 PHE A CA    
1707 C C     . PHE A 231 ? 0.1459 0.2320 0.3444 0.0166  -0.0147 0.0425  372 PHE A C     
1708 O O     . PHE A 231 ? 0.1558 0.2375 0.3642 0.0172  -0.0140 0.0384  372 PHE A O     
1709 C CB    . PHE A 231 ? 0.1208 0.2055 0.3156 0.0192  -0.0141 0.0384  372 PHE A CB    
1710 C CG    . PHE A 231 ? 0.1724 0.2570 0.3696 0.0190  -0.0165 0.0414  372 PHE A CG    
1711 C CD1   . PHE A 231 ? 0.1396 0.2291 0.3285 0.0174  -0.0184 0.0469  372 PHE A CD1   
1712 C CD2   . PHE A 231 ? 0.1677 0.2482 0.3760 0.0203  -0.0167 0.0386  372 PHE A CD2   
1713 C CE1   . PHE A 231 ? 0.1752 0.2657 0.3668 0.0168  -0.0208 0.0498  372 PHE A CE1   
1714 C CE2   . PHE A 231 ? 0.1856 0.2673 0.3969 0.0202  -0.0190 0.0414  372 PHE A CE2   
1715 C CZ    . PHE A 231 ? 0.1659 0.2527 0.3688 0.0183  -0.0212 0.0471  372 PHE A CZ    
1716 N N     . PHE A 232 ? 0.1135 0.2057 0.3004 0.0162  -0.0132 0.0431  373 PHE A N     
1717 C CA    . PHE A 232 ? 0.0962 0.1910 0.2805 0.0165  -0.0104 0.0388  373 PHE A CA    
1718 C C     . PHE A 232 ? 0.1101 0.2097 0.2797 0.0187  -0.0070 0.0345  373 PHE A C     
1719 O O     . PHE A 232 ? 0.1143 0.2178 0.2760 0.0182  -0.0075 0.0390  373 PHE A O     
1720 C CB    . PHE A 232 ? 0.0850 0.1835 0.2734 0.0130  -0.0128 0.0465  373 PHE A CB    
1721 C CG    . PHE A 232 ? 0.1165 0.2188 0.3037 0.0128  -0.0102 0.0423  373 PHE A CG    
1722 C CD1   . PHE A 232 ? 0.1169 0.2155 0.3158 0.0121  -0.0103 0.0390  373 PHE A CD1   
1723 C CD2   . PHE A 232 ? 0.1135 0.2234 0.2885 0.0133  -0.0078 0.0416  373 PHE A CD2   
1724 C CE1   . PHE A 232 ? 0.1367 0.2399 0.3347 0.0113  -0.0082 0.0351  373 PHE A CE1   
1725 C CE2   . PHE A 232 ? 0.1561 0.2705 0.3302 0.0132  -0.0056 0.0378  373 PHE A CE2   
1726 C CZ    . PHE A 232 ? 0.1121 0.2235 0.2975 0.0119  -0.0060 0.0347  373 PHE A CZ    
1727 N N     . VAL A 233 ? 0.0955 0.1951 0.2614 0.0209  -0.0035 0.0263  374 VAL A N     
1728 C CA    . VAL A 233 ? 0.0750 0.1780 0.2279 0.0234  -0.0005 0.0226  374 VAL A CA    
1729 C C     . VAL A 233 ? 0.0932 0.2006 0.2416 0.0243  0.0017  0.0191  374 VAL A C     
1730 O O     . VAL A 233 ? 0.1117 0.2189 0.2669 0.0234  0.0019  0.0160  374 VAL A O     
1731 C CB    . VAL A 233 ? 0.0900 0.1895 0.2403 0.0256  0.0014  0.0163  374 VAL A CB    
1732 C CG1   . VAL A 233 ? 0.0900 0.1865 0.2446 0.0247  -0.0008 0.0198  374 VAL A CG1   
1733 C CG2   . VAL A 233 ? 0.0755 0.1725 0.2314 0.0259  0.0030  0.0094  374 VAL A CG2   
1734 N N     . PHE A 234 ? 0.0982 0.2100 0.2355 0.0259  0.0035  0.0196  375 PHE A N     
1735 C CA    . PHE A 234 ? 0.1180 0.2341 0.2504 0.0273  0.0056  0.0158  375 PHE A CA    
1736 C C     . PHE A 234 ? 0.1408 0.2581 0.2595 0.0305  0.0080  0.0147  375 PHE A C     
1737 O O     . PHE A 234 ? 0.0926 0.2088 0.2052 0.0313  0.0083  0.0175  375 PHE A O     
1738 C CB    . PHE A 234 ? 0.1211 0.2425 0.2584 0.0247  0.0045  0.0198  375 PHE A CB    
1739 C CG    . PHE A 234 ? 0.1258 0.2521 0.2577 0.0236  0.0042  0.0266  375 PHE A CG    
1740 C CD1   . PHE A 234 ? 0.1122 0.2382 0.2493 0.0205  0.0015  0.0338  375 PHE A CD1   
1741 C CD2   . PHE A 234 ? 0.1621 0.2937 0.2836 0.0255  0.0066  0.0258  375 PHE A CD2   
1742 C CE1   . PHE A 234 ? 0.1418 0.2744 0.2734 0.0188  0.0014  0.0402  375 PHE A CE1   
1743 C CE2   . PHE A 234 ? 0.1258 0.2635 0.2421 0.0245  0.0070  0.0313  375 PHE A CE2   
1744 C CZ    . PHE A 234 ? 0.1399 0.2787 0.2609 0.0208  0.0045  0.0385  375 PHE A CZ    
1745 N N     . SER A 235 ? 0.1037 0.2231 0.2176 0.0321  0.0096  0.0107  376 SER A N     
1746 C CA    . SER A 235 ? 0.1099 0.2282 0.2107 0.0354  0.0117  0.0091  376 SER A CA    
1747 C C     . SER A 235 ? 0.1118 0.2356 0.2077 0.0359  0.0123  0.0111  376 SER A C     
1748 O O     . SER A 235 ? 0.0746 0.2029 0.1759 0.0344  0.0117  0.0104  376 SER A O     
1749 C CB    . SER A 235 ? 0.1415 0.2569 0.2396 0.0368  0.0129  0.0036  376 SER A CB    
1750 O OG    . SER A 235 ? 0.1553 0.2664 0.2562 0.0366  0.0132  0.0013  376 SER A OG    
1751 N N     . GLY A 236 ? 0.0787 0.2027 0.1646 0.0383  0.0138  0.0128  377 GLY A N     
1752 C CA    . GLY A 236 ? 0.0844 0.2143 0.1660 0.0392  0.0149  0.0142  377 GLY A CA    
1753 C C     . GLY A 236 ? 0.1128 0.2437 0.1921 0.0409  0.0152  0.0108  377 GLY A C     
1754 O O     . GLY A 236 ? 0.1035 0.2411 0.1850 0.0402  0.0152  0.0116  377 GLY A O     
1755 N N     . HIS A 237 ? 0.0953 0.2208 0.1704 0.0431  0.0153  0.0075  378 HIS A N     
1756 C CA    . HIS A 237 ? 0.1099 0.2375 0.1818 0.0451  0.0153  0.0053  378 HIS A CA    
1757 C C     . HIS A 237 ? 0.1115 0.2445 0.1926 0.0422  0.0139  0.0039  378 HIS A C     
1758 O O     . HIS A 237 ? 0.1200 0.2578 0.2002 0.0431  0.0135  0.0030  378 HIS A O     
1759 C CB    . HIS A 237 ? 0.1074 0.2291 0.1718 0.0482  0.0156  0.0032  378 HIS A CB    
1760 C CG    . HIS A 237 ? 0.1540 0.2729 0.2228 0.0461  0.0151  0.0007  378 HIS A CG    
1761 N ND1   . HIS A 237 ? 0.1188 0.2409 0.1904 0.0454  0.0144  -0.0020 378 HIS A ND1   
1762 C CD2   . HIS A 237 ? 0.1289 0.2431 0.2000 0.0447  0.0155  0.0003  378 HIS A CD2   
1763 C CE1   . HIS A 237 ? 0.1539 0.2733 0.2293 0.0436  0.0147  -0.0044 378 HIS A CE1   
1764 N NE2   . HIS A 237 ? 0.1635 0.2779 0.2391 0.0432  0.0153  -0.0030 378 HIS A NE2   
1765 N N1    . LLP A 238 ? 0.1622 0.2696 0.3026 0.0280  0.0145  -0.0189 379 LLP A N1    
1766 C C2    . LLP A 238 ? 0.1781 0.2905 0.3200 0.0271  0.0142  -0.0201 379 LLP A C2    
1767 C "C2'" . LLP A 238 ? 0.1838 0.2957 0.3393 0.0239  0.0132  -0.0232 379 LLP A "C2'" 
1768 C C3    . LLP A 238 ? 0.2150 0.3326 0.3469 0.0288  0.0147  -0.0186 379 LLP A C3    
1769 O O3    . LLP A 238 ? 0.2389 0.3629 0.3723 0.0277  0.0141  -0.0197 379 LLP A O3    
1770 C C4    . LLP A 238 ? 0.1991 0.3149 0.3204 0.0315  0.0156  -0.0162 379 LLP A C4    
1771 C "C4'" . LLP A 238 ? 0.2076 0.3268 0.3182 0.0336  0.0158  -0.0152 379 LLP A "C4'" 
1772 C C5    . LLP A 238 ? 0.1643 0.2750 0.2845 0.0322  0.0162  -0.0153 379 LLP A C5    
1773 C C6    . LLP A 238 ? 0.1911 0.2983 0.3206 0.0304  0.0155  -0.0165 379 LLP A C6    
1774 C "C5'" . LLP A 238 ? 0.2271 0.3352 0.3365 0.0345  0.0174  -0.0136 379 LLP A "C5'" 
1775 O OP4   . LLP A 238 ? 0.2135 0.3219 0.3180 0.0360  0.0163  -0.0092 379 LLP A OP4   
1776 P P     . LLP A 238 ? 0.2476 0.3533 0.3383 0.0386  0.0170  -0.0082 379 LLP A P     
1777 O OP1   . LLP A 238 ? 0.1582 0.2601 0.2488 0.0387  0.0174  -0.0070 379 LLP A OP1   
1778 O OP2   . LLP A 238 ? 0.1927 0.3001 0.2784 0.0400  0.0160  -0.0046 379 LLP A OP2   
1779 O OP3   . LLP A 238 ? 0.2068 0.3132 0.2896 0.0398  0.0183  -0.0117 379 LLP A OP3   
1780 N N     . LLP A 238 ? 0.0877 0.2207 0.1785 0.0386  0.0131  0.0039  379 LLP A N     
1781 C CA    . LLP A 238 ? 0.1021 0.2403 0.2029 0.0356  0.0120  0.0023  379 LLP A CA    
1782 C CB    . LLP A 238 ? 0.1239 0.2589 0.2338 0.0334  0.0115  0.0000  379 LLP A CB    
1783 C CG    . LLP A 238 ? 0.1711 0.3015 0.2750 0.0354  0.0125  -0.0036 379 LLP A CG    
1784 C CD    . LLP A 238 ? 0.1782 0.3067 0.2918 0.0332  0.0127  -0.0066 379 LLP A CD    
1785 C CE    . LLP A 238 ? 0.2569 0.3835 0.3633 0.0346  0.0139  -0.0109 379 LLP A CE    
1786 N NZ    . LLP A 238 ? 0.2658 0.3912 0.3803 0.0324  0.0145  -0.0149 379 LLP A NZ    
1787 C C     . LLP A 238 ? 0.1001 0.2449 0.2070 0.0329  0.0114  0.0054  379 LLP A C     
1788 O O     . LLP A 238 ? 0.0674 0.2173 0.1832 0.0299  0.0105  0.0046  379 LLP A O     
1789 N N     . ILE A 239 ? 0.0924 0.2380 0.1947 0.0335  0.0121  0.0092  380 ILE A N     
1790 C CA    . ILE A 239 ? 0.0812 0.2348 0.1876 0.0308  0.0120  0.0127  380 ILE A CA    
1791 C C     . ILE A 239 ? 0.0990 0.2563 0.1958 0.0338  0.0139  0.0137  380 ILE A C     
1792 O O     . ILE A 239 ? 0.1022 0.2635 0.1974 0.0330  0.0150  0.0172  380 ILE A O     
1793 C CB    . ILE A 239 ? 0.0620 0.2158 0.1756 0.0270  0.0109  0.0174  380 ILE A CB    
1794 C CG1   . ILE A 239 ? 0.1259 0.2888 0.2447 0.0229  0.0107  0.0217  380 ILE A CG1   
1795 C CG2   . ILE A 239 ? 0.0923 0.2417 0.1992 0.0288  0.0116  0.0199  380 ILE A CG2   
1796 C CD1   . ILE A 239 ? 0.0971 0.2598 0.2250 0.0181  0.0086  0.0275  380 ILE A CD1   
1797 N N     . TYR A 240 ? 0.1032 0.2601 0.1945 0.0373  0.0143  0.0107  381 TYR A N     
1798 C CA    . TYR A 240 ? 0.0942 0.2560 0.1794 0.0404  0.0158  0.0109  381 TYR A CA    
1799 C C     . TYR A 240 ? 0.1303 0.2884 0.2069 0.0437  0.0178  0.0118  381 TYR A C     
1800 O O     . TYR A 240 ? 0.0791 0.2420 0.1519 0.0459  0.0195  0.0122  381 TYR A O     
1801 C CB    . TYR A 240 ? 0.1330 0.3055 0.2243 0.0371  0.0160  0.0128  381 TYR A CB    
1802 C CG    . TYR A 240 ? 0.1213 0.2965 0.2222 0.0330  0.0139  0.0118  381 TYR A CG    
1803 C CD1   . TYR A 240 ? 0.1360 0.3130 0.2373 0.0343  0.0129  0.0088  381 TYR A CD1   
1804 C CD2   . TYR A 240 ? 0.1330 0.3087 0.2429 0.0280  0.0129  0.0139  381 TYR A CD2   
1805 C CE1   . TYR A 240 ? 0.1850 0.3650 0.2952 0.0304  0.0112  0.0072  381 TYR A CE1   
1806 C CE2   . TYR A 240 ? 0.1157 0.2931 0.2353 0.0244  0.0111  0.0122  381 TYR A CE2   
1807 C CZ    . TYR A 240 ? 0.1403 0.3201 0.2598 0.0256  0.0105  0.0085  381 TYR A CZ    
1808 O OH    . TYR A 240 ? 0.1827 0.3653 0.3118 0.0218  0.0090  0.0063  381 TYR A OH    
1809 N N     . GLY A 241 ? 0.1083 0.2585 0.1823 0.0441  0.0177  0.0119  382 GLY A N     
1810 C CA    . GLY A 241 ? 0.0938 0.2407 0.1599 0.0468  0.0196  0.0125  382 GLY A CA    
1811 C C     . GLY A 241 ? 0.1178 0.2559 0.1764 0.0510  0.0198  0.0099  382 GLY A C     
1812 O O     . GLY A 241 ? 0.1224 0.2577 0.1814 0.0518  0.0184  0.0080  382 GLY A O     
1813 N N     . PRO A 242 ? 0.1328 0.2670 0.1841 0.0537  0.0217  0.0100  383 PRO A N     
1814 C CA    . PRO A 242 ? 0.1276 0.2529 0.1715 0.0577  0.0221  0.0080  383 PRO A CA    
1815 C C     . PRO A 242 ? 0.1381 0.2572 0.1833 0.0560  0.0206  0.0074  383 PRO A C     
1816 O O     . PRO A 242 ? 0.1467 0.2668 0.1979 0.0522  0.0198  0.0085  383 PRO A O     
1817 C CB    . PRO A 242 ? 0.1635 0.2865 0.2005 0.0599  0.0248  0.0081  383 PRO A CB    
1818 C CG    . PRO A 242 ? 0.1805 0.3136 0.2208 0.0575  0.0261  0.0098  383 PRO A CG    
1819 C CD    . PRO A 242 ? 0.1402 0.2788 0.1899 0.0528  0.0237  0.0120  383 PRO A CD    
1820 N N     . THR A 243 ? 0.1507 0.2639 0.1908 0.0589  0.0203  0.0058  384 THR A N     
1821 C CA    . THR A 243 ? 0.1716 0.2788 0.2110 0.0579  0.0199  0.0049  384 THR A CA    
1822 C C     . THR A 243 ? 0.1570 0.2598 0.1926 0.0580  0.0215  0.0056  384 THR A C     
1823 O O     . THR A 243 ? 0.1445 0.2480 0.1760 0.0597  0.0232  0.0063  384 THR A O     
1824 C CB    . THR A 243 ? 0.1838 0.2869 0.2176 0.0612  0.0196  0.0037  384 THR A CB    
1825 O OG1   . THR A 243 ? 0.1701 0.2685 0.1957 0.0660  0.0211  0.0040  384 THR A OG1   
1826 C CG2   . THR A 243 ? 0.1526 0.2620 0.1900 0.0613  0.0179  0.0032  384 THR A CG2   
1827 N N     . GLY A 244 ? 0.1665 0.2660 0.2040 0.0560  0.0211  0.0052  385 GLY A N     
1828 C CA    . GLY A 244 ? 0.1606 0.2561 0.1940 0.0564  0.0226  0.0057  385 GLY A CA    
1829 C C     . GLY A 244 ? 0.1837 0.2841 0.2225 0.0533  0.0223  0.0083  385 GLY A C     
1830 O O     . GLY A 244 ? 0.1824 0.2770 0.2158 0.0512  0.0225  0.0089  385 GLY A O     
1831 N N     . ILE A 245 ? 0.1318 0.2392 0.1792 0.0506  0.0208  0.0101  386 ILE A N     
1832 C CA    . ILE A 245 ? 0.1304 0.2421 0.1829 0.0467  0.0197  0.0137  386 ILE A CA    
1833 C C     . ILE A 245 ? 0.1468 0.2627 0.2125 0.0435  0.0172  0.0151  386 ILE A C     
1834 O O     . ILE A 245 ? 0.1251 0.2417 0.1942 0.0431  0.0166  0.0132  386 ILE A O     
1835 C CB    . ILE A 245 ? 0.1656 0.2835 0.2143 0.0470  0.0212  0.0154  386 ILE A CB    
1836 C CG1   . ILE A 245 ? 0.1479 0.2685 0.1989 0.0414  0.0195  0.0199  386 ILE A CG1   
1837 C CG2   . ILE A 245 ? 0.1027 0.2268 0.1554 0.0482  0.0212  0.0148  386 ILE A CG2   
1838 C CD1   . ILE A 245 ? 0.1525 0.2661 0.1957 0.0391  0.0193  0.0203  386 ILE A CD1   
1839 N N     . GLY A 246 ? 0.1116 0.2255 0.1825 0.0394  0.0151  0.0178  387 GLY A N     
1840 C CA    . GLY A 246 ? 0.0972 0.2136 0.1815 0.0364  0.0126  0.0196  387 GLY A CA    
1841 C C     . GLY A 246 ? 0.1122 0.2279 0.1999 0.0322  0.0100  0.0247  387 GLY A C     
1842 O O     . GLY A 246 ? 0.1067 0.2206 0.1857 0.0312  0.0102  0.0264  387 GLY A O     
1843 N N     . VAL A 247 ? 0.0712 0.1880 0.1722 0.0296  0.0073  0.0271  388 VAL A N     
1844 C CA    . VAL A 247 ? 0.0839 0.2014 0.1903 0.0254  0.0039  0.0335  388 VAL A CA    
1845 C C     . VAL A 247 ? 0.0978 0.2119 0.2180 0.0245  0.0014  0.0337  388 VAL A C     
1846 O O     . VAL A 247 ? 0.0631 0.1753 0.1914 0.0253  0.0016  0.0298  388 VAL A O     
1847 C CB    . VAL A 247 ? 0.0988 0.2225 0.2088 0.0224  0.0026  0.0386  388 VAL A CB    
1848 C CG1   . VAL A 247 ? 0.1009 0.2248 0.2185 0.0177  -0.0017 0.0462  388 VAL A CG1   
1849 C CG2   . VAL A 247 ? 0.0914 0.2197 0.1883 0.0230  0.0054  0.0386  388 VAL A CG2   
1850 N N     . LEU A 248 ? 0.0884 0.2010 0.2098 0.0223  -0.0012 0.0377  389 LEU A N     
1851 C CA    . LEU A 248 ? 0.0917 0.2024 0.2279 0.0208  -0.0047 0.0403  389 LEU A CA    
1852 C C     . LEU A 248 ? 0.1122 0.2263 0.2525 0.0167  -0.0089 0.0496  389 LEU A C     
1853 O O     . LEU A 248 ? 0.1095 0.2257 0.2401 0.0142  -0.0100 0.0536  389 LEU A O     
1854 C CB    . LEU A 248 ? 0.0986 0.2066 0.2348 0.0215  -0.0049 0.0384  389 LEU A CB    
1855 C CG    . LEU A 248 ? 0.1451 0.2496 0.2922 0.0194  -0.0089 0.0414  389 LEU A CG    
1856 C CD1   . LEU A 248 ? 0.0727 0.1716 0.2294 0.0205  -0.0084 0.0364  389 LEU A CD1   
1857 C CD2   . LEU A 248 ? 0.1093 0.2140 0.2553 0.0195  -0.0092 0.0405  389 LEU A CD2   
1858 N N     . TYR A 249 ? 0.0754 0.1872 0.2254 0.0150  -0.0110 0.0517  390 TYR A N     
1859 C CA    . TYR A 249 ? 0.0960 0.2092 0.2520 0.0109  -0.0157 0.0611  390 TYR A CA    
1860 C C     . TYR A 249 ? 0.1300 0.2364 0.2957 0.0109  -0.0186 0.0618  390 TYR A C     
1861 O O     . TYR A 249 ? 0.1288 0.2292 0.3009 0.0135  -0.0170 0.0550  390 TYR A O     
1862 C CB    . TYR A 249 ? 0.1025 0.2167 0.2649 0.0087  -0.0165 0.0642  390 TYR A CB    
1863 C CG    . TYR A 249 ? 0.1081 0.2200 0.2813 0.0049  -0.0218 0.0733  390 TYR A CG    
1864 C CD1   . TYR A 249 ? 0.1175 0.2359 0.2870 0.0002  -0.0253 0.0834  390 TYR A CD1   
1865 C CD2   . TYR A 249 ? 0.1234 0.2269 0.3102 0.0057  -0.0234 0.0720  390 TYR A CD2   
1866 C CE1   . TYR A 249 ? 0.1157 0.2319 0.2944 -0.0036 -0.0306 0.0928  390 TYR A CE1   
1867 C CE2   . TYR A 249 ? 0.1516 0.2522 0.3491 0.0026  -0.0286 0.0811  390 TYR A CE2   
1868 C CZ    . TYR A 249 ? 0.1315 0.2384 0.3247 -0.0021 -0.0324 0.0918  390 TYR A CZ    
1869 O OH    . TYR A 249 ? 0.1638 0.2680 0.3671 -0.0056 -0.0379 0.1019  390 TYR A OH    
1870 N N     . GLY A 250 ? 0.1327 0.2410 0.2990 0.0079  -0.0229 0.0697  391 GLY A N     
1871 C CA    . GLY A 250 ? 0.1048 0.2074 0.2814 0.0079  -0.0260 0.0714  391 GLY A CA    
1872 C C     . GLY A 250 ? 0.1529 0.2573 0.3339 0.0033  -0.0316 0.0830  391 GLY A C     
1873 O O     . GLY A 250 ? 0.1410 0.2527 0.3128 -0.0002 -0.0333 0.0891  391 GLY A O     
1874 N N     . ARG A 251 ? 0.1475 0.2458 0.3423 0.0030  -0.0346 0.0864  392 ARG A N     
1875 C CA    . ARG A 251 ? 0.1952 0.2948 0.3947 -0.0015 -0.0406 0.0983  392 ARG A CA    
1876 C C     . ARG A 251 ? 0.1836 0.2878 0.3754 -0.0033 -0.0429 0.1017  392 ARG A C     
1877 O O     . ARG A 251 ? 0.1608 0.2641 0.3511 -0.0004 -0.0409 0.0951  392 ARG A O     
1878 C CB    . ARG A 251 ? 0.2175 0.3088 0.4346 -0.0006 -0.0433 0.1004  392 ARG A CB    
1879 C CG    . ARG A 251 ? 0.2486 0.3357 0.4750 -0.0005 -0.0425 0.0998  392 ARG A CG    
1880 C CD    . ARG A 251 ? 0.2437 0.3222 0.4889 0.0004  -0.0453 0.1015  392 ARG A CD    
1881 N NE    . ARG A 251 ? 0.2847 0.3637 0.5360 -0.0041 -0.0517 0.1146  392 ARG A NE    
1882 C CZ    . ARG A 251 ? 0.3804 0.4610 0.6339 -0.0088 -0.0550 0.1243  392 ARG A CZ    
1883 N NH1   . ARG A 251 ? 0.2968 0.3791 0.5481 -0.0094 -0.0527 0.1224  392 ARG A NH1   
1884 N NH2   . ARG A 251 ? 0.2983 0.3799 0.5565 -0.0135 -0.0610 0.1363  392 ARG A NH2   
1885 N N     . GLU A 252 ? 0.1852 0.2953 0.3720 -0.0088 -0.0472 0.1122  393 GLU A N     
1886 C CA    . GLU A 252 ? 0.2122 0.3276 0.3913 -0.0118 -0.0501 0.1163  393 GLU A CA    
1887 C C     . GLU A 252 ? 0.2195 0.3301 0.4085 -0.0093 -0.0516 0.1144  393 GLU A C     
1888 O O     . GLU A 252 ? 0.1975 0.3110 0.3809 -0.0086 -0.0509 0.1106  393 GLU A O     
1889 C CB    . GLU A 252 ? 0.2981 0.4192 0.4733 -0.0189 -0.0552 0.1289  393 GLU A CB    
1890 C CG    . GLU A 252 ? 0.3464 0.4753 0.5097 -0.0236 -0.0579 0.1332  393 GLU A CG    
1891 C CD    . GLU A 252 ? 0.4522 0.5876 0.6102 -0.0315 -0.0625 0.1452  393 GLU A CD    
1892 O OE1   . GLU A 252 ? 0.5032 0.6369 0.6679 -0.0334 -0.0639 0.1508  393 GLU A OE1   
1893 O OE2   . GLU A 252 ? 0.5148 0.6572 0.6618 -0.0366 -0.0648 0.1489  393 GLU A OE2   
1894 N N     . ASP A 253 ? 0.2337 0.3377 0.4384 -0.0081 -0.0539 0.1169  394 ASP A N     
1895 C CA    . ASP A 253 ? 0.2424 0.3434 0.4574 -0.0058 -0.0554 0.1154  394 ASP A CA    
1896 C C     . ASP A 253 ? 0.2441 0.3418 0.4609 0.0001  -0.0500 0.1026  394 ASP A C     
1897 O O     . ASP A 253 ? 0.2518 0.3506 0.4710 0.0017  -0.0502 0.0996  394 ASP A O     
1898 C CB    . ASP A 253 ? 0.2670 0.3625 0.4990 -0.0063 -0.0596 0.1220  394 ASP A CB    
1899 C CG    . ASP A 253 ? 0.4002 0.4879 0.6427 -0.0032 -0.0569 0.1172  394 ASP A CG    
1900 O OD1   . ASP A 253 ? 0.3583 0.4466 0.5959 -0.0049 -0.0557 0.1185  394 ASP A OD1   
1901 O OD2   . ASP A 253 ? 0.4639 0.5456 0.7201 0.0007  -0.0560 0.1122  394 ASP A OD2   
1902 N N     . ALA A 254 ? 0.2065 0.3009 0.4217 0.0029  -0.0453 0.0950  395 ALA A N     
1903 C CA    . ALA A 254 ? 0.2007 0.2931 0.4154 0.0075  -0.0400 0.0830  395 ALA A CA    
1904 C C     . ALA A 254 ? 0.1884 0.2869 0.3889 0.0071  -0.0378 0.0795  395 ALA A C     
1905 O O     . ALA A 254 ? 0.2050 0.3041 0.4061 0.0093  -0.0358 0.0733  395 ALA A O     
1906 C CB    . ALA A 254 ? 0.2069 0.2947 0.4233 0.0100  -0.0357 0.0761  395 ALA A CB    
1907 N N     . LEU A 255 ? 0.1570 0.2606 0.3453 0.0041  -0.0381 0.0834  396 LEU A N     
1908 C CA    . LEU A 255 ? 0.1729 0.2824 0.3486 0.0034  -0.0364 0.0806  396 LEU A CA    
1909 C C     . LEU A 255 ? 0.1985 0.3124 0.3737 0.0005  -0.0404 0.0853  396 LEU A C     
1910 O O     . LEU A 255 ? 0.1928 0.3098 0.3630 0.0009  -0.0388 0.0809  396 LEU A O     
1911 C CB    . LEU A 255 ? 0.1882 0.3031 0.3515 0.0009  -0.0356 0.0835  396 LEU A CB    
1912 C CG    . LEU A 255 ? 0.1600 0.2729 0.3214 0.0038  -0.0310 0.0779  396 LEU A CG    
1913 C CD1   . LEU A 255 ? 0.1679 0.2882 0.3180 0.0010  -0.0306 0.0819  396 LEU A CD1   
1914 C CD2   . LEU A 255 ? 0.1640 0.2743 0.3235 0.0083  -0.0257 0.0672  396 LEU A CD2   
1915 N N     . ALA A 256 ? 0.1942 0.3087 0.3747 -0.0027 -0.0458 0.0946  397 ALA A N     
1916 C CA    . ALA A 256 ? 0.1749 0.2940 0.3555 -0.0057 -0.0501 0.0995  397 ALA A CA    
1917 C C     . ALA A 256 ? 0.2321 0.3491 0.4227 -0.0019 -0.0488 0.0932  397 ALA A C     
1918 O O     . ALA A 256 ? 0.2416 0.3637 0.4291 -0.0035 -0.0500 0.0928  397 ALA A O     
1919 C CB    . ALA A 256 ? 0.1588 0.2784 0.3448 -0.0097 -0.0560 0.1108  397 ALA A CB    
1920 N N     . GLU A 257 ? 0.1894 0.2997 0.3917 0.0027  -0.0463 0.0880  398 GLU A N     
1921 C CA    . GLU A 257 ? 0.2030 0.3124 0.4143 0.0062  -0.0444 0.0812  398 GLU A CA    
1922 C C     . GLU A 257 ? 0.2363 0.3456 0.4416 0.0090  -0.0382 0.0703  398 GLU A C     
1923 O O     . GLU A 257 ? 0.2505 0.3596 0.4625 0.0117  -0.0358 0.0638  398 GLU A O     
1924 C CB    . GLU A 257 ? 0.2633 0.3664 0.4909 0.0092  -0.0451 0.0811  398 GLU A CB    
1925 C CG    . GLU A 257 ? 0.3168 0.4134 0.5476 0.0129  -0.0400 0.0727  398 GLU A CG    
1926 C CD    . GLU A 257 ? 0.3577 0.4480 0.6050 0.0147  -0.0415 0.0743  398 GLU A CD    
1927 O OE1   . GLU A 257 ? 0.3641 0.4550 0.6203 0.0132  -0.0468 0.0828  398 GLU A OE1   
1928 O OE2   . GLU A 257 ? 0.2930 0.3780 0.5447 0.0174  -0.0377 0.0673  398 GLU A OE2   
1929 N N     . THR A 258 ? 0.1852 0.2955 0.3781 0.0081  -0.0356 0.0685  399 THR A N     
1930 C CA    . THR A 258 ? 0.1981 0.3088 0.3844 0.0101  -0.0301 0.0594  399 THR A CA    
1931 C C     . THR A 258 ? 0.1559 0.2735 0.3330 0.0069  -0.0309 0.0607  399 THR A C     
1932 O O     . THR A 258 ? 0.1671 0.2886 0.3353 0.0033  -0.0335 0.0668  399 THR A O     
1933 C CB    . THR A 258 ? 0.1506 0.2583 0.3303 0.0116  -0.0266 0.0564  399 THR A CB    
1934 O OG1   . THR A 258 ? 0.2014 0.3029 0.3901 0.0137  -0.0263 0.0554  399 THR A OG1   
1935 C CG2   . THR A 258 ? 0.1188 0.2266 0.2920 0.0138  -0.0209 0.0475  399 THR A CG2   
1936 N N     . PRO A 259 ? 0.1752 0.2954 0.3540 0.0074  -0.0288 0.0554  400 PRO A N     
1937 C CA    . PRO A 259 ? 0.1691 0.2961 0.3394 0.0035  -0.0294 0.0566  400 PRO A CA    
1938 C C     . PRO A 259 ? 0.1781 0.3042 0.3351 0.0035  -0.0252 0.0534  400 PRO A C     
1939 O O     . PRO A 259 ? 0.1523 0.2737 0.3091 0.0073  -0.0214 0.0490  400 PRO A O     
1940 C CB    . PRO A 259 ? 0.1686 0.2977 0.3461 0.0043  -0.0275 0.0509  400 PRO A CB    
1941 C CG    . PRO A 259 ? 0.2147 0.3378 0.3991 0.0094  -0.0230 0.0436  400 PRO A CG    
1942 C CD    . PRO A 259 ? 0.2153 0.3330 0.4035 0.0110  -0.0253 0.0478  400 PRO A CD    
1943 N N     . PRO A 260 ? 0.1542 0.2794 0.2933 -0.0008 -0.0247 0.0530  401 PRO A N     
1944 C CA    . PRO A 260 ? 0.1770 0.2947 0.2970 -0.0003 -0.0191 0.0471  401 PRO A CA    
1945 C C     . PRO A 260 ? 0.1695 0.2830 0.2908 0.0032  -0.0137 0.0388  401 PRO A C     
1946 O O     . PRO A 260 ? 0.1377 0.2545 0.2707 0.0036  -0.0135 0.0367  401 PRO A O     
1947 C CB    . PRO A 260 ? 0.1507 0.2681 0.2542 -0.0059 -0.0199 0.0478  401 PRO A CB    
1948 C CG    . PRO A 260 ? 0.2098 0.3360 0.3227 -0.0101 -0.0268 0.0555  401 PRO A CG    
1949 C CD    . PRO A 260 ? 0.1549 0.2857 0.2913 -0.0063 -0.0289 0.0571  401 PRO A CD    
1950 N N     . TRP A 261 ? 0.1272 0.2341 0.2368 0.0057  -0.0091 0.0343  402 TRP A N     
1951 C CA    . TRP A 261 ? 0.1277 0.2308 0.2366 0.0086  -0.0041 0.0270  402 TRP A CA    
1952 C C     . TRP A 261 ? 0.1711 0.2678 0.2611 0.0066  -0.0007 0.0233  402 TRP A C     
1953 O O     . TRP A 261 ? 0.1390 0.2359 0.2274 0.0037  -0.0001 0.0215  402 TRP A O     
1954 C CB    . TRP A 261 ? 0.1179 0.2187 0.2299 0.0132  -0.0018 0.0247  402 TRP A CB    
1955 C CG    . TRP A 261 ? 0.1476 0.2456 0.2593 0.0158  0.0030  0.0176  402 TRP A CG    
1956 C CD1   . TRP A 261 ? 0.1606 0.2604 0.2779 0.0151  0.0049  0.0136  402 TRP A CD1   
1957 C CD2   . TRP A 261 ? 0.1165 0.2106 0.2216 0.0190  0.0064  0.0138  402 TRP A CD2   
1958 N NE1   . TRP A 261 ? 0.1508 0.2477 0.2645 0.0173  0.0093  0.0076  402 TRP A NE1   
1959 C CE2   . TRP A 261 ? 0.1636 0.2570 0.2699 0.0199  0.0100  0.0079  402 TRP A CE2   
1960 C CE3   . TRP A 261 ? 0.1152 0.2073 0.2136 0.0211  0.0067  0.0151  402 TRP A CE3   
1961 C CZ2   . TRP A 261 ? 0.1428 0.2333 0.2433 0.0226  0.0134  0.0035  402 TRP A CZ2   
1962 C CZ3   . TRP A 261 ? 0.1317 0.2213 0.2256 0.0242  0.0101  0.0106  402 TRP A CZ3   
1963 C CH2   . TRP A 261 ? 0.1737 0.2624 0.2684 0.0248  0.0132  0.0051  402 TRP A CH2   
1964 N N     . GLN A 262 ? 0.1049 0.1958 0.1810 0.0081  0.0015  0.0223  403 GLN A N     
1965 C CA    . GLN A 262 ? 0.1044 0.1878 0.1627 0.0067  0.0044  0.0191  403 GLN A CA    
1966 C C     . GLN A 262 ? 0.1497 0.2336 0.1995 0.0016  0.0018  0.0223  403 GLN A C     
1967 O O     . GLN A 262 ? 0.1755 0.2642 0.2277 0.0003  -0.0015 0.0271  403 GLN A O     
1968 C CB    . GLN A 262 ? 0.1184 0.1960 0.1667 0.0108  0.0077  0.0168  403 GLN A CB    
1969 C CG    . GLN A 262 ? 0.1565 0.2326 0.2090 0.0148  0.0107  0.0127  403 GLN A CG    
1970 C CD    . GLN A 262 ? 0.2192 0.2914 0.2636 0.0191  0.0131  0.0112  403 GLN A CD    
1971 O OE1   . GLN A 262 ? 0.2411 0.3073 0.2718 0.0194  0.0146  0.0105  403 GLN A OE1   
1972 N NE2   . GLN A 262 ? 0.2132 0.2889 0.2666 0.0224  0.0134  0.0104  403 GLN A NE2   
1973 N N     . GLY A 263 ? 0.1102 0.1892 0.1494 -0.0019 0.0032  0.0197  404 GLY A N     
1974 C CA    . GLY A 263 ? 0.1470 0.2262 0.1769 -0.0076 0.0010  0.0216  404 GLY A CA    
1975 C C     . GLY A 263 ? 0.1490 0.2182 0.1599 -0.0078 0.0044  0.0181  404 GLY A C     
1976 O O     . GLY A 263 ? 0.1496 0.2105 0.1540 -0.0044 0.0084  0.0140  404 GLY A O     
1977 N N     . GLY A 264 ? 0.1823 0.2523 0.1842 -0.0118 0.0027  0.0197  405 GLY A N     
1978 C CA    . GLY A 264 ? 0.1659 0.2261 0.1499 -0.0126 0.0061  0.0155  405 GLY A CA    
1979 C C     . GLY A 264 ? 0.2330 0.2972 0.2103 -0.0150 0.0047  0.0175  405 GLY A C     
1980 O O     . GLY A 264 ? 0.1839 0.2580 0.1678 -0.0187 0.0002  0.0228  405 GLY A O     
1981 N N     . GLY A 265 ? 0.2188 0.2754 0.1830 -0.0128 0.0087  0.0134  406 GLY A N     
1982 C CA    . GLY A 265 ? 0.2250 0.2857 0.1819 -0.0148 0.0086  0.0143  406 GLY A CA    
1983 C C     . GLY A 265 ? 0.2315 0.3023 0.1993 -0.0122 0.0065  0.0196  406 GLY A C     
1984 O O     . GLY A 265 ? 0.2026 0.2751 0.1823 -0.0073 0.0063  0.0211  406 GLY A O     
1985 N N     . ASN A 266 ? 0.2313 0.3090 0.1945 -0.0161 0.0049  0.0223  407 ASN A N     
1986 C CA    . ASN A 266 ? 0.2361 0.3233 0.2071 -0.0149 0.0031  0.0277  407 ASN A CA    
1987 C C     . ASN A 266 ? 0.2408 0.3366 0.2277 -0.0171 -0.0030 0.0353  407 ASN A C     
1988 O O     . ASN A 266 ? 0.2166 0.3213 0.2066 -0.0207 -0.0067 0.0416  407 ASN A O     
1989 C CB    . ASN A 266 ? 0.2131 0.2977 0.1878 -0.0070 0.0070  0.0253  407 ASN A CB    
1990 C CG    . ASN A 266 ? 0.2694 0.3633 0.2489 -0.0067 0.0060  0.0299  407 ASN A CG    
1991 O OD1   . ASN A 266 ? 0.2667 0.3641 0.2367 -0.0095 0.0074  0.0296  407 ASN A OD1   
1992 N ND2   . ASN A 266 ? 0.2151 0.3129 0.2094 -0.0039 0.0037  0.0340  407 ASN A ND2   
1993 N N     . MET A 267 ? 0.1829 0.2765 0.1804 -0.0150 -0.0041 0.0351  408 MET A N     
1994 C CA    . MET A 267 ? 0.1941 0.2958 0.2080 -0.0165 -0.0098 0.0419  408 MET A CA    
1995 C C     . MET A 267 ? 0.1706 0.2773 0.1837 -0.0237 -0.0146 0.0454  408 MET A C     
1996 O O     . MET A 267 ? 0.1839 0.2987 0.2103 -0.0255 -0.0201 0.0523  408 MET A O     
1997 C CB    . MET A 267 ? 0.1763 0.2752 0.2036 -0.0111 -0.0087 0.0399  408 MET A CB    
1998 C CG    . MET A 267 ? 0.1784 0.2699 0.2010 -0.0106 -0.0057 0.0338  408 MET A CG    
1999 S SD    . MET A 267 ? 0.1786 0.2747 0.2065 -0.0169 -0.0099 0.0359  408 MET A SD    
2000 C CE    . MET A 267 ? 0.1566 0.2610 0.2095 -0.0134 -0.0137 0.0409  408 MET A CE    
2001 N N     . ILE A 268 ? 0.1773 0.2797 0.1762 -0.0279 -0.0129 0.0411  409 ILE A N     
2002 C CA    . ILE A 268 ? 0.2126 0.3206 0.2095 -0.0356 -0.0176 0.0442  409 ILE A CA    
2003 C C     . ILE A 268 ? 0.2630 0.3777 0.2501 -0.0415 -0.0202 0.0482  409 ILE A C     
2004 O O     . ILE A 268 ? 0.2780 0.3901 0.2543 -0.0405 -0.0164 0.0455  409 ILE A O     
2005 C CB    . ILE A 268 ? 0.2724 0.3726 0.2585 -0.0386 -0.0149 0.0375  409 ILE A CB    
2006 C CG1   . ILE A 268 ? 0.2740 0.3640 0.2412 -0.0380 -0.0089 0.0303  409 ILE A CG1   
2007 C CG2   . ILE A 268 ? 0.2085 0.3045 0.2049 -0.0343 -0.0131 0.0348  409 ILE A CG2   
2008 C CD1   . ILE A 268 ? 0.3224 0.4149 0.2741 -0.0460 -0.0100 0.0297  409 ILE A CD1   
2009 N N     . ALA A 269 ? 0.2385 0.3626 0.2294 -0.0481 -0.0266 0.0547  410 ALA A N     
2010 C CA    . ALA A 269 ? 0.2644 0.3954 0.2433 -0.0560 -0.0296 0.0580  410 ALA A CA    
2011 C C     . ALA A 269 ? 0.3177 0.4463 0.2822 -0.0631 -0.0291 0.0529  410 ALA A C     
2012 O O     . ALA A 269 ? 0.2709 0.4006 0.2192 -0.0688 -0.0280 0.0509  410 ALA A O     
2013 C CB    . ALA A 269 ? 0.2393 0.3831 0.2312 -0.0595 -0.0379 0.0695  410 ALA A CB    
2014 N N     . ASP A 270 ? 0.2611 0.3870 0.2312 -0.0634 -0.0297 0.0506  411 ASP A N     
2015 C CA    . ASP A 270 ? 0.2810 0.4044 0.2387 -0.0707 -0.0296 0.0459  411 ASP A CA    
2016 C C     . ASP A 270 ? 0.2521 0.3691 0.2170 -0.0679 -0.0276 0.0417  411 ASP A C     
2017 O O     . ASP A 270 ? 0.2460 0.3677 0.2290 -0.0640 -0.0302 0.0458  411 ASP A O     
2018 C CB    . ASP A 270 ? 0.2821 0.4191 0.2408 -0.0799 -0.0376 0.0532  411 ASP A CB    
2019 C CG    . ASP A 270 ? 0.3667 0.5016 0.3098 -0.0888 -0.0373 0.0477  411 ASP A CG    
2020 O OD1   . ASP A 270 ? 0.3997 0.5286 0.3241 -0.0919 -0.0331 0.0416  411 ASP A OD1   
2021 O OD2   . ASP A 270 ? 0.4049 0.5443 0.3546 -0.0928 -0.0411 0.0491  411 ASP A OD2   
2022 N N     . VAL A 271 ? 0.2308 0.3368 0.1817 -0.0701 -0.0229 0.0335  412 VAL A N     
2023 C CA    . VAL A 271 ? 0.2794 0.3784 0.2346 -0.0686 -0.0205 0.0293  412 VAL A CA    
2024 C C     . VAL A 271 ? 0.3222 0.4212 0.2677 -0.0783 -0.0221 0.0265  412 VAL A C     
2025 O O     . VAL A 271 ? 0.2925 0.3856 0.2203 -0.0833 -0.0201 0.0217  412 VAL A O     
2026 C CB    . VAL A 271 ? 0.2791 0.3628 0.2273 -0.0615 -0.0129 0.0220  412 VAL A CB    
2027 C CG1   . VAL A 271 ? 0.2391 0.3145 0.1872 -0.0622 -0.0103 0.0175  412 VAL A CG1   
2028 C CG2   . VAL A 271 ? 0.2283 0.3132 0.1883 -0.0521 -0.0117 0.0247  412 VAL A CG2   
2029 N N     . THR A 272 ? 0.2613 0.3674 0.2189 -0.0811 -0.0258 0.0293  413 THR A N     
2030 C CA    . THR A 272 ? 0.3136 0.4172 0.2639 -0.0891 -0.0259 0.0253  413 THR A CA    
2031 C C     . THR A 272 ? 0.3263 0.4247 0.2859 -0.0852 -0.0226 0.0226  413 THR A C     
2032 O O     . THR A 272 ? 0.2752 0.3761 0.2495 -0.0774 -0.0220 0.0251  413 THR A O     
2033 C CB    . THR A 272 ? 0.3088 0.4285 0.2648 -0.0979 -0.0337 0.0312  413 THR A CB    
2034 O OG1   . THR A 272 ? 0.3158 0.4472 0.2945 -0.0944 -0.0377 0.0374  413 THR A OG1   
2035 C CG2   . THR A 272 ? 0.3401 0.4679 0.2894 -0.1016 -0.0379 0.0360  413 THR A CG2   
2036 N N     . LEU A 273 ? 0.2683 0.3595 0.2190 -0.0911 -0.0205 0.0174  414 LEU A N     
2037 C CA    . LEU A 273 ? 0.3411 0.4271 0.2986 -0.0884 -0.0169 0.0147  414 LEU A CA    
2038 C C     . LEU A 273 ? 0.3118 0.4134 0.2918 -0.0868 -0.0209 0.0202  414 LEU A C     
2039 O O     . LEU A 273 ? 0.2800 0.3803 0.2704 -0.0807 -0.0179 0.0194  414 LEU A O     
2040 C CB    . LEU A 273 ? 0.3333 0.4101 0.2778 -0.0966 -0.0147 0.0092  414 LEU A CB    
2041 C CG    . LEU A 273 ? 0.3544 0.4127 0.2778 -0.0970 -0.0096 0.0025  414 LEU A CG    
2042 C CD1   . LEU A 273 ? 0.3750 0.4249 0.2863 -0.1066 -0.0084 -0.0025 414 LEU A CD1   
2043 C CD2   . LEU A 273 ? 0.3032 0.3491 0.2263 -0.0868 -0.0039 0.0002  414 LEU A CD2   
2044 N N     . GLU A 274 ? 0.2730 0.3899 0.2611 -0.0920 -0.0276 0.0258  415 GLU A N     
2045 C CA    . GLU A 274 ? 0.2854 0.4178 0.2963 -0.0904 -0.0317 0.0310  415 GLU A CA    
2046 C C     . GLU A 274 ? 0.3056 0.4446 0.3320 -0.0817 -0.0340 0.0367  415 GLU A C     
2047 O O     . GLU A 274 ? 0.2145 0.3609 0.2603 -0.0768 -0.0345 0.0387  415 GLU A O     
2048 C CB    . GLU A 274 ? 0.3215 0.4680 0.3354 -0.1000 -0.0385 0.0349  415 GLU A CB    
2049 C CG    . GLU A 274 ? 0.4524 0.6030 0.4555 -0.1053 -0.0436 0.0387  415 GLU A CG    
2050 C CD    . GLU A 274 ? 0.5564 0.6938 0.5333 -0.1121 -0.0402 0.0321  415 GLU A CD    
2051 O OE1   . GLU A 274 ? 0.5037 0.6255 0.4697 -0.1110 -0.0335 0.0246  415 GLU A OE1   
2052 O OE2   . GLU A 274 ? 0.6298 0.7727 0.5972 -0.1188 -0.0445 0.0343  415 GLU A OE2   
2053 N N     . ARG A 275 ? 0.2551 0.3913 0.2736 -0.0797 -0.0349 0.0390  416 ARG A N     
2054 C CA    . ARG A 275 ? 0.2522 0.3950 0.2854 -0.0727 -0.0378 0.0452  416 ARG A CA    
2055 C C     . ARG A 275 ? 0.2708 0.4056 0.2908 -0.0699 -0.0357 0.0449  416 ARG A C     
2056 O O     . ARG A 275 ? 0.2221 0.3533 0.2244 -0.0756 -0.0356 0.0432  416 ARG A O     
2057 C CB    . ARG A 275 ? 0.2625 0.4224 0.3095 -0.0766 -0.0465 0.0541  416 ARG A CB    
2058 C CG    . ARG A 275 ? 0.2598 0.4260 0.3240 -0.0695 -0.0499 0.0611  416 ARG A CG    
2059 C CD    . ARG A 275 ? 0.2731 0.4546 0.3473 -0.0740 -0.0592 0.0709  416 ARG A CD    
2060 N NE    . ARG A 275 ? 0.2582 0.4441 0.3490 -0.0673 -0.0626 0.0782  416 ARG A NE    
2061 C CZ    . ARG A 275 ? 0.3095 0.5040 0.4033 -0.0698 -0.0698 0.0876  416 ARG A CZ    
2062 N NH1   . ARG A 275 ? 0.3192 0.5183 0.3999 -0.0783 -0.0738 0.0906  416 ARG A NH1   
2063 N NH2   . ARG A 275 ? 0.2901 0.4817 0.3957 -0.0624 -0.0704 0.0924  416 ARG A NH2   
2064 N N     . SER A 276 ? 0.2292 0.3619 0.2584 -0.0614 -0.0339 0.0462  417 SER A N     
2065 C CA    . SER A 276 ? 0.2368 0.3648 0.2573 -0.0583 -0.0324 0.0470  417 SER A CA    
2066 C C     . SER A 276 ? 0.2601 0.3985 0.2965 -0.0554 -0.0379 0.0557  417 SER A C     
2067 O O     . SER A 276 ? 0.2350 0.3797 0.2911 -0.0519 -0.0404 0.0590  417 SER A O     
2068 C CB    . SER A 276 ? 0.2119 0.3270 0.2275 -0.0509 -0.0250 0.0405  417 SER A CB    
2069 O OG    . SER A 276 ? 0.2312 0.3354 0.2315 -0.0534 -0.0202 0.0331  417 SER A OG    
2070 N N     . LEU A 277 ? 0.2510 0.3908 0.2788 -0.0571 -0.0396 0.0594  418 LEU A N     
2071 C CA    . LEU A 277 ? 0.2273 0.3747 0.2672 -0.0546 -0.0442 0.0679  418 LEU A CA    
2072 C C     . LEU A 277 ? 0.2445 0.3839 0.2802 -0.0483 -0.0390 0.0653  418 LEU A C     
2073 O O     . LEU A 277 ? 0.1962 0.3269 0.2153 -0.0481 -0.0334 0.0586  418 LEU A O     
2074 C CB    . LEU A 277 ? 0.2610 0.4178 0.2939 -0.0625 -0.0505 0.0752  418 LEU A CB    
2075 C CG    . LEU A 277 ? 0.2686 0.4325 0.2983 -0.0707 -0.0549 0.0762  418 LEU A CG    
2076 C CD1   . LEU A 277 ? 0.3596 0.5304 0.3747 -0.0795 -0.0592 0.0808  418 LEU A CD1   
2077 C CD2   . LEU A 277 ? 0.2603 0.4341 0.3135 -0.0689 -0.0608 0.0827  418 LEU A CD2   
2078 N N     . TYR A 278 ? 0.2052 0.3479 0.2564 -0.0433 -0.0412 0.0707  419 TYR A N     
2079 C CA    . TYR A 278 ? 0.1989 0.3349 0.2492 -0.0369 -0.0363 0.0679  419 TYR A CA    
2080 C C     . TYR A 278 ? 0.2420 0.3829 0.2902 -0.0387 -0.0393 0.0750  419 TYR A C     
2081 O O     . TYR A 278 ? 0.2090 0.3589 0.2641 -0.0428 -0.0461 0.0839  419 TYR A O     
2082 C CB    . TYR A 278 ? 0.2038 0.3382 0.2732 -0.0297 -0.0353 0.0669  419 TYR A CB    
2083 C CG    . TYR A 278 ? 0.2681 0.3988 0.3380 -0.0291 -0.0322 0.0601  419 TYR A CG    
2084 C CD1   . TYR A 278 ? 0.2735 0.3951 0.3260 -0.0298 -0.0264 0.0523  419 TYR A CD1   
2085 C CD2   . TYR A 278 ? 0.2645 0.4012 0.3516 -0.0286 -0.0352 0.0619  419 TYR A CD2   
2086 C CE1   . TYR A 278 ? 0.3169 0.4349 0.3687 -0.0302 -0.0237 0.0468  419 TYR A CE1   
2087 C CE2   . TYR A 278 ? 0.2127 0.3471 0.2995 -0.0290 -0.0321 0.0557  419 TYR A CE2   
2088 C CZ    . TYR A 278 ? 0.2752 0.4000 0.3437 -0.0302 -0.0265 0.0485  419 TYR A CZ    
2089 O OH    . TYR A 278 ? 0.3074 0.4295 0.3746 -0.0315 -0.0234 0.0430  419 TYR A OH    
2090 N N     . GLN A 279 ? 0.1755 0.3110 0.2144 -0.0358 -0.0342 0.0712  420 GLN A N     
2091 C CA    . GLN A 279 ? 0.2487 0.3889 0.2862 -0.0371 -0.0360 0.0774  420 GLN A CA    
2092 C C     . GLN A 279 ? 0.2133 0.3554 0.2709 -0.0324 -0.0387 0.0830  420 GLN A C     
2093 O O     . GLN A 279 ? 0.1932 0.3319 0.2644 -0.0271 -0.0378 0.0804  420 GLN A O     
2094 C CB    . GLN A 279 ? 0.2826 0.4172 0.3042 -0.0355 -0.0292 0.0709  420 GLN A CB    
2095 C CG    . GLN A 279 ? 0.3226 0.4565 0.3240 -0.0413 -0.0271 0.0666  420 GLN A CG    
2096 C CD    . GLN A 279 ? 0.3941 0.5265 0.3815 -0.0409 -0.0218 0.0628  420 GLN A CD    
2097 O OE1   . GLN A 279 ? 0.4603 0.5981 0.4507 -0.0409 -0.0227 0.0678  420 GLN A OE1   
2098 N NE2   . GLN A 279 ? 0.4034 0.5283 0.3760 -0.0406 -0.0162 0.0538  420 GLN A NE2   
2099 N N     . GLY A 280 ? 0.1877 0.3350 0.2466 -0.0348 -0.0419 0.0907  421 GLY A N     
2100 C CA    . GLY A 280 ? 0.2039 0.3513 0.2793 -0.0305 -0.0435 0.0954  421 GLY A CA    
2101 C C     . GLY A 280 ? 0.2216 0.3626 0.2937 -0.0250 -0.0367 0.0885  421 GLY A C     
2102 O O     . GLY A 280 ? 0.1566 0.2932 0.2138 -0.0240 -0.0307 0.0805  421 GLY A O     
2103 N N     . PRO A 281 ? 0.2127 0.3530 0.2993 -0.0213 -0.0376 0.0916  422 PRO A N     
2104 C CA    . PRO A 281 ? 0.1945 0.3300 0.2796 -0.0164 -0.0318 0.0856  422 PRO A CA    
2105 C C     . PRO A 281 ? 0.2038 0.3427 0.2753 -0.0195 -0.0296 0.0869  422 PRO A C     
2106 O O     . PRO A 281 ? 0.1968 0.3422 0.2643 -0.0256 -0.0336 0.0947  422 PRO A O     
2107 C CB    . PRO A 281 ? 0.2182 0.3528 0.3241 -0.0129 -0.0345 0.0893  422 PRO A CB    
2108 C CG    . PRO A 281 ? 0.2787 0.4189 0.3942 -0.0173 -0.0423 0.1002  422 PRO A CG    
2109 C CD    . PRO A 281 ? 0.2296 0.3732 0.3356 -0.0216 -0.0444 0.1006  422 PRO A CD    
2110 N N     . PRO A 282 ? 0.2095 0.3449 0.2736 -0.0156 -0.0233 0.0797  423 PRO A N     
2111 C CA    . PRO A 282 ? 0.1791 0.3075 0.2466 -0.0088 -0.0186 0.0710  423 PRO A CA    
2112 C C     . PRO A 282 ? 0.1954 0.3186 0.2522 -0.0078 -0.0156 0.0639  423 PRO A C     
2113 O O     . PRO A 282 ? 0.1657 0.2835 0.2268 -0.0032 -0.0132 0.0582  423 PRO A O     
2114 C CB    . PRO A 282 ? 0.1932 0.3222 0.2552 -0.0064 -0.0140 0.0680  423 PRO A CB    
2115 C CG    . PRO A 282 ? 0.2238 0.3584 0.2713 -0.0117 -0.0135 0.0705  423 PRO A CG    
2116 C CD    . PRO A 282 ? 0.2000 0.3397 0.2517 -0.0181 -0.0203 0.0799  423 PRO A CD    
2117 N N     . ASN A 283 ? 0.1387 0.2636 0.1814 -0.0126 -0.0157 0.0639  424 ASN A N     
2118 C CA    . ASN A 283 ? 0.1619 0.2808 0.1933 -0.0123 -0.0126 0.0569  424 ASN A CA    
2119 C C     . ASN A 283 ? 0.1807 0.2962 0.2222 -0.0106 -0.0142 0.0554  424 ASN A C     
2120 O O     . ASN A 283 ? 0.1396 0.2483 0.1762 -0.0077 -0.0104 0.0485  424 ASN A O     
2121 C CB    . ASN A 283 ? 0.2223 0.3445 0.2397 -0.0193 -0.0140 0.0584  424 ASN A CB    
2122 C CG    . ASN A 283 ? 0.2743 0.4010 0.2808 -0.0216 -0.0118 0.0592  424 ASN A CG    
2123 O OD1   . ASN A 283 ? 0.2351 0.3679 0.2481 -0.0225 -0.0138 0.0652  424 ASN A OD1   
2124 N ND2   . ASN A 283 ? 0.3121 0.4356 0.3022 -0.0227 -0.0073 0.0527  424 ASN A ND2   
2125 N N     . LYS A 284 ? 0.1626 0.2833 0.2186 -0.0124 -0.0199 0.0621  425 LYS A N     
2126 C CA    . LYS A 284 ? 0.1486 0.2683 0.2164 -0.0111 -0.0216 0.0611  425 LYS A CA    
2127 C C     . LYS A 284 ? 0.1947 0.3077 0.2664 -0.0049 -0.0167 0.0536  425 LYS A C     
2128 O O     . LYS A 284 ? 0.1330 0.2434 0.2061 -0.0043 -0.0155 0.0495  425 LYS A O     
2129 C CB    . LYS A 284 ? 0.1566 0.2826 0.2430 -0.0119 -0.0279 0.0694  425 LYS A CB    
2130 C CG    . LYS A 284 ? 0.1955 0.3219 0.2983 -0.0096 -0.0297 0.0685  425 LYS A CG    
2131 C CD    . LYS A 284 ? 0.2034 0.3354 0.3253 -0.0097 -0.0360 0.0772  425 LYS A CD    
2132 C CE    . LYS A 284 ? 0.2381 0.3728 0.3777 -0.0080 -0.0387 0.0774  425 LYS A CE    
2133 N NZ    . LYS A 284 ? 0.2191 0.3504 0.3727 -0.0062 -0.0418 0.0821  425 LYS A NZ    
2134 N N     . PHE A 285 ? 0.1692 0.2804 0.2422 -0.0008 -0.0139 0.0519  426 PHE A N     
2135 C CA    . PHE A 285 ? 0.1861 0.2924 0.2639 0.0046  -0.0099 0.0456  426 PHE A CA    
2136 C C     . PHE A 285 ? 0.1862 0.2869 0.2492 0.0074  -0.0045 0.0395  426 PHE A C     
2137 O O     . PHE A 285 ? 0.1823 0.2796 0.2477 0.0118  -0.0013 0.0347  426 PHE A O     
2138 C CB    . PHE A 285 ? 0.1335 0.2423 0.2272 0.0074  -0.0114 0.0480  426 PHE A CB    
2139 C CG    . PHE A 285 ? 0.1724 0.2857 0.2829 0.0057  -0.0168 0.0541  426 PHE A CG    
2140 C CD1   . PHE A 285 ? 0.1703 0.2835 0.2919 0.0069  -0.0174 0.0518  426 PHE A CD1   
2141 C CD2   . PHE A 285 ? 0.1813 0.2992 0.2968 0.0028  -0.0215 0.0625  426 PHE A CD2   
2142 C CE1   . PHE A 285 ? 0.1576 0.2753 0.2963 0.0061  -0.0225 0.0574  426 PHE A CE1   
2143 C CE2   . PHE A 285 ? 0.1909 0.3126 0.3227 0.0016  -0.0271 0.0689  426 PHE A CE2   
2144 C CZ    . PHE A 285 ? 0.1888 0.3103 0.3328 0.0036  -0.0276 0.0662  426 PHE A CZ    
2145 N N     . GLU A 286 ? 0.1565 0.2565 0.2046 0.0050  -0.0033 0.0393  427 GLU A N     
2146 C CA    . GLU A 286 ? 0.1782 0.2727 0.2134 0.0084  0.0019  0.0337  427 GLU A CA    
2147 C C     . GLU A 286 ? 0.2145 0.3028 0.2361 0.0062  0.0037  0.0298  427 GLU A C     
2148 O O     . GLU A 286 ? 0.2081 0.2974 0.2197 0.0021  0.0032  0.0308  427 GLU A O     
2149 C CB    . GLU A 286 ? 0.1515 0.2503 0.1817 0.0083  0.0028  0.0356  427 GLU A CB    
2150 C CG    . GLU A 286 ? 0.1800 0.2848 0.2240 0.0094  0.0007  0.0400  427 GLU A CG    
2151 C CD    . GLU A 286 ? 0.2368 0.3471 0.2767 0.0087  0.0016  0.0423  427 GLU A CD    
2152 O OE1   . GLU A 286 ? 0.2275 0.3391 0.2547 0.0061  0.0031  0.0419  427 GLU A OE1   
2153 O OE2   . GLU A 286 ? 0.2043 0.3182 0.2542 0.0101  0.0009  0.0446  427 GLU A OE2   
2154 N N     . ALA A 287 ? 0.1839 0.2657 0.2046 0.0086  0.0059  0.0253  428 ALA A N     
2155 C CA    . ALA A 287 ? 0.1960 0.2710 0.2053 0.0060  0.0073  0.0219  428 ALA A CA    
2156 C C     . ALA A 287 ? 0.2172 0.2837 0.2134 0.0098  0.0121  0.0167  428 ALA A C     
2157 O O     . ALA A 287 ? 0.1847 0.2489 0.1833 0.0152  0.0144  0.0146  428 ALA A O     
2158 C CB    . ALA A 287 ? 0.1406 0.2141 0.1570 0.0052  0.0066  0.0208  428 ALA A CB    
2159 N N     . GLY A 288 ? 0.1933 0.2552 0.1760 0.0070  0.0135  0.0146  429 GLY A N     
2160 C CA    . GLY A 288 ? 0.2430 0.2959 0.2138 0.0108  0.0180  0.0095  429 GLY A CA    
2161 C C     . GLY A 288 ? 0.2827 0.3399 0.2520 0.0145  0.0199  0.0095  429 GLY A C     
2162 O O     . GLY A 288 ? 0.2264 0.2933 0.2031 0.0136  0.0179  0.0135  429 GLY A O     
2163 N N     . THR A 289 ? 0.2522 0.3018 0.2121 0.0188  0.0241  0.0048  430 THR A N     
2164 C CA    . THR A 289 ? 0.2696 0.3235 0.2285 0.0231  0.0266  0.0039  430 THR A CA    
2165 C C     . THR A 289 ? 0.2733 0.3347 0.2449 0.0270  0.0254  0.0069  430 THR A C     
2166 O O     . THR A 289 ? 0.2421 0.3000 0.2183 0.0306  0.0254  0.0063  430 THR A O     
2167 C CB    . THR A 289 ? 0.2785 0.3220 0.2276 0.0283  0.0311  -0.0017 430 THR A CB    
2168 O OG1   . THR A 289 ? 0.2811 0.3166 0.2183 0.0241  0.0323  -0.0052 430 THR A OG1   
2169 C CG2   . THR A 289 ? 0.2862 0.3354 0.2354 0.0334  0.0340  -0.0031 430 THR A CG2   
2170 N N     . GLY A 290 ? 0.2509 0.3227 0.2275 0.0258  0.0243  0.0101  431 GLY A N     
2171 C CA    . GLY A 290 ? 0.2537 0.3326 0.2420 0.0290  0.0234  0.0126  431 GLY A CA    
2172 C C     . GLY A 290 ? 0.2450 0.3226 0.2317 0.0361  0.0269  0.0091  431 GLY A C     
2173 O O     . GLY A 290 ? 0.2212 0.2936 0.1983 0.0390  0.0303  0.0051  431 GLY A O     
2174 N N     . ASN A 291 ? 0.1888 0.2714 0.1856 0.0390  0.0259  0.0106  432 ASN A N     
2175 C CA    . ASN A 291 ? 0.1949 0.2792 0.1922 0.0455  0.0285  0.0083  432 ASN A CA    
2176 C C     . ASN A 291 ? 0.1860 0.2805 0.1843 0.0451  0.0298  0.0094  432 ASN A C     
2177 O O     . ASN A 291 ? 0.1645 0.2681 0.1719 0.0449  0.0286  0.0121  432 ASN A O     
2178 C CB    . ASN A 291 ? 0.1688 0.2551 0.1758 0.0479  0.0268  0.0091  432 ASN A CB    
2179 C CG    . ASN A 291 ? 0.2118 0.3005 0.2193 0.0543  0.0288  0.0070  432 ASN A CG    
2180 O OD1   . ASN A 291 ? 0.1995 0.2892 0.2015 0.0575  0.0316  0.0052  432 ASN A OD1   
2181 N ND2   . ASN A 291 ? 0.2065 0.2965 0.2205 0.0564  0.0275  0.0070  432 ASN A ND2   
2182 N N     . ILE A 292 ? 0.1902 0.2833 0.1786 0.0446  0.0327  0.0070  433 ILE A N     
2183 C CA    . ILE A 292 ? 0.1874 0.2910 0.1753 0.0423  0.0341  0.0081  433 ILE A CA    
2184 C C     . ILE A 292 ? 0.2026 0.3144 0.1964 0.0478  0.0363  0.0072  433 ILE A C     
2185 O O     . ILE A 292 ? 0.1748 0.2976 0.1757 0.0453  0.0353  0.0106  433 ILE A O     
2186 C CB    . ILE A 292 ? 0.1909 0.2912 0.1662 0.0403  0.0372  0.0045  433 ILE A CB    
2187 C CG1   . ILE A 292 ? 0.2730 0.3676 0.2434 0.0335  0.0343  0.0063  433 ILE A CG1   
2188 C CG2   . ILE A 292 ? 0.1803 0.2926 0.1542 0.0375  0.0393  0.0053  433 ILE A CG2   
2189 C CD1   . ILE A 292 ? 0.3685 0.4534 0.3258 0.0331  0.0372  0.0008  433 ILE A CD1   
2190 N N     . ALA A 293 ? 0.1887 0.2953 0.1800 0.0550  0.0389  0.0030  434 ALA A N     
2191 C CA    . ALA A 293 ? 0.1825 0.2979 0.1795 0.0606  0.0409  0.0019  434 ALA A CA    
2192 C C     . ALA A 293 ? 0.1431 0.2661 0.1518 0.0597  0.0376  0.0058  434 ALA A C     
2193 O O     . ALA A 293 ? 0.1422 0.2755 0.1569 0.0588  0.0376  0.0072  434 ALA A O     
2194 C CB    . ALA A 293 ? 0.1642 0.2698 0.1575 0.0677  0.0423  -0.0021 434 ALA A CB    
2195 N N     . ASP A 294 ? 0.1704 0.2871 0.1825 0.0588  0.0344  0.0072  435 ASP A N     
2196 C CA    . ASP A 294 ? 0.1601 0.2833 0.1831 0.0583  0.0317  0.0096  435 ASP A CA    
2197 C C     . ASP A 294 ? 0.1338 0.2641 0.1637 0.0515  0.0294  0.0140  435 ASP A C     
2198 O O     . ASP A 294 ? 0.1194 0.2581 0.1584 0.0507  0.0283  0.0158  435 ASP A O     
2199 C CB    . ASP A 294 ? 0.1376 0.2521 0.1620 0.0593  0.0293  0.0089  435 ASP A CB    
2200 C CG    . ASP A 294 ? 0.2679 0.3734 0.2858 0.0641  0.0299  0.0058  435 ASP A CG    
2201 O OD1   . ASP A 294 ? 0.2199 0.3272 0.2364 0.0669  0.0308  0.0046  435 ASP A OD1   
2202 O OD2   . ASP A 294 ? 0.2601 0.3572 0.2743 0.0652  0.0296  0.0050  435 ASP A OD2   
2203 N N     . ALA A 295 ? 0.1150 0.2418 0.1411 0.0463  0.0283  0.0160  436 ALA A N     
2204 C CA    . ALA A 295 ? 0.1402 0.2741 0.1721 0.0399  0.0260  0.0212  436 ALA A CA    
2205 C C     . ALA A 295 ? 0.1061 0.2515 0.1379 0.0392  0.0284  0.0220  436 ALA A C     
2206 O O     . ALA A 295 ? 0.1271 0.2807 0.1673 0.0360  0.0268  0.0258  436 ALA A O     
2207 C CB    . ALA A 295 ? 0.1303 0.2595 0.1568 0.0345  0.0242  0.0235  436 ALA A CB    
2208 N N     . VAL A 296 ? 0.1330 0.2791 0.1555 0.0420  0.0325  0.0182  437 VAL A N     
2209 C CA    . VAL A 296 ? 0.1194 0.2776 0.1418 0.0418  0.0357  0.0181  437 VAL A CA    
2210 C C     . VAL A 296 ? 0.1379 0.3039 0.1699 0.0459  0.0360  0.0176  437 VAL A C     
2211 O O     . VAL A 296 ? 0.1503 0.3262 0.1878 0.0424  0.0356  0.0202  437 VAL A O     
2212 C CB    . VAL A 296 ? 0.1429 0.2993 0.1540 0.0451  0.0406  0.0127  437 VAL A CB    
2213 C CG1   . VAL A 296 ? 0.1477 0.3159 0.1596 0.0461  0.0442  0.0110  437 VAL A CG1   
2214 C CG2   . VAL A 296 ? 0.1412 0.2927 0.1427 0.0390  0.0401  0.0136  437 VAL A CG2   
2215 N N     . GLY A 297 ? 0.1543 0.3104 0.1864 0.0510  0.0346  0.0143  438 GLY A N     
2216 C CA    . GLY A 297 ? 0.1331 0.2902 0.1715 0.0523  0.0325  0.0136  438 GLY A CA    
2217 C C     . GLY A 297 ? 0.1439 0.3052 0.1923 0.0475  0.0292  0.0175  438 GLY A C     
2218 O O     . GLY A 297 ? 0.1479 0.3156 0.2020 0.0457  0.0283  0.0184  438 GLY A O     
2219 N N     . LEU A 298 ? 0.1126 0.2700 0.1637 0.0452  0.0272  0.0198  439 LEU A N     
2220 C CA    . LEU A 298 ? 0.1054 0.2653 0.1670 0.0404  0.0239  0.0235  439 LEU A CA    
2221 C C     . LEU A 298 ? 0.1196 0.2914 0.1859 0.0350  0.0241  0.0286  439 LEU A C     
2222 O O     . LEU A 298 ? 0.1196 0.2949 0.1939 0.0316  0.0221  0.0307  439 LEU A O     
2223 C CB    . LEU A 298 ? 0.0912 0.2448 0.1558 0.0392  0.0218  0.0251  439 LEU A CB    
2224 C CG    . LEU A 298 ? 0.1209 0.2751 0.1972 0.0341  0.0181  0.0289  439 LEU A CG    
2225 C CD1   . LEU A 298 ? 0.0682 0.2210 0.1500 0.0342  0.0169  0.0259  439 LEU A CD1   
2226 C CD2   . LEU A 298 ? 0.1152 0.2591 0.1927 0.0328  0.0156  0.0293  439 LEU A CD2   
2227 N N     . GLY A 299 ? 0.1330 0.3076 0.1921 0.0329  0.0260  0.0304  440 GLY A N     
2228 C CA    . GLY A 299 ? 0.1283 0.3131 0.1888 0.0267  0.0261  0.0352  440 GLY A CA    
2229 C C     . GLY A 299 ? 0.1433 0.3387 0.2067 0.0280  0.0286  0.0335  440 GLY A C     
2230 O O     . GLY A 299 ? 0.1552 0.3579 0.2254 0.0228  0.0272  0.0376  440 GLY A O     
2231 N N     . GLU A 300 ? 0.1077 0.2997 0.1648 0.0341  0.0311  0.0273  441 GLU A N     
2232 C CA    . GLU A 300 ? 0.1527 0.3503 0.2120 0.0351  0.0319  0.0252  441 GLU A CA    
2233 C C     . GLU A 300 ? 0.1531 0.3493 0.2217 0.0338  0.0285  0.0259  441 GLU A C     
2234 O O     . GLU A 300 ? 0.1220 0.3265 0.1959 0.0305  0.0282  0.0275  441 GLU A O     
2235 C CB    . GLU A 300 ? 0.1641 0.3570 0.2167 0.0422  0.0344  0.0191  441 GLU A CB    
2236 C CG    . GLU A 300 ? 0.1465 0.3474 0.2011 0.0435  0.0360  0.0170  441 GLU A CG    
2237 C CD    . GLU A 300 ? 0.2349 0.4485 0.2888 0.0386  0.0388  0.0190  441 GLU A CD    
2238 O OE1   . GLU A 300 ? 0.3050 0.5197 0.3524 0.0365  0.0410  0.0196  441 GLU A OE1   
2239 O OE2   . GLU A 300 ? 0.2554 0.4781 0.3148 0.0363  0.0388  0.0199  441 GLU A OE2   
2240 N N     . ALA A 301 ? 0.1067 0.2927 0.1769 0.0360  0.0260  0.0244  442 ALA A N     
2241 C CA    . ALA A 301 ? 0.1263 0.3104 0.2046 0.0343  0.0231  0.0240  442 ALA A CA    
2242 C C     . ALA A 301 ? 0.1430 0.3323 0.2305 0.0273  0.0211  0.0293  442 ALA A C     
2243 O O     . ALA A 301 ? 0.1079 0.3016 0.2024 0.0244  0.0199  0.0297  442 ALA A O     
2244 C CB    . ALA A 301 ? 0.0881 0.2604 0.1656 0.0372  0.0212  0.0211  442 ALA A CB    
2245 N N     . ILE A 302 ? 0.1078 0.2969 0.1958 0.0243  0.0205  0.0338  443 ILE A N     
2246 C CA    . ILE A 302 ? 0.1217 0.3147 0.2188 0.0172  0.0179  0.0403  443 ILE A CA    
2247 C C     . ILE A 302 ? 0.1406 0.3455 0.2380 0.0128  0.0194  0.0434  443 ILE A C     
2248 O O     . ILE A 302 ? 0.1398 0.3478 0.2455 0.0078  0.0176  0.0462  443 ILE A O     
2249 C CB    . ILE A 302 ? 0.1320 0.3225 0.2292 0.0148  0.0164  0.0455  443 ILE A CB    
2250 C CG1   . ILE A 302 ? 0.1054 0.2841 0.2065 0.0174  0.0138  0.0431  443 ILE A CG1   
2251 C CG2   . ILE A 302 ? 0.1342 0.3293 0.2378 0.0064  0.0137  0.0538  443 ILE A CG2   
2252 C CD1   . ILE A 302 ? 0.1790 0.3503 0.2769 0.0157  0.0119  0.0464  443 ILE A CD1   
2253 N N     . ARG A 303 ? 0.1562 0.3677 0.2447 0.0142  0.0230  0.0424  444 ARG A N     
2254 C CA    . ARG A 303 ? 0.1833 0.4065 0.2715 0.0100  0.0249  0.0445  444 ARG A CA    
2255 C C     . ARG A 303 ? 0.1885 0.4142 0.2812 0.0116  0.0249  0.0407  444 ARG A C     
2256 O O     . ARG A 303 ? 0.1474 0.3810 0.2452 0.0061  0.0246  0.0437  444 ARG A O     
2257 C CB    . ARG A 303 ? 0.1827 0.4115 0.2601 0.0121  0.0293  0.0423  444 ARG A CB    
2258 C CG    . ARG A 303 ? 0.2252 0.4560 0.2976 0.0070  0.0294  0.0477  444 ARG A CG    
2259 C CD    . ARG A 303 ? 0.2680 0.5051 0.3291 0.0075  0.0341  0.0448  444 ARG A CD    
2260 N NE    . ARG A 303 ? 0.2570 0.4870 0.3114 0.0161  0.0367  0.0371  444 ARG A NE    
2261 C CZ    . ARG A 303 ? 0.2728 0.4947 0.3222 0.0187  0.0367  0.0360  444 ARG A CZ    
2262 N NH1   . ARG A 303 ? 0.2185 0.4379 0.2683 0.0134  0.0339  0.0418  444 ARG A NH1   
2263 N NH2   . ARG A 303 ? 0.2356 0.4496 0.2792 0.0264  0.0389  0.0290  444 ARG A NH2   
2264 N N     . TYR A 304 ? 0.1404 0.3598 0.2312 0.0185  0.0252  0.0344  445 TYR A N     
2265 C CA    . TYR A 304 ? 0.1926 0.4149 0.2881 0.0195  0.0246  0.0313  445 TYR A CA    
2266 C C     . TYR A 304 ? 0.1623 0.3837 0.2681 0.0140  0.0213  0.0338  445 TYR A C     
2267 O O     . TYR A 304 ? 0.1311 0.3603 0.2424 0.0099  0.0211  0.0348  445 TYR A O     
2268 C CB    . TYR A 304 ? 0.1370 0.3516 0.2284 0.0270  0.0246  0.0254  445 TYR A CB    
2269 C CG    . TYR A 304 ? 0.1631 0.3821 0.2588 0.0279  0.0239  0.0228  445 TYR A CG    
2270 C CD1   . TYR A 304 ? 0.1401 0.3563 0.2427 0.0258  0.0209  0.0220  445 TYR A CD1   
2271 C CD2   . TYR A 304 ? 0.1400 0.3670 0.2335 0.0306  0.0261  0.0210  445 TYR A CD2   
2272 C CE1   . TYR A 304 ? 0.1799 0.4018 0.2863 0.0261  0.0202  0.0198  445 TYR A CE1   
2273 C CE2   . TYR A 304 ? 0.1624 0.3951 0.2606 0.0312  0.0252  0.0191  445 TYR A CE2   
2274 C CZ    . TYR A 304 ? 0.1635 0.3937 0.2677 0.0288  0.0221  0.0187  445 TYR A CZ    
2275 O OH    . TYR A 304 ? 0.1765 0.4136 0.2851 0.0290  0.0211  0.0170  445 TYR A OH    
2276 N N     . VAL A 305 ? 0.1544 0.3663 0.2633 0.0137  0.0189  0.0345  446 VAL A N     
2277 C CA    . VAL A 305 ? 0.1356 0.3451 0.2553 0.0089  0.0158  0.0360  446 VAL A CA    
2278 C C     . VAL A 305 ? 0.1693 0.3855 0.2947 0.0009  0.0149  0.0431  446 VAL A C     
2279 O O     . VAL A 305 ? 0.1410 0.3600 0.2748 -0.0040 0.0134  0.0442  446 VAL A O     
2280 C CB    . VAL A 305 ? 0.1344 0.3323 0.2565 0.0105  0.0135  0.0351  446 VAL A CB    
2281 C CG1   . VAL A 305 ? 0.1320 0.3274 0.2666 0.0047  0.0104  0.0379  446 VAL A CG1   
2282 C CG2   . VAL A 305 ? 0.1545 0.3460 0.2725 0.0168  0.0139  0.0280  446 VAL A CG2   
2283 N N     . GLU A 306 ? 0.1742 0.3930 0.2947 -0.0013 0.0158  0.0483  447 GLU A N     
2284 C CA    . GLU A 306 ? 0.1653 0.3903 0.2897 -0.0097 0.0147  0.0562  447 GLU A CA    
2285 C C     . GLU A 306 ? 0.1968 0.4332 0.3204 -0.0124 0.0170  0.0557  447 GLU A C     
2286 O O     . GLU A 306 ? 0.2108 0.4507 0.3408 -0.0197 0.0154  0.0603  447 GLU A O     
2287 C CB    . GLU A 306 ? 0.1749 0.4013 0.2929 -0.0120 0.0150  0.0620  447 GLU A CB    
2288 C CG    . GLU A 306 ? 0.2008 0.4169 0.3213 -0.0109 0.0121  0.0644  447 GLU A CG    
2289 C CD    . GLU A 306 ? 0.2904 0.5092 0.4032 -0.0130 0.0125  0.0695  447 GLU A CD    
2290 O OE1   . GLU A 306 ? 0.2481 0.4729 0.3502 -0.0099 0.0166  0.0661  447 GLU A OE1   
2291 O OE2   . GLU A 306 ? 0.3185 0.5319 0.4357 -0.0176 0.0085  0.0765  447 GLU A OE2   
2292 N N     . ARG A 307 ? 0.1801 0.4220 0.2961 -0.0069 0.0206  0.0503  448 ARG A N     
2293 C CA    . ARG A 307 ? 0.1770 0.4301 0.2930 -0.0087 0.0227  0.0491  448 ARG A CA    
2294 C C     . ARG A 307 ? 0.1830 0.4362 0.3083 -0.0106 0.0207  0.0471  448 ARG A C     
2295 O O     . ARG A 307 ? 0.2525 0.5134 0.3824 -0.0168 0.0205  0.0499  448 ARG A O     
2296 C CB    . ARG A 307 ? 0.2369 0.4940 0.3449 -0.0012 0.0264  0.0430  448 ARG A CB    
2297 C CG    . ARG A 307 ? 0.3601 0.6202 0.4584 0.0001  0.0296  0.0436  448 ARG A CG    
2298 C CD    . ARG A 307 ? 0.4473 0.7083 0.5394 0.0087  0.0328  0.0364  448 ARG A CD    
2299 N NE    . ARG A 307 ? 0.3770 0.6279 0.4626 0.0149  0.0332  0.0334  448 ARG A NE    
2300 C CZ    . ARG A 307 ? 0.3757 0.6217 0.4577 0.0229  0.0344  0.0276  448 ARG A CZ    
2301 N NH1   . ARG A 307 ? 0.3989 0.6498 0.4833 0.0261  0.0353  0.0242  448 ARG A NH1   
2302 N NH2   . ARG A 307 ? 0.3942 0.6299 0.4706 0.0275  0.0344  0.0256  448 ARG A NH2   
2303 N N     . VAL A 308 ? 0.1540 0.3993 0.2816 -0.0055 0.0191  0.0420  449 VAL A N     
2304 C CA    . VAL A 308 ? 0.1603 0.4060 0.2967 -0.0077 0.0171  0.0396  449 VAL A CA    
2305 C C     . VAL A 308 ? 0.2195 0.4616 0.3654 -0.0156 0.0141  0.0445  449 VAL A C     
2306 O O     . VAL A 308 ? 0.1930 0.4401 0.3460 -0.0215 0.0132  0.0457  449 VAL A O     
2307 C CB    . VAL A 308 ? 0.1996 0.4378 0.3351 -0.0010 0.0161  0.0331  449 VAL A CB    
2308 C CG1   . VAL A 308 ? 0.1520 0.3909 0.2968 -0.0042 0.0138  0.0305  449 VAL A CG1   
2309 C CG2   . VAL A 308 ? 0.1890 0.4302 0.3161 0.0063  0.0185  0.0290  449 VAL A CG2   
2310 N N     . GLY A 309 ? 0.1462 0.3791 0.2929 -0.0160 0.0124  0.0478  450 GLY A N     
2311 C CA    . GLY A 309 ? 0.1849 0.4126 0.3414 -0.0231 0.0091  0.0534  450 GLY A CA    
2312 C C     . GLY A 309 ? 0.1532 0.3706 0.3177 -0.0214 0.0065  0.0494  450 GLY A C     
2313 O O     . GLY A 309 ? 0.1433 0.3622 0.3119 -0.0206 0.0064  0.0435  450 GLY A O     
2314 N N     . ILE A 310 ? 0.1443 0.3519 0.3113 -0.0210 0.0044  0.0526  451 ILE A N     
2315 C CA    . ILE A 310 ? 0.1699 0.3679 0.3435 -0.0180 0.0027  0.0477  451 ILE A CA    
2316 C C     . ILE A 310 ? 0.1717 0.3676 0.3584 -0.0238 0.0005  0.0469  451 ILE A C     
2317 O O     . ILE A 310 ? 0.1568 0.3503 0.3480 -0.0217 0.0003  0.0399  451 ILE A O     
2318 C CB    . ILE A 310 ? 0.1796 0.3676 0.3535 -0.0161 0.0010  0.0513  451 ILE A CB    
2319 C CG1   . ILE A 310 ? 0.1472 0.3256 0.3268 -0.0121 0.0000  0.0450  451 ILE A CG1   
2320 C CG2   . ILE A 310 ? 0.1611 0.3454 0.3425 -0.0231 -0.0022 0.0611  451 ILE A CG2   
2321 C CD1   . ILE A 310 ? 0.1535 0.3340 0.3249 -0.0054 0.0025  0.0360  451 ILE A CD1   
2322 N N     . GLU A 311 ? 0.1579 0.3548 0.3506 -0.0316 -0.0012 0.0540  452 GLU A N     
2323 C CA    . GLU A 311 ? 0.2268 0.4208 0.4320 -0.0377 -0.0032 0.0531  452 GLU A CA    
2324 C C     . GLU A 311 ? 0.1599 0.3645 0.3643 -0.0386 -0.0014 0.0465  452 GLU A C     
2325 O O     . GLU A 311 ? 0.1731 0.3758 0.3861 -0.0408 -0.0024 0.0412  452 GLU A O     
2326 C CB    . GLU A 311 ? 0.2202 0.4110 0.4309 -0.0461 -0.0058 0.0630  452 GLU A CB    
2327 C CG    . GLU A 311 ? 0.2479 0.4272 0.4617 -0.0456 -0.0087 0.0699  452 GLU A CG    
2328 C CD    . GLU A 311 ? 0.4436 0.6286 0.6459 -0.0451 -0.0078 0.0769  452 GLU A CD    
2329 O OE1   . GLU A 311 ? 0.3548 0.5509 0.5456 -0.0419 -0.0041 0.0736  452 GLU A OE1   
2330 O OE2   . GLU A 311 ? 0.5083 0.6862 0.7131 -0.0477 -0.0110 0.0854  452 GLU A OE2   
2331 N N     . ARG A 312 ? 0.1509 0.3667 0.3454 -0.0368 0.0013  0.0464  453 ARG A N     
2332 C CA    . ARG A 312 ? 0.1503 0.3759 0.3439 -0.0365 0.0028  0.0402  453 ARG A CA    
2333 C C     . ARG A 312 ? 0.1558 0.3800 0.3468 -0.0291 0.0033  0.0317  453 ARG A C     
2334 O O     . ARG A 312 ? 0.1120 0.3398 0.3078 -0.0304 0.0028  0.0261  453 ARG A O     
2335 C CB    . ARG A 312 ? 0.1279 0.3645 0.3123 -0.0356 0.0056  0.0426  453 ARG A CB    
2336 C CG    . ARG A 312 ? 0.1278 0.3678 0.3142 -0.0440 0.0052  0.0508  453 ARG A CG    
2337 C CD    . ARG A 312 ? 0.1957 0.4492 0.3765 -0.0448 0.0080  0.0508  453 ARG A CD    
2338 N NE    . ARG A 312 ? 0.2381 0.4957 0.4077 -0.0370 0.0110  0.0491  453 ARG A NE    
2339 C CZ    . ARG A 312 ? 0.3660 0.6342 0.5291 -0.0369 0.0138  0.0504  453 ARG A CZ    
2340 N NH1   . ARG A 312 ? 0.2885 0.5655 0.4548 -0.0440 0.0143  0.0535  453 ARG A NH1   
2341 N NH2   . ARG A 312 ? 0.3412 0.6115 0.4948 -0.0296 0.0164  0.0482  453 ARG A NH2   
2342 N N     . ILE A 313 ? 0.1420 0.3611 0.3251 -0.0219 0.0043  0.0310  454 ILE A N     
2343 C CA    . ILE A 313 ? 0.1283 0.3437 0.3082 -0.0154 0.0045  0.0239  454 ILE A CA    
2344 C C     . ILE A 313 ? 0.1312 0.3413 0.3225 -0.0184 0.0025  0.0201  454 ILE A C     
2345 O O     . ILE A 313 ? 0.1398 0.3523 0.3329 -0.0173 0.0023  0.0136  454 ILE A O     
2346 C CB    . ILE A 313 ? 0.1651 0.3738 0.3352 -0.0085 0.0057  0.0247  454 ILE A CB    
2347 C CG1   . ILE A 313 ? 0.1403 0.3548 0.2986 -0.0041 0.0082  0.0253  454 ILE A CG1   
2348 C CG2   . ILE A 313 ? 0.1155 0.3169 0.2849 -0.0035 0.0053  0.0185  454 ILE A CG2   
2349 C CD1   . ILE A 313 ? 0.1458 0.3555 0.2952 -0.0003 0.0095  0.0285  454 ILE A CD1   
2350 N N     . ALA A 314 ? 0.1279 0.3297 0.3271 -0.0222 0.0008  0.0246  455 ALA A N     
2351 C CA    . ALA A 314 ? 0.1439 0.3378 0.3548 -0.0246 -0.0010 0.0210  455 ALA A CA    
2352 C C     . ALA A 314 ? 0.1307 0.3302 0.3503 -0.0314 -0.0018 0.0174  455 ALA A C     
2353 O O     . ALA A 314 ? 0.1190 0.3179 0.3435 -0.0314 -0.0021 0.0099  455 ALA A O     
2354 C CB    . ALA A 314 ? 0.1242 0.3051 0.3426 -0.0271 -0.0031 0.0274  455 ALA A CB    
2355 N N     . ALA A 315 ? 0.1463 0.3517 0.3673 -0.0374 -0.0022 0.0221  456 ALA A N     
2356 C CA    . ALA A 315 ? 0.1297 0.3404 0.3587 -0.0447 -0.0031 0.0188  456 ALA A CA    
2357 C C     . ALA A 315 ? 0.1283 0.3512 0.3523 -0.0417 -0.0018 0.0114  456 ALA A C     
2358 O O     . ALA A 315 ? 0.1457 0.3713 0.3765 -0.0454 -0.0028 0.0050  456 ALA A O     
2359 C CB    . ALA A 315 ? 0.1258 0.3395 0.3566 -0.0520 -0.0035 0.0260  456 ALA A CB    
2360 N N     . TYR A 316 ? 0.1081 0.3364 0.3203 -0.0350 0.0000  0.0125  457 TYR A N     
2361 C CA    . TYR A 316 ? 0.1232 0.3589 0.3294 -0.0312 0.0004  0.0078  457 TYR A CA    
2362 C C     . TYR A 316 ? 0.1263 0.3576 0.3314 -0.0271 -0.0002 0.0017  457 TYR A C     
2363 O O     . TYR A 316 ? 0.1163 0.3522 0.3223 -0.0288 -0.0013 -0.0031 457 TYR A O     
2364 C CB    . TYR A 316 ? 0.0888 0.3288 0.2823 -0.0246 0.0023  0.0108  457 TYR A CB    
2365 C CG    . TYR A 316 ? 0.1166 0.3637 0.3036 -0.0204 0.0023  0.0071  457 TYR A CG    
2366 C CD1   . TYR A 316 ? 0.1102 0.3680 0.3001 -0.0245 0.0017  0.0066  457 TYR A CD1   
2367 C CD2   . TYR A 316 ? 0.1257 0.3687 0.3036 -0.0127 0.0026  0.0044  457 TYR A CD2   
2368 C CE1   . TYR A 316 ? 0.1316 0.3966 0.3159 -0.0206 0.0011  0.0037  457 TYR A CE1   
2369 C CE2   . TYR A 316 ? 0.1272 0.3767 0.2992 -0.0091 0.0020  0.0018  457 TYR A CE2   
2370 C CZ    . TYR A 316 ? 0.1159 0.3767 0.2913 -0.0129 0.0012  0.0015  457 TYR A CZ    
2371 O OH    . TYR A 316 ? 0.1502 0.4182 0.3201 -0.0093 0.0002  -0.0007 457 TYR A OH    
2372 N N     . GLU A 317 ? 0.1163 0.3393 0.3182 -0.0219 0.0005  0.0019  458 GLU A N     
2373 C CA    . GLU A 317 ? 0.1101 0.3287 0.3092 -0.0182 0.0004  -0.0037 458 GLU A CA    
2374 C C     . GLU A 317 ? 0.1154 0.3320 0.3255 -0.0248 -0.0008 -0.0094 458 GLU A C     
2375 O O     . GLU A 317 ? 0.1252 0.3422 0.3322 -0.0245 -0.0010 -0.0167 458 GLU A O     
2376 C CB    . GLU A 317 ? 0.1218 0.3314 0.3161 -0.0120 0.0016  -0.0022 458 GLU A CB    
2377 C CG    . GLU A 317 ? 0.0988 0.3076 0.2780 -0.0045 0.0030  -0.0001 458 GLU A CG    
2378 C CD    . GLU A 317 ? 0.1571 0.3567 0.3320 -0.0001 0.0040  0.0025  458 GLU A CD    
2379 O OE1   . GLU A 317 ? 0.1377 0.3352 0.3006 0.0053  0.0053  0.0041  458 GLU A OE1   
2380 O OE2   . GLU A 317 ? 0.1309 0.3256 0.3148 -0.0025 0.0034  0.0029  458 GLU A OE2   
2381 N N     . HIS A 318 ? 0.1277 0.3397 0.3498 -0.0311 -0.0016 -0.0073 459 HIS A N     
2382 C CA    . HIS A 318 ? 0.1436 0.3476 0.3760 -0.0375 -0.0026 -0.0138 459 HIS A CA    
2383 C C     . HIS A 318 ? 0.1647 0.3795 0.3969 -0.0430 -0.0035 -0.0179 459 HIS A C     
2384 O O     . HIS A 318 ? 0.1538 0.3656 0.3878 -0.0455 -0.0037 -0.0267 459 HIS A O     
2385 C CB    . HIS A 318 ? 0.1574 0.3504 0.4013 -0.0428 -0.0038 -0.0081 459 HIS A CB    
2386 C CG    . HIS A 318 ? 0.2227 0.4045 0.4784 -0.0490 -0.0047 -0.0143 459 HIS A CG    
2387 N ND1   . HIS A 318 ? 0.2442 0.4286 0.5063 -0.0578 -0.0060 -0.0148 459 HIS A ND1   
2388 C CD2   . HIS A 318 ? 0.2492 0.4164 0.5107 -0.0477 -0.0043 -0.0204 459 HIS A CD2   
2389 C CE1   . HIS A 318 ? 0.2324 0.4036 0.5043 -0.0615 -0.0063 -0.0212 459 HIS A CE1   
2390 N NE2   . HIS A 318 ? 0.2634 0.4246 0.5360 -0.0554 -0.0052 -0.0250 459 HIS A NE2   
2391 N N     . ALA A 319 ? 0.0959 0.3225 0.3261 -0.0449 -0.0040 -0.0118 460 ALA A N     
2392 C CA    . ALA A 319 ? 0.1163 0.3522 0.3456 -0.0493 -0.0052 -0.0152 460 ALA A CA    
2393 C C     . ALA A 319 ? 0.1406 0.3807 0.3591 -0.0436 -0.0050 -0.0212 460 ALA A C     
2394 O O     . ALA A 319 ? 0.1140 0.3574 0.3329 -0.0478 -0.0061 -0.0281 460 ALA A O     
2395 C CB    . ALA A 319 ? 0.1603 0.4054 0.3888 -0.0506 -0.0052 -0.0085 460 ALA A CB    
2396 N N     . LEU A 320 ? 0.1354 0.3749 0.3436 -0.0346 -0.0038 -0.0187 461 LEU A N     
2397 C CA    . LEU A 320 ? 0.1354 0.3781 0.3330 -0.0295 -0.0040 -0.0235 461 LEU A CA    
2398 C C     . LEU A 320 ? 0.1563 0.3932 0.3560 -0.0318 -0.0039 -0.0325 461 LEU A C     
2399 O O     . LEU A 320 ? 0.1228 0.3655 0.3193 -0.0339 -0.0049 -0.0389 461 LEU A O     
2400 C CB    . LEU A 320 ? 0.1562 0.3960 0.3430 -0.0200 -0.0026 -0.0193 461 LEU A CB    
2401 C CG    . LEU A 320 ? 0.1681 0.4138 0.3490 -0.0161 -0.0022 -0.0132 461 LEU A CG    
2402 C CD1   . LEU A 320 ? 0.0961 0.3349 0.2669 -0.0076 -0.0006 -0.0106 461 LEU A CD1   
2403 C CD2   . LEU A 320 ? 0.1146 0.3723 0.2920 -0.0168 -0.0038 -0.0149 461 LEU A CD2   
2404 N N     . LEU A 321 ? 0.1008 0.3260 0.3062 -0.0313 -0.0026 -0.0337 462 LEU A N     
2405 C CA    . LEU A 321 ? 0.1127 0.3302 0.3206 -0.0327 -0.0016 -0.0433 462 LEU A CA    
2406 C C     . LEU A 321 ? 0.1339 0.3512 0.3510 -0.0419 -0.0024 -0.0507 462 LEU A C     
2407 O O     . LEU A 321 ? 0.1596 0.3778 0.3746 -0.0440 -0.0021 -0.0600 462 LEU A O     
2408 C CB    . LEU A 321 ? 0.1274 0.3311 0.3406 -0.0295 0.0000  -0.0424 462 LEU A CB    
2409 C CG    . LEU A 321 ? 0.1895 0.3834 0.4054 -0.0290 0.0017  -0.0518 462 LEU A CG    
2410 C CD1   . LEU A 321 ? 0.1052 0.3053 0.3084 -0.0252 0.0025  -0.0569 462 LEU A CD1   
2411 C CD2   . LEU A 321 ? 0.2116 0.3923 0.4327 -0.0249 0.0029  -0.0484 462 LEU A CD2   
2412 N N     . GLU A 322 ? 0.1316 0.3475 0.3584 -0.0479 -0.0035 -0.0467 463 GLU A N     
2413 C CA    . GLU A 322 ? 0.1610 0.3757 0.3961 -0.0572 -0.0044 -0.0529 463 GLU A CA    
2414 C C     . GLU A 322 ? 0.1777 0.4064 0.4053 -0.0601 -0.0059 -0.0562 463 GLU A C     
2415 O O     . GLU A 322 ? 0.1922 0.4201 0.4224 -0.0665 -0.0062 -0.0650 463 GLU A O     
2416 C CB    . GLU A 322 ? 0.2136 0.4249 0.4591 -0.0631 -0.0055 -0.0460 463 GLU A CB    
2417 C CG    . GLU A 322 ? 0.2552 0.4503 0.5103 -0.0621 -0.0048 -0.0430 463 GLU A CG    
2418 C CD    . GLU A 322 ? 0.3294 0.5094 0.5935 -0.0649 -0.0038 -0.0527 463 GLU A CD    
2419 O OE1   . GLU A 322 ? 0.4330 0.6110 0.7024 -0.0726 -0.0045 -0.0583 463 GLU A OE1   
2420 O OE2   . GLU A 322 ? 0.4372 0.6073 0.7029 -0.0593 -0.0023 -0.0550 463 GLU A OE2   
2421 N N     . TYR A 323 ? 0.1514 0.3923 0.3704 -0.0556 -0.0069 -0.0494 464 TYR A N     
2422 C CA    . TYR A 323 ? 0.1396 0.3938 0.3519 -0.0574 -0.0087 -0.0518 464 TYR A CA    
2423 C C     . TYR A 323 ? 0.1723 0.4284 0.3753 -0.0542 -0.0084 -0.0592 464 TYR A C     
2424 O O     . TYR A 323 ? 0.1834 0.4445 0.3848 -0.0596 -0.0094 -0.0669 464 TYR A O     
2425 C CB    . TYR A 323 ? 0.1270 0.3915 0.3339 -0.0526 -0.0096 -0.0425 464 TYR A CB    
2426 C CG    . TYR A 323 ? 0.1567 0.4354 0.3568 -0.0528 -0.0116 -0.0434 464 TYR A CG    
2427 C CD1   . TYR A 323 ? 0.1237 0.4103 0.3288 -0.0602 -0.0134 -0.0435 464 TYR A CD1   
2428 C CD2   . TYR A 323 ? 0.1228 0.4068 0.3117 -0.0454 -0.0121 -0.0433 464 TYR A CD2   
2429 C CE1   . TYR A 323 ? 0.1272 0.4276 0.3267 -0.0600 -0.0155 -0.0439 464 TYR A CE1   
2430 C CE2   . TYR A 323 ? 0.1561 0.4534 0.3394 -0.0452 -0.0143 -0.0432 464 TYR A CE2   
2431 C CZ    . TYR A 323 ? 0.1368 0.4425 0.3255 -0.0524 -0.0160 -0.0436 464 TYR A CZ    
2432 O OH    . TYR A 323 ? 0.1467 0.4662 0.3304 -0.0519 -0.0185 -0.0433 464 TYR A OH    
2433 N N     . ALA A 324 ? 0.1606 0.4128 0.3572 -0.0459 -0.0070 -0.0571 465 ALA A N     
2434 C CA    . ALA A 324 ? 0.1577 0.4135 0.3441 -0.0424 -0.0069 -0.0623 465 ALA A CA    
2435 C C     . ALA A 324 ? 0.1780 0.4275 0.3679 -0.0477 -0.0054 -0.0741 465 ALA A C     
2436 O O     . ALA A 324 ? 0.1698 0.4265 0.3531 -0.0502 -0.0061 -0.0808 465 ALA A O     
2437 C CB    . ALA A 324 ? 0.1039 0.3553 0.2830 -0.0327 -0.0056 -0.0568 465 ALA A CB    
2438 N N     . THR A 325 ? 0.1497 0.3855 0.3501 -0.0495 -0.0033 -0.0768 466 THR A N     
2439 C CA    . THR A 325 ? 0.2020 0.4295 0.4058 -0.0526 -0.0009 -0.0884 466 THR A CA    
2440 C C     . THR A 325 ? 0.2089 0.4409 0.4131 -0.0615 -0.0015 -0.0983 466 THR A C     
2441 O O     . THR A 325 ? 0.2136 0.4490 0.4110 -0.0625 -0.0005 -0.1068 466 THR A O     
2442 C CB    . THR A 325 ? 0.1672 0.3781 0.3840 -0.0524 0.0012  -0.0885 466 THR A CB    
2443 O OG1   . THR A 325 ? 0.1824 0.3896 0.3967 -0.0441 0.0018  -0.0799 466 THR A OG1   
2444 C CG2   . THR A 325 ? 0.2180 0.4193 0.4399 -0.0550 0.0041  -0.1009 466 THR A CG2   
2445 N N     . PRO A 326 ? 0.2123 0.4448 0.4233 -0.0684 -0.0031 -0.0978 467 PRO A N     
2446 C CA    . PRO A 326 ? 0.1960 0.4322 0.4060 -0.0771 -0.0036 -0.1077 467 PRO A CA    
2447 C C     . PRO A 326 ? 0.2276 0.4810 0.4242 -0.0772 -0.0059 -0.1083 467 PRO A C     
2448 O O     . PRO A 326 ? 0.2255 0.4818 0.4173 -0.0824 -0.0055 -0.1183 467 PRO A O     
2449 C CB    . PRO A 326 ? 0.2295 0.4633 0.4492 -0.0837 -0.0053 -0.1042 467 PRO A CB    
2450 C CG    . PRO A 326 ? 0.2417 0.4673 0.4692 -0.0794 -0.0049 -0.0945 467 PRO A CG    
2451 C CD    . PRO A 326 ? 0.2491 0.4792 0.4683 -0.0695 -0.0045 -0.0884 467 PRO A CD    
2452 N N     . ARG A 327 ? 0.1822 0.4466 0.3728 -0.0718 -0.0084 -0.0978 468 ARG A N     
2453 C CA    . ARG A 327 ? 0.1844 0.4648 0.3633 -0.0713 -0.0112 -0.0971 468 ARG A CA    
2454 C C     . ARG A 327 ? 0.2046 0.4869 0.3733 -0.0671 -0.0101 -0.1012 468 ARG A C     
2455 O O     . ARG A 327 ? 0.2115 0.5035 0.3715 -0.0705 -0.0114 -0.1065 468 ARG A O     
2456 C CB    . ARG A 327 ? 0.2210 0.5107 0.3976 -0.0656 -0.0137 -0.0847 468 ARG A CB    
2457 C CG    . ARG A 327 ? 0.2361 0.5239 0.4230 -0.0694 -0.0142 -0.0796 468 ARG A CG    
2458 C CD    . ARG A 327 ? 0.2448 0.5423 0.4292 -0.0638 -0.0160 -0.0685 468 ARG A CD    
2459 N NE    . ARG A 327 ? 0.2221 0.5348 0.4011 -0.0661 -0.0191 -0.0686 468 ARG A NE    
2460 C CZ    . ARG A 327 ? 0.2045 0.5229 0.3884 -0.0743 -0.0207 -0.0708 468 ARG A CZ    
2461 N NH1   . ARG A 327 ? 0.2400 0.5499 0.4342 -0.0812 -0.0197 -0.0726 468 ARG A NH1   
2462 N NH2   . ARG A 327 ? 0.2307 0.5635 0.4091 -0.0759 -0.0236 -0.0710 468 ARG A NH2   
2463 N N     . LEU A 328 ? 0.1578 0.4313 0.3272 -0.0602 -0.0077 -0.0987 469 LEU A N     
2464 C CA    . LEU A 328 ? 0.1752 0.4489 0.3360 -0.0571 -0.0062 -0.1034 469 LEU A CA    
2465 C C     . LEU A 328 ? 0.2413 0.5099 0.4040 -0.0644 -0.0034 -0.1173 469 LEU A C     
2466 O O     . LEU A 328 ? 0.2035 0.4799 0.3562 -0.0669 -0.0035 -0.1234 469 LEU A O     
2467 C CB    . LEU A 328 ? 0.1401 0.4042 0.3024 -0.0485 -0.0040 -0.0977 469 LEU A CB    
2468 C CG    . LEU A 328 ? 0.1795 0.4429 0.3339 -0.0448 -0.0019 -0.1016 469 LEU A CG    
2469 C CD1   . LEU A 328 ? 0.1740 0.4524 0.3146 -0.0435 -0.0050 -0.0992 469 LEU A CD1   
2470 C CD2   . LEU A 328 ? 0.1179 0.3711 0.2739 -0.0364 0.0000  -0.0946 469 LEU A CD2   
2471 N N     . ALA A 329 ? 0.2156 0.4706 0.3908 -0.0680 -0.0008 -0.1224 470 ALA A N     
2472 C CA    . ALA A 329 ? 0.2265 0.4739 0.4045 -0.0741 0.0026  -0.1362 470 ALA A CA    
2473 C C     . ALA A 329 ? 0.2492 0.5055 0.4210 -0.0827 0.0013  -0.1436 470 ALA A C     
2474 O O     . ALA A 329 ? 0.2585 0.5126 0.4269 -0.0872 0.0042  -0.1553 470 ALA A O     
2475 C CB    . ALA A 329 ? 0.1936 0.4236 0.3877 -0.0756 0.0051  -0.1388 470 ALA A CB    
2476 N N     . ALA A 330 ? 0.2090 0.4756 0.3790 -0.0851 -0.0028 -0.1372 471 ALA A N     
2477 C CA    . ALA A 330 ? 0.2709 0.5463 0.4353 -0.0935 -0.0043 -0.1437 471 ALA A CA    
2478 C C     . ALA A 330 ? 0.2916 0.5824 0.4403 -0.0931 -0.0061 -0.1442 471 ALA A C     
2479 O O     . ALA A 330 ? 0.2909 0.5895 0.4335 -0.1002 -0.0071 -0.1501 471 ALA A O     
2480 C CB    . ALA A 330 ? 0.1987 0.4797 0.3680 -0.0968 -0.0079 -0.1368 471 ALA A CB    
2481 N N     . ILE A 331 ? 0.2527 0.5480 0.3946 -0.0854 -0.0068 -0.1377 472 ILE A N     
2482 C CA    . ILE A 331 ? 0.2628 0.5719 0.3895 -0.0853 -0.0088 -0.1377 472 ILE A CA    
2483 C C     . ILE A 331 ? 0.2743 0.5791 0.3955 -0.0901 -0.0046 -0.1505 472 ILE A C     
2484 O O     . ILE A 331 ? 0.2181 0.5109 0.3443 -0.0875 -0.0003 -0.1551 472 ILE A O     
2485 C CB    . ILE A 331 ? 0.2501 0.5637 0.3714 -0.0754 -0.0108 -0.1267 472 ILE A CB    
2486 C CG1   . ILE A 331 ? 0.2757 0.5921 0.4028 -0.0701 -0.0139 -0.1144 472 ILE A CG1   
2487 C CG2   . ILE A 331 ? 0.2521 0.5793 0.3578 -0.0756 -0.0133 -0.1257 472 ILE A CG2   
2488 C CD1   . ILE A 331 ? 0.2324 0.5510 0.3546 -0.0597 -0.0152 -0.1038 472 ILE A CD1   
2489 N N     . PRO A 332 ? 0.2864 0.6005 0.3976 -0.0970 -0.0051 -0.1566 473 PRO A N     
2490 C CA    . PRO A 332 ? 0.2977 0.6075 0.4032 -0.1017 -0.0001 -0.1692 473 PRO A CA    
2491 C C     . PRO A 332 ? 0.2818 0.5915 0.3797 -0.0960 0.0016  -0.1676 473 PRO A C     
2492 O O     . PRO A 332 ? 0.2830 0.6029 0.3718 -0.0913 -0.0024 -0.1578 473 PRO A O     
2493 C CB    . PRO A 332 ? 0.3132 0.6365 0.4075 -0.1094 -0.0021 -0.1724 473 PRO A CB    
2494 C CG    . PRO A 332 ? 0.2725 0.6012 0.3732 -0.1110 -0.0068 -0.1658 473 PRO A CG    
2495 C CD    . PRO A 332 ? 0.2217 0.5498 0.3278 -0.1015 -0.0097 -0.1530 473 PRO A CD    
2496 N N     . GLY A 333 ? 0.2824 0.5796 0.3847 -0.0961 0.0075  -0.1769 474 GLY A N     
2497 C CA    . GLY A 333 ? 0.2660 0.5613 0.3625 -0.0915 0.0099  -0.1769 474 GLY A CA    
2498 C C     . GLY A 333 ? 0.2679 0.5533 0.3755 -0.0834 0.0103  -0.1710 474 GLY A C     
2499 O O     . GLY A 333 ? 0.2438 0.5242 0.3496 -0.0801 0.0135  -0.1731 474 GLY A O     
2500 N N     . VAL A 334 ? 0.2470 0.5293 0.3656 -0.0802 0.0074  -0.1630 475 VAL A N     
2501 C CA    . VAL A 334 ? 0.2187 0.4906 0.3471 -0.0717 0.0082  -0.1552 475 VAL A CA    
2502 C C     . VAL A 334 ? 0.2361 0.4905 0.3782 -0.0724 0.0136  -0.1637 475 VAL A C     
2503 O O     . VAL A 334 ? 0.2512 0.5010 0.4019 -0.0788 0.0148  -0.1720 475 VAL A O     
2504 C CB    . VAL A 334 ? 0.2345 0.5102 0.3691 -0.0683 0.0036  -0.1434 475 VAL A CB    
2505 C CG1   . VAL A 334 ? 0.1705 0.4306 0.3160 -0.0607 0.0056  -0.1365 475 VAL A CG1   
2506 C CG2   . VAL A 334 ? 0.2235 0.5142 0.3457 -0.0642 -0.0013 -0.1329 475 VAL A CG2   
2507 N N     . ARG A 335 ? 0.1811 0.4239 0.3248 -0.0651 0.0168  -0.1605 476 ARG A N     
2508 C CA    . ARG A 335 ? 0.2234 0.4492 0.3821 -0.0634 0.0210  -0.1651 476 ARG A CA    
2509 C C     . ARG A 335 ? 0.2088 0.4264 0.3730 -0.0544 0.0197  -0.1518 476 ARG A C     
2510 O O     . ARG A 335 ? 0.1961 0.4150 0.3510 -0.0480 0.0194  -0.1441 476 ARG A O     
2511 C CB    . ARG A 335 ? 0.2640 0.4844 0.4206 -0.0640 0.0269  -0.1762 476 ARG A CB    
2512 C CG    . ARG A 335 ? 0.3308 0.5340 0.5020 -0.0590 0.0311  -0.1778 476 ARG A CG    
2513 C CD    . ARG A 335 ? 0.4102 0.6114 0.5761 -0.0569 0.0365  -0.1843 476 ARG A CD    
2514 N NE    . ARG A 335 ? 0.3891 0.5754 0.5695 -0.0515 0.0401  -0.1851 476 ARG A NE    
2515 C CZ    . ARG A 335 ? 0.4168 0.6001 0.5957 -0.0478 0.0444  -0.1878 476 ARG A CZ    
2516 N NH1   . ARG A 335 ? 0.4117 0.6047 0.5749 -0.0496 0.0463  -0.1910 476 ARG A NH1   
2517 N NH2   . ARG A 335 ? 0.3882 0.5589 0.5819 -0.0424 0.0466  -0.1869 476 ARG A NH2   
2518 N N     . ILE A 336 ? 0.2007 0.4099 0.3793 -0.0546 0.0187  -0.1488 477 ILE A N     
2519 C CA    . ILE A 336 ? 0.1671 0.3675 0.3519 -0.0470 0.0178  -0.1372 477 ILE A CA    
2520 C C     . ILE A 336 ? 0.1881 0.3749 0.3791 -0.0427 0.0222  -0.1404 477 ILE A C     
2521 O O     . ILE A 336 ? 0.2399 0.4190 0.4401 -0.0461 0.0256  -0.1513 477 ILE A O     
2522 C CB    . ILE A 336 ? 0.1791 0.3752 0.3771 -0.0495 0.0154  -0.1327 477 ILE A CB    
2523 C CG1   . ILE A 336 ? 0.1897 0.4005 0.3834 -0.0551 0.0114  -0.1312 477 ILE A CG1   
2524 C CG2   . ILE A 336 ? 0.1819 0.3713 0.3837 -0.0421 0.0142  -0.1198 477 ILE A CG2   
2525 C CD1   . ILE A 336 ? 0.1795 0.4035 0.3606 -0.0502 0.0083  -0.1211 477 ILE A CD1   
2526 N N     . VAL A 337 ? 0.1810 0.3649 0.3676 -0.0350 0.0221  -0.1312 478 VAL A N     
2527 C CA    . VAL A 337 ? 0.1889 0.3617 0.3808 -0.0304 0.0257  -0.1329 478 VAL A CA    
2528 C C     . VAL A 337 ? 0.1766 0.3400 0.3784 -0.0254 0.0239  -0.1222 478 VAL A C     
2529 O O     . VAL A 337 ? 0.2056 0.3724 0.4004 -0.0210 0.0213  -0.1111 478 VAL A O     
2530 C CB    . VAL A 337 ? 0.1855 0.3631 0.3629 -0.0267 0.0274  -0.1318 478 VAL A CB    
2531 C CG1   . VAL A 337 ? 0.1841 0.3512 0.3682 -0.0224 0.0313  -0.1338 478 VAL A CG1   
2532 C CG2   . VAL A 337 ? 0.1993 0.3875 0.3656 -0.0325 0.0287  -0.1414 478 VAL A CG2   
2533 N N     . GLY A 338 ? 0.1767 0.3284 0.3948 -0.0262 0.0252  -0.1255 479 GLY A N     
2534 C CA    . GLY A 338 ? 0.1491 0.2922 0.3773 -0.0227 0.0229  -0.1152 479 GLY A CA    
2535 C C     . GLY A 338 ? 0.2326 0.3755 0.4686 -0.0277 0.0199  -0.1126 479 GLY A C     
2536 O O     . GLY A 338 ? 0.2129 0.3651 0.4414 -0.0287 0.0168  -0.1057 479 GLY A O     
2537 N N     . THR A 339 ? 0.1904 0.3229 0.4418 -0.0312 0.0208  -0.1185 480 THR A N     
2538 C CA    . THR A 339 ? 0.2178 0.3483 0.4782 -0.0370 0.0181  -0.1165 480 THR A CA    
2539 C C     . THR A 339 ? 0.2565 0.3719 0.5339 -0.0355 0.0172  -0.1115 480 THR A C     
2540 O O     . THR A 339 ? 0.2520 0.3587 0.5426 -0.0403 0.0171  -0.1163 480 THR A O     
2541 C CB    . THR A 339 ? 0.2993 0.4324 0.5616 -0.0448 0.0196  -0.1298 480 THR A CB    
2542 O OG1   . THR A 339 ? 0.2702 0.3935 0.5411 -0.0445 0.0238  -0.1415 480 THR A OG1   
2543 C CG2   . THR A 339 ? 0.2480 0.3979 0.4928 -0.0469 0.0193  -0.1328 480 THR A CG2   
2544 N N     . ALA A 340 ? 0.1880 0.3000 0.4651 -0.0290 0.0162  -0.1015 481 ALA A N     
2545 C CA    . ALA A 340 ? 0.2458 0.3441 0.5382 -0.0269 0.0148  -0.0955 481 ALA A CA    
2546 C C     . ALA A 340 ? 0.2568 0.3520 0.5569 -0.0322 0.0112  -0.0882 481 ALA A C     
2547 O O     . ALA A 340 ? 0.2826 0.3881 0.5744 -0.0361 0.0094  -0.0847 481 ALA A O     
2548 C CB    . ALA A 340 ? 0.2090 0.3070 0.4968 -0.0197 0.0139  -0.0852 481 ALA A CB    
2549 N N     . GLN A 341 ? 0.2422 0.3233 0.5589 -0.0323 0.0100  -0.0855 482 GLN A N     
2550 C CA    . GLN A 341 ? 0.2876 0.3638 0.6127 -0.0375 0.0064  -0.0774 482 GLN A CA    
2551 C C     . GLN A 341 ? 0.3283 0.4147 0.6424 -0.0372 0.0034  -0.0638 482 GLN A C     
2552 O O     . GLN A 341 ? 0.3041 0.3960 0.6167 -0.0431 0.0014  -0.0599 482 GLN A O     
2553 C CB    . GLN A 341 ? 0.3661 0.4252 0.7098 -0.0358 0.0050  -0.0737 482 GLN A CB    
2554 C CG    . GLN A 341 ? 0.3637 0.4100 0.7235 -0.0388 0.0070  -0.0860 482 GLN A CG    
2555 C CD    . GLN A 341 ? 0.5104 0.5600 0.8691 -0.0477 0.0076  -0.0942 482 GLN A CD    
2556 O OE1   . GLN A 341 ? 0.4948 0.5535 0.8441 -0.0496 0.0106  -0.1055 482 GLN A OE1   
2557 N NE2   . GLN A 341 ? 0.5460 0.5880 0.9133 -0.0535 0.0044  -0.0881 482 GLN A NE2   
2558 N N     . GLU A 342 ? 0.2695 0.3589 0.5758 -0.0305 0.0032  -0.0569 483 GLU A N     
2559 C CA    . GLU A 342 ? 0.3169 0.4168 0.6113 -0.0297 0.0012  -0.0458 483 GLU A CA    
2560 C C     . GLU A 342 ? 0.2204 0.3304 0.4991 -0.0240 0.0033  -0.0477 483 GLU A C     
2561 O O     . GLU A 342 ? 0.1898 0.2955 0.4681 -0.0190 0.0053  -0.0519 483 GLU A O     
2562 C CB    . GLU A 342 ? 0.3273 0.4204 0.6273 -0.0281 -0.0018 -0.0327 483 GLU A CB    
2563 C CG    . GLU A 342 ? 0.4490 0.5327 0.7635 -0.0343 -0.0045 -0.0283 483 GLU A CG    
2564 C CD    . GLU A 342 ? 0.6889 0.7594 1.0153 -0.0316 -0.0070 -0.0207 483 GLU A CD    
2565 O OE1   . GLU A 342 ? 0.7892 0.8624 1.1107 -0.0300 -0.0093 -0.0087 483 GLU A OE1   
2566 O OE2   . GLU A 342 ? 0.6780 0.7360 1.0188 -0.0310 -0.0065 -0.0267 483 GLU A OE2   
2567 N N     . LYS A 343 ? 0.1838 0.3070 0.4502 -0.0248 0.0029  -0.0446 484 LYS A N     
2568 C CA    . LYS A 343 ? 0.1621 0.2949 0.4133 -0.0198 0.0045  -0.0459 484 LYS A CA    
2569 C C     . LYS A 343 ? 0.2308 0.3729 0.4726 -0.0181 0.0029  -0.0355 484 LYS A C     
2570 O O     . LYS A 343 ? 0.1979 0.3425 0.4436 -0.0223 0.0010  -0.0291 484 LYS A O     
2571 C CB    . LYS A 343 ? 0.2185 0.3602 0.4633 -0.0223 0.0060  -0.0561 484 LYS A CB    
2572 C CG    . LYS A 343 ? 0.1653 0.3000 0.4159 -0.0235 0.0086  -0.0683 484 LYS A CG    
2573 C CD    . LYS A 343 ? 0.1822 0.3278 0.4242 -0.0267 0.0097  -0.0775 484 LYS A CD    
2574 C CE    . LYS A 343 ? 0.1719 0.3282 0.3974 -0.0217 0.0100  -0.0751 484 LYS A CE    
2575 N NZ    . LYS A 343 ? 0.1578 0.3252 0.3746 -0.0250 0.0105  -0.0831 484 LYS A NZ    
2576 N N     . ALA A 344 ? 0.1524 0.2996 0.3818 -0.0123 0.0041  -0.0341 485 ALA A N     
2577 C CA    . ALA A 344 ? 0.2023 0.3591 0.4211 -0.0099 0.0034  -0.0263 485 ALA A CA    
2578 C C     . ALA A 344 ? 0.1915 0.3559 0.3957 -0.0058 0.0048  -0.0301 485 ALA A C     
2579 O O     . ALA A 344 ? 0.1945 0.3536 0.3933 -0.0019 0.0063  -0.0337 485 ALA A O     
2580 C CB    . ALA A 344 ? 0.1824 0.3333 0.3993 -0.0064 0.0027  -0.0172 485 ALA A CB    
2581 N N     . SER A 345 ? 0.1366 0.3130 0.3350 -0.0070 0.0040  -0.0292 486 SER A N     
2582 C CA    . SER A 345 ? 0.1853 0.3690 0.3690 -0.0023 0.0045  -0.0283 486 SER A CA    
2583 C C     . SER A 345 ? 0.1591 0.3444 0.3367 -0.0016 0.0053  -0.0366 486 SER A C     
2584 O O     . SER A 345 ? 0.1567 0.3512 0.3265 -0.0012 0.0044  -0.0373 486 SER A O     
2585 C CB    . SER A 345 ? 0.2147 0.3936 0.3899 0.0040  0.0053  -0.0217 486 SER A CB    
2586 O OG    . SER A 345 ? 0.2103 0.3919 0.3719 0.0087  0.0058  -0.0218 486 SER A OG    
2587 N N     . VAL A 346 ? 0.1530 0.3299 0.3341 -0.0016 0.0068  -0.0427 487 VAL A N     
2588 C CA    . VAL A 346 ? 0.1727 0.3511 0.3465 -0.0006 0.0082  -0.0500 487 VAL A CA    
2589 C C     . VAL A 346 ? 0.1729 0.3569 0.3531 -0.0070 0.0082  -0.0597 487 VAL A C     
2590 O O     . VAL A 346 ? 0.1387 0.3175 0.3320 -0.0116 0.0085  -0.0636 487 VAL A O     
2591 C CB    . VAL A 346 ? 0.1550 0.3222 0.3292 0.0024  0.0104  -0.0521 487 VAL A CB    
2592 C CG1   . VAL A 346 ? 0.1620 0.3315 0.3310 0.0018  0.0124  -0.0612 487 VAL A CG1   
2593 C CG2   . VAL A 346 ? 0.1634 0.3260 0.3290 0.0082  0.0103  -0.0431 487 VAL A CG2   
2594 N N     . LEU A 347 ? 0.1240 0.3182 0.2951 -0.0076 0.0078  -0.0637 488 LEU A N     
2595 C CA    . LEU A 347 ? 0.1564 0.3572 0.3312 -0.0144 0.0078  -0.0735 488 LEU A CA    
2596 C C     . LEU A 347 ? 0.1615 0.3653 0.3254 -0.0138 0.0092  -0.0798 488 LEU A C     
2597 O O     . LEU A 347 ? 0.1559 0.3715 0.3104 -0.0143 0.0074  -0.0798 488 LEU A O     
2598 C CB    . LEU A 347 ? 0.1471 0.3596 0.3211 -0.0179 0.0047  -0.0705 488 LEU A CB    
2599 C CG    . LEU A 347 ? 0.1249 0.3452 0.3020 -0.0260 0.0039  -0.0798 488 LEU A CG    
2600 C CD1   . LEU A 347 ? 0.1297 0.3390 0.3196 -0.0314 0.0060  -0.0877 488 LEU A CD1   
2601 C CD2   . LEU A 347 ? 0.1236 0.3542 0.2999 -0.0289 0.0007  -0.0749 488 LEU A CD2   
2602 N N     . SER A 348 ? 0.1402 0.3340 0.3057 -0.0131 0.0123  -0.0850 489 SER A N     
2603 C CA    . SER A 348 ? 0.1489 0.3455 0.3044 -0.0137 0.0142  -0.0917 489 SER A CA    
2604 C C     . SER A 348 ? 0.1482 0.3518 0.3043 -0.0213 0.0144  -0.1020 489 SER A C     
2605 O O     . SER A 348 ? 0.1506 0.3504 0.3184 -0.0263 0.0149  -0.1075 489 SER A O     
2606 C CB    . SER A 348 ? 0.1145 0.2996 0.2731 -0.0114 0.0180  -0.0954 489 SER A CB    
2607 O OG    . SER A 348 ? 0.1742 0.3565 0.3252 -0.0049 0.0180  -0.0875 489 SER A OG    
2608 N N     . PHE A 349 ? 0.1671 0.3804 0.3102 -0.0227 0.0139  -0.1047 490 PHE A N     
2609 C CA    . PHE A 349 ? 0.1452 0.3659 0.2864 -0.0305 0.0143  -0.1153 490 PHE A CA    
2610 C C     . PHE A 349 ? 0.1820 0.4088 0.3083 -0.0310 0.0154  -0.1187 490 PHE A C     
2611 O O     . PHE A 349 ? 0.1450 0.3713 0.2619 -0.0253 0.0151  -0.1117 490 PHE A O     
2612 C CB    . PHE A 349 ? 0.1224 0.3552 0.2644 -0.0346 0.0100  -0.1133 490 PHE A CB    
2613 C CG    . PHE A 349 ? 0.1762 0.4220 0.3059 -0.0314 0.0060  -0.1051 490 PHE A CG    
2614 C CD1   . PHE A 349 ? 0.1417 0.3873 0.2709 -0.0240 0.0041  -0.0934 490 PHE A CD1   
2615 C CD2   . PHE A 349 ? 0.1669 0.4258 0.2861 -0.0360 0.0041  -0.1090 490 PHE A CD2   
2616 C CE1   . PHE A 349 ? 0.1595 0.4165 0.2787 -0.0204 0.0005  -0.0861 490 PHE A CE1   
2617 C CE2   . PHE A 349 ? 0.1602 0.4311 0.2691 -0.0325 -0.0001 -0.1007 490 PHE A CE2   
2618 C CZ    . PHE A 349 ? 0.1166 0.3862 0.2262 -0.0244 -0.0018 -0.0893 490 PHE A CZ    
2619 N N     . VAL A 350 ? 0.1387 0.3707 0.2629 -0.0385 0.0170  -0.1300 491 VAL A N     
2620 C CA    . VAL A 350 ? 0.1888 0.4299 0.2976 -0.0412 0.0174  -0.1336 491 VAL A CA    
2621 C C     . VAL A 350 ? 0.2087 0.4637 0.3133 -0.0492 0.0144  -0.1388 491 VAL A C     
2622 O O     . VAL A 350 ? 0.2122 0.4677 0.3271 -0.0536 0.0134  -0.1429 491 VAL A O     
2623 C CB    . VAL A 350 ? 0.2312 0.4657 0.3393 -0.0433 0.0234  -0.1440 491 VAL A CB    
2624 C CG1   . VAL A 350 ? 0.2700 0.4932 0.3798 -0.0355 0.0258  -0.1380 491 VAL A CG1   
2625 C CG2   . VAL A 350 ? 0.2620 0.4911 0.3834 -0.0492 0.0269  -0.1570 491 VAL A CG2   
2626 N N     . LEU A 351 ? 0.2178 0.4843 0.3069 -0.0514 0.0126  -0.1385 492 LEU A N     
2627 C CA    . LEU A 351 ? 0.2264 0.5084 0.3090 -0.0592 0.0090  -0.1424 492 LEU A CA    
2628 C C     . LEU A 351 ? 0.2845 0.5720 0.3547 -0.0656 0.0118  -0.1520 492 LEU A C     
2629 O O     . LEU A 351 ? 0.2316 0.5202 0.2895 -0.0626 0.0122  -0.1474 492 LEU A O     
2630 C CB    . LEU A 351 ? 0.2467 0.5406 0.3219 -0.0551 0.0024  -0.1295 492 LEU A CB    
2631 C CG    . LEU A 351 ? 0.2576 0.5702 0.3255 -0.0619 -0.0029 -0.1305 492 LEU A CG    
2632 C CD1   . LEU A 351 ? 0.2622 0.5779 0.3422 -0.0687 -0.0036 -0.1374 492 LEU A CD1   
2633 C CD2   . LEU A 351 ? 0.2660 0.5886 0.3277 -0.0554 -0.0090 -0.1164 492 LEU A CD2   
2634 N N     . ALA A 352 ? 0.2569 0.5478 0.3300 -0.0749 0.0139  -0.1654 493 ALA A N     
2635 C CA    . ALA A 352 ? 0.2922 0.5879 0.3542 -0.0818 0.0178  -0.1762 493 ALA A CA    
2636 C C     . ALA A 352 ? 0.3136 0.6228 0.3567 -0.0825 0.0137  -0.1677 493 ALA A C     
2637 O O     . ALA A 352 ? 0.2839 0.6036 0.3234 -0.0830 0.0077  -0.1602 493 ALA A O     
2638 C CB    . ALA A 352 ? 0.2305 0.5248 0.2980 -0.0895 0.0215  -0.1873 493 ALA A CB    
2639 N N     . GLY A 353 ? 0.3354 0.6437 0.3674 -0.0823 0.0172  -0.1679 494 GLY A N     
2640 C CA    . GLY A 353 ? 0.3031 0.6224 0.3179 -0.0838 0.0139  -0.1597 494 GLY A CA    
2641 C C     . GLY A 353 ? 0.3175 0.6396 0.3248 -0.0761 0.0078  -0.1454 494 GLY A C     
2642 O O     . GLY A 353 ? 0.3083 0.6387 0.3021 -0.0767 0.0043  -0.1369 494 GLY A O     
2643 N N     . HIS A 354 ? 0.3001 0.6126 0.3174 -0.0678 0.0071  -0.1400 495 HIS A N     
2644 C CA    . HIS A 354 ? 0.2659 0.5767 0.2791 -0.0584 0.0028  -0.1244 495 HIS A CA    
2645 C C     . HIS A 354 ? 0.2662 0.5601 0.2848 -0.0509 0.0075  -0.1215 495 HIS A C     
2646 O O     . HIS A 354 ? 0.2926 0.5761 0.3251 -0.0498 0.0117  -0.1274 495 HIS A O     
2647 C CB    . HIS A 354 ? 0.2541 0.5698 0.2762 -0.0544 -0.0029 -0.1165 495 HIS A CB    
2648 C CG    . HIS A 354 ? 0.2767 0.6106 0.2932 -0.0610 -0.0086 -0.1171 495 HIS A CG    
2649 N ND1   . HIS A 354 ? 0.2791 0.6248 0.2849 -0.0587 -0.0152 -0.1062 495 HIS A ND1   
2650 C CD2   . HIS A 354 ? 0.2993 0.6403 0.3196 -0.0697 -0.0083 -0.1265 495 HIS A CD2   
2651 C CE1   . HIS A 354 ? 0.2845 0.6405 0.2885 -0.0645 -0.0176 -0.1070 495 HIS A CE1   
2652 N NE2   . HIS A 354 ? 0.3359 0.6892 0.3478 -0.0714 -0.0134 -0.1193 495 HIS A NE2   
2653 N N     . GLU A 355 ? 0.2450 0.5362 0.2529 -0.0459 0.0065  -0.1122 496 GLU A N     
2654 C CA    . GLU A 355 ? 0.3041 0.5802 0.3164 -0.0388 0.0104  -0.1084 496 GLU A CA    
2655 C C     . GLU A 355 ? 0.2613 0.5306 0.2855 -0.0305 0.0079  -0.1001 496 GLU A C     
2656 O O     . GLU A 355 ? 0.2188 0.4952 0.2412 -0.0273 0.0023  -0.0915 496 GLU A O     
2657 C CB    . GLU A 355 ? 0.2904 0.5652 0.2874 -0.0364 0.0097  -0.1003 496 GLU A CB    
2658 C CG    . GLU A 355 ? 0.3305 0.6094 0.3156 -0.0441 0.0136  -0.1080 496 GLU A CG    
2659 C CD    . GLU A 355 ? 0.4333 0.7042 0.4278 -0.0468 0.0215  -0.1204 496 GLU A CD    
2660 O OE1   . GLU A 355 ? 0.4242 0.7014 0.4199 -0.0548 0.0246  -0.1330 496 GLU A OE1   
2661 O OE2   . GLU A 355 ? 0.4735 0.7320 0.4747 -0.0409 0.0245  -0.1177 496 GLU A OE2   
2662 N N     . PRO A 356 ? 0.2614 0.5180 0.2980 -0.0269 0.0120  -0.1022 497 PRO A N     
2663 C CA    . PRO A 356 ? 0.2117 0.4620 0.2584 -0.0195 0.0099  -0.0939 497 PRO A CA    
2664 C C     . PRO A 356 ? 0.2549 0.5060 0.2934 -0.0122 0.0058  -0.0809 497 PRO A C     
2665 O O     . PRO A 356 ? 0.2062 0.4611 0.2494 -0.0082 0.0019  -0.0744 497 PRO A O     
2666 C CB    . PRO A 356 ? 0.2119 0.4479 0.2684 -0.0170 0.0151  -0.0972 497 PRO A CB    
2667 C CG    . PRO A 356 ? 0.2590 0.4957 0.3183 -0.0245 0.0196  -0.1106 497 PRO A CG    
2668 C CD    . PRO A 356 ? 0.2348 0.4834 0.2783 -0.0303 0.0185  -0.1132 497 PRO A CD    
2669 N N     . LEU A 357 ? 0.2349 0.4822 0.2614 -0.0105 0.0066  -0.0771 498 LEU A N     
2670 C CA    . LEU A 357 ? 0.2853 0.5308 0.3046 -0.0031 0.0030  -0.0649 498 LEU A CA    
2671 C C     . LEU A 357 ? 0.2867 0.5461 0.3000 -0.0032 -0.0033 -0.0594 498 LEU A C     
2672 O O     . LEU A 357 ? 0.2803 0.5406 0.2951 0.0038  -0.0070 -0.0503 498 LEU A O     
2673 C CB    . LEU A 357 ? 0.3518 0.5899 0.3594 -0.0024 0.0053  -0.0625 498 LEU A CB    
2674 C CG    . LEU A 357 ? 0.4519 0.6862 0.4503 0.0045  0.0019  -0.0503 498 LEU A CG    
2675 C CD1   . LEU A 357 ? 0.4384 0.6655 0.4460 0.0131  0.0009  -0.0438 498 LEU A CD1   
2676 C CD2   . LEU A 357 ? 0.4354 0.6612 0.4233 0.0035  0.0050  -0.0494 498 LEU A CD2   
2677 N N     . GLU A 358 ? 0.2667 0.5378 0.2736 -0.0109 -0.0047 -0.0649 499 GLU A N     
2678 C CA    . GLU A 358 ? 0.2921 0.5779 0.2944 -0.0113 -0.0112 -0.0594 499 GLU A CA    
2679 C C     . GLU A 358 ? 0.2498 0.5421 0.2655 -0.0100 -0.0136 -0.0596 499 GLU A C     
2680 O O     . GLU A 358 ? 0.2467 0.5477 0.2629 -0.0057 -0.0189 -0.0515 499 GLU A O     
2681 C CB    . GLU A 358 ? 0.3292 0.6269 0.3204 -0.0208 -0.0123 -0.0653 499 GLU A CB    
2682 C CG    . GLU A 358 ? 0.4301 0.7246 0.4052 -0.0220 -0.0115 -0.0621 499 GLU A CG    
2683 C CD    . GLU A 358 ? 0.4311 0.7203 0.4003 -0.0129 -0.0154 -0.0479 499 GLU A CD    
2684 O OE1   . GLU A 358 ? 0.4095 0.7085 0.3767 -0.0099 -0.0219 -0.0398 499 GLU A OE1   
2685 O OE2   . GLU A 358 ? 0.4273 0.7026 0.3946 -0.0088 -0.0119 -0.0452 499 GLU A OE2   
2686 N N     . VAL A 359 ? 0.2298 0.5182 0.2573 -0.0137 -0.0098 -0.0684 500 VAL A N     
2687 C CA    . VAL A 359 ? 0.2292 0.5222 0.2698 -0.0126 -0.0116 -0.0678 500 VAL A CA    
2688 C C     . VAL A 359 ? 0.1982 0.4844 0.2441 -0.0027 -0.0123 -0.0580 500 VAL A C     
2689 O O     . VAL A 359 ? 0.1723 0.4671 0.2232 0.0008  -0.0160 -0.0523 500 VAL A O     
2690 C CB    . VAL A 359 ? 0.2315 0.5193 0.2835 -0.0187 -0.0073 -0.0789 500 VAL A CB    
2691 C CG1   . VAL A 359 ? 0.1665 0.4583 0.2323 -0.0182 -0.0091 -0.0776 500 VAL A CG1   
2692 C CG2   . VAL A 359 ? 0.1670 0.4621 0.2135 -0.0288 -0.0062 -0.0898 500 VAL A CG2   
2693 N N     . GLY A 360 ? 0.1858 0.4570 0.2309 0.0018  -0.0084 -0.0564 501 GLY A N     
2694 C CA    . GLY A 360 ? 0.2070 0.4713 0.2558 0.0108  -0.0087 -0.0477 501 GLY A CA    
2695 C C     . GLY A 360 ? 0.2366 0.5075 0.2777 0.0170  -0.0134 -0.0380 501 GLY A C     
2696 O O     . GLY A 360 ? 0.1994 0.4734 0.2464 0.0230  -0.0154 -0.0318 501 GLY A O     
2697 N N     . LYS A 361 ? 0.2373 0.5111 0.2656 0.0154  -0.0153 -0.0364 502 LYS A N     
2698 C CA    . LYS A 361 ? 0.2635 0.5427 0.2849 0.0215  -0.0203 -0.0264 502 LYS A CA    
2699 C C     . LYS A 361 ? 0.2115 0.5089 0.2375 0.0207  -0.0257 -0.0244 502 LYS A C     
2700 O O     . LYS A 361 ? 0.2497 0.5519 0.2782 0.0281  -0.0293 -0.0163 502 LYS A O     
2701 C CB    . LYS A 361 ? 0.3221 0.5990 0.3281 0.0194  -0.0211 -0.0244 502 LYS A CB    
2702 C CG    . LYS A 361 ? 0.4004 0.6601 0.4018 0.0209  -0.0161 -0.0250 502 LYS A CG    
2703 C CD    . LYS A 361 ? 0.4771 0.7313 0.4663 0.0255  -0.0184 -0.0159 502 LYS A CD    
2704 C CE    . LYS A 361 ? 0.4604 0.7124 0.4369 0.0185  -0.0165 -0.0191 502 LYS A CE    
2705 N NZ    . LYS A 361 ? 0.4972 0.7358 0.4757 0.0169  -0.0099 -0.0250 502 LYS A NZ    
2706 N N     . ALA A 362 ? 0.1954 0.5032 0.2232 0.0117  -0.0263 -0.0321 503 ALA A N     
2707 C CA    . ALA A 362 ? 0.1971 0.5230 0.2305 0.0102  -0.0315 -0.0307 503 ALA A CA    
2708 C C     . ALA A 362 ? 0.1892 0.5161 0.2373 0.0147  -0.0307 -0.0291 503 ALA A C     
2709 O O     . ALA A 362 ? 0.2446 0.5754 0.2949 0.0189  -0.0331 -0.0225 503 ALA A O     
2710 C CB    . ALA A 362 ? 0.2187 0.5546 0.2509 -0.0014 -0.0318 -0.0405 503 ALA A CB    
2711 N N     . LEU A 363 ? 0.1719 0.4867 0.2272 0.0135  -0.0253 -0.0343 504 LEU A N     
2712 C CA    . LEU A 363 ? 0.1996 0.5110 0.2664 0.0170  -0.0237 -0.0321 504 LEU A CA    
2713 C C     . LEU A 363 ? 0.1930 0.4968 0.2575 0.0274  -0.0238 -0.0225 504 LEU A C     
2714 O O     . LEU A 363 ? 0.2347 0.5388 0.3032 0.0305  -0.0244 -0.0181 504 LEU A O     
2715 C CB    . LEU A 363 ? 0.1779 0.4785 0.2528 0.0139  -0.0186 -0.0387 504 LEU A CB    
2716 C CG    . LEU A 363 ? 0.2023 0.5074 0.2815 0.0034  -0.0178 -0.0488 504 LEU A CG    
2717 C CD1   . LEU A 363 ? 0.1901 0.4807 0.2774 0.0009  -0.0127 -0.0546 504 LEU A CD1   
2718 C CD2   . LEU A 363 ? 0.1590 0.4745 0.2422 -0.0005 -0.0208 -0.0484 504 LEU A CD2   
2719 N N     . ASN A 364 ? 0.1876 0.4846 0.2455 0.0326  -0.0232 -0.0195 505 ASN A N     
2720 C CA    . ASN A 364 ? 0.2045 0.4928 0.2594 0.0422  -0.0232 -0.0110 505 ASN A CA    
2721 C C     . ASN A 364 ? 0.2775 0.5744 0.3291 0.0453  -0.0277 -0.0046 505 ASN A C     
2722 O O     . ASN A 364 ? 0.2192 0.5117 0.2734 0.0516  -0.0274 0.0008  505 ASN A O     
2723 C CB    . ASN A 364 ? 0.1971 0.4749 0.2439 0.0462  -0.0218 -0.0090 505 ASN A CB    
2724 C CG    . ASN A 364 ? 0.2428 0.5125 0.2866 0.0561  -0.0222 -0.0006 505 ASN A CG    
2725 O OD1   . ASN A 364 ? 0.1585 0.4183 0.2069 0.0596  -0.0190 0.0008  505 ASN A OD1   
2726 N ND2   . ASN A 364 ? 0.2056 0.4768 0.2404 0.0597  -0.0259 0.0050  505 ASN A ND2   
2727 N N     . ALA A 365 ? 0.2184 0.5272 0.2642 0.0406  -0.0318 -0.0053 506 ALA A N     
2728 C CA    . ALA A 365 ? 0.2807 0.5982 0.3247 0.0427  -0.0362 0.0007  506 ALA A CA    
2729 C C     . ALA A 365 ? 0.3155 0.6388 0.3696 0.0417  -0.0360 0.0001  506 ALA A C     
2730 O O     . ALA A 365 ? 0.2871 0.6143 0.3430 0.0462  -0.0383 0.0059  506 ALA A O     
2731 C CB    . ALA A 365 ? 0.2489 0.5778 0.2843 0.0357  -0.0404 -0.0006 506 ALA A CB    
2732 N N     . GLU A 366 ? 0.2830 0.6066 0.3438 0.0355  -0.0332 -0.0069 507 GLU A N     
2733 C CA    . GLU A 366 ? 0.2609 0.5881 0.3310 0.0344  -0.0326 -0.0071 507 GLU A CA    
2734 C C     . GLU A 366 ? 0.2909 0.6056 0.3660 0.0404  -0.0286 -0.0044 507 GLU A C     
2735 O O     . GLU A 366 ? 0.2271 0.5435 0.3096 0.0389  -0.0275 -0.0049 507 GLU A O     
2736 C CB    . GLU A 366 ? 0.2610 0.5934 0.3362 0.0243  -0.0317 -0.0154 507 GLU A CB    
2737 C CG    . GLU A 366 ? 0.3101 0.6557 0.3808 0.0167  -0.0353 -0.0193 507 GLU A CG    
2738 C CD    . GLU A 366 ? 0.4413 0.7990 0.5117 0.0181  -0.0396 -0.0138 507 GLU A CD    
2739 O OE1   . GLU A 366 ? 0.5453 0.9079 0.6077 0.0199  -0.0431 -0.0097 507 GLU A OE1   
2740 O OE2   . GLU A 366 ? 0.4976 0.8595 0.5760 0.0175  -0.0396 -0.0131 507 GLU A OE2   
2741 N N     . GLY A 367 ? 0.2349 0.5371 0.3055 0.0465  -0.0264 -0.0018 508 GLY A N     
2742 C CA    . GLY A 367 ? 0.2325 0.5218 0.3063 0.0509  -0.0225 -0.0002 508 GLY A CA    
2743 C C     . GLY A 367 ? 0.2212 0.5008 0.2980 0.0466  -0.0186 -0.0052 508 GLY A C     
2744 O O     . GLY A 367 ? 0.2094 0.4776 0.2877 0.0496  -0.0154 -0.0037 508 GLY A O     
2745 N N     . ILE A 368 ? 0.1958 0.4795 0.2739 0.0395  -0.0188 -0.0112 509 ILE A N     
2746 C CA    . ILE A 368 ? 0.1899 0.4647 0.2730 0.0350  -0.0153 -0.0160 509 ILE A CA    
2747 C C     . ILE A 368 ? 0.1566 0.4207 0.2346 0.0374  -0.0130 -0.0170 509 ILE A C     
2748 O O     . ILE A 368 ? 0.1375 0.4068 0.2104 0.0365  -0.0143 -0.0191 509 ILE A O     
2749 C CB    . ILE A 368 ? 0.2003 0.4840 0.2888 0.0258  -0.0162 -0.0230 509 ILE A CB    
2750 C CG1   . ILE A 368 ? 0.2006 0.4949 0.2943 0.0230  -0.0184 -0.0219 509 ILE A CG1   
2751 C CG2   . ILE A 368 ? 0.1524 0.4255 0.2470 0.0217  -0.0125 -0.0279 509 ILE A CG2   
2752 C CD1   . ILE A 368 ? 0.2013 0.5087 0.2964 0.0146  -0.0210 -0.0279 509 ILE A CD1   
2753 N N     . ALA A 369 ? 0.1236 0.3738 0.2032 0.0395  -0.0096 -0.0158 510 ALA A N     
2754 C CA    . ALA A 369 ? 0.1341 0.3731 0.2097 0.0414  -0.0071 -0.0166 510 ALA A CA    
2755 C C     . ALA A 369 ? 0.1448 0.3793 0.2268 0.0351  -0.0046 -0.0230 510 ALA A C     
2756 O O     . ALA A 369 ? 0.1304 0.3598 0.2195 0.0325  -0.0033 -0.0231 510 ALA A O     
2757 C CB    . ALA A 369 ? 0.1297 0.3555 0.2022 0.0473  -0.0050 -0.0114 510 ALA A CB    
2758 N N     . VAL A 370 ? 0.0879 0.3252 0.1682 0.0323  -0.0041 -0.0283 511 VAL A N     
2759 C CA    . VAL A 370 ? 0.1043 0.3356 0.1905 0.0271  -0.0011 -0.0350 511 VAL A CA    
2760 C C     . VAL A 370 ? 0.1841 0.4083 0.2629 0.0284  0.0011  -0.0367 511 VAL A C     
2761 O O     . VAL A 370 ? 0.2041 0.4288 0.2726 0.0319  -0.0003 -0.0330 511 VAL A O     
2762 C CB    . VAL A 370 ? 0.1456 0.3878 0.2381 0.0192  -0.0019 -0.0428 511 VAL A CB    
2763 C CG1   . VAL A 370 ? 0.1285 0.3769 0.2263 0.0171  -0.0043 -0.0407 511 VAL A CG1   
2764 C CG2   . VAL A 370 ? 0.1760 0.4253 0.2584 0.0168  -0.0036 -0.0456 511 VAL A CG2   
2765 N N     . ARG A 371 ? 0.1769 0.3914 0.2601 0.0253  0.0043  -0.0416 512 ARG A N     
2766 C CA    . ARG A 371 ? 0.1858 0.3920 0.2614 0.0246  0.0067  -0.0443 512 ARG A CA    
2767 C C     . ARG A 371 ? 0.1974 0.4073 0.2740 0.0173  0.0079  -0.0534 512 ARG A C     
2768 O O     . ARG A 371 ? 0.1748 0.3862 0.2618 0.0128  0.0085  -0.0588 512 ARG A O     
2769 C CB    . ARG A 371 ? 0.1855 0.3787 0.2653 0.0265  0.0099  -0.0437 512 ARG A CB    
2770 C CG    . ARG A 371 ? 0.3043 0.4924 0.3814 0.0331  0.0095  -0.0357 512 ARG A CG    
2771 C CD    . ARG A 371 ? 0.3004 0.4832 0.3648 0.0369  0.0097  -0.0320 512 ARG A CD    
2772 N NE    . ARG A 371 ? 0.2756 0.4552 0.3380 0.0433  0.0090  -0.0249 512 ARG A NE    
2773 C CZ    . ARG A 371 ? 0.2713 0.4439 0.3241 0.0475  0.0092  -0.0207 512 ARG A CZ    
2774 N NH1   . ARG A 371 ? 0.3080 0.4759 0.3521 0.0458  0.0102  -0.0221 512 ARG A NH1   
2775 N NH2   . ARG A 371 ? 0.2326 0.4009 0.2835 0.0527  0.0087  -0.0151 512 ARG A NH2   
2776 N N     . ALA A 372 ? 0.1599 0.3709 0.2255 0.0157  0.0083  -0.0552 513 ALA A N     
2777 C CA    . ALA A 372 ? 0.2137 0.4272 0.2783 0.0087  0.0105  -0.0647 513 ALA A CA    
2778 C C     . ALA A 372 ? 0.3178 0.5220 0.3772 0.0090  0.0142  -0.0663 513 ALA A C     
2779 O O     . ALA A 372 ? 0.3489 0.5508 0.3972 0.0123  0.0135  -0.0604 513 ALA A O     
2780 C CB    . ALA A 372 ? 0.2252 0.4517 0.2803 0.0050  0.0073  -0.0656 513 ALA A CB    
2781 N N     . GLY A 373 ? 0.2714 0.4701 0.3395 0.0059  0.0182  -0.0739 514 GLY A N     
2782 C CA    . GLY A 373 ? 0.2076 0.3977 0.2734 0.0067  0.0219  -0.0751 514 GLY A CA    
2783 C C     . GLY A 373 ? 0.2157 0.3990 0.2964 0.0055  0.0254  -0.0815 514 GLY A C     
2784 O O     . GLY A 373 ? 0.1864 0.3718 0.2777 0.0026  0.0253  -0.0866 514 GLY A O     
2785 N N     . HIS A 374 ? 0.1698 0.3448 0.2517 0.0078  0.0281  -0.0806 515 HIS A N     
2786 C CA    . HIS A 374 ? 0.2355 0.4034 0.3322 0.0073  0.0308  -0.0854 515 HIS A CA    
2787 C C     . HIS A 374 ? 0.2030 0.3614 0.3067 0.0118  0.0283  -0.0770 515 HIS A C     
2788 O O     . HIS A 374 ? 0.1827 0.3325 0.2973 0.0114  0.0290  -0.0783 515 HIS A O     
2789 C CB    . HIS A 374 ? 0.2043 0.3661 0.2981 0.0055  0.0343  -0.0892 515 HIS A CB    
2790 C CG    . HIS A 374 ? 0.2277 0.3859 0.3112 0.0087  0.0343  -0.0821 515 HIS A CG    
2791 N ND1   . HIS A 374 ? 0.2233 0.3741 0.3079 0.0136  0.0323  -0.0732 515 HIS A ND1   
2792 C CD2   . HIS A 374 ? 0.2351 0.3958 0.3066 0.0070  0.0364  -0.0827 515 HIS A CD2   
2793 C CE1   . HIS A 374 ? 0.2906 0.4395 0.3651 0.0151  0.0332  -0.0694 515 HIS A CE1   
2794 N NE2   . HIS A 374 ? 0.2872 0.4419 0.3538 0.0112  0.0356  -0.0747 515 HIS A NE2   
2795 N N     . HIS A 375 ? 0.1674 0.3274 0.2649 0.0159  0.0256  -0.0685 516 HIS A N     
2796 C CA    . HIS A 375 ? 0.1838 0.3370 0.2868 0.0192  0.0231  -0.0608 516 HIS A CA    
2797 C C     . HIS A 375 ? 0.1692 0.3104 0.2753 0.0208  0.0242  -0.0576 516 HIS A C     
2798 O O     . HIS A 375 ? 0.1756 0.3109 0.2898 0.0217  0.0229  -0.0536 516 HIS A O     
2799 C CB    . HIS A 375 ? 0.1358 0.2913 0.2505 0.0168  0.0218  -0.0630 516 HIS A CB    
2800 C CG    . HIS A 375 ? 0.1867 0.3553 0.2999 0.0138  0.0209  -0.0678 516 HIS A CG    
2801 N ND1   . HIS A 375 ? 0.1587 0.3352 0.2621 0.0159  0.0182  -0.0627 516 HIS A ND1   
2802 C CD2   . HIS A 375 ? 0.1389 0.3128 0.2579 0.0085  0.0220  -0.0768 516 HIS A CD2   
2803 C CE1   . HIS A 375 ? 0.1903 0.3759 0.2925 0.0117  0.0171  -0.0674 516 HIS A CE1   
2804 N NE2   . HIS A 375 ? 0.1694 0.3534 0.2804 0.0068  0.0194  -0.0762 516 HIS A NE2   
2805 N N     . CYS A 376 ? 0.1474 0.2861 0.2472 0.0207  0.0265  -0.0591 517 CYS A N     
2806 C CA    . CYS A 376 ? 0.1172 0.2463 0.2203 0.0215  0.0275  -0.0569 517 CYS A CA    
2807 C C     . CYS A 376 ? 0.1553 0.2798 0.2724 0.0196  0.0279  -0.0605 517 CYS A C     
2808 O O     . CYS A 376 ? 0.1660 0.2836 0.2893 0.0211  0.0268  -0.0559 517 CYS A O     
2809 C CB    . CYS A 376 ? 0.1724 0.2967 0.2721 0.0255  0.0257  -0.0478 517 CYS A CB    
2810 S SG    . CYS A 376 ? 0.3757 0.5029 0.4593 0.0287  0.0256  -0.0436 517 CYS A SG    
2811 N N     . ALA A 377 ? 0.1417 0.2703 0.2637 0.0161  0.0293  -0.0690 518 ALA A N     
2812 C CA    . ALA A 377 ? 0.1518 0.2757 0.2878 0.0143  0.0300  -0.0740 518 ALA A CA    
2813 C C     . ALA A 377 ? 0.1779 0.3057 0.3150 0.0102  0.0333  -0.0852 518 ALA A C     
2814 O O     . ALA A 377 ? 0.1553 0.2854 0.3009 0.0074  0.0340  -0.0923 518 ALA A O     
2815 C CB    . ALA A 377 ? 0.1646 0.2889 0.3100 0.0142  0.0275  -0.0721 518 ALA A CB    
2816 N N     . GLN A 378 ? 0.1456 0.2745 0.2740 0.0093  0.0356  -0.0872 519 GLN A N     
2817 C CA    . GLN A 378 ? 0.2185 0.3521 0.3462 0.0048  0.0390  -0.0978 519 GLN A CA    
2818 C C     . GLN A 378 ? 0.1432 0.2721 0.2860 0.0030  0.0407  -0.1053 519 GLN A C     
2819 O O     . GLN A 378 ? 0.2219 0.3556 0.3675 -0.0010 0.0427  -0.1150 519 GLN A O     
2820 C CB    . GLN A 378 ? 0.2080 0.3429 0.3249 0.0040  0.0413  -0.0975 519 GLN A CB    
2821 C CG    . GLN A 378 ? 0.2449 0.3855 0.3466 0.0049  0.0403  -0.0921 519 GLN A CG    
2822 C CD    . GLN A 378 ? 0.2843 0.4252 0.3760 0.0036  0.0426  -0.0915 519 GLN A CD    
2823 O OE1   . GLN A 378 ? 0.3089 0.4446 0.3986 0.0066  0.0421  -0.0848 519 GLN A OE1   
2824 N NE2   . GLN A 378 ? 0.3036 0.4510 0.3892 -0.0012 0.0453  -0.0985 519 GLN A NE2   
2825 N N     . PRO A 379 ? 0.1783 0.2983 0.3312 0.0056  0.0400  -0.1019 520 PRO A N     
2826 C CA    . PRO A 379 ? 0.2137 0.3297 0.3816 0.0039  0.0418  -0.1099 520 PRO A CA    
2827 C C     . PRO A 379 ? 0.2149 0.3312 0.3936 0.0023  0.0413  -0.1150 520 PRO A C     
2828 O O     . PRO A 379 ? 0.1914 0.3093 0.3770 -0.0013 0.0441  -0.1259 520 PRO A O     
2829 C CB    . PRO A 379 ? 0.1984 0.3059 0.3741 0.0076  0.0401  -0.1028 520 PRO A CB    
2830 C CG    . PRO A 379 ? 0.2066 0.3156 0.3685 0.0093  0.0397  -0.0955 520 PRO A CG    
2831 C CD    . PRO A 379 ? 0.1929 0.3074 0.3435 0.0094  0.0382  -0.0921 520 PRO A CD    
2832 N N     . ILE A 380 ? 0.1934 0.3087 0.3737 0.0044  0.0379  -0.1079 521 ILE A N     
2833 C CA    . ILE A 380 ? 0.2017 0.3181 0.3933 0.0023  0.0375  -0.1127 521 ILE A CA    
2834 C C     . ILE A 380 ? 0.1929 0.3202 0.3776 -0.0022 0.0396  -0.1217 521 ILE A C     
2835 O O     . ILE A 380 ? 0.2207 0.3496 0.4153 -0.0058 0.0415  -0.1317 521 ILE A O     
2836 C CB    . ILE A 380 ? 0.1702 0.2846 0.3646 0.0049  0.0333  -0.1022 521 ILE A CB    
2837 C CG1   . ILE A 380 ? 0.1804 0.2948 0.3898 0.0023  0.0329  -0.1071 521 ILE A CG1   
2838 C CG2   . ILE A 380 ? 0.1386 0.2609 0.3174 0.0059  0.0315  -0.0955 521 ILE A CG2   
2839 C CD1   . ILE A 380 ? 0.1867 0.2927 0.4143 0.0015  0.0348  -0.1145 521 ILE A CD1   
2840 N N     . LEU A 381 ? 0.1653 0.3005 0.3333 -0.0023 0.0393  -0.1188 522 LEU A N     
2841 C CA    . LEU A 381 ? 0.2207 0.3677 0.3812 -0.0070 0.0409  -0.1268 522 LEU A CA    
2842 C C     . LEU A 381 ? 0.2437 0.3921 0.4049 -0.0115 0.0453  -0.1389 522 LEU A C     
2843 O O     . LEU A 381 ? 0.2470 0.4019 0.4106 -0.0165 0.0473  -0.1494 522 LEU A O     
2844 C CB    . LEU A 381 ? 0.1918 0.3471 0.3348 -0.0058 0.0393  -0.1200 522 LEU A CB    
2845 C CG    . LEU A 381 ? 0.2508 0.4083 0.3920 -0.0023 0.0350  -0.1094 522 LEU A CG    
2846 C CD1   . LEU A 381 ? 0.2205 0.3902 0.3467 -0.0027 0.0337  -0.1068 522 LEU A CD1   
2847 C CD2   . LEU A 381 ? 0.1788 0.3368 0.3336 -0.0039 0.0333  -0.1111 522 LEU A CD2   
2848 N N     . ARG A 382 ? 0.2432 0.3861 0.4024 -0.0103 0.0468  -0.1379 523 ARG A N     
2849 C CA    . ARG A 382 ? 0.2402 0.3845 0.4016 -0.0147 0.0509  -0.1487 523 ARG A CA    
2850 C C     . ARG A 382 ? 0.2535 0.3921 0.4339 -0.0161 0.0524  -0.1572 523 ARG A C     
2851 O O     . ARG A 382 ? 0.2624 0.4055 0.4458 -0.0213 0.0557  -0.1687 523 ARG A O     
2852 C CB    . ARG A 382 ? 0.2599 0.4003 0.4173 -0.0129 0.0520  -0.1449 523 ARG A CB    
2853 C CG    . ARG A 382 ? 0.3095 0.4552 0.4487 -0.0123 0.0511  -0.1377 523 ARG A CG    
2854 C CD    . ARG A 382 ? 0.5042 0.6496 0.6395 -0.0136 0.0539  -0.1391 523 ARG A CD    
2855 N NE    . ARG A 382 ? 0.4319 0.5781 0.5537 -0.0115 0.0528  -0.1300 523 ARG A NE    
2856 C CZ    . ARG A 382 ? 0.4135 0.5525 0.5369 -0.0065 0.0508  -0.1207 523 ARG A CZ    
2857 N NH1   . ARG A 382 ? 0.2966 0.4275 0.4337 -0.0030 0.0492  -0.1183 523 ARG A NH1   
2858 N NH2   . ARG A 382 ? 0.3979 0.5381 0.5088 -0.0053 0.0503  -0.1136 523 ARG A NH2   
2859 N N     . ARG A 383 ? 0.2304 0.3592 0.4240 -0.0117 0.0501  -0.1515 524 ARG A N     
2860 C CA    . ARG A 383 ? 0.2397 0.3624 0.4528 -0.0128 0.0512  -0.1586 524 ARG A CA    
2861 C C     . ARG A 383 ? 0.3061 0.4354 0.5217 -0.0173 0.0521  -0.1672 524 ARG A C     
2862 O O     . ARG A 383 ? 0.3179 0.4459 0.5458 -0.0209 0.0549  -0.1781 524 ARG A O     
2863 C CB    . ARG A 383 ? 0.2361 0.3481 0.4615 -0.0075 0.0477  -0.1488 524 ARG A CB    
2864 C CG    . ARG A 383 ? 0.2538 0.3594 0.4995 -0.0081 0.0474  -0.1533 524 ARG A CG    
2865 C CD    . ARG A 383 ? 0.2399 0.3411 0.5000 -0.0101 0.0508  -0.1634 524 ARG A CD    
2866 N NE    . ARG A 383 ? 0.2751 0.3686 0.5563 -0.0101 0.0502  -0.1662 524 ARG A NE    
2867 C CZ    . ARG A 383 ? 0.3068 0.4026 0.5951 -0.0145 0.0522  -0.1763 524 ARG A CZ    
2868 N NH1   . ARG A 383 ? 0.2877 0.3944 0.5634 -0.0194 0.0547  -0.1845 524 ARG A NH1   
2869 N NH2   . ARG A 383 ? 0.2635 0.3507 0.5720 -0.0142 0.0514  -0.1777 524 ARG A NH2   
2870 N N     . MET A 384 ? 0.2356 0.3729 0.4401 -0.0175 0.0499  -0.1625 525 MET A N     
2871 C CA    . MET A 384 ? 0.2734 0.4202 0.4783 -0.0225 0.0507  -0.1705 525 MET A CA    
2872 C C     . MET A 384 ? 0.2551 0.4132 0.4455 -0.0285 0.0536  -0.1798 525 MET A C     
2873 O O     . MET A 384 ? 0.2840 0.4521 0.4707 -0.0333 0.0541  -0.1863 525 MET A O     
2874 C CB    . MET A 384 ? 0.2687 0.4220 0.4694 -0.0206 0.0464  -0.1600 525 MET A CB    
2875 C CG    . MET A 384 ? 0.2926 0.4360 0.5073 -0.0167 0.0428  -0.1506 525 MET A CG    
2876 S SD    . MET A 384 ? 0.4716 0.6044 0.7092 -0.0197 0.0446  -0.1607 525 MET A SD    
2877 C CE    . MET A 384 ? 0.2920 0.4117 0.5459 -0.0129 0.0419  -0.1493 525 MET A CE    
2878 N N     . GLY A 385 ? 0.2735 0.4314 0.4553 -0.0289 0.0553  -0.1799 526 GLY A N     
2879 C CA    . GLY A 385 ? 0.2363 0.4054 0.4043 -0.0351 0.0576  -0.1870 526 GLY A CA    
2880 C C     . GLY A 385 ? 0.3136 0.4939 0.4619 -0.0358 0.0552  -0.1808 526 GLY A C     
2881 O O     . GLY A 385 ? 0.2840 0.4754 0.4215 -0.0420 0.0560  -0.1869 526 GLY A O     
2882 N N     . LEU A 386 ? 0.2622 0.4400 0.4054 -0.0296 0.0520  -0.1682 527 LEU A N     
2883 C CA    . LEU A 386 ? 0.2627 0.4511 0.3897 -0.0292 0.0493  -0.1610 527 LEU A CA    
2884 C C     . LEU A 386 ? 0.2947 0.4787 0.4123 -0.0240 0.0477  -0.1494 527 LEU A C     
2885 O O     . LEU A 386 ? 0.2504 0.4229 0.3757 -0.0194 0.0476  -0.1444 527 LEU A O     
2886 C CB    . LEU A 386 ? 0.2646 0.4556 0.3960 -0.0273 0.0450  -0.1549 527 LEU A CB    
2887 C CG    . LEU A 386 ? 0.2931 0.4874 0.4308 -0.0335 0.0443  -0.1635 527 LEU A CG    
2888 C CD1   . LEU A 386 ? 0.2458 0.4356 0.3930 -0.0310 0.0396  -0.1553 527 LEU A CD1   
2889 C CD2   . LEU A 386 ? 0.2817 0.4897 0.4028 -0.0400 0.0431  -0.1672 527 LEU A CD2   
2890 N N     . GLU A 387 ? 0.2824 0.4759 0.3831 -0.0249 0.0464  -0.1450 528 GLU A N     
2891 C CA    . GLU A 387 ? 0.3033 0.4938 0.3939 -0.0202 0.0449  -0.1340 528 GLU A CA    
2892 C C     . GLU A 387 ? 0.2515 0.4437 0.3413 -0.0146 0.0408  -0.1233 528 GLU A C     
2893 O O     . GLU A 387 ? 0.2263 0.4121 0.3127 -0.0095 0.0395  -0.1139 528 GLU A O     
2894 C CB    . GLU A 387 ? 0.3594 0.5584 0.4317 -0.0245 0.0456  -0.1343 528 GLU A CB    
2895 C CG    . GLU A 387 ? 0.3703 0.5670 0.4419 -0.0294 0.0494  -0.1414 528 GLU A CG    
2896 C CD    . GLU A 387 ? 0.6097 0.7941 0.6905 -0.0253 0.0510  -0.1387 528 GLU A CD    
2897 O OE1   . GLU A 387 ? 0.6614 0.8404 0.7559 -0.0263 0.0533  -0.1458 528 GLU A OE1   
2898 O OE2   . GLU A 387 ? 0.6601 0.8403 0.7345 -0.0212 0.0499  -0.1295 528 GLU A OE2   
2899 N N     . ALA A 388 ? 0.2460 0.4428 0.3373 -0.0161 0.0371  -0.1225 529 ALA A N     
2900 C CA    . ALA A 388 ? 0.2410 0.4379 0.3295 -0.0114 0.0317  -0.1107 529 ALA A CA    
2901 C C     . ALA A 388 ? 0.2132 0.4140 0.3100 -0.0140 0.0290  -0.1129 529 ALA A C     
2902 O O     . ALA A 388 ? 0.2150 0.4202 0.3153 -0.0201 0.0306  -0.1230 529 ALA A O     
2903 C CB    . ALA A 388 ? 0.1924 0.3961 0.2627 -0.0108 0.0287  -0.1036 529 ALA A CB    
2904 N N     . THR A 389 ? 0.1806 0.3800 0.2808 -0.0096 0.0251  -0.1035 530 THR A N     
2905 C CA    . THR A 389 ? 0.1827 0.3881 0.2885 -0.0121 0.0218  -0.1035 530 THR A CA    
2906 C C     . THR A 389 ? 0.1512 0.3623 0.2494 -0.0077 0.0171  -0.0922 530 THR A C     
2907 O O     . THR A 389 ? 0.1861 0.3930 0.2780 -0.0018 0.0166  -0.0843 530 THR A O     
2908 C CB    . THR A 389 ? 0.1699 0.3670 0.2933 -0.0120 0.0225  -0.1049 530 THR A CB    
2909 O OG1   . THR A 389 ? 0.1542 0.3440 0.2809 -0.0055 0.0214  -0.0950 530 THR A OG1   
2910 C CG2   . THR A 389 ? 0.1577 0.3477 0.2908 -0.0149 0.0272  -0.1155 530 THR A CG2   
2911 N N     . VAL A 390 ? 0.1657 0.3868 0.2647 -0.0107 0.0137  -0.0921 531 VAL A N     
2912 C CA    . VAL A 390 ? 0.1269 0.3539 0.2243 -0.0063 0.0093  -0.0822 531 VAL A CA    
2913 C C     . VAL A 390 ? 0.1364 0.3571 0.2474 -0.0045 0.0094  -0.0791 531 VAL A C     
2914 O O     . VAL A 390 ? 0.1357 0.3546 0.2576 -0.0094 0.0104  -0.0852 531 VAL A O     
2915 C CB    . VAL A 390 ? 0.1563 0.3985 0.2496 -0.0107 0.0055  -0.0834 531 VAL A CB    
2916 C CG1   . VAL A 390 ? 0.1272 0.3770 0.2177 -0.0052 0.0012  -0.0728 531 VAL A CG1   
2917 C CG2   . VAL A 390 ? 0.1604 0.4089 0.2412 -0.0151 0.0058  -0.0888 531 VAL A CG2   
2918 N N     . ARG A 391 ? 0.1224 0.3392 0.2330 0.0021  0.0086  -0.0699 532 ARG A N     
2919 C CA    . ARG A 391 ? 0.1338 0.3433 0.2559 0.0037  0.0091  -0.0664 532 ARG A CA    
2920 C C     . ARG A 391 ? 0.1383 0.3528 0.2595 0.0078  0.0062  -0.0572 532 ARG A C     
2921 O O     . ARG A 391 ? 0.1628 0.3701 0.2789 0.0136  0.0064  -0.0498 532 ARG A O     
2922 C CB    . ARG A 391 ? 0.1576 0.3540 0.2813 0.0073  0.0120  -0.0652 532 ARG A CB    
2923 C CG    . ARG A 391 ? 0.1866 0.3740 0.3221 0.0075  0.0122  -0.0621 532 ARG A CG    
2924 C CD    . ARG A 391 ? 0.1223 0.2975 0.2553 0.0124  0.0134  -0.0561 532 ARG A CD    
2925 N NE    . ARG A 391 ? 0.1570 0.3330 0.2777 0.0176  0.0123  -0.0488 532 ARG A NE    
2926 C CZ    . ARG A 391 ? 0.1704 0.3372 0.2860 0.0215  0.0134  -0.0443 532 ARG A CZ    
2927 N NH1   . ARG A 391 ? 0.1488 0.3059 0.2699 0.0210  0.0152  -0.0456 532 ARG A NH1   
2928 N NH2   . ARG A 391 ? 0.1970 0.3643 0.3020 0.0260  0.0125  -0.0385 532 ARG A NH2   
2929 N N     . PRO A 392 ? 0.1314 0.3551 0.2561 0.0045  0.0038  -0.0571 533 PRO A N     
2930 C CA    . PRO A 392 ? 0.1217 0.3450 0.2474 0.0072  0.0020  -0.0486 533 PRO A CA    
2931 C C     . PRO A 392 ? 0.1754 0.3870 0.3099 0.0070  0.0038  -0.0461 533 PRO A C     
2932 O O     . PRO A 392 ? 0.1226 0.3292 0.2664 0.0028  0.0053  -0.0519 533 PRO A O     
2933 C CB    . PRO A 392 ? 0.1599 0.3955 0.2894 0.0018  -0.0005 -0.0510 533 PRO A CB    
2934 C CG    . PRO A 392 ? 0.1309 0.3677 0.2664 -0.0053 0.0008  -0.0617 533 PRO A CG    
2935 C CD    . PRO A 392 ? 0.1132 0.3473 0.2419 -0.0029 0.0028  -0.0653 533 PRO A CD    
2936 N N     . SER A 393 ? 0.1186 0.3257 0.2504 0.0115  0.0036  -0.0377 534 SER A N     
2937 C CA    . SER A 393 ? 0.1538 0.3524 0.2934 0.0111  0.0046  -0.0339 534 SER A CA    
2938 C C     . SER A 393 ? 0.1491 0.3509 0.2875 0.0127  0.0036  -0.0265 534 SER A C     
2939 O O     . SER A 393 ? 0.1620 0.3652 0.2908 0.0175  0.0032  -0.0228 534 SER A O     
2940 C CB    . SER A 393 ? 0.1493 0.3359 0.2858 0.0149  0.0066  -0.0323 534 SER A CB    
2941 O OG    . SER A 393 ? 0.1637 0.3487 0.2878 0.0205  0.0067  -0.0289 534 SER A OG    
2942 N N     . PHE A 394 ? 0.1392 0.3423 0.2876 0.0086  0.0033  -0.0248 535 PHE A N     
2943 C CA    . PHE A 394 ? 0.1529 0.3618 0.3018 0.0084  0.0025  -0.0193 535 PHE A CA    
2944 C C     . PHE A 394 ? 0.1553 0.3576 0.3044 0.0107  0.0037  -0.0131 535 PHE A C     
2945 O O     . PHE A 394 ? 0.1825 0.3772 0.3366 0.0101  0.0045  -0.0125 535 PHE A O     
2946 C CB    . PHE A 394 ? 0.1747 0.3913 0.3344 0.0011  0.0012  -0.0213 535 PHE A CB    
2947 C CG    . PHE A 394 ? 0.1782 0.4018 0.3383 -0.0027 -0.0001 -0.0286 535 PHE A CG    
2948 C CD1   . PHE A 394 ? 0.1603 0.3919 0.3112 0.0000  -0.0014 -0.0292 535 PHE A CD1   
2949 C CD2   . PHE A 394 ? 0.1622 0.3842 0.3320 -0.0091 -0.0001 -0.0352 535 PHE A CD2   
2950 C CE1   . PHE A 394 ? 0.1795 0.4191 0.3302 -0.0040 -0.0029 -0.0360 535 PHE A CE1   
2951 C CE2   . PHE A 394 ? 0.1966 0.4250 0.3661 -0.0133 -0.0010 -0.0430 535 PHE A CE2   
2952 C CZ    . PHE A 394 ? 0.1869 0.4250 0.3464 -0.0109 -0.0025 -0.0432 535 PHE A CZ    
2953 N N     . ALA A 395 ? 0.1302 0.3358 0.2738 0.0133  0.0038  -0.0088 536 ALA A N     
2954 C CA    . ALA A 395 ? 0.1476 0.3502 0.2911 0.0142  0.0050  -0.0037 536 ALA A CA    
2955 C C     . ALA A 395 ? 0.1436 0.3559 0.2904 0.0113  0.0047  -0.0014 536 ALA A C     
2956 O O     . ALA A 395 ? 0.1012 0.3221 0.2501 0.0092  0.0034  -0.0035 536 ALA A O     
2957 C CB    . ALA A 395 ? 0.1205 0.3167 0.2520 0.0207  0.0063  -0.0018 536 ALA A CB    
2958 N N     . PHE A 396 ? 0.0846 0.2968 0.2319 0.0107  0.0059  0.0029  537 PHE A N     
2959 C CA    . PHE A 396 ? 0.1124 0.3343 0.2640 0.0068  0.0059  0.0053  537 PHE A CA    
2960 C C     . PHE A 396 ? 0.1124 0.3418 0.2568 0.0107  0.0065  0.0055  537 PHE A C     
2961 O O     . PHE A 396 ? 0.1193 0.3581 0.2675 0.0075  0.0066  0.0070  537 PHE A O     
2962 C CB    . PHE A 396 ? 0.1370 0.3577 0.2911 0.0040  0.0070  0.0102  537 PHE A CB    
2963 C CG    . PHE A 396 ? 0.1291 0.3455 0.2730 0.0093  0.0090  0.0126  537 PHE A CG    
2964 C CD1   . PHE A 396 ? 0.1309 0.3371 0.2718 0.0118  0.0092  0.0128  537 PHE A CD1   
2965 C CD2   . PHE A 396 ? 0.1602 0.3833 0.2984 0.0113  0.0108  0.0145  537 PHE A CD2   
2966 C CE1   . PHE A 396 ? 0.1645 0.3671 0.2961 0.0160  0.0109  0.0149  537 PHE A CE1   
2967 C CE2   . PHE A 396 ? 0.2005 0.4200 0.3299 0.0158  0.0127  0.0162  537 PHE A CE2   
2968 C CZ    . PHE A 396 ? 0.1586 0.3678 0.2845 0.0179  0.0127  0.0164  537 PHE A CZ    
2969 N N     . TYR A 397 ? 0.1061 0.3320 0.2413 0.0172  0.0067  0.0043  538 TYR A N     
2970 C CA    . TYR A 397 ? 0.1172 0.3511 0.2480 0.0209  0.0065  0.0041  538 TYR A CA    
2971 C C     . TYR A 397 ? 0.1212 0.3610 0.2533 0.0202  0.0040  0.0010  538 TYR A C     
2972 O O     . TYR A 397 ? 0.1195 0.3669 0.2488 0.0233  0.0033  0.0011  538 TYR A O     
2973 C CB    . TYR A 397 ? 0.0825 0.3108 0.2031 0.0282  0.0080  0.0050  538 TYR A CB    
2974 C CG    . TYR A 397 ? 0.1256 0.3419 0.2403 0.0313  0.0079  0.0038  538 TYR A CG    
2975 C CD1   . TYR A 397 ? 0.1086 0.3234 0.2230 0.0311  0.0060  0.0009  538 TYR A CD1   
2976 C CD2   . TYR A 397 ? 0.1318 0.3396 0.2408 0.0341  0.0098  0.0053  538 TYR A CD2   
2977 C CE1   . TYR A 397 ? 0.1482 0.3530 0.2572 0.0337  0.0062  -0.0002 538 TYR A CE1   
2978 C CE2   . TYR A 397 ? 0.1011 0.2983 0.2048 0.0366  0.0097  0.0043  538 TYR A CE2   
2979 C CZ    . TYR A 397 ? 0.1272 0.3228 0.2310 0.0364  0.0080  0.0016  538 TYR A CZ    
2980 O OH    . TYR A 397 ? 0.1156 0.3016 0.2143 0.0385  0.0083  0.0005  538 TYR A OH    
2981 N N     . ASN A 398 ? 0.0919 0.3293 0.2286 0.0162  0.0027  -0.0019 539 ASN A N     
2982 C CA    . ASN A 398 ? 0.1041 0.3491 0.2423 0.0143  0.0003  -0.0054 539 ASN A CA    
2983 C C     . ASN A 398 ? 0.0904 0.3462 0.2373 0.0078  -0.0008 -0.0057 539 ASN A C     
2984 O O     . ASN A 398 ? 0.1185 0.3739 0.2722 0.0034  0.0001  -0.0038 539 ASN A O     
2985 C CB    . ASN A 398 ? 0.1092 0.3482 0.2486 0.0123  -0.0004 -0.0095 539 ASN A CB    
2986 C CG    . ASN A 398 ? 0.1641 0.3940 0.2942 0.0183  0.0004  -0.0097 539 ASN A CG    
2987 O OD1   . ASN A 398 ? 0.1147 0.3349 0.2454 0.0183  0.0016  -0.0103 539 ASN A OD1   
2988 N ND2   . ASN A 398 ? 0.1029 0.3360 0.2248 0.0236  -0.0004 -0.0087 539 ASN A ND2   
2989 N N     . THR A 399 ? 0.0920 0.3580 0.2387 0.0069  -0.0030 -0.0078 540 THR A N     
2990 C CA    . THR A 399 ? 0.1171 0.3944 0.2711 0.0009  -0.0043 -0.0081 540 THR A CA    
2991 C C     . THR A 399 ? 0.1777 0.4596 0.3359 -0.0053 -0.0067 -0.0133 540 THR A C     
2992 O O     . THR A 399 ? 0.1090 0.3884 0.2626 -0.0039 -0.0077 -0.0169 540 THR A O     
2993 C CB    . THR A 399 ? 0.1608 0.4492 0.3120 0.0047  -0.0049 -0.0059 540 THR A CB    
2994 O OG1   . THR A 399 ? 0.1416 0.4345 0.2872 0.0082  -0.0072 -0.0077 540 THR A OG1   
2995 C CG2   . THR A 399 ? 0.1159 0.4006 0.2627 0.0108  -0.0022 -0.0019 540 THR A CG2   
2996 N N     . PHE A 400 ? 0.0983 0.3874 0.2648 -0.0127 -0.0076 -0.0141 541 PHE A N     
2997 C CA    . PHE A 400 ? 0.1228 0.4176 0.2930 -0.0195 -0.0100 -0.0196 541 PHE A CA    
2998 C C     . PHE A 400 ? 0.1422 0.4476 0.3057 -0.0167 -0.0125 -0.0212 541 PHE A C     
2999 O O     . PHE A 400 ? 0.1251 0.4327 0.2865 -0.0195 -0.0142 -0.0264 541 PHE A O     
3000 C CB    . PHE A 400 ? 0.1242 0.4241 0.3045 -0.0282 -0.0105 -0.0196 541 PHE A CB    
3001 C CG    . PHE A 400 ? 0.1273 0.4170 0.3155 -0.0323 -0.0087 -0.0181 541 PHE A CG    
3002 C CD1   . PHE A 400 ? 0.1205 0.4081 0.3100 -0.0303 -0.0066 -0.0121 541 PHE A CD1   
3003 C CD2   . PHE A 400 ? 0.1352 0.4176 0.3295 -0.0381 -0.0090 -0.0229 541 PHE A CD2   
3004 C CE1   . PHE A 400 ? 0.1321 0.4111 0.3288 -0.0343 -0.0054 -0.0100 541 PHE A CE1   
3005 C CE2   . PHE A 400 ? 0.1486 0.4216 0.3512 -0.0418 -0.0078 -0.0209 541 PHE A CE2   
3006 C CZ    . PHE A 400 ? 0.1609 0.4326 0.3649 -0.0399 -0.0063 -0.0139 541 PHE A CZ    
3007 N N     . ASP A 401 ? 0.1347 0.4473 0.2948 -0.0113 -0.0126 -0.0168 542 ASP A N     
3008 C CA    . ASP A 401 ? 0.1314 0.4542 0.2857 -0.0078 -0.0152 -0.0170 542 ASP A CA    
3009 C C     . ASP A 401 ? 0.1713 0.4881 0.3170 -0.0027 -0.0157 -0.0185 542 ASP A C     
3010 O O     . ASP A 401 ? 0.1507 0.4746 0.2928 -0.0041 -0.0184 -0.0215 542 ASP A O     
3011 C CB    . ASP A 401 ? 0.1606 0.4900 0.3141 -0.0018 -0.0147 -0.0118 542 ASP A CB    
3012 C CG    . ASP A 401 ? 0.2489 0.5906 0.4101 -0.0072 -0.0154 -0.0111 542 ASP A CG    
3013 O OD1   . ASP A 401 ? 0.2313 0.5742 0.3987 -0.0159 -0.0160 -0.0141 542 ASP A OD1   
3014 O OD2   . ASP A 401 ? 0.2496 0.5991 0.4111 -0.0028 -0.0151 -0.0077 542 ASP A OD2   
3015 N N     . GLU A 402 ? 0.1242 0.4286 0.2661 0.0029  -0.0132 -0.0163 543 GLU A N     
3016 C CA    . GLU A 402 ? 0.1686 0.4663 0.3026 0.0073  -0.0133 -0.0176 543 GLU A CA    
3017 C C     . GLU A 402 ? 0.1073 0.4037 0.2426 0.0009  -0.0139 -0.0242 543 GLU A C     
3018 O O     . GLU A 402 ? 0.1418 0.4415 0.2711 0.0016  -0.0155 -0.0270 543 GLU A O     
3019 C CB    . GLU A 402 ? 0.1219 0.4055 0.2526 0.0129  -0.0101 -0.0145 543 GLU A CB    
3020 C CG    . GLU A 402 ? 0.1478 0.4314 0.2752 0.0200  -0.0091 -0.0093 543 GLU A CG    
3021 C CD    . GLU A 402 ? 0.1701 0.4396 0.2938 0.0243  -0.0060 -0.0071 543 GLU A CD    
3022 O OE1   . GLU A 402 ? 0.1279 0.3895 0.2551 0.0206  -0.0045 -0.0083 543 GLU A OE1   
3023 O OE2   . GLU A 402 ? 0.1668 0.4333 0.2845 0.0312  -0.0053 -0.0042 543 GLU A OE2   
3024 N N     . ILE A 403 ? 0.1037 0.3957 0.2473 -0.0056 -0.0126 -0.0270 544 ILE A N     
3025 C CA    . ILE A 403 ? 0.1082 0.3988 0.2547 -0.0124 -0.0129 -0.0345 544 ILE A CA    
3026 C C     . ILE A 403 ? 0.1357 0.4398 0.2807 -0.0174 -0.0160 -0.0388 544 ILE A C     
3027 O O     . ILE A 403 ? 0.1349 0.4407 0.2760 -0.0201 -0.0168 -0.0449 544 ILE A O     
3028 C CB    . ILE A 403 ? 0.1293 0.4129 0.2866 -0.0186 -0.0112 -0.0360 544 ILE A CB    
3029 C CG1   . ILE A 403 ? 0.0978 0.3677 0.2556 -0.0139 -0.0084 -0.0326 544 ILE A CG1   
3030 C CG2   . ILE A 403 ? 0.1545 0.4379 0.3163 -0.0269 -0.0116 -0.0452 544 ILE A CG2   
3031 C CD1   . ILE A 403 ? 0.1278 0.3915 0.2968 -0.0192 -0.0071 -0.0318 544 ILE A CD1   
3032 N N     . ASP A 404 ? 0.1288 0.4433 0.2765 -0.0191 -0.0179 -0.0359 545 ASP A N     
3033 C CA    . ASP A 404 ? 0.1494 0.4776 0.2955 -0.0240 -0.0211 -0.0392 545 ASP A CA    
3034 C C     . ASP A 404 ? 0.1329 0.4670 0.2686 -0.0187 -0.0232 -0.0385 545 ASP A C     
3035 O O     . ASP A 404 ? 0.1801 0.5206 0.3118 -0.0234 -0.0252 -0.0439 545 ASP A O     
3036 C CB    . ASP A 404 ? 0.1597 0.4981 0.3107 -0.0254 -0.0225 -0.0352 545 ASP A CB    
3037 C CG    . ASP A 404 ? 0.1653 0.5008 0.3266 -0.0331 -0.0213 -0.0367 545 ASP A CG    
3038 O OD1   . ASP A 404 ? 0.1438 0.4708 0.3087 -0.0386 -0.0201 -0.0421 545 ASP A OD1   
3039 O OD2   . ASP A 404 ? 0.1637 0.5053 0.3299 -0.0337 -0.0214 -0.0325 545 ASP A OD2   
3040 N N     . VAL A 405 ? 0.1569 0.4889 0.2881 -0.0094 -0.0229 -0.0317 546 VAL A N     
3041 C CA    . VAL A 405 ? 0.1603 0.4968 0.2821 -0.0040 -0.0250 -0.0299 546 VAL A CA    
3042 C C     . VAL A 405 ? 0.1759 0.5065 0.2926 -0.0059 -0.0241 -0.0355 546 VAL A C     
3043 O O     . VAL A 405 ? 0.1975 0.5360 0.3078 -0.0080 -0.0266 -0.0383 546 VAL A O     
3044 C CB    . VAL A 405 ? 0.2221 0.5538 0.3407 0.0063  -0.0240 -0.0223 546 VAL A CB    
3045 C CG1   . VAL A 405 ? 0.2187 0.5535 0.3281 0.0119  -0.0263 -0.0199 546 VAL A CG1   
3046 C CG2   . VAL A 405 ? 0.1693 0.5090 0.2932 0.0079  -0.0247 -0.0178 546 VAL A CG2   
3047 N N     . PHE A 406 ? 0.1383 0.4554 0.2580 -0.0058 -0.0206 -0.0375 547 PHE A N     
3048 C CA    . PHE A 406 ? 0.1503 0.4613 0.2664 -0.0073 -0.0192 -0.0433 547 PHE A CA    
3049 C C     . PHE A 406 ? 0.1501 0.4672 0.2679 -0.0173 -0.0199 -0.0528 547 PHE A C     
3050 O O     . PHE A 406 ? 0.1669 0.4877 0.2781 -0.0194 -0.0206 -0.0577 547 PHE A O     
3051 C CB    . PHE A 406 ? 0.1048 0.4001 0.2254 -0.0049 -0.0152 -0.0428 547 PHE A CB    
3052 C CG    . PHE A 406 ? 0.1733 0.4617 0.2954 -0.0090 -0.0129 -0.0507 547 PHE A CG    
3053 C CD1   . PHE A 406 ? 0.1984 0.4845 0.3131 -0.0057 -0.0121 -0.0523 547 PHE A CD1   
3054 C CD2   . PHE A 406 ? 0.1392 0.4231 0.2710 -0.0161 -0.0113 -0.0567 547 PHE A CD2   
3055 C CE1   . PHE A 406 ? 0.1780 0.4579 0.2948 -0.0095 -0.0094 -0.0603 547 PHE A CE1   
3056 C CE2   . PHE A 406 ? 0.1614 0.4379 0.2958 -0.0195 -0.0087 -0.0647 547 PHE A CE2   
3057 C CZ    . PHE A 406 ? 0.1637 0.4385 0.2907 -0.0162 -0.0075 -0.0668 547 PHE A CZ    
3058 N N     . ILE A 407 ? 0.1550 0.4732 0.2813 -0.0241 -0.0198 -0.0558 548 ILE A N     
3059 C CA    . ILE A 407 ? 0.1553 0.4779 0.2834 -0.0341 -0.0203 -0.0654 548 ILE A CA    
3060 C C     . ILE A 407 ? 0.2415 0.5791 0.3610 -0.0364 -0.0241 -0.0662 548 ILE A C     
3061 O O     . ILE A 407 ? 0.2309 0.5716 0.3449 -0.0418 -0.0243 -0.0738 548 ILE A O     
3062 C CB    . ILE A 407 ? 0.2039 0.5245 0.3430 -0.0408 -0.0198 -0.0672 548 ILE A CB    
3063 C CG1   . ILE A 407 ? 0.1371 0.4426 0.2848 -0.0392 -0.0163 -0.0661 548 ILE A CG1   
3064 C CG2   . ILE A 407 ? 0.2311 0.5555 0.3711 -0.0513 -0.0203 -0.0776 548 ILE A CG2   
3065 C CD1   . ILE A 407 ? 0.1533 0.4482 0.3035 -0.0424 -0.0133 -0.0748 548 ILE A CD1   
3066 N N     . ASP A 408 ? 0.2082 0.5554 0.3265 -0.0326 -0.0271 -0.0584 549 ASP A N     
3067 C CA    . ASP A 408 ? 0.2600 0.6217 0.3705 -0.0341 -0.0312 -0.0576 549 ASP A CA    
3068 C C     . ASP A 408 ? 0.2660 0.6284 0.3657 -0.0302 -0.0319 -0.0571 549 ASP A C     
3069 O O     . ASP A 408 ? 0.2623 0.6332 0.3545 -0.0354 -0.0340 -0.0612 549 ASP A O     
3070 C CB    . ASP A 408 ? 0.2094 0.5802 0.3217 -0.0289 -0.0339 -0.0486 549 ASP A CB    
3071 C CG    . ASP A 408 ? 0.3533 0.7285 0.4748 -0.0349 -0.0342 -0.0496 549 ASP A CG    
3072 O OD1   . ASP A 408 ? 0.4397 0.8135 0.5645 -0.0442 -0.0334 -0.0577 549 ASP A OD1   
3073 O OD2   . ASP A 408 ? 0.3828 0.7628 0.5082 -0.0305 -0.0351 -0.0428 549 ASP A OD2   
3074 N N     . ALA A 409 ? 0.1961 0.5494 0.2942 -0.0215 -0.0301 -0.0520 550 ALA A N     
3075 C CA    . ALA A 409 ? 0.2143 0.5677 0.3023 -0.0177 -0.0309 -0.0508 550 ALA A CA    
3076 C C     . ALA A 409 ? 0.2394 0.5900 0.3240 -0.0251 -0.0288 -0.0612 550 ALA A C     
3077 O O     . ALA A 409 ? 0.2383 0.5960 0.3130 -0.0281 -0.0306 -0.0634 550 ALA A O     
3078 C CB    . ALA A 409 ? 0.2255 0.5680 0.3133 -0.0074 -0.0289 -0.0438 550 ALA A CB    
3079 N N     . VAL A 410 ? 0.1795 0.5193 0.2724 -0.0283 -0.0246 -0.0677 551 VAL A N     
3080 C CA    . VAL A 410 ? 0.2237 0.5597 0.3151 -0.0353 -0.0218 -0.0788 551 VAL A CA    
3081 C C     . VAL A 410 ? 0.2502 0.5959 0.3376 -0.0452 -0.0235 -0.0864 551 VAL A C     
3082 O O     . VAL A 410 ? 0.2200 0.5686 0.2987 -0.0501 -0.0229 -0.0930 551 VAL A O     
3083 C CB    . VAL A 410 ? 0.2100 0.5315 0.3131 -0.0364 -0.0171 -0.0839 551 VAL A CB    
3084 C CG1   . VAL A 410 ? 0.1605 0.4775 0.2633 -0.0438 -0.0136 -0.0967 551 VAL A CG1   
3085 C CG2   . VAL A 410 ? 0.1545 0.4656 0.2597 -0.0268 -0.0151 -0.0764 551 VAL A CG2   
3086 N N     . ARG A 411 ? 0.2221 0.5728 0.3151 -0.0488 -0.0252 -0.0855 552 ARG A N     
3087 C CA    . ARG A 411 ? 0.2859 0.6458 0.3753 -0.0584 -0.0268 -0.0923 552 ARG A CA    
3088 C C     . ARG A 411 ? 0.3007 0.6735 0.3767 -0.0582 -0.0306 -0.0886 552 ARG A C     
3089 O O     . ARG A 411 ? 0.3102 0.6874 0.3782 -0.0657 -0.0303 -0.0961 552 ARG A O     
3090 C CB    . ARG A 411 ? 0.3832 0.7472 0.4813 -0.0612 -0.0286 -0.0900 552 ARG A CB    
3091 C CG    . ARG A 411 ? 0.4082 0.7663 0.5135 -0.0711 -0.0259 -0.1008 552 ARG A CG    
3092 C CD    . ARG A 411 ? 0.3592 0.7229 0.4719 -0.0749 -0.0282 -0.0983 552 ARG A CD    
3093 N NE    . ARG A 411 ? 0.3640 0.7158 0.4877 -0.0806 -0.0250 -0.1051 552 ARG A NE    
3094 C CZ    . ARG A 411 ? 0.4218 0.7680 0.5460 -0.0892 -0.0224 -0.1169 552 ARG A CZ    
3095 N NH1   . ARG A 411 ? 0.4296 0.7822 0.5432 -0.0940 -0.0226 -0.1237 552 ARG A NH1   
3096 N NH2   . ARG A 411 ? 0.3535 0.6865 0.4890 -0.0929 -0.0195 -0.1219 552 ARG A NH2   
3097 N N     . ARG A 412 ? 0.2429 0.6213 0.3164 -0.0497 -0.0341 -0.0769 553 ARG A N     
3098 C CA    . ARG A 412 ? 0.2986 0.6879 0.3601 -0.0486 -0.0381 -0.0717 553 ARG A CA    
3099 C C     . ARG A 412 ? 0.3234 0.7086 0.3742 -0.0491 -0.0364 -0.0751 553 ARG A C     
3100 O O     . ARG A 412 ? 0.2955 0.6881 0.3350 -0.0538 -0.0382 -0.0761 553 ARG A O     
3101 C CB    . ARG A 412 ? 0.2954 0.6887 0.3581 -0.0383 -0.0416 -0.0586 553 ARG A CB    
3102 C CG    . ARG A 412 ? 0.3662 0.7682 0.4365 -0.0392 -0.0441 -0.0551 553 ARG A CG    
3103 C CD    . ARG A 412 ? 0.4310 0.8380 0.5015 -0.0292 -0.0475 -0.0429 553 ARG A CD    
3104 N NE    . ARG A 412 ? 0.4373 0.8324 0.5101 -0.0193 -0.0451 -0.0377 553 ARG A NE    
3105 C CZ    . ARG A 412 ? 0.4085 0.7965 0.4908 -0.0150 -0.0425 -0.0356 553 ARG A CZ    
3106 N NH1   . ARG A 412 ? 0.4216 0.8131 0.5124 -0.0194 -0.0422 -0.0377 553 ARG A NH1   
3107 N NH2   . ARG A 412 ? 0.3935 0.7703 0.4761 -0.0063 -0.0402 -0.0310 553 ARG A NH2   
3108 N N     . ILE A 413 ? 0.2792 0.6525 0.3331 -0.0447 -0.0328 -0.0764 554 ILE A N     
3109 C CA    . ILE A 413 ? 0.3059 0.6749 0.3500 -0.0462 -0.0307 -0.0809 554 ILE A CA    
3110 C C     . ILE A 413 ? 0.3396 0.7082 0.3812 -0.0575 -0.0272 -0.0946 554 ILE A C     
3111 O O     . ILE A 413 ? 0.3733 0.7451 0.4025 -0.0622 -0.0267 -0.0977 554 ILE A O     
3112 C CB    . ILE A 413 ? 0.3252 0.6819 0.3746 -0.0392 -0.0275 -0.0798 554 ILE A CB    
3113 C CG1   . ILE A 413 ? 0.2500 0.6064 0.2990 -0.0278 -0.0305 -0.0662 554 ILE A CG1   
3114 C CG2   . ILE A 413 ? 0.2781 0.6288 0.3183 -0.0422 -0.0242 -0.0864 554 ILE A CG2   
3115 C CD1   . ILE A 413 ? 0.2262 0.5692 0.2837 -0.0204 -0.0268 -0.0641 554 ILE A CD1   
3116 N N     . ALA A 414 ? 0.3185 0.6821 0.3715 -0.0622 -0.0244 -0.1025 555 ALA A N     
3117 C CA    . ALA A 414 ? 0.3136 0.6738 0.3656 -0.0722 -0.0201 -0.1163 555 ALA A CA    
3118 C C     . ALA A 414 ? 0.4335 0.8060 0.4768 -0.0798 -0.0225 -0.1182 555 ALA A C     
3119 O O     . ALA A 414 ? 0.4495 0.8223 0.4854 -0.0872 -0.0194 -0.1274 555 ALA A O     
3120 C CB    . ALA A 414 ? 0.3178 0.6676 0.3854 -0.0745 -0.0167 -0.1233 555 ALA A CB    
3121 N N     . GLU A 415 ? 0.3899 0.7727 0.4345 -0.0782 -0.0277 -0.1098 556 GLU A N     
3122 C CA    . GLU A 415 ? 0.3899 0.7859 0.4264 -0.0849 -0.0308 -0.1099 556 GLU A CA    
3123 C C     . GLU A 415 ? 0.4706 0.8743 0.4935 -0.0816 -0.0342 -0.1012 556 GLU A C     
3124 O O     . GLU A 415 ? 0.5767 0.9928 0.5929 -0.0848 -0.0382 -0.0971 556 GLU A O     
3125 C CB    . GLU A 415 ? 0.3926 0.7968 0.4372 -0.0848 -0.0349 -0.1045 556 GLU A CB    
3126 C CG    . GLU A 415 ? 0.4510 0.8483 0.5076 -0.0905 -0.0320 -0.1133 556 GLU A CG    
3127 C CD    . GLU A 415 ? 0.6133 1.0156 0.6798 -0.0881 -0.0355 -0.1061 556 GLU A CD    
3128 O OE1   . GLU A 415 ? 0.5810 0.9925 0.6459 -0.0815 -0.0399 -0.0948 556 GLU A OE1   
3129 O OE2   . GLU A 415 ? 0.5871 0.9837 0.6636 -0.0928 -0.0335 -0.1118 556 GLU A OE2   
3130 N N     . PHE B 15  ? 0.6309 0.3710 0.5689 0.1651  0.0811  -0.0901 156 PHE B N     
3131 C CA    . PHE B 15  ? 0.6777 0.4397 0.6126 0.1607  0.0805  -0.0859 156 PHE B CA    
3132 C C     . PHE B 15  ? 0.6376 0.4228 0.5823 0.1631  0.0848  -0.0936 156 PHE B C     
3133 O O     . PHE B 15  ? 0.6398 0.4274 0.5808 0.1590  0.0898  -0.1047 156 PHE B O     
3134 C CB    . PHE B 15  ? 0.7045 0.4621 0.6219 0.1488  0.0812  -0.0866 156 PHE B CB    
3135 C CG    . PHE B 15  ? 0.6053 0.3828 0.5198 0.1445  0.0795  -0.0805 156 PHE B CG    
3136 C CD1   . PHE B 15  ? 0.5545 0.3539 0.4717 0.1422  0.0827  -0.0859 156 PHE B CD1   
3137 C CD2   . PHE B 15  ? 0.6027 0.3768 0.5121 0.1428  0.0746  -0.0695 156 PHE B CD2   
3138 C CE1   . PHE B 15  ? 0.5859 0.4029 0.5013 0.1382  0.0808  -0.0802 156 PHE B CE1   
3139 C CE2   . PHE B 15  ? 0.5781 0.3701 0.4856 0.1391  0.0729  -0.0645 156 PHE B CE2   
3140 C CZ    . PHE B 15  ? 0.5573 0.3706 0.4683 0.1369  0.0759  -0.0697 156 PHE B CZ    
3141 N N     . ASP B 16  ? 0.6639 0.4668 0.6206 0.1691  0.0826  -0.0876 157 ASP B N     
3142 C CA    . ASP B 16  ? 0.5784 0.4026 0.5474 0.1727  0.0864  -0.0940 157 ASP B CA    
3143 C C     . ASP B 16  ? 0.5593 0.4043 0.5227 0.1650  0.0877  -0.0938 157 ASP B C     
3144 O O     . ASP B 16  ? 0.5421 0.4035 0.5105 0.1658  0.0848  -0.0862 157 ASP B O     
3145 C CB    . ASP B 16  ? 0.5714 0.4035 0.5569 0.1828  0.0832  -0.0876 157 ASP B CB    
3146 C CG    . ASP B 16  ? 0.6301 0.4813 0.6297 0.1871  0.0879  -0.0951 157 ASP B CG    
3147 O OD1   . ASP B 16  ? 0.6401 0.4958 0.6365 0.1828  0.0939  -0.1061 157 ASP B OD1   
3148 O OD2   . ASP B 16  ? 0.6792 0.5414 0.6927 0.1942  0.0856  -0.0900 157 ASP B OD2   
3149 N N     . VAL B 17  ? 0.5861 0.4305 0.5391 0.1572  0.0920  -0.1025 158 VAL B N     
3150 C CA    . VAL B 17  ? 0.5991 0.4618 0.5459 0.1490  0.0932  -0.1024 158 VAL B CA    
3151 C C     . VAL B 17  ? 0.5987 0.4858 0.5579 0.1517  0.0959  -0.1046 158 VAL B C     
3152 O O     . VAL B 17  ? 0.5228 0.4268 0.4813 0.1475  0.0947  -0.0997 158 VAL B O     
3153 C CB    . VAL B 17  ? 0.5972 0.4535 0.5296 0.1397  0.0967  -0.1112 158 VAL B CB    
3154 C CG1   . VAL B 17  ? 0.5823 0.4377 0.5184 0.1419  0.1025  -0.1246 158 VAL B CG1   
3155 C CG2   . VAL B 17  ? 0.5280 0.4018 0.4531 0.1307  0.0969  -0.1095 158 VAL B CG2   
3156 N N     . ASN B 18  ? 0.5899 0.4791 0.5613 0.1587  0.0997  -0.1117 159 ASN B N     
3157 C CA    . ASN B 18  ? 0.5698 0.4817 0.5528 0.1604  0.1033  -0.1140 159 ASN B CA    
3158 C C     . ASN B 18  ? 0.5590 0.4826 0.5518 0.1651  0.0981  -0.1025 159 ASN B C     
3159 O O     . ASN B 18  ? 0.5168 0.4600 0.5121 0.1617  0.0983  -0.0994 159 ASN B O     
3160 C CB    . ASN B 18  ? 0.6265 0.5373 0.6207 0.1667  0.1091  -0.1251 159 ASN B CB    
3161 C CG    . ASN B 18  ? 0.7543 0.6754 0.7441 0.1601  0.1166  -0.1373 159 ASN B CG    
3162 O OD1   . ASN B 18  ? 0.7016 0.6224 0.6767 0.1509  0.1170  -0.1396 159 ASN B OD1   
3163 N ND2   . ASN B 18  ? 0.8337 0.7645 0.8363 0.1646  0.1229  -0.1452 159 ASN B ND2   
3164 N N     . ALA B 19  ? 0.5447 0.4567 0.5431 0.1725  0.0931  -0.0957 160 ALA B N     
3165 C CA    . ALA B 19  ? 0.5282 0.4509 0.5340 0.1761  0.0874  -0.0845 160 ALA B CA    
3166 C C     . ALA B 19  ? 0.4815 0.4113 0.4769 0.1682  0.0836  -0.0771 160 ALA B C     
3167 O O     . ALA B 19  ? 0.4705 0.4182 0.4713 0.1674  0.0813  -0.0716 160 ALA B O     
3168 C CB    . ALA B 19  ? 0.5193 0.4263 0.5298 0.1840  0.0822  -0.0781 160 ALA B CB    
3169 N N     . ILE B 20  ? 0.4809 0.3969 0.4617 0.1620  0.0829  -0.0771 161 ILE B N     
3170 C CA    . ILE B 20  ? 0.4628 0.3848 0.4346 0.1548  0.0794  -0.0704 161 ILE B CA    
3171 C C     . ILE B 20  ? 0.4741 0.4157 0.4454 0.1483  0.0827  -0.0738 161 ILE B C     
3172 O O     . ILE B 20  ? 0.4143 0.3709 0.3880 0.1458  0.0797  -0.0675 161 ILE B O     
3173 C CB    . ILE B 20  ? 0.5073 0.4094 0.4641 0.1497  0.0785  -0.0700 161 ILE B CB    
3174 C CG1   . ILE B 20  ? 0.4864 0.3730 0.4430 0.1547  0.0734  -0.0621 161 ILE B CG1   
3175 C CG2   . ILE B 20  ? 0.5118 0.4219 0.4589 0.1406  0.0774  -0.0672 161 ILE B CG2   
3176 C CD1   . ILE B 20  ? 0.6026 0.4653 0.5465 0.1513  0.0736  -0.0635 161 ILE B CD1   
3177 N N     . ARG B 21  ? 0.4454 0.3871 0.4135 0.1451  0.0888  -0.0839 162 ARG B N     
3178 C CA    . ARG B 21  ? 0.4835 0.4431 0.4502 0.1383  0.0924  -0.0874 162 ARG B CA    
3179 C C     . ARG B 21  ? 0.4078 0.3871 0.3876 0.1416  0.0923  -0.0842 162 ARG B C     
3180 O O     . ARG B 21  ? 0.4096 0.4045 0.3886 0.1360  0.0921  -0.0814 162 ARG B O     
3181 C CB    . ARG B 21  ? 0.4349 0.3915 0.3972 0.1353  0.0996  -0.0997 162 ARG B CB    
3182 C CG    . ARG B 21  ? 0.4607 0.4028 0.4075 0.1285  0.0999  -0.1036 162 ARG B CG    
3183 C CD    . ARG B 21  ? 0.4640 0.4046 0.4067 0.1255  0.1067  -0.1168 162 ARG B CD    
3184 N NE    . ARG B 21  ? 0.4026 0.3628 0.3453 0.1195  0.1116  -0.1208 162 ARG B NE    
3185 C CZ    . ARG B 21  ? 0.4617 0.4290 0.3927 0.1093  0.1121  -0.1209 162 ARG B CZ    
3186 N NH1   . ARG B 21  ? 0.4508 0.4089 0.3702 0.1043  0.1076  -0.1171 162 ARG B NH1   
3187 N NH2   . ARG B 21  ? 0.3851 0.3681 0.3156 0.1038  0.1176  -0.1243 162 ARG B NH2   
3188 N N     . ALA B 22  ? 0.4452 0.4239 0.4374 0.1505  0.0922  -0.0841 163 ALA B N     
3189 C CA    . ALA B 22  ? 0.4335 0.4313 0.4382 0.1534  0.0918  -0.0807 163 ALA B CA    
3190 C C     . ALA B 22  ? 0.3746 0.3816 0.3793 0.1510  0.0849  -0.0700 163 ALA B C     
3191 O O     . ALA B 22  ? 0.4039 0.4286 0.4158 0.1501  0.0845  -0.0674 163 ALA B O     
3192 C CB    . ALA B 22  ? 0.4148 0.4101 0.4334 0.1638  0.0921  -0.0818 163 ALA B CB    
3193 N N     . ASP B 23  ? 0.3960 0.3917 0.3927 0.1496  0.0798  -0.0642 164 ASP B N     
3194 C CA    . ASP B 23  ? 0.3727 0.3772 0.3697 0.1471  0.0738  -0.0549 164 ASP B CA    
3195 C C     . ASP B 23  ? 0.3734 0.3884 0.3639 0.1379  0.0741  -0.0541 164 ASP B C     
3196 O O     . ASP B 23  ? 0.3701 0.3962 0.3635 0.1355  0.0700  -0.0477 164 ASP B O     
3197 C CB    . ASP B 23  ? 0.3672 0.3562 0.3583 0.1489  0.0687  -0.0487 164 ASP B CB    
3198 C CG    . ASP B 23  ? 0.4191 0.3993 0.4176 0.1581  0.0667  -0.0467 164 ASP B CG    
3199 O OD1   . ASP B 23  ? 0.4379 0.4293 0.4485 0.1631  0.0664  -0.0461 164 ASP B OD1   
3200 O OD2   . ASP B 23  ? 0.3865 0.3480 0.3787 0.1601  0.0652  -0.0454 164 ASP B OD2   
3201 N N     . PHE B 24  ? 0.3792 0.3910 0.3612 0.1325  0.0788  -0.0605 165 PHE B N     
3202 C CA    . PHE B 24  ? 0.3605 0.3801 0.3352 0.1236  0.0785  -0.0591 165 PHE B CA    
3203 C C     . PHE B 24  ? 0.3949 0.4311 0.3732 0.1202  0.0829  -0.0628 165 PHE B C     
3204 O O     . PHE B 24  ? 0.3905 0.4248 0.3643 0.1181  0.0889  -0.0706 165 PHE B O     
3205 C CB    . PHE B 24  ? 0.3226 0.3279 0.2837 0.1187  0.0801  -0.0628 165 PHE B CB    
3206 C CG    . PHE B 24  ? 0.3488 0.3382 0.3047 0.1205  0.0757  -0.0582 165 PHE B CG    
3207 C CD1   . PHE B 24  ? 0.3368 0.3115 0.2947 0.1277  0.0753  -0.0588 165 PHE B CD1   
3208 C CD2   . PHE B 24  ? 0.3436 0.3327 0.2930 0.1150  0.0723  -0.0530 165 PHE B CD2   
3209 C CE1   . PHE B 24  ? 0.3604 0.3202 0.3127 0.1288  0.0715  -0.0540 165 PHE B CE1   
3210 C CE2   . PHE B 24  ? 0.3144 0.2891 0.2586 0.1162  0.0689  -0.0489 165 PHE B CE2   
3211 C CZ    . PHE B 24  ? 0.3782 0.3380 0.3232 0.1229  0.0685  -0.0492 165 PHE B CZ    
3212 N N     . PRO B 25  ? 0.3509 0.4033 0.3363 0.1188  0.0805  -0.0576 166 PRO B N     
3213 C CA    . PRO B 25  ? 0.3645 0.4324 0.3541 0.1163  0.0849  -0.0606 166 PRO B CA    
3214 C C     . PRO B 25  ? 0.3531 0.4239 0.3322 0.1078  0.0887  -0.0642 166 PRO B C     
3215 O O     . PRO B 25  ? 0.3733 0.4498 0.3518 0.1063  0.0948  -0.0701 166 PRO B O     
3216 C CB    . PRO B 25  ? 0.3105 0.3929 0.3087 0.1159  0.0800  -0.0531 166 PRO B CB    
3217 C CG    . PRO B 25  ? 0.3288 0.4040 0.3230 0.1144  0.0738  -0.0466 166 PRO B CG    
3218 C CD    . PRO B 25  ? 0.3107 0.3676 0.3006 0.1193  0.0738  -0.0489 166 PRO B CD    
3219 N N     . ILE B 26  ? 0.3237 0.3909 0.2942 0.1020  0.0855  -0.0607 167 ILE B N     
3220 C CA    . ILE B 26  ? 0.3173 0.3883 0.2774 0.0933  0.0884  -0.0629 167 ILE B CA    
3221 C C     . ILE B 26  ? 0.3701 0.4312 0.3216 0.0923  0.0948  -0.0722 167 ILE B C     
3222 O O     . ILE B 26  ? 0.3780 0.4441 0.3212 0.0856  0.0988  -0.0755 167 ILE B O     
3223 C CB    . ILE B 26  ? 0.3078 0.3756 0.2610 0.0880  0.0834  -0.0573 167 ILE B CB    
3224 C CG1   . ILE B 26  ? 0.3170 0.3965 0.2641 0.0789  0.0841  -0.0556 167 ILE B CG1   
3225 C CG2   . ILE B 26  ? 0.3245 0.3740 0.2683 0.0884  0.0837  -0.0608 167 ILE B CG2   
3226 C CD1   . ILE B 26  ? 0.2735 0.3549 0.2188 0.0745  0.0783  -0.0483 167 ILE B CD1   
3227 N N     . LEU B 27  ? 0.3071 0.3538 0.2597 0.0986  0.0958  -0.0765 168 LEU B N     
3228 C CA    . LEU B 27  ? 0.4025 0.4387 0.3475 0.0976  0.1019  -0.0863 168 LEU B CA    
3229 C C     . LEU B 27  ? 0.4241 0.4689 0.3725 0.0982  0.1092  -0.0925 168 LEU B C     
3230 O O     . LEU B 27  ? 0.3896 0.4270 0.3306 0.0961  0.1156  -0.1011 168 LEU B O     
3231 C CB    . LEU B 27  ? 0.3889 0.4074 0.3359 0.1048  0.1007  -0.0890 168 LEU B CB    
3232 C CG    . LEU B 27  ? 0.4675 0.4735 0.4083 0.1042  0.0946  -0.0835 168 LEU B CG    
3233 C CD1   . LEU B 27  ? 0.4334 0.4204 0.3746 0.1109  0.0944  -0.0867 168 LEU B CD1   
3234 C CD2   . LEU B 27  ? 0.3943 0.3987 0.3209 0.0944  0.0944  -0.0841 168 LEU B CD2   
3235 N N     . ARG B 28  ? 0.3993 0.4593 0.3583 0.1007  0.1087  -0.0884 169 ARG B N     
3236 C CA    . ARG B 28  ? 0.4796 0.5497 0.4419 0.1011  0.1156  -0.0930 169 ARG B CA    
3237 C C     . ARG B 28  ? 0.4800 0.5621 0.4329 0.0919  0.1174  -0.0914 169 ARG B C     
3238 O O     . ARG B 28  ? 0.5481 0.6386 0.5007 0.0912  0.1232  -0.0950 169 ARG B O     
3239 C CB    . ARG B 28  ? 0.4715 0.5528 0.4502 0.1083  0.1137  -0.0893 169 ARG B CB    
3240 C CG    . ARG B 28  ? 0.5424 0.6145 0.5316 0.1185  0.1147  -0.0929 169 ARG B CG    
3241 C CD    . ARG B 28  ? 0.6207 0.7041 0.6212 0.1234  0.1200  -0.0962 169 ARG B CD    
3242 N NE    . ARG B 28  ? 0.7714 0.8438 0.7774 0.1309  0.1252  -0.1040 169 ARG B NE    
3243 C CZ    . ARG B 28  ? 0.7561 0.8314 0.7644 0.1329  0.1340  -0.1114 169 ARG B CZ    
3244 N NH1   . ARG B 28  ? 0.7026 0.7917 0.7070 0.1279  0.1385  -0.1118 169 ARG B NH1   
3245 N NH2   . ARG B 28  ? 0.6996 0.7634 0.7143 0.1403  0.1382  -0.1184 169 ARG B NH2   
3246 N N     . GLU B 29  ? 0.4052 0.4887 0.3508 0.0851  0.1121  -0.0856 170 GLU B N     
3247 C CA    . GLU B 29  ? 0.4431 0.5390 0.3808 0.0762  0.1122  -0.0825 170 GLU B CA    
3248 C C     . GLU B 29  ? 0.4778 0.5681 0.4004 0.0712  0.1183  -0.0895 170 GLU B C     
3249 O O     . GLU B 29  ? 0.4529 0.5270 0.3690 0.0736  0.1218  -0.0962 170 GLU B O     
3250 C CB    . GLU B 29  ? 0.4621 0.5596 0.3967 0.0708  0.1048  -0.0746 170 GLU B CB    
3251 C CG    . GLU B 29  ? 0.5222 0.6372 0.4569 0.0637  0.1022  -0.0681 170 GLU B CG    
3252 C CD    . GLU B 29  ? 0.4553 0.5827 0.4047 0.0673  0.0988  -0.0622 170 GLU B CD    
3253 O OE1   . GLU B 29  ? 0.4510 0.5735 0.4100 0.0753  0.0974  -0.0621 170 GLU B OE1   
3254 O OE2   . GLU B 29  ? 0.4800 0.6221 0.4309 0.0617  0.0972  -0.0574 170 GLU B OE2   
3255 N N     . THR B 30  ? 0.4921 0.5959 0.4088 0.0641  0.1190  -0.0877 171 THR B N     
3256 C CA    . THR B 30  ? 0.5170 0.6187 0.4189 0.0588  0.1235  -0.0933 171 THR B CA    
3257 C C     . THR B 30  ? 0.5205 0.6307 0.4127 0.0477  0.1186  -0.0877 171 THR B C     
3258 O O     . THR B 30  ? 0.4719 0.5952 0.3704 0.0438  0.1137  -0.0798 171 THR B O     
3259 C CB    . THR B 30  ? 0.5379 0.6502 0.4423 0.0606  0.1301  -0.0982 171 THR B CB    
3260 O OG1   . THR B 30  ? 0.5140 0.6456 0.4280 0.0580  0.1276  -0.0917 171 THR B OG1   
3261 C CG2   . THR B 30  ? 0.5468 0.6495 0.4596 0.0715  0.1359  -0.1048 171 THR B CG2   
3262 N N     . VAL B 31  ? 0.5334 0.6364 0.4108 0.0424  0.1195  -0.0919 172 VAL B N     
3263 C CA    . VAL B 31  ? 0.5978 0.7090 0.4657 0.0309  0.1148  -0.0874 172 VAL B CA    
3264 C C     . VAL B 31  ? 0.6399 0.7561 0.4971 0.0256  0.1193  -0.0937 172 VAL B C     
3265 O O     . VAL B 31  ? 0.6676 0.7718 0.5171 0.0286  0.1235  -0.1024 172 VAL B O     
3266 C CB    . VAL B 31  ? 0.5560 0.6545 0.4162 0.0278  0.1099  -0.0857 172 VAL B CB    
3267 C CG1   . VAL B 31  ? 0.5629 0.6719 0.4159 0.0155  0.1043  -0.0796 172 VAL B CG1   
3268 C CG2   . VAL B 31  ? 0.4358 0.5274 0.3063 0.0343  0.1065  -0.0813 172 VAL B CG2   
3269 N N     . ASN B 32  ? 0.7145 0.8485 0.5713 0.0175  0.1181  -0.0896 173 ASN B N     
3270 C CA    . ASN B 32  ? 0.7206 0.8622 0.5681 0.0115  0.1222  -0.0952 173 ASN B CA    
3271 C C     . ASN B 32  ? 0.7449 0.8826 0.5949 0.0205  0.1308  -0.1050 173 ASN B C     
3272 O O     . ASN B 32  ? 0.7867 0.9203 0.6270 0.0193  0.1352  -0.1135 173 ASN B O     
3273 C CB    . ASN B 32  ? 0.7346 0.8692 0.5674 0.0034  0.1199  -0.0980 173 ASN B CB    
3274 C CG    . ASN B 32  ? 0.8532 0.9979 0.6827 -0.0085 0.1123  -0.0884 173 ASN B CG    
3275 O OD1   . ASN B 32  ? 1.0133 1.1741 0.8428 -0.0158 0.1113  -0.0841 173 ASN B OD1   
3276 N ND2   . ASN B 32  ? 0.8062 0.9414 0.6329 -0.0105 0.1067  -0.0847 173 ASN B ND2   
3277 N N     . GLY B 33  ? 0.6570 0.7960 0.5206 0.0297  0.1329  -0.1038 174 GLY B N     
3278 C CA    . GLY B 33  ? 0.6120 0.7466 0.4803 0.0393  0.1407  -0.1122 174 GLY B CA    
3279 C C     . GLY B 33  ? 0.6554 0.7684 0.5196 0.0474  0.1434  -0.1194 174 GLY B C     
3280 O O     . GLY B 33  ? 0.6836 0.7915 0.5518 0.0560  0.1499  -0.1265 174 GLY B O     
3281 N N     . LYS B 34  ? 0.6552 0.7550 0.5120 0.0449  0.1384  -0.1176 175 LYS B N     
3282 C CA    . LYS B 34  ? 0.6069 0.6852 0.4589 0.0517  0.1396  -0.1234 175 LYS B CA    
3283 C C     . LYS B 34  ? 0.5490 0.6170 0.4112 0.0584  0.1363  -0.1180 175 LYS B C     
3284 O O     . LYS B 34  ? 0.5251 0.6012 0.3933 0.0544  0.1308  -0.1095 175 LYS B O     
3285 C CB    . LYS B 34  ? 0.6196 0.6914 0.4563 0.0431  0.1360  -0.1257 175 LYS B CB    
3286 C CG    . LYS B 34  ? 0.6433 0.7256 0.4698 0.0345  0.1388  -0.1312 175 LYS B CG    
3287 C CD    . LYS B 34  ? 0.7033 0.7737 0.5161 0.0298  0.1381  -0.1383 175 LYS B CD    
3288 C CE    . LYS B 34  ? 0.7202 0.8021 0.5229 0.0198  0.1407  -0.1433 175 LYS B CE    
3289 N NZ    . LYS B 34  ? 0.7704 0.8734 0.5762 0.0118  0.1387  -0.1354 175 LYS B NZ    
3290 N N     . PRO B 35  ? 0.5303 0.5810 0.3955 0.0682  0.1396  -0.1228 176 PRO B N     
3291 C CA    . PRO B 35  ? 0.5188 0.5598 0.3945 0.0727  0.1366  -0.1182 176 PRO B CA    
3292 C C     . PRO B 35  ? 0.4970 0.5322 0.3650 0.0663  0.1295  -0.1133 176 PRO B C     
3293 O O     . PRO B 35  ? 0.5037 0.5311 0.3571 0.0627  0.1278  -0.1166 176 PRO B O     
3294 C CB    . PRO B 35  ? 0.4912 0.5127 0.3688 0.0824  0.1420  -0.1255 176 PRO B CB    
3295 C CG    . PRO B 35  ? 0.5470 0.5652 0.4092 0.0833  0.1455  -0.1338 176 PRO B CG    
3296 C CD    . PRO B 35  ? 0.5305 0.5707 0.3914 0.0755  0.1462  -0.1328 176 PRO B CD    
3297 N N     . LEU B 36  ? 0.4631 0.5050 0.3422 0.0649  0.1244  -0.1057 177 LEU B N     
3298 C CA    . LEU B 36  ? 0.4441 0.4803 0.3188 0.0602  0.1180  -0.1011 177 LEU B CA    
3299 C C     . LEU B 36  ? 0.4715 0.4854 0.3417 0.0634  0.1193  -0.1067 177 LEU B C     
3300 O O     . LEU B 36  ? 0.4707 0.4788 0.3535 0.0694  0.1218  -0.1120 177 LEU B O     
3301 C CB    . LEU B 36  ? 0.4080 0.4553 0.2975 0.0611  0.1120  -0.0928 177 LEU B CB    
3302 C CG    . LEU B 36  ? 0.3619 0.4025 0.2505 0.0593  0.1054  -0.0882 177 LEU B CG    
3303 C CD1   . LEU B 36  ? 0.3471 0.3934 0.2237 0.0495  0.1018  -0.0836 177 LEU B CD1   
3304 C CD2   . LEU B 36  ? 0.3406 0.3892 0.2449 0.0650  0.1001  -0.0808 177 LEU B CD2   
3305 N N     . ILE B 37  ? 0.4341 0.4401 0.2899 0.0591  0.1149  -0.1057 178 ILE B N     
3306 C CA    . ILE B 37  ? 0.4363 0.4241 0.2881 0.0631  0.1114  -0.1080 178 ILE B CA    
3307 C C     . ILE B 37  ? 0.4232 0.4124 0.2776 0.0528  0.1066  -0.1034 178 ILE B C     
3308 O O     . ILE B 37  ? 0.4011 0.4003 0.2430 0.0502  0.1009  -0.1002 178 ILE B O     
3309 C CB    . ILE B 37  ? 0.4895 0.4787 0.3297 0.0638  0.1097  -0.1192 178 ILE B CB    
3310 C CG1   . ILE B 37  ? 0.4611 0.4478 0.3022 0.0713  0.1163  -0.1260 178 ILE B CG1   
3311 C CG2   . ILE B 37  ? 0.4487 0.4264 0.2899 0.0623  0.1057  -0.1255 178 ILE B CG2   
3312 C CD1   . ILE B 37  ? 0.4875 0.4675 0.3168 0.0682  0.1189  -0.1374 178 ILE B CD1   
3313 N N     . TRP B 38  ? 0.4094 0.4058 0.2803 0.0579  0.1015  -0.1041 179 TRP B N     
3314 C CA    . TRP B 38  ? 0.3804 0.3755 0.2491 0.0558  0.0953  -0.0941 179 TRP B CA    
3315 C C     . TRP B 38  ? 0.4023 0.3794 0.2611 0.0542  0.0923  -0.0956 179 TRP B C     
3316 O O     . TRP B 38  ? 0.3692 0.3302 0.2315 0.0606  0.0913  -0.0949 179 TRP B O     
3317 C CB    . TRP B 38  ? 0.3328 0.3303 0.2153 0.0642  0.0920  -0.0857 179 TRP B CB    
3318 C CG    . TRP B 38  ? 0.3369 0.3361 0.2187 0.0619  0.0860  -0.0761 179 TRP B CG    
3319 C CD1   . TRP B 38  ? 0.3447 0.3307 0.2264 0.0651  0.0822  -0.0719 179 TRP B CD1   
3320 C CD2   . TRP B 38  ? 0.3095 0.3242 0.1905 0.0556  0.0834  -0.0697 179 TRP B CD2   
3321 N NE1   . TRP B 38  ? 0.3486 0.3416 0.2300 0.0614  0.0779  -0.0641 179 TRP B NE1   
3322 C CE2   . TRP B 38  ? 0.3540 0.3650 0.2358 0.0559  0.0781  -0.0625 179 TRP B CE2   
3323 C CE3   . TRP B 38  ? 0.3158 0.3467 0.1958 0.0496  0.0847  -0.0688 179 TRP B CE3   
3324 C CZ2   . TRP B 38  ? 0.2993 0.3234 0.1841 0.0497  0.0734  -0.0547 179 TRP B CZ2   
3325 C CZ3   . TRP B 38  ? 0.3123 0.3563 0.1937 0.0442  0.0800  -0.0607 179 TRP B CZ3   
3326 C CH2   . TRP B 38  ? 0.2956 0.3365 0.1798 0.0446  0.0745  -0.0541 179 TRP B CH2   
3327 N N     . PHE B 39  ? 0.3920 0.3698 0.2375 0.0449  0.0909  -0.0962 180 PHE B N     
3328 C CA    . PHE B 39  ? 0.4129 0.3726 0.2484 0.0393  0.0888  -0.0966 180 PHE B CA    
3329 C C     . PHE B 39  ? 0.3872 0.3502 0.2197 0.0320  0.0842  -0.0877 180 PHE B C     
3330 O O     . PHE B 39  ? 0.3769 0.3342 0.2000 0.0224  0.0820  -0.0878 180 PHE B O     
3331 C CB    . PHE B 39  ? 0.3791 0.3348 0.2028 0.0324  0.0905  -0.1044 180 PHE B CB    
3332 C CG    . PHE B 39  ? 0.4396 0.3841 0.2644 0.0394  0.0946  -0.1140 180 PHE B CG    
3333 C CD1   . PHE B 39  ? 0.4289 0.3662 0.2654 0.0503  0.0960  -0.1148 180 PHE B CD1   
3334 C CD2   . PHE B 39  ? 0.4341 0.3757 0.2489 0.0346  0.0970  -0.1219 180 PHE B CD2   
3335 C CE1   . PHE B 39  ? 0.4411 0.3684 0.2799 0.0567  0.0995  -0.1235 180 PHE B CE1   
3336 C CE2   . PHE B 39  ? 0.4974 0.4284 0.3135 0.0413  0.1010  -0.1312 180 PHE B CE2   
3337 C CZ    . PHE B 39  ? 0.4643 0.3884 0.2928 0.0526  0.1021  -0.1320 180 PHE B CZ    
3338 N N     . ASP B 40  ? 0.3951 0.3694 0.2376 0.0361  0.0819  -0.0797 181 ASP B N     
3339 C CA    . ASP B 40  ? 0.3568 0.3392 0.2043 0.0301  0.0748  -0.0696 181 ASP B CA    
3340 C C     . ASP B 40  ? 0.3752 0.3501 0.2322 0.0365  0.0712  -0.0633 181 ASP B C     
3341 O O     . ASP B 40  ? 0.3288 0.3141 0.1947 0.0357  0.0665  -0.0551 181 ASP B O     
3342 C CB    . ASP B 40  ? 0.3533 0.3578 0.2065 0.0273  0.0733  -0.0644 181 ASP B CB    
3343 C CG    . ASP B 40  ? 0.3901 0.4029 0.2442 0.0176  0.0667  -0.0563 181 ASP B CG    
3344 O OD1   . ASP B 40  ? 0.4230 0.4263 0.2708 0.0114  0.0642  -0.0566 181 ASP B OD1   
3345 O OD2   . ASP B 40  ? 0.3934 0.4222 0.2553 0.0163  0.0640  -0.0496 181 ASP B OD2   
3346 N N     . ASN B 41  ? 0.3997 0.3564 0.2546 0.0425  0.0732  -0.0671 182 ASN B N     
3347 C CA    . ASN B 41  ? 0.3707 0.3207 0.2339 0.0491  0.0703  -0.0613 182 ASN B CA    
3348 C C     . ASN B 41  ? 0.3838 0.3318 0.2473 0.0420  0.0646  -0.0549 182 ASN B C     
3349 O O     . ASN B 41  ? 0.3885 0.3381 0.2605 0.0456  0.0613  -0.0486 182 ASN B O     
3350 C CB    . ASN B 41  ? 0.3584 0.2888 0.2185 0.0568  0.0737  -0.0665 182 ASN B CB    
3351 C CG    . ASN B 41  ? 0.4305 0.3646 0.2943 0.0648  0.0787  -0.0724 182 ASN B CG    
3352 O OD1   . ASN B 41  ? 0.4085 0.3535 0.2843 0.0717  0.0779  -0.0686 182 ASN B OD1   
3353 N ND2   . ASN B 41  ? 0.3875 0.3158 0.2449 0.0621  0.0825  -0.0811 182 ASN B ND2   
3354 N N     . ALA B 42  ? 0.3950 0.3405 0.2499 0.0318  0.0634  -0.0565 183 ALA B N     
3355 C CA    . ALA B 42  ? 0.3945 0.3404 0.2514 0.0251  0.0580  -0.0504 183 ALA B CA    
3356 C C     . ALA B 42  ? 0.3942 0.3594 0.2610 0.0228  0.0539  -0.0430 183 ALA B C     
3357 O O     . ALA B 42  ? 0.4435 0.4109 0.3158 0.0197  0.0496  -0.0374 183 ALA B O     
3358 C CB    . ALA B 42  ? 0.3997 0.3389 0.2454 0.0146  0.0575  -0.0539 183 ALA B CB    
3359 N N     . ALA B 43  ? 0.3390 0.3181 0.2085 0.0240  0.0553  -0.0432 184 ALA B N     
3360 C CA    . ALA B 43  ? 0.3514 0.3476 0.2315 0.0229  0.0515  -0.0359 184 ALA B CA    
3361 C C     . ALA B 43  ? 0.3211 0.3205 0.2120 0.0325  0.0518  -0.0330 184 ALA B C     
3362 O O     . ALA B 43  ? 0.3055 0.3096 0.2056 0.0330  0.0480  -0.0270 184 ALA B O     
3363 C CB    . ALA B 43  ? 0.3415 0.3518 0.2187 0.0179  0.0523  -0.0365 184 ALA B CB    
3364 N N     . THR B 44  ? 0.3211 0.3185 0.2115 0.0402  0.0563  -0.0375 185 THR B N     
3365 C CA    . THR B 44  ? 0.3065 0.3054 0.2063 0.0496  0.0565  -0.0352 185 THR B CA    
3366 C C     . THR B 44  ? 0.3713 0.3630 0.2682 0.0579  0.0618  -0.0416 185 THR B C     
3367 O O     . THR B 44  ? 0.3077 0.2959 0.1962 0.0563  0.0659  -0.0482 185 THR B O     
3368 C CB    . THR B 44  ? 0.2766 0.2939 0.1872 0.0499  0.0545  -0.0299 185 THR B CB    
3369 O OG1   . THR B 44  ? 0.2803 0.2983 0.2003 0.0567  0.0528  -0.0262 185 THR B OG1   
3370 C CG2   . THR B 44  ? 0.3079 0.3358 0.2180 0.0519  0.0586  -0.0334 185 THR B CG2   
3371 N N     . THR B 45  ? 0.2876 0.2770 0.1916 0.0668  0.0617  -0.0398 186 THR B N     
3372 C CA    . THR B 45  ? 0.2955 0.2781 0.1991 0.0761  0.0662  -0.0451 186 THR B CA    
3373 C C     . THR B 45  ? 0.2710 0.2698 0.1867 0.0808  0.0664  -0.0434 186 THR B C     
3374 O O     . THR B 45  ? 0.2699 0.2821 0.1931 0.0797  0.0635  -0.0379 186 THR B O     
3375 C CB    . THR B 45  ? 0.2733 0.2395 0.1768 0.0820  0.0650  -0.0438 186 THR B CB    
3376 O OG1   . THR B 45  ? 0.2868 0.2593 0.1987 0.0833  0.0605  -0.0365 186 THR B OG1   
3377 C CG2   . THR B 45  ? 0.3388 0.2877 0.2315 0.0756  0.0645  -0.0457 186 THR B CG2   
3378 N N     . GLN B 46  ? 0.2740 0.2709 0.1927 0.0855  0.0694  -0.0481 187 GLN B N     
3379 C CA    . GLN B 46  ? 0.3105 0.3214 0.2413 0.0895  0.0695  -0.0469 187 GLN B CA    
3380 C C     . GLN B 46  ? 0.2870 0.2936 0.2261 0.0972  0.0664  -0.0429 187 GLN B C     
3381 O O     . GLN B 46  ? 0.2788 0.2701 0.2138 0.1001  0.0653  -0.0423 187 GLN B O     
3382 C CB    . GLN B 46  ? 0.2582 0.2714 0.1884 0.0900  0.0749  -0.0545 187 GLN B CB    
3383 C CG    . GLN B 46  ? 0.2881 0.3060 0.2081 0.0813  0.0779  -0.0584 187 GLN B CG    
3384 C CD    . GLN B 46  ? 0.3043 0.3397 0.2271 0.0758  0.0756  -0.0526 187 GLN B CD    
3385 O OE1   . GLN B 46  ? 0.2745 0.3194 0.2078 0.0785  0.0726  -0.0470 187 GLN B OE1   
3386 N NE2   . GLN B 46  ? 0.2954 0.3351 0.2087 0.0675  0.0767  -0.0539 187 GLN B NE2   
3387 N N     . LYS B 47  ? 0.3046 0.3253 0.2550 0.0998  0.0648  -0.0396 188 LYS B N     
3388 C CA    . LYS B 47  ? 0.3039 0.3238 0.2618 0.1055  0.0608  -0.0344 188 LYS B CA    
3389 C C     . LYS B 47  ? 0.3196 0.3398 0.2849 0.1127  0.0622  -0.0367 188 LYS B C     
3390 O O     . LYS B 47  ? 0.3083 0.3388 0.2783 0.1127  0.0653  -0.0401 188 LYS B O     
3391 C CB    . LYS B 47  ? 0.2537 0.2885 0.2191 0.1029  0.0570  -0.0285 188 LYS B CB    
3392 C CG    . LYS B 47  ? 0.2766 0.3171 0.2381 0.0954  0.0565  -0.0270 188 LYS B CG    
3393 C CD    . LYS B 47  ? 0.2565 0.2837 0.2089 0.0933  0.0556  -0.0264 188 LYS B CD    
3394 C CE    . LYS B 47  ? 0.2586 0.2922 0.2074 0.0859  0.0554  -0.0252 188 LYS B CE    
3395 N NZ    . LYS B 47  ? 0.2497 0.2707 0.1889 0.0833  0.0552  -0.0253 188 LYS B NZ    
3396 N N     . PRO B 48  ? 0.3159 0.3258 0.2825 0.1187  0.0600  -0.0344 189 PRO B N     
3397 C CA    . PRO B 48  ? 0.3024 0.3152 0.2783 0.1259  0.0603  -0.0349 189 PRO B CA    
3398 C C     . PRO B 48  ? 0.2821 0.3125 0.2681 0.1260  0.0572  -0.0303 189 PRO B C     
3399 O O     . PRO B 48  ? 0.2802 0.3167 0.2661 0.1220  0.0536  -0.0254 189 PRO B O     
3400 C CB    . PRO B 48  ? 0.3077 0.3042 0.2810 0.1314  0.0578  -0.0322 189 PRO B CB    
3401 C CG    . PRO B 48  ? 0.3463 0.3372 0.3118 0.1268  0.0548  -0.0277 189 PRO B CG    
3402 C CD    . PRO B 48  ? 0.3133 0.3090 0.2732 0.1191  0.0572  -0.0307 189 PRO B CD    
3403 N N     . GLN B 49  ? 0.2779 0.3162 0.2729 0.1306  0.0588  -0.0323 190 GLN B N     
3404 C CA    . GLN B 49  ? 0.3069 0.3616 0.3115 0.1307  0.0562  -0.0285 190 GLN B CA    
3405 C C     . GLN B 49  ? 0.3049 0.3590 0.3112 0.1323  0.0503  -0.0216 190 GLN B C     
3406 O O     . GLN B 49  ? 0.2804 0.3469 0.2912 0.1292  0.0473  -0.0179 190 GLN B O     
3407 C CB    . GLN B 49  ? 0.3214 0.3830 0.3355 0.1363  0.0591  -0.0321 190 GLN B CB    
3408 C CG    . GLN B 49  ? 0.3130 0.3930 0.3365 0.1351  0.0574  -0.0293 190 GLN B CG    
3409 C CD    . GLN B 49  ? 0.3047 0.3960 0.3266 0.1277  0.0598  -0.0308 190 GLN B CD    
3410 O OE1   . GLN B 49  ? 0.3829 0.4733 0.4011 0.1259  0.0650  -0.0364 190 GLN B OE1   
3411 N NE2   . GLN B 49  ? 0.2937 0.3954 0.3178 0.1231  0.0562  -0.0260 190 GLN B NE2   
3412 N N     . ALA B 50  ? 0.2934 0.3332 0.2958 0.1367  0.0486  -0.0199 191 ALA B N     
3413 C CA    . ALA B 50  ? 0.2666 0.3057 0.2692 0.1378  0.0434  -0.0133 191 ALA B CA    
3414 C C     . ALA B 50  ? 0.2831 0.3256 0.2808 0.1305  0.0411  -0.0104 191 ALA B C     
3415 O O     . ALA B 50  ? 0.2329 0.2837 0.2339 0.1290  0.0373  -0.0060 191 ALA B O     
3416 C CB    . ALA B 50  ? 0.2756 0.2970 0.2732 0.1433  0.0424  -0.0118 191 ALA B CB    
3417 N N     . VAL B 51  ? 0.2514 0.2882 0.2418 0.1256  0.0435  -0.0130 192 VAL B N     
3418 C CA    . VAL B 51  ? 0.2561 0.2963 0.2433 0.1189  0.0416  -0.0105 192 VAL B CA    
3419 C C     . VAL B 51  ? 0.2344 0.2919 0.2288 0.1143  0.0409  -0.0099 192 VAL B C     
3420 O O     . VAL B 51  ? 0.2009 0.2656 0.1983 0.1111  0.0375  -0.0063 192 VAL B O     
3421 C CB    . VAL B 51  ? 0.2384 0.2679 0.2162 0.1152  0.0443  -0.0134 192 VAL B CB    
3422 C CG1   . VAL B 51  ? 0.2004 0.2357 0.1770 0.1083  0.0426  -0.0111 192 VAL B CG1   
3423 C CG2   . VAL B 51  ? 0.2463 0.2573 0.2161 0.1190  0.0444  -0.0132 192 VAL B CG2   
3424 N N     . ILE B 52  ? 0.2295 0.2934 0.2266 0.1138  0.0443  -0.0137 193 ILE B N     
3425 C CA    . ILE B 52  ? 0.2405 0.3201 0.2440 0.1097  0.0441  -0.0132 193 ILE B CA    
3426 C C     . ILE B 52  ? 0.2270 0.3159 0.2386 0.1116  0.0406  -0.0097 193 ILE B C     
3427 O O     . ILE B 52  ? 0.2752 0.3732 0.2904 0.1071  0.0381  -0.0070 193 ILE B O     
3428 C CB    . ILE B 52  ? 0.2409 0.3254 0.2457 0.1100  0.0490  -0.0181 193 ILE B CB    
3429 C CG1   . ILE B 52  ? 0.2582 0.3328 0.2535 0.1078  0.0526  -0.0221 193 ILE B CG1   
3430 C CG2   . ILE B 52  ? 0.2182 0.3190 0.2291 0.1056  0.0491  -0.0172 193 ILE B CG2   
3431 C CD1   . ILE B 52  ? 0.2522 0.3309 0.2469 0.1074  0.0582  -0.0279 193 ILE B CD1   
3432 N N     . ASP B 53  ? 0.2636 0.3501 0.2783 0.1184  0.0405  -0.0099 194 ASP B N     
3433 C CA    . ASP B 53  ? 0.2456 0.3410 0.2677 0.1209  0.0372  -0.0068 194 ASP B CA    
3434 C C     . ASP B 53  ? 0.2524 0.3456 0.2720 0.1192  0.0327  -0.0023 194 ASP B C     
3435 O O     . ASP B 53  ? 0.2284 0.3319 0.2531 0.1173  0.0298  0.0002  194 ASP B O     
3436 C CB    . ASP B 53  ? 0.2433 0.3358 0.2696 0.1291  0.0381  -0.0078 194 ASP B CB    
3437 C CG    . ASP B 53  ? 0.3002 0.4000 0.3323 0.1309  0.0425  -0.0125 194 ASP B CG    
3438 O OD1   . ASP B 53  ? 0.3763 0.4854 0.4094 0.1256  0.0443  -0.0140 194 ASP B OD1   
3439 O OD2   . ASP B 53  ? 0.3536 0.4501 0.3897 0.1378  0.0441  -0.0145 194 ASP B OD2   
3440 N N     . ARG B 54  ? 0.2221 0.3021 0.2340 0.1199  0.0323  -0.0014 195 ARG B N     
3441 C CA    . ARG B 54  ? 0.1992 0.2778 0.2085 0.1181  0.0286  0.0025  195 ARG B CA    
3442 C C     . ARG B 54  ? 0.2262 0.3134 0.2372 0.1104  0.0275  0.0029  195 ARG B C     
3443 O O     . ARG B 54  ? 0.1940 0.2883 0.2081 0.1084  0.0244  0.0053  195 ARG B O     
3444 C CB    . ARG B 54  ? 0.2114 0.2744 0.2117 0.1196  0.0289  0.0031  195 ARG B CB    
3445 C CG    . ARG B 54  ? 0.2046 0.2659 0.2021 0.1195  0.0254  0.0072  195 ARG B CG    
3446 C CD    . ARG B 54  ? 0.2038 0.2706 0.2059 0.1245  0.0223  0.0105  195 ARG B CD    
3447 N NE    . ARG B 54  ? 0.2520 0.3201 0.2517 0.1238  0.0189  0.0145  195 ARG B NE    
3448 C CZ    . ARG B 54  ? 0.2569 0.3375 0.2607 0.1196  0.0166  0.0153  195 ARG B CZ    
3449 N NH1   . ARG B 54  ? 0.2085 0.2998 0.2185 0.1152  0.0174  0.0129  195 ARG B NH1   
3450 N NH2   . ARG B 54  ? 0.2247 0.3070 0.2260 0.1198  0.0136  0.0187  195 ARG B NH2   
3451 N N     . LEU B 55  ? 0.1986 0.2856 0.2081 0.1060  0.0300  0.0005  196 LEU B N     
3452 C CA    . LEU B 55  ? 0.2136 0.3084 0.2260 0.0990  0.0289  0.0012  196 LEU B CA    
3453 C C     . LEU B 55  ? 0.2368 0.3453 0.2574 0.0976  0.0276  0.0018  196 LEU B C     
3454 O O     . LEU B 55  ? 0.1918 0.3063 0.2158 0.0937  0.0250  0.0035  196 LEU B O     
3455 C CB    . LEU B 55  ? 0.2126 0.3057 0.2222 0.0952  0.0317  -0.0009 196 LEU B CB    
3456 C CG    . LEU B 55  ? 0.2600 0.3412 0.2617 0.0943  0.0330  -0.0017 196 LEU B CG    
3457 C CD1   . LEU B 55  ? 0.2222 0.3049 0.2218 0.0906  0.0359  -0.0038 196 LEU B CD1   
3458 C CD2   . LEU B 55  ? 0.2208 0.3002 0.2221 0.0912  0.0302  0.0007  196 LEU B CD2   
3459 N N     . SER B 56  ? 0.2004 0.3141 0.2245 0.1006  0.0298  0.0001  197 SER B N     
3460 C CA    . SER B 56  ? 0.2100 0.3371 0.2420 0.0995  0.0289  0.0007  197 SER B CA    
3461 C C     . SER B 56  ? 0.1789 0.3097 0.2140 0.1016  0.0253  0.0032  197 SER B C     
3462 O O     . SER B 56  ? 0.1792 0.3195 0.2192 0.0979  0.0233  0.0043  197 SER B O     
3463 C CB    . SER B 56  ? 0.1877 0.3194 0.2230 0.1035  0.0322  -0.0019 197 SER B CB    
3464 O OG    . SER B 56  ? 0.3010 0.4324 0.3336 0.1005  0.0357  -0.0043 197 SER B OG    
3465 N N     . HIS B 57  ? 0.1935 0.3175 0.2260 0.1076  0.0245  0.0041  198 HIS B N     
3466 C CA    . HIS B 57  ? 0.2129 0.3409 0.2476 0.1099  0.0209  0.0069  198 HIS B CA    
3467 C C     . HIS B 57  ? 0.1931 0.3216 0.2256 0.1047  0.0183  0.0084  198 HIS B C     
3468 O O     . HIS B 57  ? 0.1898 0.3276 0.2265 0.1029  0.0157  0.0097  198 HIS B O     
3469 C CB    . HIS B 57  ? 0.2120 0.3308 0.2435 0.1174  0.0204  0.0083  198 HIS B CB    
3470 C CG    . HIS B 57  ? 0.2547 0.3795 0.2895 0.1209  0.0166  0.0117  198 HIS B CG    
3471 N ND1   . HIS B 57  ? 0.3081 0.4314 0.3389 0.1198  0.0135  0.0146  198 HIS B ND1   
3472 C CD2   . HIS B 57  ? 0.2631 0.3962 0.3051 0.1255  0.0154  0.0127  198 HIS B CD2   
3473 C CE1   . HIS B 57  ? 0.2488 0.3794 0.2836 0.1234  0.0103  0.0175  198 HIS B CE1   
3474 N NE2   . HIS B 57  ? 0.3546 0.4909 0.3964 0.1270  0.0113  0.0165  198 HIS B NE2   
3475 N N     . PHE B 58  ? 0.2075 0.3265 0.2339 0.1022  0.0191  0.0080  199 PHE B N     
3476 C CA    . PHE B 58  ? 0.2018 0.3215 0.2271 0.0973  0.0171  0.0088  199 PHE B CA    
3477 C C     . PHE B 58  ? 0.1680 0.2978 0.1997 0.0912  0.0165  0.0079  199 PHE B C     
3478 O O     . PHE B 58  ? 0.1527 0.2892 0.1874 0.0888  0.0141  0.0085  199 PHE B O     
3479 C CB    . PHE B 58  ? 0.2049 0.3136 0.2238 0.0954  0.0185  0.0081  199 PHE B CB    
3480 C CG    . PHE B 58  ? 0.2259 0.3357 0.2448 0.0905  0.0169  0.0083  199 PHE B CG    
3481 C CD1   . PHE B 58  ? 0.1897 0.2982 0.2052 0.0927  0.0150  0.0099  199 PHE B CD1   
3482 C CD2   . PHE B 58  ? 0.1848 0.2978 0.2077 0.0841  0.0173  0.0069  199 PHE B CD2   
3483 C CE1   . PHE B 58  ? 0.2108 0.3218 0.2270 0.0883  0.0140  0.0093  199 PHE B CE1   
3484 C CE2   . PHE B 58  ? 0.1817 0.2959 0.2060 0.0798  0.0160  0.0064  199 PHE B CE2   
3485 C CZ    . PHE B 58  ? 0.1666 0.2801 0.1876 0.0818  0.0146  0.0072  199 PHE B CZ    
3486 N N     . TYR B 59  ? 0.1690 0.3001 0.2028 0.0885  0.0188  0.0065  200 TYR B N     
3487 C CA    . TYR B 59  ? 0.1962 0.3357 0.2360 0.0826  0.0183  0.0061  200 TYR B CA    
3488 C C     . TYR B 59  ? 0.1813 0.3325 0.2275 0.0832  0.0169  0.0066  200 TYR B C     
3489 O O     . TYR B 59  ? 0.1594 0.3175 0.2104 0.0786  0.0153  0.0067  200 TYR B O     
3490 C CB    . TYR B 59  ? 0.1543 0.2936 0.1945 0.0799  0.0210  0.0052  200 TYR B CB    
3491 C CG    . TYR B 59  ? 0.1265 0.2571 0.1626 0.0769  0.0216  0.0050  200 TYR B CG    
3492 C CD1   . TYR B 59  ? 0.1458 0.2755 0.1838 0.0727  0.0197  0.0054  200 TYR B CD1   
3493 C CD2   . TYR B 59  ? 0.1400 0.2641 0.1709 0.0784  0.0241  0.0042  200 TYR B CD2   
3494 C CE1   . TYR B 59  ? 0.1588 0.2816 0.1944 0.0701  0.0202  0.0052  200 TYR B CE1   
3495 C CE2   . TYR B 59  ? 0.1630 0.2804 0.1906 0.0757  0.0245  0.0042  200 TYR B CE2   
3496 C CZ    . TYR B 59  ? 0.1623 0.2793 0.1927 0.0716  0.0225  0.0049  200 TYR B CZ    
3497 O OH    . TYR B 59  ? 0.1406 0.2519 0.1691 0.0691  0.0229  0.0049  200 TYR B OH    
3498 N N     . ALA B 60  ? 0.1501 0.3038 0.1969 0.0890  0.0173  0.0069  201 ALA B N     
3499 C CA    . ALA B 60  ? 0.1763 0.3423 0.2299 0.0898  0.0161  0.0074  201 ALA B CA    
3500 C C     . ALA B 60  ? 0.1858 0.3557 0.2400 0.0918  0.0126  0.0092  201 ALA B C     
3501 O O     . ALA B 60  ? 0.2133 0.3945 0.2734 0.0909  0.0109  0.0096  201 ALA B O     
3502 C CB    . ALA B 60  ? 0.1915 0.3605 0.2475 0.0951  0.0183  0.0067  201 ALA B CB    
3503 N N     . HIS B 61  ? 0.1733 0.3349 0.2215 0.0944  0.0114  0.0103  202 HIS B N     
3504 C CA    . HIS B 61  ? 0.1997 0.3658 0.2478 0.0974  0.0081  0.0125  202 HIS B CA    
3505 C C     . HIS B 61  ? 0.2047 0.3665 0.2475 0.0955  0.0064  0.0131  202 HIS B C     
3506 O O     . HIS B 61  ? 0.2164 0.3854 0.2598 0.0960  0.0033  0.0147  202 HIS B O     
3507 C CB    . HIS B 61  ? 0.2058 0.3685 0.2529 0.1056  0.0079  0.0144  202 HIS B CB    
3508 C CG    . HIS B 61  ? 0.2724 0.4412 0.3259 0.1085  0.0095  0.0136  202 HIS B CG    
3509 N ND1   . HIS B 61  ? 0.2855 0.4679 0.3465 0.1086  0.0078  0.0142  202 HIS B ND1   
3510 C CD2   . HIS B 61  ? 0.2667 0.4307 0.3206 0.1114  0.0129  0.0117  202 HIS B CD2   
3511 C CE1   . HIS B 61  ? 0.2928 0.4787 0.3589 0.1116  0.0102  0.0129  202 HIS B CE1   
3512 N NE2   . HIS B 61  ? 0.2928 0.4679 0.3547 0.1133  0.0134  0.0112  202 HIS B NE2   
3513 N N     . GLU B 62  ? 0.1680 0.3195 0.2058 0.0933  0.0081  0.0120  203 GLU B N     
3514 C CA    . GLU B 62  ? 0.1943 0.3417 0.2270 0.0926  0.0069  0.0125  203 GLU B CA    
3515 C C     . GLU B 62  ? 0.2177 0.3640 0.2515 0.0857  0.0078  0.0099  203 GLU B C     
3516 O O     . GLU B 62  ? 0.2296 0.3743 0.2602 0.0846  0.0071  0.0096  203 GLU B O     
3517 C CB    . GLU B 62  ? 0.1993 0.3341 0.2244 0.0977  0.0081  0.0140  203 GLU B CB    
3518 C CG    . GLU B 62  ? 0.2375 0.3711 0.2614 0.1053  0.0068  0.0172  203 GLU B CG    
3519 C CD    . GLU B 62  ? 0.2876 0.4067 0.3054 0.1099  0.0090  0.0177  203 GLU B CD    
3520 O OE1   . GLU B 62  ? 0.3576 0.4723 0.3763 0.1095  0.0120  0.0152  203 GLU B OE1   
3521 O OE2   . GLU B 62  ? 0.3438 0.4560 0.3558 0.1139  0.0077  0.0206  203 GLU B OE2   
3522 N N     . ASN B 63  ? 0.1792 0.3272 0.2180 0.0812  0.0092  0.0081  204 ASN B N     
3523 C CA    . ASN B 63  ? 0.1800 0.3234 0.2198 0.0756  0.0104  0.0062  204 ASN B CA    
3524 C C     . ASN B 63  ? 0.1638 0.3132 0.2074 0.0712  0.0087  0.0045  204 ASN B C     
3525 O O     . ASN B 63  ? 0.1550 0.3142 0.2043 0.0690  0.0073  0.0039  204 ASN B O     
3526 C CB    . ASN B 63  ? 0.1490 0.2934 0.1934 0.0725  0.0121  0.0056  204 ASN B CB    
3527 C CG    . ASN B 63  ? 0.1772 0.3183 0.2245 0.0668  0.0128  0.0043  204 ASN B CG    
3528 O OD1   . ASN B 63  ? 0.1993 0.3319 0.2426 0.0667  0.0139  0.0040  204 ASN B OD1   
3529 N ND2   . ASN B 63  ? 0.1538 0.3016 0.2085 0.0622  0.0120  0.0034  204 ASN B ND2   
3530 N N     . SER B 64  ? 0.1523 0.2962 0.1934 0.0695  0.0093  0.0032  205 SER B N     
3531 C CA    . SER B 64  ? 0.1556 0.3043 0.2000 0.0655  0.0084  0.0005  205 SER B CA    
3532 C C     . SER B 64  ? 0.1745 0.3147 0.2153 0.0646  0.0100  -0.0007 205 SER B C     
3533 O O     . SER B 64  ? 0.1824 0.3147 0.2167 0.0682  0.0111  0.0011  205 SER B O     
3534 C CB    . SER B 64  ? 0.1581 0.3173 0.2011 0.0677  0.0059  0.0008  205 SER B CB    
3535 O OG    . SER B 64  ? 0.1669 0.3316 0.2120 0.0639  0.0054  -0.0027 205 SER B OG    
3536 N N     . ASN B 65  ? 0.1611 0.3031 0.2068 0.0599  0.0104  -0.0041 206 ASN B N     
3537 C CA    . ASN B 65  ? 0.2207 0.3579 0.2628 0.0594  0.0119  -0.0059 206 ASN B CA    
3538 C C     . ASN B 65  ? 0.2151 0.3582 0.2506 0.0632  0.0111  -0.0054 206 ASN B C     
3539 O O     . ASN B 65  ? 0.2314 0.3839 0.2668 0.0653  0.0087  -0.0041 206 ASN B O     
3540 C CB    . ASN B 65  ? 0.2344 0.3726 0.2841 0.0536  0.0128  -0.0104 206 ASN B CB    
3541 C CG    . ASN B 65  ? 0.3969 0.5255 0.4466 0.0521  0.0149  -0.0110 206 ASN B CG    
3542 O OD1   . ASN B 65  ? 0.3412 0.4657 0.3839 0.0542  0.0162  -0.0105 206 ASN B OD1   
3543 N ND2   . ASN B 65  ? 0.3598 0.4855 0.4177 0.0486  0.0152  -0.0115 206 ASN B ND2   
3544 N N     . ILE B 66  ? 0.2440 0.3809 0.2733 0.0631  0.0127  -0.0059 207 ILE B N     
3545 C CA    . ILE B 66  ? 0.3008 0.4361 0.3197 0.0642  0.0112  -0.0038 207 ILE B CA    
3546 C C     . ILE B 66  ? 0.3099 0.4532 0.3288 0.0587  0.0103  -0.0076 207 ILE B C     
3547 O O     . ILE B 66  ? 0.2893 0.4393 0.3170 0.0548  0.0108  -0.0121 207 ILE B O     
3548 C CB    . ILE B 66  ? 0.3417 0.4635 0.3514 0.0645  0.0129  -0.0020 207 ILE B CB    
3549 C CG1   . ILE B 66  ? 0.3893 0.5066 0.4024 0.0590  0.0157  -0.0063 207 ILE B CG1   
3550 C CG2   . ILE B 66  ? 0.3026 0.4169 0.3101 0.0706  0.0134  0.0019  207 ILE B CG2   
3551 C CD1   . ILE B 66  ? 0.5056 0.6103 0.5117 0.0593  0.0175  -0.0045 207 ILE B CD1   
3552 N N     A HIS B 67  ? 0.3269 0.4688 0.3353 0.0580  0.0091  -0.0058 208 HIS B N     
3553 N N     B HIS B 67  ? 0.3260 0.4679 0.3345 0.0579  0.0091  -0.0058 208 HIS B N     
3554 C CA    A HIS B 67  ? 0.3591 0.5086 0.3636 0.0528  0.0080  -0.0085 208 HIS B CA    
3555 C CA    B HIS B 67  ? 0.3588 0.5086 0.3635 0.0527  0.0080  -0.0086 208 HIS B CA    
3556 C C     A HIS B 67  ? 0.3289 0.4893 0.3323 0.0554  0.0038  -0.0052 208 HIS B C     
3557 C C     B HIS B 67  ? 0.3288 0.4894 0.3323 0.0554  0.0038  -0.0052 208 HIS B C     
3558 O O     A HIS B 67  ? 0.3380 0.5093 0.3498 0.0542  0.0026  -0.0079 208 HIS B O     
3559 O O     B HIS B 67  ? 0.3378 0.5091 0.3496 0.0544  0.0025  -0.0077 208 HIS B O     
3560 C CB    A HIS B 67  ? 0.3476 0.5020 0.3604 0.0464  0.0103  -0.0164 208 HIS B CB    
3561 C CB    B HIS B 67  ? 0.3469 0.5021 0.3602 0.0464  0.0102  -0.0165 208 HIS B CB    
3562 C CG    A HIS B 67  ? 0.3662 0.5120 0.3786 0.0429  0.0141  -0.0198 208 HIS B CG    
3563 C CG    B HIS B 67  ? 0.3615 0.5246 0.3702 0.0404  0.0097  -0.0206 208 HIS B CG    
3564 N ND1   A HIS B 67  ? 0.3710 0.5064 0.3845 0.0456  0.0159  -0.0176 208 HIS B ND1   
3565 N ND1   B HIS B 67  ? 0.3778 0.5527 0.3922 0.0371  0.0083  -0.0248 208 HIS B ND1   
3566 C CD2   A HIS B 67  ? 0.3947 0.5416 0.4060 0.0369  0.0166  -0.0256 208 HIS B CD2   
3567 C CD2   B HIS B 67  ? 0.3910 0.5522 0.3896 0.0364  0.0108  -0.0215 208 HIS B CD2   
3568 C CE1   A HIS B 67  ? 0.3716 0.5024 0.3854 0.0415  0.0189  -0.0214 208 HIS B CE1   
3569 C CE1   B HIS B 67  ? 0.3794 0.5596 0.3870 0.0315  0.0084  -0.0284 208 HIS B CE1   
3570 N NE2   A HIS B 67  ? 0.4198 0.5575 0.4326 0.0364  0.0196  -0.0264 208 HIS B NE2   
3571 N NE2   B HIS B 67  ? 0.3635 0.5358 0.3614 0.0310  0.0100  -0.0264 208 HIS B NE2   
3572 N N     . ARG B 68  ? 0.3331 0.4908 0.3265 0.0587  0.0012  0.0009  209 ARG B N     
3573 C CA    . ARG B 68  ? 0.3196 0.4868 0.3130 0.0631  -0.0033 0.0058  209 ARG B CA    
3574 C C     . ARG B 68  ? 0.3558 0.5379 0.3497 0.0577  -0.0060 0.0029  209 ARG B C     
3575 O O     . ARG B 68  ? 0.3580 0.5513 0.3559 0.0606  -0.0097 0.0055  209 ARG B O     
3576 C CB    . ARG B 68  ? 0.3582 0.5173 0.3409 0.0679  -0.0057 0.0135  209 ARG B CB    
3577 C CG    . ARG B 68  ? 0.4373 0.5920 0.4078 0.0623  -0.0056 0.0141  209 ARG B CG    
3578 C CD    . ARG B 68  ? 0.4723 0.6206 0.4327 0.0669  -0.0091 0.0230  209 ARG B CD    
3579 N NE    . ARG B 68  ? 0.4556 0.5870 0.4129 0.0710  -0.0067 0.0257  209 ARG B NE    
3580 C CZ    . ARG B 68  ? 0.4558 0.5813 0.4163 0.0795  -0.0076 0.0299  209 ARG B CZ    
3581 N NH1   . ARG B 68  ? 0.4726 0.6083 0.4405 0.0853  -0.0106 0.0321  209 ARG B NH1   
3582 N NH2   . ARG B 68  ? 0.4082 0.5176 0.3646 0.0820  -0.0051 0.0315  209 ARG B NH2   
3583 N N     . ALA B 69  ? 0.3529 0.5362 0.3432 0.0498  -0.0041 -0.0028 210 ALA B N     
3584 C CA    . ALA B 69  ? 0.3707 0.5684 0.3613 0.0440  -0.0062 -0.0068 210 ALA B CA    
3585 C C     . ALA B 69  ? 0.3400 0.5467 0.3441 0.0427  -0.0059 -0.0119 210 ALA B C     
3586 O O     . ALA B 69  ? 0.3499 0.5698 0.3555 0.0389  -0.0086 -0.0143 210 ALA B O     
3587 C CB    . ALA B 69  ? 0.3476 0.5445 0.3313 0.0356  -0.0034 -0.0128 210 ALA B CB    
3588 N N     . ALA B 70  ? 0.2920 0.4920 0.3054 0.0452  -0.0029 -0.0136 211 ALA B N     
3589 C CA    . ALA B 70  ? 0.3073 0.5142 0.3334 0.0428  -0.0023 -0.0185 211 ALA B CA    
3590 C C     . ALA B 70  ? 0.2821 0.5013 0.3132 0.0463  -0.0063 -0.0146 211 ALA B C     
3591 O O     . ALA B 70  ? 0.2156 0.4472 0.2509 0.0418  -0.0083 -0.0181 211 ALA B O     
3592 C CB    . ALA B 70  ? 0.2838 0.4804 0.3178 0.0445  0.0015  -0.0198 211 ALA B CB    
3593 N N     . HIS B 71  ? 0.2543 0.4709 0.2856 0.0542  -0.0074 -0.0079 212 HIS B N     
3594 C CA    . HIS B 71  ? 0.1848 0.4137 0.2225 0.0584  -0.0108 -0.0043 212 HIS B CA    
3595 C C     . HIS B 71  ? 0.2010 0.4240 0.2362 0.0679  -0.0114 0.0030  212 HIS B C     
3596 O O     . HIS B 71  ? 0.1974 0.4064 0.2259 0.0705  -0.0092 0.0049  212 HIS B O     
3597 C CB    . HIS B 71  ? 0.1973 0.4324 0.2479 0.0558  -0.0093 -0.0083 212 HIS B CB    
3598 C CG    . HIS B 71  ? 0.1751 0.3952 0.2286 0.0554  -0.0048 -0.0099 212 HIS B CG    
3599 N ND1   . HIS B 71  ? 0.1635 0.3709 0.2144 0.0605  -0.0032 -0.0054 212 HIS B ND1   
3600 C CD2   . HIS B 71  ? 0.2303 0.4455 0.2891 0.0500  -0.0019 -0.0154 212 HIS B CD2   
3601 C CE1   . HIS B 71  ? 0.1585 0.3549 0.2123 0.0579  0.0000  -0.0076 212 HIS B CE1   
3602 N NE2   . HIS B 71  ? 0.1635 0.3638 0.2223 0.0518  0.0007  -0.0132 212 HIS B NE2   
3603 N N     . GLU B 72  ? 0.2161 0.4451 0.2551 0.0713  -0.0135 0.0064  213 GLU B N     
3604 C CA    . GLU B 72  ? 0.1979 0.4191 0.2332 0.0789  -0.0140 0.0126  213 GLU B CA    
3605 C C     . GLU B 72  ? 0.2134 0.4182 0.2480 0.0818  -0.0095 0.0125  213 GLU B C     
3606 O O     . GLU B 72  ? 0.2491 0.4440 0.2773 0.0867  -0.0090 0.0157  213 GLU B O     
3607 C CB    . GLU B 72  ? 0.2174 0.4465 0.2580 0.0800  -0.0159 0.0146  213 GLU B CB    
3608 C CG    . GLU B 72  ? 0.2346 0.4557 0.2748 0.0874  -0.0153 0.0193  213 GLU B CG    
3609 C CD    . GLU B 72  ? 0.2662 0.4824 0.2988 0.0932  -0.0179 0.0249  213 GLU B CD    
3610 O OE1   . GLU B 72  ? 0.2914 0.5139 0.3187 0.0911  -0.0214 0.0264  213 GLU B OE1   
3611 O OE2   . GLU B 72  ? 0.3084 0.5141 0.3401 0.0993  -0.0166 0.0278  213 GLU B OE2   
3612 N N     . LEU B 73  ? 0.1649 0.3662 0.2055 0.0782  -0.0065 0.0091  214 LEU B N     
3613 C CA    . LEU B 73  ? 0.1864 0.3732 0.2257 0.0797  -0.0028 0.0090  214 LEU B CA    
3614 C C     . LEU B 73  ? 0.1708 0.3488 0.2051 0.0790  -0.0010 0.0077  214 LEU B C     
3615 O O     . LEU B 73  ? 0.1853 0.3514 0.2150 0.0825  0.0010  0.0094  214 LEU B O     
3616 C CB    . LEU B 73  ? 0.1186 0.3044 0.1648 0.0749  -0.0008 0.0063  214 LEU B CB    
3617 C CG    . LEU B 73  ? 0.1956 0.3892 0.2472 0.0756  -0.0017 0.0075  214 LEU B CG    
3618 C CD1   . LEU B 73  ? 0.1250 0.3162 0.1823 0.0713  0.0007  0.0056  214 LEU B CD1   
3619 C CD2   . LEU B 73  ? 0.2004 0.3909 0.2490 0.0829  -0.0018 0.0112  214 LEU B CD2   
3620 N N     . ALA B 74  ? 0.1418 0.3261 0.1776 0.0744  -0.0012 0.0041  215 ALA B N     
3621 C CA    . ALA B 74  ? 0.1655 0.3430 0.1971 0.0738  0.0009  0.0026  215 ALA B CA    
3622 C C     . ALA B 74  ? 0.2081 0.3775 0.2282 0.0777  -0.0005 0.0072  215 ALA B C     
3623 O O     . ALA B 74  ? 0.1992 0.3550 0.2133 0.0783  0.0018  0.0079  215 ALA B O     
3624 C CB    . ALA B 74  ? 0.2062 0.3873 0.2387 0.0655  0.0012  -0.0030 215 ALA B CB    
3625 N N     . ALA B 75  ? 0.1941 0.3717 0.2115 0.0802  -0.0045 0.0109  216 ALA B N     
3626 C CA    . ALA B 75  ? 0.2145 0.3842 0.2213 0.0841  -0.0065 0.0165  216 ALA B CA    
3627 C C     . ALA B 75  ? 0.2143 0.3745 0.2212 0.0927  -0.0055 0.0206  216 ALA B C     
3628 O O     . ALA B 75  ? 0.2354 0.3815 0.2338 0.0944  -0.0046 0.0232  216 ALA B O     
3629 C CB    . ALA B 75  ? 0.2134 0.3954 0.2180 0.0845  -0.0117 0.0202  216 ALA B CB    
3630 N N     . ARG B 76  ? 0.1909 0.3559 0.2059 0.0959  -0.0050 0.0203  217 ARG B N     
3631 C CA    . ARG B 76  ? 0.2206 0.3728 0.2344 0.1005  -0.0026 0.0218  217 ARG B CA    
3632 C C     . ARG B 76  ? 0.2135 0.3529 0.2245 0.0990  0.0015  0.0192  217 ARG B C     
3633 O O     . ARG B 76  ? 0.2238 0.3507 0.2289 0.1034  0.0027  0.0213  217 ARG B O     
3634 C CB    . ARG B 76  ? 0.1993 0.3566 0.2208 0.0997  -0.0019 0.0203  217 ARG B CB    
3635 C CG    . ARG B 76  ? 0.2387 0.4086 0.2638 0.1013  -0.0058 0.0229  217 ARG B CG    
3636 C CD    . ARG B 76  ? 0.2333 0.4075 0.2660 0.1012  -0.0046 0.0215  217 ARG B CD    
3637 N NE    . ARG B 76  ? 0.2468 0.4347 0.2843 0.1018  -0.0082 0.0234  217 ARG B NE    
3638 C CZ    . ARG B 76  ? 0.2754 0.4707 0.3202 0.1015  -0.0080 0.0225  217 ARG B CZ    
3639 N NH1   . ARG B 76  ? 0.1944 0.3855 0.2425 0.1004  -0.0044 0.0198  217 ARG B NH1   
3640 N NH2   . ARG B 76  ? 0.2661 0.4742 0.3151 0.1022  -0.0116 0.0246  217 ARG B NH2   
3641 N N     . ALA B 77  ? 0.1856 0.3274 0.2008 0.0926  0.0035  0.0147  218 ALA B N     
3642 C CA    . ALA B 77  ? 0.2027 0.3333 0.2159 0.0903  0.0070  0.0124  218 ALA B CA    
3643 C C     . ALA B 77  ? 0.1882 0.3108 0.1931 0.0906  0.0075  0.0134  218 ALA B C     
3644 O O     . ALA B 77  ? 0.1727 0.2821 0.1723 0.0916  0.0097  0.0138  218 ALA B O     
3645 C CB    . ALA B 77  ? 0.1512 0.2855 0.1712 0.0827  0.0083  0.0080  218 ALA B CB    
3646 N N     . THR B 78  ? 0.2045 0.3312 0.2058 0.0865  0.0053  0.0134  219 THR B N     
3647 C CA    . THR B 78  ? 0.2398 0.3557 0.2306 0.0830  0.0057  0.0143  219 THR B CA    
3648 C C     . THR B 78  ? 0.2279 0.3330 0.2103 0.0889  0.0045  0.0200  219 THR B C     
3649 O O     . THR B 78  ? 0.2466 0.3378 0.2218 0.0879  0.0064  0.0207  219 THR B O     
3650 C CB    . THR B 78  ? 0.2916 0.4159 0.2798 0.0772  0.0038  0.0130  219 THR B CB    
3651 O OG1   . THR B 78  ? 0.3001 0.4333 0.2971 0.0720  0.0052  0.0071  219 THR B OG1   
3652 C CG2   . THR B 78  ? 0.3276 0.4418 0.3049 0.0726  0.0049  0.0135  219 THR B CG2   
3653 N N     . ASP B 79  ? 0.2510 0.3621 0.2347 0.0951  0.0011  0.0243  220 ASP B N     
3654 C CA    . ASP B 79  ? 0.2915 0.3915 0.2688 0.1018  -0.0002 0.0299  220 ASP B CA    
3655 C C     . ASP B 79  ? 0.2742 0.3616 0.2518 0.1054  0.0035  0.0285  220 ASP B C     
3656 O O     . ASP B 79  ? 0.2442 0.3160 0.2133 0.1060  0.0044  0.0305  220 ASP B O     
3657 C CB    . ASP B 79  ? 0.2553 0.3655 0.2374 0.1091  -0.0043 0.0343  220 ASP B CB    
3658 C CG    . ASP B 79  ? 0.3860 0.5061 0.3644 0.1059  -0.0090 0.0376  220 ASP B CG    
3659 O OD1   . ASP B 79  ? 0.3766 0.4921 0.3461 0.0991  -0.0090 0.0376  220 ASP B OD1   
3660 O OD2   . ASP B 79  ? 0.4706 0.6038 0.4550 0.1099  -0.0127 0.0402  220 ASP B OD2   
3661 N N     . ALA B 80  ? 0.1912 0.2852 0.1780 0.1074  0.0057  0.0249  221 ALA B N     
3662 C CA    . ALA B 80  ? 0.2438 0.3274 0.2304 0.1108  0.0092  0.0233  221 ALA B CA    
3663 C C     . ALA B 80  ? 0.2087 0.2803 0.1891 0.1042  0.0121  0.0206  221 ALA B C     
3664 O O     . ALA B 80  ? 0.2238 0.2811 0.1980 0.1060  0.0139  0.0211  221 ALA B O     
3665 C CB    . ALA B 80  ? 0.1871 0.2781 0.1821 0.1083  0.0107  0.0197  221 ALA B CB    
3666 N N     . TYR B 81  ? 0.1909 0.2683 0.1733 0.0966  0.0126  0.0177  222 TYR B N     
3667 C CA    . TYR B 81  ? 0.1999 0.2682 0.1783 0.0903  0.0151  0.0151  222 TYR B CA    
3668 C C     . TYR B 81  ? 0.2447 0.3006 0.2119 0.0884  0.0146  0.0179  222 TYR B C     
3669 O O     . TYR B 81  ? 0.2123 0.2555 0.1738 0.0868  0.0167  0.0175  222 TYR B O     
3670 C CB    . TYR B 81  ? 0.2150 0.2933 0.1998 0.0835  0.0154  0.0114  222 TYR B CB    
3671 C CG    . TYR B 81  ? 0.2302 0.3035 0.2161 0.0778  0.0181  0.0082  222 TYR B CG    
3672 C CD1   . TYR B 81  ? 0.2327 0.3002 0.2193 0.0791  0.0201  0.0075  222 TYR B CD1   
3673 C CD2   . TYR B 81  ? 0.2813 0.3570 0.2683 0.0712  0.0185  0.0056  222 TYR B CD2   
3674 C CE1   . TYR B 81  ? 0.2384 0.3027 0.2267 0.0739  0.0218  0.0051  222 TYR B CE1   
3675 C CE2   . TYR B 81  ? 0.2605 0.3330 0.2504 0.0665  0.0206  0.0028  222 TYR B CE2   
3676 C CZ    . TYR B 81  ? 0.2854 0.3522 0.2759 0.0679  0.0219  0.0031  222 TYR B CZ    
3677 O OH    . TYR B 81  ? 0.2388 0.3032 0.2323 0.0633  0.0233  0.0011  222 TYR B OH    
3678 N N     . GLU B 82  ? 0.2359 0.2956 0.1993 0.0878  0.0118  0.0208  223 GLU B N     
3679 C CA    . GLU B 82  ? 0.2838 0.3320 0.2358 0.0858  0.0110  0.0245  223 GLU B CA    
3680 C C     . GLU B 82  ? 0.2740 0.3078 0.2207 0.0922  0.0109  0.0283  223 GLU B C     
3681 O O     . GLU B 82  ? 0.2816 0.3011 0.2199 0.0897  0.0122  0.0294  223 GLU B O     
3682 C CB    . GLU B 82  ? 0.2807 0.3372 0.2294 0.0842  0.0075  0.0277  223 GLU B CB    
3683 C CG    . GLU B 82  ? 0.3890 0.4584 0.3419 0.0769  0.0081  0.0229  223 GLU B CG    
3684 C CD    . GLU B 82  ? 0.4615 0.5408 0.4104 0.0745  0.0047  0.0253  223 GLU B CD    
3685 O OE1   . GLU B 82  ? 0.4384 0.5183 0.3843 0.0797  0.0009  0.0312  223 GLU B OE1   
3686 O OE2   . GLU B 82  ? 0.4994 0.5860 0.4484 0.0674  0.0058  0.0212  223 GLU B OE2   
3687 N N     . ASP B 83  ? 0.2642 0.3014 0.2160 0.1004  0.0094  0.0301  224 ASP B N     
3688 C CA    . ASP B 83  ? 0.2758 0.2991 0.2240 0.1073  0.0097  0.0328  224 ASP B CA    
3689 C C     . ASP B 83  ? 0.2936 0.3063 0.2407 0.1062  0.0140  0.0284  224 ASP B C     
3690 O O     . ASP B 83  ? 0.2708 0.2671 0.2108 0.1075  0.0150  0.0297  224 ASP B O     
3691 C CB    . ASP B 83  ? 0.3229 0.3545 0.2790 0.1166  0.0078  0.0347  224 ASP B CB    
3692 C CG    . ASP B 83  ? 0.4970 0.5315 0.4507 0.1199  0.0028  0.0414  224 ASP B CG    
3693 O OD1   . ASP B 83  ? 0.5376 0.5701 0.4833 0.1138  0.0009  0.0442  224 ASP B OD1   
3694 O OD2   . ASP B 83  ? 0.6075 0.6468 0.5673 0.1284  0.0007  0.0440  224 ASP B OD2   
3695 N N     . ALA B 84  ? 0.2147 0.2363 0.1687 0.1033  0.0163  0.0234  225 ALA B N     
3696 C CA    . ALA B 84  ? 0.2313 0.2440 0.1836 0.1011  0.0199  0.0195  225 ALA B CA    
3697 C C     . ALA B 84  ? 0.2311 0.2325 0.1748 0.0936  0.0208  0.0195  225 ALA B C     
3698 O O     . ALA B 84  ? 0.2668 0.2539 0.2041 0.0932  0.0226  0.0189  225 ALA B O     
3699 C CB    . ALA B 84  ? 0.2428 0.2682 0.2041 0.0987  0.0216  0.0153  225 ALA B CB    
3700 N N     . ARG B 85  ? 0.2275 0.2357 0.1710 0.0874  0.0197  0.0197  226 ARG B N     
3701 C CA    . ARG B 85  ? 0.2502 0.2497 0.1865 0.0799  0.0209  0.0195  226 ARG B CA    
3702 C C     . ARG B 85  ? 0.2783 0.2624 0.2038 0.0812  0.0199  0.0241  226 ARG B C     
3703 O O     . ARG B 85  ? 0.2783 0.2496 0.1969 0.0773  0.0216  0.0237  226 ARG B O     
3704 C CB    . ARG B 85  ? 0.2164 0.2273 0.1554 0.0734  0.0203  0.0183  226 ARG B CB    
3705 C CG    . ARG B 85  ? 0.2491 0.2550 0.1842 0.0652  0.0224  0.0163  226 ARG B CG    
3706 C CD    . ARG B 85  ? 0.2602 0.2770 0.1976 0.0591  0.0223  0.0147  226 ARG B CD    
3707 N NE    . ARG B 85  ? 0.1947 0.2259 0.1436 0.0597  0.0222  0.0111  226 ARG B NE    
3708 C CZ    . ARG B 85  ? 0.2305 0.2664 0.1878 0.0570  0.0238  0.0071  226 ARG B CZ    
3709 N NH1   . ARG B 85  ? 0.1987 0.2275 0.1546 0.0534  0.0257  0.0059  226 ARG B NH1   
3710 N NH2   . ARG B 85  ? 0.2233 0.2711 0.1907 0.0577  0.0233  0.0046  226 ARG B NH2   
3711 N N     . GLU B 86  ? 0.2972 0.2822 0.2213 0.0866  0.0169  0.0288  227 GLU B N     
3712 C CA    . GLU B 86  ? 0.2948 0.2644 0.2090 0.0882  0.0154  0.0343  227 GLU B CA    
3713 C C     . GLU B 86  ? 0.3173 0.2716 0.2297 0.0940  0.0169  0.0338  227 GLU B C     
3714 O O     . GLU B 86  ? 0.3225 0.2600 0.2260 0.0923  0.0173  0.0361  227 GLU B O     
3715 C CB    . GLU B 86  ? 0.3652 0.3412 0.2793 0.0925  0.0111  0.0401  227 GLU B CB    
3716 C CG    . GLU B 86  ? 0.3814 0.3420 0.2881 0.0975  0.0086  0.0469  227 GLU B CG    
3717 C CD    . GLU B 86  ? 0.4318 0.3782 0.3264 0.0900  0.0090  0.0500  227 GLU B CD    
3718 O OE1   . GLU B 86  ? 0.3855 0.3379 0.2777 0.0809  0.0105  0.0476  227 GLU B OE1   
3719 O OE2   . GLU B 86  ? 0.4320 0.3617 0.3201 0.0931  0.0077  0.0549  227 GLU B OE2   
3720 N N     . ALA B 87  ? 0.3235 0.2832 0.2440 0.1003  0.0182  0.0304  228 ALA B N     
3721 C CA    . ALA B 87  ? 0.2904 0.2364 0.2092 0.1049  0.0207  0.0281  228 ALA B CA    
3722 C C     . ALA B 87  ? 0.3306 0.2670 0.2438 0.0973  0.0238  0.0241  228 ALA B C     
3723 O O     . ALA B 87  ? 0.2894 0.2084 0.1955 0.0975  0.0251  0.0240  228 ALA B O     
3724 C CB    . ALA B 87  ? 0.2569 0.2134 0.1856 0.1120  0.0220  0.0245  228 ALA B CB    
3725 N N     . VAL B 88  ? 0.2882 0.2357 0.2049 0.0905  0.0249  0.0207  229 VAL B N     
3726 C CA    . VAL B 88  ? 0.2861 0.2262 0.1981 0.0828  0.0273  0.0174  229 VAL B CA    
3727 C C     . VAL B 88  ? 0.3020 0.2293 0.2040 0.0772  0.0267  0.0208  229 VAL B C     
3728 O O     . VAL B 88  ? 0.2975 0.2099 0.1924 0.0743  0.0283  0.0198  229 VAL B O     
3729 C CB    . VAL B 88  ? 0.2779 0.2329 0.1969 0.0770  0.0281  0.0141  229 VAL B CB    
3730 C CG1   . VAL B 88  ? 0.2571 0.2052 0.1713 0.0686  0.0298  0.0119  229 VAL B CG1   
3731 C CG2   . VAL B 88  ? 0.2535 0.2184 0.1808 0.0811  0.0292  0.0108  229 VAL B CG2   
3732 N N     . ARG B 89  ? 0.2637 0.1972 0.1647 0.0748  0.0245  0.0247  230 ARG B N     
3733 C CA    . ARG B 89  ? 0.2997 0.2228 0.1909 0.0686  0.0239  0.0284  230 ARG B CA    
3734 C C     . ARG B 89  ? 0.3389 0.2420 0.2219 0.0725  0.0233  0.0321  230 ARG B C     
3735 O O     . ARG B 89  ? 0.3285 0.2173 0.2035 0.0672  0.0246  0.0323  230 ARG B O     
3736 C CB    . ARG B 89  ? 0.2926 0.2263 0.1835 0.0666  0.0215  0.0323  230 ARG B CB    
3737 C CG    . ARG B 89  ? 0.3085 0.2333 0.1887 0.0591  0.0211  0.0364  230 ARG B CG    
3738 C CD    . ARG B 89  ? 0.3796 0.3085 0.2558 0.0602  0.0177  0.0427  230 ARG B CD    
3739 N NE    . ARG B 89  ? 0.3470 0.2678 0.2221 0.0694  0.0147  0.0479  230 ARG B NE    
3740 C CZ    . ARG B 89  ? 0.4296 0.3310 0.2976 0.0718  0.0141  0.0520  230 ARG B CZ    
3741 N NH1   . ARG B 89  ? 0.4170 0.3045 0.2775 0.0652  0.0163  0.0513  230 ARG B NH1   
3742 N NH2   . ARG B 89  ? 0.3911 0.2869 0.2603 0.0811  0.0112  0.0566  230 ARG B NH2   
3743 N N     . ARG B 90  ? 0.3490 0.2509 0.2346 0.0820  0.0213  0.0351  231 ARG B N     
3744 C CA    . ARG B 90  ? 0.3633 0.2458 0.2430 0.0872  0.0205  0.0386  231 ARG B CA    
3745 C C     . ARG B 90  ? 0.3848 0.2541 0.2626 0.0870  0.0241  0.0330  231 ARG B C     
3746 O O     . ARG B 90  ? 0.3874 0.2379 0.2566 0.0842  0.0247  0.0342  231 ARG B O     
3747 C CB    . ARG B 90  ? 0.4023 0.2889 0.2883 0.0984  0.0179  0.0418  231 ARG B CB    
3748 C CG    . ARG B 90  ? 0.3812 0.2477 0.2632 0.1055  0.0170  0.0455  231 ARG B CG    
3749 C CD    . ARG B 90  ? 0.4446 0.3183 0.3353 0.1172  0.0144  0.0482  231 ARG B CD    
3750 N NE    . ARG B 90  ? 0.4264 0.3109 0.3268 0.1222  0.0174  0.0410  231 ARG B NE    
3751 C CZ    . ARG B 90  ? 0.3923 0.2978 0.3020 0.1246  0.0166  0.0397  231 ARG B CZ    
3752 N NH1   . ARG B 90  ? 0.3152 0.2337 0.2260 0.1227  0.0129  0.0445  231 ARG B NH1   
3753 N NH2   . ARG B 90  ? 0.4121 0.3260 0.3296 0.1283  0.0198  0.0333  231 ARG B NH2   
3754 N N     . PHE B 91  ? 0.3791 0.2582 0.2643 0.0894  0.0264  0.0267  232 PHE B N     
3755 C CA    . PHE B 91  ? 0.3606 0.2283 0.2439 0.0902  0.0297  0.0211  232 PHE B CA    
3756 C C     . PHE B 91  ? 0.3601 0.2188 0.2356 0.0797  0.0315  0.0188  232 PHE B C     
3757 O O     . PHE B 91  ? 0.3842 0.2258 0.2534 0.0788  0.0333  0.0165  232 PHE B O     
3758 C CB    . PHE B 91  ? 0.3473 0.2295 0.2395 0.0937  0.0318  0.0154  232 PHE B CB    
3759 C CG    . PHE B 91  ? 0.3743 0.2462 0.2644 0.0956  0.0353  0.0093  232 PHE B CG    
3760 C CD1   . PHE B 91  ? 0.4076 0.2661 0.2968 0.1041  0.0361  0.0091  232 PHE B CD1   
3761 C CD2   . PHE B 91  ? 0.3804 0.2560 0.2695 0.0887  0.0378  0.0039  232 PHE B CD2   
3762 C CE1   . PHE B 91  ? 0.4453 0.2939 0.3322 0.1056  0.0400  0.0024  232 PHE B CE1   
3763 C CE2   . PHE B 91  ? 0.3844 0.2510 0.2705 0.0896  0.0411  -0.0021 232 PHE B CE2   
3764 C CZ    . PHE B 91  ? 0.3833 0.2361 0.2679 0.0980  0.0425  -0.0033 232 PHE B CZ    
3765 N N     . ILE B 92  ? 0.3754 0.2456 0.2517 0.0714  0.0311  0.0191  233 ILE B N     
3766 C CA    . ILE B 92  ? 0.3830 0.2466 0.2531 0.0613  0.0326  0.0169  233 ILE B CA    
3767 C C     . ILE B 92  ? 0.3920 0.2459 0.2536 0.0553  0.0313  0.0223  233 ILE B C     
3768 O O     . ILE B 92  ? 0.4285 0.2769 0.2848 0.0463  0.0325  0.0211  233 ILE B O     
3769 C CB    . ILE B 92  ? 0.3591 0.2402 0.2358 0.0553  0.0335  0.0132  233 ILE B CB    
3770 C CG1   . ILE B 92  ? 0.3559 0.2527 0.2378 0.0534  0.0317  0.0161  233 ILE B CG1   
3771 C CG2   . ILE B 92  ? 0.3619 0.2517 0.2458 0.0604  0.0347  0.0086  233 ILE B CG2   
3772 C CD1   . ILE B 92  ? 0.2996 0.2106 0.1877 0.0464  0.0325  0.0128  233 ILE B CD1   
3773 N N     . GLY B 93  ? 0.3733 0.2251 0.2333 0.0596  0.0287  0.0285  234 GLY B N     
3774 C CA    . GLY B 93  ? 0.3530 0.1949 0.2038 0.0535  0.0274  0.0342  234 GLY B CA    
3775 C C     . GLY B 93  ? 0.4040 0.2597 0.2550 0.0443  0.0276  0.0346  234 GLY B C     
3776 O O     . GLY B 93  ? 0.4396 0.2876 0.2828 0.0359  0.0281  0.0369  234 GLY B O     
3777 N N     . ALA B 94  ? 0.3498 0.2257 0.2100 0.0453  0.0275  0.0322  235 ALA B N     
3778 C CA    . ALA B 94  ? 0.3336 0.2231 0.1949 0.0376  0.0278  0.0323  235 ALA B CA    
3779 C C     . ALA B 94  ? 0.3676 0.2585 0.2239 0.0377  0.0253  0.0389  235 ALA B C     
3780 O O     . ALA B 94  ? 0.3885 0.2777 0.2450 0.0457  0.0226  0.0427  235 ALA B O     
3781 C CB    . ALA B 94  ? 0.2742 0.1837 0.1476 0.0388  0.0285  0.0272  235 ALA B CB    
3782 N N     . ALA B 95  ? 0.4011 0.2961 0.2527 0.0286  0.0261  0.0402  236 ALA B N     
3783 C CA    . ALA B 95  ? 0.3642 0.2610 0.2092 0.0272  0.0237  0.0467  236 ALA B CA    
3784 C C     . ALA B 95  ? 0.3727 0.2885 0.2252 0.0312  0.0222  0.0459  236 ALA B C     
3785 O O     . ALA B 95  ? 0.3552 0.2717 0.2038 0.0344  0.0190  0.0517  236 ALA B O     
3786 C CB    . ALA B 95  ? 0.3599 0.2572 0.1976 0.0156  0.0256  0.0479  236 ALA B CB    
3787 N N     . LYS B 96  ? 0.3635 0.2946 0.2266 0.0309  0.0241  0.0391  237 LYS B N     
3788 C CA    . LYS B 96  ? 0.3127 0.2617 0.1825 0.0330  0.0230  0.0376  237 LYS B CA    
3789 C C     . LYS B 96  ? 0.3332 0.2914 0.2156 0.0389  0.0234  0.0321  237 LYS B C     
3790 O O     . LYS B 96  ? 0.3046 0.2612 0.1918 0.0377  0.0257  0.0277  237 LYS B O     
3791 C CB    . LYS B 96  ? 0.3565 0.3182 0.2263 0.0239  0.0251  0.0348  237 LYS B CB    
3792 C CG    . LYS B 96  ? 0.3715 0.3285 0.2285 0.0173  0.0245  0.0406  237 LYS B CG    
3793 C CD    . LYS B 96  ? 0.4060 0.3773 0.2639 0.0082  0.0276  0.0364  237 LYS B CD    
3794 C CE    . LYS B 96  ? 0.4456 0.4134 0.2898 0.0009  0.0271  0.0425  237 LYS B CE    
3795 N NZ    . LYS B 96  ? 0.4449 0.4260 0.2899 -0.0086 0.0311  0.0375  237 LYS B NZ    
3796 N N     . ALA B 97  ? 0.3540 0.3225 0.2416 0.0447  0.0212  0.0328  238 ALA B N     
3797 C CA    . ALA B 97  ? 0.3415 0.3206 0.2412 0.0493  0.0216  0.0279  238 ALA B CA    
3798 C C     . ALA B 97  ? 0.3170 0.3078 0.2246 0.0432  0.0243  0.0216  238 ALA B C     
3799 O O     . ALA B 97  ? 0.3060 0.3009 0.2226 0.0451  0.0253  0.0176  238 ALA B O     
3800 C CB    . ALA B 97  ? 0.3481 0.3375 0.2516 0.0553  0.0185  0.0299  238 ALA B CB    
3801 N N     . GLU B 98  ? 0.2683 0.2645 0.1728 0.0359  0.0255  0.0208  239 GLU B N     
3802 C CA    . GLU B 98  ? 0.3005 0.3075 0.2132 0.0303  0.0283  0.0147  239 GLU B CA    
3803 C C     . GLU B 98  ? 0.2932 0.2939 0.2079 0.0270  0.0305  0.0123  239 GLU B C     
3804 O O     . GLU B 98  ? 0.3026 0.3120 0.2260 0.0233  0.0326  0.0074  239 GLU B O     
3805 C CB    . GLU B 98  ? 0.3400 0.3538 0.2479 0.0231  0.0295  0.0142  239 GLU B CB    
3806 C CG    . GLU B 98  ? 0.4236 0.4478 0.3305 0.0245  0.0275  0.0151  239 GLU B CG    
3807 C CD    . GLU B 98  ? 0.4620 0.4775 0.3579 0.0281  0.0239  0.0230  239 GLU B CD    
3808 O OE1   . GLU B 98  ? 0.4400 0.4413 0.3270 0.0271  0.0237  0.0276  239 GLU B OE1   
3809 O OE2   . GLU B 98  ? 0.6426 0.6655 0.5392 0.0318  0.0210  0.0248  239 GLU B OE2   
3810 N N     . GLU B 99  ? 0.2772 0.2629 0.1841 0.0280  0.0302  0.0155  240 GLU B N     
3811 C CA    . GLU B 99  ? 0.2680 0.2474 0.1760 0.0247  0.0320  0.0133  240 GLU B CA    
3812 C C     . GLU B 99  ? 0.2640 0.2427 0.1788 0.0304  0.0314  0.0114  240 GLU B C     
3813 O O     . GLU B 99  ? 0.2411 0.2152 0.1567 0.0279  0.0325  0.0096  240 GLU B O     
3814 C CB    . GLU B 99  ? 0.2785 0.2414 0.1738 0.0214  0.0322  0.0173  240 GLU B CB    
3815 C CG    . GLU B 99  ? 0.3218 0.2864 0.2102 0.0136  0.0333  0.0191  240 GLU B CG    
3816 C CD    . GLU B 99  ? 0.3694 0.3168 0.2444 0.0102  0.0331  0.0242  240 GLU B CD    
3817 O OE1   . GLU B 99  ? 0.3310 0.2656 0.2002 0.0160  0.0310  0.0282  240 GLU B OE1   
3818 O OE2   . GLU B 99  ? 0.3722 0.3189 0.2428 0.0016  0.0351  0.0241  240 GLU B OE2   
3819 N N     . ILE B 100 ? 0.2712 0.2552 0.1907 0.0374  0.0298  0.0118  241 ILE B N     
3820 C CA    . ILE B 100 ? 0.2446 0.2289 0.1698 0.0429  0.0294  0.0103  241 ILE B CA    
3821 C C     . ILE B 100 ? 0.2346 0.2344 0.1726 0.0429  0.0294  0.0068  241 ILE B C     
3822 O O     . ILE B 100 ? 0.2140 0.2234 0.1563 0.0447  0.0284  0.0067  241 ILE B O     
3823 C CB    . ILE B 100 ? 0.2506 0.2298 0.1725 0.0511  0.0277  0.0134  241 ILE B CB    
3824 C CG1   . ILE B 100 ? 0.2568 0.2190 0.1666 0.0515  0.0274  0.0173  241 ILE B CG1   
3825 C CG2   . ILE B 100 ? 0.1948 0.1765 0.1233 0.0562  0.0280  0.0111  241 ILE B CG2   
3826 C CD1   . ILE B 100 ? 0.2699 0.2192 0.1745 0.0479  0.0293  0.0157  241 ILE B CD1   
3827 N N     . ILE B 101 ? 0.2091 0.2113 0.1533 0.0408  0.0302  0.0042  242 ILE B N     
3828 C CA    . ILE B 101 ? 0.1881 0.2032 0.1451 0.0407  0.0300  0.0015  242 ILE B CA    
3829 C C     . ILE B 101 ? 0.2038 0.2189 0.1638 0.0453  0.0293  0.0016  242 ILE B C     
3830 O O     . ILE B 101 ? 0.2005 0.2076 0.1559 0.0448  0.0299  0.0018  242 ILE B O     
3831 C CB    . ILE B 101 ? 0.1723 0.1913 0.1351 0.0342  0.0311  -0.0009 242 ILE B CB    
3832 C CG1   . ILE B 101 ? 0.2154 0.2331 0.1733 0.0288  0.0325  -0.0013 242 ILE B CG1   
3833 C CG2   . ILE B 101 ? 0.1798 0.2118 0.1571 0.0343  0.0306  -0.0034 242 ILE B CG2   
3834 C CD1   . ILE B 101 ? 0.2852 0.3106 0.2445 0.0293  0.0326  -0.0020 242 ILE B CD1   
3835 N N     . PHE B 102 ? 0.1890 0.2133 0.1563 0.0494  0.0283  0.0014  243 PHE B N     
3836 C CA    . PHE B 102 ? 0.1816 0.2087 0.1532 0.0529  0.0280  0.0014  243 PHE B CA    
3837 C C     . PHE B 102 ? 0.1843 0.2192 0.1661 0.0492  0.0277  -0.0001 243 PHE B C     
3838 O O     . PHE B 102 ? 0.1835 0.2261 0.1734 0.0465  0.0274  -0.0015 243 PHE B O     
3839 C CB    . PHE B 102 ? 0.2021 0.2363 0.1773 0.0586  0.0270  0.0021  243 PHE B CB    
3840 C CG    . PHE B 102 ? 0.1987 0.2255 0.1654 0.0641  0.0268  0.0043  243 PHE B CG    
3841 C CD1   . PHE B 102 ? 0.2359 0.2521 0.1957 0.0666  0.0279  0.0047  243 PHE B CD1   
3842 C CD2   . PHE B 102 ? 0.2025 0.2332 0.1686 0.0668  0.0253  0.0059  243 PHE B CD2   
3843 C CE1   . PHE B 102 ? 0.2269 0.2355 0.1803 0.0724  0.0276  0.0067  243 PHE B CE1   
3844 C CE2   . PHE B 102 ? 0.2548 0.2788 0.2142 0.0725  0.0245  0.0088  243 PHE B CE2   
3845 C CZ    . PHE B 102 ? 0.2486 0.2611 0.2021 0.0756  0.0258  0.0092  243 PHE B CZ    
3846 N N     . LEU B 103 ? 0.1864 0.2194 0.1678 0.0489  0.0278  0.0002  244 LEU B N     
3847 C CA    . LEU B 103 ? 0.1936 0.2343 0.1847 0.0460  0.0269  0.0001  244 LEU B CA    
3848 C C     . LEU B 103 ? 0.2014 0.2415 0.1899 0.0478  0.0270  0.0009  244 LEU B C     
3849 O O     . LEU B 103 ? 0.1941 0.2305 0.1765 0.0525  0.0280  0.0008  244 LEU B O     
3850 C CB    . LEU B 103 ? 0.1901 0.2296 0.1831 0.0400  0.0267  -0.0005 244 LEU B CB    
3851 C CG    . LEU B 103 ? 0.2101 0.2390 0.1921 0.0378  0.0280  -0.0009 244 LEU B CG    
3852 C CD1   . LEU B 103 ? 0.2313 0.2511 0.2034 0.0382  0.0286  -0.0005 244 LEU B CD1   
3853 C CD2   . LEU B 103 ? 0.2006 0.2316 0.1869 0.0319  0.0281  -0.0018 244 LEU B CD2   
3854 N N     . ARG B 104 ? 0.2067 0.2509 0.2000 0.0443  0.0260  0.0016  245 ARG B N     
3855 C CA    . ARG B 104 ? 0.1828 0.2289 0.1741 0.0454  0.0263  0.0024  245 ARG B CA    
3856 C C     . ARG B 104 ? 0.1921 0.2281 0.1710 0.0451  0.0280  0.0011  245 ARG B C     
3857 O O     . ARG B 104 ? 0.1742 0.2092 0.1485 0.0483  0.0295  0.0003  245 ARG B O     
3858 C CB    . ARG B 104 ? 0.1753 0.2295 0.1754 0.0412  0.0242  0.0045  245 ARG B CB    
3859 C CG    . ARG B 104 ? 0.1844 0.2418 0.1814 0.0412  0.0245  0.0056  245 ARG B CG    
3860 C CD    . ARG B 104 ? 0.2242 0.2909 0.2309 0.0374  0.0219  0.0090  245 ARG B CD    
3861 N NE    . ARG B 104 ? 0.2265 0.2938 0.2398 0.0330  0.0195  0.0103  245 ARG B NE    
3862 C CZ    . ARG B 104 ? 0.3019 0.3738 0.3273 0.0327  0.0179  0.0110  245 ARG B CZ    
3863 N NH1   . ARG B 104 ? 0.2484 0.3246 0.2802 0.0360  0.0182  0.0106  245 ARG B NH1   
3864 N NH2   . ARG B 104 ? 0.2141 0.2864 0.2457 0.0292  0.0162  0.0118  245 ARG B NH2   
3865 N N     . GLY B 105 ? 0.2090 0.2378 0.1829 0.0409  0.0279  0.0005  246 GLY B N     
3866 C CA    . GLY B 105 ? 0.1974 0.2163 0.1599 0.0395  0.0294  -0.0012 246 GLY B CA    
3867 C C     . GLY B 105 ? 0.1933 0.2060 0.1521 0.0338  0.0289  -0.0015 246 GLY B C     
3868 O O     . GLY B 105 ? 0.2102 0.2266 0.1755 0.0314  0.0278  -0.0006 246 GLY B O     
3869 N N     . THR B 106 ? 0.1970 0.2003 0.1453 0.0313  0.0301  -0.0033 247 THR B N     
3870 C CA    . THR B 106 ? 0.2252 0.2223 0.1691 0.0250  0.0297  -0.0038 247 THR B CA    
3871 C C     . THR B 106 ? 0.1731 0.1809 0.1269 0.0195  0.0271  -0.0019 247 THR B C     
3872 O O     . THR B 106 ? 0.1843 0.1921 0.1408 0.0159  0.0266  -0.0016 247 THR B O     
3873 C CB    . THR B 106 ? 0.2398 0.2270 0.1717 0.0223  0.0311  -0.0064 247 THR B CB    
3874 O OG1   . THR B 106 ? 0.2327 0.2083 0.1563 0.0279  0.0337  -0.0084 247 THR B OG1   
3875 C CG2   . THR B 106 ? 0.2298 0.2117 0.1575 0.0146  0.0304  -0.0068 247 THR B CG2   
3876 N N     . THR B 107 ? 0.1863 0.2035 0.1459 0.0188  0.0253  -0.0003 248 THR B N     
3877 C CA    . THR B 107 ? 0.1473 0.1742 0.1169 0.0138  0.0223  0.0022  248 THR B CA    
3878 C C     . THR B 107 ? 0.1576 0.1911 0.1398 0.0154  0.0215  0.0032  248 THR B C     
3879 O O     . THR B 107 ? 0.1529 0.1897 0.1413 0.0115  0.0203  0.0036  248 THR B O     
3880 C CB    . THR B 107 ? 0.1734 0.2087 0.1462 0.0129  0.0203  0.0045  248 THR B CB    
3881 O OG1   . THR B 107 ? 0.2047 0.2344 0.1649 0.0105  0.0215  0.0026  248 THR B OG1   
3882 C CG2   . THR B 107 ? 0.1562 0.2015 0.1404 0.0082  0.0164  0.0081  248 THR B CG2   
3883 N N     . GLU B 108 ? 0.1378 0.1738 0.1242 0.0210  0.0223  0.0032  249 GLU B N     
3884 C CA    . GLU B 108 ? 0.1806 0.2222 0.1779 0.0223  0.0221  0.0031  249 GLU B CA    
3885 C C     . GLU B 108 ? 0.1496 0.1851 0.1422 0.0209  0.0239  0.0010  249 GLU B C     
3886 O O     . GLU B 108 ? 0.1326 0.1731 0.1335 0.0187  0.0237  0.0004  249 GLU B O     
3887 C CB    . GLU B 108 ? 0.1671 0.2124 0.1685 0.0280  0.0226  0.0031  249 GLU B CB    
3888 C CG    . GLU B 108 ? 0.1690 0.2217 0.1834 0.0282  0.0220  0.0025  249 GLU B CG    
3889 C CD    . GLU B 108 ? 0.2542 0.3114 0.2736 0.0328  0.0223  0.0021  249 GLU B CD    
3890 O OE1   . GLU B 108 ? 0.2575 0.3202 0.2870 0.0327  0.0221  0.0009  249 GLU B OE1   
3891 O OE2   . GLU B 108 ? 0.2178 0.2735 0.2315 0.0363  0.0229  0.0026  249 GLU B OE2   
3892 N N     . ALA B 109 ? 0.1710 0.1958 0.1505 0.0222  0.0259  -0.0001 250 ALA B N     
3893 C CA    . ALA B 109 ? 0.1672 0.1853 0.1408 0.0204  0.0275  -0.0013 250 ALA B CA    
3894 C C     . ALA B 109 ? 0.1710 0.1898 0.1459 0.0135  0.0270  -0.0016 250 ALA B C     
3895 O O     . ALA B 109 ? 0.1718 0.1937 0.1510 0.0109  0.0278  -0.0024 250 ALA B O     
3896 C CB    . ALA B 109 ? 0.1724 0.1774 0.1319 0.0230  0.0292  -0.0017 250 ALA B CB    
3897 N N     . ILE B 110 ? 0.1582 0.1753 0.1297 0.0100  0.0259  -0.0011 251 ILE B N     
3898 C CA    . ILE B 110 ? 0.1506 0.1698 0.1240 0.0031  0.0249  -0.0011 251 ILE B CA    
3899 C C     . ILE B 110 ? 0.1520 0.1849 0.1420 0.0020  0.0230  -0.0001 251 ILE B C     
3900 O O     . ILE B 110 ? 0.1460 0.1828 0.1413 -0.0020 0.0233  -0.0009 251 ILE B O     
3901 C CB    . ILE B 110 ? 0.1618 0.1769 0.1273 -0.0008 0.0237  -0.0009 251 ILE B CB    
3902 C CG1   . ILE B 110 ? 0.1655 0.1652 0.1149 0.0000  0.0262  -0.0029 251 ILE B CG1   
3903 C CG2   . ILE B 110 ? 0.1510 0.1711 0.1204 -0.0083 0.0220  -0.0005 251 ILE B CG2   
3904 C CD1   . ILE B 110 ? 0.2060 0.2005 0.1460 -0.0032 0.0257  -0.0041 251 ILE B CD1   
3905 N N     . ASN B 111 ? 0.1453 0.1857 0.1445 0.0056  0.0212  0.0015  252 ASN B N     
3906 C CA    . ASN B 111 ? 0.1208 0.1728 0.1370 0.0052  0.0194  0.0024  252 ASN B CA    
3907 C C     . ASN B 111 ? 0.1434 0.1979 0.1656 0.0069  0.0218  -0.0003 252 ASN B C     
3908 O O     . ASN B 111 ? 0.1151 0.1772 0.1492 0.0049  0.0215  -0.0012 252 ASN B O     
3909 C CB    . ASN B 111 ? 0.1197 0.1779 0.1440 0.0083  0.0169  0.0051  252 ASN B CB    
3910 C CG    . ASN B 111 ? 0.1596 0.2207 0.1834 0.0047  0.0136  0.0084  252 ASN B CG    
3911 O OD1   . ASN B 111 ? 0.1526 0.2213 0.1872 0.0016  0.0108  0.0106  252 ASN B OD1   
3912 N ND2   . ASN B 111 ? 0.1220 0.1773 0.1331 0.0048  0.0140  0.0087  252 ASN B ND2   
3913 N N     . LEU B 112 ? 0.1484 0.1971 0.1628 0.0106  0.0241  -0.0018 253 LEU B N     
3914 C CA    . LEU B 112 ? 0.1435 0.1943 0.1608 0.0113  0.0265  -0.0045 253 LEU B CA    
3915 C C     . LEU B 112 ? 0.1358 0.1854 0.1501 0.0058  0.0282  -0.0059 253 LEU B C     
3916 O O     . LEU B 112 ? 0.1469 0.2043 0.1714 0.0040  0.0292  -0.0081 253 LEU B O     
3917 C CB    . LEU B 112 ? 0.1500 0.1943 0.1572 0.0156  0.0280  -0.0049 253 LEU B CB    
3918 C CG    . LEU B 112 ? 0.1998 0.2486 0.2109 0.0167  0.0300  -0.0075 253 LEU B CG    
3919 C CD1   . LEU B 112 ? 0.1887 0.2359 0.1956 0.0221  0.0300  -0.0072 253 LEU B CD1   
3920 C CD2   . LEU B 112 ? 0.1764 0.2212 0.1794 0.0126  0.0324  -0.0088 253 LEU B CD2   
3921 N N     . VAL B 113 ? 0.1359 0.1756 0.1364 0.0030  0.0287  -0.0051 254 VAL B N     
3922 C CA    . VAL B 113 ? 0.1398 0.1779 0.1365 -0.0031 0.0303  -0.0061 254 VAL B CA    
3923 C C     . VAL B 113 ? 0.1514 0.1997 0.1608 -0.0075 0.0289  -0.0063 254 VAL B C     
3924 O O     . VAL B 113 ? 0.1792 0.2338 0.1947 -0.0110 0.0306  -0.0083 254 VAL B O     
3925 C CB    . VAL B 113 ? 0.1801 0.2043 0.1599 -0.0058 0.0309  -0.0051 254 VAL B CB    
3926 C CG1   . VAL B 113 ? 0.1508 0.1736 0.1268 -0.0130 0.0326  -0.0059 254 VAL B CG1   
3927 C CG2   . VAL B 113 ? 0.1666 0.1809 0.1355 -0.0007 0.0320  -0.0045 254 VAL B CG2   
3928 N N     . ALA B 114 ? 0.1413 0.1924 0.1551 -0.0074 0.0256  -0.0041 255 ALA B N     
3929 C CA    . ALA B 114 ? 0.1693 0.2304 0.1954 -0.0114 0.0234  -0.0033 255 ALA B CA    
3930 C C     . ALA B 114 ? 0.1616 0.2348 0.2066 -0.0088 0.0234  -0.0046 255 ALA B C     
3931 O O     . ALA B 114 ? 0.1787 0.2599 0.2333 -0.0121 0.0242  -0.0062 255 ALA B O     
3932 C CB    . ALA B 114 ? 0.1462 0.2078 0.1717 -0.0120 0.0194  0.0001  255 ALA B CB    
3933 N N     . HIS B 115 ? 0.1560 0.2309 0.2069 -0.0031 0.0229  -0.0044 256 HIS B N     
3934 C CA    . HIS B 115 ? 0.1906 0.2759 0.2602 -0.0007 0.0229  -0.0061 256 HIS B CA    
3935 C C     . HIS B 115 ? 0.1907 0.2781 0.2616 -0.0010 0.0273  -0.0112 256 HIS B C     
3936 O O     . HIS B 115 ? 0.1490 0.2457 0.2341 -0.0020 0.0284  -0.0139 256 HIS B O     
3937 C CB    . HIS B 115 ? 0.2044 0.2900 0.2794 0.0048  0.0211  -0.0047 256 HIS B CB    
3938 C CG    . HIS B 115 ? 0.2730 0.3603 0.3518 0.0049  0.0166  0.0004  256 HIS B CG    
3939 N ND1   . HIS B 115 ? 0.2576 0.3385 0.3226 0.0034  0.0151  0.0033  256 HIS B ND1   
3940 C CD2   . HIS B 115 ? 0.2957 0.3903 0.3904 0.0063  0.0132  0.0031  256 HIS B CD2   
3941 C CE1   . HIS B 115 ? 0.2662 0.3514 0.3375 0.0033  0.0110  0.0077  256 HIS B CE1   
3942 N NE2   . HIS B 115 ? 0.3097 0.4030 0.3992 0.0050  0.0095  0.0082  256 HIS B NE2   
3943 N N     . ALA B 116 ? 0.1512 0.2309 0.2082 0.0000  0.0299  -0.0125 257 ALA B N     
3944 C CA    . ALA B 116 ? 0.1412 0.2238 0.1988 -0.0002 0.0338  -0.0170 257 ALA B CA    
3945 C C     . ALA B 116 ? 0.1353 0.2171 0.1855 -0.0062 0.0366  -0.0183 257 ALA B C     
3946 O O     . ALA B 116 ? 0.1571 0.2480 0.2173 -0.0089 0.0390  -0.0218 257 ALA B O     
3947 C CB    . ALA B 116 ? 0.1385 0.2148 0.1858 0.0037  0.0347  -0.0172 257 ALA B CB    
3948 N N     . TRP B 117 ? 0.1465 0.2172 0.1792 -0.0085 0.0366  -0.0158 258 TRP B N     
3949 C CA    . TRP B 117 ? 0.1730 0.2415 0.1976 -0.0151 0.0390  -0.0163 258 TRP B CA    
3950 C C     . TRP B 117 ? 0.1630 0.2389 0.1974 -0.0197 0.0378  -0.0161 258 TRP B C     
3951 O O     . TRP B 117 ? 0.1553 0.2389 0.1952 -0.0243 0.0403  -0.0187 258 TRP B O     
3952 C CB    . TRP B 117 ? 0.1745 0.2279 0.1792 -0.0163 0.0387  -0.0132 258 TRP B CB    
3953 C CG    . TRP B 117 ? 0.2202 0.2702 0.2158 -0.0236 0.0412  -0.0134 258 TRP B CG    
3954 C CD1   . TRP B 117 ? 0.2309 0.2795 0.2189 -0.0260 0.0445  -0.0144 258 TRP B CD1   
3955 C CD2   . TRP B 117 ? 0.2266 0.2750 0.2197 -0.0302 0.0407  -0.0124 258 TRP B CD2   
3956 N NE1   . TRP B 117 ? 0.2245 0.2703 0.2055 -0.0338 0.0461  -0.0138 258 TRP B NE1   
3957 C CE2   . TRP B 117 ? 0.2546 0.3002 0.2389 -0.0364 0.0438  -0.0128 258 TRP B CE2   
3958 C CE3   . TRP B 117 ? 0.2189 0.2685 0.2161 -0.0320 0.0376  -0.0111 258 TRP B CE3   
3959 C CZ2   . TRP B 117 ? 0.2171 0.2607 0.1970 -0.0444 0.0442  -0.0122 258 TRP B CZ2   
3960 C CZ3   . TRP B 117 ? 0.2401 0.2881 0.2327 -0.0399 0.0378  -0.0106 258 TRP B CZ3   
3961 C CH2   . TRP B 117 ? 0.2151 0.2599 0.1993 -0.0459 0.0411  -0.0113 258 TRP B CH2   
3962 N N     . GLY B 118 ? 0.1494 0.2239 0.1859 -0.0188 0.0338  -0.0130 259 GLY B N     
3963 C CA    . GLY B 118 ? 0.1454 0.2275 0.1909 -0.0233 0.0318  -0.0121 259 GLY B CA    
3964 C C     . GLY B 118 ? 0.1623 0.2596 0.2296 -0.0220 0.0320  -0.0144 259 GLY B C     
3965 O O     . GLY B 118 ? 0.1960 0.3021 0.2717 -0.0265 0.0326  -0.0156 259 GLY B O     
3966 N N     . GLY B 119 ? 0.2047 0.3052 0.2820 -0.0157 0.0314  -0.0152 260 GLY B N     
3967 C CA    . GLY B 119 ? 0.1815 0.2949 0.2802 -0.0137 0.0318  -0.0180 260 GLY B CA    
3968 C C     . GLY B 119 ? 0.2342 0.3544 0.3362 -0.0168 0.0371  -0.0235 260 GLY B C     
3969 O O     . GLY B 119 ? 0.1752 0.3073 0.2937 -0.0180 0.0379  -0.0259 260 GLY B O     
3970 N N     . LYS B 120 ? 0.1772 0.2904 0.2637 -0.0184 0.0407  -0.0254 261 LYS B N     
3971 C CA    . LYS B 120 ? 0.1873 0.3070 0.2745 -0.0222 0.0460  -0.0305 261 LYS B CA    
3972 C C     . LYS B 120 ? 0.2226 0.3432 0.3034 -0.0300 0.0472  -0.0296 261 LYS B C     
3973 O O     . LYS B 120 ? 0.2205 0.3521 0.3100 -0.0337 0.0509  -0.0336 261 LYS B O     
3974 C CB    . LYS B 120 ? 0.2256 0.3383 0.2986 -0.0212 0.0490  -0.0322 261 LYS B CB    
3975 C CG    . LYS B 120 ? 0.2614 0.3827 0.3364 -0.0248 0.0548  -0.0381 261 LYS B CG    
3976 C CD    . LYS B 120 ? 0.3282 0.4425 0.3870 -0.0246 0.0569  -0.0386 261 LYS B CD    
3977 C CE    . LYS B 120 ? 0.4789 0.6017 0.5365 -0.0297 0.0627  -0.0441 261 LYS B CE    
3978 N NZ    . LYS B 120 ? 0.4603 0.5740 0.4960 -0.0348 0.0640  -0.0407 261 LYS B NZ    
3979 N N     . HIS B 121 ? 0.1882 0.2980 0.2546 -0.0328 0.0445  -0.0248 262 HIS B N     
3980 C CA    . HIS B 121 ? 0.2166 0.3236 0.2721 -0.0410 0.0461  -0.0239 262 HIS B CA    
3981 C C     . HIS B 121 ? 0.1975 0.3063 0.2558 -0.0451 0.0424  -0.0209 262 HIS B C     
3982 O O     . HIS B 121 ? 0.2344 0.3426 0.2860 -0.0527 0.0437  -0.0206 262 HIS B O     
3983 C CB    . HIS B 121 ? 0.2087 0.2990 0.2410 -0.0423 0.0469  -0.0215 262 HIS B CB    
3984 C CG    . HIS B 121 ? 0.2160 0.3055 0.2427 -0.0407 0.0507  -0.0240 262 HIS B CG    
3985 N ND1   . HIS B 121 ? 0.2467 0.3447 0.2750 -0.0457 0.0554  -0.0275 262 HIS B ND1   
3986 C CD2   . HIS B 121 ? 0.2472 0.3300 0.2673 -0.0350 0.0504  -0.0235 262 HIS B CD2   
3987 C CE1   . HIS B 121 ? 0.2757 0.3717 0.2974 -0.0435 0.0577  -0.0291 262 HIS B CE1   
3988 N NE2   . HIS B 121 ? 0.2759 0.3628 0.2929 -0.0369 0.0545  -0.0265 262 HIS B NE2   
3989 N N     . LEU B 122 ? 0.1651 0.2760 0.2325 -0.0412 0.0377  -0.0183 263 LEU B N     
3990 C CA    . LEU B 122 ? 0.2006 0.3141 0.2701 -0.0456 0.0337  -0.0152 263 LEU B CA    
3991 C C     . LEU B 122 ? 0.2086 0.3394 0.3023 -0.0440 0.0317  -0.0157 263 LEU B C     
3992 O O     . LEU B 122 ? 0.2896 0.4234 0.3944 -0.0379 0.0284  -0.0140 263 LEU B O     
3993 C CB    . LEU B 122 ? 0.1953 0.2972 0.2537 -0.0433 0.0294  -0.0111 263 LEU B CB    
3994 C CG    . LEU B 122 ? 0.2557 0.3405 0.2909 -0.0463 0.0309  -0.0103 263 LEU B CG    
3995 C CD1   . LEU B 122 ? 0.2924 0.3666 0.3183 -0.0419 0.0277  -0.0076 263 LEU B CD1   
3996 C CD2   . LEU B 122 ? 0.2889 0.3727 0.3173 -0.0556 0.0307  -0.0098 263 LEU B CD2   
3997 N N     . GLY B 123 ? 0.2177 0.3599 0.3201 -0.0495 0.0336  -0.0177 264 GLY B N     
3998 C CA    . GLY B 123 ? 0.1789 0.3385 0.3058 -0.0479 0.0319  -0.0184 264 GLY B CA    
3999 C C     . GLY B 123 ? 0.2108 0.3777 0.3417 -0.0541 0.0278  -0.0150 264 GLY B C     
4000 O O     . GLY B 123 ? 0.1670 0.3246 0.2811 -0.0598 0.0259  -0.0123 264 GLY B O     
4001 N N     . PRO B 124 ? 0.1634 0.3476 0.3175 -0.0533 0.0263  -0.0155 265 PRO B N     
4002 C CA    . PRO B 124 ? 0.1184 0.3122 0.2791 -0.0589 0.0216  -0.0118 265 PRO B CA    
4003 C C     . PRO B 124 ? 0.1786 0.3698 0.3241 -0.0693 0.0238  -0.0126 265 PRO B C     
4004 O O     . PRO B 124 ? 0.1598 0.3544 0.3042 -0.0730 0.0297  -0.0171 265 PRO B O     
4005 C CB    . PRO B 124 ? 0.1436 0.3567 0.3327 -0.0555 0.0217  -0.0138 265 PRO B CB    
4006 C CG    . PRO B 124 ? 0.1284 0.3377 0.3253 -0.0458 0.0236  -0.0160 265 PRO B CG    
4007 C CD    . PRO B 124 ? 0.1633 0.3588 0.3396 -0.0465 0.0286  -0.0194 265 PRO B CD    
4008 N N     . GLY B 125 ? 0.1664 0.3516 0.3000 -0.0746 0.0190  -0.0084 266 GLY B N     
4009 C CA    . GLY B 125 ? 0.1990 0.3800 0.3176 -0.0850 0.0205  -0.0089 266 GLY B CA    
4010 C C     . GLY B 125 ? 0.2420 0.4022 0.3349 -0.0872 0.0243  -0.0102 266 GLY B C     
4011 O O     . GLY B 125 ? 0.2444 0.3974 0.3226 -0.0959 0.0247  -0.0099 266 GLY B O     
4012 N N     . ASP B 126 ? 0.1923 0.3426 0.2799 -0.0797 0.0269  -0.0115 267 ASP B N     
4013 C CA    . ASP B 126 ? 0.2045 0.3348 0.2685 -0.0807 0.0296  -0.0118 267 ASP B CA    
4014 C C     . ASP B 126 ? 0.2551 0.3726 0.3053 -0.0811 0.0251  -0.0084 267 ASP B C     
4015 O O     . ASP B 126 ? 0.2309 0.3532 0.2892 -0.0773 0.0203  -0.0058 267 ASP B O     
4016 C CB    . ASP B 126 ? 0.2010 0.3259 0.2641 -0.0725 0.0331  -0.0138 267 ASP B CB    
4017 C CG    . ASP B 126 ? 0.2410 0.3775 0.3149 -0.0727 0.0385  -0.0182 267 ASP B CG    
4018 O OD1   . ASP B 126 ? 0.2248 0.3676 0.2986 -0.0807 0.0412  -0.0197 267 ASP B OD1   
4019 O OD2   . ASP B 126 ? 0.2073 0.3468 0.2894 -0.0654 0.0403  -0.0204 267 ASP B OD2   
4020 N N     . GLU B 127 ? 0.2112 0.3124 0.2406 -0.0862 0.0266  -0.0085 268 GLU B N     
4021 C CA    . GLU B 127 ? 0.2156 0.3047 0.2310 -0.0883 0.0230  -0.0066 268 GLU B CA    
4022 C C     . GLU B 127 ? 0.2358 0.3066 0.2359 -0.0821 0.0244  -0.0065 268 GLU B C     
4023 O O     . GLU B 127 ? 0.2148 0.2766 0.2070 -0.0803 0.0285  -0.0078 268 GLU B O     
4024 C CB    . GLU B 127 ? 0.2579 0.3423 0.2622 -0.0997 0.0231  -0.0070 268 GLU B CB    
4025 C CG    . GLU B 127 ? 0.3322 0.4341 0.3499 -0.1057 0.0189  -0.0058 268 GLU B CG    
4026 C CD    . GLU B 127 ? 0.3821 0.4858 0.3950 -0.1177 0.0201  -0.0069 268 GLU B CD    
4027 O OE1   . GLU B 127 ? 0.4005 0.4870 0.3947 -0.1228 0.0227  -0.0081 268 GLU B OE1   
4028 O OE2   . GLU B 127 ? 0.3889 0.5113 0.4174 -0.1220 0.0182  -0.0065 268 GLU B OE2   
4029 N N     . ILE B 128 ? 0.2113 0.2778 0.2077 -0.0789 0.0207  -0.0049 269 ILE B N     
4030 C CA    . ILE B 128 ? 0.2326 0.2824 0.2145 -0.0735 0.0214  -0.0049 269 ILE B CA    
4031 C C     . ILE B 128 ? 0.2859 0.3247 0.2526 -0.0796 0.0197  -0.0052 269 ILE B C     
4032 O O     . ILE B 128 ? 0.2577 0.3052 0.2287 -0.0842 0.0157  -0.0041 269 ILE B O     
4033 C CB    . ILE B 128 ? 0.2650 0.3201 0.2559 -0.0644 0.0192  -0.0033 269 ILE B CB    
4034 C CG1   . ILE B 128 ? 0.2758 0.3440 0.2846 -0.0591 0.0204  -0.0035 269 ILE B CG1   
4035 C CG2   . ILE B 128 ? 0.2414 0.2805 0.2179 -0.0586 0.0205  -0.0036 269 ILE B CG2   
4036 C CD1   . ILE B 128 ? 0.2539 0.3321 0.2771 -0.0525 0.0168  -0.0012 269 ILE B CD1   
4037 N N     . VAL B 129 ? 0.2504 0.2702 0.1996 -0.0798 0.0224  -0.0067 270 VAL B N     
4038 C CA    . VAL B 129 ? 0.2872 0.2940 0.2211 -0.0849 0.0215  -0.0081 270 VAL B CA    
4039 C C     . VAL B 129 ? 0.2734 0.2677 0.1980 -0.0769 0.0221  -0.0087 270 VAL B C     
4040 O O     . VAL B 129 ? 0.2567 0.2411 0.1767 -0.0708 0.0251  -0.0088 270 VAL B O     
4041 C CB    . VAL B 129 ? 0.3082 0.3021 0.2295 -0.0933 0.0241  -0.0097 270 VAL B CB    
4042 C CG1   . VAL B 129 ? 0.3057 0.2850 0.2112 -0.0986 0.0234  -0.0120 270 VAL B CG1   
4043 C CG2   . VAL B 129 ? 0.2868 0.2955 0.2186 -0.1014 0.0237  -0.0092 270 VAL B CG2   
4044 N N     . ILE B 130 ? 0.2675 0.2638 0.1901 -0.0769 0.0193  -0.0089 271 ILE B N     
4045 C CA    . ILE B 130 ? 0.2364 0.2212 0.1489 -0.0710 0.0201  -0.0103 271 ILE B CA    
4046 C C     . ILE B 130 ? 0.3321 0.3059 0.2298 -0.0783 0.0199  -0.0136 271 ILE B C     
4047 O O     . ILE B 130 ? 0.3323 0.3096 0.2291 -0.0878 0.0183  -0.0141 271 ILE B O     
4048 C CB    . ILE B 130 ? 0.2688 0.2661 0.1913 -0.0646 0.0175  -0.0080 271 ILE B CB    
4049 C CG1   . ILE B 130 ? 0.2822 0.2929 0.2098 -0.0712 0.0128  -0.0065 271 ILE B CG1   
4050 C CG2   . ILE B 130 ? 0.2407 0.2490 0.1788 -0.0580 0.0176  -0.0054 271 ILE B CG2   
4051 C CD1   . ILE B 130 ? 0.3232 0.3453 0.2593 -0.0660 0.0097  -0.0034 271 ILE B CD1   
4052 N N     . THR B 131 ? 0.3178 0.2792 0.2045 -0.0740 0.0215  -0.0162 272 THR B N     
4053 C CA    . THR B 131 ? 0.3303 0.2819 0.2032 -0.0807 0.0215  -0.0203 272 THR B CA    
4054 C C     . THR B 131 ? 0.3373 0.2999 0.2114 -0.0811 0.0185  -0.0203 272 THR B C     
4055 O O     . THR B 131 ? 0.3301 0.3042 0.2140 -0.0746 0.0170  -0.0171 272 THR B O     
4056 C CB    . THR B 131 ? 0.3595 0.2885 0.2181 -0.0768 0.0257  -0.0242 272 THR B CB    
4057 O OG1   . THR B 131 ? 0.4052 0.3338 0.2626 -0.0684 0.0266  -0.0253 272 THR B OG1   
4058 C CG2   . THR B 131 ? 0.3217 0.2413 0.1809 -0.0729 0.0284  -0.0224 272 THR B CG2   
4059 N N     . HIS B 132 ? 0.3455 0.3038 0.2085 -0.0894 0.0177  -0.0239 273 HIS B N     
4060 C CA    . HIS B 132 ? 0.3338 0.3016 0.1949 -0.0914 0.0150  -0.0243 273 HIS B CA    
4061 C C     . HIS B 132 ? 0.3481 0.3092 0.2033 -0.0828 0.0179  -0.0267 273 HIS B C     
4062 O O     . HIS B 132 ? 0.3572 0.3285 0.2128 -0.0829 0.0159  -0.0259 273 HIS B O     
4063 C CB    . HIS B 132 ? 0.3429 0.3071 0.1920 -0.1033 0.0138  -0.0285 273 HIS B CB    
4064 C CG    . HIS B 132 ? 0.3681 0.3510 0.2212 -0.1096 0.0084  -0.0258 273 HIS B CG    
4065 N ND1   . HIS B 132 ? 0.3902 0.3781 0.2391 -0.1216 0.0052  -0.0269 273 HIS B ND1   
4066 C CD2   . HIS B 132 ? 0.3404 0.3384 0.2012 -0.1059 0.0053  -0.0215 273 HIS B CD2   
4067 C CE1   . HIS B 132 ? 0.3635 0.3695 0.2176 -0.1248 0.0000  -0.0231 273 HIS B CE1   
4068 N NE2   . HIS B 132 ? 0.3456 0.3575 0.2069 -0.1154 0.0000  -0.0196 273 HIS B NE2   
4069 N N     . LEU B 133 ? 0.3341 0.2791 0.1844 -0.0756 0.0225  -0.0292 274 LEU B N     
4070 C CA    . LEU B 133 ? 0.3279 0.2657 0.1730 -0.0672 0.0257  -0.0320 274 LEU B CA    
4071 C C     . LEU B 133 ? 0.3347 0.2838 0.1923 -0.0574 0.0251  -0.0273 274 LEU B C     
4072 O O     . LEU B 133 ? 0.3709 0.3164 0.2257 -0.0502 0.0277  -0.0292 274 LEU B O     
4073 C CB    . LEU B 133 ? 0.3735 0.2886 0.2087 -0.0634 0.0305  -0.0364 274 LEU B CB    
4074 C CG    . LEU B 133 ? 0.4601 0.3590 0.2813 -0.0720 0.0321  -0.0422 274 LEU B CG    
4075 C CD1   . LEU B 133 ? 0.4280 0.3063 0.2444 -0.0688 0.0354  -0.0432 274 LEU B CD1   
4076 C CD2   . LEU B 133 ? 0.3970 0.2910 0.2070 -0.0734 0.0341  -0.0489 274 LEU B CD2   
4077 N N     . GLU B 134 ? 0.3698 0.3322 0.2414 -0.0570 0.0221  -0.0216 275 GLU B N     
4078 C CA    . GLU B 134 ? 0.2741 0.2436 0.1571 -0.0476 0.0222  -0.0178 275 GLU B CA    
4079 C C     . GLU B 134 ? 0.3299 0.3102 0.2161 -0.0442 0.0209  -0.0164 275 GLU B C     
4080 O O     . GLU B 134 ? 0.3359 0.3258 0.2214 -0.0502 0.0179  -0.0154 275 GLU B O     
4081 C CB    . GLU B 134 ? 0.2886 0.2700 0.1863 -0.0484 0.0195  -0.0130 275 GLU B CB    
4082 C CG    . GLU B 134 ? 0.2976 0.2706 0.1931 -0.0523 0.0209  -0.0139 275 GLU B CG    
4083 C CD    . GLU B 134 ? 0.3721 0.3277 0.2593 -0.0466 0.0252  -0.0161 275 GLU B CD    
4084 O OE1   . GLU B 134 ? 0.3652 0.3206 0.2556 -0.0375 0.0266  -0.0153 275 GLU B OE1   
4085 O OE2   . GLU B 134 ? 0.3900 0.3319 0.2672 -0.0514 0.0270  -0.0186 275 GLU B OE2   
4086 N N     . HIS B 135 ? 0.2961 0.2747 0.1852 -0.0349 0.0232  -0.0160 276 HIS B N     
4087 C CA    . HIS B 135 ? 0.2676 0.2584 0.1641 -0.0304 0.0219  -0.0131 276 HIS B CA    
4088 C C     . HIS B 135 ? 0.2652 0.2717 0.1774 -0.0317 0.0174  -0.0069 276 HIS B C     
4089 O O     . HIS B 135 ? 0.2421 0.2494 0.1615 -0.0326 0.0166  -0.0054 276 HIS B O     
4090 C CB    . HIS B 135 ? 0.3016 0.2860 0.1986 -0.0203 0.0255  -0.0143 276 HIS B CB    
4091 C CG    . HIS B 135 ? 0.3116 0.3058 0.2135 -0.0154 0.0254  -0.0125 276 HIS B CG    
4092 N ND1   . HIS B 135 ? 0.2764 0.2841 0.1922 -0.0132 0.0224  -0.0071 276 HIS B ND1   
4093 C CD2   . HIS B 135 ? 0.3197 0.3120 0.2150 -0.0119 0.0282  -0.0156 276 HIS B CD2   
4094 C CE1   . HIS B 135 ? 0.2713 0.2849 0.1883 -0.0093 0.0231  -0.0065 276 HIS B CE1   
4095 N NE2   . HIS B 135 ? 0.3225 0.3277 0.2272 -0.0085 0.0267  -0.0116 276 HIS B NE2   
4096 N N     . HIS B 136 ? 0.2369 0.2561 0.1549 -0.0318 0.0146  -0.0034 277 HIS B N     
4097 C CA    . HIS B 136 ? 0.2303 0.2637 0.1644 -0.0323 0.0101  0.0028  277 HIS B CA    
4098 C C     . HIS B 136 ? 0.2445 0.2780 0.1902 -0.0254 0.0113  0.0039  277 HIS B C     
4099 O O     . HIS B 136 ? 0.2034 0.2450 0.1620 -0.0264 0.0086  0.0071  277 HIS B O     
4100 C CB    . HIS B 136 ? 0.2039 0.2488 0.1417 -0.0323 0.0073  0.0068  277 HIS B CB    
4101 C CG    . HIS B 136 ? 0.2721 0.3209 0.2003 -0.0405 0.0050  0.0069  277 HIS B CG    
4102 N ND1   . HIS B 136 ? 0.2112 0.2688 0.1381 -0.0419 0.0031  0.0099  277 HIS B ND1   
4103 C CD2   . HIS B 136 ? 0.2700 0.3157 0.1892 -0.0485 0.0041  0.0043  277 HIS B CD2   
4104 C CE1   . HIS B 136 ? 0.2746 0.3347 0.1915 -0.0503 0.0011  0.0091  277 HIS B CE1   
4105 N NE2   . HIS B 136 ? 0.2751 0.3281 0.1874 -0.0544 0.0016  0.0056  277 HIS B NE2   
4106 N N     . ALA B 137 ? 0.2098 0.2348 0.1512 -0.0185 0.0153  0.0012  278 ALA B N     
4107 C CA    . ALA B 137 ? 0.2209 0.2457 0.1714 -0.0125 0.0165  0.0018  278 ALA B CA    
4108 C C     . ALA B 137 ? 0.2049 0.2256 0.1565 -0.0153 0.0171  0.0008  278 ALA B C     
4109 O O     . ALA B 137 ? 0.2218 0.2470 0.1840 -0.0128 0.0171  0.0020  278 ALA B O     
4110 C CB    . ALA B 137 ? 0.2126 0.2286 0.1565 -0.0052 0.0204  -0.0009 278 ALA B CB    
4111 N N     . ASN B 138 ? 0.2125 0.2245 0.1531 -0.0209 0.0180  -0.0019 279 ASN B N     
4112 C CA    . ASN B 138 ? 0.1914 0.1996 0.1319 -0.0250 0.0187  -0.0027 279 ASN B CA    
4113 C C     . ASN B 138 ? 0.2555 0.2727 0.2007 -0.0333 0.0152  -0.0012 279 ASN B C     
4114 O O     . ASN B 138 ? 0.2394 0.2523 0.1805 -0.0392 0.0158  -0.0027 279 ASN B O     
4115 C CB    . ASN B 138 ? 0.2276 0.2185 0.1527 -0.0254 0.0222  -0.0066 279 ASN B CB    
4116 C CG    . ASN B 138 ? 0.2980 0.2833 0.2233 -0.0265 0.0240  -0.0068 279 ASN B CG    
4117 O OD1   . ASN B 138 ? 0.2154 0.2095 0.1520 -0.0248 0.0236  -0.0049 279 ASN B OD1   
4118 N ND2   . ASN B 138 ? 0.3358 0.3063 0.2482 -0.0298 0.0262  -0.0093 279 ASN B ND2   
4119 N N     . ILE B 139 ? 0.2303 0.2604 0.1845 -0.0343 0.0113  0.0023  280 ILE B N     
4120 C CA    . ILE B 139 ? 0.2144 0.2557 0.1760 -0.0414 0.0071  0.0049  280 ILE B CA    
4121 C C     . ILE B 139 ? 0.1930 0.2488 0.1739 -0.0382 0.0039  0.0095  280 ILE B C     
4122 O O     . ILE B 139 ? 0.1863 0.2493 0.1789 -0.0398 0.0029  0.0104  280 ILE B O     
4123 C CB    . ILE B 139 ? 0.2246 0.2674 0.1768 -0.0472 0.0045  0.0053  280 ILE B CB    
4124 C CG1   . ILE B 139 ? 0.2391 0.2668 0.1726 -0.0510 0.0078  -0.0002 280 ILE B CG1   
4125 C CG2   . ILE B 139 ? 0.2334 0.2903 0.1953 -0.0541 -0.0010 0.0093  280 ILE B CG2   
4126 C CD1   . ILE B 139 ? 0.2636 0.2928 0.1863 -0.0573 0.0057  -0.0010 280 ILE B CD1   
4127 N N     . VAL B 140 ? 0.1658 0.2259 0.1508 -0.0336 0.0025  0.0122  281 VAL B N     
4128 C CA    . VAL B 140 ? 0.1533 0.2265 0.1567 -0.0312 -0.0012 0.0171  281 VAL B CA    
4129 C C     . VAL B 140 ? 0.1855 0.2605 0.2018 -0.0265 0.0008  0.0159  281 VAL B C     
4130 O O     . VAL B 140 ? 0.1571 0.2428 0.1896 -0.0270 -0.0020 0.0185  281 VAL B O     
4131 C CB    . VAL B 140 ? 0.2017 0.2775 0.2051 -0.0278 -0.0026 0.0202  281 VAL B CB    
4132 C CG1   . VAL B 140 ? 0.1528 0.2408 0.1755 -0.0257 -0.0069 0.0258  281 VAL B CG1   
4133 C CG2   . VAL B 140 ? 0.1729 0.2478 0.1625 -0.0334 -0.0042 0.0207  281 VAL B CG2   
4134 N N     . PRO B 141 ? 0.1651 0.2313 0.1761 -0.0217 0.0054  0.0122  282 PRO B N     
4135 C CA    . PRO B 141 ? 0.1686 0.2378 0.1913 -0.0182 0.0074  0.0106  282 PRO B CA    
4136 C C     . PRO B 141 ? 0.1652 0.2383 0.1927 -0.0233 0.0076  0.0093  282 PRO B C     
4137 O O     . PRO B 141 ? 0.1836 0.2657 0.2269 -0.0220 0.0073  0.0094  282 PRO B O     
4138 C CB    . PRO B 141 ? 0.1557 0.2137 0.1673 -0.0137 0.0119  0.0071  282 PRO B CB    
4139 C CG    . PRO B 141 ? 0.1545 0.2068 0.1549 -0.0121 0.0117  0.0079  282 PRO B CG    
4140 C CD    . PRO B 141 ? 0.1749 0.2288 0.1699 -0.0189 0.0089  0.0092  282 PRO B CD    
4141 N N     . TRP B 142 ? 0.1797 0.2466 0.1944 -0.0293 0.0082  0.0079  283 TRP B N     
4142 C CA    . TRP B 142 ? 0.1658 0.2371 0.1846 -0.0352 0.0084  0.0068  283 TRP B CA    
4143 C C     . TRP B 142 ? 0.1837 0.2695 0.2170 -0.0386 0.0034  0.0105  283 TRP B C     
4144 O O     . TRP B 142 ? 0.2028 0.2981 0.2496 -0.0400 0.0032  0.0102  283 TRP B O     
4145 C CB    . TRP B 142 ? 0.1921 0.2516 0.1928 -0.0411 0.0105  0.0042  283 TRP B CB    
4146 C CG    . TRP B 142 ? 0.2026 0.2473 0.1897 -0.0369 0.0148  0.0015  283 TRP B CG    
4147 C CD1   . TRP B 142 ? 0.1974 0.2293 0.1686 -0.0363 0.0159  0.0002  283 TRP B CD1   
4148 C CD2   . TRP B 142 ? 0.1872 0.2292 0.1763 -0.0326 0.0184  -0.0003 283 TRP B CD2   
4149 N NE1   . TRP B 142 ? 0.1926 0.2140 0.1567 -0.0312 0.0196  -0.0016 283 TRP B NE1   
4150 C CE2   . TRP B 142 ? 0.2213 0.2489 0.1956 -0.0292 0.0209  -0.0016 283 TRP B CE2   
4151 C CE3   . TRP B 142 ? 0.2318 0.2827 0.2339 -0.0312 0.0197  -0.0010 283 TRP B CE3   
4152 C CZ2   . TRP B 142 ? 0.2151 0.2373 0.1869 -0.0249 0.0241  -0.0028 283 TRP B CZ2   
4153 C CZ3   . TRP B 142 ? 0.2153 0.2609 0.2139 -0.0275 0.0234  -0.0029 283 TRP B CZ3   
4154 C CH2   . TRP B 142 ? 0.2059 0.2374 0.1894 -0.0245 0.0252  -0.0034 283 TRP B CH2   
4155 N N     . GLN B 143 ? 0.1649 0.2535 0.1964 -0.0399 -0.0009 0.0142  284 GLN B N     
4156 C CA    . GLN B 143 ? 0.1798 0.2828 0.2259 -0.0425 -0.0066 0.0190  284 GLN B CA    
4157 C C     . GLN B 143 ? 0.1978 0.3102 0.2651 -0.0362 -0.0077 0.0211  284 GLN B C     
4158 O O     . GLN B 143 ? 0.1845 0.3085 0.2683 -0.0375 -0.0102 0.0228  284 GLN B O     
4159 C CB    . GLN B 143 ? 0.1517 0.2556 0.1903 -0.0450 -0.0109 0.0231  284 GLN B CB    
4160 C CG    . GLN B 143 ? 0.1705 0.2666 0.1893 -0.0523 -0.0104 0.0207  284 GLN B CG    
4161 C CD    . GLN B 143 ? 0.2207 0.3191 0.2321 -0.0549 -0.0143 0.0242  284 GLN B CD    
4162 O OE1   . GLN B 143 ? 0.2033 0.3038 0.2186 -0.0500 -0.0154 0.0273  284 GLN B OE1   
4163 N NE2   . GLN B 143 ? 0.2209 0.3194 0.2211 -0.0633 -0.0163 0.0236  284 GLN B NE2   
4164 N N     . LEU B 144 ? 0.1520 0.2597 0.2199 -0.0295 -0.0059 0.0208  285 LEU B N     
4165 C CA    . LEU B 144 ? 0.1715 0.2867 0.2592 -0.0237 -0.0068 0.0222  285 LEU B CA    
4166 C C     . LEU B 144 ? 0.2040 0.3224 0.3016 -0.0226 -0.0029 0.0174  285 LEU B C     
4167 O O     . LEU B 144 ? 0.2110 0.3402 0.3282 -0.0214 -0.0047 0.0184  285 LEU B O     
4168 C CB    . LEU B 144 ? 0.1738 0.2825 0.2580 -0.0176 -0.0051 0.0221  285 LEU B CB    
4169 C CG    . LEU B 144 ? 0.2273 0.3353 0.3050 -0.0180 -0.0088 0.0271  285 LEU B CG    
4170 C CD1   . LEU B 144 ? 0.2051 0.3062 0.2771 -0.0125 -0.0059 0.0257  285 LEU B CD1   
4171 C CD2   . LEU B 144 ? 0.2063 0.3257 0.3008 -0.0185 -0.0151 0.0339  285 LEU B CD2   
4172 N N     . LEU B 145 ? 0.2080 0.3174 0.2926 -0.0231 0.0024  0.0124  286 LEU B N     
4173 C CA    . LEU B 145 ? 0.2025 0.3153 0.2939 -0.0235 0.0064  0.0078  286 LEU B CA    
4174 C C     . LEU B 145 ? 0.2031 0.3265 0.3037 -0.0293 0.0044  0.0085  286 LEU B C     
4175 O O     . LEU B 145 ? 0.2268 0.3609 0.3454 -0.0280 0.0050  0.0071  286 LEU B O     
4176 C CB    . LEU B 145 ? 0.1975 0.2984 0.2706 -0.0247 0.0115  0.0036  286 LEU B CB    
4177 C CG    . LEU B 145 ? 0.2320 0.3365 0.3104 -0.0256 0.0161  -0.0010 286 LEU B CG    
4178 C CD1   . LEU B 145 ? 0.2202 0.3307 0.3139 -0.0192 0.0176  -0.0031 286 LEU B CD1   
4179 C CD2   . LEU B 145 ? 0.2500 0.3420 0.3090 -0.0276 0.0203  -0.0036 286 LEU B CD2   
4180 N N     . SER B 146 ? 0.2111 0.3319 0.2997 -0.0359 0.0023  0.0103  287 SER B N     
4181 C CA    . SER B 146 ? 0.2145 0.3456 0.3102 -0.0424 0.0000  0.0113  287 SER B CA    
4182 C C     . SER B 146 ? 0.2094 0.3557 0.3283 -0.0401 -0.0050 0.0154  287 SER B C     
4183 O O     . SER B 146 ? 0.2495 0.4075 0.3833 -0.0419 -0.0051 0.0145  287 SER B O     
4184 C CB    . SER B 146 ? 0.1985 0.3240 0.2772 -0.0495 -0.0027 0.0132  287 SER B CB    
4185 O OG    . SER B 146 ? 0.3878 0.5039 0.4513 -0.0544 0.0017  0.0090  287 SER B OG    
4186 N N     . ARG B 147 ? 0.1646 0.3112 0.2870 -0.0364 -0.0094 0.0203  288 ARG B N     
4187 C CA    . ARG B 147 ? 0.1944 0.3544 0.3392 -0.0340 -0.0148 0.0253  288 ARG B CA    
4188 C C     . ARG B 147 ? 0.2224 0.3873 0.3868 -0.0273 -0.0119 0.0221  288 ARG B C     
4189 O O     . ARG B 147 ? 0.2186 0.3958 0.4046 -0.0255 -0.0149 0.0243  288 ARG B O     
4190 C CB    . ARG B 147 ? 0.1847 0.3430 0.3271 -0.0325 -0.0202 0.0319  288 ARG B CB    
4191 C CG    . ARG B 147 ? 0.1781 0.3330 0.3019 -0.0395 -0.0232 0.0347  288 ARG B CG    
4192 C CD    . ARG B 147 ? 0.1843 0.3404 0.3078 -0.0384 -0.0288 0.0418  288 ARG B CD    
4193 N NE    . ARG B 147 ? 0.3310 0.4893 0.4420 -0.0463 -0.0329 0.0449  288 ARG B NE    
4194 C CZ    . ARG B 147 ? 0.1928 0.3621 0.3116 -0.0496 -0.0403 0.0523  288 ARG B CZ    
4195 N NH1   . ARG B 147 ? 0.1857 0.3630 0.3238 -0.0449 -0.0448 0.0585  288 ARG B NH1   
4196 N NH2   . ARG B 147 ? 0.2985 0.4704 0.4050 -0.0580 -0.0434 0.0538  288 ARG B NH2   
4197 N N     . GLN B 148 ? 0.1912 0.3469 0.3487 -0.0233 -0.0061 0.0168  289 GLN B N     
4198 C CA    . GLN B 148 ? 0.1873 0.3476 0.3621 -0.0176 -0.0026 0.0125  289 GLN B CA    
4199 C C     . GLN B 148 ? 0.2131 0.3811 0.3947 -0.0204 0.0018  0.0069  289 GLN B C     
4200 O O     . GLN B 148 ? 0.1654 0.3432 0.3679 -0.0170 0.0029  0.0044  289 GLN B O     
4201 C CB    . GLN B 148 ? 0.2112 0.3603 0.3759 -0.0131 0.0018  0.0088  289 GLN B CB    
4202 C CG    . GLN B 148 ? 0.3292 0.4738 0.4938 -0.0092 -0.0022 0.0139  289 GLN B CG    
4203 C CD    . GLN B 148 ? 0.4197 0.5742 0.6080 -0.0060 -0.0072 0.0183  289 GLN B CD    
4204 O OE1   . GLN B 148 ? 0.3513 0.5086 0.5416 -0.0075 -0.0134 0.0256  289 GLN B OE1   
4205 N NE2   . GLN B 148 ? 0.3874 0.5448 0.5893 -0.0019 -0.0044 0.0133  289 GLN B NE2   
4206 N N     . THR B 149 ? 0.1857 0.3492 0.3502 -0.0267 0.0047  0.0046  290 THR B N     
4207 C CA    . THR B 149 ? 0.1854 0.3543 0.3526 -0.0298 0.0101  -0.0013 290 THR B CA    
4208 C C     . THR B 149 ? 0.1935 0.3708 0.3615 -0.0376 0.0086  -0.0001 290 THR B C     
4209 O O     . THR B 149 ? 0.1854 0.3696 0.3580 -0.0407 0.0130  -0.0047 290 THR B O     
4210 C CB    . THR B 149 ? 0.1995 0.3555 0.3458 -0.0311 0.0160  -0.0057 290 THR B CB    
4211 O OG1   . THR B 149 ? 0.2443 0.3903 0.3697 -0.0368 0.0146  -0.0031 290 THR B OG1   
4212 C CG2   . THR B 149 ? 0.1988 0.3464 0.3423 -0.0240 0.0174  -0.0067 290 THR B CG2   
4213 N N     . GLY B 150 ? 0.1473 0.3248 0.3101 -0.0416 0.0027  0.0055  291 GLY B N     
4214 C CA    . GLY B 150 ? 0.1024 0.2869 0.2631 -0.0501 0.0013  0.0062  291 GLY B CA    
4215 C C     . GLY B 150 ? 0.1936 0.3663 0.3306 -0.0571 0.0054  0.0032  291 GLY B C     
4216 O O     . GLY B 150 ? 0.2275 0.4060 0.3630 -0.0649 0.0053  0.0028  291 GLY B O     
4217 N N     . ALA B 151 ? 0.2181 0.3748 0.3374 -0.0546 0.0088  0.0013  292 ALA B N     
4218 C CA    . ALA B 151 ? 0.2162 0.3592 0.3121 -0.0608 0.0115  -0.0003 292 ALA B CA    
4219 C C     . ALA B 151 ? 0.2246 0.3644 0.3098 -0.0669 0.0065  0.0034  292 ALA B C     
4220 O O     . ALA B 151 ? 0.2456 0.3901 0.3367 -0.0650 0.0011  0.0077  292 ALA B O     
4221 C CB    . ALA B 151 ? 0.2229 0.3498 0.3037 -0.0557 0.0150  -0.0020 292 ALA B CB    
4222 N N     . VAL B 152 ? 0.2225 0.3537 0.2910 -0.0746 0.0084  0.0017  293 VAL B N     
4223 C CA    . VAL B 152 ? 0.2623 0.3910 0.3202 -0.0822 0.0043  0.0039  293 VAL B CA    
4224 C C     . VAL B 152 ? 0.2758 0.3840 0.3102 -0.0821 0.0059  0.0028  293 VAL B C     
4225 O O     . VAL B 152 ? 0.2577 0.3532 0.2799 -0.0823 0.0109  -0.0002 293 VAL B O     
4226 C CB    . VAL B 152 ? 0.2734 0.4087 0.3316 -0.0922 0.0050  0.0024  293 VAL B CB    
4227 C CG1   . VAL B 152 ? 0.3436 0.4750 0.3888 -0.1008 0.0010  0.0039  293 VAL B CG1   
4228 C CG2   . VAL B 152 ? 0.3008 0.4581 0.3844 -0.0917 0.0035  0.0033  293 VAL B CG2   
4229 N N     . LEU B 153 ? 0.2388 0.3441 0.2670 -0.0817 0.0018  0.0053  294 LEU B N     
4230 C CA    . LEU B 153 ? 0.2393 0.3263 0.2466 -0.0811 0.0033  0.0038  294 LEU B CA    
4231 C C     . LEU B 153 ? 0.2977 0.3789 0.2905 -0.0912 0.0020  0.0026  294 LEU B C     
4232 O O     . LEU B 153 ? 0.3145 0.4061 0.3113 -0.0963 -0.0031 0.0050  294 LEU B O     
4233 C CB    . LEU B 153 ? 0.2715 0.3588 0.2802 -0.0743 0.0005  0.0066  294 LEU B CB    
4234 C CG    . LEU B 153 ? 0.3207 0.3918 0.3103 -0.0725 0.0020  0.0050  294 LEU B CG    
4235 C CD1   . LEU B 153 ? 0.2649 0.3209 0.2448 -0.0678 0.0078  0.0016  294 LEU B CD1   
4236 C CD2   . LEU B 153 ? 0.3427 0.4186 0.3369 -0.0668 -0.0012 0.0085  294 LEU B CD2   
4237 N N     . LYS B 154 ? 0.2554 0.3201 0.2316 -0.0943 0.0062  -0.0010 295 LYS B N     
4238 C CA    . LYS B 154 ? 0.3162 0.3716 0.2766 -0.1038 0.0057  -0.0031 295 LYS B CA    
4239 C C     . LYS B 154 ? 0.3190 0.3554 0.2612 -0.1006 0.0076  -0.0055 295 LYS B C     
4240 O O     . LYS B 154 ? 0.2921 0.3194 0.2317 -0.0922 0.0108  -0.0060 295 LYS B O     
4241 C CB    . LYS B 154 ? 0.2926 0.3433 0.2485 -0.1114 0.0089  -0.0054 295 LYS B CB    
4242 C CG    . LYS B 154 ? 0.3590 0.4290 0.3337 -0.1139 0.0083  -0.0039 295 LYS B CG    
4243 C CD    . LYS B 154 ? 0.4180 0.4909 0.3894 -0.1263 0.0079  -0.0051 295 LYS B CD    
4244 C CE    . LYS B 154 ? 0.4418 0.5304 0.4294 -0.1286 0.0096  -0.0048 295 LYS B CE    
4245 N NZ    . LYS B 154 ? 0.5558 0.6340 0.5323 -0.1361 0.0144  -0.0072 295 LYS B NZ    
4246 N N     . VAL B 155 ? 0.2929 0.3237 0.2226 -0.1076 0.0058  -0.0073 296 VAL B N     
4247 C CA    . VAL B 155 ? 0.3291 0.3436 0.2424 -0.1050 0.0075  -0.0104 296 VAL B CA    
4248 C C     . VAL B 155 ? 0.3344 0.3323 0.2304 -0.1136 0.0097  -0.0150 296 VAL B C     
4249 O O     . VAL B 155 ? 0.3402 0.3433 0.2336 -0.1238 0.0070  -0.0158 296 VAL B O     
4250 C CB    . VAL B 155 ? 0.3913 0.4151 0.3055 -0.1045 0.0033  -0.0087 296 VAL B CB    
4251 C CG1   . VAL B 155 ? 0.3294 0.3372 0.2265 -0.1021 0.0059  -0.0128 296 VAL B CG1   
4252 C CG2   . VAL B 155 ? 0.2972 0.3357 0.2289 -0.0960 0.0011  -0.0037 296 VAL B CG2   
4253 N N     . ALA B 156 ? 0.3319 0.3102 0.2166 -0.1098 0.0144  -0.0178 297 ALA B N     
4254 C CA    . ALA B 156 ? 0.3849 0.3444 0.2531 -0.1173 0.0168  -0.0223 297 ALA B CA    
4255 C C     . ALA B 156 ? 0.3488 0.2999 0.2038 -0.1192 0.0164  -0.0266 297 ALA B C     
4256 O O     . ALA B 156 ? 0.3545 0.3032 0.2079 -0.1108 0.0172  -0.0271 297 ALA B O     
4257 C CB    . ALA B 156 ? 0.3687 0.3098 0.2303 -0.1120 0.0216  -0.0229 297 ALA B CB    
4258 N N     . PRO B 157 ? 0.4229 0.3697 0.2681 -0.1304 0.0153  -0.0302 298 PRO B N     
4259 C CA    . PRO B 157 ? 0.3641 0.3064 0.1974 -0.1336 0.0146  -0.0348 298 PRO B CA    
4260 C C     . PRO B 157 ? 0.4356 0.3526 0.2530 -0.1303 0.0197  -0.0409 298 PRO B C     
4261 O O     . PRO B 157 ? 0.4628 0.3635 0.2768 -0.1270 0.0233  -0.0413 298 PRO B O     
4262 C CB    . PRO B 157 ? 0.3932 0.3419 0.2232 -0.1480 0.0114  -0.0363 298 PRO B CB    
4263 C CG    . PRO B 157 ? 0.3932 0.3346 0.2245 -0.1524 0.0134  -0.0355 298 PRO B CG    
4264 C CD    . PRO B 157 ? 0.3786 0.3266 0.2239 -0.1417 0.0146  -0.0302 298 PRO B CD    
4265 N N     . VAL B 158 ? 0.4120 0.3262 0.2196 -0.1316 0.0198  -0.0457 299 VAL B N     
4266 C CA    . VAL B 158 ? 0.4763 0.3676 0.2685 -0.1296 0.0245  -0.0530 299 VAL B CA    
4267 C C     . VAL B 158 ? 0.4929 0.3806 0.2722 -0.1421 0.0237  -0.0595 299 VAL B C     
4268 O O     . VAL B 158 ? 0.4806 0.3860 0.2629 -0.1508 0.0190  -0.0578 299 VAL B O     
4269 C CB    . VAL B 158 ? 0.4547 0.3457 0.2470 -0.1178 0.0267  -0.0540 299 VAL B CB    
4270 C CG1   . VAL B 158 ? 0.4189 0.3127 0.2232 -0.1059 0.0276  -0.0481 299 VAL B CG1   
4271 C CG2   . VAL B 158 ? 0.4302 0.3409 0.2245 -0.1205 0.0232  -0.0533 299 VAL B CG2   
4272 N N     . ASP B 159 ? 0.4799 0.3443 0.2447 -0.1429 0.0281  -0.0672 300 ASP B N     
4273 C CA    . ASP B 159 ? 0.5024 0.3622 0.2536 -0.1540 0.0281  -0.0750 300 ASP B CA    
4274 C C     . ASP B 159 ? 0.5266 0.3925 0.2729 -0.1499 0.0290  -0.0790 300 ASP B C     
4275 O O     . ASP B 159 ? 0.5127 0.3868 0.2670 -0.1388 0.0295  -0.0753 300 ASP B O     
4276 C CB    . ASP B 159 ? 0.5142 0.3459 0.2523 -0.1583 0.0324  -0.0820 300 ASP B CB    
4277 C CG    . ASP B 159 ? 0.5919 0.4020 0.3252 -0.1461 0.0381  -0.0860 300 ASP B CG    
4278 O OD1   . ASP B 159 ? 0.6255 0.4416 0.3614 -0.1362 0.0395  -0.0864 300 ASP B OD1   
4279 O OD2   . ASP B 159 ? 0.6114 0.3981 0.3384 -0.1465 0.0412  -0.0885 300 ASP B OD2   
4280 N N     . ASP B 160 ? 0.5129 0.3754 0.2465 -0.1591 0.0295  -0.0867 301 ASP B N     
4281 C CA    . ASP B 160 ? 0.5700 0.4427 0.3015 -0.1560 0.0302  -0.0891 301 ASP B CA    
4282 C C     . ASP B 160 ? 0.5990 0.4572 0.3279 -0.1430 0.0363  -0.0936 301 ASP B C     
4283 O O     . ASP B 160 ? 0.5647 0.4339 0.2951 -0.1373 0.0369  -0.0936 301 ASP B O     
4284 C CB    . ASP B 160 ? 0.5634 0.4374 0.2876 -0.1661 0.0300  -0.0941 301 ASP B CB    
4285 C CG    . ASP B 160 ? 0.6322 0.5275 0.3607 -0.1780 0.0232  -0.0887 301 ASP B CG    
4286 O OD1   . ASP B 160 ? 0.6072 0.5182 0.3455 -0.1776 0.0184  -0.0810 301 ASP B OD1   
4287 O OD2   . ASP B 160 ? 0.7675 0.6643 0.4902 -0.1875 0.0226  -0.0919 301 ASP B OD2   
4288 N N     . ALA B 161 ? 0.5279 0.3624 0.2536 -0.1380 0.0406  -0.0967 302 ALA B N     
4289 C CA    . ALA B 161 ? 0.5486 0.3687 0.2734 -0.1249 0.0462  -0.1003 302 ALA B CA    
4290 C C     . ALA B 161 ? 0.5764 0.4031 0.3119 -0.1133 0.0458  -0.0931 302 ALA B C     
4291 O O     . ALA B 161 ? 0.5840 0.4041 0.3207 -0.1017 0.0498  -0.0952 302 ALA B O     
4292 C CB    . ALA B 161 ? 0.5956 0.3882 0.3150 -0.1235 0.0503  -0.1049 302 ALA B CB    
4293 N N     . GLY B 162 ? 0.5356 0.3777 0.2829 -0.1148 0.0408  -0.0837 303 GLY B N     
4294 C CA    . GLY B 162 ? 0.5051 0.3551 0.2662 -0.1032 0.0401  -0.0756 303 GLY B CA    
4295 C C     . GLY B 162 ? 0.5128 0.3480 0.2777 -0.0986 0.0414  -0.0721 303 GLY B C     
4296 O O     . GLY B 162 ? 0.4955 0.3338 0.2699 -0.0879 0.0418  -0.0669 303 GLY B O     
4297 N N     . ASN B 163 ? 0.5423 0.3617 0.2996 -0.1066 0.0421  -0.0747 304 ASN B N     
4298 C CA    . ASN B 163 ? 0.5089 0.3151 0.2691 -0.1040 0.0428  -0.0704 304 ASN B CA    
4299 C C     . ASN B 163 ? 0.5280 0.3520 0.2994 -0.1085 0.0386  -0.0622 304 ASN B C     
4300 O O     . ASN B 163 ? 0.5204 0.3578 0.2927 -0.1190 0.0351  -0.0619 304 ASN B O     
4301 C CB    . ASN B 163 ? 0.5336 0.3154 0.2812 -0.1119 0.0451  -0.0759 304 ASN B CB    
4302 C CG    . ASN B 163 ? 0.5545 0.3153 0.2914 -0.1072 0.0500  -0.0848 304 ASN B CG    
4303 O OD1   . ASN B 163 ? 0.6202 0.3689 0.3588 -0.0955 0.0529  -0.0842 304 ASN B OD1   
4304 N ND2   . ASN B 163 ? 0.5846 0.3407 0.3104 -0.1165 0.0509  -0.0932 304 ASN B ND2   
4305 N N     . LEU B 164 ? 0.5018 0.3257 0.2817 -0.1010 0.0388  -0.0560 305 LEU B N     
4306 C CA    . LEU B 164 ? 0.4739 0.3121 0.2638 -0.1055 0.0357  -0.0493 305 LEU B CA    
4307 C C     . LEU B 164 ? 0.5202 0.3473 0.3032 -0.1174 0.0358  -0.0504 305 LEU B C     
4308 O O     . LEU B 164 ? 0.5540 0.3579 0.3273 -0.1176 0.0387  -0.0528 305 LEU B O     
4309 C CB    . LEU B 164 ? 0.4772 0.3170 0.2763 -0.0950 0.0365  -0.0433 305 LEU B CB    
4310 C CG    . LEU B 164 ? 0.4872 0.3446 0.2988 -0.0979 0.0339  -0.0369 305 LEU B CG    
4311 C CD1   . LEU B 164 ? 0.4242 0.3065 0.2473 -0.0974 0.0304  -0.0348 305 LEU B CD1   
4312 C CD2   . LEU B 164 ? 0.4386 0.2924 0.2553 -0.0888 0.0355  -0.0322 305 LEU B CD2   
4313 N N     . LEU B 165 ? 0.4918 0.3355 0.2801 -0.1275 0.0323  -0.0484 306 LEU B N     
4314 C CA    . LEU B 165 ? 0.4929 0.3296 0.2756 -0.1403 0.0320  -0.0493 306 LEU B CA    
4315 C C     . LEU B 165 ? 0.5082 0.3473 0.2987 -0.1396 0.0324  -0.0429 306 LEU B C     
4316 O O     . LEU B 165 ? 0.4652 0.3259 0.2690 -0.1396 0.0300  -0.0382 306 LEU B O     
4317 C CB    . LEU B 165 ? 0.4913 0.3463 0.2764 -0.1517 0.0279  -0.0504 306 LEU B CB    
4318 C CG    . LEU B 165 ? 0.5140 0.3666 0.2891 -0.1549 0.0275  -0.0572 306 LEU B CG    
4319 C CD1   . LEU B 165 ? 0.5153 0.3906 0.2948 -0.1653 0.0224  -0.0565 306 LEU B CD1   
4320 C CD2   . LEU B 165 ? 0.5594 0.3844 0.3177 -0.1604 0.0311  -0.0645 306 LEU B CD2   
4321 N N     . LEU B 166 ? 0.5259 0.3427 0.3081 -0.1393 0.0354  -0.0428 307 LEU B N     
4322 C CA    . LEU B 166 ? 0.5000 0.3182 0.2882 -0.1372 0.0363  -0.0365 307 LEU B CA    
4323 C C     . LEU B 166 ? 0.5161 0.3474 0.3094 -0.1495 0.0347  -0.0341 307 LEU B C     
4324 O O     . LEU B 166 ? 0.5177 0.3640 0.3220 -0.1478 0.0344  -0.0291 307 LEU B O     
4325 C CB    . LEU B 166 ? 0.5504 0.3412 0.3280 -0.1337 0.0395  -0.0361 307 LEU B CB    
4326 C CG    . LEU B 166 ? 0.5960 0.3782 0.3737 -0.1187 0.0411  -0.0356 307 LEU B CG    
4327 C CD1   . LEU B 166 ? 0.6417 0.3967 0.4096 -0.1163 0.0436  -0.0342 307 LEU B CD1   
4328 C CD2   . LEU B 166 ? 0.5392 0.3423 0.3307 -0.1101 0.0400  -0.0303 307 LEU B CD2   
4329 N N     . GLY B 167 ? 0.5445 0.3708 0.3302 -0.1622 0.0339  -0.0379 308 GLY B N     
4330 C CA    . GLY B 167 ? 0.5393 0.3796 0.3306 -0.1743 0.0323  -0.0358 308 GLY B CA    
4331 C C     . GLY B 167 ? 0.5543 0.4257 0.3621 -0.1735 0.0289  -0.0333 308 GLY B C     
4332 O O     . GLY B 167 ? 0.5057 0.3929 0.3248 -0.1753 0.0286  -0.0291 308 GLY B O     
4333 N N     . GLU B 168 ? 0.5124 0.3930 0.3219 -0.1708 0.0263  -0.0358 309 GLU B N     
4334 C CA    . GLU B 168 ? 0.4876 0.3966 0.3132 -0.1690 0.0224  -0.0328 309 GLU B CA    
4335 C C     . GLU B 168 ? 0.4735 0.3922 0.3118 -0.1565 0.0234  -0.0281 309 GLU B C     
4336 O O     . GLU B 168 ? 0.4825 0.4227 0.3364 -0.1563 0.0216  -0.0245 309 GLU B O     
4337 C CB    . GLU B 168 ? 0.4850 0.3993 0.3075 -0.1688 0.0195  -0.0361 309 GLU B CB    
4338 C CG    . GLU B 168 ? 0.5377 0.4467 0.3486 -0.1825 0.0179  -0.0412 309 GLU B CG    
4339 C CD    . GLU B 168 ? 0.6553 0.5341 0.4470 -0.1846 0.0218  -0.0474 309 GLU B CD    
4340 O OE1   . GLU B 168 ? 0.6497 0.5099 0.4369 -0.1797 0.0257  -0.0467 309 GLU B OE1   
4341 O OE2   . GLU B 168 ? 0.7699 0.6434 0.5510 -0.1915 0.0209  -0.0532 309 GLU B OE2   
4342 N N     . PHE B 169 ? 0.4329 0.3360 0.2653 -0.1460 0.0262  -0.0284 310 PHE B N     
4343 C CA    . PHE B 169 ? 0.4585 0.3692 0.3016 -0.1349 0.0273  -0.0243 310 PHE B CA    
4344 C C     . PHE B 169 ? 0.4426 0.3585 0.2917 -0.1388 0.0289  -0.0210 310 PHE B C     
4345 O O     . PHE B 169 ? 0.4134 0.3491 0.2775 -0.1360 0.0281  -0.0181 310 PHE B O     
4346 C CB    . PHE B 169 ? 0.3972 0.2887 0.2316 -0.1242 0.0301  -0.0252 310 PHE B CB    
4347 C CG    . PHE B 169 ? 0.4245 0.3193 0.2665 -0.1147 0.0318  -0.0210 310 PHE B CG    
4348 C CD1   . PHE B 169 ? 0.4215 0.3357 0.2779 -0.1072 0.0303  -0.0187 310 PHE B CD1   
4349 C CD2   . PHE B 169 ? 0.3852 0.2639 0.2199 -0.1139 0.0347  -0.0193 310 PHE B CD2   
4350 C CE1   . PHE B 169 ? 0.4400 0.3574 0.3029 -0.0992 0.0319  -0.0156 310 PHE B CE1   
4351 C CE2   . PHE B 169 ? 0.3879 0.2704 0.2286 -0.1059 0.0361  -0.0155 310 PHE B CE2   
4352 C CZ    . PHE B 169 ? 0.3903 0.2924 0.2451 -0.0987 0.0348  -0.0141 310 PHE B CZ    
4353 N N     . GLU B 170 ? 0.4141 0.3122 0.2515 -0.1456 0.0314  -0.0215 311 GLU B N     
4354 C CA    . GLU B 170 ? 0.4609 0.3633 0.3023 -0.1503 0.0334  -0.0182 311 GLU B CA    
4355 C C     . GLU B 170 ? 0.4734 0.3995 0.3274 -0.1594 0.0313  -0.0177 311 GLU B C     
4356 O O     . GLU B 170 ? 0.3985 0.3399 0.2640 -0.1589 0.0324  -0.0151 311 GLU B O     
4357 C CB    . GLU B 170 ? 0.4613 0.3390 0.2868 -0.1572 0.0360  -0.0183 311 GLU B CB    
4358 C CG    . GLU B 170 ? 0.4888 0.3716 0.3166 -0.1653 0.0380  -0.0150 311 GLU B CG    
4359 C CD    . GLU B 170 ? 0.5360 0.3930 0.3484 -0.1694 0.0407  -0.0132 311 GLU B CD    
4360 O OE1   . GLU B 170 ? 0.5506 0.3844 0.3502 -0.1685 0.0408  -0.0155 311 GLU B OE1   
4361 O OE2   . GLU B 170 ? 0.5604 0.4204 0.3738 -0.1739 0.0427  -0.0095 311 GLU B OE2   
4362 N N     . ASP B 171 ? 0.4605 0.3908 0.3128 -0.1675 0.0284  -0.0204 312 ASP B N     
4363 C CA    . ASP B 171 ? 0.4457 0.4005 0.3115 -0.1753 0.0255  -0.0197 312 ASP B CA    
4364 C C     . ASP B 171 ? 0.4380 0.4165 0.3229 -0.1664 0.0235  -0.0173 312 ASP B C     
4365 O O     . ASP B 171 ? 0.4270 0.4271 0.3266 -0.1706 0.0220  -0.0158 312 ASP B O     
4366 C CB    . ASP B 171 ? 0.5249 0.4807 0.3852 -0.1845 0.0219  -0.0229 312 ASP B CB    
4367 C CG    . ASP B 171 ? 0.5838 0.5196 0.4276 -0.1965 0.0235  -0.0258 312 ASP B CG    
4368 O OD1   . ASP B 171 ? 0.5853 0.5098 0.4241 -0.1993 0.0271  -0.0244 312 ASP B OD1   
4369 O OD2   . ASP B 171 ? 0.6170 0.5484 0.4526 -0.2035 0.0212  -0.0296 312 ASP B OD2   
4370 N N     . LEU B 172 ? 0.3925 0.3677 0.2781 -0.1543 0.0233  -0.0169 313 LEU B N     
4371 C CA    . LEU B 172 ? 0.3679 0.3641 0.2719 -0.1459 0.0215  -0.0144 313 LEU B CA    
4372 C C     . LEU B 172 ? 0.3953 0.3968 0.3080 -0.1407 0.0250  -0.0125 313 LEU B C     
4373 O O     . LEU B 172 ? 0.3409 0.3615 0.2709 -0.1355 0.0240  -0.0110 313 LEU B O     
4374 C CB    . LEU B 172 ? 0.3391 0.3312 0.2413 -0.1357 0.0199  -0.0145 313 LEU B CB    
4375 C CG    . LEU B 172 ? 0.4047 0.3977 0.3015 -0.1400 0.0159  -0.0162 313 LEU B CG    
4376 C CD1   . LEU B 172 ? 0.3828 0.3742 0.2793 -0.1296 0.0149  -0.0159 313 LEU B CD1   
4377 C CD2   . LEU B 172 ? 0.3896 0.4056 0.2999 -0.1470 0.0113  -0.0144 313 LEU B CD2   
4378 N N     . LEU B 173 ? 0.3691 0.3544 0.2705 -0.1420 0.0291  -0.0125 314 LEU B N     
4379 C CA    . LEU B 173 ? 0.3905 0.3801 0.2979 -0.1373 0.0325  -0.0108 314 LEU B CA    
4380 C C     . LEU B 173 ? 0.3598 0.3646 0.2761 -0.1465 0.0341  -0.0105 314 LEU B C     
4381 O O     . LEU B 173 ? 0.3615 0.3649 0.2728 -0.1579 0.0337  -0.0112 314 LEU B O     
4382 C CB    . LEU B 173 ? 0.3876 0.3537 0.2788 -0.1345 0.0358  -0.0101 314 LEU B CB    
4383 C CG    . LEU B 173 ? 0.3990 0.3482 0.2801 -0.1262 0.0347  -0.0109 314 LEU B CG    
4384 C CD1   . LEU B 173 ? 0.3967 0.3226 0.2627 -0.1239 0.0376  -0.0097 314 LEU B CD1   
4385 C CD2   . LEU B 173 ? 0.3729 0.3344 0.2660 -0.1147 0.0333  -0.0104 314 LEU B CD2   
4386 N N     . GLY B 174 ? 0.3243 0.3444 0.2542 -0.1418 0.0362  -0.0099 315 GLY B N     
4387 C CA    . GLY B 174 ? 0.3169 0.3531 0.2565 -0.1495 0.0385  -0.0102 315 GLY B CA    
4388 C C     . GLY B 174 ? 0.3389 0.3864 0.2891 -0.1430 0.0421  -0.0104 315 GLY B C     
4389 O O     . GLY B 174 ? 0.2886 0.3290 0.2363 -0.1332 0.0429  -0.0099 315 GLY B O     
4390 N N     . PRO B 175 ? 0.3002 0.3667 0.2631 -0.1485 0.0445  -0.0115 316 PRO B N     
4391 C CA    . PRO B 175 ? 0.2854 0.3632 0.2577 -0.1436 0.0487  -0.0127 316 PRO B CA    
4392 C C     . PRO B 175 ? 0.3187 0.4084 0.3075 -0.1316 0.0471  -0.0139 316 PRO B C     
4393 O O     . PRO B 175 ? 0.2844 0.3797 0.2787 -0.1262 0.0505  -0.0154 316 PRO B O     
4394 C CB    . PRO B 175 ? 0.3180 0.4145 0.3008 -0.1536 0.0516  -0.0143 316 PRO B CB    
4395 C CG    . PRO B 175 ? 0.3437 0.4460 0.3308 -0.1603 0.0472  -0.0139 316 PRO B CG    
4396 C CD    . PRO B 175 ? 0.2865 0.3652 0.2551 -0.1602 0.0437  -0.0121 316 PRO B CD    
4397 N N     . ARG B 176 ? 0.2922 0.3850 0.2881 -0.1274 0.0420  -0.0132 317 ARG B N     
4398 C CA    . ARG B 176 ? 0.2771 0.3794 0.2880 -0.1163 0.0401  -0.0136 317 ARG B CA    
4399 C C     . ARG B 176 ? 0.2756 0.3609 0.2754 -0.1080 0.0379  -0.0120 317 ARG B C     
4400 O O     . ARG B 176 ? 0.2459 0.3372 0.2566 -0.0992 0.0357  -0.0118 317 ARG B O     
4401 C CB    . ARG B 176 ? 0.2383 0.3598 0.2687 -0.1167 0.0358  -0.0133 317 ARG B CB    
4402 C CG    . ARG B 176 ? 0.2987 0.4401 0.3436 -0.1240 0.0380  -0.0152 317 ARG B CG    
4403 C CD    . ARG B 176 ? 0.3014 0.4535 0.3571 -0.1202 0.0438  -0.0186 317 ARG B CD    
4404 N NE    . ARG B 176 ? 0.3187 0.4756 0.3874 -0.1083 0.0428  -0.0194 317 ARG B NE    
4405 C CZ    . ARG B 176 ? 0.2993 0.4729 0.3902 -0.1035 0.0398  -0.0196 317 ARG B CZ    
4406 N NH1   . ARG B 176 ? 0.2947 0.4840 0.3989 -0.1090 0.0374  -0.0190 317 ARG B NH1   
4407 N NH2   . ARG B 176 ? 0.2173 0.3921 0.3179 -0.0930 0.0390  -0.0201 317 ARG B NH2   
4408 N N     . THR B 177 ? 0.2984 0.3626 0.2773 -0.1104 0.0384  -0.0109 318 THR B N     
4409 C CA    . THR B 177 ? 0.2737 0.3223 0.2424 -0.1024 0.0367  -0.0097 318 THR B CA    
4410 C C     . THR B 177 ? 0.2648 0.3105 0.2331 -0.0944 0.0398  -0.0100 318 THR B C     
4411 O O     . THR B 177 ? 0.3042 0.3415 0.2620 -0.0971 0.0433  -0.0098 318 THR B O     
4412 C CB    . THR B 177 ? 0.3223 0.3492 0.2702 -0.1072 0.0364  -0.0089 318 THR B CB    
4413 O OG1   . THR B 177 ? 0.3023 0.3323 0.2497 -0.1164 0.0338  -0.0093 318 THR B OG1   
4414 C CG2   . THR B 177 ? 0.2532 0.2667 0.1932 -0.0985 0.0346  -0.0084 318 THR B CG2   
4415 N N     . LYS B 178 ? 0.1998 0.2523 0.1788 -0.0851 0.0383  -0.0102 319 LYS B N     
4416 C CA    . LYS B 178 ? 0.2530 0.3032 0.2317 -0.0774 0.0407  -0.0108 319 LYS B CA    
4417 C C     . LYS B 178 ? 0.2557 0.2886 0.2210 -0.0709 0.0394  -0.0091 319 LYS B C     
4418 O O     . LYS B 178 ? 0.2233 0.2488 0.1815 -0.0669 0.0416  -0.0087 319 LYS B O     
4419 C CB    . LYS B 178 ? 0.2135 0.2812 0.2126 -0.0709 0.0402  -0.0124 319 LYS B CB    
4420 C CG    . LYS B 178 ? 0.2929 0.3787 0.3071 -0.0751 0.0430  -0.0152 319 LYS B CG    
4421 C CD    . LYS B 178 ? 0.3361 0.4231 0.3481 -0.0740 0.0480  -0.0175 319 LYS B CD    
4422 C CE    . LYS B 178 ? 0.3448 0.4518 0.3748 -0.0758 0.0512  -0.0216 319 LYS B CE    
4423 N NZ    . LYS B 178 ? 0.3504 0.4673 0.3970 -0.0670 0.0510  -0.0242 319 LYS B NZ    
4424 N N     . LEU B 179 ? 0.2263 0.2535 0.1882 -0.0699 0.0360  -0.0081 320 LEU B N     
4425 C CA    . LEU B 179 ? 0.2445 0.2579 0.1964 -0.0629 0.0350  -0.0072 320 LEU B CA    
4426 C C     . LEU B 179 ? 0.2569 0.2588 0.1976 -0.0667 0.0329  -0.0069 320 LEU B C     
4427 O O     . LEU B 179 ? 0.2752 0.2850 0.2213 -0.0713 0.0302  -0.0071 320 LEU B O     
4428 C CB    . LEU B 179 ? 0.2276 0.2507 0.1921 -0.0542 0.0331  -0.0070 320 LEU B CB    
4429 C CG    . LEU B 179 ? 0.2540 0.2661 0.2105 -0.0466 0.0321  -0.0062 320 LEU B CG    
4430 C CD1   . LEU B 179 ? 0.2616 0.2641 0.2096 -0.0424 0.0349  -0.0059 320 LEU B CD1   
4431 C CD2   . LEU B 179 ? 0.2672 0.2915 0.2380 -0.0406 0.0297  -0.0058 320 LEU B CD2   
4432 N N     . VAL B 180 ? 0.2528 0.2362 0.1781 -0.0645 0.0339  -0.0066 321 VAL B N     
4433 C CA    . VAL B 180 ? 0.2583 0.2292 0.1727 -0.0654 0.0324  -0.0074 321 VAL B CA    
4434 C C     . VAL B 180 ? 0.2721 0.2386 0.1853 -0.0551 0.0320  -0.0072 321 VAL B C     
4435 O O     . VAL B 180 ? 0.2897 0.2509 0.2005 -0.0491 0.0337  -0.0063 321 VAL B O     
4436 C CB    . VAL B 180 ? 0.3023 0.2540 0.2002 -0.0713 0.0343  -0.0078 321 VAL B CB    
4437 C CG1   . VAL B 180 ? 0.2864 0.2239 0.1729 -0.0710 0.0333  -0.0098 321 VAL B CG1   
4438 C CG2   . VAL B 180 ? 0.2574 0.2146 0.1567 -0.0825 0.0348  -0.0079 321 VAL B CG2   
4439 N N     . ALA B 181 ? 0.2598 0.2303 0.1753 -0.0534 0.0295  -0.0078 322 ALA B N     
4440 C CA    . ALA B 181 ? 0.2919 0.2589 0.2060 -0.0446 0.0293  -0.0079 322 ALA B CA    
4441 C C     . ALA B 181 ? 0.2842 0.2398 0.1863 -0.0466 0.0289  -0.0101 322 ALA B C     
4442 O O     . ALA B 181 ? 0.3256 0.2880 0.2293 -0.0516 0.0265  -0.0108 322 ALA B O     
4443 C CB    . ALA B 181 ? 0.2279 0.2123 0.1573 -0.0402 0.0269  -0.0065 322 ALA B CB    
4444 N N     . ALA B 182 ? 0.3183 0.2568 0.2085 -0.0427 0.0312  -0.0114 323 ALA B N     
4445 C CA    . ALA B 182 ? 0.3568 0.2817 0.2344 -0.0450 0.0318  -0.0147 323 ALA B CA    
4446 C C     . ALA B 182 ? 0.3307 0.2477 0.2040 -0.0355 0.0332  -0.0160 323 ALA B C     
4447 O O     . ALA B 182 ? 0.3634 0.2768 0.2379 -0.0283 0.0345  -0.0142 323 ALA B O     
4448 C CB    . ALA B 182 ? 0.3160 0.2239 0.1818 -0.0514 0.0336  -0.0158 323 ALA B CB    
4449 N N     . THR B 183 ? 0.3623 0.2777 0.2306 -0.0359 0.0331  -0.0192 324 THR B N     
4450 C CA    . THR B 183 ? 0.3373 0.2443 0.2006 -0.0275 0.0352  -0.0213 324 THR B CA    
4451 C C     . THR B 183 ? 0.3714 0.2561 0.2224 -0.0269 0.0380  -0.0238 324 THR B C     
4452 O O     . THR B 183 ? 0.4427 0.3175 0.2859 -0.0349 0.0383  -0.0257 324 THR B O     
4453 C CB    . THR B 183 ? 0.3916 0.3044 0.2529 -0.0286 0.0347  -0.0244 324 THR B CB    
4454 O OG1   . THR B 183 ? 0.4213 0.3301 0.2809 -0.0194 0.0370  -0.0262 324 THR B OG1   
4455 C CG2   . THR B 183 ? 0.3928 0.2953 0.2422 -0.0372 0.0353  -0.0291 324 THR B CG2   
4456 N N     . GLN B 184 ? 0.3804 0.2572 0.2303 -0.0173 0.0398  -0.0236 325 GLN B N     
4457 C CA    . GLN B 184 ? 0.4008 0.2555 0.2398 -0.0153 0.0424  -0.0260 325 GLN B CA    
4458 C C     . GLN B 184 ? 0.3969 0.2438 0.2285 -0.0145 0.0445  -0.0324 325 GLN B C     
4459 O O     . GLN B 184 ? 0.4448 0.2738 0.2660 -0.0179 0.0463  -0.0363 325 GLN B O     
4460 C CB    . GLN B 184 ? 0.3749 0.2240 0.2162 -0.0052 0.0431  -0.0227 325 GLN B CB    
4461 C CG    . GLN B 184 ? 0.4079 0.2329 0.2389 -0.0034 0.0451  -0.0238 325 GLN B CG    
4462 C CD    . GLN B 184 ? 0.4159 0.2362 0.2492 0.0048  0.0447  -0.0187 325 GLN B CD    
4463 O OE1   . GLN B 184 ? 0.3783 0.2134 0.2206 0.0100  0.0435  -0.0154 325 GLN B OE1   
4464 N NE2   . GLN B 184 ? 0.4473 0.2469 0.2726 0.0058  0.0456  -0.0178 325 GLN B NE2   
4465 N N     . VAL B 185 ? 0.4012 0.2610 0.2376 -0.0102 0.0446  -0.0339 326 VAL B N     
4466 C CA    . VAL B 185 ? 0.3681 0.2238 0.1977 -0.0102 0.0469  -0.0405 326 VAL B CA    
4467 C C     . VAL B 185 ? 0.4114 0.2871 0.2457 -0.0145 0.0449  -0.0404 326 VAL B C     
4468 O O     . VAL B 185 ? 0.3304 0.2219 0.1750 -0.0102 0.0432  -0.0363 326 VAL B O     
4469 C CB    . VAL B 185 ? 0.3603 0.2092 0.1899 0.0014  0.0500  -0.0428 326 VAL B CB    
4470 C CG1   . VAL B 185 ? 0.4197 0.2682 0.2432 0.0011  0.0530  -0.0503 326 VAL B CG1   
4471 C CG2   . VAL B 185 ? 0.4098 0.2374 0.2344 0.0055  0.0516  -0.0425 326 VAL B CG2   
4472 N N     . SER B 186 ? 0.3861 0.2609 0.2126 -0.0232 0.0449  -0.0448 327 SER B N     
4473 C CA    . SER B 186 ? 0.3914 0.2847 0.2211 -0.0283 0.0424  -0.0442 327 SER B CA    
4474 C C     . SER B 186 ? 0.4301 0.3295 0.2599 -0.0218 0.0447  -0.0470 327 SER B C     
4475 O O     . SER B 186 ? 0.4175 0.3052 0.2385 -0.0194 0.0488  -0.0537 327 SER B O     
4476 C CB    . SER B 186 ? 0.4005 0.2908 0.2207 -0.0402 0.0415  -0.0482 327 SER B CB    
4477 O OG    . SER B 186 ? 0.3947 0.3005 0.2149 -0.0445 0.0398  -0.0487 327 SER B OG    
4478 N N     . ASN B 187 ? 0.3630 0.2806 0.2031 -0.0190 0.0424  -0.0421 328 ASN B N     
4479 C CA    . ASN B 187 ? 0.3967 0.3219 0.2374 -0.0136 0.0446  -0.0442 328 ASN B CA    
4480 C C     . ASN B 187 ? 0.3930 0.3229 0.2246 -0.0210 0.0452  -0.0489 328 ASN B C     
4481 O O     . ASN B 187 ? 0.4031 0.3358 0.2317 -0.0174 0.0484  -0.0528 328 ASN B O     
4482 C CB    . ASN B 187 ? 0.3469 0.2898 0.2010 -0.0095 0.0418  -0.0374 328 ASN B CB    
4483 C CG    . ASN B 187 ? 0.4144 0.3728 0.2732 -0.0177 0.0370  -0.0329 328 ASN B CG    
4484 O OD1   . ASN B 187 ? 0.4067 0.3644 0.2665 -0.0241 0.0342  -0.0308 328 ASN B OD1   
4485 N ND2   . ASN B 187 ? 0.3760 0.3489 0.2382 -0.0179 0.0360  -0.0309 328 ASN B ND2   
4486 N N     . ALA B 188 ? 0.3778 0.3103 0.2053 -0.0317 0.0421  -0.0486 329 ALA B N     
4487 C CA    . ALA B 188 ? 0.4135 0.3517 0.2315 -0.0399 0.0422  -0.0528 329 ALA B CA    
4488 C C     . ALA B 188 ? 0.4782 0.3987 0.2815 -0.0444 0.0460  -0.0619 329 ALA B C     
4489 O O     . ALA B 188 ? 0.4544 0.3759 0.2481 -0.0477 0.0486  -0.0683 329 ALA B O     
4490 C CB    . ALA B 188 ? 0.3612 0.3146 0.1831 -0.0496 0.0360  -0.0470 329 ALA B CB    
4491 N N     . LEU B 189 ? 0.4382 0.3426 0.2393 -0.0451 0.0464  -0.0629 330 LEU B N     
4492 C CA    . LEU B 189 ? 0.4550 0.3409 0.2427 -0.0502 0.0496  -0.0713 330 LEU B CA    
4493 C C     . LEU B 189 ? 0.4509 0.3155 0.2362 -0.0411 0.0544  -0.0754 330 LEU B C     
4494 O O     . LEU B 189 ? 0.4827 0.3307 0.2569 -0.0433 0.0582  -0.0837 330 LEU B O     
4495 C CB    . LEU B 189 ? 0.4525 0.3353 0.2378 -0.0610 0.0459  -0.0694 330 LEU B CB    
4496 C CG    . LEU B 189 ? 0.4507 0.3522 0.2372 -0.0719 0.0406  -0.0659 330 LEU B CG    
4497 C CD1   . LEU B 189 ? 0.4679 0.3628 0.2503 -0.0824 0.0382  -0.0662 330 LEU B CD1   
4498 C CD2   . LEU B 189 ? 0.4918 0.3999 0.2685 -0.0765 0.0420  -0.0718 330 LEU B CD2   
4499 N N     . GLY B 190 ? 0.4199 0.2843 0.2153 -0.0311 0.0542  -0.0697 331 GLY B N     
4500 C CA    . GLY B 190 ? 0.4698 0.3146 0.2641 -0.0225 0.0576  -0.0718 331 GLY B CA    
4501 C C     . GLY B 190 ? 0.4516 0.2796 0.2424 -0.0267 0.0566  -0.0702 331 GLY B C     
4502 O O     . GLY B 190 ? 0.4780 0.2887 0.2678 -0.0197 0.0589  -0.0708 331 GLY B O     
4503 N N     . THR B 191 ? 0.4308 0.2638 0.2202 -0.0377 0.0530  -0.0678 332 THR B N     
4504 C CA    . THR B 191 ? 0.4973 0.3152 0.2830 -0.0429 0.0522  -0.0663 332 THR B CA    
4505 C C     . THR B 191 ? 0.4743 0.2887 0.2681 -0.0348 0.0515  -0.0593 332 THR B C     
4506 O O     . THR B 191 ? 0.4187 0.2497 0.2233 -0.0306 0.0492  -0.0532 332 THR B O     
4507 C CB    . THR B 191 ? 0.5035 0.3326 0.2896 -0.0555 0.0481  -0.0636 332 THR B CB    
4508 O OG1   . THR B 191 ? 0.4804 0.3145 0.2587 -0.0639 0.0480  -0.0695 332 THR B OG1   
4509 C CG2   . THR B 191 ? 0.4967 0.3102 0.2785 -0.0617 0.0477  -0.0623 332 THR B CG2   
4510 N N     . VAL B 192 ? 0.4891 0.2816 0.2774 -0.0328 0.0535  -0.0602 333 VAL B N     
4511 C CA    . VAL B 192 ? 0.4780 0.2651 0.2714 -0.0275 0.0525  -0.0532 333 VAL B CA    
4512 C C     . VAL B 192 ? 0.4997 0.2850 0.2910 -0.0384 0.0501  -0.0497 333 VAL B C     
4513 O O     . VAL B 192 ? 0.5538 0.3247 0.3356 -0.0467 0.0510  -0.0537 333 VAL B O     
4514 C CB    . VAL B 192 ? 0.5320 0.2964 0.3210 -0.0188 0.0556  -0.0551 333 VAL B CB    
4515 C CG1   . VAL B 192 ? 0.5067 0.2666 0.3003 -0.0139 0.0539  -0.0469 333 VAL B CG1   
4516 C CG2   . VAL B 192 ? 0.4903 0.2578 0.2819 -0.0082 0.0584  -0.0595 333 VAL B CG2   
4517 N N     . THR B 193 ? 0.4633 0.2639 0.2640 -0.0388 0.0473  -0.0428 334 THR B N     
4518 C CA    . THR B 193 ? 0.4687 0.2698 0.2685 -0.0491 0.0454  -0.0396 334 THR B CA    
4519 C C     . THR B 193 ? 0.4867 0.2728 0.2843 -0.0469 0.0460  -0.0350 334 THR B C     
4520 O O     . THR B 193 ? 0.4846 0.2669 0.2851 -0.0365 0.0467  -0.0322 334 THR B O     
4521 C CB    . THR B 193 ? 0.4333 0.2596 0.2448 -0.0519 0.0422  -0.0352 334 THR B CB    
4522 O OG1   . THR B 193 ? 0.4293 0.2633 0.2499 -0.0427 0.0419  -0.0300 334 THR B OG1   
4523 C CG2   . THR B 193 ? 0.4407 0.2823 0.2550 -0.0531 0.0411  -0.0384 334 THR B CG2   
4524 N N     . PRO B 194 ? 0.4989 0.2766 0.2911 -0.0570 0.0456  -0.0338 335 PRO B N     
4525 C CA    . PRO B 194 ? 0.4923 0.2555 0.2812 -0.0563 0.0460  -0.0286 335 PRO B CA    
4526 C C     . PRO B 194 ? 0.5184 0.2983 0.3169 -0.0546 0.0443  -0.0217 335 PRO B C     
4527 O O     . PRO B 194 ? 0.4764 0.2634 0.2764 -0.0634 0.0434  -0.0189 335 PRO B O     
4528 C CB    . PRO B 194 ? 0.5253 0.2758 0.3049 -0.0694 0.0463  -0.0306 335 PRO B CB    
4529 C CG    . PRO B 194 ? 0.5013 0.2716 0.2854 -0.0779 0.0446  -0.0331 335 PRO B CG    
4530 C CD    . PRO B 194 ? 0.5129 0.2945 0.3015 -0.0702 0.0445  -0.0368 335 PRO B CD    
4531 N N     . VAL B 195 ? 0.4795 0.2663 0.2846 -0.0432 0.0442  -0.0192 336 VAL B N     
4532 C CA    . VAL B 195 ? 0.4990 0.3046 0.3142 -0.0413 0.0427  -0.0141 336 VAL B CA    
4533 C C     . VAL B 195 ? 0.4674 0.2662 0.2792 -0.0453 0.0427  -0.0085 336 VAL B C     
4534 O O     . VAL B 195 ? 0.4425 0.2568 0.2607 -0.0495 0.0420  -0.0057 336 VAL B O     
4535 C CB    . VAL B 195 ? 0.4794 0.2933 0.3020 -0.0287 0.0425  -0.0130 336 VAL B CB    
4536 C CG1   . VAL B 195 ? 0.4317 0.2599 0.2603 -0.0269 0.0421  -0.0172 336 VAL B CG1   
4537 C CG2   . VAL B 195 ? 0.5359 0.3302 0.3521 -0.0202 0.0437  -0.0126 336 VAL B CG2   
4538 N N     . GLU B 196 ? 0.5043 0.2805 0.3064 -0.0442 0.0436  -0.0068 337 GLU B N     
4539 C CA    . GLU B 196 ? 0.4988 0.2685 0.2965 -0.0494 0.0434  -0.0008 337 GLU B CA    
4540 C C     . GLU B 196 ? 0.5172 0.2924 0.3135 -0.0633 0.0436  -0.0014 337 GLU B C     
4541 O O     . GLU B 196 ? 0.5228 0.3099 0.3227 -0.0681 0.0434  0.0024  337 GLU B O     
4542 C CB    . GLU B 196 ? 0.5888 0.3311 0.3758 -0.0467 0.0439  0.0015  337 GLU B CB    
4543 C CG    . GLU B 196 ? 0.6176 0.3552 0.4069 -0.0327 0.0434  0.0035  337 GLU B CG    
4544 C CD    . GLU B 196 ? 0.7467 0.4788 0.5367 -0.0255 0.0446  -0.0033 337 GLU B CD    
4545 O OE1   . GLU B 196 ? 0.7386 0.4721 0.5270 -0.0317 0.0456  -0.0096 337 GLU B OE1   
4546 O OE2   . GLU B 196 ? 0.7694 0.4968 0.5616 -0.0140 0.0445  -0.0023 337 GLU B OE2   
4547 N N     . THR B 197 ? 0.5047 0.2727 0.2961 -0.0701 0.0440  -0.0067 338 THR B N     
4548 C CA    . THR B 197 ? 0.5084 0.2834 0.2995 -0.0836 0.0439  -0.0076 338 THR B CA    
4549 C C     . THR B 197 ? 0.4918 0.2953 0.2961 -0.0848 0.0428  -0.0077 338 THR B C     
4550 O O     . THR B 197 ? 0.4892 0.3039 0.2972 -0.0927 0.0429  -0.0054 338 THR B O     
4551 C CB    . THR B 197 ? 0.5080 0.2712 0.2916 -0.0902 0.0442  -0.0139 338 THR B CB    
4552 O OG1   . THR B 197 ? 0.5917 0.3273 0.3643 -0.0873 0.0455  -0.0145 338 THR B OG1   
4553 C CG2   . THR B 197 ? 0.5076 0.2757 0.2897 -0.1050 0.0439  -0.0142 338 THR B CG2   
4554 N N     . ILE B 198 ? 0.4594 0.2751 0.2714 -0.0770 0.0419  -0.0104 339 ILE B N     
4555 C CA    . ILE B 198 ? 0.4169 0.2587 0.2424 -0.0775 0.0405  -0.0104 339 ILE B CA    
4556 C C     . ILE B 198 ? 0.3986 0.2519 0.2313 -0.0751 0.0409  -0.0058 339 ILE B C     
4557 O O     . ILE B 198 ? 0.4211 0.2904 0.2616 -0.0814 0.0408  -0.0050 339 ILE B O     
4558 C CB    . ILE B 198 ? 0.4260 0.2763 0.2574 -0.0691 0.0394  -0.0132 339 ILE B CB    
4559 C CG1   . ILE B 198 ? 0.4380 0.2800 0.2620 -0.0734 0.0392  -0.0185 339 ILE B CG1   
4560 C CG2   . ILE B 198 ? 0.3480 0.2239 0.1943 -0.0682 0.0377  -0.0123 339 ILE B CG2   
4561 C CD1   . ILE B 198 ? 0.4734 0.3209 0.3005 -0.0651 0.0387  -0.0214 339 ILE B CD1   
4562 N N     . VAL B 199 ? 0.3979 0.2435 0.2282 -0.0663 0.0415  -0.0029 340 VAL B N     
4563 C CA    . VAL B 199 ? 0.3916 0.2475 0.2273 -0.0643 0.0419  0.0012  340 VAL B CA    
4564 C C     . VAL B 199 ? 0.4059 0.2588 0.2364 -0.0750 0.0432  0.0039  340 VAL B C     
4565 O O     . VAL B 199 ? 0.4107 0.2807 0.2490 -0.0791 0.0439  0.0047  340 VAL B O     
4566 C CB    . VAL B 199 ? 0.4037 0.2506 0.2362 -0.0536 0.0419  0.0042  340 VAL B CB    
4567 C CG1   . VAL B 199 ? 0.3867 0.2421 0.2216 -0.0535 0.0424  0.0087  340 VAL B CG1   
4568 C CG2   . VAL B 199 ? 0.3749 0.2293 0.2147 -0.0434 0.0409  0.0017  340 VAL B CG2   
4569 N N     . GLU B 200 ? 0.4384 0.2696 0.2559 -0.0797 0.0437  0.0053  341 GLU B N     
4570 C CA    . GLU B 200 ? 0.4625 0.2898 0.2740 -0.0904 0.0450  0.0086  341 GLU B CA    
4571 C C     . GLU B 200 ? 0.4393 0.2827 0.2575 -0.1011 0.0454  0.0057  341 GLU B C     
4572 O O     . GLU B 200 ? 0.4613 0.3166 0.2830 -0.1076 0.0467  0.0077  341 GLU B O     
4573 C CB    . GLU B 200 ? 0.4769 0.2763 0.2737 -0.0939 0.0452  0.0104  341 GLU B CB    
4574 C CG    . GLU B 200 ? 0.6224 0.4144 0.4110 -0.1043 0.0464  0.0154  341 GLU B CG    
4575 C CD    . GLU B 200 ? 0.7462 0.5475 0.5364 -0.1182 0.0474  0.0132  341 GLU B CD    
4576 O OE1   . GLU B 200 ? 0.7495 0.5585 0.5394 -0.1262 0.0488  0.0166  341 GLU B OE1   
4577 O OE2   . GLU B 200 ? 0.7240 0.5259 0.5158 -0.1215 0.0467  0.0080  341 GLU B OE2   
4578 N N     . LEU B 201 ? 0.4438 0.2889 0.2643 -0.1031 0.0442  0.0011  342 LEU B N     
4579 C CA    . LEU B 201 ? 0.4131 0.2744 0.2407 -0.1130 0.0439  -0.0014 342 LEU B CA    
4580 C C     . LEU B 201 ? 0.4088 0.2968 0.2528 -0.1097 0.0437  -0.0014 342 LEU B C     
4581 O O     . LEU B 201 ? 0.3856 0.2878 0.2360 -0.1172 0.0448  -0.0010 342 LEU B O     
4582 C CB    . LEU B 201 ? 0.3846 0.2423 0.2105 -0.1151 0.0421  -0.0061 342 LEU B CB    
4583 C CG    . LEU B 201 ? 0.5161 0.3519 0.3277 -0.1242 0.0426  -0.0075 342 LEU B CG    
4584 C CD1   . LEU B 201 ? 0.4794 0.3100 0.2878 -0.1241 0.0411  -0.0129 342 LEU B CD1   
4585 C CD2   . LEU B 201 ? 0.5242 0.3652 0.3353 -0.1382 0.0433  -0.0064 342 LEU B CD2   
4586 N N     . GLY B 202 ? 0.3988 0.2939 0.2501 -0.0987 0.0426  -0.0023 343 GLY B N     
4587 C CA    . GLY B 202 ? 0.3613 0.2800 0.2285 -0.0952 0.0424  -0.0025 343 GLY B CA    
4588 C C     . GLY B 202 ? 0.3670 0.2921 0.2359 -0.0969 0.0450  0.0000  343 GLY B C     
4589 O O     . GLY B 202 ? 0.3584 0.3021 0.2384 -0.1011 0.0460  -0.0009 343 GLY B O     
4590 N N     . HIS B 203 ? 0.3629 0.2729 0.2209 -0.0937 0.0460  0.0032  344 HIS B N     
4591 C CA    . HIS B 203 ? 0.4142 0.3297 0.2716 -0.0959 0.0484  0.0060  344 HIS B CA    
4592 C C     . HIS B 203 ? 0.4067 0.3247 0.2613 -0.1090 0.0504  0.0067  344 HIS B C     
4593 O O     . HIS B 203 ? 0.4111 0.3455 0.2727 -0.1129 0.0527  0.0064  344 HIS B O     
4594 C CB    . HIS B 203 ? 0.3703 0.2677 0.2153 -0.0904 0.0483  0.0104  344 HIS B CB    
4595 C CG    . HIS B 203 ? 0.4140 0.3151 0.2642 -0.0779 0.0471  0.0102  344 HIS B CG    
4596 N ND1   . HIS B 203 ? 0.4026 0.2887 0.2440 -0.0707 0.0462  0.0137  344 HIS B ND1   
4597 C CD2   . HIS B 203 ? 0.3696 0.2879 0.2335 -0.0715 0.0464  0.0071  344 HIS B CD2   
4598 C CE1   . HIS B 203 ? 0.4059 0.3008 0.2552 -0.0608 0.0451  0.0125  344 HIS B CE1   
4599 N NE2   . HIS B 203 ? 0.4109 0.3248 0.2736 -0.0612 0.0453  0.0086  344 HIS B NE2   
4600 N N     . ARG B 204 ? 0.3907 0.2930 0.2352 -0.1162 0.0498  0.0070  345 ARG B N     
4601 C CA    . ARG B 204 ? 0.4511 0.3555 0.2925 -0.1296 0.0516  0.0077  345 ARG B CA    
4602 C C     . ARG B 204 ? 0.4330 0.3633 0.2906 -0.1342 0.0522  0.0040  345 ARG B C     
4603 O O     . ARG B 204 ? 0.3985 0.3406 0.2594 -0.1425 0.0548  0.0044  345 ARG B O     
4604 C CB    . ARG B 204 ? 0.4942 0.3774 0.3231 -0.1365 0.0505  0.0077  345 ARG B CB    
4605 C CG    . ARG B 204 ? 0.5958 0.4821 0.4224 -0.1514 0.0520  0.0079  345 ARG B CG    
4606 C CD    . ARG B 204 ? 0.6555 0.5214 0.4708 -0.1584 0.0507  0.0068  345 ARG B CD    
4607 N NE    . ARG B 204 ? 0.7000 0.5384 0.5013 -0.1529 0.0502  0.0094  345 ARG B NE    
4608 C CZ    . ARG B 204 ? 0.7734 0.5911 0.5652 -0.1540 0.0489  0.0073  345 ARG B CZ    
4609 N NH1   . ARG B 204 ? 0.7071 0.5279 0.5004 -0.1614 0.0479  0.0027  345 ARG B NH1   
4610 N NH2   . ARG B 204 ? 0.8350 0.6286 0.6159 -0.1476 0.0486  0.0097  345 ARG B NH2   
4611 N N     . TYR B 205 ? 0.3899 0.3301 0.2584 -0.1287 0.0497  0.0007  346 TYR B N     
4612 C CA    . TYR B 205 ? 0.3627 0.3270 0.2478 -0.1321 0.0494  -0.0022 346 TYR B CA    
4613 C C     . TYR B 205 ? 0.4085 0.3924 0.3088 -0.1244 0.0506  -0.0034 346 TYR B C     
4614 O O     . TYR B 205 ? 0.3965 0.4010 0.3131 -0.1253 0.0502  -0.0059 346 TYR B O     
4615 C CB    . TYR B 205 ? 0.3853 0.3505 0.2741 -0.1318 0.0457  -0.0046 346 TYR B CB    
4616 C CG    . TYR B 205 ? 0.4214 0.3740 0.2990 -0.1428 0.0450  -0.0049 346 TYR B CG    
4617 C CD1   . TYR B 205 ? 0.4138 0.3406 0.2744 -0.1427 0.0446  -0.0042 346 TYR B CD1   
4618 C CD2   . TYR B 205 ? 0.4396 0.4063 0.3241 -0.1537 0.0448  -0.0061 346 TYR B CD2   
4619 C CE1   . TYR B 205 ? 0.4580 0.3721 0.3082 -0.1532 0.0442  -0.0051 346 TYR B CE1   
4620 C CE2   . TYR B 205 ? 0.4225 0.3778 0.2966 -0.1647 0.0441  -0.0067 346 TYR B CE2   
4621 C CZ    . TYR B 205 ? 0.4947 0.4231 0.3512 -0.1646 0.0439  -0.0063 346 TYR B CZ    
4622 O OH    . TYR B 205 ? 0.5112 0.4270 0.3570 -0.1757 0.0433  -0.0074 346 TYR B OH    
4623 N N     . GLY B 206 ? 0.3878 0.3662 0.2839 -0.1170 0.0518  -0.0018 347 GLY B N     
4624 C CA    . GLY B 206 ? 0.3482 0.3440 0.2571 -0.1109 0.0535  -0.0034 347 GLY B CA    
4625 C C     . GLY B 206 ? 0.3906 0.3912 0.3091 -0.0993 0.0510  -0.0049 347 GLY B C     
4626 O O     . GLY B 206 ? 0.3420 0.3588 0.2740 -0.0947 0.0521  -0.0070 347 GLY B O     
4627 N N     . ALA B 207 ? 0.3131 0.3004 0.2254 -0.0945 0.0479  -0.0041 348 ALA B N     
4628 C CA    . ALA B 207 ? 0.3248 0.3170 0.2459 -0.0843 0.0455  -0.0052 348 ALA B CA    
4629 C C     . ALA B 207 ? 0.2750 0.2549 0.1875 -0.0756 0.0455  -0.0034 348 ALA B C     
4630 O O     . ALA B 207 ? 0.3318 0.2941 0.2294 -0.0767 0.0461  -0.0009 348 ALA B O     
4631 C CB    . ALA B 207 ? 0.2818 0.2707 0.2031 -0.0847 0.0420  -0.0058 348 ALA B CB    
4632 N N     . ARG B 208 ? 0.2604 0.2495 0.1831 -0.0668 0.0447  -0.0044 349 ARG B N     
4633 C CA    . ARG B 208 ? 0.2671 0.2454 0.1833 -0.0578 0.0436  -0.0030 349 ARG B CA    
4634 C C     . ARG B 208 ? 0.2759 0.2434 0.1869 -0.0556 0.0410  -0.0030 349 ARG B C     
4635 O O     . ARG B 208 ? 0.2589 0.2316 0.1747 -0.0596 0.0394  -0.0044 349 ARG B O     
4636 C CB    . ARG B 208 ? 0.2354 0.2270 0.1643 -0.0499 0.0434  -0.0043 349 ARG B CB    
4637 C CG    . ARG B 208 ? 0.3469 0.3504 0.2816 -0.0516 0.0463  -0.0055 349 ARG B CG    
4638 C CD    . ARG B 208 ? 0.3475 0.3419 0.2711 -0.0486 0.0473  -0.0032 349 ARG B CD    
4639 N NE    . ARG B 208 ? 0.3560 0.3627 0.2847 -0.0493 0.0500  -0.0048 349 ARG B NE    
4640 C CZ    . ARG B 208 ? 0.3795 0.3808 0.2977 -0.0494 0.0512  -0.0025 349 ARG B CZ    
4641 N NH1   . ARG B 208 ? 0.3364 0.3203 0.2401 -0.0478 0.0497  0.0020  349 ARG B NH1   
4642 N NH2   . ARG B 208 ? 0.3574 0.3713 0.2800 -0.0513 0.0540  -0.0047 349 ARG B NH2   
4643 N N     . VAL B 209 ? 0.2717 0.2247 0.1730 -0.0493 0.0405  -0.0016 350 VAL B N     
4644 C CA    . VAL B 209 ? 0.2514 0.1935 0.1467 -0.0469 0.0388  -0.0024 350 VAL B CA    
4645 C C     . VAL B 209 ? 0.2701 0.2122 0.1679 -0.0362 0.0379  -0.0022 350 VAL B C     
4646 O O     . VAL B 209 ? 0.2709 0.2078 0.1648 -0.0309 0.0386  -0.0003 350 VAL B O     
4647 C CB    . VAL B 209 ? 0.3105 0.2315 0.1898 -0.0511 0.0396  -0.0015 350 VAL B CB    
4648 C CG1   . VAL B 209 ? 0.3060 0.2167 0.1796 -0.0494 0.0384  -0.0038 350 VAL B CG1   
4649 C CG2   . VAL B 209 ? 0.3101 0.2313 0.1866 -0.0626 0.0407  -0.0013 350 VAL B CG2   
4650 N N     . LEU B 210 ? 0.2474 0.1967 0.1520 -0.0335 0.0361  -0.0038 351 LEU B N     
4651 C CA    . LEU B 210 ? 0.2884 0.2378 0.1950 -0.0244 0.0352  -0.0039 351 LEU B CA    
4652 C C     . LEU B 210 ? 0.2819 0.2180 0.1784 -0.0239 0.0350  -0.0054 351 LEU B C     
4653 O O     . LEU B 210 ? 0.2938 0.2293 0.1881 -0.0304 0.0342  -0.0071 351 LEU B O     
4654 C CB    . LEU B 210 ? 0.2165 0.1839 0.1382 -0.0219 0.0335  -0.0044 351 LEU B CB    
4655 C CG    . LEU B 210 ? 0.2445 0.2143 0.1694 -0.0140 0.0323  -0.0045 351 LEU B CG    
4656 C CD1   . LEU B 210 ? 0.2115 0.1974 0.1514 -0.0103 0.0313  -0.0039 351 LEU B CD1   
4657 C CD2   . LEU B 210 ? 0.2830 0.2513 0.2050 -0.0162 0.0308  -0.0057 351 LEU B CD2   
4658 N N     . ILE B 211 ? 0.2865 0.2128 0.1773 -0.0164 0.0357  -0.0052 352 ILE B N     
4659 C CA    . ILE B 211 ? 0.3063 0.2194 0.1878 -0.0145 0.0362  -0.0075 352 ILE B CA    
4660 C C     . ILE B 211 ? 0.2935 0.2147 0.1811 -0.0067 0.0356  -0.0083 352 ILE B C     
4661 O O     . ILE B 211 ? 0.2901 0.2161 0.1828 0.0004  0.0355  -0.0065 352 ILE B O     
4662 C CB    . ILE B 211 ? 0.3074 0.2008 0.1773 -0.0120 0.0378  -0.0065 352 ILE B CB    
4663 C CG1   . ILE B 211 ? 0.3561 0.2414 0.2195 -0.0209 0.0383  -0.0052 352 ILE B CG1   
4664 C CG2   . ILE B 211 ? 0.2891 0.1686 0.1506 -0.0090 0.0388  -0.0099 352 ILE B CG2   
4665 C CD1   . ILE B 211 ? 0.3148 0.1985 0.1748 -0.0304 0.0381  -0.0082 352 ILE B CD1   
4666 N N     . ASP B 212 ? 0.2986 0.2225 0.1856 -0.0089 0.0350  -0.0108 353 ASP B N     
4667 C CA    . ASP B 212 ? 0.3102 0.2404 0.2007 -0.0029 0.0348  -0.0119 353 ASP B CA    
4668 C C     . ASP B 212 ? 0.3136 0.2286 0.1943 0.0026  0.0371  -0.0144 353 ASP B C     
4669 O O     . ASP B 212 ? 0.2980 0.2025 0.1695 -0.0009 0.0383  -0.0179 353 ASP B O     
4670 C CB    . ASP B 212 ? 0.3386 0.2784 0.2315 -0.0085 0.0330  -0.0132 353 ASP B CB    
4671 C CG    . ASP B 212 ? 0.3543 0.3025 0.2511 -0.0034 0.0327  -0.0136 353 ASP B CG    
4672 O OD1   . ASP B 212 ? 0.3465 0.2913 0.2426 0.0046  0.0344  -0.0141 353 ASP B OD1   
4673 O OD2   . ASP B 212 ? 0.3356 0.2945 0.2362 -0.0078 0.0306  -0.0133 353 ASP B OD2   
4674 N N     . GLY B 213 ? 0.3276 0.2414 0.2105 0.0113  0.0378  -0.0129 354 GLY B N     
4675 C CA    . GLY B 213 ? 0.3161 0.2165 0.1920 0.0180  0.0399  -0.0148 354 GLY B CA    
4676 C C     . GLY B 213 ? 0.2976 0.2048 0.1769 0.0246  0.0409  -0.0170 354 GLY B C     
4677 O O     . GLY B 213 ? 0.3143 0.2130 0.1908 0.0321  0.0427  -0.0181 354 GLY B O     
4678 N N     . ALA B 214 ? 0.2813 0.2036 0.1669 0.0222  0.0398  -0.0172 355 ALA B N     
4679 C CA    . ALA B 214 ? 0.3255 0.2560 0.2147 0.0280  0.0407  -0.0187 355 ALA B CA    
4680 C C     . ALA B 214 ? 0.3437 0.2624 0.2236 0.0304  0.0440  -0.0240 355 ALA B C     
4681 O O     . ALA B 214 ? 0.3088 0.2298 0.1905 0.0377  0.0459  -0.0256 355 ALA B O     
4682 C CB    . ALA B 214 ? 0.2942 0.2413 0.1901 0.0233  0.0387  -0.0177 355 ALA B CB    
4683 N N     . GLN B 215 ? 0.3351 0.2416 0.2052 0.0242  0.0450  -0.0273 356 GLN B N     
4684 C CA    . GLN B 215 ? 0.3811 0.2753 0.2420 0.0257  0.0484  -0.0335 356 GLN B CA    
4685 C C     . GLN B 215 ? 0.3824 0.2552 0.2359 0.0282  0.0501  -0.0347 356 GLN B C     
4686 O O     . GLN B 215 ? 0.4247 0.2849 0.2712 0.0306  0.0533  -0.0402 356 GLN B O     
4687 C CB    . GLN B 215 ? 0.3505 0.2466 0.2047 0.0161  0.0484  -0.0374 356 GLN B CB    
4688 C CG    . GLN B 215 ? 0.5310 0.4260 0.3794 0.0176  0.0519  -0.0439 356 GLN B CG    
4689 C CD    . GLN B 215 ? 0.5063 0.4183 0.3626 0.0228  0.0522  -0.0427 356 GLN B CD    
4690 O OE1   . GLN B 215 ? 0.5439 0.4541 0.4007 0.0307  0.0555  -0.0458 356 GLN B OE1   
4691 N NE2   . GLN B 215 ? 0.4759 0.4047 0.3396 0.0186  0.0486  -0.0378 356 GLN B NE2   
4692 N N     . SER B 216 ? 0.3704 0.2386 0.2253 0.0275  0.0481  -0.0298 357 SER B N     
4693 C CA    . SER B 216 ? 0.3480 0.1956 0.1961 0.0301  0.0492  -0.0296 357 SER B CA    
4694 C C     . SER B 216 ? 0.3881 0.2343 0.2413 0.0414  0.0493  -0.0266 357 SER B C     
4695 O O     . SER B 216 ? 0.4459 0.2768 0.2950 0.0474  0.0513  -0.0287 357 SER B O     
4696 C CB    . SER B 216 ? 0.3912 0.2332 0.2362 0.0220  0.0471  -0.0258 357 SER B CB    
4697 O OG    . SER B 216 ? 0.3191 0.1745 0.1724 0.0223  0.0446  -0.0199 357 SER B OG    
4698 N N     . ILE B 217 ? 0.3631 0.2251 0.2257 0.0446  0.0472  -0.0219 358 ILE B N     
4699 C CA    . ILE B 217 ? 0.3678 0.2301 0.2354 0.0547  0.0467  -0.0185 358 ILE B CA    
4700 C C     . ILE B 217 ? 0.3795 0.2398 0.2488 0.0641  0.0493  -0.0224 358 ILE B C     
4701 O O     . ILE B 217 ? 0.3770 0.2284 0.2469 0.0722  0.0494  -0.0204 358 ILE B O     
4702 C CB    . ILE B 217 ? 0.3587 0.2398 0.2361 0.0553  0.0439  -0.0137 358 ILE B CB    
4703 C CG1   . ILE B 217 ? 0.3815 0.2594 0.2611 0.0624  0.0424  -0.0086 358 ILE B CG1   
4704 C CG2   . ILE B 217 ? 0.3504 0.2495 0.2360 0.0575  0.0443  -0.0156 358 ILE B CG2   
4705 C CD1   . ILE B 217 ? 0.3986 0.2944 0.2876 0.0641  0.0401  -0.0048 358 ILE B CD1   
4706 N N     . PRO B 218 ? 0.3929 0.2606 0.2628 0.0638  0.0517  -0.0278 359 PRO B N     
4707 C CA    . PRO B 218 ? 0.4070 0.2717 0.2782 0.0730  0.0550  -0.0322 359 PRO B CA    
4708 C C     . PRO B 218 ? 0.4276 0.2703 0.2897 0.0740  0.0581  -0.0375 359 PRO B C     
4709 O O     . PRO B 218 ? 0.4202 0.2582 0.2840 0.0826  0.0611  -0.0415 359 PRO B O     
4710 C CB    . PRO B 218 ? 0.3708 0.2527 0.2453 0.0709  0.0566  -0.0359 359 PRO B CB    
4711 C CG    . PRO B 218 ? 0.4007 0.2931 0.2755 0.0606  0.0537  -0.0332 359 PRO B CG    
4712 C CD    . PRO B 218 ? 0.3987 0.2780 0.2682 0.0553  0.0517  -0.0303 359 PRO B CD    
4713 N N     . HIS B 219 ? 0.4186 0.2478 0.2719 0.0655  0.0576  -0.0381 360 HIS B N     
4714 C CA    . HIS B 219 ? 0.4507 0.2599 0.2946 0.0640  0.0609  -0.0447 360 HIS B CA    
4715 C C     . HIS B 219 ? 0.4868 0.2737 0.3243 0.0627  0.0598  -0.0418 360 HIS B C     
4716 O O     . HIS B 219 ? 0.5098 0.2777 0.3398 0.0621  0.0625  -0.0474 360 HIS B O     
4717 C CB    . HIS B 219 ? 0.4328 0.2458 0.2698 0.0530  0.0620  -0.0502 360 HIS B CB    
4718 C CG    . HIS B 219 ? 0.4679 0.3005 0.3093 0.0535  0.0635  -0.0535 360 HIS B CG    
4719 N ND1   . HIS B 219 ? 0.4930 0.3282 0.3375 0.0621  0.0672  -0.0583 360 HIS B ND1   
4720 C CD2   . HIS B 219 ? 0.4378 0.2888 0.2816 0.0466  0.0615  -0.0520 360 HIS B CD2   
4721 C CE1   . HIS B 219 ? 0.4807 0.3351 0.3282 0.0597  0.0677  -0.0598 360 HIS B CE1   
4722 N NE2   . HIS B 219 ? 0.4855 0.3492 0.3327 0.0504  0.0641  -0.0556 360 HIS B NE2   
4723 N N     . MET B 220 ? 0.4550 0.2432 0.2948 0.0619  0.0560  -0.0336 361 MET B N     
4724 C CA    . MET B 220 ? 0.4585 0.2262 0.2916 0.0595  0.0547  -0.0299 361 MET B CA    
4725 C C     . MET B 220 ? 0.4816 0.2558 0.3197 0.0621  0.0509  -0.0205 361 MET B C     
4726 O O     . MET B 220 ? 0.4713 0.2661 0.3165 0.0619  0.0491  -0.0178 361 MET B O     
4727 C CB    . MET B 220 ? 0.4651 0.2260 0.2892 0.0462  0.0547  -0.0319 361 MET B CB    
4728 C CG    . MET B 220 ? 0.5423 0.3245 0.3702 0.0381  0.0525  -0.0299 361 MET B CG    
4729 S SD    . MET B 220 ? 0.5886 0.3655 0.4074 0.0227  0.0524  -0.0327 361 MET B SD    
4730 C CE    . MET B 220 ? 0.5349 0.3132 0.3502 0.0219  0.0559  -0.0429 361 MET B CE    
4731 N N     . PRO B 221 ? 0.4888 0.2458 0.3230 0.0643  0.0494  -0.0155 362 PRO B N     
4732 C CA    . PRO B 221 ? 0.4316 0.1953 0.2693 0.0661  0.0456  -0.0064 362 PRO B CA    
4733 C C     . PRO B 221 ? 0.4713 0.2453 0.3072 0.0547  0.0439  -0.0036 362 PRO B C     
4734 O O     . PRO B 221 ? 0.4766 0.2429 0.3055 0.0450  0.0448  -0.0059 362 PRO B O     
4735 C CB    . PRO B 221 ? 0.4721 0.2121 0.3042 0.0697  0.0446  -0.0019 362 PRO B CB    
4736 C CG    . PRO B 221 ? 0.5298 0.2496 0.3537 0.0654  0.0476  -0.0082 362 PRO B CG    
4737 C CD    . PRO B 221 ? 0.5152 0.2456 0.3419 0.0658  0.0510  -0.0176 362 PRO B CD    
4738 N N     . ILE B 222 ? 0.4504 0.2426 0.2932 0.0561  0.0416  0.0010  363 ILE B N     
4739 C CA    . ILE B 222 ? 0.4395 0.2438 0.2826 0.0467  0.0402  0.0036  363 ILE B CA    
4740 C C     . ILE B 222 ? 0.4420 0.2448 0.2837 0.0472  0.0375  0.0116  363 ILE B C     
4741 O O     . ILE B 222 ? 0.3998 0.2073 0.2461 0.0557  0.0358  0.0152  363 ILE B O     
4742 C CB    . ILE B 222 ? 0.3903 0.2187 0.2433 0.0469  0.0400  0.0014  363 ILE B CB    
4743 C CG1   . ILE B 222 ? 0.4107 0.2416 0.2645 0.0461  0.0424  -0.0058 363 ILE B CG1   
4744 C CG2   . ILE B 222 ? 0.4001 0.2408 0.2550 0.0380  0.0387  0.0038  363 ILE B CG2   
4745 C CD1   . ILE B 222 ? 0.3818 0.2062 0.2287 0.0353  0.0434  -0.0091 363 ILE B CD1   
4746 N N     . ASP B 223 ? 0.4666 0.2643 0.3019 0.0376  0.0370  0.0144  364 ASP B N     
4747 C CA    . ASP B 223 ? 0.4270 0.2250 0.2596 0.0357  0.0347  0.0219  364 ASP B CA    
4748 C C     . ASP B 223 ? 0.4318 0.2426 0.2649 0.0247  0.0351  0.0216  364 ASP B C     
4749 O O     . ASP B 223 ? 0.4069 0.2081 0.2329 0.0156  0.0360  0.0217  364 ASP B O     
4750 C CB    . ASP B 223 ? 0.4070 0.1810 0.2298 0.0354  0.0339  0.0266  364 ASP B CB    
4751 C CG    . ASP B 223 ? 0.4824 0.2574 0.3024 0.0355  0.0310  0.0354  364 ASP B CG    
4752 O OD1   . ASP B 223 ? 0.4628 0.2554 0.2856 0.0307  0.0304  0.0368  364 ASP B OD1   
4753 O OD2   . ASP B 223 ? 0.6013 0.3596 0.4163 0.0400  0.0292  0.0409  364 ASP B OD2   
4754 N N     . VAL B 224 ? 0.3484 0.1806 0.1904 0.0256  0.0346  0.0209  365 VAL B N     
4755 C CA    . VAL B 224 ? 0.3791 0.2249 0.2242 0.0163  0.0354  0.0191  365 VAL B CA    
4756 C C     . VAL B 224 ? 0.4277 0.2719 0.2668 0.0093  0.0350  0.0242  365 VAL B C     
4757 O O     . VAL B 224 ? 0.4072 0.2553 0.2453 -0.0003 0.0363  0.0230  365 VAL B O     
4758 C CB    . VAL B 224 ? 0.3919 0.2601 0.2491 0.0194  0.0352  0.0165  365 VAL B CB    
4759 C CG1   . VAL B 224 ? 0.3559 0.2264 0.2183 0.0248  0.0358  0.0117  365 VAL B CG1   
4760 C CG2   . VAL B 224 ? 0.3630 0.2394 0.2233 0.0252  0.0334  0.0206  365 VAL B CG2   
4761 N N     . ALA B 225 ? 0.4295 0.2689 0.2646 0.0135  0.0331  0.0302  366 ALA B N     
4762 C CA    . ALA B 225 ? 0.4676 0.3054 0.2956 0.0059  0.0327  0.0355  366 ALA B CA    
4763 C C     . ALA B 225 ? 0.4816 0.2995 0.2990 -0.0015 0.0336  0.0371  366 ALA B C     
4764 O O     . ALA B 225 ? 0.5258 0.3457 0.3391 -0.0118 0.0348  0.0382  366 ALA B O     
4765 C CB    . ALA B 225 ? 0.4438 0.2809 0.2691 0.0118  0.0300  0.0423  366 ALA B CB    
4766 N N     . ALA B 226 ? 0.4649 0.2638 0.2782 0.0033  0.0333  0.0367  367 ALA B N     
4767 C CA    . ALA B 226 ? 0.5095 0.2880 0.3131 -0.0038 0.0342  0.0374  367 ALA B CA    
4768 C C     . ALA B 226 ? 0.5243 0.3066 0.3297 -0.0116 0.0367  0.0303  367 ALA B C     
4769 O O     . ALA B 226 ? 0.5476 0.3215 0.3462 -0.0218 0.0377  0.0308  367 ALA B O     
4770 C CB    . ALA B 226 ? 0.5291 0.2853 0.3283 0.0044  0.0333  0.0387  367 ALA B CB    
4771 N N     . LEU B 227 ? 0.4549 0.2500 0.2692 -0.0074 0.0374  0.0242  368 LEU B N     
4772 C CA    . LEU B 227 ? 0.4463 0.2481 0.2633 -0.0148 0.0390  0.0182  368 LEU B CA    
4773 C C     . LEU B 227 ? 0.4605 0.2786 0.2810 -0.0242 0.0395  0.0189  368 LEU B C     
4774 O O     . LEU B 227 ? 0.5162 0.3340 0.3347 -0.0339 0.0406  0.0168  368 LEU B O     
4775 C CB    . LEU B 227 ? 0.4440 0.2573 0.2700 -0.0080 0.0392  0.0127  368 LEU B CB    
4776 C CG    . LEU B 227 ? 0.5190 0.3415 0.3490 -0.0144 0.0401  0.0070  368 LEU B CG    
4777 C CD1   . LEU B 227 ? 0.5246 0.3305 0.3449 -0.0232 0.0411  0.0051  368 LEU B CD1   
4778 C CD2   . LEU B 227 ? 0.4720 0.3016 0.3084 -0.0065 0.0402  0.0026  368 LEU B CD2   
4779 N N     . GLY B 228 ? 0.4009 0.2338 0.2268 -0.0216 0.0389  0.0216  369 GLY B N     
4780 C CA    . GLY B 228 ? 0.4118 0.2613 0.2421 -0.0296 0.0400  0.0215  369 GLY B CA    
4781 C C     . GLY B 228 ? 0.3803 0.2493 0.2231 -0.0302 0.0406  0.0160  369 GLY B C     
4782 O O     . GLY B 228 ? 0.3626 0.2457 0.2107 -0.0369 0.0417  0.0150  369 GLY B O     
4783 N N     . ALA B 229 ? 0.3546 0.2252 0.2026 -0.0236 0.0398  0.0125  370 ALA B N     
4784 C CA    . ALA B 229 ? 0.3435 0.2320 0.2035 -0.0242 0.0398  0.0082  370 ALA B CA    
4785 C C     . ALA B 229 ? 0.3111 0.2182 0.1811 -0.0219 0.0398  0.0087  370 ALA B C     
4786 O O     . ALA B 229 ? 0.3209 0.2281 0.1900 -0.0159 0.0393  0.0113  370 ALA B O     
4787 C CB    . ALA B 229 ? 0.3294 0.2164 0.1922 -0.0171 0.0390  0.0052  370 ALA B CB    
4788 N N     . ASP B 230 ? 0.2711 0.1942 0.1512 -0.0266 0.0404  0.0060  371 ASP B N     
4789 C CA    . ASP B 230 ? 0.2841 0.2249 0.1749 -0.0246 0.0408  0.0052  371 ASP B CA    
4790 C C     . ASP B 230 ? 0.3115 0.2595 0.2108 -0.0155 0.0393  0.0039  371 ASP B C     
4791 O O     . ASP B 230 ? 0.2739 0.2301 0.1779 -0.0111 0.0392  0.0043  371 ASP B O     
4792 C CB    . ASP B 230 ? 0.2778 0.2330 0.1781 -0.0319 0.0419  0.0025  371 ASP B CB    
4793 C CG    . ASP B 230 ? 0.3378 0.2876 0.2302 -0.0416 0.0437  0.0038  371 ASP B CG    
4794 O OD1   . ASP B 230 ? 0.3589 0.3126 0.2492 -0.0442 0.0454  0.0052  371 ASP B OD1   
4795 O OD2   . ASP B 230 ? 0.3046 0.2462 0.1922 -0.0468 0.0433  0.0035  371 ASP B OD2   
4796 N N     . PHE B 231 ? 0.2528 0.1987 0.1542 -0.0135 0.0382  0.0021  372 PHE B N     
4797 C CA    . PHE B 231 ? 0.2737 0.2256 0.1821 -0.0056 0.0368  0.0012  372 PHE B CA    
4798 C C     . PHE B 231 ? 0.2806 0.2194 0.1814 -0.0021 0.0363  0.0008  372 PHE B C     
4799 O O     . PHE B 231 ? 0.2661 0.1956 0.1601 -0.0071 0.0367  -0.0002 372 PHE B O     
4800 C CB    . PHE B 231 ? 0.2324 0.2005 0.1548 -0.0068 0.0360  -0.0012 372 PHE B CB    
4801 C CG    . PHE B 231 ? 0.2201 0.2017 0.1520 -0.0106 0.0369  -0.0021 372 PHE B CG    
4802 C CD1   . PHE B 231 ? 0.2193 0.2097 0.1577 -0.0064 0.0373  -0.0024 372 PHE B CD1   
4803 C CD2   . PHE B 231 ? 0.2250 0.2111 0.1598 -0.0184 0.0375  -0.0031 372 PHE B CD2   
4804 C CE1   . PHE B 231 ? 0.2235 0.2263 0.1708 -0.0098 0.0387  -0.0043 372 PHE B CE1   
4805 C CE2   . PHE B 231 ? 0.2556 0.2548 0.2001 -0.0216 0.0389  -0.0047 372 PHE B CE2   
4806 C CZ    . PHE B 231 ? 0.2629 0.2703 0.2138 -0.0171 0.0397  -0.0055 372 PHE B CZ    
4807 N N     . PHE B 232 ? 0.2703 0.2094 0.1727 0.0063  0.0357  0.0011  373 PHE B N     
4808 C CA    . PHE B 232 ? 0.2373 0.1660 0.1339 0.0107  0.0358  0.0000  373 PHE B CA    
4809 C C     . PHE B 232 ? 0.2337 0.1737 0.1393 0.0173  0.0350  -0.0009 373 PHE B C     
4810 O O     . PHE B 232 ? 0.2614 0.2090 0.1725 0.0220  0.0344  0.0005  373 PHE B O     
4811 C CB    . PHE B 232 ? 0.2724 0.1845 0.1585 0.0147  0.0363  0.0021  373 PHE B CB    
4812 C CG    . PHE B 232 ? 0.3163 0.2166 0.1968 0.0195  0.0370  0.0000  373 PHE B CG    
4813 C CD1   . PHE B 232 ? 0.3063 0.1928 0.1780 0.0146  0.0381  -0.0022 373 PHE B CD1   
4814 C CD2   . PHE B 232 ? 0.3036 0.2075 0.1881 0.0285  0.0369  -0.0003 373 PHE B CD2   
4815 C CE1   . PHE B 232 ? 0.3254 0.2011 0.1920 0.0190  0.0393  -0.0052 373 PHE B CE1   
4816 C CE2   . PHE B 232 ? 0.3392 0.2335 0.2193 0.0331  0.0382  -0.0030 373 PHE B CE2   
4817 C CZ    . PHE B 232 ? 0.3077 0.1876 0.1787 0.0284  0.0395  -0.0057 373 PHE B CZ    
4818 N N     . VAL B 233 ? 0.2359 0.1775 0.1425 0.0172  0.0348  -0.0032 374 VAL B N     
4819 C CA    . VAL B 233 ? 0.2322 0.1863 0.1480 0.0221  0.0340  -0.0036 374 VAL B CA    
4820 C C     . VAL B 233 ? 0.2409 0.1886 0.1517 0.0270  0.0350  -0.0055 374 VAL B C     
4821 O O     . VAL B 233 ? 0.2531 0.1899 0.1551 0.0243  0.0361  -0.0077 374 VAL B O     
4822 C CB    . VAL B 233 ? 0.2073 0.1748 0.1326 0.0169  0.0325  -0.0040 374 VAL B CB    
4823 C CG1   . VAL B 233 ? 0.1814 0.1571 0.1142 0.0134  0.0320  -0.0029 374 VAL B CG1   
4824 C CG2   . VAL B 233 ? 0.2156 0.1783 0.1352 0.0102  0.0324  -0.0057 374 VAL B CG2   
4825 N N     . PHE B 234 ? 0.2331 0.1879 0.1494 0.0340  0.0349  -0.0051 375 PHE B N     
4826 C CA    . PHE B 234 ? 0.2452 0.1972 0.1583 0.0384  0.0363  -0.0075 375 PHE B CA    
4827 C C     . PHE B 234 ? 0.2664 0.2326 0.1891 0.0433  0.0358  -0.0068 375 PHE B C     
4828 O O     . PHE B 234 ? 0.2583 0.2344 0.1894 0.0442  0.0343  -0.0046 375 PHE B O     
4829 C CB    . PHE B 234 ? 0.2552 0.1915 0.1595 0.0437  0.0381  -0.0083 375 PHE B CB    
4830 C CG    . PHE B 234 ? 0.2533 0.1909 0.1610 0.0513  0.0375  -0.0055 375 PHE B CG    
4831 C CD1   . PHE B 234 ? 0.2704 0.2039 0.1763 0.0503  0.0364  -0.0022 375 PHE B CD1   
4832 C CD2   . PHE B 234 ? 0.2730 0.2161 0.1850 0.0591  0.0382  -0.0061 375 PHE B CD2   
4833 C CE1   . PHE B 234 ? 0.2987 0.2340 0.2070 0.0569  0.0354  0.0008  375 PHE B CE1   
4834 C CE2   . PHE B 234 ? 0.2514 0.1965 0.1666 0.0660  0.0372  -0.0033 375 PHE B CE2   
4835 C CZ    . PHE B 234 ? 0.2527 0.1938 0.1658 0.0648  0.0356  0.0003  375 PHE B CZ    
4836 N N     . SER B 235 ? 0.2258 0.1928 0.1467 0.0460  0.0373  -0.0092 376 SER B N     
4837 C CA    . SER B 235 ? 0.2331 0.2136 0.1620 0.0495  0.0371  -0.0088 376 SER B CA    
4838 C C     . SER B 235 ? 0.2337 0.2111 0.1610 0.0580  0.0392  -0.0103 376 SER B C     
4839 O O     . SER B 235 ? 0.2425 0.2087 0.1616 0.0598  0.0416  -0.0135 376 SER B O     
4840 C CB    . SER B 235 ? 0.2597 0.2465 0.1882 0.0446  0.0372  -0.0103 376 SER B CB    
4841 O OG    . SER B 235 ? 0.2479 0.2415 0.1812 0.0376  0.0345  -0.0081 376 SER B OG    
4842 N N     . GLY B 236 ? 0.2264 0.2144 0.1622 0.0630  0.0384  -0.0083 377 GLY B N     
4843 C CA    . GLY B 236 ? 0.2157 0.2028 0.1518 0.0715  0.0401  -0.0092 377 GLY B CA    
4844 C C     . GLY B 236 ? 0.2218 0.2104 0.1556 0.0735  0.0432  -0.0131 377 GLY B C     
4845 O O     . GLY B 236 ? 0.2422 0.2237 0.1726 0.0798  0.0456  -0.0156 377 GLY B O     
4846 N N     . HIS B 237 ? 0.2042 0.2023 0.1399 0.0682  0.0431  -0.0136 378 HIS B N     
4847 C CA    . HIS B 237 ? 0.2302 0.2331 0.1643 0.0696  0.0462  -0.0171 378 HIS B CA    
4848 C C     . HIS B 237 ? 0.2860 0.2753 0.2086 0.0681  0.0492  -0.0222 378 HIS B C     
4849 O O     . HIS B 237 ? 0.2919 0.2824 0.2116 0.0705  0.0527  -0.0265 378 HIS B O     
4850 C CB    . HIS B 237 ? 0.2456 0.2631 0.1848 0.0638  0.0448  -0.0152 378 HIS B CB    
4851 C CG    . HIS B 237 ? 0.2482 0.2635 0.1833 0.0549  0.0429  -0.0144 378 HIS B CG    
4852 N ND1   . HIS B 237 ? 0.2447 0.2571 0.1712 0.0502  0.0447  -0.0177 378 HIS B ND1   
4853 C CD2   . HIS B 237 ? 0.2426 0.2588 0.1815 0.0498  0.0395  -0.0109 378 HIS B CD2   
4854 C CE1   . HIS B 237 ? 0.2448 0.2568 0.1700 0.0425  0.0419  -0.0157 378 HIS B CE1   
4855 N NE2   . HIS B 237 ? 0.2615 0.2758 0.1947 0.0424  0.0388  -0.0117 378 HIS B NE2   
4856 N N1    . LLP B 238 ? 0.3271 0.2954 0.2279 0.0005  0.0318  -0.0150 379 LLP B N1    
4857 C C2    . LLP B 238 ? 0.3625 0.3211 0.2524 0.0016  0.0347  -0.0196 379 LLP B C2    
4858 C "C2'" . LLP B 238 ? 0.3436 0.2854 0.2210 -0.0030 0.0365  -0.0238 379 LLP B "C2'" 
4859 C C3    . LLP B 238 ? 0.3469 0.3107 0.2372 0.0067  0.0363  -0.0208 379 LLP B C3    
4860 O O3    . LLP B 238 ? 0.4069 0.3611 0.2866 0.0081  0.0399  -0.0265 379 LLP B O3    
4861 C C4    . LLP B 238 ? 0.3510 0.3292 0.2525 0.0102  0.0346  -0.0169 379 LLP B C4    
4862 C "C4'" . LLP B 238 ? 0.4025 0.3870 0.3038 0.0152  0.0368  -0.0185 379 LLP B "C4'" 
4863 C C5    . LLP B 238 ? 0.3460 0.3328 0.2585 0.0091  0.0315  -0.0122 379 LLP B C5    
4864 C C6    . LLP B 238 ? 0.3187 0.3008 0.2310 0.0044  0.0302  -0.0115 379 LLP B C6    
4865 C "C5'" . LLP B 238 ? 0.2752 0.2769 0.2007 0.0124  0.0294  -0.0080 379 LLP B "C5'" 
4866 O OP4   . LLP B 238 ? 0.3557 0.3570 0.2844 0.0206  0.0313  -0.0082 379 LLP B OP4   
4867 P P     . LLP B 238 ? 0.3045 0.3197 0.2447 0.0240  0.0300  -0.0049 379 LLP B P     
4868 O OP1   . LLP B 238 ? 0.2995 0.3124 0.2389 0.0322  0.0328  -0.0065 379 LLP B OP1   
4869 O OP2   . LLP B 238 ? 0.3261 0.3503 0.2661 0.0195  0.0287  -0.0036 379 LLP B OP2   
4870 O OP3   . LLP B 238 ? 0.2570 0.2787 0.2089 0.0233  0.0272  -0.0014 379 LLP B OP3   
4871 N N     . LLP B 238 ? 0.2615 0.2382 0.1776 0.0638  0.0481  -0.0221 379 LLP B N     
4872 C CA    . LLP B 238 ? 0.2768 0.2383 0.1816 0.0622  0.0508  -0.0272 379 LLP B CA    
4873 C CB    . LLP B 238 ? 0.3198 0.2751 0.2190 0.0530  0.0488  -0.0265 379 LLP B CB    
4874 C CG    . LLP B 238 ? 0.3437 0.3123 0.2448 0.0451  0.0471  -0.0255 379 LLP B CG    
4875 C CD    . LLP B 238 ? 0.3890 0.3499 0.2825 0.0361  0.0458  -0.0264 379 LLP B CD    
4876 C CE    . LLP B 238 ? 0.3806 0.3548 0.2760 0.0280  0.0434  -0.0246 379 LLP B CE    
4877 N NZ    . LLP B 238 ? 0.4583 0.4371 0.3609 0.0241  0.0394  -0.0196 379 LLP B NZ    
4878 C C     . LLP B 238 ? 0.3298 0.2768 0.2319 0.0697  0.0524  -0.0284 379 LLP B C     
4879 O O     . LLP B 238 ? 0.3355 0.2680 0.2290 0.0694  0.0548  -0.0328 379 LLP B O     
4880 N N     . ILE B 239 ? 0.2889 0.2392 0.1981 0.0762  0.0507  -0.0244 380 ILE B N     
4881 C CA    . ILE B 239 ? 0.3128 0.2503 0.2203 0.0844  0.0518  -0.0248 380 ILE B CA    
4882 C C     . ILE B 239 ? 0.2895 0.2381 0.2061 0.0938  0.0526  -0.0242 380 ILE B C     
4883 O O     . ILE B 239 ? 0.2554 0.2038 0.1766 0.0998  0.0506  -0.0203 380 ILE B O     
4884 C CB    . ILE B 239 ? 0.3030 0.2301 0.2080 0.0828  0.0487  -0.0200 380 ILE B CB    
4885 C CG1   . ILE B 239 ? 0.3195 0.2295 0.2205 0.0901  0.0497  -0.0202 380 ILE B CG1   
4886 C CG2   . ILE B 239 ? 0.2395 0.1802 0.1529 0.0824  0.0451  -0.0144 380 ILE B CG2   
4887 C CD1   . ILE B 239 ? 0.3685 0.2639 0.2628 0.0860  0.0476  -0.0167 380 ILE B CD1   
4888 N N     . TYR B 240 ? 0.2794 0.2384 0.1982 0.0946  0.0556  -0.0282 381 TYR B N     
4889 C CA    . TYR B 240 ? 0.2596 0.2300 0.1882 0.1007  0.0561  -0.0285 381 TYR B CA    
4890 C C     . TYR B 240 ? 0.2622 0.2479 0.2015 0.1017  0.0522  -0.0227 381 TYR B C     
4891 O O     . TYR B 240 ? 0.2738 0.2675 0.2217 0.1061  0.0512  -0.0215 381 TYR B O     
4892 C CB    . TYR B 240 ? 0.2930 0.2508 0.2218 0.1079  0.0571  -0.0304 381 TYR B CB    
4893 C CG    . TYR B 240 ? 0.3615 0.3016 0.2790 0.1058  0.0606  -0.0362 381 TYR B CG    
4894 C CD1   . TYR B 240 ? 0.3340 0.2772 0.2488 0.1026  0.0645  -0.0429 381 TYR B CD1   
4895 C CD2   . TYR B 240 ? 0.3089 0.2295 0.2173 0.1055  0.0600  -0.0351 381 TYR B CD2   
4896 C CE1   . TYR B 240 ? 0.3891 0.3169 0.2930 0.0993  0.0675  -0.0488 381 TYR B CE1   
4897 C CE2   . TYR B 240 ? 0.3299 0.2339 0.2273 0.1020  0.0630  -0.0406 381 TYR B CE2   
4898 C CZ    . TYR B 240 ? 0.4062 0.3141 0.3015 0.0988  0.0666  -0.0476 381 TYR B CZ    
4899 O OH    . TYR B 240 ? 0.4876 0.3795 0.3719 0.0945  0.0695  -0.0536 381 TYR B OH    
4900 N N     . GLY B 241 ? 0.2473 0.2377 0.1863 0.0971  0.0501  -0.0194 382 GLY B N     
4901 C CA    . GLY B 241 ? 0.2182 0.2220 0.1668 0.0970  0.0465  -0.0145 382 GLY B CA    
4902 C C     . GLY B 241 ? 0.2199 0.2394 0.1741 0.0915  0.0461  -0.0139 382 GLY B C     
4903 O O     . GLY B 241 ? 0.2156 0.2370 0.1658 0.0878  0.0486  -0.0168 382 GLY B O     
4904 N N     . PRO B 242 ? 0.2288 0.2598 0.1920 0.0906  0.0428  -0.0101 383 PRO B N     
4905 C CA    . PRO B 242 ? 0.2508 0.2960 0.2203 0.0856  0.0421  -0.0088 383 PRO B CA    
4906 C C     . PRO B 242 ? 0.2232 0.2669 0.1890 0.0789  0.0418  -0.0083 383 PRO B C     
4907 O O     . PRO B 242 ? 0.2099 0.2429 0.1709 0.0762  0.0405  -0.0079 383 PRO B O     
4908 C CB    . PRO B 242 ? 0.2343 0.2880 0.2130 0.0857  0.0382  -0.0051 383 PRO B CB    
4909 C CG    . PRO B 242 ? 0.2573 0.3041 0.2348 0.0915  0.0373  -0.0046 383 PRO B CG    
4910 C CD    . PRO B 242 ? 0.2265 0.2575 0.1938 0.0939  0.0397  -0.0067 383 PRO B CD    
4911 N N     . THR B 243 ? 0.1865 0.2409 0.1560 0.0741  0.0416  -0.0075 384 THR B N     
4912 C CA    . THR B 243 ? 0.2123 0.2669 0.1823 0.0661  0.0390  -0.0052 384 THR B CA    
4913 C C     . THR B 243 ? 0.2008 0.2588 0.1791 0.0652  0.0357  -0.0020 384 THR B C     
4914 O O     . THR B 243 ? 0.1997 0.2618 0.1833 0.0699  0.0352  -0.0013 384 THR B O     
4915 C CB    . THR B 243 ? 0.2365 0.3019 0.2087 0.0610  0.0391  -0.0040 384 THR B CB    
4916 O OG1   . THR B 243 ? 0.2268 0.3051 0.2084 0.0630  0.0387  -0.0020 384 THR B OG1   
4917 C CG2   . THR B 243 ? 0.2184 0.2817 0.1815 0.0610  0.0429  -0.0080 384 THR B CG2   
4918 N N     . GLY B 244 ? 0.1581 0.2147 0.1378 0.0591  0.0334  -0.0003 385 GLY B N     
4919 C CA    . GLY B 244 ? 0.1986 0.2591 0.1870 0.0575  0.0306  0.0019  385 GLY B CA    
4920 C C     . GLY B 244 ? 0.1714 0.2243 0.1575 0.0597  0.0303  0.0012  385 GLY B C     
4921 O O     . GLY B 244 ? 0.1769 0.2341 0.1701 0.0589  0.0285  0.0022  385 GLY B O     
4922 N N     . ILE B 245 ? 0.1835 0.2251 0.1598 0.0621  0.0319  -0.0005 386 ILE B N     
4923 C CA    . ILE B 245 ? 0.1694 0.2035 0.1426 0.0637  0.0315  -0.0004 386 ILE B CA    
4924 C C     . ILE B 245 ? 0.2175 0.2380 0.1804 0.0609  0.0324  -0.0016 386 ILE B C     
4925 O O     . ILE B 245 ? 0.1801 0.1944 0.1362 0.0614  0.0343  -0.0034 386 ILE B O     
4926 C CB    . ILE B 245 ? 0.1657 0.2001 0.1385 0.0711  0.0319  -0.0002 386 ILE B CB    
4927 C CG1   . ILE B 245 ? 0.1690 0.1982 0.1395 0.0716  0.0306  0.0011  386 ILE B CG1   
4928 C CG2   . ILE B 245 ? 0.1628 0.1900 0.1286 0.0761  0.0345  -0.0020 386 ILE B CG2   
4929 C CD1   . ILE B 245 ? 0.1959 0.2352 0.1751 0.0687  0.0287  0.0019  386 ILE B CD1   
4930 N N     . GLY B 246 ? 0.1908 0.2073 0.1529 0.0575  0.0314  -0.0008 387 GLY B N     
4931 C CA    . GLY B 246 ? 0.1936 0.1975 0.1464 0.0543  0.0321  -0.0016 387 GLY B CA    
4932 C C     . GLY B 246 ? 0.2264 0.2280 0.1790 0.0528  0.0313  -0.0003 387 GLY B C     
4933 O O     . GLY B 246 ? 0.1884 0.1985 0.1478 0.0542  0.0302  0.0006  387 GLY B O     
4934 N N     . VAL B 247 ? 0.1964 0.1869 0.1408 0.0491  0.0319  -0.0005 388 VAL B N     
4935 C CA    . VAL B 247 ? 0.1942 0.1806 0.1354 0.0476  0.0316  0.0009  388 VAL B CA    
4936 C C     . VAL B 247 ? 0.1879 0.1711 0.1270 0.0397  0.0319  0.0003  388 VAL B C     
4937 O O     . VAL B 247 ? 0.2190 0.1952 0.1528 0.0364  0.0325  -0.0009 388 VAL B O     
4938 C CB    . VAL B 247 ? 0.2400 0.2138 0.1717 0.0523  0.0322  0.0023  388 VAL B CB    
4939 C CG1   . VAL B 247 ? 0.2482 0.2156 0.1742 0.0488  0.0319  0.0043  388 VAL B CG1   
4940 C CG2   . VAL B 247 ? 0.2025 0.1821 0.1383 0.0600  0.0315  0.0034  388 VAL B CG2   
4941 N N     . LEU B 248 ? 0.1928 0.1819 0.1361 0.0365  0.0315  0.0007  389 LEU B N     
4942 C CA    . LEU B 248 ? 0.1953 0.1809 0.1355 0.0296  0.0321  0.0005  389 LEU B CA    
4943 C C     . LEU B 248 ? 0.2320 0.2109 0.1644 0.0298  0.0327  0.0024  389 LEU B C     
4944 O O     . LEU B 248 ? 0.2104 0.1964 0.1463 0.0318  0.0322  0.0030  389 LEU B O     
4945 C CB    . LEU B 248 ? 0.1841 0.1827 0.1359 0.0253  0.0318  -0.0009 389 LEU B CB    
4946 C CG    . LEU B 248 ? 0.2215 0.2201 0.1724 0.0185  0.0329  -0.0015 389 LEU B CG    
4947 C CD1   . LEU B 248 ? 0.1819 0.1719 0.1259 0.0131  0.0332  -0.0015 389 LEU B CD1   
4948 C CD2   . LEU B 248 ? 0.2032 0.2161 0.1679 0.0161  0.0328  -0.0034 389 LEU B CD2   
4949 N N     . TYR B 249 ? 0.2213 0.1863 0.1427 0.0273  0.0334  0.0035  390 TYR B N     
4950 C CA    . TYR B 249 ? 0.2482 0.2068 0.1619 0.0251  0.0337  0.0060  390 TYR B CA    
4951 C C     . TYR B 249 ? 0.2596 0.2219 0.1744 0.0164  0.0349  0.0049  390 TYR B C     
4952 O O     . TYR B 249 ? 0.2322 0.1934 0.1480 0.0119  0.0353  0.0031  390 TYR B O     
4953 C CB    . TYR B 249 ? 0.2516 0.1921 0.1531 0.0270  0.0338  0.0083  390 TYR B CB    
4954 C CG    . TYR B 249 ? 0.2864 0.2179 0.1785 0.0215  0.0342  0.0112  390 TYR B CG    
4955 C CD1   . TYR B 249 ? 0.2360 0.1675 0.1245 0.0235  0.0333  0.0150  390 TYR B CD1   
4956 C CD2   . TYR B 249 ? 0.2728 0.1966 0.1596 0.0137  0.0354  0.0105  390 TYR B CD2   
4957 C CE1   . TYR B 249 ? 0.2873 0.2111 0.1666 0.0177  0.0336  0.0184  390 TYR B CE1   
4958 C CE2   . TYR B 249 ? 0.2928 0.2087 0.1708 0.0080  0.0360  0.0135  390 TYR B CE2   
4959 C CZ    . TYR B 249 ? 0.3087 0.2244 0.1828 0.0099  0.0351  0.0176  390 TYR B CZ    
4960 O OH    . TYR B 249 ? 0.3231 0.2310 0.1878 0.0035  0.0356  0.0211  390 TYR B OH    
4961 N N     . GLY B 250 ? 0.2376 0.2056 0.1526 0.0139  0.0354  0.0057  391 GLY B N     
4962 C CA    . GLY B 250 ? 0.2663 0.2376 0.1813 0.0055  0.0370  0.0048  391 GLY B CA    
4963 C C     . GLY B 250 ? 0.3131 0.2798 0.2185 0.0029  0.0377  0.0079  391 GLY B C     
4964 O O     . GLY B 250 ? 0.2712 0.2419 0.1762 0.0069  0.0368  0.0093  391 GLY B O     
4965 N N     . ARG B 251 ? 0.2830 0.2415 0.1802 -0.0042 0.0389  0.0093  392 ARG B N     
4966 C CA    . ARG B 251 ? 0.3291 0.2851 0.2175 -0.0085 0.0397  0.0125  392 ARG B CA    
4967 C C     . ARG B 251 ? 0.3025 0.2761 0.1987 -0.0102 0.0411  0.0098  392 ARG B C     
4968 O O     . ARG B 251 ? 0.2726 0.2589 0.1809 -0.0115 0.0423  0.0051  392 ARG B O     
4969 C CB    . ARG B 251 ? 0.3339 0.2818 0.2147 -0.0176 0.0413  0.0135  392 ARG B CB    
4970 C CG    . ARG B 251 ? 0.4152 0.3442 0.2871 -0.0172 0.0403  0.0157  392 ARG B CG    
4971 C CD    . ARG B 251 ? 0.4396 0.3624 0.3051 -0.0275 0.0420  0.0162  392 ARG B CD    
4972 N NE    . ARG B 251 ? 0.4324 0.3527 0.2889 -0.0330 0.0429  0.0204  392 ARG B NE    
4973 C CZ    . ARG B 251 ? 0.5640 0.4670 0.4076 -0.0332 0.0417  0.0260  392 ARG B CZ    
4974 N NH1   . ARG B 251 ? 0.5076 0.3939 0.3464 -0.0275 0.0399  0.0275  392 ARG B NH1   
4975 N NH2   . ARG B 251 ? 0.5122 0.4146 0.3476 -0.0391 0.0424  0.0303  392 ARG B NH2   
4976 N N     . GLU B 252 ? 0.2928 0.2671 0.1821 -0.0103 0.0408  0.0128  393 GLU B N     
4977 C CA    . GLU B 252 ? 0.3106 0.3016 0.2071 -0.0111 0.0421  0.0094  393 GLU B CA    
4978 C C     . GLU B 252 ? 0.2755 0.2774 0.1778 -0.0193 0.0457  0.0050  393 GLU B C     
4979 O O     . GLU B 252 ? 0.2736 0.2900 0.1876 -0.0189 0.0472  -0.0003 393 GLU B O     
4980 C CB    . GLU B 252 ? 0.3774 0.3679 0.2641 -0.0105 0.0408  0.0137  393 GLU B CB    
4981 C CG    . GLU B 252 ? 0.4382 0.4218 0.3115 -0.0181 0.0417  0.0182  393 GLU B CG    
4982 C CD    . GLU B 252 ? 0.5094 0.4930 0.3731 -0.0171 0.0397  0.0233  393 GLU B CD    
4983 O OE1   . GLU B 252 ? 0.5830 0.5555 0.4335 -0.0209 0.0388  0.0297  393 GLU B OE1   
4984 O OE2   . GLU B 252 ? 0.4683 0.4629 0.3373 -0.0127 0.0386  0.0213  393 GLU B OE2   
4985 N N     . ASP B 253 ? 0.2862 0.2813 0.1813 -0.0267 0.0472  0.0067  394 ASP B N     
4986 C CA    . ASP B 253 ? 0.3330 0.3399 0.2351 -0.0344 0.0508  0.0022  394 ASP B CA    
4987 C C     . ASP B 253 ? 0.3383 0.3520 0.2556 -0.0325 0.0508  -0.0025 394 ASP B C     
4988 O O     . ASP B 253 ? 0.3301 0.3590 0.2604 -0.0341 0.0531  -0.0078 394 ASP B O     
4989 C CB    . ASP B 253 ? 0.3350 0.3333 0.2252 -0.0433 0.0523  0.0058  394 ASP B CB    
4990 C CG    . ASP B 253 ? 0.4750 0.4583 0.3611 -0.0440 0.0507  0.0081  394 ASP B CG    
4991 O OD1   . ASP B 253 ? 0.5086 0.4760 0.3853 -0.0395 0.0480  0.0127  394 ASP B OD1   
4992 O OD2   . ASP B 253 ? 0.5111 0.4983 0.4030 -0.0493 0.0522  0.0054  394 ASP B OD2   
4993 N N     . ALA B 254 ? 0.2772 0.2805 0.1938 -0.0286 0.0482  -0.0006 395 ALA B N     
4994 C CA    . ALA B 254 ? 0.3190 0.3287 0.2490 -0.0264 0.0474  -0.0040 395 ALA B CA    
4995 C C     . ALA B 254 ? 0.2810 0.3023 0.2237 -0.0199 0.0467  -0.0072 395 ALA B C     
4996 O O     . ALA B 254 ? 0.2828 0.3163 0.2399 -0.0204 0.0475  -0.0112 395 ALA B O     
4997 C CB    . ALA B 254 ? 0.2949 0.2909 0.2195 -0.0238 0.0448  -0.0015 395 ALA B CB    
4998 N N     . LEU B 255 ? 0.2505 0.2680 0.1887 -0.0137 0.0451  -0.0053 396 LEU B N     
4999 C CA    . LEU B 255 ? 0.2457 0.2740 0.1952 -0.0082 0.0445  -0.0083 396 LEU B CA    
5000 C C     . LEU B 255 ? 0.2833 0.3254 0.2399 -0.0118 0.0475  -0.0129 396 LEU B C     
5001 O O     . LEU B 255 ? 0.2681 0.3211 0.2389 -0.0097 0.0480  -0.0173 396 LEU B O     
5002 C CB    . LEU B 255 ? 0.2406 0.2629 0.1830 -0.0017 0.0422  -0.0051 396 LEU B CB    
5003 C CG    . LEU B 255 ? 0.2880 0.2985 0.2261 0.0036  0.0396  -0.0019 396 LEU B CG    
5004 C CD1   . LEU B 255 ? 0.2986 0.3067 0.2333 0.0108  0.0374  0.0005  396 LEU B CD1   
5005 C CD2   . LEU B 255 ? 0.2405 0.2552 0.1900 0.0048  0.0388  -0.0042 396 LEU B CD2   
5006 N N     . ALA B 256 ? 0.2348 0.2764 0.1816 -0.0175 0.0497  -0.0121 397 ALA B N     
5007 C CA    . ALA B 256 ? 0.3044 0.3596 0.2564 -0.0217 0.0533  -0.0171 397 ALA B CA    
5008 C C     . ALA B 256 ? 0.3247 0.3905 0.2918 -0.0248 0.0558  -0.0223 397 ALA B C     
5009 O O     . ALA B 256 ? 0.3139 0.3926 0.2923 -0.0251 0.0583  -0.0283 397 ALA B O     
5010 C CB    . ALA B 256 ? 0.2692 0.3215 0.2062 -0.0284 0.0553  -0.0144 397 ALA B CB    
5011 N N     . GLU B 257 ? 0.2843 0.3450 0.2522 -0.0271 0.0550  -0.0204 398 GLU B N     
5012 C CA    . GLU B 257 ? 0.2978 0.3693 0.2813 -0.0296 0.0566  -0.0246 398 GLU B CA    
5013 C C     . GLU B 257 ? 0.2835 0.3569 0.2808 -0.0235 0.0535  -0.0251 398 GLU B C     
5014 O O     . GLU B 257 ? 0.2850 0.3658 0.2952 -0.0250 0.0536  -0.0271 398 GLU B O     
5015 C CB    . GLU B 257 ? 0.2593 0.3273 0.2371 -0.0371 0.0577  -0.0226 398 GLU B CB    
5016 C CG    . GLU B 257 ? 0.3444 0.3993 0.3158 -0.0364 0.0541  -0.0179 398 GLU B CG    
5017 C CD    . GLU B 257 ? 0.4111 0.4632 0.3771 -0.0450 0.0554  -0.0165 398 GLU B CD    
5018 O OE1   . GLU B 257 ? 0.3327 0.3792 0.2988 -0.0458 0.0530  -0.0147 398 GLU B OE1   
5019 O OE2   . GLU B 257 ? 0.3815 0.4377 0.3427 -0.0514 0.0589  -0.0174 398 GLU B OE2   
5020 N N     . THR B 258 ? 0.2045 0.2724 0.1999 -0.0168 0.0506  -0.0232 399 THR B N     
5021 C CA    . THR B 258 ? 0.2366 0.3060 0.2437 -0.0115 0.0475  -0.0229 399 THR B CA    
5022 C C     . THR B 258 ? 0.2414 0.3203 0.2611 -0.0073 0.0480  -0.0271 399 THR B C     
5023 O O     . THR B 258 ? 0.2687 0.3462 0.2822 -0.0047 0.0481  -0.0273 399 THR B O     
5024 C CB    . THR B 258 ? 0.2279 0.2848 0.2246 -0.0073 0.0441  -0.0179 399 THR B CB    
5025 O OG1   . THR B 258 ? 0.2589 0.3058 0.2439 -0.0114 0.0438  -0.0147 399 THR B OG1   
5026 C CG2   . THR B 258 ? 0.2294 0.2888 0.2374 -0.0026 0.0410  -0.0174 399 THR B CG2   
5027 N N     . PRO B 259 ? 0.2397 0.3283 0.2772 -0.0064 0.0481  -0.0304 400 PRO B N     
5028 C CA    . PRO B 259 ? 0.2066 0.3027 0.2565 -0.0024 0.0486  -0.0347 400 PRO B CA    
5029 C C     . PRO B 259 ? 0.2083 0.2988 0.2574 0.0034  0.0448  -0.0312 400 PRO B C     
5030 O O     . PRO B 259 ? 0.2077 0.2897 0.2483 0.0045  0.0420  -0.0261 400 PRO B O     
5031 C CB    . PRO B 259 ? 0.2059 0.3119 0.2757 -0.0030 0.0492  -0.0380 400 PRO B CB    
5032 C CG    . PRO B 259 ? 0.2811 0.3835 0.3492 -0.0053 0.0468  -0.0333 400 PRO B CG    
5033 C CD    . PRO B 259 ? 0.2374 0.3300 0.2849 -0.0090 0.0474  -0.0300 400 PRO B CD    
5034 N N     . PRO B 260 ? 0.2671 0.3621 0.3240 0.0068  0.0447  -0.0343 401 PRO B N     
5035 C CA    . PRO B 260 ? 0.2183 0.3093 0.2757 0.0119  0.0412  -0.0309 401 PRO B CA    
5036 C C     . PRO B 260 ? 0.1956 0.2870 0.2640 0.0133  0.0382  -0.0280 401 PRO B C     
5037 O O     . PRO B 260 ? 0.1865 0.2833 0.2670 0.0115  0.0386  -0.0296 401 PRO B O     
5038 C CB    . PRO B 260 ? 0.2198 0.3171 0.2852 0.0139  0.0423  -0.0358 401 PRO B CB    
5039 C CG    . PRO B 260 ? 0.3102 0.4130 0.3730 0.0097  0.0467  -0.0414 401 PRO B CG    
5040 C CD    . PRO B 260 ? 0.2763 0.3802 0.3411 0.0058  0.0482  -0.0412 401 PRO B CD    
5041 N N     . TRP B 261 ? 0.1558 0.2417 0.2198 0.0164  0.0350  -0.0234 402 TRP B N     
5042 C CA    . TRP B 261 ? 0.1439 0.2304 0.2167 0.0173  0.0318  -0.0199 402 TRP B CA    
5043 C C     . TRP B 261 ? 0.1898 0.2803 0.2751 0.0209  0.0301  -0.0203 402 TRP B C     
5044 O O     . TRP B 261 ? 0.1666 0.2633 0.2679 0.0209  0.0302  -0.0229 402 TRP B O     
5045 C CB    . TRP B 261 ? 0.1763 0.2545 0.2357 0.0175  0.0298  -0.0148 402 TRP B CB    
5046 C CG    . TRP B 261 ? 0.1901 0.2692 0.2560 0.0174  0.0263  -0.0108 402 TRP B CG    
5047 C CD1   . TRP B 261 ? 0.1740 0.2597 0.2547 0.0159  0.0247  -0.0104 402 TRP B CD1   
5048 C CD2   . TRP B 261 ? 0.1363 0.2104 0.1942 0.0187  0.0240  -0.0065 402 TRP B CD2   
5049 N NE1   . TRP B 261 ? 0.2059 0.2910 0.2874 0.0158  0.0211  -0.0055 402 TRP B NE1   
5050 C CE2   . TRP B 261 ? 0.1950 0.2731 0.2623 0.0173  0.0209  -0.0034 402 TRP B CE2   
5051 C CE3   . TRP B 261 ? 0.1709 0.2380 0.2150 0.0211  0.0243  -0.0052 402 TRP B CE3   
5052 C CZ2   . TRP B 261 ? 0.1656 0.2413 0.2275 0.0173  0.0183  0.0008  402 TRP B CZ2   
5053 C CZ3   . TRP B 261 ? 0.2199 0.2845 0.2598 0.0218  0.0222  -0.0016 402 TRP B CZ3   
5054 C CH2   . TRP B 261 ? 0.1947 0.2638 0.2429 0.0195  0.0193  0.0012  402 TRP B CH2   
5055 N N     . GLN B 262 ? 0.1321 0.2193 0.2108 0.0239  0.0287  -0.0180 403 GLN B N     
5056 C CA    . GLN B 262 ? 0.1392 0.2299 0.2286 0.0266  0.0272  -0.0182 403 GLN B CA    
5057 C C     . GLN B 262 ? 0.1266 0.2209 0.2181 0.0270  0.0297  -0.0239 403 GLN B C     
5058 O O     . GLN B 262 ? 0.1393 0.2321 0.2190 0.0264  0.0318  -0.0257 403 GLN B O     
5059 C CB    . GLN B 262 ? 0.1149 0.2020 0.1966 0.0291  0.0249  -0.0135 403 GLN B CB    
5060 C CG    . GLN B 262 ? 0.1347 0.2190 0.2141 0.0280  0.0224  -0.0083 403 GLN B CG    
5061 C CD    . GLN B 262 ? 0.1956 0.2770 0.2664 0.0303  0.0209  -0.0045 403 GLN B CD    
5062 O OE1   . GLN B 262 ? 0.1926 0.2764 0.2665 0.0326  0.0204  -0.0044 403 GLN B OE1   
5063 N NE2   . GLN B 262 ? 0.1736 0.2498 0.2334 0.0293  0.0206  -0.0018 403 GLN B NE2   
5064 N N     . GLY B 263 ? 0.1257 0.2231 0.2304 0.0274  0.0291  -0.0260 404 GLY B N     
5065 C CA    . GLY B 263 ? 0.1043 0.2022 0.2084 0.0266  0.0305  -0.0306 404 GLY B CA    
5066 C C     . GLY B 263 ? 0.1514 0.2485 0.2562 0.0283  0.0285  -0.0292 404 GLY B C     
5067 O O     . GLY B 263 ? 0.1071 0.2030 0.2165 0.0297  0.0256  -0.0246 404 GLY B O     
5068 N N     . GLY B 264 ? 0.1387 0.2373 0.2389 0.0278  0.0299  -0.0331 405 GLY B N     
5069 C CA    . GLY B 264 ? 0.1252 0.2245 0.2267 0.0288  0.0282  -0.0326 405 GLY B CA    
5070 C C     . GLY B 264 ? 0.1596 0.2624 0.2515 0.0287  0.0296  -0.0358 405 GLY B C     
5071 O O     . GLY B 264 ? 0.1601 0.2650 0.2460 0.0271  0.0321  -0.0395 405 GLY B O     
5072 N N     . GLY B 265 ? 0.1437 0.2483 0.2344 0.0302  0.0278  -0.0341 406 GLY B N     
5073 C CA    . GLY B 265 ? 0.1427 0.2520 0.2241 0.0307  0.0283  -0.0360 406 GLY B CA    
5074 C C     . GLY B 265 ? 0.1836 0.2926 0.2524 0.0330  0.0290  -0.0332 406 GLY B C     
5075 O O     . GLY B 265 ? 0.1468 0.2517 0.2137 0.0345  0.0289  -0.0296 406 GLY B O     
5076 N N     . ASN B 266 ? 0.1522 0.2655 0.2114 0.0330  0.0295  -0.0347 407 ASN B N     
5077 C CA    . ASN B 266 ? 0.1781 0.2869 0.2220 0.0342  0.0292  -0.0304 407 ASN B CA    
5078 C C     . ASN B 266 ? 0.2105 0.3157 0.2495 0.0311  0.0318  -0.0317 407 ASN B C     
5079 O O     . ASN B 266 ? 0.1846 0.2893 0.2122 0.0295  0.0325  -0.0314 407 ASN B O     
5080 C CB    . ASN B 266 ? 0.1821 0.2852 0.2219 0.0386  0.0271  -0.0238 407 ASN B CB    
5081 C CG    . ASN B 266 ? 0.2803 0.3787 0.3051 0.0407  0.0264  -0.0196 407 ASN B CG    
5082 O OD1   . ASN B 266 ? 0.2936 0.3960 0.3132 0.0416  0.0252  -0.0192 407 ASN B OD1   
5083 N ND2   . ASN B 266 ? 0.2106 0.3002 0.2286 0.0413  0.0270  -0.0164 407 ASN B ND2   
5084 N N     . MET B 267 ? 0.1454 0.2484 0.1928 0.0299  0.0330  -0.0328 408 MET B N     
5085 C CA    . MET B 267 ? 0.1772 0.2779 0.2206 0.0266  0.0356  -0.0342 408 MET B CA    
5086 C C     . MET B 267 ? 0.1888 0.2966 0.2379 0.0225  0.0389  -0.0417 408 MET B C     
5087 O O     . MET B 267 ? 0.1675 0.2752 0.2112 0.0190  0.0415  -0.0433 408 MET B O     
5088 C CB    . MET B 267 ? 0.1478 0.2441 0.1974 0.0269  0.0353  -0.0318 408 MET B CB    
5089 C CG    . MET B 267 ? 0.1323 0.2322 0.1994 0.0273  0.0348  -0.0341 408 MET B CG    
5090 S SD    . MET B 267 ? 0.1793 0.2832 0.2577 0.0233  0.0377  -0.0408 408 MET B SD    
5091 C CE    . MET B 267 ? 0.1854 0.2885 0.2633 0.0214  0.0395  -0.0398 408 MET B CE    
5092 N N     . ILE B 268 ? 0.1756 0.2890 0.2346 0.0223  0.0389  -0.0466 409 ILE B N     
5093 C CA    . ILE B 268 ? 0.2121 0.3288 0.2745 0.0178  0.0413  -0.0533 409 ILE B CA    
5094 C C     . ILE B 268 ? 0.2154 0.3386 0.2665 0.0158  0.0423  -0.0559 409 ILE B C     
5095 O O     . ILE B 268 ? 0.2222 0.3469 0.2664 0.0183  0.0400  -0.0525 409 ILE B O     
5096 C CB    . ILE B 268 ? 0.2183 0.3339 0.2950 0.0176  0.0400  -0.0564 409 ILE B CB    
5097 C CG1   . ILE B 268 ? 0.1822 0.2991 0.2606 0.0199  0.0372  -0.0549 409 ILE B CG1   
5098 C CG2   . ILE B 268 ? 0.2382 0.3485 0.3255 0.0188  0.0390  -0.0537 409 ILE B CG2   
5099 C CD1   . ILE B 268 ? 0.2824 0.4062 0.3581 0.0172  0.0380  -0.0610 409 ILE B CD1   
5100 N N     . ALA B 269 ? 0.2228 0.3493 0.2713 0.0109  0.0452  -0.0613 410 ALA B N     
5101 C CA    . ALA B 269 ? 0.2481 0.3818 0.2877 0.0075  0.0461  -0.0650 410 ALA B CA    
5102 C C     . ALA B 269 ? 0.2388 0.3758 0.2883 0.0051  0.0464  -0.0725 410 ALA B C     
5103 O O     . ALA B 269 ? 0.3197 0.4631 0.3650 0.0037  0.0456  -0.0750 410 ALA B O     
5104 C CB    . ALA B 269 ? 0.2727 0.4084 0.3007 0.0026  0.0492  -0.0660 410 ALA B CB    
5105 N N     . ASP B 270 ? 0.2414 0.3747 0.3039 0.0046  0.0473  -0.0759 411 ASP B N     
5106 C CA    . ASP B 270 ? 0.2495 0.3848 0.3222 0.0024  0.0479  -0.0835 411 ASP B CA    
5107 C C     . ASP B 270 ? 0.2666 0.3951 0.3545 0.0047  0.0473  -0.0835 411 ASP B C     
5108 O O     . ASP B 270 ? 0.2486 0.3738 0.3388 0.0053  0.0481  -0.0811 411 ASP B O     
5109 C CB    . ASP B 270 ? 0.2729 0.4140 0.3408 -0.0034 0.0514  -0.0910 411 ASP B CB    
5110 C CG    . ASP B 270 ? 0.3266 0.4705 0.4041 -0.0060 0.0522  -0.0999 411 ASP B CG    
5111 O OD1   . ASP B 270 ? 0.3377 0.4865 0.4120 -0.0071 0.0512  -0.1024 411 ASP B OD1   
5112 O OD2   . ASP B 270 ? 0.3816 0.5231 0.4697 -0.0069 0.0541  -0.1048 411 ASP B OD2   
5113 N N     . VAL B 271 ? 0.1965 0.3235 0.2949 0.0056  0.0457  -0.0861 412 VAL B N     
5114 C CA    . VAL B 271 ? 0.2189 0.3397 0.3320 0.0076  0.0448  -0.0859 412 VAL B CA    
5115 C C     . VAL B 271 ? 0.2751 0.3973 0.3981 0.0048  0.0465  -0.0954 412 VAL B C     
5116 O O     . VAL B 271 ? 0.1891 0.3149 0.3116 0.0032  0.0462  -0.0996 412 VAL B O     
5117 C CB    . VAL B 271 ? 0.2250 0.3409 0.3426 0.0117  0.0409  -0.0784 412 VAL B CB    
5118 C CG1   . VAL B 271 ? 0.1730 0.2829 0.3058 0.0132  0.0397  -0.0781 412 VAL B CG1   
5119 C CG2   . VAL B 271 ? 0.1771 0.2914 0.2859 0.0144  0.0396  -0.0698 412 VAL B CG2   
5120 N N     . THR B 272 ? 0.2030 0.3232 0.3352 0.0041  0.0483  -0.0993 413 THR B N     
5121 C CA    . THR B 272 ? 0.2289 0.3476 0.3750 0.0030  0.0494  -0.1071 413 THR B CA    
5122 C C     . THR B 272 ? 0.2274 0.3389 0.3867 0.0066  0.0474  -0.1027 413 THR B C     
5123 O O     . THR B 272 ? 0.1913 0.3004 0.3479 0.0092  0.0458  -0.0948 413 THR B O     
5124 C CB    . THR B 272 ? 0.2563 0.3804 0.4023 -0.0014 0.0537  -0.1169 413 THR B CB    
5125 O OG1   . THR B 272 ? 0.2720 0.3949 0.4214 -0.0006 0.0551  -0.1155 413 THR B OG1   
5126 C CG2   . THR B 272 ? 0.2461 0.3783 0.3760 -0.0054 0.0554  -0.1191 413 THR B CG2   
5127 N N     . LEU B 273 ? 0.2073 0.3155 0.3814 0.0067  0.0475  -0.1078 414 LEU B N     
5128 C CA    . LEU B 273 ? 0.2324 0.3342 0.4197 0.0100  0.0455  -0.1035 414 LEU B CA    
5129 C C     . LEU B 273 ? 0.2611 0.3643 0.4494 0.0103  0.0472  -0.1032 414 LEU B C     
5130 O O     . LEU B 273 ? 0.2675 0.3673 0.4613 0.0133  0.0449  -0.0965 414 LEU B O     
5131 C CB    . LEU B 273 ? 0.2100 0.3081 0.4141 0.0096  0.0458  -0.1101 414 LEU B CB    
5132 C CG    . LEU B 273 ? 0.2917 0.3880 0.4976 0.0093  0.0438  -0.1100 414 LEU B CG    
5133 C CD1   . LEU B 273 ? 0.2617 0.3533 0.4864 0.0088  0.0441  -0.1163 414 LEU B CD1   
5134 C CD2   . LEU B 273 ? 0.2346 0.3279 0.4358 0.0124  0.0395  -0.0982 414 LEU B CD2   
5135 N N     . GLU B 274 ? 0.2313 0.3405 0.4140 0.0070  0.0512  -0.1103 415 GLU B N     
5136 C CA    . GLU B 274 ? 0.3028 0.4146 0.4874 0.0068  0.0533  -0.1111 415 GLU B CA    
5137 C C     . GLU B 274 ? 0.3204 0.4336 0.4930 0.0076  0.0523  -0.1028 415 GLU B C     
5138 O O     . GLU B 274 ? 0.3068 0.4192 0.4842 0.0096  0.0515  -0.0985 415 GLU B O     
5139 C CB    . GLU B 274 ? 0.3244 0.4428 0.5080 0.0024  0.0582  -0.1220 415 GLU B CB    
5140 C CG    . GLU B 274 ? 0.5079 0.6289 0.6996 0.0025  0.0608  -0.1250 415 GLU B CG    
5141 C CD    . GLU B 274 ? 0.6279 0.7574 0.8117 -0.0024 0.0656  -0.1326 415 GLU B CD    
5142 O OE1   . GLU B 274 ? 0.6164 0.7497 0.7844 -0.0055 0.0663  -0.1315 415 GLU B OE1   
5143 O OE2   . GLU B 274 ? 0.7155 0.8481 0.9092 -0.0033 0.0688  -0.1394 415 GLU B OE2   
5144 N N     . ARG B 275 ? 0.2586 0.3743 0.4160 0.0060  0.0524  -0.1006 416 ARG B N     
5145 C CA    . ARG B 275 ? 0.2609 0.3780 0.4070 0.0062  0.0521  -0.0939 416 ARG B CA    
5146 C C     . ARG B 275 ? 0.2699 0.3875 0.4025 0.0061  0.0507  -0.0900 416 ARG B C     
5147 O O     . ARG B 275 ? 0.2573 0.3766 0.3872 0.0047  0.0509  -0.0939 416 ARG B O     
5148 C CB    . ARG B 275 ? 0.2688 0.3920 0.4102 0.0026  0.0562  -0.0985 416 ARG B CB    
5149 C CG    . ARG B 275 ? 0.3773 0.5063 0.5118 -0.0021 0.0594  -0.1067 416 ARG B CG    
5150 C CD    . ARG B 275 ? 0.4097 0.5419 0.5264 -0.0044 0.0598  -0.1032 416 ARG B CD    
5151 N NE    . ARG B 275 ? 0.3634 0.5010 0.4720 -0.0085 0.0616  -0.1093 416 ARG B NE    
5152 C CZ    . ARG B 275 ? 0.3789 0.5166 0.4814 -0.0082 0.0596  -0.1081 416 ARG B CZ    
5153 N NH1   . ARG B 275 ? 0.3073 0.4396 0.4126 -0.0037 0.0560  -0.1019 416 ARG B NH1   
5154 N NH2   . ARG B 275 ? 0.4039 0.5483 0.4974 -0.0127 0.0613  -0.1132 416 ARG B NH2   
5155 N N     . SER B 276 ? 0.2566 0.3733 0.3809 0.0074  0.0496  -0.0826 417 SER B N     
5156 C CA    . SER B 276 ? 0.2739 0.3913 0.3850 0.0076  0.0486  -0.0785 417 SER B CA    
5157 C C     . SER B 276 ? 0.2652 0.3859 0.3639 0.0051  0.0510  -0.0773 417 SER B C     
5158 O O     . SER B 276 ? 0.2751 0.3955 0.3759 0.0048  0.0519  -0.0754 417 SER B O     
5159 C CB    . SER B 276 ? 0.2236 0.3360 0.3361 0.0118  0.0447  -0.0703 417 SER B CB    
5160 O OG    . SER B 276 ? 0.2904 0.3998 0.4138 0.0136  0.0424  -0.0709 417 SER B OG    
5161 N N     . LEU B 277 ? 0.2095 0.3338 0.2955 0.0030  0.0520  -0.0781 418 LEU B N     
5162 C CA    . LEU B 277 ? 0.2415 0.3682 0.3135 0.0004  0.0540  -0.0758 418 LEU B CA    
5163 C C     . LEU B 277 ? 0.2235 0.3471 0.2872 0.0038  0.0517  -0.0684 418 LEU B C     
5164 O O     . LEU B 277 ? 0.1948 0.3174 0.2597 0.0069  0.0490  -0.0666 418 LEU B O     
5165 C CB    . LEU B 277 ? 0.2529 0.3861 0.3148 -0.0045 0.0564  -0.0809 418 LEU B CB    
5166 C CG    . LEU B 277 ? 0.3200 0.4574 0.3895 -0.0081 0.0589  -0.0898 418 LEU B CG    
5167 C CD1   . LEU B 277 ? 0.3418 0.4864 0.3991 -0.0137 0.0611  -0.0942 418 LEU B CD1   
5168 C CD2   . LEU B 277 ? 0.2839 0.4209 0.3605 -0.0091 0.0611  -0.0909 418 LEU B CD2   
5169 N N     . TYR B 278 ? 0.2427 0.3652 0.2977 0.0030  0.0528  -0.0643 419 TYR B N     
5170 C CA    . TYR B 278 ? 0.2467 0.3655 0.2950 0.0067  0.0509  -0.0576 419 TYR B CA    
5171 C C     . TYR B 278 ? 0.2577 0.3776 0.2877 0.0051  0.0515  -0.0550 419 TYR B C     
5172 O O     . TYR B 278 ? 0.2614 0.3851 0.2830 0.0001  0.0543  -0.0574 419 TYR B O     
5173 C CB    . TYR B 278 ? 0.2665 0.3818 0.3184 0.0073  0.0512  -0.0542 419 TYR B CB    
5174 C CG    . TYR B 278 ? 0.2920 0.4059 0.3611 0.0090  0.0495  -0.0552 419 TYR B CG    
5175 C CD1   . TYR B 278 ? 0.3038 0.4153 0.3810 0.0128  0.0461  -0.0539 419 TYR B CD1   
5176 C CD2   . TYR B 278 ? 0.3005 0.4160 0.3775 0.0066  0.0511  -0.0574 419 TYR B CD2   
5177 C CE1   . TYR B 278 ? 0.3520 0.4616 0.4436 0.0141  0.0443  -0.0539 419 TYR B CE1   
5178 C CE2   . TYR B 278 ? 0.3868 0.5012 0.4793 0.0086  0.0491  -0.0578 419 TYR B CE2   
5179 C CZ    . TYR B 278 ? 0.3638 0.4748 0.4629 0.0123  0.0456  -0.0558 419 TYR B CZ    
5180 O OH    . TYR B 278 ? 0.3477 0.4570 0.4607 0.0140  0.0435  -0.0553 419 TYR B OH    
5181 N N     . GLN B 279 ? 0.2372 0.3507 0.2605 0.0093  0.0473  -0.0482 420 GLN B N     
5182 C CA    . GLN B 279 ? 0.2649 0.3740 0.2706 0.0091  0.0454  -0.0423 420 GLN B CA    
5183 C C     . GLN B 279 ? 0.2623 0.3633 0.2586 0.0072  0.0460  -0.0374 420 GLN B C     
5184 O O     . GLN B 279 ? 0.2896 0.3882 0.2930 0.0067  0.0471  -0.0378 420 GLN B O     
5185 C CB    . GLN B 279 ? 0.2871 0.3919 0.2907 0.0150  0.0409  -0.0367 420 GLN B CB    
5186 C CG    . GLN B 279 ? 0.2939 0.4061 0.3060 0.0167  0.0398  -0.0406 420 GLN B CG    
5187 C CD    . GLN B 279 ? 0.4443 0.5587 0.4454 0.0175  0.0372  -0.0376 420 GLN B CD    
5188 O OE1   . GLN B 279 ? 0.5080 0.6279 0.5016 0.0132  0.0385  -0.0401 420 GLN B OE1   
5189 N NE2   . GLN B 279 ? 0.4797 0.5908 0.4797 0.0229  0.0336  -0.0321 420 GLN B NE2   
5190 N N     . GLY B 280 ? 0.2850 0.3815 0.2654 0.0061  0.0447  -0.0322 421 GLY B N     
5191 C CA    . GLY B 280 ? 0.3152 0.4012 0.2853 0.0051  0.0443  -0.0262 421 GLY B CA    
5192 C C     . GLY B 280 ? 0.3053 0.3813 0.2737 0.0115  0.0405  -0.0201 421 GLY B C     
5193 O O     . GLY B 280 ? 0.2898 0.3679 0.2648 0.0165  0.0383  -0.0202 421 GLY B O     
5194 N N     . PRO B 281 ? 0.3218 0.3869 0.2815 0.0109  0.0401  -0.0152 422 PRO B N     
5195 C CA    . PRO B 281 ? 0.3079 0.3630 0.2659 0.0167  0.0372  -0.0103 422 PRO B CA    
5196 C C     . PRO B 281 ? 0.3010 0.3525 0.2505 0.0215  0.0341  -0.0055 422 PRO B C     
5197 O O     . PRO B 281 ? 0.3259 0.3792 0.2667 0.0195  0.0337  -0.0038 422 PRO B O     
5198 C CB    . PRO B 281 ? 0.3316 0.3762 0.2821 0.0133  0.0382  -0.0075 422 PRO B CB    
5199 C CG    . PRO B 281 ? 0.3989 0.4463 0.3422 0.0064  0.0407  -0.0083 422 PRO B CG    
5200 C CD    . PRO B 281 ? 0.3203 0.3822 0.2729 0.0044  0.0427  -0.0147 422 PRO B CD    
5201 N N     . PRO B 282 ? 0.2905 0.3380 0.2426 0.0279  0.0318  -0.0031 423 PRO B N     
5202 C CA    . PRO B 282 ? 0.2765 0.3222 0.2374 0.0304  0.0318  -0.0044 423 PRO B CA    
5203 C C     . PRO B 282 ? 0.2623 0.3194 0.2379 0.0309  0.0321  -0.0091 423 PRO B C     
5204 O O     . PRO B 282 ? 0.2384 0.2956 0.2223 0.0311  0.0323  -0.0103 423 PRO B O     
5205 C CB    . PRO B 282 ? 0.2604 0.2985 0.2163 0.0370  0.0294  0.0001  423 PRO B CB    
5206 C CG    . PRO B 282 ? 0.3236 0.3657 0.2751 0.0396  0.0274  0.0023  423 PRO B CG    
5207 C CD    . PRO B 282 ? 0.2487 0.2950 0.1953 0.0333  0.0288  0.0010  423 PRO B CD    
5208 N N     . ASN B 283 ? 0.2232 0.2897 0.2020 0.0306  0.0319  -0.0117 424 ASN B N     
5209 C CA    . ASN B 283 ? 0.2407 0.3167 0.2333 0.0313  0.0319  -0.0160 424 ASN B CA    
5210 C C     . ASN B 283 ? 0.2091 0.2875 0.2125 0.0280  0.0340  -0.0200 424 ASN B C     
5211 O O     . ASN B 283 ? 0.1732 0.2547 0.1883 0.0296  0.0333  -0.0213 424 ASN B O     
5212 C CB    . ASN B 283 ? 0.2538 0.3393 0.2468 0.0297  0.0320  -0.0193 424 ASN B CB    
5213 C CG    . ASN B 283 ? 0.3225 0.4072 0.3052 0.0329  0.0293  -0.0148 424 ASN B CG    
5214 O OD1   . ASN B 283 ? 0.3227 0.4005 0.2932 0.0326  0.0287  -0.0105 424 ASN B OD1   
5215 N ND2   . ASN B 283 ? 0.3390 0.4307 0.3271 0.0358  0.0273  -0.0154 424 ASN B ND2   
5216 N N     . LYS B 284 ? 0.1890 0.2667 0.1890 0.0231  0.0365  -0.0217 425 LYS B N     
5217 C CA    . LYS B 284 ? 0.1953 0.2761 0.2059 0.0198  0.0387  -0.0254 425 LYS B CA    
5218 C C     . LYS B 284 ? 0.1792 0.2562 0.1967 0.0221  0.0370  -0.0230 425 LYS B C     
5219 O O     . LYS B 284 ? 0.1500 0.2319 0.1811 0.0214  0.0373  -0.0257 425 LYS B O     
5220 C CB    . LYS B 284 ? 0.2108 0.2890 0.2131 0.0145  0.0412  -0.0255 425 LYS B CB    
5221 C CG    . LYS B 284 ? 0.2863 0.3694 0.2995 0.0107  0.0438  -0.0295 425 LYS B CG    
5222 C CD    . LYS B 284 ? 0.2916 0.3724 0.2945 0.0049  0.0464  -0.0291 425 LYS B CD    
5223 C CE    . LYS B 284 ? 0.3261 0.4132 0.3395 0.0006  0.0493  -0.0332 425 LYS B CE    
5224 N NZ    . LYS B 284 ? 0.3605 0.4432 0.3621 -0.0051 0.0511  -0.0310 425 LYS B NZ    
5225 N N     . PHE B 285 ? 0.1552 0.2236 0.1637 0.0247  0.0351  -0.0179 426 PHE B N     
5226 C CA    . PHE B 285 ? 0.1527 0.2173 0.1651 0.0259  0.0336  -0.0155 426 PHE B CA    
5227 C C     . PHE B 285 ? 0.1774 0.2425 0.1929 0.0309  0.0313  -0.0133 426 PHE B C     
5228 O O     . PHE B 285 ? 0.2017 0.2638 0.2187 0.0318  0.0300  -0.0110 426 PHE B O     
5229 C CB    . PHE B 285 ? 0.1885 0.2427 0.1884 0.0243  0.0338  -0.0122 426 PHE B CB    
5230 C CG    . PHE B 285 ? 0.1824 0.2362 0.1786 0.0187  0.0362  -0.0138 426 PHE B CG    
5231 C CD1   . PHE B 285 ? 0.2618 0.3218 0.2687 0.0149  0.0374  -0.0167 426 PHE B CD1   
5232 C CD2   . PHE B 285 ? 0.2290 0.2775 0.2121 0.0170  0.0372  -0.0123 426 PHE B CD2   
5233 C CE1   . PHE B 285 ? 0.2184 0.2799 0.2229 0.0094  0.0401  -0.0186 426 PHE B CE1   
5234 C CE2   . PHE B 285 ? 0.2858 0.3351 0.2655 0.0110  0.0397  -0.0137 426 PHE B CE2   
5235 C CZ    . PHE B 285 ? 0.2424 0.2985 0.2328 0.0072  0.0413  -0.0171 426 PHE B CZ    
5236 N N     . GLU B 286 ? 0.1674 0.2368 0.1836 0.0336  0.0307  -0.0141 427 GLU B N     
5237 C CA    . GLU B 286 ? 0.1884 0.2596 0.2080 0.0379  0.0287  -0.0121 427 GLU B CA    
5238 C C     . GLU B 286 ? 0.1660 0.2465 0.1989 0.0375  0.0284  -0.0155 427 GLU B C     
5239 O O     . GLU B 286 ? 0.1676 0.2530 0.2004 0.0376  0.0287  -0.0179 427 GLU B O     
5240 C CB    . GLU B 286 ? 0.1812 0.2491 0.1901 0.0419  0.0278  -0.0094 427 GLU B CB    
5241 C CG    . GLU B 286 ? 0.2065 0.2634 0.2023 0.0422  0.0282  -0.0064 427 GLU B CG    
5242 C CD    . GLU B 286 ? 0.2654 0.3182 0.2514 0.0468  0.0272  -0.0034 427 GLU B CD    
5243 O OE1   . GLU B 286 ? 0.2622 0.3216 0.2495 0.0486  0.0261  -0.0036 427 GLU B OE1   
5244 O OE2   . GLU B 286 ? 0.2493 0.2920 0.2261 0.0483  0.0273  -0.0007 427 GLU B OE2   
5245 N N     . ALA B 287 ? 0.1586 0.2414 0.2030 0.0368  0.0277  -0.0156 428 ALA B N     
5246 C CA    . ALA B 287 ? 0.1788 0.2687 0.2372 0.0362  0.0273  -0.0186 428 ALA B CA    
5247 C C     . ALA B 287 ? 0.1670 0.2592 0.2283 0.0391  0.0252  -0.0160 428 ALA B C     
5248 O O     . ALA B 287 ? 0.1555 0.2449 0.2146 0.0405  0.0239  -0.0118 428 ALA B O     
5249 C CB    . ALA B 287 ? 0.1351 0.2260 0.2055 0.0338  0.0273  -0.0195 428 ALA B CB    
5250 N N     . GLY B 288 ? 0.1277 0.2257 0.1938 0.0394  0.0250  -0.0186 429 GLY B N     
5251 C CA    . GLY B 288 ? 0.1361 0.2355 0.2050 0.0406  0.0229  -0.0160 429 GLY B CA    
5252 C C     . GLY B 288 ? 0.2238 0.3234 0.2817 0.0442  0.0223  -0.0134 429 GLY B C     
5253 O O     . GLY B 288 ? 0.2020 0.2994 0.2495 0.0461  0.0233  -0.0131 429 GLY B O     
5254 N N     . THR B 289 ? 0.1566 0.2581 0.2171 0.0447  0.0205  -0.0113 430 THR B N     
5255 C CA    . THR B 289 ? 0.1939 0.2960 0.2460 0.0482  0.0197  -0.0087 430 THR B CA    
5256 C C     . THR B 289 ? 0.1800 0.2763 0.2234 0.0513  0.0206  -0.0057 430 THR B C     
5257 O O     . THR B 289 ? 0.2144 0.3083 0.2600 0.0504  0.0207  -0.0040 430 THR B O     
5258 C CB    . THR B 289 ? 0.2321 0.3379 0.2899 0.0475  0.0181  -0.0072 430 THR B CB    
5259 O OG1   . THR B 289 ? 0.1916 0.3025 0.2576 0.0447  0.0175  -0.0102 430 THR B OG1   
5260 C CG2   . THR B 289 ? 0.2027 0.3101 0.2530 0.0513  0.0174  -0.0048 430 THR B CG2   
5261 N N     . GLY B 290 ? 0.2036 0.2979 0.2373 0.0550  0.0213  -0.0051 431 GLY B N     
5262 C CA    . GLY B 290 ? 0.2536 0.3409 0.2786 0.0581  0.0224  -0.0027 431 GLY B CA    
5263 C C     . GLY B 290 ? 0.2439 0.3315 0.2682 0.0604  0.0217  -0.0004 431 GLY B C     
5264 O O     . GLY B 290 ? 0.2548 0.3478 0.2834 0.0600  0.0201  -0.0002 431 GLY B O     
5265 N N     . ASN B 291 ? 0.1979 0.2796 0.2163 0.0625  0.0231  0.0008  432 ASN B N     
5266 C CA    . ASN B 291 ? 0.2320 0.3135 0.2479 0.0650  0.0232  0.0022  432 ASN B CA    
5267 C C     . ASN B 291 ? 0.1961 0.2752 0.2056 0.0702  0.0231  0.0029  432 ASN B C     
5268 O O     . ASN B 291 ? 0.1953 0.2669 0.1970 0.0743  0.0246  0.0033  432 ASN B O     
5269 C CB    . ASN B 291 ? 0.1769 0.2536 0.1886 0.0653  0.0253  0.0026  432 ASN B CB    
5270 C CG    . ASN B 291 ? 0.1932 0.2717 0.2036 0.0671  0.0259  0.0032  432 ASN B CG    
5271 O OD1   . ASN B 291 ? 0.1930 0.2760 0.2057 0.0684  0.0248  0.0035  432 ASN B OD1   
5272 N ND2   . ASN B 291 ? 0.2019 0.2776 0.2084 0.0666  0.0278  0.0031  432 ASN B ND2   
5273 N N     . ILE B 292 ? 0.1578 0.2436 0.1711 0.0704  0.0212  0.0030  433 ILE B N     
5274 C CA    . ILE B 292 ? 0.1870 0.2726 0.1956 0.0757  0.0204  0.0043  433 ILE B CA    
5275 C C     . ILE B 292 ? 0.1953 0.2777 0.2006 0.0799  0.0212  0.0053  433 ILE B C     
5276 O O     . ILE B 292 ? 0.1909 0.2664 0.1895 0.0853  0.0218  0.0064  433 ILE B O     
5277 C CB    . ILE B 292 ? 0.2371 0.3328 0.2511 0.0747  0.0181  0.0041  433 ILE B CB    
5278 C CG1   . ILE B 292 ? 0.2807 0.3802 0.2992 0.0699  0.0179  0.0019  433 ILE B CG1   
5279 C CG2   . ILE B 292 ? 0.1916 0.2884 0.2007 0.0806  0.0169  0.0062  433 ILE B CG2   
5280 C CD1   . ILE B 292 ? 0.3422 0.4384 0.3546 0.0716  0.0190  0.0016  433 ILE B CD1   
5281 N N     . ALA B 293 ? 0.1943 0.2818 0.2047 0.0779  0.0213  0.0048  434 ALA B N     
5282 C CA    . ALA B 293 ? 0.1714 0.2585 0.1801 0.0818  0.0223  0.0050  434 ALA B CA    
5283 C C     . ALA B 293 ? 0.1785 0.2551 0.1798 0.0846  0.0249  0.0043  434 ALA B C     
5284 O O     . ALA B 293 ? 0.1874 0.2590 0.1848 0.0900  0.0258  0.0043  434 ALA B O     
5285 C CB    . ALA B 293 ? 0.1625 0.2581 0.1779 0.0787  0.0224  0.0046  434 ALA B CB    
5286 N N     . ASP B 294 ? 0.1744 0.2475 0.1741 0.0811  0.0263  0.0034  435 ASP B N     
5287 C CA    . ASP B 294 ? 0.1973 0.2607 0.1894 0.0833  0.0291  0.0021  435 ASP B CA    
5288 C C     . ASP B 294 ? 0.2168 0.2689 0.2011 0.0869  0.0296  0.0025  435 ASP B C     
5289 O O     . ASP B 294 ? 0.1829 0.2249 0.1602 0.0906  0.0317  0.0014  435 ASP B O     
5290 C CB    . ASP B 294 ? 0.1755 0.2396 0.1678 0.0786  0.0305  0.0013  435 ASP B CB    
5291 C CG    . ASP B 294 ? 0.2859 0.3602 0.2843 0.0759  0.0305  0.0014  435 ASP B CG    
5292 O OD1   . ASP B 294 ? 0.2714 0.3492 0.2708 0.0784  0.0310  0.0009  435 ASP B OD1   
5293 O OD2   . ASP B 294 ? 0.2631 0.3421 0.2654 0.0716  0.0302  0.0022  435 ASP B OD2   
5294 N N     . ALA B 295 ? 0.1725 0.2256 0.1576 0.0858  0.0280  0.0038  436 ALA B N     
5295 C CA    . ALA B 295 ? 0.1829 0.2253 0.1601 0.0881  0.0277  0.0051  436 ALA B CA    
5296 C C     . ALA B 295 ? 0.2016 0.2427 0.1775 0.0962  0.0273  0.0068  436 ALA B C     
5297 O O     . ALA B 295 ? 0.2325 0.2606 0.2007 0.0993  0.0279  0.0075  436 ALA B O     
5298 C CB    . ALA B 295 ? 0.1695 0.2151 0.1481 0.0834  0.0257  0.0060  436 ALA B CB    
5299 N N     . VAL B 296 ? 0.2329 0.2855 0.2160 0.0968  0.0251  0.0076  437 VAL B N     
5300 C CA    . VAL B 296 ? 0.2330 0.2854 0.2162 0.1029  0.0239  0.0093  437 VAL B CA    
5301 C C     . VAL B 296 ? 0.2197 0.2645 0.2006 0.1060  0.0265  0.0073  437 VAL B C     
5302 O O     . VAL B 296 ? 0.2200 0.2554 0.1968 0.1119  0.0268  0.0082  437 VAL B O     
5303 C CB    . VAL B 296 ? 0.1927 0.2598 0.1845 0.1016  0.0215  0.0099  437 VAL B CB    
5304 C CG1   . VAL B 296 ? 0.2212 0.2897 0.2149 0.1075  0.0207  0.0112  437 VAL B CG1   
5305 C CG2   . VAL B 296 ? 0.1983 0.2722 0.1915 0.0997  0.0189  0.0116  437 VAL B CG2   
5306 N N     . GLY B 297 ? 0.2137 0.2623 0.1971 0.1020  0.0284  0.0044  438 GLY B N     
5307 C CA    . GLY B 297 ? 0.1809 0.2235 0.1617 0.1044  0.0315  0.0016  438 GLY B CA    
5308 C C     . GLY B 297 ? 0.2342 0.2602 0.2052 0.1062  0.0338  0.0003  438 GLY B C     
5309 O O     . GLY B 297 ? 0.2366 0.2536 0.2042 0.1106  0.0357  -0.0015 438 GLY B O     
5310 N N     . LEU B 298 ? 0.2196 0.2409 0.1860 0.1027  0.0338  0.0009  439 LEU B N     
5311 C CA    . LEU B 298 ? 0.2105 0.2148 0.1665 0.1030  0.0358  -0.0001 439 LEU B CA    
5312 C C     . LEU B 298 ? 0.2484 0.2416 0.2002 0.1085  0.0343  0.0028  439 LEU B C     
5313 O O     . LEU B 298 ? 0.2613 0.2391 0.2060 0.1107  0.0359  0.0017  439 LEU B O     
5314 C CB    . LEU B 298 ? 0.2212 0.2241 0.1748 0.0938  0.0346  0.0004  439 LEU B CB    
5315 C CG    . LEU B 298 ? 0.2655 0.2512 0.2087 0.0901  0.0351  0.0003  439 LEU B CG    
5316 C CD1   . LEU B 298 ? 0.2496 0.2258 0.1869 0.0904  0.0382  -0.0037 439 LEU B CD1   
5317 C CD2   . LEU B 298 ? 0.2780 0.2648 0.2204 0.0813  0.0338  0.0010  439 LEU B CD2   
5318 N N     . GLY B 299 ? 0.2133 0.2137 0.1690 0.1104  0.0311  0.0068  440 GLY B N     
5319 C CA    . GLY B 299 ? 0.2578 0.2490 0.2099 0.1161  0.0291  0.0106  440 GLY B CA    
5320 C C     . GLY B 299 ? 0.2687 0.2566 0.2234 0.1238  0.0302  0.0096  440 GLY B C     
5321 O O     . GLY B 299 ? 0.2906 0.2632 0.2398 0.1284  0.0303  0.0109  440 GLY B O     
5322 N N     . GLU B 300 ? 0.2487 0.2505 0.2121 0.1229  0.0305  0.0071  441 GLU B N     
5323 C CA    . GLU B 300 ? 0.2874 0.2876 0.2544 0.1277  0.0318  0.0050  441 GLU B CA    
5324 C C     . GLU B 300 ? 0.3073 0.2929 0.2677 0.1280  0.0359  0.0004  441 GLU B C     
5325 O O     . GLU B 300 ? 0.3133 0.2884 0.2729 0.1334  0.0368  -0.0006 441 GLU B O     
5326 C CB    . GLU B 300 ? 0.2566 0.2748 0.2335 0.1259  0.0318  0.0032  441 GLU B CB    
5327 C CG    . GLU B 300 ? 0.2985 0.3190 0.2815 0.1310  0.0331  0.0010  441 GLU B CG    
5328 C CD    . GLU B 300 ? 0.3873 0.4068 0.3739 0.1377  0.0300  0.0052  441 GLU B CD    
5329 O OE1   . GLU B 300 ? 0.3748 0.4028 0.3638 0.1369  0.0263  0.0095  441 GLU B OE1   
5330 O OE2   . GLU B 300 ? 0.3778 0.3892 0.3658 0.1435  0.0312  0.0039  441 GLU B OE2   
5331 N N     . ALA B 301 ? 0.2626 0.2475 0.2186 0.1221  0.0382  -0.0027 442 ALA B N     
5332 C CA    . ALA B 301 ? 0.2683 0.2394 0.2166 0.1212  0.0421  -0.0075 442 ALA B CA    
5333 C C     . ALA B 301 ? 0.2907 0.2406 0.2294 0.1239  0.0421  -0.0059 442 ALA B C     
5334 O O     . ALA B 301 ? 0.2891 0.2248 0.2234 0.1263  0.0445  -0.0092 442 ALA B O     
5335 C CB    . ALA B 301 ? 0.2324 0.2081 0.1776 0.1137  0.0439  -0.0102 442 ALA B CB    
5336 N N     . ILE B 302 ? 0.2756 0.2226 0.2108 0.1228  0.0395  -0.0011 443 ILE B N     
5337 C CA    . ILE B 302 ? 0.2946 0.2224 0.2210 0.1216  0.0382  0.0018  443 ILE B CA    
5338 C C     . ILE B 302 ? 0.3473 0.2661 0.2753 0.1320  0.0373  0.0043  443 ILE B C     
5339 O O     . ILE B 302 ? 0.3672 0.2669 0.2889 0.1340  0.0386  0.0034  443 ILE B O     
5340 C CB    . ILE B 302 ? 0.3183 0.2493 0.2424 0.1146  0.0346  0.0069  443 ILE B CB    
5341 C CG1   . ILE B 302 ? 0.3014 0.2355 0.2226 0.1041  0.0357  0.0041  443 ILE B CG1   
5342 C CG2   . ILE B 302 ? 0.3371 0.2508 0.2532 0.1148  0.0325  0.0116  443 ILE B CG2   
5343 C CD1   . ILE B 302 ? 0.3187 0.2583 0.2393 0.0974  0.0329  0.0079  443 ILE B CD1   
5344 N N     . ARG B 303 ? 0.3098 0.2436 0.2475 0.1357  0.0343  0.0076  444 ARG B N     
5345 C CA    . ARG B 303 ? 0.3728 0.3020 0.3149 0.1427  0.0324  0.0101  444 ARG B CA    
5346 C C     . ARG B 303 ? 0.3646 0.2880 0.3096 0.1454  0.0361  0.0038  444 ARG B C     
5347 O O     . ARG B 303 ? 0.3478 0.2567 0.2919 0.1501  0.0359  0.0044  444 ARG B O     
5348 C CB    . ARG B 303 ? 0.3593 0.3079 0.3119 0.1452  0.0287  0.0138  444 ARG B CB    
5349 C CG    . ARG B 303 ? 0.3342 0.2850 0.2836 0.1444  0.0243  0.0211  444 ARG B CG    
5350 C CD    . ARG B 303 ? 0.3746 0.3439 0.3339 0.1467  0.0205  0.0243  444 ARG B CD    
5351 N NE    . ARG B 303 ? 0.3629 0.3515 0.3294 0.1426  0.0216  0.0207  444 ARG B NE    
5352 C CZ    . ARG B 303 ? 0.3520 0.3495 0.3172 0.1370  0.0211  0.0208  444 ARG B CZ    
5353 N NH1   . ARG B 303 ? 0.3578 0.3480 0.3149 0.1352  0.0199  0.0243  444 ARG B NH1   
5354 N NH2   . ARG B 303 ? 0.3371 0.3507 0.3095 0.1330  0.0219  0.0177  444 ARG B NH2   
5355 N N     . TYR B 304 ? 0.3596 0.2942 0.3082 0.1423  0.0394  -0.0023 445 TYR B N     
5356 C CA    . TYR B 304 ? 0.3544 0.2839 0.3048 0.1443  0.0434  -0.0091 445 TYR B CA    
5357 C C     . TYR B 304 ? 0.3700 0.2762 0.3091 0.1429  0.0460  -0.0121 445 TYR B C     
5358 O O     . TYR B 304 ? 0.4029 0.2961 0.3426 0.1474  0.0473  -0.0143 445 TYR B O     
5359 C CB    . TYR B 304 ? 0.3478 0.2932 0.3020 0.1398  0.0464  -0.0144 445 TYR B CB    
5360 C CG    . TYR B 304 ? 0.3686 0.3128 0.3264 0.1423  0.0508  -0.0216 445 TYR B CG    
5361 C CD1   . TYR B 304 ? 0.3401 0.2707 0.2894 0.1396  0.0548  -0.0278 445 TYR B CD1   
5362 C CD2   . TYR B 304 ? 0.3647 0.3214 0.3343 0.1471  0.0510  -0.0227 445 TYR B CD2   
5363 C CE1   . TYR B 304 ? 0.3887 0.3185 0.3412 0.1416  0.0591  -0.0352 445 TYR B CE1   
5364 C CE2   . TYR B 304 ? 0.3688 0.3249 0.3422 0.1494  0.0555  -0.0299 445 TYR B CE2   
5365 C CZ    . TYR B 304 ? 0.4158 0.3584 0.3805 0.1467  0.0597  -0.0363 445 TYR B CZ    
5366 O OH    . TYR B 304 ? 0.4475 0.3896 0.4157 0.1487  0.0646  -0.0444 445 TYR B OH    
5367 N N     . VAL B 305 ? 0.3342 0.2347 0.2633 0.1364  0.0468  -0.0123 446 VAL B N     
5368 C CA    . VAL B 305 ? 0.3792 0.2571 0.2966 0.1337  0.0491  -0.0151 446 VAL B CA    
5369 C C     . VAL B 305 ? 0.4327 0.2923 0.3470 0.1380  0.0464  -0.0097 446 VAL B C     
5370 O O     . VAL B 305 ? 0.4306 0.2718 0.3406 0.1391  0.0481  -0.0125 446 VAL B O     
5371 C CB    . VAL B 305 ? 0.3964 0.2726 0.3042 0.1255  0.0500  -0.0156 446 VAL B CB    
5372 C CG1   . VAL B 305 ? 0.3925 0.2457 0.2883 0.1201  0.0512  -0.0175 446 VAL B CG1   
5373 C CG2   . VAL B 305 ? 0.3435 0.2363 0.2543 0.1208  0.0526  -0.0210 446 VAL B CG2   
5374 N N     . GLU B 306 ? 0.3910 0.2559 0.3077 0.1403  0.0419  -0.0016 447 GLU B N     
5375 C CA    . GLU B 306 ? 0.4351 0.2831 0.3478 0.1434  0.0386  0.0050  447 GLU B CA    
5376 C C     . GLU B 306 ? 0.4532 0.2977 0.3746 0.1509  0.0380  0.0045  447 GLU B C     
5377 O O     . GLU B 306 ? 0.4632 0.2878 0.3808 0.1527  0.0373  0.0063  447 GLU B O     
5378 C CB    . GLU B 306 ? 0.4097 0.2669 0.3230 0.1436  0.0337  0.0137  447 GLU B CB    
5379 C CG    . GLU B 306 ? 0.4281 0.2841 0.3323 0.1333  0.0330  0.0157  447 GLU B CG    
5380 C CD    . GLU B 306 ? 0.5143 0.3836 0.4204 0.1311  0.0282  0.0231  447 GLU B CD    
5381 O OE1   . GLU B 306 ? 0.4476 0.3339 0.3631 0.1370  0.0265  0.0246  447 GLU B OE1   
5382 O OE2   . GLU B 306 ? 0.4698 0.3337 0.3681 0.1229  0.0264  0.0270  447 GLU B OE2   
5383 N N     . ARG B 307 ? 0.4675 0.3309 0.4013 0.1551  0.0382  0.0022  448 ARG B N     
5384 C CA    . ARG B 307 ? 0.4464 0.3076 0.3901 0.1625  0.0383  0.0007  448 ARG B CA    
5385 C C     . ARG B 307 ? 0.4829 0.3283 0.4233 0.1622  0.0432  -0.0076 448 ARG B C     
5386 O O     . ARG B 307 ? 0.4891 0.3200 0.4323 0.1671  0.0428  -0.0076 448 ARG B O     
5387 C CB    . ARG B 307 ? 0.5112 0.3964 0.4684 0.1659  0.0382  -0.0010 448 ARG B CB    
5388 C CG    . ARG B 307 ? 0.5415 0.4404 0.5046 0.1682  0.0326  0.0073  448 ARG B CG    
5389 C CD    . ARG B 307 ? 0.5940 0.5135 0.5715 0.1723  0.0325  0.0056  448 ARG B CD    
5390 N NE    . ARG B 307 ? 0.5661 0.4993 0.5456 0.1680  0.0367  -0.0014 448 ARG B NE    
5391 C CZ    . ARG B 307 ? 0.5370 0.4859 0.5160 0.1625  0.0360  -0.0003 448 ARG B CZ    
5392 N NH1   . ARG B 307 ? 0.4770 0.4310 0.4539 0.1608  0.0316  0.0064  448 ARG B NH1   
5393 N NH2   . ARG B 307 ? 0.4618 0.4216 0.4425 0.1584  0.0397  -0.0063 448 ARG B NH2   
5394 N N     . VAL B 308 ? 0.4632 0.3110 0.3979 0.1562  0.0476  -0.0147 449 VAL B N     
5395 C CA    . VAL B 308 ? 0.5088 0.3421 0.4398 0.1551  0.0522  -0.0232 449 VAL B CA    
5396 C C     . VAL B 308 ? 0.4820 0.2892 0.4007 0.1518  0.0517  -0.0213 449 VAL B C     
5397 O O     . VAL B 308 ? 0.5564 0.3467 0.4749 0.1541  0.0532  -0.0249 449 VAL B O     
5398 C CB    . VAL B 308 ? 0.4548 0.2988 0.3827 0.1489  0.0569  -0.0313 449 VAL B CB    
5399 C CG1   . VAL B 308 ? 0.4534 0.2824 0.3763 0.1470  0.0616  -0.0405 449 VAL B CG1   
5400 C CG2   . VAL B 308 ? 0.4216 0.2903 0.3617 0.1516  0.0575  -0.0330 449 VAL B CG2   
5401 N N     . GLY B 309 ? 0.4651 0.2684 0.3738 0.1461  0.0495  -0.0158 450 GLY B N     
5402 C CA    . GLY B 309 ? 0.5157 0.2949 0.4120 0.1414  0.0488  -0.0133 450 GLY B CA    
5403 C C     . GLY B 309 ? 0.5167 0.2887 0.4010 0.1320  0.0526  -0.0195 450 GLY B C     
5404 O O     . GLY B 309 ? 0.4886 0.2581 0.3724 0.1303  0.0568  -0.0284 450 GLY B O     
5405 N N     . ILE B 310 ? 0.4852 0.2540 0.3599 0.1254  0.0512  -0.0152 451 ILE B N     
5406 C CA    . ILE B 310 ? 0.4700 0.2376 0.3355 0.1150  0.0541  -0.0209 451 ILE B CA    
5407 C C     . ILE B 310 ? 0.5477 0.2902 0.4029 0.1105  0.0568  -0.0261 451 ILE B C     
5408 O O     . ILE B 310 ? 0.5126 0.2553 0.3626 0.1035  0.0601  -0.0339 451 ILE B O     
5409 C CB    . ILE B 310 ? 0.5053 0.2843 0.3685 0.1052  0.0502  -0.0145 451 ILE B CB    
5410 C CG1   . ILE B 310 ? 0.5029 0.2895 0.3615 0.0939  0.0521  -0.0199 451 ILE B CG1   
5411 C CG2   . ILE B 310 ? 0.4991 0.2612 0.3553 0.1014  0.0470  -0.0073 451 ILE B CG2   
5412 C CD1   . ILE B 310 ? 0.4717 0.2773 0.3365 0.0957  0.0548  -0.0259 451 ILE B CD1   
5413 N N     . GLU B 311 ? 0.5418 0.2649 0.3952 0.1128  0.0547  -0.0217 452 GLU B N     
5414 C CA    . GLU B 311 ? 0.5969 0.2981 0.4429 0.1079  0.0569  -0.0269 452 GLU B CA    
5415 C C     . GLU B 311 ? 0.5112 0.2148 0.3646 0.1126  0.0605  -0.0363 452 GLU B C     
5416 O O     . GLU B 311 ? 0.5622 0.2564 0.4092 0.1064  0.0640  -0.0446 452 GLU B O     
5417 C CB    . GLU B 311 ? 0.5754 0.2557 0.4184 0.1085  0.0534  -0.0191 452 GLU B CB    
5418 C CG    . GLU B 311 ? 0.6558 0.3332 0.4914 0.1037  0.0496  -0.0089 452 GLU B CG    
5419 C CD    . GLU B 311 ? 0.7312 0.4279 0.5755 0.1108  0.0459  -0.0010 452 GLU B CD    
5420 O OE1   . GLU B 311 ? 0.6692 0.3834 0.5246 0.1188  0.0467  -0.0040 452 GLU B OE1   
5421 O OE2   . GLU B 311 ? 0.7674 0.4668 0.6089 0.1061  0.0418  0.0078  452 GLU B OE2   
5422 N N     . ARG B 312 ? 0.5013 0.2181 0.3683 0.1228  0.0598  -0.0355 453 ARG B N     
5423 C CA    . ARG B 312 ? 0.5217 0.2433 0.3966 0.1271  0.0637  -0.0451 453 ARG B CA    
5424 C C     . ARG B 312 ? 0.5426 0.2806 0.4150 0.1217  0.0676  -0.0530 453 ARG B C     
5425 O O     . ARG B 312 ? 0.5544 0.2890 0.4248 0.1188  0.0717  -0.0627 453 ARG B O     
5426 C CB    . ARG B 312 ? 0.5438 0.2772 0.4345 0.1387  0.0620  -0.0422 453 ARG B CB    
5427 C CG    . ARG B 312 ? 0.6377 0.3581 0.5321 0.1444  0.0572  -0.0330 453 ARG B CG    
5428 C CD    . ARG B 312 ? 0.6248 0.3584 0.5359 0.1555  0.0555  -0.0310 453 ARG B CD    
5429 N NE    . ARG B 312 ? 0.6799 0.4153 0.6000 0.1600  0.0598  -0.0413 453 ARG B NE    
5430 C CZ    . ARG B 312 ? 0.7590 0.5157 0.6904 0.1647  0.0618  -0.0455 453 ARG B CZ    
5431 N NH1   . ARG B 312 ? 0.6530 0.4313 0.5875 0.1645  0.0600  -0.0410 453 ARG B NH1   
5432 N NH2   . ARG B 312 ? 0.6007 0.3570 0.5407 0.1692  0.0657  -0.0548 453 ARG B NH2   
5433 N N     . ILE B 313 ? 0.5013 0.2575 0.3742 0.1199  0.0662  -0.0489 454 ILE B N     
5434 C CA    . ILE B 313 ? 0.5329 0.3047 0.4029 0.1137  0.0691  -0.0549 454 ILE B CA    
5435 C C     . ILE B 313 ? 0.5229 0.2806 0.3786 0.1027  0.0712  -0.0601 454 ILE B C     
5436 O O     . ILE B 313 ? 0.5106 0.2724 0.3634 0.0981  0.0748  -0.0688 454 ILE B O     
5437 C CB    . ILE B 313 ? 0.4952 0.2867 0.3680 0.1132  0.0665  -0.0485 454 ILE B CB    
5438 C CG1   . ILE B 313 ? 0.5094 0.3216 0.3971 0.1217  0.0657  -0.0469 454 ILE B CG1   
5439 C CG2   . ILE B 313 ? 0.4995 0.3002 0.3648 0.1036  0.0685  -0.0526 454 ILE B CG2   
5440 C CD1   . ILE B 313 ? 0.4689 0.2950 0.3616 0.1239  0.0615  -0.0378 454 ILE B CD1   
5441 N N     . ALA B 314 ? 0.5017 0.2433 0.3482 0.0977  0.0689  -0.0548 455 ALA B N     
5442 C CA    . ALA B 314 ? 0.5039 0.2328 0.3370 0.0860  0.0703  -0.0591 455 ALA B CA    
5443 C C     . ALA B 314 ? 0.5331 0.2475 0.3638 0.0846  0.0733  -0.0676 455 ALA B C     
5444 O O     . ALA B 314 ? 0.5839 0.2996 0.4078 0.0764  0.0760  -0.0754 455 ALA B O     
5445 C CB    . ALA B 314 ? 0.5170 0.2327 0.3429 0.0804  0.0667  -0.0512 455 ALA B CB    
5446 N N     . ALA B 315 ? 0.5500 0.2516 0.3867 0.0924  0.0727  -0.0663 456 ALA B N     
5447 C CA    . ALA B 315 ? 0.6098 0.2971 0.4458 0.0920  0.0756  -0.0748 456 ALA B CA    
5448 C C     . ALA B 315 ? 0.5758 0.2788 0.4171 0.0939  0.0798  -0.0849 456 ALA B C     
5449 O O     . ALA B 315 ? 0.6156 0.3137 0.4505 0.0873  0.0829  -0.0942 456 ALA B O     
5450 C CB    . ALA B 315 ? 0.5843 0.2566 0.4281 0.1013  0.0737  -0.0706 456 ALA B CB    
5451 N N     . TYR B 316 ? 0.5701 0.2929 0.4230 0.1022  0.0798  -0.0834 457 TYR B N     
5452 C CA    . TYR B 316 ? 0.5319 0.2707 0.3905 0.1040  0.0838  -0.0928 457 TYR B CA    
5453 C C     . TYR B 316 ? 0.5742 0.3243 0.4228 0.0931  0.0856  -0.0975 457 TYR B C     
5454 O O     . TYR B 316 ? 0.5455 0.2966 0.3903 0.0887  0.0892  -0.1073 457 TYR B O     
5455 C CB    . TYR B 316 ? 0.5491 0.3078 0.4222 0.1140  0.0831  -0.0892 457 TYR B CB    
5456 C CG    . TYR B 316 ? 0.5521 0.3289 0.4314 0.1154  0.0873  -0.0984 457 TYR B CG    
5457 C CD1   . TYR B 316 ? 0.5960 0.3664 0.4792 0.1188  0.0911  -0.1084 457 TYR B CD1   
5458 C CD2   . TYR B 316 ? 0.5265 0.3270 0.4077 0.1130  0.0876  -0.0973 457 TYR B CD2   
5459 C CE1   . TYR B 316 ? 0.5454 0.3330 0.4338 0.1197  0.0952  -0.1173 457 TYR B CE1   
5460 C CE2   . TYR B 316 ? 0.5293 0.3467 0.4155 0.1134  0.0916  -0.1054 457 TYR B CE2   
5461 C CZ    . TYR B 316 ? 0.5646 0.3759 0.4542 0.1168  0.0955  -0.1156 457 TYR B CZ    
5462 O OH    . TYR B 316 ? 0.4780 0.3067 0.3721 0.1170  0.0998  -0.1242 457 TYR B OH    
5463 N N     . GLU B 317 ? 0.5101 0.2691 0.3545 0.0883  0.0830  -0.0905 458 GLU B N     
5464 C CA    . GLU B 317 ? 0.5272 0.2980 0.3631 0.0778  0.0839  -0.0935 458 GLU B CA    
5465 C C     . GLU B 317 ? 0.5674 0.3219 0.3902 0.0670  0.0849  -0.0990 458 GLU B C     
5466 O O     . GLU B 317 ? 0.5603 0.3226 0.3770 0.0591  0.0869  -0.1057 458 GLU B O     
5467 C CB    . GLU B 317 ? 0.4963 0.2782 0.3318 0.0757  0.0805  -0.0845 458 GLU B CB    
5468 C CG    . GLU B 317 ? 0.4968 0.2996 0.3451 0.0844  0.0795  -0.0799 458 GLU B CG    
5469 C CD    . GLU B 317 ? 0.5264 0.3395 0.3749 0.0826  0.0760  -0.0713 458 GLU B CD    
5470 O OE1   . GLU B 317 ? 0.4853 0.2879 0.3254 0.0761  0.0739  -0.0679 458 GLU B OE1   
5471 O OE2   . GLU B 317 ? 0.4567 0.2893 0.3148 0.0873  0.0751  -0.0679 458 GLU B OE2   
5472 N N     . HIS B 318 ? 0.5406 0.2730 0.3587 0.0657  0.0832  -0.0957 459 HIS B N     
5473 C CA    . HIS B 318 ? 0.5862 0.3024 0.3929 0.0553  0.0840  -0.1012 459 HIS B CA    
5474 C C     . HIS B 318 ? 0.6128 0.3262 0.4207 0.0566  0.0879  -0.1122 459 HIS B C     
5475 O O     . HIS B 318 ? 0.6111 0.3248 0.4103 0.0468  0.0895  -0.1194 459 HIS B O     
5476 C CB    . HIS B 318 ? 0.6219 0.3146 0.4249 0.0547  0.0816  -0.0953 459 HIS B CB    
5477 C CG    . HIS B 318 ? 0.7396 0.4150 0.5318 0.0437  0.0822  -0.1003 459 HIS B CG    
5478 N ND1   . HIS B 318 ? 0.7233 0.3999 0.5049 0.0304  0.0808  -0.0998 459 HIS B ND1   
5479 C CD2   . HIS B 318 ? 0.7526 0.4100 0.5435 0.0438  0.0839  -0.1062 459 HIS B CD2   
5480 C CE1   . HIS B 318 ? 0.8099 0.4705 0.5841 0.0225  0.0815  -0.1048 459 HIS B CE1   
5481 N NE2   . HIS B 318 ? 0.7648 0.4129 0.5441 0.0304  0.0835  -0.1089 459 HIS B NE2   
5482 N N     . ALA B 319 ? 0.6106 0.3221 0.4295 0.0684  0.0893  -0.1140 460 ALA B N     
5483 C CA    . ALA B 319 ? 0.5849 0.2956 0.4062 0.0706  0.0934  -0.1254 460 ALA B CA    
5484 C C     . ALA B 319 ? 0.6153 0.3489 0.4347 0.0662  0.0958  -0.1317 460 ALA B C     
5485 O O     . ALA B 319 ? 0.6095 0.3423 0.4220 0.0599  0.0984  -0.1410 460 ALA B O     
5486 C CB    . ALA B 319 ? 0.5559 0.2640 0.3915 0.0846  0.0941  -0.1256 460 ALA B CB    
5487 N N     . LEU B 320 ? 0.6021 0.3566 0.4273 0.0693  0.0949  -0.1264 461 LEU B N     
5488 C CA    . LEU B 320 ? 0.6118 0.3888 0.4352 0.0649  0.0968  -0.1311 461 LEU B CA    
5489 C C     . LEU B 320 ? 0.5995 0.3765 0.4086 0.0505  0.0961  -0.1332 461 LEU B C     
5490 O O     . LEU B 320 ? 0.6128 0.3962 0.4162 0.0450  0.0985  -0.1416 461 LEU B O     
5491 C CB    . LEU B 320 ? 0.5482 0.3460 0.3796 0.0691  0.0951  -0.1233 461 LEU B CB    
5492 C CG    . LEU B 320 ? 0.5437 0.3505 0.3905 0.0820  0.0961  -0.1221 461 LEU B CG    
5493 C CD1   . LEU B 320 ? 0.5349 0.3608 0.3877 0.0836  0.0936  -0.1132 461 LEU B CD1   
5494 C CD2   . LEU B 320 ? 0.4842 0.3010 0.3354 0.0851  0.1006  -0.1330 461 LEU B CD2   
5495 N N     . LEU B 321 ? 0.5844 0.3554 0.3877 0.0441  0.0925  -0.1256 462 LEU B N     
5496 C CA    . LEU B 321 ? 0.5786 0.3514 0.3697 0.0300  0.0911  -0.1267 462 LEU B CA    
5497 C C     . LEU B 321 ? 0.6104 0.3672 0.3932 0.0235  0.0929  -0.1353 462 LEU B C     
5498 O O     . LEU B 321 ? 0.6371 0.4015 0.4119 0.0138  0.0934  -0.1407 462 LEU B O     
5499 C CB    . LEU B 321 ? 0.5897 0.3576 0.3775 0.0251  0.0870  -0.1172 462 LEU B CB    
5500 C CG    . LEU B 321 ? 0.5874 0.3591 0.3643 0.0103  0.0846  -0.1171 462 LEU B CG    
5501 C CD1   . LEU B 321 ? 0.5624 0.3590 0.3392 0.0060  0.0845  -0.1182 462 LEU B CD1   
5502 C CD2   . LEU B 321 ? 0.5712 0.3377 0.3461 0.0065  0.0808  -0.1083 462 LEU B CD2   
5503 N N     . GLU B 322 ? 0.5576 0.2923 0.3423 0.0287  0.0935  -0.1363 463 GLU B N     
5504 C CA    . GLU B 322 ? 0.6655 0.3832 0.4434 0.0233  0.0953  -0.1446 463 GLU B CA    
5505 C C     . GLU B 322 ? 0.6719 0.3978 0.4506 0.0255  0.0994  -0.1557 463 GLU B C     
5506 O O     . GLU B 322 ? 0.6818 0.4044 0.4515 0.0166  0.1006  -0.1632 463 GLU B O     
5507 C CB    . GLU B 322 ? 0.6619 0.3551 0.4437 0.0301  0.0950  -0.1427 463 GLU B CB    
5508 C CG    . GLU B 322 ? 0.7592 0.4399 0.5360 0.0244  0.0913  -0.1336 463 GLU B CG    
5509 C CD    . GLU B 322 ? 0.9392 0.6076 0.7043 0.0108  0.0907  -0.1374 463 GLU B CD    
5510 O OE1   . GLU B 322 ? 0.9827 0.6358 0.7461 0.0107  0.0929  -0.1448 463 GLU B OE1   
5511 O OE2   . GLU B 322 ? 0.9055 0.5806 0.6635 0.0002  0.0881  -0.1332 463 GLU B OE2   
5512 N N     . TYR B 323 ? 0.6448 0.3814 0.4342 0.0372  0.1014  -0.1570 464 TYR B N     
5513 C CA    . TYR B 323 ? 0.6273 0.3739 0.4177 0.0399  0.1055  -0.1674 464 TYR B CA    
5514 C C     . TYR B 323 ? 0.6748 0.4417 0.4564 0.0295  0.1054  -0.1691 464 TYR B C     
5515 O O     . TYR B 323 ? 0.6478 0.4156 0.4216 0.0236  0.1078  -0.1779 464 TYR B O     
5516 C CB    . TYR B 323 ? 0.6408 0.3973 0.4457 0.0543  0.1072  -0.1672 464 TYR B CB    
5517 C CG    . TYR B 323 ? 0.6801 0.4477 0.4871 0.0587  0.1116  -0.1780 464 TYR B CG    
5518 C CD1   . TYR B 323 ? 0.7236 0.4762 0.5316 0.0633  0.1146  -0.1879 464 TYR B CD1   
5519 C CD2   . TYR B 323 ? 0.6375 0.4304 0.4455 0.0587  0.1127  -0.1780 464 TYR B CD2   
5520 C CE1   . TYR B 323 ? 0.6737 0.4364 0.4829 0.0679  0.1188  -0.1981 464 TYR B CE1   
5521 C CE2   . TYR B 323 ? 0.6279 0.4311 0.4364 0.0629  0.1168  -0.1874 464 TYR B CE2   
5522 C CZ    . TYR B 323 ? 0.6951 0.4831 0.5040 0.0676  0.1200  -0.1976 464 TYR B CZ    
5523 O OH    . TYR B 323 ? 0.6421 0.4398 0.4505 0.0720  0.1244  -0.2070 464 TYR B OH    
5524 N N     . ALA B 324 ? 0.6353 0.4180 0.4177 0.0267  0.1025  -0.1602 465 ALA B N     
5525 C CA    . ALA B 324 ? 0.6175 0.4220 0.3939 0.0184  0.1021  -0.1604 465 ALA B CA    
5526 C C     . ALA B 324 ? 0.6186 0.4195 0.3820 0.0033  0.1000  -0.1616 465 ALA B C     
5527 O O     . ALA B 324 ? 0.6057 0.4180 0.3618 -0.0041 0.1009  -0.1663 465 ALA B O     
5528 C CB    . ALA B 324 ? 0.6083 0.4304 0.3908 0.0205  0.0994  -0.1504 465 ALA B CB    
5529 N N     . THR B 325 ? 0.6244 0.4100 0.3846 -0.0017 0.0970  -0.1570 466 THR B N     
5530 C CA    . THR B 325 ? 0.5983 0.3850 0.3478 -0.0166 0.0940  -0.1560 466 THR B CA    
5531 C C     . THR B 325 ? 0.6329 0.4146 0.3732 -0.0245 0.0962  -0.1661 466 THR B C     
5532 O O     . THR B 325 ? 0.6324 0.4287 0.3657 -0.0349 0.0947  -0.1667 466 THR B O     
5533 C CB    . THR B 325 ? 0.5999 0.3706 0.3483 -0.0198 0.0907  -0.1493 466 THR B CB    
5534 O OG1   . THR B 325 ? 0.6301 0.4084 0.3857 -0.0141 0.0884  -0.1397 466 THR B OG1   
5535 C CG2   . THR B 325 ? 0.6070 0.3796 0.3454 -0.0354 0.0873  -0.1485 466 THR B CG2   
5536 N N     . PRO B 326 ? 0.6265 0.3885 0.3663 -0.0205 0.0994  -0.1739 467 PRO B N     
5537 C CA    . PRO B 326 ? 0.6483 0.4069 0.3789 -0.0284 0.1017  -0.1840 467 PRO B CA    
5538 C C     . PRO B 326 ? 0.6792 0.4558 0.4088 -0.0267 0.1048  -0.1902 467 PRO B C     
5539 O O     . PRO B 326 ? 0.6440 0.4274 0.3642 -0.0371 0.1052  -0.1952 467 PRO B O     
5540 C CB    . PRO B 326 ? 0.6416 0.3742 0.3741 -0.0223 0.1044  -0.1903 467 PRO B CB    
5541 C CG    . PRO B 326 ? 0.6771 0.4058 0.4220 -0.0077 0.1048  -0.1854 467 PRO B CG    
5542 C CD    . PRO B 326 ? 0.6197 0.3608 0.3668 -0.0099 0.1006  -0.1736 467 PRO B CD    
5543 N N     . ARG B 327 ? 0.6559 0.4409 0.3949 -0.0142 0.1072  -0.1898 468 ARG B N     
5544 C CA    . ARG B 327 ? 0.6561 0.4579 0.3939 -0.0124 0.1107  -0.1957 468 ARG B CA    
5545 C C     . ARG B 327 ? 0.6641 0.4893 0.3969 -0.0220 0.1077  -0.1896 468 ARG B C     
5546 O O     . ARG B 327 ? 0.6596 0.4958 0.3848 -0.0288 0.1094  -0.1946 468 ARG B O     
5547 C CB    . ARG B 327 ? 0.6136 0.4193 0.3633 0.0034  0.1136  -0.1963 468 ARG B CB    
5548 C CG    . ARG B 327 ? 0.6600 0.4447 0.4149 0.0131  0.1168  -0.2039 468 ARG B CG    
5549 C CD    . ARG B 327 ? 0.6760 0.4623 0.4455 0.0287  0.1178  -0.2011 468 ARG B CD    
5550 N NE    . ARG B 327 ? 0.7035 0.4706 0.4782 0.0378  0.1206  -0.2092 468 ARG B NE    
5551 C CZ    . ARG B 327 ? 0.7344 0.4783 0.5111 0.0388  0.1191  -0.2081 468 ARG B CZ    
5552 N NH1   . ARG B 327 ? 0.6419 0.3788 0.4162 0.0324  0.1149  -0.1990 468 ARG B NH1   
5553 N NH2   . ARG B 327 ? 0.7321 0.4592 0.5132 0.0466  0.1217  -0.2162 468 ARG B NH2   
5554 N N     . LEU B 328 ? 0.6341 0.4670 0.3711 -0.0229 0.1033  -0.1787 469 LEU B N     
5555 C CA    . LEU B 328 ? 0.5949 0.4485 0.3279 -0.0328 0.0995  -0.1719 469 LEU B CA    
5556 C C     . LEU B 328 ? 0.5909 0.4421 0.3130 -0.0479 0.0967  -0.1732 469 LEU B C     
5557 O O     . LEU B 328 ? 0.6360 0.5029 0.3519 -0.0571 0.0955  -0.1732 469 LEU B O     
5558 C CB    . LEU B 328 ? 0.5464 0.4069 0.2870 -0.0299 0.0954  -0.1603 469 LEU B CB    
5559 C CG    . LEU B 328 ? 0.5766 0.4573 0.3146 -0.0400 0.0905  -0.1520 469 LEU B CG    
5560 C CD1   . LEU B 328 ? 0.5518 0.4529 0.2899 -0.0393 0.0922  -0.1524 469 LEU B CD1   
5561 C CD2   . LEU B 328 ? 0.5827 0.4661 0.3280 -0.0374 0.0863  -0.1412 469 LEU B CD2   
5562 N N     . ALA B 329 ? 0.5910 0.4231 0.3109 -0.0511 0.0953  -0.1737 470 ALA B N     
5563 C CA    . ALA B 329 ? 0.6218 0.4520 0.3323 -0.0658 0.0922  -0.1741 470 ALA B CA    
5564 C C     . ALA B 329 ? 0.7064 0.5361 0.4077 -0.0722 0.0954  -0.1846 470 ALA B C     
5565 O O     . ALA B 329 ? 0.6556 0.4920 0.3489 -0.0854 0.0926  -0.1845 470 ALA B O     
5566 C CB    . ALA B 329 ? 0.5913 0.3999 0.3016 -0.0672 0.0906  -0.1727 470 ALA B CB    
5567 N N     . ALA B 330 ? 0.6973 0.5199 0.4001 -0.0631 0.1012  -0.1937 471 ALA B N     
5568 C CA    . ALA B 330 ? 0.6801 0.5004 0.3744 -0.0681 0.1050  -0.2049 471 ALA B CA    
5569 C C     . ALA B 330 ? 0.7259 0.5697 0.4158 -0.0731 0.1057  -0.2054 471 ALA B C     
5570 O O     . ALA B 330 ? 0.7145 0.5593 0.3958 -0.0797 0.1085  -0.2140 471 ALA B O     
5571 C CB    . ALA B 330 ? 0.6690 0.4722 0.3674 -0.0557 0.1109  -0.2146 471 ALA B CB    
5572 N N     . ILE B 331 ? 0.6417 0.5038 0.3371 -0.0705 0.1032  -0.1963 472 ILE B N     
5573 C CA    . ILE B 331 ? 0.7139 0.5985 0.4055 -0.0757 0.1035  -0.1955 472 ILE B CA    
5574 C C     . ILE B 331 ? 0.7100 0.6047 0.3932 -0.0921 0.0984  -0.1917 472 ILE B C     
5575 O O     . ILE B 331 ? 0.6496 0.5462 0.3350 -0.0969 0.0925  -0.1825 472 ILE B O     
5576 C CB    . ILE B 331 ? 0.6766 0.5771 0.3772 -0.0681 0.1023  -0.1864 472 ILE B CB    
5577 C CG1   . ILE B 331 ? 0.6720 0.5644 0.3813 -0.0519 0.1075  -0.1906 472 ILE B CG1   
5578 C CG2   . ILE B 331 ? 0.6277 0.5515 0.3241 -0.0754 0.1018  -0.1841 472 ILE B CG2   
5579 C CD1   . ILE B 331 ? 0.5770 0.4841 0.2958 -0.0438 0.1066  -0.1821 472 ILE B CD1   
5580 N N     . PRO B 332 ? 0.7132 0.6148 0.3870 -0.1011 0.1003  -0.1983 473 PRO B N     
5581 C CA    . PRO B 332 ? 0.7325 0.6459 0.3989 -0.1169 0.0949  -0.1939 473 PRO B CA    
5582 C C     . PRO B 332 ? 0.6773 0.6118 0.3489 -0.1195 0.0890  -0.1806 473 PRO B C     
5583 O O     . PRO B 332 ? 0.6917 0.6390 0.3677 -0.1136 0.0904  -0.1776 473 PRO B O     
5584 C CB    . PRO B 332 ? 0.7373 0.6567 0.3938 -0.1236 0.0992  -0.2037 473 PRO B CB    
5585 C CG    . PRO B 332 ? 0.7763 0.6946 0.4369 -0.1107 0.1061  -0.2100 473 PRO B CG    
5586 C CD    . PRO B 332 ? 0.7413 0.6409 0.4109 -0.0974 0.1074  -0.2101 473 PRO B CD    
5587 N N     . GLY B 333 ? 0.6143 0.5523 0.2860 -0.1284 0.0822  -0.1724 474 GLY B N     
5588 C CA    . GLY B 333 ? 0.6122 0.5680 0.2900 -0.1307 0.0757  -0.1593 474 GLY B CA    
5589 C C     . GLY B 333 ? 0.6044 0.5531 0.2920 -0.1226 0.0730  -0.1518 474 GLY B C     
5590 O O     . GLY B 333 ? 0.5677 0.5274 0.2598 -0.1271 0.0665  -0.1411 474 GLY B O     
5591 N N     . VAL B 334 ? 0.5706 0.5017 0.2621 -0.1110 0.0777  -0.1569 475 VAL B N     
5592 C CA    . VAL B 334 ? 0.5885 0.5139 0.2894 -0.1023 0.0759  -0.1498 475 VAL B CA    
5593 C C     . VAL B 334 ? 0.6343 0.5468 0.3342 -0.1079 0.0723  -0.1479 475 VAL B C     
5594 O O     . VAL B 334 ? 0.6175 0.5143 0.3111 -0.1116 0.0746  -0.1556 475 VAL B O     
5595 C CB    . VAL B 334 ? 0.6355 0.5485 0.3419 -0.0872 0.0821  -0.1553 475 VAL B CB    
5596 C CG1   . VAL B 334 ? 0.5886 0.4884 0.3026 -0.0799 0.0806  -0.1504 475 VAL B CG1   
5597 C CG2   . VAL B 334 ? 0.6232 0.5524 0.3343 -0.0805 0.0842  -0.1532 475 VAL B CG2   
5598 N N     . ARG B 335 ? 0.6205 0.5393 0.3266 -0.1087 0.0669  -0.1375 476 ARG B N     
5599 C CA    . ARG B 335 ? 0.5819 0.4886 0.2889 -0.1120 0.0638  -0.1346 476 ARG B CA    
5600 C C     . ARG B 335 ? 0.6222 0.5223 0.3382 -0.1007 0.0641  -0.1294 476 ARG B C     
5601 O O     . ARG B 335 ? 0.5432 0.4576 0.2660 -0.0961 0.0623  -0.1224 476 ARG B O     
5602 C CB    . ARG B 335 ? 0.6085 0.5299 0.3147 -0.1247 0.0564  -0.1267 476 ARG B CB    
5603 C CG    . ARG B 335 ? 0.6605 0.5720 0.3687 -0.1284 0.0529  -0.1228 476 ARG B CG    
5604 C CD    . ARG B 335 ? 0.6842 0.6144 0.3978 -0.1353 0.0451  -0.1116 476 ARG B CD    
5605 N NE    . ARG B 335 ? 0.7423 0.6640 0.4607 -0.1345 0.0427  -0.1070 476 ARG B NE    
5606 C CZ    . ARG B 335 ? 0.7673 0.7020 0.4915 -0.1398 0.0361  -0.0979 476 ARG B CZ    
5607 N NH1   . ARG B 335 ? 0.7458 0.7023 0.4725 -0.1461 0.0308  -0.0916 476 ARG B NH1   
5608 N NH2   . ARG B 335 ? 0.6905 0.6162 0.4185 -0.1388 0.0348  -0.0949 476 ARG B NH2   
5609 N N     . ILE B 336 ? 0.5817 0.4602 0.2977 -0.0965 0.0665  -0.1327 477 ILE B N     
5610 C CA    . ILE B 336 ? 0.5924 0.4633 0.3163 -0.0866 0.0666  -0.1276 477 ILE B CA    
5611 C C     . ILE B 336 ? 0.5834 0.4601 0.3098 -0.0935 0.0605  -0.1186 477 ILE B C     
5612 O O     . ILE B 336 ? 0.5873 0.4605 0.3089 -0.1041 0.0576  -0.1188 477 ILE B O     
5613 C CB    . ILE B 336 ? 0.6049 0.4501 0.3282 -0.0795 0.0712  -0.1338 477 ILE B CB    
5614 C CG1   . ILE B 336 ? 0.6215 0.4614 0.3430 -0.0729 0.0772  -0.1436 477 ILE B CG1   
5615 C CG2   . ILE B 336 ? 0.5793 0.4173 0.3106 -0.0695 0.0712  -0.1278 477 ILE B CG2   
5616 C CD1   . ILE B 336 ? 0.5707 0.4248 0.2986 -0.0632 0.0794  -0.1424 477 ILE B CD1   
5617 N N     . VAL B 337 ? 0.5594 0.4455 0.2939 -0.0875 0.0584  -0.1107 478 VAL B N     
5618 C CA    . VAL B 337 ? 0.5330 0.4265 0.2714 -0.0927 0.0527  -0.1020 478 VAL B CA    
5619 C C     . VAL B 337 ? 0.5227 0.4008 0.2653 -0.0844 0.0543  -0.0998 478 VAL B C     
5620 O O     . VAL B 337 ? 0.4843 0.3641 0.2332 -0.0737 0.0563  -0.0973 478 VAL B O     
5621 C CB    . VAL B 337 ? 0.5466 0.4647 0.2911 -0.0937 0.0483  -0.0939 478 VAL B CB    
5622 C CG1   . VAL B 337 ? 0.5252 0.4517 0.2747 -0.0994 0.0420  -0.0853 478 VAL B CG1   
5623 C CG2   . VAL B 337 ? 0.5751 0.5072 0.3150 -0.1014 0.0470  -0.0959 478 VAL B CG2   
5624 N N     . GLY B 338 ? 0.5442 0.4078 0.2834 -0.0896 0.0533  -0.1004 479 GLY B N     
5625 C CA    . GLY B 338 ? 0.5286 0.3753 0.2706 -0.0824 0.0550  -0.0986 479 GLY B CA    
5626 C C     . GLY B 338 ? 0.5566 0.3792 0.2939 -0.0775 0.0602  -0.1060 479 GLY B C     
5627 O O     . GLY B 338 ? 0.5152 0.3333 0.2550 -0.0668 0.0645  -0.1094 479 GLY B O     
5628 N N     . THR B 339 ? 0.5551 0.3631 0.2867 -0.0853 0.0597  -0.1082 480 THR B N     
5629 C CA    . THR B 339 ? 0.6052 0.3892 0.3328 -0.0819 0.0640  -0.1145 480 THR B CA    
5630 C C     . THR B 339 ? 0.5949 0.3612 0.3217 -0.0835 0.0629  -0.1107 480 THR B C     
5631 O O     . THR B 339 ? 0.6116 0.3628 0.3329 -0.0902 0.0633  -0.1137 480 THR B O     
5632 C CB    . THR B 339 ? 0.6334 0.4156 0.3535 -0.0909 0.0649  -0.1222 480 THR B CB    
5633 O OG1   . THR B 339 ? 0.6452 0.4390 0.3622 -0.1048 0.0600  -0.1193 480 THR B OG1   
5634 C CG2   . THR B 339 ? 0.6540 0.4500 0.3744 -0.0871 0.0671  -0.1269 480 THR B CG2   
5635 N N     . ALA B 340 ? 0.5686 0.3377 0.3012 -0.0777 0.0615  -0.1036 481 ALA B N     
5636 C CA    . ALA B 340 ? 0.6340 0.3924 0.3700 -0.0787 0.0594  -0.0971 481 ALA B CA    
5637 C C     . ALA B 340 ? 0.6458 0.3752 0.3768 -0.0725 0.0637  -0.1010 481 ALA B C     
5638 O O     . ALA B 340 ? 0.6057 0.3283 0.3372 -0.0632 0.0675  -0.1060 481 ALA B O     
5639 C CB    . ALA B 340 ? 0.5377 0.3125 0.2879 -0.0714 0.0561  -0.0861 481 ALA B CB    
5640 N N     . GLN B 341 ? 0.5994 0.3152 0.3291 -0.0770 0.0622  -0.0969 482 GLN B N     
5641 C CA    . GLN B 341 ? 0.6698 0.3576 0.3955 -0.0721 0.0653  -0.0989 482 GLN B CA    
5642 C C     . GLN B 341 ? 0.6724 0.3557 0.4053 -0.0559 0.0672  -0.0957 482 GLN B C     
5643 O O     . GLN B 341 ? 0.6759 0.3422 0.4089 -0.0481 0.0701  -0.0988 482 GLN B O     
5644 C CB    . GLN B 341 ? 0.6876 0.3637 0.4105 -0.0807 0.0629  -0.0935 482 GLN B CB    
5645 C CG    . GLN B 341 ? 0.8219 0.4908 0.5375 -0.0936 0.0627  -0.0983 482 GLN B CG    
5646 C CD    . GLN B 341 ? 0.8567 0.5169 0.5697 -0.0900 0.0662  -0.1071 482 GLN B CD    
5647 O OE1   . GLN B 341 ? 0.8726 0.5419 0.5818 -0.0979 0.0662  -0.1130 482 GLN B OE1   
5648 N NE2   . GLN B 341 ? 0.9356 0.5783 0.6509 -0.0784 0.0691  -0.1079 482 GLN B NE2   
5649 N N     . GLU B 342 ? 0.6186 0.3225 0.3627 -0.0498 0.0644  -0.0874 483 GLU B N     
5650 C CA    . GLU B 342 ? 0.6374 0.3416 0.3900 -0.0349 0.0654  -0.0833 483 GLU B CA    
5651 C C     . GLU B 342 ? 0.6002 0.3313 0.3614 -0.0303 0.0644  -0.0817 483 GLU B C     
5652 O O     . GLU B 342 ? 0.5686 0.3194 0.3346 -0.0361 0.0607  -0.0766 483 GLU B O     
5653 C CB    . GLU B 342 ? 0.6891 0.3888 0.4469 -0.0324 0.0626  -0.0731 483 GLU B CB    
5654 C CG    . GLU B 342 ? 0.8182 0.4885 0.5706 -0.0290 0.0643  -0.0731 483 GLU B CG    
5655 C CD    . GLU B 342 ? 1.0073 0.6666 0.7621 -0.0148 0.0677  -0.0768 483 GLU B CD    
5656 O OE1   . GLU B 342 ? 1.0217 0.6686 0.7708 -0.0145 0.0715  -0.0864 483 GLU B OE1   
5657 O OE2   . GLU B 342 ? 1.0794 0.7441 0.8428 -0.0040 0.0666  -0.0701 483 GLU B OE2   
5658 N N     . LYS B 343 ? 0.5316 0.2635 0.2951 -0.0199 0.0678  -0.0862 484 LYS B N     
5659 C CA    . LYS B 343 ? 0.5461 0.3022 0.3169 -0.0158 0.0674  -0.0853 484 LYS B CA    
5660 C C     . LYS B 343 ? 0.5859 0.3434 0.3659 -0.0010 0.0688  -0.0823 484 LYS B C     
5661 O O     . LYS B 343 ? 0.5646 0.3031 0.3437 0.0068  0.0712  -0.0838 484 LYS B O     
5662 C CB    . LYS B 343 ? 0.5460 0.3068 0.3094 -0.0202 0.0705  -0.0951 484 LYS B CB    
5663 C CG    . LYS B 343 ? 0.5568 0.3228 0.3122 -0.0354 0.0683  -0.0974 484 LYS B CG    
5664 C CD    . LYS B 343 ? 0.5796 0.3546 0.3287 -0.0397 0.0707  -0.1059 484 LYS B CD    
5665 C CE    . LYS B 343 ? 0.5855 0.3783 0.3420 -0.0305 0.0722  -0.1051 484 LYS B CE    
5666 N NZ    . LYS B 343 ? 0.5904 0.4010 0.3443 -0.0371 0.0720  -0.1091 484 LYS B NZ    
5667 N N     . ALA B 344 ? 0.5444 0.3248 0.3335 0.0029  0.0671  -0.0779 485 ALA B N     
5668 C CA    . ALA B 344 ? 0.5327 0.3186 0.3307 0.0161  0.0685  -0.0761 485 ALA B CA    
5669 C C     . ALA B 344 ? 0.5626 0.3705 0.3645 0.0170  0.0694  -0.0782 485 ALA B C     
5670 O O     . ALA B 344 ? 0.4974 0.3229 0.3018 0.0100  0.0661  -0.0743 485 ALA B O     
5671 C CB    . ALA B 344 ? 0.4956 0.2862 0.3029 0.0211  0.0648  -0.0659 485 ALA B CB    
5672 N N     . SER B 345 ? 0.5704 0.3772 0.3731 0.0253  0.0740  -0.0843 486 SER B N     
5673 C CA    . SER B 345 ? 0.5402 0.3679 0.3488 0.0292  0.0753  -0.0850 486 SER B CA    
5674 C C     . SER B 345 ? 0.5208 0.3616 0.3227 0.0191  0.0759  -0.0897 486 SER B C     
5675 O O     . SER B 345 ? 0.5284 0.3746 0.3284 0.0213  0.0800  -0.0964 486 SER B O     
5676 C CB    . SER B 345 ? 0.5316 0.3762 0.3523 0.0332  0.0710  -0.0749 486 SER B CB    
5677 O OG    . SER B 345 ? 0.5409 0.4036 0.3681 0.0382  0.0725  -0.0754 486 SER B OG    
5678 N N     . VAL B 346 ? 0.5101 0.3573 0.3092 0.0080  0.0715  -0.0857 487 VAL B N     
5679 C CA    . VAL B 346 ? 0.4778 0.3423 0.2733 -0.0013 0.0701  -0.0867 487 VAL B CA    
5680 C C     . VAL B 346 ? 0.5123 0.3666 0.2935 -0.0099 0.0732  -0.0967 487 VAL B C     
5681 O O     . VAL B 346 ? 0.5405 0.3761 0.3149 -0.0137 0.0737  -0.0998 487 VAL B O     
5682 C CB    . VAL B 346 ? 0.5225 0.3993 0.3233 -0.0087 0.0636  -0.0775 487 VAL B CB    
5683 C CG1   . VAL B 346 ? 0.4515 0.3422 0.2467 -0.0204 0.0613  -0.0784 487 VAL B CG1   
5684 C CG2   . VAL B 346 ? 0.4771 0.3677 0.2918 -0.0011 0.0610  -0.0689 487 VAL B CG2   
5685 N N     . LEU B 347 ? 0.4995 0.3679 0.2775 -0.0136 0.0748  -0.1010 488 LEU B N     
5686 C CA    . LEU B 347 ? 0.4979 0.3633 0.2671 -0.0221 0.0756  -0.1085 488 LEU B CA    
5687 C C     . LEU B 347 ? 0.5335 0.4208 0.3001 -0.0318 0.0725  -0.1063 488 LEU B C     
5688 O O     . LEU B 347 ? 0.5448 0.4446 0.3118 -0.0305 0.0744  -0.1091 488 LEU B O     
5689 C CB    . LEU B 347 ? 0.5020 0.3603 0.2723 -0.0142 0.0808  -0.1171 488 LEU B CB    
5690 C CG    . LEU B 347 ? 0.5349 0.3877 0.2963 -0.0215 0.0826  -0.1261 488 LEU B CG    
5691 C CD1   . LEU B 347 ? 0.5318 0.3668 0.2860 -0.0297 0.0807  -0.1270 488 LEU B CD1   
5692 C CD2   . LEU B 347 ? 0.5301 0.3757 0.2945 -0.0117 0.0879  -0.1342 488 LEU B CD2   
5693 N N     . SER B 348 ? 0.4934 0.3858 0.2575 -0.0416 0.0675  -0.1008 489 SER B N     
5694 C CA    . SER B 348 ? 0.4760 0.3883 0.2379 -0.0516 0.0634  -0.0975 489 SER B CA    
5695 C C     . SER B 348 ? 0.5030 0.4135 0.2558 -0.0600 0.0642  -0.1048 489 SER B C     
5696 O O     . SER B 348 ? 0.5050 0.3985 0.2521 -0.0628 0.0656  -0.1105 489 SER B O     
5697 C CB    . SER B 348 ? 0.4816 0.4003 0.2450 -0.0594 0.0572  -0.0895 489 SER B CB    
5698 O OG    . SER B 348 ? 0.4831 0.4177 0.2593 -0.0543 0.0539  -0.0798 489 SER B OG    
5699 N N     . PHE B 349 ? 0.4696 0.3981 0.2210 -0.0648 0.0629  -0.1040 490 PHE B N     
5700 C CA    . PHE B 349 ? 0.4893 0.4192 0.2317 -0.0742 0.0631  -0.1099 490 PHE B CA    
5701 C C     . PHE B 349 ? 0.5065 0.4596 0.2488 -0.0820 0.0587  -0.1040 490 PHE B C     
5702 O O     . PHE B 349 ? 0.4701 0.4374 0.2196 -0.0789 0.0564  -0.0963 490 PHE B O     
5703 C CB    . PHE B 349 ? 0.4830 0.4029 0.2218 -0.0681 0.0699  -0.1205 490 PHE B CB    
5704 C CG    . PHE B 349 ? 0.5106 0.4442 0.2533 -0.0613 0.0729  -0.1208 490 PHE B CG    
5705 C CD1   . PHE B 349 ? 0.4524 0.3867 0.2041 -0.0492 0.0750  -0.1180 490 PHE B CD1   
5706 C CD2   . PHE B 349 ? 0.5102 0.4561 0.2471 -0.0673 0.0737  -0.1239 490 PHE B CD2   
5707 C CE1   . PHE B 349 ? 0.4794 0.4265 0.2348 -0.0434 0.0779  -0.1183 490 PHE B CE1   
5708 C CE2   . PHE B 349 ? 0.4725 0.4310 0.2127 -0.0616 0.0766  -0.1240 490 PHE B CE2   
5709 C CZ    . PHE B 349 ? 0.4952 0.4544 0.2448 -0.0497 0.0788  -0.1212 490 PHE B CZ    
5710 N N     . VAL B 350 ? 0.4496 0.4061 0.1840 -0.0927 0.0573  -0.1073 491 VAL B N     
5711 C CA    . VAL B 350 ? 0.4952 0.4723 0.2280 -0.1006 0.0538  -0.1029 491 VAL B CA    
5712 C C     . VAL B 350 ? 0.5311 0.5066 0.2547 -0.1041 0.0583  -0.1126 491 VAL B C     
5713 O O     . VAL B 350 ? 0.5706 0.5292 0.2888 -0.1028 0.0627  -0.1220 491 VAL B O     
5714 C CB    . VAL B 350 ? 0.5224 0.5098 0.2554 -0.1124 0.0458  -0.0951 491 VAL B CB    
5715 C CG1   . VAL B 350 ? 0.5278 0.5224 0.2712 -0.1091 0.0409  -0.0844 491 VAL B CG1   
5716 C CG2   . VAL B 350 ? 0.5782 0.5515 0.3045 -0.1197 0.0456  -0.1005 491 VAL B CG2   
5717 N N     . LEU B 351 ? 0.5351 0.5284 0.2572 -0.1087 0.0571  -0.1100 492 LEU B N     
5718 C CA    . LEU B 351 ? 0.5381 0.5328 0.2515 -0.1124 0.0615  -0.1188 492 LEU B CA    
5719 C C     . LEU B 351 ? 0.5273 0.5389 0.2358 -0.1260 0.0562  -0.1143 492 LEU B C     
5720 O O     . LEU B 351 ? 0.5237 0.5529 0.2372 -0.1282 0.0517  -0.1046 492 LEU B O     
5721 C CB    . LEU B 351 ? 0.5672 0.5665 0.2835 -0.1026 0.0671  -0.1215 492 LEU B CB    
5722 C CG    . LEU B 351 ? 0.5941 0.5977 0.3024 -0.1055 0.0721  -0.1302 492 LEU B CG    
5723 C CD1   . LEU B 351 ? 0.5659 0.5514 0.2663 -0.1064 0.0768  -0.1426 492 LEU B CD1   
5724 C CD2   . LEU B 351 ? 0.5405 0.5495 0.2540 -0.0950 0.0771  -0.1312 492 LEU B CD2   
5725 N N     . ALA B 352 ? 0.5148 0.5213 0.2140 -0.1352 0.0567  -0.1209 493 ALA B N     
5726 C CA    . ALA B 352 ? 0.5587 0.5809 0.2528 -0.1489 0.0516  -0.1170 493 ALA B CA    
5727 C C     . ALA B 352 ? 0.5762 0.6163 0.2695 -0.1503 0.0522  -0.1145 493 ALA B C     
5728 O O     . ALA B 352 ? 0.5958 0.6334 0.2867 -0.1442 0.0589  -0.1218 493 ALA B O     
5729 C CB    . ALA B 352 ? 0.6181 0.6306 0.3013 -0.1574 0.0540  -0.1271 493 ALA B CB    
5730 N N     . GLY B 353 ? 0.6100 0.6686 0.3062 -0.1584 0.0450  -0.1036 494 GLY B N     
5731 C CA    . GLY B 353 ? 0.5735 0.6499 0.2689 -0.1615 0.0446  -0.0998 494 GLY B CA    
5732 C C     . GLY B 353 ? 0.6375 0.7199 0.3420 -0.1515 0.0455  -0.0938 494 GLY B C     
5733 O O     . GLY B 353 ? 0.5952 0.6913 0.2990 -0.1534 0.0462  -0.0915 494 GLY B O     
5734 N N     . HIS B 354 ? 0.5441 0.6172 0.2572 -0.1414 0.0455  -0.0912 495 HIS B N     
5735 C CA    . HIS B 354 ? 0.5678 0.6457 0.2901 -0.1316 0.0466  -0.0857 495 HIS B CA    
5736 C C     . HIS B 354 ? 0.5702 0.6471 0.3030 -0.1277 0.0410  -0.0761 495 HIS B C     
5737 O O     . HIS B 354 ? 0.5506 0.6140 0.2836 -0.1259 0.0407  -0.0787 495 HIS B O     
5738 C CB    . HIS B 354 ? 0.5544 0.6195 0.2761 -0.1197 0.0556  -0.0959 495 HIS B CB    
5739 C CG    . HIS B 354 ? 0.6319 0.6984 0.3446 -0.1220 0.0618  -0.1058 495 HIS B CG    
5740 N ND1   . HIS B 354 ? 0.6305 0.7099 0.3441 -0.1206 0.0645  -0.1047 495 HIS B ND1   
5741 C CD2   . HIS B 354 ? 0.5692 0.6262 0.2719 -0.1259 0.0660  -0.1171 495 HIS B CD2   
5742 C CE1   . HIS B 354 ? 0.6373 0.7153 0.3417 -0.1233 0.0702  -0.1152 495 HIS B CE1   
5743 N NE2   . HIS B 354 ? 0.6562 0.7205 0.3540 -0.1264 0.0712  -0.1229 495 HIS B NE2   
5744 N N     . GLU B 355 ? 0.5456 0.6363 0.2870 -0.1265 0.0368  -0.0652 496 GLU B N     
5745 C CA    . GLU B 355 ? 0.5677 0.6578 0.3200 -0.1216 0.0321  -0.0564 496 GLU B CA    
5746 C C     . GLU B 355 ? 0.5378 0.6165 0.2948 -0.1082 0.0381  -0.0605 496 GLU B C     
5747 O O     . GLU B 355 ? 0.4982 0.5784 0.2548 -0.1025 0.0437  -0.0644 496 GLU B O     
5748 C CB    . GLU B 355 ? 0.5929 0.7015 0.3537 -0.1252 0.0251  -0.0429 496 GLU B CB    
5749 C CG    . GLU B 355 ? 0.6808 0.7915 0.4527 -0.1238 0.0181  -0.0325 496 GLU B CG    
5750 C CD    . GLU B 355 ? 0.7514 0.8613 0.5338 -0.1129 0.0194  -0.0281 496 GLU B CD    
5751 O OE1   . GLU B 355 ? 0.7492 0.8714 0.5375 -0.1123 0.0176  -0.0207 496 GLU B OE1   
5752 O OE2   . GLU B 355 ? 0.6381 0.7353 0.4229 -0.1054 0.0221  -0.0315 496 GLU B OE2   
5753 N N     . PRO B 356 ? 0.5831 0.6509 0.3447 -0.1033 0.0372  -0.0598 497 PRO B N     
5754 C CA    . PRO B 356 ? 0.5374 0.5937 0.3034 -0.0907 0.0430  -0.0638 497 PRO B CA    
5755 C C     . PRO B 356 ? 0.4745 0.5407 0.2481 -0.0835 0.0448  -0.0594 497 PRO B C     
5756 O O     . PRO B 356 ? 0.4697 0.5293 0.2432 -0.0748 0.0516  -0.0662 497 PRO B O     
5757 C CB    . PRO B 356 ? 0.4959 0.5452 0.2673 -0.0894 0.0391  -0.0594 497 PRO B CB    
5758 C CG    . PRO B 356 ? 0.5105 0.5581 0.2754 -0.1003 0.0351  -0.0604 497 PRO B CG    
5759 C CD    . PRO B 356 ? 0.5443 0.6079 0.3058 -0.1094 0.0319  -0.0572 497 PRO B CD    
5760 N N     . LEU B 357 ? 0.5136 0.5951 0.2945 -0.0867 0.0389  -0.0481 498 LEU B N     
5761 C CA    . LEU B 357 ? 0.4605 0.5508 0.2495 -0.0801 0.0405  -0.0435 498 LEU B CA    
5762 C C     . LEU B 357 ? 0.5456 0.6408 0.3293 -0.0799 0.0461  -0.0494 498 LEU B C     
5763 O O     . LEU B 357 ? 0.4925 0.5870 0.2801 -0.0713 0.0514  -0.0521 498 LEU B O     
5764 C CB    . LEU B 357 ? 0.5181 0.6235 0.3160 -0.0847 0.0325  -0.0300 498 LEU B CB    
5765 C CG    . LEU B 357 ? 0.6509 0.7680 0.4565 -0.0810 0.0331  -0.0241 498 LEU B CG    
5766 C CD1   . LEU B 357 ? 0.5571 0.6678 0.3699 -0.0689 0.0382  -0.0263 498 LEU B CD1   
5767 C CD2   . LEU B 357 ? 0.6922 0.8233 0.5063 -0.0869 0.0245  -0.0104 498 LEU B CD2   
5768 N N     . GLU B 358 ? 0.4906 0.5916 0.2656 -0.0896 0.0449  -0.0514 499 GLU B N     
5769 C CA    . GLU B 358 ? 0.4856 0.5912 0.2545 -0.0903 0.0506  -0.0580 499 GLU B CA    
5770 C C     . GLU B 358 ? 0.4583 0.5485 0.2227 -0.0818 0.0591  -0.0708 499 GLU B C     
5771 O O     . GLU B 358 ? 0.4492 0.5414 0.2141 -0.0760 0.0652  -0.0756 499 GLU B O     
5772 C CB    . GLU B 358 ? 0.5038 0.6183 0.2637 -0.1032 0.0476  -0.0578 499 GLU B CB    
5773 C CG    . GLU B 358 ? 0.6085 0.7114 0.3571 -0.1071 0.0507  -0.0689 499 GLU B CG    
5774 C CD    . GLU B 358 ? 0.7005 0.8134 0.4394 -0.1193 0.0495  -0.0706 499 GLU B CD    
5775 O OE1   . GLU B 358 ? 0.7612 0.8804 0.4958 -0.1199 0.0543  -0.0753 499 GLU B OE1   
5776 O OE2   . GLU B 358 ? 0.6708 0.7856 0.4065 -0.1286 0.0437  -0.0674 499 GLU B OE2   
5777 N N     . VAL B 359 ? 0.4782 0.5530 0.2390 -0.0807 0.0596  -0.0763 500 VAL B N     
5778 C CA    . VAL B 359 ? 0.4895 0.5481 0.2476 -0.0718 0.0670  -0.0877 500 VAL B CA    
5779 C C     . VAL B 359 ? 0.4642 0.5199 0.2324 -0.0590 0.0702  -0.0863 500 VAL B C     
5780 O O     . VAL B 359 ? 0.4365 0.4884 0.2054 -0.0508 0.0768  -0.0933 500 VAL B O     
5781 C CB    . VAL B 359 ? 0.4878 0.5300 0.2409 -0.0739 0.0661  -0.0927 500 VAL B CB    
5782 C CG1   . VAL B 359 ? 0.4531 0.4776 0.2044 -0.0642 0.0734  -0.1040 500 VAL B CG1   
5783 C CG2   . VAL B 359 ? 0.4737 0.5199 0.2170 -0.0871 0.0631  -0.0944 500 VAL B CG2   
5784 N N     . GLY B 360 ? 0.4544 0.5131 0.2311 -0.0572 0.0654  -0.0771 501 GLY B N     
5785 C CA    . GLY B 360 ? 0.4772 0.5343 0.2639 -0.0457 0.0681  -0.0752 501 GLY B CA    
5786 C C     . GLY B 360 ? 0.4368 0.5071 0.2278 -0.0428 0.0711  -0.0736 501 GLY B C     
5787 O O     . GLY B 360 ? 0.4314 0.4981 0.2270 -0.0327 0.0766  -0.0778 501 GLY B O     
5788 N N     . LYS B 361 ? 0.4732 0.5590 0.2630 -0.0518 0.0673  -0.0674 502 LYS B N     
5789 C CA    . LYS B 361 ? 0.4380 0.5370 0.2315 -0.0505 0.0700  -0.0656 502 LYS B CA    
5790 C C     . LYS B 361 ? 0.4149 0.5108 0.2016 -0.0480 0.0777  -0.0767 502 LYS B C     
5791 O O     . LYS B 361 ? 0.4365 0.5359 0.2284 -0.0407 0.0828  -0.0790 502 LYS B O     
5792 C CB    . LYS B 361 ? 0.5108 0.6265 0.3043 -0.0614 0.0638  -0.0559 502 LYS B CB    
5793 C CG    . LYS B 361 ? 0.5598 0.6805 0.3633 -0.0616 0.0568  -0.0440 502 LYS B CG    
5794 C CD    . LYS B 361 ? 0.7051 0.8366 0.5074 -0.0732 0.0487  -0.0347 502 LYS B CD    
5795 C CE    . LYS B 361 ? 0.7005 0.8469 0.5119 -0.0748 0.0450  -0.0239 502 LYS B CE    
5796 N NZ    . LYS B 361 ? 0.8237 0.9796 0.6364 -0.0848 0.0362  -0.0134 502 LYS B NZ    
5797 N N     . ALA B 362 ? 0.4733 0.5629 0.2492 -0.0538 0.0786  -0.0838 503 ALA B N     
5798 C CA    . ALA B 362 ? 0.4594 0.5449 0.2289 -0.0512 0.0860  -0.0953 503 ALA B CA    
5799 C C     . ALA B 362 ? 0.4620 0.5329 0.2362 -0.0375 0.0919  -0.1024 503 ALA B C     
5800 O O     . ALA B 362 ? 0.4316 0.5035 0.2074 -0.0309 0.0983  -0.1084 503 ALA B O     
5801 C CB    . ALA B 362 ? 0.4545 0.5351 0.2118 -0.0604 0.0855  -0.1017 503 ALA B CB    
5802 N N     . LEU B 363 ? 0.4491 0.5067 0.2261 -0.0332 0.0896  -0.1015 504 LEU B N     
5803 C CA    . LEU B 363 ? 0.4519 0.4955 0.2341 -0.0201 0.0943  -0.1072 504 LEU B CA    
5804 C C     . LEU B 363 ? 0.4731 0.5248 0.2669 -0.0113 0.0962  -0.1024 504 LEU B C     
5805 O O     . LEU B 363 ? 0.5096 0.5562 0.3076 -0.0010 0.1019  -0.1080 504 LEU B O     
5806 C CB    . LEU B 363 ? 0.4418 0.4704 0.2247 -0.0185 0.0909  -0.1064 504 LEU B CB    
5807 C CG    . LEU B 363 ? 0.4916 0.5075 0.2640 -0.0246 0.0909  -0.1141 504 LEU B CG    
5808 C CD1   . LEU B 363 ? 0.4556 0.4601 0.2281 -0.0270 0.0860  -0.1107 504 LEU B CD1   
5809 C CD2   . LEU B 363 ? 0.4694 0.4730 0.2396 -0.0165 0.0978  -0.1258 504 LEU B CD2   
5810 N N     . ASN B 364 ? 0.4290 0.4936 0.2288 -0.0154 0.0912  -0.0919 505 ASN B N     
5811 C CA    . ASN B 364 ? 0.4170 0.4906 0.2283 -0.0085 0.0926  -0.0869 505 ASN B CA    
5812 C C     . ASN B 364 ? 0.4803 0.5645 0.2914 -0.0081 0.0980  -0.0906 505 ASN B C     
5813 O O     . ASN B 364 ? 0.4735 0.5593 0.2930 0.0008  0.1022  -0.0918 505 ASN B O     
5814 C CB    . ASN B 364 ? 0.4181 0.5039 0.2356 -0.0141 0.0858  -0.0750 505 ASN B CB    
5815 C CG    . ASN B 364 ? 0.4421 0.5389 0.2715 -0.0087 0.0869  -0.0699 505 ASN B CG    
5816 O OD1   . ASN B 364 ? 0.3861 0.4769 0.2237 0.0014  0.0894  -0.0712 505 ASN B OD1   
5817 N ND2   . ASN B 364 ? 0.4323 0.5455 0.2629 -0.0155 0.0852  -0.0644 505 ASN B ND2   
5818 N N     . ALA B 365 ? 0.4559 0.5479 0.2577 -0.0180 0.0978  -0.0923 506 ALA B N     
5819 C CA    . ALA B 365 ? 0.5350 0.6371 0.3356 -0.0182 0.1034  -0.0969 506 ALA B CA    
5820 C C     . ALA B 365 ? 0.5695 0.6600 0.3702 -0.0076 0.1112  -0.1080 506 ALA B C     
5821 O O     . ALA B 365 ? 0.6646 0.7623 0.4689 -0.0035 0.1167  -0.1112 506 ALA B O     
5822 C CB    . ALA B 365 ? 0.4725 0.5834 0.2619 -0.0310 0.1019  -0.0979 506 ALA B CB    
5823 N N     . GLU B 366 ? 0.5552 0.6278 0.3522 -0.0032 0.1116  -0.1137 507 GLU B N     
5824 C CA    . GLU B 366 ? 0.5616 0.6209 0.3596 0.0080  0.1180  -0.1235 507 GLU B CA    
5825 C C     . GLU B 366 ? 0.5680 0.6205 0.3783 0.0205  0.1187  -0.1205 507 GLU B C     
5826 O O     . GLU B 366 ? 0.5752 0.6158 0.3879 0.0309  0.1233  -0.1272 507 GLU B O     
5827 C CB    . GLU B 366 ? 0.5861 0.6290 0.3745 0.0060  0.1175  -0.1312 507 GLU B CB    
5828 C CG    . GLU B 366 ? 0.7577 0.8031 0.5345 -0.0021 0.1205  -0.1394 507 GLU B CG    
5829 C CD    . GLU B 366 ? 0.8210 0.8793 0.5992 -0.0006 0.1266  -0.1429 507 GLU B CD    
5830 O OE1   . GLU B 366 ? 0.8128 0.8649 0.5957 0.0104  0.1327  -0.1495 507 GLU B OE1   
5831 O OE2   . GLU B 366 ? 0.7889 0.8639 0.5642 -0.0104 0.1251  -0.1385 507 GLU B OE2   
5832 N N     . GLY B 367 ? 0.4917 0.5514 0.3100 0.0196  0.1141  -0.1104 508 GLY B N     
5833 C CA    . GLY B 367 ? 0.4965 0.5507 0.3266 0.0300  0.1144  -0.1069 508 GLY B CA    
5834 C C     . GLY B 367 ? 0.5135 0.5536 0.3436 0.0322  0.1099  -0.1047 508 GLY B C     
5835 O O     . GLY B 367 ? 0.4383 0.4744 0.2785 0.0395  0.1095  -0.1009 508 GLY B O     
5836 N N     . ILE B 368 ? 0.4305 0.4639 0.2503 0.0251  0.1066  -0.1069 509 ILE B N     
5837 C CA    . ILE B 368 ? 0.4995 0.5186 0.3184 0.0266  0.1029  -0.1065 509 ILE B CA    
5838 C C     . ILE B 368 ? 0.4376 0.4643 0.2587 0.0192  0.0964  -0.0966 509 ILE B C     
5839 O O     . ILE B 368 ? 0.4291 0.4657 0.2446 0.0082  0.0931  -0.0931 509 ILE B O     
5840 C CB    . ILE B 368 ? 0.4710 0.4782 0.2786 0.0217  0.1030  -0.1148 509 ILE B CB    
5841 C CG1   . ILE B 368 ? 0.4650 0.4659 0.2708 0.0286  0.1094  -0.1252 509 ILE B CG1   
5842 C CG2   . ILE B 368 ? 0.4505 0.4426 0.2581 0.0222  0.0993  -0.1147 509 ILE B CG2   
5843 C CD1   . ILE B 368 ? 0.5160 0.5094 0.3098 0.0209  0.1103  -0.1337 509 ILE B CD1   
5844 N N     . ALA B 369 ? 0.3929 0.4150 0.2222 0.0253  0.0944  -0.0920 510 ALA B N     
5845 C CA    . ALA B 369 ? 0.3802 0.4087 0.2130 0.0197  0.0883  -0.0831 510 ALA B CA    
5846 C C     . ALA B 369 ? 0.4082 0.4229 0.2349 0.0160  0.0852  -0.0845 510 ALA B C     
5847 O O     . ALA B 369 ? 0.3821 0.3826 0.2111 0.0233  0.0863  -0.0877 510 ALA B O     
5848 C CB    . ALA B 369 ? 0.3396 0.3730 0.1861 0.0274  0.0880  -0.0774 510 ALA B CB    
5849 N N     . VAL B 370 ? 0.3532 0.3721 0.1728 0.0043  0.0808  -0.0814 511 VAL B N     
5850 C CA    . VAL B 370 ? 0.3859 0.3938 0.2006 -0.0013 0.0772  -0.0807 511 VAL B CA    
5851 C C     . VAL B 370 ? 0.4156 0.4366 0.2322 -0.0102 0.0707  -0.0709 511 VAL B C     
5852 O O     . VAL B 370 ? 0.4496 0.4872 0.2694 -0.0134 0.0689  -0.0655 511 VAL B O     
5853 C CB    . VAL B 370 ? 0.4289 0.4258 0.2319 -0.0075 0.0781  -0.0884 511 VAL B CB    
5854 C CG1   . VAL B 370 ? 0.3979 0.3813 0.2001 0.0015  0.0840  -0.0983 511 VAL B CG1   
5855 C CG2   . VAL B 370 ? 0.4467 0.4575 0.2433 -0.0175 0.0766  -0.0875 511 VAL B CG2   
5856 N N     . ARG B 371 ? 0.4308 0.4438 0.2467 -0.0139 0.0666  -0.0677 512 ARG B N     
5857 C CA    . ARG B 371 ? 0.3938 0.4178 0.2137 -0.0220 0.0590  -0.0578 512 ARG B CA    
5858 C C     . ARG B 371 ? 0.3988 0.4231 0.2054 -0.0343 0.0573  -0.0607 512 ARG B C     
5859 O O     . ARG B 371 ? 0.3888 0.3984 0.1873 -0.0358 0.0593  -0.0680 512 ARG B O     
5860 C CB    . ARG B 371 ? 0.4759 0.4930 0.3066 -0.0186 0.0541  -0.0511 512 ARG B CB    
5861 C CG    . ARG B 371 ? 0.5140 0.5372 0.3601 -0.0097 0.0526  -0.0442 512 ARG B CG    
5862 C CD    . ARG B 371 ? 0.4770 0.5196 0.3293 -0.0119 0.0503  -0.0375 512 ARG B CD    
5863 N NE    . ARG B 371 ? 0.4695 0.5163 0.3336 -0.0024 0.0516  -0.0348 512 ARG B NE    
5864 C CZ    . ARG B 371 ? 0.4425 0.5029 0.3168 -0.0024 0.0484  -0.0270 512 ARG B CZ    
5865 N NH1   . ARG B 371 ? 0.4407 0.5117 0.3164 -0.0107 0.0431  -0.0200 512 ARG B NH1   
5866 N NH2   . ARG B 371 ? 0.4065 0.4701 0.2904 0.0060  0.0502  -0.0259 512 ARG B NH2   
5867 N N     . ALA B 372 ? 0.4199 0.4602 0.2274 -0.0423 0.0522  -0.0535 513 ALA B N     
5868 C CA    . ALA B 372 ? 0.4476 0.4903 0.2473 -0.0536 0.0480  -0.0531 513 ALA B CA    
5869 C C     . ALA B 372 ? 0.4545 0.5088 0.2607 -0.0596 0.0401  -0.0418 513 ALA B C     
5870 O O     . ALA B 372 ? 0.5207 0.5896 0.3343 -0.0598 0.0371  -0.0338 513 ALA B O     
5871 C CB    . ALA B 372 ? 0.4261 0.4778 0.2201 -0.0581 0.0495  -0.0557 513 ALA B CB    
5872 N N     . GLY B 373 ? 0.4391 0.4866 0.2447 -0.0639 0.0363  -0.0408 514 GLY B N     
5873 C CA    . GLY B 373 ? 0.3827 0.4397 0.2001 -0.0670 0.0281  -0.0294 514 GLY B CA    
5874 C C     . GLY B 373 ? 0.3810 0.4265 0.2015 -0.0675 0.0259  -0.0298 514 GLY B C     
5875 O O     . GLY B 373 ? 0.3855 0.4175 0.1954 -0.0696 0.0293  -0.0382 514 GLY B O     
5876 N N     . HIS B 374 ? 0.3582 0.4089 0.1936 -0.0656 0.0204  -0.0209 515 HIS B N     
5877 C CA    . HIS B 374 ? 0.4006 0.4429 0.2401 -0.0668 0.0180  -0.0205 515 HIS B CA    
5878 C C     . HIS B 374 ? 0.3337 0.3632 0.1806 -0.0563 0.0215  -0.0224 515 HIS B C     
5879 O O     . HIS B 374 ? 0.3519 0.3728 0.2008 -0.0570 0.0207  -0.0230 515 HIS B O     
5880 C CB    . HIS B 374 ? 0.3893 0.4455 0.2408 -0.0718 0.0098  -0.0103 515 HIS B CB    
5881 C CG    . HIS B 374 ? 0.3875 0.4526 0.2555 -0.0649 0.0072  -0.0020 515 HIS B CG    
5882 N ND1   . HIS B 374 ? 0.4330 0.5138 0.3099 -0.0688 0.0007  0.0074  515 HIS B ND1   
5883 C CD2   . HIS B 374 ? 0.3095 0.3698 0.1876 -0.0549 0.0098  -0.0015 515 HIS B CD2   
5884 C CE1   . HIS B 374 ? 0.3395 0.4239 0.2309 -0.0614 -0.0001 0.0128  515 HIS B CE1   
5885 N NE2   . HIS B 374 ? 0.4155 0.4881 0.3077 -0.0531 0.0053  0.0073  515 HIS B NE2   
5886 N N     . HIS B 375 ? 0.3562 0.3852 0.2069 -0.0473 0.0253  -0.0230 516 HIS B N     
5887 C CA    . HIS B 375 ? 0.3669 0.3836 0.2225 -0.0373 0.0291  -0.0255 516 HIS B CA    
5888 C C     . HIS B 375 ? 0.3338 0.3511 0.2029 -0.0349 0.0253  -0.0193 516 HIS B C     
5889 O O     . HIS B 375 ? 0.3053 0.3107 0.1757 -0.0300 0.0274  -0.0215 516 HIS B O     
5890 C CB    . HIS B 375 ? 0.3453 0.3438 0.1885 -0.0369 0.0341  -0.0347 516 HIS B CB    
5891 C CG    . HIS B 375 ? 0.4017 0.3993 0.2307 -0.0411 0.0379  -0.0421 516 HIS B CG    
5892 N ND1   . HIS B 375 ? 0.3853 0.3887 0.2126 -0.0367 0.0417  -0.0444 516 HIS B ND1   
5893 C CD2   . HIS B 375 ? 0.3828 0.3751 0.1984 -0.0499 0.0385  -0.0479 516 HIS B CD2   
5894 C CE1   . HIS B 375 ? 0.4289 0.4308 0.2424 -0.0424 0.0449  -0.0518 516 HIS B CE1   
5895 N NE2   . HIS B 375 ? 0.4189 0.4138 0.2249 -0.0506 0.0429  -0.0542 516 HIS B NE2   
5896 N N     . CYS B 376 ? 0.3000 0.3314 0.1794 -0.0384 0.0196  -0.0115 517 CYS B N     
5897 C CA    . CYS B 376 ? 0.3093 0.3430 0.2026 -0.0365 0.0161  -0.0062 517 CYS B CA    
5898 C C     . CYS B 376 ? 0.3121 0.3354 0.2012 -0.0404 0.0163  -0.0093 517 CYS B C     
5899 O O     . CYS B 376 ? 0.3237 0.3407 0.2188 -0.0362 0.0172  -0.0092 517 CYS B O     
5900 C CB    . CYS B 376 ? 0.3211 0.3530 0.2242 -0.0264 0.0183  -0.0050 517 CYS B CB    
5901 S SG    . CYS B 376 ? 0.4572 0.5025 0.3676 -0.0225 0.0176  -0.0004 517 CYS B SG    
5902 N N     . ALA B 377 ? 0.2797 0.3015 0.1576 -0.0491 0.0155  -0.0124 518 ALA B N     
5903 C CA    . ALA B 377 ? 0.2782 0.2908 0.1509 -0.0546 0.0154  -0.0155 518 ALA B CA    
5904 C C     . ALA B 377 ? 0.2750 0.2955 0.1415 -0.0659 0.0114  -0.0150 518 ALA B C     
5905 O O     . ALA B 377 ? 0.3211 0.3327 0.1742 -0.0721 0.0132  -0.0211 518 ALA B O     
5906 C CB    . ALA B 377 ? 0.3160 0.3093 0.1765 -0.0516 0.0214  -0.0235 518 ALA B CB    
5907 N N     . GLN B 378 ? 0.2972 0.3345 0.1736 -0.0689 0.0057  -0.0075 519 GLN B N     
5908 C CA    . GLN B 378 ? 0.3478 0.3949 0.2194 -0.0798 0.0009  -0.0058 519 GLN B CA    
5909 C C     . GLN B 378 ? 0.3369 0.3788 0.2050 -0.0872 -0.0003 -0.0084 519 GLN B C     
5910 O O     . GLN B 378 ? 0.3351 0.3766 0.1906 -0.0963 -0.0011 -0.0120 519 GLN B O     
5911 C CB    . GLN B 378 ? 0.3408 0.4064 0.2267 -0.0807 -0.0058 0.0042  519 GLN B CB    
5912 C CG    . GLN B 378 ? 0.3101 0.3822 0.1972 -0.0761 -0.0053 0.0073  519 GLN B CG    
5913 C CD    . GLN B 378 ? 0.3982 0.4873 0.2988 -0.0778 -0.0124 0.0176  519 GLN B CD    
5914 O OE1   . GLN B 378 ? 0.3620 0.4545 0.2790 -0.0718 -0.0142 0.0227  519 GLN B OE1   
5915 N NE2   . GLN B 378 ? 0.3707 0.4704 0.2644 -0.0862 -0.0165 0.0209  519 GLN B NE2   
5916 N N     . PRO B 379 ? 0.3026 0.3412 0.1807 -0.0846 -0.0004 -0.0070 520 PRO B N     
5917 C CA    . PRO B 379 ? 0.3092 0.3451 0.1841 -0.0932 -0.0019 -0.0090 520 PRO B CA    
5918 C C     . PRO B 379 ? 0.3719 0.3905 0.2284 -0.0974 0.0028  -0.0181 520 PRO B C     
5919 O O     . PRO B 379 ? 0.3528 0.3725 0.2009 -0.1078 0.0007  -0.0205 520 PRO B O     
5920 C CB    . PRO B 379 ? 0.3124 0.3476 0.2015 -0.0882 -0.0017 -0.0063 520 PRO B CB    
5921 C CG    . PRO B 379 ? 0.3338 0.3793 0.2377 -0.0799 -0.0033 -0.0001 520 PRO B CG    
5922 C CD    . PRO B 379 ? 0.2852 0.3263 0.1794 -0.0756 -0.0003 -0.0026 520 PRO B CD    
5923 N N     . ILE B 380 ? 0.3314 0.3339 0.1814 -0.0899 0.0090  -0.0233 521 ILE B N     
5924 C CA    . ILE B 380 ? 0.3696 0.3539 0.2028 -0.0936 0.0136  -0.0321 521 ILE B CA    
5925 C C     . ILE B 380 ? 0.4048 0.3917 0.2246 -0.0998 0.0138  -0.0367 521 ILE B C     
5926 O O     . ILE B 380 ? 0.4385 0.4168 0.2453 -0.1081 0.0149  -0.0430 521 ILE B O     
5927 C CB    . ILE B 380 ? 0.3607 0.3273 0.1913 -0.0834 0.0197  -0.0360 521 ILE B CB    
5928 C CG1   . ILE B 380 ? 0.3638 0.3098 0.1790 -0.0872 0.0241  -0.0445 521 ILE B CG1   
5929 C CG2   . ILE B 380 ? 0.3113 0.2805 0.1425 -0.0745 0.0223  -0.0363 521 ILE B CG2   
5930 C CD1   . ILE B 380 ? 0.4083 0.3499 0.2212 -0.0968 0.0221  -0.0449 521 ILE B CD1   
5931 N N     . LEU B 381 ? 0.3822 0.3811 0.2045 -0.0967 0.0127  -0.0337 522 LEU B N     
5932 C CA    . LEU B 381 ? 0.4282 0.4309 0.2370 -0.1032 0.0132  -0.0381 522 LEU B CA    
5933 C C     . LEU B 381 ? 0.4264 0.4423 0.2331 -0.1160 0.0068  -0.0351 522 LEU B C     
5934 O O     . LEU B 381 ? 0.4781 0.4911 0.2698 -0.1249 0.0076  -0.0415 522 LEU B O     
5935 C CB    . LEU B 381 ? 0.3404 0.3532 0.1522 -0.0971 0.0139  -0.0352 522 LEU B CB    
5936 C CG    . LEU B 381 ? 0.4446 0.4457 0.2558 -0.0854 0.0206  -0.0395 522 LEU B CG    
5937 C CD1   . LEU B 381 ? 0.4257 0.4377 0.2353 -0.0829 0.0218  -0.0387 522 LEU B CD1   
5938 C CD2   . LEU B 381 ? 0.4393 0.4194 0.2371 -0.0852 0.0269  -0.0502 522 LEU B CD2   
5939 N N     . ARG B 382 ? 0.3735 0.4043 0.1952 -0.1170 0.0004  -0.0257 523 ARG B N     
5940 C CA    . ARG B 382 ? 0.4270 0.4704 0.2485 -0.1289 -0.0062 -0.0224 523 ARG B CA    
5941 C C     . ARG B 382 ? 0.4642 0.4954 0.2772 -0.1364 -0.0047 -0.0290 523 ARG B C     
5942 O O     . ARG B 382 ? 0.4445 0.4798 0.2475 -0.1479 -0.0074 -0.0316 523 ARG B O     
5943 C CB    . ARG B 382 ? 0.3987 0.4589 0.2405 -0.1271 -0.0129 -0.0115 523 ARG B CB    
5944 C CG    . ARG B 382 ? 0.5188 0.5917 0.3700 -0.1211 -0.0155 -0.0039 523 ARG B CG    
5945 C CD    . ARG B 382 ? 0.4946 0.5869 0.3620 -0.1240 -0.0240 0.0067  523 ARG B CD    
5946 N NE    . ARG B 382 ? 0.4834 0.5847 0.3621 -0.1166 -0.0258 0.0141  523 ARG B NE    
5947 C CZ    . ARG B 382 ? 0.5370 0.6369 0.4313 -0.1066 -0.0248 0.0175  523 ARG B CZ    
5948 N NH1   . ARG B 382 ? 0.3601 0.4507 0.2604 -0.1024 -0.0216 0.0143  523 ARG B NH1   
5949 N NH2   . ARG B 382 ? 0.4583 0.5665 0.3620 -0.1012 -0.0268 0.0242  523 ARG B NH2   
5950 N N     . ARG B 383 ? 0.4241 0.4404 0.2405 -0.1305 -0.0005 -0.0315 524 ARG B N     
5951 C CA    . ARG B 383 ? 0.4451 0.4474 0.2524 -0.1376 0.0015  -0.0379 524 ARG B CA    
5952 C C     . ARG B 383 ? 0.4729 0.4616 0.2597 -0.1429 0.0059  -0.0483 524 ARG B C     
5953 O O     . ARG B 383 ? 0.4956 0.4784 0.2725 -0.1535 0.0056  -0.0534 524 ARG B O     
5954 C CB    . ARG B 383 ? 0.3955 0.3834 0.2091 -0.1295 0.0056  -0.0383 524 ARG B CB    
5955 C CG    . ARG B 383 ? 0.4389 0.4065 0.2408 -0.1347 0.0096  -0.0457 524 ARG B CG    
5956 C CD    . ARG B 383 ? 0.4303 0.4047 0.2341 -0.1467 0.0052  -0.0441 524 ARG B CD    
5957 N NE    . ARG B 383 ? 0.4255 0.3796 0.2174 -0.1524 0.0090  -0.0512 524 ARG B NE    
5958 C CZ    . ARG B 383 ? 0.5113 0.4532 0.2862 -0.1594 0.0114  -0.0598 524 ARG B CZ    
5959 N NH1   . ARG B 383 ? 0.4708 0.4200 0.2377 -0.1623 0.0105  -0.0627 524 ARG B NH1   
5960 N NH2   . ARG B 383 ? 0.4868 0.4087 0.2523 -0.1640 0.0149  -0.0656 524 ARG B NH2   
5961 N N     . MET B 384 ? 0.4508 0.4351 0.2316 -0.1361 0.0102  -0.0518 525 MET B N     
5962 C CA    . MET B 384 ? 0.4970 0.4694 0.2593 -0.1400 0.0151  -0.0624 525 MET B CA    
5963 C C     . MET B 384 ? 0.5248 0.5139 0.2836 -0.1478 0.0116  -0.0613 525 MET B C     
5964 O O     . MET B 384 ? 0.5233 0.5058 0.2731 -0.1494 0.0156  -0.0684 525 MET B O     
5965 C CB    . MET B 384 ? 0.5172 0.4778 0.2781 -0.1273 0.0220  -0.0665 525 MET B CB    
5966 C CG    . MET B 384 ? 0.5163 0.4547 0.2785 -0.1195 0.0270  -0.0699 525 MET B CG    
5967 S SD    . MET B 384 ? 0.6450 0.5673 0.3997 -0.1298 0.0269  -0.0744 525 MET B SD    
5968 C CE    . MET B 384 ? 0.6012 0.5038 0.3628 -0.1182 0.0310  -0.0731 525 MET B CE    
5969 N N     . GLY B 385 ? 0.4740 0.4845 0.2415 -0.1520 0.0042  -0.0518 526 GLY B N     
5970 C CA    . GLY B 385 ? 0.5087 0.5356 0.2753 -0.1589 0.0004  -0.0488 526 GLY B CA    
5971 C C     . GLY B 385 ? 0.5142 0.5495 0.2819 -0.1526 0.0017  -0.0465 526 GLY B C     
5972 O O     . GLY B 385 ? 0.5579 0.6026 0.3216 -0.1579 0.0007  -0.0465 526 GLY B O     
5973 N N     . LEU B 386 ? 0.4787 0.5118 0.2520 -0.1420 0.0040  -0.0443 527 LEU B N     
5974 C CA    . LEU B 386 ? 0.5020 0.5395 0.2755 -0.1350 0.0070  -0.0439 527 LEU B CA    
5975 C C     . LEU B 386 ? 0.5258 0.5767 0.3119 -0.1293 0.0028  -0.0333 527 LEU B C     
5976 O O     . LEU B 386 ? 0.4442 0.4949 0.2429 -0.1255 0.0001  -0.0279 527 LEU B O     
5977 C CB    . LEU B 386 ? 0.4890 0.5072 0.2560 -0.1259 0.0160  -0.0537 527 LEU B CB    
5978 C CG    . LEU B 386 ? 0.5420 0.5456 0.2970 -0.1302 0.0209  -0.0647 527 LEU B CG    
5979 C CD1   . LEU B 386 ? 0.5490 0.5337 0.3002 -0.1198 0.0292  -0.0731 527 LEU B CD1   
5980 C CD2   . LEU B 386 ? 0.4969 0.5123 0.2465 -0.1372 0.0200  -0.0657 527 LEU B CD2   
5981 N N     . GLU B 387 ? 0.4812 0.5431 0.2695 -0.1269 0.0026  -0.0296 528 GLU B N     
5982 C CA    . GLU B 387 ? 0.4941 0.5673 0.2942 -0.1206 -0.0004 -0.0201 528 GLU B CA    
5983 C C     . GLU B 387 ? 0.4637 0.5279 0.2653 -0.1088 0.0067  -0.0238 528 GLU B C     
5984 O O     . GLU B 387 ? 0.4361 0.5053 0.2524 -0.1007 0.0053  -0.0167 528 GLU B O     
5985 C CB    . GLU B 387 ? 0.4924 0.5844 0.2969 -0.1256 -0.0061 -0.0115 528 GLU B CB    
5986 C CG    . GLU B 387 ? 0.5893 0.6942 0.4001 -0.1346 -0.0150 -0.0034 528 GLU B CG    
5987 C CD    . GLU B 387 ? 0.7160 0.8257 0.5423 -0.1306 -0.0204 0.0052  528 GLU B CD    
5988 O OE1   . GLU B 387 ? 0.6961 0.8097 0.5354 -0.1221 -0.0208 0.0115  528 GLU B OE1   
5989 O OE2   . GLU B 387 ? 0.6837 0.7922 0.5144 -0.1345 -0.0234 0.0054  528 GLU B OE2   
5990 N N     . ALA B 388 ? 0.4323 0.4833 0.2221 -0.1068 0.0141  -0.0348 529 ALA B N     
5991 C CA    . ALA B 388 ? 0.4733 0.5181 0.2629 -0.0966 0.0210  -0.0391 529 ALA B CA    
5992 C C     . ALA B 388 ? 0.4659 0.4933 0.2446 -0.0951 0.0282  -0.0516 529 ALA B C     
5993 O O     . ALA B 388 ? 0.4809 0.5051 0.2516 -0.1031 0.0277  -0.0562 529 ALA B O     
5994 C CB    . ALA B 388 ? 0.4335 0.4936 0.2260 -0.0962 0.0203  -0.0346 529 ALA B CB    
5995 N N     . THR B 389 ? 0.4349 0.4511 0.2142 -0.0846 0.0346  -0.0566 530 THR B N     
5996 C CA    . THR B 389 ? 0.4452 0.4461 0.2163 -0.0811 0.0416  -0.0679 530 THR B CA    
5997 C C     . THR B 389 ? 0.4554 0.4583 0.2302 -0.0707 0.0470  -0.0699 530 THR B C     
5998 O O     . THR B 389 ? 0.3740 0.3868 0.1575 -0.0658 0.0457  -0.0630 530 THR B O     
5999 C CB    . THR B 389 ? 0.4263 0.4060 0.1944 -0.0785 0.0443  -0.0735 530 THR B CB    
6000 O OG1   . THR B 389 ? 0.4628 0.4368 0.2390 -0.0679 0.0463  -0.0708 530 THR B OG1   
6001 C CG2   . THR B 389 ? 0.4646 0.4436 0.2308 -0.0886 0.0388  -0.0704 530 THR B CG2   
6002 N N     . VAL B 390 ? 0.4159 0.4099 0.1844 -0.0677 0.0529  -0.0795 531 VAL B N     
6003 C CA    . VAL B 390 ? 0.4153 0.4073 0.1874 -0.0565 0.0590  -0.0834 531 VAL B CA    
6004 C C     . VAL B 390 ? 0.4302 0.4025 0.2040 -0.0478 0.0626  -0.0878 531 VAL B C     
6005 O O     . VAL B 390 ? 0.4315 0.3882 0.1991 -0.0506 0.0636  -0.0934 531 VAL B O     
6006 C CB    . VAL B 390 ? 0.4452 0.4383 0.2103 -0.0575 0.0635  -0.0916 531 VAL B CB    
6007 C CG1   . VAL B 390 ? 0.4295 0.4239 0.1998 -0.0460 0.0693  -0.0947 531 VAL B CG1   
6008 C CG2   . VAL B 390 ? 0.4333 0.4439 0.1946 -0.0685 0.0593  -0.0873 531 VAL B CG2   
6009 N N     . ARG B 391 ? 0.3895 0.3622 0.1720 -0.0376 0.0645  -0.0848 532 ARG B N     
6010 C CA    . ARG B 391 ? 0.4339 0.3890 0.2193 -0.0298 0.0666  -0.0861 532 ARG B CA    
6011 C C     . ARG B 391 ? 0.4393 0.3917 0.2316 -0.0167 0.0717  -0.0887 532 ARG B C     
6012 O O     . ARG B 391 ? 0.4706 0.4306 0.2731 -0.0103 0.0707  -0.0823 532 ARG B O     
6013 C CB    . ARG B 391 ? 0.4247 0.3836 0.2196 -0.0306 0.0603  -0.0756 532 ARG B CB    
6014 C CG    . ARG B 391 ? 0.4380 0.3793 0.2379 -0.0238 0.0605  -0.0749 532 ARG B CG    
6015 C CD    . ARG B 391 ? 0.4000 0.3489 0.2143 -0.0201 0.0552  -0.0641 532 ARG B CD    
6016 N NE    . ARG B 391 ? 0.3935 0.3543 0.2178 -0.0118 0.0560  -0.0603 532 ARG B NE    
6017 C CZ    . ARG B 391 ? 0.4165 0.3874 0.2536 -0.0088 0.0519  -0.0515 532 ARG B CZ    
6018 N NH1   . ARG B 391 ? 0.3839 0.3545 0.2262 -0.0125 0.0470  -0.0458 532 ARG B NH1   
6019 N NH2   . ARG B 391 ? 0.4500 0.4317 0.2951 -0.0022 0.0529  -0.0489 532 ARG B NH2   
6020 N N     . PRO B 392 ? 0.4327 0.3751 0.2223 -0.0119 0.0765  -0.0975 533 PRO B N     
6021 C CA    . PRO B 392 ? 0.4429 0.3779 0.2403 0.0015  0.0807  -0.0999 533 PRO B CA    
6022 C C     . PRO B 392 ? 0.4355 0.3525 0.2352 0.0060  0.0797  -0.0973 533 PRO B C     
6023 O O     . PRO B 392 ? 0.4502 0.3548 0.2431 -0.0008 0.0776  -0.0975 533 PRO B O     
6024 C CB    . PRO B 392 ? 0.4430 0.3707 0.2361 0.0038  0.0851  -0.1103 533 PRO B CB    
6025 C CG    . PRO B 392 ? 0.4472 0.3681 0.2290 -0.0081 0.0832  -0.1135 533 PRO B CG    
6026 C CD    . PRO B 392 ? 0.4235 0.3603 0.2035 -0.0182 0.0780  -0.1055 533 PRO B CD    
6027 N N     . SER B 393 ? 0.4413 0.3575 0.2508 0.0172  0.0809  -0.0941 534 SER B N     
6028 C CA    . SER B 393 ? 0.4492 0.3495 0.2626 0.0233  0.0795  -0.0904 534 SER B CA    
6029 C C     . SER B 393 ? 0.4700 0.3672 0.2930 0.0368  0.0826  -0.0918 534 SER B C     
6030 O O     . SER B 393 ? 0.4699 0.3834 0.3011 0.0419  0.0836  -0.0906 534 SER B O     
6031 C CB    . SER B 393 ? 0.4523 0.3627 0.2746 0.0209  0.0727  -0.0789 534 SER B CB    
6032 O OG    . SER B 393 ? 0.4282 0.3587 0.2601 0.0241  0.0714  -0.0736 534 SER B OG    
6033 N N     . PHE B 394 ? 0.4459 0.3234 0.2691 0.0419  0.0833  -0.0939 535 PHE B N     
6034 C CA    . PHE B 394 ? 0.5080 0.3815 0.3408 0.0536  0.0857  -0.0963 535 PHE B CA    
6035 C C     . PHE B 394 ? 0.4941 0.3635 0.3356 0.0623  0.0830  -0.0881 535 PHE B C     
6036 O O     . PHE B 394 ? 0.5343 0.3947 0.3718 0.0598  0.0801  -0.0825 535 PHE B O     
6037 C CB    . PHE B 394 ? 0.5056 0.3599 0.3338 0.0540  0.0883  -0.1043 535 PHE B CB    
6038 C CG    . PHE B 394 ? 0.5189 0.3760 0.3376 0.0450  0.0904  -0.1127 535 PHE B CG    
6039 C CD1   . PHE B 394 ? 0.5365 0.4098 0.3578 0.0464  0.0934  -0.1184 535 PHE B CD1   
6040 C CD2   . PHE B 394 ? 0.5543 0.3991 0.3613 0.0347  0.0892  -0.1147 535 PHE B CD2   
6041 C CE1   . PHE B 394 ? 0.5431 0.4197 0.3547 0.0382  0.0951  -0.1256 535 PHE B CE1   
6042 C CE2   . PHE B 394 ? 0.5830 0.4315 0.3811 0.0260  0.0907  -0.1220 535 PHE B CE2   
6043 C CZ    . PHE B 394 ? 0.5429 0.4072 0.3430 0.0279  0.0936  -0.1273 535 PHE B CZ    
6044 N N     . ALA B 395 ? 0.4971 0.3743 0.3508 0.0722  0.0840  -0.0876 536 ALA B N     
6045 C CA    . ALA B 395 ? 0.4787 0.3538 0.3419 0.0811  0.0812  -0.0801 536 ALA B CA    
6046 C C     . ALA B 395 ? 0.4840 0.3522 0.3554 0.0904  0.0833  -0.0839 536 ALA B C     
6047 O O     . ALA B 395 ? 0.4687 0.3379 0.3402 0.0904  0.0872  -0.0925 536 ALA B O     
6048 C CB    . ALA B 395 ? 0.4426 0.3397 0.3149 0.0831  0.0790  -0.0736 536 ALA B CB    
6049 N N     . PHE B 396 ? 0.4396 0.3018 0.3183 0.0984  0.0805  -0.0775 537 PHE B N     
6050 C CA    . PHE B 396 ? 0.4871 0.3400 0.3734 0.1072  0.0816  -0.0799 537 PHE B CA    
6051 C C     . PHE B 396 ? 0.4610 0.3318 0.3601 0.1131  0.0840  -0.0834 537 PHE B C     
6052 O O     . PHE B 396 ? 0.5246 0.3893 0.4314 0.1206  0.0853  -0.0862 537 PHE B O     
6053 C CB    . PHE B 396 ? 0.4896 0.3317 0.3794 0.1134  0.0773  -0.0710 537 PHE B CB    
6054 C CG    . PHE B 396 ? 0.4573 0.3167 0.3562 0.1172  0.0737  -0.0626 537 PHE B CG    
6055 C CD1   . PHE B 396 ? 0.5304 0.4025 0.4430 0.1251  0.0734  -0.0615 537 PHE B CD1   
6056 C CD2   . PHE B 396 ? 0.4497 0.3125 0.3438 0.1126  0.0706  -0.0561 537 PHE B CD2   
6057 C CE1   . PHE B 396 ? 0.5071 0.3952 0.4278 0.1277  0.0697  -0.0539 537 PHE B CE1   
6058 C CE2   . PHE B 396 ? 0.4845 0.3631 0.3872 0.1158  0.0672  -0.0490 537 PHE B CE2   
6059 C CZ    . PHE B 396 ? 0.4846 0.3759 0.4002 0.1230  0.0666  -0.0479 537 PHE B CZ    
6060 N N     . TYR B 397 ? 0.4215 0.3136 0.3236 0.1100  0.0848  -0.0832 538 TYR B N     
6061 C CA    . TYR B 397 ? 0.4498 0.3567 0.3620 0.1137  0.0884  -0.0887 538 TYR B CA    
6062 C C     . TYR B 397 ? 0.4295 0.3388 0.3348 0.1077  0.0937  -0.0996 538 TYR B C     
6063 O O     . TYR B 397 ? 0.4575 0.3799 0.3699 0.1095  0.0977  -0.1053 538 TYR B O     
6064 C CB    . TYR B 397 ? 0.4295 0.3591 0.3505 0.1141  0.0867  -0.0828 538 TYR B CB    
6065 C CG    . TYR B 397 ? 0.4163 0.3545 0.3305 0.1061  0.0841  -0.0776 538 TYR B CG    
6066 C CD1   . TYR B 397 ? 0.4627 0.4025 0.3658 0.0970  0.0863  -0.0822 538 TYR B CD1   
6067 C CD2   . TYR B 397 ? 0.3848 0.3308 0.3045 0.1076  0.0793  -0.0682 538 TYR B CD2   
6068 C CE1   . TYR B 397 ? 0.3919 0.3399 0.2897 0.0901  0.0837  -0.0769 538 TYR B CE1   
6069 C CE2   . TYR B 397 ? 0.4164 0.3704 0.3314 0.1008  0.0770  -0.0637 538 TYR B CE2   
6070 C CZ    . TYR B 397 ? 0.4011 0.3561 0.3056 0.0923  0.0791  -0.0678 538 TYR B CZ    
6071 O OH    . TYR B 397 ? 0.3250 0.2882 0.2259 0.0860  0.0764  -0.0628 538 TYR B OH    
6072 N N     . ASN B 398 ? 0.4444 0.3422 0.3357 0.1000  0.0939  -0.1027 539 ASN B N     
6073 C CA    . ASN B 398 ? 0.4749 0.3746 0.3585 0.0941  0.0982  -0.1133 539 ASN B CA    
6074 C C     . ASN B 398 ? 0.5438 0.4271 0.4285 0.0991  0.1010  -0.1219 539 ASN B C     
6075 O O     . ASN B 398 ? 0.4766 0.3429 0.3648 0.1052  0.0991  -0.1186 539 ASN B O     
6076 C CB    . ASN B 398 ? 0.4146 0.3098 0.2826 0.0829  0.0967  -0.1128 539 ASN B CB    
6077 C CG    . ASN B 398 ? 0.4514 0.3644 0.3183 0.0773  0.0943  -0.1059 539 ASN B CG    
6078 O OD1   . ASN B 398 ? 0.4350 0.3432 0.2950 0.0719  0.0909  -0.0999 539 ASN B OD1   
6079 N ND2   . ASN B 398 ? 0.3954 0.3292 0.2696 0.0782  0.0964  -0.1067 539 ASN B ND2   
6080 N N     . THR B 399 ? 0.4619 0.3506 0.3432 0.0967  0.1053  -0.1328 540 THR B N     
6081 C CA    . THR B 399 ? 0.5074 0.3832 0.3909 0.1021  0.1083  -0.1425 540 THR B CA    
6082 C C     . THR B 399 ? 0.5256 0.3934 0.3936 0.0944  0.1101  -0.1514 540 THR B C     
6083 O O     . THR B 399 ? 0.5170 0.3945 0.3738 0.0852  0.1097  -0.1512 540 THR B O     
6084 C CB    . THR B 399 ? 0.5240 0.4154 0.4212 0.1097  0.1124  -0.1490 540 THR B CB    
6085 O OG1   . THR B 399 ? 0.5688 0.4801 0.4599 0.1040  0.1150  -0.1551 540 THR B OG1   
6086 C CG2   . THR B 399 ? 0.4739 0.3752 0.3863 0.1160  0.1109  -0.1398 540 THR B CG2   
6087 N N     . PHE B 400 ? 0.5853 0.4351 0.4531 0.0984  0.1118  -0.1589 541 PHE B N     
6088 C CA    . PHE B 400 ? 0.5864 0.4280 0.4401 0.0919  0.1141  -0.1684 541 PHE B CA    
6089 C C     . PHE B 400 ? 0.5445 0.4064 0.3941 0.0912  0.1175  -0.1756 541 PHE B C     
6090 O O     . PHE B 400 ? 0.5605 0.4236 0.3951 0.0819  0.1185  -0.1789 541 PHE B O     
6091 C CB    . PHE B 400 ? 0.6080 0.4261 0.4639 0.0975  0.1154  -0.1750 541 PHE B CB    
6092 C CG    . PHE B 400 ? 0.6523 0.4490 0.5101 0.0984  0.1118  -0.1668 541 PHE B CG    
6093 C CD1   . PHE B 400 ? 0.6540 0.4357 0.4984 0.0881  0.1097  -0.1640 541 PHE B CD1   
6094 C CD2   . PHE B 400 ? 0.6338 0.4258 0.5063 0.1091  0.1103  -0.1614 541 PHE B CD2   
6095 C CE1   . PHE B 400 ? 0.6680 0.4303 0.5127 0.0888  0.1063  -0.1560 541 PHE B CE1   
6096 C CE2   . PHE B 400 ? 0.6700 0.4423 0.5424 0.1101  0.1066  -0.1526 541 PHE B CE2   
6097 C CZ    . PHE B 400 ? 0.5971 0.3545 0.4552 0.1000  0.1047  -0.1500 541 PHE B CZ    
6098 N N     . ASP B 401 ? 0.5799 0.4579 0.4421 0.1005  0.1194  -0.1775 542 ASP B N     
6099 C CA    . ASP B 401 ? 0.5742 0.4711 0.4303 0.1011  0.1228  -0.1823 542 ASP B CA    
6100 C C     . ASP B 401 ? 0.6029 0.5151 0.4482 0.0910  0.1213  -0.1749 542 ASP B C     
6101 O O     . ASP B 401 ? 0.5259 0.4422 0.3565 0.0844  0.1241  -0.1775 542 ASP B O     
6102 C CB    . ASP B 401 ? 0.5809 0.4935 0.4538 0.1127  0.1244  -0.1837 542 ASP B CB    
6103 C CG    . ASP B 401 ? 0.7085 0.6095 0.5877 0.1228  0.1273  -0.1932 542 ASP B CG    
6104 O OD1   . ASP B 401 ? 0.7479 0.6281 0.6176 0.1215  0.1285  -0.1999 542 ASP B OD1   
6105 O OD2   . ASP B 401 ? 0.7676 0.6806 0.6624 0.1311  0.1283  -0.1934 542 ASP B OD2   
6106 N N     . GLU B 402 ? 0.5183 0.4385 0.3716 0.0890  0.1174  -0.1653 543 GLU B N     
6107 C CA    . GLU B 402 ? 0.5160 0.4493 0.3600 0.0797  0.1153  -0.1576 543 GLU B CA    
6108 C C     . GLU B 402 ? 0.4984 0.4195 0.3260 0.0675  0.1142  -0.1583 543 GLU B C     
6109 O O     . GLU B 402 ? 0.5530 0.4835 0.3692 0.0586  0.1147  -0.1569 543 GLU B O     
6110 C CB    . GLU B 402 ? 0.4705 0.4111 0.3265 0.0794  0.1114  -0.1476 543 GLU B CB    
6111 C CG    . GLU B 402 ? 0.5137 0.4700 0.3894 0.0865  0.1131  -0.1466 543 GLU B CG    
6112 C CD    . GLU B 402 ? 0.5058 0.4641 0.3903 0.0846  0.1106  -0.1350 543 GLU B CD    
6113 O OE1   . GLU B 402 ? 0.5204 0.4628 0.3996 0.0834  0.1066  -0.1288 543 GLU B OE1   
6114 O OE2   . GLU B 402 ? 0.5048 0.4781 0.3993 0.0843  0.1128  -0.1307 543 GLU B OE2   
6115 N N     . ILE B 403 ? 0.5133 0.4134 0.3400 0.0661  0.1127  -0.1599 544 ILE B N     
6116 C CA    . ILE B 403 ? 0.5354 0.4238 0.3476 0.0543  0.1116  -0.1615 544 ILE B CA    
6117 C C     . ILE B 403 ? 0.5348 0.4241 0.3366 0.0504  0.1157  -0.1712 544 ILE B C     
6118 O O     . ILE B 403 ? 0.5622 0.4548 0.3518 0.0384  0.1149  -0.1714 544 ILE B O     
6119 C CB    . ILE B 403 ? 0.5525 0.4161 0.3657 0.0549  0.1099  -0.1614 544 ILE B CB    
6120 C CG1   . ILE B 403 ? 0.5302 0.3926 0.3497 0.0558  0.1057  -0.1501 544 ILE B CG1   
6121 C CG2   . ILE B 403 ? 0.5736 0.4244 0.3723 0.0431  0.1095  -0.1655 544 ILE B CG2   
6122 C CD1   . ILE B 403 ? 0.5508 0.3885 0.3718 0.0585  0.1042  -0.1480 544 ILE B CD1   
6123 N N     . ASP B 404 ? 0.5732 0.4606 0.3797 0.0601  0.1200  -0.1793 545 ASP B N     
6124 C CA    . ASP B 404 ? 0.5534 0.4412 0.3495 0.0565  0.1247  -0.1888 545 ASP B CA    
6125 C C     . ASP B 404 ? 0.5916 0.5011 0.3814 0.0504  0.1262  -0.1856 545 ASP B C     
6126 O O     . ASP B 404 ? 0.5795 0.4919 0.3573 0.0394  0.1274  -0.1892 545 ASP B O     
6127 C CB    . ASP B 404 ? 0.5760 0.4566 0.3792 0.0692  0.1291  -0.1978 545 ASP B CB    
6128 C CG    . ASP B 404 ? 0.6265 0.4824 0.4328 0.0724  0.1283  -0.2029 545 ASP B CG    
6129 O OD1   . ASP B 404 ? 0.6075 0.4504 0.4052 0.0623  0.1260  -0.2025 545 ASP B OD1   
6130 O OD2   . ASP B 404 ? 0.6966 0.5458 0.5140 0.0847  0.1298  -0.2070 545 ASP B OD2   
6131 N N     . VAL B 405 ? 0.5638 0.4888 0.3621 0.0567  0.1260  -0.1785 546 VAL B N     
6132 C CA    . VAL B 405 ? 0.5718 0.5167 0.3653 0.0499  0.1271  -0.1735 546 VAL B CA    
6133 C C     . VAL B 405 ? 0.5667 0.5156 0.3516 0.0352  0.1222  -0.1675 546 VAL B C     
6134 O O     . VAL B 405 ? 0.5396 0.4982 0.3151 0.0246  0.1229  -0.1683 546 VAL B O     
6135 C CB    . VAL B 405 ? 0.5862 0.5444 0.3909 0.0586  0.1273  -0.1653 546 VAL B CB    
6136 C CG1   . VAL B 405 ? 0.5947 0.5722 0.3952 0.0499  0.1283  -0.1594 546 VAL B CG1   
6137 C CG2   . VAL B 405 ? 0.5922 0.5477 0.4051 0.0729  0.1323  -0.1708 546 VAL B CG2   
6138 N N     . PHE B 406 ? 0.5562 0.4983 0.3448 0.0343  0.1169  -0.1612 547 PHE B N     
6139 C CA    . PHE B 406 ? 0.4926 0.4378 0.2742 0.0213  0.1118  -0.1547 547 PHE B CA    
6140 C C     . PHE B 406 ? 0.5398 0.4770 0.3088 0.0103  0.1120  -0.1615 547 PHE B C     
6141 O O     . PHE B 406 ? 0.5132 0.4610 0.2744 -0.0017 0.1096  -0.1586 547 PHE B O     
6142 C CB    . PHE B 406 ? 0.4904 0.4265 0.2786 0.0237  0.1073  -0.1482 547 PHE B CB    
6143 C CG    . PHE B 406 ? 0.5004 0.4331 0.2810 0.0113  0.1024  -0.1437 547 PHE B CG    
6144 C CD1   . PHE B 406 ? 0.4990 0.4476 0.2778 0.0030  0.0985  -0.1351 547 PHE B CD1   
6145 C CD2   . PHE B 406 ? 0.5422 0.4555 0.3181 0.0079  0.1014  -0.1476 547 PHE B CD2   
6146 C CE1   . PHE B 406 ? 0.4593 0.4061 0.2323 -0.0080 0.0935  -0.1306 547 PHE B CE1   
6147 C CE2   . PHE B 406 ? 0.4989 0.4096 0.2679 -0.0036 0.0968  -0.1431 547 PHE B CE2   
6148 C CZ    . PHE B 406 ? 0.5081 0.4362 0.2760 -0.0114 0.0927  -0.1348 547 PHE B CZ    
6149 N N     . ILE B 407 ? 0.5311 0.4496 0.2985 0.0138  0.1144  -0.1705 548 ILE B N     
6150 C CA    . ILE B 407 ? 0.5664 0.4758 0.3221 0.0035  0.1149  -0.1777 548 ILE B CA    
6151 C C     . ILE B 407 ? 0.6075 0.5297 0.3554 -0.0017 0.1187  -0.1833 548 ILE B C     
6152 O O     . ILE B 407 ? 0.5751 0.5022 0.3128 -0.0147 0.1171  -0.1840 548 ILE B O     
6153 C CB    . ILE B 407 ? 0.5622 0.4478 0.3191 0.0096  0.1171  -0.1861 548 ILE B CB    
6154 C CG1   . ILE B 407 ? 0.5942 0.4665 0.3579 0.0129  0.1130  -0.1796 548 ILE B CG1   
6155 C CG2   . ILE B 407 ? 0.6238 0.5000 0.3684 -0.0008 0.1183  -0.1947 548 ILE B CG2   
6156 C CD1   . ILE B 407 ? 0.5679 0.4381 0.3246 0.0003  0.1079  -0.1734 548 ILE B CD1   
6157 N N     . ASP B 408 ? 0.5832 0.5117 0.3361 0.0079  0.1238  -0.1871 549 ASP B N     
6158 C CA    . ASP B 408 ? 0.6178 0.5589 0.3636 0.0028  0.1282  -0.1925 549 ASP B CA    
6159 C C     . ASP B 408 ? 0.6252 0.5876 0.3681 -0.0075 0.1248  -0.1832 549 ASP B C     
6160 O O     . ASP B 408 ? 0.5796 0.5507 0.3128 -0.0186 0.1253  -0.1858 549 ASP B O     
6161 C CB    . ASP B 408 ? 0.6455 0.5885 0.3981 0.0158  0.1346  -0.1981 549 ASP B CB    
6162 C CG    . ASP B 408 ? 0.8518 0.7743 0.6058 0.0244  0.1382  -0.2091 549 ASP B CG    
6163 O OD1   . ASP B 408 ? 0.9122 0.8221 0.6575 0.0170  0.1380  -0.2157 549 ASP B OD1   
6164 O OD2   . ASP B 408 ? 0.9042 0.8230 0.6682 0.0384  0.1411  -0.2110 549 ASP B OD2   
6165 N N     . ALA B 409 ? 0.5741 0.5449 0.3253 -0.0043 0.1211  -0.1723 550 ALA B N     
6166 C CA    . ALA B 409 ? 0.5709 0.5612 0.3206 -0.0139 0.1172  -0.1627 550 ALA B CA    
6167 C C     . ALA B 409 ? 0.5384 0.5281 0.2798 -0.0277 0.1113  -0.1593 550 ALA B C     
6168 O O     . ALA B 409 ? 0.5793 0.5830 0.3143 -0.0390 0.1093  -0.1566 550 ALA B O     
6169 C CB    . ALA B 409 ? 0.5715 0.5692 0.3327 -0.0070 0.1147  -0.1522 550 ALA B CB    
6170 N N     . VAL B 410 ? 0.5218 0.4958 0.2634 -0.0274 0.1082  -0.1592 551 VAL B N     
6171 C CA    . VAL B 410 ? 0.5492 0.5221 0.2831 -0.0405 0.1029  -0.1564 551 VAL B CA    
6172 C C     . VAL B 410 ? 0.5882 0.5601 0.3105 -0.0496 0.1054  -0.1656 551 VAL B C     
6173 O O     . VAL B 410 ? 0.5894 0.5721 0.3048 -0.0623 0.1017  -0.1624 551 VAL B O     
6174 C CB    . VAL B 410 ? 0.5133 0.4684 0.2496 -0.0386 0.0998  -0.1552 551 VAL B CB    
6175 C CG1   . VAL B 410 ? 0.5155 0.4704 0.2438 -0.0527 0.0944  -0.1524 551 VAL B CG1   
6176 C CG2   . VAL B 410 ? 0.5279 0.4857 0.2752 -0.0307 0.0972  -0.1457 551 VAL B CG2   
6177 N N     . ARG B 411 ? 0.5921 0.5514 0.3124 -0.0434 0.1116  -0.1772 552 ARG B N     
6178 C CA    . ARG B 411 ? 0.6110 0.5691 0.3199 -0.0525 0.1142  -0.1865 552 ARG B CA    
6179 C C     . ARG B 411 ? 0.6212 0.6002 0.3260 -0.0585 0.1161  -0.1861 552 ARG B C     
6180 O O     . ARG B 411 ? 0.6689 0.6543 0.3638 -0.0710 0.1149  -0.1883 552 ARG B O     
6181 C CB    . ARG B 411 ? 0.6950 0.6342 0.4032 -0.0443 0.1204  -0.1993 552 ARG B CB    
6182 C CG    . ARG B 411 ? 0.8428 0.7779 0.5389 -0.0543 0.1230  -0.2097 552 ARG B CG    
6183 C CD    . ARG B 411 ? 0.9708 0.8859 0.6667 -0.0459 0.1291  -0.2227 552 ARG B CD    
6184 N NE    . ARG B 411 ? 0.9890 0.8981 0.6966 -0.0294 0.1320  -0.2229 552 ARG B NE    
6185 C CZ    . ARG B 411 ? 0.9675 0.8583 0.6822 -0.0206 0.1309  -0.2227 552 ARG B CZ    
6186 N NH1   . ARG B 411 ? 0.9338 0.8096 0.6450 -0.0267 0.1273  -0.2223 552 ARG B NH1   
6187 N NH2   . ARG B 411 ? 0.9290 0.8170 0.6548 -0.0057 0.1334  -0.2225 552 ARG B NH2   
6188 N N     . ARG B 412 ? 0.5800 0.5702 0.2921 -0.0504 0.1187  -0.1829 553 ARG B N     
6189 C CA    . ARG B 412 ? 0.6276 0.6386 0.3363 -0.0572 0.1198  -0.1808 553 ARG B CA    
6190 C C     . ARG B 412 ? 0.6380 0.6633 0.3444 -0.0698 0.1120  -0.1694 553 ARG B C     
6191 O O     . ARG B 412 ? 0.5919 0.6306 0.2907 -0.0810 0.1112  -0.1693 553 ARG B O     
6192 C CB    . ARG B 412 ? 0.6380 0.6583 0.3561 -0.0465 0.1236  -0.1783 553 ARG B CB    
6193 C CG    . ARG B 412 ? 0.6216 0.6341 0.3415 -0.0357 0.1320  -0.1898 553 ARG B CG    
6194 C CD    . ARG B 412 ? 0.7046 0.7323 0.4315 -0.0295 0.1360  -0.1872 553 ARG B CD    
6195 N NE    . ARG B 412 ? 0.7221 0.7490 0.4615 -0.0189 0.1340  -0.1788 553 ARG B NE    
6196 C CZ    . ARG B 412 ? 0.7630 0.7748 0.5100 -0.0057 0.1359  -0.1816 553 ARG B CZ    
6197 N NH1   . ARG B 412 ? 0.8031 0.7983 0.5472 -0.0006 0.1397  -0.1926 553 ARG B NH1   
6198 N NH2   . ARG B 412 ? 0.7050 0.7186 0.4630 0.0026  0.1338  -0.1731 553 ARG B NH2   
6199 N N     . ILE B 413 ? 0.5867 0.6098 0.2998 -0.0681 0.1061  -0.1595 554 ILE B N     
6200 C CA    . ILE B 413 ? 0.5695 0.6058 0.2815 -0.0794 0.0983  -0.1484 554 ILE B CA    
6201 C C     . ILE B 413 ? 0.5897 0.6219 0.2913 -0.0919 0.0953  -0.1517 554 ILE B C     
6202 O O     . ILE B 413 ? 0.6467 0.6932 0.3430 -0.1039 0.0914  -0.1473 554 ILE B O     
6203 C CB    . ILE B 413 ? 0.5527 0.5872 0.2746 -0.0745 0.0929  -0.1377 554 ILE B CB    
6204 C CG1   . ILE B 413 ? 0.5453 0.5908 0.2770 -0.0664 0.0941  -0.1314 554 ILE B CG1   
6205 C CG2   . ILE B 413 ? 0.5439 0.5876 0.2642 -0.0863 0.0844  -0.1277 554 ILE B CG2   
6206 C CD1   . ILE B 413 ? 0.5552 0.5899 0.2970 -0.0541 0.0942  -0.1288 554 ILE B CD1   
6207 N N     . ALA B 414 ? 0.5609 0.5737 0.2598 -0.0894 0.0971  -0.1595 555 ALA B N     
6208 C CA    . ALA B 414 ? 0.6124 0.6200 0.3018 -0.1012 0.0945  -0.1630 555 ALA B CA    
6209 C C     . ALA B 414 ? 0.6607 0.6751 0.3395 -0.1093 0.0985  -0.1716 555 ALA B C     
6210 O O     . ALA B 414 ? 0.6509 0.6732 0.3222 -0.1227 0.0946  -0.1701 555 ALA B O     
6211 C CB    . ALA B 414 ? 0.5801 0.5642 0.2693 -0.0963 0.0960  -0.1695 555 ALA B CB    
6212 N N     . GLU B 415 ? 0.6137 0.6256 0.2921 -0.1016 0.1062  -0.1809 556 GLU B N     
6213 C CA    . GLU B 415 ? 0.6677 0.6867 0.3363 -0.1088 0.1108  -0.1898 556 GLU B CA    
6214 C C     . GLU B 415 ? 0.6547 0.6978 0.3222 -0.1159 0.1090  -0.1827 556 GLU B C     
6215 O O     . GLU B 415 ? 0.6790 0.7310 0.3375 -0.1246 0.1117  -0.1885 556 GLU B O     
6216 C CB    . GLU B 415 ? 0.6856 0.6938 0.3549 -0.0977 0.1199  -0.2026 556 GLU B CB    
6217 C CG    . GLU B 415 ? 0.7076 0.6914 0.3757 -0.0925 0.1224  -0.2119 556 GLU B CG    
6218 C CD    . GLU B 415 ? 0.8930 0.8666 0.5637 -0.0800 0.1309  -0.2235 556 GLU B CD    
6219 O OE1   . GLU B 415 ? 0.9286 0.9149 0.5978 -0.0794 0.1358  -0.2273 556 GLU B OE1   
6220 O OE2   . GLU B 415 ? 0.9144 0.8677 0.5889 -0.0712 0.1326  -0.2288 556 GLU B OE2   
6221 N N     . GLY B 416 ? 0.6894 0.7430 0.3659 -0.1127 0.1047  -0.1706 557 GLY B N     
6222 C CA    . GLY B 416 ? 0.6694 0.7453 0.3458 -0.1200 0.1020  -0.1624 557 GLY B CA    
6223 C C     . GLY B 416 ? 0.6428 0.7290 0.3140 -0.1349 0.0940  -0.1545 557 GLY B C     
6224 O O     . GLY B 416 ? 0.6597 0.7373 0.3251 -0.1413 0.0916  -0.1574 557 GLY B O     
6225 N N     . SER B 417 ? 0.6660 0.7714 0.3399 -0.1404 0.0895  -0.1438 558 SER B N     
6226 C CA    . SER B 417 ? 0.7229 0.8405 0.3933 -0.1542 0.0812  -0.1346 558 SER B CA    
6227 C C     . SER B 417 ? 0.6887 0.8013 0.3671 -0.1526 0.0736  -0.1243 558 SER B C     
6228 O O     . SER B 417 ? 0.6567 0.7660 0.3453 -0.1425 0.0729  -0.1188 558 SER B O     
6229 C CB    . SER B 417 ? 0.7033 0.8429 0.3744 -0.1604 0.0790  -0.1265 558 SER B CB    
6230 O OG    . SER B 417 ? 0.7694 0.9204 0.4440 -0.1687 0.0693  -0.1126 558 SER B OG    
6231 N N     . VAL B 418 ? 0.7074 0.8196 0.3812 -0.1628 0.0680  -0.1220 559 VAL B N     
6232 C CA    . VAL B 418 ? 0.7435 0.8539 0.4248 -0.1632 0.0600  -0.1115 559 VAL B CA    
6233 C C     . VAL B 418 ? 0.8101 0.9390 0.4989 -0.1663 0.0532  -0.0969 559 VAL B C     
6234 O O     . VAL B 418 ? 0.7737 0.9163 0.4611 -0.1691 0.0545  -0.0951 559 VAL B O     
6235 C CB    . VAL B 418 ? 0.7351 0.8416 0.4098 -0.1739 0.0560  -0.1130 559 VAL B CB    
6236 C CG1   . VAL B 418 ? 0.7132 0.8006 0.3803 -0.1713 0.0629  -0.1277 559 VAL B CG1   
6237 C CG2   . VAL B 418 ? 0.7251 0.8498 0.3928 -0.1884 0.0520  -0.1091 559 VAL B CG2   
6238 N N     . ASP B 419 ? 0.8311 0.9606 0.5283 -0.1660 0.0458  -0.0863 560 ASP B N     
6239 C CA    . ASP B 419 ? 0.9600 1.1054 0.6662 -0.1678 0.0390  -0.0720 560 ASP B CA    
6240 C C     . ASP B 419 ? 1.0540 1.2153 0.7560 -0.1822 0.0322  -0.0650 560 ASP B C     
6241 O O     . ASP B 419 ? 1.0518 1.2106 0.7492 -0.1898 0.0291  -0.0663 560 ASP B O     
6242 C CB    . ASP B 419 ? 0.9417 1.0814 0.6595 -0.1607 0.0342  -0.0638 560 ASP B CB    
6243 C CG    . ASP B 419 ? 1.0386 1.1914 0.7672 -0.1585 0.0293  -0.0508 560 ASP B CG    
6244 O OD1   . ASP B 419 ? 1.0712 1.2372 0.7982 -0.1624 0.0297  -0.0481 560 ASP B OD1   
6245 O OD2   . ASP B 419 ? 1.0247 1.1746 0.7636 -0.1530 0.0252  -0.0434 560 ASP B OD2   
6246 O O     . HOH C .   ? 0.3805 0.4582 0.7469 0.0429  0.0214  -0.0658 601 HOH A O     
6247 O O     . HOH C .   ? 0.5101 0.5407 0.8673 0.0035  -0.0516 0.0955  602 HOH A O     
6248 O O     . HOH C .   ? 0.2897 0.4310 0.3540 -0.0617 -0.0281 0.0363  603 HOH A O     
6249 O O     . HOH C .   ? 0.2586 0.3568 0.3287 0.0432  0.0185  -0.0034 604 HOH A O     
6250 O O     . HOH C .   ? 0.2484 0.2926 0.6070 0.0352  0.0079  -0.0450 605 HOH A O     
6251 O O     . HOH C .   ? 0.2904 0.3899 0.5100 -0.0142 -0.0590 0.1325  606 HOH A O     
6252 O O     . HOH C .   ? 0.2650 0.6195 0.4058 -0.0460 -0.0281 -0.0581 607 HOH A O     
6253 O O     . HOH C .   ? 0.2966 0.6606 0.3946 -0.0012 -0.0352 -0.0280 608 HOH A O     
6254 O O     . HOH C .   ? 0.1615 0.3460 0.3117 0.0124  0.0070  0.0079  609 HOH A O     
6255 O O     . HOH C .   ? 0.2101 0.4015 0.3166 0.0235  0.0072  -0.0370 610 HOH A O     
6256 O O     . HOH C .   ? 0.3686 0.5075 0.4590 -0.0367 -0.0298 0.0469  611 HOH A O     
6257 O O     . HOH C .   ? 0.3933 0.5571 0.6497 -0.0442 -0.0002 -0.0491 612 HOH A O     
6258 O O     . HOH C .   ? 0.3301 0.5496 0.4025 0.0873  0.0454  -0.0065 613 HOH A O     
6259 O O     . HOH C .   ? 0.2946 0.5386 0.3836 -0.0141 0.0230  0.0658  614 HOH A O     
6260 O O     . HOH C .   ? 0.3311 0.4976 0.5400 -0.0472 0.0368  -0.1756 615 HOH A O     
6261 O O     . HOH C .   ? 0.5120 0.8692 0.6046 0.0245  -0.0363 -0.0077 616 HOH A O     
6262 O O     . HOH C .   ? 0.4362 0.5887 0.3759 -0.1111 -0.0495 0.0506  617 HOH A O     
6263 O O     . HOH C .   ? 0.3372 0.3751 0.7070 -0.0020 0.0070  -0.0640 618 HOH A O     
6264 O O     . HOH C .   ? 0.2146 0.5779 0.3750 -0.0251 -0.0249 -0.0254 619 HOH A O     
6265 O O     . HOH C .   ? 0.2309 0.3462 0.2413 -0.0046 0.0001  0.0457  620 HOH A O     
6266 O O     . HOH C .   ? 0.2523 0.3608 0.3665 0.0018  -0.0016 0.0200  621 HOH A O     
6267 O O     . HOH C .   ? 0.1912 0.2524 0.2031 0.0219  0.0164  0.0110  622 HOH A O     
6268 O O     . HOH C .   ? 0.1660 0.2839 0.3612 -0.0167 -0.0444 0.1222  623 HOH A O     
6269 O O     . HOH C .   ? 0.2930 0.3935 0.4113 0.0148  0.0163  -0.0033 624 HOH A O     
6270 O O     . HOH C .   ? 0.5190 0.5242 0.9683 0.0070  0.0223  -0.1142 625 HOH A O     
6271 O O     . HOH C .   ? 0.4393 0.4733 0.8060 -0.0054 -0.0240 0.0290  626 HOH A O     
6272 O O     . HOH C .   ? 0.3641 0.4597 0.3167 -0.0343 -0.0041 0.0312  627 HOH A O     
6273 O O     . HOH C .   ? 0.1351 0.2645 0.1885 0.0565  0.0146  0.0023  628 HOH A O     
6274 O O     . HOH C .   ? 0.4619 0.6723 0.4637 -0.0287 0.0178  0.0720  629 HOH A O     
6275 O O     . HOH C .   ? 0.2893 0.4722 0.2503 0.0233  0.0607  -0.0019 630 HOH A O     
6276 O O     . HOH C .   ? 0.5738 0.7764 0.6243 -0.0964 -0.0748 0.0837  631 HOH A O     
6277 O O     . HOH C .   ? 0.5166 0.6961 0.4426 -0.0421 0.0180  0.0482  632 HOH A O     
6278 O O     . HOH C .   ? 0.4432 0.4923 0.7953 -0.0155 0.0080  -0.0718 633 HOH A O     
6279 O O     . HOH C .   ? 0.2942 0.3944 0.3128 0.0307  0.0191  0.0210  634 HOH A O     
6280 O O     . HOH C .   ? 0.2102 0.3213 0.4093 -0.0017 0.0489  -0.1342 635 HOH A O     
6281 O O     . HOH C .   ? 0.1452 0.2588 0.2063 0.0473  0.0174  0.0074  636 HOH A O     
6282 O O     . HOH C .   ? 0.1792 0.2737 0.3525 0.0232  0.0152  -0.0318 637 HOH A O     
6283 O O     . HOH C .   ? 0.2525 0.3466 0.3163 0.0201  0.0047  0.0280  638 HOH A O     
6284 O O     . HOH C .   ? 0.2670 0.4857 0.3351 -0.0391 0.0033  0.1017  639 HOH A O     
6285 O O     . HOH C .   ? 0.2257 0.4082 0.4297 -0.0093 0.0016  -0.0038 640 HOH A O     
6286 O O     . HOH C .   ? 0.3623 0.5912 0.3999 0.0334  0.0485  0.0160  641 HOH A O     
6287 O O     . HOH C .   ? 0.3390 0.6224 0.5201 -0.0501 0.0120  0.0470  642 HOH A O     
6288 O O     . HOH C .   ? 0.2769 0.4376 0.3637 -0.0441 -0.0539 0.0848  643 HOH A O     
6289 O O     . HOH C .   ? 0.1689 0.2551 0.4054 -0.0026 -0.0398 0.0984  644 HOH A O     
6290 O O     . HOH C .   ? 0.3134 0.5464 0.4885 -0.0830 0.0136  -0.1703 645 HOH A O     
6291 O O     . HOH C .   ? 0.3223 0.5632 0.3795 0.0227  0.0412  0.0279  646 HOH A O     
6292 O O     . HOH C .   ? 0.3052 0.4664 0.3489 0.0951  0.0426  -0.0080 647 HOH A O     
6293 O O     . HOH C .   ? 0.4180 0.5759 0.4914 -0.0372 -0.0474 0.1140  648 HOH A O     
6294 O O     . HOH C .   ? 0.6082 0.7793 0.5794 -0.1286 -0.0592 0.0485  649 HOH A O     
6295 O O     . HOH C .   ? 0.2975 0.3579 0.2907 0.0262  0.0200  0.0103  650 HOH A O     
6296 O O     . HOH C .   ? 0.1767 0.3395 0.2367 0.0517  0.0078  -0.0108 651 HOH A O     
6297 O O     . HOH C .   ? 0.3456 0.4042 0.6387 0.0086  -0.0482 0.0935  652 HOH A O     
6298 O O     . HOH C .   ? 0.3387 0.5737 0.5433 -0.0958 -0.0007 -0.1397 653 HOH A O     
6299 O O     . HOH C .   ? 0.2970 0.4633 0.5222 -0.0580 0.0276  -0.1685 654 HOH A O     
6300 O O     . HOH C .   ? 0.2867 0.3222 0.6445 0.0141  0.0218  -0.0925 655 HOH A O     
6301 O O     . HOH C .   ? 0.2299 0.3291 0.2330 0.0128  0.0127  0.0283  656 HOH A O     
6302 O O     . HOH C .   ? 0.2041 0.3824 0.4414 -0.0492 -0.0079 0.0444  657 HOH A O     
6303 O O     . HOH C .   ? 0.2612 0.4142 0.4959 -0.0206 -0.0036 0.0107  658 HOH A O     
6304 O O     . HOH C .   ? 0.4683 0.6221 0.3772 -0.0365 0.0226  0.0295  659 HOH A O     
6305 O O     . HOH C .   ? 0.2946 0.4291 0.5498 -0.0469 0.0314  -0.1642 660 HOH A O     
6306 O O     . HOH C .   ? 0.2586 0.5727 0.3545 0.0419  -0.0239 -0.0015 661 HOH A O     
6307 O O     . HOH C .   ? 0.1735 0.4269 0.2748 0.0510  -0.0026 0.0030  662 HOH A O     
6308 O O     . HOH C .   ? 0.2327 0.4084 0.4620 -0.0247 -0.0018 0.0004  663 HOH A O     
6309 O O     . HOH C .   ? 0.1850 0.4695 0.2987 0.0393  -0.0094 -0.0008 664 HOH A O     
6310 O O     . HOH C .   ? 0.2326 0.5454 0.2121 -0.0477 -0.0041 -0.0968 665 HOH A O     
6311 O O     . HOH C .   ? 0.2526 0.5006 0.3384 0.0386  0.0351  0.0160  666 HOH A O     
6312 O O     . HOH C .   ? 0.2388 0.4293 0.2514 0.0219  0.0397  0.0274  667 HOH A O     
6313 O O     . HOH C .   ? 0.2105 0.3269 0.3864 0.0138  0.0215  -0.0630 668 HOH A O     
6314 O O     . HOH C .   ? 0.2646 0.5577 0.4107 -0.0045 0.0203  0.0261  669 HOH A O     
6315 O O     . HOH C .   ? 0.2258 0.3259 0.2725 0.0523  0.0188  0.0016  670 HOH A O     
6316 O O     . HOH C .   ? 0.2032 0.3816 0.4298 -0.0375 0.0064  -0.0828 671 HOH A O     
6317 O O     . HOH C .   ? 0.2737 0.4931 0.4549 -0.0426 0.0019  0.0660  672 HOH A O     
6318 O O     . HOH C .   ? 0.2411 0.3174 0.5346 0.0004  0.0434  -0.1430 673 HOH A O     
6319 O O     . HOH C .   ? 0.1975 0.4965 0.3301 0.0415  0.0104  0.0085  674 HOH A O     
6320 O O     . HOH C .   ? 0.1399 0.2495 0.3232 0.0184  0.0064  -0.0098 675 HOH A O     
6321 O O     . HOH C .   ? 0.2827 0.3855 0.5331 -0.0130 -0.0239 0.0723  676 HOH A O     
6322 O O     . HOH C .   ? 0.2511 0.3798 0.4043 -0.0141 -0.0494 0.1101  677 HOH A O     
6323 O O     . HOH C .   ? 0.3052 0.4798 0.4523 -0.0394 -0.0198 0.1186  678 HOH A O     
6324 O O     . HOH C .   ? 0.2444 0.5418 0.4324 -0.0473 0.0112  0.0356  679 HOH A O     
6325 O O     . HOH C .   ? 0.2464 0.3462 0.2622 0.0730  0.0278  0.0033  680 HOH A O     
6326 O O     . HOH C .   ? 0.1786 0.3334 0.3045 0.0272  0.0095  -0.0033 681 HOH A O     
6327 O O     . HOH C .   ? 0.3694 0.4753 0.5775 -0.0169 -0.0549 0.1326  682 HOH A O     
6328 O O     . HOH C .   ? 0.1360 0.2930 0.3088 -0.0017 -0.0016 0.0456  683 HOH A O     
6329 O O     . HOH C .   ? 0.1600 0.2643 0.3390 0.0124  0.0317  -0.0846 684 HOH A O     
6330 O O     . HOH C .   ? 0.1608 0.4191 0.2238 0.0349  -0.0108 -0.0250 685 HOH A O     
6331 O O     . HOH C .   ? 0.2129 0.4442 0.4590 -0.0637 -0.0049 0.0056  686 HOH A O     
6332 O O     . HOH C .   ? 0.1675 0.2967 0.2929 0.0293  0.0090  0.0071  687 HOH A O     
6333 O O     . HOH C .   ? 0.2361 0.5674 0.3955 -0.0523 -0.0225 -0.0610 688 HOH A O     
6334 O O     . HOH C .   ? 0.4299 0.4608 0.8355 0.0206  0.0302  -0.1143 689 HOH A O     
6335 O O     . HOH C .   ? 0.1267 0.3147 0.1984 0.0667  0.0147  0.0065  690 HOH A O     
6336 O O     . HOH C .   ? 0.1632 0.3339 0.3578 -0.0163 0.0147  -0.0888 691 HOH A O     
6337 O O     . HOH C .   ? 0.2805 0.4526 0.3044 -0.0201 0.0017  0.0751  692 HOH A O     
6338 O O     . HOH C .   ? 0.4306 0.6926 0.5298 0.1027  -0.0054 0.0188  693 HOH A O     
6339 O O     . HOH C .   ? 0.3530 0.4705 0.6066 -0.0227 -0.0158 0.0522  694 HOH A O     
6340 O O     . HOH C .   ? 0.2402 0.2819 0.1796 0.0672  0.0530  -0.0219 695 HOH A O     
6341 O O     . HOH C .   ? 0.7391 0.8669 0.5706 -0.0375 0.0642  -0.0391 696 HOH A O     
6342 O O     . HOH C .   ? 0.1319 0.4409 0.2718 0.0191  -0.0085 -0.0029 697 HOH A O     
6343 O O     . HOH C .   ? 0.2688 0.4951 0.3241 -0.0044 0.0272  0.0584  698 HOH A O     
6344 O O     . HOH C .   ? 0.2650 0.3455 0.3025 0.0175  0.0086  0.0211  699 HOH A O     
6345 O O     . HOH C .   ? 0.3055 0.5115 0.3490 0.0256  0.0056  -0.0409 700 HOH A O     
6346 O O     . HOH C .   ? 0.3127 0.6144 0.4494 0.0343  0.0041  0.0065  701 HOH A O     
6347 O O     . HOH C .   ? 0.3300 0.4196 0.5841 -0.0206 -0.0593 0.1427  702 HOH A O     
6348 O O     . HOH C .   ? 0.3463 0.6915 0.3261 -0.0942 0.0080  -0.1469 703 HOH A O     
6349 O O     . HOH C .   ? 0.2506 0.3920 0.4861 -0.0337 0.0329  -0.1523 704 HOH A O     
6350 O O     . HOH C .   ? 0.1743 0.3624 0.3856 -0.0170 0.0012  -0.0203 705 HOH A O     
6351 O O     . HOH C .   ? 0.2754 0.3504 0.6030 -0.0411 0.0184  -0.1227 706 HOH A O     
6352 O O     . HOH C .   ? 0.3616 0.5805 0.4428 -0.0379 0.0463  -0.1580 707 HOH A O     
6353 O O     . HOH C .   ? 0.3052 0.3889 0.3058 0.0162  0.0140  0.0216  708 HOH A O     
6354 O O     . HOH C .   ? 0.2466 0.4160 0.4848 -0.0286 -0.0010 -0.0200 709 HOH A O     
6355 O O     . HOH C .   ? 0.2824 0.5449 0.3483 -0.0425 0.0148  -0.1283 710 HOH A O     
6356 O O     . HOH C .   ? 0.1464 0.3876 0.2510 0.0396  -0.0019 -0.0026 711 HOH A O     
6357 O O     . HOH C .   ? 0.2599 0.5791 0.4120 -0.0789 -0.0185 -0.1035 712 HOH A O     
6358 O O     . HOH C .   ? 0.2414 0.4539 0.2860 -0.0123 0.0204  0.0666  713 HOH A O     
6359 O O     . HOH C .   ? 0.3281 0.5187 0.3968 0.0963  0.0263  0.0024  714 HOH A O     
6360 O O     . HOH C .   ? 0.5247 0.6545 0.6981 -0.0305 -0.0592 0.1482  715 HOH A O     
6361 O O     . HOH C .   ? 0.1472 0.2479 0.2251 0.0034  -0.0076 0.0366  716 HOH A O     
6362 O O     . HOH C .   ? 0.5282 0.5012 1.0325 0.0173  -0.0258 -0.0024 717 HOH A O     
6363 O O     . HOH C .   ? 0.4245 0.5748 0.4700 0.0107  0.0391  -0.0691 718 HOH A O     
6364 O O     . HOH C .   ? 0.4431 0.5856 0.2953 -0.0123 0.0853  -0.0526 719 HOH A O     
6365 O O     . HOH C .   ? 0.1759 0.4229 0.2669 0.0578  0.0323  0.0074  720 HOH A O     
6366 O O     . HOH C .   ? 0.2883 0.5742 0.3060 0.0457  -0.0315 0.0014  721 HOH A O     
6367 O O     . HOH C .   ? 0.2524 0.5033 0.3443 -0.0072 0.0269  0.0549  722 HOH A O     
6368 O O     . HOH C .   ? 0.2237 0.3333 0.3088 0.0367  0.0211  -0.0220 723 HOH A O     
6369 O O     . HOH C .   ? 0.4566 0.6012 0.4555 -0.0262 -0.0090 0.0674  724 HOH A O     
6370 O O     . HOH C .   ? 0.2162 0.4662 0.4512 -0.0666 -0.0090 -0.0298 725 HOH A O     
6371 O O     . HOH C .   ? 0.2986 0.5221 0.3784 -0.0335 0.0341  -0.1400 726 HOH A O     
6372 O O     . HOH C .   ? 0.2002 0.4480 0.2625 0.0578  -0.0131 -0.0016 727 HOH A O     
6373 O O     . HOH C .   ? 0.2280 0.4814 0.3326 0.0628  0.0117  0.0077  728 HOH A O     
6374 O O     . HOH C .   ? 0.3040 0.5051 0.4464 -0.0272 -0.0006 0.0869  729 HOH A O     
6375 O O     . HOH C .   ? 0.2711 0.3538 0.5581 -0.0046 -0.0113 0.0170  730 HOH A O     
6376 O O     . HOH C .   ? 0.3774 0.4125 0.7328 0.0000  -0.0443 0.0836  731 HOH A O     
6377 O O     . HOH C .   ? 0.2471 0.3346 0.3153 0.0223  0.0075  0.0200  732 HOH A O     
6378 O O     . HOH C .   ? 0.3675 0.5547 0.4035 -0.0352 -0.0074 0.0977  733 HOH A O     
6379 O O     . HOH C .   ? 0.4505 0.7193 0.5814 -0.1020 0.0148  -0.1928 734 HOH A O     
6380 O O     . HOH C .   ? 0.4315 0.6003 0.4908 -0.0562 -0.0600 0.0962  735 HOH A O     
6381 O O     . HOH C .   ? 0.4767 0.5548 0.9072 0.0545  0.0125  -0.0559 736 HOH A O     
6382 O O     . HOH C .   ? 0.4432 0.8057 0.4860 0.0271  -0.0495 0.0021  737 HOH A O     
6383 O O     . HOH C .   ? 0.2849 0.5147 0.3723 0.0795  0.0270  0.0039  738 HOH A O     
6384 O O     . HOH C .   ? 0.3596 0.4637 0.6594 -0.0570 0.0241  -0.1551 739 HOH A O     
6385 O O     . HOH C .   ? 0.5847 0.6603 0.4391 -0.0346 0.0360  -0.0187 740 HOH A O     
6386 O O     . HOH C .   ? 0.3059 0.5816 0.4076 0.0356  0.0351  0.0152  741 HOH A O     
6387 O O     . HOH C .   ? 0.3994 0.5153 0.4198 -0.0809 -0.0171 0.0196  742 HOH A O     
6388 O O     . HOH C .   ? 0.4445 0.5969 0.4565 -0.0433 -0.0317 0.0871  743 HOH A O     
6389 O O     . HOH C .   ? 0.4289 0.6962 0.4967 0.1014  -0.0287 0.0338  744 HOH A O     
6390 O O     . HOH C .   ? 0.3657 0.4556 0.3929 0.0255  0.0136  0.0222  745 HOH A O     
6391 O O     . HOH C .   ? 0.2577 0.4644 0.4138 -0.0232 0.0039  0.0664  746 HOH A O     
6392 O O     . HOH C .   ? 0.3401 0.6164 0.4412 0.0680  -0.0079 0.0098  747 HOH A O     
6393 O O     . HOH C .   ? 0.4253 0.7850 0.4466 -0.0888 -0.0099 -0.1385 748 HOH A O     
6394 O O     . HOH C .   ? 0.3664 0.5361 0.4465 -0.0081 0.0436  -0.1103 749 HOH A O     
6395 O O     . HOH C .   ? 0.3937 0.5281 0.5951 -0.0387 -0.0415 0.1381  750 HOH A O     
6396 O O     . HOH C .   ? 0.3185 0.5562 0.3366 -0.0182 0.0171  -0.0909 751 HOH A O     
6397 O O     . HOH C .   ? 0.2710 0.4368 0.4139 0.0198  0.0082  -0.0140 752 HOH A O     
6398 O O     . HOH C .   ? 0.1982 0.3014 0.2634 0.0454  0.0172  0.0020  753 HOH A O     
6399 O O     . HOH C .   ? 0.1839 0.3441 0.3602 -0.0114 -0.0060 0.0644  754 HOH A O     
6400 O O     . HOH C .   ? 0.5087 0.6018 0.8292 -0.0582 0.0030  -0.0804 755 HOH A O     
6401 O O     . HOH C .   ? 0.3268 0.3707 0.7379 0.0436  0.0048  -0.0448 756 HOH A O     
6402 O O     . HOH C .   ? 0.3711 0.4462 0.3887 0.0495  0.0237  0.0061  757 HOH A O     
6403 O O     . HOH C .   ? 0.3261 0.6825 0.3651 0.0106  -0.0424 -0.0190 758 HOH A O     
6404 O O     . HOH C .   ? 0.4326 0.6030 0.5763 -0.0447 -0.0281 0.1332  759 HOH A O     
6405 O O     . HOH C .   ? 0.4363 0.6614 0.5827 -0.0323 0.0069  0.0752  760 HOH A O     
6406 O O     . HOH C .   ? 0.2822 0.3554 0.6001 -0.0169 0.0055  -0.0578 761 HOH A O     
6407 O O     . HOH C .   ? 0.2648 0.3692 0.4456 0.0186  0.0162  -0.0421 762 HOH A O     
6408 O O     . HOH C .   ? 0.3605 0.4353 0.2318 0.0288  0.0871  -0.0640 763 HOH A O     
6409 O O     . HOH C .   ? 0.3229 0.4566 0.5962 -0.0395 -0.0006 -0.0415 764 HOH A O     
6410 O O     . HOH C .   ? 0.3936 0.5924 0.5451 -0.0534 0.0571  -0.2077 765 HOH A O     
6411 O O     . HOH C .   ? 0.1665 0.3956 0.2491 0.0500  0.0311  0.0111  766 HOH A O     
6412 O O     . HOH C .   ? 0.2979 0.4674 0.3825 0.0270  0.0166  -0.0467 767 HOH A O     
6413 O O     . HOH C .   ? 0.2929 0.5022 0.3390 0.0560  0.0464  0.0043  768 HOH A O     
6414 O O     . HOH C .   ? 0.2873 0.3560 0.5883 0.0197  0.0394  -0.1108 769 HOH A O     
6415 O O     . HOH C .   ? 0.2827 0.5686 0.4029 0.0515  0.0008  0.0067  770 HOH A O     
6416 O O     . HOH C .   ? 0.4939 0.7621 0.6402 -0.1003 0.0071  -0.1767 771 HOH A O     
6417 O O     . HOH C .   ? 0.4044 0.7365 0.5485 -0.0192 0.0301  0.0362  772 HOH A O     
6418 O O     . HOH C .   ? 0.3550 0.3557 0.7898 0.0020  0.0123  -0.0906 773 HOH A O     
6419 O O     . HOH C .   ? 0.4394 0.6798 0.5205 0.1061  -0.0092 0.0226  774 HOH A O     
6420 O O     . HOH C .   ? 0.2999 0.4404 0.4093 0.0285  0.0160  -0.0332 775 HOH A O     
6421 O O     . HOH C .   ? 0.3843 0.7026 0.3745 -0.0027 -0.0303 -0.0342 776 HOH A O     
6422 O O     . HOH C .   ? 0.2530 0.6083 0.3983 -0.0064 -0.0243 -0.0189 777 HOH A O     
6423 O O     . HOH C .   ? 0.3121 0.5159 0.5121 -0.0717 0.0192  -0.1675 778 HOH A O     
6424 O O     . HOH C .   ? 0.2325 0.3514 0.3880 0.0096  -0.0062 0.0240  779 HOH A O     
6425 O O     . HOH C .   ? 0.3042 0.3698 0.6076 0.0289  -0.0276 0.0399  780 HOH A O     
6426 O O     . HOH C .   ? 0.3517 0.6304 0.4667 0.0697  0.0215  0.0066  781 HOH A O     
6427 O O     . HOH C .   ? 0.2477 0.4944 0.3421 0.0674  0.0289  0.0054  782 HOH A O     
6428 O O     . HOH C .   ? 0.3341 0.4198 0.3621 0.0423  0.0206  0.0116  783 HOH A O     
6429 O O     . HOH C .   ? 0.5916 0.8116 0.5229 -0.0415 0.0364  0.0420  784 HOH A O     
6430 O O     . HOH C .   ? 0.4152 0.5896 0.4484 0.0856  0.0571  -0.0163 785 HOH A O     
6431 O O     . HOH C .   ? 0.2125 0.3473 0.2757 -0.0495 -0.0292 0.0425  786 HOH A O     
6432 O O     . HOH C .   ? 0.3218 0.4722 0.4333 -0.0266 -0.0506 0.0930  787 HOH A O     
6433 O O     . HOH C .   ? 0.2881 0.3511 0.2961 0.0534  0.0252  0.0024  788 HOH A O     
6434 O O     . HOH C .   ? 0.1639 0.2597 0.2400 0.0410  0.0183  -0.0009 789 HOH A O     
6435 O O     . HOH C .   ? 0.5514 0.8919 0.6075 -0.1010 -0.0018 -0.1643 790 HOH A O     
6436 O O     . HOH C .   ? 0.3458 0.4285 0.3084 0.0138  0.0237  0.0127  791 HOH A O     
6437 O O     . HOH C .   ? 0.4886 0.7752 0.6083 -0.0215 0.0275  0.0524  792 HOH A O     
6438 O O     . HOH C .   ? 0.3291 0.4799 0.3861 -0.0829 -0.0290 0.0306  793 HOH A O     
6439 O O     . HOH C .   ? 0.3501 0.5289 0.4185 -0.0446 -0.0295 0.1261  794 HOH A O     
6440 O O     . HOH C .   ? 0.4357 0.5537 0.6211 0.0193  0.0094  -0.0052 795 HOH A O     
6441 O O     . HOH C .   ? 0.4045 0.5280 0.5156 0.0026  0.0546  -0.0691 796 HOH A O     
6442 O O     . HOH C .   ? 0.4830 0.8197 0.5307 -0.0870 -0.0026 -0.1516 797 HOH A O     
6443 O O     . HOH C .   ? 0.1585 0.2509 0.2358 0.0139  0.0011  0.0262  798 HOH A O     
6444 O O     . HOH C .   ? 0.2550 0.3184 0.5837 -0.0034 0.0092  -0.0626 799 HOH A O     
6445 O O     . HOH C .   ? 0.3482 0.4826 0.6200 -0.0470 0.0086  -0.0938 800 HOH A O     
6446 O O     . HOH C .   ? 0.3072 0.6460 0.4998 -0.0976 -0.0263 -0.0780 801 HOH A O     
6447 O O     . HOH C .   ? 0.2644 0.4006 0.4024 -0.0154 -0.0442 0.1094  802 HOH A O     
6448 O O     . HOH C .   ? 0.3834 0.4912 0.5727 0.0176  0.0429  -0.0743 803 HOH A O     
6449 O O     . HOH C .   ? 0.3521 0.4902 0.5168 -0.0089 -0.0462 0.0814  804 HOH A O     
6450 O O     . HOH C .   ? 0.3015 0.5577 0.4055 0.0771  0.0167  0.0071  805 HOH A O     
6451 O O     . HOH C .   ? 0.2054 0.3781 0.3385 0.0225  0.0079  -0.0024 806 HOH A O     
6452 O O     . HOH C .   ? 0.3122 0.5295 0.5702 -0.0699 -0.0074 -0.0093 807 HOH A O     
6453 O O     . HOH C .   ? 0.2761 0.3787 0.5306 -0.0105 -0.0175 0.0519  808 HOH A O     
6454 O O     . HOH C .   ? 0.4659 0.6355 0.6616 -0.0406 -0.0139 0.0939  809 HOH A O     
6455 O O     . HOH C .   ? 0.5339 0.6476 0.6991 0.0121  0.0484  -0.0806 810 HOH A O     
6456 O O     . HOH C .   ? 0.2341 0.5547 0.3739 0.0469  0.0140  0.0089  811 HOH A O     
6457 O O     . HOH C .   ? 0.2081 0.3407 0.4609 0.0265  0.0078  -0.0137 812 HOH A O     
6458 O O     . HOH C .   ? 0.5351 0.8146 0.5588 -0.0634 0.0271  -0.1555 813 HOH A O     
6459 O O     . HOH C .   ? 0.3116 0.4838 0.3829 0.0211  0.0196  -0.0559 814 HOH A O     
6460 O O     . HOH C .   ? 0.4004 0.7749 0.5783 -0.0134 -0.0147 -0.0053 815 HOH A O     
6461 O O     . HOH C .   ? 0.2517 0.4023 0.3414 0.0318  0.0159  -0.0349 816 HOH A O     
6462 O O     . HOH C .   ? 0.3247 0.4810 0.5055 -0.0293 -0.0186 0.1005  817 HOH A O     
6463 O O     . HOH C .   ? 0.3818 0.5396 0.3972 -0.0181 -0.0007 0.0694  818 HOH A O     
6464 O O     . HOH C .   ? 0.1298 0.2470 0.3030 -0.0009 0.0507  -0.1259 819 HOH A O     
6465 O O     . HOH C .   ? 0.3441 0.5525 0.3426 0.0197  0.0498  0.0200  820 HOH A O     
6466 O O     . HOH C .   ? 0.2134 0.5320 0.3827 -0.0116 -0.0084 -0.0074 821 HOH A O     
6467 O O     . HOH C .   ? 0.4776 0.8655 0.5840 -0.0584 -0.0367 -0.0729 822 HOH A O     
6468 O O     . HOH C .   ? 0.3659 0.5099 0.3664 -0.0062 0.0096  0.0500  823 HOH A O     
6469 O O     . HOH C .   ? 0.5176 0.8456 0.6272 0.0788  -0.0263 0.0209  824 HOH A O     
6470 O O     . HOH C .   ? 0.4420 0.5546 0.7397 -0.0578 0.0114  -0.1139 825 HOH A O     
6471 O O     . HOH C .   ? 0.3183 0.6097 0.4338 0.0512  -0.0071 0.0054  826 HOH A O     
6472 O O     . HOH C .   ? 0.2974 0.4306 0.5255 0.0211  0.0052  -0.0059 827 HOH A O     
6473 O O     . HOH C .   ? 0.4388 0.5116 0.7284 0.0085  0.0437  -0.1315 828 HOH A O     
6474 O O     . HOH C .   ? 0.3680 0.6063 0.4627 0.0905  0.0145  0.0080  829 HOH A O     
6475 O O     . HOH C .   ? 0.5023 0.6435 0.3517 -0.0283 0.0666  -0.0333 830 HOH A O     
6476 O O     . HOH C .   ? 0.4588 0.6321 0.7154 -0.0606 0.0016  -0.0832 831 HOH A O     
6477 O O     . HOH C .   ? 0.4637 0.5601 0.7555 -0.0142 0.0593  -0.1855 832 HOH A O     
6478 O O     . HOH C .   ? 0.4557 0.5250 0.3980 0.0035  0.0229  0.0078  833 HOH A O     
6479 O O     . HOH C .   ? 0.3290 0.4927 0.5806 -0.0446 0.0030  -0.0698 834 HOH A O     
6480 O O     . HOH C .   ? 0.3136 0.5930 0.4329 0.0533  0.0071  0.0076  835 HOH A O     
6481 O O     . HOH C .   ? 0.5251 0.6786 0.6904 -0.0445 -0.0404 0.1456  836 HOH A O     
6482 O O     . HOH C .   ? 0.4974 0.6557 0.6920 -0.0316 -0.0161 0.0928  837 HOH A O     
6483 O O     . HOH C .   ? 0.4030 0.5100 0.6236 -0.0228 -0.0560 0.1418  838 HOH A O     
6484 O O     . HOH C .   ? 0.5193 0.9135 0.6100 0.0090  -0.0465 -0.0114 839 HOH A O     
6485 O O     . HOH C .   ? 0.3148 0.5150 0.3464 0.0607  0.0539  -0.0037 840 HOH A O     
6486 O O     . HOH C .   ? 0.2727 0.5953 0.4061 0.0191  -0.0158 -0.0068 841 HOH A O     
6487 O O     . HOH C .   ? 0.4841 0.6498 0.5808 -0.0411 -0.0621 0.1099  842 HOH A O     
6488 O O     . HOH C .   ? 0.4896 0.6561 0.5426 0.0186  0.0241  -0.0584 843 HOH A O     
6489 O O     . HOH C .   ? 0.3583 0.4489 0.6740 -0.0477 0.0553  -0.2208 844 HOH A O     
6490 O O     . HOH C .   ? 0.3533 0.4098 0.2969 -0.0010 0.0191  0.0073  845 HOH A O     
6491 O O     . HOH C .   ? 0.3644 0.4439 0.6705 -0.0037 0.0517  -0.1638 846 HOH A O     
6492 O O     . HOH C .   ? 0.4170 0.5857 0.4738 0.1008  0.0296  0.0002  847 HOH A O     
6493 O O     . HOH C .   ? 0.3521 0.5594 0.3308 0.0115  0.0527  0.0172  848 HOH A O     
6494 O O     . HOH C .   ? 0.4568 0.6634 0.4502 0.0361  0.0637  -0.0037 849 HOH A O     
6495 O O     . HOH C .   ? 0.3009 0.4831 0.4666 -0.0232 -0.0045 0.0781  850 HOH A O     
6496 O O     . HOH C .   ? 0.4838 0.7428 0.5524 -0.0603 0.0302  -0.1667 851 HOH A O     
6497 O O     . HOH C .   ? 0.5404 0.9563 0.6264 -0.0027 -0.0528 -0.0149 852 HOH A O     
6498 O O     . HOH C .   ? 0.4227 0.5983 0.5921 -0.0332 -0.0124 0.0982  853 HOH A O     
6499 O O     . HOH C .   ? 0.2739 0.6544 0.4480 -0.0383 -0.0266 -0.0262 854 HOH A O     
6500 O O     . HOH C .   ? 0.6029 0.8353 0.5372 -0.0379 0.0452  0.0344  855 HOH A O     
6501 O O     . HOH C .   ? 0.4948 0.7889 0.5148 0.0593  -0.0398 0.0188  856 HOH A O     
6502 O O     . HOH C .   ? 0.3437 0.6623 0.5098 -0.0031 -0.0031 0.0003  857 HOH A O     
6503 O O     . HOH C .   ? 0.4307 0.5959 0.6853 -0.0476 -0.0083 0.0253  858 HOH A O     
6504 O O     . HOH C .   ? 0.3635 0.4795 0.6429 -0.0502 0.0408  -0.1916 859 HOH A O     
6505 O O     . HOH C .   ? 0.2917 0.4504 0.5381 -0.0464 0.0102  -0.1032 860 HOH A O     
6506 O O     . HOH C .   ? 0.3791 0.6287 0.4359 -0.0155 0.0299  0.0649  861 HOH A O     
6507 O O     . HOH C .   ? 0.5062 0.7028 0.4842 0.0385  0.0717  -0.0157 862 HOH A O     
6508 O O     . HOH C .   ? 0.6110 0.7651 0.6323 -0.0239 -0.0104 0.0778  863 HOH A O     
6509 O O     . HOH C .   ? 0.5405 0.7076 0.5011 -0.0885 -0.0512 0.0779  864 HOH A O     
6510 O O     . HOH C .   ? 0.4067 0.5334 0.4608 -0.0627 -0.0169 0.0242  865 HOH A O     
6511 O O     . HOH C .   ? 0.3453 0.5904 0.4152 -0.0449 0.0284  -0.1463 866 HOH A O     
6512 O O     . HOH C .   ? 0.5981 0.7758 0.5600 -0.1021 -0.0607 0.0790  867 HOH A O     
6513 O O     . HOH C .   ? 0.2826 0.4423 0.5211 -0.0407 -0.0100 0.0494  868 HOH A O     
6514 O O     . HOH C .   ? 0.4053 0.7053 0.5157 0.0719  -0.0121 0.0128  869 HOH A O     
6515 O O     . HOH C .   ? 0.5455 0.6656 0.8363 -0.0664 0.0159  -0.1392 870 HOH A O     
6516 O O     . HOH C .   ? 0.4750 0.5594 0.7938 -0.0491 0.0421  -0.1959 871 HOH A O     
6517 O O     . HOH C .   ? 0.3007 0.6285 0.4118 0.0346  -0.0233 -0.0028 872 HOH A O     
6518 O O     . HOH C .   ? 0.3330 0.4747 0.5850 -0.0312 -0.0088 0.0276  873 HOH A O     
6519 O O     . HOH C .   ? 0.4058 0.6338 0.6614 -0.0766 -0.0088 -0.0244 874 HOH A O     
6520 O O     . HOH C .   ? 0.3114 0.6659 0.4504 0.0129  -0.0228 -0.0078 875 HOH A O     
6521 O O     . HOH C .   ? 0.3478 0.6834 0.3339 -0.1037 0.0224  -0.1691 876 HOH A O     
6522 O O     . HOH C .   ? 0.4742 0.5466 0.8082 -0.0517 0.0266  -0.1583 877 HOH A O     
6523 O O     . HOH C .   ? 0.4709 0.6776 0.4732 -0.0391 0.0071  0.0858  878 HOH A O     
6524 O O     . HOH C .   ? 0.5141 0.6551 0.7656 -0.0500 -0.0177 0.0723  879 HOH A O     
6525 O O     . HOH C .   ? 0.4338 0.7910 0.5553 0.0626  -0.0295 0.0159  880 HOH A O     
6526 O O     . HOH C .   ? 0.2203 0.5319 0.3388 0.0336  -0.0162 -0.0028 881 HOH A O     
6527 O O     . HOH C .   ? 0.4683 0.6422 0.7016 -0.0700 0.0198  -0.1624 882 HOH A O     
6528 O O     . HOH C .   ? 0.4512 0.8119 0.5718 0.0276  -0.0300 -0.0024 883 HOH A O     
6529 O O     . HOH C .   ? 0.4021 0.7472 0.3721 -0.1162 0.0283  -0.1751 884 HOH A O     
6530 O O     . HOH D .   ? 0.4277 0.5364 0.4771 0.1442  0.0500  -0.0209 601 HOH B O     
6531 O O     . HOH D .   ? 0.4777 0.6448 0.4451 0.0617  0.0954  -0.0509 602 HOH B O     
6532 O O     . HOH D .   ? 0.6224 0.4359 0.4113 -0.1601 0.0395  -0.0229 603 HOH B O     
6533 O O     . HOH D .   ? 0.4705 0.4605 0.3693 0.0790  0.1246  -0.1350 604 HOH B O     
6534 O O     . HOH D .   ? 0.6001 0.6607 0.5514 0.1068  -0.0026 0.0429  605 HOH B O     
6535 O O     . HOH D .   ? 0.7606 0.4878 0.5399 -0.0510 0.0467  -0.0169 606 HOH B O     
6536 O O     . HOH D .   ? 0.6488 0.6368 0.4206 0.0233  0.1335  -0.1741 607 HOH B O     
6537 O O     . HOH D .   ? 0.3848 0.4212 0.3512 0.0308  0.0267  0.0016  608 HOH B O     
6538 O O     . HOH D .   ? 0.5780 0.2954 0.4522 0.1329  0.0483  -0.0108 609 HOH B O     
6539 O O     . HOH D .   ? 0.4046 0.2601 0.2739 0.0903  0.0682  -0.0529 610 HOH B O     
6540 O O     . HOH D .   ? 0.3895 0.4288 0.3395 -0.1125 0.0494  -0.0099 611 HOH B O     
6541 O O     . HOH D .   ? 0.7345 0.5459 0.5007 -0.1749 0.0327  -0.0510 612 HOH B O     
6542 O O     . HOH D .   ? 0.6707 0.5259 0.3633 -0.1035 0.0804  -0.1663 613 HOH B O     
6543 O O     . HOH D .   ? 0.2605 0.3791 0.2668 0.1143  0.0020  0.0261  614 HOH B O     
6544 O O     . HOH D .   ? 0.4179 0.4540 0.4152 0.1452  0.0198  0.0171  615 HOH B O     
6545 O O     . HOH D .   ? 0.5287 0.3846 0.3489 -0.0219 0.0365  0.0385  616 HOH B O     
6546 O O     . HOH D .   ? 0.3981 0.3783 0.3744 0.1470  0.0363  -0.0013 617 HOH B O     
6547 O O     . HOH D .   ? 0.6359 0.7887 0.5208 0.0312  0.1244  -0.0881 618 HOH B O     
6548 O O     . HOH D .   ? 0.4967 0.5176 0.3241 0.0548  0.1294  -0.1319 619 HOH B O     
6549 O O     . HOH D .   ? 0.5362 0.4371 0.3860 0.0407  0.0641  -0.0578 620 HOH B O     
6550 O O     . HOH D .   ? 0.4313 0.5437 0.6349 0.0119  0.0529  -0.1034 621 HOH B O     
6551 O O     . HOH D .   ? 0.3089 0.3548 0.2689 -0.1171 0.0253  -0.0087 622 HOH B O     
6552 O O     . HOH D .   ? 0.1357 0.3027 0.1965 0.0675  0.0138  0.0059  623 HOH B O     
6553 O O     . HOH D .   ? 0.4196 0.3642 0.2652 -0.0420 0.0321  -0.0351 624 HOH B O     
6554 O O     . HOH D .   ? 0.5905 0.5479 0.4347 -0.2012 0.0131  -0.0311 625 HOH B O     
6555 O O     . HOH D .   ? 0.3895 0.4462 0.3567 -0.0947 0.0537  -0.0132 626 HOH B O     
6556 O O     . HOH D .   ? 0.2639 0.4977 0.3084 0.0277  -0.0040 -0.0340 627 HOH B O     
6557 O O     . HOH D .   ? 0.4075 0.6187 0.5460 -0.0998 0.0266  -0.0144 628 HOH B O     
6558 O O     . HOH D .   ? 0.3536 0.2394 0.2059 -0.0104 0.0379  0.0202  629 HOH B O     
6559 O O     . HOH D .   ? 0.3780 0.5112 0.5285 -0.0080 0.0627  -0.1313 630 HOH B O     
6560 O O     . HOH D .   ? 0.3379 0.4453 0.4623 0.0172  0.0316  -0.0267 631 HOH B O     
6561 O O     . HOH D .   ? 0.2624 0.3123 0.2165 0.0909  0.0686  -0.0415 632 HOH B O     
6562 O O     . HOH D .   ? 0.2571 0.3453 0.3078 0.0456  0.0221  -0.0051 633 HOH B O     
6563 O O     . HOH D .   ? 0.2677 0.3423 0.2581 0.0448  0.0259  -0.0079 634 HOH B O     
6564 O O     . HOH D .   ? 0.3130 0.3424 0.2370 -0.0077 0.0445  -0.0031 635 HOH B O     
6565 O O     . HOH D .   ? 0.2045 0.2281 0.1598 0.0617  0.0371  -0.0062 636 HOH B O     
6566 O O     . HOH D .   ? 0.3864 0.2148 0.2504 0.0746  0.0455  -0.0102 637 HOH B O     
6567 O O     . HOH D .   ? 0.4772 0.3770 0.3036 -0.1279 0.0251  -0.0335 638 HOH B O     
6568 O O     . HOH D .   ? 0.4474 0.4426 0.4316 0.1523  0.0247  0.0140  639 HOH B O     
6569 O O     . HOH D .   ? 0.4742 0.3709 0.4046 0.1511  0.0204  0.0323  640 HOH B O     
6570 O O     . HOH D .   ? 0.2784 0.4214 0.4061 -0.0266 0.0332  -0.0210 641 HOH B O     
6571 O O     . HOH D .   ? 0.3473 0.3047 0.2361 -0.0232 0.0287  -0.0170 642 HOH B O     
6572 O O     . HOH D .   ? 0.4687 0.4392 0.2972 0.0048  0.0663  -0.0677 643 HOH B O     
6573 O O     . HOH D .   ? 0.7025 0.6300 0.5620 -0.0507 0.0468  0.0162  644 HOH B O     
6574 O O     . HOH D .   ? 0.6311 0.3602 0.3463 -0.1063 0.0598  -0.1089 645 HOH B O     
6575 O O     . HOH D .   ? 0.4946 0.5260 0.2326 -0.1112 0.0454  -0.0854 646 HOH B O     
6576 O O     . HOH D .   ? 0.3134 0.3588 0.2003 0.0251  0.0587  -0.0362 647 HOH B O     
6577 O O     . HOH D .   ? 0.6451 0.5882 0.5177 -0.0608 0.0488  0.0098  648 HOH B O     
6578 O O     . HOH D .   ? 0.3288 0.3893 0.3259 0.0635  0.0249  0.0013  649 HOH B O     
6579 O O     . HOH D .   ? 0.4439 0.3617 0.3406 0.1135  0.0052  0.0587  650 HOH B O     
6580 O O     . HOH D .   ? 0.5216 0.5290 0.4364 0.0861  0.1154  -0.1113 651 HOH B O     
6581 O O     . HOH D .   ? 0.3735 0.2747 0.2262 0.0099  0.0319  0.0322  652 HOH B O     
6582 O O     . HOH D .   ? 0.3314 0.4927 0.4049 -0.1139 0.0185  -0.0070 653 HOH B O     
6583 O O     . HOH D .   ? 0.6827 0.5047 0.5260 0.1014  0.1258  -0.2038 654 HOH B O     
6584 O O     . HOH D .   ? 0.3191 0.4013 0.3445 0.0487  0.0244  -0.0083 655 HOH B O     
6585 O O     . HOH D .   ? 0.2884 0.4135 0.3803 -0.0003 0.0566  -0.0741 656 HOH B O     
6586 O O     . HOH D .   ? 0.6588 0.5656 0.3887 -0.1485 0.0308  -0.0915 657 HOH B O     
6587 O O     . HOH D .   ? 0.4209 0.4838 0.2333 -0.0310 0.0637  -0.0589 658 HOH B O     
6588 O O     . HOH D .   ? 0.3506 0.3776 0.3219 0.1214  0.0218  0.0165  659 HOH B O     
6589 O O     . HOH D .   ? 0.6039 0.6142 0.5016 -0.0014 0.0321  -0.0158 660 HOH B O     
6590 O O     . HOH D .   ? 0.2089 0.2459 0.1615 -0.0011 0.0177  0.0046  661 HOH B O     
6591 O O     . HOH D .   ? 0.2890 0.3425 0.2976 0.0373  0.0275  -0.0051 662 HOH B O     
6592 O O     . HOH D .   ? 0.5138 0.4516 0.4830 0.1646  0.0228  0.0211  663 HOH B O     
6593 O O     . HOH D .   ? 0.3166 0.4423 0.3578 -0.0971 0.0472  -0.0196 664 HOH B O     
6594 O O     . HOH D .   ? 0.1387 0.2415 0.2343 0.0338  0.0231  -0.0240 665 HOH B O     
6595 O O     . HOH D .   ? 0.4438 0.4288 0.3376 0.0779  0.1043  -0.1076 666 HOH B O     
6596 O O     . HOH D .   ? 0.2657 0.3142 0.2423 0.1198  0.0152  0.0224  667 HOH B O     
6597 O O     . HOH D .   ? 0.2946 0.3693 0.2993 0.0538  0.0240  -0.0046 668 HOH B O     
6598 O O     . HOH D .   ? 0.6088 0.3314 0.3956 0.0302  0.0779  -0.0907 669 HOH B O     
6599 O O     . HOH D .   ? 0.4096 0.4586 0.2236 -0.0094 0.0803  -0.0776 670 HOH B O     
6600 O O     . HOH D .   ? 0.2977 0.4841 0.5075 -0.0203 -0.0268 0.0348  671 HOH B O     
6601 O O     . HOH D .   ? 0.5272 0.3538 0.3803 0.0803  0.0196  0.0488  672 HOH B O     
6602 O O     . HOH D .   ? 0.6816 0.3789 0.4893 0.0595  0.1025  -0.1573 673 HOH B O     
6603 O O     . HOH D .   ? 0.4933 0.7157 0.5103 0.0985  -0.0299 0.0394  674 HOH B O     
6604 O O     . HOH D .   ? 0.2704 0.3316 0.2981 0.0317  0.0255  -0.0047 675 HOH B O     
6605 O O     . HOH D .   ? 0.7540 0.5881 0.4679 -0.1243 0.0525  -0.1170 676 HOH B O     
6606 O O     . HOH D .   ? 0.5405 0.6101 0.3131 -0.1363 0.0060  -0.0371 677 HOH B O     
6607 O O     . HOH D .   ? 0.4230 0.4868 0.2695 0.0224  0.0957  -0.0801 678 HOH B O     
6608 O O     . HOH D .   ? 0.3377 0.4522 0.4514 0.0101  0.0424  -0.0393 679 HOH B O     
6609 O O     . HOH D .   ? 0.3413 0.4693 0.3754 0.1116  0.0431  -0.0115 680 HOH B O     
6610 O O     . HOH D .   ? 0.4939 0.5649 0.3189 -0.0391 0.0485  -0.0384 681 HOH B O     
6611 O O     . HOH D .   ? 0.2622 0.3523 0.2629 0.0765  0.0352  -0.0009 682 HOH B O     
6612 O O     . HOH D .   ? 0.4277 0.5162 0.2766 -0.0999 -0.0083 0.0034  683 HOH B O     
6613 O O     . HOH D .   ? 0.5121 0.3716 0.2701 -0.0478 0.0650  -0.0996 684 HOH B O     
6614 O O     . HOH D .   ? 0.3158 0.3639 0.2818 0.1035  0.0738  -0.0490 685 HOH B O     
6615 O O     . HOH D .   ? 0.3805 0.5524 0.5099 -0.0594 -0.0100 0.0168  686 HOH B O     
6616 O O     . HOH D .   ? 0.3923 0.4575 0.3803 0.1271  0.0096  0.0271  687 HOH B O     
6617 O O     . HOH D .   ? 0.2265 0.3699 0.3750 -0.0155 -0.0158 0.0307  688 HOH B O     
6618 O O     . HOH D .   ? 0.3069 0.2476 0.2076 0.0478  0.0426  -0.0171 689 HOH B O     
6619 O O     . HOH D .   ? 0.3989 0.6008 0.4719 0.0963  0.0111  0.0100  690 HOH B O     
6620 O O     . HOH D .   ? 0.4591 0.5857 0.2690 -0.0406 0.0785  -0.0616 691 HOH B O     
6621 O O     . HOH D .   ? 0.3531 0.3866 0.2890 0.0044  0.0236  -0.0005 692 HOH B O     
6622 O O     . HOH D .   ? 0.5775 0.3531 0.3278 -0.0281 0.0801  -0.1248 693 HOH B O     
6623 O O     . HOH D .   ? 0.4816 0.4352 0.3422 -0.0290 0.0434  0.0221  694 HOH B O     
6624 O O     . HOH D .   ? 0.3992 0.5087 0.4314 -0.0614 0.0581  -0.0281 695 HOH B O     
6625 O O     . HOH D .   ? 0.3152 0.3648 0.2828 0.0479  0.0333  -0.0011 696 HOH B O     
6626 O O     . HOH D .   ? 0.3131 0.3102 0.1856 -0.0704 0.0126  -0.0177 697 HOH B O     
6627 O O     . HOH D .   ? 0.1831 0.2642 0.2324 0.0233  0.0338  -0.0219 698 HOH B O     
6628 O O     . HOH D .   ? 0.3754 0.4219 0.2447 -0.1217 -0.0109 -0.0101 699 HOH B O     
6629 O O     . HOH D .   ? 0.1827 0.2676 0.2455 0.0385  0.0214  -0.0049 700 HOH B O     
6630 O O     . HOH D .   ? 0.5242 0.5722 0.2862 -0.1225 0.0211  -0.0537 701 HOH B O     
6631 O O     . HOH D .   ? 0.6185 0.7437 0.2265 -0.1084 0.0164  0.0095  702 HOH B O     
6632 O O     . HOH D .   ? 0.3295 0.5783 0.3547 0.0770  -0.0265 0.0201  703 HOH B O     
6633 O O     . HOH D .   ? 0.5970 0.3203 0.4015 0.0529  0.0748  -0.0760 704 HOH B O     
6634 O O     . HOH D .   ? 0.4874 0.5090 0.3407 -0.0226 0.0394  -0.0319 705 HOH B O     
6635 O O     . HOH D .   ? 0.8673 0.7148 0.5627 -0.0464 0.1234  -0.2293 706 HOH B O     
6636 O O     . HOH D .   ? 0.3724 0.5502 0.4121 0.0317  0.0120  -0.0365 707 HOH B O     
6637 O O     . HOH D .   ? 0.5017 0.3216 0.2609 -0.0622 0.0562  -0.0875 708 HOH B O     
6638 O O     . HOH D .   ? 0.3326 0.3464 0.2558 0.0742  0.0127  0.0308  709 HOH B O     
6639 O O     . HOH D .   ? 0.4392 0.4730 0.4264 0.1286  0.0999  -0.0849 710 HOH B O     
6640 O O     . HOH D .   ? 0.5666 0.4929 0.4192 -0.0146 0.0378  0.0286  711 HOH B O     
6641 O O     . HOH D .   ? 0.6806 0.5094 0.4025 -0.0189 0.1209  -0.2172 712 HOH B O     
6642 O O     . HOH D .   ? 0.4396 0.4512 0.3309 0.0015  0.0361  0.0139  713 HOH B O     
6643 O O     . HOH D .   ? 0.3525 0.3131 0.2913 0.1354  0.0151  0.0352  714 HOH B O     
6644 O O     . HOH D .   ? 0.5222 0.3626 0.3353 -0.0783 0.0458  0.0207  715 HOH B O     
6645 O O     . HOH D .   ? 0.3733 0.2953 0.2482 0.0557  0.0589  -0.0435 716 HOH B O     
6646 O O     . HOH D .   ? 0.5662 0.3502 0.4445 0.1270  0.0416  0.0038  717 HOH B O     
6647 O O     . HOH D .   ? 0.3765 0.4368 0.3184 -0.1257 -0.0037 -0.0041 718 HOH B O     
6648 O O     . HOH D .   ? 0.4920 0.2684 0.3143 0.0194  0.0445  -0.0080 719 HOH B O     
6649 O O     . HOH D .   ? 0.4317 0.5447 0.5535 0.0013  0.0216  -0.0100 720 HOH B O     
6650 O O     . HOH D .   ? 0.3638 0.4516 0.3616 -0.1037 0.0497  -0.0158 721 HOH B O     
6651 O O     . HOH D .   ? 0.4727 0.4316 0.3378 -0.1275 0.0597  0.0078  722 HOH B O     
6652 O O     . HOH D .   ? 0.4866 0.5451 0.4987 0.1374  0.0830  -0.0608 723 HOH B O     
6653 O O     . HOH D .   ? 0.1894 0.4068 0.2446 0.0653  -0.0068 0.0013  724 HOH B O     
6654 O O     . HOH D .   ? 0.3147 0.4409 0.3640 0.0253  0.0331  -0.0463 725 HOH B O     
6655 O O     . HOH D .   ? 0.4160 0.6393 0.4217 0.0647  -0.0192 0.0111  726 HOH B O     
6656 O O     . HOH D .   ? 0.3586 0.2539 0.2192 0.0052  0.0423  -0.0268 727 HOH B O     
6657 O O     . HOH D .   ? 0.5365 0.6576 0.5602 0.1159  0.0692  -0.0374 728 HOH B O     
6658 O O     . HOH D .   ? 0.6164 0.3596 0.3750 -0.0636 0.0545  -0.0694 729 HOH B O     
6659 O O     . HOH D .   ? 0.2626 0.2922 0.2220 0.0446  0.0322  -0.0026 730 HOH B O     
6660 O O     . HOH D .   ? 0.5796 0.3457 0.3826 0.0424  0.0794  -0.0901 731 HOH B O     
6661 O O     . HOH D .   ? 0.4680 0.4580 0.3704 0.0730  0.0098  0.0420  732 HOH B O     
6662 O O     . HOH D .   ? 0.5716 0.7352 0.5477 0.0418  0.0030  -0.0068 733 HOH B O     
6663 O O     . HOH D .   ? 0.5137 0.3049 0.2905 -0.0783 0.0454  -0.0557 734 HOH B O     
6664 O O     . HOH D .   ? 0.5282 0.2957 0.3326 -0.0123 0.0484  -0.0274 735 HOH B O     
6665 O O     . HOH D .   ? 0.5093 0.5551 0.4361 -0.0513 0.0613  -0.0117 736 HOH B O     
6666 O O     . HOH D .   ? 0.3347 0.4185 0.3203 -0.1369 0.0323  -0.0108 737 HOH B O     
6667 O O     . HOH D .   ? 0.5299 0.3483 0.4071 0.1135  0.0278  0.0288  738 HOH B O     
6668 O O     . HOH D .   ? 0.6026 0.4748 0.3326 -0.1170 0.0453  -0.1005 739 HOH B O     
6669 O O     . HOH D .   ? 0.2609 0.3884 0.3163 -0.0057 0.0593  -0.0695 740 HOH B O     
6670 O O     . HOH D .   ? 0.3435 0.3139 0.2739 0.1205  0.0109  0.0402  741 HOH B O     
6671 O O     . HOH D .   ? 0.6467 0.3508 0.5259 0.1278  0.0753  -0.0743 742 HOH B O     
6672 O O     . HOH D .   ? 0.6270 0.6409 0.5497 0.0991  0.0003  0.0493  743 HOH B O     
6673 O O     . HOH D .   ? 0.2671 0.3411 0.3091 0.0361  0.0256  -0.0087 744 HOH B O     
6674 O O     . HOH D .   ? 0.4319 0.5461 0.5658 0.0113  0.0465  -0.0644 745 HOH B O     
6675 O O     . HOH D .   ? 0.3605 0.4204 0.3738 0.1395  0.0307  0.0012  746 HOH B O     
6676 O O     . HOH D .   ? 0.5058 0.6150 0.5044 -0.1180 -0.0090 0.0055  747 HOH B O     
6677 O O     . HOH D .   ? 0.7198 0.3673 0.5405 0.0776  0.0825  -0.0976 748 HOH B O     
6678 O O     . HOH D .   ? 0.4375 0.4060 0.3115 0.0487  0.0138  0.0463  749 HOH B O     
6679 O O     . HOH D .   ? 0.4832 0.3833 0.4267 0.1570  0.0257  0.0214  750 HOH B O     
6680 O O     . HOH D .   ? 0.7266 0.6583 0.5160 -0.1763 0.0097  -0.0536 751 HOH B O     
6681 O O     . HOH D .   ? 0.2250 0.3366 0.2403 0.0940  0.0400  -0.0072 752 HOH B O     
6682 O O     . HOH D .   ? 0.2999 0.3425 0.2655 -0.0697 0.0495  -0.0119 753 HOH B O     
6683 O O     . HOH D .   ? 0.5997 0.3664 0.3660 -0.0944 0.0454  -0.0540 754 HOH B O     
6684 O O     . HOH D .   ? 0.2984 0.3877 0.3659 -0.0092 0.0092  0.0083  755 HOH B O     
6685 O O     . HOH D .   ? 0.4454 0.4277 0.3158 -0.0008 0.0414  -0.0314 756 HOH B O     
6686 O O     . HOH D .   ? 0.4500 0.6951 0.4630 0.0469  -0.0187 -0.0042 757 HOH B O     
6687 O O     . HOH D .   ? 0.3786 0.4861 0.3931 -0.0032 0.0551  -0.0462 758 HOH B O     
6688 O O     . HOH D .   ? 0.6465 0.4890 0.3474 -0.1039 0.0732  -0.1518 759 HOH B O     
6689 O O     . HOH D .   ? 0.2049 0.2454 0.1878 0.0291  0.0236  0.0040  760 HOH B O     
6690 O O     . HOH D .   ? 0.5597 0.3235 0.3794 0.0582  0.0716  -0.0681 761 HOH B O     
6691 O O     . HOH D .   ? 0.2508 0.3784 0.2773 0.0880  0.0343  -0.0019 762 HOH B O     
6692 O O     . HOH D .   ? 0.5042 0.5511 0.3543 -0.0407 0.0305  -0.0226 763 HOH B O     
6693 O O     . HOH D .   ? 0.3315 0.4686 0.3884 -0.0831 -0.0116 0.0152  764 HOH B O     
6694 O O     . HOH D .   ? 0.5046 0.4774 0.3860 -0.1820 0.0339  -0.0135 765 HOH B O     
6695 O O     . HOH D .   ? 0.4476 0.2629 0.3090 0.0790  0.0400  0.0036  766 HOH B O     
6696 O O     . HOH D .   ? 0.5813 0.5354 0.4989 0.1097  0.1232  -0.1601 767 HOH B O     
6697 O O     . HOH D .   ? 0.7613 0.5137 0.4664 -0.1175 0.0621  -0.1264 768 HOH B O     
6698 O O     . HOH D .   ? 0.5102 0.5409 0.5333 0.1584  0.0603  -0.0359 769 HOH B O     
6699 O O     . HOH D .   ? 0.5861 0.3689 0.3843 -0.0532 0.0423  0.0165  770 HOH B O     
6700 O O     . HOH D .   ? 0.4071 0.3439 0.2706 -0.0273 0.0330  -0.0271 771 HOH B O     
6701 O O     . HOH D .   ? 0.4014 0.4782 0.4262 0.1394  0.0742  -0.0488 772 HOH B O     
6702 O O     . HOH D .   ? 0.4046 0.5381 0.3818 -0.0006 0.0446  -0.0485 773 HOH B O     
6703 O O     . HOH D .   ? 0.3956 0.5304 0.3697 0.0528  0.0059  0.0018  774 HOH B O     
6704 O O     . HOH D .   ? 0.2992 0.4123 0.4020 -0.0027 0.0391  -0.0285 775 HOH B O     
6705 O O     . HOH D .   ? 0.3714 0.4856 0.5095 0.0103  0.0482  -0.0746 776 HOH B O     
6706 O O     . HOH D .   ? 0.3470 0.4514 0.3753 0.0558  0.0204  -0.0084 777 HOH B O     
6707 O O     . HOH D .   ? 0.6434 0.4928 0.3681 -0.1830 0.0282  -0.0907 778 HOH B O     
6708 O O     . HOH D .   ? 0.2039 0.2750 0.2465 0.0270  0.0285  -0.0121 779 HOH B O     
6709 O O     . HOH D .   ? 0.3247 0.3344 0.3243 0.1488  0.0546  -0.0284 780 HOH B O     
6710 O O     . HOH D .   ? 0.3974 0.5493 0.5117 -0.0417 0.0470  -0.0313 781 HOH B O     
6711 O O     . HOH D .   ? 0.4654 0.4734 0.3359 -0.0050 0.0411  -0.0296 782 HOH B O     
6712 O O     . HOH D .   ? 0.4436 0.6763 0.4934 0.1035  -0.0224 0.0322  783 HOH B O     
6713 O O     . HOH D .   ? 0.4619 0.5594 0.4249 0.0119  0.0375  -0.0241 784 HOH B O     
6714 O O     . HOH D .   ? 0.6288 0.4883 0.4943 0.0990  0.0072  0.0664  785 HOH B O     
6715 O O     . HOH D .   ? 0.3269 0.4291 0.4261 0.0081  0.0339  -0.0240 786 HOH B O     
6716 O O     . HOH D .   ? 0.5616 0.6635 0.5542 -0.0980 -0.0141 0.0119  787 HOH B O     
6717 O O     . HOH D .   ? 0.3919 0.4021 0.3029 0.0060  0.0375  0.0069  788 HOH B O     
6718 O O     . HOH D .   ? 0.3975 0.4515 0.3572 0.0691  0.0172  0.0128  789 HOH B O     
6719 O O     . HOH D .   ? 0.6295 0.4811 0.6025 0.1664  0.1057  -0.1321 790 HOH B O     
6720 O O     . HOH D .   ? 0.7155 0.4941 0.4874 -0.1703 0.0453  -0.0086 791 HOH B O     
6721 O O     . HOH D .   ? 0.3280 0.4596 0.3720 0.1213  0.0298  -0.0003 792 HOH B O     
6722 O O     . HOH D .   ? 0.4270 0.6460 0.5836 -0.0886 0.0348  -0.0213 793 HOH B O     
6723 O O     . HOH D .   ? 0.5825 0.6814 0.5302 -0.0039 0.0456  -0.0273 794 HOH B O     
6724 O O     . HOH D .   ? 0.3706 0.4854 0.4111 0.0485  0.0209  -0.0163 795 HOH B O     
6725 O O     . HOH D .   ? 0.4919 0.3917 0.3593 0.0692  0.0682  -0.0564 796 HOH B O     
6726 O O     . HOH D .   ? 0.4450 0.5984 0.5449 -0.0559 0.0507  -0.0313 797 HOH B O     
6727 O O     . HOH D .   ? 0.7091 0.4327 0.4796 -0.0500 0.0517  -0.0450 798 HOH B O     
6728 O O     . HOH D .   ? 0.4491 0.5004 0.4389 0.1349  0.0125  0.0252  799 HOH B O     
6729 O O     . HOH D .   ? 0.4316 0.5517 0.4157 0.0543  0.0117  -0.0019 800 HOH B O     
6730 O O     . HOH D .   ? 0.8428 0.6140 0.6469 0.0254  0.0248  0.0571  801 HOH B O     
6731 O O     . HOH D .   ? 0.5593 0.4297 0.4647 0.1253  0.1197  -0.1749 802 HOH B O     
6732 O O     . HOH D .   ? 0.6943 0.7720 0.6753 0.1325  -0.0055 0.0452  803 HOH B O     
6733 O O     . HOH D .   ? 0.6481 0.4408 0.4950 0.0752  0.0298  0.0299  804 HOH B O     
6734 O O     . HOH D .   ? 0.5993 0.6803 0.5474 0.0191  0.0321  -0.0110 805 HOH B O     
6735 O O     . HOH D .   ? 0.4627 0.5908 0.4855 0.1077  0.0611  -0.0276 806 HOH B O     
6736 O O     . HOH D .   ? 0.3817 0.3723 0.3840 0.1608  0.0475  -0.0191 807 HOH B O     
6737 O O     . HOH D .   ? 0.7170 0.8211 0.3289 -0.0902 0.0172  0.0099  808 HOH B O     
6738 O O     . HOH D .   ? 0.5594 0.5426 0.4874 0.1205  0.0029  0.0507  809 HOH B O     
6739 O O     . HOH D .   ? 0.4208 0.5065 0.4103 0.1240  0.0028  0.0322  810 HOH B O     
6740 O O     . HOH D .   ? 0.5186 0.7437 0.5245 0.0787  -0.0249 0.0239  811 HOH B O     
6741 O O     . HOH D .   ? 0.6968 0.6656 0.5436 -0.0433 0.0469  0.0259  812 HOH B O     
6742 O O     . HOH D .   ? 0.3879 0.4518 0.3698 -0.0636 0.0546  -0.0173 813 HOH B O     
6743 O O     . HOH D .   ? 0.5711 0.6205 0.4199 -0.1435 -0.0151 -0.0159 814 HOH B O     
6744 O O     . HOH D .   ? 0.6919 0.3876 0.5665 0.1220  0.0839  -0.0969 815 HOH B O     
6745 O O     . HOH D .   ? 0.5516 0.7148 0.6519 -0.0706 -0.0177 0.0226  816 HOH B O     
6746 O O     . HOH D .   ? 0.3645 0.4504 0.3868 0.1343  0.0240  0.0074  817 HOH B O     
6747 O O     . HOH D .   ? 0.5733 0.3753 0.3726 -0.0652 0.0433  0.0232  818 HOH B O     
6748 O O     . HOH D .   ? 0.4555 0.3416 0.2879 -0.0087 0.0337  0.0395  819 HOH B O     
6749 O O     . HOH D .   ? 0.4622 0.5745 0.5028 0.1355  0.0263  0.0036  820 HOH B O     
6750 O O     . HOH D .   ? 0.5576 0.6004 0.2996 -0.1293 0.0301  -0.0708 821 HOH B O     
6751 O O     . HOH D .   ? 0.5926 0.6541 0.6034 0.1360  0.0998  -0.0800 822 HOH B O     
6752 O O     . HOH D .   ? 0.6349 0.3967 0.3691 -0.0522 0.0764  -0.1281 823 HOH B O     
6753 O O     . HOH D .   ? 0.7444 0.4569 0.6450 0.1390  0.0902  -0.1132 824 HOH B O     
6754 O O     . HOH D .   ? 0.5913 0.4742 0.4716 0.1136  0.0019  0.0704  825 HOH B O     
6755 O O     . HOH D .   ? 0.7343 0.5261 0.5977 0.1002  0.0361  0.0143  826 HOH B O     
6756 O O     . HOH D .   ? 0.7097 0.4365 0.4587 -0.0231 0.0802  -0.1212 827 HOH B O     
6757 O O     . HOH D .   ? 0.3986 0.4806 0.3827 0.0533  0.0209  -0.0024 828 HOH B O     
6758 O O     . HOH D .   ? 0.6709 0.4511 0.4646 0.0047  0.0261  0.0615  829 HOH B O     
6759 O O     . HOH D .   ? 0.3606 0.5599 0.4362 0.1027  0.0204  0.0056  830 HOH B O     
6760 O O     . HOH D .   ? 0.3829 0.4570 0.3521 0.0624  0.0168  0.0072  831 HOH B O     
6761 O O     . HOH D .   ? 0.4204 0.4792 0.4521 0.1528  0.0685  -0.0444 832 HOH B O     
6762 O O     . HOH D .   ? 0.2740 0.4294 0.4257 -0.0224 -0.0291 0.0455  833 HOH B O     
6763 O O     . HOH D .   ? 0.6106 0.5691 0.5288 0.1278  -0.0015 0.0619  834 HOH B O     
6764 O O     . HOH D .   ? 0.6918 0.3884 0.4978 0.0499  0.0599  -0.0403 835 HOH B O     
6765 O O     . HOH D .   ? 0.5290 0.6530 0.5615 -0.0104 0.0621  -0.0601 836 HOH B O     
6766 O O     . HOH D .   ? 0.5992 0.6929 0.5660 -0.1126 -0.0165 0.0086  837 HOH B O     
6767 O O     . HOH D .   ? 0.6312 0.3006 0.4442 0.0722  0.0578  -0.0300 838 HOH B O     
6768 O O     . HOH D .   ? 0.6917 0.4941 0.3955 -0.0962 0.0754  -0.1524 839 HOH B O     
6769 O O     . HOH D .   ? 0.5964 0.5687 0.4544 0.1019  0.1280  -0.1448 840 HOH B O     
6770 O O     . HOH D .   ? 0.6567 0.6140 0.4739 -0.1862 0.0046  -0.0421 841 HOH B O     
6771 O O     . HOH D .   ? 0.8046 0.4491 0.6106 0.0687  0.0519  -0.0145 842 HOH B O     
6772 O O     . HOH D .   ? 0.4874 0.6501 0.5238 -0.0300 0.0684  -0.1063 843 HOH B O     
6773 O O     . HOH D .   ? 0.9283 0.6323 0.8041 0.1195  0.0965  -0.1311 844 HOH B O     
6774 O O     . HOH D .   ? 0.4230 0.5775 0.4359 -0.0253 0.0638  -0.0875 845 HOH B O     
# 
