data_9JOC
# 
_entry.id   9JOC 
# 
_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   9JOC         pdb_00009joc 10.2210/pdb9joc/pdb 
WWPDB D_1300051808 ?            ?                   
# 
_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       2024-11-27 
# 
_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                        9JOC 
_pdbx_database_status.recvd_initial_deposition_date   2024-09-24 
_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                 2 
_pdbx_contact_author.email              changyg@ouc.edu.cn 
_pdbx_contact_author.name_first         Yaoguang 
_pdbx_contact_author.name_last          Chang 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-8234-7272 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Chen, G.N.'  1 0000-0001-6456-3919 
'Chang, Y.G.' 2 0000-0002-8234-7272 
# 
_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                     'Structure of endo-1.3-fucanase (Fun168D) from GH168 family at 1.29 Angstroms resulution.' 
_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 'Chen, G.N.'  1 0000-0001-6456-3919 
primary 'Chang, Y.G.' 2 0000-0002-8234-7272 
# 
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 endo-1.3-fucanase 44452.410 1   ? ? ? ? 
2 water   nat water             18.015    517 ? ? ? ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;STKNGIIELEQETEEELEQNQEIDYSNYPEFSWDTMPLYMHVRKNTAYTDEEINYLASFPLITLEKSQAQNTYGSTEEGT
LATASAIKLKNNKAKVLYYRNVVINWGNYKNDDEFISKNPSALLKNQNNELVYMPNGSTPFFDITKSFVQEYWLKSVEDM
VATPNIDGTFIDANIKVLVPSFFSSKVGVNKQAEIENSYFSMMSRLKESLSNNLILANIIRVRPEFEENGLEYLGYFNGS
YLEGFDSEAFGMSNAEYLVEGIEATQKAAQSGKIITMTLGLGEAIDNNTGIDDQREDVDLNDEELNKRVDYLLAIFLICA
EKYSYVYLHDGYLATNSAVWLHQFDQYKKALGAPLGKAIKNGYIYTRKFENLDVWLNLETQTATLTWKE
;
_entity_poly.pdbx_seq_one_letter_code_can   
;STKNGIIELEQETEEELEQNQEIDYSNYPEFSWDTMPLYMHVRKNTAYTDEEINYLASFPLITLEKSQAQNTYGSTEEGT
LATASAIKLKNNKAKVLYYRNVVINWGNYKNDDEFISKNPSALLKNQNNELVYMPNGSTPFFDITKSFVQEYWLKSVEDM
VATPNIDGTFIDANIKVLVPSFFSSKVGVNKQAEIENSYFSMMSRLKESLSNNLILANIIRVRPEFEENGLEYLGYFNGS
YLEGFDSEAFGMSNAEYLVEGIEATQKAAQSGKIITMTLGLGEAIDNNTGIDDQREDVDLNDEELNKRVDYLLAIFLICA
EKYSYVYLHDGYLATNSAVWLHQFDQYKKALGAPLGKAIKNGYIYTRKFENLDVWLNLETQTATLTWKE
;
_entity_poly.pdbx_strand_id                 A 
_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   SER n 
1 2   THR n 
1 3   LYS n 
1 4   ASN n 
1 5   GLY n 
1 6   ILE n 
1 7   ILE n 
1 8   GLU n 
1 9   LEU n 
1 10  GLU n 
1 11  GLN n 
1 12  GLU n 
1 13  THR n 
1 14  GLU n 
1 15  GLU n 
1 16  GLU n 
1 17  LEU n 
1 18  GLU n 
1 19  GLN n 
1 20  ASN n 
1 21  GLN n 
1 22  GLU n 
1 23  ILE n 
1 24  ASP n 
1 25  TYR n 
1 26  SER n 
1 27  ASN n 
1 28  TYR n 
1 29  PRO n 
1 30  GLU n 
1 31  PHE n 
1 32  SER n 
1 33  TRP n 
1 34  ASP n 
1 35  THR n 
1 36  MET n 
1 37  PRO n 
1 38  LEU n 
1 39  TYR n 
1 40  MET n 
1 41  HIS n 
1 42  VAL n 
1 43  ARG n 
1 44  LYS n 
1 45  ASN n 
1 46  THR n 
1 47  ALA n 
1 48  TYR n 
1 49  THR n 
1 50  ASP n 
1 51  GLU n 
1 52  GLU n 
1 53  ILE n 
1 54  ASN n 
1 55  TYR n 
1 56  LEU n 
1 57  ALA n 
1 58  SER n 
1 59  PHE n 
1 60  PRO n 
1 61  LEU n 
1 62  ILE n 
1 63  THR n 
1 64  LEU n 
1 65  GLU n 
1 66  LYS n 
1 67  SER n 
1 68  GLN n 
1 69  ALA n 
1 70  GLN n 
1 71  ASN n 
1 72  THR n 
1 73  TYR n 
1 74  GLY n 
1 75  SER n 
1 76  THR n 
1 77  GLU n 
1 78  GLU n 
1 79  GLY n 
1 80  THR n 
1 81  LEU n 
1 82  ALA n 
1 83  THR n 
1 84  ALA n 
1 85  SER n 
1 86  ALA n 
1 87  ILE n 
1 88  LYS n 
1 89  LEU n 
1 90  LYS n 
1 91  ASN n 
1 92  ASN n 
1 93  LYS n 
1 94  ALA n 
1 95  LYS n 
1 96  VAL n 
1 97  LEU n 
1 98  TYR n 
1 99  TYR n 
1 100 ARG n 
1 101 ASN n 
1 102 VAL n 
1 103 VAL n 
1 104 ILE n 
1 105 ASN n 
1 106 TRP n 
1 107 GLY n 
1 108 ASN n 
1 109 TYR n 
1 110 LYS n 
1 111 ASN n 
1 112 ASP n 
1 113 ASP n 
1 114 GLU n 
1 115 PHE n 
1 116 ILE n 
1 117 SER n 
1 118 LYS n 
1 119 ASN n 
1 120 PRO n 
1 121 SER n 
1 122 ALA n 
1 123 LEU n 
1 124 LEU n 
1 125 LYS n 
1 126 ASN n 
1 127 GLN n 
1 128 ASN n 
1 129 ASN n 
1 130 GLU n 
1 131 LEU n 
1 132 VAL n 
1 133 TYR n 
1 134 MET n 
1 135 PRO n 
1 136 ASN n 
1 137 GLY n 
1 138 SER n 
1 139 THR n 
1 140 PRO n 
1 141 PHE n 
1 142 PHE n 
1 143 ASP n 
1 144 ILE n 
1 145 THR n 
1 146 LYS n 
1 147 SER n 
1 148 PHE n 
1 149 VAL n 
1 150 GLN n 
1 151 GLU n 
1 152 TYR n 
1 153 TRP n 
1 154 LEU n 
1 155 LYS n 
1 156 SER n 
1 157 VAL n 
1 158 GLU n 
1 159 ASP n 
1 160 MET n 
1 161 VAL n 
1 162 ALA n 
1 163 THR n 
1 164 PRO n 
1 165 ASN n 
1 166 ILE n 
1 167 ASP n 
1 168 GLY n 
1 169 THR n 
1 170 PHE n 
1 171 ILE n 
1 172 ASP n 
1 173 ALA n 
1 174 ASN n 
1 175 ILE n 
1 176 LYS n 
1 177 VAL n 
1 178 LEU n 
1 179 VAL n 
1 180 PRO n 
1 181 SER n 
1 182 PHE n 
1 183 PHE n 
1 184 SER n 
1 185 SER n 
1 186 LYS n 
1 187 VAL n 
1 188 GLY n 
1 189 VAL n 
1 190 ASN n 
1 191 LYS n 
1 192 GLN n 
1 193 ALA n 
1 194 GLU n 
1 195 ILE n 
1 196 GLU n 
1 197 ASN n 
1 198 SER n 
1 199 TYR n 
1 200 PHE n 
1 201 SER n 
1 202 MET n 
1 203 MET n 
1 204 SER n 
1 205 ARG n 
1 206 LEU n 
1 207 LYS n 
1 208 GLU n 
1 209 SER n 
1 210 LEU n 
1 211 SER n 
1 212 ASN n 
1 213 ASN n 
1 214 LEU n 
1 215 ILE n 
1 216 LEU n 
1 217 ALA n 
1 218 ASN n 
1 219 ILE n 
1 220 ILE n 
1 221 ARG n 
1 222 VAL n 
1 223 ARG n 
1 224 PRO n 
1 225 GLU n 
1 226 PHE n 
1 227 GLU n 
1 228 GLU n 
1 229 ASN n 
1 230 GLY n 
1 231 LEU n 
1 232 GLU n 
1 233 TYR n 
1 234 LEU n 
1 235 GLY n 
1 236 TYR n 
1 237 PHE n 
1 238 ASN n 
1 239 GLY n 
1 240 SER n 
1 241 TYR n 
1 242 LEU n 
1 243 GLU n 
1 244 GLY n 
1 245 PHE n 
1 246 ASP n 
1 247 SER n 
1 248 GLU n 
1 249 ALA n 
1 250 PHE n 
1 251 GLY n 
1 252 MET n 
1 253 SER n 
1 254 ASN n 
1 255 ALA n 
1 256 GLU n 
1 257 TYR n 
1 258 LEU n 
1 259 VAL n 
1 260 GLU n 
1 261 GLY n 
1 262 ILE n 
1 263 GLU n 
1 264 ALA n 
1 265 THR n 
1 266 GLN n 
1 267 LYS n 
1 268 ALA n 
1 269 ALA n 
1 270 GLN n 
1 271 SER n 
1 272 GLY n 
1 273 LYS n 
1 274 ILE n 
1 275 ILE n 
1 276 THR n 
1 277 MET n 
1 278 THR n 
1 279 LEU n 
1 280 GLY n 
1 281 LEU n 
1 282 GLY n 
1 283 GLU n 
1 284 ALA n 
1 285 ILE n 
1 286 ASP n 
1 287 ASN n 
1 288 ASN n 
1 289 THR n 
1 290 GLY n 
1 291 ILE n 
1 292 ASP n 
1 293 ASP n 
1 294 GLN n 
1 295 ARG n 
1 296 GLU n 
1 297 ASP n 
1 298 VAL n 
1 299 ASP n 
1 300 LEU n 
1 301 ASN n 
1 302 ASP n 
1 303 GLU n 
1 304 GLU n 
1 305 LEU n 
1 306 ASN n 
1 307 LYS n 
1 308 ARG n 
1 309 VAL n 
1 310 ASP n 
1 311 TYR n 
1 312 LEU n 
1 313 LEU n 
1 314 ALA n 
1 315 ILE n 
1 316 PHE n 
1 317 LEU n 
1 318 ILE n 
1 319 CYS n 
1 320 ALA n 
1 321 GLU n 
1 322 LYS n 
1 323 TYR n 
1 324 SER n 
1 325 TYR n 
1 326 VAL n 
1 327 TYR n 
1 328 LEU n 
1 329 HIS n 
1 330 ASP n 
1 331 GLY n 
1 332 TYR n 
1 333 LEU n 
1 334 ALA n 
1 335 THR n 
1 336 ASN n 
1 337 SER n 
1 338 ALA n 
1 339 VAL n 
1 340 TRP n 
1 341 LEU n 
1 342 HIS n 
1 343 GLN n 
1 344 PHE n 
1 345 ASP n 
1 346 GLN n 
1 347 TYR n 
1 348 LYS n 
1 349 LYS n 
1 350 ALA n 
1 351 LEU n 
1 352 GLY n 
1 353 ALA n 
1 354 PRO n 
1 355 LEU n 
1 356 GLY n 
1 357 LYS n 
1 358 ALA n 
1 359 ILE n 
1 360 LYS n 
1 361 ASN n 
1 362 GLY n 
1 363 TYR n 
1 364 ILE n 
1 365 TYR n 
1 366 THR n 
1 367 ARG n 
1 368 LYS n 
1 369 PHE n 
1 370 GLU n 
1 371 ASN n 
1 372 LEU n 
1 373 ASP n 
1 374 VAL n 
1 375 TRP n 
1 376 LEU n 
1 377 ASN n 
1 378 LEU n 
1 379 GLU n 
1 380 THR n 
1 381 GLN n 
1 382 THR n 
1 383 ALA n 
1 384 THR n 
1 385 LEU n 
1 386 THR n 
1 387 TRP n 
1 388 LYS n 
1 389 GLU 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                   389 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 AXE80_08865 
_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      'Wenyingzhuangia fucanilytica' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     1790137 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_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 
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   SER 1   1   ?   ?   ?   A . n 
A 1 2   THR 2   2   ?   ?   ?   A . n 
A 1 3   LYS 3   3   ?   ?   ?   A . n 
A 1 4   ASN 4   4   ?   ?   ?   A . n 
A 1 5   GLY 5   5   ?   ?   ?   A . n 
A 1 6   ILE 6   6   ?   ?   ?   A . n 
A 1 7   ILE 7   7   ?   ?   ?   A . n 
A 1 8   GLU 8   8   ?   ?   ?   A . n 
A 1 9   LEU 9   9   ?   ?   ?   A . n 
A 1 10  GLU 10  10  ?   ?   ?   A . n 
A 1 11  GLN 11  11  ?   ?   ?   A . n 
A 1 12  GLU 12  12  ?   ?   ?   A . n 
A 1 13  THR 13  13  ?   ?   ?   A . n 
A 1 14  GLU 14  14  ?   ?   ?   A . n 
A 1 15  GLU 15  15  ?   ?   ?   A . n 
A 1 16  GLU 16  16  ?   ?   ?   A . n 
A 1 17  LEU 17  17  ?   ?   ?   A . n 
A 1 18  GLU 18  18  ?   ?   ?   A . n 
A 1 19  GLN 19  19  ?   ?   ?   A . n 
A 1 20  ASN 20  20  ?   ?   ?   A . n 
A 1 21  GLN 21  21  ?   ?   ?   A . n 
A 1 22  GLU 22  22  ?   ?   ?   A . n 
A 1 23  ILE 23  23  23  ILE ILE A . n 
A 1 24  ASP 24  24  24  ASP ASP A . n 
A 1 25  TYR 25  25  25  TYR TYR A . n 
A 1 26  SER 26  26  26  SER SER A . n 
A 1 27  ASN 27  27  27  ASN ASN A . n 
A 1 28  TYR 28  28  28  TYR TYR A . n 
A 1 29  PRO 29  29  29  PRO PRO A . n 
A 1 30  GLU 30  30  30  GLU GLU A . n 
A 1 31  PHE 31  31  31  PHE PHE A . n 
A 1 32  SER 32  32  32  SER SER A . n 
A 1 33  TRP 33  33  33  TRP TRP A . n 
A 1 34  ASP 34  34  34  ASP ASP A . n 
A 1 35  THR 35  35  35  THR THR A . n 
A 1 36  MET 36  36  36  MET MET A . n 
A 1 37  PRO 37  37  37  PRO PRO A . n 
A 1 38  LEU 38  38  38  LEU LEU A . n 
A 1 39  TYR 39  39  39  TYR TYR A . n 
A 1 40  MET 40  40  40  MET MET A . n 
A 1 41  HIS 41  41  41  HIS HIS A . n 
A 1 42  VAL 42  42  42  VAL VAL A . n 
A 1 43  ARG 43  43  43  ARG ARG A . n 
A 1 44  LYS 44  44  44  LYS LYS A . n 
A 1 45  ASN 45  45  45  ASN ASN A . n 
A 1 46  THR 46  46  46  THR THR A . n 
A 1 47  ALA 47  47  47  ALA ALA A . n 
A 1 48  TYR 48  48  48  TYR TYR A . n 
A 1 49  THR 49  49  49  THR THR A . n 
A 1 50  ASP 50  50  50  ASP ASP A . n 
A 1 51  GLU 51  51  51  GLU GLU A . n 
A 1 52  GLU 52  52  52  GLU GLU A . n 
A 1 53  ILE 53  53  53  ILE ILE A . n 
A 1 54  ASN 54  54  54  ASN ASN A . n 
A 1 55  TYR 55  55  55  TYR TYR A . n 
A 1 56  LEU 56  56  56  LEU LEU A . n 
A 1 57  ALA 57  57  57  ALA ALA A . n 
A 1 58  SER 58  58  58  SER SER A . n 
A 1 59  PHE 59  59  59  PHE PHE A . n 
A 1 60  PRO 60  60  60  PRO PRO A . n 
A 1 61  LEU 61  61  61  LEU LEU A . n 
A 1 62  ILE 62  62  62  ILE ILE A . n 
A 1 63  THR 63  63  63  THR THR A . n 
A 1 64  LEU 64  64  64  LEU LEU A . n 
A 1 65  GLU 65  65  65  GLU GLU A . n 
A 1 66  LYS 66  66  66  LYS LYS A . n 
A 1 67  SER 67  67  67  SER SER A . n 
A 1 68  GLN 68  68  68  GLN GLN A . n 
A 1 69  ALA 69  69  69  ALA ALA A . n 
A 1 70  GLN 70  70  70  GLN GLN A . n 
A 1 71  ASN 71  71  71  ASN ASN A . n 
A 1 72  THR 72  72  72  THR THR A . n 
A 1 73  TYR 73  73  73  TYR TYR A . n 
A 1 74  GLY 74  74  74  GLY GLY A . n 
A 1 75  SER 75  75  75  SER SER A . n 
A 1 76  THR 76  76  76  THR THR A . n 
A 1 77  GLU 77  77  77  GLU GLU A . n 
A 1 78  GLU 78  78  78  GLU GLU A . n 
A 1 79  GLY 79  79  79  GLY GLY A . n 
A 1 80  THR 80  80  80  THR THR A . n 
A 1 81  LEU 81  81  81  LEU LEU A . n 
A 1 82  ALA 82  82  82  ALA ALA A . n 
A 1 83  THR 83  83  83  THR THR A . n 
A 1 84  ALA 84  84  84  ALA ALA A . n 
A 1 85  SER 85  85  85  SER SER A . n 
A 1 86  ALA 86  86  86  ALA ALA A . n 
A 1 87  ILE 87  87  87  ILE ILE A . n 
A 1 88  LYS 88  88  88  LYS LYS A . n 
A 1 89  LEU 89  89  89  LEU LEU A . n 
A 1 90  LYS 90  90  90  LYS LYS A . n 
A 1 91  ASN 91  91  91  ASN ASN A . n 
A 1 92  ASN 92  92  92  ASN ASN A . n 
A 1 93  LYS 93  93  93  LYS LYS A . n 
A 1 94  ALA 94  94  94  ALA ALA A . n 
A 1 95  LYS 95  95  95  LYS LYS A . n 
A 1 96  VAL 96  96  96  VAL VAL A . n 
A 1 97  LEU 97  97  97  LEU LEU A . n 
A 1 98  TYR 98  98  98  TYR TYR A . n 
A 1 99  TYR 99  99  99  TYR TYR A . n 
A 1 100 ARG 100 100 100 ARG ARG A . n 
A 1 101 ASN 101 101 101 ASN ASN A . n 
A 1 102 VAL 102 102 102 VAL VAL A . n 
A 1 103 VAL 103 103 103 VAL VAL A . n 
A 1 104 ILE 104 104 104 ILE ILE A . n 
A 1 105 ASN 105 105 105 ASN ASN A . n 
A 1 106 TRP 106 106 106 TRP TRP A . n 
A 1 107 GLY 107 107 107 GLY GLY A . n 
A 1 108 ASN 108 108 108 ASN ASN A . n 
A 1 109 TYR 109 109 109 TYR TYR A . n 
A 1 110 LYS 110 110 110 LYS LYS A . n 
A 1 111 ASN 111 111 111 ASN ASN A . n 
A 1 112 ASP 112 112 112 ASP ASP A . n 
A 1 113 ASP 113 113 113 ASP ASP A . n 
A 1 114 GLU 114 114 114 GLU GLU A . n 
A 1 115 PHE 115 115 115 PHE PHE A . n 
A 1 116 ILE 116 116 116 ILE ILE A . n 
A 1 117 SER 117 117 117 SER SER A . n 
A 1 118 LYS 118 118 118 LYS LYS A . n 
A 1 119 ASN 119 119 119 ASN ASN A . n 
A 1 120 PRO 120 120 120 PRO PRO A . n 
A 1 121 SER 121 121 121 SER SER A . n 
A 1 122 ALA 122 122 122 ALA ALA A . n 
A 1 123 LEU 123 123 123 LEU LEU A . n 
A 1 124 LEU 124 124 124 LEU LEU A . n 
A 1 125 LYS 125 125 125 LYS LYS A . n 
A 1 126 ASN 126 126 126 ASN ASN A . n 
A 1 127 GLN 127 127 127 GLN GLN A . n 
A 1 128 ASN 128 128 128 ASN ASN A . n 
A 1 129 ASN 129 129 129 ASN ASN A . n 
A 1 130 GLU 130 130 130 GLU GLU A . n 
A 1 131 LEU 131 131 131 LEU LEU A . n 
A 1 132 VAL 132 132 132 VAL VAL A . n 
A 1 133 TYR 133 133 133 TYR TYR A . n 
A 1 134 MET 134 134 134 MET MET A . n 
A 1 135 PRO 135 135 135 PRO PRO A . n 
A 1 136 ASN 136 136 136 ASN ASN A . n 
A 1 137 GLY 137 137 137 GLY GLY A . n 
A 1 138 SER 138 138 138 SER SER A . n 
A 1 139 THR 139 139 139 THR THR A . n 
A 1 140 PRO 140 140 140 PRO PRO A . n 
A 1 141 PHE 141 141 141 PHE PHE A . n 
A 1 142 PHE 142 142 142 PHE PHE A . n 
A 1 143 ASP 143 143 143 ASP ASP A . n 
A 1 144 ILE 144 144 144 ILE ILE A . n 
A 1 145 THR 145 145 145 THR THR A . n 
A 1 146 LYS 146 146 146 LYS LYS A . n 
A 1 147 SER 147 147 147 SER SER A . n 
A 1 148 PHE 148 148 148 PHE PHE A . n 
A 1 149 VAL 149 149 149 VAL VAL A . n 
A 1 150 GLN 150 150 150 GLN GLN A . n 
A 1 151 GLU 151 151 151 GLU GLU A . n 
A 1 152 TYR 152 152 152 TYR TYR A . n 
A 1 153 TRP 153 153 153 TRP TRP A . n 
A 1 154 LEU 154 154 154 LEU LEU A . n 
A 1 155 LYS 155 155 155 LYS LYS A . n 
A 1 156 SER 156 156 156 SER SER A . n 
A 1 157 VAL 157 157 157 VAL VAL A . n 
A 1 158 GLU 158 158 158 GLU GLU A . n 
A 1 159 ASP 159 159 159 ASP ASP A . n 
A 1 160 MET 160 160 160 MET MET A . n 
A 1 161 VAL 161 161 161 VAL VAL A . n 
A 1 162 ALA 162 162 162 ALA ALA A . n 
A 1 163 THR 163 163 163 THR THR A . n 
A 1 164 PRO 164 164 164 PRO PRO A . n 
A 1 165 ASN 165 165 165 ASN ASN A . n 
A 1 166 ILE 166 166 166 ILE ILE A . n 
A 1 167 ASP 167 167 167 ASP ASP A . n 
A 1 168 GLY 168 168 168 GLY GLY A . n 
A 1 169 THR 169 169 169 THR THR A . n 
A 1 170 PHE 170 170 170 PHE PHE A . n 
A 1 171 ILE 171 171 171 ILE ILE A . n 
A 1 172 ASP 172 172 172 ASP ASP A . n 
A 1 173 ALA 173 173 173 ALA ALA A . n 
A 1 174 ASN 174 174 174 ASN ASN A . n 
A 1 175 ILE 175 175 175 ILE ILE A . n 
A 1 176 LYS 176 176 176 LYS LYS A . n 
A 1 177 VAL 177 177 177 VAL VAL A . n 
A 1 178 LEU 178 178 178 LEU LEU A . n 
A 1 179 VAL 179 179 179 VAL VAL A . n 
A 1 180 PRO 180 180 180 PRO PRO A . n 
A 1 181 SER 181 181 181 SER SER A . n 
A 1 182 PHE 182 182 182 PHE PHE A . n 
A 1 183 PHE 183 183 183 PHE PHE A . n 
A 1 184 SER 184 184 184 SER SER A . n 
A 1 185 SER 185 185 185 SER SER A . n 
A 1 186 LYS 186 186 186 LYS LYS A . n 
A 1 187 VAL 187 187 187 VAL VAL A . n 
A 1 188 GLY 188 188 188 GLY GLY A . n 
A 1 189 VAL 189 189 189 VAL VAL A . n 
A 1 190 ASN 190 190 190 ASN ASN A . n 
A 1 191 LYS 191 191 191 LYS LYS A . n 
A 1 192 GLN 192 192 192 GLN GLN A . n 
A 1 193 ALA 193 193 193 ALA ALA A . n 
A 1 194 GLU 194 194 194 GLU GLU A . n 
A 1 195 ILE 195 195 195 ILE ILE A . n 
A 1 196 GLU 196 196 196 GLU GLU A . n 
A 1 197 ASN 197 197 197 ASN ASN A . n 
A 1 198 SER 198 198 198 SER SER A . n 
A 1 199 TYR 199 199 199 TYR TYR A . n 
A 1 200 PHE 200 200 200 PHE PHE A . n 
A 1 201 SER 201 201 201 SER SER A . n 
A 1 202 MET 202 202 202 MET MET A . n 
A 1 203 MET 203 203 203 MET MET A . n 
A 1 204 SER 204 204 204 SER SER A . n 
A 1 205 ARG 205 205 205 ARG ARG A . n 
A 1 206 LEU 206 206 206 LEU LEU A . n 
A 1 207 LYS 207 207 207 LYS LYS A . n 
A 1 208 GLU 208 208 208 GLU GLU A . n 
A 1 209 SER 209 209 209 SER SER A . n 
A 1 210 LEU 210 210 210 LEU LEU A . n 
A 1 211 SER 211 211 211 SER SER A . n 
A 1 212 ASN 212 212 212 ASN ASN A . n 
A 1 213 ASN 213 213 213 ASN ASN A . n 
A 1 214 LEU 214 214 214 LEU LEU A . n 
A 1 215 ILE 215 215 215 ILE ILE A . n 
A 1 216 LEU 216 216 216 LEU LEU A . n 
A 1 217 ALA 217 217 217 ALA ALA A . n 
A 1 218 ASN 218 218 218 ASN ASN A . n 
A 1 219 ILE 219 219 219 ILE ILE A . n 
A 1 220 ILE 220 220 220 ILE ILE A . n 
A 1 221 ARG 221 221 221 ARG ARG A . n 
A 1 222 VAL 222 222 222 VAL VAL A . n 
A 1 223 ARG 223 223 223 ARG ARG A . n 
A 1 224 PRO 224 224 224 PRO PRO A . n 
A 1 225 GLU 225 225 225 GLU GLU A . n 
A 1 226 PHE 226 226 226 PHE PHE A . n 
A 1 227 GLU 227 227 227 GLU GLU A . n 
A 1 228 GLU 228 228 228 GLU GLU A . n 
A 1 229 ASN 229 229 229 ASN ASN A . n 
A 1 230 GLY 230 230 230 GLY GLY A . n 
A 1 231 LEU 231 231 231 LEU LEU A . n 
A 1 232 GLU 232 232 232 GLU GLU A . n 
A 1 233 TYR 233 233 233 TYR TYR A . n 
A 1 234 LEU 234 234 234 LEU LEU A . n 
A 1 235 GLY 235 235 235 GLY GLY A . n 
A 1 236 TYR 236 236 236 TYR TYR A . n 
A 1 237 PHE 237 237 237 PHE PHE A . n 
A 1 238 ASN 238 238 238 ASN ASN A . n 
A 1 239 GLY 239 239 239 GLY GLY A . n 
A 1 240 SER 240 240 240 SER SER A . n 
A 1 241 TYR 241 241 241 TYR TYR A . n 
A 1 242 LEU 242 242 242 LEU LEU A . n 
A 1 243 GLU 243 243 243 GLU GLU A . n 
A 1 244 GLY 244 244 244 GLY GLY A . n 
A 1 245 PHE 245 245 245 PHE PHE A . n 
A 1 246 ASP 246 246 246 ASP ASP A . n 
A 1 247 SER 247 247 247 SER SER A . n 
A 1 248 GLU 248 248 248 GLU GLU A . n 
A 1 249 ALA 249 249 249 ALA ALA A . n 
A 1 250 PHE 250 250 250 PHE PHE A . n 
A 1 251 GLY 251 251 251 GLY GLY A . n 
A 1 252 MET 252 252 252 MET MET A . n 
A 1 253 SER 253 253 253 SER SER A . n 
A 1 254 ASN 254 254 254 ASN ASN A . n 
A 1 255 ALA 255 255 255 ALA ALA A . n 
A 1 256 GLU 256 256 256 GLU GLU A . n 
A 1 257 TYR 257 257 257 TYR TYR A . n 
A 1 258 LEU 258 258 258 LEU LEU A . n 
A 1 259 VAL 259 259 259 VAL VAL A . n 
A 1 260 GLU 260 260 260 GLU GLU A . n 
A 1 261 GLY 261 261 261 GLY GLY A . n 
A 1 262 ILE 262 262 262 ILE ILE A . n 
A 1 263 GLU 263 263 263 GLU GLU A . n 
A 1 264 ALA 264 264 264 ALA ALA A . n 
A 1 265 THR 265 265 265 THR THR A . n 
A 1 266 GLN 266 266 266 GLN GLN A . n 
A 1 267 LYS 267 267 267 LYS LYS A . n 
A 1 268 ALA 268 268 268 ALA ALA A . n 
A 1 269 ALA 269 269 269 ALA ALA A . n 
A 1 270 GLN 270 270 270 GLN GLN A . n 
A 1 271 SER 271 271 271 SER SER A . n 
A 1 272 GLY 272 272 272 GLY GLY A . n 
A 1 273 LYS 273 273 273 LYS LYS A . n 
A 1 274 ILE 274 274 274 ILE ILE A . n 
A 1 275 ILE 275 275 275 ILE ILE A . n 
A 1 276 THR 276 276 276 THR THR A . n 
A 1 277 MET 277 277 277 MET MET A . n 
A 1 278 THR 278 278 278 THR THR A . n 
A 1 279 LEU 279 279 279 LEU LEU A . n 
A 1 280 GLY 280 280 280 GLY GLY A . n 
A 1 281 LEU 281 281 281 LEU LEU A . n 
A 1 282 GLY 282 282 282 GLY GLY A . n 
A 1 283 GLU 283 283 283 GLU GLU A . n 
A 1 284 ALA 284 284 284 ALA ALA A . n 
A 1 285 ILE 285 285 285 ILE ILE A . n 
A 1 286 ASP 286 286 286 ASP ASP A . n 
A 1 287 ASN 287 287 287 ASN ASN A . n 
A 1 288 ASN 288 288 288 ASN ASN A . n 
A 1 289 THR 289 289 289 THR THR A . n 
A 1 290 GLY 290 290 290 GLY GLY A . n 
A 1 291 ILE 291 291 291 ILE ILE A . n 
A 1 292 ASP 292 292 292 ASP ASP A . n 
A 1 293 ASP 293 293 293 ASP ASP A . n 
A 1 294 GLN 294 294 294 GLN GLN A . n 
A 1 295 ARG 295 295 295 ARG ARG A . n 
A 1 296 GLU 296 296 296 GLU GLU A . n 
A 1 297 ASP 297 297 297 ASP ASP A . n 
A 1 298 VAL 298 298 298 VAL VAL A . n 
A 1 299 ASP 299 299 299 ASP ASP A . n 
A 1 300 LEU 300 300 300 LEU LEU A . n 
A 1 301 ASN 301 301 301 ASN ASN A . n 
A 1 302 ASP 302 302 302 ASP ASP A . n 
A 1 303 GLU 303 303 303 GLU GLU A . n 
A 1 304 GLU 304 304 304 GLU GLU A . n 
A 1 305 LEU 305 305 305 LEU LEU A . n 
A 1 306 ASN 306 306 306 ASN ASN A . n 
A 1 307 LYS 307 307 307 LYS LYS A . n 
A 1 308 ARG 308 308 308 ARG ARG A . n 
A 1 309 VAL 309 309 309 VAL VAL A . n 
A 1 310 ASP 310 310 310 ASP ASP A . n 
A 1 311 TYR 311 311 311 TYR TYR A . n 
A 1 312 LEU 312 312 312 LEU LEU A . n 
A 1 313 LEU 313 313 313 LEU LEU A . n 
A 1 314 ALA 314 314 314 ALA ALA A . n 
A 1 315 ILE 315 315 315 ILE ILE A . n 
A 1 316 PHE 316 316 316 PHE PHE A . n 
A 1 317 LEU 317 317 317 LEU LEU A . n 
A 1 318 ILE 318 318 318 ILE ILE A . n 
A 1 319 CYS 319 319 319 CYS CYS A . n 
A 1 320 ALA 320 320 320 ALA ALA A . n 
A 1 321 GLU 321 321 321 GLU GLU A . n 
A 1 322 LYS 322 322 322 LYS LYS A . n 
A 1 323 TYR 323 323 323 TYR TYR A . n 
A 1 324 SER 324 324 324 SER SER A . n 
A 1 325 TYR 325 325 325 TYR TYR A . n 
A 1 326 VAL 326 326 326 VAL VAL A . n 
A 1 327 TYR 327 327 327 TYR TYR A . n 
A 1 328 LEU 328 328 328 LEU LEU A . n 
A 1 329 HIS 329 329 329 HIS HIS A . n 
A 1 330 ASP 330 330 330 ASP ASP A . n 
A 1 331 GLY 331 331 331 GLY GLY A . n 
A 1 332 TYR 332 332 332 TYR TYR A . n 
A 1 333 LEU 333 333 333 LEU LEU A . n 
A 1 334 ALA 334 334 334 ALA ALA A . n 
A 1 335 THR 335 335 335 THR THR A . n 
A 1 336 ASN 336 336 336 ASN ASN A . n 
A 1 337 SER 337 337 337 SER SER A . n 
A 1 338 ALA 338 338 338 ALA ALA A . n 
A 1 339 VAL 339 339 339 VAL VAL A . n 
A 1 340 TRP 340 340 340 TRP TRP A . n 
A 1 341 LEU 341 341 341 LEU LEU A . n 
A 1 342 HIS 342 342 342 HIS HIS A . n 
A 1 343 GLN 343 343 343 GLN GLN A . n 
A 1 344 PHE 344 344 344 PHE PHE A . n 
A 1 345 ASP 345 345 345 ASP ASP A . n 
A 1 346 GLN 346 346 346 GLN GLN A . n 
A 1 347 TYR 347 347 347 TYR TYR A . n 
A 1 348 LYS 348 348 348 LYS LYS A . n 
A 1 349 LYS 349 349 349 LYS LYS A . n 
A 1 350 ALA 350 350 350 ALA ALA A . n 
A 1 351 LEU 351 351 351 LEU LEU A . n 
A 1 352 GLY 352 352 352 GLY GLY A . n 
A 1 353 ALA 353 353 353 ALA ALA A . n 
A 1 354 PRO 354 354 354 PRO PRO A . n 
A 1 355 LEU 355 355 355 LEU LEU A . n 
A 1 356 GLY 356 356 356 GLY GLY A . n 
A 1 357 LYS 357 357 357 LYS LYS A . n 
A 1 358 ALA 358 358 358 ALA ALA A . n 
A 1 359 ILE 359 359 359 ILE ILE A . n 
A 1 360 LYS 360 360 360 LYS LYS A . n 
A 1 361 ASN 361 361 361 ASN ASN A . n 
A 1 362 GLY 362 362 362 GLY GLY A . n 
A 1 363 TYR 363 363 363 TYR TYR A . n 
A 1 364 ILE 364 364 364 ILE ILE A . n 
A 1 365 TYR 365 365 365 TYR TYR A . n 
A 1 366 THR 366 366 366 THR THR A . n 
A 1 367 ARG 367 367 367 ARG ARG A . n 
A 1 368 LYS 368 368 368 LYS LYS A . n 
A 1 369 PHE 369 369 369 PHE PHE A . n 
A 1 370 GLU 370 370 370 GLU GLU A . n 
A 1 371 ASN 371 371 371 ASN ASN A . n 
A 1 372 LEU 372 372 372 LEU LEU A . n 
A 1 373 ASP 373 373 373 ASP ASP A . n 
A 1 374 VAL 374 374 374 VAL VAL A . n 
A 1 375 TRP 375 375 375 TRP TRP A . n 
A 1 376 LEU 376 376 376 LEU LEU A . n 
A 1 377 ASN 377 377 377 ASN ASN A . n 
A 1 378 LEU 378 378 378 LEU LEU A . n 
A 1 379 GLU 379 379 379 GLU GLU A . n 
A 1 380 THR 380 380 380 THR THR A . n 
A 1 381 GLN 381 381 381 GLN GLN A . n 
A 1 382 THR 382 382 382 THR THR A . n 
A 1 383 ALA 383 383 383 ALA ALA A . n 
A 1 384 THR 384 384 384 THR THR A . n 
A 1 385 LEU 385 385 385 LEU LEU A . n 
A 1 386 THR 386 386 386 THR THR A . n 
A 1 387 TRP 387 387 387 TRP TRP A . n 
A 1 388 LYS 388 388 388 LYS LYS A . n 
A 1 389 GLU 389 389 ?   ?   ?   A . n 
# 
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 
B 2 HOH 1   401 465 HOH HOH A . 
B 2 HOH 2   402 128 HOH HOH A . 
B 2 HOH 3   403 2   HOH HOH A . 
B 2 HOH 4   404 1   HOH HOH A . 
B 2 HOH 5   405 326 HOH HOH A . 
B 2 HOH 6   406 514 HOH HOH A . 
B 2 HOH 7   407 28  HOH HOH A . 
B 2 HOH 8   408 417 HOH HOH A . 
B 2 HOH 9   409 421 HOH HOH A . 
B 2 HOH 10  410 403 HOH HOH A . 
B 2 HOH 11  411 293 HOH HOH A . 
B 2 HOH 12  412 375 HOH HOH A . 
B 2 HOH 13  413 223 HOH HOH A . 
B 2 HOH 14  414 164 HOH HOH A . 
B 2 HOH 15  415 357 HOH HOH A . 
B 2 HOH 16  416 367 HOH HOH A . 
B 2 HOH 17  417 104 HOH HOH A . 
B 2 HOH 18  418 455 HOH HOH A . 
B 2 HOH 19  419 347 HOH HOH A . 
B 2 HOH 20  420 442 HOH HOH A . 
B 2 HOH 21  421 96  HOH HOH A . 
B 2 HOH 22  422 401 HOH HOH A . 
B 2 HOH 23  423 350 HOH HOH A . 
B 2 HOH 24  424 133 HOH HOH A . 
B 2 HOH 25  425 23  HOH HOH A . 
B 2 HOH 26  426 374 HOH HOH A . 
B 2 HOH 27  427 358 HOH HOH A . 
B 2 HOH 28  428 274 HOH HOH A . 
B 2 HOH 29  429 114 HOH HOH A . 
B 2 HOH 30  430 213 HOH HOH A . 
B 2 HOH 31  431 157 HOH HOH A . 
B 2 HOH 32  432 277 HOH HOH A . 
B 2 HOH 33  433 57  HOH HOH A . 
B 2 HOH 34  434 68  HOH HOH A . 
B 2 HOH 35  435 264 HOH HOH A . 
B 2 HOH 36  436 84  HOH HOH A . 
B 2 HOH 37  437 182 HOH HOH A . 
B 2 HOH 38  438 253 HOH HOH A . 
B 2 HOH 39  439 138 HOH HOH A . 
B 2 HOH 40  440 163 HOH HOH A . 
B 2 HOH 41  441 238 HOH HOH A . 
B 2 HOH 42  442 74  HOH HOH A . 
B 2 HOH 43  443 247 HOH HOH A . 
B 2 HOH 44  444 396 HOH HOH A . 
B 2 HOH 45  445 240 HOH HOH A . 
B 2 HOH 46  446 140 HOH HOH A . 
B 2 HOH 47  447 489 HOH HOH A . 
B 2 HOH 48  448 284 HOH HOH A . 
B 2 HOH 49  449 343 HOH HOH A . 
B 2 HOH 50  450 47  HOH HOH A . 
B 2 HOH 51  451 118 HOH HOH A . 
B 2 HOH 52  452 344 HOH HOH A . 
B 2 HOH 53  453 7   HOH HOH A . 
B 2 HOH 54  454 33  HOH HOH A . 
B 2 HOH 55  455 146 HOH HOH A . 
B 2 HOH 56  456 127 HOH HOH A . 
B 2 HOH 57  457 132 HOH HOH A . 
B 2 HOH 58  458 256 HOH HOH A . 
B 2 HOH 59  459 400 HOH HOH A . 
B 2 HOH 60  460 112 HOH HOH A . 
B 2 HOH 61  461 69  HOH HOH A . 
B 2 HOH 62  462 39  HOH HOH A . 
B 2 HOH 63  463 310 HOH HOH A . 
B 2 HOH 64  464 26  HOH HOH A . 
B 2 HOH 65  465 416 HOH HOH A . 
B 2 HOH 66  466 71  HOH HOH A . 
B 2 HOH 67  467 345 HOH HOH A . 
B 2 HOH 68  468 43  HOH HOH A . 
B 2 HOH 69  469 207 HOH HOH A . 
B 2 HOH 70  470 81  HOH HOH A . 
B 2 HOH 71  471 156 HOH HOH A . 
B 2 HOH 72  472 44  HOH HOH A . 
B 2 HOH 73  473 151 HOH HOH A . 
B 2 HOH 74  474 107 HOH HOH A . 
B 2 HOH 75  475 59  HOH HOH A . 
B 2 HOH 76  476 89  HOH HOH A . 
B 2 HOH 77  477 31  HOH HOH A . 
B 2 HOH 78  478 368 HOH HOH A . 
B 2 HOH 79  479 276 HOH HOH A . 
B 2 HOH 80  480 14  HOH HOH A . 
B 2 HOH 81  481 170 HOH HOH A . 
B 2 HOH 82  482 60  HOH HOH A . 
B 2 HOH 83  483 56  HOH HOH A . 
B 2 HOH 84  484 13  HOH HOH A . 
B 2 HOH 85  485 11  HOH HOH A . 
B 2 HOH 86  486 17  HOH HOH A . 
B 2 HOH 87  487 423 HOH HOH A . 
B 2 HOH 88  488 244 HOH HOH A . 
B 2 HOH 89  489 22  HOH HOH A . 
B 2 HOH 90  490 32  HOH HOH A . 
B 2 HOH 91  491 37  HOH HOH A . 
B 2 HOH 92  492 45  HOH HOH A . 
B 2 HOH 93  493 5   HOH HOH A . 
B 2 HOH 94  494 215 HOH HOH A . 
B 2 HOH 95  495 480 HOH HOH A . 
B 2 HOH 96  496 278 HOH HOH A . 
B 2 HOH 97  497 92  HOH HOH A . 
B 2 HOH 98  498 41  HOH HOH A . 
B 2 HOH 99  499 272 HOH HOH A . 
B 2 HOH 100 500 21  HOH HOH A . 
B 2 HOH 101 501 55  HOH HOH A . 
B 2 HOH 102 502 105 HOH HOH A . 
B 2 HOH 103 503 8   HOH HOH A . 
B 2 HOH 104 504 90  HOH HOH A . 
B 2 HOH 105 505 218 HOH HOH A . 
B 2 HOH 106 506 387 HOH HOH A . 
B 2 HOH 107 507 20  HOH HOH A . 
B 2 HOH 108 508 87  HOH HOH A . 
B 2 HOH 109 509 186 HOH HOH A . 
B 2 HOH 110 510 349 HOH HOH A . 
B 2 HOH 111 511 224 HOH HOH A . 
B 2 HOH 112 512 444 HOH HOH A . 
B 2 HOH 113 513 275 HOH HOH A . 
B 2 HOH 114 514 220 HOH HOH A . 
B 2 HOH 115 515 500 HOH HOH A . 
B 2 HOH 116 516 176 HOH HOH A . 
B 2 HOH 117 517 501 HOH HOH A . 
B 2 HOH 118 518 67  HOH HOH A . 
B 2 HOH 119 519 65  HOH HOH A . 
B 2 HOH 120 520 16  HOH HOH A . 
B 2 HOH 121 521 155 HOH HOH A . 
B 2 HOH 122 522 29  HOH HOH A . 
B 2 HOH 123 523 389 HOH HOH A . 
B 2 HOH 124 524 149 HOH HOH A . 
B 2 HOH 125 525 152 HOH HOH A . 
B 2 HOH 126 526 161 HOH HOH A . 
B 2 HOH 127 527 386 HOH HOH A . 
B 2 HOH 128 528 103 HOH HOH A . 
B 2 HOH 129 529 134 HOH HOH A . 
B 2 HOH 130 530 24  HOH HOH A . 
B 2 HOH 131 531 97  HOH HOH A . 
B 2 HOH 132 532 51  HOH HOH A . 
B 2 HOH 133 533 135 HOH HOH A . 
B 2 HOH 134 534 162 HOH HOH A . 
B 2 HOH 135 535 211 HOH HOH A . 
B 2 HOH 136 536 428 HOH HOH A . 
B 2 HOH 137 537 168 HOH HOH A . 
B 2 HOH 138 538 342 HOH HOH A . 
B 2 HOH 139 539 210 HOH HOH A . 
B 2 HOH 140 540 147 HOH HOH A . 
B 2 HOH 141 541 129 HOH HOH A . 
B 2 HOH 142 542 232 HOH HOH A . 
B 2 HOH 143 543 217 HOH HOH A . 
B 2 HOH 144 544 116 HOH HOH A . 
B 2 HOH 145 545 130 HOH HOH A . 
B 2 HOH 146 546 124 HOH HOH A . 
B 2 HOH 147 547 191 HOH HOH A . 
B 2 HOH 148 548 72  HOH HOH A . 
B 2 HOH 149 549 290 HOH HOH A . 
B 2 HOH 150 550 111 HOH HOH A . 
B 2 HOH 151 551 397 HOH HOH A . 
B 2 HOH 152 552 18  HOH HOH A . 
B 2 HOH 153 553 330 HOH HOH A . 
B 2 HOH 154 554 478 HOH HOH A . 
B 2 HOH 155 555 376 HOH HOH A . 
B 2 HOH 156 556 273 HOH HOH A . 
B 2 HOH 157 557 254 HOH HOH A . 
B 2 HOH 158 558 3   HOH HOH A . 
B 2 HOH 159 559 245 HOH HOH A . 
B 2 HOH 160 560 242 HOH HOH A . 
B 2 HOH 161 561 306 HOH HOH A . 
B 2 HOH 162 562 212 HOH HOH A . 
B 2 HOH 163 563 106 HOH HOH A . 
B 2 HOH 164 564 202 HOH HOH A . 
B 2 HOH 165 565 283 HOH HOH A . 
B 2 HOH 166 566 263 HOH HOH A . 
B 2 HOH 167 567 101 HOH HOH A . 
B 2 HOH 168 568 113 HOH HOH A . 
B 2 HOH 169 569 188 HOH HOH A . 
B 2 HOH 170 570 502 HOH HOH A . 
B 2 HOH 171 571 222 HOH HOH A . 
B 2 HOH 172 572 352 HOH HOH A . 
B 2 HOH 173 573 9   HOH HOH A . 
B 2 HOH 174 574 98  HOH HOH A . 
B 2 HOH 175 575 100 HOH HOH A . 
B 2 HOH 176 576 15  HOH HOH A . 
B 2 HOH 177 577 328 HOH HOH A . 
B 2 HOH 178 578 61  HOH HOH A . 
B 2 HOH 179 579 288 HOH HOH A . 
B 2 HOH 180 580 339 HOH HOH A . 
B 2 HOH 181 581 19  HOH HOH A . 
B 2 HOH 182 582 27  HOH HOH A . 
B 2 HOH 183 583 434 HOH HOH A . 
B 2 HOH 184 584 145 HOH HOH A . 
B 2 HOH 185 585 362 HOH HOH A . 
B 2 HOH 186 586 497 HOH HOH A . 
B 2 HOH 187 587 248 HOH HOH A . 
B 2 HOH 188 588 110 HOH HOH A . 
B 2 HOH 189 589 66  HOH HOH A . 
B 2 HOH 190 590 126 HOH HOH A . 
B 2 HOH 191 591 4   HOH HOH A . 
B 2 HOH 192 592 419 HOH HOH A . 
B 2 HOH 193 593 282 HOH HOH A . 
B 2 HOH 194 594 192 HOH HOH A . 
B 2 HOH 195 595 481 HOH HOH A . 
B 2 HOH 196 596 333 HOH HOH A . 
B 2 HOH 197 597 142 HOH HOH A . 
B 2 HOH 198 598 109 HOH HOH A . 
B 2 HOH 199 599 435 HOH HOH A . 
B 2 HOH 200 600 265 HOH HOH A . 
B 2 HOH 201 601 490 HOH HOH A . 
B 2 HOH 202 602 150 HOH HOH A . 
B 2 HOH 203 603 94  HOH HOH A . 
B 2 HOH 204 604 425 HOH HOH A . 
B 2 HOH 205 605 370 HOH HOH A . 
B 2 HOH 206 606 454 HOH HOH A . 
B 2 HOH 207 607 53  HOH HOH A . 
B 2 HOH 208 608 405 HOH HOH A . 
B 2 HOH 209 609 476 HOH HOH A . 
B 2 HOH 210 610 73  HOH HOH A . 
B 2 HOH 211 611 257 HOH HOH A . 
B 2 HOH 212 612 131 HOH HOH A . 
B 2 HOH 213 613 169 HOH HOH A . 
B 2 HOH 214 614 300 HOH HOH A . 
B 2 HOH 215 615 30  HOH HOH A . 
B 2 HOH 216 616 412 HOH HOH A . 
B 2 HOH 217 617 121 HOH HOH A . 
B 2 HOH 218 618 259 HOH HOH A . 
B 2 HOH 219 619 38  HOH HOH A . 
B 2 HOH 220 620 10  HOH HOH A . 
B 2 HOH 221 621 371 HOH HOH A . 
B 2 HOH 222 622 312 HOH HOH A . 
B 2 HOH 223 623 377 HOH HOH A . 
B 2 HOH 224 624 148 HOH HOH A . 
B 2 HOH 225 625 440 HOH HOH A . 
B 2 HOH 226 626 199 HOH HOH A . 
B 2 HOH 227 627 93  HOH HOH A . 
B 2 HOH 228 628 302 HOH HOH A . 
B 2 HOH 229 629 34  HOH HOH A . 
B 2 HOH 230 630 208 HOH HOH A . 
B 2 HOH 231 631 82  HOH HOH A . 
B 2 HOH 232 632 340 HOH HOH A . 
B 2 HOH 233 633 91  HOH HOH A . 
B 2 HOH 234 634 99  HOH HOH A . 
B 2 HOH 235 635 6   HOH HOH A . 
B 2 HOH 236 636 50  HOH HOH A . 
B 2 HOH 237 637 313 HOH HOH A . 
B 2 HOH 238 638 353 HOH HOH A . 
B 2 HOH 239 639 413 HOH HOH A . 
B 2 HOH 240 640 475 HOH HOH A . 
B 2 HOH 241 641 261 HOH HOH A . 
B 2 HOH 242 642 183 HOH HOH A . 
B 2 HOH 243 643 311 HOH HOH A . 
B 2 HOH 244 644 346 HOH HOH A . 
B 2 HOH 245 645 341 HOH HOH A . 
B 2 HOH 246 646 83  HOH HOH A . 
B 2 HOH 247 647 119 HOH HOH A . 
B 2 HOH 248 648 159 HOH HOH A . 
B 2 HOH 249 649 316 HOH HOH A . 
B 2 HOH 250 650 86  HOH HOH A . 
B 2 HOH 251 651 414 HOH HOH A . 
B 2 HOH 252 652 214 HOH HOH A . 
B 2 HOH 253 653 366 HOH HOH A . 
B 2 HOH 254 654 436 HOH HOH A . 
B 2 HOH 255 655 115 HOH HOH A . 
B 2 HOH 256 656 267 HOH HOH A . 
B 2 HOH 257 657 195 HOH HOH A . 
B 2 HOH 258 658 167 HOH HOH A . 
B 2 HOH 259 659 136 HOH HOH A . 
B 2 HOH 260 660 204 HOH HOH A . 
B 2 HOH 261 661 205 HOH HOH A . 
B 2 HOH 262 662 285 HOH HOH A . 
B 2 HOH 263 663 477 HOH HOH A . 
B 2 HOH 264 664 258 HOH HOH A . 
B 2 HOH 265 665 173 HOH HOH A . 
B 2 HOH 266 666 12  HOH HOH A . 
B 2 HOH 267 667 443 HOH HOH A . 
B 2 HOH 268 668 239 HOH HOH A . 
B 2 HOH 269 669 54  HOH HOH A . 
B 2 HOH 270 670 286 HOH HOH A . 
B 2 HOH 271 671 63  HOH HOH A . 
B 2 HOH 272 672 79  HOH HOH A . 
B 2 HOH 273 673 351 HOH HOH A . 
B 2 HOH 274 674 177 HOH HOH A . 
B 2 HOH 275 675 364 HOH HOH A . 
B 2 HOH 276 676 382 HOH HOH A . 
B 2 HOH 277 677 189 HOH HOH A . 
B 2 HOH 278 678 123 HOH HOH A . 
B 2 HOH 279 679 102 HOH HOH A . 
B 2 HOH 280 680 95  HOH HOH A . 
B 2 HOH 281 681 363 HOH HOH A . 
B 2 HOH 282 682 301 HOH HOH A . 
B 2 HOH 283 683 294 HOH HOH A . 
B 2 HOH 284 684 160 HOH HOH A . 
B 2 HOH 285 685 390 HOH HOH A . 
B 2 HOH 286 686 411 HOH HOH A . 
B 2 HOH 287 687 299 HOH HOH A . 
B 2 HOH 288 688 46  HOH HOH A . 
B 2 HOH 289 689 190 HOH HOH A . 
B 2 HOH 290 690 229 HOH HOH A . 
B 2 HOH 291 691 58  HOH HOH A . 
B 2 HOH 292 692 25  HOH HOH A . 
B 2 HOH 293 693 49  HOH HOH A . 
B 2 HOH 294 694 359 HOH HOH A . 
B 2 HOH 295 695 431 HOH HOH A . 
B 2 HOH 296 696 206 HOH HOH A . 
B 2 HOH 297 697 185 HOH HOH A . 
B 2 HOH 298 698 439 HOH HOH A . 
B 2 HOH 299 699 449 HOH HOH A . 
B 2 HOH 300 700 360 HOH HOH A . 
B 2 HOH 301 701 268 HOH HOH A . 
B 2 HOH 302 702 201 HOH HOH A . 
B 2 HOH 303 703 235 HOH HOH A . 
B 2 HOH 304 704 137 HOH HOH A . 
B 2 HOH 305 705 174 HOH HOH A . 
B 2 HOH 306 706 77  HOH HOH A . 
B 2 HOH 307 707 329 HOH HOH A . 
B 2 HOH 308 708 335 HOH HOH A . 
B 2 HOH 309 709 461 HOH HOH A . 
B 2 HOH 310 710 36  HOH HOH A . 
B 2 HOH 311 711 422 HOH HOH A . 
B 2 HOH 312 712 78  HOH HOH A . 
B 2 HOH 313 713 35  HOH HOH A . 
B 2 HOH 314 714 379 HOH HOH A . 
B 2 HOH 315 715 179 HOH HOH A . 
B 2 HOH 316 716 365 HOH HOH A . 
B 2 HOH 317 717 332 HOH HOH A . 
B 2 HOH 318 718 354 HOH HOH A . 
B 2 HOH 319 719 75  HOH HOH A . 
B 2 HOH 320 720 178 HOH HOH A . 
B 2 HOH 321 721 319 HOH HOH A . 
B 2 HOH 322 722 394 HOH HOH A . 
B 2 HOH 323 723 221 HOH HOH A . 
B 2 HOH 324 724 426 HOH HOH A . 
B 2 HOH 325 725 117 HOH HOH A . 
B 2 HOH 326 726 392 HOH HOH A . 
B 2 HOH 327 727 80  HOH HOH A . 
B 2 HOH 328 728 348 HOH HOH A . 
B 2 HOH 329 729 200 HOH HOH A . 
B 2 HOH 330 730 209 HOH HOH A . 
B 2 HOH 331 731 108 HOH HOH A . 
B 2 HOH 332 732 64  HOH HOH A . 
B 2 HOH 333 733 495 HOH HOH A . 
B 2 HOH 334 734 408 HOH HOH A . 
B 2 HOH 335 735 391 HOH HOH A . 
B 2 HOH 336 736 48  HOH HOH A . 
B 2 HOH 337 737 508 HOH HOH A . 
B 2 HOH 338 738 88  HOH HOH A . 
B 2 HOH 339 739 420 HOH HOH A . 
B 2 HOH 340 740 197 HOH HOH A . 
B 2 HOH 341 741 298 HOH HOH A . 
B 2 HOH 342 742 457 HOH HOH A . 
B 2 HOH 343 743 122 HOH HOH A . 
B 2 HOH 344 744 279 HOH HOH A . 
B 2 HOH 345 745 488 HOH HOH A . 
B 2 HOH 346 746 388 HOH HOH A . 
B 2 HOH 347 747 318 HOH HOH A . 
B 2 HOH 348 748 184 HOH HOH A . 
B 2 HOH 349 749 62  HOH HOH A . 
B 2 HOH 350 750 241 HOH HOH A . 
B 2 HOH 351 751 270 HOH HOH A . 
B 2 HOH 352 752 505 HOH HOH A . 
B 2 HOH 353 753 520 HOH HOH A . 
B 2 HOH 354 754 323 HOH HOH A . 
B 2 HOH 355 755 409 HOH HOH A . 
B 2 HOH 356 756 171 HOH HOH A . 
B 2 HOH 357 757 484 HOH HOH A . 
B 2 HOH 358 758 144 HOH HOH A . 
B 2 HOH 359 759 154 HOH HOH A . 
B 2 HOH 360 760 507 HOH HOH A . 
B 2 HOH 361 761 451 HOH HOH A . 
B 2 HOH 362 762 70  HOH HOH A . 
B 2 HOH 363 763 334 HOH HOH A . 
B 2 HOH 364 764 491 HOH HOH A . 
B 2 HOH 365 765 518 HOH HOH A . 
B 2 HOH 366 766 427 HOH HOH A . 
B 2 HOH 367 767 331 HOH HOH A . 
B 2 HOH 368 768 516 HOH HOH A . 
B 2 HOH 369 769 462 HOH HOH A . 
B 2 HOH 370 770 441 HOH HOH A . 
B 2 HOH 371 771 380 HOH HOH A . 
B 2 HOH 372 772 398 HOH HOH A . 
B 2 HOH 373 773 175 HOH HOH A . 
B 2 HOH 374 774 40  HOH HOH A . 
B 2 HOH 375 775 399 HOH HOH A . 
B 2 HOH 376 776 438 HOH HOH A . 
B 2 HOH 377 777 249 HOH HOH A . 
B 2 HOH 378 778 433 HOH HOH A . 
B 2 HOH 379 779 52  HOH HOH A . 
B 2 HOH 380 780 307 HOH HOH A . 
B 2 HOH 381 781 499 HOH HOH A . 
B 2 HOH 382 782 42  HOH HOH A . 
B 2 HOH 383 783 378 HOH HOH A . 
B 2 HOH 384 784 327 HOH HOH A . 
B 2 HOH 385 785 181 HOH HOH A . 
B 2 HOH 386 786 467 HOH HOH A . 
B 2 HOH 387 787 472 HOH HOH A . 
B 2 HOH 388 788 482 HOH HOH A . 
B 2 HOH 389 789 381 HOH HOH A . 
B 2 HOH 390 790 304 HOH HOH A . 
B 2 HOH 391 791 303 HOH HOH A . 
B 2 HOH 392 792 230 HOH HOH A . 
B 2 HOH 393 793 314 HOH HOH A . 
B 2 HOH 394 794 289 HOH HOH A . 
B 2 HOH 395 795 296 HOH HOH A . 
B 2 HOH 396 796 498 HOH HOH A . 
B 2 HOH 397 797 445 HOH HOH A . 
B 2 HOH 398 798 504 HOH HOH A . 
B 2 HOH 399 799 125 HOH HOH A . 
B 2 HOH 400 800 369 HOH HOH A . 
B 2 HOH 401 801 322 HOH HOH A . 
B 2 HOH 402 802 305 HOH HOH A . 
B 2 HOH 403 803 280 HOH HOH A . 
B 2 HOH 404 804 309 HOH HOH A . 
B 2 HOH 405 805 447 HOH HOH A . 
B 2 HOH 406 806 308 HOH HOH A . 
B 2 HOH 407 807 291 HOH HOH A . 
B 2 HOH 408 808 172 HOH HOH A . 
B 2 HOH 409 809 424 HOH HOH A . 
B 2 HOH 410 810 228 HOH HOH A . 
B 2 HOH 411 811 452 HOH HOH A . 
B 2 HOH 412 812 383 HOH HOH A . 
B 2 HOH 413 813 166 HOH HOH A . 
B 2 HOH 414 814 320 HOH HOH A . 
B 2 HOH 415 815 446 HOH HOH A . 
B 2 HOH 416 816 234 HOH HOH A . 
B 2 HOH 417 817 297 HOH HOH A . 
B 2 HOH 418 818 407 HOH HOH A . 
B 2 HOH 419 819 269 HOH HOH A . 
B 2 HOH 420 820 225 HOH HOH A . 
B 2 HOH 421 821 262 HOH HOH A . 
B 2 HOH 422 822 317 HOH HOH A . 
B 2 HOH 423 823 521 HOH HOH A . 
B 2 HOH 424 824 519 HOH HOH A . 
B 2 HOH 425 825 139 HOH HOH A . 
B 2 HOH 426 826 456 HOH HOH A . 
B 2 HOH 427 827 418 HOH HOH A . 
B 2 HOH 428 828 468 HOH HOH A . 
B 2 HOH 429 829 246 HOH HOH A . 
B 2 HOH 430 830 404 HOH HOH A . 
B 2 HOH 431 831 336 HOH HOH A . 
B 2 HOH 432 832 324 HOH HOH A . 
B 2 HOH 433 833 511 HOH HOH A . 
B 2 HOH 434 834 361 HOH HOH A . 
B 2 HOH 435 835 494 HOH HOH A . 
B 2 HOH 436 836 372 HOH HOH A . 
B 2 HOH 437 837 196 HOH HOH A . 
B 2 HOH 438 838 251 HOH HOH A . 
B 2 HOH 439 839 406 HOH HOH A . 
B 2 HOH 440 840 485 HOH HOH A . 
B 2 HOH 441 841 321 HOH HOH A . 
B 2 HOH 442 842 255 HOH HOH A . 
B 2 HOH 443 843 250 HOH HOH A . 
B 2 HOH 444 844 384 HOH HOH A . 
B 2 HOH 445 845 120 HOH HOH A . 
B 2 HOH 446 846 510 HOH HOH A . 
B 2 HOH 447 847 356 HOH HOH A . 
B 2 HOH 448 848 486 HOH HOH A . 
B 2 HOH 449 849 203 HOH HOH A . 
B 2 HOH 450 850 515 HOH HOH A . 
B 2 HOH 451 851 266 HOH HOH A . 
B 2 HOH 452 852 509 HOH HOH A . 
B 2 HOH 453 853 141 HOH HOH A . 
B 2 HOH 454 854 450 HOH HOH A . 
B 2 HOH 455 855 271 HOH HOH A . 
B 2 HOH 456 856 337 HOH HOH A . 
B 2 HOH 457 857 231 HOH HOH A . 
B 2 HOH 458 858 415 HOH HOH A . 
B 2 HOH 459 859 429 HOH HOH A . 
B 2 HOH 460 860 281 HOH HOH A . 
B 2 HOH 461 861 474 HOH HOH A . 
B 2 HOH 462 862 466 HOH HOH A . 
B 2 HOH 463 863 437 HOH HOH A . 
B 2 HOH 464 864 522 HOH HOH A . 
B 2 HOH 465 865 460 HOH HOH A . 
B 2 HOH 466 866 483 HOH HOH A . 
B 2 HOH 467 867 226 HOH HOH A . 
B 2 HOH 468 868 216 HOH HOH A . 
B 2 HOH 469 869 252 HOH HOH A . 
B 2 HOH 470 870 243 HOH HOH A . 
B 2 HOH 471 871 496 HOH HOH A . 
B 2 HOH 472 872 143 HOH HOH A . 
B 2 HOH 473 873 180 HOH HOH A . 
B 2 HOH 474 874 385 HOH HOH A . 
B 2 HOH 475 875 473 HOH HOH A . 
B 2 HOH 476 876 198 HOH HOH A . 
B 2 HOH 477 877 194 HOH HOH A . 
B 2 HOH 478 878 76  HOH HOH A . 
B 2 HOH 479 879 373 HOH HOH A . 
B 2 HOH 480 880 315 HOH HOH A . 
B 2 HOH 481 881 85  HOH HOH A . 
B 2 HOH 482 882 469 HOH HOH A . 
B 2 HOH 483 883 453 HOH HOH A . 
B 2 HOH 484 884 165 HOH HOH A . 
B 2 HOH 485 885 503 HOH HOH A . 
B 2 HOH 486 886 153 HOH HOH A . 
B 2 HOH 487 887 158 HOH HOH A . 
B 2 HOH 488 888 430 HOH HOH A . 
B 2 HOH 489 889 233 HOH HOH A . 
B 2 HOH 490 890 410 HOH HOH A . 
B 2 HOH 491 891 227 HOH HOH A . 
B 2 HOH 492 892 236 HOH HOH A . 
B 2 HOH 493 893 512 HOH HOH A . 
B 2 HOH 494 894 432 HOH HOH A . 
B 2 HOH 495 895 325 HOH HOH A . 
B 2 HOH 496 896 517 HOH HOH A . 
B 2 HOH 497 897 448 HOH HOH A . 
B 2 HOH 498 898 237 HOH HOH A . 
B 2 HOH 499 899 487 HOH HOH A . 
B 2 HOH 500 900 355 HOH HOH A . 
B 2 HOH 501 901 287 HOH HOH A . 
B 2 HOH 502 902 219 HOH HOH A . 
B 2 HOH 503 903 393 HOH HOH A . 
B 2 HOH 504 904 260 HOH HOH A . 
B 2 HOH 505 905 506 HOH HOH A . 
B 2 HOH 506 906 402 HOH HOH A . 
B 2 HOH 507 907 479 HOH HOH A . 
B 2 HOH 508 908 292 HOH HOH A . 
B 2 HOH 509 909 513 HOH HOH A . 
B 2 HOH 510 910 464 HOH HOH A . 
B 2 HOH 511 911 338 HOH HOH A . 
B 2 HOH 512 912 493 HOH HOH A . 
B 2 HOH 513 913 395 HOH HOH A . 
B 2 HOH 514 914 458 HOH HOH A . 
B 2 HOH 515 915 459 HOH HOH A . 
B 2 HOH 516 916 492 HOH HOH A . 
B 2 HOH 517 917 471 HOH HOH A . 
# 
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 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .               1 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? 1.20.1-4487-000 2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .               3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .               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                     9JOC 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     84.449 
_cell.length_a_esd                 ? 
_cell.length_b                     84.449 
_cell.length_b_esd                 ? 
_cell.length_c                     93.114 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        6 
_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                         9JOC 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                173 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 63' 
_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                   9JOC 
_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             2.16 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          42.96 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.2M Ammonium chloride, 20% w/v Polyethylene glycol 3,350, pH 6.3' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            290 
# 
_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         2021-10-18 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.97918 
_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 BL19U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97918 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL19U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9JOC 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.29 
_reflns.d_resolution_low                               73.13 
_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                                     93037 
_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                           98.7 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                8.7 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          25.1 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.79 
_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                                0.044 
_reflns.pdbx_Rpim_I_all                                0.014 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.042 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.29 
_reflns_shell.d_res_low                                     1.36 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           46926 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             12605 
_reflns_shell.percent_possible_obs                          92.0 
_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                               3.7 
_reflns_shell.pdbx_chi_squared                              0.43 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     2.7 
_reflns_shell.pdbx_Rrim_I_all                               0.435 
_reflns_shell.pdbx_Rpim_I_all                               0.218 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.886 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.374 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9JOC 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.29 
_refine.ls_d_res_low                             31.28 
_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                     93037 
_refine.ls_number_reflns_R_free                  3901 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    97.46 
_refine.ls_percent_reflns_R_free                 2.15 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1373 
_refine.ls_R_factor_R_free                       0.1565 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1369 
_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                          1.39 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 16.95 
_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                            0.10 
_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.pdbx_number_atoms_protein        2945 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         0 
_refine_hist.number_atoms_solvent             517 
_refine_hist.number_atoms_total               3462 
_refine_hist.d_res_high                       1.29 
_refine_hist.d_res_low                        31.28 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.010 ? 3028 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.098 ? 4110 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 5.911 ? 402  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.088 ? 448  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.010 ? 531  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.29 1.31 . . 119 5164 80.00  . . . . 0.2451 . . . . . . . . . . . 0.2597 
'X-RAY DIFFRACTION' 1.31 1.32 . . 107 5573 85.00  . . . . 0.2338 . . . . . . . . . . . 0.2462 
'X-RAY DIFFRACTION' 1.32 1.34 . . 112 5723 88.00  . . . . 0.2180 . . . . . . . . . . . 0.2306 
'X-RAY DIFFRACTION' 1.34 1.36 . . 130 5972 91.00  . . . . 0.2009 . . . . . . . . . . . 0.2171 
'X-RAY DIFFRACTION' 1.36 1.38 . . 137 6127 94.00  . . . . 0.1935 . . . . . . . . . . . 0.2212 
'X-RAY DIFFRACTION' 1.38 1.40 . . 143 6298 97.00  . . . . 0.1896 . . . . . . . . . . . 0.1956 
'X-RAY DIFFRACTION' 1.40 1.42 . . 140 6396 98.00  . . . . 0.1681 . . . . . . . . . . . 0.1775 
'X-RAY DIFFRACTION' 1.42 1.44 . . 136 6474 99.00  . . . . 0.1615 . . . . . . . . . . . 0.1631 
'X-RAY DIFFRACTION' 1.44 1.47 . . 148 6445 99.00  . . . . 0.1540 . . . . . . . . . . . 0.1581 
'X-RAY DIFFRACTION' 1.47 1.50 . . 148 6562 100.00 . . . . 0.1455 . . . . . . . . . . . 0.1980 
'X-RAY DIFFRACTION' 1.50 1.53 . . 146 6459 100.00 . . . . 0.1395 . . . . . . . . . . . 0.1530 
'X-RAY DIFFRACTION' 1.53 1.56 . . 142 6520 100.00 . . . . 0.1375 . . . . . . . . . . . 0.1803 
'X-RAY DIFFRACTION' 1.56 1.59 . . 148 6532 100.00 . . . . 0.1366 . . . . . . . . . . . 0.1799 
'X-RAY DIFFRACTION' 1.59 1.63 . . 142 6489 100.00 . . . . 0.1316 . . . . . . . . . . . 0.1449 
'X-RAY DIFFRACTION' 1.63 1.67 . . 141 6502 100.00 . . . . 0.1401 . . . . . . . . . . . 0.1529 
'X-RAY DIFFRACTION' 1.67 1.71 . . 144 6457 100.00 . . . . 0.1380 . . . . . . . . . . . 0.1776 
'X-RAY DIFFRACTION' 1.71 1.76 . . 143 6565 100.00 . . . . 0.1344 . . . . . . . . . . . 0.1408 
'X-RAY DIFFRACTION' 1.76 1.82 . . 144 6487 100.00 . . . . 0.1310 . . . . . . . . . . . 0.1310 
'X-RAY DIFFRACTION' 1.82 1.89 . . 143 6499 100.00 . . . . 0.1378 . . . . . . . . . . . 0.1751 
'X-RAY DIFFRACTION' 1.89 1.96 . . 150 6502 100.00 . . . . 0.1307 . . . . . . . . . . . 0.1450 
'X-RAY DIFFRACTION' 1.96 2.05 . . 142 6515 100.00 . . . . 0.1217 . . . . . . . . . . . 0.1548 
'X-RAY DIFFRACTION' 2.05 2.16 . . 134 6533 100.00 . . . . 0.1237 . . . . . . . . . . . 0.1237 
'X-RAY DIFFRACTION' 2.16 2.29 . . 142 6500 100.00 . . . . 0.1260 . . . . . . . . . . . 0.1484 
'X-RAY DIFFRACTION' 2.29 2.47 . . 138 6547 100.00 . . . . 0.1282 . . . . . . . . . . . 0.1468 
'X-RAY DIFFRACTION' 2.47 2.72 . . 150 6514 100.00 . . . . 0.1323 . . . . . . . . . . . 0.1739 
'X-RAY DIFFRACTION' 2.72 3.11 . . 142 6494 100.00 . . . . 0.1366 . . . . . . . . . . . 0.1659 
'X-RAY DIFFRACTION' 3.11 3.92 . . 146 6490 100.00 . . . . 0.1236 . . . . . . . . . . . 0.1385 
'X-RAY DIFFRACTION' 3.92 10   . . 144 6504 100.00 . . . . 0.1369 . . . . . . . . . . . 0.1496 
# 
_struct.entry_id                     9JOC 
_struct.title                        'CRYSTAL STRUCTURE OF ENDO-1,3-FUCANASE (FUN168D) FROM GH168 FAMILY' 
_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        9JOC 
_struct_keywords.text            'Endo-1.3-fucanase, GH168, HYDROLASE' 
_struct_keywords.pdbx_keywords   HYDROLASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A0A1B1Y6G8_9FLAO 
_struct_ref.pdbx_db_accession          A0A1B1Y6G8 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;STKNGIIELEQETEEELEQNQEIDYSNYPEFSWDTMPLYMHVRKNTAYTDEEINYLASFPLITLEKSQAQNTYGSTEEGT
LATASAIKLKNNKAKVLYYRNVVINWGNYKNDDEFISKNPSALLKNQNNELVYMPNGSTPFFDITKSFVQEYWLKSVEDM
VATPNIDGTFIDANIKVLVPSFFSSKVGVNKQAEIENSYFSMMSRLKESLSNNLILANIIRVRPEFEENGLEYLGYFNGS
YLEGFDSEAFGMSNAEYLVEGIEATQKAAQSGKIITMTLGLGEAIDNNTGIDDQREDVDLNDEELNKRVDYLLAIFLICA
EKYSYVYLHDGYLATNSAVWLHQFDQYKKALGAPLGKAIKNGYIYTRKFENLDVWLNLETQTATLTWKE
;
_struct_ref.pdbx_align_begin           22 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9JOC 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 389 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             A0A1B1Y6G8 
_struct_ref_seq.db_align_beg                  22 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  410 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       389 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_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 THR A 49  ? SER A 58  ? THR A 49  SER A 58  1 ? 10 
HELX_P HELX_P2  AA2 ALA A 69  ? GLY A 74  ? ALA A 69  GLY A 74  1 ? 6  
HELX_P HELX_P3  AA3 SER A 75  ? ASN A 91  ? SER A 75  ASN A 91  1 ? 17 
HELX_P HELX_P4  AA4 TYR A 109 ? ASN A 119 ? TYR A 109 ASN A 119 1 ? 11 
HELX_P HELX_P5  AA5 PRO A 120 ? LEU A 123 ? PRO A 120 LEU A 123 5 ? 4  
HELX_P HELX_P6  AA6 LYS A 146 ? ALA A 162 ? LYS A 146 ALA A 162 1 ? 17 
HELX_P HELX_P7  AA7 ALA A 173 ? VAL A 179 ? ALA A 173 VAL A 179 1 ? 7  
HELX_P HELX_P8  AA8 VAL A 179 ? GLY A 188 ? VAL A 179 GLY A 188 1 ? 10 
HELX_P HELX_P9  AA9 GLY A 188 ? LEU A 210 ? GLY A 188 LEU A 210 1 ? 23 
HELX_P HELX_P10 AB1 GLY A 230 ? PHE A 237 ? GLY A 230 PHE A 237 5 ? 8  
HELX_P HELX_P11 AB2 SER A 253 ? SER A 271 ? SER A 253 SER A 271 1 ? 19 
HELX_P HELX_P12 AB3 ASN A 301 ? ALA A 320 ? ASN A 301 ALA A 320 1 ? 20 
HELX_P HELX_P13 AB4 LEU A 333 ? SER A 337 ? LEU A 333 SER A 337 5 ? 5  
HELX_P HELX_P14 AB5 PHE A 344 ? LYS A 348 ? PHE A 344 LYS A 348 5 ? 5  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 8 ? 
AA2 ? 4 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel      
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA1 4 5 ? parallel      
AA1 5 6 ? parallel      
AA1 6 7 ? parallel      
AA1 7 8 ? parallel      
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? 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 TYR A 39  ? VAL A 42  ? TYR A 39  VAL A 42  
AA1 2 LEU A 61  ? LEU A 64  ? LEU A 61  LEU A 64  
AA1 3 LYS A 95  ? ASN A 101 ? LYS A 95  ASN A 101 
AA1 4 GLY A 168 ? ASP A 172 ? GLY A 168 ASP A 172 
AA1 5 LEU A 214 ? ASN A 218 ? LEU A 214 ASN A 218 
AA1 6 GLY A 239 ? LEU A 242 ? GLY A 239 LEU A 242 
AA1 7 ILE A 274 ? GLY A 280 ? ILE A 274 GLY A 280 
AA1 8 SER A 324 ? HIS A 329 ? SER A 324 HIS A 329 
AA2 1 ILE A 359 ? ASN A 361 ? ILE A 359 ASN A 361 
AA2 2 ILE A 364 ? PHE A 369 ? ILE A 364 PHE A 369 
AA2 3 LEU A 372 ? ASN A 377 ? LEU A 372 ASN A 377 
AA2 4 THR A 382 ? TRP A 387 ? THR A 382 TRP A 387 
# 
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 42  ? N VAL A 42  O THR A 63  ? O THR A 63  
AA1 2 3 N ILE A 62  ? N ILE A 62  O LEU A 97  ? O LEU A 97  
AA1 3 4 N ARG A 100 ? N ARG A 100 O PHE A 170 ? O PHE A 170 
AA1 4 5 N ILE A 171 ? N ILE A 171 O LEU A 216 ? O LEU A 216 
AA1 5 6 N ALA A 217 ? N ALA A 217 O TYR A 241 ? O TYR A 241 
AA1 6 7 N SER A 240 ? N SER A 240 O ILE A 274 ? O ILE A 274 
AA1 7 8 N ILE A 275 ? N ILE A 275 O TYR A 325 ? O TYR A 325 
AA2 1 2 N ASN A 361 ? N ASN A 361 O ILE A 364 ? O ILE A 364 
AA2 2 3 N PHE A 369 ? N PHE A 369 O LEU A 372 ? O LEU A 372 
AA2 3 4 N ASN A 377 ? N ASN A 377 O THR A 382 ? O THR A 382 
# 
_pdbx_entry_details.entry_id                   9JOC 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1  1 HZ2 A LYS 368 ? ? O A HOH 401 ? ? 1.25 
2  1 NZ  A LYS 368 ? ? O A HOH 401 ? ? 1.66 
3  1 O   A HOH 417 ? ? O A HOH 478 ? ? 1.80 
4  1 O   A HOH 667 ? ? O A HOH 811 ? ? 1.94 
5  1 O   A HOH 653 ? ? O A HOH 746 ? ? 1.96 
6  1 O   A HOH 689 ? ? O A HOH 771 ? ? 2.00 
7  1 O   A HOH 682 ? ? O A HOH 787 ? ? 2.01 
8  1 O   A HOH 465 ? ? O A HOH 824 ? ? 2.06 
9  1 O   A HOH 783 ? ? O A HOH 829 ? ? 2.12 
10 1 O   A HOH 658 ? ? O A HOH 702 ? ? 2.18 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 HE21 A GLN 127 ? ? 1_555 HD22 A ASN 336 ? ? 3_655 1.33 
2 1 O    A HOH 412 ? ? 1_555 O    A HOH 570 ? ? 2_545 2.07 
3 1 O    A HOH 840 ? ? 1_555 O    A HOH 910 ? ? 2_545 2.08 
4 1 O    A HOH 807 ? ? 1_555 O    A HOH 845 ? ? 4_655 2.10 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             CB 
_pdbx_validate_rmsd_angle.auth_asym_id_1             A 
_pdbx_validate_rmsd_angle.auth_comp_id_1             TYR 
_pdbx_validate_rmsd_angle.auth_seq_id_1              327 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             CG 
_pdbx_validate_rmsd_angle.auth_asym_id_2             A 
_pdbx_validate_rmsd_angle.auth_comp_id_2             TYR 
_pdbx_validate_rmsd_angle.auth_seq_id_2              327 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             CD2 
_pdbx_validate_rmsd_angle.auth_asym_id_3             A 
_pdbx_validate_rmsd_angle.auth_comp_id_3             TYR 
_pdbx_validate_rmsd_angle.auth_seq_id_3              327 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                117.06 
_pdbx_validate_rmsd_angle.angle_target_value         121.00 
_pdbx_validate_rmsd_angle.angle_deviation            -3.94 
_pdbx_validate_rmsd_angle.angle_standard_deviation   0.60 
_pdbx_validate_rmsd_angle.linker_flag                N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASN A 287 ? ? -161.71 115.18 
2 1 ASP A 292 ? ? 69.86   178.67 
3 1 ASP A 293 ? ? -161.11 55.60  
4 1 ASP A 330 ? ? -115.07 57.39  
5 1 LEU A 351 ? ? -107.90 -66.10 
# 
_pdbx_struct_special_symmetry.id              1 
_pdbx_struct_special_symmetry.PDB_model_num   1 
_pdbx_struct_special_symmetry.auth_asym_id    A 
_pdbx_struct_special_symmetry.auth_comp_id    HOH 
_pdbx_struct_special_symmetry.auth_seq_id     917 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   B 
_pdbx_struct_special_symmetry.label_comp_id   HOH 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1 'X-RAY DIFFRACTION' ? refined 23.4244 2.6400  -10.2898 0.1238 ? 0.0245  ? -0.0234 ? 0.1440 ? -0.0017 ? 0.1118 ? 1.4020 ? -0.8372 
? -0.5686 ? 1.4871 ? 0.8609  ? 1.7790 ? 0.0769  ? 0.2025  ? 0.0181  ? -0.1303 ? -0.1007 ? 0.0289  ? -0.1651 ? -0.1273 ? 0.0250  ? 
2 'X-RAY DIFFRACTION' ? refined 42.6050 -5.5673 -10.0712 0.1026 ? -0.0049 ? 0.0017  ? 0.0891 ? 0.0015  ? 0.0971 ? 1.5004 ? -0.5849 
? -0.1864 ? 0.8124 ? 0.1394  ? 0.8793 ? -0.0111 ? 0.0573  ? -0.0478 ? -0.0277 ? -0.0113 ? -0.0001 ? -0.0036 ? -0.0295 ? 0.0091  ? 
3 'X-RAY DIFFRACTION' ? refined 50.6429 2.7619  -5.5520  0.1319 ? -0.0084 ? -0.0044 ? 0.1276 ? -0.0074 ? 0.1548 ? 2.5289 ? -1.4527 
? 0.4478  ? 2.1561 ? -0.6969 ? 1.9191 ? 0.0056  ? 0.0943  ? 0.2352  ? 0.0191  ? -0.0202 ? -0.1707 ? -0.1313 ? 0.1468  ? 0.0062  ? 
4 'X-RAY DIFFRACTION' ? refined 38.6275 3.7533  5.2968   0.1315 ? 0.0166  ? -0.0092 ? 0.1298 ? -0.0213 ? 0.1409 ? 0.7474 ? 0.2201  
? -0.5659 ? 1.0149 ? -0.5934 ? 2.0340 ? 0.0017  ? -0.0786 ? 0.0307  ? 0.0132  ? -0.0126 ? -0.1025 ? 0.0009  ? 0.1421  ? 0.0082  ? 
5 'X-RAY DIFFRACTION' ? refined 31.8596 2.3164  10.8598  0.1223 ? 0.0164  ? -0.0070 ? 0.1255 ? -0.0129 ? 0.1293 ? 1.0613 ? -0.0549 
? -0.1636 ? 0.8443 ? -0.0867 ? 1.7920 ? 0.0263  ? -0.0651 ? -0.0524 ? 0.0734  ? -0.0320 ? -0.0503 ? 0.0498  ? 0.1124  ? 0.0120  ? 
6 'X-RAY DIFFRACTION' ? refined 20.2529 -3.2723 10.3666  0.1199 ? -0.0055 ? -0.0046 ? 0.1220 ? -0.0049 ? 0.1274 ? 1.8447 ? 0.1782  
? -0.1688 ? 1.9238 ? 0.5684  ? 1.5291 ? -0.0239 ? -0.0199 ? -0.1857 ? 0.0724  ? -0.0548 ? 0.2056  ? 0.1585  ? -0.1286 ? 0.0753  ? 
7 'X-RAY DIFFRACTION' ? refined 18.9409 4.3460  2.9214   0.1246 ? 0.0214  ? -0.0141 ? 0.1377 ? -0.0142 ? 0.1200 ? 0.7562 ? -0.2161 
? -0.0456 ? 1.7313 ? 0.8583  ? 1.1545 ? 0.0209  ? 0.0427  ? 0.0046  ? -0.0082 ? -0.1217 ? 0.2022  ? -0.0399 ? -0.1965 ? 0.0999  ? 
8 'X-RAY DIFFRACTION' ? refined 19.8459 9.2033  18.8840  0.1077 ? 0.0161  ? 0.0085  ? 0.1150 ? -0.0254 ? 0.1160 ? 1.8499 ? -0.0009 
? 0.9821  ? 1.8094 ? -0.7574 ? 3.0712 ? -0.0104 ? -0.0673 ? 0.0484  ? 0.0665  ? 0.0364  ? 0.1663  ? -0.1530 ? -0.2100 ? -0.0145 ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_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 
1 'X-RAY DIFFRACTION' 1 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 23 through 90 )
;
2 'X-RAY DIFFRACTION' 2 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 91 through 188 )
;
3 'X-RAY DIFFRACTION' 3 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 189 through 209 )
;
4 'X-RAY DIFFRACTION' 4 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 210 through 253 )
;
5 'X-RAY DIFFRACTION' 5 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 254 through 290 )
;
6 'X-RAY DIFFRACTION' 6 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 291 through 319 )
;
7 'X-RAY DIFFRACTION' 7 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 320 through 358 )
;
8 'X-RAY DIFFRACTION' 8 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 359 through 388 )
;
# 
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 913 ? 5.81 . 
2 1 O ? A HOH 914 ? 6.61 . 
3 1 O ? A HOH 915 ? 6.79 . 
4 1 O ? A HOH 916 ? 8.55 . 
5 1 O ? A HOH 917 ? 9.95 . 
# 
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 SER 1   ? A SER 1   
2  1 Y 1 A THR 2   ? A THR 2   
3  1 Y 1 A LYS 3   ? A LYS 3   
4  1 Y 1 A ASN 4   ? A ASN 4   
5  1 Y 1 A GLY 5   ? A GLY 5   
6  1 Y 1 A ILE 6   ? A ILE 6   
7  1 Y 1 A ILE 7   ? A ILE 7   
8  1 Y 1 A GLU 8   ? A GLU 8   
9  1 Y 1 A LEU 9   ? A LEU 9   
10 1 Y 1 A GLU 10  ? A GLU 10  
11 1 Y 1 A GLN 11  ? A GLN 11  
12 1 Y 1 A GLU 12  ? A GLU 12  
13 1 Y 1 A THR 13  ? A THR 13  
14 1 Y 1 A GLU 14  ? A GLU 14  
15 1 Y 1 A GLU 15  ? A GLU 15  
16 1 Y 1 A GLU 16  ? A GLU 16  
17 1 Y 1 A LEU 17  ? A LEU 17  
18 1 Y 1 A GLU 18  ? A GLU 18  
19 1 Y 1 A GLN 19  ? A GLN 19  
20 1 Y 1 A ASN 20  ? A ASN 20  
21 1 Y 1 A GLN 21  ? A GLN 21  
22 1 Y 1 A GLU 22  ? A GLU 22  
23 1 Y 1 A GLU 389 ? A GLU 389 
# 
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 
LYS N    N N N 205 
LYS CA   C N S 206 
LYS C    C N N 207 
LYS O    O N N 208 
LYS CB   C N N 209 
LYS CG   C N N 210 
LYS CD   C N N 211 
LYS CE   C N N 212 
LYS NZ   N N N 213 
LYS OXT  O N N 214 
LYS H    H N N 215 
LYS H2   H N N 216 
LYS HA   H N N 217 
LYS HB2  H N N 218 
LYS HB3  H N N 219 
LYS HG2  H N N 220 
LYS HG3  H N N 221 
LYS HD2  H N N 222 
LYS HD3  H N N 223 
LYS HE2  H N N 224 
LYS HE3  H N N 225 
LYS HZ1  H N N 226 
LYS HZ2  H N N 227 
LYS HZ3  H N N 228 
LYS HXT  H N N 229 
MET N    N N N 230 
MET CA   C N S 231 
MET C    C N N 232 
MET O    O N N 233 
MET CB   C N N 234 
MET CG   C N N 235 
MET SD   S N N 236 
MET CE   C N N 237 
MET OXT  O N N 238 
MET H    H N N 239 
MET H2   H N N 240 
MET HA   H N N 241 
MET HB2  H N N 242 
MET HB3  H N N 243 
MET HG2  H N N 244 
MET HG3  H N N 245 
MET HE1  H N N 246 
MET HE2  H N N 247 
MET HE3  H N N 248 
MET HXT  H N N 249 
PHE N    N N N 250 
PHE CA   C N S 251 
PHE C    C N N 252 
PHE O    O N N 253 
PHE CB   C N N 254 
PHE CG   C Y N 255 
PHE CD1  C Y N 256 
PHE CD2  C Y N 257 
PHE CE1  C Y N 258 
PHE CE2  C Y N 259 
PHE CZ   C Y N 260 
PHE OXT  O N N 261 
PHE H    H N N 262 
PHE H2   H N N 263 
PHE HA   H N N 264 
PHE HB2  H N N 265 
PHE HB3  H N N 266 
PHE HD1  H N N 267 
PHE HD2  H N N 268 
PHE HE1  H N N 269 
PHE HE2  H N N 270 
PHE HZ   H N N 271 
PHE HXT  H N N 272 
PRO N    N N N 273 
PRO CA   C N S 274 
PRO C    C N N 275 
PRO O    O N N 276 
PRO CB   C N N 277 
PRO CG   C N N 278 
PRO CD   C N N 279 
PRO OXT  O N N 280 
PRO H    H N N 281 
PRO HA   H N N 282 
PRO HB2  H N N 283 
PRO HB3  H N N 284 
PRO HG2  H N N 285 
PRO HG3  H N N 286 
PRO HD2  H N N 287 
PRO HD3  H N N 288 
PRO HXT  H N N 289 
SER N    N N N 290 
SER CA   C N S 291 
SER C    C N N 292 
SER O    O N N 293 
SER CB   C N N 294 
SER OG   O N N 295 
SER OXT  O N N 296 
SER H    H N N 297 
SER H2   H N N 298 
SER HA   H N N 299 
SER HB2  H N N 300 
SER HB3  H N N 301 
SER HG   H N N 302 
SER HXT  H N N 303 
THR N    N N N 304 
THR CA   C N S 305 
THR C    C N N 306 
THR O    O N N 307 
THR CB   C N R 308 
THR OG1  O N N 309 
THR CG2  C N N 310 
THR OXT  O N N 311 
THR H    H N N 312 
THR H2   H N N 313 
THR HA   H N N 314 
THR HB   H N N 315 
THR HG1  H N N 316 
THR HG21 H N N 317 
THR HG22 H N N 318 
THR HG23 H N N 319 
THR HXT  H N N 320 
TRP N    N N N 321 
TRP CA   C N S 322 
TRP C    C N N 323 
TRP O    O N N 324 
TRP CB   C N N 325 
TRP CG   C Y N 326 
TRP CD1  C Y N 327 
TRP CD2  C Y N 328 
TRP NE1  N Y N 329 
TRP CE2  C Y N 330 
TRP CE3  C Y N 331 
TRP CZ2  C Y N 332 
TRP CZ3  C Y N 333 
TRP CH2  C Y N 334 
TRP OXT  O N N 335 
TRP H    H N N 336 
TRP H2   H N N 337 
TRP HA   H N N 338 
TRP HB2  H N N 339 
TRP HB3  H N N 340 
TRP HD1  H N N 341 
TRP HE1  H N N 342 
TRP HE3  H N N 343 
TRP HZ2  H N N 344 
TRP HZ3  H N N 345 
TRP HH2  H N N 346 
TRP HXT  H N N 347 
TYR N    N N N 348 
TYR CA   C N S 349 
TYR C    C N N 350 
TYR O    O N N 351 
TYR CB   C N N 352 
TYR CG   C Y N 353 
TYR CD1  C Y N 354 
TYR CD2  C Y N 355 
TYR CE1  C Y N 356 
TYR CE2  C Y N 357 
TYR CZ   C Y N 358 
TYR OH   O N N 359 
TYR OXT  O N N 360 
TYR H    H N N 361 
TYR H2   H N N 362 
TYR HA   H N N 363 
TYR HB2  H N N 364 
TYR HB3  H N N 365 
TYR HD1  H N N 366 
TYR HD2  H N N 367 
TYR HE1  H N N 368 
TYR HE2  H N N 369 
TYR HH   H N N 370 
TYR HXT  H N N 371 
VAL N    N N N 372 
VAL CA   C N S 373 
VAL C    C N N 374 
VAL O    O N N 375 
VAL CB   C N N 376 
VAL CG1  C N N 377 
VAL CG2  C N N 378 
VAL OXT  O N N 379 
VAL H    H N N 380 
VAL H2   H N N 381 
VAL HA   H N N 382 
VAL HB   H N N 383 
VAL HG11 H N N 384 
VAL HG12 H N N 385 
VAL HG13 H N N 386 
VAL HG21 H N N 387 
VAL HG22 H N N 388 
VAL HG23 H N N 389 
VAL HXT  H N N 390 
# 
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 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
MET N   CA   sing N N 218 
MET N   H    sing N N 219 
MET N   H2   sing N N 220 
MET CA  C    sing N N 221 
MET CA  CB   sing N N 222 
MET CA  HA   sing N N 223 
MET C   O    doub N N 224 
MET C   OXT  sing N N 225 
MET CB  CG   sing N N 226 
MET CB  HB2  sing N N 227 
MET CB  HB3  sing N N 228 
MET CG  SD   sing N N 229 
MET CG  HG2  sing N N 230 
MET CG  HG3  sing N N 231 
MET SD  CE   sing N N 232 
MET CE  HE1  sing N N 233 
MET CE  HE2  sing N N 234 
MET CE  HE3  sing N N 235 
MET OXT HXT  sing N N 236 
PHE N   CA   sing N N 237 
PHE N   H    sing N N 238 
PHE N   H2   sing N N 239 
PHE CA  C    sing N N 240 
PHE CA  CB   sing N N 241 
PHE CA  HA   sing N N 242 
PHE C   O    doub N N 243 
PHE C   OXT  sing N N 244 
PHE CB  CG   sing N N 245 
PHE CB  HB2  sing N N 246 
PHE CB  HB3  sing N N 247 
PHE CG  CD1  doub Y N 248 
PHE CG  CD2  sing Y N 249 
PHE CD1 CE1  sing Y N 250 
PHE CD1 HD1  sing N N 251 
PHE CD2 CE2  doub Y N 252 
PHE CD2 HD2  sing N N 253 
PHE CE1 CZ   doub Y N 254 
PHE CE1 HE1  sing N N 255 
PHE CE2 CZ   sing Y N 256 
PHE CE2 HE2  sing N N 257 
PHE CZ  HZ   sing N N 258 
PHE OXT HXT  sing N N 259 
PRO N   CA   sing N N 260 
PRO N   CD   sing N N 261 
PRO N   H    sing N N 262 
PRO CA  C    sing N N 263 
PRO CA  CB   sing N N 264 
PRO CA  HA   sing N N 265 
PRO C   O    doub N N 266 
PRO C   OXT  sing N N 267 
PRO CB  CG   sing N N 268 
PRO CB  HB2  sing N N 269 
PRO CB  HB3  sing N N 270 
PRO CG  CD   sing N N 271 
PRO CG  HG2  sing N N 272 
PRO CG  HG3  sing N N 273 
PRO CD  HD2  sing N N 274 
PRO CD  HD3  sing N N 275 
PRO OXT HXT  sing N N 276 
SER N   CA   sing N N 277 
SER N   H    sing N N 278 
SER N   H2   sing N N 279 
SER CA  C    sing N N 280 
SER CA  CB   sing N N 281 
SER CA  HA   sing N N 282 
SER C   O    doub N N 283 
SER C   OXT  sing N N 284 
SER CB  OG   sing N N 285 
SER CB  HB2  sing N N 286 
SER CB  HB3  sing N N 287 
SER OG  HG   sing N N 288 
SER OXT HXT  sing N N 289 
THR N   CA   sing N N 290 
THR N   H    sing N N 291 
THR N   H2   sing N N 292 
THR CA  C    sing N N 293 
THR CA  CB   sing N N 294 
THR CA  HA   sing N N 295 
THR C   O    doub N N 296 
THR C   OXT  sing N N 297 
THR CB  OG1  sing N N 298 
THR CB  CG2  sing N N 299 
THR CB  HB   sing N N 300 
THR OG1 HG1  sing N N 301 
THR CG2 HG21 sing N N 302 
THR CG2 HG22 sing N N 303 
THR CG2 HG23 sing N N 304 
THR OXT HXT  sing N N 305 
TRP N   CA   sing N N 306 
TRP N   H    sing N N 307 
TRP N   H2   sing N N 308 
TRP CA  C    sing N N 309 
TRP CA  CB   sing N N 310 
TRP CA  HA   sing N N 311 
TRP C   O    doub N N 312 
TRP C   OXT  sing N N 313 
TRP CB  CG   sing N N 314 
TRP CB  HB2  sing N N 315 
TRP CB  HB3  sing N N 316 
TRP CG  CD1  doub Y N 317 
TRP CG  CD2  sing Y N 318 
TRP CD1 NE1  sing Y N 319 
TRP CD1 HD1  sing N N 320 
TRP CD2 CE2  doub Y N 321 
TRP CD2 CE3  sing Y N 322 
TRP NE1 CE2  sing Y N 323 
TRP NE1 HE1  sing N N 324 
TRP CE2 CZ2  sing Y N 325 
TRP CE3 CZ3  doub Y N 326 
TRP CE3 HE3  sing N N 327 
TRP CZ2 CH2  doub Y N 328 
TRP CZ2 HZ2  sing N N 329 
TRP CZ3 CH2  sing Y N 330 
TRP CZ3 HZ3  sing N N 331 
TRP CH2 HH2  sing N N 332 
TRP OXT HXT  sing N N 333 
TYR N   CA   sing N N 334 
TYR N   H    sing N N 335 
TYR N   H2   sing N N 336 
TYR CA  C    sing N N 337 
TYR CA  CB   sing N N 338 
TYR CA  HA   sing N N 339 
TYR C   O    doub N N 340 
TYR C   OXT  sing N N 341 
TYR CB  CG   sing N N 342 
TYR CB  HB2  sing N N 343 
TYR CB  HB3  sing N N 344 
TYR CG  CD1  doub Y N 345 
TYR CG  CD2  sing Y N 346 
TYR CD1 CE1  sing Y N 347 
TYR CD1 HD1  sing N N 348 
TYR CD2 CE2  doub Y N 349 
TYR CD2 HD2  sing N N 350 
TYR CE1 CZ   doub Y N 351 
TYR CE1 HE1  sing N N 352 
TYR CE2 CZ   sing Y N 353 
TYR CE2 HE2  sing N N 354 
TYR CZ  OH   sing N N 355 
TYR OH  HH   sing N N 356 
TYR OXT HXT  sing N N 357 
VAL N   CA   sing N N 358 
VAL N   H    sing N N 359 
VAL N   H2   sing N N 360 
VAL CA  C    sing N N 361 
VAL CA  CB   sing N N 362 
VAL CA  HA   sing N N 363 
VAL C   O    doub N N 364 
VAL C   OXT  sing N N 365 
VAL CB  CG1  sing N N 366 
VAL CB  CG2  sing N N 367 
VAL CB  HB   sing N N 368 
VAL CG1 HG11 sing N N 369 
VAL CG1 HG12 sing N N 370 
VAL CG1 HG13 sing N N 371 
VAL CG2 HG21 sing N N 372 
VAL CG2 HG22 sing N N 373 
VAL CG2 HG23 sing N N 374 
VAL OXT HXT  sing N N 375 
# 
_pdbx_audit_support.funding_organization   'National Natural Science Foundation of China (NSFC)' 
_pdbx_audit_support.country                China 
_pdbx_audit_support.grant_number           U22A20542 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'in silico model' 
_pdbx_initial_refinement_model.source_name      AlphaFold 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9JOC 
_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]   0.011841 
_atom_sites.fract_transf_matrix[1][2]   0.006837 
_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]   0.013673 
_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]   0.010740 
_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 
H 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N    . ILE A 1 23  ? 37.443 22.939  -1.363  1.00 54.09 ? 23  ILE A N    1 
ATOM   2    C CA   . ILE A 1 23  ? 37.044 21.734  -2.088  1.00 52.50 ? 23  ILE A CA   1 
ATOM   3    C C    . ILE A 1 23  ? 36.187 22.109  -3.297  1.00 53.52 ? 23  ILE A C    1 
ATOM   4    O O    . ILE A 1 23  ? 35.291 22.959  -3.213  1.00 51.89 ? 23  ILE A O    1 
ATOM   5    C CB   . ILE A 1 23  ? 36.332 20.703  -1.173  1.00 52.71 ? 23  ILE A CB   1 
ATOM   6    C CG1  . ILE A 1 23  ? 37.307 20.100  -0.159  1.00 53.09 ? 23  ILE A CG1  1 
ATOM   7    C CG2  . ILE A 1 23  ? 35.693 19.563  -1.985  1.00 49.56 ? 23  ILE A CG2  1 
ATOM   8    C CD1  . ILE A 1 23  ? 37.142 20.628  1.243   1.00 53.51 ? 23  ILE A CD1  1 
ATOM   9    H HA   . ILE A 1 23  ? 37.847 21.296  -2.412  1.00 63.00 ? 23  ILE A HA   1 
ATOM   10   H HB   . ILE A 1 23  ? 35.633 21.188  -0.707  1.00 63.26 ? 23  ILE A HB   1 
ATOM   11   H HG12 . ILE A 1 23  ? 37.172 19.140  -0.130  1.00 63.71 ? 23  ILE A HG12 1 
ATOM   12   H HG13 . ILE A 1 23  ? 38.213 20.299  -0.444  1.00 63.71 ? 23  ILE A HG13 1 
ATOM   13   H HG21 . ILE A 1 23  ? 35.442 18.847  -1.381  1.00 59.47 ? 23  ILE A HG21 1 
ATOM   14   H HG22 . ILE A 1 23  ? 34.907 19.902  -2.442  1.00 59.47 ? 23  ILE A HG22 1 
ATOM   15   H HG23 . ILE A 1 23  ? 36.337 19.238  -2.634  1.00 59.47 ? 23  ILE A HG23 1 
ATOM   16   H HD11 . ILE A 1 23  ? 37.797 20.204  1.819   1.00 64.21 ? 23  ILE A HD11 1 
ATOM   17   H HD12 . ILE A 1 23  ? 37.279 21.589  1.237   1.00 64.21 ? 23  ILE A HD12 1 
ATOM   18   H HD13 . ILE A 1 23  ? 36.246 20.424  1.554   1.00 64.21 ? 23  ILE A HD13 1 
ATOM   19   N N    . ASP A 1 24  ? 36.501 21.470  -4.421  1.00 48.21 ? 24  ASP A N    1 
ATOM   20   C CA   . ASP A 1 24  ? 35.699 21.548  -5.635  1.00 45.36 ? 24  ASP A CA   1 
ATOM   21   C C    . ASP A 1 24  ? 34.547 20.559  -5.571  1.00 42.64 ? 24  ASP A C    1 
ATOM   22   O O    . ASP A 1 24  ? 34.770 19.342  -5.554  1.00 40.64 ? 24  ASP A O    1 
ATOM   23   C CB   . ASP A 1 24  ? 36.577 21.219  -6.839  1.00 45.70 ? 24  ASP A CB   1 
ATOM   24   C CG   . ASP A 1 24  ? 35.805 21.233  -8.143  1.00 48.62 ? 24  ASP A CG   1 
ATOM   25   O OD1  . ASP A 1 24  ? 34.633 21.669  -8.143  1.00 47.06 ? 24  ASP A OD1  1 
ATOM   26   O OD2  . ASP A 1 24  ? 36.378 20.815  -9.171  1.00 54.43 ? 24  ASP A OD2  1 
ATOM   27   H H    . ASP A 1 24  ? 37.196 20.970  -4.508  1.00 57.85 ? 24  ASP A H    1 
ATOM   28   H HA   . ASP A 1 24  ? 35.333 22.442  -5.719  1.00 54.43 ? 24  ASP A HA   1 
ATOM   29   H HB2  . ASP A 1 24  ? 37.287 21.877  -6.903  1.00 54.84 ? 24  ASP A HB2  1 
ATOM   30   H HB3  . ASP A 1 24  ? 36.955 20.333  -6.723  1.00 54.84 ? 24  ASP A HB3  1 
ATOM   31   N N    . TYR A 1 25  ? 33.318 21.074  -5.576  1.00 37.89 ? 25  TYR A N    1 
ATOM   32   C CA   . TYR A 1 25  ? 32.120 20.243  -5.506  1.00 33.42 ? 25  TYR A CA   1 
ATOM   33   C C    . TYR A 1 25  ? 31.415 20.074  -6.851  1.00 31.49 ? 25  TYR A C    1 
ATOM   34   O O    . TYR A 1 25  ? 30.348 19.457  -6.896  1.00 29.79 ? 25  TYR A O    1 
ATOM   35   C CB   . TYR A 1 25  ? 31.143 20.808  -4.466  1.00 33.49 ? 25  TYR A CB   1 
ATOM   36   C CG   . TYR A 1 25  ? 31.678 20.806  -3.050  1.00 33.55 ? 25  TYR A CG   1 
ATOM   37   C CD1  . TYR A 1 25  ? 31.765 19.623  -2.322  1.00 32.63 ? 25  TYR A CD1  1 
ATOM   38   C CD2  . TYR A 1 25  ? 32.099 21.983  -2.442  1.00 39.26 ? 25  TYR A CD2  1 
ATOM   39   C CE1  . TYR A 1 25  ? 32.258 19.614  -1.027  1.00 34.45 ? 25  TYR A CE1  1 
ATOM   40   C CE2  . TYR A 1 25  ? 32.595 21.981  -1.150  1.00 39.99 ? 25  TYR A CE2  1 
ATOM   41   C CZ   . TYR A 1 25  ? 32.671 20.793  -0.448  1.00 38.50 ? 25  TYR A CZ   1 
ATOM   42   O OH   . TYR A 1 25  ? 33.167 20.796  0.838   1.00 45.73 ? 25  TYR A OH   1 
ATOM   43   H H    . TYR A 1 25  ? 33.152 21.917  -5.620  1.00 45.46 ? 25  TYR A H    1 
ATOM   44   H HA   . TYR A 1 25  ? 32.390 19.358  -5.215  1.00 40.10 ? 25  TYR A HA   1 
ATOM   45   H HB2  . TYR A 1 25  ? 30.935 21.726  -4.701  1.00 40.19 ? 25  TYR A HB2  1 
ATOM   46   H HB3  . TYR A 1 25  ? 30.335 20.272  -4.476  1.00 40.19 ? 25  TYR A HB3  1 
ATOM   47   H HD1  . TYR A 1 25  ? 31.486 18.826  -2.710  1.00 39.16 ? 25  TYR A HD1  1 
ATOM   48   H HD2  . TYR A 1 25  ? 32.048 22.784  -2.911  1.00 47.11 ? 25  TYR A HD2  1 
ATOM   49   H HE1  . TYR A 1 25  ? 32.311 18.816  -0.552  1.00 41.34 ? 25  TYR A HE1  1 
ATOM   50   H HE2  . TYR A 1 25  ? 32.876 22.775  -0.755  1.00 47.99 ? 25  TYR A HE2  1 
ATOM   51   H HH   . TYR A 1 25  ? 33.205 20.011  1.133   1.00 54.87 ? 25  TYR A HH   1 
ATOM   52   N N    . SER A 1 26  ? 32.005 20.561  -7.951  1.00 30.39 ? 26  SER A N    1 
ATOM   53   C CA   . SER A 1 26  ? 31.270 20.636  -9.218  1.00 31.53 ? 26  SER A CA   1 
ATOM   54   C C    . SER A 1 26  ? 30.849 19.266  -9.759  1.00 29.33 ? 26  SER A C    1 
ATOM   55   O O    . SER A 1 26  ? 29.826 19.164  -10.444 1.00 32.43 ? 26  SER A O    1 
ATOM   56   C CB   . SER A 1 26  ? 32.082 21.420  -10.260 1.00 35.70 ? 26  SER A CB   1 
ATOM   57   O OG   . SER A 1 26  ? 33.350 20.836  -10.519 1.00 39.45 ? 26  SER A OG   1 
ATOM   58   H H    . SER A 1 26  ? 32.814 20.850  -7.989  1.00 36.47 ? 26  SER A H    1 
ATOM   59   H HA   . SER A 1 26  ? 30.447 21.123  -9.053  1.00 37.84 ? 26  SER A HA   1 
ATOM   60   H HB2  . SER A 1 26  ? 31.579 21.444  -11.088 1.00 42.84 ? 26  SER A HB2  1 
ATOM   61   H HB3  . SER A 1 26  ? 32.220 22.321  -9.928  1.00 42.84 ? 26  SER A HB3  1 
ATOM   62   H HG   . SER A 1 26  ? 33.762 20.711  -9.798  1.00 47.34 ? 26  SER A HG   1 
ATOM   63   N N    . ASN A 1 27  ? 31.598 18.208  -9.467  1.00 29.33 ? 27  ASN A N    1 
ATOM   64   C CA   . ASN A 1 27  ? 31.297 16.885  -10.010 1.00 27.20 ? 27  ASN A CA   1 
ATOM   65   C C    . ASN A 1 27  ? 30.563 15.993  -9.021  1.00 21.91 ? 27  ASN A C    1 
ATOM   66   O O    . ASN A 1 27  ? 30.362 14.800  -9.293  1.00 21.36 ? 27  ASN A O    1 
ATOM   67   C CB   . ASN A 1 27  ? 32.588 16.229  -10.480 1.00 26.74 ? 27  ASN A CB   1 
ATOM   68   C CG   . ASN A 1 27  ? 33.350 17.110  -11.430 1.00 31.71 ? 27  ASN A CG   1 
ATOM   69   O OD1  . ASN A 1 27  ? 32.795 17.574  -12.430 1.00 35.40 ? 27  ASN A OD1  1 
ATOM   70   N ND2  . ASN A 1 27  ? 34.612 17.397  -11.111 1.00 30.72 ? 27  ASN A ND2  1 
ATOM   71   H H    . ASN A 1 27  ? 32.288 18.229  -8.955  1.00 35.20 ? 27  ASN A H    1 
ATOM   72   H HA   . ASN A 1 27  ? 30.714 16.982  -10.779 1.00 32.64 ? 27  ASN A HA   1 
ATOM   73   H HB2  . ASN A 1 27  ? 33.153 16.050  -9.713  1.00 32.09 ? 27  ASN A HB2  1 
ATOM   74   H HB3  . ASN A 1 27  ? 32.377 15.400  -10.938 1.00 32.09 ? 27  ASN A HB3  1 
ATOM   75   H HD21 . ASN A 1 27  ? 35.083 17.898  -11.627 1.00 36.86 ? 27  ASN A HD21 1 
ATOM   76   H HD22 . ASN A 1 27  ? 34.955 17.081  -10.388 1.00 36.86 ? 27  ASN A HD22 1 
ATOM   77   N N    . TYR A 1 28  ? 30.152 16.551  -7.890  1.00 22.18 ? 28  TYR A N    1 
ATOM   78   C CA   . TYR A 1 28  ? 29.548 15.771  -6.841  1.00 18.70 ? 28  TYR A CA   1 
ATOM   79   C C    . TYR A 1 28  ? 28.104 15.409  -7.202  1.00 17.45 ? 28  TYR A C    1 
ATOM   80   O O    . TYR A 1 28  ? 27.463 16.067  -8.038  1.00 19.00 ? 28  TYR A O    1 
ATOM   81   C CB   . TYR A 1 28  ? 29.588 16.568  -5.539  1.00 20.92 ? 28  TYR A CB   1 
ATOM   82   C CG   . TYR A 1 28  ? 30.808 16.397  -4.590  1.00 21.13 ? 28  TYR A CG   1 
ATOM   83   C CD1  . TYR A 1 28  ? 32.125 16.371  -5.056  1.00 28.22 ? 28  TYR A CD1  1 
ATOM   84   C CD2  . TYR A 1 28  ? 30.603 16.327  -3.210  1.00 24.03 ? 28  TYR A CD2  1 
ATOM   85   C CE1  . TYR A 1 28  ? 33.217 16.254  -4.147  1.00 22.05 ? 28  TYR A CE1  1 
ATOM   86   C CE2  . TYR A 1 28  ? 31.673 16.208  -2.309  1.00 26.30 ? 28  TYR A CE2  1 
ATOM   87   C CZ   . TYR A 1 28  ? 32.968 16.163  -2.782  1.00 26.52 ? 28  TYR A CZ   1 
ATOM   88   O OH   . TYR A 1 28  ? 34.026 16.058  -1.882  1.00 26.19 ? 28  TYR A OH   1 
ATOM   89   H H    . TYR A 1 28  ? 30.215 17.390  -7.710  1.00 26.62 ? 28  TYR A H    1 
ATOM   90   H HA   . TYR A 1 28  ? 30.033 14.941  -6.715  1.00 22.44 ? 28  TYR A HA   1 
ATOM   91   H HB2  . TYR A 1 28  ? 29.552 17.509  -5.772  1.00 25.10 ? 28  TYR A HB2  1 
ATOM   92   H HB3  . TYR A 1 28  ? 28.804 16.323  -5.023  1.00 25.10 ? 28  TYR A HB3  1 
ATOM   93   H HD1  . TYR A 1 28  ? 32.291 16.430  -5.969  1.00 33.87 ? 28  TYR A HD1  1 
ATOM   94   H HD2  . TYR A 1 28  ? 29.735 16.361  -2.879  1.00 28.83 ? 28  TYR A HD2  1 
ATOM   95   H HE1  . TYR A 1 28  ? 34.091 16.240  -4.466  1.00 26.47 ? 28  TYR A HE1  1 
ATOM   96   H HE2  . TYR A 1 28  ? 31.508 16.159  -1.395  1.00 31.56 ? 28  TYR A HE2  1 
ATOM   97   H HH   . TYR A 1 28  ? 33.734 15.869  -1.117  1.00 31.43 ? 28  TYR A HH   1 
ATOM   98   N N    . PRO A 1 29  ? 27.569 14.386  -6.560  1.00 15.81 ? 29  PRO A N    1 
ATOM   99   C CA   . PRO A 1 29  ? 26.171 13.986  -6.775  1.00 15.20 ? 29  PRO A CA   1 
ATOM   100  C C    . PRO A 1 29  ? 25.202 15.009  -6.186  1.00 15.28 ? 29  PRO A C    1 
ATOM   101  O O    . PRO A 1 29  ? 25.565 15.904  -5.416  1.00 16.71 ? 29  PRO A O    1 
ATOM   102  C CB   . PRO A 1 29  ? 26.055 12.632  -6.055  1.00 16.21 ? 29  PRO A CB   1 
ATOM   103  C CG   . PRO A 1 29  ? 27.201 12.574  -5.153  1.00 20.33 ? 29  PRO A CG   1 
ATOM   104  C CD   . PRO A 1 29  ? 28.277 13.480  -5.643  1.00 17.01 ? 29  PRO A CD   1 
ATOM   105  H HA   . PRO A 1 29  ? 25.990 13.864  -7.720  1.00 18.24 ? 29  PRO A HA   1 
ATOM   106  H HB2  . PRO A 1 29  ? 25.223 12.593  -5.559  1.00 19.45 ? 29  PRO A HB2  1 
ATOM   107  H HB3  . PRO A 1 29  ? 26.089 11.911  -6.703  1.00 19.45 ? 29  PRO A HB3  1 
ATOM   108  H HG2  . PRO A 1 29  ? 26.914 12.851  -4.269  1.00 24.39 ? 29  PRO A HG2  1 
ATOM   109  H HG3  . PRO A 1 29  ? 27.528 11.661  -5.125  1.00 24.39 ? 29  PRO A HG3  1 
ATOM   110  H HD2  . PRO A 1 29  ? 28.673 13.974  -4.908  1.00 20.42 ? 29  PRO A HD2  1 
ATOM   111  H HD3  . PRO A 1 29  ? 28.962 12.980  -6.114  1.00 20.42 ? 29  PRO A HD3  1 
ATOM   112  N N    . GLU A 1 30  ? 23.941 14.885  -6.610  1.00 15.64 ? 30  GLU A N    1 
ATOM   113  C CA   . GLU A 1 30  ? 22.881 15.660  -5.977  1.00 14.82 ? 30  GLU A CA   1 
ATOM   114  C C    . GLU A 1 30  ? 22.813 15.268  -4.506  1.00 14.14 ? 30  GLU A C    1 
ATOM   115  O O    . GLU A 1 30  ? 23.093 14.131  -4.142  1.00 14.44 ? 30  GLU A O    1 
ATOM   116  C CB   . GLU A 1 30  ? 21.536 15.365  -6.642  1.00 16.87 ? 30  GLU A CB   1 
ATOM   117  C CG   . GLU A 1 30  ? 21.476 15.700  -8.123  1.00 18.16 ? 30  GLU A CG   1 
ATOM   118  C CD   . GLU A 1 30  ? 21.657 17.174  -8.441  1.00 28.08 ? 30  GLU A CD   1 
ATOM   119  O OE1  . GLU A 1 30  ? 21.147 18.049  -7.710  1.00 33.59 ? 30  GLU A OE1  1 
ATOM   120  O OE2  . GLU A 1 30  ? 22.357 17.457  -9.439  1.00 36.54 ? 30  GLU A OE2  1 
ATOM   121  H H    . GLU A 1 30  ? 23.683 14.370  -7.248  1.00 18.77 ? 30  GLU A H    1 
ATOM   122  H HA   . GLU A 1 30  ? 23.054 16.610  -6.063  1.00 17.78 ? 30  GLU A HA   1 
ATOM   123  H HB2  . GLU A 1 30  ? 21.347 14.418  -6.549  1.00 20.24 ? 30  GLU A HB2  1 
ATOM   124  H HB3  . GLU A 1 30  ? 20.850 15.886  -6.197  1.00 20.24 ? 30  GLU A HB3  1 
ATOM   125  H HG2  . GLU A 1 30  ? 22.181 15.213  -8.580  1.00 21.79 ? 30  GLU A HG2  1 
ATOM   126  H HG3  . GLU A 1 30  ? 20.610 15.430  -8.467  1.00 21.79 ? 30  GLU A HG3  1 
ATOM   127  N N    . PHE A 1 31  ? 22.402 16.228  -3.690  1.00 14.99 ? 31  PHE A N    1 
ATOM   128  C CA   . PHE A 1 31  ? 22.216 15.975  -2.275  1.00 14.29 ? 31  PHE A CA   1 
ATOM   129  C C    . PHE A 1 31  ? 21.114 16.872  -1.744  1.00 17.02 ? 31  PHE A C    1 
ATOM   130  O O    . PHE A 1 31  ? 21.093 18.065  -2.003  1.00 17.75 ? 31  PHE A O    1 
ATOM   131  C CB   . PHE A 1 31  ? 23.470 16.273  -1.468  1.00 15.06 ? 31  PHE A CB   1 
ATOM   132  C CG   . PHE A 1 31  ? 23.287 15.992  0.006   1.00 14.68 ? 31  PHE A CG   1 
ATOM   133  C CD1  . PHE A 1 31  ? 23.494 14.714  0.489   1.00 13.80 ? 31  PHE A CD1  1 
ATOM   134  C CD2  . PHE A 1 31  ? 22.830 16.959  0.855   1.00 15.50 ? 31  PHE A CD2  1 
ATOM   135  C CE1  . PHE A 1 31  ? 23.285 14.413  1.858   1.00 13.46 ? 31  PHE A CE1  1 
ATOM   136  C CE2  . PHE A 1 31  ? 22.632 16.682  2.213   1.00 15.85 ? 31  PHE A CE2  1 
ATOM   137  C CZ   . PHE A 1 31  ? 22.855 15.403  2.691   1.00 15.59 ? 31  PHE A CZ   1 
ATOM   138  H H    . PHE A 1 31  ? 22.224 17.033  -3.934  1.00 17.99 ? 31  PHE A H    1 
ATOM   139  H HA   . PHE A 1 31  ? 21.971 15.042  -2.170  1.00 17.15 ? 31  PHE A HA   1 
ATOM   140  H HB2  . PHE A 1 31  ? 24.196 15.719  -1.794  1.00 18.08 ? 31  PHE A HB2  1 
ATOM   141  H HB3  . PHE A 1 31  ? 23.698 17.211  -1.571  1.00 18.08 ? 31  PHE A HB3  1 
ATOM   142  H HD1  . PHE A 1 31  ? 23.775 14.044  -0.091  1.00 16.56 ? 31  PHE A HD1  1 
ATOM   143  H HD2  . PHE A 1 31  ? 22.648 17.810  0.528   1.00 18.60 ? 31  PHE A HD2  1 
ATOM   144  H HE1  . PHE A 1 31  ? 23.438 13.555  2.183   1.00 16.15 ? 31  PHE A HE1  1 
ATOM   145  H HE2  . PHE A 1 31  ? 22.352 17.355  2.791   1.00 19.02 ? 31  PHE A HE2  1 
ATOM   146  H HZ   . PHE A 1 31  ? 22.710 15.216  3.590   1.00 18.70 ? 31  PHE A HZ   1 
ATOM   147  N N    . SER A 1 32  ? 20.244 16.278  -0.925  1.00 16.97 ? 32  SER A N    1 
ATOM   148  C CA   . SER A 1 32  ? 19.218 17.021  -0.220  1.00 17.47 ? 32  SER A CA   1 
ATOM   149  C C    . SER A 1 32  ? 19.006 16.384  1.137   1.00 15.93 ? 32  SER A C    1 
ATOM   150  O O    . SER A 1 32  ? 19.037 15.170  1.266   1.00 17.13 ? 32  SER A O    1 
ATOM   151  C CB   . SER A 1 32  ? 17.901 16.956  -0.992  1.00 19.65 ? 32  SER A CB   1 
ATOM   152  O OG   . SER A 1 32  ? 16.894 17.643  -0.284  1.00 20.46 ? 32  SER A OG   1 
ATOM   153  H H    . SER A 1 32  ? 20.233 15.433  -0.764  1.00 20.37 ? 32  SER A H    1 
ATOM   154  H HA   . SER A 1 32  ? 19.496 17.943  -0.103  1.00 20.96 ? 32  SER A HA   1 
ATOM   155  H HB2  . SER A 1 32  ? 18.020 17.371  -1.861  1.00 23.58 ? 32  SER A HB2  1 
ATOM   156  H HB3  . SER A 1 32  ? 17.640 16.028  -1.101  1.00 23.58 ? 32  SER A HB3  1 
ATOM   157  H HG   . SER A 1 32  ? 16.170 17.610  -0.710  1.00 24.55 ? 32  SER A HG   1 
ATOM   158  N N    . TRP A 1 33  ? 18.768 17.228  2.130   1.00 15.98 ? 33  TRP A N    1 
ATOM   159  C CA   . TRP A 1 33  ? 18.346 16.767  3.457   1.00 15.82 ? 33  TRP A CA   1 
ATOM   160  C C    . TRP A 1 33  ? 16.842 16.536  3.546   1.00 17.67 ? 33  TRP A C    1 
ATOM   161  O O    . TRP A 1 33  ? 16.349 16.165  4.620   1.00 17.31 ? 33  TRP A O    1 
ATOM   162  C CB   . TRP A 1 33  ? 18.716 17.792  4.510   1.00 17.73 ? 33  TRP A CB   1 
ATOM   163  C CG   . TRP A 1 33  ? 20.172 17.948  4.839   1.00 16.06 ? 33  TRP A CG   1 
ATOM   164  C CD1  . TRP A 1 33  ? 20.942 19.041  4.614   1.00 17.45 ? 33  TRP A CD1  1 
ATOM   165  C CD2  . TRP A 1 33  ? 21.006 16.989  5.493   1.00 15.50 ? 33  TRP A CD2  1 
ATOM   166  N NE1  . TRP A 1 33  ? 22.216 18.836  5.095   1.00 16.93 ? 33  TRP A NE1  1 
ATOM   167  C CE2  . TRP A 1 33  ? 22.272 17.583  5.638   1.00 15.72 ? 33  TRP A CE2  1 
ATOM   168  C CE3  . TRP A 1 33  ? 20.800 15.694  5.982   1.00 15.76 ? 33  TRP A CE3  1 
ATOM   169  C CZ2  . TRP A 1 33  ? 23.344 16.927  6.251   1.00 17.53 ? 33  TRP A CZ2  1 
ATOM   170  C CZ3  . TRP A 1 33  ? 21.861 15.035  6.597   1.00 14.65 ? 33  TRP A CZ3  1 
ATOM   171  C CH2  . TRP A 1 33  ? 23.114 15.657  6.712   1.00 17.38 ? 33  TRP A CH2  1 
ATOM   172  H H    . TRP A 1 33  ? 18.843 18.082  2.066   1.00 19.18 ? 33  TRP A H    1 
ATOM   173  H HA   . TRP A 1 33  ? 18.811 15.937  3.646   1.00 18.99 ? 33  TRP A HA   1 
ATOM   174  H HB2  . TRP A 1 33  ? 18.402 18.658  4.206   1.00 21.28 ? 33  TRP A HB2  1 
ATOM   175  H HB3  . TRP A 1 33  ? 18.267 17.547  5.334   1.00 21.28 ? 33  TRP A HB3  1 
ATOM   176  H HD1  . TRP A 1 33  ? 20.652 19.819  4.195   1.00 20.94 ? 33  TRP A HD1  1 
ATOM   177  H HE1  . TRP A 1 33  ? 22.865 19.399  5.060   1.00 20.32 ? 33  TRP A HE1  1 
ATOM   178  H HE3  . TRP A 1 33  ? 19.970 15.282  5.898   1.00 18.91 ? 33  TRP A HE3  1 
ATOM   179  H HZ2  . TRP A 1 33  ? 24.175 17.334  6.343   1.00 21.03 ? 33  TRP A HZ2  1 
ATOM   180  H HZ3  . TRP A 1 33  ? 21.739 14.178  6.935   1.00 17.58 ? 33  TRP A HZ3  1 
ATOM   181  H HH2  . TRP A 1 33  ? 23.811 15.192  7.113   1.00 20.86 ? 33  TRP A HH2  1 
ATOM   182  N N    . ASP A 1 34  ? 16.084 16.780  2.475   1.00 16.29 ? 34  ASP A N    1 
ATOM   183  C CA   . ASP A 1 34  ? 14.626 16.765  2.601   1.00 18.00 ? 34  ASP A CA   1 
ATOM   184  C C    . ASP A 1 34  ? 14.121 15.428  3.127   1.00 17.03 ? 34  ASP A C    1 
ATOM   185  O O    . ASP A 1 34  ? 13.211 15.396  3.967   1.00 16.98 ? 34  ASP A O    1 
ATOM   186  C CB   . ASP A 1 34  ? 13.977 17.077  1.256   1.00 20.22 ? 34  ASP A CB   1 
ATOM   187  C CG   . ASP A 1 34  ? 14.122 18.523  0.856   1.00 22.02 ? 34  ASP A CG   1 
ATOM   188  O OD1  . ASP A 1 34  ? 14.657 19.343  1.630   1.00 27.00 ? 34  ASP A OD1  1 
ATOM   189  O OD2  . ASP A 1 34  ? 13.674 18.834  -0.272  1.00 29.78 ? 34  ASP A OD2  1 
ATOM   190  H H    . ASP A 1 34  ? 16.380 16.952  1.687   1.00 19.55 ? 34  ASP A H    1 
ATOM   191  H HA   . ASP A 1 34  ? 14.370 17.455  3.233   1.00 21.61 ? 34  ASP A HA   1 
ATOM   192  H HB2  . ASP A 1 34  ? 14.395 16.533  0.570   1.00 24.26 ? 34  ASP A HB2  1 
ATOM   193  H HB3  . ASP A 1 34  ? 13.030 16.874  1.308   1.00 24.26 ? 34  ASP A HB3  1 
ATOM   194  N N    . THR A 1 35  ? 14.682 14.325  2.628   1.00 16.69 ? 35  THR A N    1 
ATOM   195  C CA   . THR A 1 35  ? 14.425 12.970  3.114   1.00 15.33 ? 35  THR A CA   1 
ATOM   196  C C    . THR A 1 35  ? 15.767 12.240  3.139   1.00 14.66 ? 35  THR A C    1 
ATOM   197  O O    . THR A 1 35  ? 16.780 12.770  2.689   1.00 15.49 ? 35  THR A O    1 
ATOM   198  C CB   . THR A 1 35  ? 13.421 12.223  2.228   1.00 17.26 ? 35  THR A CB   1 
ATOM   199  O OG1  . THR A 1 35  ? 13.933 12.155  0.897   1.00 18.25 ? 35  THR A OG1  1 
ATOM   200  C CG2  . THR A 1 35  ? 12.069 12.905  2.228   1.00 18.44 ? 35  THR A CG2  1 
ATOM   201  H H    . THR A 1 35  ? 15.242 14.338  1.975   1.00 20.03 ? 35  THR A H    1 
ATOM   202  H HA   . THR A 1 35  ? 14.052 13.016  4.009   1.00 18.39 ? 35  THR A HA   1 
ATOM   203  H HB   . THR A 1 35  ? 13.290 11.326  2.574   1.00 20.72 ? 35  THR A HB   1 
ATOM   204  H HG1  . THR A 1 35  ? 14.610 11.657  0.874   1.00 21.89 ? 35  THR A HG1  1 
ATOM   205  H HG21 . THR A 1 35  ? 11.443 12.401  1.686   1.00 22.12 ? 35  THR A HG21 1 
ATOM   206  H HG22 . THR A 1 35  ? 11.727 12.962  3.134   1.00 22.12 ? 35  THR A HG22 1 
ATOM   207  H HG23 . THR A 1 35  ? 12.150 13.801  1.865   1.00 22.12 ? 35  THR A HG23 1 
ATOM   208  N N    . MET A 1 36  ? 15.777 11.016  3.636   1.00 13.97 ? 36  MET A N    1 
ATOM   209  C CA   . MET A 1 36  ? 17.023 10.270  3.798   1.00 14.10 ? 36  MET A CA   1 
ATOM   210  C C    . MET A 1 36  ? 17.887 10.291  2.538   1.00 13.27 ? 36  MET A C    1 
ATOM   211  O O    . MET A 1 36  ? 17.402 9.927   1.460   1.00 14.79 ? 36  MET A O    1 
ATOM   212  C CB   . MET A 1 36  ? 16.722 8.829   4.158   1.00 14.14 ? 36  MET A CB   1 
ATOM   213  C CG   . MET A 1 36  ? 17.820 8.136   4.922   1.00 14.17 ? 36  MET A CG   1 
ATOM   214  S SD   . MET A 1 36  ? 18.341 8.889   6.472   1.00 14.98 ? 36  MET A SD   1 
ATOM   215  C CE   . MET A 1 36  ? 16.785 8.930   7.320   1.00 17.28 ? 36  MET A CE   1 
ATOM   216  H H    . MET A 1 36  ? 15.075 10.587  3.890   1.00 16.77 ? 36  MET A H    1 
ATOM   217  H HA   . MET A 1 36  ? 17.518 10.694  4.516   1.00 16.92 ? 36  MET A HA   1 
ATOM   218  H HB2  . MET A 1 36  ? 15.923 8.808   4.708   1.00 16.96 ? 36  MET A HB2  1 
ATOM   219  H HB3  . MET A 1 36  ? 16.574 8.330   3.339   1.00 16.96 ? 36  MET A HB3  1 
ATOM   220  H HG2  . MET A 1 36  ? 17.518 7.238   5.133   1.00 17.00 ? 36  MET A HG2  1 
ATOM   221  H HG3  . MET A 1 36  ? 18.603 8.096   4.352   1.00 17.00 ? 36  MET A HG3  1 
ATOM   222  H HE1  . MET A 1 36  ? 16.906 9.358   8.182   1.00 20.73 ? 36  MET A HE1  1 
ATOM   223  H HE2  . MET A 1 36  ? 16.148 9.432   6.788   1.00 20.73 ? 36  MET A HE2  1 
ATOM   224  H HE3  . MET A 1 36  ? 16.469 8.021   7.444   1.00 20.73 ? 36  MET A HE3  1 
ATOM   225  N N    . PRO A 1 37  ? 19.160 10.681  2.631   1.00 12.76 ? 37  PRO A N    1 
ATOM   226  C CA   . PRO A 1 37  ? 20.056 10.584  1.463   1.00 12.12 ? 37  PRO A CA   1 
ATOM   227  C C    . PRO A 1 37  ? 20.538 9.157   1.295   1.00 12.18 ? 37  PRO A C    1 
ATOM   228  O O    . PRO A 1 37  ? 21.176 8.609   2.191   1.00 13.01 ? 37  PRO A O    1 
ATOM   229  C CB   . PRO A 1 37  ? 21.212 11.531  1.824   1.00 12.45 ? 37  PRO A CB   1 
ATOM   230  C CG   . PRO A 1 37  ? 21.238 11.536  3.335   1.00 13.46 ? 37  PRO A CG   1 
ATOM   231  C CD   . PRO A 1 37  ? 19.795 11.381  3.768   1.00 14.91 ? 37  PRO A CD   1 
ATOM   232  H HA   . PRO A 1 37  ? 19.617 10.888  0.653   1.00 14.54 ? 37  PRO A HA   1 
ATOM   233  H HB2  . PRO A 1 37  ? 22.045 11.192  1.461   1.00 14.94 ? 37  PRO A HB2  1 
ATOM   234  H HB3  . PRO A 1 37  ? 21.035 12.419  1.475   1.00 14.94 ? 37  PRO A HB3  1 
ATOM   235  H HG2  . PRO A 1 37  ? 21.775 10.795  3.656   1.00 16.15 ? 37  PRO A HG2  1 
ATOM   236  H HG3  . PRO A 1 37  ? 21.605 12.375  3.654   1.00 16.15 ? 37  PRO A HG3  1 
ATOM   237  H HD2  . PRO A 1 37  ? 19.735 10.848  4.576   1.00 17.89 ? 37  PRO A HD2  1 
ATOM   238  H HD3  . PRO A 1 37  ? 19.384 12.248  3.911   1.00 17.89 ? 37  PRO A HD3  1 
ATOM   239  N N    . LEU A 1 38  ? 20.242 8.550   0.137   1.00 12.86 ? 38  LEU A N    1 
ATOM   240  C CA   . LEU A 1 38  ? 20.418 7.114   -0.090  1.00 11.72 ? 38  LEU A CA   1 
ATOM   241  C C    . LEU A 1 38  ? 21.511 6.809   -1.109  1.00 13.02 ? 38  LEU A C    1 
ATOM   242  O O    . LEU A 1 38  ? 21.647 7.514   -2.116  1.00 14.00 ? 38  LEU A O    1 
ATOM   243  C CB   . LEU A 1 38  ? 19.120 6.482   -0.596  1.00 13.43 ? 38  LEU A CB   1 
ATOM   244  C CG   . LEU A 1 38  ? 17.935 6.653   0.350   1.00 13.15 ? 38  LEU A CG   1 
ATOM   245  C CD1  . LEU A 1 38  ? 16.683 5.991   -0.273  1.00 17.59 ? 38  LEU A CD1  1 
ATOM   246  C CD2  . LEU A 1 38  ? 18.199 6.066   1.712   1.00 15.18 ? 38  LEU A CD2  1 
ATOM   247  H H    . LEU A 1 38  ? 19.928 8.964   -0.549  1.00 15.43 ? 38  LEU A H    1 
ATOM   248  H HA   . LEU A 1 38  ? 20.685 6.723   0.757   1.00 14.06 ? 38  LEU A HA   1 
ATOM   249  H HB2  . LEU A 1 38  ? 18.885 6.893   -1.442  1.00 16.12 ? 38  LEU A HB2  1 
ATOM   250  H HB3  . LEU A 1 38  ? 19.266 5.531   -0.719  1.00 16.12 ? 38  LEU A HB3  1 
ATOM   251  H HG   . LEU A 1 38  ? 17.781 7.602   0.477   1.00 15.78 ? 38  LEU A HG   1 
ATOM   252  H HD11 . LEU A 1 38  ? 15.928 6.119   0.323   1.00 21.11 ? 38  LEU A HD11 1 
ATOM   253  H HD12 . LEU A 1 38  ? 16.501 6.405   -1.131  1.00 21.11 ? 38  LEU A HD12 1 
ATOM   254  H HD13 . LEU A 1 38  ? 16.853 5.044   -0.392  1.00 21.11 ? 38  LEU A HD13 1 
ATOM   255  H HD21 . LEU A 1 38  ? 17.375 6.073   2.224   1.00 18.22 ? 38  LEU A HD21 1 
ATOM   256  H HD22 . LEU A 1 38  ? 18.515 5.155   1.607   1.00 18.22 ? 38  LEU A HD22 1 
ATOM   257  H HD23 . LEU A 1 38  ? 18.873 6.600   2.161   1.00 18.22 ? 38  LEU A HD23 1 
ATOM   258  N N    . TYR A 1 39  ? 22.227 5.712   -0.852  1.00 11.85 ? 39  TYR A N    1 
ATOM   259  C CA   . TYR A 1 39  ? 23.285 5.177   -1.736  1.00 11.33 ? 39  TYR A CA   1 
ATOM   260  C C    . TYR A 1 39  ? 22.803 3.815   -2.232  1.00 13.00 ? 39  TYR A C    1 
ATOM   261  O O    . TYR A 1 39  ? 22.111 3.134   -1.494  1.00 12.83 ? 39  TYR A O    1 
ATOM   262  C CB   . TYR A 1 39  ? 24.557 5.001   -0.906  1.00 13.52 ? 39  TYR A CB   1 
ATOM   263  C CG   . TYR A 1 39  ? 25.721 4.323   -1.572  1.00 11.38 ? 39  TYR A CG   1 
ATOM   264  C CD1  . TYR A 1 39  ? 26.295 4.856   -2.714  1.00 11.91 ? 39  TYR A CD1  1 
ATOM   265  C CD2  . TYR A 1 39  ? 26.306 3.204   -1.004  1.00 11.96 ? 39  TYR A CD2  1 
ATOM   266  C CE1  . TYR A 1 39  ? 27.393 4.264   -3.305  1.00 11.92 ? 39  TYR A CE1  1 
ATOM   267  C CE2  . TYR A 1 39  ? 27.422 2.619   -1.565  1.00 11.45 ? 39  TYR A CE2  1 
ATOM   268  C CZ   . TYR A 1 39  ? 27.951 3.144   -2.726  1.00 10.96 ? 39  TYR A CZ   1 
ATOM   269  O OH   . TYR A 1 39  ? 29.049 2.577   -3.269  1.00 11.91 ? 39  TYR A OH   1 
ATOM   270  H H    . TYR A 1 39  ? 22.092 5.162   -0.135  1.00 14.23 ? 39  TYR A H    1 
ATOM   271  H HA   . TYR A 1 39  ? 23.451 5.784   -2.497  1.00 13.60 ? 39  TYR A HA   1 
ATOM   272  H HB2  . TYR A 1 39  ? 24.850 5.883   -0.623  1.00 16.23 ? 39  TYR A HB2  1 
ATOM   273  H HB3  . TYR A 1 39  ? 24.327 4.502   -0.096  1.00 16.23 ? 39  TYR A HB3  1 
ATOM   274  H HD1  . TYR A 1 39  ? 25.918 5.623   -3.109  1.00 14.30 ? 39  TYR A HD1  1 
ATOM   275  H HD2  . TYR A 1 39  ? 25.954 2.845   -0.207  1.00 14.36 ? 39  TYR A HD2  1 
ATOM   276  H HE1  . TYR A 1 39  ? 27.770 4.632   -4.089  1.00 14.30 ? 39  TYR A HE1  1 
ATOM   277  H HE2  . TYR A 1 39  ? 27.804 1.850   -1.175  1.00 13.75 ? 39  TYR A HE2  1 
ATOM   278  H HH   . TYR A 1 39  ? 29.754 2.941   -2.945  1.00 14.29 ? 39  TYR A HH   1 
ATOM   279  N N    . MET A 1 40  ? 23.186 3.444   -3.444  1.00 11.21 ? 40  MET A N    1 
ATOM   280  C CA   . MET A 1 40  ? 22.875 2.106   -3.990  1.00 11.89 ? 40  MET A CA   1 
ATOM   281  C C    . MET A 1 40  ? 24.191 1.475   -4.421  1.00 10.93 ? 40  MET A C    1 
ATOM   282  O O    . MET A 1 40  ? 24.990 2.177   -4.885  1.00 12.62 ? 40  MET A O    1 
ATOM   283  C CB   . MET A 1 40  ? 21.910 2.219   -5.167  1.00 12.19 ? 40  MET A CB   1 
ATOM   284  C CG   . MET A 1 40  ? 21.545 0.891   -5.814  1.00 13.47 ? 40  MET A CG   1 
ATOM   285  S SD   . MET A 1 40  ? 21.087 -0.449  -4.667  1.00 13.99 ? 40  MET A SD   1 
ATOM   286  C CE   . MET A 1 40  ? 19.639 0.262   -3.888  1.00 16.73 ? 40  MET A CE   1 
ATOM   287  H H    . MET A 1 40  ? 23.663 3.977   -4.009  1.00 13.45 ? 40  MET A H    1 
ATOM   288  H HA   . MET A 1 40  ? 22.479 1.554   -3.288  1.00 14.27 ? 40  MET A HA   1 
ATOM   289  H HB2  . MET A 1 40  ? 21.095 2.654   -4.857  1.00 14.62 ? 40  MET A HB2  1 
ATOM   290  H HB3  . MET A 1 40  ? 22.313 2.800   -5.846  1.00 14.62 ? 40  MET A HB3  1 
ATOM   291  H HG2  . MET A 1 40  ? 20.788 1.046   -6.412  1.00 16.16 ? 40  MET A HG2  1 
ATOM   292  H HG3  . MET A 1 40  ? 22.297 0.586   -6.365  1.00 16.16 ? 40  MET A HG3  1 
ATOM   293  H HE1  . MET A 1 40  ? 19.219 -0.402  -3.338  1.00 20.07 ? 40  MET A HE1  1 
ATOM   294  H HE2  . MET A 1 40  ? 19.899 1.013   -3.342  1.00 20.07 ? 40  MET A HE2  1 
ATOM   295  H HE3  . MET A 1 40  ? 19.020 0.553   -4.568  1.00 20.07 ? 40  MET A HE3  1 
ATOM   296  N N    . HIS A 1 41  ? 24.388 0.199   -4.149  1.00 11.45 ? 41  HIS A N    1 
ATOM   297  C CA   . HIS A 1 41  ? 25.643 -0.549  -4.405  1.00 10.62 ? 41  HIS A CA   1 
ATOM   298  C C    . HIS A 1 41  ? 25.132 -1.929  -4.766  1.00 11.99 ? 41  HIS A C    1 
ATOM   299  O O    . HIS A 1 41  ? 24.703 -2.616  -3.895  1.00 12.36 ? 41  HIS A O    1 
ATOM   300  C CB   . HIS A 1 41  ? 26.484 -0.455  -3.144  1.00 12.29 ? 41  HIS A CB   1 
ATOM   301  C CG   . HIS A 1 41  ? 27.876 -0.927  -3.270  1.00 11.33 ? 41  HIS A CG   1 
ATOM   302  N ND1  . HIS A 1 41  ? 28.914 -0.066  -3.429  1.00 11.09 ? 41  HIS A ND1  1 
ATOM   303  C CD2  . HIS A 1 41  ? 28.408 -2.149  -3.186  1.00 12.75 ? 41  HIS A CD2  1 
ATOM   304  C CE1  . HIS A 1 41  ? 30.031 -0.729  -3.479  1.00 11.51 ? 41  HIS A CE1  1 
ATOM   305  N NE2  . HIS A 1 41  ? 29.749 -1.994  -3.333  1.00 12.62 ? 41  HIS A NE2  1 
ATOM   306  H H    . HIS A 1 41  ? 23.741 -0.338  -3.799  1.00 13.74 ? 41  HIS A H    1 
ATOM   307  H HA   . HIS A 1 41  ? 26.117 -0.153  -5.160  1.00 12.74 ? 41  HIS A HA   1 
ATOM   308  H HB2  . HIS A 1 41  ? 26.498 0.480   -2.861  1.00 14.75 ? 41  HIS A HB2  1 
ATOM   309  H HB3  . HIS A 1 41  ? 26.056 -0.963  -2.430  1.00 14.75 ? 41  HIS A HB3  1 
ATOM   310  H HD2  . HIS A 1 41  ? 27.948 -2.951  -3.057  1.00 15.30 ? 41  HIS A HD2  1 
ATOM   311  H HE1  . HIS A 1 41  ? 30.886 -0.357  -3.581  1.00 13.81 ? 41  HIS A HE1  1 
ATOM   312  H HE2  . HIS A 1 41  ? 30.313 -2.583  -3.257  1.00 15.14 ? 41  HIS A HE2  1 
ATOM   313  N N    . VAL A 1 42  ? 25.236 -2.316  -6.027  1.00 11.36 ? 42  VAL A N    1 
ATOM   314  C CA   . VAL A 1 42  ? 24.446 -3.488  -6.475  1.00 11.85 ? 42  VAL A CA   1 
ATOM   315  C C    . VAL A 1 42  ? 25.006 -4.210  -7.678  1.00 11.18 ? 42  VAL A C    1 
ATOM   316  O O    . VAL A 1 42  ? 25.647 -3.595  -8.449  1.00 11.78 ? 42  VAL A O    1 
ATOM   317  C CB   . VAL A 1 42  ? 23.025 -2.974  -6.824  1.00 15.15 ? 42  VAL A CB   1 
ATOM   318  C CG1  . VAL A 1 42  ? 23.012 -2.005  -8.004  1.00 16.34 ? 42  VAL A CG1  1 
ATOM   319  C CG2  . VAL A 1 42  ? 22.023 -4.098  -7.056  1.00 18.37 ? 42  VAL A CG2  1 
ATOM   320  H H    . VAL A 1 42  ? 25.799 -1.955  -6.648  1.00 13.63 ? 42  VAL A H    1 
ATOM   321  H HA   . VAL A 1 42  ? 24.381 -4.116  -5.752  1.00 14.22 ? 42  VAL A HA   1 
ATOM   322  H HB   . VAL A 1 42  ? 22.706 -2.470  -6.040  1.00 18.17 ? 42  VAL A HB   1 
ATOM   323  H HG11 . VAL A 1 42  ? 22.216 -1.459  -7.949  1.00 19.60 ? 42  VAL A HG11 1 
ATOM   324  H HG12 . VAL A 1 42  ? 23.792 -1.427  -7.977  1.00 19.60 ? 42  VAL A HG12 1 
ATOM   325  H HG13 . VAL A 1 42  ? 23.006 -2.497  -8.842  1.00 19.60 ? 42  VAL A HG13 1 
ATOM   326  H HG21 . VAL A 1 42  ? 21.128 -3.738  -7.014  1.00 22.04 ? 42  VAL A HG21 1 
ATOM   327  H HG22 . VAL A 1 42  ? 22.161 -4.498  -7.931  1.00 22.04 ? 42  VAL A HG22 1 
ATOM   328  H HG23 . VAL A 1 42  ? 22.125 -4.778  -6.369  1.00 22.04 ? 42  VAL A HG23 1 
ATOM   329  N N    . ARG A 1 43  ? 24.664 -5.469  -7.784  1.00 11.64 ? 43  ARG A N    1 
ATOM   330  C CA   . ARG A 1 43  ? 24.991 -6.262  -8.971  1.00 11.51 ? 43  ARG A CA   1 
ATOM   331  C C    . ARG A 1 43  ? 23.820 -7.200  -9.199  1.00 12.15 ? 43  ARG A C    1 
ATOM   332  O O    . ARG A 1 43  ? 23.031 -7.312  -8.363  1.00 12.20 ? 43  ARG A O    1 
ATOM   333  C CB   . ARG A 1 43  ? 26.298 -7.044  -8.846  1.00 11.75 ? 43  ARG A CB   1 
ATOM   334  C CG   . ARG A 1 43  ? 26.419 -7.960  -7.631  1.00 12.31 ? 43  ARG A CG   1 
ATOM   335  C CD   . ARG A 1 43  ? 27.653 -8.853  -7.695  1.00 12.69 ? 43  ARG A CD   1 
ATOM   336  N NE   . ARG A 1 43  ? 27.528 -9.673  -8.895  1.00 13.92 ? 43  ARG A NE   1 
ATOM   337  C CZ   . ARG A 1 43  ? 26.965 -10.875 -9.011  1.00 14.19 ? 43  ARG A CZ   1 
ATOM   338  N NH1  . ARG A 1 43  ? 26.547 -11.578 -7.966  1.00 16.41 ? 43  ARG A NH1  1 
ATOM   339  N NH2  . ARG A 1 43  ? 26.870 -11.407 -10.216 1.00 14.98 ? 43  ARG A NH2  1 
ATOM   340  H H    . ARG A 1 43  ? 24.220 -5.933  -7.146  1.00 13.97 ? 43  ARG A H    1 
ATOM   341  H HA   . ARG A 1 43  ? 25.046 -5.677  -9.737  1.00 13.82 ? 43  ARG A HA   1 
ATOM   342  H HB2  . ARG A 1 43  ? 26.393 -7.562  -9.661  1.00 14.10 ? 43  ARG A HB2  1 
ATOM   343  H HB3  . ARG A 1 43  ? 27.034 -6.403  -8.827  1.00 14.10 ? 43  ARG A HB3  1 
ATOM   344  H HG2  . ARG A 1 43  ? 26.467 -7.412  -6.818  1.00 14.77 ? 43  ARG A HG2  1 
ATOM   345  H HG3  . ARG A 1 43  ? 25.622 -8.527  -7.564  1.00 14.77 ? 43  ARG A HG3  1 
ATOM   346  H HD2  . ARG A 1 43  ? 28.458 -8.299  -7.748  1.00 15.22 ? 43  ARG A HD2  1 
ATOM   347  H HD3  . ARG A 1 43  ? 27.718 -9.402  -6.890  1.00 15.22 ? 43  ARG A HD3  1 
ATOM   348  H HE   . ARG A 1 43  ? 27.758 -9.290  -9.635  1.00 16.71 ? 43  ARG A HE   1 
ATOM   349  H HH11 . ARG A 1 43  ? 26.567 -11.258 -7.158  1.00 19.69 ? 43  ARG A HH11 1 
ATOM   350  H HH12 . ARG A 1 43  ? 26.193 -12.373 -8.089  1.00 19.69 ? 43  ARG A HH12 1 
ATOM   351  H HH21 . ARG A 1 43  ? 27.131 -10.974 -10.924 1.00 17.98 ? 43  ARG A HH21 1 
ATOM   352  H HH22 . ARG A 1 43  ? 26.543 -12.205 -10.310 1.00 17.98 ? 43  ARG A HH22 1 
ATOM   353  N N    . LYS A 1 44  ? 23.761 -7.808  -10.351 1.00 12.47 ? 44  LYS A N    1 
ATOM   354  C CA   . LYS A 1 44  ? 22.738 -8.745  -10.775 1.00 13.46 ? 44  LYS A CA   1 
ATOM   355  C C    . LYS A 1 44  ? 23.391 -9.601  -11.849 1.00 12.32 ? 44  LYS A C    1 
ATOM   356  O O    . LYS A 1 44  ? 24.266 -9.116  -12.580 1.00 14.20 ? 44  LYS A O    1 
ATOM   357  C CB   . LYS A 1 44  ? 21.520 -8.002  -11.337 1.00 13.24 ? 44  LYS A CB   1 
ATOM   358  C CG   . LYS A 1 44  ? 20.296 -8.867  -11.489 1.00 15.22 ? 44  LYS A CG   1 
ATOM   359  C CD   . LYS A 1 44  ? 19.139 -8.135  -12.169 1.00 15.45 ? 44  LYS A CD   1 
ATOM   360  C CE   . LYS A 1 44  ? 17.957 -9.054  -12.385 1.00 17.49 ? 44  LYS A CE   1 
ATOM   361  N NZ   . LYS A 1 44  ? 16.918 -8.440  -13.274 1.00 18.94 ? 44  LYS A NZ   1 
ATOM   362  H H    . LYS A 1 44  ? 24.357 -7.680  -10.957 1.00 14.97 ? 44  LYS A H    1 
ATOM   363  H HA   . LYS A 1 44  ? 22.426 -9.303  -10.046 1.00 16.16 ? 44  LYS A HA   1 
ATOM   364  H HB2  . LYS A 1 44  ? 21.295 -7.274  -10.737 1.00 15.89 ? 44  LYS A HB2  1 
ATOM   365  H HB3  . LYS A 1 44  ? 21.745 -7.652  -12.213 1.00 15.89 ? 44  LYS A HB3  1 
ATOM   366  H HG2  . LYS A 1 44  ? 20.520 -9.642  -12.029 1.00 18.27 ? 44  LYS A HG2  1 
ATOM   367  H HG3  . LYS A 1 44  ? 19.997 -9.151  -10.611 1.00 18.27 ? 44  LYS A HG3  1 
ATOM   368  H HD2  . LYS A 1 44  ? 18.853 -7.396  -11.611 1.00 18.54 ? 44  LYS A HD2  1 
ATOM   369  H HD3  . LYS A 1 44  ? 19.431 -7.805  -13.033 1.00 18.54 ? 44  LYS A HD3  1 
ATOM   370  H HE2  . LYS A 1 44  ? 18.263 -9.875  -12.801 1.00 20.99 ? 44  LYS A HE2  1 
ATOM   371  H HE3  . LYS A 1 44  ? 17.545 -9.249  -11.529 1.00 20.99 ? 44  LYS A HE3  1 
ATOM   372  H HZ1  . LYS A 1 44  ? 16.231 -8.998  -13.370 1.00 22.73 ? 44  LYS A HZ1  1 
ATOM   373  H HZ2  . LYS A 1 44  ? 16.625 -7.679  -12.919 1.00 22.73 ? 44  LYS A HZ2  1 
ATOM   374  H HZ3  . LYS A 1 44  ? 17.265 -8.269  -14.076 1.00 22.73 ? 44  LYS A HZ3  1 
ATOM   375  N N    . ASN A 1 45  ? 23.028 -10.878 -11.917 1.00 14.23 ? 45  ASN A N    1 
ATOM   376  C CA   . ASN A 1 45  ? 23.671 -11.746 -12.907 1.00 15.41 ? 45  ASN A CA   1 
ATOM   377  C C    . ASN A 1 45  ? 23.150 -11.520 -14.311 1.00 14.05 ? 45  ASN A C    1 
ATOM   378  O O    . ASN A 1 45  ? 23.818 -11.914 -15.281 1.00 16.23 ? 45  ASN A O    1 
ATOM   379  C CB   . ASN A 1 45  ? 23.501 -13.210 -12.512 1.00 16.39 ? 45  ASN A CB   1 
ATOM   380  C CG   . ASN A 1 45  ? 24.350 -13.580 -11.322 1.00 16.46 ? 45  ASN A CG   1 
ATOM   381  O OD1  . ASN A 1 45  ? 25.570 -13.529 -11.401 1.00 19.11 ? 45  ASN A OD1  1 
ATOM   382  N ND2  . ASN A 1 45  ? 23.707 -13.874 -10.212 1.00 17.67 ? 45  ASN A ND2  1 
ATOM   383  H H    . ASN A 1 45  ? 22.436 -11.255 -11.421 1.00 17.08 ? 45  ASN A H    1 
ATOM   384  H HA   . ASN A 1 45  ? 24.622 -11.555 -12.918 1.00 18.50 ? 45  ASN A HA   1 
ATOM   385  H HB2  . ASN A 1 45  ? 22.573 -13.372 -12.283 1.00 19.66 ? 45  ASN A HB2  1 
ATOM   386  H HB3  . ASN A 1 45  ? 23.763 -13.773 -13.257 1.00 19.66 ? 45  ASN A HB3  1 
ATOM   387  H HD21 . ASN A 1 45  ? 24.146 -14.092 -9.505  1.00 21.20 ? 45  ASN A HD21 1 
ATOM   388  H HD22 . ASN A 1 45  ? 22.847 -13.849 -10.193 1.00 21.20 ? 45  ASN A HD22 1 
ATOM   389  N N    . THR A 1 46  ? 21.984 -10.913 -14.451 1.00 15.98 ? 46  THR A N    1 
ATOM   390  C CA   . THR A 1 46  ? 21.360 -10.635 -15.745 1.00 16.85 ? 46  THR A CA   1 
ATOM   391  C C    . THR A 1 46  ? 21.001 -9.156  -15.790 1.00 15.25 ? 46  THR A C    1 
ATOM   392  O O    . THR A 1 46  ? 21.116 -8.432  -14.790 1.00 15.73 ? 46  THR A O    1 
ATOM   393  C CB   . THR A 1 46  ? 20.104 -11.489 -15.942 1.00 19.30 ? 46  THR A CB   1 
ATOM   394  O OG1  . THR A 1 46  ? 19.224 -11.295 -14.829 1.00 19.50 ? 46  THR A OG1  1 
ATOM   395  C CG2  . THR A 1 46  ? 20.460 -12.961 -16.069 1.00 20.29 ? 46  THR A CG2  1 
ATOM   396  H H    . THR A 1 46  ? 21.511 -10.639 -13.787 1.00 19.18 ? 46  THR A H    1 
ATOM   397  H HA   . THR A 1 46  ? 21.987 -10.836 -16.458 1.00 20.22 ? 46  THR A HA   1 
ATOM   398  H HB   . THR A 1 46  ? 19.656 -11.225 -16.761 1.00 23.15 ? 46  THR A HB   1 
ATOM   399  H HG1  . THR A 1 46  ? 19.604 -11.532 -14.118 1.00 23.40 ? 46  THR A HG1  1 
ATOM   400  H HG21 . THR A 1 46  ? 19.654 -13.488 -16.186 1.00 24.34 ? 46  THR A HG21 1 
ATOM   401  H HG22 . THR A 1 46  ? 21.040 -13.097 -16.834 1.00 24.34 ? 46  THR A HG22 1 
ATOM   402  H HG23 . THR A 1 46  ? 20.919 -13.261 -15.269 1.00 24.34 ? 46  THR A HG23 1 
ATOM   403  N N    . ALA A 1 47  ? 20.511 -8.704  -16.943 1.00 17.51 ? 47  ALA A N    1 
ATOM   404  C CA   . ALA A 1 47  ? 20.158 -7.301  -17.093 1.00 16.41 ? 47  ALA A CA   1 
ATOM   405  C C    . ALA A 1 47  ? 19.049 -6.900  -16.123 1.00 16.56 ? 47  ALA A C    1 
ATOM   406  O O    . ALA A 1 47  ? 18.171 -7.697  -15.782 1.00 17.83 ? 47  ALA A O    1 
ATOM   407  C CB   . ALA A 1 47  ? 19.658 -7.043  -18.516 1.00 17.83 ? 47  ALA A CB   1 
ATOM   408  H H    . ALA A 1 47  ? 20.376 -9.185  -17.643 1.00 21.01 ? 47  ALA A H    1 
ATOM   409  H HA   . ALA A 1 47  ? 20.945 -6.764  -16.911 1.00 19.69 ? 47  ALA A HA   1 
ATOM   410  H HB1  . ALA A 1 47  ? 19.405 -6.110  -18.597 1.00 21.39 ? 47  ALA A HB1  1 
ATOM   411  H HB2  . ALA A 1 47  ? 20.368 -7.249  -19.143 1.00 21.39 ? 47  ALA A HB2  1 
ATOM   412  H HB3  . ALA A 1 47  ? 18.889 -7.610  -18.688 1.00 21.39 ? 47  ALA A HB3  1 
ATOM   413  N N    . TYR A 1 48  ? 19.071 -5.631  -15.714 1.00 17.45 ? 48  TYR A N    1 
ATOM   414  C CA   . TYR A 1 48  ? 17.986 -5.080  -14.905 1.00 17.28 ? 48  TYR A CA   1 
ATOM   415  C C    . TYR A 1 48  ? 16.725 -4.916  -15.757 1.00 19.72 ? 48  TYR A C    1 
ATOM   416  O O    . TYR A 1 48  ? 16.793 -4.593  -16.947 1.00 19.83 ? 48  TYR A O    1 
ATOM   417  C CB   . TYR A 1 48  ? 18.393 -3.726  -14.298 1.00 16.77 ? 48  TYR A CB   1 
ATOM   418  C CG   . TYR A 1 48  ? 19.559 -3.892  -13.359 1.00 15.38 ? 48  TYR A CG   1 
ATOM   419  C CD1  . TYR A 1 48  ? 19.361 -4.266  -12.024 1.00 14.83 ? 48  TYR A CD1  1 
ATOM   420  C CD2  . TYR A 1 48  ? 20.853 -3.700  -13.781 1.00 15.73 ? 48  TYR A CD2  1 
ATOM   421  C CE1  . TYR A 1 48  ? 20.415 -4.451  -11.164 1.00 13.96 ? 48  TYR A CE1  1 
ATOM   422  C CE2  . TYR A 1 48  ? 21.928 -3.878  -12.915 1.00 16.08 ? 48  TYR A CE2  1 
ATOM   423  C CZ   . TYR A 1 48  ? 21.698 -4.271  -11.605 1.00 12.48 ? 48  TYR A CZ   1 
ATOM   424  O OH   . TYR A 1 48  ? 22.763 -4.464  -10.777 1.00 14.07 ? 48  TYR A OH   1 
ATOM   425  H H    . TYR A 1 48  ? 19.700 -5.071  -15.891 1.00 20.94 ? 48  TYR A H    1 
ATOM   426  H HA   . TYR A 1 48  ? 17.788 -5.684  -14.172 1.00 20.74 ? 48  TYR A HA   1 
ATOM   427  H HB2  . TYR A 1 48  ? 18.652 -3.117  -15.008 1.00 20.12 ? 48  TYR A HB2  1 
ATOM   428  H HB3  . TYR A 1 48  ? 17.646 -3.357  -13.801 1.00 20.12 ? 48  TYR A HB3  1 
ATOM   429  H HD1  . TYR A 1 48  ? 18.494 -4.393  -11.713 1.00 17.80 ? 48  TYR A HD1  1 
ATOM   430  H HD2  . TYR A 1 48  ? 21.013 -3.447  -14.662 1.00 18.88 ? 48  TYR A HD2  1 
ATOM   431  H HE1  . TYR A 1 48  ? 20.258 -4.697  -10.281 1.00 16.75 ? 48  TYR A HE1  1 
ATOM   432  H HE2  . TYR A 1 48  ? 22.797 -3.734  -13.213 1.00 19.30 ? 48  TYR A HE2  1 
ATOM   433  H HH   . TYR A 1 48  ? 23.479 -4.310  -11.189 1.00 16.89 ? 48  TYR A HH   1 
ATOM   434  N N    . THR A 1 49  ? 15.550 -5.124  -15.146 1.00 19.38 ? 49  THR A N    1 
ATOM   435  C CA   . THR A 1 49  ? 14.297 -4.832  -15.833 1.00 17.92 ? 49  THR A CA   1 
ATOM   436  C C    . THR A 1 49  ? 14.096 -3.320  -15.925 1.00 19.24 ? 49  THR A C    1 
ATOM   437  O O    . THR A 1 49  ? 14.770 -2.541  -15.258 1.00 19.13 ? 49  THR A O    1 
ATOM   438  C CB   . THR A 1 49  ? 13.113 -5.421  -15.072 1.00 20.27 ? 49  THR A CB   1 
ATOM   439  O OG1  . THR A 1 49  ? 13.006 -4.773  -13.804 1.00 20.86 ? 49  THR A OG1  1 
ATOM   440  C CG2  . THR A 1 49  ? 13.262 -6.910  -14.879 1.00 23.72 ? 49  THR A CG2  1 
ATOM   441  H H    . THR A 1 49  ? 15.459 -5.428  -14.347 1.00 23.25 ? 49  THR A H    1 
ATOM   442  H HA   . THR A 1 49  ? 14.332 -5.221  -16.721 1.00 21.51 ? 49  THR A HA   1 
ATOM   443  H HB   . THR A 1 49  ? 12.300 -5.281  -15.583 1.00 24.32 ? 49  THR A HB   1 
ATOM   444  H HG1  . THR A 1 49  ? 12.399 -5.133  -13.348 1.00 25.03 ? 49  THR A HG1  1 
ATOM   445  H HG21 . THR A 1 49  ? 12.455 -7.276  -14.484 1.00 28.46 ? 49  THR A HG21 1 
ATOM   446  H HG22 . THR A 1 49  ? 13.419 -7.342  -15.733 1.00 28.46 ? 49  THR A HG22 1 
ATOM   447  H HG23 . THR A 1 49  ? 14.011 -7.095  -14.291 1.00 28.46 ? 49  THR A HG23 1 
ATOM   448  N N    . ASP A 1 50  ? 13.121 -2.896  -16.733 1.00 21.24 ? 50  ASP A N    1 
ATOM   449  C CA   . ASP A 1 50  ? 12.808 -1.469  -16.801 1.00 22.53 ? 50  ASP A CA   1 
ATOM   450  C C    . ASP A 1 50  ? 12.439 -0.921  -15.423 1.00 22.22 ? 50  ASP A C    1 
ATOM   451  O O    . ASP A 1 50  ? 12.870 0.173   -15.047 1.00 20.50 ? 50  ASP A O    1 
ATOM   452  C CB   . ASP A 1 50  ? 11.667 -1.233  -17.801 1.00 23.35 ? 50  ASP A CB   1 
ATOM   453  C CG   . ASP A 1 50  ? 11.431 0.251   -18.091 1.00 36.22 ? 50  ASP A CG   1 
ATOM   454  O OD1  . ASP A 1 50  ? 10.248 0.659   -18.118 1.00 45.30 ? 50  ASP A OD1  1 
ATOM   455  O OD2  . ASP A 1 50  ? 12.407 0.999   -18.328 1.00 38.02 ? 50  ASP A OD2  1 
ATOM   456  H H    . ASP A 1 50  ? 12.639 -3.399  -17.237 1.00 25.49 ? 50  ASP A H    1 
ATOM   457  H HA   . ASP A 1 50  ? 13.589 -0.987  -17.117 1.00 27.03 ? 50  ASP A HA   1 
ATOM   458  H HB2  . ASP A 1 50  ? 11.885 -1.670  -18.639 1.00 28.03 ? 50  ASP A HB2  1 
ATOM   459  H HB3  . ASP A 1 50  ? 10.847 -1.602  -17.438 1.00 28.03 ? 50  ASP A HB3  1 
ATOM   460  N N    . GLU A 1 51  ? 11.635 -1.670  -14.656 1.00 20.35 ? 51  GLU A N    1 
ATOM   461  C CA   . GLU A 1 51  ? 11.278 -1.255  -13.303 1.00 19.86 ? 51  GLU A CA   1 
ATOM   462  C C    . GLU A 1 51  ? 12.522 -1.101  -12.434 1.00 19.29 ? 51  GLU A C    1 
ATOM   463  O O    . GLU A 1 51  ? 12.628 -0.152  -11.633 1.00 19.07 ? 51  GLU A O    1 
ATOM   464  C CB   . GLU A 1 51  ? 10.324 -2.272  -12.679 1.00 22.14 ? 51  GLU A CB   1 
ATOM   465  C CG   . GLU A 1 51  ? 9.969  -1.998  -11.231 1.00 25.67 ? 51  GLU A CG   1 
ATOM   466  C CD   . GLU A 1 51  ? 9.219  -3.134  -10.531 1.00 31.33 ? 51  GLU A CD   1 
ATOM   467  O OE1  . GLU A 1 51  ? 9.343  -4.322  -10.908 1.00 33.27 ? 51  GLU A OE1  1 
ATOM   468  O OE2  . GLU A 1 51  ? 8.486  -2.806  -9.571  1.00 38.12 ? 51  GLU A OE2  1 
ATOM   469  H H    . GLU A 1 51  ? 11.287 -2.418  -14.898 1.00 24.42 ? 51  GLU A H    1 
ATOM   470  H HA   . GLU A 1 51  ? 10.825 -0.399  -13.347 1.00 23.83 ? 51  GLU A HA   1 
ATOM   471  H HB2  . GLU A 1 51  ? 9.498  -2.273  -13.188 1.00 26.57 ? 51  GLU A HB2  1 
ATOM   472  H HB3  . GLU A 1 51  ? 10.739 -3.148  -12.717 1.00 26.57 ? 51  GLU A HB3  1 
ATOM   473  H HG2  . GLU A 1 51  ? 10.789 -1.841  -10.736 1.00 30.81 ? 51  GLU A HG2  1 
ATOM   474  H HG3  . GLU A 1 51  ? 9.404  -1.210  -11.196 1.00 30.81 ? 51  GLU A HG3  1 
ATOM   475  N N    . GLU A 1 52  ? 13.463 -2.039  -12.549 1.00 18.95 ? 52  GLU A N    1 
ATOM   476  C CA   . GLU A 1 52  ? 14.696 -1.971  -11.769 1.00 16.64 ? 52  GLU A CA   1 
ATOM   477  C C    . GLU A 1 52  ? 15.554 -0.785  -12.185 1.00 15.57 ? 52  GLU A C    1 
ATOM   478  O O    . GLU A 1 52  ? 16.149 -0.126  -11.331 1.00 15.41 ? 52  GLU A O    1 
ATOM   479  C CB   . GLU A 1 52  ? 15.473 -3.284  -11.859 1.00 17.25 ? 52  GLU A CB   1 
ATOM   480  C CG   . GLU A 1 52  ? 14.782 -4.402  -11.119 1.00 18.70 ? 52  GLU A CG   1 
ATOM   481  C CD   . GLU A 1 52  ? 15.400 -5.761  -11.347 1.00 19.40 ? 52  GLU A CD   1 
ATOM   482  O OE1  . GLU A 1 52  ? 15.996 -5.970  -12.423 1.00 18.66 ? 52  GLU A OE1  1 
ATOM   483  O OE2  . GLU A 1 52  ? 15.229 -6.648  -10.492 1.00 22.47 ? 52  GLU A OE2  1 
ATOM   484  H H    . GLU A 1 52  ? 13.412 -2.722  -13.070 1.00 22.74 ? 52  GLU A H    1 
ATOM   485  H HA   . GLU A 1 52  ? 14.460 -1.849  -10.836 1.00 19.96 ? 52  GLU A HA   1 
ATOM   486  H HB2  . GLU A 1 52  ? 15.556 -3.542  -12.791 1.00 20.70 ? 52  GLU A HB2  1 
ATOM   487  H HB3  . GLU A 1 52  ? 16.353 -3.161  -11.470 1.00 20.70 ? 52  GLU A HB3  1 
ATOM   488  H HG2  . GLU A 1 52  ? 14.819 -4.216  -10.168 1.00 22.44 ? 52  GLU A HG2  1 
ATOM   489  H HG3  . GLU A 1 52  ? 13.858 -4.445  -11.413 1.00 22.44 ? 52  GLU A HG3  1 
ATOM   490  N N    . ILE A 1 53  ? 15.629 -0.489  -13.485 1.00 18.08 ? 53  ILE A N    1 
ATOM   491  C CA   . ILE A 1 53  ? 16.357 0.698   -13.924 1.00 17.73 ? 53  ILE A CA   1 
ATOM   492  C C    . ILE A 1 53  ? 15.719 1.965   -13.356 1.00 19.02 ? 53  ILE A C    1 
ATOM   493  O O    . ILE A 1 53  ? 16.422 2.882   -12.905 1.00 17.15 ? 53  ILE A O    1 
ATOM   494  C CB   . ILE A 1 53  ? 16.439 0.732   -15.467 1.00 18.31 ? 53  ILE A CB   1 
ATOM   495  C CG1  . ILE A 1 53  ? 17.341 -0.395  -15.989 1.00 18.29 ? 53  ILE A CG1  1 
ATOM   496  C CG2  . ILE A 1 53  ? 16.900 2.104   -15.932 1.00 21.46 ? 53  ILE A CG2  1 
ATOM   497  C CD1  . ILE A 1 53  ? 18.789 -0.311  -15.582 1.00 18.57 ? 53  ILE A CD1  1 
ATOM   498  H H    . ILE A 1 53  ? 15.274 -0.950  -14.119 1.00 21.70 ? 53  ILE A H    1 
ATOM   499  H HA   . ILE A 1 53  ? 17.262 0.649   -13.578 1.00 21.27 ? 53  ILE A HA   1 
ATOM   500  H HB   . ILE A 1 53  ? 15.556 0.577   -15.836 1.00 21.97 ? 53  ILE A HB   1 
ATOM   501  H HG12 . ILE A 1 53  ? 16.997 -1.239  -15.657 1.00 21.94 ? 53  ILE A HG12 1 
ATOM   502  H HG13 . ILE A 1 53  ? 17.313 -0.383  -16.958 1.00 21.94 ? 53  ILE A HG13 1 
ATOM   503  H HG21 . ILE A 1 53  ? 17.173 2.048   -16.861 1.00 25.75 ? 53  ILE A HG21 1 
ATOM   504  H HG22 . ILE A 1 53  ? 16.165 2.731   -15.840 1.00 25.75 ? 53  ILE A HG22 1 
ATOM   505  H HG23 . ILE A 1 53  ? 17.648 2.389   -15.384 1.00 25.75 ? 53  ILE A HG23 1 
ATOM   506  H HD11 . ILE A 1 53  ? 19.291 -0.990  -16.059 1.00 22.29 ? 53  ILE A HD11 1 
ATOM   507  H HD12 . ILE A 1 53  ? 19.129 0.570   -15.806 1.00 22.29 ? 53  ILE A HD12 1 
ATOM   508  H HD13 . ILE A 1 53  ? 18.857 -0.459  -14.626 1.00 22.29 ? 53  ILE A HD13 1 
ATOM   509  N N    . ASN A 1 54  ? 14.393 2.039   -13.361 1.00 19.38 ? 54  ASN A N    1 
ATOM   510  C CA   . ASN A 1 54  ? 13.743 3.204   -12.760 1.00 19.73 ? 54  ASN A CA   1 
ATOM   511  C C    . ASN A 1 54  ? 14.086 3.337   -11.287 1.00 17.87 ? 54  ASN A C    1 
ATOM   512  O O    . ASN A 1 54  ? 14.324 4.444   -10.792 1.00 20.38 ? 54  ASN A O    1 
ATOM   513  C CB   . ASN A 1 54  ? 12.229 3.125   -12.934 1.00 21.59 ? 54  ASN A CB   1 
ATOM   514  C CG   . ASN A 1 54  ? 11.789 3.280   -14.354 1.00 27.88 ? 54  ASN A CG   1 
ATOM   515  O OD1  . ASN A 1 54  ? 12.536 3.758   -15.206 1.00 32.25 ? 54  ASN A OD1  1 
ATOM   516  N ND2  . ASN A 1 54  ? 10.583 2.827   -14.628 1.00 31.89 ? 54  ASN A ND2  1 
ATOM   517  H H    . ASN A 1 54  ? 13.862 1.450   -13.694 1.00 23.26 ? 54  ASN A H    1 
ATOM   518  H HA   . ASN A 1 54  ? 14.062 3.994   -13.224 1.00 23.67 ? 54  ASN A HA   1 
ATOM   519  H HB2  . ASN A 1 54  ? 11.921 2.260   -12.619 1.00 25.90 ? 54  ASN A HB2  1 
ATOM   520  H HB3  . ASN A 1 54  ? 11.816 3.833   -12.415 1.00 25.90 ? 54  ASN A HB3  1 
ATOM   521  H HD21 . ASN A 1 54  ? 10.273 2.887   -15.428 1.00 38.27 ? 54  ASN A HD21 1 
ATOM   522  H HD22 . ASN A 1 54  ? 10.106 2.470   -14.008 1.00 38.27 ? 54  ASN A HD22 1 
ATOM   523  N N    . TYR A 1 55  ? 14.130 2.214   -10.576 1.00 16.88 ? 55  TYR A N    1 
ATOM   524  C CA   . TYR A 1 55  ? 14.517 2.222   -9.177  1.00 17.63 ? 55  TYR A CA   1 
ATOM   525  C C    . TYR A 1 55  ? 15.947 2.725   -9.020  1.00 17.56 ? 55  TYR A C    1 
ATOM   526  O O    . TYR A 1 55  ? 16.216 3.627   -8.227  1.00 16.61 ? 55  TYR A O    1 
ATOM   527  C CB   . TYR A 1 55  ? 14.374 0.803   -8.641  1.00 18.41 ? 55  TYR A CB   1 
ATOM   528  C CG   . TYR A 1 55  ? 14.731 0.578   -7.197  1.00 16.95 ? 55  TYR A CG   1 
ATOM   529  C CD1  . TYR A 1 55  ? 14.002 1.157   -6.162  1.00 20.00 ? 55  TYR A CD1  1 
ATOM   530  C CD2  . TYR A 1 55  ? 15.778 -0.249  -6.854  1.00 16.54 ? 55  TYR A CD2  1 
ATOM   531  C CE1  . TYR A 1 55  ? 14.325 0.916   -4.828  1.00 20.52 ? 55  TYR A CE1  1 
ATOM   532  C CE2  . TYR A 1 55  ? 16.114 -0.488  -5.522  1.00 16.07 ? 55  TYR A CE2  1 
ATOM   533  C CZ   . TYR A 1 55  ? 15.379 0.094   -4.534  1.00 17.24 ? 55  TYR A CZ   1 
ATOM   534  O OH   . TYR A 1 55  ? 15.703 -0.155  -3.222  1.00 22.34 ? 55  TYR A OH   1 
ATOM   535  H H    . TYR A 1 55  ? 13.940 1.434   -10.884 1.00 20.26 ? 55  TYR A H    1 
ATOM   536  H HA   . TYR A 1 55  ? 13.942 2.813   -8.666  1.00 21.15 ? 55  TYR A HA   1 
ATOM   537  H HB2  . TYR A 1 55  ? 13.447 0.536   -8.747  1.00 22.09 ? 55  TYR A HB2  1 
ATOM   538  H HB3  . TYR A 1 55  ? 14.948 0.225   -9.167  1.00 22.09 ? 55  TYR A HB3  1 
ATOM   539  H HD1  . TYR A 1 55  ? 13.285 1.714   -6.365  1.00 24.00 ? 55  TYR A HD1  1 
ATOM   540  H HD2  . TYR A 1 55  ? 16.272 -0.659  -7.527  1.00 19.85 ? 55  TYR A HD2  1 
ATOM   541  H HE1  . TYR A 1 55  ? 13.830 1.309   -4.146  1.00 24.63 ? 55  TYR A HE1  1 
ATOM   542  H HE2  . TYR A 1 55  ? 16.833 -1.039  -5.310  1.00 19.28 ? 55  TYR A HE2  1 
ATOM   543  H HH   . TYR A 1 55  ? 16.400 -0.621  -3.181  1.00 26.81 ? 55  TYR A HH   1 
ATOM   544  N N    . LEU A 1 56  ? 16.885 2.174   -9.786  1.00 15.91 ? 56  LEU A N    1 
ATOM   545  C CA   . LEU A 1 56  ? 18.263 2.630   -9.697  1.00 15.20 ? 56  LEU A CA   1 
ATOM   546  C C    . LEU A 1 56  ? 18.375 4.131   -9.952  1.00 17.02 ? 56  LEU A C    1 
ATOM   547  O O    . LEU A 1 56  ? 19.119 4.835   -9.261  1.00 15.46 ? 56  LEU A O    1 
ATOM   548  C CB   . LEU A 1 56  ? 19.160 1.862   -10.664 1.00 16.50 ? 56  LEU A CB   1 
ATOM   549  C CG   . LEU A 1 56  ? 19.334 0.394   -10.335 1.00 14.98 ? 56  LEU A CG   1 
ATOM   550  C CD1  . LEU A 1 56  ? 20.152 -0.328  -11.379 1.00 17.95 ? 56  LEU A CD1  1 
ATOM   551  C CD2  . LEU A 1 56  ? 20.016 0.189   -8.984  1.00 18.27 ? 56  LEU A CD2  1 
ATOM   552  H H    . LEU A 1 56  ? 16.750 1.544   -10.356 1.00 19.09 ? 56  LEU A H    1 
ATOM   553  H HA   . LEU A 1 56  ? 18.573 2.449   -8.796  1.00 18.25 ? 56  LEU A HA   1 
ATOM   554  H HB2  . LEU A 1 56  ? 18.776 1.919   -11.552 1.00 19.80 ? 56  LEU A HB2  1 
ATOM   555  H HB3  . LEU A 1 56  ? 20.041 2.269   -10.656 1.00 19.80 ? 56  LEU A HB3  1 
ATOM   556  H HG   . LEU A 1 56  ? 18.440 0.018   -10.309 1.00 17.98 ? 56  LEU A HG   1 
ATOM   557  H HD11 . LEU A 1 56  ? 20.222 -1.263  -11.134 1.00 21.54 ? 56  LEU A HD11 1 
ATOM   558  H HD12 . LEU A 1 56  ? 19.711 -0.243  -12.239 1.00 21.54 ? 56  LEU A HD12 1 
ATOM   559  H HD13 . LEU A 1 56  ? 21.035 0.071   -11.420 1.00 21.54 ? 56  LEU A HD13 1 
ATOM   560  H HD21 . LEU A 1 56  ? 20.253 -0.747  -8.889  1.00 21.93 ? 56  LEU A HD21 1 
ATOM   561  H HD22 . LEU A 1 56  ? 20.815 0.738   -8.947  1.00 21.93 ? 56  LEU A HD22 1 
ATOM   562  H HD23 . LEU A 1 56  ? 19.404 0.449   -8.278  1.00 21.93 ? 56  LEU A HD23 1 
ATOM   563  N N    . ALA A 1 57  ? 17.695 4.629   -10.977 1.00 17.14 ? 57  ALA A N    1 
ATOM   564  C CA   . ALA A 1 57  ? 17.797 6.026   -11.374 1.00 16.77 ? 57  ALA A CA   1 
ATOM   565  C C    . ALA A 1 57  ? 17.256 6.980   -10.322 1.00 18.62 ? 57  ALA A C    1 
ATOM   566  O O    . ALA A 1 57  ? 17.506 8.189   -10.418 1.00 20.18 ? 57  ALA A O    1 
ATOM   567  C CB   . ALA A 1 57  ? 17.049 6.230   -12.701 1.00 19.22 ? 57  ALA A CB   1 
ATOM   568  H H    . ALA A 1 57  ? 17.157 4.172   -11.468 1.00 20.56 ? 57  ALA A H    1 
ATOM   569  H HA   . ALA A 1 57  ? 18.733 6.245   -11.506 1.00 20.13 ? 57  ALA A HA   1 
ATOM   570  H HB1  . ALA A 1 57  ? 17.103 7.166   -12.953 1.00 23.06 ? 57  ALA A HB1  1 
ATOM   571  H HB2  . ALA A 1 57  ? 17.461 5.679   -13.385 1.00 23.06 ? 57  ALA A HB2  1 
ATOM   572  H HB3  . ALA A 1 57  ? 16.121 5.973   -12.583 1.00 23.06 ? 57  ALA A HB3  1 
ATOM   573  N N    . SER A 1 58  ? 16.534 6.470   -9.326  1.00 17.38 ? 58  SER A N    1 
ATOM   574  C CA   . SER A 1 58  ? 16.019 7.301   -8.249  1.00 18.39 ? 58  SER A CA   1 
ATOM   575  C C    . SER A 1 58  ? 17.048 7.580   -7.163  1.00 15.97 ? 58  SER A C    1 
ATOM   576  O O    . SER A 1 58  ? 16.771 8.389   -6.266  1.00 19.46 ? 58  SER A O    1 
ATOM   577  C CB   . SER A 1 58  ? 14.768 6.665   -7.620  1.00 18.05 ? 58  SER A CB   1 
ATOM   578  O OG   . SER A 1 58  ? 15.077 5.589   -6.762  1.00 19.65 ? 58  SER A OG   1 
ATOM   579  H H    . SER A 1 58  ? 16.328 5.638   -9.253  1.00 20.86 ? 58  SER A H    1 
ATOM   580  H HA   . SER A 1 58  ? 15.752 8.152   -8.632  1.00 22.06 ? 58  SER A HA   1 
ATOM   581  H HB2  . SER A 1 58  ? 14.302 7.344   -7.107  1.00 21.66 ? 58  SER A HB2  1 
ATOM   582  H HB3  . SER A 1 58  ? 14.197 6.337   -8.332  1.00 21.66 ? 58  SER A HB3  1 
ATOM   583  H HG   . SER A 1 58  ? 15.487 4.992   -7.187  1.00 23.58 ? 58  SER A HG   1 
ATOM   584  N N    . PHE A 1 59  ? 18.214 6.920   -7.183  1.00 15.19 ? 59  PHE A N    1 
ATOM   585  C CA   . PHE A 1 59  ? 19.293 7.137   -6.225  1.00 16.61 ? 59  PHE A CA   1 
ATOM   586  C C    . PHE A 1 59  ? 20.263 8.196   -6.729  1.00 15.55 ? 59  PHE A C    1 
ATOM   587  O O    . PHE A 1 59  ? 20.589 8.232   -7.937  1.00 17.63 ? 59  PHE A O    1 
ATOM   588  C CB   . PHE A 1 59  ? 20.045 5.831   -5.949  1.00 15.60 ? 59  PHE A CB   1 
ATOM   589  C CG   . PHE A 1 59  ? 19.219 4.830   -5.215  1.00 13.12 ? 59  PHE A CG   1 
ATOM   590  C CD1  . PHE A 1 59  ? 18.368 4.000   -5.907  1.00 15.21 ? 59  PHE A CD1  1 
ATOM   591  C CD2  . PHE A 1 59  ? 19.239 4.750   -3.841  1.00 13.78 ? 59  PHE A CD2  1 
ATOM   592  C CE1  . PHE A 1 59  ? 17.545 3.110   -5.253  1.00 15.43 ? 59  PHE A CE1  1 
ATOM   593  C CE2  . PHE A 1 59  ? 18.432 3.860   -3.161  1.00 16.56 ? 59  PHE A CE2  1 
ATOM   594  C CZ   . PHE A 1 59  ? 17.581 3.028   -3.859  1.00 16.59 ? 59  PHE A CZ   1 
ATOM   595  H H    . PHE A 1 59  ? 18.409 6.319   -7.766  1.00 18.23 ? 59  PHE A H    1 
ATOM   596  H HA   . PHE A 1 59  ? 18.921 7.454   -5.387  1.00 19.93 ? 59  PHE A HA   1 
ATOM   597  H HB2  . PHE A 1 59  ? 20.312 5.437   -6.794  1.00 18.72 ? 59  PHE A HB2  1 
ATOM   598  H HB3  . PHE A 1 59  ? 20.828 6.026   -5.412  1.00 18.72 ? 59  PHE A HB3  1 
ATOM   599  H HD1  . PHE A 1 59  ? 18.348 4.041   -6.836  1.00 18.26 ? 59  PHE A HD1  1 
ATOM   600  H HD2  . PHE A 1 59  ? 19.807 5.308   -3.361  1.00 16.54 ? 59  PHE A HD2  1 
ATOM   601  H HE1  . PHE A 1 59  ? 16.968 2.565   -5.738  1.00 18.52 ? 59  PHE A HE1  1 
ATOM   602  H HE2  . PHE A 1 59  ? 18.463 3.821   -2.232  1.00 19.87 ? 59  PHE A HE2  1 
ATOM   603  H HZ   . PHE A 1 59  ? 17.039 2.422   -3.407  1.00 19.91 ? 59  PHE A HZ   1 
ATOM   604  N N    . PRO A 1 60  ? 20.766 9.071   -5.855  1.00 14.09 ? 60  PRO A N    1 
ATOM   605  C CA   . PRO A 1 60  ? 21.706 10.104  -6.327  1.00 14.56 ? 60  PRO A CA   1 
ATOM   606  C C    . PRO A 1 60  ? 23.068 9.545   -6.685  1.00 13.44 ? 60  PRO A C    1 
ATOM   607  O O    . PRO A 1 60  ? 23.773 10.145  -7.513  1.00 15.39 ? 60  PRO A O    1 
ATOM   608  C CB   . PRO A 1 60  ? 21.768 11.091  -5.152  1.00 16.23 ? 60  PRO A CB   1 
ATOM   609  C CG   . PRO A 1 60  ? 21.365 10.256  -3.968  1.00 15.93 ? 60  PRO A CG   1 
ATOM   610  C CD   . PRO A 1 60  ? 20.348 9.272   -4.457  1.00 15.36 ? 60  PRO A CD   1 
ATOM   611  H HA   . PRO A 1 60  ? 21.342 10.566  -7.099  1.00 17.47 ? 60  PRO A HA   1 
ATOM   612  H HB2  . PRO A 1 60  ? 22.669 11.435  -5.050  1.00 19.48 ? 60  PRO A HB2  1 
ATOM   613  H HB3  . PRO A 1 60  ? 21.147 11.822  -5.295  1.00 19.48 ? 60  PRO A HB3  1 
ATOM   614  H HG2  . PRO A 1 60  ? 22.143 9.794   -3.618  1.00 19.12 ? 60  PRO A HG2  1 
ATOM   615  H HG3  . PRO A 1 60  ? 20.983 10.828  -3.284  1.00 19.12 ? 60  PRO A HG3  1 
ATOM   616  H HD2  . PRO A 1 60  ? 20.393 8.444   -3.955  1.00 18.43 ? 60  PRO A HD2  1 
ATOM   617  H HD3  . PRO A 1 60  ? 19.453 9.642   -4.409  1.00 18.43 ? 60  PRO A HD3  1 
ATOM   618  N N    . LEU A 1 61  ? 23.454 8.413   -6.102  1.00 13.77 ? 61  LEU A N    1 
ATOM   619  C CA   . LEU A 1 61  ? 24.790 7.859   -6.270  1.00 13.18 ? 61  LEU A CA   1 
ATOM   620  C C    . LEU A 1 61  ? 24.645 6.346   -6.246  1.00 14.29 ? 61  LEU A C    1 
ATOM   621  O O    . LEU A 1 61  ? 24.110 5.771   -5.288  1.00 13.40 ? 61  LEU A O    1 
ATOM   622  C CB   . LEU A 1 61  ? 25.685 8.339   -5.125  1.00 14.11 ? 61  LEU A CB   1 
ATOM   623  C CG   . LEU A 1 61  ? 27.156 7.930   -5.218  1.00 13.79 ? 61  LEU A CG   1 
ATOM   624  C CD1  . LEU A 1 61  ? 27.834 8.339   -6.508  1.00 14.88 ? 61  LEU A CD1  1 
ATOM   625  C CD2  . LEU A 1 61  ? 27.913 8.466   -3.992  1.00 16.15 ? 61  LEU A CD2  1 
ATOM   626  H H    . LEU A 1 61  ? 22.949 7.938   -5.593  1.00 16.53 ? 61  LEU A H    1 
ATOM   627  H HA   . LEU A 1 61  ? 25.195 8.123   -7.111  1.00 15.82 ? 61  LEU A HA   1 
ATOM   628  H HB2  . LEU A 1 61  ? 25.656 9.308   -5.102  1.00 16.93 ? 61  LEU A HB2  1 
ATOM   629  H HB3  . LEU A 1 61  ? 25.337 7.977   -4.295  1.00 16.93 ? 61  LEU A HB3  1 
ATOM   630  H HG   . LEU A 1 61  ? 27.189 6.960   -5.225  1.00 16.54 ? 61  LEU A HG   1 
ATOM   631  H HD11 . LEU A 1 61  ? 28.782 8.142   -6.443  1.00 17.86 ? 61  LEU A HD11 1 
ATOM   632  H HD12 . LEU A 1 61  ? 27.442 7.842   -7.243  1.00 17.86 ? 61  LEU A HD12 1 
ATOM   633  H HD13 . LEU A 1 61  ? 27.704 9.291   -6.646  1.00 17.86 ? 61  LEU A HD13 1 
ATOM   634  H HD21 . LEU A 1 61  ? 28.839 8.185   -4.045  1.00 19.38 ? 61  LEU A HD21 1 
ATOM   635  H HD22 . LEU A 1 61  ? 27.860 9.435   -3.987  1.00 19.38 ? 61  LEU A HD22 1 
ATOM   636  H HD23 . LEU A 1 61  ? 27.505 8.109   -3.188  1.00 19.38 ? 61  LEU A HD23 1 
ATOM   637  N N    . ILE A 1 62  ? 25.161 5.705   -7.291  1.00 13.05 ? 62  ILE A N    1 
ATOM   638  C CA   . ILE A 1 62  ? 25.030 4.278   -7.540  1.00 12.64 ? 62  ILE A CA   1 
ATOM   639  C C    . ILE A 1 62  ? 26.403 3.740   -7.894  1.00 12.62 ? 62  ILE A C    1 
ATOM   640  O O    . ILE A 1 62  ? 27.029 4.240   -8.846  1.00 14.33 ? 62  ILE A O    1 
ATOM   641  C CB   . ILE A 1 62  ? 24.073 4.000   -8.718  1.00 13.14 ? 62  ILE A CB   1 
ATOM   642  C CG1  . ILE A 1 62  ? 22.716 4.633   -8.498  1.00 14.43 ? 62  ILE A CG1  1 
ATOM   643  C CG2  . ILE A 1 62  ? 23.957 2.507   -8.954  1.00 15.46 ? 62  ILE A CG2  1 
ATOM   644  C CD1  . ILE A 1 62  ? 22.230 5.437   -9.647  1.00 22.71 ? 62  ILE A CD1  1 
ATOM   645  H H    . ILE A 1 62  ? 25.618 6.101   -7.902  1.00 15.66 ? 62  ILE A H    1 
ATOM   646  H HA   . ILE A 1 62  ? 24.700 3.842   -6.739  1.00 15.17 ? 62  ILE A HA   1 
ATOM   647  H HB   . ILE A 1 62  ? 24.448 4.411   -9.513  1.00 15.77 ? 62  ILE A HB   1 
ATOM   648  H HG12 . ILE A 1 62  ? 22.068 3.929   -8.335  1.00 17.32 ? 62  ILE A HG12 1 
ATOM   649  H HG13 . ILE A 1 62  ? 22.768 5.220   -7.728  1.00 17.32 ? 62  ILE A HG13 1 
ATOM   650  H HG21 . ILE A 1 62  ? 23.194 2.336   -9.527  1.00 18.55 ? 62  ILE A HG21 1 
ATOM   651  H HG22 . ILE A 1 62  ? 24.769 2.191   -9.380  1.00 18.55 ? 62  ILE A HG22 1 
ATOM   652  H HG23 . ILE A 1 62  ? 23.837 2.061   -8.101  1.00 18.55 ? 62  ILE A HG23 1 
ATOM   653  H HD11 . ILE A 1 62  ? 21.389 5.856   -9.406  1.00 27.25 ? 62  ILE A HD11 1 
ATOM   654  H HD12 . ILE A 1 62  ? 22.890 6.116   -9.859  1.00 27.25 ? 62  ILE A HD12 1 
ATOM   655  H HD13 . ILE A 1 62  ? 22.101 4.851   -10.410 1.00 27.25 ? 62  ILE A HD13 1 
ATOM   656  N N    . THR A 1 63  ? 26.845 2.702   -7.203  1.00 11.62 ? 63  THR A N    1 
ATOM   657  C CA   . THR A 1 63  ? 28.003 1.934   -7.610  1.00 10.64 ? 63  THR A CA   1 
ATOM   658  C C    . THR A 1 63  ? 27.549 0.622   -8.214  1.00 11.65 ? 63  THR A C    1 
ATOM   659  O O    . THR A 1 63  ? 26.782 -0.141  -7.603  1.00 11.94 ? 63  THR A O    1 
ATOM   660  C CB   . THR A 1 63  ? 28.949 1.650   -6.453  1.00 11.26 ? 63  THR A CB   1 
ATOM   661  O OG1  . THR A 1 63  ? 29.499 2.892   -6.036  1.00 12.48 ? 63  THR A OG1  1 
ATOM   662  C CG2  . THR A 1 63  ? 30.069 0.716   -6.899  1.00 12.13 ? 63  THR A CG2  1 
ATOM   663  H H    . THR A 1 63  ? 26.481 2.418   -6.477  1.00 13.95 ? 63  THR A H    1 
ATOM   664  H HA   . THR A 1 63  ? 28.489 2.450   -8.272  1.00 12.77 ? 63  THR A HA   1 
ATOM   665  H HB   . THR A 1 63  ? 28.484 1.220   -5.719  1.00 13.52 ? 63  THR A HB   1 
ATOM   666  H HG1  . THR A 1 63  ? 30.064 2.766   -5.427  1.00 14.98 ? 63  THR A HG1  1 
ATOM   667  H HG21 . THR A 1 63  ? 30.791 0.729   -6.252  1.00 14.55 ? 63  THR A HG21 1 
ATOM   668  H HG22 . THR A 1 63  ? 29.733 -0.191  -6.977  1.00 14.55 ? 63  THR A HG22 1 
ATOM   669  H HG23 . THR A 1 63  ? 30.413 0.999   -7.761  1.00 14.55 ? 63  THR A HG23 1 
ATOM   670  N N    . LEU A 1 64  ? 28.016 0.361   -9.435  1.00 10.84 ? 64  LEU A N    1 
ATOM   671  C CA   . LEU A 1 64  ? 27.794 -0.924  -10.099 1.00 11.18 ? 64  LEU A CA   1 
ATOM   672  C C    . LEU A 1 64  ? 28.940 -1.847  -9.731  1.00 11.42 ? 64  LEU A C    1 
ATOM   673  O O    . LEU A 1 64  ? 30.088 -1.607  -10.112 1.00 12.82 ? 64  LEU A O    1 
ATOM   674  C CB   . LEU A 1 64  ? 27.666 -0.750  -11.605 1.00 11.85 ? 64  LEU A CB   1 
ATOM   675  C CG   . LEU A 1 64  ? 26.476 0.131   -12.015 1.00 13.42 ? 64  LEU A CG   1 
ATOM   676  C CD1  . LEU A 1 64  ? 26.444 0.341   -13.550 1.00 13.97 ? 64  LEU A CD1  1 
ATOM   677  C CD2  . LEU A 1 64  ? 25.133 -0.419  -11.518 1.00 14.50 ? 64  LEU A CD2  1 
ATOM   678  H H    . LEU A 1 64  ? 28.470 0.919   -9.906  1.00 13.00 ? 64  LEU A H    1 
ATOM   679  H HA   . LEU A 1 64  ? 26.965 -1.317  -9.784  1.00 13.42 ? 64  LEU A HA   1 
ATOM   680  H HB2  . LEU A 1 64  ? 28.475 -0.335  -11.942 1.00 14.22 ? 64  LEU A HB2  1 
ATOM   681  H HB3  . LEU A 1 64  ? 27.547 -1.623  -12.012 1.00 14.22 ? 64  LEU A HB3  1 
ATOM   682  H HG   . LEU A 1 64  ? 26.597 0.993   -11.589 1.00 16.10 ? 64  LEU A HG   1 
ATOM   683  H HD11 . LEU A 1 64  ? 25.698 0.917   -13.774 1.00 16.76 ? 64  LEU A HD11 1 
ATOM   684  H HD12 . LEU A 1 64  ? 27.277 0.753   -13.829 1.00 16.76 ? 64  LEU A HD12 1 
ATOM   685  H HD13 . LEU A 1 64  ? 26.340 -0.520  -13.984 1.00 16.76 ? 64  LEU A HD13 1 
ATOM   686  H HD21 . LEU A 1 64  ? 24.413 0.090   -11.924 1.00 17.40 ? 64  LEU A HD21 1 
ATOM   687  H HD22 . LEU A 1 64  ? 25.061 -1.353  -11.770 1.00 17.40 ? 64  LEU A HD22 1 
ATOM   688  H HD23 . LEU A 1 64  ? 25.094 -0.332  -10.552 1.00 17.40 ? 64  LEU A HD23 1 
ATOM   689  N N    . GLU A 1 65  ? 28.620 -2.865  -8.932  1.00 10.71 ? 65  GLU A N    1 
ATOM   690  C CA   . GLU A 1 65  ? 29.580 -3.827  -8.426  1.00 11.39 ? 65  GLU A CA   1 
ATOM   691  C C    . GLU A 1 65  ? 30.154 -4.723  -9.531  1.00 10.68 ? 65  GLU A C    1 
ATOM   692  O O    . GLU A 1 65  ? 29.746 -4.682  -10.707 1.00 11.76 ? 65  GLU A O    1 
ATOM   693  C CB   . GLU A 1 65  ? 28.908 -4.726  -7.388  1.00 12.95 ? 65  GLU A CB   1 
ATOM   694  C CG   . GLU A 1 65  ? 29.199 -4.375  -5.965  1.00 14.58 ? 65  GLU A CG   1 
ATOM   695  C CD   . GLU A 1 65  ? 30.540 -4.863  -5.496  1.00 14.10 ? 65  GLU A CD   1 
ATOM   696  O OE1  . GLU A 1 65  ? 30.964 -4.410  -4.385  1.00 15.37 ? 65  GLU A OE1  1 
ATOM   697  O OE2  . GLU A 1 65  ? 31.198 -5.653  -6.189  1.00 13.97 ? 65  GLU A OE2  1 
ATOM   698  H H    . GLU A 1 65  ? 27.819 -3.022  -8.661  1.00 12.86 ? 65  GLU A H    1 
ATOM   699  H HA   . GLU A 1 65  ? 30.306 -3.316  -8.037  1.00 13.67 ? 65  GLU A HA   1 
ATOM   700  H HB2  . GLU A 1 65  ? 27.947 -4.672  -7.511  1.00 15.54 ? 65  GLU A HB2  1 
ATOM   701  H HB3  . GLU A 1 65  ? 29.210 -5.637  -7.530  1.00 15.54 ? 65  GLU A HB3  1 
ATOM   702  H HG2  . GLU A 1 65  ? 29.183 -3.410  -5.870  1.00 17.49 ? 65  GLU A HG2  1 
ATOM   703  H HG3  . GLU A 1 65  ? 28.521 -4.775  -5.398  1.00 17.49 ? 65  GLU A HG3  1 
ATOM   704  N N    . LYS A 1 66  ? 31.103 -5.581  -9.131  1.00 10.88 ? 66  LYS A N    1 
ATOM   705  C CA   . LYS A 1 66  ? 31.696 -6.592  -9.997  1.00 12.04 ? 66  LYS A CA   1 
ATOM   706  C C    . LYS A 1 66  ? 30.627 -7.564  -10.482 1.00 11.22 ? 66  LYS A C    1 
ATOM   707  O O    . LYS A 1 66  ? 29.502 -7.603  -9.975  1.00 12.07 ? 66  LYS A O    1 
ATOM   708  C CB   . LYS A 1 66  ? 32.781 -7.335  -9.216  1.00 14.24 ? 66  LYS A CB   1 
ATOM   709  C CG   . LYS A 1 66  ? 32.220 -8.286  -8.147  1.00 14.26 ? 66  LYS A CG   1 
ATOM   710  C CD   . LYS A 1 66  ? 33.266 -8.954  -7.302  1.00 16.66 ? 66  LYS A CD   1 
ATOM   711  C CE   . LYS A 1 66  ? 33.888 -8.023  -6.281  1.00 18.95 ? 66  LYS A CE   1 
ATOM   712  N NZ   . LYS A 1 66  ? 32.946 -7.571  -5.276  1.00 16.59 ? 66  LYS A NZ   1 
ATOM   713  H H    . LYS A 1 66  ? 31.428 -5.594  -8.335  1.00 13.06 ? 66  LYS A H    1 
ATOM   714  H HA   . LYS A 1 66  ? 32.095 -6.179  -10.779 1.00 14.45 ? 66  LYS A HA   1 
ATOM   715  H HB2  . LYS A 1 66  ? 33.308 -7.863  -9.836  1.00 17.09 ? 66  LYS A HB2  1 
ATOM   716  H HB3  . LYS A 1 66  ? 33.347 -6.686  -8.770  1.00 17.09 ? 66  LYS A HB3  1 
ATOM   717  H HG2  . LYS A 1 66  ? 31.644 -7.779  -7.553  1.00 17.11 ? 66  LYS A HG2  1 
ATOM   718  H HG3  . LYS A 1 66  ? 31.710 -8.983  -8.588  1.00 17.11 ? 66  LYS A HG3  1 
ATOM   719  H HD2  . LYS A 1 66  ? 32.860 -9.693  -6.824  1.00 19.99 ? 66  LYS A HD2  1 
ATOM   720  H HD3  . LYS A 1 66  ? 33.975 -9.281  -7.878  1.00 19.99 ? 66  LYS A HD3  1 
ATOM   721  H HE2  . LYS A 1 66  ? 34.608 -8.489  -5.827  1.00 22.73 ? 66  LYS A HE2  1 
ATOM   722  H HE3  . LYS A 1 66  ? 34.236 -7.241  -6.738  1.00 22.73 ? 66  LYS A HE3  1 
ATOM   723  H HZ1  . LYS A 1 66  ? 33.365 -7.076  -4.666  1.00 19.91 ? 66  LYS A HZ1  1 
ATOM   724  H HZ2  . LYS A 1 66  ? 32.307 -7.081  -5.656  1.00 19.91 ? 66  LYS A HZ2  1 
ATOM   725  H HZ3  . LYS A 1 66  ? 32.572 -8.271  -4.872  1.00 19.91 ? 66  LYS A HZ3  1 
ATOM   726  N N    . SER A 1 67  ? 30.973 -8.345  -11.500 1.00 12.06 ? 67  SER A N    1 
ATOM   727  C CA   . SER A 1 67  ? 30.078 -9.339  -12.091 1.00 12.76 ? 67  SER A CA   1 
ATOM   728  C C    . SER A 1 67  ? 28.730 -8.704  -12.374 1.00 12.14 ? 67  SER A C    1 
ATOM   729  O O    . SER A 1 67  ? 27.694 -9.035  -11.799 1.00 14.22 ? 67  SER A O    1 
ATOM   730  C CB   . SER A 1 67  ? 29.977 -10.584 -11.218 1.00 14.51 ? 67  SER A CB   1 
ATOM   731  O OG   . SER A 1 67  ? 31.164 -11.320 -11.337 1.00 21.18 ? 67  SER A OG   1 
ATOM   732  H H    . SER A 1 67  ? 31.745 -8.318  -11.878 1.00 14.48 ? 67  SER A H    1 
ATOM   733  H HA   . SER A 1 67  ? 30.441 -9.637  -12.940 1.00 15.32 ? 67  SER A HA   1 
ATOM   734  H HB2  . SER A 1 67  ? 29.851 -10.320 -10.293 1.00 17.41 ? 67  SER A HB2  1 
ATOM   735  H HB3  . SER A 1 67  ? 29.229 -11.126 -11.513 1.00 17.41 ? 67  SER A HB3  1 
ATOM   736  H HG   . SER A 1 67  ? 31.226 -11.643 -12.109 1.00 25.42 ? 67  SER A HG   1 
ATOM   737  N N    . GLN A 1 68  ? 28.763 -7.725  -13.270 1.00 12.67 ? 68  GLN A N    1 
ATOM   738  C CA   . GLN A 1 68  ? 27.621 -6.859  -13.533 1.00 12.68 ? 68  GLN A CA   1 
ATOM   739  C C    . GLN A 1 68  ? 26.872 -7.324  -14.772 1.00 13.86 ? 68  GLN A C    1 
ATOM   740  O O    . GLN A 1 68  ? 27.277 -7.031  -15.898 1.00 14.43 ? 68  GLN A O    1 
ATOM   741  C CB   . GLN A 1 68  ? 28.083 -5.413  -13.687 1.00 12.43 ? 68  GLN A CB   1 
ATOM   742  C CG   . GLN A 1 68  ? 26.982 -4.384  -13.642 1.00 13.01 ? 68  GLN A CG   1 
ATOM   743  C CD   . GLN A 1 68  ? 26.230 -4.356  -12.355 1.00 13.16 ? 68  GLN A CD   1 
ATOM   744  O OE1  . GLN A 1 68  ? 25.005 -4.363  -12.329 1.00 15.17 ? 68  GLN A OE1  1 
ATOM   745  N NE2  . GLN A 1 68  ? 26.943 -4.268  -11.241 1.00 12.69 ? 68  GLN A NE2  1 
ATOM   746  H H    . GLN A 1 68  ? 29.453 -7.539  -13.749 1.00 15.21 ? 68  GLN A H    1 
ATOM   747  H HA   . GLN A 1 68  ? 27.009 -6.938  -12.785 1.00 15.22 ? 68  GLN A HA   1 
ATOM   748  H HB2  . GLN A 1 68  ? 28.701 -5.210  -12.968 1.00 14.92 ? 68  GLN A HB2  1 
ATOM   749  H HB3  . GLN A 1 68  ? 28.530 -5.324  -14.544 1.00 14.92 ? 68  GLN A HB3  1 
ATOM   750  H HG2  . GLN A 1 68  ? 27.371 -3.505  -13.774 1.00 15.61 ? 68  GLN A HG2  1 
ATOM   751  H HG3  . GLN A 1 68  ? 26.347 -4.575  -14.350 1.00 15.61 ? 68  GLN A HG3  1 
ATOM   752  H HE21 . GLN A 1 68  ? 27.802 -4.230  -11.282 1.00 15.23 ? 68  GLN A HE21 1 
ATOM   753  H HE22 . GLN A 1 68  ? 26.548 -4.250  -10.478 1.00 15.23 ? 68  GLN A HE22 1 
ATOM   754  N N    . ALA A 1 69  ? 25.752 -8.009  -14.553 1.00 13.88 ? 69  ALA A N    1 
ATOM   755  C CA   . ALA A 1 69  ? 24.869 -8.492  -15.622 1.00 15.82 ? 69  ALA A CA   1 
ATOM   756  C C    . ALA A 1 69  ? 25.631 -9.338  -16.631 1.00 15.93 ? 69  ALA A C    1 
ATOM   757  O O    . ALA A 1 69  ? 25.313 -9.370  -17.824 1.00 16.08 ? 69  ALA A O    1 
ATOM   758  C CB   . ALA A 1 69  ? 24.131 -7.329  -16.284 1.00 16.15 ? 69  ALA A CB   1 
ATOM   759  H H    . ALA A 1 69  ? 25.469 -8.215  -13.767 1.00 16.65 ? 69  ALA A H    1 
ATOM   760  H HA   . ALA A 1 69  ? 24.194 -9.072  -15.236 1.00 18.98 ? 69  ALA A HA   1 
ATOM   761  H HB1  . ALA A 1 69  ? 23.566 -7.676  -16.992 1.00 19.39 ? 69  ALA A HB1  1 
ATOM   762  H HB2  . ALA A 1 69  ? 23.589 -6.879  -15.618 1.00 19.39 ? 69  ALA A HB2  1 
ATOM   763  H HB3  . ALA A 1 69  ? 24.782 -6.711  -16.653 1.00 19.39 ? 69  ALA A HB3  1 
ATOM   764  N N    . GLN A 1 70  ? 26.617 -10.085 -16.134 1.00 16.92 ? 70  GLN A N    1 
ATOM   765  C CA   . GLN A 1 70  ? 27.531 -10.767 -17.032 1.00 16.64 ? 70  GLN A CA   1 
ATOM   766  C C    . GLN A 1 70  ? 26.880 -11.921 -17.770 1.00 18.80 ? 70  GLN A C    1 
ATOM   767  O O    . GLN A 1 70  ? 27.328 -12.267 -18.860 1.00 18.76 ? 70  GLN A O    1 
ATOM   768  C CB   . GLN A 1 70  ? 28.771 -11.250 -16.280 1.00 18.27 ? 70  GLN A CB   1 
ATOM   769  C CG   . GLN A 1 70  ? 28.590 -12.518 -15.492 1.00 18.18 ? 70  GLN A CG   1 
ATOM   770  C CD   . GLN A 1 70  ? 27.708 -12.368 -14.271 1.00 17.20 ? 70  GLN A CD   1 
ATOM   771  O OE1  . GLN A 1 70  ? 27.522 -11.267 -13.713 1.00 19.04 ? 70  GLN A OE1  1 
ATOM   772  N NE2  . GLN A 1 70  ? 27.141 -13.465 -13.823 1.00 19.30 ? 70  GLN A NE2  1 
ATOM   773  H H    . GLN A 1 70  ? 26.771 -10.209 -15.297 1.00 20.30 ? 70  GLN A H    1 
ATOM   774  H HA   . GLN A 1 70  ? 27.819 -10.123 -17.698 1.00 19.97 ? 70  GLN A HA   1 
ATOM   775  H HB2  . GLN A 1 70  ? 29.478 -11.407 -16.925 1.00 21.92 ? 70  GLN A HB2  1 
ATOM   776  H HB3  . GLN A 1 70  ? 29.039 -10.557 -15.656 1.00 21.92 ? 70  GLN A HB3  1 
ATOM   777  H HG2  . GLN A 1 70  ? 28.186 -13.186 -16.067 1.00 21.82 ? 70  GLN A HG2  1 
ATOM   778  H HG3  . GLN A 1 70  ? 29.460 -12.823 -15.190 1.00 21.82 ? 70  GLN A HG3  1 
ATOM   779  H HE21 . GLN A 1 70  ? 27.282 -14.214 -14.221 1.00 23.16 ? 70  GLN A HE21 1 
ATOM   780  H HE22 . GLN A 1 70  ? 26.630 -13.434 -13.132 1.00 23.16 ? 70  GLN A HE22 1 
ATOM   781  N N    . ASN A 1 71  ? 25.859 -12.557 -17.200 1.00 17.10 ? 71  ASN A N    1 
ATOM   782  C CA   . ASN A 1 71  ? 25.225 -13.665 -17.918 1.00 17.16 ? 71  ASN A CA   1 
ATOM   783  C C    . ASN A 1 71  ? 24.376 -13.180 -19.090 1.00 19.54 ? 71  ASN A C    1 
ATOM   784  O O    . ASN A 1 71  ? 24.089 -13.974 -20.000 1.00 18.99 ? 71  ASN A O    1 
ATOM   785  C CB   . ASN A 1 71  ? 24.434 -14.567 -16.963 1.00 18.85 ? 71  ASN A CB   1 
ATOM   786  C CG   . ASN A 1 71  ? 25.319 -15.331 -15.969 1.00 19.35 ? 71  ASN A CG   1 
ATOM   787  O OD1  . ASN A 1 71  ? 26.537 -15.452 -16.137 1.00 27.22 ? 71  ASN A OD1  1 
ATOM   788  N ND2  . ASN A 1 71  ? 24.694 -15.819 -14.910 1.00 21.99 ? 71  ASN A ND2  1 
ATOM   789  H H    . ASN A 1 71  ? 25.524 -12.375 -16.429 1.00 20.52 ? 71  ASN A H    1 
ATOM   790  H HA   . ASN A 1 71  ? 25.917 -14.234 -18.289 1.00 20.59 ? 71  ASN A HA   1 
ATOM   791  H HB2  . ASN A 1 71  ? 23.818 -14.019 -16.452 1.00 22.61 ? 71  ASN A HB2  1 
ATOM   792  H HB3  . ASN A 1 71  ? 23.941 -15.220 -17.485 1.00 22.61 ? 71  ASN A HB3  1 
ATOM   793  H HD21 . ASN A 1 71  ? 25.134 -16.258 -14.316 1.00 26.39 ? 71  ASN A HD21 1 
ATOM   794  H HD22 . ASN A 1 71  ? 23.848 -15.698 -14.816 1.00 26.39 ? 71  ASN A HD22 1 
ATOM   795  N N    . THR A 1 72  ? 23.981 -11.905 -19.112 1.00 18.77 ? 72  THR A N    1 
ATOM   796  C CA   . THR A 1 72  ? 23.259 -11.320 -20.235 1.00 20.04 ? 72  THR A CA   1 
ATOM   797  C C    . THR A 1 72  ? 24.190 -10.686 -21.269 1.00 20.30 ? 72  THR A C    1 
ATOM   798  O O    . THR A 1 72  ? 24.009 -10.879 -22.479 1.00 21.87 ? 72  THR A O    1 
ATOM   799  C CB   . THR A 1 72  ? 22.298 -10.231 -19.748 1.00 20.09 ? 72  THR A CB   1 
ATOM   800  O OG1  . THR A 1 72  ? 21.317 -10.789 -18.862 1.00 19.37 ? 72  THR A OG1  1 
ATOM   801  C CG2  . THR A 1 72  ? 21.608 -9.560  -20.936 1.00 21.47 ? 72  THR A CG2  1 
ATOM   802  H H    . THR A 1 72  ? 24.125 -11.348 -18.472 1.00 22.52 ? 72  THR A H    1 
ATOM   803  H HA   . THR A 1 72  ? 22.750 -12.032 -20.654 1.00 24.05 ? 72  THR A HA   1 
ATOM   804  H HB   . THR A 1 72  ? 22.799 -9.555  -19.264 1.00 24.11 ? 72  THR A HB   1 
ATOM   805  H HG1  . THR A 1 72  ? 20.919 -11.426 -19.238 1.00 23.25 ? 72  THR A HG1  1 
ATOM   806  H HG21 . THR A 1 72  ? 20.809 -9.098  -20.638 1.00 25.76 ? 72  THR A HG21 1 
ATOM   807  H HG22 . THR A 1 72  ? 22.207 -8.919  -21.349 1.00 25.76 ? 72  THR A HG22 1 
ATOM   808  H HG23 . THR A 1 72  ? 21.358 -10.227 -21.594 1.00 25.76 ? 72  THR A HG23 1 
ATOM   809  N N    . TYR A 1 73  ? 25.197 -9.947  -20.824 1.00 19.66 ? 73  TYR A N    1 
ATOM   810  C CA   . TYR A 1 73  ? 26.028 -9.182  -21.730 1.00 20.35 ? 73  TYR A CA   1 
ATOM   811  C C    . TYR A 1 73  ? 27.366 -9.836  -22.023 1.00 18.70 ? 73  TYR A C    1 
ATOM   812  O O    . TYR A 1 73  ? 28.070 -9.379  -22.934 1.00 22.96 ? 73  TYR A O    1 
ATOM   813  C CB   . TYR A 1 73  ? 26.208 -7.758  -21.196 1.00 20.80 ? 73  TYR A CB   1 
ATOM   814  C CG   . TYR A 1 73  ? 24.903 -7.007  -21.180 1.00 21.43 ? 73  TYR A CG   1 
ATOM   815  C CD1  . TYR A 1 73  ? 24.175 -6.807  -20.005 1.00 22.57 ? 73  TYR A CD1  1 
ATOM   816  C CD2  . TYR A 1 73  ? 24.371 -6.546  -22.369 1.00 23.84 ? 73  TYR A CD2  1 
ATOM   817  C CE1  . TYR A 1 73  ? 22.940 -6.131  -20.042 1.00 24.66 ? 73  TYR A CE1  1 
ATOM   818  C CE2  . TYR A 1 73  ? 23.168 -5.876  -22.418 1.00 29.91 ? 73  TYR A CE2  1 
ATOM   819  C CZ   . TYR A 1 73  ? 22.455 -5.668  -21.258 1.00 28.36 ? 73  TYR A CZ   1 
ATOM   820  O OH   . TYR A 1 73  ? 21.245 -4.997  -21.373 1.00 33.57 ? 73  TYR A OH   1 
ATOM   821  H H    . TYR A 1 73  ? 25.418 -9.875  -19.996 1.00 23.60 ? 73  TYR A H    1 
ATOM   822  H HA   . TYR A 1 73  ? 25.579 -9.102  -22.586 1.00 24.43 ? 73  TYR A HA   1 
ATOM   823  H HB2  . TYR A 1 73  ? 26.550 -7.796  -20.289 1.00 24.96 ? 73  TYR A HB2  1 
ATOM   824  H HB3  . TYR A 1 73  ? 26.830 -7.278  -21.764 1.00 24.96 ? 73  TYR A HB3  1 
ATOM   825  H HD1  . TYR A 1 73  ? 24.507 -7.121  -19.195 1.00 27.09 ? 73  TYR A HD1  1 
ATOM   826  H HD2  . TYR A 1 73  ? 24.840 -6.692  -23.159 1.00 28.61 ? 73  TYR A HD2  1 
ATOM   827  H HE1  . TYR A 1 73  ? 22.454 -5.997  -19.261 1.00 29.59 ? 73  TYR A HE1  1 
ATOM   828  H HE2  . TYR A 1 73  ? 22.839 -5.566  -23.230 1.00 35.89 ? 73  TYR A HE2  1 
ATOM   829  H HH   . TYR A 1 73  ? 21.198 -4.615  -22.120 1.00 40.29 ? 73  TYR A HH   1 
ATOM   830  N N    . GLY A 1 74  ? 27.707 -10.904 -21.313 1.00 18.67 ? 74  GLY A N    1 
ATOM   831  C CA   . GLY A 1 74  ? 28.927 -11.638 -21.553 1.00 18.33 ? 74  GLY A CA   1 
ATOM   832  C C    . GLY A 1 74  ? 30.110 -11.220 -20.717 1.00 19.28 ? 74  GLY A C    1 
ATOM   833  O O    . GLY A 1 74  ? 31.111 -11.952 -20.680 1.00 22.01 ? 74  GLY A O    1 
ATOM   834  H H    . GLY A 1 74  ? 27.232 -11.226 -20.672 1.00 22.40 ? 74  GLY A H    1 
ATOM   835  H HA2  . GLY A 1 74  ? 28.761 -12.577 -21.377 1.00 21.99 ? 74  GLY A HA2  1 
ATOM   836  H HA3  . GLY A 1 74  ? 29.174 -11.530 -22.485 1.00 21.99 ? 74  GLY A HA3  1 
ATOM   837  N N    . SER A 1 75  ? 30.031 -10.073 -20.052 1.00 16.64 ? 75  SER A N    1 
ATOM   838  C CA   . SER A 1 75  ? 31.165 -9.526  -19.309 1.00 16.63 ? 75  SER A CA   1 
ATOM   839  C C    . SER A 1 75  ? 30.649 -8.392  -18.439 1.00 15.47 ? 75  SER A C    1 
ATOM   840  O O    . SER A 1 75  ? 29.640 -7.750  -18.742 1.00 15.34 ? 75  SER A O    1 
ATOM   841  C CB   . SER A 1 75  ? 32.254 -8.999  -20.257 1.00 16.80 ? 75  SER A CB   1 
ATOM   842  O OG   . SER A 1 75  ? 31.829 -7.851  -20.988 1.00 17.92 ? 75  SER A OG   1 
ATOM   843  H H    . SER A 1 75  ? 29.323 -9.586  -20.013 1.00 19.97 ? 75  SER A H    1 
ATOM   844  H HA   . SER A 1 75  ? 31.548 -10.214 -18.744 1.00 19.96 ? 75  SER A HA   1 
ATOM   845  H HB2  . SER A 1 75  ? 33.034 -8.761  -19.731 1.00 20.16 ? 75  SER A HB2  1 
ATOM   846  H HB3  . SER A 1 75  ? 32.481 -9.701  -20.887 1.00 20.16 ? 75  SER A HB3  1 
ATOM   847  H HG   . SER A 1 75  ? 31.186 -8.052  -21.490 1.00 21.51 ? 75  SER A HG   1 
ATOM   848  N N    . THR A 1 76  ? 31.411 -8.109  -17.400 1.00 13.83 ? 76  THR A N    1 
ATOM   849  C CA   . THR A 1 76  ? 31.129 -6.964  -16.542 1.00 13.74 ? 76  THR A CA   1 
ATOM   850  C C    . THR A 1 76  ? 31.297 -5.655  -17.295 1.00 13.06 ? 76  THR A C    1 
ATOM   851  O O    . THR A 1 76  ? 30.544 -4.702  -17.061 1.00 13.15 ? 76  THR A O    1 
ATOM   852  C CB   . THR A 1 76  ? 32.037 -7.016  -15.330 1.00 13.82 ? 76  THR A CB   1 
ATOM   853  O OG1  . THR A 1 76  ? 31.635 -8.161  -14.570 1.00 14.60 ? 76  THR A OG1  1 
ATOM   854  C CG2  . THR A 1 76  ? 31.924 -5.776  -14.454 1.00 13.53 ? 76  THR A CG2  1 
ATOM   855  H H    . THR A 1 76  ? 32.103 -8.562  -17.164 1.00 16.60 ? 76  THR A H    1 
ATOM   856  H HA   . THR A 1 76  ? 30.209 -7.006  -16.237 1.00 16.49 ? 76  THR A HA   1 
ATOM   857  H HB   . THR A 1 76  ? 32.963 -7.063  -15.613 1.00 16.59 ? 76  THR A HB   1 
ATOM   858  H HG1  . THR A 1 76  ? 32.141 -8.258  -13.906 1.00 17.52 ? 76  THR A HG1  1 
ATOM   859  H HG21 . THR A 1 76  ? 32.337 -5.941  -13.592 1.00 16.23 ? 76  THR A HG21 1 
ATOM   860  H HG22 . THR A 1 76  ? 32.372 -5.028  -14.879 1.00 16.23 ? 76  THR A HG22 1 
ATOM   861  H HG23 . THR A 1 76  ? 30.991 -5.549  -14.319 1.00 16.23 ? 76  THR A HG23 1 
ATOM   862  N N    . GLU A 1 77  ? 32.284 -5.573  -18.189 1.00 13.00 ? 77  GLU A N    1 
ATOM   863  C CA   . GLU A 1 77  ? 32.494 -4.310  -18.888 1.00 14.59 ? 77  GLU A CA   1 
ATOM   864  C C    . GLU A 1 77  ? 31.258 -3.956  -19.711 1.00 15.76 ? 77  GLU A C    1 
ATOM   865  O O    . GLU A 1 77  ? 30.741 -2.831  -19.646 1.00 15.87 ? 77  GLU A O    1 
ATOM   866  C CB   . GLU A 1 77  ? 33.734 -4.417  -19.773 1.00 16.22 ? 77  GLU A CB   1 
ATOM   867  C CG   . GLU A 1 77  ? 35.054 -4.679  -19.034 1.00 16.80 ? 77  GLU A CG   1 
ATOM   868  C CD   . GLU A 1 77  ? 35.445 -6.149  -18.981 1.00 14.53 ? 77  GLU A CD   1 
ATOM   869  O OE1  . GLU A 1 77  ? 34.534 -7.010  -18.954 1.00 14.96 ? 77  GLU A OE1  1 
ATOM   870  O OE2  . GLU A 1 77  ? 36.649 -6.412  -18.977 1.00 15.09 ? 77  GLU A OE2  1 
ATOM   871  H H    . GLU A 1 77  ? 32.822 -6.209  -18.400 1.00 15.60 ? 77  GLU A H    1 
ATOM   872  H HA   . GLU A 1 77  ? 32.649 -3.597  -18.248 1.00 17.51 ? 77  GLU A HA   1 
ATOM   873  H HB2  . GLU A 1 77  ? 33.601 -5.149  -20.396 1.00 19.47 ? 77  GLU A HB2  1 
ATOM   874  H HB3  . GLU A 1 77  ? 33.835 -3.583  -20.258 1.00 19.47 ? 77  GLU A HB3  1 
ATOM   875  H HG2  . GLU A 1 77  ? 35.766 -4.200  -19.486 1.00 20.16 ? 77  GLU A HG2  1 
ATOM   876  H HG3  . GLU A 1 77  ? 34.969 -4.363  -18.121 1.00 20.16 ? 77  GLU A HG3  1 
ATOM   877  N N    . GLU A 1 78  ? 30.742 -4.926  -20.461 1.00 16.42 ? 78  GLU A N    1 
ATOM   878  C CA   . GLU A 1 78  ? 29.569 -4.654  -21.281 1.00 15.94 ? 78  GLU A CA   1 
ATOM   879  C C    . GLU A 1 78  ? 28.310 -4.493  -20.447 1.00 17.08 ? 78  GLU A C    1 
ATOM   880  O O    . GLU A 1 78  ? 27.472 -3.642  -20.755 1.00 17.39 ? 78  GLU A O    1 
ATOM   881  C CB   . GLU A 1 78  ? 29.400 -5.725  -22.357 1.00 19.20 ? 78  GLU A CB   1 
ATOM   882  C CG   . GLU A 1 78  ? 30.519 -5.755  -23.374 1.00 25.07 ? 78  GLU A CG   1 
ATOM   883  C CD   . GLU A 1 78  ? 30.448 -4.579  -24.330 1.00 38.20 ? 78  GLU A CD   1 
ATOM   884  O OE1  . GLU A 1 78  ? 31.526 -4.168  -24.840 1.00 39.96 ? 78  GLU A OE1  1 
ATOM   885  O OE2  . GLU A 1 78  ? 29.344 -4.022  -24.508 1.00 40.33 ? 78  GLU A OE2  1 
ATOM   886  H H    . GLU A 1 78  ? 31.045 -5.730  -20.512 1.00 19.70 ? 78  GLU A H    1 
ATOM   887  H HA   . GLU A 1 78  ? 29.713 -3.810  -21.738 1.00 19.13 ? 78  GLU A HA   1 
ATOM   888  H HB2  . GLU A 1 78  ? 29.368 -6.595  -21.928 1.00 23.04 ? 78  GLU A HB2  1 
ATOM   889  H HB3  . GLU A 1 78  ? 28.572 -5.560  -22.834 1.00 23.04 ? 78  GLU A HB3  1 
ATOM   890  H HG2  . GLU A 1 78  ? 31.371 -5.719  -22.912 1.00 30.09 ? 78  GLU A HG2  1 
ATOM   891  H HG3  . GLU A 1 78  ? 30.457 -6.572  -23.893 1.00 30.09 ? 78  GLU A HG3  1 
ATOM   892  N N    . GLY A 1 79  ? 28.158 -5.275  -19.384 1.00 15.43 ? 79  GLY A N    1 
ATOM   893  C CA   . GLY A 1 79  ? 26.978 -5.121  -18.549 1.00 15.11 ? 79  GLY A CA   1 
ATOM   894  C C    . GLY A 1 79  ? 26.940 -3.789  -17.828 1.00 16.27 ? 79  GLY A C    1 
ATOM   895  O O    . GLY A 1 79  ? 25.875 -3.208  -17.634 1.00 15.49 ? 79  GLY A O    1 
ATOM   896  H H    . GLY A 1 79  ? 28.708 -5.885  -19.131 1.00 18.51 ? 79  GLY A H    1 
ATOM   897  H HA2  . GLY A 1 79  ? 26.184 -5.191  -19.103 1.00 18.14 ? 79  GLY A HA2  1 
ATOM   898  H HA3  . GLY A 1 79  ? 26.962 -5.828  -17.885 1.00 18.14 ? 79  GLY A HA3  1 
ATOM   899  N N    . THR A 1 80  ? 28.105 -3.290  -17.424 1.00 13.80 ? 80  THR A N    1 
ATOM   900  C CA   . THR A 1 80  ? 28.209 -1.972  -16.811 1.00 15.18 ? 80  THR A CA   1 
ATOM   901  C C    . THR A 1 80  ? 27.798 -0.896  -17.803 1.00 14.45 ? 80  THR A C    1 
ATOM   902  O O    . THR A 1 80  ? 27.022 0.004   -17.463 1.00 15.28 ? 80  THR A O    1 
ATOM   903  C CB   . THR A 1 80  ? 29.636 -1.742  -16.329 1.00 13.10 ? 80  THR A CB   1 
ATOM   904  O OG1  . THR A 1 80  ? 29.923 -2.713  -15.317 1.00 13.86 ? 80  THR A OG1  1 
ATOM   905  C CG2  . THR A 1 80  ? 29.803 -0.352  -15.760 1.00 15.97 ? 80  THR A CG2  1 
ATOM   906  H H    . THR A 1 80  ? 28.858 -3.699  -17.495 1.00 16.57 ? 80  THR A H    1 
ATOM   907  H HA   . THR A 1 80  ? 27.621 -1.925  -16.042 1.00 18.22 ? 80  THR A HA   1 
ATOM   908  H HB   . THR A 1 80  ? 30.257 -1.826  -17.069 1.00 15.72 ? 80  THR A HB   1 
ATOM   909  H HG1  . THR A 1 80  ? 29.937 -3.482  -15.654 1.00 16.63 ? 80  THR A HG1  1 
ATOM   910  H HG21 . THR A 1 80  ? 30.673 -0.267  -15.341 1.00 19.16 ? 80  THR A HG21 1 
ATOM   911  H HG22 . THR A 1 80  ? 29.728 0.308   -16.468 1.00 19.16 ? 80  THR A HG22 1 
ATOM   912  H HG23 . THR A 1 80  ? 29.116 -0.180  -15.097 1.00 19.16 ? 80  THR A HG23 1 
ATOM   913  N N    . LEU A 1 81  ? 28.334 -0.957  -19.024 1.00 15.50 ? 81  LEU A N    1 
ATOM   914  C CA   . LEU A 1 81  ? 28.005 0.050   -20.028 1.00 15.82 ? 81  LEU A CA   1 
ATOM   915  C C    . LEU A 1 81  ? 26.521 0.055   -20.341 1.00 16.55 ? 81  LEU A C    1 
ATOM   916  O O    . LEU A 1 81  ? 25.904 1.123   -20.426 1.00 18.40 ? 81  LEU A O    1 
ATOM   917  C CB   . LEU A 1 81  ? 28.849 -0.176  -21.286 1.00 18.01 ? 81  LEU A CB   1 
ATOM   918  C CG   . LEU A 1 81  ? 30.342 0.141   -21.168 1.00 19.29 ? 81  LEU A CG   1 
ATOM   919  C CD1  . LEU A 1 81  ? 31.043 -0.422  -22.383 1.00 22.29 ? 81  LEU A CD1  1 
ATOM   920  C CD2  . LEU A 1 81  ? 30.588 1.641   -21.012 1.00 20.14 ? 81  LEU A CD2  1 
ATOM   921  H H    . LEU A 1 81  ? 28.882 -1.563  -19.291 1.00 18.60 ? 81  LEU A H    1 
ATOM   922  H HA   . LEU A 1 81  ? 28.226 0.930   -19.684 1.00 18.98 ? 81  LEU A HA   1 
ATOM   923  H HB2  . LEU A 1 81  ? 28.774 -1.111  -21.534 1.00 21.61 ? 81  LEU A HB2  1 
ATOM   924  H HB3  . LEU A 1 81  ? 28.492 0.385   -21.992 1.00 21.61 ? 81  LEU A HB3  1 
ATOM   925  H HG   . LEU A 1 81  ? 30.711 -0.269  -20.370 1.00 23.14 ? 81  LEU A HG   1 
ATOM   926  H HD11 . LEU A 1 81  ? 31.993 -0.239  -22.312 1.00 26.75 ? 81  LEU A HD11 1 
ATOM   927  H HD12 . LEU A 1 81  ? 30.892 -1.379  -22.420 1.00 26.75 ? 81  LEU A HD12 1 
ATOM   928  H HD13 . LEU A 1 81  ? 30.683 0.000   -23.179 1.00 26.75 ? 81  LEU A HD13 1 
ATOM   929  H HD21 . LEU A 1 81  ? 31.543 1.809   -21.037 1.00 24.17 ? 81  LEU A HD21 1 
ATOM   930  H HD22 . LEU A 1 81  ? 30.150 2.110   -21.739 1.00 24.17 ? 81  LEU A HD22 1 
ATOM   931  H HD23 . LEU A 1 81  ? 30.223 1.934   -20.162 1.00 24.17 ? 81  LEU A HD23 1 
ATOM   932  N N    . ALA A 1 82  ? 25.914 -1.122  -20.459 1.00 15.78 ? 82  ALA A N    1 
ATOM   933  C CA   . ALA A 1 82  ? 24.493 -1.183  -20.791 1.00 17.77 ? 82  ALA A CA   1 
ATOM   934  C C    . ALA A 1 82  ? 23.648 -0.653  -19.649 1.00 16.93 ? 82  ALA A C    1 
ATOM   935  O O    . ALA A 1 82  ? 22.682 0.083   -19.876 1.00 18.68 ? 82  ALA A O    1 
ATOM   936  C CB   . ALA A 1 82  ? 24.100 -2.615  -21.109 1.00 18.92 ? 82  ALA A CB   1 
ATOM   937  H H    . ALA A 1 82  ? 26.293 -1.886  -20.354 1.00 18.93 ? 82  ALA A H    1 
ATOM   938  H HA   . ALA A 1 82  ? 24.328 -0.639  -21.576 1.00 21.32 ? 82  ALA A HA   1 
ATOM   939  H HB1  . ALA A 1 82  ? 23.152 -2.645  -21.310 1.00 22.70 ? 82  ALA A HB1  1 
ATOM   940  H HB2  . ALA A 1 82  ? 24.611 -2.920  -21.875 1.00 22.70 ? 82  ALA A HB2  1 
ATOM   941  H HB3  . ALA A 1 82  ? 24.293 -3.174  -20.339 1.00 22.70 ? 82  ALA A HB3  1 
ATOM   942  N N    . THR A 1 83  ? 23.990 -1.032  -18.415 1.00 15.40 ? 83  THR A N    1 
ATOM   943  C CA   . THR A 1 83  ? 23.230 -0.590  -17.251 1.00 16.45 ? 83  THR A CA   1 
ATOM   944  C C    . THR A 1 83  ? 23.342 0.922   -17.088 1.00 15.95 ? 83  THR A C    1 
ATOM   945  O O    . THR A 1 83  ? 22.337 1.610   -16.850 1.00 16.13 ? 83  THR A O    1 
ATOM   946  C CB   . THR A 1 83  ? 23.718 -1.334  -16.003 1.00 14.71 ? 83  THR A CB   1 
ATOM   947  O OG1  . THR A 1 83  ? 23.528 -2.746  -16.187 1.00 16.04 ? 83  THR A OG1  1 
ATOM   948  C CG2  . THR A 1 83  ? 22.982 -0.864  -14.766 1.00 16.21 ? 83  THR A CG2  1 
ATOM   949  H H    . THR A 1 83  ? 24.655 -1.543  -18.228 1.00 18.47 ? 83  THR A H    1 
ATOM   950  H HA   . THR A 1 83  ? 22.291 -0.806  -17.367 1.00 19.74 ? 83  THR A HA   1 
ATOM   951  H HB   . THR A 1 83  ? 24.661 -1.152  -15.865 1.00 17.65 ? 83  THR A HB   1 
ATOM   952  H HG1  . THR A 1 83  ? 23.983 -3.015  -16.840 1.00 19.25 ? 83  THR A HG1  1 
ATOM   953  H HG21 . THR A 1 83  ? 23.189 -1.445  -14.017 1.00 19.45 ? 83  THR A HG21 1 
ATOM   954  H HG22 . THR A 1 83  ? 23.249 0.041   -14.544 1.00 19.45 ? 83  THR A HG22 1 
ATOM   955  H HG23 . THR A 1 83  ? 22.025 -0.881  -14.922 1.00 19.45 ? 83  THR A HG23 1 
ATOM   956  N N    . ALA A 1 84  ? 24.565 1.453   -17.205 1.00 15.29 ? 84  ALA A N    1 
ATOM   957  C CA   . ALA A 1 84  ? 24.756 2.885   -17.006 1.00 16.74 ? 84  ALA A CA   1 
ATOM   958  C C    . ALA A 1 84  ? 23.993 3.678   -18.048 1.00 16.47 ? 84  ALA A C    1 
ATOM   959  O O    . ALA A 1 84  ? 23.405 4.714   -17.737 1.00 16.54 ? 84  ALA A O    1 
ATOM   960  C CB   . ALA A 1 84  ? 26.247 3.235   -17.041 1.00 16.55 ? 84  ALA A CB   1 
ATOM   961  H H    . ALA A 1 84  ? 25.279 1.014   -17.394 1.00 18.35 ? 84  ALA A H    1 
ATOM   962  H HA   . ALA A 1 84  ? 24.420 3.128   -16.130 1.00 20.09 ? 84  ALA A HA   1 
ATOM   963  H HB1  . ALA A 1 84  ? 26.349 4.192   -16.926 1.00 19.86 ? 84  ALA A HB1  1 
ATOM   964  H HB2  . ALA A 1 84  ? 26.698 2.765   -16.323 1.00 19.86 ? 84  ALA A HB2  1 
ATOM   965  H HB3  . ALA A 1 84  ? 26.615 2.964   -17.897 1.00 19.86 ? 84  ALA A HB3  1 
ATOM   966  N N    . SER A 1 85  ? 24.007 3.220   -19.300 1.00 16.18 ? 85  SER A N    1 
ATOM   967  C CA   . SER A 1 85  ? 23.245 3.895   -20.345 1.00 19.27 ? 85  SER A CA   1 
ATOM   968  C C    . SER A 1 85  ? 21.767 3.950   -20.001 1.00 17.82 ? 85  SER A C    1 
ATOM   969  O O    . SER A 1 85  ? 21.122 4.996   -20.148 1.00 19.21 ? 85  SER A O    1 
ATOM   970  C CB   . SER A 1 85  ? 23.438 3.157   -21.661 1.00 18.88 ? 85  SER A CB   1 
ATOM   971  O OG   . SER A 1 85  ? 22.562 3.650   -22.667 1.00 23.44 ? 85  SER A OG   1 
ATOM   972  H H    . SER A 1 85  ? 24.443 2.528   -19.566 1.00 19.42 ? 85  SER A H    1 
ATOM   973  H HA   . SER A 1 85  ? 23.573 4.804   -20.433 1.00 23.12 ? 85  SER A HA   1 
ATOM   974  H HB2  . SER A 1 85  ? 24.354 3.277   -21.957 1.00 22.66 ? 85  SER A HB2  1 
ATOM   975  H HB3  . SER A 1 85  ? 23.256 2.215   -21.521 1.00 22.66 ? 85  SER A HB3  1 
ATOM   976  H HG   . SER A 1 85  ? 21.773 3.413   -22.503 1.00 28.13 ? 85  SER A HG   1 
ATOM   977  N N    . ALA A 1 86  ? 21.211 2.827   -19.543 1.00 17.67 ? 86  ALA A N    1 
ATOM   978  C CA   . ALA A 1 86  ? 19.785 2.786   -19.239 1.00 18.63 ? 86  ALA A CA   1 
ATOM   979  C C    . ALA A 1 86  ? 19.436 3.693   -18.056 1.00 17.87 ? 86  ALA A C    1 
ATOM   980  O O    . ALA A 1 86  ? 18.402 4.370   -18.079 1.00 19.77 ? 86  ALA A O    1 
ATOM   981  C CB   . ALA A 1 86  ? 19.343 1.346   -18.961 1.00 19.77 ? 86  ALA A CB   1 
ATOM   982  H H    . ALA A 1 86  ? 21.631 2.090   -19.401 1.00 21.21 ? 86  ALA A H    1 
ATOM   983  H HA   . ALA A 1 86  ? 19.298 3.105   -20.014 1.00 22.36 ? 86  ALA A HA   1 
ATOM   984  H HB1  . ALA A 1 86  ? 18.392 1.339   -18.770 1.00 23.72 ? 86  ALA A HB1  1 
ATOM   985  H HB2  . ALA A 1 86  ? 19.527 0.802   -19.743 1.00 23.72 ? 86  ALA A HB2  1 
ATOM   986  H HB3  . ALA A 1 86  ? 19.836 1.006   -18.198 1.00 23.72 ? 86  ALA A HB3  1 
ATOM   987  N N    . ILE A 1 87  ? 20.275 3.715   -17.013 1.00 16.67 ? 87  ILE A N    1 
ATOM   988  C CA   . ILE A 1 87  ? 20.056 4.613   -15.881 1.00 17.55 ? 87  ILE A CA   1 
ATOM   989  C C    . ILE A 1 87  ? 20.028 6.060   -16.344 1.00 17.84 ? 87  ILE A C    1 
ATOM   990  O O    . ILE A 1 87  ? 19.136 6.837   -15.978 1.00 18.42 ? 87  ILE A O    1 
ATOM   991  C CB   . ILE A 1 87  ? 21.147 4.399   -14.814 1.00 14.90 ? 87  ILE A CB   1 
ATOM   992  C CG1  . ILE A 1 87  ? 21.017 3.027   -14.142 1.00 15.98 ? 87  ILE A CG1  1 
ATOM   993  C CG2  . ILE A 1 87  ? 21.098 5.505   -13.762 1.00 17.14 ? 87  ILE A CG2  1 
ATOM   994  C CD1  . ILE A 1 87  ? 22.201 2.681   -13.283 1.00 15.36 ? 87  ILE A CD1  1 
ATOM   995  H H    . ILE A 1 87  ? 20.975 3.221   -16.939 1.00 20.00 ? 87  ILE A H    1 
ATOM   996  H HA   . ILE A 1 87  ? 19.193 4.406   -15.490 1.00 21.06 ? 87  ILE A HA   1 
ATOM   997  H HB   . ILE A 1 87  ? 22.003 4.431   -15.269 1.00 17.89 ? 87  ILE A HB   1 
ATOM   998  H HG12 . ILE A 1 87  ? 20.228 3.026   -13.578 1.00 19.17 ? 87  ILE A HG12 1 
ATOM   999  H HG13 . ILE A 1 87  ? 20.936 2.346   -14.828 1.00 19.17 ? 87  ILE A HG13 1 
ATOM   1000 H HG21 . ILE A 1 87  ? 21.597 5.220   -12.981 1.00 20.57 ? 87  ILE A HG21 1 
ATOM   1001 H HG22 . ILE A 1 87  ? 21.493 6.310   -14.132 1.00 20.57 ? 87  ILE A HG22 1 
ATOM   1002 H HG23 . ILE A 1 87  ? 20.173 5.670   -13.521 1.00 20.57 ? 87  ILE A HG23 1 
ATOM   1003 H HD11 . ILE A 1 87  ? 22.182 1.731   -13.086 1.00 18.44 ? 87  ILE A HD11 1 
ATOM   1004 H HD12 . ILE A 1 87  ? 23.015 2.903   -13.762 1.00 18.44 ? 87  ILE A HD12 1 
ATOM   1005 H HD13 . ILE A 1 87  ? 22.153 3.190   -12.458 1.00 18.44 ? 87  ILE A HD13 1 
ATOM   1006 N N    . LYS A 1 88  ? 21.016 6.454   -17.145 1.00 18.04 ? 88  LYS A N    1 
ATOM   1007 C CA   . LYS A 1 88  ? 21.131 7.854   -17.520 1.00 18.72 ? 88  LYS A CA   1 
ATOM   1008 C C    . LYS A 1 88  ? 19.976 8.277   -18.407 1.00 22.12 ? 88  LYS A C    1 
ATOM   1009 O O    . LYS A 1 88  ? 19.577 9.443   -18.389 1.00 22.94 ? 88  LYS A O    1 
ATOM   1010 C CB   . LYS A 1 88  ? 22.466 8.112   -18.214 1.00 20.87 ? 88  LYS A CB   1 
ATOM   1011 C CG   . LYS A 1 88  ? 23.643 7.990   -17.273 1.00 20.16 ? 88  LYS A CG   1 
ATOM   1012 C CD   . LYS A 1 88  ? 23.748 9.173   -16.317 1.00 19.95 ? 88  LYS A CD   1 
ATOM   1013 C CE   . LYS A 1 88  ? 25.065 9.120   -15.544 1.00 21.75 ? 88  LYS A CE   1 
ATOM   1014 N NZ   . LYS A 1 88  ? 25.279 10.438  -14.881 1.00 23.60 ? 88  LYS A NZ   1 
ATOM   1015 H H    . LYS A 1 88  ? 21.621 5.939   -17.476 1.00 21.65 ? 88  LYS A H    1 
ATOM   1016 H HA   . LYS A 1 88  ? 21.112 8.399   -16.718 1.00 22.46 ? 88  LYS A HA   1 
ATOM   1017 H HB2  . LYS A 1 88  ? 22.582 7.465   -18.927 1.00 25.04 ? 88  LYS A HB2  1 
ATOM   1018 H HB3  . LYS A 1 88  ? 22.464 9.011   -18.579 1.00 25.04 ? 88  LYS A HB3  1 
ATOM   1019 H HG2  . LYS A 1 88  ? 23.544 7.184   -16.744 1.00 24.20 ? 88  LYS A HG2  1 
ATOM   1020 H HG3  . LYS A 1 88  ? 24.461 7.949   -17.792 1.00 24.20 ? 88  LYS A HG3  1 
ATOM   1021 H HD2  . LYS A 1 88  ? 23.719 10.002  -16.821 1.00 23.94 ? 88  LYS A HD2  1 
ATOM   1022 H HD3  . LYS A 1 88  ? 23.016 9.144   -15.682 1.00 23.94 ? 88  LYS A HD3  1 
ATOM   1023 H HE2  . LYS A 1 88  ? 25.025 8.427   -14.866 1.00 26.10 ? 88  LYS A HE2  1 
ATOM   1024 H HE3  . LYS A 1 88  ? 25.801 8.947   -16.152 1.00 26.10 ? 88  LYS A HE3  1 
ATOM   1025 H HZ1  . LYS A 1 88  ? 26.029 10.420  -14.402 1.00 28.32 ? 88  LYS A HZ1  1 
ATOM   1026 H HZ2  . LYS A 1 88  ? 25.343 11.080  -15.494 1.00 28.32 ? 88  LYS A HZ2  1 
ATOM   1027 H HZ3  . LYS A 1 88  ? 24.596 10.622  -14.341 1.00 28.32 ? 88  LYS A HZ3  1 
ATOM   1028 N N    . LEU A 1 89  ? 19.421 7.356   -19.185 1.00 20.97 ? 89  LEU A N    1 
ATOM   1029 C CA   . LEU A 1 89  ? 18.284 7.730   -20.012 1.00 21.39 ? 89  LEU A CA   1 
ATOM   1030 C C    . LEU A 1 89  ? 17.064 8.037   -19.156 1.00 24.79 ? 89  LEU A C    1 
ATOM   1031 O O    . LEU A 1 89  ? 16.187 8.791   -19.591 1.00 26.87 ? 89  LEU A O    1 
ATOM   1032 C CB   . LEU A 1 89  ? 17.956 6.596   -20.980 1.00 23.46 ? 89  LEU A CB   1 
ATOM   1033 C CG   . LEU A 1 89  ? 18.883 6.476   -22.188 1.00 28.92 ? 89  LEU A CG   1 
ATOM   1034 C CD1  . LEU A 1 89  ? 18.676 5.173   -22.976 1.00 34.28 ? 89  LEU A CD1  1 
ATOM   1035 C CD2  . LEU A 1 89  ? 18.746 7.661   -23.122 1.00 31.61 ? 89  LEU A CD2  1 
ATOM   1036 H H    . LEU A 1 89  ? 19.674 6.537   -19.250 1.00 25.16 ? 89  LEU A H    1 
ATOM   1037 H HA   . LEU A 1 89  ? 18.512 8.520   -20.527 1.00 25.67 ? 89  LEU A HA   1 
ATOM   1038 H HB2  . LEU A 1 89  ? 18.003 5.757   -20.494 1.00 28.15 ? 89  LEU A HB2  1 
ATOM   1039 H HB3  . LEU A 1 89  ? 17.057 6.734   -21.318 1.00 28.15 ? 89  LEU A HB3  1 
ATOM   1040 H HG   . LEU A 1 89  ? 19.785 6.461   -21.832 1.00 34.71 ? 89  LEU A HG   1 
ATOM   1041 H HD11 . LEU A 1 89  ? 19.268 5.172   -23.745 1.00 41.14 ? 89  LEU A HD11 1 
ATOM   1042 H HD12 . LEU A 1 89  ? 18.880 4.420   -22.400 1.00 41.14 ? 89  LEU A HD12 1 
ATOM   1043 H HD13 . LEU A 1 89  ? 17.753 5.125   -23.270 1.00 41.14 ? 89  LEU A HD13 1 
ATOM   1044 H HD21 . LEU A 1 89  ? 19.359 7.550   -23.866 1.00 37.93 ? 89  LEU A HD21 1 
ATOM   1045 H HD22 . LEU A 1 89  ? 17.833 7.701   -23.449 1.00 37.93 ? 89  LEU A HD22 1 
ATOM   1046 H HD23 . LEU A 1 89  ? 18.959 8.473   -22.636 1.00 37.93 ? 89  LEU A HD23 1 
ATOM   1047 N N    . LYS A 1 90  ? 16.980 7.474   -17.952 1.00 24.18 ? 90  LYS A N    1 
ATOM   1048 C CA   . LYS A 1 90  ? 15.862 7.763   -17.052 1.00 22.55 ? 90  LYS A CA   1 
ATOM   1049 C C    . LYS A 1 90  ? 16.131 8.973   -16.170 1.00 25.75 ? 90  LYS A C    1 
ATOM   1050 O O    . LYS A 1 90  ? 15.215 9.747   -15.879 1.00 29.16 ? 90  LYS A O    1 
ATOM   1051 C CB   . LYS A 1 90  ? 15.560 6.550   -16.170 1.00 23.65 ? 90  LYS A CB   1 
ATOM   1052 C CG   . LYS A 1 90  ? 14.933 5.356   -16.903 1.00 33.24 ? 90  LYS A CG   1 
ATOM   1053 C CD   . LYS A 1 90  ? 13.738 5.748   -17.764 1.00 37.77 ? 90  LYS A CD   1 
ATOM   1054 C CE   . LYS A 1 90  ? 13.276 4.571   -18.628 1.00 42.38 ? 90  LYS A CE   1 
ATOM   1055 N NZ   . LYS A 1 90  ? 12.201 3.786   -17.950 1.00 42.11 ? 90  LYS A NZ   1 
ATOM   1056 H H    . LYS A 1 90  ? 17.557 6.921   -17.632 1.00 29.01 ? 90  LYS A H    1 
ATOM   1057 H HA   . LYS A 1 90  ? 15.076 7.946   -17.590 1.00 27.07 ? 90  LYS A HA   1 
ATOM   1058 H HB2  . LYS A 1 90  ? 16.391 6.244   -15.773 1.00 28.38 ? 90  LYS A HB2  1 
ATOM   1059 H HB3  . LYS A 1 90  ? 14.941 6.822   -15.475 1.00 28.38 ? 90  LYS A HB3  1 
ATOM   1060 H HG2  . LYS A 1 90  ? 15.600 4.955   -17.483 1.00 39.89 ? 90  LYS A HG2  1 
ATOM   1061 H HG3  . LYS A 1 90  ? 14.629 4.707   -16.249 1.00 39.89 ? 90  LYS A HG3  1 
ATOM   1062 H HD2  . LYS A 1 90  ? 13.002 6.016   -17.192 1.00 45.32 ? 90  LYS A HD2  1 
ATOM   1063 H HD3  . LYS A 1 90  ? 13.988 6.479   -18.349 1.00 45.32 ? 90  LYS A HD3  1 
ATOM   1064 H HE2  . LYS A 1 90  ? 12.926 4.907   -19.468 1.00 50.86 ? 90  LYS A HE2  1 
ATOM   1065 H HE3  . LYS A 1 90  ? 14.027 3.980   -18.794 1.00 50.86 ? 90  LYS A HE3  1 
ATOM   1066 H HZ1  . LYS A 1 90  ? 11.928 3.124   -18.478 1.00 50.54 ? 90  LYS A HZ1  1 
ATOM   1067 H HZ2  . LYS A 1 90  ? 12.509 3.441   -17.190 1.00 50.54 ? 90  LYS A HZ2  1 
ATOM   1068 H HZ3  . LYS A 1 90  ? 11.508 4.314   -17.767 1.00 50.54 ? 90  LYS A HZ3  1 
ATOM   1069 N N    . ASN A 1 91  ? 17.370 9.149   -15.738 1.00 23.88 ? 91  ASN A N    1 
ATOM   1070 C CA   . ASN A 1 91  ? 17.780 10.262  -14.880 1.00 22.33 ? 91  ASN A CA   1 
ATOM   1071 C C    . ASN A 1 91  ? 19.244 10.586  -15.127 1.00 22.11 ? 91  ASN A C    1 
ATOM   1072 O O    . ASN A 1 91  ? 20.112 9.936   -14.567 1.00 20.70 ? 91  ASN A O    1 
ATOM   1073 C CB   . ASN A 1 91  ? 17.480 9.977   -13.423 1.00 23.69 ? 91  ASN A CB   1 
ATOM   1074 C CG   . ASN A 1 91  ? 17.914 11.106  -12.544 1.00 29.57 ? 91  ASN A CG   1 
ATOM   1075 O OD1  . ASN A 1 91  ? 18.034 12.221  -13.002 1.00 25.85 ? 91  ASN A OD1  1 
ATOM   1076 N ND2  . ASN A 1 91  ? 18.090 10.833  -11.264 1.00 34.87 ? 91  ASN A ND2  1 
ATOM   1077 H H    . ASN A 1 91  ? 18.020 8.620   -15.931 1.00 28.66 ? 91  ASN A H    1 
ATOM   1078 H HA   . ASN A 1 91  ? 17.280 11.049  -15.147 1.00 26.80 ? 91  ASN A HA   1 
ATOM   1079 H HB2  . ASN A 1 91  ? 16.525 9.852   -13.311 1.00 28.43 ? 91  ASN A HB2  1 
ATOM   1080 H HB3  . ASN A 1 91  ? 17.954 9.176   -13.148 1.00 28.43 ? 91  ASN A HB3  1 
ATOM   1081 H HD21 . ASN A 1 91  ? 18.339 11.452  -10.722 1.00 41.84 ? 91  ASN A HD21 1 
ATOM   1082 H HD22 . ASN A 1 91  ? 17.955 10.035  -10.972 1.00 41.84 ? 91  ASN A HD22 1 
ATOM   1083 N N    . ASN A 1 92  ? 19.467 11.567  -15.992 1.00 21.12 ? 92  ASN A N    1 
ATOM   1084 C CA   A ASN A 1 92  ? 20.877 11.982  -16.254 0.70 22.69 ? 92  ASN A CA   1 
ATOM   1085 C CA   B ASN A 1 92  ? 20.867 11.988  -16.265 0.30 22.58 ? 92  ASN A CA   1 
ATOM   1086 C C    . ASN A 1 92  ? 21.663 12.635  -15.080 1.00 22.49 ? 92  ASN A C    1 
ATOM   1087 O O    . ASN A 1 92  ? 22.962 12.758  -15.057 1.00 25.66 ? 92  ASN A O    1 
ATOM   1088 C CB   A ASN A 1 92  ? 20.959 12.879  -17.499 0.70 25.98 ? 92  ASN A CB   1 
ATOM   1089 C CB   B ASN A 1 92  ? 20.933 12.963  -17.442 0.30 25.71 ? 92  ASN A CB   1 
ATOM   1090 C CG   A ASN A 1 92  ? 20.224 14.191  -17.338 0.70 25.80 ? 92  ASN A CG   1 
ATOM   1091 C CG   B ASN A 1 92  ? 22.140 12.716  -18.322 0.30 29.38 ? 92  ASN A CG   1 
ATOM   1092 O OD1  A ASN A 1 92  ? 20.140 14.776  -16.259 0.70 34.51 ? 92  ASN A OD1  1 
ATOM   1093 O OD1  B ASN A 1 92  ? 23.114 13.463  -18.268 0.30 30.98 ? 92  ASN A OD1  1 
ATOM   1094 N ND2  A ASN A 1 92  ? 19.693 14.690  -18.457 0.70 33.22 ? 92  ASN A ND2  1 
ATOM   1095 N ND2  B ASN A 1 92  ? 22.094 11.665  -19.124 0.30 32.96 ? 92  ASN A ND2  1 
ATOM   1096 H H    A ASN A 1 92  ? 18.905 12.075  -16.360 0.70 25.34 ? 92  ASN A H    1 
ATOM   1097 H H    B ASN A 1 92  ? 18.936 12.316  -16.001 0.30 25.34 ? 92  ASN A H    1 
ATOM   1098 H HA   A ASN A 1 92  ? 21.364 11.176  -16.485 0.70 27.22 ? 92  ASN A HA   1 
ATOM   1099 H HA   B ASN A 1 92  ? 21.362 11.180  -16.542 0.30 27.09 ? 92  ASN A HA   1 
ATOM   1100 H HB2  A ASN A 1 92  ? 21.890 13.079  -17.682 0.70 31.18 ? 92  ASN A HB2  1 
ATOM   1101 H HB2  B ASN A 1 92  ? 20.120 12.876  -17.979 0.30 30.85 ? 92  ASN A HB2  1 
ATOM   1102 H HB3  A ASN A 1 92  ? 20.567 12.409  -18.252 0.70 31.18 ? 92  ASN A HB3  1 
ATOM   1103 H HB3  B ASN A 1 92  ? 20.971 13.876  -17.093 0.30 30.85 ? 92  ASN A HB3  1 
ATOM   1104 H HD21 A ASN A 1 92  ? 19.262 15.434  -18.434 0.70 39.87 ? 92  ASN A HD21 1 
ATOM   1105 H HD21 B ASN A 1 92  ? 22.819 11.410  -19.558 0.30 39.55 ? 92  ASN A HD21 1 
ATOM   1106 H HD22 A ASN A 1 92  ? 19.782 14.268  -19.201 0.70 39.87 ? 92  ASN A HD22 1 
ATOM   1107 H HD22 B ASN A 1 92  ? 21.342 11.209  -19.219 0.30 39.55 ? 92  ASN A HD22 1 
ATOM   1108 N N    . LYS A 1 93  ? 20.897 12.957  -14.009 1.00 21.77 ? 93  LYS A N    1 
ATOM   1109 C CA   . LYS A 1 93  ? 21.551 13.554  -12.855 1.00 21.93 ? 93  LYS A CA   1 
ATOM   1110 C C    . LYS A 1 93  ? 22.076 12.515  -11.876 1.00 22.73 ? 93  LYS A C    1 
ATOM   1111 O O    . LYS A 1 93  ? 22.860 12.877  -10.991 1.00 21.87 ? 93  LYS A O    1 
ATOM   1112 C CB   . LYS A 1 93  ? 20.577 14.472  -12.119 1.00 22.21 ? 93  LYS A CB   1 
ATOM   1113 C CG   . LYS A 1 93  ? 20.243 15.773  -12.864 1.00 25.35 ? 93  LYS A CG   1 
ATOM   1114 C CD   . LYS A 1 93  ? 19.642 16.835  -11.922 1.00 32.53 ? 93  LYS A CD   1 
ATOM   1115 C CE   . LYS A 1 93  ? 19.087 18.036  -12.695 1.00 39.11 ? 93  LYS A CE   1 
ATOM   1116 N NZ   . LYS A 1 93  ? 20.198 18.785  -13.347 1.00 45.62 ? 93  LYS A NZ   1 
ATOM   1117 H H    . LYS A 1 93  ? 20.044 12.873  -13.937 1.00 26.13 ? 93  LYS A H    1 
ATOM   1118 H HA   . LYS A 1 93  ? 22.299 14.089  -13.165 1.00 26.32 ? 93  LYS A HA   1 
ATOM   1119 H HB2  . LYS A 1 93  ? 19.746 13.993  -11.979 1.00 26.66 ? 93  LYS A HB2  1 
ATOM   1120 H HB3  . LYS A 1 93  ? 20.967 14.716  -11.265 1.00 26.66 ? 93  LYS A HB3  1 
ATOM   1121 H HG2  . LYS A 1 93  ? 21.054 16.136  -13.254 1.00 30.42 ? 93  LYS A HG2  1 
ATOM   1122 H HG3  . LYS A 1 93  ? 19.596 15.585  -13.562 1.00 30.42 ? 93  LYS A HG3  1 
ATOM   1123 H HD2  . LYS A 1 93  ? 18.917 16.439  -11.415 1.00 39.04 ? 93  LYS A HD2  1 
ATOM   1124 H HD3  . LYS A 1 93  ? 20.332 17.155  -11.320 1.00 39.04 ? 93  LYS A HD3  1 
ATOM   1125 H HE2  . LYS A 1 93  ? 18.475 17.727  -13.381 1.00 46.93 ? 93  LYS A HE2  1 
ATOM   1126 H HE3  . LYS A 1 93  ? 18.626 18.632  -12.084 1.00 46.93 ? 93  LYS A HE3  1 
ATOM   1127 H HZ1  . LYS A 1 93  ? 19.873 19.479  -13.799 1.00 54.74 ? 93  LYS A HZ1  1 
ATOM   1128 H HZ2  . LYS A 1 93  ? 20.768 19.082  -12.730 1.00 54.74 ? 93  LYS A HZ2  1 
ATOM   1129 H HZ3  . LYS A 1 93  ? 20.635 18.252  -13.910 1.00 54.74 ? 93  LYS A HZ3  1 
ATOM   1130 N N    . ALA A 1 94  ? 21.661 11.254  -11.987 1.00 17.49 ? 94  ALA A N    1 
ATOM   1131 C CA   . ALA A 1 94  ? 22.199 10.204  -11.138 1.00 17.69 ? 94  ALA A CA   1 
ATOM   1132 C C    . ALA A 1 94  ? 23.664 9.973   -11.460 1.00 17.46 ? 94  ALA A C    1 
ATOM   1133 O O    . ALA A 1 94  ? 24.055 9.953   -12.631 1.00 20.11 ? 94  ALA A O    1 
ATOM   1134 C CB   . ALA A 1 94  ? 21.424 8.907   -11.385 1.00 19.86 ? 94  ALA A CB   1 
ATOM   1135 H H    . ALA A 1 94  ? 21.068 10.983  -12.547 1.00 20.99 ? 94  ALA A H    1 
ATOM   1136 H HA   . ALA A 1 94  ? 22.118 10.458  -10.205 1.00 21.23 ? 94  ALA A HA   1 
ATOM   1137 H HB1  . ALA A 1 94  ? 21.785 8.210   -10.815 1.00 23.83 ? 94  ALA A HB1  1 
ATOM   1138 H HB2  . ALA A 1 94  ? 20.488 9.054   -11.175 1.00 23.83 ? 94  ALA A HB2  1 
ATOM   1139 H HB3  . ALA A 1 94  ? 21.519 8.655   -12.316 1.00 23.83 ? 94  ALA A HB3  1 
ATOM   1140 N N    . LYS A 1 95  ? 24.494 9.811   -10.435 1.00 14.50 ? 95  LYS A N    1 
ATOM   1141 C CA   . LYS A 1 95  ? 25.905 9.543   -10.619 1.00 14.75 ? 95  LYS A CA   1 
ATOM   1142 C C    . LYS A 1 95  ? 26.151 8.042   -10.544 1.00 15.44 ? 95  LYS A C    1 
ATOM   1143 O O    . LYS A 1 95  ? 25.715 7.390   -9.584  1.00 15.54 ? 95  LYS A O    1 
ATOM   1144 C CB   . LYS A 1 95  ? 26.736 10.257  -9.548  1.00 15.85 ? 95  LYS A CB   1 
ATOM   1145 C CG   . LYS A 1 95  ? 26.678 11.778  -9.609  1.00 14.84 ? 95  LYS A CG   1 
ATOM   1146 C CD   . LYS A 1 95  ? 27.308 12.334  -10.868 1.00 18.52 ? 95  LYS A CD   1 
ATOM   1147 C CE   . LYS A 1 95  ? 27.326 13.844  -10.793 1.00 20.53 ? 95  LYS A CE   1 
ATOM   1148 N NZ   . LYS A 1 95  ? 28.001 14.429  -11.975 1.00 24.50 ? 95  LYS A NZ   1 
ATOM   1149 H H    . LYS A 1 95  ? 24.254 9.854   -9.610  1.00 17.40 ? 95  LYS A H    1 
ATOM   1150 H HA   . LYS A 1 95  ? 26.184 9.861   -11.492 1.00 17.70 ? 95  LYS A HA   1 
ATOM   1151 H HB2  . LYS A 1 95  ? 26.412 9.987   -8.675  1.00 19.02 ? 95  LYS A HB2  1 
ATOM   1152 H HB3  . LYS A 1 95  ? 27.664 9.996   -9.653  1.00 19.02 ? 95  LYS A HB3  1 
ATOM   1153 H HG2  . LYS A 1 95  ? 25.751 12.061  -9.586  1.00 17.81 ? 95  LYS A HG2  1 
ATOM   1154 H HG3  . LYS A 1 95  ? 27.155 12.144  -8.847  1.00 17.81 ? 95  LYS A HG3  1 
ATOM   1155 H HD2  . LYS A 1 95  ? 28.220 12.013  -10.951 1.00 22.22 ? 95  LYS A HD2  1 
ATOM   1156 H HD3  . LYS A 1 95  ? 26.790 12.065  -11.642 1.00 22.22 ? 95  LYS A HD3  1 
ATOM   1157 H HE2  . LYS A 1 95  ? 26.416 14.177  -10.763 1.00 24.64 ? 95  LYS A HE2  1 
ATOM   1158 H HE3  . LYS A 1 95  ? 27.807 14.122  -9.997  1.00 24.64 ? 95  LYS A HE3  1 
ATOM   1159 H HZ1  . LYS A 1 95  ? 27.993 15.318  -11.923 1.00 29.39 ? 95  LYS A HZ1  1 
ATOM   1160 H HZ2  . LYS A 1 95  ? 28.846 14.150  -12.013 1.00 29.39 ? 95  LYS A HZ2  1 
ATOM   1161 H HZ3  . LYS A 1 95  ? 27.582 14.180  -12.720 1.00 29.39 ? 95  LYS A HZ3  1 
ATOM   1162 N N    . VAL A 1 96  ? 26.873 7.503   -11.521 1.00 14.13 ? 96  VAL A N    1 
ATOM   1163 C CA   . VAL A 1 96  ? 27.111 6.073   -11.652 1.00 13.88 ? 96  VAL A CA   1 
ATOM   1164 C C    . VAL A 1 96  ? 28.606 5.821   -11.567 1.00 14.18 ? 96  VAL A C    1 
ATOM   1165 O O    . VAL A 1 96  ? 29.392 6.383   -12.345 1.00 14.50 ? 96  VAL A O    1 
ATOM   1166 C CB   . VAL A 1 96  ? 26.516 5.538   -12.964 1.00 15.03 ? 96  VAL A CB   1 
ATOM   1167 C CG1  . VAL A 1 96  ? 26.847 4.087   -13.086 1.00 16.95 ? 96  VAL A CG1  1 
ATOM   1168 C CG2  . VAL A 1 96  ? 25.011 5.720   -12.984 1.00 17.42 ? 96  VAL A CG2  1 
ATOM   1169 H H    . VAL A 1 96  ? 27.248 7.964   -12.143 1.00 16.95 ? 96  VAL A H    1 
ATOM   1170 H HA   . VAL A 1 96  ? 26.702 5.601   -10.909 1.00 16.66 ? 96  VAL A HA   1 
ATOM   1171 H HB   . VAL A 1 96  ? 26.890 6.029   -13.713 1.00 18.04 ? 96  VAL A HB   1 
ATOM   1172 H HG11 . VAL A 1 96  ? 26.326 3.704   -13.810 1.00 20.35 ? 96  VAL A HG11 1 
ATOM   1173 H HG12 . VAL A 1 96  ? 27.793 3.993   -13.275 1.00 20.35 ? 96  VAL A HG12 1 
ATOM   1174 H HG13 . VAL A 1 96  ? 26.630 3.642   -12.252 1.00 20.35 ? 96  VAL A HG13 1 
ATOM   1175 H HG21 . VAL A 1 96  ? 24.655 5.319   -13.792 1.00 20.90 ? 96  VAL A HG21 1 
ATOM   1176 H HG22 . VAL A 1 96  ? 24.631 5.286   -12.204 1.00 20.90 ? 96  VAL A HG22 1 
ATOM   1177 H HG23 . VAL A 1 96  ? 24.808 6.668   -12.967 1.00 20.90 ? 96  VAL A HG23 1 
ATOM   1178 N N    . LEU A 1 97  ? 29.014 4.972   -10.631 1.00 11.92 ? 97  LEU A N    1 
ATOM   1179 C CA   . LEU A 1 97  ? 30.415 4.627   -10.437 1.00 11.79 ? 97  LEU A CA   1 
ATOM   1180 C C    . LEU A 1 97  ? 30.704 3.202   -10.876 1.00 11.57 ? 97  LEU A C    1 
ATOM   1181 O O    . LEU A 1 97  ? 29.902 2.288   -10.657 1.00 13.10 ? 97  LEU A O    1 
ATOM   1182 C CB   . LEU A 1 97  ? 30.817 4.759   -8.967  1.00 11.98 ? 97  LEU A CB   1 
ATOM   1183 C CG   . LEU A 1 97  ? 30.533 6.097   -8.319  1.00 12.38 ? 97  LEU A CG   1 
ATOM   1184 C CD1  . LEU A 1 97  ? 31.048 6.055   -6.887  1.00 14.61 ? 97  LEU A CD1  1 
ATOM   1185 C CD2  . LEU A 1 97  ? 31.166 7.270   -9.053  1.00 14.80 ? 97  LEU A CD2  1 
ATOM   1186 H H    . LEU A 1 97  ? 28.484 4.574   -10.083 1.00 14.30 ? 97  LEU A H    1 
ATOM   1187 H HA   . LEU A 1 97  ? 30.944 5.230   -10.982 1.00 14.15 ? 97  LEU A HA   1 
ATOM   1188 H HB2  . LEU A 1 97  ? 30.335 4.087   -8.460  1.00 14.38 ? 97  LEU A HB2  1 
ATOM   1189 H HB3  . LEU A 1 97  ? 31.772 4.605   -8.900  1.00 14.38 ? 97  LEU A HB3  1 
ATOM   1190 H HG   . LEU A 1 97  ? 29.575 6.248   -8.345  1.00 14.85 ? 97  LEU A HG   1 
ATOM   1191 H HD11 . LEU A 1 97  ? 30.841 6.896   -6.452  1.00 17.53 ? 97  LEU A HD11 1 
ATOM   1192 H HD12 . LEU A 1 97  ? 30.617 5.324   -6.417  1.00 17.53 ? 97  LEU A HD12 1 
ATOM   1193 H HD13 . LEU A 1 97  ? 32.008 5.918   -6.901  1.00 17.53 ? 97  LEU A HD13 1 
ATOM   1194 H HD21 . LEU A 1 97  ? 30.976 8.087   -8.565  1.00 17.76 ? 97  LEU A HD21 1 
ATOM   1195 H HD22 . LEU A 1 97  ? 32.124 7.131   -9.104  1.00 17.76 ? 97  LEU A HD22 1 
ATOM   1196 H HD23 . LEU A 1 97  ? 30.791 7.324   -9.946  1.00 17.76 ? 97  LEU A HD23 1 
ATOM   1197 N N    . TYR A 1 98  ? 31.885 3.005   -11.433 1.00 12.17 ? 98  TYR A N    1 
ATOM   1198 C CA   . TYR A 1 98  ? 32.375 1.689   -11.840 1.00 11.16 ? 98  TYR A CA   1 
ATOM   1199 C C    . TYR A 1 98  ? 33.238 1.086   -10.743 1.00 11.18 ? 98  TYR A C    1 
ATOM   1200 O O    . TYR A 1 98  ? 34.283 1.640   -10.391 1.00 12.37 ? 98  TYR A O    1 
ATOM   1201 C CB   . TYR A 1 98  ? 33.255 1.857   -13.063 1.00 13.93 ? 98  TYR A CB   1 
ATOM   1202 C CG   . TYR A 1 98  ? 33.797 0.599   -13.673 1.00 12.54 ? 98  TYR A CG   1 
ATOM   1203 C CD1  . TYR A 1 98  ? 32.979 -0.479  -13.916 1.00 13.08 ? 98  TYR A CD1  1 
ATOM   1204 C CD2  . TYR A 1 98  ? 35.129 0.520   -14.069 1.00 13.07 ? 98  TYR A CD2  1 
ATOM   1205 C CE1  . TYR A 1 98  ? 33.456 -1.613  -14.563 1.00 14.06 ? 98  TYR A CE1  1 
ATOM   1206 C CE2  . TYR A 1 98  ? 35.619 -0.622  -14.724 1.00 13.22 ? 98  TYR A CE2  1 
ATOM   1207 C CZ   . TYR A 1 98  ? 34.775 -1.677  -14.939 1.00 12.38 ? 98  TYR A CZ   1 
ATOM   1208 O OH   . TYR A 1 98  ? 35.209 -2.811  -15.627 1.00 16.65 ? 98  TYR A OH   1 
ATOM   1209 H H    . TYR A 1 98  ? 32.446 3.637   -11.593 1.00 14.61 ? 98  TYR A H    1 
ATOM   1210 H HA   . TYR A 1 98  ? 31.617 1.109   -12.011 1.00 13.40 ? 98  TYR A HA   1 
ATOM   1211 H HB2  . TYR A 1 98  ? 32.735 2.304   -13.749 1.00 16.72 ? 98  TYR A HB2  1 
ATOM   1212 H HB3  . TYR A 1 98  ? 34.016 2.404   -12.814 1.00 16.72 ? 98  TYR A HB3  1 
ATOM   1213 H HD1  . TYR A 1 98  ? 32.090 -0.449  -13.643 1.00 15.70 ? 98  TYR A HD1  1 
ATOM   1214 H HD2  . TYR A 1 98  ? 35.702 1.232   -13.897 1.00 15.68 ? 98  TYR A HD2  1 
ATOM   1215 H HE1  . TYR A 1 98  ? 32.885 -2.326  -14.739 1.00 16.87 ? 98  TYR A HE1  1 
ATOM   1216 H HE2  . TYR A 1 98  ? 36.504 -0.660  -15.007 1.00 15.87 ? 98  TYR A HE2  1 
ATOM   1217 H HH   . TYR A 1 98  ? 36.030 -2.749  -15.794 1.00 19.98 ? 98  TYR A HH   1 
ATOM   1218 N N    . TYR A 1 99  ? 32.854 -0.088  -10.257 1.00 11.40 ? 99  TYR A N    1 
ATOM   1219 C CA   . TYR A 1 99  ? 33.679 -0.819  -9.283  1.00 10.41 ? 99  TYR A CA   1 
ATOM   1220 C C    . TYR A 1 99  ? 34.999 -1.228  -9.923  1.00 11.30 ? 99  TYR A C    1 
ATOM   1221 O O    . TYR A 1 99  ? 35.029 -1.743  -11.046 1.00 11.08 ? 99  TYR A O    1 
ATOM   1222 C CB   . TYR A 1 99  ? 32.904 -2.063  -8.828  1.00 10.82 ? 99  TYR A CB   1 
ATOM   1223 C CG   . TYR A 1 99  ? 33.670 -3.009  -7.952  1.00 10.45 ? 99  TYR A CG   1 
ATOM   1224 C CD1  . TYR A 1 99  ? 34.576 -3.913  -8.463  1.00 11.44 ? 99  TYR A CD1  1 
ATOM   1225 C CD2  . TYR A 1 99  ? 33.448 -3.029  -6.575  1.00 11.90 ? 99  TYR A CD2  1 
ATOM   1226 C CE1  . TYR A 1 99  ? 35.296 -4.770  -7.632  1.00 11.46 ? 99  TYR A CE1  1 
ATOM   1227 C CE2  . TYR A 1 99  ? 34.175 -3.884  -5.734  1.00 11.67 ? 99  TYR A CE2  1 
ATOM   1228 C CZ   . TYR A 1 99  ? 35.083 -4.731  -6.263  1.00 11.67 ? 99  TYR A CZ   1 
ATOM   1229 O OH   . TYR A 1 99  ? 35.800 -5.590  -5.435  1.00 13.46 ? 99  TYR A OH   1 
ATOM   1230 H H    . TYR A 1 99  ? 32.123 -0.488  -10.470 1.00 13.68 ? 99  TYR A H    1 
ATOM   1231 H HA   . TYR A 1 99  ? 33.876 -0.265  -8.511  1.00 12.49 ? 99  TYR A HA   1 
ATOM   1232 H HB2  . TYR A 1 99  ? 32.125 -1.772  -8.329  1.00 12.98 ? 99  TYR A HB2  1 
ATOM   1233 H HB3  . TYR A 1 99  ? 32.628 -2.556  -9.616  1.00 12.98 ? 99  TYR A HB3  1 
ATOM   1234 H HD1  . TYR A 1 99  ? 34.709 -3.953  -9.383  1.00 13.72 ? 99  TYR A HD1  1 
ATOM   1235 H HD2  . TYR A 1 99  ? 32.806 -2.465  -6.208  1.00 14.28 ? 99  TYR A HD2  1 
ATOM   1236 H HE1  . TYR A 1 99  ? 35.914 -5.364  -7.993  1.00 13.75 ? 99  TYR A HE1  1 
ATOM   1237 H HE2  . TYR A 1 99  ? 34.032 -3.868  -4.815  1.00 14.01 ? 99  TYR A HE2  1 
ATOM   1238 H HH   . TYR A 1 99  ? 35.598 -5.451  -4.632  1.00 16.15 ? 99  TYR A HH   1 
ATOM   1239 N N    . ARG A 1 100 ? 36.095 -1.075  -9.194  1.00 10.72 ? 100 ARG A N    1 
ATOM   1240 C CA   . ARG A 1 100 ? 37.335 -1.715  -9.605  1.00 10.70 ? 100 ARG A CA   1 
ATOM   1241 C C    . ARG A 1 100 ? 38.141 -2.130  -8.392  1.00 10.85 ? 100 ARG A C    1 
ATOM   1242 O O    . ARG A 1 100 ? 38.369 -1.328  -7.477  1.00 11.36 ? 100 ARG A O    1 
ATOM   1243 C CB   . ARG A 1 100 ? 38.160 -0.797  -10.512 1.00 12.03 ? 100 ARG A CB   1 
ATOM   1244 C CG   . ARG A 1 100 ? 39.189 -1.550  -11.323 1.00 12.07 ? 100 ARG A CG   1 
ATOM   1245 C CD   . ARG A 1 100 ? 38.540 -2.284  -12.520 1.00 13.95 ? 100 ARG A CD   1 
ATOM   1246 N NE   . ARG A 1 100 ? 39.532 -2.758  -13.481 1.00 13.52 ? 100 ARG A NE   1 
ATOM   1247 C CZ   . ARG A 1 100 ? 39.744 -4.015  -13.840 1.00 12.27 ? 100 ARG A CZ   1 
ATOM   1248 N NH1  . ARG A 1 100 ? 39.075 -5.014  -13.315 1.00 12.67 ? 100 ARG A NH1  1 
ATOM   1249 N NH2  . ARG A 1 100 ? 40.638 -4.274  -14.802 1.00 14.00 ? 100 ARG A NH2  1 
ATOM   1250 H H    . ARG A 1 100 ? 36.145 -0.615  -8.469  1.00 12.87 ? 100 ARG A H    1 
ATOM   1251 H HA   . ARG A 1 100 ? 37.119 -2.523  -10.097 1.00 12.84 ? 100 ARG A HA   1 
ATOM   1252 H HB2  . ARG A 1 100 ? 37.564 -0.343  -11.128 1.00 14.43 ? 100 ARG A HB2  1 
ATOM   1253 H HB3  . ARG A 1 100 ? 38.627 -0.147  -9.963  1.00 14.43 ? 100 ARG A HB3  1 
ATOM   1254 H HG2  . ARG A 1 100 ? 39.847 -0.925  -11.669 1.00 14.48 ? 100 ARG A HG2  1 
ATOM   1255 H HG3  . ARG A 1 100 ? 39.623 -2.210  -10.760 1.00 14.48 ? 100 ARG A HG3  1 
ATOM   1256 H HD2  . ARG A 1 100 ? 38.045 -3.051  -12.193 1.00 16.74 ? 100 ARG A HD2  1 
ATOM   1257 H HD3  . ARG A 1 100 ? 37.941 -1.674  -12.980 1.00 16.74 ? 100 ARG A HD3  1 
ATOM   1258 H HE   . ARG A 1 100 ? 40.028 -2.161  -13.851 1.00 16.22 ? 100 ARG A HE   1 
ATOM   1259 H HH11 . ARG A 1 100 ? 38.476 -4.863  -12.716 1.00 15.20 ? 100 ARG A HH11 1 
ATOM   1260 H HH12 . ARG A 1 100 ? 39.235 -5.820  -13.569 1.00 15.20 ? 100 ARG A HH12 1 
ATOM   1261 H HH21 . ARG A 1 100 ? 41.066 -3.628  -15.177 1.00 16.81 ? 100 ARG A HH21 1 
ATOM   1262 H HH22 . ARG A 1 100 ? 40.786 -5.085  -15.045 1.00 16.81 ? 100 ARG A HH22 1 
ATOM   1263 N N    . ASN A 1 101 ? 38.550 -3.380  -8.354  1.00 10.22 ? 101 ASN A N    1 
ATOM   1264 C CA   . ASN A 1 101 ? 39.387 -3.895  -7.267  1.00 9.93  ? 101 ASN A CA   1 
ATOM   1265 C C    . ASN A 1 101 ? 40.840 -3.652  -7.634  1.00 9.99  ? 101 ASN A C    1 
ATOM   1266 O O    . ASN A 1 101 ? 41.270 -4.019  -8.732  1.00 11.18 ? 101 ASN A O    1 
ATOM   1267 C CB   . ASN A 1 101 ? 39.125 -5.361  -7.031  1.00 10.91 ? 101 ASN A CB   1 
ATOM   1268 C CG   . ASN A 1 101 ? 39.591 -5.783  -5.673  1.00 9.25  ? 101 ASN A CG   1 
ATOM   1269 O OD1  . ASN A 1 101 ? 40.791 -5.875  -5.417  1.00 10.80 ? 101 ASN A OD1  1 
ATOM   1270 N ND2  . ASN A 1 101 ? 38.661 -5.988  -4.782  1.00 11.59 ? 101 ASN A ND2  1 
ATOM   1271 H H    . ASN A 1 101 ? 38.358 -3.968  -8.951  1.00 12.27 ? 101 ASN A H    1 
ATOM   1272 H HA   . ASN A 1 101 ? 39.188 -3.435  -6.436  1.00 11.91 ? 101 ASN A HA   1 
ATOM   1273 H HB2  . ASN A 1 101 ? 38.173 -5.532  -7.095  1.00 13.10 ? 101 ASN A HB2  1 
ATOM   1274 H HB3  . ASN A 1 101 ? 39.602 -5.884  -7.695  1.00 13.10 ? 101 ASN A HB3  1 
ATOM   1275 H HD21 . ASN A 1 101 ? 38.875 -6.232  -3.985  1.00 13.90 ? 101 ASN A HD21 1 
ATOM   1276 H HD22 . ASN A 1 101 ? 37.834 -5.878  -4.990  1.00 13.90 ? 101 ASN A HD22 1 
ATOM   1277 N N    . VAL A 1 102 ? 41.612 -3.053  -6.733  1.00 10.53 ? 102 VAL A N    1 
ATOM   1278 C CA   . VAL A 1 102 ? 42.981 -2.651  -7.048  1.00 11.02 ? 102 VAL A CA   1 
ATOM   1279 C C    . VAL A 1 102 ? 43.947 -3.823  -7.060  1.00 11.31 ? 102 VAL A C    1 
ATOM   1280 O O    . VAL A 1 102 ? 45.028 -3.698  -7.650  1.00 12.68 ? 102 VAL A O    1 
ATOM   1281 C CB   . VAL A 1 102 ? 43.419 -1.513  -6.102  1.00 12.35 ? 102 VAL A CB   1 
ATOM   1282 C CG1  . VAL A 1 102 ? 43.678 -1.988  -4.676  1.00 12.48 ? 102 VAL A CG1  1 
ATOM   1283 C CG2  . VAL A 1 102 ? 44.631 -0.802  -6.673  1.00 13.82 ? 102 VAL A CG2  1 
ATOM   1284 H H    . VAL A 1 102 ? 41.368 -2.865  -5.930  1.00 12.63 ? 102 VAL A H    1 
ATOM   1285 H HA   . VAL A 1 102 ? 43.015 -2.297  -7.950  1.00 13.23 ? 102 VAL A HA   1 
ATOM   1286 H HB   . VAL A 1 102 ? 42.684 -0.883  -6.038  1.00 14.81 ? 102 VAL A HB   1 
ATOM   1287 H HG11 . VAL A 1 102 ? 43.843 -1.217  -4.111  1.00 14.98 ? 102 VAL A HG11 1 
ATOM   1288 H HG12 . VAL A 1 102 ? 42.900 -2.471  -4.357  1.00 14.98 ? 102 VAL A HG12 1 
ATOM   1289 H HG13 . VAL A 1 102 ? 44.453 -2.572  -4.673  1.00 14.98 ? 102 VAL A HG13 1 
ATOM   1290 H HG21 . VAL A 1 102 ? 44.873 -0.069  -6.086  1.00 16.58 ? 102 VAL A HG21 1 
ATOM   1291 H HG22 . VAL A 1 102 ? 45.366 -1.431  -6.737  1.00 16.58 ? 102 VAL A HG22 1 
ATOM   1292 H HG23 . VAL A 1 102 ? 44.410 -0.461  -7.554  1.00 16.58 ? 102 VAL A HG23 1 
ATOM   1293 N N    . VAL A 1 103 ? 43.607 -4.947  -6.432  1.00 10.94 ? 103 VAL A N    1 
ATOM   1294 C CA   . VAL A 1 103 ? 44.538 -6.072  -6.380  1.00 10.76 ? 103 VAL A CA   1 
ATOM   1295 C C    . VAL A 1 103 ? 43.950 -7.443  -6.663  1.00 11.81 ? 103 VAL A C    1 
ATOM   1296 O O    . VAL A 1 103 ? 44.713 -8.341  -7.033  1.00 12.62 ? 103 VAL A O    1 
ATOM   1297 C CB   . VAL A 1 103 ? 45.338 -6.155  -5.063  1.00 13.01 ? 103 VAL A CB   1 
ATOM   1298 C CG1  . VAL A 1 103 ? 46.404 -5.130  -5.009  1.00 14.90 ? 103 VAL A CG1  1 
ATOM   1299 C CG2  . VAL A 1 103 ? 44.443 -6.122  -3.836  1.00 12.20 ? 103 VAL A CG2  1 
ATOM   1300 H H    . VAL A 1 103 ? 42.855 -5.081  -6.035  1.00 13.13 ? 103 VAL A H    1 
ATOM   1301 H HA   . VAL A 1 103 ? 45.116 -5.865  -7.131  1.00 12.92 ? 103 VAL A HA   1 
ATOM   1302 H HB   . VAL A 1 103 ? 45.777 -7.019  -5.046  1.00 15.62 ? 103 VAL A HB   1 
ATOM   1303 H HG11 . VAL A 1 103 ? 46.872 -5.205  -4.162  1.00 17.89 ? 103 VAL A HG11 1 
ATOM   1304 H HG12 . VAL A 1 103 ? 47.022 -5.278  -5.742  1.00 17.89 ? 103 VAL A HG12 1 
ATOM   1305 H HG13 . VAL A 1 103 ? 46.002 -4.251  -5.088  1.00 17.89 ? 103 VAL A HG13 1 
ATOM   1306 H HG21 . VAL A 1 103 ? 44.988 -6.258  -3.045  1.00 14.64 ? 103 VAL A HG21 1 
ATOM   1307 H HG22 . VAL A 1 103 ? 44.002 -5.259  -3.790  1.00 14.64 ? 103 VAL A HG22 1 
ATOM   1308 H HG23 . VAL A 1 103 ? 43.783 -6.828  -3.908  1.00 14.64 ? 103 VAL A HG23 1 
ATOM   1309 N N    . ILE A 1 104 ? 42.655 -7.678  -6.457  1.00 11.26 ? 104 ILE A N    1 
ATOM   1310 C CA   . ILE A 1 104 ? 42.088 -9.012  -6.621  1.00 11.65 ? 104 ILE A CA   1 
ATOM   1311 C C    . ILE A 1 104 ? 41.626 -9.186  -8.062  1.00 11.53 ? 104 ILE A C    1 
ATOM   1312 O O    . ILE A 1 104 ? 40.869 -8.362  -8.591  1.00 12.31 ? 104 ILE A O    1 
ATOM   1313 C CB   . ILE A 1 104 ? 40.928 -9.264  -5.646  1.00 11.47 ? 104 ILE A CB   1 
ATOM   1314 C CG1  . ILE A 1 104 ? 41.413 -9.114  -4.198  1.00 12.86 ? 104 ILE A CG1  1 
ATOM   1315 C CG2  . ILE A 1 104 ? 40.371 -10.655 -5.901  1.00 12.62 ? 104 ILE A CG2  1 
ATOM   1316 C CD1  . ILE A 1 104 ? 40.322 -9.166  -3.188  1.00 16.13 ? 104 ILE A CD1  1 
ATOM   1317 H H    . ILE A 1 104 ? 42.085 -7.079  -6.221  1.00 13.52 ? 104 ILE A H    1 
ATOM   1318 H HA   . ILE A 1 104 ? 42.784 -9.662  -6.438  1.00 13.97 ? 104 ILE A HA   1 
ATOM   1319 H HB   . ILE A 1 104 ? 40.226 -8.610  -5.788  1.00 13.76 ? 104 ILE A HB   1 
ATOM   1320 H HG12 . ILE A 1 104 ? 42.033 -9.833  -4.000  1.00 15.43 ? 104 ILE A HG12 1 
ATOM   1321 H HG13 . ILE A 1 104 ? 41.860 -8.257  -4.106  1.00 15.43 ? 104 ILE A HG13 1 
ATOM   1322 H HG21 . ILE A 1 104 ? 39.755 -10.884 -5.187  1.00 15.15 ? 104 ILE A HG21 1 
ATOM   1323 H HG22 . ILE A 1 104 ? 39.906 -10.657 -6.752  1.00 15.15 ? 104 ILE A HG22 1 
ATOM   1324 H HG23 . ILE A 1 104 ? 41.104 -11.290 -5.922  1.00 15.15 ? 104 ILE A HG23 1 
ATOM   1325 H HD11 . ILE A 1 104 ? 40.667 -8.862  -2.334  1.00 19.36 ? 104 ILE A HD11 1 
ATOM   1326 H HD12 . ILE A 1 104 ? 39.597 -8.589  -3.477  1.00 19.36 ? 104 ILE A HD12 1 
ATOM   1327 H HD13 . ILE A 1 104 ? 40.006 -10.080 -3.111  1.00 19.36 ? 104 ILE A HD13 1 
ATOM   1328 N N    . ASN A 1 105 ? 42.053 -10.289 -8.694  1.00 11.67 ? 105 ASN A N    1 
ATOM   1329 C CA   . ASN A 1 105 ? 41.705 -10.628 -10.081 1.00 11.36 ? 105 ASN A CA   1 
ATOM   1330 C C    . ASN A 1 105 ? 40.432 -11.473 -10.098 1.00 11.32 ? 105 ASN A C    1 
ATOM   1331 O O    . ASN A 1 105 ? 40.460 -12.668 -10.322 1.00 13.07 ? 105 ASN A O    1 
ATOM   1332 C CB   . ASN A 1 105 ? 42.911 -11.320 -10.709 1.00 11.95 ? 105 ASN A CB   1 
ATOM   1333 C CG   . ASN A 1 105 ? 42.660 -11.914 -12.090 1.00 12.43 ? 105 ASN A CG   1 
ATOM   1334 O OD1  . ASN A 1 105 ? 43.219 -12.969 -12.404 1.00 14.38 ? 105 ASN A OD1  1 
ATOM   1335 N ND2  . ASN A 1 105 ? 41.888 -11.224 -12.927 1.00 13.34 ? 105 ASN A ND2  1 
ATOM   1336 H H    . ASN A 1 105 ? 42.563 -10.876 -8.328  1.00 14.00 ? 105 ASN A H    1 
ATOM   1337 H HA   . ASN A 1 105 ? 41.501 -9.833  -10.597 1.00 13.64 ? 105 ASN A HA   1 
ATOM   1338 H HB2  . ASN A 1 105 ? 43.627 -10.672 -10.797 1.00 14.34 ? 105 ASN A HB2  1 
ATOM   1339 H HB3  . ASN A 1 105 ? 43.188 -12.045 -10.127 1.00 14.34 ? 105 ASN A HB3  1 
ATOM   1340 H HD21 . ASN A 1 105 ? 41.726 -11.531 -13.714 1.00 16.01 ? 105 ASN A HD21 1 
ATOM   1341 H HD22 . ASN A 1 105 ? 41.551 -10.472 -12.681 1.00 16.01 ? 105 ASN A HD22 1 
ATOM   1342 N N    . TRP A 1 106 ? 39.293 -10.822 -9.811  1.00 11.85 ? 106 TRP A N    1 
ATOM   1343 C CA   . TRP A 1 106 ? 38.008 -11.487 -9.894  1.00 11.98 ? 106 TRP A CA   1 
ATOM   1344 C C    . TRP A 1 106 ? 37.707 -11.940 -11.323 1.00 12.79 ? 106 TRP A C    1 
ATOM   1345 O O    . TRP A 1 106 ? 38.249 -11.399 -12.294 1.00 13.46 ? 106 TRP A O    1 
ATOM   1346 C CB   . TRP A 1 106 ? 36.892 -10.528 -9.501  1.00 14.19 ? 106 TRP A CB   1 
ATOM   1347 C CG   . TRP A 1 106 ? 36.969 -9.937  -8.140  1.00 15.65 ? 106 TRP A CG   1 
ATOM   1348 C CD1  . TRP A 1 106 ? 37.167 -8.616  -7.872  1.00 19.18 ? 106 TRP A CD1  1 
ATOM   1349 C CD2  . TRP A 1 106 ? 36.822 -10.597 -6.899  1.00 15.71 ? 106 TRP A CD2  1 
ATOM   1350 N NE1  . TRP A 1 106 ? 37.128 -8.408  -6.516  1.00 21.02 ? 106 TRP A NE1  1 
ATOM   1351 C CE2  . TRP A 1 106 ? 36.958 -9.608  -5.884  1.00 16.44 ? 106 TRP A CE2  1 
ATOM   1352 C CE3  . TRP A 1 106 ? 36.621 -11.916 -6.525  1.00 15.78 ? 106 TRP A CE3  1 
ATOM   1353 C CZ2  . TRP A 1 106 ? 36.846 -9.902  -4.531  1.00 20.99 ? 106 TRP A CZ2  1 
ATOM   1354 C CZ3  . TRP A 1 106 ? 36.532 -12.213 -5.160  1.00 19.90 ? 106 TRP A CZ3  1 
ATOM   1355 C CH2  . TRP A 1 106 ? 36.665 -11.202 -4.191  1.00 19.85 ? 106 TRP A CH2  1 
ATOM   1356 H H    . TRP A 1 106 ? 39.249 -9.998  -9.568  1.00 14.22 ? 106 TRP A H    1 
ATOM   1357 H HA   . TRP A 1 106 ? 38.032 -12.254 -9.301  1.00 14.38 ? 106 TRP A HA   1 
ATOM   1358 H HB2  . TRP A 1 106 ? 36.894 -9.790  -10.131 1.00 17.02 ? 106 TRP A HB2  1 
ATOM   1359 H HB3  . TRP A 1 106 ? 36.051 -11.007 -9.555  1.00 17.02 ? 106 TRP A HB3  1 
ATOM   1360 H HD1  . TRP A 1 106 ? 37.307 -7.955  -8.511  1.00 23.02 ? 106 TRP A HD1  1 
ATOM   1361 H HE1  . TRP A 1 106 ? 37.198 -7.645  -6.126  1.00 25.22 ? 106 TRP A HE1  1 
ATOM   1362 H HE3  . TRP A 1 106 ? 36.548 -12.587 -7.165  1.00 18.94 ? 106 TRP A HE3  1 
ATOM   1363 H HZ2  . TRP A 1 106 ? 36.893 -9.235  -3.885  1.00 25.19 ? 106 TRP A HZ2  1 
ATOM   1364 H HZ3  . TRP A 1 106 ? 36.384 -13.091 -4.890  1.00 23.88 ? 106 TRP A HZ3  1 
ATOM   1365 H HH2  . TRP A 1 106 ? 36.627 -11.432 -3.291  1.00 23.82 ? 106 TRP A HH2  1 
ATOM   1366 N N    . GLY A 1 107 ? 36.830 -12.916 -11.442 1.00 13.60 ? 107 GLY A N    1 
ATOM   1367 C CA   . GLY A 1 107 ? 36.325 -13.321 -12.744 1.00 13.75 ? 107 GLY A CA   1 
ATOM   1368 C C    . GLY A 1 107 ? 35.332 -12.345 -13.331 1.00 14.61 ? 107 GLY A C    1 
ATOM   1369 O O    . GLY A 1 107 ? 34.951 -11.336 -12.748 1.00 15.09 ? 107 GLY A O    1 
ATOM   1370 H H    . GLY A 1 107 ? 36.508 -13.365 -10.783 1.00 16.33 ? 107 GLY A H    1 
ATOM   1371 H HA2  . GLY A 1 107 ? 37.068 -13.403 -13.362 1.00 16.51 ? 107 GLY A HA2  1 
ATOM   1372 H HA3  . GLY A 1 107 ? 35.887 -14.183 -12.661 1.00 16.51 ? 107 GLY A HA3  1 
ATOM   1373 N N    . ASN A 1 108 ? 34.954 -12.644 -14.563 1.00 13.37 ? 108 ASN A N    1 
ATOM   1374 C CA   . ASN A 1 108 ? 33.869 -12.005 -15.303 1.00 14.50 ? 108 ASN A CA   1 
ATOM   1375 C C    . ASN A 1 108 ? 34.242 -10.662 -15.914 1.00 13.78 ? 108 ASN A C    1 
ATOM   1376 O O    . ASN A 1 108 ? 33.342 -9.943  -16.402 1.00 17.04 ? 108 ASN A O    1 
ATOM   1377 C CB   . ASN A 1 108 ? 32.576 -11.916 -14.489 1.00 17.07 ? 108 ASN A CB   1 
ATOM   1378 C CG   . ASN A 1 108 ? 32.176 -13.253 -13.922 1.00 22.49 ? 108 ASN A CG   1 
ATOM   1379 O OD1  . ASN A 1 108 ? 32.189 -13.461 -12.713 1.00 31.36 ? 108 ASN A OD1  1 
ATOM   1380 N ND2  . ASN A 1 108 ? 31.890 -14.187 -14.806 1.00 22.78 ? 108 ASN A ND2  1 
ATOM   1381 H H    . ASN A 1 108 ? 35.337 -13.259 -15.028 1.00 16.05 ? 108 ASN A H    1 
ATOM   1382 H HA   . ASN A 1 108 ? 33.670 -12.575 -16.062 1.00 17.40 ? 108 ASN A HA   1 
ATOM   1383 H HB2  . ASN A 1 108 ? 32.705 -11.300 -13.751 1.00 20.48 ? 108 ASN A HB2  1 
ATOM   1384 H HB3  . ASN A 1 108 ? 31.859 -11.603 -15.062 1.00 20.48 ? 108 ASN A HB3  1 
ATOM   1385 H HD21 . ASN A 1 108 ? 31.655 -14.971 -14.543 1.00 27.34 ? 108 ASN A HD21 1 
ATOM   1386 H HD22 . ASN A 1 108 ? 31.940 -14.012 -15.647 1.00 27.34 ? 108 ASN A HD22 1 
ATOM   1387 N N    . TYR A 1 109 ? 35.504 -10.320 -15.986 1.00 12.43 ? 109 TYR A N    1 
ATOM   1388 C CA   . TYR A 1 109 ? 35.981 -9.195  -16.795 1.00 12.22 ? 109 TYR A CA   1 
ATOM   1389 C C    . TYR A 1 109 ? 36.603 -9.774  -18.071 1.00 12.69 ? 109 TYR A C    1 
ATOM   1390 O O    . TYR A 1 109 ? 37.658 -10.412 -18.014 1.00 13.83 ? 109 TYR A O    1 
ATOM   1391 C CB   . TYR A 1 109 ? 37.019 -8.362  -16.045 1.00 12.96 ? 109 TYR A CB   1 
ATOM   1392 C CG   . TYR A 1 109 ? 36.481 -7.620  -14.841 1.00 13.39 ? 109 TYR A CG   1 
ATOM   1393 C CD1  . TYR A 1 109 ? 35.899 -6.362  -14.951 1.00 12.73 ? 109 TYR A CD1  1 
ATOM   1394 C CD2  . TYR A 1 109 ? 36.572 -8.184  -13.585 1.00 13.39 ? 109 TYR A CD2  1 
ATOM   1395 C CE1  . TYR A 1 109 ? 35.407 -5.685  -13.839 1.00 12.55 ? 109 TYR A CE1  1 
ATOM   1396 C CE2  . TYR A 1 109 ? 36.109 -7.509  -12.467 1.00 11.75 ? 109 TYR A CE2  1 
ATOM   1397 C CZ   . TYR A 1 109 ? 35.518 -6.287  -12.612 1.00 11.04 ? 109 TYR A CZ   1 
ATOM   1398 O OH   . TYR A 1 109 ? 35.032 -5.655  -11.489 1.00 11.95 ? 109 TYR A OH   1 
ATOM   1399 H H    . TYR A 1 109 ? 36.134 -10.729 -15.567 1.00 14.91 ? 109 TYR A H    1 
ATOM   1400 H HA   . TYR A 1 109 ? 35.230 -8.622  -17.017 1.00 14.67 ? 109 TYR A HA   1 
ATOM   1401 H HB2  . TYR A 1 109 ? 37.722 -8.953  -15.734 1.00 15.55 ? 109 TYR A HB2  1 
ATOM   1402 H HB3  . TYR A 1 109 ? 37.385 -7.703  -16.655 1.00 15.55 ? 109 TYR A HB3  1 
ATOM   1403 H HD1  . TYR A 1 109 ? 35.837 -5.963  -15.788 1.00 15.27 ? 109 TYR A HD1  1 
ATOM   1404 H HD2  . TYR A 1 109 ? 36.948 -9.029  -13.487 1.00 16.06 ? 109 TYR A HD2  1 
ATOM   1405 H HE1  . TYR A 1 109 ? 35.013 -4.847  -13.925 1.00 15.06 ? 109 TYR A HE1  1 
ATOM   1406 H HE2  . TYR A 1 109 ? 36.200 -7.886  -11.622 1.00 14.10 ? 109 TYR A HE2  1 
ATOM   1407 H HH   . TYR A 1 109 ? 35.123 -6.152  -10.818 1.00 14.34 ? 109 TYR A HH   1 
ATOM   1408 N N    . LYS A 1 110 ? 35.969 -9.564  -19.216 1.00 13.20 ? 110 LYS A N    1 
ATOM   1409 C CA   . LYS A 1 110 ? 36.507 -10.155 -20.434 1.00 14.39 ? 110 LYS A CA   1 
ATOM   1410 C C    . LYS A 1 110 ? 37.913 -9.646  -20.729 1.00 14.40 ? 110 LYS A C    1 
ATOM   1411 O O    . LYS A 1 110 ? 38.769 -10.411 -21.198 1.00 14.52 ? 110 LYS A O    1 
ATOM   1412 C CB   . LYS A 1 110 ? 35.566 -9.934  -21.613 1.00 18.44 ? 110 LYS A CB   1 
ATOM   1413 C CG   . LYS A 1 110 ? 35.333 -8.512  -22.054 1.00 20.35 ? 110 LYS A CG   1 
ATOM   1414 C CD   . LYS A 1 110 ? 34.486 -8.418  -23.333 1.00 21.95 ? 110 LYS A CD   1 
ATOM   1415 C CE   . LYS A 1 110 ? 34.313 -6.957  -23.729 1.00 30.37 ? 110 LYS A CE   1 
ATOM   1416 N NZ   . LYS A 1 110 ? 35.471 -6.424  -24.495 1.00 37.30 ? 110 LYS A NZ   1 
ATOM   1417 H H    . LYS A 1 110 ? 35.252 -9.100  -19.313 1.00 15.85 ? 110 LYS A H    1 
ATOM   1418 H HA   . LYS A 1 110 ? 36.569 -11.115 -20.306 1.00 17.27 ? 110 LYS A HA   1 
ATOM   1419 H HB2  . LYS A 1 110 ? 35.928 -10.409 -22.377 1.00 22.13 ? 110 LYS A HB2  1 
ATOM   1420 H HB3  . LYS A 1 110 ? 34.700 -10.299 -21.375 1.00 22.13 ? 110 LYS A HB3  1 
ATOM   1421 H HG2  . LYS A 1 110 ? 34.866 -8.035  -21.350 1.00 24.42 ? 110 LYS A HG2  1 
ATOM   1422 H HG3  . LYS A 1 110 ? 36.189 -8.091  -22.229 1.00 24.42 ? 110 LYS A HG3  1 
ATOM   1423 H HD2  . LYS A 1 110 ? 34.932 -8.887  -24.056 1.00 26.34 ? 110 LYS A HD2  1 
ATOM   1424 H HD3  . LYS A 1 110 ? 33.611 -8.805  -23.176 1.00 26.34 ? 110 LYS A HD3  1 
ATOM   1425 H HE2  . LYS A 1 110 ? 33.522 -6.872  -24.285 1.00 36.45 ? 110 LYS A HE2  1 
ATOM   1426 H HE3  . LYS A 1 110 ? 34.213 -6.422  -22.926 1.00 36.45 ? 110 LYS A HE3  1 
ATOM   1427 H HZ1  . LYS A 1 110 ? 35.326 -5.573  -24.713 1.00 44.76 ? 110 LYS A HZ1  1 
ATOM   1428 H HZ2  . LYS A 1 110 ? 36.210 -6.473  -24.002 1.00 44.76 ? 110 LYS A HZ2  1 
ATOM   1429 H HZ3  . LYS A 1 110 ? 35.588 -6.897  -25.239 1.00 44.76 ? 110 LYS A HZ3  1 
ATOM   1430 N N    . ASN A 1 111 ? 38.176 -8.371  -20.476 1.00 13.17 ? 111 ASN A N    1 
ATOM   1431 C CA   . ASN A 1 111 ? 39.478 -7.837  -20.834 1.00 13.61 ? 111 ASN A CA   1 
ATOM   1432 C C    . ASN A 1 111 ? 40.541 -8.345  -19.885 1.00 12.28 ? 111 ASN A C    1 
ATOM   1433 O O    . ASN A 1 111 ? 41.685 -8.592  -20.291 1.00 13.20 ? 111 ASN A O    1 
ATOM   1434 C CB   . ASN A 1 111 ? 39.430 -6.308  -20.907 1.00 15.38 ? 111 ASN A CB   1 
ATOM   1435 C CG   . ASN A 1 111 ? 38.477 -5.826  -21.983 1.00 17.64 ? 111 ASN A CG   1 
ATOM   1436 O OD1  . ASN A 1 111 ? 38.211 -6.532  -22.952 1.00 19.04 ? 111 ASN A OD1  1 
ATOM   1437 N ND2  . ASN A 1 111 ? 37.984 -4.612  -21.829 1.00 20.99 ? 111 ASN A ND2  1 
ATOM   1438 H H    . ASN A 1 111 ? 37.635 -7.812  -20.109 1.00 15.80 ? 111 ASN A H    1 
ATOM   1439 H HA   . ASN A 1 111 ? 39.726 -8.132  -21.725 1.00 16.33 ? 111 ASN A HA   1 
ATOM   1440 H HB2  . ASN A 1 111 ? 39.129 -5.957  -20.055 1.00 18.46 ? 111 ASN A HB2  1 
ATOM   1441 H HB3  . ASN A 1 111 ? 40.316 -5.969  -21.111 1.00 18.46 ? 111 ASN A HB3  1 
ATOM   1442 H HD21 . ASN A 1 111 ? 37.439 -4.292  -22.412 1.00 25.19 ? 111 ASN A HD21 1 
ATOM   1443 H HD22 . ASN A 1 111 ? 38.207 -4.141  -21.145 1.00 25.19 ? 111 ASN A HD22 1 
ATOM   1444 N N    . ASP A 1 112 ? 40.179 -8.546  -18.614 1.00 12.70 ? 112 ASP A N    1 
ATOM   1445 C CA   . ASP A 1 112 ? 41.143 -9.073  -17.658 1.00 11.81 ? 112 ASP A CA   1 
ATOM   1446 C C    . ASP A 1 112 ? 41.476 -10.520 -17.981 1.00 12.35 ? 112 ASP A C    1 
ATOM   1447 O O    . ASP A 1 112 ? 42.640 -10.922 -17.921 1.00 12.89 ? 112 ASP A O    1 
ATOM   1448 C CB   . ASP A 1 112 ? 40.589 -9.018  -16.230 1.00 12.29 ? 112 ASP A CB   1 
ATOM   1449 C CG   . ASP A 1 112 ? 40.346 -7.614  -15.697 1.00 12.91 ? 112 ASP A CG   1 
ATOM   1450 O OD1  . ASP A 1 112 ? 40.506 -6.615  -16.408 1.00 13.21 ? 112 ASP A OD1  1 
ATOM   1451 O OD2  . ASP A 1 112 ? 39.951 -7.501  -14.518 1.00 12.12 ? 112 ASP A OD2  1 
ATOM   1452 H H    . ASP A 1 112 ? 39.398 -8.388  -18.291 1.00 15.24 ? 112 ASP A H    1 
ATOM   1453 H HA   . ASP A 1 112 ? 41.940 -8.522  -17.706 1.00 14.17 ? 112 ASP A HA   1 
ATOM   1454 H HB2  . ASP A 1 112 ? 39.742 -9.490  -16.209 1.00 14.75 ? 112 ASP A HB2  1 
ATOM   1455 H HB3  . ASP A 1 112 ? 41.224 -9.450  -15.636 1.00 14.75 ? 112 ASP A HB3  1 
ATOM   1456 N N    . ASP A 1 113 ? 40.463 -11.303 -18.342 1.00 13.22 ? 113 ASP A N    1 
ATOM   1457 C CA   . ASP A 1 113 ? 40.699 -12.698 -18.685 1.00 14.21 ? 113 ASP A CA   1 
ATOM   1458 C C    . ASP A 1 113 ? 41.662 -12.786 -19.865 1.00 14.08 ? 113 ASP A C    1 
ATOM   1459 O O    . ASP A 1 113 ? 42.582 -13.609 -19.883 1.00 14.91 ? 113 ASP A O    1 
ATOM   1460 C CB   . ASP A 1 113 ? 39.391 -13.419 -19.024 1.00 15.53 ? 113 ASP A CB   1 
ATOM   1461 C CG   . ASP A 1 113 ? 38.536 -13.699 -17.805 1.00 15.69 ? 113 ASP A CG   1 
ATOM   1462 O OD1  . ASP A 1 113 ? 38.980 -13.461 -16.678 1.00 16.32 ? 113 ASP A OD1  1 
ATOM   1463 O OD2  . ASP A 1 113 ? 37.398 -14.170 -18.009 1.00 19.95 ? 113 ASP A OD2  1 
ATOM   1464 H H    . ASP A 1 113 ? 39.642 -11.055 -18.395 1.00 15.87 ? 113 ASP A H    1 
ATOM   1465 H HA   . ASP A 1 113 ? 41.080 -13.146 -17.913 1.00 17.05 ? 113 ASP A HA   1 
ATOM   1466 H HB2  . ASP A 1 113 ? 38.875 -12.866 -19.631 1.00 18.64 ? 113 ASP A HB2  1 
ATOM   1467 H HB3  . ASP A 1 113 ? 39.599 -14.268 -19.444 1.00 18.64 ? 113 ASP A HB3  1 
ATOM   1468 N N    . GLU A 1 114 ? 41.462 -11.942 -20.875 1.00 14.11 ? 114 GLU A N    1 
ATOM   1469 C CA   . GLU A 1 114 ? 42.350 -11.952 -22.024 1.00 13.46 ? 114 GLU A CA   1 
ATOM   1470 C C    . GLU A 1 114 ? 43.764 -11.513 -21.640 1.00 13.39 ? 114 GLU A C    1 
ATOM   1471 O O    . GLU A 1 114 ? 44.748 -12.139 -22.061 1.00 14.82 ? 114 GLU A O    1 
ATOM   1472 C CB   . GLU A 1 114 ? 41.749 -11.047 -23.091 1.00 17.00 ? 114 GLU A CB   1 
ATOM   1473 C CG   . GLU A 1 114 ? 42.650 -10.781 -24.262 1.00 23.82 ? 114 GLU A CG   1 
ATOM   1474 C CD   . GLU A 1 114 ? 42.793 -11.972 -25.204 1.00 36.27 ? 114 GLU A CD   1 
ATOM   1475 O OE1  . GLU A 1 114 ? 43.724 -11.940 -26.044 1.00 31.96 ? 114 GLU A OE1  1 
ATOM   1476 O OE2  . GLU A 1 114 ? 41.979 -12.922 -25.130 1.00 34.85 ? 114 GLU A OE2  1 
ATOM   1477 H H    . GLU A 1 114 ? 40.827 -11.363 -20.916 1.00 16.93 ? 114 GLU A H    1 
ATOM   1478 H HA   . GLU A 1 114 ? 42.430 -12.850 -22.382 1.00 16.15 ? 114 GLU A HA   1 
ATOM   1479 H HB2  . GLU A 1 114 ? 40.941 -11.463 -23.431 1.00 20.40 ? 114 GLU A HB2  1 
ATOM   1480 H HB3  . GLU A 1 114 ? 41.535 -10.191 -22.686 1.00 20.40 ? 114 GLU A HB3  1 
ATOM   1481 H HG2  . GLU A 1 114 ? 42.288 -10.041 -24.774 1.00 28.58 ? 114 GLU A HG2  1 
ATOM   1482 H HG3  . GLU A 1 114 ? 43.533 -10.556 -23.932 1.00 28.58 ? 114 GLU A HG3  1 
ATOM   1483 N N    . PHE A 1 115 ? 43.881 -10.444 -20.864 1.00 13.47 ? 115 PHE A N    1 
ATOM   1484 C CA   . PHE A 1 115 ? 45.177 -9.950  -20.415 1.00 12.66 ? 115 PHE A CA   1 
ATOM   1485 C C    . PHE A 1 115 ? 45.957 -10.999 -19.626 1.00 13.58 ? 115 PHE A C    1 
ATOM   1486 O O    . PHE A 1 115 ? 47.151 -11.230 -19.867 1.00 13.44 ? 115 PHE A O    1 
ATOM   1487 C CB   . PHE A 1 115 ? 44.962 -8.687  -19.574 1.00 13.93 ? 115 PHE A CB   1 
ATOM   1488 C CG   . PHE A 1 115 ? 46.216 -8.123  -18.956 1.00 11.63 ? 115 PHE A CG   1 
ATOM   1489 C CD1  . PHE A 1 115 ? 47.231 -7.607  -19.749 1.00 13.93 ? 115 PHE A CD1  1 
ATOM   1490 C CD2  . PHE A 1 115 ? 46.366 -8.086  -17.589 1.00 13.50 ? 115 PHE A CD2  1 
ATOM   1491 C CE1  . PHE A 1 115 ? 48.365 -7.076  -19.155 1.00 14.28 ? 115 PHE A CE1  1 
ATOM   1492 C CE2  . PHE A 1 115 ? 47.496 -7.545  -17.018 1.00 13.66 ? 115 PHE A CE2  1 
ATOM   1493 C CZ   . PHE A 1 115 ? 48.496 -7.047  -17.808 1.00 13.80 ? 115 PHE A CZ   1 
ATOM   1494 H H    . PHE A 1 115 ? 43.217 -9.978  -20.579 1.00 16.16 ? 115 PHE A H    1 
ATOM   1495 H HA   . PHE A 1 115 ? 45.712 -9.729  -21.193 1.00 15.19 ? 115 PHE A HA   1 
ATOM   1496 H HB2  . PHE A 1 115 ? 44.581 -8.000  -20.142 1.00 16.72 ? 115 PHE A HB2  1 
ATOM   1497 H HB3  . PHE A 1 115 ? 44.350 -8.898  -18.852 1.00 16.72 ? 115 PHE A HB3  1 
ATOM   1498 H HD1  . PHE A 1 115 ? 47.151 -7.617  -20.675 1.00 16.71 ? 115 PHE A HD1  1 
ATOM   1499 H HD2  . PHE A 1 115 ? 45.696 -8.430  -17.043 1.00 16.20 ? 115 PHE A HD2  1 
ATOM   1500 H HE1  . PHE A 1 115 ? 49.045 -6.735  -19.689 1.00 17.13 ? 115 PHE A HE1  1 
ATOM   1501 H HE2  . PHE A 1 115 ? 47.580 -7.517  -16.093 1.00 16.39 ? 115 PHE A HE2  1 
ATOM   1502 H HZ   . PHE A 1 115 ? 49.263 -6.691  -17.421 1.00 16.55 ? 115 PHE A HZ   1 
ATOM   1503 N N    . ILE A 1 116 ? 45.296 -11.652 -18.670 1.00 12.28 ? 116 ILE A N    1 
ATOM   1504 C CA   . ILE A 1 116 ? 45.953 -12.667 -17.862 1.00 12.75 ? 116 ILE A CA   1 
ATOM   1505 C C    . ILE A 1 116 ? 46.325 -13.894 -18.684 1.00 13.87 ? 116 ILE A C    1 
ATOM   1506 O O    . ILE A 1 116 ? 47.395 -14.492 -18.478 1.00 15.37 ? 116 ILE A O    1 
ATOM   1507 C CB   . ILE A 1 116 ? 45.110 -12.999 -16.607 1.00 14.28 ? 116 ILE A CB   1 
ATOM   1508 C CG1  . ILE A 1 116 ? 44.915 -11.753 -15.727 1.00 13.37 ? 116 ILE A CG1  1 
ATOM   1509 C CG2  . ILE A 1 116 ? 45.697 -14.186 -15.858 1.00 15.25 ? 116 ILE A CG2  1 
ATOM   1510 C CD1  . ILE A 1 116 ? 46.178 -11.120 -15.255 1.00 15.40 ? 116 ILE A CD1  1 
ATOM   1511 H H    . ILE A 1 116 ? 44.469 -11.523 -18.472 1.00 14.74 ? 116 ILE A H    1 
ATOM   1512 H HA   . ILE A 1 116 ? 46.793 -12.298 -17.547 1.00 15.30 ? 116 ILE A HA   1 
ATOM   1513 H HB   . ILE A 1 116 ? 44.223 -13.269 -16.890 1.00 17.13 ? 116 ILE A HB   1 
ATOM   1514 H HG12 . ILE A 1 116 ? 44.429 -11.088 -16.239 1.00 16.05 ? 116 ILE A HG12 1 
ATOM   1515 H HG13 . ILE A 1 116 ? 44.405 -12.007 -14.943 1.00 16.05 ? 116 ILE A HG13 1 
ATOM   1516 H HG21 . ILE A 1 116 ? 45.252 -14.269 -15.000 1.00 18.30 ? 116 ILE A HG21 1 
ATOM   1517 H HG22 . ILE A 1 116 ? 45.559 -14.990 -16.382 1.00 18.30 ? 116 ILE A HG22 1 
ATOM   1518 H HG23 . ILE A 1 116 ? 46.646 -14.037 -15.724 1.00 18.30 ? 116 ILE A HG23 1 
ATOM   1519 H HD11 . ILE A 1 116 ? 45.969 -10.485 -14.552 1.00 18.48 ? 116 ILE A HD11 1 
ATOM   1520 H HD12 . ILE A 1 116 ? 46.768 -11.809 -14.914 1.00 18.48 ? 116 ILE A HD12 1 
ATOM   1521 H HD13 . ILE A 1 116 ? 46.599 -10.662 -15.999 1.00 18.48 ? 116 ILE A HD13 1 
ATOM   1522 N N    . SER A 1 117 ? 45.475 -14.287 -19.628 1.00 14.29 ? 117 SER A N    1 
ATOM   1523 C CA   . SER A 1 117 ? 45.794 -15.429 -20.488 1.00 15.57 ? 117 SER A CA   1 
ATOM   1524 C C    . SER A 1 117 ? 47.086 -15.198 -21.267 1.00 16.61 ? 117 SER A C    1 
ATOM   1525 O O    . SER A 1 117 ? 47.854 -16.136 -21.498 1.00 18.73 ? 117 SER A O    1 
ATOM   1526 C CB   . SER A 1 117 ? 44.614 -15.689 -21.413 1.00 18.48 ? 117 SER A CB   1 
ATOM   1527 O OG   . SER A 1 117 ? 44.649 -14.883 -22.578 1.00 30.78 ? 117 SER A OG   1 
ATOM   1528 H H    . SER A 1 117 ? 44.716 -13.918 -19.792 1.00 17.15 ? 117 SER A H    1 
ATOM   1529 H HA   . SER A 1 117 ? 45.935 -16.222 -19.948 1.00 18.69 ? 117 SER A HA   1 
ATOM   1530 H HB2  . SER A 1 117 ? 44.631 -16.621 -21.682 1.00 22.17 ? 117 SER A HB2  1 
ATOM   1531 H HB3  . SER A 1 117 ? 43.794 -15.498 -20.930 1.00 22.17 ? 117 SER A HB3  1 
ATOM   1532 H HG   . SER A 1 117 ? 44.671 -14.071 -22.364 1.00 36.94 ? 117 SER A HG   1 
ATOM   1533 N N    . LYS A 1 118 ? 47.338 -13.963 -21.692 1.00 15.08 ? 118 LYS A N    1 
ATOM   1534 C CA   . LYS A 1 118 ? 48.538 -13.643 -22.452 1.00 16.01 ? 118 LYS A CA   1 
ATOM   1535 C C    . LYS A 1 118 ? 49.731 -13.333 -21.569 1.00 14.39 ? 118 LYS A C    1 
ATOM   1536 O O    . LYS A 1 118 ? 50.866 -13.293 -22.056 1.00 16.41 ? 118 LYS A O    1 
ATOM   1537 C CB   . LYS A 1 118 ? 48.252 -12.465 -23.385 1.00 17.46 ? 118 LYS A CB   1 
ATOM   1538 C CG   . LYS A 1 118 ? 47.257 -12.840 -24.463 1.00 19.07 ? 118 LYS A CG   1 
ATOM   1539 C CD   . LYS A 1 118 ? 47.014 -11.731 -25.428 1.00 25.59 ? 118 LYS A CD   1 
ATOM   1540 C CE   . LYS A 1 118 ? 46.492 -10.525 -24.716 1.00 22.81 ? 118 LYS A CE   1 
ATOM   1541 N NZ   . LYS A 1 118 ? 45.610 -9.711  -25.615 1.00 24.56 ? 118 LYS A NZ   1 
ATOM   1542 H H    . LYS A 1 118 ? 46.824 -13.288 -21.551 1.00 18.10 ? 118 LYS A H    1 
ATOM   1543 H HA   . LYS A 1 118 ? 48.780 -14.405 -23.001 1.00 19.21 ? 118 LYS A HA   1 
ATOM   1544 H HB2  . LYS A 1 118 ? 47.883 -11.730 -22.870 1.00 20.95 ? 118 LYS A HB2  1 
ATOM   1545 H HB3  . LYS A 1 118 ? 49.077 -12.188 -23.814 1.00 20.95 ? 118 LYS A HB3  1 
ATOM   1546 H HG2  . LYS A 1 118 ? 47.598 -13.601 -24.959 1.00 22.89 ? 118 LYS A HG2  1 
ATOM   1547 H HG3  . LYS A 1 118 ? 46.410 -13.068 -24.047 1.00 22.89 ? 118 LYS A HG3  1 
ATOM   1548 H HD2  . LYS A 1 118 ? 47.845 -11.495 -25.868 1.00 30.71 ? 118 LYS A HD2  1 
ATOM   1549 H HD3  . LYS A 1 118 ? 46.357 -12.010 -26.085 1.00 30.71 ? 118 LYS A HD3  1 
ATOM   1550 H HE2  . LYS A 1 118 ? 45.973 -10.803 -23.946 1.00 27.37 ? 118 LYS A HE2  1 
ATOM   1551 H HE3  . LYS A 1 118 ? 47.236 -9.970  -24.432 1.00 27.37 ? 118 LYS A HE3  1 
ATOM   1552 H HZ1  . LYS A 1 118 ? 45.283 -9.013  -25.170 1.00 29.47 ? 118 LYS A HZ1  1 
ATOM   1553 H HZ2  . LYS A 1 118 ? 46.077 -9.415  -26.313 1.00 29.47 ? 118 LYS A HZ2  1 
ATOM   1554 H HZ3  . LYS A 1 118 ? 44.934 -10.209 -25.910 1.00 29.47 ? 118 LYS A HZ3  1 
ATOM   1555 N N    . ASN A 1 119 ? 49.510 -13.132 -20.276 1.00 13.43 ? 119 ASN A N    1 
ATOM   1556 C CA   . ASN A 1 119 ? 50.529 -12.644 -19.352 1.00 14.54 ? 119 ASN A CA   1 
ATOM   1557 C C    . ASN A 1 119 ? 50.375 -13.328 -17.995 1.00 14.44 ? 119 ASN A C    1 
ATOM   1558 O O    . ASN A 1 119 ? 50.019 -12.686 -17.004 1.00 13.93 ? 119 ASN A O    1 
ATOM   1559 C CB   . ASN A 1 119 ? 50.416 -11.132 -19.162 1.00 13.63 ? 119 ASN A CB   1 
ATOM   1560 C CG   . ASN A 1 119 ? 50.605 -10.364 -20.430 1.00 12.62 ? 119 ASN A CG   1 
ATOM   1561 O OD1  . ASN A 1 119 ? 51.720 -10.120 -20.880 1.00 13.97 ? 119 ASN A OD1  1 
ATOM   1562 N ND2  . ASN A 1 119 ? 49.495 -9.951  -21.014 1.00 13.09 ? 119 ASN A ND2  1 
ATOM   1563 H H    . ASN A 1 119 ? 48.752 -13.275 -19.897 1.00 16.12 ? 119 ASN A H    1 
ATOM   1564 H HA   . ASN A 1 119 ? 51.394 -12.872 -19.725 1.00 17.45 ? 119 ASN A HA   1 
ATOM   1565 H HB2  . ASN A 1 119 ? 49.534 -10.924 -18.816 1.00 16.35 ? 119 ASN A HB2  1 
ATOM   1566 H HB3  . ASN A 1 119 ? 51.095 -10.843 -18.533 1.00 16.35 ? 119 ASN A HB3  1 
ATOM   1567 H HD21 . ASN A 1 119 ? 49.535 -9.504  -21.747 1.00 15.70 ? 119 ASN A HD21 1 
ATOM   1568 H HD22 . ASN A 1 119 ? 48.731 -10.129 -20.661 1.00 15.70 ? 119 ASN A HD22 1 
ATOM   1569 N N    . PRO A 1 120 ? 50.685 -14.622 -17.909 1.00 14.27 ? 120 PRO A N    1 
ATOM   1570 C CA   . PRO A 1 120 ? 50.623 -15.300 -16.602 1.00 17.45 ? 120 PRO A CA   1 
ATOM   1571 C C    . PRO A 1 120 ? 51.501 -14.638 -15.566 1.00 15.45 ? 120 PRO A C    1 
ATOM   1572 O O    . PRO A 1 120 ? 51.191 -14.708 -14.362 1.00 16.09 ? 120 PRO A O    1 
ATOM   1573 C CB   . PRO A 1 120 ? 51.041 -16.744 -16.926 1.00 18.13 ? 120 PRO A CB   1 
ATOM   1574 C CG   . PRO A 1 120 ? 51.710 -16.665 -18.281 1.00 20.24 ? 120 PRO A CG   1 
ATOM   1575 C CD   . PRO A 1 120 ? 51.045 -15.532 -19.005 1.00 17.90 ? 120 PRO A CD   1 
ATOM   1576 H HA   . PRO A 1 120 ? 49.713 -15.330 -16.269 1.00 20.94 ? 120 PRO A HA   1 
ATOM   1577 H HB2  . PRO A 1 120 ? 51.659 -17.067 -16.252 1.00 21.76 ? 120 PRO A HB2  1 
ATOM   1578 H HB3  . PRO A 1 120 ? 50.257 -17.315 -16.959 1.00 21.76 ? 120 PRO A HB3  1 
ATOM   1579 H HG2  . PRO A 1 120 ? 52.657 -16.491 -18.168 1.00 24.29 ? 120 PRO A HG2  1 
ATOM   1580 H HG3  . PRO A 1 120 ? 51.581 -17.499 -18.759 1.00 24.29 ? 120 PRO A HG3  1 
ATOM   1581 H HD2  . PRO A 1 120 ? 51.659 -15.106 -19.624 1.00 21.48 ? 120 PRO A HD2  1 
ATOM   1582 H HD3  . PRO A 1 120 ? 50.255 -15.836 -19.478 1.00 21.48 ? 120 PRO A HD3  1 
ATOM   1583 N N    . SER A 1 121 ? 52.572 -13.946 -15.961 1.00 16.17 ? 121 SER A N    1 
ATOM   1584 C CA   . SER A 1 121 ? 53.436 -13.248 -15.028 1.00 16.92 ? 121 SER A CA   1 
ATOM   1585 C C    . SER A 1 121 ? 52.788 -12.012 -14.404 1.00 16.70 ? 121 SER A C    1 
ATOM   1586 O O    . SER A 1 121 ? 53.383 -11.395 -13.528 1.00 18.85 ? 121 SER A O    1 
ATOM   1587 C CB   . SER A 1 121 ? 54.740 -12.841 -15.723 1.00 19.39 ? 121 SER A CB   1 
ATOM   1588 O OG   . SER A 1 121 ? 54.503 -11.844 -16.710 1.00 23.06 ? 121 SER A OG   1 
ATOM   1589 H H    . SER A 1 121 ? 52.820 -13.867 -16.781 1.00 19.40 ? 121 SER A H    1 
ATOM   1590 H HA   . SER A 1 121 ? 53.650 -13.860 -14.306 1.00 20.30 ? 121 SER A HA   1 
ATOM   1591 H HB2  . SER A 1 121 ? 55.353 -12.488 -15.060 1.00 23.27 ? 121 SER A HB2  1 
ATOM   1592 H HB3  . SER A 1 121 ? 55.126 -13.621 -16.150 1.00 23.27 ? 121 SER A HB3  1 
ATOM   1593 H HG   . SER A 1 121 ? 55.227 -11.626 -17.077 1.00 27.67 ? 121 SER A HG   1 
ATOM   1594 N N    . ALA A 1 122 ? 51.597 -11.618 -14.850 1.00 12.93 ? 122 ALA A N    1 
ATOM   1595 C CA   . ALA A 1 122 ? 50.925 -10.463 -14.289 1.00 12.47 ? 122 ALA A CA   1 
ATOM   1596 C C    . ALA A 1 122 ? 50.338 -10.731 -12.909 1.00 13.11 ? 122 ALA A C    1 
ATOM   1597 O O    . ALA A 1 122 ? 49.930 -9.781  -12.237 1.00 14.64 ? 122 ALA A O    1 
ATOM   1598 C CB   . ALA A 1 122 ? 49.820 -9.995  -15.238 1.00 14.23 ? 122 ALA A CB   1 
ATOM   1599 H H    . ALA A 1 122 ? 51.159 -12.008 -15.479 1.00 15.51 ? 122 ALA A H    1 
ATOM   1600 H HA   . ALA A 1 122 ? 51.574 -9.748  -14.195 1.00 14.96 ? 122 ALA A HA   1 
ATOM   1601 H HB1  . ALA A 1 122 ? 49.350 -9.250  -14.832 1.00 17.07 ? 122 ALA A HB1  1 
ATOM   1602 H HB2  . ALA A 1 122 ? 50.221 -9.717  -16.076 1.00 17.07 ? 122 ALA A HB2  1 
ATOM   1603 H HB3  . ALA A 1 122 ? 49.205 -10.729 -15.393 1.00 17.07 ? 122 ALA A HB3  1 
ATOM   1604 N N    . LEU A 1 123 ? 50.238 -11.989 -12.510 1.00 12.37 ? 123 LEU A N    1 
ATOM   1605 C CA   . LEU A 1 123 ? 49.659 -12.388 -11.239 1.00 12.22 ? 123 LEU A CA   1 
ATOM   1606 C C    . LEU A 1 123 ? 50.736 -12.541 -10.169 1.00 13.00 ? 123 LEU A C    1 
ATOM   1607 O O    . LEU A 1 123 ? 51.887 -12.891 -10.457 1.00 14.36 ? 123 LEU A O    1 
ATOM   1608 C CB   . LEU A 1 123 ? 48.906 -13.692 -11.405 1.00 13.71 ? 123 LEU A CB   1 
ATOM   1609 C CG   . LEU A 1 123 ? 47.698 -13.612 -12.355 1.00 13.36 ? 123 LEU A CG   1 
ATOM   1610 C CD1  . LEU A 1 123 ? 47.024 -14.974 -12.410 1.00 16.15 ? 123 LEU A CD1  1 
ATOM   1611 C CD2  . LEU A 1 123 ? 46.699 -12.598 -11.960 1.00 13.75 ? 123 LEU A CD2  1 
ATOM   1612 H H    . LEU A 1 123 ? 50.509 -12.658 -12.978 1.00 14.85 ? 123 LEU A H    1 
ATOM   1613 H HA   . LEU A 1 123 ? 49.042 -11.704 -10.934 1.00 14.66 ? 123 LEU A HA   1 
ATOM   1614 H HB2  . LEU A 1 123 ? 49.516 -14.357 -11.761 1.00 16.46 ? 123 LEU A HB2  1 
ATOM   1615 H HB3  . LEU A 1 123 ? 48.578 -13.972 -10.536 1.00 16.46 ? 123 LEU A HB3  1 
ATOM   1616 H HG   . LEU A 1 123 ? 48.032 -13.346 -13.226 1.00 16.03 ? 123 LEU A HG   1 
ATOM   1617 H HD11 . LEU A 1 123 ? 46.252 -14.921 -12.996 1.00 19.38 ? 123 LEU A HD11 1 
ATOM   1618 H HD12 . LEU A 1 123 ? 47.655 -15.626 -12.753 1.00 19.38 ? 123 LEU A HD12 1 
ATOM   1619 H HD13 . LEU A 1 123 ? 46.743 -15.224 -11.516 1.00 19.38 ? 123 LEU A HD13 1 
ATOM   1620 H HD21 . LEU A 1 123 ? 45.916 -12.689 -12.526 1.00 16.50 ? 123 LEU A HD21 1 
ATOM   1621 H HD22 . LEU A 1 123 ? 46.454 -12.740 -11.032 1.00 16.50 ? 123 LEU A HD22 1 
ATOM   1622 H HD23 . LEU A 1 123 ? 47.085 -11.715 -12.068 1.00 16.50 ? 123 LEU A HD23 1 
ATOM   1623 N N    . LEU A 1 124 ? 50.349 -12.258 -8.931  1.00 12.03 ? 124 LEU A N    1 
ATOM   1624 C CA   . LEU A 1 124 ? 51.269 -12.281 -7.811  1.00 12.52 ? 124 LEU A CA   1 
ATOM   1625 C C    . LEU A 1 124 ? 51.662 -13.698 -7.430  1.00 11.57 ? 124 LEU A C    1 
ATOM   1626 O O    . LEU A 1 124 ? 50.817 -14.563 -7.221  1.00 12.55 ? 124 LEU A O    1 
ATOM   1627 C CB   . LEU A 1 124 ? 50.565 -11.607 -6.649  1.00 13.17 ? 124 LEU A CB   1 
ATOM   1628 C CG   . LEU A 1 124 ? 51.382 -11.381 -5.385  1.00 12.28 ? 124 LEU A CG   1 
ATOM   1629 C CD1  . LEU A 1 124 ? 52.543 -10.466 -5.637  1.00 14.52 ? 124 LEU A CD1  1 
ATOM   1630 C CD2  . LEU A 1 124 ? 50.484 -10.820 -4.293  1.00 13.23 ? 124 LEU A CD2  1 
ATOM   1631 H H    . LEU A 1 124 ? 49.545 -12.047 -8.712  1.00 14.44 ? 124 LEU A H    1 
ATOM   1632 H HA   . LEU A 1 124 ? 52.091 -11.821 -8.039  1.00 15.02 ? 124 LEU A HA   1 
ATOM   1633 H HB2  . LEU A 1 124 ? 50.260 -10.737 -6.949  1.00 15.80 ? 124 LEU A HB2  1 
ATOM   1634 H HB3  . LEU A 1 124 ? 49.806 -12.157 -6.400  1.00 15.80 ? 124 LEU A HB3  1 
ATOM   1635 H HG   . LEU A 1 124 ? 51.749 -12.229 -5.089  1.00 14.74 ? 124 LEU A HG   1 
ATOM   1636 H HD11 . LEU A 1 124 ? 53.025 -10.331 -4.806  1.00 17.42 ? 124 LEU A HD11 1 
ATOM   1637 H HD12 . LEU A 1 124 ? 53.128 -10.873 -6.296  1.00 17.42 ? 124 LEU A HD12 1 
ATOM   1638 H HD13 . LEU A 1 124 ? 52.210 -9.618  -5.969  1.00 17.42 ? 124 LEU A HD13 1 
ATOM   1639 H HD21 . LEU A 1 124 ? 51.010 -10.684 -3.490  1.00 15.88 ? 124 LEU A HD21 1 
ATOM   1640 H HD22 . LEU A 1 124 ? 50.112 -9.975  -4.592  1.00 15.88 ? 124 LEU A HD22 1 
ATOM   1641 H HD23 . LEU A 1 124 ? 49.769 -11.452 -4.117  1.00 15.88 ? 124 LEU A HD23 1 
ATOM   1642 N N    . LYS A 1 125 ? 52.957 -13.921 -7.300  1.00 12.95 ? 125 LYS A N    1 
ATOM   1643 C CA   . LYS A 1 125 ? 53.531 -15.207 -6.964  1.00 13.46 ? 125 LYS A CA   1 
ATOM   1644 C C    . LYS A 1 125 ? 54.536 -15.068 -5.837  1.00 16.02 ? 125 LYS A C    1 
ATOM   1645 O O    . LYS A 1 125 ? 55.163 -14.015 -5.665  1.00 16.66 ? 125 LYS A O    1 
ATOM   1646 C CB   . LYS A 1 125 ? 54.194 -15.806 -8.219  1.00 13.98 ? 125 LYS A CB   1 
ATOM   1647 C CG   . LYS A 1 125 ? 53.202 -16.017 -9.351  1.00 13.99 ? 125 LYS A CG   1 
ATOM   1648 C CD   . LYS A 1 125 ? 53.792 -16.738 -10.542 1.00 16.80 ? 125 LYS A CD   1 
ATOM   1649 C CE   . LYS A 1 125 ? 52.761 -16.720 -11.628 1.00 17.51 ? 125 LYS A CE   1 
ATOM   1650 N NZ   . LYS A 1 125 ? 53.216 -17.454 -12.843 1.00 23.98 ? 125 LYS A NZ   1 
ATOM   1651 H H    . LYS A 1 125 ? 53.554 -13.311 -7.409  1.00 15.54 ? 125 LYS A H    1 
ATOM   1652 H HA   . LYS A 1 125 ? 52.849 -15.814 -6.636  1.00 16.15 ? 125 LYS A HA   1 
ATOM   1653 H HB2  . LYS A 1 125 ? 54.886 -15.203 -8.532  1.00 16.78 ? 125 LYS A HB2  1 
ATOM   1654 H HB3  . LYS A 1 125 ? 54.581 -16.667 -7.993  1.00 16.78 ? 125 LYS A HB3  1 
ATOM   1655 H HG2  . LYS A 1 125 ? 52.459 -16.546 -9.022  1.00 16.79 ? 125 LYS A HG2  1 
ATOM   1656 H HG3  . LYS A 1 125 ? 52.885 -15.152 -9.655  1.00 16.79 ? 125 LYS A HG3  1 
ATOM   1657 H HD2  . LYS A 1 125 ? 54.592 -16.283 -10.850 1.00 20.16 ? 125 LYS A HD2  1 
ATOM   1658 H HD3  . LYS A 1 125 ? 54.001 -17.657 -10.311 1.00 20.16 ? 125 LYS A HD3  1 
ATOM   1659 H HE2  . LYS A 1 125 ? 51.950 -17.143 -11.305 1.00 21.02 ? 125 LYS A HE2  1 
ATOM   1660 H HE3  . LYS A 1 125 ? 52.578 -15.801 -11.880 1.00 21.02 ? 125 LYS A HE3  1 
ATOM   1661 H HZ1  . LYS A 1 125 ? 52.597 -17.401 -13.480 1.00 28.77 ? 125 LYS A HZ1  1 
ATOM   1662 H HZ2  . LYS A 1 125 ? 53.974 -17.100 -13.146 1.00 28.77 ? 125 LYS A HZ2  1 
ATOM   1663 H HZ3  . LYS A 1 125 ? 53.355 -18.311 -12.646 1.00 28.77 ? 125 LYS A HZ3  1 
ATOM   1664 N N    . ASN A 1 126 ? 54.684 -16.140 -5.076  1.00 14.78 ? 126 ASN A N    1 
ATOM   1665 C CA   . ASN A 1 126 ? 55.644 -16.197 -3.977  1.00 15.22 ? 126 ASN A CA   1 
ATOM   1666 C C    . ASN A 1 126 ? 57.052 -16.488 -4.489  1.00 16.45 ? 126 ASN A C    1 
ATOM   1667 O O    . ASN A 1 126 ? 57.330 -16.507 -5.693  1.00 16.02 ? 126 ASN A O    1 
ATOM   1668 C CB   . ASN A 1 126 ? 55.141 -17.166 -2.919  1.00 18.29 ? 126 ASN A CB   1 
ATOM   1669 C CG   . ASN A 1 126 ? 55.050 -18.594 -3.418  1.00 19.48 ? 126 ASN A CG   1 
ATOM   1670 O OD1  . ASN A 1 126 ? 55.727 -18.990 -4.360  1.00 19.92 ? 126 ASN A OD1  1 
ATOM   1671 N ND2  . ASN A 1 126 ? 54.233 -19.394 -2.742  1.00 25.48 ? 126 ASN A ND2  1 
ATOM   1672 H H    . ASN A 1 126 ? 54.232 -16.865 -5.175  1.00 17.74 ? 126 ASN A H    1 
ATOM   1673 H HA   . ASN A 1 126 ? 55.701 -15.318 -3.570  1.00 18.26 ? 126 ASN A HA   1 
ATOM   1674 H HB2  . ASN A 1 126 ? 55.750 -17.152 -2.164  1.00 21.95 ? 126 ASN A HB2  1 
ATOM   1675 H HB3  . ASN A 1 126 ? 54.255 -16.892 -2.635  1.00 21.95 ? 126 ASN A HB3  1 
ATOM   1676 H HD21 . ASN A 1 126 ? 54.141 -20.215 -2.981  1.00 30.57 ? 126 ASN A HD21 1 
ATOM   1677 H HD22 . ASN A 1 126 ? 53.796 -19.091 -2.066  1.00 30.57 ? 126 ASN A HD22 1 
ATOM   1678 N N    . GLN A 1 127 ? 57.996 -16.700 -3.559  1.00 18.23 ? 127 GLN A N    1 
ATOM   1679 C CA   . GLN A 1 127 ? 59.389 -16.886 -3.944  1.00 19.84 ? 127 GLN A CA   1 
ATOM   1680 C C    . GLN A 1 127 ? 59.625 -18.194 -4.667  1.00 18.19 ? 127 GLN A C    1 
ATOM   1681 O O    . GLN A 1 127 ? 60.658 -18.336 -5.342  1.00 19.11 ? 127 GLN A O    1 
ATOM   1682 C CB   . GLN A 1 127 ? 60.333 -16.791 -2.744  1.00 25.83 ? 127 GLN A CB   1 
ATOM   1683 C CG   . GLN A 1 127 ? 60.781 -15.389 -2.504  1.00 25.80 ? 127 GLN A CG   1 
ATOM   1684 C CD   . GLN A 1 127 ? 61.580 -15.186 -1.247  1.00 24.86 ? 127 GLN A CD   1 
ATOM   1685 O OE1  . GLN A 1 127 ? 61.999 -16.125 -0.557  1.00 30.30 ? 127 GLN A OE1  1 
ATOM   1686 N NE2  . GLN A 1 127 ? 61.769 -13.933 -0.919  1.00 21.55 ? 127 GLN A NE2  1 
ATOM   1687 H H    . GLN A 1 127 ? 57.851 -16.738 -2.712  1.00 21.88 ? 127 GLN A H    1 
ATOM   1688 H HA   . GLN A 1 127 ? 59.617 -16.157 -4.542  1.00 23.81 ? 127 GLN A HA   1 
ATOM   1689 H HB2  . GLN A 1 127 ? 59.872 -17.103 -1.950  1.00 31.00 ? 127 GLN A HB2  1 
ATOM   1690 H HB3  . GLN A 1 127 ? 61.117 -17.337 -2.909  1.00 31.00 ? 127 GLN A HB3  1 
ATOM   1691 H HG2  . GLN A 1 127 ? 61.337 -15.112 -3.249  1.00 30.97 ? 127 GLN A HG2  1 
ATOM   1692 H HG3  . GLN A 1 127 ? 59.997 -14.821 -2.445  1.00 30.97 ? 127 GLN A HG3  1 
ATOM   1693 H HE21 . GLN A 1 127 ? 61.445 -13.307 -1.410  1.00 25.86 ? 127 GLN A HE21 1 
ATOM   1694 H HE22 . GLN A 1 127 ? 62.217 -13.737 -0.211  1.00 25.86 ? 127 GLN A HE22 1 
ATOM   1695 N N    . ASN A 1 128 ? 58.721 -19.175 -4.530  1.00 19.44 ? 128 ASN A N    1 
ATOM   1696 C CA   . ASN A 1 128 ? 58.735 -20.391 -5.333  1.00 21.62 ? 128 ASN A CA   1 
ATOM   1697 C C    . ASN A 1 128 ? 58.096 -20.203 -6.691  1.00 21.10 ? 128 ASN A C    1 
ATOM   1698 O O    . ASN A 1 128 ? 58.001 -21.165 -7.475  1.00 22.54 ? 128 ASN A O    1 
ATOM   1699 C CB   . ASN A 1 128 ? 57.966 -21.501 -4.627  1.00 24.05 ? 128 ASN A CB   1 
ATOM   1700 C CG   . ASN A 1 128 ? 58.858 -22.472 -3.929  1.00 21.59 ? 128 ASN A CG   1 
ATOM   1701 O OD1  . ASN A 1 128 ? 60.060 -22.567 -4.202  1.00 22.61 ? 128 ASN A OD1  1 
ATOM   1702 N ND2  . ASN A 1 128 ? 58.283 -23.189 -2.989  1.00 32.63 ? 128 ASN A ND2  1 
ATOM   1703 H H    . ASN A 1 128 ? 58.076 -19.153 -3.962  1.00 23.32 ? 128 ASN A H    1 
ATOM   1704 H HA   . ASN A 1 128 ? 59.660 -20.660 -5.441  1.00 25.94 ? 128 ASN A HA   1 
ATOM   1705 H HB2  . ASN A 1 128 ? 57.378 -21.105 -3.964  1.00 28.86 ? 128 ASN A HB2  1 
ATOM   1706 H HB3  . ASN A 1 128 ? 57.445 -21.990 -5.282  1.00 28.86 ? 128 ASN A HB3  1 
ATOM   1707 H HD21 . ASN A 1 128 ? 58.742 -23.768 -2.548  1.00 39.16 ? 128 ASN A HD21 1 
ATOM   1708 H HD22 . ASN A 1 128 ? 57.448 -23.080 -2.815  1.00 39.16 ? 128 ASN A HD22 1 
ATOM   1709 N N    . ASN A 1 129 ? 57.679 -18.979 -6.989  1.00 18.02 ? 129 ASN A N    1 
ATOM   1710 C CA   . ASN A 1 129 ? 56.962 -18.637 -8.206  1.00 17.76 ? 129 ASN A CA   1 
ATOM   1711 C C    . ASN A 1 129 ? 55.651 -19.400 -8.351  1.00 17.19 ? 129 ASN A C    1 
ATOM   1712 O O    . ASN A 1 129 ? 55.224 -19.717 -9.460  1.00 20.61 ? 129 ASN A O    1 
ATOM   1713 C CB   . ASN A 1 129 ? 57.793 -18.766 -9.478  1.00 17.78 ? 129 ASN A CB   1 
ATOM   1714 C CG   . ASN A 1 129 ? 57.396 -17.744 -10.491 1.00 18.14 ? 129 ASN A CG   1 
ATOM   1715 O OD1  . ASN A 1 129 ? 57.249 -16.564 -10.144 1.00 17.85 ? 129 ASN A OD1  1 
ATOM   1716 N ND2  . ASN A 1 129 ? 57.176 -18.154 -11.739 1.00 19.28 ? 129 ASN A ND2  1 
ATOM   1717 H H    . ASN A 1 129 ? 57.807 -18.299 -6.478  1.00 21.62 ? 129 ASN A H    1 
ATOM   1718 H HA   . ASN A 1 129 ? 56.747 -17.696 -8.110  1.00 21.32 ? 129 ASN A HA   1 
ATOM   1719 H HB2  . ASN A 1 129 ? 58.730 -18.638 -9.264  1.00 21.34 ? 129 ASN A HB2  1 
ATOM   1720 H HB3  . ASN A 1 129 ? 57.658 -19.647 -9.862  1.00 21.34 ? 129 ASN A HB3  1 
ATOM   1721 H HD21 . ASN A 1 129 ? 56.946 -17.587 -12.344 1.00 23.14 ? 129 ASN A HD21 1 
ATOM   1722 H HD22 . ASN A 1 129 ? 57.264 -18.985 -11.941 1.00 23.14 ? 129 ASN A HD22 1 
ATOM   1723 N N    . GLU A 1 130 ? 54.984 -19.641 -7.246  1.00 18.87 ? 130 GLU A N    1 
ATOM   1724 C CA   . GLU A 1 130 ? 53.626 -20.172 -7.320  1.00 20.65 ? 130 GLU A CA   1 
ATOM   1725 C C    . GLU A 1 130 ? 52.618 -19.112 -6.884  1.00 16.92 ? 130 GLU A C    1 
ATOM   1726 O O    . GLU A 1 130 ? 52.898 -18.217 -6.084  1.00 15.75 ? 130 GLU A O    1 
ATOM   1727 C CB   . GLU A 1 130 ? 53.462 -21.492 -6.565  1.00 24.57 ? 130 GLU A CB   1 
ATOM   1728 C CG   . GLU A 1 130 ? 54.236 -22.715 -7.197  1.00 28.91 ? 130 GLU A CG   1 
ATOM   1729 C CD   . GLU A 1 130 ? 53.906 -23.122 -8.675  1.00 24.91 ? 130 GLU A CD   1 
ATOM   1730 O OE1  . GLU A 1 130 ? 52.760 -22.973 -9.158  1.00 34.15 ? 130 GLU A OE1  1 
ATOM   1731 O OE2  . GLU A 1 130 ? 54.830 -23.605 -9.357  1.00 22.89 ? 130 GLU A OE2  1 
ATOM   1732 H H    . GLU A 1 130 ? 55.284 -19.510 -6.451  1.00 22.64 ? 130 GLU A H    1 
ATOM   1733 H HA   . GLU A 1 130 ? 53.417 -20.387 -8.242  1.00 24.78 ? 130 GLU A HA   1 
ATOM   1734 H HB2  . GLU A 1 130 ? 53.792 -21.373 -5.661  1.00 29.49 ? 130 GLU A HB2  1 
ATOM   1735 H HB3  . GLU A 1 130 ? 52.519 -21.721 -6.546  1.00 29.49 ? 130 GLU A HB3  1 
ATOM   1736 H HG2  . GLU A 1 130 ? 55.183 -22.508 -7.173  1.00 34.70 ? 130 GLU A HG2  1 
ATOM   1737 H HG3  . GLU A 1 130 ? 54.052 -23.494 -6.649  1.00 34.70 ? 130 GLU A HG3  1 
ATOM   1738 N N    . LEU A 1 131 ? 51.442 -19.216 -7.461  1.00 14.57 ? 131 LEU A N    1 
ATOM   1739 C CA   . LEU A 1 131 ? 50.404 -18.250 -7.217  1.00 14.53 ? 131 LEU A CA   1 
ATOM   1740 C C    . LEU A 1 131 ? 49.962 -18.266 -5.766  1.00 14.09 ? 131 LEU A C    1 
ATOM   1741 O O    . LEU A 1 131 ? 49.929 -19.314 -5.115  1.00 16.55 ? 131 LEU A O    1 
ATOM   1742 C CB   . LEU A 1 131 ? 49.190 -18.561 -8.084  1.00 16.43 ? 131 LEU A CB   1 
ATOM   1743 C CG   . LEU A 1 131 ? 49.336 -18.260 -9.570  1.00 15.57 ? 131 LEU A CG   1 
ATOM   1744 C CD1  . LEU A 1 131 ? 48.165 -18.923 -10.304 1.00 22.58 ? 131 LEU A CD1  1 
ATOM   1745 C CD2  . LEU A 1 131 ? 49.359 -16.800 -9.827  1.00 16.04 ? 131 LEU A CD2  1 
ATOM   1746 H H    . LEU A 1 131 ? 51.219 -19.844 -8.004  1.00 17.48 ? 131 LEU A H    1 
ATOM   1747 H HA   . LEU A 1 131 ? 50.752 -17.370 -7.433  1.00 17.44 ? 131 LEU A HA   1 
ATOM   1748 H HB2  . LEU A 1 131 ? 48.993 -19.507 -8.001  1.00 19.71 ? 131 LEU A HB2  1 
ATOM   1749 H HB3  . LEU A 1 131 ? 48.443 -18.036 -7.757  1.00 19.71 ? 131 LEU A HB3  1 
ATOM   1750 H HG   . LEU A 1 131 ? 50.178 -18.611 -9.902  1.00 18.68 ? 131 LEU A HG   1 
ATOM   1751 H HD11 . LEU A 1 131 ? 48.267 -18.778 -11.258 1.00 27.09 ? 131 LEU A HD11 1 
ATOM   1752 H HD12 . LEU A 1 131 ? 48.170 -19.874 -10.112 1.00 27.09 ? 131 LEU A HD12 1 
ATOM   1753 H HD13 . LEU A 1 131 ? 47.335 -18.528 -9.996  1.00 27.09 ? 131 LEU A HD13 1 
ATOM   1754 H HD21 . LEU A 1 131 ? 49.383 -16.648 -10.785 1.00 19.24 ? 131 LEU A HD21 1 
ATOM   1755 H HD22 . LEU A 1 131 ? 48.560 -16.401 -9.449  1.00 19.24 ? 131 LEU A HD22 1 
ATOM   1756 H HD23 . LEU A 1 131 ? 50.148 -16.419 -9.411  1.00 19.24 ? 131 LEU A HD23 1 
ATOM   1757 N N    . VAL A 1 132 ? 49.634 -17.086 -5.270  1.00 14.67 ? 132 VAL A N    1 
ATOM   1758 C CA   . VAL A 1 132 ? 48.986 -16.925 -3.975  1.00 15.63 ? 132 VAL A CA   1 
ATOM   1759 C C    . VAL A 1 132 ? 47.554 -16.506 -4.245  1.00 16.34 ? 132 VAL A C    1 
ATOM   1760 O O    . VAL A 1 132 ? 47.246 -15.886 -5.261  1.00 14.87 ? 132 VAL A O    1 
ATOM   1761 C CB   . VAL A 1 132 ? 49.725 -15.963 -3.022  1.00 16.81 ? 132 VAL A CB   1 
ATOM   1762 C CG1  . VAL A 1 132 ? 51.102 -16.553 -2.665  1.00 18.92 ? 132 VAL A CG1  1 
ATOM   1763 C CG2  . VAL A 1 132 ? 49.851 -14.589 -3.623  1.00 16.57 ? 132 VAL A CG2  1 
ATOM   1764 H H    . VAL A 1 132 ? 49.779 -16.341 -5.675  1.00 17.60 ? 132 VAL A H    1 
ATOM   1765 H HA   . VAL A 1 132 ? 48.979 -17.775 -3.506  1.00 18.75 ? 132 VAL A HA   1 
ATOM   1766 H HB   . VAL A 1 132 ? 49.212 -15.862 -2.205  1.00 20.17 ? 132 VAL A HB   1 
ATOM   1767 H HG11 . VAL A 1 132 ? 51.550 -15.956 -2.046  1.00 22.70 ? 132 VAL A HG11 1 
ATOM   1768 H HG12 . VAL A 1 132 ? 50.976 -17.422 -2.254  1.00 22.70 ? 132 VAL A HG12 1 
ATOM   1769 H HG13 . VAL A 1 132 ? 51.626 -16.643 -3.476  1.00 22.70 ? 132 VAL A HG13 1 
ATOM   1770 H HG21 . VAL A 1 132 ? 50.309 -14.010 -2.994  1.00 19.88 ? 132 VAL A HG21 1 
ATOM   1771 H HG22 . VAL A 1 132 ? 50.360 -14.650 -4.446  1.00 19.88 ? 132 VAL A HG22 1 
ATOM   1772 H HG23 . VAL A 1 132 ? 48.964 -14.242 -3.807  1.00 19.88 ? 132 VAL A HG23 1 
ATOM   1773 N N    . TYR A 1 133 ? 46.661 -16.876 -3.334  1.00 16.50 ? 133 TYR A N    1 
ATOM   1774 C CA   . TYR A 1 133 ? 45.241 -16.757 -3.599  1.00 16.68 ? 133 TYR A CA   1 
ATOM   1775 C C    . TYR A 1 133 ? 44.461 -16.208 -2.416  1.00 18.96 ? 133 TYR A C    1 
ATOM   1776 O O    . TYR A 1 133 ? 44.924 -16.213 -1.278  1.00 19.75 ? 133 TYR A O    1 
ATOM   1777 C CB   . TYR A 1 133 ? 44.660 -18.136 -3.859  1.00 19.05 ? 133 TYR A CB   1 
ATOM   1778 C CG   . TYR A 1 133 ? 45.204 -18.890 -5.040  1.00 18.33 ? 133 TYR A CG   1 
ATOM   1779 C CD1  . TYR A 1 133 ? 44.844 -18.549 -6.335  1.00 19.13 ? 133 TYR A CD1  1 
ATOM   1780 C CD2  . TYR A 1 133 ? 46.065 -19.960 -4.858  1.00 21.72 ? 133 TYR A CD2  1 
ATOM   1781 C CE1  . TYR A 1 133 ? 45.305 -19.270 -7.415  1.00 18.90 ? 133 TYR A CE1  1 
ATOM   1782 C CE2  . TYR A 1 133 ? 46.538 -20.677 -5.931  1.00 22.27 ? 133 TYR A CE2  1 
ATOM   1783 C CZ   . TYR A 1 133 ? 46.161 -20.321 -7.200  1.00 19.44 ? 133 TYR A CZ   1 
ATOM   1784 O OH   . TYR A 1 133 ? 46.630 -21.061 -8.259  1.00 23.47 ? 133 TYR A OH   1 
ATOM   1785 H H    . TYR A 1 133 ? 46.855 -17.196 -2.560  1.00 19.80 ? 133 TYR A H    1 
ATOM   1786 H HA   . TYR A 1 133 ? 45.145 -16.139 -4.340  1.00 20.01 ? 133 TYR A HA   1 
ATOM   1787 H HB2  . TYR A 1 133 ? 44.824 -18.683 -3.075  1.00 22.86 ? 133 TYR A HB2  1 
ATOM   1788 H HB3  . TYR A 1 133 ? 43.706 -18.038 -4.002  1.00 22.86 ? 133 TYR A HB3  1 
ATOM   1789 H HD1  . TYR A 1 133 ? 44.282 -17.821 -6.477  1.00 22.95 ? 133 TYR A HD1  1 
ATOM   1790 H HD2  . TYR A 1 133 ? 46.327 -20.197 -3.997  1.00 26.07 ? 133 TYR A HD2  1 
ATOM   1791 H HE1  . TYR A 1 133 ? 45.040 -19.048 -8.279  1.00 22.68 ? 133 TYR A HE1  1 
ATOM   1792 H HE2  . TYR A 1 133 ? 47.110 -21.399 -5.797  1.00 26.73 ? 133 TYR A HE2  1 
ATOM   1793 H HH   . TYR A 1 133 ? 47.167 -21.646 -7.984  1.00 28.17 ? 133 TYR A HH   1 
ATOM   1794 N N    . MET A 1 134 ? 43.257 -15.739 -2.729  1.00 17.25 ? 134 MET A N    1 
ATOM   1795 C CA   . MET A 1 134 ? 42.235 -15.491 -1.720  1.00 18.65 ? 134 MET A CA   1 
ATOM   1796 C C    . MET A 1 134 ? 41.780 -16.800 -1.095  1.00 21.07 ? 134 MET A C    1 
ATOM   1797 O O    . MET A 1 134 ? 41.936 -17.874 -1.680  1.00 21.71 ? 134 MET A O    1 
ATOM   1798 C CB   . MET A 1 134 ? 41.045 -14.811 -2.394  1.00 21.45 ? 134 MET A CB   1 
ATOM   1799 C CG   . MET A 1 134 ? 41.250 -13.373 -2.787  1.00 19.51 ? 134 MET A CG   1 
ATOM   1800 S SD   . MET A 1 134 ? 41.433 -12.257 -1.389  1.00 21.06 ? 134 MET A SD   1 
ATOM   1801 C CE   . MET A 1 134 ? 39.774 -12.183 -0.793  1.00 27.04 ? 134 MET A CE   1 
ATOM   1802 H H    . MET A 1 134 ? 43.004 -15.555 -3.529  1.00 20.70 ? 134 MET A H    1 
ATOM   1803 H HA   . MET A 1 134 ? 42.585 -14.916 -1.021  1.00 22.38 ? 134 MET A HA   1 
ATOM   1804 H HB2  . MET A 1 134 ? 40.833 -15.303 -3.203  1.00 25.74 ? 134 MET A HB2  1 
ATOM   1805 H HB3  . MET A 1 134 ? 40.293 -14.838 -1.782  1.00 25.74 ? 134 MET A HB3  1 
ATOM   1806 H HG2  . MET A 1 134 ? 42.055 -13.308 -3.324  1.00 23.41 ? 134 MET A HG2  1 
ATOM   1807 H HG3  . MET A 1 134 ? 40.483 -13.078 -3.303  1.00 23.41 ? 134 MET A HG3  1 
ATOM   1808 H HE1  . MET A 1 134 ? 39.737 -11.577 -0.037  1.00 32.45 ? 134 MET A HE1  1 
ATOM   1809 H HE2  . MET A 1 134 ? 39.197 -11.862 -1.503  1.00 32.45 ? 134 MET A HE2  1 
ATOM   1810 H HE3  . MET A 1 134 ? 39.498 -13.072 -0.518  1.00 32.45 ? 134 MET A HE3  1 
ATOM   1811 N N    . PRO A 1 135 ? 41.225 -16.739 0.115   1.00 25.08 ? 135 PRO A N    1 
ATOM   1812 C CA   . PRO A 1 135 ? 40.812 -17.969 0.790   1.00 25.53 ? 135 PRO A CA   1 
ATOM   1813 C C    . PRO A 1 135 ? 39.766 -18.716 -0.019  1.00 25.77 ? 135 PRO A C    1 
ATOM   1814 O O    . PRO A 1 135 ? 38.987 -18.121 -0.770  1.00 31.72 ? 135 PRO A O    1 
ATOM   1815 C CB   . PRO A 1 135 ? 40.212 -17.467 2.110   1.00 29.71 ? 135 PRO A CB   1 
ATOM   1816 C CG   . PRO A 1 135 ? 40.784 -16.073 2.295   1.00 27.44 ? 135 PRO A CG   1 
ATOM   1817 C CD   . PRO A 1 135 ? 40.946 -15.528 0.907   1.00 25.91 ? 135 PRO A CD   1 
ATOM   1818 H HA   . PRO A 1 135 ? 41.578 -18.540 0.961   1.00 30.64 ? 135 PRO A HA   1 
ATOM   1819 H HB2  . PRO A 1 135 ? 39.245 -17.439 2.044   1.00 35.65 ? 135 PRO A HB2  1 
ATOM   1820 H HB3  . PRO A 1 135 ? 40.479 -18.051 2.838   1.00 35.65 ? 135 PRO A HB3  1 
ATOM   1821 H HG2  . PRO A 1 135 ? 40.168 -15.530 2.811   1.00 32.93 ? 135 PRO A HG2  1 
ATOM   1822 H HG3  . PRO A 1 135 ? 41.640 -16.126 2.749   1.00 32.93 ? 135 PRO A HG3  1 
ATOM   1823 H HD2  . PRO A 1 135 ? 40.132 -15.095 0.606   1.00 31.10 ? 135 PRO A HD2  1 
ATOM   1824 H HD3  . PRO A 1 135 ? 41.689 -14.905 0.862   1.00 31.10 ? 135 PRO A HD3  1 
ATOM   1825 N N    . ASN A 1 136 ? 39.733 -20.032 0.177   1.00 37.04 ? 136 ASN A N    1 
ATOM   1826 C CA   . ASN A 1 136 ? 38.636 -20.873 -0.305  1.00 46.03 ? 136 ASN A CA   1 
ATOM   1827 C C    . ASN A 1 136 ? 38.457 -20.771 -1.812  1.00 44.46 ? 136 ASN A C    1 
ATOM   1828 O O    . ASN A 1 136 ? 37.346 -20.617 -2.323  1.00 49.18 ? 136 ASN A O    1 
ATOM   1829 C CB   . ASN A 1 136 ? 37.320 -20.608 0.432   1.00 41.14 ? 136 ASN A CB   1 
ATOM   1830 C CG   . ASN A 1 136 ? 37.474 -20.659 1.933   1.00 45.65 ? 136 ASN A CG   1 
ATOM   1831 O OD1  . ASN A 1 136 ? 38.004 -21.631 2.475   1.00 52.42 ? 136 ASN A OD1  1 
ATOM   1832 N ND2  . ASN A 1 136 ? 37.000 -19.627 2.616   1.00 50.37 ? 136 ASN A ND2  1 
ATOM   1833 H H    . ASN A 1 136 ? 40.344 -20.471 0.593   1.00 44.44 ? 136 ASN A H    1 
ATOM   1834 H HA   . ASN A 1 136 ? 38.886 -21.790 -0.109  1.00 55.23 ? 136 ASN A HA   1 
ATOM   1835 H HB2  . ASN A 1 136 ? 36.995 -19.726 0.193   1.00 49.37 ? 136 ASN A HB2  1 
ATOM   1836 H HB3  . ASN A 1 136 ? 36.671 -21.281 0.173   1.00 49.37 ? 136 ASN A HB3  1 
ATOM   1837 H HD21 . ASN A 1 136 ? 37.066 -19.612 3.473   1.00 60.44 ? 136 ASN A HD21 1 
ATOM   1838 H HD22 . ASN A 1 136 ? 36.627 -18.972 2.201   1.00 60.44 ? 136 ASN A HD22 1 
ATOM   1839 N N    . GLY A 1 137 ? 39.564 -20.859 -2.529  1.00 33.50 ? 137 GLY A N    1 
ATOM   1840 C CA   . GLY A 1 137 ? 39.451 -20.974 -3.960  1.00 37.54 ? 137 GLY A CA   1 
ATOM   1841 C C    . GLY A 1 137 ? 40.747 -20.613 -4.647  1.00 36.12 ? 137 GLY A C    1 
ATOM   1842 O O    . GLY A 1 137 ? 41.823 -20.658 -4.060  1.00 34.29 ? 137 GLY A O    1 
ATOM   1843 H H    . GLY A 1 137 ? 40.365 -20.854 -2.216  1.00 40.19 ? 137 GLY A H    1 
ATOM   1844 H HA2  . GLY A 1 137 ? 39.219 -21.885 -4.197  1.00 45.04 ? 137 GLY A HA2  1 
ATOM   1845 H HA3  . GLY A 1 137 ? 38.755 -20.378 -4.281  1.00 45.04 ? 137 GLY A HA3  1 
ATOM   1846 N N    . SER A 1 138 ? 40.601 -20.274 -5.910  1.00 28.08 ? 138 SER A N    1 
ATOM   1847 C CA   . SER A 1 138 ? 41.719 -19.982 -6.770  1.00 26.16 ? 138 SER A CA   1 
ATOM   1848 C C    . SER A 1 138 ? 41.600 -18.587 -7.362  1.00 17.84 ? 138 SER A C    1 
ATOM   1849 O O    . SER A 1 138 ? 41.994 -18.382 -8.502  1.00 21.86 ? 138 SER A O    1 
ATOM   1850 C CB   . SER A 1 138 ? 41.765 -21.013 -7.892  1.00 37.01 ? 138 SER A CB   1 
ATOM   1851 O OG   . SER A 1 138 ? 40.445 -21.213 -8.366  1.00 39.58 ? 138 SER A OG   1 
ATOM   1852 H H    . SER A 1 138 ? 39.838 -20.205 -6.302  1.00 33.70 ? 138 SER A H    1 
ATOM   1853 H HA   . SER A 1 138 ? 42.542 -20.022 -6.259  1.00 31.40 ? 138 SER A HA   1 
ATOM   1854 H HB2  . SER A 1 138 ? 42.324 -20.685 -8.614  1.00 44.41 ? 138 SER A HB2  1 
ATOM   1855 H HB3  . SER A 1 138 ? 42.119 -21.849 -7.552  1.00 44.41 ? 138 SER A HB3  1 
ATOM   1856 H HG   . SER A 1 138 ? 40.444 -21.789 -8.977  1.00 47.50 ? 138 SER A HG   1 
ATOM   1857 N N    . THR A 1 139 ? 41.041 -17.622 -6.620  1.00 19.17 ? 139 THR A N    1 
ATOM   1858 C CA   . THR A 1 139 ? 41.051 -16.230 -7.078  1.00 17.49 ? 139 THR A CA   1 
ATOM   1859 C C    . THR A 1 139 ? 42.414 -15.616 -6.762  1.00 16.26 ? 139 THR A C    1 
ATOM   1860 O O    . THR A 1 139 ? 42.788 -15.527 -5.579  1.00 16.36 ? 139 THR A O    1 
ATOM   1861 C CB   . THR A 1 139 ? 39.956 -15.398 -6.422  1.00 20.52 ? 139 THR A CB   1 
ATOM   1862 O OG1  . THR A 1 139 ? 38.679 -16.026 -6.632  1.00 23.80 ? 139 THR A OG1  1 
ATOM   1863 C CG2  . THR A 1 139 ? 39.917 -14.002 -7.028  1.00 18.94 ? 139 THR A CG2  1 
ATOM   1864 H H    . THR A 1 139 ? 40.655 -17.746 -5.861  1.00 23.00 ? 139 THR A H    1 
ATOM   1865 H HA   . THR A 1 139 ? 40.890 -16.215 -8.034  1.00 20.99 ? 139 THR A HA   1 
ATOM   1866 H HB   . THR A 1 139 ? 40.135 -15.326 -5.472  1.00 24.63 ? 139 THR A HB   1 
ATOM   1867 H HG1  . THR A 1 139 ? 38.079 -15.600 -6.227  1.00 28.56 ? 139 THR A HG1  1 
ATOM   1868 H HG21 . THR A 1 139 ? 39.132 -13.526 -6.715  1.00 22.72 ? 139 THR A HG21 1 
ATOM   1869 H HG22 . THR A 1 139 ? 40.710 -13.506 -6.769  1.00 22.72 ? 139 THR A HG22 1 
ATOM   1870 H HG23 . THR A 1 139 ? 39.885 -14.060 -7.996  1.00 22.72 ? 139 THR A HG23 1 
ATOM   1871 N N    . PRO A 1 140 ? 43.178 -15.224 -7.756  1.00 13.94 ? 140 PRO A N    1 
ATOM   1872 C CA   . PRO A 1 140 ? 44.524 -14.692 -7.524  1.00 13.36 ? 140 PRO A CA   1 
ATOM   1873 C C    . PRO A 1 140 ? 44.541 -13.170 -7.468  1.00 11.85 ? 140 PRO A C    1 
ATOM   1874 O O    . PRO A 1 140 ? 43.480 -12.529 -7.492  1.00 13.20 ? 140 PRO A O    1 
ATOM   1875 C CB   . PRO A 1 140 ? 45.283 -15.203 -8.755  1.00 14.19 ? 140 PRO A CB   1 
ATOM   1876 C CG   . PRO A 1 140 ? 44.222 -15.107 -9.840  1.00 15.74 ? 140 PRO A CG   1 
ATOM   1877 C CD   . PRO A 1 140 ? 42.890 -15.365 -9.199  1.00 15.75 ? 140 PRO A CD   1 
ATOM   1878 H HA   . PRO A 1 140 ? 44.909 -15.051 -6.710  1.00 16.04 ? 140 PRO A HA   1 
ATOM   1879 H HB2  . PRO A 1 140 ? 46.045 -14.634 -8.948  1.00 17.03 ? 140 PRO A HB2  1 
ATOM   1880 H HB3  . PRO A 1 140 ? 45.577 -16.117 -8.621  1.00 17.03 ? 140 PRO A HB3  1 
ATOM   1881 H HG2  . PRO A 1 140 ? 44.243 -14.219 -10.229 1.00 18.89 ? 140 PRO A HG2  1 
ATOM   1882 H HG3  . PRO A 1 140 ? 44.402 -15.773 -10.522 1.00 18.89 ? 140 PRO A HG3  1 
ATOM   1883 H HD2  . PRO A 1 140 ? 42.235 -14.709 -9.486  1.00 18.91 ? 140 PRO A HD2  1 
ATOM   1884 H HD3  . PRO A 1 140 ? 42.575 -16.259 -9.403  1.00 18.91 ? 140 PRO A HD3  1 
ATOM   1885 N N    . PHE A 1 141 ? 45.740 -12.589 -7.453  1.00 11.96 ? 141 PHE A N    1 
ATOM   1886 C CA   . PHE A 1 141 ? 45.928 -11.158 -7.317  1.00 11.27 ? 141 PHE A CA   1 
ATOM   1887 C C    . PHE A 1 141 ? 46.779 -10.622 -8.457  1.00 11.55 ? 141 PHE A C    1 
ATOM   1888 O O    . PHE A 1 141 ? 47.700 -11.293 -8.949  1.00 12.22 ? 141 PHE A O    1 
ATOM   1889 C CB   . PHE A 1 141 ? 46.677 -10.800 -6.011  1.00 12.38 ? 141 PHE A CB   1 
ATOM   1890 C CG   . PHE A 1 141 ? 46.028 -11.297 -4.752  1.00 12.30 ? 141 PHE A CG   1 
ATOM   1891 C CD1  . PHE A 1 141 ? 45.064 -10.559 -4.093  1.00 13.35 ? 141 PHE A CD1  1 
ATOM   1892 C CD2  . PHE A 1 141 ? 46.396 -12.511 -4.210  1.00 13.06 ? 141 PHE A CD2  1 
ATOM   1893 C CE1  . PHE A 1 141 ? 44.489 -11.030 -2.907  1.00 13.61 ? 141 PHE A CE1  1 
ATOM   1894 C CE2  . PHE A 1 141 ? 45.825 -12.991 -3.045  1.00 14.93 ? 141 PHE A CE2  1 
ATOM   1895 C CZ   . PHE A 1 141 ? 44.882 -12.235 -2.385  1.00 14.11 ? 141 PHE A CZ   1 
ATOM   1896 H H    . PHE A 1 141 ? 46.479 -13.023 -7.523  1.00 14.35 ? 141 PHE A H    1 
ATOM   1897 H HA   . PHE A 1 141 ? 45.050 -10.746 -7.328  1.00 13.52 ? 141 PHE A HA   1 
ATOM   1898 H HB2  . PHE A 1 141 ? 47.566 -11.184 -6.051  1.00 14.86 ? 141 PHE A HB2  1 
ATOM   1899 H HB3  . PHE A 1 141 ? 46.736 -9.834  -5.946  1.00 14.86 ? 141 PHE A HB3  1 
ATOM   1900 H HD1  . PHE A 1 141 ? 44.794 -9.740  -4.442  1.00 16.02 ? 141 PHE A HD1  1 
ATOM   1901 H HD2  . PHE A 1 141 ? 47.044 -13.020 -4.639  1.00 15.68 ? 141 PHE A HD2  1 
ATOM   1902 H HE1  . PHE A 1 141 ? 43.839 -10.525 -2.473  1.00 16.33 ? 141 PHE A HE1  1 
ATOM   1903 H HE2  . PHE A 1 141 ? 46.078 -13.820 -2.709  1.00 17.91 ? 141 PHE A HE2  1 
ATOM   1904 H HZ   . PHE A 1 141 ? 44.513 -12.540 -1.588  1.00 16.93 ? 141 PHE A HZ   1 
ATOM   1905 N N    . PHE A 1 142 ? 46.480 -9.409  -8.901  1.00 11.84 ? 142 PHE A N    1 
ATOM   1906 C CA   . PHE A 1 142 ? 47.381 -8.703  -9.798  1.00 11.88 ? 142 PHE A CA   1 
ATOM   1907 C C    . PHE A 1 142 ? 48.673 -8.348  -9.077  1.00 12.40 ? 142 PHE A C    1 
ATOM   1908 O O    . PHE A 1 142 ? 48.638 -7.836  -7.965  1.00 14.15 ? 142 PHE A O    1 
ATOM   1909 C CB   . PHE A 1 142 ? 46.746 -7.386  -10.254 1.00 11.60 ? 142 PHE A CB   1 
ATOM   1910 C CG   . PHE A 1 142 ? 45.437 -7.522  -10.982 1.00 12.52 ? 142 PHE A CG   1 
ATOM   1911 C CD1  . PHE A 1 142 ? 45.370 -8.174  -12.176 1.00 14.70 ? 142 PHE A CD1  1 
ATOM   1912 C CD2  . PHE A 1 142 ? 44.294 -6.938  -10.473 1.00 14.20 ? 142 PHE A CD2  1 
ATOM   1913 C CE1  . PHE A 1 142 ? 44.163 -8.264  -12.856 1.00 16.26 ? 142 PHE A CE1  1 
ATOM   1914 C CE2  . PHE A 1 142 ? 43.097 -7.023  -11.142 1.00 15.69 ? 142 PHE A CE2  1 
ATOM   1915 C CZ   . PHE A 1 142 ? 43.037 -7.681  -12.318 1.00 16.69 ? 142 PHE A CZ   1 
ATOM   1916 H H    . PHE A 1 142 ? 45.766 -8.974  -8.698  1.00 14.21 ? 142 PHE A H    1 
ATOM   1917 H HA   . PHE A 1 142 ? 47.564 -9.271  -10.563 1.00 14.26 ? 142 PHE A HA   1 
ATOM   1918 H HB2  . PHE A 1 142 ? 46.586 -6.836  -9.472  1.00 13.92 ? 142 PHE A HB2  1 
ATOM   1919 H HB3  . PHE A 1 142 ? 47.365 -6.939  -10.853 1.00 13.92 ? 142 PHE A HB3  1 
ATOM   1920 H HD1  . PHE A 1 142 ? 46.135 -8.561  -12.536 1.00 17.64 ? 142 PHE A HD1  1 
ATOM   1921 H HD2  . PHE A 1 142 ? 44.335 -6.479  -9.665  1.00 17.03 ? 142 PHE A HD2  1 
ATOM   1922 H HE1  . PHE A 1 142 ? 44.115 -8.713  -13.669 1.00 19.51 ? 142 PHE A HE1  1 
ATOM   1923 H HE2  . PHE A 1 142 ? 42.333 -6.630  -10.787 1.00 18.83 ? 142 PHE A HE2  1 
ATOM   1924 H HZ   . PHE A 1 142 ? 42.226 -7.742  -12.770 1.00 20.02 ? 142 PHE A HZ   1 
ATOM   1925 N N    . ASP A 1 143 ? 49.808 -8.526  -9.726  1.00 11.20 ? 143 ASP A N    1 
ATOM   1926 C CA   . ASP A 1 143 ? 51.084 -8.034  -9.200  1.00 10.92 ? 143 ASP A CA   1 
ATOM   1927 C C    . ASP A 1 143 ? 51.259 -6.604  -9.651  1.00 11.23 ? 143 ASP A C    1 
ATOM   1928 O O    . ASP A 1 143 ? 51.841 -6.309  -10.691 1.00 11.46 ? 143 ASP A O    1 
ATOM   1929 C CB   . ASP A 1 143 ? 52.284 -8.892  -9.575  1.00 12.45 ? 143 ASP A CB   1 
ATOM   1930 C CG   . ASP A 1 143 ? 53.535 -8.434  -8.882  1.00 12.55 ? 143 ASP A CG   1 
ATOM   1931 O OD1  . ASP A 1 143 ? 53.505 -7.342  -8.272  1.00 12.14 ? 143 ASP A OD1  1 
ATOM   1932 O OD2  . ASP A 1 143 ? 54.547 -9.163  -8.921  1.00 14.63 ? 143 ASP A OD2  1 
ATOM   1933 H H    . ASP A 1 143 ? 49.874 -8.931  -10.481 1.00 13.44 ? 143 ASP A H    1 
ATOM   1934 H HA   . ASP A 1 143 ? 51.021 -8.068  -8.232  1.00 13.10 ? 143 ASP A HA   1 
ATOM   1935 H HB2  . ASP A 1 143 ? 52.112 -9.811  -9.318  1.00 14.94 ? 143 ASP A HB2  1 
ATOM   1936 H HB3  . ASP A 1 143 ? 52.429 -8.836  -10.533 1.00 14.94 ? 143 ASP A HB3  1 
ATOM   1937 N N    . ILE A 1 144 ? 50.749 -5.687  -8.851  1.00 11.49 ? 144 ILE A N    1 
ATOM   1938 C CA   . ILE A 1 144 ? 50.730 -4.281  -9.203  1.00 10.31 ? 144 ILE A CA   1 
ATOM   1939 C C    . ILE A 1 144 ? 52.089 -3.631  -9.074  1.00 10.01 ? 144 ILE A C    1 
ATOM   1940 O O    . ILE A 1 144 ? 52.240 -2.440  -9.380  1.00 12.54 ? 144 ILE A O    1 
ATOM   1941 C CB   . ILE A 1 144 ? 49.655 -3.485  -8.450  1.00 11.01 ? 144 ILE A CB   1 
ATOM   1942 C CG1  . ILE A 1 144 ? 49.888 -3.492  -6.930  1.00 12.37 ? 144 ILE A CG1  1 
ATOM   1943 C CG2  . ILE A 1 144 ? 48.245 -4.025  -8.831  1.00 13.02 ? 144 ILE A CG2  1 
ATOM   1944 C CD1  . ILE A 1 144 ? 48.984 -2.519  -6.172  1.00 13.69 ? 144 ILE A CD1  1 
ATOM   1945 H H    . ILE A 1 144 ? 50.400 -5.857  -8.084  1.00 13.79 ? 144 ILE A H    1 
ATOM   1946 H HA   . ILE A 1 144 ? 50.509 -4.257  -10.147 1.00 12.38 ? 144 ILE A HA   1 
ATOM   1947 H HB   . ILE A 1 144 ? 49.716 -2.556  -8.722  1.00 13.21 ? 144 ILE A HB   1 
ATOM   1948 H HG12 . ILE A 1 144 ? 49.715 -4.384  -6.591  1.00 14.84 ? 144 ILE A HG12 1 
ATOM   1949 H HG13 . ILE A 1 144 ? 50.808 -3.242  -6.753  1.00 14.84 ? 144 ILE A HG13 1 
ATOM   1950 H HG21 . ILE A 1 144 ? 47.570 -3.477  -8.400  1.00 15.63 ? 144 ILE A HG21 1 
ATOM   1951 H HG22 . ILE A 1 144 ? 48.140 -3.983  -9.794  1.00 15.63 ? 144 ILE A HG22 1 
ATOM   1952 H HG23 . ILE A 1 144 ? 48.167 -4.944  -8.529  1.00 15.63 ? 144 ILE A HG23 1 
ATOM   1953 H HD11 . ILE A 1 144 ? 49.233 -2.522  -5.235  1.00 16.43 ? 144 ILE A HD11 1 
ATOM   1954 H HD12 . ILE A 1 144 ? 49.097 -1.630  -6.542  1.00 16.43 ? 144 ILE A HD12 1 
ATOM   1955 H HD13 . ILE A 1 144 ? 48.062 -2.803  -6.271  1.00 16.43 ? 144 ILE A HD13 1 
ATOM   1956 N N    . THR A 1 145 ? 53.107 -4.388  -8.618  1.00 11.54 ? 145 THR A N    1 
ATOM   1957 C CA   . THR A 1 145 ? 54.462 -3.832  -8.661  1.00 11.92 ? 145 THR A CA   1 
ATOM   1958 C C    . THR A 1 145 ? 55.031 -3.753  -10.078 1.00 11.44 ? 145 THR A C    1 
ATOM   1959 O O    . THR A 1 145 ? 56.041 -3.090  -10.287 1.00 13.49 ? 145 THR A O    1 
ATOM   1960 C CB   . THR A 1 145 ? 55.447 -4.611  -7.782  1.00 12.60 ? 145 THR A CB   1 
ATOM   1961 O OG1  . THR A 1 145 ? 55.749 -5.892  -8.342  1.00 13.17 ? 145 THR A OG1  1 
ATOM   1962 C CG2  . THR A 1 145 ? 54.910 -4.754  -6.352  1.00 13.35 ? 145 THR A CG2  1 
ATOM   1963 H H    . THR A 1 145 ? 53.036 -5.183  -8.298  1.00 13.84 ? 145 THR A H    1 
ATOM   1964 H HA   . THR A 1 145 ? 54.399 -2.938  -8.290  1.00 14.31 ? 145 THR A HA   1 
ATOM   1965 H HB   . THR A 1 145 ? 56.278 -4.113  -7.737  1.00 15.12 ? 145 THR A HB   1 
ATOM   1966 H HG1  . THR A 1 145 ? 55.046 -6.345  -8.419  1.00 15.81 ? 145 THR A HG1  1 
ATOM   1967 H HG21 . THR A 1 145 ? 55.587 -5.149  -5.782  1.00 16.02 ? 145 THR A HG21 1 
ATOM   1968 H HG22 . THR A 1 145 ? 54.669 -3.883  -6.000  1.00 16.02 ? 145 THR A HG22 1 
ATOM   1969 H HG23 . THR A 1 145 ? 54.124 -5.323  -6.349  1.00 16.02 ? 145 THR A HG23 1 
ATOM   1970 N N    . LYS A 1 146 ? 54.414 -4.431  -11.049 1.00 11.86 ? 146 LYS A N    1 
ATOM   1971 C CA   . LYS A 1 146 ? 54.910 -4.464  -12.423 1.00 11.61 ? 146 LYS A CA   1 
ATOM   1972 C C    . LYS A 1 146 ? 54.280 -3.317  -13.198 1.00 11.92 ? 146 LYS A C    1 
ATOM   1973 O O    . LYS A 1 146 ? 53.056 -3.177  -13.231 1.00 11.85 ? 146 LYS A O    1 
ATOM   1974 C CB   . LYS A 1 146 ? 54.579 -5.813  -13.030 1.00 11.81 ? 146 LYS A CB   1 
ATOM   1975 C CG   . LYS A 1 146 ? 55.301 -6.933  -12.313 1.00 13.23 ? 146 LYS A CG   1 
ATOM   1976 C CD   . LYS A 1 146 ? 55.108 -8.281  -12.957 1.00 17.06 ? 146 LYS A CD   1 
ATOM   1977 C CE   . LYS A 1 146 ? 56.035 -9.281  -12.293 1.00 17.97 ? 146 LYS A CE   1 
ATOM   1978 N NZ   . LYS A 1 146 ? 56.112 -10.524 -13.061 1.00 28.09 ? 146 LYS A NZ   1 
ATOM   1979 H H    . LYS A 1 146 ? 53.694 -4.887  -10.933 1.00 14.23 ? 146 LYS A H    1 
ATOM   1980 H HA   . LYS A 1 146 ? 55.872 -4.346  -12.464 1.00 13.94 ? 146 LYS A HA   1 
ATOM   1981 H HB2  . LYS A 1 146 ? 53.624 -5.971  -12.961 1.00 14.17 ? 146 LYS A HB2  1 
ATOM   1982 H HB3  . LYS A 1 146 ? 54.851 -5.821  -13.961 1.00 14.17 ? 146 LYS A HB3  1 
ATOM   1983 H HG2  . LYS A 1 146 ? 56.251 -6.741  -12.307 1.00 15.88 ? 146 LYS A HG2  1 
ATOM   1984 H HG3  . LYS A 1 146 ? 54.968 -6.989  -11.403 1.00 15.88 ? 146 LYS A HG3  1 
ATOM   1985 H HD2  . LYS A 1 146 ? 54.191 -8.576  -12.841 1.00 20.47 ? 146 LYS A HD2  1 
ATOM   1986 H HD3  . LYS A 1 146 ? 55.323 -8.231  -13.901 1.00 20.47 ? 146 LYS A HD3  1 
ATOM   1987 H HE2  . LYS A 1 146 ? 56.926 -8.903  -12.232 1.00 21.56 ? 146 LYS A HE2  1 
ATOM   1988 H HE3  . LYS A 1 146 ? 55.702 -9.489  -11.406 1.00 21.56 ? 146 LYS A HE3  1 
ATOM   1989 H HZ1  . LYS A 1 146 ? 56.647 -11.104 -12.648 1.00 33.70 ? 146 LYS A HZ1  1 
ATOM   1990 H HZ2  . LYS A 1 146 ? 55.302 -10.884 -13.140 1.00 33.70 ? 146 LYS A HZ2  1 
ATOM   1991 H HZ3  . LYS A 1 146 ? 56.436 -10.361 -13.873 1.00 33.70 ? 146 LYS A HZ3  1 
ATOM   1992 N N    . SER A 1 147 ? 55.110 -2.524  -13.849 1.00 12.72 ? 147 SER A N    1 
ATOM   1993 C CA   . SER A 1 147 ? 54.584 -1.346  -14.527 1.00 12.86 ? 147 SER A CA   1 
ATOM   1994 C C    . SER A 1 147 ? 53.549 -1.701  -15.605 1.00 12.22 ? 147 SER A C    1 
ATOM   1995 O O    . SER A 1 147 ? 52.558 -0.984  -15.770 1.00 13.17 ? 147 SER A O    1 
ATOM   1996 C CB   . SER A 1 147 ? 55.685 -0.451  -15.088 1.00 16.39 ? 147 SER A CB   1 
ATOM   1997 O OG   . SER A 1 147 ? 56.396 -1.102  -16.095 1.00 16.38 ? 147 SER A OG   1 
ATOM   1998 H H    . SER A 1 147 ? 55.960 -2.638  -13.914 1.00 15.26 ? 147 SER A H    1 
ATOM   1999 H HA   . SER A 1 147 ? 54.131 -0.820  -13.849 1.00 15.43 ? 147 SER A HA   1 
ATOM   2000 H HB2  . SER A 1 147 ? 55.281 0.351   -15.456 1.00 19.67 ? 147 SER A HB2  1 
ATOM   2001 H HB3  . SER A 1 147 ? 56.295 -0.217  -14.372 1.00 19.67 ? 147 SER A HB3  1 
ATOM   2002 H HG   . SER A 1 147 ? 56.682 -1.840  -15.813 1.00 19.65 ? 147 SER A HG   1 
ATOM   2003 N N    . PHE A 1 148 ? 53.735 -2.809  -16.333 1.00 12.02 ? 148 PHE A N    1 
ATOM   2004 C CA   . PHE A 1 148 ? 52.740 -3.141  -17.365 1.00 12.12 ? 148 PHE A CA   1 
ATOM   2005 C C    . PHE A 1 148 ? 51.406 -3.520  -16.762 1.00 11.08 ? 148 PHE A C    1 
ATOM   2006 O O    . PHE A 1 148 ? 50.352 -3.338  -17.382 1.00 11.89 ? 148 PHE A O    1 
ATOM   2007 C CB   . PHE A 1 148 ? 53.272 -4.218  -18.317 1.00 11.91 ? 148 PHE A CB   1 
ATOM   2008 C CG   . PHE A 1 148 ? 53.149 -5.640  -17.837 1.00 11.08 ? 148 PHE A CG   1 
ATOM   2009 C CD1  . PHE A 1 148 ? 54.069 -6.198  -16.942 1.00 11.36 ? 148 PHE A CD1  1 
ATOM   2010 C CD2  . PHE A 1 148 ? 52.155 -6.464  -18.331 1.00 11.99 ? 148 PHE A CD2  1 
ATOM   2011 C CE1  . PHE A 1 148 ? 53.996 -7.523  -16.590 1.00 12.61 ? 148 PHE A CE1  1 
ATOM   2012 C CE2  . PHE A 1 148 ? 52.081 -7.797  -17.958 1.00 13.52 ? 148 PHE A CE2  1 
ATOM   2013 C CZ   . PHE A 1 148 ? 53.001 -8.320  -17.063 1.00 13.80 ? 148 PHE A CZ   1 
ATOM   2014 H H    . PHE A 1 148 ? 54.393 -3.357  -16.256 1.00 14.43 ? 148 PHE A H    1 
ATOM   2015 H HA   . PHE A 1 148 ? 52.588 -2.354  -17.911 1.00 14.55 ? 148 PHE A HA   1 
ATOM   2016 H HB2  . PHE A 1 148 ? 52.781 -4.153  -19.151 1.00 14.30 ? 148 PHE A HB2  1 
ATOM   2017 H HB3  . PHE A 1 148 ? 54.214 -4.047  -18.471 1.00 14.30 ? 148 PHE A HB3  1 
ATOM   2018 H HD1  . PHE A 1 148 ? 54.738 -5.663  -16.580 1.00 13.63 ? 148 PHE A HD1  1 
ATOM   2019 H HD2  . PHE A 1 148 ? 51.526 -6.118  -18.923 1.00 14.39 ? 148 PHE A HD2  1 
ATOM   2020 H HE1  . PHE A 1 148 ? 54.638 -7.881  -16.019 1.00 15.13 ? 148 PHE A HE1  1 
ATOM   2021 H HE2  . PHE A 1 148 ? 51.414 -8.342  -18.309 1.00 16.23 ? 148 PHE A HE2  1 
ATOM   2022 H HZ   . PHE A 1 148 ? 52.938 -9.207  -16.789 1.00 16.57 ? 148 PHE A HZ   1 
ATOM   2023 N N    . VAL A 1 149 ? 51.408 -4.040  -15.538 1.00 10.94 ? 149 VAL A N    1 
ATOM   2024 C CA   . VAL A 1 149 ? 50.168 -4.336  -14.828 1.00 10.88 ? 149 VAL A CA   1 
ATOM   2025 C C    . VAL A 1 149 ? 49.525 -3.052  -14.339 1.00 11.45 ? 149 VAL A C    1 
ATOM   2026 O O    . VAL A 1 149 ? 48.309 -2.871  -14.468 1.00 11.65 ? 149 VAL A O    1 
ATOM   2027 C CB   . VAL A 1 149 ? 50.441 -5.315  -13.670 1.00 10.81 ? 149 VAL A CB   1 
ATOM   2028 C CG1  . VAL A 1 149 ? 49.180 -5.554  -12.858 1.00 12.36 ? 149 VAL A CG1  1 
ATOM   2029 C CG2  . VAL A 1 149 ? 50.991 -6.616  -14.204 1.00 11.49 ? 149 VAL A CG2  1 
ATOM   2030 H H    . VAL A 1 149 ? 52.118 -4.234  -15.093 1.00 13.12 ? 149 VAL A H    1 
ATOM   2031 H HA   . VAL A 1 149 ? 49.551 -4.764  -15.441 1.00 13.06 ? 149 VAL A HA   1 
ATOM   2032 H HB   . VAL A 1 149 ? 51.104 -4.925  -13.078 1.00 12.97 ? 149 VAL A HB   1 
ATOM   2033 H HG11 . VAL A 1 149 ? 49.351 -6.253  -12.208 1.00 14.83 ? 149 VAL A HG11 1 
ATOM   2034 H HG12 . VAL A 1 149 ? 48.937 -4.733  -12.404 1.00 14.83 ? 149 VAL A HG12 1 
ATOM   2035 H HG13 . VAL A 1 149 ? 48.467 -5.826  -13.456 1.00 14.83 ? 149 VAL A HG13 1 
ATOM   2036 H HG21 . VAL A 1 149 ? 51.077 -7.246  -13.471 1.00 13.79 ? 149 VAL A HG21 1 
ATOM   2037 H HG22 . VAL A 1 149 ? 50.380 -6.967  -14.871 1.00 13.79 ? 149 VAL A HG22 1 
ATOM   2038 H HG23 . VAL A 1 149 ? 51.859 -6.452  -14.603 1.00 13.79 ? 149 VAL A HG23 1 
ATOM   2039 N N    . GLN A 1 150 ? 50.326 -2.136  -13.795 1.00 11.87 ? 150 GLN A N    1 
ATOM   2040 C CA   . GLN A 1 150 ? 49.813 -0.818  -13.410 1.00 11.72 ? 150 GLN A CA   1 
ATOM   2041 C C    . GLN A 1 150 ? 49.135 -0.140  -14.583 1.00 12.37 ? 150 GLN A C    1 
ATOM   2042 O O    . GLN A 1 150 ? 48.026 0.391   -14.443 1.00 12.57 ? 150 GLN A O    1 
ATOM   2043 C CB   . GLN A 1 150 ? 50.944 0.066   -12.907 1.00 13.29 ? 150 GLN A CB   1 
ATOM   2044 C CG   . GLN A 1 150 ? 51.577 -0.416  -11.633 1.00 12.27 ? 150 GLN A CG   1 
ATOM   2045 C CD   . GLN A 1 150 ? 52.787 0.350   -11.281 1.00 15.36 ? 150 GLN A CD   1 
ATOM   2046 O OE1  . GLN A 1 150 ? 52.988 1.496   -11.703 1.00 20.07 ? 150 GLN A OE1  1 
ATOM   2047 N NE2  . GLN A 1 150 ? 53.642 -0.257  -10.475 1.00 15.62 ? 150 GLN A NE2  1 
ATOM   2048 H H    . GLN A 1 150 ? 51.164 -2.250  -13.637 1.00 14.24 ? 150 GLN A H    1 
ATOM   2049 H HA   . GLN A 1 150 ? 49.172 -0.939  -12.693 1.00 14.06 ? 150 GLN A HA   1 
ATOM   2050 H HB2  . GLN A 1 150 ? 51.637 0.102   -13.585 1.00 15.94 ? 150 GLN A HB2  1 
ATOM   2051 H HB3  . GLN A 1 150 ? 50.594 0.956   -12.743 1.00 15.94 ? 150 GLN A HB3  1 
ATOM   2052 H HG2  . GLN A 1 150 ? 50.940 -0.324  -10.907 1.00 14.72 ? 150 GLN A HG2  1 
ATOM   2053 H HG3  . GLN A 1 150 ? 51.829 -1.347  -11.737 1.00 14.72 ? 150 GLN A HG3  1 
ATOM   2054 H HE21 . GLN A 1 150 ? 53.475 -1.051  -10.191 1.00 18.75 ? 150 GLN A HE21 1 
ATOM   2055 H HE22 . GLN A 1 150 ? 54.366 0.142   -10.237 1.00 18.75 ? 150 GLN A HE22 1 
ATOM   2056 N N    . GLU A 1 151 ? 49.784 -0.158  -15.751 1.00 12.79 ? 151 GLU A N    1 
ATOM   2057 C CA   . GLU A 1 151 ? 49.242 0.544   -16.903 1.00 13.44 ? 151 GLU A CA   1 
ATOM   2058 C C    . GLU A 1 151 ? 47.966 -0.125  -17.371 1.00 12.34 ? 151 GLU A C    1 
ATOM   2059 O O    . GLU A 1 151 ? 46.977 0.551   -17.683 1.00 13.68 ? 151 GLU A O    1 
ATOM   2060 C CB   . GLU A 1 151 ? 50.253 0.621   -18.049 1.00 14.32 ? 151 GLU A CB   1 
ATOM   2061 C CG   . GLU A 1 151 ? 49.745 1.400   -19.289 1.00 19.69 ? 151 GLU A CG   1 
ATOM   2062 C CD   . GLU A 1 151 ? 49.637 2.902   -19.043 1.00 24.16 ? 151 GLU A CD   1 
ATOM   2063 O OE1  . GLU A 1 151 ? 50.237 3.400   -18.043 1.00 24.83 ? 151 GLU A OE1  1 
ATOM   2064 O OE2  . GLU A 1 151 ? 48.939 3.570   -19.860 1.00 25.05 ? 151 GLU A OE2  1 
ATOM   2065 H H    . GLU A 1 151 ? 50.528 -0.565  -15.895 1.00 15.35 ? 151 GLU A H    1 
ATOM   2066 H HA   . GLU A 1 151 ? 49.052 1.457   -16.637 1.00 16.13 ? 151 GLU A HA   1 
ATOM   2067 H HB2  . GLU A 1 151 ? 51.053 1.066   -17.728 1.00 17.19 ? 151 GLU A HB2  1 
ATOM   2068 H HB3  . GLU A 1 151 ? 50.467 -0.281  -18.335 1.00 17.19 ? 151 GLU A HB3  1 
ATOM   2069 H HG2  . GLU A 1 151 ? 50.363 1.261   -20.024 1.00 23.62 ? 151 GLU A HG2  1 
ATOM   2070 H HG3  . GLU A 1 151 ? 48.865 1.072   -19.530 1.00 23.62 ? 151 GLU A HG3  1 
ATOM   2071 N N    . TYR A 1 152 ? 47.966 -1.464  -17.438 1.00 12.14 ? 152 TYR A N    1 
ATOM   2072 C CA   . TYR A 1 152 ? 46.747 -2.193  -17.790 1.00 11.89 ? 152 TYR A CA   1 
ATOM   2073 C C    . TYR A 1 152 ? 45.596 -1.767  -16.881 1.00 12.07 ? 152 TYR A C    1 
ATOM   2074 O O    . TYR A 1 152 ? 44.500 -1.427  -17.347 1.00 12.98 ? 152 TYR A O    1 
ATOM   2075 C CB   . TYR A 1 152 ? 46.959 -3.721  -17.727 1.00 12.71 ? 152 TYR A CB   1 
ATOM   2076 C CG   . TYR A 1 152 ? 45.643 -4.404  -17.942 1.00 12.45 ? 152 TYR A CG   1 
ATOM   2077 C CD1  . TYR A 1 152 ? 45.148 -4.572  -19.235 1.00 12.88 ? 152 TYR A CD1  1 
ATOM   2078 C CD2  . TYR A 1 152 ? 44.839 -4.792  -16.885 1.00 11.96 ? 152 TYR A CD2  1 
ATOM   2079 C CE1  . TYR A 1 152 ? 43.908 -5.114  -19.443 1.00 13.27 ? 152 TYR A CE1  1 
ATOM   2080 C CE2  . TYR A 1 152 ? 43.595 -5.324  -17.093 1.00 13.09 ? 152 TYR A CE2  1 
ATOM   2081 C CZ   . TYR A 1 152 ? 43.142 -5.491  -18.374 1.00 12.43 ? 152 TYR A CZ   1 
ATOM   2082 O OH   . TYR A 1 152 ? 41.882 -5.990  -18.617 1.00 13.74 ? 152 TYR A OH   1 
ATOM   2083 H H    . TYR A 1 152 ? 48.650 -1.964  -17.287 1.00 14.57 ? 152 TYR A H    1 
ATOM   2084 H HA   . TYR A 1 152 ? 46.521 -1.984  -18.710 1.00 14.27 ? 152 TYR A HA   1 
ATOM   2085 H HB2  . TYR A 1 152 ? 47.577 -3.998  -18.422 1.00 15.25 ? 152 TYR A HB2  1 
ATOM   2086 H HB3  . TYR A 1 152 ? 47.306 -3.971  -16.856 1.00 15.25 ? 152 TYR A HB3  1 
ATOM   2087 H HD1  . TYR A 1 152 ? 45.665 -4.314  -19.963 1.00 15.46 ? 152 TYR A HD1  1 
ATOM   2088 H HD2  . TYR A 1 152 ? 45.150 -4.690  -16.015 1.00 14.36 ? 152 TYR A HD2  1 
ATOM   2089 H HE1  . TYR A 1 152 ? 43.587 -5.225  -20.309 1.00 15.93 ? 152 TYR A HE1  1 
ATOM   2090 H HE2  . TYR A 1 152 ? 43.063 -5.570  -16.371 1.00 15.71 ? 152 TYR A HE2  1 
ATOM   2091 H HH   . TYR A 1 152 ? 41.503 -6.179  -17.891 1.00 16.49 ? 152 TYR A HH   1 
ATOM   2092 N N    . TRP A 1 153 ? 45.835 -1.795  -15.569 1.00 11.56 ? 153 TRP A N    1 
ATOM   2093 C CA   . TRP A 1 153 ? 44.781 -1.528  -14.592 1.00 12.17 ? 153 TRP A CA   1 
ATOM   2094 C C    . TRP A 1 153 ? 44.307 -0.089  -14.678 1.00 10.98 ? 153 TRP A C    1 
ATOM   2095 O O    . TRP A 1 153 ? 43.101 0.185   -14.754 1.00 11.23 ? 153 TRP A O    1 
ATOM   2096 C CB   . TRP A 1 153 ? 45.302 -1.865  -13.204 1.00 12.54 ? 153 TRP A CB   1 
ATOM   2097 C CG   . TRP A 1 153 ? 44.245 -1.840  -12.131 1.00 10.80 ? 153 TRP A CG   1 
ATOM   2098 C CD1  . TRP A 1 153 ? 43.513 -2.895  -11.702 1.00 12.05 ? 153 TRP A CD1  1 
ATOM   2099 C CD2  . TRP A 1 153 ? 43.792 -0.696  -11.390 1.00 11.03 ? 153 TRP A CD2  1 
ATOM   2100 N NE1  . TRP A 1 153 ? 42.628 -2.493  -10.718 1.00 11.94 ? 153 TRP A NE1  1 
ATOM   2101 C CE2  . TRP A 1 153 ? 42.771 -1.144  -10.533 1.00 11.26 ? 153 TRP A CE2  1 
ATOM   2102 C CE3  . TRP A 1 153 ? 44.131 0.652   -11.381 1.00 12.32 ? 153 TRP A CE3  1 
ATOM   2103 C CZ2  . TRP A 1 153 ? 42.109 -0.290  -9.648  1.00 12.11 ? 153 TRP A CZ2  1 
ATOM   2104 C CZ3  . TRP A 1 153 ? 43.481 1.505   -10.489 1.00 12.87 ? 153 TRP A CZ3  1 
ATOM   2105 C CH2  . TRP A 1 153 ? 42.469 1.006   -9.648  1.00 12.80 ? 153 TRP A CH2  1 
ATOM   2106 H H    . TRP A 1 153 ? 46.600 -1.967  -15.217 1.00 13.87 ? 153 TRP A H    1 
ATOM   2107 H HA   . TRP A 1 153 ? 44.012 -2.090  -14.774 1.00 14.60 ? 153 TRP A HA   1 
ATOM   2108 H HB2  . TRP A 1 153 ? 45.682 -2.757  -13.222 1.00 15.04 ? 153 TRP A HB2  1 
ATOM   2109 H HB3  . TRP A 1 153 ? 45.983 -1.218  -12.962 1.00 15.04 ? 153 TRP A HB3  1 
ATOM   2110 H HD1  . TRP A 1 153 ? 43.594 -3.765  -12.022 1.00 14.46 ? 153 TRP A HD1  1 
ATOM   2111 H HE1  . TRP A 1 153 ? 42.080 -3.004  -10.294 1.00 14.33 ? 153 TRP A HE1  1 
ATOM   2112 H HE3  . TRP A 1 153 ? 44.780 0.980   -11.960 1.00 14.79 ? 153 TRP A HE3  1 
ATOM   2113 H HZ2  . TRP A 1 153 ? 41.444 -0.606  -9.080  1.00 14.53 ? 153 TRP A HZ2  1 
ATOM   2114 H HZ3  . TRP A 1 153 ? 43.717 2.404   -10.449 1.00 15.45 ? 153 TRP A HZ3  1 
ATOM   2115 H HH2  . TRP A 1 153 ? 42.033 1.593   -9.073  1.00 15.36 ? 153 TRP A HH2  1 
ATOM   2116 N N    . LEU A 1 154 ? 45.239 0.850   -14.714 1.00 11.40 ? 154 LEU A N    1 
ATOM   2117 C CA   . LEU A 1 154 ? 44.884 2.260   -14.787 1.00 11.29 ? 154 LEU A CA   1 
ATOM   2118 C C    . LEU A 1 154 ? 44.046 2.545   -16.016 1.00 13.22 ? 154 LEU A C    1 
ATOM   2119 O O    . LEU A 1 154 ? 43.026 3.240   -15.948 1.00 13.82 ? 154 LEU A O    1 
ATOM   2120 C CB   . LEU A 1 154 ? 46.121 3.135   -14.739 1.00 12.96 ? 154 LEU A CB   1 
ATOM   2121 C CG   . LEU A 1 154 ? 46.786 3.197   -13.364 1.00 12.81 ? 154 LEU A CG   1 
ATOM   2122 C CD1  . LEU A 1 154 ? 48.187 3.726   -13.501 1.00 15.69 ? 154 LEU A CD1  1 
ATOM   2123 C CD2  . LEU A 1 154 ? 45.953 4.070   -12.408 1.00 15.43 ? 154 LEU A CD2  1 
ATOM   2124 H H    . LEU A 1 154 ? 46.085 0.699   -14.697 1.00 13.68 ? 154 LEU A H    1 
ATOM   2125 H HA   . LEU A 1 154 ? 44.354 2.486   -14.006 1.00 13.55 ? 154 LEU A HA   1 
ATOM   2126 H HB2  . LEU A 1 154 ? 46.773 2.785   -15.367 1.00 15.55 ? 154 LEU A HB2  1 
ATOM   2127 H HB3  . LEU A 1 154 ? 45.872 4.038   -14.988 1.00 15.55 ? 154 LEU A HB3  1 
ATOM   2128 H HG   . LEU A 1 154 ? 46.836 2.308   -12.980 1.00 15.37 ? 154 LEU A HG   1 
ATOM   2129 H HD11 . LEU A 1 154 ? 48.416 4.225   -12.701 1.00 18.82 ? 154 LEU A HD11 1 
ATOM   2130 H HD12 . LEU A 1 154 ? 48.797 2.979   -13.610 1.00 18.82 ? 154 LEU A HD12 1 
ATOM   2131 H HD13 . LEU A 1 154 ? 48.231 4.306   -14.277 1.00 18.82 ? 154 LEU A HD13 1 
ATOM   2132 H HD21 . LEU A 1 154 ? 46.432 4.167   -11.571 1.00 18.51 ? 154 LEU A HD21 1 
ATOM   2133 H HD22 . LEU A 1 154 ? 45.815 4.940   -12.814 1.00 18.51 ? 154 LEU A HD22 1 
ATOM   2134 H HD23 . LEU A 1 154 ? 45.098 3.639   -12.251 1.00 18.51 ? 154 LEU A HD23 1 
ATOM   2135 N N    . LYS A 1 155 ? 44.485 2.060   -17.174 1.00 12.59 ? 155 LYS A N    1 
ATOM   2136 C CA   . LYS A 1 155 ? 43.724 2.303   -18.393 1.00 14.07 ? 155 LYS A CA   1 
ATOM   2137 C C    . LYS A 1 155 ? 42.359 1.642   -18.343 1.00 13.43 ? 155 LYS A C    1 
ATOM   2138 O O    . LYS A 1 155 ? 41.396 2.190   -18.903 1.00 14.59 ? 155 LYS A O    1 
ATOM   2139 C CB   . LYS A 1 155 ? 44.506 1.848   -19.610 1.00 14.44 ? 155 LYS A CB   1 
ATOM   2140 C CG   . LYS A 1 155 ? 45.521 2.855   -20.064 1.00 19.33 ? 155 LYS A CG   1 
ATOM   2141 C CD   . LYS A 1 155 ? 44.855 4.150   -20.511 1.00 22.83 ? 155 LYS A CD   1 
ATOM   2142 C CE   . LYS A 1 155 ? 45.812 5.024   -21.264 1.00 25.57 ? 155 LYS A CE   1 
ATOM   2143 N NZ   . LYS A 1 155 ? 45.123 6.251   -21.691 1.00 24.01 ? 155 LYS A NZ   1 
ATOM   2144 H H    . LYS A 1 155 ? 45.203 1.598   -17.278 1.00 15.11 ? 155 LYS A H    1 
ATOM   2145 H HA   . LYS A 1 155 ? 43.583 3.258   -18.486 1.00 16.89 ? 155 LYS A HA   1 
ATOM   2146 H HB2  . LYS A 1 155 ? 44.975 1.026   -19.394 1.00 17.33 ? 155 LYS A HB2  1 
ATOM   2147 H HB3  . LYS A 1 155 ? 43.889 1.694   -20.343 1.00 17.33 ? 155 LYS A HB3  1 
ATOM   2148 H HG2  . LYS A 1 155 ? 46.123 3.058   -19.330 1.00 23.20 ? 155 LYS A HG2  1 
ATOM   2149 H HG3  . LYS A 1 155 ? 46.021 2.494   -20.812 1.00 23.20 ? 155 LYS A HG3  1 
ATOM   2150 H HD2  . LYS A 1 155 ? 44.107 3.943   -21.093 1.00 27.39 ? 155 LYS A HD2  1 
ATOM   2151 H HD3  . LYS A 1 155 ? 44.543 4.637   -19.732 1.00 27.39 ? 155 LYS A HD3  1 
ATOM   2152 H HE2  . LYS A 1 155 ? 46.557 5.266   -20.691 1.00 30.69 ? 155 LYS A HE2  1 
ATOM   2153 H HE3  . LYS A 1 155 ? 46.137 4.556   -22.049 1.00 30.69 ? 155 LYS A HE3  1 
ATOM   2154 H HZ1  . LYS A 1 155 ? 45.678 6.765   -22.160 1.00 28.81 ? 155 LYS A HZ1  1 
ATOM   2155 H HZ2  . LYS A 1 155 ? 44.422 6.045   -22.200 1.00 28.81 ? 155 LYS A HZ2  1 
ATOM   2156 H HZ3  . LYS A 1 155 ? 44.840 6.705   -20.980 1.00 28.81 ? 155 LYS A HZ3  1 
ATOM   2157 N N    . SER A 1 156 ? 42.239 0.481   -17.719 1.00 13.05 ? 156 SER A N    1 
ATOM   2158 C CA   . SER A 1 156 ? 40.931 -0.158  -17.635 1.00 13.72 ? 156 SER A CA   1 
ATOM   2159 C C    . SER A 1 156 ? 39.949 0.753   -16.902 1.00 14.54 ? 156 SER A C    1 
ATOM   2160 O O    . SER A 1 156 ? 38.797 0.935   -17.338 1.00 17.88 ? 156 SER A O    1 
ATOM   2161 C CB   . SER A 1 156 ? 41.037 -1.547  -17.012 1.00 14.87 ? 156 SER A CB   1 
ATOM   2162 O OG   . SER A 1 156 ? 41.235 -1.525  -15.609 1.00 13.93 ? 156 SER A OG   1 
ATOM   2163 H H    . SER A 1 156 ? 42.882 0.050   -17.343 1.00 15.65 ? 156 SER A H    1 
ATOM   2164 H HA   . SER A 1 156 ? 40.579 -0.307  -18.527 1.00 16.46 ? 156 SER A HA   1 
ATOM   2165 H HB2  . SER A 1 156 ? 40.215 -2.028  -17.197 1.00 17.84 ? 156 SER A HB2  1 
ATOM   2166 H HB3  . SER A 1 156 ? 41.789 -2.006  -17.419 1.00 17.84 ? 156 SER A HB3  1 
ATOM   2167 H HG   . SER A 1 156 ? 41.917 -1.070  -15.422 1.00 16.72 ? 156 SER A HG   1 
ATOM   2168 N N    . VAL A 1 157 ? 40.417 1.429   -15.862 1.00 12.74 ? 157 VAL A N    1 
ATOM   2169 C CA   . VAL A 1 157 ? 39.566 2.358   -15.116 1.00 13.12 ? 157 VAL A CA   1 
ATOM   2170 C C    . VAL A 1 157 ? 39.320 3.626   -15.916 1.00 13.79 ? 157 VAL A C    1 
ATOM   2171 O O    . VAL A 1 157 ? 38.173 4.059   -16.108 1.00 13.95 ? 157 VAL A O    1 
ATOM   2172 C CB   . VAL A 1 157 ? 40.189 2.664   -13.749 1.00 12.32 ? 157 VAL A CB   1 
ATOM   2173 C CG1  . VAL A 1 157 ? 39.385 3.727   -13.021 1.00 14.60 ? 157 VAL A CG1  1 
ATOM   2174 C CG2  . VAL A 1 157 ? 40.293 1.404   -12.918 1.00 13.62 ? 157 VAL A CG2  1 
ATOM   2175 H H    . VAL A 1 157 ? 41.222 1.371   -15.564 1.00 15.29 ? 157 VAL A H    1 
ATOM   2176 H HA   . VAL A 1 157 ? 38.706 1.935   -14.965 1.00 15.74 ? 157 VAL A HA   1 
ATOM   2177 H HB   . VAL A 1 157 ? 41.086 3.008   -13.884 1.00 14.78 ? 157 VAL A HB   1 
ATOM   2178 H HG11 . VAL A 1 157 ? 39.673 3.762   -12.095 1.00 17.52 ? 157 VAL A HG11 1 
ATOM   2179 H HG12 . VAL A 1 157 ? 39.538 4.585   -13.447 1.00 17.52 ? 157 VAL A HG12 1 
ATOM   2180 H HG13 . VAL A 1 157 ? 38.444 3.498   -13.066 1.00 17.52 ? 157 VAL A HG13 1 
ATOM   2181 H HG21 . VAL A 1 157 ? 40.638 1.632   -12.041 1.00 16.35 ? 157 VAL A HG21 1 
ATOM   2182 H HG22 . VAL A 1 157 ? 39.412 1.008   -12.834 1.00 16.35 ? 157 VAL A HG22 1 
ATOM   2183 H HG23 . VAL A 1 157 ? 40.894 0.784   -13.359 1.00 16.35 ? 157 VAL A HG23 1 
ATOM   2184 N N    . GLU A 1 158 ? 40.394 4.255   -16.403 1.00 13.47 ? 158 GLU A N    1 
ATOM   2185 C CA   . GLU A 1 158 ? 40.269 5.514   -17.118 1.00 15.26 ? 158 GLU A CA   1 
ATOM   2186 C C    . GLU A 1 158 ? 39.411 5.370   -18.363 1.00 14.93 ? 158 GLU A C    1 
ATOM   2187 O O    . GLU A 1 158 ? 38.570 6.231   -18.658 1.00 15.50 ? 158 GLU A O    1 
ATOM   2188 C CB   . GLU A 1 158 ? 41.669 6.057   -17.449 1.00 15.76 ? 158 GLU A CB   1 
ATOM   2189 C CG   . GLU A 1 158 ? 42.455 6.463   -16.195 1.00 16.39 ? 158 GLU A CG   1 
ATOM   2190 C CD   . GLU A 1 158 ? 43.964 6.620   -16.426 1.00 22.33 ? 158 GLU A CD   1 
ATOM   2191 O OE1  . GLU A 1 158 ? 44.484 6.213   -17.489 1.00 22.84 ? 158 GLU A OE1  1 
ATOM   2192 O OE2  . GLU A 1 158 ? 44.652 7.122   -15.507 1.00 20.85 ? 158 GLU A OE2  1 
ATOM   2193 H H    . GLU A 1 158 ? 41.202 3.970   -16.331 1.00 16.16 ? 158 GLU A H    1 
ATOM   2194 H HA   . GLU A 1 158 ? 39.827 6.163   -16.549 1.00 18.32 ? 158 GLU A HA   1 
ATOM   2195 H HB2  . GLU A 1 158 ? 42.174 5.370   -17.912 1.00 18.91 ? 158 GLU A HB2  1 
ATOM   2196 H HB3  . GLU A 1 158 ? 41.579 6.840   -18.015 1.00 18.91 ? 158 GLU A HB3  1 
ATOM   2197 H HG2  . GLU A 1 158 ? 42.116 7.315   -15.877 1.00 19.66 ? 158 GLU A HG2  1 
ATOM   2198 H HG3  . GLU A 1 158 ? 42.330 5.783   -15.515 1.00 19.66 ? 158 GLU A HG3  1 
ATOM   2199 N N    . ASP A 1 159 ? 39.610 4.293   -19.116 1.00 14.50 ? 159 ASP A N    1 
ATOM   2200 C CA   . ASP A 1 159 ? 38.849 4.122   -20.360 1.00 16.61 ? 159 ASP A CA   1 
ATOM   2201 C C    . ASP A 1 159 ? 37.372 3.916   -20.050 1.00 16.12 ? 159 ASP A C    1 
ATOM   2202 O O    . ASP A 1 159 ? 36.505 4.412   -20.784 1.00 18.72 ? 159 ASP A O    1 
ATOM   2203 C CB   . ASP A 1 159 ? 39.385 2.933   -21.165 1.00 17.31 ? 159 ASP A CB   1 
ATOM   2204 C CG   . ASP A 1 159 ? 40.714 3.222   -21.872 1.00 18.58 ? 159 ASP A CG   1 
ATOM   2205 O OD1  . ASP A 1 159 ? 41.047 4.396   -22.139 1.00 24.28 ? 159 ASP A OD1  1 
ATOM   2206 O OD2  . ASP A 1 159 ? 41.385 2.226   -22.202 1.00 21.88 ? 159 ASP A OD2  1 
ATOM   2207 H H    . ASP A 1 159 ? 40.164 3.659   -18.939 1.00 17.40 ? 159 ASP A H    1 
ATOM   2208 H HA   . ASP A 1 159 ? 38.955 4.915   -20.908 1.00 19.93 ? 159 ASP A HA   1 
ATOM   2209 H HB2  . ASP A 1 159 ? 39.526 2.185   -20.564 1.00 20.78 ? 159 ASP A HB2  1 
ATOM   2210 H HB3  . ASP A 1 159 ? 38.734 2.695   -21.844 1.00 20.78 ? 159 ASP A HB3  1 
ATOM   2211 N N    . MET A 1 160 ? 37.042 3.237   -18.941 1.00 15.25 ? 160 MET A N    1 
ATOM   2212 C CA   . MET A 1 160 ? 35.626 3.042   -18.626 1.00 14.42 ? 160 MET A CA   1 
ATOM   2213 C C    . MET A 1 160 ? 35.021 4.362   -18.120 1.00 15.37 ? 160 MET A C    1 
ATOM   2214 O O    . MET A 1 160 ? 33.906 4.729   -18.494 1.00 15.89 ? 160 MET A O    1 
ATOM   2215 C CB   . MET A 1 160 ? 35.437 1.937   -17.580 1.00 14.86 ? 160 MET A CB   1 
ATOM   2216 C CG   . MET A 1 160 ? 33.977 1.843   -17.172 1.00 16.97 ? 160 MET A CG   1 
ATOM   2217 S SD   . MET A 1 160 ? 32.931 1.074   -18.425 1.00 18.29 ? 160 MET A SD   1 
ATOM   2218 C CE   . MET A 1 160 ? 33.472 -0.608  -18.397 1.00 21.81 ? 160 MET A CE   1 
ATOM   2219 H H    . MET A 1 160 ? 37.597 2.895   -18.381 1.00 18.30 ? 160 MET A H    1 
ATOM   2220 H HA   . MET A 1 160 ? 35.168 2.747   -19.429 1.00 17.30 ? 160 MET A HA   1 
ATOM   2221 H HB2  . MET A 1 160 ? 35.711 1.085   -17.953 1.00 17.84 ? 160 MET A HB2  1 
ATOM   2222 H HB3  . MET A 1 160 ? 35.967 2.140   -16.793 1.00 17.84 ? 160 MET A HB3  1 
ATOM   2223 H HG2  . MET A 1 160 ? 33.911 1.312   -16.363 1.00 20.37 ? 160 MET A HG2  1 
ATOM   2224 H HG3  . MET A 1 160 ? 33.639 2.738   -17.011 1.00 20.37 ? 160 MET A HG3  1 
ATOM   2225 H HE1  . MET A 1 160 ? 32.917 -1.128  -18.998 1.00 26.17 ? 160 MET A HE1  1 
ATOM   2226 H HE2  . MET A 1 160 ? 34.398 -0.647  -18.684 1.00 26.17 ? 160 MET A HE2  1 
ATOM   2227 H HE3  . MET A 1 160 ? 33.391 -0.950  -17.492 1.00 26.17 ? 160 MET A HE3  1 
ATOM   2228 N N    . VAL A 1 161 ? 35.739 5.100   -17.263 1.00 14.74 ? 161 VAL A N    1 
ATOM   2229 C CA   . VAL A 1 161 ? 35.199 6.357   -16.751 1.00 15.73 ? 161 VAL A CA   1 
ATOM   2230 C C    . VAL A 1 161 ? 35.053 7.386   -17.867 1.00 15.94 ? 161 VAL A C    1 
ATOM   2231 O O    . VAL A 1 161 ? 34.190 8.264   -17.793 1.00 17.52 ? 161 VAL A O    1 
ATOM   2232 C CB   . VAL A 1 161 ? 36.054 6.863   -15.581 1.00 14.40 ? 161 VAL A CB   1 
ATOM   2233 C CG1  . VAL A 1 161 ? 35.602 8.225   -15.105 1.00 15.83 ? 161 VAL A CG1  1 
ATOM   2234 C CG2  . VAL A 1 161 ? 35.978 5.871   -14.442 1.00 14.61 ? 161 VAL A CG2  1 
ATOM   2235 H H    . VAL A 1 161 ? 36.522 4.897   -16.971 1.00 17.68 ? 161 VAL A H    1 
ATOM   2236 H HA   . VAL A 1 161 ? 34.307 6.197   -16.405 1.00 18.88 ? 161 VAL A HA   1 
ATOM   2237 H HB   . VAL A 1 161 ? 36.971 6.951   -15.883 1.00 17.29 ? 161 VAL A HB   1 
ATOM   2238 H HG11 . VAL A 1 161 ? 36.043 8.429   -14.265 1.00 19.00 ? 161 VAL A HG11 1 
ATOM   2239 H HG12 . VAL A 1 161 ? 35.839 8.888   -15.772 1.00 19.00 ? 161 VAL A HG12 1 
ATOM   2240 H HG13 . VAL A 1 161 ? 34.640 8.212   -14.979 1.00 19.00 ? 161 VAL A HG13 1 
ATOM   2241 H HG21 . VAL A 1 161 ? 36.479 6.217   -13.687 1.00 17.54 ? 161 VAL A HG21 1 
ATOM   2242 H HG22 . VAL A 1 161 ? 35.048 5.746   -14.193 1.00 17.54 ? 161 VAL A HG22 1 
ATOM   2243 H HG23 . VAL A 1 161 ? 36.358 5.027   -14.733 1.00 17.54 ? 161 VAL A HG23 1 
ATOM   2244 N N    . ALA A 1 162 ? 35.854 7.284   -18.931 1.00 15.63 ? 162 ALA A N    1 
ATOM   2245 C CA   . ALA A 1 162 ? 35.782 8.243   -20.013 1.00 17.71 ? 162 ALA A CA   1 
ATOM   2246 C C    . ALA A 1 162 ? 34.524 8.100   -20.846 1.00 17.50 ? 162 ALA A C    1 
ATOM   2247 O O    . ALA A 1 162 ? 34.218 9.018   -21.616 1.00 20.22 ? 162 ALA A O    1 
ATOM   2248 C CB   . ALA A 1 162 ? 37.014 8.081   -20.907 1.00 18.71 ? 162 ALA A CB   1 
ATOM   2249 H H    . ALA A 1 162 ? 36.443 6.667   -19.042 1.00 18.75 ? 162 ALA A H    1 
ATOM   2250 H HA   . ALA A 1 162 ? 35.783 9.140   -19.643 1.00 21.26 ? 162 ALA A HA   1 
ATOM   2251 H HB1  . ALA A 1 162 ? 36.953 8.707   -21.646 1.00 22.45 ? 162 ALA A HB1  1 
ATOM   2252 H HB2  . ALA A 1 162 ? 37.810 8.265   -20.384 1.00 22.45 ? 162 ALA A HB2  1 
ATOM   2253 H HB3  . ALA A 1 162 ? 37.042 7.172   -21.244 1.00 22.45 ? 162 ALA A HB3  1 
ATOM   2254 N N    . THR A 1 163 ? 33.791 6.991   -20.716 1.00 17.20 ? 163 THR A N    1 
ATOM   2255 C CA   . THR A 1 163 ? 32.564 6.791   -21.483 1.00 18.45 ? 163 THR A CA   1 
ATOM   2256 C C    . THR A 1 163 ? 31.437 7.677   -20.940 1.00 19.80 ? 163 THR A C    1 
ATOM   2257 O O    . THR A 1 163 ? 31.498 8.178   -19.815 1.00 17.68 ? 163 THR A O    1 
ATOM   2258 C CB   . THR A 1 163 ? 32.137 5.315   -21.468 1.00 17.87 ? 163 THR A CB   1 
ATOM   2259 O OG1  . THR A 1 163 ? 31.731 4.904   -20.159 1.00 17.95 ? 163 THR A OG1  1 
ATOM   2260 C CG2  . THR A 1 163 ? 33.262 4.411   -21.958 1.00 19.28 ? 163 THR A CG2  1 
ATOM   2261 H H    . THR A 1 163 ? 33.985 6.340   -20.190 1.00 20.64 ? 163 THR A H    1 
ATOM   2262 H HA   . THR A 1 163 ? 32.725 7.039   -22.407 1.00 22.14 ? 163 THR A HA   1 
ATOM   2263 H HB   . THR A 1 163 ? 31.381 5.217   -22.067 1.00 21.44 ? 163 THR A HB   1 
ATOM   2264 H HG1  . THR A 1 163 ? 32.383 4.942   -19.631 1.00 21.54 ? 163 THR A HG1  1 
ATOM   2265 H HG21 . THR A 1 163 ? 32.946 3.497   -22.031 1.00 23.14 ? 163 THR A HG21 1 
ATOM   2266 H HG22 . THR A 1 163 ? 33.571 4.707   -22.829 1.00 23.14 ? 163 THR A HG22 1 
ATOM   2267 H HG23 . THR A 1 163 ? 34.005 4.438   -21.335 1.00 23.14 ? 163 THR A HG23 1 
ATOM   2268 N N    . PRO A 1 164 ? 30.443 8.036   -21.779 1.00 20.17 ? 164 PRO A N    1 
ATOM   2269 C CA   . PRO A 1 164 ? 29.516 9.094   -21.395 1.00 20.87 ? 164 PRO A CA   1 
ATOM   2270 C C    . PRO A 1 164 ? 28.615 8.857   -20.190 1.00 19.72 ? 164 PRO A C    1 
ATOM   2271 O O    . PRO A 1 164 ? 28.228 9.841   -19.646 1.00 24.51 ? 164 PRO A O    1 
ATOM   2272 C CB   . PRO A 1 164 ? 28.654 9.287   -22.657 1.00 23.09 ? 164 PRO A CB   1 
ATOM   2273 C CG   . PRO A 1 164 ? 28.693 7.973   -23.343 1.00 25.49 ? 164 PRO A CG   1 
ATOM   2274 C CD   . PRO A 1 164 ? 30.113 7.521   -23.131 1.00 20.93 ? 164 PRO A CD   1 
ATOM   2275 H HA   . PRO A 1 164 ? 30.035 9.924   -21.248 1.00 25.04 ? 164 PRO A HA   1 
ATOM   2276 H HB2  . PRO A 1 164 ? 27.734 9.526   -22.419 1.00 27.70 ? 164 PRO A HB2  1 
ATOM   2277 H HB3  . PRO A 1 164 ? 29.026 9.989   -23.230 1.00 27.70 ? 164 PRO A HB3  1 
ATOM   2278 H HG2  . PRO A 1 164 ? 28.061 7.345   -22.936 1.00 30.58 ? 164 PRO A HG2  1 
ATOM   2279 H HG3  . PRO A 1 164 ? 28.489 8.064   -24.295 1.00 30.58 ? 164 PRO A HG3  1 
ATOM   2280 H HD2  . PRO A 1 164 ? 30.157 6.553   -23.180 1.00 25.12 ? 164 PRO A HD2  1 
ATOM   2281 H HD3  . PRO A 1 164 ? 30.707 7.900   -23.805 1.00 25.12 ? 164 PRO A HD3  1 
ATOM   2282 N N    . ASN A 1 165 ? 28.356 7.607   -19.816 1.00 17.57 ? 165 ASN A N    1 
ATOM   2283 C CA   . ASN A 1 165 ? 27.371 7.339   -18.771 1.00 17.82 ? 165 ASN A CA   1 
ATOM   2284 C C    . ASN A 1 165 ? 27.969 6.913   -17.448 1.00 16.37 ? 165 ASN A C    1 
ATOM   2285 O O    . ASN A 1 165 ? 27.218 6.549   -16.543 1.00 17.01 ? 165 ASN A O    1 
ATOM   2286 C CB   . ASN A 1 165 ? 26.368 6.300   -19.262 1.00 16.57 ? 165 ASN A CB   1 
ATOM   2287 C CG   . ASN A 1 165 ? 25.696 6.736   -20.522 1.00 18.89 ? 165 ASN A CG   1 
ATOM   2288 O OD1  . ASN A 1 165 ? 25.057 7.777   -20.552 1.00 20.48 ? 165 ASN A OD1  1 
ATOM   2289 N ND2  . ASN A 1 165 ? 25.868 5.963   -21.581 1.00 20.59 ? 165 ASN A ND2  1 
ATOM   2290 H H    . ASN A 1 165 ? 28.736 6.902   -20.131 1.00 21.09 ? 165 ASN A H    1 
ATOM   2291 H HA   . ASN A 1 165 ? 26.895 8.165   -18.597 1.00 21.39 ? 165 ASN A HA   1 
ATOM   2292 H HB2  . ASN A 1 165 ? 26.830 5.465   -19.436 1.00 19.89 ? 165 ASN A HB2  1 
ATOM   2293 H HB3  . ASN A 1 165 ? 25.687 6.167   -18.584 1.00 19.89 ? 165 ASN A HB3  1 
ATOM   2294 H HD21 . ASN A 1 165 ? 25.501 6.172   -22.330 1.00 24.71 ? 165 ASN A HD21 1 
ATOM   2295 H HD22 . ASN A 1 165 ? 26.347 5.251   -21.520 1.00 24.71 ? 165 ASN A HD22 1 
ATOM   2296 N N    . ILE A 1 166 ? 29.281 6.957   -17.305 1.00 15.14 ? 166 ILE A N    1 
ATOM   2297 C CA   . ILE A 1 166 ? 29.964 6.615   -16.068 1.00 14.30 ? 166 ILE A CA   1 
ATOM   2298 C C    . ILE A 1 166 ? 30.612 7.890   -15.547 1.00 15.32 ? 166 ILE A C    1 
ATOM   2299 O O    . ILE A 1 166 ? 31.282 8.608   -16.306 1.00 15.57 ? 166 ILE A O    1 
ATOM   2300 C CB   . ILE A 1 166 ? 31.025 5.533   -16.332 1.00 15.53 ? 166 ILE A CB   1 
ATOM   2301 C CG1  . ILE A 1 166 ? 30.375 4.234   -16.821 1.00 17.08 ? 166 ILE A CG1  1 
ATOM   2302 C CG2  . ILE A 1 166 ? 31.860 5.283   -15.098 1.00 14.03 ? 166 ILE A CG2  1 
ATOM   2303 C CD1  . ILE A 1 166 ? 29.565 3.541   -15.812 1.00 23.48 ? 166 ILE A CD1  1 
ATOM   2304 H H    . ILE A 1 166 ? 29.819 7.190   -17.935 1.00 18.17 ? 166 ILE A H    1 
ATOM   2305 H HA   . ILE A 1 166 ? 29.336 6.288   -15.405 1.00 17.16 ? 166 ILE A HA   1 
ATOM   2306 H HB   . ILE A 1 166 ? 31.610 5.859   -17.034 1.00 18.64 ? 166 ILE A HB   1 
ATOM   2307 H HG12 . ILE A 1 166 ? 29.794 4.442   -17.570 1.00 20.50 ? 166 ILE A HG12 1 
ATOM   2308 H HG13 . ILE A 1 166 ? 31.075 3.625   -17.103 1.00 20.50 ? 166 ILE A HG13 1 
ATOM   2309 H HG21 . ILE A 1 166 ? 32.416 4.502   -15.246 1.00 16.84 ? 166 ILE A HG21 1 
ATOM   2310 H HG22 . ILE A 1 166 ? 32.417 6.059   -14.931 1.00 16.84 ? 166 ILE A HG22 1 
ATOM   2311 H HG23 . ILE A 1 166 ? 31.270 5.131   -14.343 1.00 16.84 ? 166 ILE A HG23 1 
ATOM   2312 H HD11 . ILE A 1 166 ? 29.163 2.756   -16.214 1.00 28.18 ? 166 ILE A HD11 1 
ATOM   2313 H HD12 . ILE A 1 166 ? 30.138 3.279   -15.074 1.00 28.18 ? 166 ILE A HD12 1 
ATOM   2314 H HD13 . ILE A 1 166 ? 28.873 4.142   -15.496 1.00 28.18 ? 166 ILE A HD13 1 
ATOM   2315 N N    . ASP A 1 167 ? 30.409 8.184   -14.256 1.00 14.35 ? 167 ASP A N    1 
ATOM   2316 C CA   . ASP A 1 167 ? 30.875 9.427   -13.660 1.00 14.56 ? 167 ASP A CA   1 
ATOM   2317 C C    . ASP A 1 167 ? 32.132 9.264   -12.834 1.00 14.17 ? 167 ASP A C    1 
ATOM   2318 O O    . ASP A 1 167 ? 32.745 10.273  -12.467 1.00 15.61 ? 167 ASP A O    1 
ATOM   2319 C CB   . ASP A 1 167 ? 29.777 10.031  -12.806 1.00 15.53 ? 167 ASP A CB   1 
ATOM   2320 C CG   . ASP A 1 167 ? 28.582 10.334  -13.619 1.00 17.77 ? 167 ASP A CG   1 
ATOM   2321 O OD1  . ASP A 1 167 ? 28.691 11.212  -14.524 1.00 19.27 ? 167 ASP A OD1  1 
ATOM   2322 O OD2  . ASP A 1 167 ? 27.527 9.703   -13.417 1.00 16.52 ? 167 ASP A OD2  1 
ATOM   2323 H H    . ASP A 1 167 ? 29.997 7.669   -13.704 1.00 17.22 ? 167 ASP A H    1 
ATOM   2324 H HA   . ASP A 1 167 ? 31.080 10.056  -14.370 1.00 17.47 ? 167 ASP A HA   1 
ATOM   2325 H HB2  . ASP A 1 167 ? 29.525 9.402   -12.112 1.00 18.63 ? 167 ASP A HB2  1 
ATOM   2326 H HB3  . ASP A 1 167 ? 30.095 10.856  -12.407 1.00 18.63 ? 167 ASP A HB3  1 
ATOM   2327 N N    . GLY A 1 168 ? 32.531 8.045   -12.528 1.00 13.57 ? 168 GLY A N    1 
ATOM   2328 C CA   . GLY A 1 168 ? 33.695 7.841   -11.695 1.00 13.05 ? 168 GLY A CA   1 
ATOM   2329 C C    . GLY A 1 168 ? 33.855 6.376   -11.359 1.00 12.79 ? 168 GLY A C    1 
ATOM   2330 O O    . GLY A 1 168 ? 33.277 5.495   -12.015 1.00 12.43 ? 168 GLY A O    1 
ATOM   2331 H H    . GLY A 1 168 ? 32.146 7.322   -12.790 1.00 16.29 ? 168 GLY A H    1 
ATOM   2332 H HA2  . GLY A 1 168 ? 34.490 8.145   -12.160 1.00 15.66 ? 168 GLY A HA2  1 
ATOM   2333 H HA3  . GLY A 1 168 ? 33.601 8.343   -10.870 1.00 15.66 ? 168 GLY A HA3  1 
ATOM   2334 N N    . THR A 1 169 ? 34.668 6.132   -10.330 1.00 12.21 ? 169 THR A N    1 
ATOM   2335 C CA   . THR A 1 169 ? 35.037 4.787   -9.967  1.00 12.27 ? 169 THR A CA   1 
ATOM   2336 C C    . THR A 1 169 ? 34.954 4.621   -8.459  1.00 10.92 ? 169 THR A C    1 
ATOM   2337 O O    . THR A 1 169 ? 35.124 5.582   -7.696  1.00 12.08 ? 169 THR A O    1 
ATOM   2338 C CB   . THR A 1 169 ? 36.434 4.434   -10.532 1.00 12.41 ? 169 THR A CB   1 
ATOM   2339 O OG1  . THR A 1 169 ? 36.710 3.061   -10.329 1.00 13.26 ? 169 THR A OG1  1 
ATOM   2340 C CG2  . THR A 1 169 ? 37.508 5.238   -9.898  1.00 13.92 ? 169 THR A CG2  1 
ATOM   2341 H H    . THR A 1 169 ? 35.014 6.741   -9.831  1.00 14.66 ? 169 THR A H    1 
ATOM   2342 H HA   . THR A 1 169 ? 34.413 4.142   -10.336 1.00 14.72 ? 169 THR A HA   1 
ATOM   2343 H HB   . THR A 1 169 ? 36.432 4.632   -11.481 1.00 14.89 ? 169 THR A HB   1 
ATOM   2344 H HG1  . THR A 1 169 ? 36.152 2.591   -10.745 1.00 15.91 ? 169 THR A HG1  1 
ATOM   2345 H HG21 . THR A 1 169 ? 38.358 5.055   -10.328 1.00 16.71 ? 169 THR A HG21 1 
ATOM   2346 H HG22 . THR A 1 169 ? 37.309 6.184   -9.985  1.00 16.71 ? 169 THR A HG22 1 
ATOM   2347 H HG23 . THR A 1 169 ? 37.577 5.016   -8.956  1.00 16.71 ? 169 THR A HG23 1 
ATOM   2348 N N    . PHE A 1 170 ? 34.679 3.386   -8.050  1.00 10.90 ? 170 PHE A N    1 
ATOM   2349 C CA   . PHE A 1 170 ? 34.761 2.978   -6.661  1.00 10.83 ? 170 PHE A CA   1 
ATOM   2350 C C    . PHE A 1 170 ? 35.910 1.984   -6.587  1.00 11.17 ? 170 PHE A C    1 
ATOM   2351 O O    . PHE A 1 170 ? 35.855 0.916   -7.208  1.00 11.51 ? 170 PHE A O    1 
ATOM   2352 C CB   . PHE A 1 170 ? 33.471 2.281   -6.233  1.00 13.71 ? 170 PHE A CB   1 
ATOM   2353 C CG   . PHE A 1 170 ? 33.611 1.421   -5.000  1.00 12.27 ? 170 PHE A CG   1 
ATOM   2354 C CD1  . PHE A 1 170 ? 33.903 1.977   -3.751  1.00 15.58 ? 170 PHE A CD1  1 
ATOM   2355 C CD2  . PHE A 1 170 ? 33.525 0.052   -5.080  1.00 15.98 ? 170 PHE A CD2  1 
ATOM   2356 C CE1  . PHE A 1 170 ? 34.006 1.158   -2.633  1.00 16.92 ? 170 PHE A CE1  1 
ATOM   2357 C CE2  . PHE A 1 170 ? 33.654 -0.744  -3.951  1.00 16.20 ? 170 PHE A CE2  1 
ATOM   2358 C CZ   . PHE A 1 170 ? 33.905 -0.182  -2.760  1.00 15.54 ? 170 PHE A CZ   1 
ATOM   2359 H H    . PHE A 1 170 ? 34.437 2.752   -8.578  1.00 13.09 ? 170 PHE A H    1 
ATOM   2360 H HA   . PHE A 1 170 ? 34.914 3.740   -6.080  1.00 12.99 ? 170 PHE A HA   1 
ATOM   2361 H HB2  . PHE A 1 170 ? 32.800 2.956   -6.045  1.00 16.45 ? 170 PHE A HB2  1 
ATOM   2362 H HB3  . PHE A 1 170 ? 33.172 1.709   -6.957  1.00 16.45 ? 170 PHE A HB3  1 
ATOM   2363 H HD1  . PHE A 1 170 ? 34.028 2.895   -3.669  1.00 18.70 ? 170 PHE A HD1  1 
ATOM   2364 H HD2  . PHE A 1 170 ? 33.377 -0.348  -5.906  1.00 19.18 ? 170 PHE A HD2  1 
ATOM   2365 H HE1  . PHE A 1 170 ? 34.144 1.535   -1.794  1.00 20.30 ? 170 PHE A HE1  1 
ATOM   2366 H HE2  . PHE A 1 170 ? 33.566 -1.668  -4.020  1.00 19.44 ? 170 PHE A HE2  1 
ATOM   2367 H HZ   . PHE A 1 170 ? 34.012 -0.723  -2.011  1.00 18.65 ? 170 PHE A HZ   1 
ATOM   2368 N N    . ILE A 1 171 ? 36.949 2.324   -5.832  1.00 10.45 ? 171 ILE A N    1 
ATOM   2369 C CA   . ILE A 1 171 ? 38.147 1.519   -5.699  1.00 10.32 ? 171 ILE A CA   1 
ATOM   2370 C C    . ILE A 1 171 ? 38.053 0.676   -4.443  1.00 10.39 ? 171 ILE A C    1 
ATOM   2371 O O    . ILE A 1 171 ? 37.878 1.200   -3.337  1.00 11.14 ? 171 ILE A O    1 
ATOM   2372 C CB   . ILE A 1 171 ? 39.421 2.380   -5.681  1.00 12.16 ? 171 ILE A CB   1 
ATOM   2373 C CG1  . ILE A 1 171 ? 39.518 3.278   -6.912  1.00 12.84 ? 171 ILE A CG1  1 
ATOM   2374 C CG2  . ILE A 1 171 ? 40.649 1.471   -5.581  1.00 12.52 ? 171 ILE A CG2  1 
ATOM   2375 C CD1  . ILE A 1 171 ? 39.387 2.569   -8.236  1.00 16.12 ? 171 ILE A CD1  1 
ATOM   2376 H H    . ILE A 1 171 ? 36.980 3.049   -5.370  1.00 12.54 ? 171 ILE A H    1 
ATOM   2377 H HA   . ILE A 1 171 ? 38.188 0.919   -6.460  1.00 12.38 ? 171 ILE A HA   1 
ATOM   2378 H HB   . ILE A 1 171 ? 39.380 2.963   -4.906  1.00 14.59 ? 171 ILE A HB   1 
ATOM   2379 H HG12 . ILE A 1 171 ? 38.809 3.939   -6.866  1.00 15.41 ? 171 ILE A HG12 1 
ATOM   2380 H HG13 . ILE A 1 171 ? 40.382 3.718   -6.904  1.00 15.41 ? 171 ILE A HG13 1 
ATOM   2381 H HG21 . ILE A 1 171 ? 41.449 2.005   -5.707  1.00 15.03 ? 171 ILE A HG21 1 
ATOM   2382 H HG22 . ILE A 1 171 ? 40.664 1.056   -4.704  1.00 15.03 ? 171 ILE A HG22 1 
ATOM   2383 H HG23 . ILE A 1 171 ? 40.594 0.789   -6.269  1.00 15.03 ? 171 ILE A HG23 1 
ATOM   2384 H HD11 . ILE A 1 171 ? 39.589 3.194   -8.950  1.00 19.34 ? 171 ILE A HD11 1 
ATOM   2385 H HD12 . ILE A 1 171 ? 40.010 1.827   -8.260  1.00 19.34 ? 171 ILE A HD12 1 
ATOM   2386 H HD13 . ILE A 1 171 ? 38.479 2.242   -8.330  1.00 19.34 ? 171 ILE A HD13 1 
ATOM   2387 N N    . ASP A 1 172 ? 38.183 -0.631  -4.597  1.00 10.60 ? 172 ASP A N    1 
ATOM   2388 C CA   . ASP A 1 172 ? 38.085 -1.593  -3.510  1.00 11.12 ? 172 ASP A CA   1 
ATOM   2389 C C    . ASP A 1 172 ? 39.426 -2.283  -3.283  1.00 10.27 ? 172 ASP A C    1 
ATOM   2390 O O    . ASP A 1 172 ? 40.286 -2.329  -4.153  1.00 10.32 ? 172 ASP A O    1 
ATOM   2391 C CB   . ASP A 1 172 ? 36.998 -2.626  -3.832  1.00 11.27 ? 172 ASP A CB   1 
ATOM   2392 C CG   . ASP A 1 172 ? 36.450 -3.322  -2.629  1.00 15.16 ? 172 ASP A CG   1 
ATOM   2393 O OD1  . ASP A 1 172 ? 36.706 -2.888  -1.468  1.00 13.32 ? 172 ASP A OD1  1 
ATOM   2394 O OD2  . ASP A 1 172 ? 35.812 -4.383  -2.871  1.00 18.55 ? 172 ASP A OD2  1 
ATOM   2395 H H    . ASP A 1 172 ? 38.334 -1.003  -5.357  1.00 12.72 ? 172 ASP A H    1 
ATOM   2396 H HA   . ASP A 1 172 ? 37.852 -1.141  -2.684  1.00 13.35 ? 172 ASP A HA   1 
ATOM   2397 H HB2  . ASP A 1 172 ? 36.261 -2.176  -4.274  1.00 13.52 ? 172 ASP A HB2  1 
ATOM   2398 H HB3  . ASP A 1 172 ? 37.374 -3.302  -4.418  1.00 13.52 ? 172 ASP A HB3  1 
ATOM   2399 N N    . ALA A 1 173 ? 39.588 -2.793  -2.069  1.00 10.94 ? 173 ALA A N    1 
ATOM   2400 C CA   . ALA A 1 173 ? 40.747 -3.534  -1.564  1.00 9.78  ? 173 ALA A CA   1 
ATOM   2401 C C    . ALA A 1 173 ? 41.936 -2.654  -1.241  1.00 11.55 ? 173 ALA A C    1 
ATOM   2402 O O    . ALA A 1 173 ? 43.057 -3.162  -1.014  1.00 11.99 ? 173 ALA A O    1 
ATOM   2403 C CB   . ALA A 1 173 ? 41.146 -4.703  -2.485  1.00 11.36 ? 173 ALA A CB   1 
ATOM   2404 H H    . ALA A 1 173 ? 38.986 -2.717  -1.459  1.00 13.13 ? 173 ALA A H    1 
ATOM   2405 H HA   . ALA A 1 173 ? 40.479 -3.932  -0.721  1.00 11.74 ? 173 ALA A HA   1 
ATOM   2406 H HB1  . ALA A 1 173 ? 41.902 -5.168  -2.095  1.00 13.64 ? 173 ALA A HB1  1 
ATOM   2407 H HB2  . ALA A 1 173 ? 40.393 -5.309  -2.571  1.00 13.64 ? 173 ALA A HB2  1 
ATOM   2408 H HB3  . ALA A 1 173 ? 41.388 -4.351  -3.356  1.00 13.64 ? 173 ALA A HB3  1 
ATOM   2409 N N    . ASN A 1 174 ? 41.733 -1.351  -1.122  1.00 10.99 ? 174 ASN A N    1 
ATOM   2410 C CA   . ASN A 1 174 ? 42.735 -0.484  -0.505  1.00 11.03 ? 174 ASN A CA   1 
ATOM   2411 C C    . ASN A 1 174 ? 43.201 -1.031  0.836   1.00 11.68 ? 174 ASN A C    1 
ATOM   2412 O O    . ASN A 1 174 ? 44.386 -0.971  1.161   1.00 12.35 ? 174 ASN A O    1 
ATOM   2413 C CB   . ASN A 1 174 ? 42.157 0.911   -0.282  1.00 11.70 ? 174 ASN A CB   1 
ATOM   2414 C CG   . ASN A 1 174 ? 41.332 1.404   -1.443  1.00 10.55 ? 174 ASN A CG   1 
ATOM   2415 O OD1  . ASN A 1 174 ? 41.882 1.911   -2.433  1.00 12.72 ? 174 ASN A OD1  1 
ATOM   2416 N ND2  . ASN A 1 174 ? 40.034 1.190   -1.411  1.00 12.70 ? 174 ASN A ND2  1 
ATOM   2417 H H    . ASN A 1 174 ? 41.026 -0.939  -1.388  1.00 13.19 ? 174 ASN A H    1 
ATOM   2418 H HA   . ASN A 1 174 ? 43.493 -0.430  -1.108  1.00 13.23 ? 174 ASN A HA   1 
ATOM   2419 H HB2  . ASN A 1 174 ? 41.586 0.894   0.502   1.00 14.04 ? 174 ASN A HB2  1 
ATOM   2420 H HB3  . ASN A 1 174 ? 42.886 1.536   -0.148  1.00 14.04 ? 174 ASN A HB3  1 
ATOM   2421 H HD21 . ASN A 1 174 ? 39.538 1.460   -2.060  1.00 15.24 ? 174 ASN A HD21 1 
ATOM   2422 H HD22 . ASN A 1 174 ? 39.682 0.781   -0.742  1.00 15.24 ? 174 ASN A HD22 1 
ATOM   2423 N N    . ILE A 1 175 ? 42.272 -1.524  1.643   1.00 11.20 ? 175 ILE A N    1 
ATOM   2424 C CA   . ILE A 1 175 ? 42.602 -1.973  2.988   1.00 12.17 ? 175 ILE A CA   1 
ATOM   2425 C C    . ILE A 1 175 ? 43.489 -3.203  2.935   1.00 11.77 ? 175 ILE A C    1 
ATOM   2426 O O    . ILE A 1 175 ? 44.391 -3.368  3.750   1.00 12.54 ? 175 ILE A O    1 
ATOM   2427 C CB   . ILE A 1 175 ? 41.311 -2.205  3.783   1.00 11.83 ? 175 ILE A CB   1 
ATOM   2428 C CG1  . ILE A 1 175 ? 40.603 -0.865  4.045   1.00 13.63 ? 175 ILE A CG1  1 
ATOM   2429 C CG2  . ILE A 1 175 ? 41.572 -2.924  5.082   1.00 15.07 ? 175 ILE A CG2  1 
ATOM   2430 C CD1  . ILE A 1 175 ? 39.125 -0.989  4.429   1.00 14.98 ? 175 ILE A CD1  1 
ATOM   2431 H H    . ILE A 1 175 ? 41.442 -1.610  1.436   1.00 13.43 ? 175 ILE A H    1 
ATOM   2432 H HA   . ILE A 1 175 ? 43.107 -1.282  3.445   1.00 14.60 ? 175 ILE A HA   1 
ATOM   2433 H HB   . ILE A 1 175 ? 40.736 -2.772  3.246   1.00 14.19 ? 175 ILE A HB   1 
ATOM   2434 H HG12 . ILE A 1 175 ? 41.057 -0.414  4.774   1.00 16.35 ? 175 ILE A HG12 1 
ATOM   2435 H HG13 . ILE A 1 175 ? 40.652 -0.327  3.240   1.00 16.35 ? 175 ILE A HG13 1 
ATOM   2436 H HG21 . ILE A 1 175 ? 40.783 -2.860  5.642   1.00 18.08 ? 175 ILE A HG21 1 
ATOM   2437 H HG22 . ILE A 1 175 ? 41.769 -3.854  4.894   1.00 18.08 ? 175 ILE A HG22 1 
ATOM   2438 H HG23 . ILE A 1 175 ? 42.328 -2.509  5.526   1.00 18.08 ? 175 ILE A HG23 1 
ATOM   2439 H HD11 . ILE A 1 175 ? 38.754 -0.100  4.548   1.00 17.98 ? 175 ILE A HD11 1 
ATOM   2440 H HD12 . ILE A 1 175 ? 38.652 -1.452  3.720   1.00 17.98 ? 175 ILE A HD12 1 
ATOM   2441 H HD13 . ILE A 1 175 ? 39.054 -1.490  5.256   1.00 17.98 ? 175 ILE A HD13 1 
ATOM   2442 N N    . LYS A 1 176 ? 43.264 -4.076  1.960   1.00 12.14 ? 176 LYS A N    1 
ATOM   2443 C CA   . LYS A 1 176 ? 44.122 -5.247  1.781   1.00 12.55 ? 176 LYS A CA   1 
ATOM   2444 C C    . LYS A 1 176 ? 45.552 -4.862  1.425   1.00 11.99 ? 176 LYS A C    1 
ATOM   2445 O O    . LYS A 1 176 ? 46.502 -5.530  1.859   1.00 13.87 ? 176 LYS A O    1 
ATOM   2446 C CB   . LYS A 1 176 ? 43.528 -6.209  0.763   1.00 13.02 ? 176 LYS A CB   1 
ATOM   2447 C CG   . LYS A 1 176 ? 42.214 -6.822  1.218   1.00 12.56 ? 176 LYS A CG   1 
ATOM   2448 C CD   . LYS A 1 176 ? 41.646 -7.787  0.191   1.00 12.70 ? 176 LYS A CD   1 
ATOM   2449 C CE   . LYS A 1 176 ? 40.415 -8.499  0.691   1.00 15.18 ? 176 LYS A CE   1 
ATOM   2450 N NZ   . LYS A 1 176 ? 39.263 -7.609  0.799   1.00 16.55 ? 176 LYS A NZ   1 
ATOM   2451 H H    . LYS A 1 176 ? 42.624 -4.016  1.388   1.00 14.57 ? 176 LYS A H    1 
ATOM   2452 H HA   . LYS A 1 176 ? 44.160 -5.720  2.627   1.00 15.06 ? 176 LYS A HA   1 
ATOM   2453 H HB2  . LYS A 1 176 ? 43.364 -5.729  -0.064  1.00 15.63 ? 176 LYS A HB2  1 
ATOM   2454 H HB3  . LYS A 1 176 ? 44.158 -6.930  0.608   1.00 15.63 ? 176 LYS A HB3  1 
ATOM   2455 H HG2  . LYS A 1 176 ? 42.359 -7.311  2.043   1.00 15.07 ? 176 LYS A HG2  1 
ATOM   2456 H HG3  . LYS A 1 176 ? 41.565 -6.116  1.360   1.00 15.07 ? 176 LYS A HG3  1 
ATOM   2457 H HD2  . LYS A 1 176 ? 41.405 -7.294  -0.609  1.00 15.24 ? 176 LYS A HD2  1 
ATOM   2458 H HD3  . LYS A 1 176 ? 42.316 -8.456  -0.021  1.00 15.24 ? 176 LYS A HD3  1 
ATOM   2459 H HE2  . LYS A 1 176 ? 40.188 -9.213  0.075   1.00 18.21 ? 176 LYS A HE2  1 
ATOM   2460 H HE3  . LYS A 1 176 ? 40.595 -8.866  1.571   1.00 18.21 ? 176 LYS A HE3  1 
ATOM   2461 H HZ1  . LYS A 1 176 ? 38.559 -8.058  1.105   1.00 19.86 ? 176 LYS A HZ1  1 
ATOM   2462 H HZ2  . LYS A 1 176 ? 39.446 -6.941  1.358   1.00 19.86 ? 176 LYS A HZ2  1 
ATOM   2463 H HZ3  . LYS A 1 176 ? 39.065 -7.270  -0.000  1.00 19.86 ? 176 LYS A HZ3  1 
ATOM   2464 N N    . VAL A 1 177 ? 45.735 -3.790  0.654   1.00 11.71 ? 177 VAL A N    1 
ATOM   2465 C CA   . VAL A 1 177 ? 47.077 -3.277  0.381   1.00 12.31 ? 177 VAL A CA   1 
ATOM   2466 C C    . VAL A 1 177 ? 47.704 -2.681  1.624   1.00 13.00 ? 177 VAL A C    1 
ATOM   2467 O O    . VAL A 1 177 ? 48.892 -2.883  1.882   1.00 13.73 ? 177 VAL A O    1 
ATOM   2468 C CB   . VAL A 1 177 ? 47.030 -2.233  -0.748  1.00 11.80 ? 177 VAL A CB   1 
ATOM   2469 C CG1  . VAL A 1 177 ? 48.360 -1.512  -0.856  1.00 13.50 ? 177 VAL A CG1  1 
ATOM   2470 C CG2  . VAL A 1 177 ? 46.645 -2.871  -2.080  1.00 12.92 ? 177 VAL A CG2  1 
ATOM   2471 H H    . VAL A 1 177 ? 45.103 -3.343  0.279   1.00 14.05 ? 177 VAL A H    1 
ATOM   2472 H HA   . VAL A 1 177 ? 47.622 -4.027  0.097   1.00 14.77 ? 177 VAL A HA   1 
ATOM   2473 H HB   . VAL A 1 177 ? 46.346 -1.580  -0.534  1.00 14.15 ? 177 VAL A HB   1 
ATOM   2474 H HG11 . VAL A 1 177 ? 48.382 -1.014  -1.689  1.00 16.20 ? 177 VAL A HG11 1 
ATOM   2475 H HG12 . VAL A 1 177 ? 48.451 -0.905  -0.105  1.00 16.20 ? 177 VAL A HG12 1 
ATOM   2476 H HG13 . VAL A 1 177 ? 49.076 -2.166  -0.843  1.00 16.20 ? 177 VAL A HG13 1 
ATOM   2477 H HG21 . VAL A 1 177 ? 46.612 -2.182  -2.762  1.00 15.50 ? 177 VAL A HG21 1 
ATOM   2478 H HG22 . VAL A 1 177 ? 47.309 -3.538  -2.314  1.00 15.50 ? 177 VAL A HG22 1 
ATOM   2479 H HG23 . VAL A 1 177 ? 45.774 -3.289  -1.990  1.00 15.50 ? 177 VAL A HG23 1 
ATOM   2480 N N    . LEU A 1 178 ? 46.941 -1.917  2.393   1.00 12.11 ? 178 LEU A N    1 
ATOM   2481 C CA   . LEU A 1 178 ? 47.486 -1.029  3.408   1.00 14.04 ? 178 LEU A CA   1 
ATOM   2482 C C    . LEU A 1 178 ? 47.607 -1.656  4.788   1.00 14.22 ? 178 LEU A C    1 
ATOM   2483 O O    . LEU A 1 178 ? 48.354 -1.124  5.619   1.00 15.92 ? 178 LEU A O    1 
ATOM   2484 C CB   . LEU A 1 178 ? 46.639 0.254   3.470   1.00 13.32 ? 178 LEU A CB   1 
ATOM   2485 C CG   . LEU A 1 178 ? 46.729 1.083   2.174   1.00 15.04 ? 178 LEU A CG   1 
ATOM   2486 C CD1  . LEU A 1 178 ? 45.640 2.162   2.162   1.00 17.01 ? 178 LEU A CD1  1 
ATOM   2487 C CD2  . LEU A 1 178 ? 48.122 1.705   2.003   1.00 19.40 ? 178 LEU A CD2  1 
ATOM   2488 H H    . LEU A 1 178 ? 46.082 -1.894  2.345   1.00 14.54 ? 178 LEU A H    1 
ATOM   2489 H HA   . LEU A 1 178 ? 48.388 -0.781  3.154   1.00 16.84 ? 178 LEU A HA   1 
ATOM   2490 H HB2  . LEU A 1 178 ? 45.710 0.013   3.610   1.00 15.99 ? 178 LEU A HB2  1 
ATOM   2491 H HB3  . LEU A 1 178 ? 46.953 0.805   4.203   1.00 15.99 ? 178 LEU A HB3  1 
ATOM   2492 H HG   . LEU A 1 178 ? 46.586 0.496   1.415   1.00 18.05 ? 178 LEU A HG   1 
ATOM   2493 H HD11 . LEU A 1 178 ? 45.709 2.671   1.339   1.00 20.42 ? 178 LEU A HD11 1 
ATOM   2494 H HD12 . LEU A 1 178 ? 44.771 1.734   2.214   1.00 20.42 ? 178 LEU A HD12 1 
ATOM   2495 H HD13 . LEU A 1 178 ? 45.767 2.747   2.925   1.00 20.42 ? 178 LEU A HD13 1 
ATOM   2496 H HD21 . LEU A 1 178 ? 48.105 2.315   1.249   1.00 23.28 ? 178 LEU A HD21 1 
ATOM   2497 H HD22 . LEU A 1 178 ? 48.354 2.186   2.813   1.00 23.28 ? 178 LEU A HD22 1 
ATOM   2498 H HD23 . LEU A 1 178 ? 48.766 0.998   1.842   1.00 23.28 ? 178 LEU A HD23 1 
ATOM   2499 N N    . VAL A 1 179 ? 46.934 -2.774  5.058   1.00 13.44 ? 179 VAL A N    1 
ATOM   2500 C CA   . VAL A 1 179 ? 47.147 -3.534  6.301   1.00 13.58 ? 179 VAL A CA   1 
ATOM   2501 C C    . VAL A 1 179 ? 48.343 -4.436  6.029   1.00 14.43 ? 179 VAL A C    1 
ATOM   2502 O O    . VAL A 1 179 ? 48.221 -5.354  5.201   1.00 14.02 ? 179 VAL A O    1 
ATOM   2503 C CB   . VAL A 1 179 ? 45.903 -4.357  6.650   1.00 14.17 ? 179 VAL A CB   1 
ATOM   2504 C CG1  . VAL A 1 179 ? 46.173 -5.349  7.739   1.00 15.70 ? 179 VAL A CG1  1 
ATOM   2505 C CG2  . VAL A 1 179 ? 44.738 -3.415  7.053   1.00 16.49 ? 179 VAL A CG2  1 
ATOM   2506 H H    . VAL A 1 179 ? 46.343 -3.119  4.536   1.00 16.13 ? 179 VAL A H    1 
ATOM   2507 H HA   . VAL A 1 179 ? 47.331 -2.946  7.051   1.00 16.29 ? 179 VAL A HA   1 
ATOM   2508 H HB   . VAL A 1 179 ? 45.646 -4.861  5.863   1.00 17.00 ? 179 VAL A HB   1 
ATOM   2509 H HG11 . VAL A 1 179 ? 45.328 -5.676  8.085   1.00 18.84 ? 179 VAL A HG11 1 
ATOM   2510 H HG12 . VAL A 1 179 ? 46.688 -6.086  7.374   1.00 18.84 ? 179 VAL A HG12 1 
ATOM   2511 H HG13 . VAL A 1 179 ? 46.674 -4.914  8.446   1.00 18.84 ? 179 VAL A HG13 1 
ATOM   2512 H HG21 . VAL A 1 179 ? 43.962 -3.951  7.281   1.00 19.79 ? 179 VAL A HG21 1 
ATOM   2513 H HG22 . VAL A 1 179 ? 45.010 -2.885  7.818   1.00 19.79 ? 179 VAL A HG22 1 
ATOM   2514 H HG23 . VAL A 1 179 ? 44.529 -2.833  6.305   1.00 19.79 ? 179 VAL A HG23 1 
ATOM   2515 N N    . PRO A 1 180 ? 49.522 -4.187  6.602   1.00 14.97 ? 180 PRO A N    1 
ATOM   2516 C CA   . PRO A 1 180 ? 50.717 -4.874  6.072   1.00 15.77 ? 180 PRO A CA   1 
ATOM   2517 C C    . PRO A 1 180 ? 50.644 -6.385  6.153   1.00 17.11 ? 180 PRO A C    1 
ATOM   2518 O O    . PRO A 1 180 ? 51.153 -7.059  5.251   1.00 16.38 ? 180 PRO A O    1 
ATOM   2519 C CB   . PRO A 1 180 ? 51.874 -4.290  6.878   1.00 21.16 ? 180 PRO A CB   1 
ATOM   2520 C CG   . PRO A 1 180 ? 51.366 -2.983  7.409   1.00 23.88 ? 180 PRO A CG   1 
ATOM   2521 C CD   . PRO A 1 180 ? 49.871 -3.066  7.499   1.00 19.19 ? 180 PRO A CD   1 
ATOM   2522 H HA   . PRO A 1 180 ? 50.847 -4.622  5.145   1.00 18.92 ? 180 PRO A HA   1 
ATOM   2523 H HB2  . PRO A 1 180 ? 52.106 -4.891  7.603   1.00 25.40 ? 180 PRO A HB2  1 
ATOM   2524 H HB3  . PRO A 1 180 ? 52.642 -4.154  6.301   1.00 25.40 ? 180 PRO A HB3  1 
ATOM   2525 H HG2  . PRO A 1 180 ? 51.746 -2.828  8.288   1.00 28.65 ? 180 PRO A HG2  1 
ATOM   2526 H HG3  . PRO A 1 180 ? 51.627 -2.271  6.804   1.00 28.65 ? 180 PRO A HG3  1 
ATOM   2527 H HD2  . PRO A 1 180 ? 49.592 -3.255  8.409   1.00 23.02 ? 180 PRO A HD2  1 
ATOM   2528 H HD3  . PRO A 1 180 ? 49.463 -2.241  7.192   1.00 23.02 ? 180 PRO A HD3  1 
ATOM   2529 N N    . SER A 1 181 ? 50.002 -6.950  7.175   1.00 16.30 ? 181 SER A N    1 
ATOM   2530 C CA   . SER A 1 181 ? 49.970 -8.398  7.308   1.00 15.90 ? 181 SER A CA   1 
ATOM   2531 C C    . SER A 1 181 ? 49.202 -9.086  6.194   1.00 16.54 ? 181 SER A C    1 
ATOM   2532 O O    . SER A 1 181 ? 49.424 -10.277 5.955   1.00 17.04 ? 181 SER A O    1 
ATOM   2533 C CB   . SER A 1 181 ? 49.401 -8.802  8.668   1.00 16.88 ? 181 SER A CB   1 
ATOM   2534 O OG   . SER A 1 181 ? 48.092 -8.303  8.809   1.00 20.67 ? 181 SER A OG   1 
ATOM   2535 H H    . SER A 1 181 ? 49.585 -6.521  7.793   1.00 19.56 ? 181 SER A H    1 
ATOM   2536 H HA   . SER A 1 181 ? 50.884 -8.718  7.265   1.00 19.08 ? 181 SER A HA   1 
ATOM   2537 H HB2  . SER A 1 181 ? 49.383 -9.769  8.731   1.00 20.26 ? 181 SER A HB2  1 
ATOM   2538 H HB3  . SER A 1 181 ? 49.960 -8.434  9.370   1.00 20.26 ? 181 SER A HB3  1 
ATOM   2539 H HG   . SER A 1 181 ? 48.101 -7.463  8.787   1.00 24.80 ? 181 SER A HG   1 
ATOM   2540 N N    . PHE A 1 182 ? 48.283 -8.396  5.511   1.00 14.75 ? 182 PHE A N    1 
ATOM   2541 C CA   . PHE A 1 182 ? 47.473 -9.094  4.520   1.00 15.37 ? 182 PHE A CA   1 
ATOM   2542 C C    . PHE A 1 182 ? 48.364 -9.689  3.433   1.00 14.73 ? 182 PHE A C    1 
ATOM   2543 O O    . PHE A 1 182 ? 48.294 -10.886 3.138   1.00 15.55 ? 182 PHE A O    1 
ATOM   2544 C CB   . PHE A 1 182 ? 46.373 -8.218  3.924   1.00 15.07 ? 182 PHE A CB   1 
ATOM   2545 C CG   . PHE A 1 182 ? 45.506 -8.965  2.948   1.00 15.42 ? 182 PHE A CG   1 
ATOM   2546 C CD1  . PHE A 1 182 ? 44.377 -9.656  3.382   1.00 16.69 ? 182 PHE A CD1  1 
ATOM   2547 C CD2  . PHE A 1 182 ? 45.853 -9.053  1.626   1.00 15.43 ? 182 PHE A CD2  1 
ATOM   2548 C CE1  . PHE A 1 182 ? 43.616 -10.377 2.475   1.00 17.03 ? 182 PHE A CE1  1 
ATOM   2549 C CE2  . PHE A 1 182 ? 45.098 -9.774  0.735   1.00 14.76 ? 182 PHE A CE2  1 
ATOM   2550 C CZ   . PHE A 1 182 ? 43.990 -10.446 1.162   1.00 15.45 ? 182 PHE A CZ   1 
ATOM   2551 H H    . PHE A 1 182 ? 48.118 -7.557  5.601   1.00 17.70 ? 182 PHE A H    1 
ATOM   2552 H HA   . PHE A 1 182 ? 47.004 -9.811  4.975   1.00 18.44 ? 182 PHE A HA   1 
ATOM   2553 H HB2  . PHE A 1 182 ? 45.807 -7.891  4.640   1.00 18.09 ? 182 PHE A HB2  1 
ATOM   2554 H HB3  . PHE A 1 182 ? 46.781 -7.473  3.456   1.00 18.09 ? 182 PHE A HB3  1 
ATOM   2555 H HD1  . PHE A 1 182 ? 44.134 -9.633  4.279   1.00 20.03 ? 182 PHE A HD1  1 
ATOM   2556 H HD2  . PHE A 1 182 ? 46.616 -8.615  1.326   1.00 18.52 ? 182 PHE A HD2  1 
ATOM   2557 H HE1  . PHE A 1 182 ? 42.847 -10.816 2.762   1.00 20.44 ? 182 PHE A HE1  1 
ATOM   2558 H HE2  . PHE A 1 182 ? 45.342 -9.804  -0.162  1.00 17.71 ? 182 PHE A HE2  1 
ATOM   2559 H HZ   . PHE A 1 182 ? 43.490 -10.950 0.561   1.00 18.54 ? 182 PHE A HZ   1 
ATOM   2560 N N    . PHE A 1 183 ? 49.213 -8.863  2.799   1.00 13.73 ? 183 PHE A N    1 
ATOM   2561 C CA   . PHE A 1 183 ? 50.160 -9.399  1.834   1.00 14.07 ? 183 PHE A CA   1 
ATOM   2562 C C    . PHE A 1 183 ? 51.455 -9.888  2.451   1.00 13.52 ? 183 PHE A C    1 
ATOM   2563 O O    . PHE A 1 183 ? 52.090 -10.791 1.894   1.00 13.57 ? 183 PHE A O    1 
ATOM   2564 C CB   . PHE A 1 183 ? 50.446 -8.388  0.716   1.00 13.12 ? 183 PHE A CB   1 
ATOM   2565 C CG   . PHE A 1 183 ? 49.337 -8.303  -0.292  1.00 13.05 ? 183 PHE A CG   1 
ATOM   2566 C CD1  . PHE A 1 183 ? 48.981 -9.420  -1.053  1.00 13.61 ? 183 PHE A CD1  1 
ATOM   2567 C CD2  . PHE A 1 183 ? 48.621 -7.132  -0.460  1.00 13.10 ? 183 PHE A CD2  1 
ATOM   2568 C CE1  . PHE A 1 183 ? 47.939 -9.373  -1.945  1.00 13.30 ? 183 PHE A CE1  1 
ATOM   2569 C CE2  . PHE A 1 183 ? 47.570 -7.076  -1.361  1.00 13.23 ? 183 PHE A CE2  1 
ATOM   2570 C CZ   . PHE A 1 183 ? 47.231 -8.200  -2.108  1.00 13.69 ? 183 PHE A CZ   1 
ATOM   2571 H H    . PHE A 1 183 ? 49.252 -8.012  2.914   1.00 16.48 ? 183 PHE A H    1 
ATOM   2572 H HA   . PHE A 1 183 ? 49.745 -10.169 1.414   1.00 16.89 ? 183 PHE A HA   1 
ATOM   2573 H HB2  . PHE A 1 183 ? 50.562 -7.509  1.109   1.00 15.74 ? 183 PHE A HB2  1 
ATOM   2574 H HB3  . PHE A 1 183 ? 51.254 -8.654  0.251   1.00 15.74 ? 183 PHE A HB3  1 
ATOM   2575 H HD1  . PHE A 1 183 ? 49.460 -10.211 -0.952  1.00 16.33 ? 183 PHE A HD1  1 
ATOM   2576 H HD2  . PHE A 1 183 ? 48.846 -6.378  0.035   1.00 15.72 ? 183 PHE A HD2  1 
ATOM   2577 H HE1  . PHE A 1 183 ? 47.711 -10.129 -2.437  1.00 15.97 ? 183 PHE A HE1  1 
ATOM   2578 H HE2  . PHE A 1 183 ? 47.090 -6.286  -1.466  1.00 15.88 ? 183 PHE A HE2  1 
ATOM   2579 H HZ   . PHE A 1 183 ? 46.529 -8.161  -2.717  1.00 16.42 ? 183 PHE A HZ   1 
ATOM   2580 N N    . SER A 1 184 ? 51.886 -9.368  3.593   1.00 14.58 ? 184 SER A N    1 
ATOM   2581 C CA   . SER A 1 184 ? 53.167 -9.859  4.097   1.00 15.75 ? 184 SER A CA   1 
ATOM   2582 C C    . SER A 1 184 ? 53.055 -11.318 4.511   1.00 16.06 ? 184 SER A C    1 
ATOM   2583 O O    . SER A 1 184 ? 54.021 -12.063 4.369   1.00 17.52 ? 184 SER A O    1 
ATOM   2584 C CB   . SER A 1 184 ? 53.729 -8.979  5.204   1.00 17.49 ? 184 SER A CB   1 
ATOM   2585 O OG   . SER A 1 184 ? 53.087 -9.217  6.431   1.00 19.83 ? 184 SER A OG   1 
ATOM   2586 H H    . SER A 1 184 ? 51.487 -8.770  4.066   1.00 17.49 ? 184 SER A H    1 
ATOM   2587 H HA   . SER A 1 184 ? 53.826 -9.799  3.388   1.00 18.90 ? 184 SER A HA   1 
ATOM   2588 H HB2  . SER A 1 184 ? 54.675 -9.168  5.304   1.00 20.98 ? 184 SER A HB2  1 
ATOM   2589 H HB3  . SER A 1 184 ? 53.600 -8.049  4.960   1.00 20.98 ? 184 SER A HB3  1 
ATOM   2590 H HG   . SER A 1 184 ? 53.399 -8.709  7.022   1.00 23.80 ? 184 SER A HG   1 
ATOM   2591 N N    . SER A 1 185 ? 51.873 -11.764 4.936   1.00 16.04 ? 185 SER A N    1 
ATOM   2592 C CA   . SER A 1 185 ? 51.657 -13.167 5.253   1.00 18.02 ? 185 SER A CA   1 
ATOM   2593 C C    . SER A 1 185 ? 51.644 -14.067 4.027   1.00 18.26 ? 185 SER A C    1 
ATOM   2594 O O    . SER A 1 185 ? 51.750 -15.295 4.179   1.00 20.58 ? 185 SER A O    1 
ATOM   2595 C CB   . SER A 1 185 ? 50.339 -13.314 6.021   1.00 18.74 ? 185 SER A CB   1 
ATOM   2596 O OG   . SER A 1 185 ? 49.229 -13.012 5.185   1.00 20.68 ? 185 SER A OG   1 
ATOM   2597 H H    . SER A 1 185 ? 51.179 -11.268 5.049   1.00 19.25 ? 185 SER A H    1 
ATOM   2598 H HA   . SER A 1 185 ? 52.380 -13.473 5.822   1.00 21.62 ? 185 SER A HA   1 
ATOM   2599 H HB2  . SER A 1 185 ? 50.258 -14.228 6.336   1.00 22.49 ? 185 SER A HB2  1 
ATOM   2600 H HB3  . SER A 1 185 ? 50.342 -12.702 6.773   1.00 22.49 ? 185 SER A HB3  1 
ATOM   2601 H HG   . SER A 1 185 ? 49.287 -12.223 4.904   1.00 24.81 ? 185 SER A HG   1 
ATOM   2602 N N    . LYS A 1 186 ? 51.530 -13.505 2.830   1.00 16.51 ? 186 LYS A N    1 
ATOM   2603 C CA   . LYS A 1 186 ? 51.492 -14.255 1.589   1.00 14.74 ? 186 LYS A CA   1 
ATOM   2604 C C    . LYS A 1 186 ? 52.800 -14.184 0.823   1.00 15.43 ? 186 LYS A C    1 
ATOM   2605 O O    . LYS A 1 186 ? 53.232 -15.191 0.250   1.00 17.92 ? 186 LYS A O    1 
ATOM   2606 C CB   . LYS A 1 186 ? 50.356 -13.733 0.688   1.00 16.78 ? 186 LYS A CB   1 
ATOM   2607 C CG   . LYS A 1 186 ? 48.968 -13.864 1.304   1.00 17.70 ? 186 LYS A CG   1 
ATOM   2608 C CD   . LYS A 1 186 ? 47.918 -13.133 0.461   1.00 18.88 ? 186 LYS A CD   1 
ATOM   2609 C CE   . LYS A 1 186 ? 46.501 -13.338 0.994   1.00 19.66 ? 186 LYS A CE   1 
ATOM   2610 N NZ   . LYS A 1 186 ? 46.340 -12.909 2.407   1.00 22.71 ? 186 LYS A NZ   1 
ATOM   2611 H H    . LYS A 1 186 ? 51.471 -12.655 2.709   1.00 19.81 ? 186 LYS A H    1 
ATOM   2612 H HA   . LYS A 1 186 ? 51.311 -15.186 1.794   1.00 17.69 ? 186 LYS A HA   1 
ATOM   2613 H HB2  . LYS A 1 186 ? 50.511 -12.793 0.506   1.00 20.14 ? 186 LYS A HB2  1 
ATOM   2614 H HB3  . LYS A 1 186 ? 50.360 -14.236 -0.141  1.00 20.14 ? 186 LYS A HB3  1 
ATOM   2615 H HG2  . LYS A 1 186 ? 48.723 -14.801 1.352   1.00 21.24 ? 186 LYS A HG2  1 
ATOM   2616 H HG3  . LYS A 1 186 ? 48.971 -13.476 2.193   1.00 21.24 ? 186 LYS A HG3  1 
ATOM   2617 H HD2  . LYS A 1 186 ? 48.109 -12.182 0.471   1.00 22.66 ? 186 LYS A HD2  1 
ATOM   2618 H HD3  . LYS A 1 186 ? 47.950 -13.469 -0.448  1.00 22.66 ? 186 LYS A HD3  1 
ATOM   2619 H HE2  . LYS A 1 186 ? 45.884 -12.821 0.453   1.00 23.59 ? 186 LYS A HE2  1 
ATOM   2620 H HE3  . LYS A 1 186 ? 46.278 -14.281 0.941   1.00 23.59 ? 186 LYS A HE3  1 
ATOM   2621 H HZ1  . LYS A 1 186 ? 45.502 -13.047 2.674   1.00 27.25 ? 186 LYS A HZ1  1 
ATOM   2622 H HZ2  . LYS A 1 186 ? 46.890 -13.373 2.931   1.00 27.25 ? 186 LYS A HZ2  1 
ATOM   2623 H HZ3  . LYS A 1 186 ? 46.529 -12.042 2.485   1.00 27.25 ? 186 LYS A HZ3  1 
ATOM   2624 N N    . VAL A 1 187 ? 53.441 -13.013 0.787   1.00 14.45 ? 187 VAL A N    1 
ATOM   2625 C CA   . VAL A 1 187 ? 54.587 -12.767 -0.083  1.00 14.48 ? 187 VAL A CA   1 
ATOM   2626 C C    . VAL A 1 187 ? 55.731 -12.077 0.647   1.00 15.12 ? 187 VAL A C    1 
ATOM   2627 O O    . VAL A 1 187 ? 56.733 -11.719 0.014   1.00 15.21 ? 187 VAL A O    1 
ATOM   2628 C CB   . VAL A 1 187 ? 54.211 -11.987 -1.359  1.00 14.57 ? 187 VAL A CB   1 
ATOM   2629 C CG1  . VAL A 1 187 ? 53.345 -12.867 -2.274  1.00 17.08 ? 187 VAL A CG1  1 
ATOM   2630 C CG2  . VAL A 1 187 ? 53.507 -10.715 -1.026  1.00 14.03 ? 187 VAL A CG2  1 
ATOM   2631 H H    . VAL A 1 187 ? 53.225 -12.334 1.269   1.00 17.34 ? 187 VAL A H    1 
ATOM   2632 H HA   . VAL A 1 187 ? 54.917 -13.628 -0.383  1.00 17.38 ? 187 VAL A HA   1 
ATOM   2633 H HB   . VAL A 1 187 ? 55.023 -11.750 -1.833  1.00 17.49 ? 187 VAL A HB   1 
ATOM   2634 H HG11 . VAL A 1 187 ? 53.159 -12.382 -3.094  1.00 20.49 ? 187 VAL A HG11 1 
ATOM   2635 H HG12 . VAL A 1 187 ? 53.828 -13.684 -2.475  1.00 20.49 ? 187 VAL A HG12 1 
ATOM   2636 H HG13 . VAL A 1 187 ? 52.515 -13.076 -1.818  1.00 20.49 ? 187 VAL A HG13 1 
ATOM   2637 H HG21 . VAL A 1 187 ? 53.311 -10.238 -1.847  1.00 16.84 ? 187 VAL A HG21 1 
ATOM   2638 H HG22 . VAL A 1 187 ? 52.683 -10.924 -0.560  1.00 16.84 ? 187 VAL A HG22 1 
ATOM   2639 H HG23 . VAL A 1 187 ? 54.081 -10.176 -0.459  1.00 16.84 ? 187 VAL A HG23 1 
ATOM   2640 N N    . GLY A 1 188 ? 55.615 -11.853 1.955   1.00 14.91 ? 188 GLY A N    1 
ATOM   2641 C CA   . GLY A 1 188 ? 56.684 -11.286 2.746   1.00 14.69 ? 188 GLY A CA   1 
ATOM   2642 C C    . GLY A 1 188 ? 56.630 -9.769  2.868   1.00 14.12 ? 188 GLY A C    1 
ATOM   2643 O O    . GLY A 1 188 ? 55.915 -9.056  2.159   1.00 14.42 ? 188 GLY A O    1 
ATOM   2644 H H    . GLY A 1 188 ? 54.907 -12.028 2.411   1.00 17.90 ? 188 GLY A H    1 
ATOM   2645 H HA2  . GLY A 1 188 ? 56.645 -11.659 3.641   1.00 17.62 ? 188 GLY A HA2  1 
ATOM   2646 H HA3  . GLY A 1 188 ? 57.534 -11.523 2.343   1.00 17.62 ? 188 GLY A HA3  1 
ATOM   2647 N N    . VAL A 1 189 ? 57.454 -9.282  3.781   1.00 14.53 ? 189 VAL A N    1 
ATOM   2648 C CA   . VAL A 1 189 ? 57.485 -7.877  4.134   1.00 15.45 ? 189 VAL A CA   1 
ATOM   2649 C C    . VAL A 1 189 ? 57.980 -7.015  2.978   1.00 14.96 ? 189 VAL A C    1 
ATOM   2650 O O    . VAL A 1 189 ? 57.409 -5.946  2.703   1.00 14.96 ? 189 VAL A O    1 
ATOM   2651 C CB   . VAL A 1 189 ? 58.337 -7.718  5.410   1.00 17.28 ? 189 VAL A CB   1 
ATOM   2652 C CG1  . VAL A 1 189 ? 58.714 -6.297  5.610   1.00 20.46 ? 189 VAL A CG1  1 
ATOM   2653 C CG2  . VAL A 1 189 ? 57.538 -8.228  6.597   1.00 19.33 ? 189 VAL A CG2  1 
ATOM   2654 H H    . VAL A 1 189 ? 58.020 -9.756  4.222   1.00 17.43 ? 189 VAL A H    1 
ATOM   2655 H HA   . VAL A 1 189 ? 56.584 -7.568  4.317   1.00 18.54 ? 189 VAL A HA   1 
ATOM   2656 H HB   . VAL A 1 189 ? 59.156 -8.231  5.328   1.00 20.73 ? 189 VAL A HB   1 
ATOM   2657 H HG11 . VAL A 1 189 ? 59.022 -6.177  6.522   1.00 24.55 ? 189 VAL A HG11 1 
ATOM   2658 H HG12 . VAL A 1 189 ? 59.423 -6.068  4.988   1.00 24.55 ? 189 VAL A HG12 1 
ATOM   2659 H HG13 . VAL A 1 189 ? 57.938 -5.738  5.446   1.00 24.55 ? 189 VAL A HG13 1 
ATOM   2660 H HG21 . VAL A 1 189 ? 58.064 -8.113  7.404   1.00 23.20 ? 189 VAL A HG21 1 
ATOM   2661 H HG22 . VAL A 1 189 ? 56.714 -7.721  6.664   1.00 23.20 ? 189 VAL A HG22 1 
ATOM   2662 H HG23 . VAL A 1 189 ? 57.338 -9.167  6.463   1.00 23.20 ? 189 VAL A HG23 1 
ATOM   2663 N N    . ASN A 1 190 ? 59.054 -7.427  2.303   1.00 14.35 ? 190 ASN A N    1 
ATOM   2664 C CA   . ASN A 1 190 ? 59.591 -6.603  1.219   1.00 14.53 ? 190 ASN A CA   1 
ATOM   2665 C C    . ASN A 1 190 ? 58.570 -6.403  0.111   1.00 14.85 ? 190 ASN A C    1 
ATOM   2666 O O    . ASN A 1 190 ? 58.361 -5.282  -0.383  1.00 14.66 ? 190 ASN A O    1 
ATOM   2667 C CB   . ASN A 1 190 ? 60.831 -7.252  0.598   1.00 14.99 ? 190 ASN A CB   1 
ATOM   2668 C CG   . ASN A 1 190 ? 61.983 -7.401  1.561   1.00 16.01 ? 190 ASN A CG   1 
ATOM   2669 O OD1  . ASN A 1 190 ? 62.005 -6.785  2.627   1.00 16.89 ? 190 ASN A OD1  1 
ATOM   2670 N ND2  . ASN A 1 190 ? 62.958 -8.236  1.196   1.00 16.86 ? 190 ASN A ND2  1 
ATOM   2671 H H    . ASN A 1 190 ? 59.480 -8.160  2.449   1.00 17.22 ? 190 ASN A H    1 
ATOM   2672 H HA   . ASN A 1 190 ? 59.832 -5.748  1.609   1.00 17.43 ? 190 ASN A HA   1 
ATOM   2673 H HB2  . ASN A 1 190 ? 60.594 -8.138  0.281   1.00 17.99 ? 190 ASN A HB2  1 
ATOM   2674 H HB3  . ASN A 1 190 ? 61.133 -6.704  -0.143  1.00 17.99 ? 190 ASN A HB3  1 
ATOM   2675 H HD21 . ASN A 1 190 ? 63.637 -8.356  1.710   1.00 20.23 ? 190 ASN A HD21 1 
ATOM   2676 H HD22 . ASN A 1 190 ? 62.907 -8.655  0.446   1.00 20.23 ? 190 ASN A HD22 1 
ATOM   2677 N N    . LYS A 1 191 ? 57.943 -7.493  -0.320  1.00 13.12 ? 191 LYS A N    1 
ATOM   2678 C CA   . LYS A 1 191 ? 56.980 -7.413  -1.407  1.00 12.58 ? 191 LYS A CA   1 
ATOM   2679 C C    . LYS A 1 191 ? 55.746 -6.635  -0.987  1.00 13.48 ? 191 LYS A C    1 
ATOM   2680 O O    . LYS A 1 191 ? 55.206 -5.871  -1.789  1.00 12.73 ? 191 LYS A O    1 
ATOM   2681 C CB   . LYS A 1 191 ? 56.632 -8.812  -1.909  1.00 13.08 ? 191 LYS A CB   1 
ATOM   2682 C CG   . LYS A 1 191 ? 55.755 -8.849  -3.141  1.00 13.07 ? 191 LYS A CG   1 
ATOM   2683 C CD   . LYS A 1 191 ? 56.451 -8.334  -4.414  1.00 16.42 ? 191 LYS A CD   1 
ATOM   2684 C CE   . LYS A 1 191 ? 55.611 -8.568  -5.687  1.00 16.38 ? 191 LYS A CE   1 
ATOM   2685 N NZ   . LYS A 1 191 ? 56.434 -8.663  -6.905  1.00 19.65 ? 191 LYS A NZ   1 
ATOM   2686 H H    . LYS A 1 191 ? 58.057 -8.284  -0.003  1.00 15.74 ? 191 LYS A H    1 
ATOM   2687 H HA   . LYS A 1 191 ? 57.377 -6.938  -2.154  1.00 15.09 ? 191 LYS A HA   1 
ATOM   2688 H HB2  . LYS A 1 191 ? 57.457 -9.274  -2.125  1.00 15.69 ? 191 LYS A HB2  1 
ATOM   2689 H HB3  . LYS A 1 191 ? 56.162 -9.283  -1.203  1.00 15.69 ? 191 LYS A HB3  1 
ATOM   2690 H HG2  . LYS A 1 191 ? 55.483 -9.766  -3.303  1.00 15.68 ? 191 LYS A HG2  1 
ATOM   2691 H HG3  . LYS A 1 191 ? 54.974 -8.295  -2.986  1.00 15.68 ? 191 LYS A HG3  1 
ATOM   2692 H HD2  . LYS A 1 191 ? 56.605 -7.380  -4.326  1.00 19.70 ? 191 LYS A HD2  1 
ATOM   2693 H HD3  . LYS A 1 191 ? 57.296 -8.797  -4.522  1.00 19.70 ? 191 LYS A HD3  1 
ATOM   2694 H HE2  . LYS A 1 191 ? 55.118 -9.398  -5.592  1.00 19.66 ? 191 LYS A HE2  1 
ATOM   2695 H HE3  . LYS A 1 191 ? 54.994 -7.827  -5.799  1.00 19.66 ? 191 LYS A HE3  1 
ATOM   2696 H HZ1  . LYS A 1 191 ? 55.913 -8.786  -7.616  1.00 23.58 ? 191 LYS A HZ1  1 
ATOM   2697 H HZ2  . LYS A 1 191 ? 56.902 -7.914  -7.016  1.00 23.58 ? 191 LYS A HZ2  1 
ATOM   2698 H HZ3  . LYS A 1 191 ? 56.998 -9.348  -6.838  1.00 23.58 ? 191 LYS A HZ3  1 
ATOM   2699 N N    . GLN A 1 192 ? 55.283 -6.780  0.255   1.00 13.07 ? 192 GLN A N    1 
ATOM   2700 C CA   . GLN A 1 192 ? 54.160 -5.951  0.682   1.00 12.80 ? 192 GLN A CA   1 
ATOM   2701 C C    . GLN A 1 192 ? 54.499 -4.470  0.563   1.00 12.67 ? 192 GLN A C    1 
ATOM   2702 O O    . GLN A 1 192 ? 53.657 -3.657  0.144   1.00 12.56 ? 192 GLN A O    1 
ATOM   2703 C CB   . GLN A 1 192 ? 53.720 -6.281  2.107   1.00 13.43 ? 192 GLN A CB   1 
ATOM   2704 C CG   . GLN A 1 192 ? 52.420 -5.566  2.527   1.00 13.64 ? 192 GLN A CG   1 
ATOM   2705 C CD   . GLN A 1 192 ? 52.603 -4.106  2.934   1.00 14.92 ? 192 GLN A CD   1 
ATOM   2706 O OE1  . GLN A 1 192 ? 53.679 -3.684  3.394   1.00 15.57 ? 192 GLN A OE1  1 
ATOM   2707 N NE2  . GLN A 1 192 ? 51.546 -3.324  2.810   1.00 14.80 ? 192 GLN A NE2  1 
ATOM   2708 H H    . GLN A 1 192 ? 55.589 -7.327  0.844   1.00 15.68 ? 192 GLN A H    1 
ATOM   2709 H HA   . GLN A 1 192 ? 53.409 -6.152  0.102   1.00 15.36 ? 192 GLN A HA   1 
ATOM   2710 H HB2  . GLN A 1 192 ? 53.570 -7.237  2.175   1.00 16.11 ? 192 GLN A HB2  1 
ATOM   2711 H HB3  . GLN A 1 192 ? 54.421 -6.010  2.721   1.00 16.11 ? 192 GLN A HB3  1 
ATOM   2712 H HG2  . GLN A 1 192 ? 51.801 -5.586  1.781   1.00 16.36 ? 192 GLN A HG2  1 
ATOM   2713 H HG3  . GLN A 1 192 ? 52.040 -6.035  3.286   1.00 16.36 ? 192 GLN A HG3  1 
ATOM   2714 H HE21 . GLN A 1 192 ? 50.805 -3.646  2.513   1.00 17.76 ? 192 GLN A HE21 1 
ATOM   2715 H HE22 . GLN A 1 192 ? 51.597 -2.493  3.025   1.00 17.76 ? 192 GLN A HE22 1 
ATOM   2716 N N    . ALA A 1 193 ? 55.721 -4.094  0.944   1.00 13.65 ? 193 ALA A N    1 
ATOM   2717 C CA   . ALA A 1 193 ? 56.089 -2.683  0.887   1.00 13.91 ? 193 ALA A CA   1 
ATOM   2718 C C    . ALA A 1 193 ? 56.118 -2.188  -0.558  1.00 13.88 ? 193 ALA A C    1 
ATOM   2719 O O    . ALA A 1 193 ? 55.710 -1.048  -0.838  1.00 14.28 ? 193 ALA A O    1 
ATOM   2720 C CB   . ALA A 1 193 ? 57.424 -2.433  1.604   1.00 15.47 ? 193 ALA A CB   1 
ATOM   2721 H H    . ALA A 1 193 ? 56.337 -4.622  1.229   1.00 16.38 ? 193 ALA A H    1 
ATOM   2722 H HA   . ALA A 1 193 ? 55.424 -2.164  1.366   1.00 16.69 ? 193 ALA A HA   1 
ATOM   2723 H HB1  . ALA A 1 193 ? 57.640 -1.489  1.549   1.00 18.56 ? 193 ALA A HB1  1 
ATOM   2724 H HB2  . ALA A 1 193 ? 57.339 -2.700  2.532   1.00 18.56 ? 193 ALA A HB2  1 
ATOM   2725 H HB3  . ALA A 1 193 ? 58.117 -2.957  1.172   1.00 18.56 ? 193 ALA A HB3  1 
ATOM   2726 N N    . GLU A 1 194 ? 56.542 -3.041  -1.497  1.00 13.37 ? 194 GLU A N    1 
ATOM   2727 C CA   . GLU A 1 194 ? 56.565 -2.671  -2.904  1.00 12.27 ? 194 GLU A CA   1 
ATOM   2728 C C    . GLU A 1 194 ? 55.156 -2.572  -3.457  1.00 12.89 ? 194 GLU A C    1 
ATOM   2729 O O    . GLU A 1 194 ? 54.843 -1.646  -4.218  1.00 13.05 ? 194 GLU A O    1 
ATOM   2730 C CB   . GLU A 1 194 ? 57.384 -3.714  -3.655  1.00 14.33 ? 194 GLU A CB   1 
ATOM   2731 C CG   . GLU A 1 194 ? 58.873 -3.585  -3.369  1.00 16.99 ? 194 GLU A CG   1 
ATOM   2732 C CD   . GLU A 1 194 ? 59.661 -4.898  -3.440  1.00 31.02 ? 194 GLU A CD   1 
ATOM   2733 O OE1  . GLU A 1 194 ? 59.163 -5.894  -4.008  1.00 27.96 ? 194 GLU A OE1  1 
ATOM   2734 O OE2  . GLU A 1 194 ? 60.812 -4.915  -2.941  1.00 36.79 ? 194 GLU A OE2  1 
ATOM   2735 H H    . GLU A 1 194 ? 56.821 -3.839  -1.341  1.00 16.05 ? 194 GLU A H    1 
ATOM   2736 H HA   . GLU A 1 194 ? 56.982 -1.804  -3.023  1.00 14.73 ? 194 GLU A HA   1 
ATOM   2737 H HB2  . GLU A 1 194 ? 57.098 -4.600  -3.383  1.00 17.19 ? 194 GLU A HB2  1 
ATOM   2738 H HB3  . GLU A 1 194 ? 57.247 -3.599  -4.608  1.00 17.19 ? 194 GLU A HB3  1 
ATOM   2739 H HG2  . GLU A 1 194 ? 59.260 -2.978  -4.019  1.00 20.39 ? 194 GLU A HG2  1 
ATOM   2740 H HG3  . GLU A 1 194 ? 58.984 -3.227  -2.474  1.00 20.39 ? 194 GLU A HG3  1 
ATOM   2741 N N    . ILE A 1 195 ? 54.275 -3.492  -3.071  1.00 11.82 ? 195 ILE A N    1 
ATOM   2742 C CA   . ILE A 1 195 ? 52.874 -3.394  -3.462  1.00 11.34 ? 195 ILE A CA   1 
ATOM   2743 C C    . ILE A 1 195 ? 52.288 -2.068  -2.992  1.00 11.59 ? 195 ILE A C    1 
ATOM   2744 O O    . ILE A 1 195 ? 51.584 -1.381  -3.738  1.00 12.54 ? 195 ILE A O    1 
ATOM   2745 C CB   . ILE A 1 195 ? 52.067 -4.604  -2.937  1.00 12.08 ? 195 ILE A CB   1 
ATOM   2746 C CG1  . ILE A 1 195 ? 52.495 -5.894  -3.629  1.00 11.82 ? 195 ILE A CG1  1 
ATOM   2747 C CG2  . ILE A 1 195 ? 50.564 -4.374  -3.085  1.00 12.75 ? 195 ILE A CG2  1 
ATOM   2748 C CD1  . ILE A 1 195 ? 51.994 -7.172  -2.961  1.00 13.32 ? 195 ILE A CD1  1 
ATOM   2749 H H    . ILE A 1 195 ? 54.462 -4.178  -2.586  1.00 14.19 ? 195 ILE A H    1 
ATOM   2750 H HA   . ILE A 1 195 ? 52.823 -3.414  -4.430  1.00 13.61 ? 195 ILE A HA   1 
ATOM   2751 H HB   . ILE A 1 195 ? 52.263 -4.694  -1.991  1.00 14.50 ? 195 ILE A HB   1 
ATOM   2752 H HG12 . ILE A 1 195 ? 52.152 -5.886  -4.536  1.00 14.19 ? 195 ILE A HG12 1 
ATOM   2753 H HG13 . ILE A 1 195 ? 53.464 -5.931  -3.641  1.00 14.19 ? 195 ILE A HG13 1 
ATOM   2754 H HG21 . ILE A 1 195 ? 50.095 -5.191  -2.851  1.00 15.29 ? 195 ILE A HG21 1 
ATOM   2755 H HG22 . ILE A 1 195 ? 50.294 -3.656  -2.491  1.00 15.29 ? 195 ILE A HG22 1 
ATOM   2756 H HG23 . ILE A 1 195 ? 50.370 -4.133  -4.004  1.00 15.29 ? 195 ILE A HG23 1 
ATOM   2757 H HD11 . ILE A 1 195 ? 52.408 -7.937  -3.392  1.00 15.98 ? 195 ILE A HD11 1 
ATOM   2758 H HD12 . ILE A 1 195 ? 52.235 -7.153  -2.021  1.00 15.98 ? 195 ILE A HD12 1 
ATOM   2759 H HD13 . ILE A 1 195 ? 51.030 -7.221  -3.054  1.00 15.98 ? 195 ILE A HD13 1 
ATOM   2760 N N    . GLU A 1 196 ? 52.540 -1.702  -1.737  1.00 12.02 ? 196 GLU A N    1 
ATOM   2761 C CA   . GLU A 1 196 ? 52.030 -0.444  -1.205  1.00 12.37 ? 196 GLU A CA   1 
ATOM   2762 C C    . GLU A 1 196 ? 52.575 0.769   -1.946  1.00 12.95 ? 196 GLU A C    1 
ATOM   2763 O O    . GLU A 1 196 ? 51.812 1.689   -2.268  1.00 12.87 ? 196 GLU A O    1 
ATOM   2764 C CB   . GLU A 1 196 ? 52.338 -0.378  0.280   1.00 14.16 ? 196 GLU A CB   1 
ATOM   2765 C CG   . GLU A 1 196 ? 51.783 0.830   0.965   1.00 16.82 ? 196 GLU A CG   1 
ATOM   2766 C CD   . GLU A 1 196 ? 52.086 0.824   2.448   1.00 18.89 ? 196 GLU A CD   1 
ATOM   2767 O OE1  . GLU A 1 196 ? 52.526 1.876   2.980   1.00 22.28 ? 196 GLU A OE1  1 
ATOM   2768 O OE2  . GLU A 1 196 ? 51.881 -0.230  3.084   1.00 19.95 ? 196 GLU A OE2  1 
ATOM   2769 H H    . GLU A 1 196 ? 53.000 -2.162  -1.175  1.00 14.42 ? 196 GLU A H    1 
ATOM   2770 H HA   . GLU A 1 196 ? 51.068 -0.417  -1.324  1.00 14.84 ? 196 GLU A HA   1 
ATOM   2771 H HB2  . GLU A 1 196 ? 51.960 -1.161  0.710   1.00 17.00 ? 196 GLU A HB2  1 
ATOM   2772 H HB3  . GLU A 1 196 ? 53.301 -0.368  0.397   1.00 17.00 ? 196 GLU A HB3  1 
ATOM   2773 H HG2  . GLU A 1 196 ? 52.177 1.627   0.578   1.00 20.18 ? 196 GLU A HG2  1 
ATOM   2774 H HG3  . GLU A 1 196 ? 50.820 0.848   0.852   1.00 20.18 ? 196 GLU A HG3  1 
ATOM   2775 N N    . ASN A 1 197 ? 53.876 0.800   -2.232  1.00 12.57 ? 197 ASN A N    1 
ATOM   2776 C CA   . ASN A 1 197 ? 54.435 1.906   -3.007  1.00 13.47 ? 197 ASN A CA   1 
ATOM   2777 C C    . ASN A 1 197 ? 53.744 2.020   -4.366  1.00 12.59 ? 197 ASN A C    1 
ATOM   2778 O O    . ASN A 1 197 ? 53.409 3.117   -4.831  1.00 13.31 ? 197 ASN A O    1 
ATOM   2779 C CB   . ASN A 1 197 ? 55.950 1.735   -3.209  1.00 15.85 ? 197 ASN A CB   1 
ATOM   2780 C CG   . ASN A 1 197 ? 56.761 1.905   -1.942  1.00 24.02 ? 197 ASN A CG   1 
ATOM   2781 O OD1  . ASN A 1 197 ? 56.350 2.592   -1.018  1.00 28.65 ? 197 ASN A OD1  1 
ATOM   2782 N ND2  . ASN A 1 197 ? 57.931 1.267   -1.900  1.00 31.94 ? 197 ASN A ND2  1 
ATOM   2783 H H    . ASN A 1 197 ? 54.448 0.204   -1.994  1.00 15.09 ? 197 ASN A H    1 
ATOM   2784 H HA   . ASN A 1 197 ? 54.293 2.723   -2.505  1.00 16.17 ? 197 ASN A HA   1 
ATOM   2785 H HB2  . ASN A 1 197 ? 56.120 0.843   -3.551  1.00 19.02 ? 197 ASN A HB2  1 
ATOM   2786 H HB3  . ASN A 1 197 ? 56.257 2.398   -3.847  1.00 19.02 ? 197 ASN A HB3  1 
ATOM   2787 H HD21 . ASN A 1 197 ? 58.187 0.792   -2.570  1.00 38.32 ? 197 ASN A HD21 1 
ATOM   2788 H HD22 . ASN A 1 197 ? 58.430 1.331   -1.203  1.00 38.32 ? 197 ASN A HD22 1 
ATOM   2789 N N    . SER A 1 198 ? 53.564 0.897   -5.032  1.00 12.00 ? 198 SER A N    1 
ATOM   2790 C CA   . SER A 1 198 ? 52.930 0.906   -6.348  1.00 12.03 ? 198 SER A CA   1 
ATOM   2791 C C    . SER A 1 198 ? 51.483 1.363   -6.257  1.00 12.43 ? 198 SER A C    1 
ATOM   2792 O O    . SER A 1 198 ? 50.988 2.114   -7.118  1.00 13.13 ? 198 SER A O    1 
ATOM   2793 C CB   . SER A 1 198 ? 53.019 -0.473  -7.004  1.00 12.27 ? 198 SER A CB   1 
ATOM   2794 O OG   . SER A 1 198 ? 54.370 -0.846  -7.223  1.00 13.69 ? 198 SER A OG   1 
ATOM   2795 H H    . SER A 1 198 ? 53.796 0.117   -4.753  1.00 14.40 ? 198 SER A H    1 
ATOM   2796 H HA   . SER A 1 198 ? 53.411 1.529   -6.915  1.00 14.44 ? 198 SER A HA   1 
ATOM   2797 H HB2  . SER A 1 198 ? 52.602 -1.127  -6.421  1.00 14.72 ? 198 SER A HB2  1 
ATOM   2798 H HB3  . SER A 1 198 ? 52.557 -0.447  -7.856  1.00 14.72 ? 198 SER A HB3  1 
ATOM   2799 H HG   . SER A 1 198 ? 54.773 -0.235  -7.635  1.00 16.43 ? 198 SER A HG   1 
ATOM   2800 N N    . TYR A 1 199 ? 50.768 0.909   -5.222  1.00 12.05 ? 199 TYR A N    1 
ATOM   2801 C CA   . TYR A 1 199 ? 49.399 1.351   -4.960  1.00 12.31 ? 199 TYR A CA   1 
ATOM   2802 C C    . TYR A 1 199 ? 49.319 2.865   -4.897  1.00 12.06 ? 199 TYR A C    1 
ATOM   2803 O O    . TYR A 1 199 ? 48.461 3.493   -5.546  1.00 12.42 ? 199 TYR A O    1 
ATOM   2804 C CB   . TYR A 1 199 ? 48.895 0.684   -3.682  1.00 11.52 ? 199 TYR A CB   1 
ATOM   2805 C CG   . TYR A 1 199 ? 47.620 1.315   -3.141  1.00 10.96 ? 199 TYR A CG   1 
ATOM   2806 C CD1  . TYR A 1 199 ? 46.387 0.947   -3.653  1.00 12.32 ? 199 TYR A CD1  1 
ATOM   2807 C CD2  . TYR A 1 199 ? 47.661 2.287   -2.176  1.00 12.73 ? 199 TYR A CD2  1 
ATOM   2808 C CE1  . TYR A 1 199 ? 45.221 1.550   -3.217  1.00 12.51 ? 199 TYR A CE1  1 
ATOM   2809 C CE2  . TYR A 1 199 ? 46.498 2.895   -1.727  1.00 12.16 ? 199 TYR A CE2  1 
ATOM   2810 C CZ   . TYR A 1 199 ? 45.287 2.516   -2.244  1.00 11.92 ? 199 TYR A CZ   1 
ATOM   2811 O OH   . TYR A 1 199 ? 44.161 3.153   -1.780  1.00 12.78 ? 199 TYR A OH   1 
ATOM   2812 H H    . TYR A 1 199 ? 51.058 0.336   -4.649  1.00 14.46 ? 199 TYR A H    1 
ATOM   2813 H HA   . TYR A 1 199 ? 48.813 1.073   -5.681  1.00 14.77 ? 199 TYR A HA   1 
ATOM   2814 H HB2  . TYR A 1 199 ? 48.711 -0.250  -3.867  1.00 13.82 ? 199 TYR A HB2  1 
ATOM   2815 H HB3  . TYR A 1 199 ? 49.578 0.758   -2.998  1.00 13.82 ? 199 TYR A HB3  1 
ATOM   2816 H HD1  . TYR A 1 199 ? 46.342 0.283   -4.302  1.00 14.78 ? 199 TYR A HD1  1 
ATOM   2817 H HD2  . TYR A 1 199 ? 48.480 2.543   -1.817  1.00 15.28 ? 199 TYR A HD2  1 
ATOM   2818 H HE1  . TYR A 1 199 ? 44.401 1.303   -3.579  1.00 15.02 ? 199 TYR A HE1  1 
ATOM   2819 H HE2  . TYR A 1 199 ? 46.540 3.558   -1.076  1.00 14.59 ? 199 TYR A HE2  1 
ATOM   2820 H HH   . TYR A 1 199 ? 43.491 2.915   -2.227  1.00 15.34 ? 199 TYR A HH   1 
ATOM   2821 N N    . PHE A 1 200 ? 50.199 3.497   -4.115  1.00 11.79 ? 200 PHE A N    1 
ATOM   2822 C CA   . PHE A 1 200 ? 50.112 4.952   -4.018  1.00 12.84 ? 200 PHE A CA   1 
ATOM   2823 C C    . PHE A 1 200 ? 50.446 5.641   -5.333  1.00 12.34 ? 200 PHE A C    1 
ATOM   2824 O O    . PHE A 1 200 ? 49.871 6.682   -5.644  1.00 14.73 ? 200 PHE A O    1 
ATOM   2825 C CB   . PHE A 1 200 ? 50.995 5.452   -2.882  1.00 14.12 ? 200 PHE A CB   1 
ATOM   2826 C CG   . PHE A 1 200 ? 50.410 5.190   -1.514  1.00 13.79 ? 200 PHE A CG   1 
ATOM   2827 C CD1  . PHE A 1 200 ? 49.194 5.728   -1.176  1.00 18.14 ? 200 PHE A CD1  1 
ATOM   2828 C CD2  . PHE A 1 200 ? 51.090 4.436   -0.598  1.00 16.84 ? 200 PHE A CD2  1 
ATOM   2829 C CE1  . PHE A 1 200 ? 48.659 5.520   0.072   1.00 21.02 ? 200 PHE A CE1  1 
ATOM   2830 C CE2  . PHE A 1 200 ? 50.556 4.240   0.681   1.00 18.53 ? 200 PHE A CE2  1 
ATOM   2831 C CZ   . PHE A 1 200 ? 49.335 4.779   0.983   1.00 17.19 ? 200 PHE A CZ   1 
ATOM   2832 H H    . PHE A 1 200 ? 50.823 3.126   -3.655  1.00 14.14 ? 200 PHE A H    1 
ATOM   2833 H HA   . PHE A 1 200 ? 49.198 5.196   -3.804  1.00 15.40 ? 200 PHE A HA   1 
ATOM   2834 H HB2  . PHE A 1 200 ? 51.853 5.002   -2.930  1.00 16.94 ? 200 PHE A HB2  1 
ATOM   2835 H HB3  . PHE A 1 200 ? 51.116 6.409   -2.976  1.00 16.94 ? 200 PHE A HB3  1 
ATOM   2836 H HD1  . PHE A 1 200 ? 48.728 6.237   -1.798  1.00 21.77 ? 200 PHE A HD1  1 
ATOM   2837 H HD2  . PHE A 1 200 ? 51.907 4.054   -0.825  1.00 20.20 ? 200 PHE A HD2  1 
ATOM   2838 H HE1  . PHE A 1 200 ? 47.834 5.889   0.291   1.00 25.23 ? 200 PHE A HE1  1 
ATOM   2839 H HE2  . PHE A 1 200 ? 51.026 3.751   1.318   1.00 22.24 ? 200 PHE A HE2  1 
ATOM   2840 H HZ   . PHE A 1 200 ? 48.964 4.634   1.823   1.00 20.62 ? 200 PHE A HZ   1 
ATOM   2841 N N    . SER A 1 201 ? 51.385 5.101   -6.102  1.00 12.46 ? 201 SER A N    1 
ATOM   2842 C CA   . SER A 1 201 ? 51.646 5.644   -7.430  1.00 14.02 ? 201 SER A CA   1 
ATOM   2843 C C    . SER A 1 201 ? 50.405 5.565   -8.289  1.00 13.11 ? 201 SER A C    1 
ATOM   2844 O O    . SER A 1 201 ? 50.058 6.527   -8.979  1.00 13.92 ? 201 SER A O    1 
ATOM   2845 C CB   . SER A 1 201 ? 52.798 4.867   -8.062  1.00 15.39 ? 201 SER A CB   1 
ATOM   2846 O OG   . SER A 1 201 ? 53.053 5.296   -9.393  1.00 21.99 ? 201 SER A OG   1 
ATOM   2847 H H    . SER A 1 201 ? 51.878 4.431   -5.884  1.00 14.96 ? 201 SER A H    1 
ATOM   2848 H HA   . SER A 1 201 ? 51.904 6.576   -7.366  1.00 16.82 ? 201 SER A HA   1 
ATOM   2849 H HB2  . SER A 1 201 ? 53.598 5.006   -7.530  1.00 18.47 ? 201 SER A HB2  1 
ATOM   2850 H HB3  . SER A 1 201 ? 52.569 3.924   -8.076  1.00 18.47 ? 201 SER A HB3  1 
ATOM   2851 H HG   . SER A 1 201 ? 53.248 6.113   -9.399  1.00 26.39 ? 201 SER A HG   1 
ATOM   2852 N N    . MET A 1 202 ? 49.694 4.444   -8.231  1.00 12.83 ? 202 MET A N    1 
ATOM   2853 C CA   . MET A 1 202 ? 48.439 4.297   -9.006  1.00 12.02 ? 202 MET A CA   1 
ATOM   2854 C C    . MET A 1 202 ? 47.377 5.267   -8.536  1.00 12.61 ? 202 MET A C    1 
ATOM   2855 O O    . MET A 1 202 ? 46.680 5.859   -9.364  1.00 13.05 ? 202 MET A O    1 
ATOM   2856 C CB   . MET A 1 202 ? 47.934 2.849   -8.962  1.00 12.71 ? 202 MET A CB   1 
ATOM   2857 C CG   . MET A 1 202 ? 48.829 1.850   -9.672  1.00 11.37 ? 202 MET A CG   1 
ATOM   2858 S SD   . MET A 1 202 ? 48.636 0.135   -9.122  1.00 14.82 ? 202 MET A SD   1 
ATOM   2859 C CE   . MET A 1 202 ? 47.133 -0.261  -9.999  1.00 18.44 ? 202 MET A CE   1 
ATOM   2860 H H    . MET A 1 202 ? 49.903 3.755   -7.761  1.00 15.40 ? 202 MET A H    1 
ATOM   2861 H HA   . MET A 1 202 ? 48.638 4.493   -9.935  1.00 14.42 ? 202 MET A HA   1 
ATOM   2862 H HB2  . MET A 1 202 ? 47.864 2.573   -8.035  1.00 15.26 ? 202 MET A HB2  1 
ATOM   2863 H HB3  . MET A 1 202 ? 47.061 2.813   -9.385  1.00 15.26 ? 202 MET A HB3  1 
ATOM   2864 H HG2  . MET A 1 202 ? 48.629 1.876   -10.621 1.00 13.64 ? 202 MET A HG2  1 
ATOM   2865 H HG3  . MET A 1 202 ? 49.753 2.102   -9.522  1.00 13.64 ? 202 MET A HG3  1 
ATOM   2866 H HE1  . MET A 1 202 ? 46.903 -1.188  -9.828  1.00 22.13 ? 202 MET A HE1  1 
ATOM   2867 H HE2  . MET A 1 202 ? 46.422 0.320   -9.686  1.00 22.13 ? 202 MET A HE2  1 
ATOM   2868 H HE3  . MET A 1 202 ? 47.277 -0.126  -10.949 1.00 22.13 ? 202 MET A HE3  1 
ATOM   2869 N N    . MET A 1 203 ? 47.211 5.435   -7.228  1.00 12.30 ? 203 MET A N    1 
ATOM   2870 C CA   . MET A 1 203 ? 46.167 6.335   -6.751  1.00 11.92 ? 203 MET A CA   1 
ATOM   2871 C C    . MET A 1 203 ? 46.513 7.771   -7.081  1.00 12.62 ? 203 MET A C    1 
ATOM   2872 O O    . MET A 1 203 ? 45.616 8.568   -7.352  1.00 13.67 ? 203 MET A O    1 
ATOM   2873 C CB   . MET A 1 203 ? 45.979 6.178   -5.232  1.00 12.63 ? 203 MET A CB   1 
ATOM   2874 C CG   . MET A 1 203 ? 45.487 4.772   -4.838  1.00 12.40 ? 203 MET A CG   1 
ATOM   2875 S SD   . MET A 1 203 ? 43.952 4.225   -5.598  1.00 13.71 ? 203 MET A SD   1 
ATOM   2876 C CE   . MET A 1 203 ? 44.553 3.087   -6.868  1.00 15.53 ? 203 MET A CE   1 
ATOM   2877 H H    . MET A 1 203 ? 47.675 5.052   -6.613  1.00 14.75 ? 203 MET A H    1 
ATOM   2878 H HA   . MET A 1 203 ? 45.328 6.095   -7.174  1.00 14.31 ? 203 MET A HA   1 
ATOM   2879 H HB2  . MET A 1 203 ? 46.829 6.334   -4.790  1.00 15.16 ? 203 MET A HB2  1 
ATOM   2880 H HB3  . MET A 1 203 ? 45.323 6.824   -4.926  1.00 15.16 ? 203 MET A HB3  1 
ATOM   2881 H HG2  . MET A 1 203 ? 46.172 4.132   -5.085  1.00 14.88 ? 203 MET A HG2  1 
ATOM   2882 H HG3  . MET A 1 203 ? 45.351 4.758   -3.877  1.00 14.88 ? 203 MET A HG3  1 
ATOM   2883 H HE1  . MET A 1 203 ? 43.795 2.723   -7.351  1.00 18.64 ? 203 MET A HE1  1 
ATOM   2884 H HE2  . MET A 1 203 ? 45.132 3.571   -7.477  1.00 18.64 ? 203 MET A HE2  1 
ATOM   2885 H HE3  . MET A 1 203 ? 45.048 2.370   -6.441  1.00 18.64 ? 203 MET A HE3  1 
ATOM   2886 N N    . SER A 1 204 ? 47.800 8.140   -7.068  1.00 13.53 ? 204 SER A N    1 
ATOM   2887 C CA   . SER A 1 204 ? 48.197 9.475   -7.493  1.00 13.97 ? 204 SER A CA   1 
ATOM   2888 C C    . SER A 1 204 ? 47.835 9.714   -8.950  1.00 14.68 ? 204 SER A C    1 
ATOM   2889 O O    . SER A 1 204 ? 47.368 10.796  -9.315  1.00 15.57 ? 204 SER A O    1 
ATOM   2890 C CB   . SER A 1 204 ? 49.687 9.679   -7.306  1.00 16.94 ? 204 SER A CB   1 
ATOM   2891 O OG   . SER A 1 204 ? 50.002 9.734   -5.932  1.00 24.37 ? 204 SER A OG   1 
ATOM   2892 H H    . SER A 1 204 ? 48.452 7.637   -6.819  1.00 16.23 ? 204 SER A H    1 
ATOM   2893 H HA   . SER A 1 204 ? 47.730 10.118  -6.937  1.00 16.76 ? 204 SER A HA   1 
ATOM   2894 H HB2  . SER A 1 204 ? 50.164 8.938   -7.712  1.00 20.33 ? 204 SER A HB2  1 
ATOM   2895 H HB3  . SER A 1 204 ? 49.950 10.513  -7.727  1.00 20.33 ? 204 SER A HB3  1 
ATOM   2896 H HG   . SER A 1 204 ? 50.830 9.831   -5.830  1.00 29.24 ? 204 SER A HG   1 
ATOM   2897 N N    A ARG A 1 205 ? 48.064 8.715   -9.808  0.49 15.13 ? 205 ARG A N    1 
ATOM   2898 N N    B ARG A 1 205 ? 48.060 8.708   -9.798  0.51 15.12 ? 205 ARG A N    1 
ATOM   2899 C CA   A ARG A 1 205 ? 47.714 8.901   -11.213 0.49 15.67 ? 205 ARG A CA   1 
ATOM   2900 C CA   B ARG A 1 205 ? 47.723 8.838   -11.210 0.51 15.59 ? 205 ARG A CA   1 
ATOM   2901 C C    A ARG A 1 205 ? 46.207 9.056   -11.375 0.49 15.97 ? 205 ARG A C    1 
ATOM   2902 C C    B ARG A 1 205 ? 46.222 9.028   -11.390 0.51 15.97 ? 205 ARG A C    1 
ATOM   2903 O O    A ARG A 1 205 ? 45.749 9.938   -12.108 0.49 16.52 ? 205 ARG A O    1 
ATOM   2904 O O    B ARG A 1 205 ? 45.782 9.916   -12.125 0.51 16.51 ? 205 ARG A O    1 
ATOM   2905 C CB   A ARG A 1 205 ? 48.230 7.757   -12.084 0.49 15.47 ? 205 ARG A CB   1 
ATOM   2906 C CB   B ARG A 1 205 ? 48.225 7.614   -11.975 0.51 15.66 ? 205 ARG A CB   1 
ATOM   2907 C CG   A ARG A 1 205 ? 47.467 7.640   -13.410 0.49 18.75 ? 205 ARG A CG   1 
ATOM   2908 C CG   B ARG A 1 205 ? 49.734 7.567   -12.159 0.51 18.26 ? 205 ARG A CG   1 
ATOM   2909 C CD   A ARG A 1 205 ? 48.321 7.080   -14.521 0.49 18.04 ? 205 ARG A CD   1 
ATOM   2910 C CD   B ARG A 1 205 ? 50.132 8.241   -13.451 0.51 24.63 ? 205 ARG A CD   1 
ATOM   2911 N NE   A ARG A 1 205 ? 47.520 6.605   -15.644 0.49 20.19 ? 205 ARG A NE   1 
ATOM   2912 N NE   B ARG A 1 205 ? 49.607 7.535   -14.614 0.51 23.63 ? 205 ARG A NE   1 
ATOM   2913 C CZ   A ARG A 1 205 ? 48.012 5.893   -16.645 0.49 18.11 ? 205 ARG A CZ   1 
ATOM   2914 C CZ   B ARG A 1 205 ? 50.161 6.461   -15.157 0.51 23.96 ? 205 ARG A CZ   1 
ATOM   2915 N NH1  A ARG A 1 205 ? 49.296 5.586   -16.702 0.49 22.51 ? 205 ARG A NH1  1 
ATOM   2916 N NH1  B ARG A 1 205 ? 51.224 5.886   -14.623 0.51 23.49 ? 205 ARG A NH1  1 
ATOM   2917 N NH2  A ARG A 1 205 ? 47.199 5.490   -17.620 0.49 16.89 ? 205 ARG A NH2  1 
ATOM   2918 N NH2  B ARG A 1 205 ? 49.631 5.949   -16.263 0.51 20.85 ? 205 ARG A NH2  1 
ATOM   2919 H H    A ARG A 1 205 ? 48.407 7.952   -9.608  0.49 18.16 ? 205 ARG A H    1 
ATOM   2920 H H    B ARG A 1 205 ? 48.403 7.950   -9.581  0.51 18.15 ? 205 ARG A H    1 
ATOM   2921 H HA   A ARG A 1 205 ? 48.153 9.707   -11.526 0.49 18.81 ? 205 ARG A HA   1 
ATOM   2922 H HA   B ARG A 1 205 ? 48.167 9.618   -11.579 0.51 18.71 ? 205 ARG A HA   1 
ATOM   2923 H HB2  A ARG A 1 205 ? 49.165 7.911   -12.287 0.49 18.56 ? 205 ARG A HB2  1 
ATOM   2924 H HB2  B ARG A 1 205 ? 47.964 6.816   -11.489 0.51 18.79 ? 205 ARG A HB2  1 
ATOM   2925 H HB3  A ARG A 1 205 ? 48.128 6.921   -11.602 0.49 18.56 ? 205 ARG A HB3  1 
ATOM   2926 H HB3  B ARG A 1 205 ? 47.821 7.612   -12.857 0.51 18.79 ? 205 ARG A HB3  1 
ATOM   2927 H HG2  A ARG A 1 205 ? 46.708 7.048   -13.287 0.49 22.50 ? 205 ARG A HG2  1 
ATOM   2928 H HG2  B ARG A 1 205 ? 50.166 8.030   -11.424 0.51 21.91 ? 205 ARG A HG2  1 
ATOM   2929 H HG3  A ARG A 1 205 ? 47.162 8.520   -13.679 0.49 22.50 ? 205 ARG A HG3  1 
ATOM   2930 H HG3  B ARG A 1 205 ? 50.030 6.644   -12.189 0.51 21.91 ? 205 ARG A HG3  1 
ATOM   2931 H HD2  A ARG A 1 205 ? 48.916 7.774   -14.846 0.49 21.65 ? 205 ARG A HD2  1 
ATOM   2932 H HD2  B ARG A 1 205 ? 49.783 9.145   -13.461 0.51 29.55 ? 205 ARG A HD2  1 
ATOM   2933 H HD3  A ARG A 1 205 ? 48.838 6.333   -14.181 0.49 21.65 ? 205 ARG A HD3  1 
ATOM   2934 H HD3  B ARG A 1 205 ? 51.100 8.258   -13.518 0.51 29.55 ? 205 ARG A HD3  1 
ATOM   2935 H HE   A ARG A 1 205 ? 46.682 6.799   -15.657 0.49 24.23 ? 205 ARG A HE   1 
ATOM   2936 H HE   B ARG A 1 205 ? 48.886 7.837   -14.973 0.51 28.36 ? 205 ARG A HE   1 
ATOM   2937 H HH11 A ARG A 1 205 ? 49.829 5.850   -16.081 0.49 27.01 ? 205 ARG A HH11 1 
ATOM   2938 H HH11 B ARG A 1 205 ? 51.572 6.209   -13.906 0.51 28.18 ? 205 ARG A HH11 1 
ATOM   2939 H HH12 A ARG A 1 205 ? 49.598 5.122   -17.360 0.49 27.01 ? 205 ARG A HH12 1 
ATOM   2940 H HH12 B ARG A 1 205 ? 51.567 5.189   -14.992 0.51 28.18 ? 205 ARG A HH12 1 
ATOM   2941 H HH21 A ARG A 1 205 ? 46.364 5.693   -17.595 0.49 20.27 ? 205 ARG A HH21 1 
ATOM   2942 H HH21 B ARG A 1 205 ? 48.938 6.315   -16.617 0.51 25.02 ? 205 ARG A HH21 1 
ATOM   2943 H HH22 A ARG A 1 205 ? 47.509 5.027   -18.275 0.49 20.27 ? 205 ARG A HH22 1 
ATOM   2944 H HH22 B ARG A 1 205 ? 49.981 5.252   -16.625 0.51 25.02 ? 205 ARG A HH22 1 
ATOM   2945 N N    . LEU A 1 206 ? 45.435 8.210   -10.703 1.00 14.25 ? 206 LEU A N    1 
ATOM   2946 C CA   . LEU A 1 206 ? 43.934 8.317   -10.843 1.00 14.21 ? 206 LEU A CA   1 
ATOM   2947 C C    . LEU A 1 206 ? 43.472 9.648   -10.269 1.00 16.84 ? 206 LEU A C    1 
ATOM   2948 O O    . LEU A 1 206 ? 42.553 10.144  -10.743 1.00 16.12 ? 206 LEU A O    1 
ATOM   2949 C CB   . LEU A 1 206 ? 43.225 7.202   -10.067 1.00 18.83 ? 206 LEU A CB   1 
ATOM   2950 C CG   . LEU A 1 206 ? 43.083 5.822   -10.710 1.00 31.41 ? 206 LEU A CG   1 
ATOM   2951 C CD1  . LEU A 1 206 ? 42.133 4.974   -9.873  1.00 21.37 ? 206 LEU A CD1  1 
ATOM   2952 C CD2  . LEU A 1 206 ? 42.606 5.886   -12.160 1.00 19.11 ? 206 LEU A CD2  1 
ATOM   2953 H H    A LEU A 1 206 ? 46.362 7.992   -10.651 0.49 17.10 ? 206 LEU A H    1 
ATOM   2954 H H    B LEU A 1 206 ? 46.362 7.992   -10.651 0.51 17.10 ? 206 LEU A H    1 
ATOM   2955 H HA   . LEU A 1 206 ? 43.703 8.288   -11.787 1.00 17.05 ? 206 LEU A HA   1 
ATOM   2956 H HB2  . LEU A 1 206 ? 43.702 7.087   -9.221  1.00 22.59 ? 206 LEU A HB2  1 
ATOM   2957 H HB3  . LEU A 1 206 ? 42.329 7.524   -9.846  1.00 22.59 ? 206 LEU A HB3  1 
ATOM   2958 H HG   . LEU A 1 206 ? 43.971 5.389   -10.697 1.00 37.69 ? 206 LEU A HG   1 
ATOM   2959 H HD11 . LEU A 1 206 ? 42.011 4.105   -10.290 1.00 25.64 ? 206 LEU A HD11 1 
ATOM   2960 H HD12 . LEU A 1 206 ? 42.505 4.851   -8.982  1.00 25.64 ? 206 LEU A HD12 1 
ATOM   2961 H HD13 . LEU A 1 206 ? 41.268 5.417   -9.805  1.00 25.64 ? 206 LEU A HD13 1 
ATOM   2962 H HD21 . LEU A 1 206 ? 41.928 6.575   -12.251 1.00 22.93 ? 206 LEU A HD21 1 
ATOM   2963 H HD22 . LEU A 1 206 ? 43.358 6.091   -12.743 1.00 22.93 ? 206 LEU A HD22 1 
ATOM   2964 H HD23 . LEU A 1 206 ? 42.228 5.028   -12.421 1.00 22.93 ? 206 LEU A HD23 1 
ATOM   2965 N N    . LYS A 1 207 ? 44.074 10.161  -9.225  1.00 15.14 ? 207 LYS A N    1 
ATOM   2966 C CA   . LYS A 1 207 ? 43.655 11.455  -8.695  1.00 16.68 ? 207 LYS A CA   1 
ATOM   2967 C C    . LYS A 1 207 ? 43.762 12.548  -9.756  1.00 17.81 ? 207 LYS A C    1 
ATOM   2968 O O    . LYS A 1 207 ? 42.902 13.432  -9.843  1.00 18.96 ? 207 LYS A O    1 
ATOM   2969 C CB   . LYS A 1 207 ? 44.484 11.798  -7.460  1.00 17.36 ? 207 LYS A CB   1 
ATOM   2970 C CG   . LYS A 1 207 ? 44.069 13.114  -6.823  1.00 19.59 ? 207 LYS A CG   1 
ATOM   2971 C CD   . LYS A 1 207 ? 44.952 13.481  -5.642  1.00 21.00 ? 207 LYS A CD   1 
ATOM   2972 C CE   . LYS A 1 207 ? 44.456 14.742  -4.952  1.00 23.32 ? 207 LYS A CE   1 
ATOM   2973 N NZ   . LYS A 1 207 ? 45.411 15.241  -3.917  1.00 33.57 ? 207 LYS A NZ   1 
ATOM   2974 H H    . LYS A 1 207 ? 44.705 9.774   -8.787  1.00 18.17 ? 207 LYS A H    1 
ATOM   2975 H HA   . LYS A 1 207 ? 42.725 11.405  -8.425  1.00 20.02 ? 207 LYS A HA   1 
ATOM   2976 H HB2  . LYS A 1 207 ? 44.373 11.096  -6.800  1.00 20.83 ? 207 LYS A HB2  1 
ATOM   2977 H HB3  . LYS A 1 207 ? 45.417 11.868  -7.715  1.00 20.83 ? 207 LYS A HB3  1 
ATOM   2978 H HG2  . LYS A 1 207 ? 44.136 13.822  -7.482  1.00 23.51 ? 207 LYS A HG2  1 
ATOM   2979 H HG3  . LYS A 1 207 ? 43.155 13.041  -6.506  1.00 23.51 ? 207 LYS A HG3  1 
ATOM   2980 H HD2  . LYS A 1 207 ? 44.944 12.756  -4.997  1.00 25.20 ? 207 LYS A HD2  1 
ATOM   2981 H HD3  . LYS A 1 207 ? 45.857 13.638  -5.954  1.00 25.20 ? 207 LYS A HD3  1 
ATOM   2982 H HE2  . LYS A 1 207 ? 44.339 15.441  -5.615  1.00 27.99 ? 207 LYS A HE2  1 
ATOM   2983 H HE3  . LYS A 1 207 ? 43.611 14.554  -4.516  1.00 27.99 ? 207 LYS A HE3  1 
ATOM   2984 H HZ1  . LYS A 1 207 ? 45.090 15.979  -3.537  1.00 40.29 ? 207 LYS A HZ1  1 
ATOM   2985 H HZ2  . LYS A 1 207 ? 45.529 14.621  -3.289  1.00 40.29 ? 207 LYS A HZ2  1 
ATOM   2986 H HZ3  . LYS A 1 207 ? 46.197 15.426  -4.291  1.00 40.29 ? 207 LYS A HZ3  1 
ATOM   2987 N N    . GLU A 1 208 ? 44.813 12.504  -10.581 1.00 16.90 ? 208 GLU A N    1 
ATOM   2988 C CA   . GLU A 1 208 ? 44.999 13.474  -11.645 1.00 19.82 ? 208 GLU A CA   1 
ATOM   2989 C C    . GLU A 1 208 ? 44.121 13.153  -12.855 1.00 18.45 ? 208 GLU A C    1 
ATOM   2990 O O    . GLU A 1 208 ? 43.435 14.029  -13.386 1.00 20.11 ? 208 GLU A O    1 
ATOM   2991 C CB   . GLU A 1 208 ? 46.480 13.457  -12.031 1.00 21.85 ? 208 GLU A CB   1 
ATOM   2992 C CG   . GLU A 1 208 ? 47.435 13.816  -10.897 1.00 30.60 ? 208 GLU A CG   1 
ATOM   2993 C CD   . GLU A 1 208 ? 48.858 14.030  -11.387 1.00 42.76 ? 208 GLU A CD   1 
ATOM   2994 O OE1  . GLU A 1 208 ? 49.051 14.271  -12.600 1.00 45.85 ? 208 GLU A OE1  1 
ATOM   2995 O OE2  . GLU A 1 208 ? 49.789 13.886  -10.562 1.00 46.81 ? 208 GLU A OE2  1 
ATOM   2996 H H    . GLU A 1 208 ? 45.436 11.913  -10.539 1.00 20.28 ? 208 GLU A H    1 
ATOM   2997 H HA   . GLU A 1 208 ? 44.749 14.360  -11.341 1.00 23.79 ? 208 GLU A HA   1 
ATOM   2998 H HB2  . GLU A 1 208 ? 46.710 12.566  -12.337 1.00 26.22 ? 208 GLU A HB2  1 
ATOM   2999 H HB3  . GLU A 1 208 ? 46.620 14.099  -12.745 1.00 26.22 ? 208 GLU A HB3  1 
ATOM   3000 H HG2  . GLU A 1 208 ? 47.134 14.636  -10.475 1.00 36.72 ? 208 GLU A HG2  1 
ATOM   3001 H HG3  . GLU A 1 208 ? 47.444 13.094  -10.249 1.00 36.72 ? 208 GLU A HG3  1 
ATOM   3002 N N    . SER A 1 209 ? 44.111 11.899  -13.306 1.00 17.14 ? 209 SER A N    1 
ATOM   3003 C CA   . SER A 1 209 ? 43.393 11.615  -14.547 1.00 17.69 ? 209 SER A CA   1 
ATOM   3004 C C    . SER A 1 209 ? 41.882 11.684  -14.372 1.00 16.97 ? 209 SER A C    1 
ATOM   3005 O O    . SER A 1 209 ? 41.158 11.994  -15.332 1.00 18.35 ? 209 SER A O    1 
ATOM   3006 C CB   . SER A 1 209 ? 43.806 10.254  -15.095 1.00 19.91 ? 209 SER A CB   1 
ATOM   3007 O OG   . SER A 1 209 ? 43.444 9.229   -14.201 1.00 20.53 ? 209 SER A OG   1 
ATOM   3008 H H    . SER A 1 209 ? 44.493 11.226  -12.930 1.00 20.57 ? 209 SER A H    1 
ATOM   3009 H HA   . SER A 1 209 ? 43.639 12.289  -15.200 1.00 21.22 ? 209 SER A HA   1 
ATOM   3010 H HB2  . SER A 1 209 ? 43.359 10.106  -15.943 1.00 23.89 ? 209 SER A HB2  1 
ATOM   3011 H HB3  . SER A 1 209 ? 44.767 10.242  -15.219 1.00 23.89 ? 209 SER A HB3  1 
ATOM   3012 H HG   . SER A 1 209 ? 43.683 8.484   -14.506 1.00 24.63 ? 209 SER A HG   1 
ATOM   3013 N N    . LEU A 1 210 ? 41.388 11.426  -13.164 1.00 16.29 ? 210 LEU A N    1 
ATOM   3014 C CA   . LEU A 1 210 ? 39.969 11.485  -12.836 1.00 14.98 ? 210 LEU A CA   1 
ATOM   3015 C C    . LEU A 1 210 ? 39.588 12.748  -12.088 1.00 15.21 ? 210 LEU A C    1 
ATOM   3016 O O    . LEU A 1 210 ? 38.569 12.778  -11.397 1.00 15.70 ? 210 LEU A O    1 
ATOM   3017 C CB   . LEU A 1 210 ? 39.524 10.241  -12.086 1.00 15.95 ? 210 LEU A CB   1 
ATOM   3018 C CG   . LEU A 1 210 ? 39.786 8.912   -12.793 1.00 17.55 ? 210 LEU A CG   1 
ATOM   3019 C CD1  . LEU A 1 210 ? 39.136 7.752   -12.021 1.00 19.52 ? 210 LEU A CD1  1 
ATOM   3020 C CD2  . LEU A 1 210 ? 39.350 8.906   -14.237 1.00 20.08 ? 210 LEU A CD2  1 
ATOM   3021 H H    . LEU A 1 210 ? 41.877 11.206  -12.491 1.00 19.54 ? 210 LEU A H    1 
ATOM   3022 H HA   . LEU A 1 210 ? 39.476 11.496  -13.672 1.00 17.97 ? 210 LEU A HA   1 
ATOM   3023 H HB2  . LEU A 1 210 ? 39.993 10.215  -11.237 1.00 19.13 ? 210 LEU A HB2  1 
ATOM   3024 H HB3  . LEU A 1 210 ? 38.568 10.304  -11.934 1.00 19.13 ? 210 LEU A HB3  1 
ATOM   3025 H HG   . LEU A 1 210 ? 40.747 8.782   -12.806 1.00 21.06 ? 210 LEU A HG   1 
ATOM   3026 H HD11 . LEU A 1 210 ? 39.432 6.912   -12.405 1.00 23.42 ? 210 LEU A HD11 1 
ATOM   3027 H HD12 . LEU A 1 210 ? 39.405 7.803   -11.090 1.00 23.42 ? 210 LEU A HD12 1 
ATOM   3028 H HD13 . LEU A 1 210 ? 38.172 7.827   -12.091 1.00 23.42 ? 210 LEU A HD13 1 
ATOM   3029 H HD21 . LEU A 1 210 ? 39.416 8.002   -14.583 1.00 24.09 ? 210 LEU A HD21 1 
ATOM   3030 H HD22 . LEU A 1 210 ? 38.432 9.215   -14.291 1.00 24.09 ? 210 LEU A HD22 1 
ATOM   3031 H HD23 . LEU A 1 210 ? 39.928 9.497   -14.744 1.00 24.09 ? 210 LEU A HD23 1 
ATOM   3032 N N    . SER A 1 211 ? 40.348 13.832  -12.275 1.00 17.29 ? 211 SER A N    1 
ATOM   3033 C CA   . SER A 1 211 ? 40.085 15.064  -11.527 1.00 18.60 ? 211 SER A CA   1 
ATOM   3034 C C    . SER A 1 211 ? 38.758 15.730  -11.888 1.00 18.43 ? 211 SER A C    1 
ATOM   3035 O O    . SER A 1 211 ? 38.255 16.536  -11.095 1.00 22.11 ? 211 SER A O    1 
ATOM   3036 C CB   . SER A 1 211 ? 41.265 16.016  -11.699 1.00 21.16 ? 211 SER A CB   1 
ATOM   3037 O OG   . SER A 1 211 ? 41.384 16.454  -13.044 1.00 24.96 ? 211 SER A OG   1 
ATOM   3038 H H    . SER A 1 211 ? 41.011 13.880  -12.820 1.00 20.75 ? 211 SER A H    1 
ATOM   3039 H HA   . SER A 1 211 ? 40.013 14.852  -10.583 1.00 22.33 ? 211 SER A HA   1 
ATOM   3040 H HB2  . SER A 1 211 ? 41.131 16.789  -11.129 1.00 25.39 ? 211 SER A HB2  1 
ATOM   3041 H HB3  . SER A 1 211 ? 42.080 15.555  -11.446 1.00 25.39 ? 211 SER A HB3  1 
ATOM   3042 H HG   . SER A 1 211 ? 42.014 17.006  -13.112 1.00 29.95 ? 211 SER A HG   1 
ATOM   3043 N N    . ASN A 1 212 ? 38.171 15.408  -13.036 1.00 17.78 ? 212 ASN A N    1 
ATOM   3044 C CA   . ASN A 1 212 ? 36.849 15.902  -13.422 1.00 21.62 ? 212 ASN A CA   1 
ATOM   3045 C C    . ASN A 1 212 ? 35.769 14.845  -13.246 1.00 18.52 ? 212 ASN A C    1 
ATOM   3046 O O    . ASN A 1 212 ? 34.678 14.958  -13.830 1.00 20.59 ? 212 ASN A O    1 
ATOM   3047 C CB   . ASN A 1 212 ? 36.885 16.422  -14.857 1.00 22.30 ? 212 ASN A CB   1 
ATOM   3048 C CG   . ASN A 1 212 ? 37.835 17.597  -15.021 1.00 27.81 ? 212 ASN A CG   1 
ATOM   3049 O OD1  . ASN A 1 212 ? 37.771 18.560  -14.260 1.00 31.49 ? 212 ASN A OD1  1 
ATOM   3050 N ND2  . ASN A 1 212 ? 38.728 17.510  -16.000 1.00 33.47 ? 212 ASN A ND2  1 
ATOM   3051 H H    . ASN A 1 212 ? 38.526 14.890  -13.624 1.00 21.34 ? 212 ASN A H    1 
ATOM   3052 H HA   . ASN A 1 212 ? 36.613 16.650  -12.851 1.00 25.95 ? 212 ASN A HA   1 
ATOM   3053 H HB2  . ASN A 1 212 ? 37.181 15.711  -15.446 1.00 26.76 ? 212 ASN A HB2  1 
ATOM   3054 H HB3  . ASN A 1 212 ? 35.996 16.715  -15.112 1.00 26.76 ? 212 ASN A HB3  1 
ATOM   3055 H HD21 . ASN A 1 212 ? 39.286 18.151  -16.131 1.00 40.17 ? 212 ASN A HD21 1 
ATOM   3056 H HD22 . ASN A 1 212 ? 38.748 16.813  -16.503 1.00 40.17 ? 212 ASN A HD22 1 
ATOM   3057 N N    . ASN A 1 213 ? 36.055 13.823  -12.458 1.00 15.79 ? 213 ASN A N    1 
ATOM   3058 C CA   . ASN A 1 213 ? 35.186 12.702  -12.184 1.00 15.55 ? 213 ASN A CA   1 
ATOM   3059 C C    . ASN A 1 213 ? 35.202 12.455  -10.680 1.00 14.73 ? 213 ASN A C    1 
ATOM   3060 O O    . ASN A 1 213 ? 35.810 13.208  -9.902  1.00 16.91 ? 213 ASN A O    1 
ATOM   3061 C CB   . ASN A 1 213 ? 35.664 11.475  -12.968 1.00 15.54 ? 213 ASN A CB   1 
ATOM   3062 C CG   . ASN A 1 213 ? 35.500 11.640  -14.448 1.00 18.33 ? 213 ASN A CG   1 
ATOM   3063 O OD1  . ASN A 1 213 ? 36.464 11.899  -15.181 1.00 18.22 ? 213 ASN A OD1  1 
ATOM   3064 N ND2  . ASN A 1 213 ? 34.272 11.477  -14.901 1.00 17.68 ? 213 ASN A ND2  1 
ATOM   3065 H H    . ASN A 1 213 ? 36.805 13.754  -12.041 1.00 18.94 ? 213 ASN A H    1 
ATOM   3066 H HA   . ASN A 1 213 ? 34.273 12.894  -12.447 1.00 18.65 ? 213 ASN A HA   1 
ATOM   3067 H HB2  . ASN A 1 213 ? 36.605 11.327  -12.784 1.00 18.65 ? 213 ASN A HB2  1 
ATOM   3068 H HB3  . ASN A 1 213 ? 35.147 10.702  -12.693 1.00 18.65 ? 213 ASN A HB3  1 
ATOM   3069 H HD21 . ASN A 1 213 ? 34.109 11.558  -15.742 1.00 21.21 ? 213 ASN A HD21 1 
ATOM   3070 H HD22 . ASN A 1 213 ? 33.634 11.289  -14.356 1.00 21.21 ? 213 ASN A HD22 1 
ATOM   3071 N N    . LEU A 1 214 ? 34.527 11.392  -10.251 1.00 14.16 ? 214 LEU A N    1 
ATOM   3072 C CA   . LEU A 1 214 ? 34.472 11.018  -8.849  1.00 13.04 ? 214 LEU A CA   1 
ATOM   3073 C C    . LEU A 1 214 ? 35.306 9.778   -8.582  1.00 13.42 ? 214 LEU A C    1 
ATOM   3074 O O    . LEU A 1 214 ? 35.291 8.814   -9.349  1.00 14.01 ? 214 LEU A O    1 
ATOM   3075 C CB   . LEU A 1 214 ? 33.045 10.733  -8.427  1.00 15.02 ? 214 LEU A CB   1 
ATOM   3076 C CG   . LEU A 1 214 ? 32.150 11.966  -8.419  1.00 16.61 ? 214 LEU A CG   1 
ATOM   3077 C CD1  . LEU A 1 214 ? 30.724 11.552  -8.200  1.00 21.17 ? 214 LEU A CD1  1 
ATOM   3078 C CD2  . LEU A 1 214 ? 32.588 12.932  -7.363  1.00 19.62 ? 214 LEU A CD2  1 
ATOM   3079 H H    . LEU A 1 214 ? 34.086 10.864  -10.767 1.00 16.99 ? 214 LEU A H    1 
ATOM   3080 H HA   . LEU A 1 214 ? 34.833 11.749  -8.323  1.00 15.65 ? 214 LEU A HA   1 
ATOM   3081 H HB2  . LEU A 1 214 ? 32.660 10.091  -9.043  1.00 18.02 ? 214 LEU A HB2  1 
ATOM   3082 H HB3  . LEU A 1 214 ? 33.054 10.367  -7.528  1.00 18.02 ? 214 LEU A HB3  1 
ATOM   3083 H HG   . LEU A 1 214 ? 32.213 12.419  -9.274  1.00 19.93 ? 214 LEU A HG   1 
ATOM   3084 H HD11 . LEU A 1 214 ? 30.162 12.342  -8.201  1.00 25.41 ? 214 LEU A HD11 1 
ATOM   3085 H HD12 . LEU A 1 214 ? 30.456 10.954  -8.916  1.00 25.41 ? 214 LEU A HD12 1 
ATOM   3086 H HD13 . LEU A 1 214 ? 30.655 11.097  -7.346  1.00 25.41 ? 214 LEU A HD13 1 
ATOM   3087 H HD21 . LEU A 1 214 ? 31.935 13.645  -7.297  1.00 23.54 ? 214 LEU A HD21 1 
ATOM   3088 H HD22 . LEU A 1 214 ? 32.655 12.464  -6.516  1.00 23.54 ? 214 LEU A HD22 1 
ATOM   3089 H HD23 . LEU A 1 214 ? 33.453 13.297  -7.608  1.00 23.54 ? 214 LEU A HD23 1 
ATOM   3090 N N    . ILE A 1 215 ? 36.023 9.798   -7.470  1.00 13.02 ? 215 ILE A N    1 
ATOM   3091 C CA   . ILE A 1 215 ? 36.762 8.640   -6.977  1.00 13.59 ? 215 ILE A CA   1 
ATOM   3092 C C    . ILE A 1 215 ? 36.307 8.378   -5.545  1.00 11.33 ? 215 ILE A C    1 
ATOM   3093 O O    . ILE A 1 215 ? 36.579 9.184   -4.639  1.00 12.52 ? 215 ILE A O    1 
ATOM   3094 C CB   . ILE A 1 215 ? 38.280 8.832   -7.007  1.00 14.97 ? 215 ILE A CB   1 
ATOM   3095 C CG1  . ILE A 1 215 ? 38.760 9.447   -8.312  1.00 16.67 ? 215 ILE A CG1  1 
ATOM   3096 C CG2  . ILE A 1 215 ? 38.928 7.481   -6.777  1.00 17.06 ? 215 ILE A CG2  1 
ATOM   3097 C CD1  . ILE A 1 215 ? 40.292 9.724   -8.320  1.00 21.24 ? 215 ILE A CD1  1 
ATOM   3098 H H    . ILE A 1 215 ? 36.100 10.490  -6.966  1.00 15.62 ? 215 ILE A H    1 
ATOM   3099 H HA   . ILE A 1 215 ? 36.535 7.879   -7.534  1.00 16.31 ? 215 ILE A HA   1 
ATOM   3100 H HB   . ILE A 1 215 ? 38.530 9.456   -6.308  1.00 17.96 ? 215 ILE A HB   1 
ATOM   3101 H HG12 . ILE A 1 215 ? 38.562 8.838   -9.040  1.00 20.01 ? 215 ILE A HG12 1 
ATOM   3102 H HG13 . ILE A 1 215 ? 38.302 10.291  -8.451  1.00 20.01 ? 215 ILE A HG13 1 
ATOM   3103 H HG21 . ILE A 1 215 ? 39.889 7.598   -6.713  1.00 20.47 ? 215 ILE A HG21 1 
ATOM   3104 H HG22 . ILE A 1 215 ? 38.585 7.103   -5.952  1.00 20.47 ? 215 ILE A HG22 1 
ATOM   3105 H HG23 . ILE A 1 215 ? 38.715 6.897   -7.521  1.00 20.47 ? 215 ILE A HG23 1 
ATOM   3106 H HD11 . ILE A 1 215 ? 40.492 10.370  -9.015  1.00 25.49 ? 215 ILE A HD11 1 
ATOM   3107 H HD12 . ILE A 1 215 ? 40.553 10.077  -7.455  1.00 25.49 ? 215 ILE A HD12 1 
ATOM   3108 H HD13 . ILE A 1 215 ? 40.762 8.893   -8.494  1.00 25.49 ? 215 ILE A HD13 1 
ATOM   3109 N N    . LEU A 1 216 ? 35.649 7.257   -5.338  1.00 11.94 ? 216 LEU A N    1 
ATOM   3110 C CA   . LEU A 1 216 ? 35.214 6.808   -4.022  1.00 11.85 ? 216 LEU A CA   1 
ATOM   3111 C C    . LEU A 1 216 ? 36.044 5.587   -3.669  1.00 11.79 ? 216 LEU A C    1 
ATOM   3112 O O    . LEU A 1 216 ? 36.259 4.731   -4.523  1.00 14.02 ? 216 LEU A O    1 
ATOM   3113 C CB   . LEU A 1 216 ? 33.759 6.390   -4.108  1.00 13.99 ? 216 LEU A CB   1 
ATOM   3114 C CG   . LEU A 1 216 ? 32.980 5.963   -2.871  1.00 14.29 ? 216 LEU A CG   1 
ATOM   3115 C CD1  . LEU A 1 216 ? 32.821 7.128   -1.884  1.00 15.31 ? 216 LEU A CD1  1 
ATOM   3116 C CD2  . LEU A 1 216 ? 31.606 5.403   -3.232  1.00 17.54 ? 216 LEU A CD2  1 
ATOM   3117 H H    . LEU A 1 216 ? 35.431 6.713   -5.968  1.00 14.33 ? 216 LEU A H    1 
ATOM   3118 H HA   . LEU A 1 216 ? 35.321 7.496   -3.346  1.00 14.22 ? 216 LEU A HA   1 
ATOM   3119 H HB2  . LEU A 1 216 ? 33.272 7.143   -4.479  1.00 16.78 ? 216 LEU A HB2  1 
ATOM   3120 H HB3  . LEU A 1 216 ? 33.719 5.636   -4.717  1.00 16.78 ? 216 LEU A HB3  1 
ATOM   3121 H HG   . LEU A 1 216 ? 33.488 5.259   -2.439  1.00 17.15 ? 216 LEU A HG   1 
ATOM   3122 H HD11 . LEU A 1 216 ? 32.298 6.828   -1.124  1.00 18.37 ? 216 LEU A HD11 1 
ATOM   3123 H HD12 . LEU A 1 216 ? 33.699 7.415   -1.589  1.00 18.37 ? 216 LEU A HD12 1 
ATOM   3124 H HD13 . LEU A 1 216 ? 32.366 7.860   -2.330  1.00 18.37 ? 216 LEU A HD13 1 
ATOM   3125 H HD21 . LEU A 1 216 ? 31.144 5.150   -2.418  1.00 21.05 ? 216 LEU A HD21 1 
ATOM   3126 H HD22 . LEU A 1 216 ? 31.100 6.085   -3.701  1.00 21.05 ? 216 LEU A HD22 1 
ATOM   3127 H HD23 . LEU A 1 216 ? 31.721 4.627   -3.802  1.00 21.05 ? 216 LEU A HD23 1 
ATOM   3128 N N    . ALA A 1 217 ? 36.533 5.491   -2.439  1.00 12.25 ? 217 ALA A N    1 
ATOM   3129 C CA   . ALA A 1 217 ? 37.357 4.357   -2.062  1.00 11.74 ? 217 ALA A CA   1 
ATOM   3130 C C    . ALA A 1 217 ? 36.861 3.723   -0.769  1.00 11.48 ? 217 ALA A C    1 
ATOM   3131 O O    . ALA A 1 217 ? 36.419 4.419   0.158   1.00 12.22 ? 217 ALA A O    1 
ATOM   3132 C CB   . ALA A 1 217 ? 38.817 4.777   -1.930  1.00 16.34 ? 217 ALA A CB   1 
ATOM   3133 H H    . ALA A 1 217 ? 36.400 6.066   -1.814  1.00 14.70 ? 217 ALA A H    1 
ATOM   3134 H HA   . ALA A 1 217 ? 37.288 3.671   -2.744  1.00 14.08 ? 217 ALA A HA   1 
ATOM   3135 H HB1  . ALA A 1 217 ? 39.352 3.997   -1.716  1.00 19.61 ? 217 ALA A HB1  1 
ATOM   3136 H HB2  . ALA A 1 217 ? 39.113 5.160   -2.771  1.00 19.61 ? 217 ALA A HB2  1 
ATOM   3137 H HB3  . ALA A 1 217 ? 38.893 5.435   -1.221  1.00 19.61 ? 217 ALA A HB3  1 
ATOM   3138 N N    . ASN A 1 218 ? 36.973 2.402   -0.694  1.00 12.06 ? 218 ASN A N    1 
ATOM   3139 C CA   . ASN A 1 218 ? 36.685 1.671   0.555   1.00 11.96 ? 218 ASN A CA   1 
ATOM   3140 C C    . ASN A 1 218 ? 37.893 1.825   1.468   1.00 11.34 ? 218 ASN A C    1 
ATOM   3141 O O    . ASN A 1 218 ? 38.843 1.058   1.374   1.00 12.01 ? 218 ASN A O    1 
ATOM   3142 C CB   . ASN A 1 218 ? 36.432 0.214   0.203   1.00 11.93 ? 218 ASN A CB   1 
ATOM   3143 C CG   . ASN A 1 218 ? 36.127 -0.642  1.379   1.00 10.85 ? 218 ASN A CG   1 
ATOM   3144 O OD1  . ASN A 1 218 ? 35.910 -0.118  2.488   1.00 12.50 ? 218 ASN A OD1  1 
ATOM   3145 N ND2  . ASN A 1 218 ? 36.106 -1.930  1.185   1.00 12.42 ? 218 ASN A ND2  1 
ATOM   3146 H H    . ASN A 1 218 ? 37.214 1.898   -1.348  1.00 14.47 ? 218 ASN A H    1 
ATOM   3147 H HA   . ASN A 1 218 ? 35.911 2.035   1.013   1.00 14.35 ? 218 ASN A HA   1 
ATOM   3148 H HB2  . ASN A 1 218 ? 35.676 0.166   -0.402  1.00 14.31 ? 218 ASN A HB2  1 
ATOM   3149 H HB3  . ASN A 1 218 ? 37.225 -0.145  -0.226  1.00 14.31 ? 218 ASN A HB3  1 
ATOM   3150 H HD21 . ASN A 1 218 ? 35.933 -2.461  1.840   1.00 14.90 ? 218 ASN A HD21 1 
ATOM   3151 H HD22 . ASN A 1 218 ? 36.266 -2.249  0.403   1.00 14.90 ? 218 ASN A HD22 1 
ATOM   3152 N N    . ILE A 1 219 ? 37.838 2.804   2.376   1.00 11.82 ? 219 ILE A N    1 
ATOM   3153 C CA   . ILE A 1 219 ? 39.011 3.219   3.150   1.00 13.65 ? 219 ILE A CA   1 
ATOM   3154 C C    . ILE A 1 219 ? 38.789 3.245   4.662   1.00 11.94 ? 219 ILE A C    1 
ATOM   3155 O O    . ILE A 1 219 ? 39.644 2.779   5.411   1.00 14.79 ? 219 ILE A O    1 
ATOM   3156 C CB   . ILE A 1 219 ? 39.496 4.618   2.675   1.00 17.70 ? 219 ILE A CB   1 
ATOM   3157 C CG1  . ILE A 1 219 ? 40.097 4.495   1.274   1.00 23.41 ? 219 ILE A CG1  1 
ATOM   3158 C CG2  . ILE A 1 219 ? 40.437 5.267   3.721   1.00 20.81 ? 219 ILE A CG2  1 
ATOM   3159 C CD1  . ILE A 1 219 ? 41.477 3.971   1.261   1.00 20.78 ? 219 ILE A CD1  1 
ATOM   3160 H H    . ILE A 1 219 ? 37.126 3.248   2.564   1.00 14.18 ? 219 ILE A H    1 
ATOM   3161 H HA   . ILE A 1 219 ? 39.679 2.532   3.000   1.00 16.38 ? 219 ILE A HA   1 
ATOM   3162 H HB   . ILE A 1 219 ? 38.744 5.227   2.604   1.00 21.24 ? 219 ILE A HB   1 
ATOM   3163 H HG12 . ILE A 1 219 ? 39.547 3.891   0.751   1.00 28.09 ? 219 ILE A HG12 1 
ATOM   3164 H HG13 . ILE A 1 219 ? 40.110 5.373   0.862   1.00 28.09 ? 219 ILE A HG13 1 
ATOM   3165 H HG21 . ILE A 1 219 ? 40.763 6.111   3.372   1.00 24.97 ? 219 ILE A HG21 1 
ATOM   3166 H HG22 . ILE A 1 219 ? 39.942 5.417   4.541   1.00 24.97 ? 219 ILE A HG22 1 
ATOM   3167 H HG23 . ILE A 1 219 ? 41.183 4.669   3.889   1.00 24.97 ? 219 ILE A HG23 1 
ATOM   3168 H HD11 . ILE A 1 219 ? 41.775 3.888   0.341   1.00 24.93 ? 219 ILE A HD11 1 
ATOM   3169 H HD12 . ILE A 1 219 ? 42.053 4.587   1.740   1.00 24.93 ? 219 ILE A HD12 1 
ATOM   3170 H HD13 . ILE A 1 219 ? 41.490 3.103   1.692   1.00 24.93 ? 219 ILE A HD13 1 
ATOM   3171 N N    . ILE A 1 220 ? 37.698 3.832   5.134   1.00 10.88 ? 220 ILE A N    1 
ATOM   3172 C CA   . ILE A 1 220 ? 37.536 4.023   6.572   1.00 11.68 ? 220 ILE A CA   1 
ATOM   3173 C C    . ILE A 1 220 ? 37.102 2.716   7.212   1.00 12.56 ? 220 ILE A C    1 
ATOM   3174 O O    . ILE A 1 220 ? 36.046 2.164   6.893   1.00 12.25 ? 220 ILE A O    1 
ATOM   3175 C CB   . ILE A 1 220 ? 36.549 5.139   6.886   1.00 12.92 ? 220 ILE A CB   1 
ATOM   3176 C CG1  . ILE A 1 220 ? 37.043 6.494   6.363   1.00 15.43 ? 220 ILE A CG1  1 
ATOM   3177 C CG2  . ILE A 1 220 ? 36.342 5.215   8.422   1.00 14.77 ? 220 ILE A CG2  1 
ATOM   3178 C CD1  . ILE A 1 220 ? 36.020 7.594   6.505   1.00 14.82 ? 220 ILE A CD1  1 
ATOM   3179 H H    . ILE A 1 220 ? 37.048 4.123   4.652   1.00 13.06 ? 220 ILE A H    1 
ATOM   3180 H HA   . ILE A 1 220 ? 38.399 4.267   6.942   1.00 14.02 ? 220 ILE A HA   1 
ATOM   3181 H HB   . ILE A 1 220 ? 35.711 4.937   6.441   1.00 15.51 ? 220 ILE A HB   1 
ATOM   3182 H HG12 . ILE A 1 220 ? 37.833 6.754   6.861   1.00 18.52 ? 220 ILE A HG12 1 
ATOM   3183 H HG13 . ILE A 1 220 ? 37.258 6.407   5.421   1.00 18.52 ? 220 ILE A HG13 1 
ATOM   3184 H HG21 . ILE A 1 220 ? 35.784 5.982   8.628   1.00 17.73 ? 220 ILE A HG21 1 
ATOM   3185 H HG22 . ILE A 1 220 ? 35.909 4.401   8.723   1.00 17.73 ? 220 ILE A HG22 1 
ATOM   3186 H HG23 . ILE A 1 220 ? 37.206 5.310   8.853   1.00 17.73 ? 220 ILE A HG23 1 
ATOM   3187 H HD11 . ILE A 1 220 ? 36.245 8.315   5.896   1.00 17.79 ? 220 ILE A HD11 1 
ATOM   3188 H HD12 . ILE A 1 220 ? 35.143 7.240   6.289   1.00 17.79 ? 220 ILE A HD12 1 
ATOM   3189 H HD13 . ILE A 1 220 ? 36.031 7.918   7.419   1.00 17.79 ? 220 ILE A HD13 1 
ATOM   3190 N N    . ARG A 1 221 ? 37.921 2.225   8.146   1.00 12.31 ? 221 ARG A N    1 
ATOM   3191 C CA   . ARG A 1 221 ? 37.639 1.000   8.903   1.00 11.60 ? 221 ARG A CA   1 
ATOM   3192 C C    . ARG A 1 221 ? 38.520 1.060   10.132  1.00 12.64 ? 221 ARG A C    1 
ATOM   3193 O O    . ARG A 1 221 ? 39.719 1.338   10.026  1.00 13.81 ? 221 ARG A O    1 
ATOM   3194 C CB   . ARG A 1 221 ? 37.965 -0.250  8.058   1.00 14.39 ? 221 ARG A CB   1 
ATOM   3195 C CG   . ARG A 1 221 ? 37.724 -1.611  8.761   1.00 13.11 ? 221 ARG A CG   1 
ATOM   3196 C CD   . ARG A 1 221 ? 36.258 -1.890  8.920   1.00 13.72 ? 221 ARG A CD   1 
ATOM   3197 N NE   . ARG A 1 221 ? 35.927 -3.116  9.646   1.00 14.84 ? 221 ARG A NE   1 
ATOM   3198 C CZ   . ARG A 1 221 ? 35.597 -4.267  9.084   1.00 13.21 ? 221 ARG A CZ   1 
ATOM   3199 N NH1  . ARG A 1 221 ? 35.577 -4.417  7.768   1.00 14.07 ? 221 ARG A NH1  1 
ATOM   3200 N NH2  . ARG A 1 221 ? 35.256 -5.295  9.862   1.00 15.07 ? 221 ARG A NH2  1 
ATOM   3201 H H    . ARG A 1 221 ? 38.667 2.592   8.367   1.00 14.77 ? 221 ARG A H    1 
ATOM   3202 H HA   . ARG A 1 221 ? 36.706 0.945   9.163   1.00 13.92 ? 221 ARG A HA   1 
ATOM   3203 H HB2  . ARG A 1 221 ? 37.411 -0.235  7.262   1.00 17.26 ? 221 ARG A HB2  1 
ATOM   3204 H HB3  . ARG A 1 221 ? 38.902 -0.215  7.810   1.00 17.26 ? 221 ARG A HB3  1 
ATOM   3205 H HG2  . ARG A 1 221 ? 38.115 -2.322  8.230   1.00 15.73 ? 221 ARG A HG2  1 
ATOM   3206 H HG3  . ARG A 1 221 ? 38.129 -1.594  9.642   1.00 15.73 ? 221 ARG A HG3  1 
ATOM   3207 H HD2  . ARG A 1 221 ? 35.857 -1.151  9.404   1.00 16.46 ? 221 ARG A HD2  1 
ATOM   3208 H HD3  . ARG A 1 221 ? 35.863 -1.962  8.037   1.00 16.46 ? 221 ARG A HD3  1 
ATOM   3209 H HE   . ARG A 1 221 ? 35.948 -3.086  10.506  1.00 17.80 ? 221 ARG A HE   1 
ATOM   3210 H HH11 . ARG A 1 221 ? 35.781 -3.756  7.257   1.00 16.88 ? 221 ARG A HH11 1 
ATOM   3211 H HH12 . ARG A 1 221 ? 35.359 -5.175  7.425   1.00 16.88 ? 221 ARG A HH12 1 
ATOM   3212 H HH21 . ARG A 1 221 ? 35.253 -5.204  10.718  1.00 18.09 ? 221 ARG A HH21 1 
ATOM   3213 H HH22 . ARG A 1 221 ? 35.040 -6.048  9.509   1.00 18.09 ? 221 ARG A HH22 1 
ATOM   3214 N N    . VAL A 1 222 ? 37.932 0.815   11.294  1.00 12.29 ? 222 VAL A N    1 
ATOM   3215 C CA   . VAL A 1 222 ? 38.698 0.846   12.537  1.00 13.36 ? 222 VAL A CA   1 
ATOM   3216 C C    . VAL A 1 222 ? 39.709 -0.294  12.524  1.00 14.31 ? 222 VAL A C    1 
ATOM   3217 O O    . VAL A 1 222 ? 39.347 -1.466  12.410  1.00 15.01 ? 222 VAL A O    1 
ATOM   3218 C CB   . VAL A 1 222 ? 37.766 0.776   13.759  1.00 13.12 ? 222 VAL A CB   1 
ATOM   3219 C CG1  . VAL A 1 222 ? 38.571 0.652   15.035  1.00 15.08 ? 222 VAL A CG1  1 
ATOM   3220 C CG2  . VAL A 1 222 ? 36.898 2.014   13.815  1.00 15.36 ? 222 VAL A CG2  1 
ATOM   3221 H H    . VAL A 1 222 ? 37.098 0.630   11.392  1.00 14.75 ? 222 VAL A H    1 
ATOM   3222 H HA   . VAL A 1 222 ? 39.192 1.679   12.588  1.00 16.03 ? 222 VAL A HA   1 
ATOM   3223 H HB   . VAL A 1 222 ? 37.198 -0.006  13.678  1.00 15.74 ? 222 VAL A HB   1 
ATOM   3224 H HG11 . VAL A 1 222 ? 37.981 0.781   15.794  1.00 18.10 ? 222 VAL A HG11 1 
ATOM   3225 H HG12 . VAL A 1 222 ? 38.969 -0.232  15.072  1.00 18.10 ? 222 VAL A HG12 1 
ATOM   3226 H HG13 . VAL A 1 222 ? 39.267 1.328   15.037  1.00 18.10 ? 222 VAL A HG13 1 
ATOM   3227 H HG21 . VAL A 1 222 ? 36.281 1.934   14.559  1.00 18.43 ? 222 VAL A HG21 1 
ATOM   3228 H HG22 . VAL A 1 222 ? 37.464 2.792   13.938  1.00 18.43 ? 222 VAL A HG22 1 
ATOM   3229 H HG23 . VAL A 1 222 ? 36.405 2.092   12.984  1.00 18.43 ? 222 VAL A HG23 1 
ATOM   3230 N N    . ARG A 1 223 ? 40.997 0.056   12.669  1.00 14.20 ? 223 ARG A N    1 
ATOM   3231 C CA   . ARG A 1 223 ? 42.133 -0.885  12.531  1.00 16.65 ? 223 ARG A CA   1 
ATOM   3232 C C    . ARG A 1 223 ? 43.207 -0.429  13.501  1.00 15.34 ? 223 ARG A C    1 
ATOM   3233 O O    . ARG A 1 223 ? 43.516 0.766   13.521  1.00 16.20 ? 223 ARG A O    1 
ATOM   3234 C CB   . ARG A 1 223 ? 42.773 -0.883  11.120  1.00 16.97 ? 223 ARG A CB   1 
ATOM   3235 C CG   . ARG A 1 223 ? 41.888 -1.227  9.946   1.00 23.65 ? 223 ARG A CG   1 
ATOM   3236 C CD   . ARG A 1 223 ? 41.737 -2.726  9.733   1.00 23.12 ? 223 ARG A CD   1 
ATOM   3237 N NE   . ARG A 1 223 ? 42.876 -3.559  10.121  1.00 18.78 ? 223 ARG A NE   1 
ATOM   3238 C CZ   . ARG A 1 223 ? 42.839 -4.877  10.056  1.00 16.30 ? 223 ARG A CZ   1 
ATOM   3239 N NH1  . ARG A 1 223 ? 41.759 -5.496  9.595   1.00 19.70 ? 223 ARG A NH1  1 
ATOM   3240 N NH2  . ARG A 1 223 ? 43.876 -5.579  10.460  1.00 18.40 ? 223 ARG A NH2  1 
ATOM   3241 H H    . ARG A 1 223 ? 41.251 0.856   12.854  1.00 17.04 ? 223 ARG A H    1 
ATOM   3242 H HA   . ARG A 1 223 ? 41.813 -1.778  12.730  1.00 19.98 ? 223 ARG A HA   1 
ATOM   3243 H HB2  . ARG A 1 223 ? 43.121 0.007   10.954  1.00 20.36 ? 223 ARG A HB2  1 
ATOM   3244 H HB3  . ARG A 1 223 ? 43.497 -1.528  11.122  1.00 20.36 ? 223 ARG A HB3  1 
ATOM   3245 H HG2  . ARG A 1 223 ? 41.005 -0.857  10.097  1.00 28.38 ? 223 ARG A HG2  1 
ATOM   3246 H HG3  . ARG A 1 223 ? 42.273 -0.849  9.140   1.00 28.38 ? 223 ARG A HG3  1 
ATOM   3247 H HD2  . ARG A 1 223 ? 40.975 -3.029  10.251  1.00 27.75 ? 223 ARG A HD2  1 
ATOM   3248 H HD3  . ARG A 1 223 ? 41.579 -2.882  8.789   1.00 27.75 ? 223 ARG A HD3  1 
ATOM   3249 H HE   . ARG A 1 223 ? 43.594 -3.177  10.401  1.00 22.53 ? 223 ARG A HE   1 
ATOM   3250 H HH11 . ARG A 1 223 ? 41.078 -5.038  9.337   1.00 23.64 ? 223 ARG A HH11 1 
ATOM   3251 H HH12 . ARG A 1 223 ? 41.739 -6.355  9.555   1.00 23.64 ? 223 ARG A HH12 1 
ATOM   3252 H HH21 . ARG A 1 223 ? 44.574 -5.179  10.765  1.00 22.07 ? 223 ARG A HH21 1 
ATOM   3253 H HH22 . ARG A 1 223 ? 43.856 -6.438  10.420  1.00 22.07 ? 223 ARG A HH22 1 
ATOM   3254 N N    . PRO A 1 224 ? 43.880 -1.346  14.208  1.00 17.01 ? 224 PRO A N    1 
ATOM   3255 C CA   . PRO A 1 224 ? 45.038 -0.922  15.014  1.00 16.47 ? 224 PRO A CA   1 
ATOM   3256 C C    . PRO A 1 224 ? 46.201 -0.449  14.171  1.00 17.72 ? 224 PRO A C    1 
ATOM   3257 O O    . PRO A 1 224 ? 46.994 0.384   14.628  1.00 20.08 ? 224 PRO A O    1 
ATOM   3258 C CB   . PRO A 1 224 ? 45.374 -2.158  15.856  1.00 21.13 ? 224 PRO A CB   1 
ATOM   3259 C CG   . PRO A 1 224 ? 44.810 -3.296  15.106  1.00 23.44 ? 224 PRO A CG   1 
ATOM   3260 C CD   . PRO A 1 224 ? 43.601 -2.785  14.346  1.00 20.04 ? 224 PRO A CD   1 
ATOM   3261 H HA   . PRO A 1 224 ? 44.782 -0.211  15.622  1.00 19.76 ? 224 PRO A HA   1 
ATOM   3262 H HB2  . PRO A 1 224 ? 46.336 -2.244  15.947  1.00 25.35 ? 224 PRO A HB2  1 
ATOM   3263 H HB3  . PRO A 1 224 ? 44.963 -2.082  16.732  1.00 25.35 ? 224 PRO A HB3  1 
ATOM   3264 H HG2  . PRO A 1 224 ? 45.478 -3.636  14.489  1.00 28.13 ? 224 PRO A HG2  1 
ATOM   3265 H HG3  . PRO A 1 224 ? 44.548 -3.992  15.728  1.00 28.13 ? 224 PRO A HG3  1 
ATOM   3266 H HD2  . PRO A 1 224 ? 43.535 -3.210  13.476  1.00 24.04 ? 224 PRO A HD2  1 
ATOM   3267 H HD3  . PRO A 1 224 ? 42.787 -2.934  14.851  1.00 24.04 ? 224 PRO A HD3  1 
ATOM   3268 N N    . GLU A 1 225 ? 46.303 -0.909  12.923  1.00 17.02 ? 225 GLU A N    1 
ATOM   3269 C CA   . GLU A 1 225 ? 47.419 -0.504  12.078  1.00 18.59 ? 225 GLU A CA   1 
ATOM   3270 C C    . GLU A 1 225 ? 47.269 0.898   11.515  1.00 20.99 ? 225 GLU A C    1 
ATOM   3271 O O    . GLU A 1 225 ? 48.255 1.437   10.995  1.00 26.05 ? 225 GLU A O    1 
ATOM   3272 C CB   . GLU A 1 225 ? 47.568 -1.460  10.894  1.00 21.39 ? 225 GLU A CB   1 
ATOM   3273 C CG   . GLU A 1 225 ? 47.733 -2.909  11.267  1.00 20.60 ? 225 GLU A CG   1 
ATOM   3274 C CD   . GLU A 1 225 ? 46.439 -3.658  11.388  1.00 19.91 ? 225 GLU A CD   1 
ATOM   3275 O OE1  . GLU A 1 225 ? 45.365 -3.037  11.511  1.00 20.71 ? 225 GLU A OE1  1 
ATOM   3276 O OE2  . GLU A 1 225 ? 46.503 -4.897  11.325  1.00 24.84 ? 225 GLU A OE2  1 
ATOM   3277 H H    . GLU A 1 225 ? 45.747 -1.449  12.550  1.00 20.42 ? 225 GLU A H    1 
ATOM   3278 H HA   . GLU A 1 225 ? 48.219 -0.539  12.624  1.00 22.31 ? 225 GLU A HA   1 
ATOM   3279 H HB2  . GLU A 1 225 ? 46.774 -1.391  10.341  1.00 25.67 ? 225 GLU A HB2  1 
ATOM   3280 H HB3  . GLU A 1 225 ? 48.351 -1.199  10.385  1.00 25.67 ? 225 GLU A HB3  1 
ATOM   3281 H HG2  . GLU A 1 225 ? 48.265 -3.347  10.584  1.00 24.72 ? 225 GLU A HG2  1 
ATOM   3282 H HG3  . GLU A 1 225 ? 48.185 -2.960  12.123  1.00 24.72 ? 225 GLU A HG3  1 
ATOM   3283 N N    . PHE A 1 226 ? 46.073 1.480   11.573  1.00 17.65 ? 226 PHE A N    1 
ATOM   3284 C CA   . PHE A 1 226 ? 45.804 2.793   10.984  1.00 17.12 ? 226 PHE A CA   1 
ATOM   3285 C C    . PHE A 1 226 ? 45.598 3.779   12.136  1.00 18.66 ? 226 PHE A C    1 
ATOM   3286 O O    . PHE A 1 226 ? 44.558 3.745   12.816  1.00 17.15 ? 226 PHE A O    1 
ATOM   3287 C CB   . PHE A 1 226 ? 44.524 2.836   10.154  1.00 17.65 ? 226 PHE A CB   1 
ATOM   3288 C CG   . PHE A 1 226 ? 44.510 1.980   8.896   1.00 17.23 ? 226 PHE A CG   1 
ATOM   3289 C CD1  . PHE A 1 226 ? 45.638 1.385   8.367   1.00 22.93 ? 226 PHE A CD1  1 
ATOM   3290 C CD2  . PHE A 1 226 ? 43.304 1.805   8.278   1.00 18.49 ? 226 PHE A CD2  1 
ATOM   3291 C CE1  . PHE A 1 226 ? 45.525 0.602   7.200   1.00 20.86 ? 226 PHE A CE1  1 
ATOM   3292 C CE2  . PHE A 1 226 ? 43.188 1.051   7.131   1.00 21.66 ? 226 PHE A CE2  1 
ATOM   3293 C CZ   . PHE A 1 226 ? 44.289 0.445   6.607   1.00 22.36 ? 226 PHE A CZ   1 
ATOM   3294 H H    . PHE A 1 226 ? 45.388 1.127   11.954  1.00 21.18 ? 226 PHE A H    1 
ATOM   3295 H HA   . PHE A 1 226 ? 46.566 3.009   10.424  1.00 20.55 ? 226 PHE A HA   1 
ATOM   3296 H HB2  . PHE A 1 226 ? 43.791 2.534   10.713  1.00 21.19 ? 226 PHE A HB2  1 
ATOM   3297 H HB3  . PHE A 1 226 ? 44.374 3.753   9.876   1.00 21.19 ? 226 PHE A HB3  1 
ATOM   3298 H HD1  . PHE A 1 226 ? 46.465 1.501   8.777   1.00 27.51 ? 226 PHE A HD1  1 
ATOM   3299 H HD2  . PHE A 1 226 ? 42.546 2.204   8.640   1.00 22.19 ? 226 PHE A HD2  1 
ATOM   3300 H HE1  . PHE A 1 226 ? 46.276 0.195   6.833   1.00 25.03 ? 226 PHE A HE1  1 
ATOM   3301 H HE2  . PHE A 1 226 ? 42.361 0.956   6.717   1.00 26.00 ? 226 PHE A HE2  1 
ATOM   3302 H HZ   . PHE A 1 226 ? 44.207 -0.079  5.843   1.00 26.83 ? 226 PHE A HZ   1 
ATOM   3303 N N    . GLU A 1 227 ? 46.556 4.685   12.330  1.00 21.04 ? 227 GLU A N    1 
ATOM   3304 C CA   . GLU A 1 227 ? 46.456 5.645   13.422  1.00 21.72 ? 227 GLU A CA   1 
ATOM   3305 C C    . GLU A 1 227 ? 45.163 6.445   13.357  1.00 21.06 ? 227 GLU A C    1 
ATOM   3306 O O    . GLU A 1 227 ? 44.557 6.755   14.388  1.00 20.78 ? 227 GLU A O    1 
ATOM   3307 C CB   . GLU A 1 227 ? 47.652 6.587   13.364  1.00 29.39 ? 227 GLU A CB   1 
ATOM   3308 C CG   . GLU A 1 227 ? 47.906 7.313   14.650  1.00 38.20 ? 227 GLU A CG   1 
ATOM   3309 C CD   . GLU A 1 227 ? 48.569 6.426   15.680  1.00 44.01 ? 227 GLU A CD   1 
ATOM   3310 O OE1  . GLU A 1 227 ? 49.801 6.235   15.584  1.00 48.86 ? 227 GLU A OE1  1 
ATOM   3311 O OE2  . GLU A 1 227 ? 47.868 5.945   16.597  1.00 44.79 ? 227 GLU A OE2  1 
ATOM   3312 H H    . GLU A 1 227 ? 47.265 4.763   11.849  1.00 25.25 ? 227 GLU A H    1 
ATOM   3313 H HA   . GLU A 1 227 ? 46.463 5.164   14.264  1.00 26.07 ? 227 GLU A HA   1 
ATOM   3314 H HB2  . GLU A 1 227 ? 48.446 6.072   13.152  1.00 35.26 ? 227 GLU A HB2  1 
ATOM   3315 H HB3  . GLU A 1 227 ? 47.493 7.251   12.675  1.00 35.26 ? 227 GLU A HB3  1 
ATOM   3316 H HG2  . GLU A 1 227 ? 48.489 8.069   14.480  1.00 45.84 ? 227 GLU A HG2  1 
ATOM   3317 H HG3  . GLU A 1 227 ? 47.061 7.620   15.015  1.00 45.84 ? 227 GLU A HG3  1 
ATOM   3318 N N    . GLU A 1 228 ? 44.715 6.787   12.155  1.00 16.75 ? 228 GLU A N    1 
ATOM   3319 C CA   . GLU A 1 228 ? 43.494 7.562   11.984  1.00 17.83 ? 228 GLU A CA   1 
ATOM   3320 C C    . GLU A 1 228 ? 42.369 6.753   11.328  1.00 16.11 ? 228 GLU A C    1 
ATOM   3321 O O    . GLU A 1 228 ? 41.426 7.340   10.786  1.00 16.66 ? 228 GLU A O    1 
ATOM   3322 C CB   . GLU A 1 228 ? 43.770 8.843   11.209  1.00 19.46 ? 228 GLU A CB   1 
ATOM   3323 C CG   . GLU A 1 228 ? 44.856 9.739   11.811  1.00 24.70 ? 228 GLU A CG   1 
ATOM   3324 C CD   . GLU A 1 228 ? 45.190 10.897  10.888  1.00 38.36 ? 228 GLU A CD   1 
ATOM   3325 O OE1  . GLU A 1 228 ? 46.376 11.057  10.527  1.00 45.21 ? 228 GLU A OE1  1 
ATOM   3326 O OE2  . GLU A 1 228 ? 44.261 11.669  10.550  1.00 44.25 ? 228 GLU A OE2  1 
ATOM   3327 H H    . GLU A 1 228 ? 45.105 6.580   11.417  1.00 20.10 ? 228 GLU A H    1 
ATOM   3328 H HA   . GLU A 1 228 ? 43.179 7.822   12.863  1.00 21.40 ? 228 GLU A HA   1 
ATOM   3329 H HB2  . GLU A 1 228 ? 44.054 8.604   10.312  1.00 23.35 ? 228 GLU A HB2  1 
ATOM   3330 H HB3  . GLU A 1 228 ? 42.952 9.362   11.171  1.00 23.35 ? 228 GLU A HB3  1 
ATOM   3331 H HG2  . GLU A 1 228 ? 44.543 10.101  12.655  1.00 29.64 ? 228 GLU A HG2  1 
ATOM   3332 H HG3  . GLU A 1 228 ? 45.662 9.218   11.952  1.00 29.64 ? 228 GLU A HG3  1 
ATOM   3333 N N    . ASN A 1 229 ? 42.437 5.415   11.377  1.00 15.30 ? 229 ASN A N    1 
ATOM   3334 C CA   . ASN A 1 229 ? 41.354 4.543   10.909  1.00 13.88 ? 229 ASN A CA   1 
ATOM   3335 C C    . ASN A 1 229 ? 40.949 4.777   9.453   1.00 13.11 ? 229 ASN A C    1 
ATOM   3336 O O    . ASN A 1 229 ? 39.802 4.539   9.078   1.00 13.62 ? 229 ASN A O    1 
ATOM   3337 C CB   . ASN A 1 229 ? 40.172 4.607   11.868  1.00 14.10 ? 229 ASN A CB   1 
ATOM   3338 C CG   . ASN A 1 229 ? 40.544 4.043   13.201  1.00 13.93 ? 229 ASN A CG   1 
ATOM   3339 O OD1  . ASN A 1 229 ? 41.305 3.065   13.295  1.00 15.14 ? 229 ASN A OD1  1 
ATOM   3340 N ND2  . ASN A 1 229 ? 40.069 4.666   14.262  1.00 15.41 ? 229 ASN A ND2  1 
ATOM   3341 H H    . ASN A 1 229 ? 43.114 4.981   11.682  1.00 18.36 ? 229 ASN A H    1 
ATOM   3342 H HA   . ASN A 1 229 ? 41.683 3.631   10.907  1.00 16.66 ? 229 ASN A HA   1 
ATOM   3343 H HB2  . ASN A 1 229 ? 39.901 5.530   11.988  1.00 16.92 ? 229 ASN A HB2  1 
ATOM   3344 H HB3  . ASN A 1 229 ? 39.435 4.089   11.509  1.00 16.92 ? 229 ASN A HB3  1 
ATOM   3345 H HD21 . ASN A 1 229 ? 40.257 4.377   15.050  1.00 18.49 ? 229 ASN A HD21 1 
ATOM   3346 H HD22 . ASN A 1 229 ? 39.570 5.360   14.166  1.00 18.49 ? 229 ASN A HD22 1 
ATOM   3347 N N    . GLY A 1 230 ? 41.928 5.181   8.647   1.00 14.09 ? 230 GLY A N    1 
ATOM   3348 C CA   . GLY A 1 230 ? 41.783 5.353   7.216   1.00 13.25 ? 230 GLY A CA   1 
ATOM   3349 C C    . GLY A 1 230 ? 41.737 6.794   6.783   1.00 15.87 ? 230 GLY A C    1 
ATOM   3350 O O    . GLY A 1 230 ? 41.962 7.087   5.609   1.00 15.20 ? 230 GLY A O    1 
ATOM   3351 H H    . GLY A 1 230 ? 42.720 5.368   8.925   1.00 16.91 ? 230 GLY A H    1 
ATOM   3352 H HA2  . GLY A 1 230 ? 42.532 4.928   6.769   1.00 15.90 ? 230 GLY A HA2  1 
ATOM   3353 H HA3  . GLY A 1 230 ? 40.961 4.926   6.928   1.00 15.90 ? 230 GLY A HA3  1 
ATOM   3354 N N    . LEU A 1 231 ? 41.459 7.713   7.689   1.00 14.90 ? 231 LEU A N    1 
ATOM   3355 C CA   . LEU A 1 231 ? 41.400 9.125   7.318   1.00 15.92 ? 231 LEU A CA   1 
ATOM   3356 C C    . LEU A 1 231 ? 42.705 9.607   6.712   1.00 16.05 ? 231 LEU A C    1 
ATOM   3357 O O    . LEU A 1 231 ? 42.703 10.558  5.912   1.00 16.91 ? 231 LEU A O    1 
ATOM   3358 C CB   . LEU A 1 231 ? 41.098 9.992   8.550   1.00 17.64 ? 231 LEU A CB   1 
ATOM   3359 C CG   . LEU A 1 231 ? 39.782 9.795   9.286   1.00 23.71 ? 231 LEU A CG   1 
ATOM   3360 C CD1  . LEU A 1 231 ? 39.550 10.829  10.362  1.00 24.26 ? 231 LEU A CD1  1 
ATOM   3361 C CD2  . LEU A 1 231 ? 38.658 9.825   8.312   1.00 22.98 ? 231 LEU A CD2  1 
ATOM   3362 H H    . LEU A 1 231 ? 41.302 7.554   8.519   1.00 17.88 ? 231 LEU A H    1 
ATOM   3363 H HA   . LEU A 1 231 ? 40.686 9.225   6.669   1.00 19.11 ? 231 LEU A HA   1 
ATOM   3364 H HB2  . LEU A 1 231 ? 41.802 9.831   9.199   1.00 21.17 ? 231 LEU A HB2  1 
ATOM   3365 H HB3  . LEU A 1 231 ? 41.117 10.919  8.265   1.00 21.17 ? 231 LEU A HB3  1 
ATOM   3366 H HG   . LEU A 1 231 ? 39.817 8.934   9.730   1.00 28.45 ? 231 LEU A HG   1 
ATOM   3367 H HD11 . LEU A 1 231 ? 38.708 10.640  10.806  1.00 29.11 ? 231 LEU A HD11 1 
ATOM   3368 H HD12 . LEU A 1 231 ? 40.278 10.787  11.002  1.00 29.11 ? 231 LEU A HD12 1 
ATOM   3369 H HD13 . LEU A 1 231 ? 39.519 11.709  9.954   1.00 29.11 ? 231 LEU A HD13 1 
ATOM   3370 H HD21 . LEU A 1 231 ? 37.819 9.828   8.798   1.00 27.58 ? 231 LEU A HD21 1 
ATOM   3371 H HD22 . LEU A 1 231 ? 38.730 10.627  7.771   1.00 27.58 ? 231 LEU A HD22 1 
ATOM   3372 H HD23 . LEU A 1 231 ? 38.710 9.039   7.746   1.00 27.58 ? 231 LEU A HD23 1 
ATOM   3373 N N    . GLU A 1 232 ? 43.830 9.010   7.109   1.00 15.09 ? 232 GLU A N    1 
ATOM   3374 C CA   . GLU A 1 232 ? 45.138 9.435   6.623   1.00 16.63 ? 232 GLU A CA   1 
ATOM   3375 C C    . GLU A 1 232 ? 45.325 9.155   5.142   1.00 16.46 ? 232 GLU A C    1 
ATOM   3376 O O    . GLU A 1 232 ? 46.296 9.659   4.570   1.00 18.94 ? 232 GLU A O    1 
ATOM   3377 C CB   . GLU A 1 232 ? 46.261 8.769   7.414   1.00 19.48 ? 232 GLU A CB   1 
ATOM   3378 C CG   . GLU A 1 232 ? 46.247 7.241   7.424   1.00 19.12 ? 232 GLU A CG   1 
ATOM   3379 C CD   . GLU A 1 232 ? 45.524 6.695   8.644   1.00 18.50 ? 232 GLU A CD   1 
ATOM   3380 O OE1  . GLU A 1 232 ? 44.274 6.722   8.673   1.00 17.20 ? 232 GLU A OE1  1 
ATOM   3381 O OE2  . GLU A 1 232 ? 46.204 6.275   9.615   1.00 22.28 ? 232 GLU A OE2  1 
ATOM   3382 H H    . GLU A 1 232 ? 43.861 8.353   7.664   1.00 18.11 ? 232 GLU A H    1 
ATOM   3383 H HA   . GLU A 1 232 ? 45.214 10.391  6.768   1.00 19.96 ? 232 GLU A HA   1 
ATOM   3384 H HB2  . GLU A 1 232 ? 47.108 9.047   7.032   1.00 23.37 ? 232 GLU A HB2  1 
ATOM   3385 H HB3  . GLU A 1 232 ? 46.201 9.064   8.336   1.00 23.37 ? 232 GLU A HB3  1 
ATOM   3386 H HG2  . GLU A 1 232 ? 45.791 6.920   6.631   1.00 22.95 ? 232 GLU A HG2  1 
ATOM   3387 H HG3  . GLU A 1 232 ? 47.159 6.912   7.439   1.00 22.95 ? 232 GLU A HG3  1 
ATOM   3388 N N    . TYR A 1 233 ? 44.433 8.393   4.515   1.00 15.78 ? 233 TYR A N    1 
ATOM   3389 C CA   . TYR A 1 233 ? 44.520 8.084   3.089   1.00 15.50 ? 233 TYR A CA   1 
ATOM   3390 C C    . TYR A 1 233 ? 43.514 8.840   2.244   1.00 16.19 ? 233 TYR A C    1 
ATOM   3391 O O    . TYR A 1 233 ? 43.512 8.683   1.011   1.00 17.74 ? 233 TYR A O    1 
ATOM   3392 C CB   . TYR A 1 233 ? 44.356 6.581   2.881   1.00 17.29 ? 233 TYR A CB   1 
ATOM   3393 C CG   . TYR A 1 233 ? 45.268 5.759   3.738   1.00 15.84 ? 233 TYR A CG   1 
ATOM   3394 C CD1  . TYR A 1 233 ? 46.636 5.826   3.597   1.00 16.34 ? 233 TYR A CD1  1 
ATOM   3395 C CD2  . TYR A 1 233 ? 44.751 4.902   4.703   1.00 16.32 ? 233 TYR A CD2  1 
ATOM   3396 C CE1  . TYR A 1 233 ? 47.478 5.061   4.393   1.00 17.78 ? 233 TYR A CE1  1 
ATOM   3397 C CE2  . TYR A 1 233 ? 45.573 4.159   5.486   1.00 17.37 ? 233 TYR A CE2  1 
ATOM   3398 C CZ   . TYR A 1 233 ? 46.921 4.226   5.334   1.00 17.75 ? 233 TYR A CZ   1 
ATOM   3399 O OH   . TYR A 1 233 ? 47.740 3.466   6.124   1.00 22.44 ? 233 TYR A OH   1 
ATOM   3400 H H    . TYR A 1 233 ? 43.753 8.036   4.902   1.00 18.93 ? 233 TYR A H    1 
ATOM   3401 H HA   . TYR A 1 233 ? 45.400 8.337   2.769   1.00 18.60 ? 233 TYR A HA   1 
ATOM   3402 H HB2  . TYR A 1 233 ? 43.443 6.333   3.095   1.00 20.75 ? 233 TYR A HB2  1 
ATOM   3403 H HB3  . TYR A 1 233 ? 44.548 6.370   1.954   1.00 20.75 ? 233 TYR A HB3  1 
ATOM   3404 H HD1  . TYR A 1 233 ? 47.003 6.393   2.957   1.00 19.61 ? 233 TYR A HD1  1 
ATOM   3405 H HD2  . TYR A 1 233 ? 43.830 4.837   4.814   1.00 19.58 ? 233 TYR A HD2  1 
ATOM   3406 H HE1  . TYR A 1 233 ? 48.401 5.113   4.293   1.00 21.33 ? 233 TYR A HE1  1 
ATOM   3407 H HE2  . TYR A 1 233 ? 45.210 3.599   6.133   1.00 20.85 ? 233 TYR A HE2  1 
ATOM   3408 H HH   . TYR A 1 233 ? 48.543 3.607   5.924   1.00 26.93 ? 233 TYR A HH   1 
ATOM   3409 N N    . LEU A 1 234 ? 42.674 9.696   2.829   1.00 15.21 ? 234 LEU A N    1 
ATOM   3410 C CA   . LEU A 1 234 ? 41.562 10.262  2.072   1.00 17.71 ? 234 LEU A CA   1 
ATOM   3411 C C    . LEU A 1 234 ? 41.964 11.371  1.120   1.00 18.10 ? 234 LEU A C    1 
ATOM   3412 O O    . LEU A 1 234 ? 41.145 11.779  0.281   1.00 17.56 ? 234 LEU A O    1 
ATOM   3413 C CB   . LEU A 1 234 ? 40.484 10.774  3.015   1.00 20.43 ? 234 LEU A CB   1 
ATOM   3414 C CG   . LEU A 1 234 ? 39.585 9.662   3.538   1.00 21.17 ? 234 LEU A CG   1 
ATOM   3415 C CD1  . LEU A 1 234 ? 38.600 10.283  4.514   1.00 24.06 ? 234 LEU A CD1  1 
ATOM   3416 C CD2  . LEU A 1 234 ? 38.872 8.931   2.403   1.00 28.22 ? 234 LEU A CD2  1 
ATOM   3417 H H    . LEU A 1 234 ? 42.727 9.958   3.647   1.00 18.25 ? 234 LEU A H    1 
ATOM   3418 H HA   . LEU A 1 234 ? 41.181 9.549   1.537   1.00 21.25 ? 234 LEU A HA   1 
ATOM   3419 H HB2  . LEU A 1 234 ? 40.908 11.201  3.776   1.00 24.52 ? 234 LEU A HB2  1 
ATOM   3420 H HB3  . LEU A 1 234 ? 39.929 11.413  2.542   1.00 24.52 ? 234 LEU A HB3  1 
ATOM   3421 H HG   . LEU A 1 234 ? 40.111 8.984   3.992   1.00 25.40 ? 234 LEU A HG   1 
ATOM   3422 H HD11 . LEU A 1 234 ? 38.013 9.590   4.855   1.00 28.87 ? 234 LEU A HD11 1 
ATOM   3423 H HD12 . LEU A 1 234 ? 39.093 10.688  5.245   1.00 28.87 ? 234 LEU A HD12 1 
ATOM   3424 H HD13 . LEU A 1 234 ? 38.081 10.959  4.052   1.00 28.87 ? 234 LEU A HD13 1 
ATOM   3425 H HD21 . LEU A 1 234 ? 37.922 8.898   2.596   1.00 33.86 ? 234 LEU A HD21 1 
ATOM   3426 H HD22 . LEU A 1 234 ? 39.025 9.409   1.574   1.00 33.86 ? 234 LEU A HD22 1 
ATOM   3427 H HD23 . LEU A 1 234 ? 39.227 8.030   2.336   1.00 33.86 ? 234 LEU A HD23 1 
ATOM   3428 N N    . GLY A 1 235 ? 43.191 11.875  1.193   1.00 18.11 ? 235 GLY A N    1 
ATOM   3429 C CA   . GLY A 1 235 ? 43.590 12.918  0.271   1.00 19.23 ? 235 GLY A CA   1 
ATOM   3430 C C    . GLY A 1 235 ? 43.569 12.490  -1.182  1.00 18.00 ? 235 GLY A C    1 
ATOM   3431 O O    . GLY A 1 235 ? 43.514 13.344  -2.071  1.00 19.66 ? 235 GLY A O    1 
ATOM   3432 H H    . GLY A 1 235 ? 43.795 11.632  1.756   1.00 21.73 ? 235 GLY A H    1 
ATOM   3433 H HA2  . GLY A 1 235 ? 42.989 13.673  0.370   1.00 23.07 ? 235 GLY A HA2  1 
ATOM   3434 H HA3  . GLY A 1 235 ? 44.492 13.201  0.487   1.00 23.07 ? 235 GLY A HA3  1 
ATOM   3435 N N    . TYR A 1 236 ? 43.620 11.175  -1.452  1.00 16.21 ? 236 TYR A N    1 
ATOM   3436 C CA   . TYR A 1 236 ? 43.604 10.682  -2.801  1.00 16.34 ? 236 TYR A CA   1 
ATOM   3437 C C    . TYR A 1 236 ? 42.220 10.694  -3.419  1.00 16.02 ? 236 TYR A C    1 
ATOM   3438 O O    . TYR A 1 236 ? 42.108 10.562  -4.649  1.00 15.73 ? 236 TYR A O    1 
ATOM   3439 C CB   . TYR A 1 236 ? 44.146 9.244   -2.857  1.00 17.41 ? 236 TYR A CB   1 
ATOM   3440 C CG   . TYR A 1 236 ? 45.618 9.185   -2.574  1.00 17.70 ? 236 TYR A CG   1 
ATOM   3441 C CD1  . TYR A 1 236 ? 46.525 9.423   -3.577  1.00 16.51 ? 236 TYR A CD1  1 
ATOM   3442 C CD2  . TYR A 1 236 ? 46.096 8.895   -1.305  1.00 21.54 ? 236 TYR A CD2  1 
ATOM   3443 C CE1  . TYR A 1 236 ? 47.876 9.401   -3.335  1.00 17.80 ? 236 TYR A CE1  1 
ATOM   3444 C CE2  . TYR A 1 236 ? 47.448 8.863   -1.051  1.00 23.20 ? 236 TYR A CE2  1 
ATOM   3445 C CZ   . TYR A 1 236 ? 48.325 9.106   -2.073  1.00 20.09 ? 236 TYR A CZ   1 
ATOM   3446 O OH   . TYR A 1 236 ? 49.676 9.070   -1.823  1.00 23.24 ? 236 TYR A OH   1 
ATOM   3447 H H    . TYR A 1 236 ? 43.666 10.558  -0.854  1.00 19.45 ? 236 TYR A H    1 
ATOM   3448 H HA   . TYR A 1 236 ? 44.183 11.252  -3.330  1.00 19.61 ? 236 TYR A HA   1 
ATOM   3449 H HB2  . TYR A 1 236 ? 43.688 8.706   -2.193  1.00 20.89 ? 236 TYR A HB2  1 
ATOM   3450 H HB3  . TYR A 1 236 ? 43.993 8.880   -3.743  1.00 20.89 ? 236 TYR A HB3  1 
ATOM   3451 H HD1  . TYR A 1 236 ? 46.218 9.603   -4.436  1.00 19.81 ? 236 TYR A HD1  1 
ATOM   3452 H HD2  . TYR A 1 236 ? 45.495 8.720   -0.617  1.00 25.84 ? 236 TYR A HD2  1 
ATOM   3453 H HE1  . TYR A 1 236 ? 48.480 9.584   -4.019  1.00 21.35 ? 236 TYR A HE1  1 
ATOM   3454 H HE2  . TYR A 1 236 ? 47.762 8.678   -0.195  1.00 27.84 ? 236 TYR A HE2  1 
ATOM   3455 H HH   . TYR A 1 236 ? 49.814 8.890   -1.015  1.00 27.88 ? 236 TYR A HH   1 
ATOM   3456 N N    . PHE A 1 237 ? 41.162 10.828  -2.622  1.00 13.30 ? 237 PHE A N    1 
ATOM   3457 C CA   . PHE A 1 237 ? 39.825 10.451  -3.043  1.00 12.15 ? 237 PHE A CA   1 
ATOM   3458 C C    . PHE A 1 237 ? 38.829 11.557  -2.774  1.00 13.73 ? 237 PHE A C    1 
ATOM   3459 O O    . PHE A 1 237 ? 39.055 12.427  -1.939  1.00 15.68 ? 237 PHE A O    1 
ATOM   3460 C CB   . PHE A 1 237 ? 39.387 9.189   -2.295  1.00 12.57 ? 237 PHE A CB   1 
ATOM   3461 C CG   . PHE A 1 237 ? 40.395 8.087   -2.378  1.00 13.10 ? 237 PHE A CG   1 
ATOM   3462 C CD1  . PHE A 1 237 ? 40.700 7.517   -3.592  1.00 15.69 ? 237 PHE A CD1  1 
ATOM   3463 C CD2  . PHE A 1 237 ? 41.052 7.619   -1.246  1.00 14.02 ? 237 PHE A CD2  1 
ATOM   3464 C CE1  . PHE A 1 237 ? 41.637 6.524   -3.696  1.00 16.31 ? 237 PHE A CE1  1 
ATOM   3465 C CE2  . PHE A 1 237 ? 41.975 6.592   -1.350  1.00 15.98 ? 237 PHE A CE2  1 
ATOM   3466 C CZ   . PHE A 1 237 ? 42.258 6.052   -2.580  1.00 14.65 ? 237 PHE A CZ   1 
ATOM   3467 H H    . PHE A 1 237 ? 41.199 11.141  -1.821  1.00 15.96 ? 237 PHE A H    1 
ATOM   3468 H HA   . PHE A 1 237 ? 39.825 10.300  -4.001  1.00 14.59 ? 237 PHE A HA   1 
ATOM   3469 H HB2  . PHE A 1 237 ? 39.256 9.406   -1.359  1.00 15.09 ? 237 PHE A HB2  1 
ATOM   3470 H HB3  . PHE A 1 237 ? 38.557 8.866   -2.680  1.00 15.09 ? 237 PHE A HB3  1 
ATOM   3471 H HD1  . PHE A 1 237 ? 40.261 7.811   -4.357  1.00 18.82 ? 237 PHE A HD1  1 
ATOM   3472 H HD2  . PHE A 1 237 ? 40.870 7.996   -0.416  1.00 16.83 ? 237 PHE A HD2  1 
ATOM   3473 H HE1  . PHE A 1 237 ? 41.851 6.172   -4.530  1.00 19.57 ? 237 PHE A HE1  1 
ATOM   3474 H HE2  . PHE A 1 237 ? 42.401 6.269   -0.589  1.00 19.17 ? 237 PHE A HE2  1 
ATOM   3475 H HZ   . PHE A 1 237 ? 42.876 5.361   -2.651  1.00 17.58 ? 237 PHE A HZ   1 
ATOM   3476 N N    . ASN A 1 238 ? 37.683 11.492  -3.446  1.00 12.13 ? 238 ASN A N    1 
ATOM   3477 C CA   . ASN A 1 238 ? 36.583 12.399  -3.127  1.00 12.71 ? 238 ASN A CA   1 
ATOM   3478 C C    . ASN A 1 238 ? 35.783 11.955  -1.917  1.00 12.43 ? 238 ASN A C    1 
ATOM   3479 O O    . ASN A 1 238 ? 35.025 12.765  -1.362  1.00 13.82 ? 238 ASN A O    1 
ATOM   3480 C CB   . ASN A 1 238 ? 35.653 12.538  -4.336  1.00 13.50 ? 238 ASN A CB   1 
ATOM   3481 C CG   . ASN A 1 238 ? 36.343 13.128  -5.528  1.00 15.34 ? 238 ASN A CG   1 
ATOM   3482 O OD1  . ASN A 1 238 ? 36.585 12.449  -6.511  1.00 13.92 ? 238 ASN A OD1  1 
ATOM   3483 N ND2  . ASN A 1 238 ? 36.680 14.394  -5.432  1.00 16.67 ? 238 ASN A ND2  1 
ATOM   3484 H H    . ASN A 1 238 ? 37.520 10.939  -4.084  1.00 14.56 ? 238 ASN A H    1 
ATOM   3485 H HA   . ASN A 1 238 ? 36.950 13.276  -2.932  1.00 15.25 ? 238 ASN A HA   1 
ATOM   3486 H HB2  . ASN A 1 238 ? 35.322 11.661  -4.584  1.00 16.20 ? 238 ASN A HB2  1 
ATOM   3487 H HB3  . ASN A 1 238 ? 34.911 13.118  -4.100  1.00 16.20 ? 238 ASN A HB3  1 
ATOM   3488 H HD21 . ASN A 1 238 ? 37.078 14.783  -6.087  1.00 20.00 ? 238 ASN A HD21 1 
ATOM   3489 H HD22 . ASN A 1 238 ? 36.502 14.833  -4.714  1.00 20.00 ? 238 ASN A HD22 1 
ATOM   3490 N N    . GLY A 1 239 ? 35.938 10.709  -1.491  1.00 12.59 ? 239 GLY A N    1 
ATOM   3491 C CA   . GLY A 1 239 ? 35.251 10.262  -0.289  1.00 13.57 ? 239 GLY A CA   1 
ATOM   3492 C C    . GLY A 1 239 ? 35.529 8.808   -0.013  1.00 12.32 ? 239 GLY A C    1 
ATOM   3493 O O    . GLY A 1 239 ? 36.279 8.130   -0.730  1.00 12.98 ? 239 GLY A O    1 
ATOM   3494 H H    . GLY A 1 239 ? 36.427 10.113  -1.873  1.00 15.10 ? 239 GLY A H    1 
ATOM   3495 H HA2  . GLY A 1 239 ? 35.550 10.785  0.471   1.00 16.28 ? 239 GLY A HA2  1 
ATOM   3496 H HA3  . GLY A 1 239 ? 34.294 10.380  -0.397  1.00 16.28 ? 239 GLY A HA3  1 
ATOM   3497 N N    . SER A 1 240 ? 34.888 8.332   1.047   1.00 12.05 ? 240 SER A N    1 
ATOM   3498 C CA   . SER A 1 240 ? 35.032 6.948   1.473   1.00 11.80 ? 240 SER A CA   1 
ATOM   3499 C C    . SER A 1 240 ? 33.697 6.239   1.497   1.00 11.11 ? 240 SER A C    1 
ATOM   3500 O O    . SER A 1 240 ? 32.703 6.786   1.978   1.00 11.61 ? 240 SER A O    1 
ATOM   3501 C CB   . SER A 1 240 ? 35.623 6.853   2.877   1.00 14.26 ? 240 SER A CB   1 
ATOM   3502 O OG   . SER A 1 240 ? 35.891 5.500   3.240   1.00 14.53 ? 240 SER A OG   1 
ATOM   3503 H H    . SER A 1 240 ? 34.359 8.797   1.540   1.00 14.46 ? 240 SER A H    1 
ATOM   3504 H HA   . SER A 1 240 ? 35.613 6.507   0.833   1.00 14.15 ? 240 SER A HA   1 
ATOM   3505 H HB2  . SER A 1 240 ? 36.453 7.355   2.902   1.00 17.12 ? 240 SER A HB2  1 
ATOM   3506 H HB3  . SER A 1 240 ? 34.990 7.228   3.510   1.00 17.12 ? 240 SER A HB3  1 
ATOM   3507 H HG   . SER A 1 240 ? 36.357 5.131   2.647   1.00 17.44 ? 240 SER A HG   1 
ATOM   3508 N N    . TYR A 1 241 ? 33.722 5.005   1.032   1.00 11.10 ? 241 TYR A N    1 
ATOM   3509 C CA   . TYR A 1 241 ? 32.700 4.008   1.295   1.00 10.78 ? 241 TYR A CA   1 
ATOM   3510 C C    . TYR A 1 241 ? 33.131 3.322   2.610   1.00 12.37 ? 241 TYR A C    1 
ATOM   3511 O O    . TYR A 1 241 ? 34.324 3.257   2.951   1.00 11.53 ? 241 TYR A O    1 
ATOM   3512 C CB   . TYR A 1 241 ? 32.726 3.007   0.135   1.00 11.77 ? 241 TYR A CB   1 
ATOM   3513 C CG   . TYR A 1 241 ? 32.200 1.628   0.368   1.00 10.88 ? 241 TYR A CG   1 
ATOM   3514 C CD1  . TYR A 1 241 ? 32.954 0.672   1.037   1.00 10.40 ? 241 TYR A CD1  1 
ATOM   3515 C CD2  . TYR A 1 241 ? 31.053 1.183   -0.335  1.00 12.54 ? 241 TYR A CD2  1 
ATOM   3516 C CE1  . TYR A 1 241 ? 32.515 -0.612  1.162   1.00 11.12 ? 241 TYR A CE1  1 
ATOM   3517 C CE2  . TYR A 1 241 ? 30.623 -0.110  -0.234  1.00 11.32 ? 241 TYR A CE2  1 
ATOM   3518 C CZ   . TYR A 1 241 ? 31.358 -1.021  0.507   1.00 11.97 ? 241 TYR A CZ   1 
ATOM   3519 O OH   . TYR A 1 241 ? 30.952 -2.333  0.594   1.00 13.00 ? 241 TYR A OH   1 
ATOM   3520 H H    . TYR A 1 241 ? 34.354 4.702   0.533   1.00 13.33 ? 241 TYR A H    1 
ATOM   3521 H HA   . TYR A 1 241 ? 31.800 4.358   1.377   1.00 12.93 ? 241 TYR A HA   1 
ATOM   3522 H HB2  . TYR A 1 241 ? 32.200 3.383   -0.588  1.00 14.13 ? 241 TYR A HB2  1 
ATOM   3523 H HB3  . TYR A 1 241 ? 33.649 2.906   -0.145  1.00 14.13 ? 241 TYR A HB3  1 
ATOM   3524 H HD1  . TYR A 1 241 ? 33.773 0.912   1.406   1.00 12.48 ? 241 TYR A HD1  1 
ATOM   3525 H HD2  . TYR A 1 241 ? 30.585 1.780   -0.874  1.00 15.05 ? 241 TYR A HD2  1 
ATOM   3526 H HE1  . TYR A 1 241 ? 32.990 -1.216  1.686   1.00 13.35 ? 241 TYR A HE1  1 
ATOM   3527 H HE2  . TYR A 1 241 ? 29.841 -0.378  -0.661  1.00 13.58 ? 241 TYR A HE2  1 
ATOM   3528 H HH   . TYR A 1 241 ? 31.519 -2.782  1.021   1.00 15.60 ? 241 TYR A HH   1 
ATOM   3529 N N    . LEU A 1 242 ? 32.149 2.847   3.354   1.00 10.85 ? 242 LEU A N    1 
ATOM   3530 C CA   . LEU A 1 242 ? 32.379 2.121   4.602   1.00 10.86 ? 242 LEU A CA   1 
ATOM   3531 C C    . LEU A 1 242 ? 31.630 0.807   4.574   1.00 11.15 ? 242 LEU A C    1 
ATOM   3532 O O    . LEU A 1 242 ? 30.452 0.766   4.205   1.00 11.70 ? 242 LEU A O    1 
ATOM   3533 C CB   . LEU A 1 242 ? 31.927 2.923   5.817   1.00 12.20 ? 242 LEU A CB   1 
ATOM   3534 C CG   . LEU A 1 242 ? 32.692 4.219   6.063   1.00 12.04 ? 242 LEU A CG   1 
ATOM   3535 C CD1  . LEU A 1 242 ? 32.038 5.353   5.340   1.00 16.75 ? 242 LEU A CD1  1 
ATOM   3536 C CD2  . LEU A 1 242 ? 32.820 4.529   7.538   1.00 15.66 ? 242 LEU A CD2  1 
ATOM   3537 H H    . LEU A 1 242 ? 31.316 2.931   3.157   1.00 13.03 ? 242 LEU A H    1 
ATOM   3538 H HA   . LEU A 1 242 ? 33.328 1.941   4.686   1.00 13.04 ? 242 LEU A HA   1 
ATOM   3539 H HB2  . LEU A 1 242 ? 30.993 3.155   5.698   1.00 14.64 ? 242 LEU A HB2  1 
ATOM   3540 H HB3  . LEU A 1 242 ? 32.034 2.368   6.605   1.00 14.64 ? 242 LEU A HB3  1 
ATOM   3541 H HG   . LEU A 1 242 ? 33.592 4.109   5.718   1.00 14.44 ? 242 LEU A HG   1 
ATOM   3542 H HD11 . LEU A 1 242 ? 32.533 6.168   5.517   1.00 20.10 ? 242 LEU A HD11 1 
ATOM   3543 H HD12 . LEU A 1 242 ? 32.041 5.165   4.388   1.00 20.10 ? 242 LEU A HD12 1 
ATOM   3544 H HD13 . LEU A 1 242 ? 31.125 5.445   5.656   1.00 20.10 ? 242 LEU A HD13 1 
ATOM   3545 H HD21 . LEU A 1 242 ? 33.310 5.360   7.645   1.00 18.79 ? 242 LEU A HD21 1 
ATOM   3546 H HD22 . LEU A 1 242 ? 31.934 4.616   7.921   1.00 18.79 ? 242 LEU A HD22 1 
ATOM   3547 H HD23 . LEU A 1 242 ? 33.299 3.806   7.973   1.00 18.79 ? 242 LEU A HD23 1 
ATOM   3548 N N    . GLU A 1 243 ? 32.309 -0.252  5.013   1.00 10.42 ? 243 GLU A N    1 
ATOM   3549 C CA   . GLU A 1 243 ? 31.681 -1.530  5.321   1.00 10.90 ? 243 GLU A CA   1 
ATOM   3550 C C    . GLU A 1 243 ? 32.293 -2.076  6.604   1.00 10.67 ? 243 GLU A C    1 
ATOM   3551 O O    . GLU A 1 243 ? 33.312 -1.581  7.107   1.00 11.53 ? 243 GLU A O    1 
ATOM   3552 C CB   . GLU A 1 243 ? 31.825 -2.524  4.150   1.00 10.99 ? 243 GLU A CB   1 
ATOM   3553 C CG   . GLU A 1 243 ? 33.254 -2.987  3.896   1.00 12.01 ? 243 GLU A CG   1 
ATOM   3554 C CD   . GLU A 1 243 ? 33.478 -3.842  2.682   1.00 14.61 ? 243 GLU A CD   1 
ATOM   3555 O OE1  . GLU A 1 243 ? 32.557 -3.987  1.835   1.00 15.06 ? 243 GLU A OE1  1 
ATOM   3556 O OE2  . GLU A 1 243 ? 34.587 -4.413  2.541   1.00 15.31 ? 243 GLU A OE2  1 
ATOM   3557 H H    . GLU A 1 243 ? 33.159 -0.253  5.144   1.00 12.51 ? 243 GLU A H    1 
ATOM   3558 H HA   . GLU A 1 243 ? 30.732 -1.403  5.478   1.00 13.07 ? 243 GLU A HA   1 
ATOM   3559 H HB2  . GLU A 1 243 ? 31.291 -3.310  4.344   1.00 13.19 ? 243 GLU A HB2  1 
ATOM   3560 H HB3  . GLU A 1 243 ? 31.506 -2.097  3.340   1.00 13.19 ? 243 GLU A HB3  1 
ATOM   3561 H HG2  . GLU A 1 243 ? 33.812 -2.200  3.796   1.00 14.42 ? 243 GLU A HG2  1 
ATOM   3562 H HG3  . GLU A 1 243 ? 33.544 -3.504  4.664   1.00 14.42 ? 243 GLU A HG3  1 
ATOM   3563 N N    . GLY A 1 244 ? 31.641 -3.091  7.161   1.00 10.93 ? 244 GLY A N    1 
ATOM   3564 C CA   . GLY A 1 244 ? 32.092 -3.647  8.421   1.00 11.00 ? 244 GLY A CA   1 
ATOM   3565 C C    . GLY A 1 244 ? 31.977 -2.710  9.591   1.00 11.83 ? 244 GLY A C    1 
ATOM   3566 O O    . GLY A 1 244 ? 32.637 -2.917  10.604  1.00 12.30 ? 244 GLY A O    1 
ATOM   3567 H H    . GLY A 1 244 ? 30.942 -3.468  6.830   1.00 13.12 ? 244 GLY A H    1 
ATOM   3568 H HA2  . GLY A 1 244 ? 31.567 -4.437  8.620   1.00 13.20 ? 244 GLY A HA2  1 
ATOM   3569 H HA3  . GLY A 1 244 ? 33.024 -3.900  8.334   1.00 13.20 ? 244 GLY A HA3  1 
ATOM   3570 N N    . PHE A 1 245 ? 31.157 -1.674  9.473   1.00 11.51 ? 245 PHE A N    1 
ATOM   3571 C CA   . PHE A 1 245 ? 31.139 -0.594  10.458  1.00 11.11 ? 245 PHE A CA   1 
ATOM   3572 C C    . PHE A 1 245 ? 30.717 -1.106  11.827  1.00 11.66 ? 245 PHE A C    1 
ATOM   3573 O O    . PHE A 1 245 ? 31.183 -0.614  12.868  1.00 12.32 ? 245 PHE A O    1 
ATOM   3574 C CB   . PHE A 1 245 ? 30.174 0.482   9.984   1.00 12.02 ? 245 PHE A CB   1 
ATOM   3575 C CG   . PHE A 1 245 ? 30.404 1.843   10.593  1.00 11.09 ? 245 PHE A CG   1 
ATOM   3576 C CD1  . PHE A 1 245 ? 31.573 2.541   10.390  1.00 10.82 ? 245 PHE A CD1  1 
ATOM   3577 C CD2  . PHE A 1 245 ? 29.425 2.417   11.372  1.00 13.24 ? 245 PHE A CD2  1 
ATOM   3578 C CE1  . PHE A 1 245 ? 31.743 3.826   10.903  1.00 11.81 ? 245 PHE A CE1  1 
ATOM   3579 C CE2  . PHE A 1 245 ? 29.600 3.688   11.931  1.00 13.02 ? 245 PHE A CE2  1 
ATOM   3580 C CZ   . PHE A 1 245 ? 30.766 4.393   11.684  1.00 13.71 ? 245 PHE A CZ   1 
ATOM   3581 H H    . PHE A 1 245 ? 30.597 -1.567  8.829   1.00 13.81 ? 245 PHE A H    1 
ATOM   3582 H HA   . PHE A 1 245 ? 32.028 -0.215  10.540  1.00 13.33 ? 245 PHE A HA   1 
ATOM   3583 H HB2  . PHE A 1 245 ? 30.261 0.573   9.022   1.00 14.42 ? 245 PHE A HB2  1 
ATOM   3584 H HB3  . PHE A 1 245 ? 29.271 0.209   10.211  1.00 14.42 ? 245 PHE A HB3  1 
ATOM   3585 H HD1  . PHE A 1 245 ? 32.261 2.148   9.903   1.00 12.99 ? 245 PHE A HD1  1 
ATOM   3586 H HD2  . PHE A 1 245 ? 28.634 1.953   11.530  1.00 15.89 ? 245 PHE A HD2  1 
ATOM   3587 H HE1  . PHE A 1 245 ? 32.521 4.301   10.715  1.00 14.17 ? 245 PHE A HE1  1 
ATOM   3588 H HE2  . PHE A 1 245 ? 28.936 4.058   12.467  1.00 15.63 ? 245 PHE A HE2  1 
ATOM   3589 H HZ   . PHE A 1 245 ? 30.887 5.242   12.043  1.00 16.45 ? 245 PHE A HZ   1 
ATOM   3590 N N    . ASP A 1 246 ? 29.815 -2.082  11.836  1.00 11.81 ? 246 ASP A N    1 
ATOM   3591 C CA   . ASP A 1 246 ? 29.321 -2.700  13.049  1.00 12.25 ? 246 ASP A CA   1 
ATOM   3592 C C    . ASP A 1 246 ? 29.932 -4.074  13.285  1.00 12.17 ? 246 ASP A C    1 
ATOM   3593 O O    . ASP A 1 246 ? 29.349 -4.884  14.024  1.00 14.18 ? 246 ASP A O    1 
ATOM   3594 C CB   . ASP A 1 246 ? 27.795 -2.823  13.018  1.00 13.56 ? 246 ASP A CB   1 
ATOM   3595 C CG   . ASP A 1 246 ? 27.316 -3.845  12.024  1.00 12.64 ? 246 ASP A CG   1 
ATOM   3596 O OD1  . ASP A 1 246 ? 26.223 -4.451  12.187  1.00 14.25 ? 246 ASP A OD1  1 
ATOM   3597 O OD2  . ASP A 1 246 ? 28.013 -4.011  10.982  1.00 13.01 ? 246 ASP A OD2  1 
ATOM   3598 H H    . ASP A 1 246 ? 29.465 -2.411  11.123  1.00 14.17 ? 246 ASP A H    1 
ATOM   3599 H HA   . ASP A 1 246 ? 29.559 -2.122  13.791  1.00 14.70 ? 246 ASP A HA   1 
ATOM   3600 H HB2  . ASP A 1 246 ? 27.481 -3.088  13.896  1.00 16.27 ? 246 ASP A HB2  1 
ATOM   3601 H HB3  . ASP A 1 246 ? 27.413 -1.965  12.774  1.00 16.27 ? 246 ASP A HB3  1 
ATOM   3602 N N    . SER A 1 247 ? 31.086 -4.364  12.683  1.00 12.77 ? 247 SER A N    1 
ATOM   3603 C CA   . SER A 1 247 ? 31.686 -5.700  12.732  1.00 12.59 ? 247 SER A CA   1 
ATOM   3604 C C    . SER A 1 247 ? 33.069 -5.635  13.367  1.00 14.77 ? 247 SER A C    1 
ATOM   3605 O O    . SER A 1 247 ? 34.089 -5.438  12.700  1.00 13.92 ? 247 SER A O    1 
ATOM   3606 C CB   . SER A 1 247 ? 31.721 -6.283  11.345  1.00 14.47 ? 247 SER A CB   1 
ATOM   3607 O OG   . SER A 1 247 ? 32.087 -7.637  11.423  1.00 16.71 ? 247 SER A OG   1 
ATOM   3608 H H    . SER A 1 247 ? 31.548 -3.794  12.233  1.00 15.32 ? 247 SER A H    1 
ATOM   3609 H HA   . SER A 1 247 ? 31.154 -6.264  13.315  1.00 15.11 ? 247 SER A HA   1 
ATOM   3610 H HB2  . SER A 1 247 ? 30.842 -6.209  10.942  1.00 17.36 ? 247 SER A HB2  1 
ATOM   3611 H HB3  . SER A 1 247 ? 32.372 -5.804  10.809  1.00 17.36 ? 247 SER A HB3  1 
ATOM   3612 H HG   . SER A 1 247 ? 32.136 -7.967  10.652  1.00 20.06 ? 247 SER A HG   1 
ATOM   3613 N N    . GLU A 1 248 ? 33.084 -5.828  14.677  1.00 14.03 ? 248 GLU A N    1 
ATOM   3614 C CA   . GLU A 1 248 ? 34.258 -5.589  15.486  1.00 13.47 ? 248 GLU A CA   1 
ATOM   3615 C C    . GLU A 1 248 ? 35.289 -6.708  15.343  1.00 13.32 ? 248 GLU A C    1 
ATOM   3616 O O    . GLU A 1 248 ? 34.990 -7.825  14.920  1.00 15.28 ? 248 GLU A O    1 
ATOM   3617 C CB   . GLU A 1 248 ? 33.853 -5.445  16.967  1.00 15.17 ? 248 GLU A CB   1 
ATOM   3618 C CG   . GLU A 1 248 ? 33.401 -6.727  17.687  1.00 14.37 ? 248 GLU A CG   1 
ATOM   3619 C CD   . GLU A 1 248 ? 31.937 -7.079  17.471  1.00 16.74 ? 248 GLU A CD   1 
ATOM   3620 O OE1  . GLU A 1 248 ? 31.242 -6.438  16.667  1.00 17.23 ? 248 GLU A OE1  1 
ATOM   3621 O OE2  . GLU A 1 248 ? 31.478 -8.037  18.134  1.00 23.67 ? 248 GLU A OE2  1 
ATOM   3622 H H    . GLU A 1 248 ? 32.407 -6.105  15.130  1.00 16.83 ? 248 GLU A H    1 
ATOM   3623 H HA   . GLU A 1 248 ? 34.680 -4.768  15.187  1.00 16.16 ? 248 GLU A HA   1 
ATOM   3624 H HB2  . GLU A 1 248 ? 34.617 -5.100  17.455  1.00 18.20 ? 248 GLU A HB2  1 
ATOM   3625 H HB3  . GLU A 1 248 ? 33.116 -4.817  17.017  1.00 18.20 ? 248 GLU A HB3  1 
ATOM   3626 H HG2  . GLU A 1 248 ? 33.933 -7.470  17.362  1.00 17.24 ? 248 GLU A HG2  1 
ATOM   3627 H HG3  . GLU A 1 248 ? 33.538 -6.613  18.640  1.00 17.24 ? 248 GLU A HG3  1 
ATOM   3628 N N    . ALA A 1 249 ? 36.513 -6.388  15.740  1.00 14.64 ? 249 ALA A N    1 
ATOM   3629 C CA   . ALA A 1 249 ? 37.626 -7.324  15.795  1.00 14.63 ? 249 ALA A CA   1 
ATOM   3630 C C    . ALA A 1 249 ? 38.608 -6.801  16.835  1.00 15.22 ? 249 ALA A C    1 
ATOM   3631 O O    . ALA A 1 249 ? 38.317 -5.829  17.539  1.00 15.86 ? 249 ALA A O    1 
ATOM   3632 C CB   . ALA A 1 249 ? 38.232 -7.478  14.391  1.00 17.52 ? 249 ALA A CB   1 
ATOM   3633 H H    . ALA A 1 249 ? 36.735 -5.597  15.996  1.00 17.57 ? 249 ALA A H    1 
ATOM   3634 H HA   . ALA A 1 249 ? 37.330 -8.199  16.091  1.00 17.56 ? 249 ALA A HA   1 
ATOM   3635 H HB1  . ALA A 1 249 ? 38.963 -8.115  14.430  1.00 21.03 ? 249 ALA A HB1  1 
ATOM   3636 H HB2  . ALA A 1 249 ? 37.547 -7.799  13.784  1.00 21.03 ? 249 ALA A HB2  1 
ATOM   3637 H HB3  . ALA A 1 249 ? 38.561 -6.616  14.092  1.00 21.03 ? 249 ALA A HB3  1 
ATOM   3638 N N    . PHE A 1 250 ? 39.761 -7.452  16.949  1.00 16.74 ? 250 PHE A N    1 
ATOM   3639 C CA   . PHE A 1 250 ? 40.861 -6.967  17.767  1.00 16.90 ? 250 PHE A CA   1 
ATOM   3640 C C    . PHE A 1 250 ? 40.520 -6.998  19.244  1.00 17.94 ? 250 PHE A C    1 
ATOM   3641 O O    . PHE A 1 250 ? 41.155 -6.298  20.037  1.00 20.70 ? 250 PHE A O    1 
ATOM   3642 C CB   . PHE A 1 250 ? 41.338 -5.567  17.319  1.00 17.82 ? 250 PHE A CB   1 
ATOM   3643 C CG   . PHE A 1 250 ? 41.287 -5.367  15.835  1.00 16.33 ? 250 PHE A CG   1 
ATOM   3644 C CD1  . PHE A 1 250 ? 42.101 -6.110  14.991  1.00 18.97 ? 250 PHE A CD1  1 
ATOM   3645 C CD2  . PHE A 1 250 ? 40.395 -4.475  15.283  1.00 17.55 ? 250 PHE A CD2  1 
ATOM   3646 C CE1  . PHE A 1 250 ? 42.029 -5.950  13.614  1.00 19.54 ? 250 PHE A CE1  1 
ATOM   3647 C CE2  . PHE A 1 250 ? 40.324 -4.301  13.906  1.00 17.67 ? 250 PHE A CE2  1 
ATOM   3648 C CZ   . PHE A 1 250 ? 41.131 -5.055  13.077  1.00 18.17 ? 250 PHE A CZ   1 
ATOM   3649 H H    . PHE A 1 250 ? 39.930 -8.196  16.551  1.00 20.09 ? 250 PHE A H    1 
ATOM   3650 H HA   . PHE A 1 250 ? 41.621 -7.556  17.646  1.00 20.28 ? 250 PHE A HA   1 
ATOM   3651 H HB2  . PHE A 1 250 ? 40.770 -4.896  17.729  1.00 21.39 ? 250 PHE A HB2  1 
ATOM   3652 H HB3  . PHE A 1 250 ? 42.256 -5.443  17.605  1.00 21.39 ? 250 PHE A HB3  1 
ATOM   3653 H HD1  . PHE A 1 250 ? 42.701 -6.722  15.352  1.00 22.77 ? 250 PHE A HD1  1 
ATOM   3654 H HD2  . PHE A 1 250 ? 39.834 -3.984  15.838  1.00 21.06 ? 250 PHE A HD2  1 
ATOM   3655 H HE1  . PHE A 1 250 ? 42.585 -6.446  13.056  1.00 23.45 ? 250 PHE A HE1  1 
ATOM   3656 H HE2  . PHE A 1 250 ? 39.735 -3.679  13.545  1.00 21.21 ? 250 PHE A HE2  1 
ATOM   3657 H HZ   . PHE A 1 250 ? 41.068 -4.957  12.154  1.00 21.80 ? 250 PHE A HZ   1 
ATOM   3658 N N    . GLY A 1 251 ? 39.557 -7.821  19.637  1.00 17.65 ? 251 GLY A N    1 
ATOM   3659 C CA   . GLY A 1 251 ? 39.142 -7.892  21.025  1.00 17.77 ? 251 GLY A CA   1 
ATOM   3660 C C    . GLY A 1 251 ? 38.228 -6.783  21.456  1.00 17.55 ? 251 GLY A C    1 
ATOM   3661 O O    . GLY A 1 251 ? 37.789 -6.772  22.616  1.00 18.56 ? 251 GLY A O    1 
ATOM   3662 H H    . GLY A 1 251 ? 39.128 -8.352  19.114  1.00 21.18 ? 251 GLY A H    1 
ATOM   3663 H HA2  . GLY A 1 251 ? 38.679 -8.732  21.170  1.00 21.32 ? 251 GLY A HA2  1 
ATOM   3664 H HA3  . GLY A 1 251 ? 39.930 -7.863  21.588  1.00 21.32 ? 251 GLY A HA3  1 
ATOM   3665 N N    . MET A 1 252 ? 37.936 -5.831  20.573  1.00 15.30 ? 252 MET A N    1 
ATOM   3666 C CA   . MET A 1 252 ? 37.022 -4.750  20.932  1.00 14.99 ? 252 MET A CA   1 
ATOM   3667 C C    . MET A 1 252 ? 35.585 -5.209  21.053  1.00 16.04 ? 252 MET A C    1 
ATOM   3668 O O    . MET A 1 252 ? 35.109 -6.072  20.317  1.00 16.36 ? 252 MET A O    1 
ATOM   3669 C CB   . MET A 1 252 ? 37.132 -3.576  19.937  1.00 15.03 ? 252 MET A CB   1 
ATOM   3670 C CG   . MET A 1 252 ? 38.564 -3.154  19.668  1.00 15.84 ? 252 MET A CG   1 
ATOM   3671 S SD   . MET A 1 252 ? 38.691 -1.757  18.448  1.00 17.51 ? 252 MET A SD   1 
ATOM   3672 C CE   . MET A 1 252 ? 37.812 -0.497  19.243  1.00 18.32 ? 252 MET A CE   1 
ATOM   3673 H H    . MET A 1 252 ? 38.249 -5.789  19.773  1.00 18.36 ? 252 MET A H    1 
ATOM   3674 H HA   . MET A 1 252 ? 37.292 -4.423  21.805  1.00 17.99 ? 252 MET A HA   1 
ATOM   3675 H HB2  . MET A 1 252 ? 36.736 -3.841  19.093  1.00 18.03 ? 252 MET A HB2  1 
ATOM   3676 H HB3  . MET A 1 252 ? 36.659 -2.811  20.300  1.00 18.03 ? 252 MET A HB3  1 
ATOM   3677 H HG2  . MET A 1 252 ? 38.969 -2.862  20.500  1.00 19.01 ? 252 MET A HG2  1 
ATOM   3678 H HG3  . MET A 1 252 ? 39.054 -3.910  19.308  1.00 19.01 ? 252 MET A HG3  1 
ATOM   3679 H HE1  . MET A 1 252 ? 37.819 0.295   18.683  1.00 21.99 ? 252 MET A HE1  1 
ATOM   3680 H HE2  . MET A 1 252 ? 36.900 -0.792  19.388  1.00 21.99 ? 252 MET A HE2  1 
ATOM   3681 H HE3  . MET A 1 252 ? 38.237 -0.305  20.094  1.00 21.99 ? 252 MET A HE3  1 
ATOM   3682 N N    . SER A 1 253 ? 34.869 -4.573  21.965  1.00 14.73 ? 253 SER A N    1 
ATOM   3683 C CA   . SER A 1 253 ? 33.437 -4.779  22.030  1.00 14.93 ? 253 SER A CA   1 
ATOM   3684 C C    . SER A 1 253 ? 32.788 -4.130  20.813  1.00 13.84 ? 253 SER A C    1 
ATOM   3685 O O    . SER A 1 253 ? 33.325 -3.213  20.187  1.00 13.70 ? 253 SER A O    1 
ATOM   3686 C CB   . SER A 1 253 ? 32.838 -4.185  23.302  1.00 14.92 ? 253 SER A CB   1 
ATOM   3687 O OG   . SER A 1 253 ? 32.830 -2.765  23.270  1.00 16.29 ? 253 SER A OG   1 
ATOM   3688 H H    . SER A 1 253 ? 35.184 -4.025  22.548  1.00 17.68 ? 253 SER A H    1 
ATOM   3689 H HA   . SER A 1 253 ? 33.248 -5.731  22.042  1.00 17.92 ? 253 SER A HA   1 
ATOM   3690 H HB2  . SER A 1 253 ? 31.925 -4.500  23.392  1.00 17.90 ? 253 SER A HB2  1 
ATOM   3691 H HB3  . SER A 1 253 ? 33.366 -4.477  24.061  1.00 17.90 ? 253 SER A HB3  1 
ATOM   3692 H HG   . SER A 1 253 ? 32.468 -2.463  23.965  1.00 19.55 ? 253 SER A HG   1 
ATOM   3693 N N    . ASN A 1 254 ? 31.607 -4.625  20.467  1.00 14.18 ? 254 ASN A N    1 
ATOM   3694 C CA   . ASN A 1 254 ? 30.835 -4.018  19.393  1.00 13.41 ? 254 ASN A CA   1 
ATOM   3695 C C    . ASN A 1 254 ? 30.619 -2.526  19.633  1.00 12.97 ? 254 ASN A C    1 
ATOM   3696 O O    . ASN A 1 254 ? 30.785 -1.712  18.727  1.00 12.42 ? 254 ASN A O    1 
ATOM   3697 C CB   . ASN A 1 254 ? 29.507 -4.748  19.248  1.00 14.34 ? 254 ASN A CB   1 
ATOM   3698 C CG   . ASN A 1 254 ? 28.683 -4.224  18.102  1.00 13.31 ? 254 ASN A CG   1 
ATOM   3699 O OD1  . ASN A 1 254 ? 27.771 -3.424  18.285  1.00 15.24 ? 254 ASN A OD1  1 
ATOM   3700 N ND2  . ASN A 1 254 ? 29.022 -4.655  16.883  1.00 14.57 ? 254 ASN A ND2  1 
ATOM   3701 H H    . ASN A 1 254 ? 31.233 -5.307  20.834  1.00 17.01 ? 254 ASN A H    1 
ATOM   3702 H HA   . ASN A 1 254 ? 31.322 -4.107  18.559  1.00 16.09 ? 254 ASN A HA   1 
ATOM   3703 H HB2  . ASN A 1 254 ? 29.678 -5.690  19.089  1.00 17.21 ? 254 ASN A HB2  1 
ATOM   3704 H HB3  . ASN A 1 254 ? 28.993 -4.637  20.063  1.00 17.21 ? 254 ASN A HB3  1 
ATOM   3705 H HD21 . ASN A 1 254 ? 28.583 -4.386  16.194  1.00 17.48 ? 254 ASN A HD21 1 
ATOM   3706 H HD22 . ASN A 1 254 ? 29.680 -5.201  16.788  1.00 17.48 ? 254 ASN A HD22 1 
ATOM   3707 N N    . ALA A 1 255 ? 30.261 -2.144  20.856  1.00 13.31 ? 255 ALA A N    1 
ATOM   3708 C CA   . ALA A 1 255 ? 30.000 -0.733  21.146  1.00 13.05 ? 255 ALA A CA   1 
ATOM   3709 C C    . ALA A 1 255 ? 31.259 0.112   20.984  1.00 12.97 ? 255 ALA A C    1 
ATOM   3710 O O    . ALA A 1 255 ? 31.210 1.188   20.378  1.00 12.54 ? 255 ALA A O    1 
ATOM   3711 C CB   . ALA A 1 255 ? 29.419 -0.610  22.555  1.00 14.36 ? 255 ALA A CB   1 
ATOM   3712 H H    . ALA A 1 255 ? 30.163 -2.672  21.528  1.00 15.98 ? 255 ALA A H    1 
ATOM   3713 H HA   . ALA A 1 255 ? 29.345 -0.388  20.520  1.00 15.67 ? 255 ALA A HA   1 
ATOM   3714 H HB1  . ALA A 1 255 ? 29.238 0.325   22.741  1.00 17.23 ? 255 ALA A HB1  1 
ATOM   3715 H HB2  . ALA A 1 255 ? 28.597 -1.122  22.604  1.00 17.23 ? 255 ALA A HB2  1 
ATOM   3716 H HB3  . ALA A 1 255 ? 30.063 -0.955  23.194  1.00 17.23 ? 255 ALA A HB3  1 
ATOM   3717 N N    . GLU A 1 256 ? 32.393 -0.351  21.503  1.00 13.48 ? 256 GLU A N    1 
ATOM   3718 C CA   . GLU A 1 256 ? 33.633 0.411   21.358  1.00 13.55 ? 256 GLU A CA   1 
ATOM   3719 C C    . GLU A 1 256 ? 34.050 0.526   19.907  1.00 13.02 ? 256 GLU A C    1 
ATOM   3720 O O    . GLU A 1 256 ? 34.574 1.558   19.478  1.00 12.85 ? 256 GLU A O    1 
ATOM   3721 C CB   . GLU A 1 256 ? 34.735 -0.218  22.197  1.00 14.36 ? 256 GLU A CB   1 
ATOM   3722 C CG   . GLU A 1 256 ? 34.509 -0.089  23.708  1.00 15.02 ? 256 GLU A CG   1 
ATOM   3723 C CD   . GLU A 1 256 ? 34.690 1.336   24.196  1.00 17.54 ? 256 GLU A CD   1 
ATOM   3724 O OE1  . GLU A 1 256 ? 34.149 1.680   25.256  1.00 16.76 ? 256 GLU A OE1  1 
ATOM   3725 O OE2  . GLU A 1 256 ? 35.451 2.117   23.601  1.00 18.94 ? 256 GLU A OE2  1 
ATOM   3726 H H    . GLU A 1 256 ? 32.473 -1.090  21.937  1.00 16.18 ? 256 GLU A H    1 
ATOM   3727 H HA   . GLU A 1 256 ? 33.487 1.311   21.689  1.00 16.27 ? 256 GLU A HA   1 
ATOM   3728 H HB2  . GLU A 1 256 ? 34.787 -1.163  21.985  1.00 17.23 ? 256 GLU A HB2  1 
ATOM   3729 H HB3  . GLU A 1 256 ? 35.575 0.217   21.985  1.00 17.23 ? 256 GLU A HB3  1 
ATOM   3730 H HG2  . GLU A 1 256 ? 33.604 -0.368  23.919  1.00 18.03 ? 256 GLU A HG2  1 
ATOM   3731 H HG3  . GLU A 1 256 ? 35.147 -0.652  24.174  1.00 18.03 ? 256 GLU A HG3  1 
ATOM   3732 N N    . TYR A 1 257 ? 33.822 -0.531  19.121  1.00 12.85 ? 257 TYR A N    1 
ATOM   3733 C CA   . TYR A 1 257 ? 34.168 -0.494  17.695  1.00 12.42 ? 257 TYR A CA   1 
ATOM   3734 C C    . TYR A 1 257 ? 33.369 0.579   16.980  1.00 11.79 ? 257 TYR A C    1 
ATOM   3735 O O    . TYR A 1 257 ? 33.917 1.363   16.199  1.00 11.84 ? 257 TYR A O    1 
ATOM   3736 C CB   . TYR A 1 257 ? 33.913 -1.873  17.116  1.00 12.50 ? 257 TYR A CB   1 
ATOM   3737 C CG   . TYR A 1 257 ? 34.650 -2.076  15.818  1.00 12.36 ? 257 TYR A CG   1 
ATOM   3738 C CD1  . TYR A 1 257 ? 36.007 -2.305  15.801  1.00 12.84 ? 257 TYR A CD1  1 
ATOM   3739 C CD2  . TYR A 1 257 ? 34.000 -2.004  14.594  1.00 12.58 ? 257 TYR A CD2  1 
ATOM   3740 C CE1  . TYR A 1 257 ? 36.718 -2.477  14.632  1.00 15.43 ? 257 TYR A CE1  1 
ATOM   3741 C CE2  . TYR A 1 257 ? 34.708 -2.186  13.412  1.00 12.61 ? 257 TYR A CE2  1 
ATOM   3742 C CZ   . TYR A 1 257 ? 36.049 -2.408  13.456  1.00 12.30 ? 257 TYR A CZ   1 
ATOM   3743 O OH   . TYR A 1 257 ? 36.772 -2.553  12.254  1.00 15.10 ? 257 TYR A OH   1 
ATOM   3744 H H    . TYR A 1 257 ? 33.473 -1.272  19.383  1.00 15.42 ? 257 TYR A H    1 
ATOM   3745 H HA   . TYR A 1 257 ? 35.105 -0.278  17.568  1.00 14.90 ? 257 TYR A HA   1 
ATOM   3746 H HB2  . TYR A 1 257 ? 34.214 -2.545  17.747  1.00 15.00 ? 257 TYR A HB2  1 
ATOM   3747 H HB3  . TYR A 1 257 ? 32.963 -1.978  16.948  1.00 15.00 ? 257 TYR A HB3  1 
ATOM   3748 H HD1  . TYR A 1 257 ? 36.463 -2.344  16.611  1.00 15.40 ? 257 TYR A HD1  1 
ATOM   3749 H HD2  . TYR A 1 257 ? 33.087 -1.834  14.565  1.00 15.09 ? 257 TYR A HD2  1 
ATOM   3750 H HE1  . TYR A 1 257 ? 37.634 -2.637  14.651  1.00 18.51 ? 257 TYR A HE1  1 
ATOM   3751 H HE2  . TYR A 1 257 ? 34.266 -2.155  12.594  1.00 15.13 ? 257 TYR A HE2  1 
ATOM   3752 H HH   . TYR A 1 257 ? 37.584 -2.689  12.422  1.00 18.12 ? 257 TYR A HH   1 
ATOM   3753 N N    . LEU A 1 258 ? 32.072 0.659   17.283  1.00 11.61 ? 258 LEU A N    1 
ATOM   3754 C CA   . LEU A 1 258 ? 31.206 1.676   16.692  1.00 11.15 ? 258 LEU A CA   1 
ATOM   3755 C C    . LEU A 1 258 ? 31.549 3.074   17.202  1.00 11.24 ? 258 LEU A C    1 
ATOM   3756 O O    . LEU A 1 258 ? 31.550 4.028   16.416  1.00 11.96 ? 258 LEU A O    1 
ATOM   3757 C CB   . LEU A 1 258 ? 29.742 1.331   16.924  1.00 11.63 ? 258 LEU A CB   1 
ATOM   3758 C CG   . LEU A 1 258 ? 29.211 0.312   15.904  1.00 11.09 ? 258 LEU A CG   1 
ATOM   3759 C CD1  . LEU A 1 258 ? 27.999 -0.434  16.405  1.00 14.59 ? 258 LEU A CD1  1 
ATOM   3760 C CD2  . LEU A 1 258 ? 28.895 1.004   14.593  1.00 13.88 ? 258 LEU A CD2  1 
ATOM   3761 H H    . LEU A 1 258 ? 31.668 0.133   17.830  1.00 13.93 ? 258 LEU A H    1 
ATOM   3762 H HA   . LEU A 1 258 ? 31.345 1.682   15.732  1.00 13.38 ? 258 LEU A HA   1 
ATOM   3763 H HB2  . LEU A 1 258 ? 29.644 0.950   17.811  1.00 13.96 ? 258 LEU A HB2  1 
ATOM   3764 H HB3  . LEU A 1 258 ? 29.211 2.139   16.849  1.00 13.96 ? 258 LEU A HB3  1 
ATOM   3765 H HG   . LEU A 1 258 ? 29.905 -0.350  15.760  1.00 13.31 ? 258 LEU A HG   1 
ATOM   3766 H HD11 . LEU A 1 258 ? 27.707 -1.057  15.721  1.00 17.51 ? 258 LEU A HD11 1 
ATOM   3767 H HD12 . LEU A 1 258 ? 28.237 -0.917  17.212  1.00 17.51 ? 258 LEU A HD12 1 
ATOM   3768 H HD13 . LEU A 1 258 ? 27.293 0.203   16.596  1.00 17.51 ? 258 LEU A HD13 1 
ATOM   3769 H HD21 . LEU A 1 258 ? 28.577 0.345   13.956  1.00 16.66 ? 258 LEU A HD21 1 
ATOM   3770 H HD22 . LEU A 1 258 ? 28.211 1.674   14.746  1.00 16.66 ? 258 LEU A HD22 1 
ATOM   3771 H HD23 . LEU A 1 258 ? 29.701 1.426   14.256  1.00 16.66 ? 258 LEU A HD23 1 
ATOM   3772 N N    . VAL A 1 259 ? 31.872 3.235   18.484  1.00 11.73 ? 259 VAL A N    1 
ATOM   3773 C CA   . VAL A 1 259 ? 32.312 4.542   18.979  1.00 11.98 ? 259 VAL A CA   1 
ATOM   3774 C C    . VAL A 1 259 ? 33.450 5.059   18.107  1.00 11.92 ? 259 VAL A C    1 
ATOM   3775 O O    . VAL A 1 259 ? 33.458 6.206   17.658  1.00 12.10 ? 259 VAL A O    1 
ATOM   3776 C CB   . VAL A 1 259 ? 32.761 4.422   20.444  1.00 12.65 ? 259 VAL A CB   1 
ATOM   3777 C CG1  . VAL A 1 259 ? 33.580 5.658   20.875  1.00 13.74 ? 259 VAL A CG1  1 
ATOM   3778 C CG2  . VAL A 1 259 ? 31.555 4.244   21.392  1.00 12.98 ? 259 VAL A CG2  1 
ATOM   3779 H H    . VAL A 1 259 ? 31.847 2.615   19.080  1.00 14.07 ? 259 VAL A H    1 
ATOM   3780 H HA   . VAL A 1 259 ? 31.571 5.167   18.931  1.00 14.37 ? 259 VAL A HA   1 
ATOM   3781 H HB   . VAL A 1 259 ? 33.322 3.634   20.512  1.00 15.19 ? 259 VAL A HB   1 
ATOM   3782 H HG11 . VAL A 1 259 ? 33.655 5.665   21.842  1.00 16.49 ? 259 VAL A HG11 1 
ATOM   3783 H HG12 . VAL A 1 259 ? 34.462 5.609   20.475  1.00 16.49 ? 259 VAL A HG12 1 
ATOM   3784 H HG13 . VAL A 1 259 ? 33.124 6.460   20.574  1.00 16.49 ? 259 VAL A HG13 1 
ATOM   3785 H HG21 . VAL A 1 259 ? 31.880 4.138   22.300  1.00 15.57 ? 259 VAL A HG21 1 
ATOM   3786 H HG22 . VAL A 1 259 ? 30.988 5.028   21.334  1.00 15.57 ? 259 VAL A HG22 1 
ATOM   3787 H HG23 . VAL A 1 259 ? 31.057 3.455   21.125  1.00 15.57 ? 259 VAL A HG23 1 
ATOM   3788 N N    . GLU A 1 260 ? 34.444 4.215   17.862  1.00 12.07 ? 260 GLU A N    1 
ATOM   3789 C CA   . GLU A 1 260 ? 35.614 4.662   17.126  1.00 13.89 ? 260 GLU A CA   1 
ATOM   3790 C C    . GLU A 1 260 ? 35.291 4.926   15.661  1.00 13.12 ? 260 GLU A C    1 
ATOM   3791 O O    . GLU A 1 260 ? 35.787 5.895   15.072  1.00 13.02 ? 260 GLU A O    1 
ATOM   3792 C CB   . GLU A 1 260 ? 36.720 3.629   17.294  1.00 16.26 ? 260 GLU A CB   1 
ATOM   3793 C CG   . GLU A 1 260 ? 38.069 4.187   17.002  1.00 16.59 ? 260 GLU A CG   1 
ATOM   3794 C CD   . GLU A 1 260 ? 39.220 3.292   17.420  1.00 17.51 ? 260 GLU A CD   1 
ATOM   3795 O OE1  . GLU A 1 260 ? 39.029 2.432   18.305  1.00 22.83 ? 260 GLU A OE1  1 
ATOM   3796 O OE2  . GLU A 1 260 ? 40.339 3.511   16.926  1.00 18.90 ? 260 GLU A OE2  1 
ATOM   3797 H H    . GLU A 1 260 ? 34.465 3.391   18.108  1.00 14.48 ? 260 GLU A H    1 
ATOM   3798 H HA   . GLU A 1 260 ? 35.931 5.504   17.488  1.00 16.67 ? 260 GLU A HA   1 
ATOM   3799 H HB2  . GLU A 1 260 ? 36.718 3.308   18.210  1.00 19.51 ? 260 GLU A HB2  1 
ATOM   3800 H HB3  . GLU A 1 260 ? 36.560 2.892   16.684  1.00 19.51 ? 260 GLU A HB3  1 
ATOM   3801 H HG2  . GLU A 1 260 ? 38.143 4.333   16.046  1.00 19.90 ? 260 GLU A HG2  1 
ATOM   3802 H HG3  . GLU A 1 260 ? 38.165 5.028   17.475  1.00 19.90 ? 260 GLU A HG3  1 
ATOM   3803 N N    . GLY A 1 261 ? 34.448 4.113   15.056  1.00 11.51 ? 261 GLY A N    1 
ATOM   3804 C CA   . GLY A 1 261 ? 34.085 4.366   13.670  1.00 12.05 ? 261 GLY A CA   1 
ATOM   3805 C C    . GLY A 1 261 ? 33.257 5.624   13.503  1.00 11.36 ? 261 GLY A C    1 
ATOM   3806 O O    . GLY A 1 261 ? 33.394 6.358   12.513  1.00 12.03 ? 261 GLY A O    1 
ATOM   3807 H H    . GLY A 1 261 ? 34.077 3.423   15.412  1.00 13.81 ? 261 GLY A H    1 
ATOM   3808 H HA2  . GLY A 1 261 ? 34.893 4.461   13.140  1.00 14.46 ? 261 GLY A HA2  1 
ATOM   3809 H HA3  . GLY A 1 261 ? 33.572 3.616   13.331  1.00 14.46 ? 261 GLY A HA3  1 
ATOM   3810 N N    . ILE A 1 262 ? 32.367 5.892   14.461  1.00 10.64 ? 262 ILE A N    1 
ATOM   3811 C CA   . ILE A 1 262 ? 31.565 7.100   14.425  1.00 10.62 ? 262 ILE A CA   1 
ATOM   3812 C C    . ILE A 1 262 ? 32.474 8.314   14.437  1.00 10.97 ? 262 ILE A C    1 
ATOM   3813 O O    . ILE A 1 262 ? 32.286 9.263   13.660  1.00 12.18 ? 262 ILE A O    1 
ATOM   3814 C CB   . ILE A 1 262 ? 30.546 7.111   15.576  1.00 12.01 ? 262 ILE A CB   1 
ATOM   3815 C CG1  . ILE A 1 262 ? 29.398 6.160   15.251  1.00 11.34 ? 262 ILE A CG1  1 
ATOM   3816 C CG2  . ILE A 1 262 ? 30.017 8.514   15.839  1.00 12.73 ? 262 ILE A CG2  1 
ATOM   3817 C CD1  . ILE A 1 262 ? 28.545 5.814   16.456  1.00 12.58 ? 262 ILE A CD1  1 
ATOM   3818 H H    . ILE A 1 262 ? 32.212 5.387   15.139  1.00 12.77 ? 262 ILE A H    1 
ATOM   3819 H HA   . ILE A 1 262 ? 31.055 7.121   13.600  1.00 12.75 ? 262 ILE A HA   1 
ATOM   3820 H HB   . ILE A 1 262 ? 30.995 6.811   16.382  1.00 14.42 ? 262 ILE A HB   1 
ATOM   3821 H HG12 . ILE A 1 262 ? 28.824 6.577   14.589  1.00 13.61 ? 262 ILE A HG12 1 
ATOM   3822 H HG13 . ILE A 1 262 ? 29.766 5.335   14.898  1.00 13.61 ? 262 ILE A HG13 1 
ATOM   3823 H HG21 . ILE A 1 262 ? 29.219 8.453   16.386  1.00 15.27 ? 262 ILE A HG21 1 
ATOM   3824 H HG22 . ILE A 1 262 ? 30.698 9.026   16.303  1.00 15.27 ? 262 ILE A HG22 1 
ATOM   3825 H HG23 . ILE A 1 262 ? 29.807 8.935   14.992  1.00 15.27 ? 262 ILE A HG23 1 
ATOM   3826 H HD11 . ILE A 1 262 ? 27.895 5.140   16.200  1.00 15.09 ? 262 ILE A HD11 1 
ATOM   3827 H HD12 . ILE A 1 262 ? 29.118 5.470   17.160  1.00 15.09 ? 262 ILE A HD12 1 
ATOM   3828 H HD13 . ILE A 1 262 ? 28.090 6.614   16.761  1.00 15.09 ? 262 ILE A HD13 1 
ATOM   3829 N N    . GLU A 1 263 ? 33.475 8.315   15.314  1.00 11.90 ? 263 GLU A N    1 
ATOM   3830 C CA   . GLU A 1 263 ? 34.356 9.464   15.403  1.00 12.51 ? 263 GLU A CA   1 
ATOM   3831 C C    . GLU A 1 263 ? 35.077 9.707   14.082  1.00 13.00 ? 263 GLU A C    1 
ATOM   3832 O O    . GLU A 1 263 ? 35.181 10.852  13.618  1.00 14.55 ? 263 GLU A O    1 
ATOM   3833 C CB   . GLU A 1 263 ? 35.331 9.252   16.558  1.00 15.46 ? 263 GLU A CB   1 
ATOM   3834 C CG   . GLU A 1 263 ? 36.335 10.366  16.724  1.00 20.08 ? 263 GLU A CG   1 
ATOM   3835 C CD   . GLU A 1 263 ? 37.392 10.060  17.756  1.00 28.20 ? 263 GLU A CD   1 
ATOM   3836 O OE1  . GLU A 1 263 ? 37.118 9.248   18.672  1.00 30.95 ? 263 GLU A OE1  1 
ATOM   3837 O OE2  . GLU A 1 263 ? 38.464 10.683  17.698  1.00 32.18 ? 263 GLU A OE2  1 
ATOM   3838 H H    . GLU A 1 263 ? 33.658 7.674   15.857  1.00 14.28 ? 263 GLU A H    1 
ATOM   3839 H HA   . GLU A 1 263 ? 33.843 10.265  15.593  1.00 15.01 ? 263 GLU A HA   1 
ATOM   3840 H HB2  . GLU A 1 263 ? 34.827 9.184   17.384  1.00 18.56 ? 263 GLU A HB2  1 
ATOM   3841 H HB3  . GLU A 1 263 ? 35.824 8.431   16.402  1.00 18.56 ? 263 GLU A HB3  1 
ATOM   3842 H HG2  . GLU A 1 263 ? 36.781 10.517  15.876  1.00 24.10 ? 263 GLU A HG2  1 
ATOM   3843 H HG3  . GLU A 1 263 ? 35.870 11.170  17.002  1.00 24.10 ? 263 GLU A HG3  1 
ATOM   3844 N N    . ALA A 1 264 ? 35.591 8.646   13.454  1.00 12.75 ? 264 ALA A N    1 
ATOM   3845 C CA   . ALA A 1 264 ? 36.310 8.800   12.187  1.00 13.35 ? 264 ALA A CA   1 
ATOM   3846 C C    . ALA A 1 264 ? 35.381 9.323   11.104  1.00 12.78 ? 264 ALA A C    1 
ATOM   3847 O O    . ALA A 1 264 ? 35.769 10.189  10.299  1.00 13.33 ? 264 ALA A O    1 
ATOM   3848 C CB   . ALA A 1 264 ? 36.890 7.456   11.732  1.00 14.54 ? 264 ALA A CB   1 
ATOM   3849 H H    . ALA A 1 264 ? 35.538 7.835   13.735  1.00 15.30 ? 264 ALA A H    1 
ATOM   3850 H HA   . ALA A 1 264 ? 37.040 9.425   12.325  1.00 16.02 ? 264 ALA A HA   1 
ATOM   3851 H HB1  . ALA A 1 264 ? 37.345 7.580   10.884  1.00 17.45 ? 264 ALA A HB1  1 
ATOM   3852 H HB2  . ALA A 1 264 ? 37.517 7.140   12.401  1.00 17.45 ? 264 ALA A HB2  1 
ATOM   3853 H HB3  . ALA A 1 264 ? 36.166 6.819   11.629  1.00 17.45 ? 264 ALA A HB3  1 
ATOM   3854 N N    . THR A 1 265 ? 34.165 8.775   11.026  1.00 11.42 ? 265 THR A N    1 
ATOM   3855 C CA   . THR A 1 265 ? 33.231 9.161   9.983   1.00 11.46 ? 265 THR A CA   1 
ATOM   3856 C C    . THR A 1 265 ? 32.776 10.596  10.141  1.00 12.29 ? 265 THR A C    1 
ATOM   3857 O O    . THR A 1 265 ? 32.674 11.324  9.153   1.00 12.35 ? 265 THR A O    1 
ATOM   3858 C CB   . THR A 1 265 ? 32.029 8.212   9.964   1.00 11.77 ? 265 THR A CB   1 
ATOM   3859 O OG1  . THR A 1 265 ? 32.469 6.853   9.825   1.00 12.65 ? 265 THR A OG1  1 
ATOM   3860 C CG2  . THR A 1 265 ? 31.099 8.524   8.832   1.00 13.57 ? 265 THR A CG2  1 
ATOM   3861 H H    . THR A 1 265 ? 33.862 8.179   11.567  1.00 13.71 ? 265 THR A H    1 
ATOM   3862 H HA   . THR A 1 265 ? 33.683 9.087   9.128   1.00 13.76 ? 265 THR A HA   1 
ATOM   3863 H HB   . THR A 1 265 ? 31.549 8.321   10.799  1.00 14.13 ? 265 THR A HB   1 
ATOM   3864 H HG1  . THR A 1 265 ? 32.953 6.640   10.478  1.00 15.18 ? 265 THR A HG1  1 
ATOM   3865 H HG21 . THR A 1 265 ? 30.375 7.878   8.809   1.00 16.28 ? 265 THR A HG21 1 
ATOM   3866 H HG22 . THR A 1 265 ? 30.725 9.412   8.945   1.00 16.28 ? 265 THR A HG22 1 
ATOM   3867 H HG23 . THR A 1 265 ? 31.578 8.490   7.989   1.00 16.28 ? 265 THR A HG23 1 
ATOM   3868 N N    . GLN A 1 266 ? 32.493 11.028  11.364  1.00 11.67 ? 266 GLN A N    1 
ATOM   3869 C CA   . GLN A 1 266 ? 32.177 12.425  11.631  1.00 11.48 ? 266 GLN A CA   1 
ATOM   3870 C C    . GLN A 1 266 ? 33.278 13.335  11.115  1.00 12.62 ? 266 GLN A C    1 
ATOM   3871 O O    . GLN A 1 266 ? 33.013 14.344  10.451  1.00 13.26 ? 266 GLN A O    1 
ATOM   3872 C CB   . GLN A 1 266 ? 31.966 12.638  13.133  1.00 12.73 ? 266 GLN A CB   1 
ATOM   3873 C CG   . GLN A 1 266 ? 30.651 12.044  13.657  1.00 11.79 ? 266 GLN A CG   1 
ATOM   3874 C CD   . GLN A 1 266 ? 30.599 12.052  15.161  1.00 11.91 ? 266 GLN A CD   1 
ATOM   3875 O OE1  . GLN A 1 266 ? 31.625 12.106  15.846  1.00 13.91 ? 266 GLN A OE1  1 
ATOM   3876 N NE2  . GLN A 1 266 ? 29.393 11.996  15.699  1.00 13.33 ? 266 GLN A NE2  1 
ATOM   3877 H H    . GLN A 1 266 ? 32.477 10.529  12.064  1.00 14.01 ? 266 GLN A H    1 
ATOM   3878 H HA   . GLN A 1 266 ? 31.351 12.654  11.176  1.00 13.78 ? 266 GLN A HA   1 
ATOM   3879 H HB2  . GLN A 1 266 ? 32.696 12.216  13.614  1.00 15.28 ? 266 GLN A HB2  1 
ATOM   3880 H HB3  . GLN A 1 266 ? 31.956 13.591  13.316  1.00 15.28 ? 266 GLN A HB3  1 
ATOM   3881 H HG2  . GLN A 1 266 ? 29.907 12.570  13.324  1.00 14.15 ? 266 GLN A HG2  1 
ATOM   3882 H HG3  . GLN A 1 266 ? 30.571 11.126  13.354  1.00 14.15 ? 266 GLN A HG3  1 
ATOM   3883 H HE21 . GLN A 1 266 ? 28.698 11.959  15.193  1.00 16.00 ? 266 GLN A HE21 1 
ATOM   3884 H HE22 . GLN A 1 266 ? 29.303 11.997  16.554  1.00 16.00 ? 266 GLN A HE22 1 
ATOM   3885 N N    . LYS A 1 267 ? 34.536 12.995  11.413  1.00 13.17 ? 267 LYS A N    1 
ATOM   3886 C CA   . LYS A 1 267 ? 35.638 13.842  10.965  1.00 14.02 ? 267 LYS A CA   1 
ATOM   3887 C C    . LYS A 1 267 ? 35.701 13.906  9.446   1.00 13.46 ? 267 LYS A C    1 
ATOM   3888 O O    . LYS A 1 267 ? 35.865 14.985  8.871   1.00 14.53 ? 267 LYS A O    1 
ATOM   3889 C CB   . LYS A 1 267 ? 36.957 13.339  11.545  1.00 14.56 ? 267 LYS A CB   1 
ATOM   3890 C CG   . LYS A 1 267 ? 37.092 13.542  13.036  1.00 20.31 ? 267 LYS A CG   1 
ATOM   3891 C CD   . LYS A 1 267 ? 38.289 12.783  13.595  1.00 26.25 ? 267 LYS A CD   1 
ATOM   3892 C CE   . LYS A 1 267 ? 38.453 13.045  15.081  1.00 31.55 ? 267 LYS A CE   1 
ATOM   3893 N NZ   . LYS A 1 267 ? 39.539 12.217  15.684  1.00 39.11 ? 267 LYS A NZ   1 
ATOM   3894 H H    . LYS A 1 267 ? 34.769 12.299  11.861  1.00 15.80 ? 267 LYS A H    1 
ATOM   3895 H HA   . LYS A 1 267 ? 35.496 14.743  11.295  1.00 16.82 ? 267 LYS A HA   1 
ATOM   3896 H HB2  . LYS A 1 267 ? 37.031 12.388  11.369  1.00 17.47 ? 267 LYS A HB2  1 
ATOM   3897 H HB3  . LYS A 1 267 ? 37.686 13.813  11.116  1.00 17.47 ? 267 LYS A HB3  1 
ATOM   3898 H HG2  . LYS A 1 267 ? 37.215 14.486  13.222  1.00 24.37 ? 267 LYS A HG2  1 
ATOM   3899 H HG3  . LYS A 1 267 ? 36.291 13.218  13.478  1.00 24.37 ? 267 LYS A HG3  1 
ATOM   3900 H HD2  . LYS A 1 267 ? 38.158 11.831  13.464  1.00 31.50 ? 267 LYS A HD2  1 
ATOM   3901 H HD3  . LYS A 1 267 ? 39.096 13.072  13.141  1.00 31.50 ? 267 LYS A HD3  1 
ATOM   3902 H HE2  . LYS A 1 267 ? 38.675 13.979  15.217  1.00 37.86 ? 267 LYS A HE2  1 
ATOM   3903 H HE3  . LYS A 1 267 ? 37.623 12.831  15.536  1.00 37.86 ? 267 LYS A HE3  1 
ATOM   3904 H HZ1  . LYS A 1 267 ? 39.614 12.399  16.552  1.00 46.93 ? 267 LYS A HZ1  1 
ATOM   3905 H HZ2  . LYS A 1 267 ? 39.353 11.352  15.586  1.00 46.93 ? 267 LYS A HZ2  1 
ATOM   3906 H HZ3  . LYS A 1 267 ? 40.314 12.393  15.284  1.00 46.93 ? 267 LYS A HZ3  1 
ATOM   3907 N N    . ALA A 1 268 ? 35.557 12.770  8.777   1.00 13.18 ? 268 ALA A N    1 
ATOM   3908 C CA   . ALA A 1 268 ? 35.624 12.758  7.322   1.00 13.32 ? 268 ALA A CA   1 
ATOM   3909 C C    . ALA A 1 268 ? 34.467 13.542  6.717   1.00 12.60 ? 268 ALA A C    1 
ATOM   3910 O O    . ALA A 1 268 ? 34.676 14.380  5.829   1.00 14.08 ? 268 ALA A O    1 
ATOM   3911 C CB   . ALA A 1 268 ? 35.623 11.320  6.811   1.00 13.12 ? 268 ALA A CB   1 
ATOM   3912 H H    . ALA A 1 268 ? 35.422 12.001  9.136   1.00 15.81 ? 268 ALA A H    1 
ATOM   3913 H HA   . ALA A 1 268 ? 36.453 13.176  7.042   1.00 15.99 ? 268 ALA A HA   1 
ATOM   3914 H HB1  . ALA A 1 268 ? 35.614 11.329  5.841   1.00 15.75 ? 268 ALA A HB1  1 
ATOM   3915 H HB2  . ALA A 1 268 ? 36.422 10.871  7.130   1.00 15.75 ? 268 ALA A HB2  1 
ATOM   3916 H HB3  . ALA A 1 268 ? 34.833 10.866  7.145   1.00 15.75 ? 268 ALA A HB3  1 
ATOM   3917 N N    . ALA A 1 269 ? 33.246 13.301  7.200   1.00 11.90 ? 269 ALA A N    1 
ATOM   3918 C CA   . ALA A 1 269 ? 32.085 14.001  6.664   1.00 12.91 ? 269 ALA A CA   1 
ATOM   3919 C C    . ALA A 1 269 ? 32.192 15.499  6.883   1.00 14.29 ? 269 ALA A C    1 
ATOM   3920 O O    . ALA A 1 269 ? 31.863 16.298  5.993   1.00 14.86 ? 269 ALA A O    1 
ATOM   3921 C CB   . ALA A 1 269 ? 30.825 13.438  7.285   1.00 11.72 ? 269 ALA A CB   1 
ATOM   3922 H H    . ALA A 1 269 ? 33.067 12.744  7.830   1.00 14.28 ? 269 ALA A H    1 
ATOM   3923 H HA   . ALA A 1 269 ? 32.035 13.856  5.706   1.00 15.49 ? 269 ALA A HA   1 
ATOM   3924 H HB1  . ALA A 1 269 ? 30.056 13.884  6.899   1.00 14.06 ? 269 ALA A HB1  1 
ATOM   3925 H HB2  . ALA A 1 269 ? 30.781 12.486  7.104   1.00 14.06 ? 269 ALA A HB2  1 
ATOM   3926 H HB3  . ALA A 1 269 ? 30.850 13.591  8.243   1.00 14.06 ? 269 ALA A HB3  1 
ATOM   3927 N N    . GLN A 1 270 ? 32.648 15.914  8.057   1.00 13.44 ? 270 GLN A N    1 
ATOM   3928 C CA   . GLN A 1 270 ? 32.757 17.336  8.362   1.00 13.66 ? 270 GLN A CA   1 
ATOM   3929 C C    . GLN A 1 270 ? 33.831 18.009  7.533   1.00 16.67 ? 270 GLN A C    1 
ATOM   3930 O O    . GLN A 1 270 ? 33.794 19.237  7.356   1.00 19.08 ? 270 GLN A O    1 
ATOM   3931 C CB   . GLN A 1 270 ? 33.009 17.530  9.855   1.00 14.62 ? 270 GLN A CB   1 
ATOM   3932 C CG   . GLN A 1 270 ? 31.794 17.156  10.692  1.00 16.30 ? 270 GLN A CG   1 
ATOM   3933 C CD   . GLN A 1 270 ? 32.092 16.970  12.163  1.00 18.56 ? 270 GLN A CD   1 
ATOM   3934 O OE1  . GLN A 1 270 ? 33.082 17.487  12.704  1.00 22.48 ? 270 GLN A OE1  1 
ATOM   3935 N NE2  . GLN A 1 270 ? 31.208 16.275  12.852  1.00 17.03 ? 270 GLN A NE2  1 
ATOM   3936 H H    . GLN A 1 270 ? 32.900 15.395  8.694   1.00 16.12 ? 270 GLN A H    1 
ATOM   3937 H HA   . GLN A 1 270 ? 31.918 17.777  8.157   1.00 16.40 ? 270 GLN A HA   1 
ATOM   3938 H HB2  . GLN A 1 270 ? 33.751 16.968  10.129  1.00 17.55 ? 270 GLN A HB2  1 
ATOM   3939 H HB3  . GLN A 1 270 ? 33.219 18.462  10.024  1.00 17.55 ? 270 GLN A HB3  1 
ATOM   3940 H HG2  . GLN A 1 270 ? 31.132 17.861  10.612  1.00 19.56 ? 270 GLN A HG2  1 
ATOM   3941 H HG3  . GLN A 1 270 ? 31.431 16.321  10.357  1.00 19.56 ? 270 GLN A HG3  1 
ATOM   3942 H HE21 . GLN A 1 270 ? 30.511 15.958  12.460  1.00 20.43 ? 270 GLN A HE21 1 
ATOM   3943 H HE22 . GLN A 1 270 ? 31.328 16.139  13.692  1.00 20.43 ? 270 GLN A HE22 1 
ATOM   3944 N N    . SER A 1 271 ? 34.781 17.244  7.004   1.00 16.10 ? 271 SER A N    1 
ATOM   3945 C CA   . SER A 1 271 ? 35.805 17.798  6.129   1.00 16.51 ? 271 SER A CA   1 
ATOM   3946 C C    . SER A 1 271 ? 35.328 17.947  4.691   1.00 16.02 ? 271 SER A C    1 
ATOM   3947 O O    . SER A 1 271 ? 36.083 18.464  3.859   1.00 19.74 ? 271 SER A O    1 
ATOM   3948 C CB   . SER A 1 271 ? 37.075 16.937  6.167   1.00 20.00 ? 271 SER A CB   1 
ATOM   3949 O OG   . SER A 1 271 ? 36.989 15.791  5.339   1.00 19.98 ? 271 SER A OG   1 
ATOM   3950 H H    . SER A 1 271 ? 34.852 16.397  7.137   1.00 19.32 ? 271 SER A H    1 
ATOM   3951 H HA   . SER A 1 271 ? 36.046 18.678  6.460   1.00 19.82 ? 271 SER A HA   1 
ATOM   3952 H HB2  . SER A 1 271 ? 37.823 17.478  5.867   1.00 24.00 ? 271 SER A HB2  1 
ATOM   3953 H HB3  . SER A 1 271 ? 37.222 16.646  7.081   1.00 24.00 ? 271 SER A HB3  1 
ATOM   3954 H HG   . SER A 1 271 ? 36.329 15.322  5.564   1.00 23.97 ? 271 SER A HG   1 
ATOM   3955 N N    . GLY A 1 272 ? 34.113 17.512  4.369   1.00 15.67 ? 272 GLY A N    1 
ATOM   3956 C CA   . GLY A 1 272 ? 33.563 17.669  3.043   1.00 17.05 ? 272 GLY A CA   1 
ATOM   3957 C C    . GLY A 1 272 ? 33.737 16.479  2.124   1.00 15.11 ? 272 GLY A C    1 
ATOM   3958 O O    . GLY A 1 272 ? 33.429 16.593  0.929   1.00 17.11 ? 272 GLY A O    1 
ATOM   3959 H H    . GLY A 1 272 ? 33.582 17.115  4.918   1.00 18.80 ? 272 GLY A H    1 
ATOM   3960 H HA2  . GLY A 1 272 ? 32.612 17.843  3.122   1.00 20.45 ? 272 GLY A HA2  1 
ATOM   3961 H HA3  . GLY A 1 272 ? 33.989 18.432  2.621   1.00 20.45 ? 272 GLY A HA3  1 
ATOM   3962 N N    . LYS A 1 273 ? 34.210 15.359  2.643   1.00 14.59 ? 273 LYS A N    1 
ATOM   3963 C CA   . LYS A 1 273 ? 34.342 14.139  1.859   1.00 13.72 ? 273 LYS A CA   1 
ATOM   3964 C C    . LYS A 1 273 ? 32.985 13.479  1.690   1.00 14.01 ? 273 LYS A C    1 
ATOM   3965 O O    . LYS A 1 273 ? 32.164 13.474  2.605   1.00 14.17 ? 273 LYS A O    1 
ATOM   3966 C CB   . LYS A 1 273 ? 35.307 13.186  2.558   1.00 15.58 ? 273 LYS A CB   1 
ATOM   3967 C CG   . LYS A 1 273 ? 36.757 13.663  2.604   1.00 17.62 ? 273 LYS A CG   1 
ATOM   3968 C CD   . LYS A 1 273 ? 37.465 13.626  1.265   1.00 17.66 ? 273 LYS A CD   1 
ATOM   3969 C CE   . LYS A 1 273 ? 38.860 14.251  1.408   1.00 20.63 ? 273 LYS A CE   1 
ATOM   3970 N NZ   . LYS A 1 273 ? 39.608 14.285  0.145   1.00 20.92 ? 273 LYS A NZ   1 
ATOM   3971 H H    . LYS A 1 273 ? 34.467 15.276  3.460   1.00 17.51 ? 273 LYS A H    1 
ATOM   3972 H HA   . LYS A 1 273 ? 34.691 14.341  0.977   1.00 16.46 ? 273 LYS A HA   1 
ATOM   3973 H HB2  . LYS A 1 273 ? 35.010 13.065  3.473   1.00 18.69 ? 273 LYS A HB2  1 
ATOM   3974 H HB3  . LYS A 1 273 ? 35.294 12.337  2.089   1.00 18.69 ? 273 LYS A HB3  1 
ATOM   3975 H HG2  . LYS A 1 273 ? 36.774 14.580  2.920   1.00 21.14 ? 273 LYS A HG2  1 
ATOM   3976 H HG3  . LYS A 1 273 ? 37.253 13.094  3.214   1.00 21.14 ? 273 LYS A HG3  1 
ATOM   3977 H HD2  . LYS A 1 273 ? 37.561 12.707  0.969   1.00 21.19 ? 273 LYS A HD2  1 
ATOM   3978 H HD3  . LYS A 1 273 ? 36.959 14.134  0.611   1.00 21.19 ? 273 LYS A HD3  1 
ATOM   3979 H HE2  . LYS A 1 273 ? 38.766 15.164  1.724   1.00 24.75 ? 273 LYS A HE2  1 
ATOM   3980 H HE3  . LYS A 1 273 ? 39.374 13.731  2.046   1.00 24.75 ? 273 LYS A HE3  1 
ATOM   3981 H HZ1  . LYS A 1 273 ? 40.400 14.671  0.271   1.00 25.11 ? 273 LYS A HZ1  1 
ATOM   3982 H HZ2  . LYS A 1 273 ? 39.734 13.457  -0.156  1.00 25.11 ? 273 LYS A HZ2  1 
ATOM   3983 H HZ3  . LYS A 1 273 ? 39.155 14.749  -0.465  1.00 25.11 ? 273 LYS A HZ3  1 
ATOM   3984 N N    . ILE A 1 274 ? 32.750 12.909  0.515   1.00 13.62 ? 274 ILE A N    1 
ATOM   3985 C CA   . ILE A 1 274 ? 31.592 12.042  0.329   1.00 12.36 ? 274 ILE A CA   1 
ATOM   3986 C C    . ILE A 1 274 ? 31.728 10.843  1.256   1.00 11.88 ? 274 ILE A C    1 
ATOM   3987 O O    . ILE A 1 274 ? 32.823 10.287  1.431   1.00 12.69 ? 274 ILE A O    1 
ATOM   3988 C CB   . ILE A 1 274 ? 31.514 11.598  -1.142  1.00 13.63 ? 274 ILE A CB   1 
ATOM   3989 C CG1  . ILE A 1 274 ? 31.309 12.798  -2.075  1.00 13.88 ? 274 ILE A CG1  1 
ATOM   3990 C CG2  . ILE A 1 274 ? 30.412 10.558  -1.341  1.00 14.56 ? 274 ILE A CG2  1 
ATOM   3991 C CD1  . ILE A 1 274 ? 31.462 12.425  -3.524  1.00 15.72 ? 274 ILE A CD1  1 
ATOM   3992 H H    . ILE A 1 274 ? 33.239 13.006  -0.185  1.00 16.34 ? 274 ILE A H    1 
ATOM   3993 H HA   . ILE A 1 274 ? 30.777 12.519  0.551   1.00 14.83 ? 274 ILE A HA   1 
ATOM   3994 H HB   . ILE A 1 274 ? 32.363 11.187  -1.369  1.00 16.36 ? 274 ILE A HB   1 
ATOM   3995 H HG12 . ILE A 1 274 ? 30.415 13.151  -1.946  1.00 16.66 ? 274 ILE A HG12 1 
ATOM   3996 H HG13 . ILE A 1 274 ? 31.968 13.479  -1.866  1.00 16.66 ? 274 ILE A HG13 1 
ATOM   3997 H HG21 . ILE A 1 274 ? 30.357 10.332  -2.283  1.00 17.47 ? 274 ILE A HG21 1 
ATOM   3998 H HG22 . ILE A 1 274 ? 30.626 9.767   -0.823  1.00 17.47 ? 274 ILE A HG22 1 
ATOM   3999 H HG23 . ILE A 1 274 ? 29.568 10.931  -1.041  1.00 17.47 ? 274 ILE A HG23 1 
ATOM   4000 H HD11 . ILE A 1 274 ? 31.524 13.235  -4.054  1.00 18.86 ? 274 ILE A HD11 1 
ATOM   4001 H HD12 . ILE A 1 274 ? 32.270 11.898  -3.630  1.00 18.86 ? 274 ILE A HD12 1 
ATOM   4002 H HD13 . ILE A 1 274 ? 30.690 11.906  -3.800  1.00 18.86 ? 274 ILE A HD13 1 
ATOM   4003 N N    . ILE A 1 275 ? 30.619 10.440  1.863   1.00 11.81 ? 275 ILE A N    1 
ATOM   4004 C CA   . ILE A 1 275 ? 30.549 9.229   2.683   1.00 11.60 ? 275 ILE A CA   1 
ATOM   4005 C C    . ILE A 1 275 ? 29.436 8.372   2.127   1.00 11.12 ? 275 ILE A C    1 
ATOM   4006 O O    . ILE A 1 275 ? 28.314 8.853   1.958   1.00 12.39 ? 275 ILE A O    1 
ATOM   4007 C CB   . ILE A 1 275 ? 30.269 9.595   4.156   1.00 11.68 ? 275 ILE A CB   1 
ATOM   4008 C CG1  . ILE A 1 275 ? 31.477 10.321  4.744   1.00 13.43 ? 275 ILE A CG1  1 
ATOM   4009 C CG2  . ILE A 1 275 ? 29.879 8.364   4.948   1.00 13.23 ? 275 ILE A CG2  1 
ATOM   4010 C CD1  . ILE A 1 275 ? 32.715 9.485   4.953   1.00 15.51 ? 275 ILE A CD1  1 
ATOM   4011 H H    . ILE A 1 275 ? 29.871 10.861  1.814   1.00 14.17 ? 275 ILE A H    1 
ATOM   4012 H HA   . ILE A 1 275 ? 31.381 8.733   2.633   1.00 13.92 ? 275 ILE A HA   1 
ATOM   4013 H HB   . ILE A 1 275 ? 29.514 10.202  4.201   1.00 14.02 ? 275 ILE A HB   1 
ATOM   4014 H HG12 . ILE A 1 275 ? 31.717 11.044  4.145   1.00 16.12 ? 275 ILE A HG12 1 
ATOM   4015 H HG13 . ILE A 1 275 ? 31.223 10.678  5.610   1.00 16.12 ? 275 ILE A HG13 1 
ATOM   4016 H HG21 . ILE A 1 275 ? 30.016 8.540   5.892   1.00 15.88 ? 275 ILE A HG21 1 
ATOM   4017 H HG22 . ILE A 1 275 ? 28.944 8.164   4.781   1.00 15.88 ? 275 ILE A HG22 1 
ATOM   4018 H HG23 . ILE A 1 275 ? 30.432 7.619   4.666   1.00 15.88 ? 275 ILE A HG23 1 
ATOM   4019 H HD11 . ILE A 1 275 ? 33.422 10.050  5.301   1.00 18.61 ? 275 ILE A HD11 1 
ATOM   4020 H HD12 . ILE A 1 275 ? 32.515 8.777   5.585   1.00 18.61 ? 275 ILE A HD12 1 
ATOM   4021 H HD13 . ILE A 1 275 ? 32.984 9.103   4.103   1.00 18.61 ? 275 ILE A HD13 1 
ATOM   4022 N N    . THR A 1 276 ? 29.736 7.116   1.845   1.00 10.89 ? 276 THR A N    1 
ATOM   4023 C CA   . THR A 1 276 ? 28.695 6.149   1.450   1.00 11.33 ? 276 THR A CA   1 
ATOM   4024 C C    . THR A 1 276 ? 28.743 5.014   2.465   1.00 11.54 ? 276 THR A C    1 
ATOM   4025 O O    . THR A 1 276 ? 29.588 4.109   2.394   1.00 11.84 ? 276 THR A O    1 
ATOM   4026 C CB   . THR A 1 276 ? 28.819 5.661   0.002   1.00 11.33 ? 276 THR A CB   1 
ATOM   4027 O OG1  . THR A 1 276 ? 30.039 4.947   -0.168  1.00 12.10 ? 276 THR A OG1  1 
ATOM   4028 C CG2  . THR A 1 276 ? 28.780 6.820   -0.971  1.00 11.55 ? 276 THR A CG2  1 
ATOM   4029 H H    . THR A 1 276 ? 30.532 6.790   1.873   1.00 13.06 ? 276 THR A H    1 
ATOM   4030 H HA   . THR A 1 276 ? 27.832 6.589   1.499   1.00 13.59 ? 276 THR A HA   1 
ATOM   4031 H HB   . THR A 1 276 ? 28.072 5.076   -0.196  1.00 13.59 ? 276 THR A HB   1 
ATOM   4032 H HG1  . THR A 1 276 ? 30.000 4.473   -0.860  1.00 14.53 ? 276 THR A HG1  1 
ATOM   4033 H HG21 . THR A 1 276 ? 28.842 6.491   -1.881  1.00 13.87 ? 276 THR A HG21 1 
ATOM   4034 H HG22 . THR A 1 276 ? 27.949 7.310   -0.870  1.00 13.87 ? 276 THR A HG22 1 
ATOM   4035 H HG23 . THR A 1 276 ? 29.522 7.421   -0.801  1.00 13.87 ? 276 THR A HG23 1 
ATOM   4036 N N    . MET A 1 277 ? 27.886 5.114   3.468   1.00 11.65 ? 277 MET A N    1 
ATOM   4037 C CA   . MET A 1 277 ? 27.937 4.191   4.595   1.00 10.90 ? 277 MET A CA   1 
ATOM   4038 C C    . MET A 1 277 ? 27.018 3.020   4.264   1.00 11.17 ? 277 MET A C    1 
ATOM   4039 O O    . MET A 1 277 ? 25.793 3.171   4.237   1.00 12.38 ? 277 MET A O    1 
ATOM   4040 C CB   . MET A 1 277 ? 27.515 4.913   5.858   1.00 12.68 ? 277 MET A CB   1 
ATOM   4041 C CG   . MET A 1 277 ? 27.513 3.983   7.045   1.00 13.24 ? 277 MET A CG   1 
ATOM   4042 S SD   . MET A 1 277 ? 27.102 4.704   8.650   1.00 13.30 ? 277 MET A SD   1 
ATOM   4043 C CE   . MET A 1 277 ? 28.516 5.744   8.971   1.00 17.57 ? 277 MET A CE   1 
ATOM   4044 H H    . MET A 1 277 ? 27.266 5.707   3.521   1.00 13.98 ? 277 MET A H    1 
ATOM   4045 H HA   . MET A 1 277 ? 28.837 3.855   4.734   1.00 13.09 ? 277 MET A HA   1 
ATOM   4046 H HB2  . MET A 1 277 ? 28.135 5.637   6.037   1.00 15.22 ? 277 MET A HB2  1 
ATOM   4047 H HB3  . MET A 1 277 ? 26.618 5.265   5.743   1.00 15.22 ? 277 MET A HB3  1 
ATOM   4048 H HG2  . MET A 1 277 ? 26.863 3.282   6.877   1.00 15.89 ? 277 MET A HG2  1 
ATOM   4049 H HG3  . MET A 1 277 ? 28.400 3.599   7.128   1.00 15.89 ? 277 MET A HG3  1 
ATOM   4050 H HE1  . MET A 1 277 ? 28.377 6.217   9.806   1.00 21.09 ? 277 MET A HE1  1 
ATOM   4051 H HE2  . MET A 1 277 ? 29.309 5.188   9.034   1.00 21.09 ? 277 MET A HE2  1 
ATOM   4052 H HE3  . MET A 1 277 ? 28.614 6.378   8.244   1.00 21.09 ? 277 MET A HE3  1 
ATOM   4053 N N    . THR A 1 278 ? 27.595 1.849   4.028   1.00 11.39 ? 278 THR A N    1 
ATOM   4054 C CA   . THR A 1 278 ? 26.803 0.635   3.905   1.00 10.98 ? 278 THR A CA   1 
ATOM   4055 C C    . THR A 1 278 ? 26.635 0.060   5.311   1.00 11.65 ? 278 THR A C    1 
ATOM   4056 O O    . THR A 1 278 ? 27.553 0.148   6.128   1.00 12.37 ? 278 THR A O    1 
ATOM   4057 C CB   . THR A 1 278 ? 27.403 -0.404  2.957   1.00 12.23 ? 278 THR A CB   1 
ATOM   4058 O OG1  . THR A 1 278 ? 28.559 -1.057  3.528   1.00 12.68 ? 278 THR A OG1  1 
ATOM   4059 C CG2  . THR A 1 278 ? 27.744 0.224   1.589   1.00 12.85 ? 278 THR A CG2  1 
ATOM   4060 H H    . THR A 1 278 ? 28.442 1.733   3.935   1.00 13.67 ? 278 THR A H    1 
ATOM   4061 H HA   . THR A 1 278 ? 25.942 0.846   3.511   1.00 13.17 ? 278 THR A HA   1 
ATOM   4062 H HB   . THR A 1 278 ? 26.737 -1.094  2.809   1.00 14.68 ? 278 THR A HB   1 
ATOM   4063 H HG1  . THR A 1 278 ? 29.136 -0.486  3.740   1.00 15.22 ? 278 THR A HG1  1 
ATOM   4064 H HG21 . THR A 1 278 ? 28.036 -0.464  0.971   1.00 15.42 ? 278 THR A HG21 1 
ATOM   4065 H HG22 . THR A 1 278 ? 26.962 0.665   1.222   1.00 15.42 ? 278 THR A HG22 1 
ATOM   4066 H HG23 . THR A 1 278 ? 28.454 0.877   1.691   1.00 15.42 ? 278 THR A HG23 1 
ATOM   4067 N N    . LEU A 1 279 ? 25.448 -0.466  5.593   1.00 11.14 ? 279 LEU A N    1 
ATOM   4068 C CA   . LEU A 1 279 ? 25.167 -1.119  6.865   1.00 11.02 ? 279 LEU A CA   1 
ATOM   4069 C C    . LEU A 1 279 ? 24.315 -2.337  6.584   1.00 11.00 ? 279 LEU A C    1 
ATOM   4070 O O    . LEU A 1 279 ? 23.229 -2.221  6.023   1.00 11.90 ? 279 LEU A O    1 
ATOM   4071 C CB   . LEU A 1 279 ? 24.447 -0.173  7.825   1.00 11.78 ? 279 LEU A CB   1 
ATOM   4072 C CG   . LEU A 1 279 ? 25.260 1.042   8.271   1.00 11.94 ? 279 LEU A CG   1 
ATOM   4073 C CD1  . LEU A 1 279 ? 24.375 2.089   8.941   1.00 13.87 ? 279 LEU A CD1  1 
ATOM   4074 C CD2  . LEU A 1 279 ? 26.372 0.647   9.187   1.00 14.16 ? 279 LEU A CD2  1 
ATOM   4075 H H    . LEU A 1 279 ? 24.778 -0.457  5.054   1.00 13.37 ? 279 LEU A H    1 
ATOM   4076 H HA   . LEU A 1 279 ? 25.996 -1.402  7.281   1.00 13.23 ? 279 LEU A HA   1 
ATOM   4077 H HB2  . LEU A 1 279 ? 23.647 0.157   7.386   1.00 14.14 ? 279 LEU A HB2  1 
ATOM   4078 H HB3  . LEU A 1 279 ? 24.207 -0.671  8.622   1.00 14.14 ? 279 LEU A HB3  1 
ATOM   4079 H HG   . LEU A 1 279 ? 25.650 1.441   7.477   1.00 14.33 ? 279 LEU A HG   1 
ATOM   4080 H HD11 . LEU A 1 279 ? 24.912 2.870   9.148   1.00 16.65 ? 279 LEU A HD11 1 
ATOM   4081 H HD12 . LEU A 1 279 ? 23.658 2.331   8.334   1.00 16.65 ? 279 LEU A HD12 1 
ATOM   4082 H HD13 . LEU A 1 279 ? 24.006 1.715   9.756   1.00 16.65 ? 279 LEU A HD13 1 
ATOM   4083 H HD21 . LEU A 1 279 ? 26.828 1.446   9.493   1.00 16.99 ? 279 LEU A HD21 1 
ATOM   4084 H HD22 . LEU A 1 279 ? 26.001 0.167   9.945   1.00 16.99 ? 279 LEU A HD22 1 
ATOM   4085 H HD23 . LEU A 1 279 ? 26.991 0.076   8.706   1.00 16.99 ? 279 LEU A HD23 1 
ATOM   4086 N N    . GLY A 1 280 ? 24.808 -3.513  6.945   1.00 11.35 ? 280 GLY A N    1 
ATOM   4087 C CA   . GLY A 1 280 ? 24.073 -4.732  6.707   1.00 12.27 ? 280 GLY A CA   1 
ATOM   4088 C C    . GLY A 1 280 ? 22.914 -4.927  7.663   1.00 12.07 ? 280 GLY A C    1 
ATOM   4089 O O    . GLY A 1 280 ? 23.081 -4.922  8.900   1.00 12.48 ? 280 GLY A O    1 
ATOM   4090 H H    . GLY A 1 280 ? 25.569 -3.626  7.329   1.00 13.63 ? 280 GLY A H    1 
ATOM   4091 H HA2  . GLY A 1 280 ? 23.720 -4.719  5.804   1.00 14.72 ? 280 GLY A HA2  1 
ATOM   4092 H HA3  . GLY A 1 280 ? 24.673 -5.488  6.801   1.00 14.72 ? 280 GLY A HA3  1 
ATOM   4093 N N    . LEU A 1 281 ? 21.724 -5.092  7.117   1.00 12.47 ? 281 LEU A N    1 
ATOM   4094 C CA   . LEU A 1 281 ? 20.561 -5.407  7.928   1.00 12.98 ? 281 LEU A CA   1 
ATOM   4095 C C    . LEU A 1 281 ? 20.720 -6.760  8.594   1.00 13.59 ? 281 LEU A C    1 
ATOM   4096 O O    . LEU A 1 281 ? 20.286 -6.950  9.739   1.00 15.54 ? 281 LEU A O    1 
ATOM   4097 C CB   . LEU A 1 281 ? 19.319 -5.392  7.056   1.00 13.44 ? 281 LEU A CB   1 
ATOM   4098 C CG   . LEU A 1 281 ? 18.885 -4.002  6.567   1.00 14.06 ? 281 LEU A CG   1 
ATOM   4099 C CD1  . LEU A 1 281 ? 17.985 -4.134  5.342   1.00 15.63 ? 281 LEU A CD1  1 
ATOM   4100 C CD2  . LEU A 1 281 ? 18.199 -3.213  7.681   1.00 14.80 ? 281 LEU A CD2  1 
ATOM   4101 H H    . LEU A 1 281 ? 21.559 -5.027  6.276   1.00 14.97 ? 281 LEU A H    1 
ATOM   4102 H HA   . LEU A 1 281 ? 20.460 -4.736  8.621   1.00 15.57 ? 281 LEU A HA   1 
ATOM   4103 H HB2  . LEU A 1 281 ? 19.489 -5.937  6.271   1.00 16.13 ? 281 LEU A HB2  1 
ATOM   4104 H HB3  . LEU A 1 281 ? 18.582 -5.765  7.565   1.00 16.13 ? 281 LEU A HB3  1 
ATOM   4105 H HG   . LEU A 1 281 ? 19.672 -3.497  6.309   1.00 16.88 ? 281 LEU A HG   1 
ATOM   4106 H HD11 . LEU A 1 281 ? 17.685 -3.252  5.074   1.00 18.75 ? 281 LEU A HD11 1 
ATOM   4107 H HD12 . LEU A 1 281 ? 18.490 -4.545  4.622   1.00 18.75 ? 281 LEU A HD12 1 
ATOM   4108 H HD13 . LEU A 1 281 ? 17.222 -4.689  5.569   1.00 18.75 ? 281 LEU A HD13 1 
ATOM   4109 H HD21 . LEU A 1 281 ? 17.964 -2.334  7.346   1.00 17.76 ? 281 LEU A HD21 1 
ATOM   4110 H HD22 . LEU A 1 281 ? 17.399 -3.687  7.956   1.00 17.76 ? 281 LEU A HD22 1 
ATOM   4111 H HD23 . LEU A 1 281 ? 18.809 -3.130  8.430   1.00 17.76 ? 281 LEU A HD23 1 
ATOM   4112 N N    . GLY A 1 282 ? 21.282 -7.747  7.882   1.00 15.21 ? 282 GLY A N    1 
ATOM   4113 C CA   . GLY A 1 282 ? 21.491 -9.061  8.465   1.00 14.66 ? 282 GLY A CA   1 
ATOM   4114 C C    . GLY A 1 282 ? 22.736 -9.074  9.318   1.00 14.35 ? 282 GLY A C    1 
ATOM   4115 O O    . GLY A 1 282 ? 23.568 -8.186  9.263   1.00 13.84 ? 282 GLY A O    1 
ATOM   4116 H H    . GLY A 1 282 ? 21.545 -7.674  7.067   1.00 18.26 ? 282 GLY A H    1 
ATOM   4117 H HA2  . GLY A 1 282 ? 20.730 -9.298  9.018   1.00 17.60 ? 282 GLY A HA2  1 
ATOM   4118 H HA3  . GLY A 1 282 ? 21.587 -9.720  7.760   1.00 17.60 ? 282 GLY A HA3  1 
ATOM   4119 N N    . GLU A 1 283 ? 22.865 -10.130 10.107  1.00 15.81 ? 283 GLU A N    1 
ATOM   4120 C CA   . GLU A 1 283 ? 23.980 -10.230 11.039  1.00 15.23 ? 283 GLU A CA   1 
ATOM   4121 C C    . GLU A 1 283 ? 25.291 -10.480 10.314  1.00 15.29 ? 283 GLU A C    1 
ATOM   4122 O O    . GLU A 1 283 ? 25.325 -11.094 9.259   1.00 17.35 ? 283 GLU A O    1 
ATOM   4123 C CB   . GLU A 1 283 ? 23.734 -11.394 11.997  1.00 20.92 ? 283 GLU A CB   1 
ATOM   4124 C CG   . GLU A 1 283 ? 22.412 -11.300 12.744  1.00 25.70 ? 283 GLU A CG   1 
ATOM   4125 C CD   . GLU A 1 283 ? 22.442 -10.244 13.813  1.00 37.65 ? 283 GLU A CD   1 
ATOM   4126 O OE1  . GLU A 1 283 ? 21.862 -9.157  13.585  1.00 40.53 ? 283 GLU A OE1  1 
ATOM   4127 O OE2  . GLU A 1 283 ? 23.006 -10.523 14.892  1.00 41.28 ? 283 GLU A OE2  1 
ATOM   4128 H H    . GLU A 1 283 ? 22.325 -10.800 10.123  1.00 18.98 ? 283 GLU A H    1 
ATOM   4129 H HA   . GLU A 1 283 ? 24.054 -9.397  11.531  1.00 18.28 ? 283 GLU A HA   1 
ATOM   4130 H HB2  . GLU A 1 283 ? 23.731 -12.221 11.490  1.00 25.10 ? 283 GLU A HB2  1 
ATOM   4131 H HB3  . GLU A 1 283 ? 24.446 -11.412 12.656  1.00 25.10 ? 283 GLU A HB3  1 
ATOM   4132 H HG2  . GLU A 1 283 ? 21.707 -11.076 12.116  1.00 30.84 ? 283 GLU A HG2  1 
ATOM   4133 H HG3  . GLU A 1 283 ? 22.223 -12.153 13.165  1.00 30.84 ? 283 GLU A HG3  1 
ATOM   4134 N N    . ALA A 1 284 ? 26.397 -10.042 10.914  1.00 16.28 ? 284 ALA A N    1 
ATOM   4135 C CA   . ALA A 1 284 ? 27.703 -10.353 10.352  1.00 17.13 ? 284 ALA A CA   1 
ATOM   4136 C C    . ALA A 1 284 ? 27.971 -11.849 10.417  1.00 17.60 ? 284 ALA A C    1 
ATOM   4137 O O    . ALA A 1 284 ? 27.733 -12.492 11.441  1.00 20.71 ? 284 ALA A O    1 
ATOM   4138 C CB   . ALA A 1 284 ? 28.808 -9.624  11.119  1.00 17.46 ? 284 ALA A CB   1 
ATOM   4139 H H    . ALA A 1 284 ? 26.415 -9.572  11.634  1.00 19.54 ? 284 ALA A H    1 
ATOM   4140 H HA   . ALA A 1 284 ? 27.719 -10.064 9.426   1.00 20.56 ? 284 ALA A HA   1 
ATOM   4141 H HB1  . ALA A 1 284 ? 29.667 -9.863  10.739  1.00 20.95 ? 284 ALA A HB1  1 
ATOM   4142 H HB2  . ALA A 1 284 ? 28.667 -8.667  11.043  1.00 20.95 ? 284 ALA A HB2  1 
ATOM   4143 H HB3  . ALA A 1 284 ? 28.773 -9.890  12.052  1.00 20.95 ? 284 ALA A HB3  1 
ATOM   4144 N N    . ILE A 1 285 ? 28.482 -12.408 9.322   1.00 18.00 ? 285 ILE A N    1 
ATOM   4145 C CA   . ILE A 1 285 ? 29.108 -13.727 9.394   1.00 23.71 ? 285 ILE A CA   1 
ATOM   4146 C C    . ILE A 1 285 ? 30.340 -13.622 10.283  1.00 22.85 ? 285 ILE A C    1 
ATOM   4147 O O    . ILE A 1 285 ? 31.051 -12.615 10.262  1.00 20.56 ? 285 ILE A O    1 
ATOM   4148 C CB   . ILE A 1 285 ? 29.488 -14.224 7.990   1.00 21.05 ? 285 ILE A CB   1 
ATOM   4149 C CG1  . ILE A 1 285 ? 28.238 -14.446 7.131   1.00 23.87 ? 285 ILE A CG1  1 
ATOM   4150 C CG2  . ILE A 1 285 ? 30.294 -15.521 8.095   1.00 24.42 ? 285 ILE A CG2  1 
ATOM   4151 C CD1  . ILE A 1 285 ? 28.506 -14.727 5.674   1.00 31.69 ? 285 ILE A CD1  1 
ATOM   4152 H H    . ILE A 1 285 ? 28.479 -12.052 8.539   1.00 21.60 ? 285 ILE A H    1 
ATOM   4153 H HA   . ILE A 1 285 ? 28.485 -14.365 9.775   1.00 28.45 ? 285 ILE A HA   1 
ATOM   4154 H HB   . ILE A 1 285 ? 30.030 -13.542 7.564   1.00 25.26 ? 285 ILE A HB   1 
ATOM   4155 H HG12 . ILE A 1 285 ? 27.751 -15.206 7.488   1.00 28.65 ? 285 ILE A HG12 1 
ATOM   4156 H HG13 . ILE A 1 285 ? 27.688 -13.649 7.177   1.00 28.65 ? 285 ILE A HG13 1 
ATOM   4157 H HG21 . ILE A 1 285 ? 30.393 -15.903 7.209   1.00 29.30 ? 285 ILE A HG21 1 
ATOM   4158 H HG22 . ILE A 1 285 ? 31.166 -15.322 8.469   1.00 29.30 ? 285 ILE A HG22 1 
ATOM   4159 H HG23 . ILE A 1 285 ? 29.820 -16.141 8.671   1.00 29.30 ? 285 ILE A HG23 1 
ATOM   4160 H HD11 . ILE A 1 285 ? 27.705 -14.533 5.163   1.00 38.03 ? 285 ILE A HD11 1 
ATOM   4161 H HD12 . ILE A 1 285 ? 29.235 -14.163 5.373   1.00 38.03 ? 285 ILE A HD12 1 
ATOM   4162 H HD13 . ILE A 1 285 ? 28.746 -15.661 5.572   1.00 38.03 ? 285 ILE A HD13 1 
ATOM   4163 N N    . ASP A 1 286 ? 30.591 -14.651 11.088  1.00 25.63 ? 286 ASP A N    1 
ATOM   4164 C CA   . ASP A 1 286 ? 31.779 -14.682 11.933  1.00 28.41 ? 286 ASP A CA   1 
ATOM   4165 C C    . ASP A 1 286 ? 33.027 -14.308 11.145  1.00 24.27 ? 286 ASP A C    1 
ATOM   4166 O O    . ASP A 1 286 ? 33.348 -14.931 10.126  1.00 27.28 ? 286 ASP A O    1 
ATOM   4167 C CB   . ASP A 1 286 ? 31.891 -16.089 12.512  1.00 29.14 ? 286 ASP A CB   1 
ATOM   4168 C CG   . ASP A 1 286 ? 31.269 -16.212 13.889  1.00 37.73 ? 286 ASP A CG   1 
ATOM   4169 O OD1  . ASP A 1 286 ? 30.229 -15.565 14.150  1.00 38.81 ? 286 ASP A OD1  1 
ATOM   4170 O OD2  . ASP A 1 286 ? 31.760 -17.055 14.672  1.00 44.95 ? 286 ASP A OD2  1 
ATOM   4171 H H    . ASP A 1 286 ? 30.088 -15.345 11.162  1.00 30.76 ? 286 ASP A H    1 
ATOM   4172 H HA   . ASP A 1 286 ? 31.704 -14.039 12.656  1.00 34.09 ? 286 ASP A HA   1 
ATOM   4173 H HB2  . ASP A 1 286 ? 31.437 -16.710 11.922  1.00 34.97 ? 286 ASP A HB2  1 
ATOM   4174 H HB3  . ASP A 1 286 ? 32.829 -16.327 12.585  1.00 34.97 ? 286 ASP A HB3  1 
ATOM   4175 N N    . ASN A 1 287 ? 33.714 -13.276 11.633  1.00 24.11 ? 287 ASN A N    1 
ATOM   4176 C CA   . ASN A 1 287 ? 34.876 -12.693 10.969  1.00 25.14 ? 287 ASN A CA   1 
ATOM   4177 C C    . ASN A 1 287 ? 35.642 -11.880 12.004  1.00 25.12 ? 287 ASN A C    1 
ATOM   4178 O O    . ASN A 1 287 ? 35.128 -10.880 12.509  1.00 25.77 ? 287 ASN A O    1 
ATOM   4179 C CB   . ASN A 1 287 ? 34.398 -11.797 9.830   1.00 26.12 ? 287 ASN A CB   1 
ATOM   4180 C CG   . ASN A 1 287 ? 35.532 -11.301 8.969   1.00 25.17 ? 287 ASN A CG   1 
ATOM   4181 O OD1  . ASN A 1 287 ? 36.667 -11.188 9.417   1.00 26.72 ? 287 ASN A OD1  1 
ATOM   4182 N ND2  . ASN A 1 287 ? 35.226 -10.981 7.715   1.00 23.70 ? 287 ASN A ND2  1 
ATOM   4183 H H    . ASN A 1 287 ? 33.520 -12.882 12.372  1.00 28.93 ? 287 ASN A H    1 
ATOM   4184 H HA   . ASN A 1 287 ? 35.462 -13.382 10.620  1.00 30.17 ? 287 ASN A HA   1 
ATOM   4185 H HB2  . ASN A 1 287 ? 33.789 -12.299 9.266   1.00 31.35 ? 287 ASN A HB2  1 
ATOM   4186 H HB3  . ASN A 1 287 ? 33.944 -11.025 10.204  1.00 31.35 ? 287 ASN A HB3  1 
ATOM   4187 H HD21 . ASN A 1 287 ? 35.837 -10.693 7.183   1.00 28.45 ? 287 ASN A HD21 1 
ATOM   4188 H HD22 . ASN A 1 287 ? 34.416 -11.063 7.436   1.00 28.45 ? 287 ASN A HD22 1 
ATOM   4189 N N    . ASN A 1 288 ? 36.868 -12.304 12.314  1.00 25.81 ? 288 ASN A N    1 
ATOM   4190 C CA   . ASN A 1 288 ? 37.702 -11.610 13.291  1.00 27.70 ? 288 ASN A CA   1 
ATOM   4191 C C    . ASN A 1 288 ? 38.897 -10.943 12.625  1.00 27.50 ? 288 ASN A C    1 
ATOM   4192 O O    . ASN A 1 288 ? 39.908 -10.670 13.275  1.00 25.64 ? 288 ASN A O    1 
ATOM   4193 C CB   . ASN A 1 288 ? 38.137 -12.561 14.414  1.00 30.66 ? 288 ASN A CB   1 
ATOM   4194 C CG   . ASN A 1 288 ? 38.532 -11.818 15.688  1.00 38.26 ? 288 ASN A CG   1 
ATOM   4195 O OD1  . ASN A 1 288 ? 37.854 -10.876 16.112  1.00 37.79 ? 288 ASN A OD1  1 
ATOM   4196 N ND2  . ASN A 1 288 ? 39.620 -12.256 16.314  1.00 39.46 ? 288 ASN A ND2  1 
ATOM   4197 H H    . ASN A 1 288 ? 37.240 -12.998 11.968  1.00 30.98 ? 288 ASN A H    1 
ATOM   4198 H HA   . ASN A 1 288 ? 37.179 -10.912 13.716  1.00 33.24 ? 288 ASN A HA   1 
ATOM   4199 H HB2  . ASN A 1 288 ? 37.401 -13.156 14.628  1.00 36.79 ? 288 ASN A HB2  1 
ATOM   4200 H HB3  . ASN A 1 288 ? 38.903 -13.076 14.115  1.00 36.79 ? 288 ASN A HB3  1 
ATOM   4201 H HD21 . ASN A 1 288 ? 40.059 -12.924 15.997  1.00 47.35 ? 288 ASN A HD21 1 
ATOM   4202 H HD22 . ASN A 1 288 ? 39.885 -11.871 17.036  1.00 47.35 ? 288 ASN A HD22 1 
ATOM   4203 N N    . THR A 1 289 ? 38.788 -10.649 11.330  1.00 23.81 ? 289 THR A N    1 
ATOM   4204 C CA   . THR A 1 289 ? 39.913 -10.118 10.583  1.00 25.95 ? 289 THR A CA   1 
ATOM   4205 C C    . THR A 1 289 ? 39.886 -8.604  10.474  1.00 18.90 ? 289 THR A C    1 
ATOM   4206 O O    . THR A 1 289 ? 40.916 -8.012  10.110  1.00 22.36 ? 289 THR A O    1 
ATOM   4207 C CB   . THR A 1 289 ? 39.932 -10.675 9.151   1.00 23.66 ? 289 THR A CB   1 
ATOM   4208 O OG1  . THR A 1 289 ? 38.873 -10.083 8.392   1.00 23.26 ? 289 THR A OG1  1 
ATOM   4209 C CG2  . THR A 1 289 ? 39.816 -12.204 9.117   1.00 27.42 ? 289 THR A CG2  1 
ATOM   4210 H H    . THR A 1 289 ? 38.070 -10.751 10.866  1.00 28.57 ? 289 THR A H    1 
ATOM   4211 H HA   . THR A 1 289 ? 40.727 -10.396 11.033  1.00 31.13 ? 289 THR A HA   1 
ATOM   4212 H HB   . THR A 1 289 ? 40.785 -10.455 8.745   1.00 28.39 ? 289 THR A HB   1 
ATOM   4213 H HG1  . THR A 1 289 ? 38.132 -10.258 8.748   1.00 27.91 ? 289 THR A HG1  1 
ATOM   4214 H HG21 . THR A 1 289 ? 39.958 -12.527 8.214   1.00 32.90 ? 289 THR A HG21 1 
ATOM   4215 H HG22 . THR A 1 289 ? 40.481 -12.600 9.701   1.00 32.90 ? 289 THR A HG22 1 
ATOM   4216 H HG23 . THR A 1 289 ? 38.934 -12.476 9.414   1.00 32.90 ? 289 THR A HG23 1 
ATOM   4217 N N    . GLY A 1 290 ? 38.744 -7.971  10.706  1.00 19.31 ? 290 GLY A N    1 
ATOM   4218 C CA   . GLY A 1 290 ? 38.633 -6.549  10.504  1.00 17.98 ? 290 GLY A CA   1 
ATOM   4219 C C    . GLY A 1 290 ? 38.680 -6.112  9.056   1.00 16.82 ? 290 GLY A C    1 
ATOM   4220 O O    . GLY A 1 290 ? 38.936 -4.939  8.775   1.00 16.76 ? 290 GLY A O    1 
ATOM   4221 H H    . GLY A 1 290 ? 38.021 -8.348  10.981  1.00 23.18 ? 290 GLY A H    1 
ATOM   4222 H HA2  . GLY A 1 290 ? 37.791 -6.245  10.878  1.00 21.58 ? 290 GLY A HA2  1 
ATOM   4223 H HA3  . GLY A 1 290 ? 39.362 -6.110  10.970  1.00 21.58 ? 290 GLY A HA3  1 
ATOM   4224 N N    . ILE A 1 291 ? 38.406 -7.027  8.126   1.00 15.93 ? 291 ILE A N    1 
ATOM   4225 C CA   . ILE A 1 291 ? 38.385 -6.754  6.690   1.00 16.34 ? 291 ILE A CA   1 
ATOM   4226 C C    . ILE A 1 291 ? 37.122 -7.425  6.154   1.00 17.10 ? 291 ILE A C    1 
ATOM   4227 O O    . ILE A 1 291 ? 36.668 -8.450  6.683   1.00 17.28 ? 291 ILE A O    1 
ATOM   4228 C CB   . ILE A 1 291 ? 39.650 -7.279  5.972   1.00 17.07 ? 291 ILE A CB   1 
ATOM   4229 C CG1  . ILE A 1 291 ? 40.958 -6.758  6.597   1.00 19.29 ? 291 ILE A CG1  1 
ATOM   4230 C CG2  . ILE A 1 291 ? 39.661 -6.926  4.453   1.00 18.46 ? 291 ILE A CG2  1 
ATOM   4231 C CD1  . ILE A 1 291 ? 42.222 -7.256  5.923   1.00 23.01 ? 291 ILE A CD1  1 
ATOM   4232 H H    . ILE A 1 291 ? 38.222 -7.847  8.310   1.00 19.12 ? 291 ILE A H    1 
ATOM   4233 H HA   . ILE A 1 291 ? 38.348 -5.800  6.520   1.00 19.60 ? 291 ILE A HA   1 
ATOM   4234 H HB   . ILE A 1 291 ? 39.607 -8.241  6.085   1.00 20.48 ? 291 ILE A HB   1 
ATOM   4235 H HG12 . ILE A 1 291 ? 40.961 -5.789  6.544   1.00 23.15 ? 291 ILE A HG12 1 
ATOM   4236 H HG13 . ILE A 1 291 ? 40.991 -7.039  7.524   1.00 23.15 ? 291 ILE A HG13 1 
ATOM   4237 H HG21 . ILE A 1 291 ? 40.421 -7.360  4.034   1.00 22.15 ? 291 ILE A HG21 1 
ATOM   4238 H HG22 . ILE A 1 291 ? 38.837 -7.240  4.049   1.00 22.15 ? 291 ILE A HG22 1 
ATOM   4239 H HG23 . ILE A 1 291 ? 39.733 -5.964  4.352   1.00 22.15 ? 291 ILE A HG23 1 
ATOM   4240 H HD11 . ILE A 1 291 ? 42.980 -7.078  6.502   1.00 27.61 ? 291 ILE A HD11 1 
ATOM   4241 H HD12 . ILE A 1 291 ? 42.142 -8.210  5.767   1.00 27.61 ? 291 ILE A HD12 1 
ATOM   4242 H HD13 . ILE A 1 291 ? 42.335 -6.792  5.079   1.00 27.61 ? 291 ILE A HD13 1 
ATOM   4243 N N    . ASP A 1 292 ? 36.537 -6.830  5.111   1.00 13.86 ? 292 ASP A N    1 
ATOM   4244 C CA   . ASP A 1 292 ? 35.329 -7.350  4.441   1.00 13.43 ? 292 ASP A CA   1 
ATOM   4245 C C    . ASP A 1 292 ? 34.107 -7.216  5.330   1.00 12.93 ? 292 ASP A C    1 
ATOM   4246 O O    . ASP A 1 292 ? 34.188 -6.706  6.459   1.00 13.79 ? 292 ASP A O    1 
ATOM   4247 C CB   . ASP A 1 292 ? 35.548 -8.795  3.967   1.00 14.87 ? 292 ASP A CB   1 
ATOM   4248 C CG   . ASP A 1 292 ? 36.757 -8.913  3.093   1.00 21.91 ? 292 ASP A CG   1 
ATOM   4249 O OD1  . ASP A 1 292 ? 36.856 -8.108  2.138   1.00 20.58 ? 292 ASP A OD1  1 
ATOM   4250 O OD2  . ASP A 1 292 ? 37.627 -9.774  3.383   1.00 27.83 ? 292 ASP A OD2  1 
ATOM   4251 H H    . ASP A 1 292 ? 36.825 -6.101  4.757   1.00 16.63 ? 292 ASP A H    1 
ATOM   4252 H HA   . ASP A 1 292 ? 35.153 -6.821  3.648   1.00 16.11 ? 292 ASP A HA   1 
ATOM   4253 H HB2  . ASP A 1 292 ? 35.672 -9.369  4.739   1.00 17.85 ? 292 ASP A HB2  1 
ATOM   4254 H HB3  . ASP A 1 292 ? 34.774 -9.085  3.459   1.00 17.85 ? 292 ASP A HB3  1 
ATOM   4255 N N    . ASP A 1 293 ? 32.943 -7.621  4.841   1.00 13.23 ? 293 ASP A N    1 
ATOM   4256 C CA   . ASP A 1 293 ? 31.715 -7.509  5.631   1.00 12.31 ? 293 ASP A CA   1 
ATOM   4257 C C    . ASP A 1 293 ? 30.625 -8.425  5.092   1.00 13.55 ? 293 ASP A C    1 
ATOM   4258 O O    . ASP A 1 293 ? 29.505 -7.984  4.815   1.00 13.11 ? 293 ASP A O    1 
ATOM   4259 C CB   . ASP A 1 293 ? 31.223 -6.068  5.707   1.00 13.09 ? 293 ASP A CB   1 
ATOM   4260 C CG   . ASP A 1 293 ? 30.162 -5.853  6.767   1.00 11.59 ? 293 ASP A CG   1 
ATOM   4261 O OD1  . ASP A 1 293 ? 30.146 -6.647  7.749   1.00 13.14 ? 293 ASP A OD1  1 
ATOM   4262 O OD2  . ASP A 1 293 ? 29.364 -4.900  6.651   1.00 13.02 ? 293 ASP A OD2  1 
ATOM   4263 H H    . ASP A 1 293 ? 32.833 -7.962  4.060   1.00 15.88 ? 293 ASP A H    1 
ATOM   4264 H HA   . ASP A 1 293 ? 31.916 -7.789  6.537   1.00 14.77 ? 293 ASP A HA   1 
ATOM   4265 H HB2  . ASP A 1 293 ? 31.974 -5.491  5.916   1.00 15.71 ? 293 ASP A HB2  1 
ATOM   4266 H HB3  . ASP A 1 293 ? 30.843 -5.821  4.850   1.00 15.71 ? 293 ASP A HB3  1 
ATOM   4267 N N    . GLN A 1 294 ? 30.936 -9.709  4.992   1.00 16.28 ? 294 GLN A N    1 
ATOM   4268 C CA   . GLN A 1 294 ? 29.948 -10.681 4.546   1.00 17.28 ? 294 GLN A CA   1 
ATOM   4269 C C    . GLN A 1 294 ? 28.869 -10.800 5.615   1.00 14.91 ? 294 GLN A C    1 
ATOM   4270 O O    . GLN A 1 294 ? 29.164 -10.879 6.808   1.00 16.06 ? 294 GLN A O    1 
ATOM   4271 C CB   . GLN A 1 294 ? 30.642 -12.021 4.358   1.00 21.65 ? 294 GLN A CB   1 
ATOM   4272 C CG   . GLN A 1 294 ? 31.911 -11.987 3.493   1.00 30.41 ? 294 GLN A CG   1 
ATOM   4273 C CD   . GLN A 1 294 ? 33.231 -11.794 4.286   1.00 34.75 ? 294 GLN A CD   1 
ATOM   4274 O OE1  . GLN A 1 294 ? 33.250 -11.344 5.446   1.00 29.49 ? 294 GLN A OE1  1 
ATOM   4275 N NE2  . GLN A 1 294 ? 34.343 -12.188 3.656   1.00 38.92 ? 294 GLN A NE2  1 
ATOM   4276 H H    . GLN A 1 294 ? 31.708 -10.042 5.175   1.00 19.53 ? 294 GLN A H    1 
ATOM   4277 H HA   . GLN A 1 294 ? 29.538 -10.415 3.709   1.00 20.73 ? 294 GLN A HA   1 
ATOM   4278 H HB2  . GLN A 1 294 ? 30.895 -12.359 5.231   1.00 25.97 ? 294 GLN A HB2  1 
ATOM   4279 H HB3  . GLN A 1 294 ? 30.018 -12.631 3.934   1.00 25.97 ? 294 GLN A HB3  1 
ATOM   4280 H HG2  . GLN A 1 294 ? 31.979 -12.827 3.013   1.00 36.49 ? 294 GLN A HG2  1 
ATOM   4281 H HG3  . GLN A 1 294 ? 31.837 -11.251 2.865   1.00 36.49 ? 294 GLN A HG3  1 
ATOM   4282 H HE21 . GLN A 1 294 ? 34.293 -12.522 2.865   1.00 46.70 ? 294 GLN A HE21 1 
ATOM   4283 H HE22 . GLN A 1 294 ? 35.107 -12.108 4.042   1.00 46.70 ? 294 GLN A HE22 1 
ATOM   4284 N N    . ARG A 1 295 ? 27.606 -10.780 5.187   1.00 15.27 ? 295 ARG A N    1 
ATOM   4285 C CA   . ARG A 1 295 ? 26.478 -10.822 6.110   1.00 14.76 ? 295 ARG A CA   1 
ATOM   4286 C C    . ARG A 1 295 ? 25.623 -12.057 5.869   1.00 15.19 ? 295 ARG A C    1 
ATOM   4287 O O    . ARG A 1 295 ? 25.507 -12.556 4.745   1.00 16.43 ? 295 ARG A O    1 
ATOM   4288 C CB   . ARG A 1 295 ? 25.564 -9.603  5.965   1.00 13.30 ? 295 ARG A CB   1 
ATOM   4289 C CG   . ARG A 1 295 ? 26.252 -8.257  5.906   1.00 13.20 ? 295 ARG A CG   1 
ATOM   4290 C CD   . ARG A 1 295 ? 27.088 -7.916  7.132   1.00 13.23 ? 295 ARG A CD   1 
ATOM   4291 N NE   . ARG A 1 295 ? 26.244 -7.595  8.279   1.00 13.50 ? 295 ARG A NE   1 
ATOM   4292 C CZ   . ARG A 1 295 ? 26.631 -6.865  9.315   1.00 13.09 ? 295 ARG A CZ   1 
ATOM   4293 N NH1  . ARG A 1 295 ? 27.879 -6.460  9.452   1.00 12.41 ? 295 ARG A NH1  1 
ATOM   4294 N NH2  . ARG A 1 295 ? 25.735 -6.548  10.242  1.00 13.72 ? 295 ARG A NH2  1 
ATOM   4295 H H    . ARG A 1 295 ? 27.379 -10.741 4.358   1.00 18.32 ? 295 ARG A H    1 
ATOM   4296 H HA   . ARG A 1 295 ? 26.843 -10.851 7.008   1.00 17.71 ? 295 ARG A HA   1 
ATOM   4297 H HB2  . ARG A 1 295 ? 25.057 -9.701  5.143   1.00 15.96 ? 295 ARG A HB2  1 
ATOM   4298 H HB3  . ARG A 1 295 ? 24.962 -9.584  6.725   1.00 15.96 ? 295 ARG A HB3  1 
ATOM   4299 H HG2  . ARG A 1 295 ? 26.844 -8.245  5.138   1.00 15.84 ? 295 ARG A HG2  1 
ATOM   4300 H HG3  . ARG A 1 295 ? 25.576 -7.567  5.815   1.00 15.84 ? 295 ARG A HG3  1 
ATOM   4301 H HD2  . ARG A 1 295 ? 27.643 -8.678  7.365   1.00 15.88 ? 295 ARG A HD2  1 
ATOM   4302 H HD3  . ARG A 1 295 ? 27.646 -7.147  6.938   1.00 15.88 ? 295 ARG A HD3  1 
ATOM   4303 H HE   . ARG A 1 295 ? 25.440 -7.900  8.283   1.00 16.20 ? 295 ARG A HE   1 
ATOM   4304 H HH11 . ARG A 1 295 ? 28.466 -6.668  8.859   1.00 14.90 ? 295 ARG A HH11 1 
ATOM   4305 H HH12 . ARG A 1 295 ? 28.105 -5.987  10.134  1.00 14.90 ? 295 ARG A HH12 1 
ATOM   4306 H HH21 . ARG A 1 295 ? 24.921 -6.815  10.162  1.00 16.46 ? 295 ARG A HH21 1 
ATOM   4307 H HH22 . ARG A 1 295 ? 25.968 -6.075  10.921  1.00 16.46 ? 295 ARG A HH22 1 
ATOM   4308 N N    . GLU A 1 296 ? 25.006 -12.537 6.938   1.00 14.00 ? 296 GLU A N    1 
ATOM   4309 C CA   . GLU A 1 296 ? 23.922 -13.506 6.819   1.00 14.86 ? 296 GLU A CA   1 
ATOM   4310 C C    . GLU A 1 296 ? 22.710 -12.853 6.168   1.00 14.50 ? 296 GLU A C    1 
ATOM   4311 O O    . GLU A 1 296 ? 22.490 -11.649 6.275   1.00 13.64 ? 296 GLU A O    1 
ATOM   4312 C CB   . GLU A 1 296 ? 23.520 -13.995 8.205   1.00 18.92 ? 296 GLU A CB   1 
ATOM   4313 C CG   . GLU A 1 296 ? 24.630 -14.706 8.950   1.00 24.41 ? 296 GLU A CG   1 
ATOM   4314 C CD   . GLU A 1 296 ? 24.946 -16.109 8.443   1.00 41.23 ? 296 GLU A CD   1 
ATOM   4315 O OE1  . GLU A 1 296 ? 24.294 -16.607 7.494   1.00 40.38 ? 296 GLU A OE1  1 
ATOM   4316 O OE2  . GLU A 1 296 ? 25.880 -16.711 9.017   1.00 44.36 ? 296 GLU A OE2  1 
ATOM   4317 H H    . GLU A 1 296 ? 25.194 -12.319 7.748   1.00 16.79 ? 296 GLU A H    1 
ATOM   4318 H HA   . GLU A 1 296 ? 24.210 -14.259 6.280   1.00 17.83 ? 296 GLU A HA   1 
ATOM   4319 H HB2  . GLU A 1 296 ? 23.248 -13.232 8.738   1.00 22.71 ? 296 GLU A HB2  1 
ATOM   4320 H HB3  . GLU A 1 296 ? 22.781 -14.617 8.114   1.00 22.71 ? 296 GLU A HB3  1 
ATOM   4321 H HG2  . GLU A 1 296 ? 25.440 -14.178 8.872   1.00 29.29 ? 296 GLU A HG2  1 
ATOM   4322 H HG3  . GLU A 1 296 ? 24.374 -14.784 9.883   1.00 29.29 ? 296 GLU A HG3  1 
ATOM   4323 N N    . ASP A 1 297 ? 21.918 -13.668 5.477   1.00 15.37 ? 297 ASP A N    1 
ATOM   4324 C CA   . ASP A 1 297 ? 20.674 -13.158 4.919   1.00 15.32 ? 297 ASP A CA   1 
ATOM   4325 C C    . ASP A 1 297 ? 19.799 -12.595 6.032   1.00 16.18 ? 297 ASP A C    1 
ATOM   4326 O O    . ASP A 1 297 ? 19.715 -13.175 7.124   1.00 16.14 ? 297 ASP A O    1 
ATOM   4327 C CB   . ASP A 1 297 ? 19.962 -14.295 4.156   1.00 16.60 ? 297 ASP A CB   1 
ATOM   4328 C CG   . ASP A 1 297 ? 20.774 -14.813 2.959   1.00 17.08 ? 297 ASP A CG   1 
ATOM   4329 O OD1  . ASP A 1 297 ? 21.518 -13.992 2.349   1.00 18.55 ? 297 ASP A OD1  1 
ATOM   4330 O OD2  . ASP A 1 297 ? 20.703 -16.010 2.698   1.00 18.25 ? 297 ASP A OD2  1 
ATOM   4331 H H    . ASP A 1 297 ? 22.076 -14.498 5.320   1.00 18.44 ? 297 ASP A H    1 
ATOM   4332 H HA   . ASP A 1 297 ? 20.841 -12.437 4.292   1.00 18.38 ? 297 ASP A HA   1 
ATOM   4333 H HB2  . ASP A 1 297 ? 19.815 -15.038 4.762   1.00 19.91 ? 297 ASP A HB2  1 
ATOM   4334 H HB3  . ASP A 1 297 ? 19.112 -13.967 3.821   1.00 19.91 ? 297 ASP A HB3  1 
ATOM   4335 N N    . VAL A 1 298 ? 19.149 -11.466 5.778   1.00 16.13 ? 298 VAL A N    1 
ATOM   4336 C CA   . VAL A 1 298 ? 18.277 -10.909 6.816   1.00 16.53 ? 298 VAL A CA   1 
ATOM   4337 C C    . VAL A 1 298 ? 17.100 -11.853 7.013   1.00 18.49 ? 298 VAL A C    1 
ATOM   4338 O O    . VAL A 1 298 ? 16.605 -12.478 6.076   1.00 18.83 ? 298 VAL A O    1 
ATOM   4339 C CB   . VAL A 1 298 ? 17.879 -9.457  6.490   1.00 20.49 ? 298 VAL A CB   1 
ATOM   4340 C CG1  . VAL A 1 298 ? 16.920 -9.418  5.386   1.00 21.34 ? 298 VAL A CG1  1 
ATOM   4341 C CG2  . VAL A 1 298 ? 17.304 -8.741  7.750   1.00 20.54 ? 298 VAL A CG2  1 
ATOM   4342 H H    . VAL A 1 298 ? 19.192 -11.018 5.045   1.00 19.35 ? 298 VAL A H    1 
ATOM   4343 H HA   . VAL A 1 298 ? 18.748 -10.854 7.662   1.00 19.83 ? 298 VAL A HA   1 
ATOM   4344 H HB   . VAL A 1 298 ? 18.673 -8.974  6.211   1.00 24.59 ? 298 VAL A HB   1 
ATOM   4345 H HG11 . VAL A 1 298 ? 16.715 -8.493  5.178   1.00 25.61 ? 298 VAL A HG11 1 
ATOM   4346 H HG12 . VAL A 1 298 ? 17.311 -9.853  4.612   1.00 25.61 ? 298 VAL A HG12 1 
ATOM   4347 H HG13 . VAL A 1 298 ? 16.112 -9.883  5.654   1.00 25.61 ? 298 VAL A HG13 1 
ATOM   4348 H HG21 . VAL A 1 298 ? 17.088 -7.824  7.521   1.00 24.65 ? 298 VAL A HG21 1 
ATOM   4349 H HG22 . VAL A 1 298 ? 16.505 -9.207  8.041   1.00 24.65 ? 298 VAL A HG22 1 
ATOM   4350 H HG23 . VAL A 1 298 ? 17.971 -8.758  8.454   1.00 24.65 ? 298 VAL A HG23 1 
ATOM   4351 N N    . ASP A 1 299 ? 16.694 -12.014 8.277   1.00 17.75 ? 299 ASP A N    1 
ATOM   4352 C CA   . ASP A 1 299 ? 15.666 -12.950 8.694   1.00 21.53 ? 299 ASP A CA   1 
ATOM   4353 C C    . ASP A 1 299 ? 14.959 -12.379 9.914   1.00 22.42 ? 299 ASP A C    1 
ATOM   4354 O O    . ASP A 1 299 ? 15.111 -12.888 11.029  1.00 31.43 ? 299 ASP A O    1 
ATOM   4355 C CB   . ASP A 1 299 ? 16.245 -14.328 9.015   1.00 23.19 ? 299 ASP A CB   1 
ATOM   4356 C CG   . ASP A 1 299 ? 15.197 -15.426 9.011   1.00 37.10 ? 299 ASP A CG   1 
ATOM   4357 O OD1  . ASP A 1 299 ? 14.112 -15.263 8.401   1.00 41.63 ? 299 ASP A OD1  1 
ATOM   4358 O OD2  . ASP A 1 299 ? 15.478 -16.471 9.632   1.00 46.77 ? 299 ASP A OD2  1 
ATOM   4359 H H    . ASP A 1 299 ? 17.020 -11.567 8.936   1.00 21.30 ? 299 ASP A H    1 
ATOM   4360 H HA   . ASP A 1 299 ? 15.025 -13.035 7.971   1.00 25.83 ? 299 ASP A HA   1 
ATOM   4361 H HB2  . ASP A 1 299 ? 16.915 -14.551 8.351   1.00 27.83 ? 299 ASP A HB2  1 
ATOM   4362 H HB3  . ASP A 1 299 ? 16.648 -14.302 9.897   1.00 27.83 ? 299 ASP A HB3  1 
ATOM   4363 N N    . LEU A 1 300 ? 14.195 -11.323 9.688   1.00 21.54 ? 300 LEU A N    1 
ATOM   4364 C CA   . LEU A 1 300 ? 13.560 -10.565 10.761  1.00 19.71 ? 300 LEU A CA   1 
ATOM   4365 C C    . LEU A 1 300 ? 12.077 -10.438 10.471  1.00 24.81 ? 300 LEU A C    1 
ATOM   4366 O O    . LEU A 1 300 ? 11.681 -10.271 9.315   1.00 24.72 ? 300 LEU A O    1 
ATOM   4367 C CB   . LEU A 1 300 ? 14.135 -9.159  10.847  1.00 20.26 ? 300 LEU A CB   1 
ATOM   4368 C CG   . LEU A 1 300 ? 15.615 -9.047  11.206  1.00 19.28 ? 300 LEU A CG   1 
ATOM   4369 C CD1  . LEU A 1 300 ? 16.097 -7.633  11.205  1.00 20.09 ? 300 LEU A CD1  1 
ATOM   4370 C CD2  . LEU A 1 300 ? 15.821 -9.702  12.568  1.00 22.06 ? 300 LEU A CD2  1 
ATOM   4371 H H    . LEU A 1 300 ? 14.023 -11.017 8.903   1.00 25.84 ? 300 LEU A H    1 
ATOM   4372 H HA   . LEU A 1 300 ? 13.694 -11.028 11.603  1.00 23.65 ? 300 LEU A HA   1 
ATOM   4373 H HB2  . LEU A 1 300 ? 14.018 -8.734  9.983   1.00 24.32 ? 300 LEU A HB2  1 
ATOM   4374 H HB3  . LEU A 1 300 ? 13.640 -8.674  11.526  1.00 24.32 ? 300 LEU A HB3  1 
ATOM   4375 H HG   . LEU A 1 300 ? 16.148 -9.501  10.534  1.00 23.13 ? 300 LEU A HG   1 
ATOM   4376 H HD11 . LEU A 1 300 ? 17.044 -7.622  11.413  1.00 24.11 ? 300 LEU A HD11 1 
ATOM   4377 H HD12 . LEU A 1 300 ? 15.946 -7.248  10.328  1.00 24.11 ? 300 LEU A HD12 1 
ATOM   4378 H HD13 . LEU A 1 300 ? 15.606 -7.132  11.875  1.00 24.11 ? 300 LEU A HD13 1 
ATOM   4379 H HD21 . LEU A 1 300 ? 16.724 -9.519  12.873  1.00 26.47 ? 300 LEU A HD21 1 
ATOM   4380 H HD22 . LEU A 1 300 ? 15.179 -9.336  13.195  1.00 26.47 ? 300 LEU A HD22 1 
ATOM   4381 H HD23 . LEU A 1 300 ? 15.690 -10.660 12.481  1.00 26.47 ? 300 LEU A HD23 1 
ATOM   4382 N N    . ASN A 1 301 ? 11.246 -10.505 11.511  1.00 19.36 ? 301 ASN A N    1 
ATOM   4383 C CA   . ASN A 1 301 ? 9.831  -10.172 11.339  1.00 19.34 ? 301 ASN A CA   1 
ATOM   4384 C C    . ASN A 1 301 ? 9.689  -8.658  11.119  1.00 18.48 ? 301 ASN A C    1 
ATOM   4385 O O    . ASN A 1 301 ? 10.655 -7.898  11.184  1.00 17.63 ? 301 ASN A O    1 
ATOM   4386 C CB   . ASN A 1 301 ? 8.982  -10.735 12.480  1.00 21.98 ? 301 ASN A CB   1 
ATOM   4387 C CG   . ASN A 1 301 ? 9.223  -10.038 13.804  1.00 21.72 ? 301 ASN A CG   1 
ATOM   4388 O OD1  . ASN A 1 301 ? 9.480  -8.843  13.874  1.00 21.02 ? 301 ASN A OD1  1 
ATOM   4389 N ND2  . ASN A 1 301 ? 9.046  -10.787 14.883  1.00 26.30 ? 301 ASN A ND2  1 
ATOM   4390 H H    . ASN A 1 301 ? 11.471 -10.735 12.308  1.00 23.23 ? 301 ASN A H    1 
ATOM   4391 H HA   . ASN A 1 301 ? 9.481  -10.604 10.544  1.00 23.20 ? 301 ASN A HA   1 
ATOM   4392 H HB2  . ASN A 1 301 ? 8.044  -10.630 12.255  1.00 26.38 ? 301 ASN A HB2  1 
ATOM   4393 H HB3  . ASN A 1 301 ? 9.193  -11.674 12.595  1.00 26.38 ? 301 ASN A HB3  1 
ATOM   4394 H HD21 . ASN A 1 301 ? 9.167  -10.451 15.665  1.00 31.56 ? 301 ASN A HD21 1 
ATOM   4395 H HD22 . ASN A 1 301 ? 8.809  -11.610 14.801  1.00 31.56 ? 301 ASN A HD22 1 
ATOM   4396 N N    . ASP A 1 302 ? 8.463  -8.209  10.843  1.00 20.63 ? 302 ASP A N    1 
ATOM   4397 C CA   . ASP A 1 302 ? 8.293  -6.811  10.426  1.00 23.21 ? 302 ASP A CA   1 
ATOM   4398 C C    . ASP A 1 302 ? 8.683  -5.845  11.537  1.00 20.76 ? 302 ASP A C    1 
ATOM   4399 O O    . ASP A 1 302 ? 9.289  -4.795  11.279  1.00 20.94 ? 302 ASP A O    1 
ATOM   4400 C CB   . ASP A 1 302 ? 6.828  -6.543  10.059  1.00 27.53 ? 302 ASP A CB   1 
ATOM   4401 C CG   . ASP A 1 302 ? 6.387  -7.210  8.762   1.00 33.24 ? 302 ASP A CG   1 
ATOM   4402 O OD1  . ASP A 1 302 ? 7.243  -7.665  7.977   1.00 42.27 ? 302 ASP A OD1  1 
ATOM   4403 O OD2  . ASP A 1 302 ? 5.155  -7.287  8.547   1.00 41.04 ? 302 ASP A OD2  1 
ATOM   4404 H H    . ASP A 1 302 ? 7.739  -8.673  10.886  1.00 24.75 ? 302 ASP A H    1 
ATOM   4405 H HA   . ASP A 1 302 ? 8.860  -6.664  9.653   1.00 27.85 ? 302 ASP A HA   1 
ATOM   4406 H HB2  . ASP A 1 302 ? 6.262  -6.879  10.771  1.00 33.03 ? 302 ASP A HB2  1 
ATOM   4407 H HB3  . ASP A 1 302 ? 6.702  -5.587  9.957   1.00 33.03 ? 302 ASP A HB3  1 
ATOM   4408 N N    . GLU A 1 303 ? 8.327  -6.177  12.769  1.00 20.89 ? 303 GLU A N    1 
ATOM   4409 C CA   . GLU A 1 303 ? 8.634  -5.302  13.898  1.00 20.93 ? 303 GLU A CA   1 
ATOM   4410 C C    . GLU A 1 303 ? 10.141 -5.225  14.122  1.00 19.10 ? 303 GLU A C    1 
ATOM   4411 O O    . GLU A 1 303 ? 10.704 -4.138  14.320  1.00 18.86 ? 303 GLU A O    1 
ATOM   4412 C CB   . GLU A 1 303 ? 7.933  -5.858  15.128  1.00 24.89 ? 303 GLU A CB   1 
ATOM   4413 C CG   . GLU A 1 303 ? 6.393  -5.778  15.078  1.00 31.43 ? 303 GLU A CG   1 
ATOM   4414 C CD   . GLU A 1 303 ? 5.723  -6.633  13.982  1.00 40.71 ? 303 GLU A CD   1 
ATOM   4415 O OE1  . GLU A 1 303 ? 6.084  -7.825  13.809  1.00 31.10 ? 303 GLU A OE1  1 
ATOM   4416 O OE2  . GLU A 1 303 ? 4.788  -6.121  13.323  1.00 38.03 ? 303 GLU A OE2  1 
ATOM   4417 H H    . GLU A 1 303 ? 7.909  -6.898  12.981  1.00 25.07 ? 303 GLU A H    1 
ATOM   4418 H HA   . GLU A 1 303 ? 8.314  -4.402  13.731  1.00 25.11 ? 303 GLU A HA   1 
ATOM   4419 H HB2  . GLU A 1 303 ? 8.175  -6.792  15.225  1.00 29.87 ? 303 GLU A HB2  1 
ATOM   4420 H HB3  . GLU A 1 303 ? 8.227  -5.356  15.904  1.00 29.87 ? 303 GLU A HB3  1 
ATOM   4421 H HG2  . GLU A 1 303 ? 6.043  -6.078  15.932  1.00 37.72 ? 303 GLU A HG2  1 
ATOM   4422 H HG3  . GLU A 1 303 ? 6.138  -4.856  14.922  1.00 37.72 ? 303 GLU A HG3  1 
ATOM   4423 N N    . GLU A 1 304 ? 10.815 -6.368  14.070  1.00 16.98 ? 304 GLU A N    1 
ATOM   4424 C CA   . GLU A 1 304 ? 12.257 -6.396  14.269  1.00 16.48 ? 304 GLU A CA   1 
ATOM   4425 C C    . GLU A 1 304 ? 12.979 -5.712  13.117  1.00 16.35 ? 304 GLU A C    1 
ATOM   4426 O O    . GLU A 1 304 ? 14.017 -5.080  13.313  1.00 15.93 ? 304 GLU A O    1 
ATOM   4427 C CB   . GLU A 1 304 ? 12.729 -7.852  14.381  1.00 18.33 ? 304 GLU A CB   1 
ATOM   4428 C CG   . GLU A 1 304 ? 12.208 -8.738  15.519  1.00 27.11 ? 304 GLU A CG   1 
ATOM   4429 C CD   . GLU A 1 304 ? 12.565 -10.266 15.370  1.00 41.94 ? 304 GLU A CD   1 
ATOM   4430 O OE1  . GLU A 1 304 ? 12.520 -10.878 14.252  1.00 33.91 ? 304 GLU A OE1  1 
ATOM   4431 O OE2  . GLU A 1 304 ? 12.876 -10.870 16.419  1.00 44.39 ? 304 GLU A OE2  1 
ATOM   4432 H H    . GLU A 1 304 ? 10.464 -7.139  13.922  1.00 20.37 ? 304 GLU A H    1 
ATOM   4433 H HA   . GLU A 1 304 ? 12.473 -5.929  15.092  1.00 19.78 ? 304 GLU A HA   1 
ATOM   4434 H HB2  . GLU A 1 304 ? 12.481 -8.298  13.556  1.00 21.99 ? 304 GLU A HB2  1 
ATOM   4435 H HB3  . GLU A 1 304 ? 13.694 -7.835  14.472  1.00 21.99 ? 304 GLU A HB3  1 
ATOM   4436 H HG2  . GLU A 1 304 ? 12.592 -8.427  16.354  1.00 32.53 ? 304 GLU A HG2  1 
ATOM   4437 H HG3  . GLU A 1 304 ? 11.241 -8.665  15.551  1.00 32.53 ? 304 GLU A HG3  1 
ATOM   4438 N N    . LEU A 1 305 ? 12.475 -5.868  11.888  1.00 15.12 ? 305 LEU A N    1 
ATOM   4439 C CA   . LEU A 1 305 ? 13.106 -5.199  10.759  1.00 15.45 ? 305 LEU A CA   1 
ATOM   4440 C C    . LEU A 1 305 ? 13.026 -3.686  10.922  1.00 15.91 ? 305 LEU A C    1 
ATOM   4441 O O    . LEU A 1 305 ? 14.009 -2.970  10.673  1.00 15.32 ? 305 LEU A O    1 
ATOM   4442 C CB   . LEU A 1 305 ? 12.476 -5.649  9.444   1.00 17.16 ? 305 LEU A CB   1 
ATOM   4443 C CG   . LEU A 1 305 ? 13.118 -5.075  8.180   1.00 17.15 ? 305 LEU A CG   1 
ATOM   4444 C CD1  . LEU A 1 305 ? 14.566 -5.401  8.004   1.00 20.04 ? 305 LEU A CD1  1 
ATOM   4445 C CD2  . LEU A 1 305 ? 12.342 -5.545  6.953   1.00 21.33 ? 305 LEU A CD2  1 
ATOM   4446 H H    . LEU A 1 305 ? 11.786 -6.345  11.691  1.00 18.15 ? 305 LEU A H    1 
ATOM   4447 H HA   . LEU A 1 305 ? 14.042 -5.452  10.722  1.00 18.54 ? 305 LEU A HA   1 
ATOM   4448 H HB2  . LEU A 1 305 ? 12.541 -6.615  9.390   1.00 20.59 ? 305 LEU A HB2  1 
ATOM   4449 H HB3  . LEU A 1 305 ? 11.544 -5.378  9.444   1.00 20.59 ? 305 LEU A HB3  1 
ATOM   4450 H HG   . LEU A 1 305 ? 13.080 -4.110  8.274   1.00 20.58 ? 305 LEU A HG   1 
ATOM   4451 H HD11 . LEU A 1 305 ? 14.854 -5.094  7.130   1.00 24.05 ? 305 LEU A HD11 1 
ATOM   4452 H HD12 . LEU A 1 305 ? 15.077 -4.954  8.697   1.00 24.05 ? 305 LEU A HD12 1 
ATOM   4453 H HD13 . LEU A 1 305 ? 14.684 -6.361  8.073   1.00 24.05 ? 305 LEU A HD13 1 
ATOM   4454 H HD21 . LEU A 1 305 ? 12.743 -5.157  6.159   1.00 25.60 ? 305 LEU A HD21 1 
ATOM   4455 H HD22 . LEU A 1 305 ? 12.383 -6.513  6.904   1.00 25.60 ? 305 LEU A HD22 1 
ATOM   4456 H HD23 . LEU A 1 305 ? 11.420 -5.256  7.032   1.00 25.60 ? 305 LEU A HD23 1 
ATOM   4457 N N    . ASN A 1 306 ? 11.872 -3.179  11.347  1.00 16.06 ? 306 ASN A N    1 
ATOM   4458 C CA   . ASN A 1 306 ? 11.753 -1.740  11.550  1.00 18.59 ? 306 ASN A CA   1 
ATOM   4459 C C    . ASN A 1 306 ? 12.694 -1.255  12.651  1.00 15.23 ? 306 ASN A C    1 
ATOM   4460 O O    . ASN A 1 306 ? 13.270 -0.162  12.550  1.00 15.76 ? 306 ASN A O    1 
ATOM   4461 C CB   . ASN A 1 306 ? 10.312 -1.364  11.885  1.00 21.54 ? 306 ASN A CB   1 
ATOM   4462 C CG   . ASN A 1 306 ? 9.526  -0.935  10.651  1.00 30.95 ? 306 ASN A CG   1 
ATOM   4463 O OD1  . ASN A 1 306 ? 10.050 -0.292  9.732   1.00 28.75 ? 306 ASN A OD1  1 
ATOM   4464 N ND2  . ASN A 1 306 ? 8.241  -1.258  10.652  1.00 37.30 ? 306 ASN A ND2  1 
ATOM   4465 H H    . ASN A 1 306 ? 11.163 -3.633  11.520  1.00 19.27 ? 306 ASN A H    1 
ATOM   4466 H HA   . ASN A 1 306 ? 11.994 -1.295  10.723  1.00 22.31 ? 306 ASN A HA   1 
ATOM   4467 H HB2  . ASN A 1 306 ? 9.865  -2.131  12.276  1.00 25.85 ? 306 ASN A HB2  1 
ATOM   4468 H HB3  . ASN A 1 306 ? 10.314 -0.626  12.514  1.00 25.85 ? 306 ASN A HB3  1 
ATOM   4469 H HD21 . ASN A 1 306 ? 7.904  -1.682  11.320  1.00 44.76 ? 306 ASN A HD21 1 
ATOM   4470 H HD22 . ASN A 1 306 ? 7.743  -1.043  9.984   1.00 44.76 ? 306 ASN A HD22 1 
ATOM   4471 N N    . LYS A 1 307 ? 12.867 -2.041  13.722  1.00 13.84 ? 307 LYS A N    1 
ATOM   4472 C CA   . LYS A 1 307 ? 13.813 -1.649  14.771  1.00 14.36 ? 307 LYS A CA   1 
ATOM   4473 C C    . LYS A 1 307 ? 15.235 -1.628  14.248  1.00 13.80 ? 307 LYS A C    1 
ATOM   4474 O O    . LYS A 1 307 ? 16.018 -0.736  14.584  1.00 14.08 ? 307 LYS A O    1 
ATOM   4475 C CB   . LYS A 1 307 ? 13.692 -2.594  15.975  1.00 17.08 ? 307 LYS A CB   1 
ATOM   4476 C CG   . LYS A 1 307 ? 12.429 -2.442  16.767  1.00 18.65 ? 307 LYS A CG   1 
ATOM   4477 C CD   . LYS A 1 307 ? 12.469 -3.247  18.064  1.00 23.40 ? 307 LYS A CD   1 
ATOM   4478 C CE   . LYS A 1 307 ? 11.163 -3.087  18.825  1.00 30.85 ? 307 LYS A CE   1 
ATOM   4479 N NZ   . LYS A 1 307 ? 11.151 -1.779  19.548  1.00 36.67 ? 307 LYS A NZ   1 
ATOM   4480 H H    . LYS A 1 307 ? 12.459 -2.786  13.861  1.00 16.60 ? 307 LYS A H    1 
ATOM   4481 H HA   . LYS A 1 307 ? 13.590 -0.755  15.073  1.00 17.23 ? 307 LYS A HA   1 
ATOM   4482 H HB2  . LYS A 1 307 ? 13.727 -3.509  15.654  1.00 20.50 ? 307 LYS A HB2  1 
ATOM   4483 H HB3  . LYS A 1 307 ? 14.435 -2.425  16.575  1.00 20.50 ? 307 LYS A HB3  1 
ATOM   4484 H HG2  . LYS A 1 307 ? 12.305 -1.507  16.995  1.00 22.38 ? 307 LYS A HG2  1 
ATOM   4485 H HG3  . LYS A 1 307 ? 11.680 -2.757  16.238  1.00 22.38 ? 307 LYS A HG3  1 
ATOM   4486 H HD2  . LYS A 1 307 ? 12.595 -4.187  17.861  1.00 28.08 ? 307 LYS A HD2  1 
ATOM   4487 H HD3  . LYS A 1 307 ? 13.194 -2.928  18.624  1.00 28.08 ? 307 LYS A HD3  1 
ATOM   4488 H HE2  . LYS A 1 307 ? 10.418 -3.106  18.204  1.00 37.02 ? 307 LYS A HE2  1 
ATOM   4489 H HE3  . LYS A 1 307 ? 11.072 -3.802  19.473  1.00 37.02 ? 307 LYS A HE3  1 
ATOM   4490 H HZ1  . LYS A 1 307 ? 10.407 -1.705  20.031  1.00 44.01 ? 307 LYS A HZ1  1 
ATOM   4491 H HZ2  . LYS A 1 307 ? 11.854 -1.725  20.091  1.00 44.01 ? 307 LYS A HZ2  1 
ATOM   4492 H HZ3  . LYS A 1 307 ? 11.185 -1.108  18.964  1.00 44.01 ? 307 LYS A HZ3  1 
ATOM   4493 N N    . ARG A 1 308 ? 15.597 -2.596  13.401  1.00 12.80 ? 308 ARG A N    1 
ATOM   4494 C CA   . ARG A 1 308 ? 16.936 -2.643  12.820  1.00 12.60 ? 308 ARG A CA   1 
ATOM   4495 C C    . ARG A 1 308 ? 17.173 -1.459  11.896  1.00 12.57 ? 308 ARG A C    1 
ATOM   4496 O O    . ARG A 1 308 ? 18.262 -0.864  11.910  1.00 12.44 ? 308 ARG A O    1 
ATOM   4497 C CB   . ARG A 1 308 ? 17.085 -3.975  12.086  1.00 13.68 ? 308 ARG A CB   1 
ATOM   4498 C CG   . ARG A 1 308 ? 18.433 -4.238  11.476  1.00 13.54 ? 308 ARG A CG   1 
ATOM   4499 C CD   . ARG A 1 308 ? 19.486 -4.583  12.515  1.00 13.73 ? 308 ARG A CD   1 
ATOM   4500 N NE   . ARG A 1 308 ? 20.760 -4.943  11.890  1.00 13.23 ? 308 ARG A NE   1 
ATOM   4501 C CZ   . ARG A 1 308 ? 21.954 -4.759  12.426  1.00 12.98 ? 308 ARG A CZ   1 
ATOM   4502 N NH1  . ARG A 1 308 ? 22.098 -4.326  13.665  1.00 13.39 ? 308 ARG A NH1  1 
ATOM   4503 N NH2  . ARG A 1 308 ? 23.034 -5.019  11.715  1.00 13.46 ? 308 ARG A NH2  1 
ATOM   4504 H H    . ARG A 1 308 ? 15.084 -3.238  13.147  1.00 15.36 ? 308 ARG A H    1 
ATOM   4505 H HA   . ARG A 1 308 ? 17.613 -2.594  13.512  1.00 15.11 ? 308 ARG A HA   1 
ATOM   4506 H HB2  . ARG A 1 308 ? 16.912 -4.691  12.718  1.00 16.41 ? 308 ARG A HB2  1 
ATOM   4507 H HB3  . ARG A 1 308 ? 16.434 -4.002  11.368  1.00 16.41 ? 308 ARG A HB3  1 
ATOM   4508 H HG2  . ARG A 1 308 ? 18.363 -4.984  10.860  1.00 16.25 ? 308 ARG A HG2  1 
ATOM   4509 H HG3  . ARG A 1 308 ? 18.727 -3.444  11.002  1.00 16.25 ? 308 ARG A HG3  1 
ATOM   4510 H HD2  . ARG A 1 308 ? 19.634 -3.815  13.089  1.00 16.48 ? 308 ARG A HD2  1 
ATOM   4511 H HD3  . ARG A 1 308 ? 19.181 -5.337  13.043  1.00 16.48 ? 308 ARG A HD3  1 
ATOM   4512 H HE   . ARG A 1 308 ? 20.728 -5.305  11.110  1.00 15.88 ? 308 ARG A HE   1 
ATOM   4513 H HH11 . ARG A 1 308 ? 21.405 -4.156  14.145  1.00 16.07 ? 308 ARG A HH11 1 
ATOM   4514 H HH12 . ARG A 1 308 ? 22.886 -4.213  13.993  1.00 16.07 ? 308 ARG A HH12 1 
ATOM   4515 H HH21 . ARG A 1 308 ? 22.958 -5.307  10.908  1.00 16.15 ? 308 ARG A HH21 1 
ATOM   4516 H HH22 . ARG A 1 308 ? 23.813 -4.901  12.058  1.00 16.15 ? 308 ARG A HH22 1 
ATOM   4517 N N    . VAL A 1 309 ? 16.174 -1.114  11.083  1.00 12.13 ? 309 VAL A N    1 
ATOM   4518 C CA   . VAL A 1 309 ? 16.273 0.062   10.225  1.00 12.71 ? 309 VAL A CA   1 
ATOM   4519 C C    . VAL A 1 309 ? 16.486 1.316   11.066  1.00 12.39 ? 309 VAL A C    1 
ATOM   4520 O O    . VAL A 1 309 ? 17.358 2.135   10.768  1.00 12.30 ? 309 VAL A O    1 
ATOM   4521 C CB   . VAL A 1 309 ? 15.027 0.177   9.329   1.00 13.50 ? 309 VAL A CB   1 
ATOM   4522 C CG1  . VAL A 1 309 ? 14.957 1.528   8.624   1.00 13.91 ? 309 VAL A CG1  1 
ATOM   4523 C CG2  . VAL A 1 309 ? 15.013 -0.950  8.295   1.00 14.85 ? 309 VAL A CG2  1 
ATOM   4524 H H    . VAL A 1 309 ? 15.432 -1.543  11.010  1.00 14.56 ? 309 VAL A H    1 
ATOM   4525 H HA   . VAL A 1 309 ? 17.046 -0.038  9.648   1.00 15.26 ? 309 VAL A HA   1 
ATOM   4526 H HB   . VAL A 1 309 ? 14.245 0.101   9.898   1.00 16.20 ? 309 VAL A HB   1 
ATOM   4527 H HG11 . VAL A 1 309 ? 14.289 1.484   7.922   1.00 16.70 ? 309 VAL A HG11 1 
ATOM   4528 H HG12 . VAL A 1 309 ? 14.714 2.209   9.270   1.00 16.70 ? 309 VAL A HG12 1 
ATOM   4529 H HG13 . VAL A 1 309 ? 15.826 1.730   8.242   1.00 16.70 ? 309 VAL A HG13 1 
ATOM   4530 H HG21 . VAL A 1 309 ? 14.194 -0.894  7.778   1.00 17.82 ? 309 VAL A HG21 1 
ATOM   4531 H HG22 . VAL A 1 309 ? 15.781 -0.852  7.710   1.00 17.82 ? 309 VAL A HG22 1 
ATOM   4532 H HG23 . VAL A 1 309 ? 15.055 -1.803  8.756   1.00 17.82 ? 309 VAL A HG23 1 
ATOM   4533 N N    . ASP A 1 310 ? 15.680 1.503   12.105  1.00 12.70 ? 310 ASP A N    1 
ATOM   4534 C CA   . ASP A 1 310 ? 15.839 2.674   12.975  1.00 12.63 ? 310 ASP A CA   1 
ATOM   4535 C C    . ASP A 1 310 ? 17.235 2.741   13.571  1.00 12.23 ? 310 ASP A C    1 
ATOM   4536 O O    . ASP A 1 310 ? 17.860 3.812   13.623  1.00 11.95 ? 310 ASP A O    1 
ATOM   4537 C CB   . ASP A 1 310 ? 14.827 2.636   14.120  1.00 13.39 ? 310 ASP A CB   1 
ATOM   4538 C CG   . ASP A 1 310 ? 13.409 2.987   13.709  1.00 16.60 ? 310 ASP A CG   1 
ATOM   4539 O OD1  . ASP A 1 310 ? 13.161 3.415   12.555  1.00 17.68 ? 310 ASP A OD1  1 
ATOM   4540 O OD2  . ASP A 1 310 ? 12.509 2.809   14.559  1.00 17.93 ? 310 ASP A OD2  1 
ATOM   4541 H H    . ASP A 1 310 ? 15.039 0.976   12.331  1.00 15.24 ? 310 ASP A H    1 
ATOM   4542 H HA   . ASP A 1 310 ? 15.679 3.462   12.433  1.00 15.15 ? 310 ASP A HA   1 
ATOM   4543 H HB2  . ASP A 1 310 ? 14.812 1.741   14.492  1.00 16.06 ? 310 ASP A HB2  1 
ATOM   4544 H HB3  . ASP A 1 310 ? 15.102 3.273   14.798  1.00 16.06 ? 310 ASP A HB3  1 
ATOM   4545 N N    . TYR A 1 311 ? 17.736 1.603   14.047  1.00 12.02 ? 311 TYR A N    1 
ATOM   4546 C CA   . TYR A 1 311 ? 19.058 1.551   14.671  1.00 11.75 ? 311 TYR A CA   1 
ATOM   4547 C C    . TYR A 1 311 ? 20.164 1.923   13.701  1.00 11.11 ? 311 TYR A C    1 
ATOM   4548 O O    . TYR A 1 311 ? 21.042 2.747   14.003  1.00 11.31 ? 311 TYR A O    1 
ATOM   4549 C CB   . TYR A 1 311 ? 19.273 0.146   15.229  1.00 11.82 ? 311 TYR A CB   1 
ATOM   4550 C CG   . TYR A 1 311 ? 20.620 -0.106  15.860  1.00 11.73 ? 311 TYR A CG   1 
ATOM   4551 C CD1  . TYR A 1 311 ? 21.018 0.595   16.991  1.00 13.31 ? 311 TYR A CD1  1 
ATOM   4552 C CD2  . TYR A 1 311 ? 21.500 -1.038  15.332  1.00 13.75 ? 311 TYR A CD2  1 
ATOM   4553 C CE1  . TYR A 1 311 ? 22.222 0.368   17.576  1.00 13.96 ? 311 TYR A CE1  1 
ATOM   4554 C CE2  . TYR A 1 311 ? 22.737 -1.273  15.922  1.00 14.37 ? 311 TYR A CE2  1 
ATOM   4555 C CZ   . TYR A 1 311 ? 23.078 -0.552  17.058  1.00 14.54 ? 311 TYR A CZ   1 
ATOM   4556 O OH   . TYR A 1 311 ? 24.286 -0.766  17.684  1.00 16.48 ? 311 TYR A OH   1 
ATOM   4557 H H    . TYR A 1 311 ? 17.332 0.845   14.022  1.00 14.43 ? 311 TYR A H    1 
ATOM   4558 H HA   . TYR A 1 311 ? 19.096 2.195   15.395  1.00 14.10 ? 311 TYR A HA   1 
ATOM   4559 H HB2  . TYR A 1 311 ? 18.601 -0.017  15.909  1.00 14.19 ? 311 TYR A HB2  1 
ATOM   4560 H HB3  . TYR A 1 311 ? 19.171 -0.489  14.503  1.00 14.19 ? 311 TYR A HB3  1 
ATOM   4561 H HD1  . TYR A 1 311 ? 20.448 1.233   17.355  1.00 15.98 ? 311 TYR A HD1  1 
ATOM   4562 H HD2  . TYR A 1 311 ? 21.259 -1.513  14.570  1.00 16.50 ? 311 TYR A HD2  1 
ATOM   4563 H HE1  . TYR A 1 311 ? 22.463 0.846   18.337  1.00 16.75 ? 311 TYR A HE1  1 
ATOM   4564 H HE2  . TYR A 1 311 ? 23.322 -1.900  15.563  1.00 17.25 ? 311 TYR A HE2  1 
ATOM   4565 H HH   . TYR A 1 311 ? 24.767 -1.272  17.217  1.00 19.77 ? 311 TYR A HH   1 
ATOM   4566 N N    . LEU A 1 312 ? 20.155 1.300   12.522  1.00 11.20 ? 312 LEU A N    1 
ATOM   4567 C CA   . LEU A 1 312 ? 21.197 1.567   11.537  1.00 10.73 ? 312 LEU A CA   1 
ATOM   4568 C C    . LEU A 1 312 ? 21.100 2.985   11.005  1.00 10.19 ? 312 LEU A C    1 
ATOM   4569 O O    . LEU A 1 312 ? 22.122 3.653   10.828  1.00 11.13 ? 312 LEU A O    1 
ATOM   4570 C CB   . LEU A 1 312 ? 21.170 0.508   10.444  1.00 12.10 ? 312 LEU A CB   1 
ATOM   4571 C CG   . LEU A 1 312 ? 21.441 -0.912  10.928  1.00 11.49 ? 312 LEU A CG   1 
ATOM   4572 C CD1  . LEU A 1 312 ? 21.318 -1.851  9.731   1.00 13.30 ? 312 LEU A CD1  1 
ATOM   4573 C CD2  . LEU A 1 312 ? 22.802 -1.035  11.538  1.00 12.19 ? 312 LEU A CD2  1 
ATOM   4574 H H    . LEU A 1 312 ? 19.564 0.726   12.273  1.00 13.44 ? 312 LEU A H    1 
ATOM   4575 H HA   . LEU A 1 312 ? 22.070 1.495   11.954  1.00 12.87 ? 312 LEU A HA   1 
ATOM   4576 H HB2  . LEU A 1 312 ? 20.292 0.514   10.031  1.00 14.51 ? 312 LEU A HB2  1 
ATOM   4577 H HB3  . LEU A 1 312 ? 21.848 0.727   9.786   1.00 14.51 ? 312 LEU A HB3  1 
ATOM   4578 H HG   . LEU A 1 312 ? 20.800 -1.151  11.616  1.00 13.78 ? 312 LEU A HG   1 
ATOM   4579 H HD11 . LEU A 1 312 ? 21.431 -2.766  10.034  1.00 15.96 ? 312 LEU A HD11 1 
ATOM   4580 H HD12 . LEU A 1 312 ? 20.441 -1.741  9.331   1.00 15.96 ? 312 LEU A HD12 1 
ATOM   4581 H HD13 . LEU A 1 312 ? 22.006 -1.630  9.084   1.00 15.96 ? 312 LEU A HD13 1 
ATOM   4582 H HD21 . LEU A 1 312 ? 22.995 -1.973  11.693  1.00 14.63 ? 312 LEU A HD21 1 
ATOM   4583 H HD22 . LEU A 1 312 ? 23.457 -0.660  10.929  1.00 14.63 ? 312 LEU A HD22 1 
ATOM   4584 H HD23 . LEU A 1 312 ? 22.817 -0.551  12.379  1.00 14.63 ? 312 LEU A HD23 1 
ATOM   4585 N N    . LEU A 1 313 ? 19.890 3.477   10.730  1.00 10.95 ? 313 LEU A N    1 
ATOM   4586 C CA   . LEU A 1 313 ? 19.765 4.868   10.310  1.00 11.23 ? 313 LEU A CA   1 
ATOM   4587 C C    . LEU A 1 313 ? 20.259 5.821   11.385  1.00 9.87  ? 313 LEU A C    1 
ATOM   4588 O O    . LEU A 1 313 ? 20.865 6.853   11.071  1.00 11.86 ? 313 LEU A O    1 
ATOM   4589 C CB   . LEU A 1 313 ? 18.330 5.214   9.946   1.00 11.70 ? 313 LEU A CB   1 
ATOM   4590 C CG   . LEU A 1 313 ? 17.821 4.606   8.657   1.00 11.70 ? 313 LEU A CG   1 
ATOM   4591 C CD1  . LEU A 1 313 ? 16.386 5.007   8.473   1.00 15.16 ? 313 LEU A CD1  1 
ATOM   4592 C CD2  . LEU A 1 313 ? 18.647 5.036   7.439   1.00 13.57 ? 313 LEU A CD2  1 
ATOM   4593 H H    . LEU A 1 313 ? 19.152 3.039   10.777  1.00 13.14 ? 313 LEU A H    1 
ATOM   4594 H HA   . LEU A 1 313 ? 20.308 4.978   9.514   1.00 13.47 ? 313 LEU A HA   1 
ATOM   4595 H HB2  . LEU A 1 313 ? 17.751 4.904   10.660  1.00 14.04 ? 313 LEU A HB2  1 
ATOM   4596 H HB3  . LEU A 1 313 ? 18.262 6.178   9.859   1.00 14.04 ? 313 LEU A HB3  1 
ATOM   4597 H HG   . LEU A 1 313 ? 17.900 3.641   8.714   1.00 14.04 ? 313 LEU A HG   1 
ATOM   4598 H HD11 . LEU A 1 313 ? 16.057 4.630   7.642   1.00 18.20 ? 313 LEU A HD11 1 
ATOM   4599 H HD12 . LEU A 1 313 ? 15.865 4.669   9.218   1.00 18.20 ? 313 LEU A HD12 1 
ATOM   4600 H HD13 . LEU A 1 313 ? 16.330 5.975   8.442   1.00 18.20 ? 313 LEU A HD13 1 
ATOM   4601 H HD21 . LEU A 1 313 ? 18.160 4.809   6.632   1.00 16.28 ? 313 LEU A HD21 1 
ATOM   4602 H HD22 . LEU A 1 313 ? 18.793 5.994   7.479   1.00 16.28 ? 313 LEU A HD22 1 
ATOM   4603 H HD23 . LEU A 1 313 ? 19.498 4.570   7.455   1.00 16.28 ? 313 LEU A HD23 1 
ATOM   4604 N N    . ALA A 1 314 ? 19.996 5.511   12.648  1.00 11.15 ? 314 ALA A N    1 
ATOM   4605 C CA   . ALA A 1 314 ? 20.484 6.361   13.725  1.00 11.41 ? 314 ALA A CA   1 
ATOM   4606 C C    . ALA A 1 314 ? 21.999 6.438   13.735  1.00 10.59 ? 314 ALA A C    1 
ATOM   4607 O O    . ALA A 1 314 ? 22.566 7.518   13.868  1.00 11.00 ? 314 ALA A O    1 
ATOM   4608 C CB   . ALA A 1 314 ? 19.941 5.848   15.049  1.00 11.66 ? 314 ALA A CB   1 
ATOM   4609 H H    . ALA A 1 314 ? 19.544 4.825   12.905  1.00 13.38 ? 314 ALA A H    1 
ATOM   4610 H HA   . ALA A 1 314 ? 20.160 7.266   13.594  1.00 13.69 ? 314 ALA A HA   1 
ATOM   4611 H HB1  . ALA A 1 314 ? 20.267 6.413   15.765  1.00 13.99 ? 314 ALA A HB1  1 
ATOM   4612 H HB2  . ALA A 1 314 ? 18.971 5.873   15.023  1.00 13.99 ? 314 ALA A HB2  1 
ATOM   4613 H HB3  . ALA A 1 314 ? 20.244 4.936   15.182  1.00 13.99 ? 314 ALA A HB3  1 
ATOM   4614 N N    . ILE A 1 315 ? 22.675 5.306   13.567  1.00 10.67 ? 315 ILE A N    1 
ATOM   4615 C CA   . ILE A 1 315 ? 24.132 5.311   13.480  1.00 10.56 ? 315 ILE A CA   1 
ATOM   4616 C C    . ILE A 1 315 ? 24.583 6.249   12.370  1.00 10.91 ? 315 ILE A C    1 
ATOM   4617 O O    . ILE A 1 315 ? 25.478 7.085   12.554  1.00 11.18 ? 315 ILE A O    1 
ATOM   4618 C CB   . ILE A 1 315 ? 24.660 3.881   13.269  1.00 10.91 ? 315 ILE A CB   1 
ATOM   4619 C CG1  . ILE A 1 315 ? 24.463 3.056   14.550  1.00 11.76 ? 315 ILE A CG1  1 
ATOM   4620 C CG2  . ILE A 1 315 ? 26.148 3.919   12.911  1.00 12.51 ? 315 ILE A CG2  1 
ATOM   4621 C CD1  . ILE A 1 315 ? 24.662 1.561   14.342  1.00 13.95 ? 315 ILE A CD1  1 
ATOM   4622 H H    . ILE A 1 315 ? 22.317 4.527   13.501  1.00 12.80 ? 315 ILE A H    1 
ATOM   4623 H HA   . ILE A 1 315 ? 24.498 5.640   14.316  1.00 12.67 ? 315 ILE A HA   1 
ATOM   4624 H HB   . ILE A 1 315 ? 24.164 3.471   12.543  1.00 13.09 ? 315 ILE A HB   1 
ATOM   4625 H HG12 . ILE A 1 315 ? 25.104 3.352   15.215  1.00 14.11 ? 315 ILE A HG12 1 
ATOM   4626 H HG13 . ILE A 1 315 ? 23.560 3.194   14.875  1.00 14.11 ? 315 ILE A HG13 1 
ATOM   4627 H HG21 . ILE A 1 315 ? 26.520 3.029   13.013  1.00 15.01 ? 315 ILE A HG21 1 
ATOM   4628 H HG22 . ILE A 1 315 ? 26.244 4.214   11.992  1.00 15.01 ? 315 ILE A HG22 1 
ATOM   4629 H HG23 . ILE A 1 315 ? 26.600 4.537   13.506  1.00 15.01 ? 315 ILE A HG23 1 
ATOM   4630 H HD11 . ILE A 1 315 ? 24.367 1.090   15.137  1.00 16.74 ? 315 ILE A HD11 1 
ATOM   4631 H HD12 . ILE A 1 315 ? 24.139 1.276   13.576  1.00 16.74 ? 315 ILE A HD12 1 
ATOM   4632 H HD13 . ILE A 1 315 ? 25.603 1.386   14.184  1.00 16.74 ? 315 ILE A HD13 1 
ATOM   4633 N N    . PHE A 1 316 ? 23.994 6.094   11.183  1.00 10.22 ? 316 PHE A N    1 
ATOM   4634 C CA   . PHE A 1 316 ? 24.338 6.949   10.050  1.00 10.15 ? 316 PHE A CA   1 
ATOM   4635 C C    . PHE A 1 316 ? 24.099 8.415   10.380  1.00 10.46 ? 316 PHE A C    1 
ATOM   4636 O O    . PHE A 1 316 ? 24.943 9.279   10.125  1.00 11.07 ? 316 PHE A O    1 
ATOM   4637 C CB   . PHE A 1 316 ? 23.516 6.522   8.842   1.00 11.12 ? 316 PHE A CB   1 
ATOM   4638 C CG   . PHE A 1 316 ? 23.570 7.487   7.705   1.00 9.99  ? 316 PHE A CG   1 
ATOM   4639 C CD1  . PHE A 1 316 ? 24.756 7.622   6.964   1.00 11.39 ? 316 PHE A CD1  1 
ATOM   4640 C CD2  . PHE A 1 316 ? 22.476 8.237   7.334   1.00 11.85 ? 316 PHE A CD2  1 
ATOM   4641 C CE1  . PHE A 1 316 ? 24.824 8.505   5.906   1.00 12.15 ? 316 PHE A CE1  1 
ATOM   4642 C CE2  . PHE A 1 316 ? 22.544 9.114   6.261   1.00 12.14 ? 316 PHE A CE2  1 
ATOM   4643 C CZ   . PHE A 1 316 ? 23.725 9.256   5.557   1.00 11.24 ? 316 PHE A CZ   1 
ATOM   4644 H H    . PHE A 1 316 ? 23.394 5.503   11.009  1.00 12.27 ? 316 PHE A H    1 
ATOM   4645 H HA   . PHE A 1 316 ? 25.279 6.847   9.837   1.00 12.18 ? 316 PHE A HA   1 
ATOM   4646 H HB2  . PHE A 1 316 ? 23.851 5.669   8.523   1.00 13.35 ? 316 PHE A HB2  1 
ATOM   4647 H HB3  . PHE A 1 316 ? 22.589 6.433   9.112   1.00 13.35 ? 316 PHE A HB3  1 
ATOM   4648 H HD1  . PHE A 1 316 ? 25.502 7.113   7.188   1.00 13.67 ? 316 PHE A HD1  1 
ATOM   4649 H HD2  . PHE A 1 316 ? 21.681 8.154   7.809   1.00 14.22 ? 316 PHE A HD2  1 
ATOM   4650 H HE1  . PHE A 1 316 ? 25.615 8.592   5.426   1.00 14.58 ? 316 PHE A HE1  1 
ATOM   4651 H HE2  . PHE A 1 316 ? 21.795 9.606   6.016   1.00 14.57 ? 316 PHE A HE2  1 
ATOM   4652 H HZ   . PHE A 1 316 ? 23.777 9.858   4.850   1.00 13.48 ? 316 PHE A HZ   1 
ATOM   4653 N N    . LEU A 1 317 ? 22.917 8.725   10.902  1.00 10.72 ? 317 LEU A N    1 
ATOM   4654 C CA   . LEU A 1 317 ? 22.546 10.120  11.125  1.00 11.36 ? 317 LEU A CA   1 
ATOM   4655 C C    . LEU A 1 317 ? 23.391 10.804  12.197  1.00 11.21 ? 317 LEU A C    1 
ATOM   4656 O O    . LEU A 1 317 ? 23.555 12.020  12.150  1.00 12.02 ? 317 LEU A O    1 
ATOM   4657 C CB   . LEU A 1 317 ? 21.077 10.234  11.467  1.00 11.49 ? 317 LEU A CB   1 
ATOM   4658 C CG   . LEU A 1 317 ? 20.163 9.928   10.280  1.00 12.26 ? 317 LEU A CG   1 
ATOM   4659 C CD1  . LEU A 1 317 ? 18.699 9.789   10.787  1.00 15.32 ? 317 LEU A CD1  1 
ATOM   4660 C CD2  . LEU A 1 317 ? 20.248 10.983  9.175   1.00 13.52 ? 317 LEU A CD2  1 
ATOM   4661 H H    . LEU A 1 317 ? 22.317 8.155   11.133  1.00 12.87 ? 317 LEU A H    1 
ATOM   4662 H HA   . LEU A 1 317 ? 22.702 10.593  10.293  1.00 13.63 ? 317 LEU A HA   1 
ATOM   4663 H HB2  . LEU A 1 317 ? 20.869 9.605   12.176  1.00 13.79 ? 317 LEU A HB2  1 
ATOM   4664 H HB3  . LEU A 1 317 ? 20.892 11.139  11.763  1.00 13.79 ? 317 LEU A HB3  1 
ATOM   4665 H HG   . LEU A 1 317 ? 20.456 9.095   9.878   1.00 14.71 ? 317 LEU A HG   1 
ATOM   4666 H HD11 . LEU A 1 317 ? 18.121 9.598   10.032  1.00 18.39 ? 317 LEU A HD11 1 
ATOM   4667 H HD12 . LEU A 1 317 ? 18.655 9.064   11.429  1.00 18.39 ? 317 LEU A HD12 1 
ATOM   4668 H HD13 . LEU A 1 317 ? 18.431 10.621  11.208  1.00 18.39 ? 317 LEU A HD13 1 
ATOM   4669 H HD21 . LEU A 1 317 ? 19.546 10.818  8.526   1.00 16.22 ? 317 LEU A HD21 1 
ATOM   4670 H HD22 . LEU A 1 317 ? 20.134 11.862  9.569   1.00 16.22 ? 317 LEU A HD22 1 
ATOM   4671 H HD23 . LEU A 1 317 ? 21.116 10.923  8.747   1.00 16.22 ? 317 LEU A HD23 1 
ATOM   4672 N N    . ILE A 1 318 ? 23.932 10.049  13.153  1.00 11.25 ? 318 ILE A N    1 
ATOM   4673 C CA   . ILE A 1 318 ? 24.867 10.610  14.124  1.00 11.55 ? 318 ILE A CA   1 
ATOM   4674 C C    . ILE A 1 318 ? 26.131 11.096  13.441  1.00 10.31 ? 318 ILE A C    1 
ATOM   4675 O O    . ILE A 1 318 ? 26.837 11.970  13.965  1.00 12.37 ? 318 ILE A O    1 
ATOM   4676 C CB   . ILE A 1 318 ? 25.119 9.552   15.216  1.00 11.48 ? 318 ILE A CB   1 
ATOM   4677 C CG1  . ILE A 1 318 ? 23.865 9.354   16.108  1.00 12.90 ? 318 ILE A CG1  1 
ATOM   4678 C CG2  . ILE A 1 318 ? 26.366 9.826   16.029  1.00 14.23 ? 318 ILE A CG2  1 
ATOM   4679 C CD1  . ILE A 1 318 ? 23.281 10.578  16.713  1.00 15.42 ? 318 ILE A CD1  1 
ATOM   4680 H H    . ILE A 1 318 ? 23.775 9.211   13.261  1.00 13.50 ? 318 ILE A H    1 
ATOM   4681 H HA   . ILE A 1 318 ? 24.488 11.394  14.551  1.00 13.86 ? 318 ILE A HA   1 
ATOM   4682 H HB   . ILE A 1 318 ? 25.284 8.715   14.755  1.00 13.78 ? 318 ILE A HB   1 
ATOM   4683 H HG12 . ILE A 1 318 ? 23.171 8.946   15.566  1.00 15.48 ? 318 ILE A HG12 1 
ATOM   4684 H HG13 . ILE A 1 318 ? 24.105 8.762   16.838  1.00 15.48 ? 318 ILE A HG13 1 
ATOM   4685 H HG21 . ILE A 1 318 ? 26.407 9.198   16.767  1.00 17.07 ? 318 ILE A HG21 1 
ATOM   4686 H HG22 . ILE A 1 318 ? 27.144 9.719   15.460  1.00 17.07 ? 318 ILE A HG22 1 
ATOM   4687 H HG23 . ILE A 1 318 ? 26.328 10.734  16.370  1.00 17.07 ? 318 ILE A HG23 1 
ATOM   4688 H HD11 . ILE A 1 318 ? 22.690 10.321  17.438  1.00 18.51 ? 318 ILE A HD11 1 
ATOM   4689 H HD12 . ILE A 1 318 ? 23.999 11.135  17.053  1.00 18.51 ? 318 ILE A HD12 1 
ATOM   4690 H HD13 . ILE A 1 318 ? 22.782 11.059  16.035  1.00 18.51 ? 318 ILE A HD13 1 
ATOM   4691 N N    . CYS A 1 319 ? 26.469 10.574  12.273  1.00 11.17 ? 319 CYS A N    1 
ATOM   4692 C CA   . CYS A 1 319 ? 27.712 10.944  11.551  1.00 11.83 ? 319 CYS A CA   1 
ATOM   4693 C C    . CYS A 1 319 ? 27.492 11.874  10.364  1.00 11.19 ? 319 CYS A C    1 
ATOM   4694 O O    . CYS A 1 319 ? 28.418 12.600  10.038  1.00 13.22 ? 319 CYS A O    1 
ATOM   4695 C CB   . CYS A 1 319 ? 28.319 9.695   10.923  1.00 11.93 ? 319 CYS A CB   1 
ATOM   4696 S SG   . CYS A 1 319 ? 28.672 8.349   12.088  1.00 13.14 ? 319 CYS A SG   1 
ATOM   4697 H H    . CYS A 1 319 ? 26.035 9.881   11.871  1.00 13.40 ? 319 CYS A H    1 
ATOM   4698 H HA   . CYS A 1 319 ? 28.356 11.334  12.160  1.00 14.19 ? 319 CYS A HA   1 
ATOM   4699 H HB2  . CYS A 1 319 ? 27.722 9.356   10.225  1.00 14.32 ? 319 CYS A HB2  1 
ATOM   4700 H HB3  . CYS A 1 319 ? 29.156 9.948   10.498  1.00 14.32 ? 319 CYS A HB3  1 
ATOM   4701 H HG   . CYS A 1 319 ? 27.625 7.764   11.980  1.00 15.77 ? 319 CYS A HG   1 
ATOM   4702 N N    . ALA A 1 320 ? 26.317 11.860  9.763   1.00 11.54 ? 320 ALA A N    1 
ATOM   4703 C CA   . ALA A 1 320 ? 26.100 12.462  8.429   1.00 12.19 ? 320 ALA A CA   1 
ATOM   4704 C C    . ALA A 1 320 ? 26.329 13.956  8.255   1.00 11.00 ? 320 ALA A C    1 
ATOM   4705 O O    . ALA A 1 320 ? 25.999 14.705  9.059   1.00 12.88 ? 320 ALA A O    1 
ATOM   4706 C CB   . ALA A 1 320 ? 24.697 12.131  7.989   1.00 12.82 ? 320 ALA A CB   1 
ATOM   4707 H H    . ALA A 1 320 ? 25.564 11.499  10.123  1.00 13.84 ? 320 ALA A H    1 
ATOM   4708 H HA   . ALA A 1 320 ? 26.711 11.997  7.816   1.00 14.63 ? 320 ALA A HA   1 
ATOM   4709 H HB1  . ALA A 1 320 ? 24.533 12.523  7.115   1.00 15.38 ? 320 ALA A HB1  1 
ATOM   4710 H HB2  . ALA A 1 320 ? 24.591 11.166  7.932   1.00 15.38 ? 320 ALA A HB2  1 
ATOM   4711 H HB3  . ALA A 1 320 ? 24.056 12.491  8.626   1.00 15.38 ? 320 ALA A HB3  1 
ATOM   4712 N N    . GLU A 1 321 ? 26.871 14.346  7.137   1.00 12.50 ? 321 GLU A N    1 
ATOM   4713 C CA   . GLU A 1 321 ? 26.946 15.766  6.752   1.00 13.32 ? 321 GLU A CA   1 
ATOM   4714 C C    . GLU A 1 321 ? 26.500 15.810  5.306   1.00 12.70 ? 321 GLU A C    1 
ATOM   4715 O O    . GLU A 1 321 ? 26.114 14.809  4.814   1.00 13.21 ? 321 GLU A O    1 
ATOM   4716 C CB   . GLU A 1 321 ? 28.362 16.306  6.889   1.00 13.01 ? 321 GLU A CB   1 
ATOM   4717 C CG   . GLU A 1 321 ? 28.886 16.338  8.301   1.00 14.00 ? 321 GLU A CG   1 
ATOM   4718 C CD   . GLU A 1 321 ? 28.091 17.241  9.214   1.00 16.81 ? 321 GLU A CD   1 
ATOM   4719 O OE1  . GLU A 1 321 ? 27.503 18.236  8.751   1.00 18.63 ? 321 GLU A OE1  1 
ATOM   4720 O OE2  . GLU A 1 321 ? 28.072 16.933  10.376  1.00 16.86 ? 321 GLU A OE2  1 
ATOM   4721 H H    . GLU A 1 321 ? 27.360 13.831  6.662   1.00 15.00 ? 321 GLU A H    1 
ATOM   4722 H HA   . GLU A 1 321 ? 26.324 16.305  7.281   1.00 15.98 ? 321 GLU A HA   1 
ATOM   4723 H HB2  . GLU A 1 321 ? 28.952 15.758  6.342   1.00 15.61 ? 321 GLU A HB2  1 
ATOM   4724 H HB3  . GLU A 1 321 ? 28.401 17.208  6.529   1.00 15.61 ? 321 GLU A HB3  1 
ATOM   4725 H HG2  . GLU A 1 321 ? 28.880 15.431  8.672   1.00 16.80 ? 321 GLU A HG2  1 
ATOM   4726 H HG3  . GLU A 1 321 ? 29.811 16.644  8.291   1.00 16.80 ? 321 GLU A HG3  1 
ATOM   4727 N N    . LYS A 1 322 ? 26.530 16.968  4.680   1.00 13.99 ? 322 LYS A N    1 
ATOM   4728 C CA   . LYS A 1 322 ? 26.258 17.065  3.259   1.00 14.44 ? 322 LYS A CA   1 
ATOM   4729 C C    . LYS A 1 322 ? 27.155 16.089  2.520   1.00 13.95 ? 322 LYS A C    1 
ATOM   4730 O O    . LYS A 1 322 ? 28.350 15.980  2.796   1.00 13.28 ? 322 LYS A O    1 
ATOM   4731 C CB   . LYS A 1 322 ? 26.530 18.486  2.769   1.00 14.69 ? 322 LYS A CB   1 
ATOM   4732 C CG   . LYS A 1 322 ? 26.049 18.707  1.349   1.00 21.07 ? 322 LYS A CG   1 
ATOM   4733 C CD   . LYS A 1 322 ? 26.097 20.158  0.940   1.00 23.07 ? 322 LYS A CD   1 
ATOM   4734 C CE   . LYS A 1 322 ? 25.418 20.347  -0.415  1.00 27.77 ? 322 LYS A CE   1 
ATOM   4735 N NZ   . LYS A 1 322 ? 25.430 21.777  -0.842  1.00 32.93 ? 322 LYS A NZ   1 
ATOM   4736 H H    . LYS A 1 322 ? 26.712 17.716  5.063   1.00 16.79 ? 322 LYS A H    1 
ATOM   4737 H HA   . LYS A 1 322 ? 25.328 16.859  3.079   1.00 17.33 ? 322 LYS A HA   1 
ATOM   4738 H HB2  . LYS A 1 322 ? 26.068 19.114  3.346   1.00 17.62 ? 322 LYS A HB2  1 
ATOM   4739 H HB3  . LYS A 1 322 ? 27.485 18.653  2.794   1.00 17.62 ? 322 LYS A HB3  1 
ATOM   4740 H HG2  . LYS A 1 322 ? 26.613 18.204  0.741   1.00 25.28 ? 322 LYS A HG2  1 
ATOM   4741 H HG3  . LYS A 1 322 ? 25.130 18.405  1.274   1.00 25.28 ? 322 LYS A HG3  1 
ATOM   4742 H HD2  . LYS A 1 322 ? 25.633 20.698  1.599   1.00 27.69 ? 322 LYS A HD2  1 
ATOM   4743 H HD3  . LYS A 1 322 ? 27.021 20.445  0.867   1.00 27.69 ? 322 LYS A HD3  1 
ATOM   4744 H HE2  . LYS A 1 322 ? 25.886 19.825  -1.084  1.00 33.32 ? 322 LYS A HE2  1 
ATOM   4745 H HE3  . LYS A 1 322 ? 24.494 20.056  -0.353  1.00 33.32 ? 322 LYS A HE3  1 
ATOM   4746 H HZ1  . LYS A 1 322 ? 25.033 21.862  -1.634  1.00 39.51 ? 322 LYS A HZ1  1 
ATOM   4747 H HZ2  . LYS A 1 322 ? 24.996 22.277  -0.247  1.00 39.51 ? 322 LYS A HZ2  1 
ATOM   4748 H HZ3  . LYS A 1 322 ? 26.269 22.068  -0.907  1.00 39.51 ? 322 LYS A HZ3  1 
ATOM   4749 N N    . TYR A 1 323 ? 26.562 15.370  1.569   1.00 12.90 ? 323 TYR A N    1 
ATOM   4750 C CA   . TYR A 1 323 ? 27.232 14.365  0.747   1.00 12.90 ? 323 TYR A CA   1 
ATOM   4751 C C    . TYR A 1 323 ? 27.509 13.065  1.488   1.00 12.92 ? 323 TYR A C    1 
ATOM   4752 O O    . TYR A 1 323 ? 28.362 12.274  1.053   1.00 12.26 ? 323 TYR A O    1 
ATOM   4753 C CB   . TYR A 1 323 ? 28.487 14.889  0.041   1.00 13.77 ? 323 TYR A CB   1 
ATOM   4754 C CG   . TYR A 1 323 ? 28.251 16.116  -0.761  1.00 15.81 ? 323 TYR A CG   1 
ATOM   4755 C CD1  . TYR A 1 323 ? 27.388 16.105  -1.855  1.00 17.35 ? 323 TYR A CD1  1 
ATOM   4756 C CD2  . TYR A 1 323 ? 28.910 17.299  -0.472  1.00 18.98 ? 323 TYR A CD2  1 
ATOM   4757 C CE1  . TYR A 1 323 ? 27.190 17.243  -2.634  1.00 20.37 ? 323 TYR A CE1  1 
ATOM   4758 C CE2  . TYR A 1 323 ? 28.714 18.445  -1.237  1.00 23.07 ? 323 TYR A CE2  1 
ATOM   4759 C CZ   . TYR A 1 323 ? 27.843 18.403  -2.306  1.00 22.21 ? 323 TYR A CZ   1 
ATOM   4760 O OH   . TYR A 1 323 ? 27.640 19.547  -3.071  1.00 27.23 ? 323 TYR A OH   1 
ATOM   4761 H H    . TYR A 1 323 ? 25.729 15.452  1.371   1.00 15.48 ? 323 TYR A H    1 
ATOM   4762 H HA   . TYR A 1 323 ? 26.613 14.142  0.035   1.00 15.48 ? 323 TYR A HA   1 
ATOM   4763 H HB2  . TYR A 1 323 ? 29.158 15.097  0.710   1.00 16.52 ? 323 TYR A HB2  1 
ATOM   4764 H HB3  . TYR A 1 323 ? 28.818 14.202  -0.558  1.00 16.52 ? 323 TYR A HB3  1 
ATOM   4765 H HD1  . TYR A 1 323 ? 26.935 15.321  -2.070  1.00 20.82 ? 323 TYR A HD1  1 
ATOM   4766 H HD2  . TYR A 1 323 ? 29.495 17.328  0.250   1.00 22.78 ? 323 TYR A HD2  1 
ATOM   4767 H HE1  . TYR A 1 323 ? 26.620 17.216  -3.368  1.00 24.45 ? 323 TYR A HE1  1 
ATOM   4768 H HE2  . TYR A 1 323 ? 29.166 19.231  -1.030  1.00 27.68 ? 323 TYR A HE2  1 
ATOM   4769 H HH   . TYR A 1 323 ? 28.088 20.185  -2.758  1.00 32.68 ? 323 TYR A HH   1 
ATOM   4770 N N    . SER A 1 324 ? 26.793 12.816  2.576   1.00 11.92 ? 324 SER A N    1 
ATOM   4771 C CA   . SER A 1 324 ? 26.729 11.518  3.229   1.00 10.63 ? 324 SER A CA   1 
ATOM   4772 C C    . SER A 1 324 ? 25.464 10.785  2.773   1.00 10.77 ? 324 SER A C    1 
ATOM   4773 O O    . SER A 1 324 ? 24.365 11.362  2.786   1.00 12.86 ? 324 SER A O    1 
ATOM   4774 C CB   . SER A 1 324 ? 26.684 11.666  4.755   1.00 11.42 ? 324 SER A CB   1 
ATOM   4775 O OG   . SER A 1 324 ? 27.874 12.203  5.334   1.00 11.70 ? 324 SER A OG   1 
ATOM   4776 H H    . SER A 1 324 ? 26.315 13.411  2.973   1.00 14.31 ? 324 SER A H    1 
ATOM   4777 H HA   . SER A 1 324 ? 27.513 11.003  2.983   1.00 12.76 ? 324 SER A HA   1 
ATOM   4778 H HB2  . SER A 1 324 ? 25.949 12.258  4.978   1.00 13.70 ? 324 SER A HB2  1 
ATOM   4779 H HB3  . SER A 1 324 ? 26.533 10.788  5.138   1.00 13.70 ? 324 SER A HB3  1 
ATOM   4780 H HG   . SER A 1 324 ? 28.064 12.937  4.973   1.00 14.04 ? 324 SER A HG   1 
ATOM   4781 N N    . TYR A 1 325 ? 25.612 9.508   2.427   1.00 11.18 ? 325 TYR A N    1 
ATOM   4782 C CA   . TYR A 1 325 ? 24.531 8.706   1.895   1.00 11.28 ? 325 TYR A CA   1 
ATOM   4783 C C    . TYR A 1 325 ? 24.586 7.335   2.552   1.00 11.41 ? 325 TYR A C    1 
ATOM   4784 O O    . TYR A 1 325 ? 25.672 6.840   2.862   1.00 11.93 ? 325 TYR A O    1 
ATOM   4785 C CB   . TYR A 1 325 ? 24.692 8.513   0.366   1.00 11.38 ? 325 TYR A CB   1 
ATOM   4786 C CG   . TYR A 1 325 ? 24.814 9.778   -0.434  1.00 11.88 ? 325 TYR A CG   1 
ATOM   4787 C CD1  . TYR A 1 325 ? 26.050 10.405  -0.624  1.00 11.69 ? 325 TYR A CD1  1 
ATOM   4788 C CD2  . TYR A 1 325 ? 23.704 10.372  -0.987  1.00 13.15 ? 325 TYR A CD2  1 
ATOM   4789 C CE1  . TYR A 1 325 ? 26.156 11.572  -1.349  1.00 12.93 ? 325 TYR A CE1  1 
ATOM   4790 C CE2  . TYR A 1 325 ? 23.793 11.544  -1.721  1.00 13.59 ? 325 TYR A CE2  1 
ATOM   4791 C CZ   . TYR A 1 325 ? 25.030 12.146  -1.903  1.00 12.68 ? 325 TYR A CZ   1 
ATOM   4792 O OH   . TYR A 1 325 ? 25.187 13.317  -2.608  1.00 14.17 ? 325 TYR A OH   1 
ATOM   4793 H H    . TYR A 1 325 ? 26.353 9.078   2.496   1.00 13.42 ? 325 TYR A H    1 
ATOM   4794 H HA   . TYR A 1 325 ? 23.678 9.129   2.083   1.00 13.53 ? 325 TYR A HA   1 
ATOM   4795 H HB2  . TYR A 1 325 ? 25.495 7.992   0.207   1.00 13.66 ? 325 TYR A HB2  1 
ATOM   4796 H HB3  . TYR A 1 325 ? 23.915 8.035   0.035   1.00 13.66 ? 325 TYR A HB3  1 
ATOM   4797 H HD1  . TYR A 1 325 ? 26.815 10.028  -0.253  1.00 14.02 ? 325 TYR A HD1  1 
ATOM   4798 H HD2  . TYR A 1 325 ? 22.871 9.976   -0.865  1.00 15.78 ? 325 TYR A HD2  1 
ATOM   4799 H HE1  . TYR A 1 325 ? 26.987 11.972  -1.465  1.00 15.52 ? 325 TYR A HE1  1 
ATOM   4800 H HE2  . TYR A 1 325 ? 23.029 11.925  -2.090  1.00 16.31 ? 325 TYR A HE2  1 
ATOM   4801 H HH   . TYR A 1 325 ? 24.472 13.513  -3.003  1.00 17.01 ? 325 TYR A HH   1 
ATOM   4802 N N    . VAL A 1 326 ? 23.419 6.707   2.773   1.00 11.22 ? 326 VAL A N    1 
ATOM   4803 C CA   . VAL A 1 326 ? 23.350 5.453   3.515   1.00 11.16 ? 326 VAL A CA   1 
ATOM   4804 C C    . VAL A 1 326 ? 22.740 4.364   2.640   1.00 10.40 ? 326 VAL A C    1 
ATOM   4805 O O    . VAL A 1 326 ? 21.842 4.609   1.835   1.00 11.65 ? 326 VAL A O    1 
ATOM   4806 C CB   . VAL A 1 326 ? 22.545 5.658   4.821   1.00 10.77 ? 326 VAL A CB   1 
ATOM   4807 C CG1  . VAL A 1 326 ? 21.105 5.981   4.580   1.00 12.31 ? 326 VAL A CG1  1 
ATOM   4808 C CG2  . VAL A 1 326 ? 22.691 4.456   5.729   1.00 12.11 ? 326 VAL A CG2  1 
ATOM   4809 H H    . VAL A 1 326 ? 22.657 6.995   2.500   1.00 13.46 ? 326 VAL A H    1 
ATOM   4810 H HA   . VAL A 1 326 ? 24.244 5.146   3.735   1.00 13.39 ? 326 VAL A HA   1 
ATOM   4811 H HB   . VAL A 1 326 ? 22.919 6.434   5.269   1.00 12.92 ? 326 VAL A HB   1 
ATOM   4812 H HG11 . VAL A 1 326 ? 20.693 6.234   5.421   1.00 14.78 ? 326 VAL A HG11 1 
ATOM   4813 H HG12 . VAL A 1 326 ? 21.047 6.716   3.949   1.00 14.78 ? 326 VAL A HG12 1 
ATOM   4814 H HG13 . VAL A 1 326 ? 20.662 5.198   4.217   1.00 14.78 ? 326 VAL A HG13 1 
ATOM   4815 H HG21 . VAL A 1 326 ? 22.263 4.648   6.578   1.00 14.53 ? 326 VAL A HG21 1 
ATOM   4816 H HG22 . VAL A 1 326 ? 22.266 3.691   5.310   1.00 14.53 ? 326 VAL A HG22 1 
ATOM   4817 H HG23 . VAL A 1 326 ? 23.634 4.276   5.867   1.00 14.53 ? 326 VAL A HG23 1 
ATOM   4818 N N    . TYR A 1 327 ? 23.215 3.142   2.838   1.00 10.89 ? 327 TYR A N    1 
ATOM   4819 C CA   . TYR A 1 327 ? 22.614 1.977   2.198   1.00 10.83 ? 327 TYR A CA   1 
ATOM   4820 C C    . TYR A 1 327 ? 22.456 0.865   3.221   1.00 10.99 ? 327 TYR A C    1 
ATOM   4821 O O    . TYR A 1 327 ? 23.447 0.220   3.614   1.00 11.87 ? 327 TYR A O    1 
ATOM   4822 C CB   . TYR A 1 327 ? 23.522 1.468   1.101   1.00 13.09 ? 327 TYR A CB   1 
ATOM   4823 C CG   . TYR A 1 327 ? 23.087 0.296   0.309   1.00 14.11 ? 327 TYR A CG   1 
ATOM   4824 C CD1  . TYR A 1 327 ? 21.782 0.052   -0.028  1.00 14.61 ? 327 TYR A CD1  1 
ATOM   4825 C CD2  . TYR A 1 327 ? 24.075 -0.530  -0.183  1.00 17.09 ? 327 TYR A CD2  1 
ATOM   4826 C CE1  . TYR A 1 327 ? 21.480 -1.047  -0.946  1.00 16.65 ? 327 TYR A CE1  1 
ATOM   4827 C CE2  . TYR A 1 327 ? 23.795 -1.585  -0.991  1.00 17.53 ? 327 TYR A CE2  1 
ATOM   4828 C CZ   . TYR A 1 327 ? 22.522 -1.826  -1.369  1.00 12.43 ? 327 TYR A CZ   1 
ATOM   4829 O OH   . TYR A 1 327 ? 22.315 -2.900  -2.255  1.00 18.32 ? 327 TYR A OH   1 
ATOM   4830 H H    . TYR A 1 327 ? 23.889 2.961   3.340   1.00 13.06 ? 327 TYR A H    1 
ATOM   4831 H HA   . TYR A 1 327 ? 21.741 2.228   1.856   1.00 12.99 ? 327 TYR A HA   1 
ATOM   4832 H HB2  . TYR A 1 327 ? 23.654 2.193   0.470   1.00 15.71 ? 327 TYR A HB2  1 
ATOM   4833 H HB3  . TYR A 1 327 ? 24.368 1.226   1.509   1.00 15.71 ? 327 TYR A HB3  1 
ATOM   4834 H HD1  . TYR A 1 327 ? 21.098 0.576   0.322   1.00 17.53 ? 327 TYR A HD1  1 
ATOM   4835 H HD2  . TYR A 1 327 ? 24.960 -0.361  0.046   1.00 20.51 ? 327 TYR A HD2  1 
ATOM   4836 H HE1  . TYR A 1 327 ? 20.610 -1.210  -1.232  1.00 19.98 ? 327 TYR A HE1  1 
ATOM   4837 H HE2  . TYR A 1 327 ? 24.480 -2.141  -1.284  1.00 21.04 ? 327 TYR A HE2  1 
ATOM   4838 H HH   . TYR A 1 327 ? 23.025 -3.340  -2.344  1.00 21.98 ? 327 TYR A HH   1 
ATOM   4839 N N    . LEU A 1 328 ? 21.215 0.631   3.627   1.00 11.55 ? 328 LEU A N    1 
ATOM   4840 C CA   . LEU A 1 328 ? 20.838 -0.508  4.470   1.00 11.46 ? 328 LEU A CA   1 
ATOM   4841 C C    . LEU A 1 328 ? 20.500 -1.668  3.550   1.00 12.22 ? 328 LEU A C    1 
ATOM   4842 O O    . LEU A 1 328 ? 19.502 -1.628  2.837   1.00 14.33 ? 328 LEU A O    1 
ATOM   4843 C CB   . LEU A 1 328 ? 19.627 -0.165  5.347   1.00 12.70 ? 328 LEU A CB   1 
ATOM   4844 C CG   . LEU A 1 328 ? 19.723 1.116   6.176   1.00 15.57 ? 328 LEU A CG   1 
ATOM   4845 C CD1  . LEU A 1 328 ? 18.544 1.157   7.170   1.00 15.41 ? 328 LEU A CD1  1 
ATOM   4846 C CD2  . LEU A 1 328 ? 21.066 1.264   6.839   1.00 15.08 ? 328 LEU A CD2  1 
ATOM   4847 H H    . LEU A 1 328 ? 20.546 1.133   3.424   1.00 13.86 ? 328 LEU A H    1 
ATOM   4848 H HA   . LEU A 1 328 ? 21.580 -0.744  5.047   1.00 13.76 ? 328 LEU A HA   1 
ATOM   4849 H HB2  . LEU A 1 328 ? 18.854 -0.073  4.768   1.00 15.24 ? 328 LEU A HB2  1 
ATOM   4850 H HB3  . LEU A 1 328 ? 19.490 -0.897  5.968   1.00 15.24 ? 328 LEU A HB3  1 
ATOM   4851 H HG   . LEU A 1 328 ? 19.654 1.893   5.598   1.00 18.68 ? 328 LEU A HG   1 
ATOM   4852 H HD11 . LEU A 1 328 ? 18.726 1.826   7.849   1.00 18.49 ? 328 LEU A HD11 1 
ATOM   4853 H HD12 . LEU A 1 328 ? 17.733 1.387   6.689   1.00 18.49 ? 328 LEU A HD12 1 
ATOM   4854 H HD13 . LEU A 1 328 ? 18.448 0.285   7.582   1.00 18.49 ? 328 LEU A HD13 1 
ATOM   4855 H HD21 . LEU A 1 328 ? 21.029 2.002   7.467   1.00 18.10 ? 328 LEU A HD21 1 
ATOM   4856 H HD22 . LEU A 1 328 ? 21.278 0.442   7.308   1.00 18.10 ? 328 LEU A HD22 1 
ATOM   4857 H HD23 . LEU A 1 328 ? 21.736 1.440   6.160   1.00 18.10 ? 328 LEU A HD23 1 
ATOM   4858 N N    . HIS A 1 329 ? 21.302 -2.721  3.583   1.00 11.91 ? 329 HIS A N    1 
ATOM   4859 C CA   . HIS A 1 329 ? 21.227 -3.725  2.537   1.00 10.94 ? 329 HIS A CA   1 
ATOM   4860 C C    . HIS A 1 329 ? 21.092 -5.122  3.103   1.00 11.38 ? 329 HIS A C    1 
ATOM   4861 O O    . HIS A 1 329 ? 21.404 -5.406  4.257   1.00 11.82 ? 329 HIS A O    1 
ATOM   4862 C CB   . HIS A 1 329 ? 22.482 -3.623  1.665   1.00 11.97 ? 329 HIS A CB   1 
ATOM   4863 C CG   . HIS A 1 329 ? 23.727 -4.031  2.378   1.00 11.98 ? 329 HIS A CG   1 
ATOM   4864 N ND1  . HIS A 1 329 ? 24.094 -5.348  2.510   1.00 12.56 ? 329 HIS A ND1  1 
ATOM   4865 C CD2  . HIS A 1 329 ? 24.678 -3.307  3.017   1.00 11.73 ? 329 HIS A CD2  1 
ATOM   4866 C CE1  . HIS A 1 329 ? 25.227 -5.420  3.189   1.00 12.76 ? 329 HIS A CE1  1 
ATOM   4867 N NE2  . HIS A 1 329 ? 25.600 -4.192  3.511   1.00 12.50 ? 329 HIS A NE2  1 
ATOM   4868 H H    . HIS A 1 329 ? 21.888 -2.874  4.193   1.00 14.29 ? 329 HIS A H    1 
ATOM   4869 H HA   . HIS A 1 329 ? 20.428 -3.586  2.005   1.00 13.13 ? 329 HIS A HA   1 
ATOM   4870 H HB2  . HIS A 1 329 ? 22.377 -4.202  0.894   1.00 14.37 ? 329 HIS A HB2  1 
ATOM   4871 H HB3  . HIS A 1 329 ? 22.590 -2.703  1.377   1.00 14.37 ? 329 HIS A HB3  1 
ATOM   4872 H HD2  . HIS A 1 329 ? 24.701 -2.381  3.105   1.00 14.07 ? 329 HIS A HD2  1 
ATOM   4873 H HE1  . HIS A 1 329 ? 25.683 -6.201  3.404   1.00 15.31 ? 329 HIS A HE1  1 
ATOM   4874 H HE2  . HIS A 1 329 ? 26.306 -3.984  3.956   1.00 15.00 ? 329 HIS A HE2  1 
ATOM   4875 N N    . ASP A 1 330 ? 20.603 -6.002  2.238   1.00 12.12 ? 330 ASP A N    1 
ATOM   4876 C CA   . ASP A 1 330 ? 20.593 -7.444  2.449   1.00 13.37 ? 330 ASP A CA   1 
ATOM   4877 C C    . ASP A 1 330 ? 21.502 -8.077  1.392   1.00 12.51 ? 330 ASP A C    1 
ATOM   4878 O O    . ASP A 1 330 ? 21.068 -8.941  0.618   1.00 13.65 ? 330 ASP A O    1 
ATOM   4879 C CB   . ASP A 1 330 ? 19.162 -7.962  2.334   1.00 13.81 ? 330 ASP A CB   1 
ATOM   4880 C CG   . ASP A 1 330 ? 19.024 -9.433  2.668   1.00 14.29 ? 330 ASP A CG   1 
ATOM   4881 O OD1  . ASP A 1 330 ? 19.887 -9.991  3.399   1.00 14.32 ? 330 ASP A OD1  1 
ATOM   4882 O OD2  . ASP A 1 330 ? 18.035 -10.036 2.218   1.00 14.86 ? 330 ASP A OD2  1 
ATOM   4883 H H    . ASP A 1 330 ? 20.254 -5.779  1.484   1.00 14.54 ? 330 ASP A H    1 
ATOM   4884 H HA   . ASP A 1 330 ? 20.915 -7.685  3.331   1.00 16.04 ? 330 ASP A HA   1 
ATOM   4885 H HB2  . ASP A 1 330 ? 18.598 -7.464  2.946   1.00 16.58 ? 330 ASP A HB2  1 
ATOM   4886 H HB3  . ASP A 1 330 ? 18.855 -7.834  1.422   1.00 16.58 ? 330 ASP A HB3  1 
ATOM   4887 N N    . GLY A 1 331 ? 22.763 -7.653  1.367   1.00 12.62 ? 331 GLY A N    1 
ATOM   4888 C CA   . GLY A 1 331 ? 23.689 -8.084  0.344   1.00 12.48 ? 331 GLY A CA   1 
ATOM   4889 C C    . GLY A 1 331 ? 23.545 -7.245  -0.909  1.00 12.57 ? 331 GLY A C    1 
ATOM   4890 O O    . GLY A 1 331 ? 22.582 -6.525  -1.112  1.00 13.69 ? 331 GLY A O    1 
ATOM   4891 H H    . GLY A 1 331 ? 23.103 -7.109  1.941   1.00 15.15 ? 331 GLY A H    1 
ATOM   4892 H HA2  . GLY A 1 331 ? 24.598 -8.002  0.671   1.00 14.97 ? 331 GLY A HA2  1 
ATOM   4893 H HA3  . GLY A 1 331 ? 23.517 -9.012  0.119   1.00 14.97 ? 331 GLY A HA3  1 
ATOM   4894 N N    . TYR A 1 332 ? 24.530 -7.372  -1.787  1.00 12.25 ? 332 TYR A N    1 
ATOM   4895 C CA   . TYR A 1 332 ? 24.618 -6.544  -2.977  1.00 13.18 ? 332 TYR A CA   1 
ATOM   4896 C C    . TYR A 1 332 ? 24.069 -7.215  -4.220  1.00 14.37 ? 332 TYR A C    1 
ATOM   4897 O O    . TYR A 1 332 ? 24.001 -6.579  -5.274  1.00 15.59 ? 332 TYR A O    1 
ATOM   4898 C CB   . TYR A 1 332 ? 26.073 -6.125  -3.204  1.00 13.54 ? 332 TYR A CB   1 
ATOM   4899 C CG   . TYR A 1 332 ? 26.701 -5.355  -2.046  1.00 12.43 ? 332 TYR A CG   1 
ATOM   4900 C CD1  . TYR A 1 332 ? 25.919 -4.582  -1.203  1.00 13.79 ? 332 TYR A CD1  1 
ATOM   4901 C CD2  . TYR A 1 332 ? 28.071 -5.373  -1.836  1.00 13.11 ? 332 TYR A CD2  1 
ATOM   4902 C CE1  . TYR A 1 332 ? 26.501 -3.857  -0.143  1.00 13.04 ? 332 TYR A CE1  1 
ATOM   4903 C CE2  . TYR A 1 332 ? 28.641 -4.636  -0.816  1.00 13.16 ? 332 TYR A CE2  1 
ATOM   4904 C CZ   . TYR A 1 332 ? 27.831 -3.900  0.025   1.00 12.67 ? 332 TYR A CZ   1 
ATOM   4905 O OH   . TYR A 1 332 ? 28.343 -3.138  1.073   1.00 13.78 ? 332 TYR A OH   1 
ATOM   4906 H H    . TYR A 1 332 ? 25.170 -7.942  -1.712  1.00 14.70 ? 332 TYR A H    1 
ATOM   4907 H HA   . TYR A 1 332 ? 24.093 -5.740  -2.836  1.00 15.82 ? 332 TYR A HA   1 
ATOM   4908 H HB2  . TYR A 1 332 ? 26.605 -6.924  -3.347  1.00 16.25 ? 332 TYR A HB2  1 
ATOM   4909 H HB3  . TYR A 1 332 ? 26.111 -5.556  -3.989  1.00 16.25 ? 332 TYR A HB3  1 
ATOM   4910 H HD1  . TYR A 1 332 ? 25.000 -4.540  -1.338  1.00 16.55 ? 332 TYR A HD1  1 
ATOM   4911 H HD2  . TYR A 1 332 ? 28.613 -5.887  -2.389  1.00 15.73 ? 332 TYR A HD2  1 
ATOM   4912 H HE1  . TYR A 1 332 ? 25.970 -3.356  0.433   1.00 15.65 ? 332 TYR A HE1  1 
ATOM   4913 H HE2  . TYR A 1 332 ? 29.564 -4.637  -0.697  1.00 15.79 ? 332 TYR A HE2  1 
ATOM   4914 H HH   . TYR A 1 332 ? 29.183 -3.140  1.046   1.00 16.54 ? 332 TYR A HH   1 
ATOM   4915 N N    . LEU A 1 333 ? 23.666 -8.471  -4.132  1.00 13.14 ? 333 LEU A N    1 
ATOM   4916 C CA   . LEU A 1 333 ? 23.062 -9.170  -5.267  1.00 12.44 ? 333 LEU A CA   1 
ATOM   4917 C C    . LEU A 1 333 ? 21.555 -8.928  -5.250  1.00 12.22 ? 333 LEU A C    1 
ATOM   4918 O O    . LEU A 1 333 ? 20.851 -9.362  -4.321  1.00 13.74 ? 333 LEU A O    1 
ATOM   4919 C CB   . LEU A 1 333 ? 23.404 -10.655 -5.220  1.00 13.91 ? 333 LEU A CB   1 
ATOM   4920 C CG   . LEU A 1 333 ? 22.753 -11.505 -6.299  1.00 13.23 ? 333 LEU A CG   1 
ATOM   4921 C CD1  . LEU A 1 333 ? 23.042 -11.002 -7.707  1.00 14.85 ? 333 LEU A CD1  1 
ATOM   4922 C CD2  . LEU A 1 333 ? 23.194 -12.954 -6.138  1.00 16.30 ? 333 LEU A CD2  1 
ATOM   4923 H H    . LEU A 1 333 ? 23.729 -8.950  -3.420  1.00 15.76 ? 333 LEU A H    1 
ATOM   4924 H HA   . LEU A 1 333 ? 23.408 -8.810  -6.099  1.00 14.92 ? 333 LEU A HA   1 
ATOM   4925 H HB2  . LEU A 1 333 ? 24.365 -10.750 -5.315  1.00 16.69 ? 333 LEU A HB2  1 
ATOM   4926 H HB3  . LEU A 1 333 ? 23.120 -11.007 -4.362  1.00 16.69 ? 333 LEU A HB3  1 
ATOM   4927 H HG   . LEU A 1 333 ? 21.790 -11.445 -6.191  1.00 15.87 ? 333 LEU A HG   1 
ATOM   4928 H HD11 . LEU A 1 333 ? 22.702 -11.645 -8.348  1.00 17.82 ? 333 LEU A HD11 1 
ATOM   4929 H HD12 . LEU A 1 333 ? 22.603 -10.146 -7.833  1.00 17.82 ? 333 LEU A HD12 1 
ATOM   4930 H HD13 . LEU A 1 333 ? 24.000 -10.901 -7.816  1.00 17.82 ? 333 LEU A HD13 1 
ATOM   4931 H HD21 . LEU A 1 333 ? 22.741 -13.498 -6.801  1.00 19.57 ? 333 LEU A HD21 1 
ATOM   4932 H HD22 . LEU A 1 333 ? 24.154 -13.007 -6.267  1.00 19.57 ? 333 LEU A HD22 1 
ATOM   4933 H HD23 . LEU A 1 333 ? 22.963 -13.257 -5.246  1.00 19.57 ? 333 LEU A HD23 1 
ATOM   4934 N N    . ALA A 1 334 ? 21.060 -8.229  -6.263  1.00 12.90 ? 334 ALA A N    1 
ATOM   4935 C CA   . ALA A 1 334 ? 19.673 -7.771  -6.246  1.00 14.31 ? 334 ALA A CA   1 
ATOM   4936 C C    . ALA A 1 334 ? 18.699 -8.923  -6.031  1.00 15.21 ? 334 ALA A C    1 
ATOM   4937 O O    . ALA A 1 334 ? 17.716 -8.787  -5.281  1.00 16.27 ? 334 ALA A O    1 
ATOM   4938 C CB   . ALA A 1 334 ? 19.345 -7.008  -7.526  1.00 14.70 ? 334 ALA A CB   1 
ATOM   4939 H H    . ALA A 1 334 ? 21.499 -8.006  -6.967  1.00 15.48 ? 334 ALA A H    1 
ATOM   4940 H HA   . ALA A 1 334 ? 19.567 -7.156  -5.503  1.00 17.17 ? 334 ALA A HA   1 
ATOM   4941 H HB1  . ALA A 1 334 ? 18.389 -6.847  -7.560  1.00 17.63 ? 334 ALA A HB1  1 
ATOM   4942 H HB2  . ALA A 1 334 ? 19.823 -6.164  -7.522  1.00 17.63 ? 334 ALA A HB2  1 
ATOM   4943 H HB3  . ALA A 1 334 ? 19.618 -7.540  -8.289  1.00 17.63 ? 334 ALA A HB3  1 
ATOM   4944 N N    . THR A 1 335 ? 18.939 -10.049 -6.691  1.00 14.39 ? 335 THR A N    1 
ATOM   4945 C CA   . THR A 1 335 ? 18.007 -11.161 -6.722  1.00 16.11 ? 335 THR A CA   1 
ATOM   4946 C C    . THR A 1 335 ? 18.016 -11.987 -5.443  1.00 16.16 ? 335 THR A C    1 
ATOM   4947 O O    . THR A 1 335 ? 17.174 -12.880 -5.306  1.00 18.76 ? 335 THR A O    1 
ATOM   4948 C CB   . THR A 1 335 ? 18.289 -12.042 -7.941  1.00 15.17 ? 335 THR A CB   1 
ATOM   4949 O OG1  . THR A 1 335 ? 19.685 -12.329 -8.021  1.00 16.84 ? 335 THR A OG1  1 
ATOM   4950 C CG2  . THR A 1 335 ? 17.845 -11.358 -9.203  1.00 18.38 ? 335 THR A CG2  1 
ATOM   4951 H H    . THR A 1 335 ? 19.657 -10.197 -7.142  1.00 17.26 ? 335 THR A H    1 
ATOM   4952 H HA   . THR A 1 335 ? 17.106 -10.815 -6.821  1.00 19.33 ? 335 THR A HA   1 
ATOM   4953 H HB   . THR A 1 335 ? 17.797 -12.874 -7.856  1.00 18.21 ? 335 THR A HB   1 
ATOM   4954 H HG1  . THR A 1 335 ? 19.931 -12.750 -7.337  1.00 20.20 ? 335 THR A HG1  1 
ATOM   4955 H HG21 . THR A 1 335 ? 18.008 -11.933 -9.967  1.00 22.05 ? 335 THR A HG21 1 
ATOM   4956 H HG22 . THR A 1 335 ? 16.897 -11.158 -9.156  1.00 22.05 ? 335 THR A HG22 1 
ATOM   4957 H HG23 . THR A 1 335 ? 18.336 -10.530 -9.322  1.00 22.05 ? 335 THR A HG23 1 
ATOM   4958 N N    . ASN A 1 336 ? 18.918 -11.714 -4.514  1.00 14.79 ? 336 ASN A N    1 
ATOM   4959 C CA   . ASN A 1 336 ? 18.957 -12.413 -3.233  1.00 14.93 ? 336 ASN A CA   1 
ATOM   4960 C C    . ASN A 1 336 ? 18.694 -11.497 -2.058  1.00 16.46 ? 336 ASN A C    1 
ATOM   4961 O O    . ASN A 1 336 ? 18.955 -11.884 -0.911  1.00 16.94 ? 336 ASN A O    1 
ATOM   4962 C CB   . ASN A 1 336 ? 20.278 -13.144 -3.060  1.00 15.84 ? 336 ASN A CB   1 
ATOM   4963 C CG   . ASN A 1 336 ? 20.195 -14.256 -2.020  1.00 15.93 ? 336 ASN A CG   1 
ATOM   4964 O OD1  . ASN A 1 336 ? 19.137 -14.859 -1.838  1.00 18.47 ? 336 ASN A OD1  1 
ATOM   4965 N ND2  . ASN A 1 336 ? 21.318 -14.567 -1.398  1.00 18.67 ? 336 ASN A ND2  1 
ATOM   4966 H H    . ASN A 1 336 ? 19.532 -11.117 -4.600  1.00 17.75 ? 336 ASN A H    1 
ATOM   4967 H HA   . ASN A 1 336 ? 18.256 -13.084 -3.235  1.00 17.92 ? 336 ASN A HA   1 
ATOM   4968 H HB2  . ASN A 1 336 ? 20.534 -13.541 -3.907  1.00 19.01 ? 336 ASN A HB2  1 
ATOM   4969 H HB3  . ASN A 1 336 ? 20.955 -12.512 -2.772  1.00 19.01 ? 336 ASN A HB3  1 
ATOM   4970 H HD21 . ASN A 1 336 ? 21.322 -15.188 -0.803  1.00 22.41 ? 336 ASN A HD21 1 
ATOM   4971 H HD22 . ASN A 1 336 ? 22.045 -14.149 -1.587  1.00 22.41 ? 336 ASN A HD22 1 
ATOM   4972 N N    . SER A 1 337 ? 18.176 -10.293 -2.306  1.00 14.50 ? 337 SER A N    1 
ATOM   4973 C CA   . SER A 1 337 ? 18.010 -9.282  -1.279  1.00 14.74 ? 337 SER A CA   1 
ATOM   4974 C C    . SER A 1 337 ? 16.543 -9.089  -0.966  1.00 17.03 ? 337 SER A C    1 
ATOM   4975 O O    . SER A 1 337 ? 15.738 -8.818  -1.857  1.00 18.09 ? 337 SER A O    1 
ATOM   4976 C CB   . SER A 1 337 ? 18.537 -7.938  -1.761  1.00 14.78 ? 337 SER A CB   1 
ATOM   4977 O OG   . SER A 1 337 ? 18.068 -6.930  -0.861  1.00 15.14 ? 337 SER A OG   1 
ATOM   4978 H H    . SER A 1 337 ? 17.909 -10.039 -3.083  1.00 17.40 ? 337 SER A H    1 
ATOM   4979 H HA   . SER A 1 337 ? 18.483 -9.579  -0.485  1.00 17.68 ? 337 SER A HA   1 
ATOM   4980 H HB2  . SER A 1 337 ? 19.507 -7.949  -1.763  1.00 17.74 ? 337 SER A HB2  1 
ATOM   4981 H HB3  . SER A 1 337 ? 18.206 -7.759  -2.655  1.00 17.74 ? 337 SER A HB3  1 
ATOM   4982 H HG   . SER A 1 337 ? 18.387 -6.183  -1.075  1.00 18.17 ? 337 SER A HG   1 
ATOM   4983 N N    . ALA A 1 338 ? 16.205 -9.139  0.313   1.00 16.32 ? 338 ALA A N    1 
ATOM   4984 C CA   . ALA A 1 338 ? 14.832 -8.917  0.743   1.00 18.07 ? 338 ALA A CA   1 
ATOM   4985 C C    . ALA A 1 338 ? 14.402 -7.467  0.633   1.00 18.41 ? 338 ALA A C    1 
ATOM   4986 O O    . ALA A 1 338 ? 13.193 -7.207  0.701   1.00 24.24 ? 338 ALA A O    1 
ATOM   4987 C CB   . ALA A 1 338 ? 14.709 -9.370  2.191   1.00 21.42 ? 338 ALA A CB   1 
ATOM   4988 H H    . ALA A 1 338 ? 16.754 -9.300  0.955   1.00 19.58 ? 338 ALA A H    1 
ATOM   4989 H HA   . ALA A 1 338 ? 14.232 -9.438  0.187   1.00 21.68 ? 338 ALA A HA   1 
ATOM   4990 H HB1  . ALA A 1 338 ? 13.797 -9.227  2.490   1.00 25.70 ? 338 ALA A HB1  1 
ATOM   4991 H HB2  . ALA A 1 338 ? 14.933 -10.312 2.248   1.00 25.70 ? 338 ALA A HB2  1 
ATOM   4992 H HB3  . ALA A 1 338 ? 15.321 -8.851  2.737   1.00 25.70 ? 338 ALA A HB3  1 
ATOM   4993 N N    . VAL A 1 339 ? 15.318 -6.519  0.470   1.00 15.42 ? 339 VAL A N    1 
ATOM   4994 C CA   . VAL A 1 339 ? 14.980 -5.102  0.419   1.00 18.48 ? 339 VAL A CA   1 
ATOM   4995 C C    . VAL A 1 339 ? 15.148 -4.497  -0.963  1.00 17.38 ? 339 VAL A C    1 
ATOM   4996 O O    . VAL A 1 339 ? 14.812 -3.325  -1.164  1.00 18.71 ? 339 VAL A O    1 
ATOM   4997 C CB   . VAL A 1 339 ? 15.739 -4.306  1.493   1.00 18.40 ? 339 VAL A CB   1 
ATOM   4998 C CG1  . VAL A 1 339 ? 15.431 -4.916  2.866   1.00 19.72 ? 339 VAL A CG1  1 
ATOM   4999 C CG2  . VAL A 1 339 ? 17.237 -4.291  1.213   1.00 17.42 ? 339 VAL A CG2  1 
ATOM   5000 H H    . VAL A 1 339 ? 16.159 -6.675  0.384   1.00 18.50 ? 339 VAL A H    1 
ATOM   5001 H HA   . VAL A 1 339 ? 14.037 -5.011  0.624   1.00 22.17 ? 339 VAL A HA   1 
ATOM   5002 H HB   . VAL A 1 339 ? 15.448 -3.381  1.485   1.00 22.08 ? 339 VAL A HB   1 
ATOM   5003 H HG11 . VAL A 1 339 ? 15.818 -4.353  3.555   1.00 23.67 ? 339 VAL A HG11 1 
ATOM   5004 H HG12 . VAL A 1 339 ? 14.469 -4.965  2.982   1.00 23.67 ? 339 VAL A HG12 1 
ATOM   5005 H HG13 . VAL A 1 339 ? 15.816 -5.805  2.911   1.00 23.67 ? 339 VAL A HG13 1 
ATOM   5006 H HG21 . VAL A 1 339 ? 17.695 -3.882  1.964   1.00 20.90 ? 339 VAL A HG21 1 
ATOM   5007 H HG22 . VAL A 1 339 ? 17.546 -5.203  1.094   1.00 20.90 ? 339 VAL A HG22 1 
ATOM   5008 H HG23 . VAL A 1 339 ? 17.402 -3.779  0.406   1.00 20.90 ? 339 VAL A HG23 1 
ATOM   5009 N N    . TRP A 1 340 ? 15.613 -5.269  -1.941  1.00 18.41 ? 340 TRP A N    1 
ATOM   5010 C CA   . TRP A 1 340 ? 15.689 -4.779  -3.308  1.00 18.66 ? 340 TRP A CA   1 
ATOM   5011 C C    . TRP A 1 340 ? 14.310 -4.348  -3.760  1.00 17.42 ? 340 TRP A C    1 
ATOM   5012 O O    . TRP A 1 340 ? 13.314 -5.035  -3.529  1.00 19.73 ? 340 TRP A O    1 
ATOM   5013 C CB   . TRP A 1 340 ? 16.244 -5.893  -4.194  1.00 20.72 ? 340 TRP A CB   1 
ATOM   5014 C CG   . TRP A 1 340 ? 16.261 -5.597  -5.660  1.00 17.79 ? 340 TRP A CG   1 
ATOM   5015 C CD1  . TRP A 1 340 ? 15.554 -6.236  -6.612  1.00 20.34 ? 340 TRP A CD1  1 
ATOM   5016 C CD2  . TRP A 1 340 ? 17.064 -4.619  -6.325  1.00 16.40 ? 340 TRP A CD2  1 
ATOM   5017 N NE1  . TRP A 1 340 ? 15.837 -5.696  -7.842  1.00 18.72 ? 340 TRP A NE1  1 
ATOM   5018 C CE2  . TRP A 1 340 ? 16.771 -4.713  -7.692  1.00 17.35 ? 340 TRP A CE2  1 
ATOM   5019 C CE3  . TRP A 1 340 ? 17.987 -3.668  -5.900  1.00 17.23 ? 340 TRP A CE3  1 
ATOM   5020 C CZ2  . TRP A 1 340 ? 17.359 -3.884  -8.646  1.00 18.17 ? 340 TRP A CZ2  1 
ATOM   5021 C CZ3  . TRP A 1 340 ? 18.587 -2.858  -6.842  1.00 18.43 ? 340 TRP A CZ3  1 
ATOM   5022 C CH2  . TRP A 1 340 ? 18.264 -2.965  -8.204  1.00 17.82 ? 340 TRP A CH2  1 
ATOM   5023 H H    . TRP A 1 340 ? 15.889 -6.077  -1.839  1.00 22.09 ? 340 TRP A H    1 
ATOM   5024 H HA   . TRP A 1 340 ? 16.281 -4.014  -3.380  1.00 22.39 ? 340 TRP A HA   1 
ATOM   5025 H HB2  . TRP A 1 340 ? 17.159 -6.070  -3.924  1.00 24.86 ? 340 TRP A HB2  1 
ATOM   5026 H HB3  . TRP A 1 340 ? 15.700 -6.685  -4.065  1.00 24.86 ? 340 TRP A HB3  1 
ATOM   5027 H HD1  . TRP A 1 340 ? 14.964 -6.938  -6.459  1.00 24.40 ? 340 TRP A HD1  1 
ATOM   5028 H HE1  . TRP A 1 340 ? 15.483 -5.938  -8.588  1.00 22.47 ? 340 TRP A HE1  1 
ATOM   5029 H HE3  . TRP A 1 340 ? 18.195 -3.580  -4.998  1.00 20.68 ? 340 TRP A HE3  1 
ATOM   5030 H HZ2  . TRP A 1 340 ? 17.142 -3.954  -9.547  1.00 21.80 ? 340 TRP A HZ2  1 
ATOM   5031 H HZ3  . TRP A 1 340 ? 19.216 -2.230  -6.570  1.00 22.11 ? 340 TRP A HZ3  1 
ATOM   5032 H HH2  . TRP A 1 340 ? 18.676 -2.399  -8.817  1.00 21.38 ? 340 TRP A HH2  1 
ATOM   5033 N N    . LEU A 1 341 ? 14.248 -3.175  -4.387  1.00 19.76 ? 341 LEU A N    1 
ATOM   5034 C CA   . LEU A 1 341 ? 13.024 -2.527  -4.856  1.00 21.73 ? 341 LEU A CA   1 
ATOM   5035 C C    . LEU A 1 341 ? 12.141 -1.990  -3.739  1.00 24.93 ? 341 LEU A C    1 
ATOM   5036 O O    . LEU A 1 341 ? 11.058 -1.483  -4.047  1.00 31.48 ? 341 LEU A O    1 
ATOM   5037 C CB   . LEU A 1 341 ? 12.184 -3.421  -5.773  1.00 23.49 ? 341 LEU A CB   1 
ATOM   5038 C CG   . LEU A 1 341 ? 12.850 -3.685  -7.127  1.00 23.41 ? 341 LEU A CG   1 
ATOM   5039 C CD1  . LEU A 1 341 ? 12.220 -4.846  -7.869  1.00 25.87 ? 341 LEU A CD1  1 
ATOM   5040 C CD2  . LEU A 1 341 ? 12.754 -2.413  -7.954  1.00 30.28 ? 341 LEU A CD2  1 
ATOM   5041 H H    . LEU A 1 341 ? 14.948 -2.709  -4.563  1.00 23.71 ? 341 LEU A H    1 
ATOM   5042 H HA   . LEU A 1 341 ? 13.307 -1.759  -5.377  1.00 26.07 ? 341 LEU A HA   1 
ATOM   5043 H HB2  . LEU A 1 341 ? 12.044 -4.276  -5.336  1.00 28.19 ? 341 LEU A HB2  1 
ATOM   5044 H HB3  . LEU A 1 341 ? 11.331 -2.989  -5.938  1.00 28.19 ? 341 LEU A HB3  1 
ATOM   5045 H HG   . LEU A 1 341 ? 13.777 -3.932  -6.984  1.00 28.09 ? 341 LEU A HG   1 
ATOM   5046 H HD11 . LEU A 1 341 ? 12.667 -4.954  -8.724  1.00 31.05 ? 341 LEU A HD11 1 
ATOM   5047 H HD12 . LEU A 1 341 ? 12.321 -5.652  -7.339  1.00 31.05 ? 341 LEU A HD12 1 
ATOM   5048 H HD13 . LEU A 1 341 ? 11.279 -4.658  -8.010  1.00 31.05 ? 341 LEU A HD13 1 
ATOM   5049 H HD21 . LEU A 1 341 ? 13.060 -2.598  -8.856  1.00 36.34 ? 341 LEU A HD21 1 
ATOM   5050 H HD22 . LEU A 1 341 ? 11.830 -2.117  -7.973  1.00 36.34 ? 341 LEU A HD22 1 
ATOM   5051 H HD23 . LEU A 1 341 ? 13.311 -1.730  -7.550  1.00 36.34 ? 341 LEU A HD23 1 
ATOM   5052 N N    . HIS A 1 342 ? 12.552 -2.050  -2.482  1.00 22.20 ? 342 HIS A N    1 
ATOM   5053 C CA   . HIS A 1 342 ? 11.679 -1.677  -1.374  1.00 21.33 ? 342 HIS A CA   1 
ATOM   5054 C C    . HIS A 1 342 ? 12.084 -0.314  -0.826  1.00 21.75 ? 342 HIS A C    1 
ATOM   5055 O O    . HIS A 1 342 ? 13.278 -0.008  -0.692  1.00 33.59 ? 342 HIS A O    1 
ATOM   5056 C CB   . HIS A 1 342 ? 11.786 -2.707  -0.238  1.00 27.17 ? 342 HIS A CB   1 
ATOM   5057 C CG   . HIS A 1 342 ? 10.923 -2.413  0.958   1.00 31.70 ? 342 HIS A CG   1 
ATOM   5058 N ND1  . HIS A 1 342 ? 9.544  -2.452  0.902   1.00 34.89 ? 342 HIS A ND1  1 
ATOM   5059 C CD2  . HIS A 1 342 ? 11.237 -2.109  2.242   1.00 29.57 ? 342 HIS A CD2  1 
ATOM   5060 C CE1  . HIS A 1 342 ? 9.046  -2.167  2.095   1.00 32.36 ? 342 HIS A CE1  1 
ATOM   5061 N NE2  . HIS A 1 342 ? 10.053 -1.961  2.926   1.00 30.34 ? 342 HIS A NE2  1 
ATOM   5062 H H    . HIS A 1 342 ? 13.337 -2.305  -2.241  1.00 26.64 ? 342 HIS A H    1 
ATOM   5063 H HA   . HIS A 1 342 ? 10.763 -1.633  -1.689  1.00 25.60 ? 342 HIS A HA   1 
ATOM   5064 H HB2  . HIS A 1 342 ? 11.522 -3.575  -0.583  1.00 32.60 ? 342 HIS A HB2  1 
ATOM   5065 H HB3  . HIS A 1 342 ? 12.707 -2.737  0.066   1.00 32.60 ? 342 HIS A HB3  1 
ATOM   5066 H HD2  . HIS A 1 342 ? 12.093 -2.018  2.594   1.00 35.49 ? 342 HIS A HD2  1 
ATOM   5067 H HE1  . HIS A 1 342 ? 8.142  -2.120  2.311   1.00 38.84 ? 342 HIS A HE1  1 
ATOM   5068 H HE2  . HIS A 1 342 ? 9.979  -1.766  3.760   1.00 36.41 ? 342 HIS A HE2  1 
ATOM   5069 N N    . GLN A 1 343 ? 11.098 0.502   -0.477  1.00 20.09 ? 343 GLN A N    1 
ATOM   5070 C CA   . GLN A 1 343 ? 11.350 1.788   0.169   1.00 22.12 ? 343 GLN A CA   1 
ATOM   5071 C C    . GLN A 1 343 ? 10.757 1.735   1.571   1.00 22.75 ? 343 GLN A C    1 
ATOM   5072 O O    . GLN A 1 343 ? 9.538  1.617   1.734   1.00 25.83 ? 343 GLN A O    1 
ATOM   5073 C CB   . GLN A 1 343 ? 10.774 2.935   -0.660  1.00 29.53 ? 343 GLN A CB   1 
ATOM   5074 C CG   . GLN A 1 343 ? 10.877 4.287   0.020   1.00 34.96 ? 343 GLN A CG   1 
ATOM   5075 C CD   . GLN A 1 343 ? 11.453 5.360   -0.912  1.00 40.47 ? 343 GLN A CD   1 
ATOM   5076 O OE1  . GLN A 1 343 ? 12.653 5.684   -0.849  1.00 38.35 ? 343 GLN A OE1  1 
ATOM   5077 N NE2  . GLN A 1 343 ? 10.611 5.896   -1.789  1.00 41.57 ? 343 GLN A NE2  1 
ATOM   5078 H H    . GLN A 1 343 ? 10.265 0.332   -0.605  1.00 24.11 ? 343 GLN A H    1 
ATOM   5079 H HA   . GLN A 1 343 ? 12.302 1.947   0.256   1.00 26.55 ? 343 GLN A HA   1 
ATOM   5080 H HB2  . GLN A 1 343 ? 11.258 2.988   -1.499  1.00 35.44 ? 343 GLN A HB2  1 
ATOM   5081 H HB3  . GLN A 1 343 ? 9.836  2.759   -0.829  1.00 35.44 ? 343 GLN A HB3  1 
ATOM   5082 H HG2  . GLN A 1 343 ? 9.992  4.571   0.299   1.00 41.95 ? 343 GLN A HG2  1 
ATOM   5083 H HG3  . GLN A 1 343 ? 11.460 4.212   0.792   1.00 41.95 ? 343 GLN A HG3  1 
ATOM   5084 H HE21 . GLN A 1 343 ? 9.791  5.637   -1.811  1.00 49.88 ? 343 GLN A HE21 1 
ATOM   5085 H HE22 . GLN A 1 343 ? 10.885 6.502   -2.333  1.00 49.88 ? 343 GLN A HE22 1 
ATOM   5086 N N    . PHE A 1 344 ? 11.626 1.806   2.578   1.00 17.52 ? 344 PHE A N    1 
ATOM   5087 C CA   . PHE A 1 344 ? 11.175 1.880   3.966   1.00 17.42 ? 344 PHE A CA   1 
ATOM   5088 C C    . PHE A 1 344 ? 10.469 3.209   4.221   1.00 16.39 ? 344 PHE A C    1 
ATOM   5089 O O    . PHE A 1 344 ? 10.817 4.246   3.637   1.00 16.95 ? 344 PHE A O    1 
ATOM   5090 C CB   . PHE A 1 344 ? 12.355 1.748   4.933   1.00 17.21 ? 344 PHE A CB   1 
ATOM   5091 C CG   . PHE A 1 344 ? 12.910 0.350   4.996   1.00 19.72 ? 344 PHE A CG   1 
ATOM   5092 C CD1  . PHE A 1 344 ? 12.186 -0.656  5.590   1.00 18.41 ? 344 PHE A CD1  1 
ATOM   5093 C CD2  . PHE A 1 344 ? 14.146 0.052   4.462   1.00 24.59 ? 344 PHE A CD2  1 
ATOM   5094 C CE1  . PHE A 1 344 ? 12.668 -1.957  5.623   1.00 21.31 ? 344 PHE A CE1  1 
ATOM   5095 C CE2  . PHE A 1 344 ? 14.642 -1.254  4.514   1.00 22.69 ? 344 PHE A CE2  1 
ATOM   5096 C CZ   . PHE A 1 344 ? 13.891 -2.249  5.093   1.00 20.30 ? 344 PHE A CZ   1 
ATOM   5097 H H    . PHE A 1 344 ? 12.480 1.814   2.484   1.00 21.03 ? 344 PHE A H    1 
ATOM   5098 H HA   . PHE A 1 344 ? 10.559 1.150   4.138   1.00 20.91 ? 344 PHE A HA   1 
ATOM   5099 H HB2  . PHE A 1 344 ? 13.066 2.341   4.645   1.00 20.65 ? 344 PHE A HB2  1 
ATOM   5100 H HB3  . PHE A 1 344 ? 12.060 1.993   5.825   1.00 20.65 ? 344 PHE A HB3  1 
ATOM   5101 H HD1  . PHE A 1 344 ? 11.361 -0.463  5.975   1.00 22.10 ? 344 PHE A HD1  1 
ATOM   5102 H HD2  . PHE A 1 344 ? 14.652 0.724   4.065   1.00 29.51 ? 344 PHE A HD2  1 
ATOM   5103 H HE1  . PHE A 1 344 ? 12.157 -2.631  6.008   1.00 25.57 ? 344 PHE A HE1  1 
ATOM   5104 H HE2  . PHE A 1 344 ? 15.478 -1.449  4.157   1.00 27.23 ? 344 PHE A HE2  1 
ATOM   5105 H HZ   . PHE A 1 344 ? 14.216 -3.120  5.123   1.00 24.35 ? 344 PHE A HZ   1 
ATOM   5106 N N    . ASP A 1 345 ? 9.509  3.192   5.153   1.00 17.37 ? 345 ASP A N    1 
ATOM   5107 C CA   . ASP A 1 345 ? 8.801  4.419   5.507   1.00 20.17 ? 345 ASP A CA   1 
ATOM   5108 C C    . ASP A 1 345 ? 9.777  5.480   5.998   1.00 17.72 ? 345 ASP A C    1 
ATOM   5109 O O    . ASP A 1 345 ? 9.578  6.678   5.763   1.00 18.76 ? 345 ASP A O    1 
ATOM   5110 C CB   . ASP A 1 345 ? 7.737  4.156   6.579   1.00 21.95 ? 345 ASP A CB   1 
ATOM   5111 C CG   . ASP A 1 345 ? 6.564  3.328   6.060   1.00 31.54 ? 345 ASP A CG   1 
ATOM   5112 O OD1  . ASP A 1 345 ? 6.350  3.265   4.825   1.00 32.78 ? 345 ASP A OD1  1 
ATOM   5113 O OD2  . ASP A 1 345 ? 5.836  2.756   6.906   1.00 40.93 ? 345 ASP A OD2  1 
ATOM   5114 H H    . ASP A 1 345 ? 9.256  2.494   5.587   1.00 20.84 ? 345 ASP A H    1 
ATOM   5115 H HA   . ASP A 1 345 ? 8.340  4.745   4.718   1.00 24.20 ? 345 ASP A HA   1 
ATOM   5116 H HB2  . ASP A 1 345 ? 8.143  3.673   7.315   1.00 26.34 ? 345 ASP A HB2  1 
ATOM   5117 H HB3  . ASP A 1 345 ? 7.388  5.006   6.892   1.00 26.34 ? 345 ASP A HB3  1 
ATOM   5118 N N    . GLN A 1 346 ? 10.850 5.053   6.676   1.00 15.76 ? 346 GLN A N    1 
ATOM   5119 C CA   . GLN A 1 346 ? 11.869 5.950   7.192   1.00 16.58 ? 346 GLN A CA   1 
ATOM   5120 C C    . GLN A 1 346 ? 12.598 6.706   6.096   1.00 15.88 ? 346 GLN A C    1 
ATOM   5121 O O    . GLN A 1 346 ? 13.301 7.694   6.393   1.00 20.15 ? 346 GLN A O    1 
ATOM   5122 C CB   . GLN A 1 346 ? 12.911 5.150   7.985   1.00 15.29 ? 346 GLN A CB   1 
ATOM   5123 C CG   . GLN A 1 346 ? 12.394 4.503   9.280   1.00 15.60 ? 346 GLN A CG   1 
ATOM   5124 C CD   . GLN A 1 346 ? 11.818 3.109   9.092   1.00 16.04 ? 346 GLN A CD   1 
ATOM   5125 O OE1  . GLN A 1 346 ? 11.333 2.737   8.019   1.00 17.89 ? 346 GLN A OE1  1 
ATOM   5126 N NE2  . GLN A 1 346 ? 11.816 2.330   10.177  1.00 18.62 ? 346 GLN A NE2  1 
ATOM   5127 H H    . GLN A 1 346 ? 11.008 4.226   6.852   1.00 18.91 ? 346 GLN A H    1 
ATOM   5128 H HA   . GLN A 1 346 ? 11.432 6.591   7.774   1.00 19.90 ? 346 GLN A HA   1 
ATOM   5129 H HB2  . GLN A 1 346 ? 13.246 4.438   7.419   1.00 18.35 ? 346 GLN A HB2  1 
ATOM   5130 H HB3  . GLN A 1 346 ? 13.635 5.748   8.229   1.00 18.35 ? 346 GLN A HB3  1 
ATOM   5131 H HG2  . GLN A 1 346 ? 13.129 4.435   9.909   1.00 18.72 ? 346 GLN A HG2  1 
ATOM   5132 H HG3  . GLN A 1 346 ? 11.693 5.063   9.649   1.00 18.72 ? 346 GLN A HG3  1 
ATOM   5133 H HE21 . GLN A 1 346 ? 12.129 2.628   10.920  1.00 22.35 ? 346 GLN A HE21 1 
ATOM   5134 H HE22 . GLN A 1 346 ? 11.503 1.531   10.131  1.00 22.35 ? 346 GLN A HE22 1 
ATOM   5135 N N    . TYR A 1 347 ? 12.506 6.251   4.844   1.00 14.79 ? 347 TYR A N    1 
ATOM   5136 C CA   . TYR A 1 347 ? 13.119 6.944   3.726   1.00 15.44 ? 347 TYR A CA   1 
ATOM   5137 C C    . TYR A 1 347 ? 12.203 8.004   3.134   1.00 17.22 ? 347 TYR A C    1 
ATOM   5138 O O    . TYR A 1 347 ? 12.680 8.849   2.357   1.00 19.06 ? 347 TYR A O    1 
ATOM   5139 C CB   . TYR A 1 347 ? 13.452 5.943   2.615   1.00 15.83 ? 347 TYR A CB   1 
ATOM   5140 C CG   . TYR A 1 347 ? 14.437 4.862   2.962   1.00 15.37 ? 347 TYR A CG   1 
ATOM   5141 C CD1  . TYR A 1 347 ? 15.165 4.863   4.153   1.00 15.75 ? 347 TYR A CD1  1 
ATOM   5142 C CD2  . TYR A 1 347 ? 14.675 3.847   2.058   1.00 15.41 ? 347 TYR A CD2  1 
ATOM   5143 C CE1  . TYR A 1 347 ? 16.083 3.865   4.402   1.00 15.21 ? 347 TYR A CE1  1 
ATOM   5144 C CE2  . TYR A 1 347 ? 15.563 2.861   2.304   1.00 17.10 ? 347 TYR A CE2  1 
ATOM   5145 C CZ   . TYR A 1 347 ? 16.263 2.862   3.474   1.00 17.15 ? 347 TYR A CZ   1 
ATOM   5146 O OH   . TYR A 1 347 ? 17.176 1.877   3.751   1.00 19.38 ? 347 TYR A OH   1 
ATOM   5147 H H    . TYR A 1 347 ? 12.088 5.534   4.621   1.00 17.74 ? 347 TYR A H    1 
ATOM   5148 H HA   . TYR A 1 347 ? 13.939 7.362   4.030   1.00 18.53 ? 347 TYR A HA   1 
ATOM   5149 H HB2  . TYR A 1 347 ? 12.630 5.504   2.348   1.00 18.99 ? 347 TYR A HB2  1 
ATOM   5150 H HB3  . TYR A 1 347 ? 13.823 6.437   1.867   1.00 18.99 ? 347 TYR A HB3  1 
ATOM   5151 H HD1  . TYR A 1 347 ? 15.030 5.537   4.779   1.00 18.90 ? 347 TYR A HD1  1 
ATOM   5152 H HD2  . TYR A 1 347 ? 14.209 3.842   1.253   1.00 18.49 ? 347 TYR A HD2  1 
ATOM   5153 H HE1  . TYR A 1 347 ? 16.577 3.869   5.190   1.00 18.25 ? 347 TYR A HE1  1 
ATOM   5154 H HE2  . TYR A 1 347 ? 15.696 2.184   1.680   1.00 20.52 ? 347 TYR A HE2  1 
ATOM   5155 H HH   . TYR A 1 347 ? 17.228 1.343   3.104   1.00 23.26 ? 347 TYR A HH   1 
ATOM   5156 N N    . LYS A 1 348 ? 10.926 7.988   3.485   1.00 16.76 ? 348 LYS A N    1 
ATOM   5157 C CA   . LYS A 1 348 ? 9.953  8.903   2.911   1.00 18.04 ? 348 LYS A CA   1 
ATOM   5158 C C    . LYS A 1 348 ? 9.622  10.065  3.830   1.00 20.16 ? 348 LYS A C    1 
ATOM   5159 O O    . LYS A 1 348 ? 9.144  11.099  3.355   1.00 22.79 ? 348 LYS A O    1 
ATOM   5160 C CB   . LYS A 1 348 ? 8.641  8.170   2.616   1.00 22.03 ? 348 LYS A CB   1 
ATOM   5161 C CG   . LYS A 1 348 ? 8.716  7.034   1.622   1.00 27.65 ? 348 LYS A CG   1 
ATOM   5162 C CD   . LYS A 1 348 ? 7.423  6.225   1.695   1.00 32.59 ? 348 LYS A CD   1 
ATOM   5163 C CE   . LYS A 1 348 ? 7.611  4.799   1.232   1.00 36.96 ? 348 LYS A CE   1 
ATOM   5164 N NZ   . LYS A 1 348 ? 6.336  4.034   1.236   1.00 41.62 ? 348 LYS A NZ   1 
ATOM   5165 H H    . LYS A 1 348 ? 10.592 7.447   4.064   1.00 20.11 ? 348 LYS A H    1 
ATOM   5166 H HA   . LYS A 1 348 ? 10.314 9.247   2.079   1.00 21.65 ? 348 LYS A HA   1 
ATOM   5167 H HB2  . LYS A 1 348 ? 8.309  7.799   3.448   1.00 26.44 ? 348 LYS A HB2  1 
ATOM   5168 H HB3  . LYS A 1 348 ? 8.008  8.815   2.264   1.00 26.44 ? 348 LYS A HB3  1 
ATOM   5169 H HG2  . LYS A 1 348 ? 8.817  7.386   0.724   1.00 33.18 ? 348 LYS A HG2  1 
ATOM   5170 H HG3  . LYS A 1 348 ? 9.463  6.455   1.838   1.00 33.18 ? 348 LYS A HG3  1 
ATOM   5171 H HD2  . LYS A 1 348 ? 7.111  6.205   2.613   1.00 39.11 ? 348 LYS A HD2  1 
ATOM   5172 H HD3  . LYS A 1 348 ? 6.755  6.640   1.126   1.00 39.11 ? 348 LYS A HD3  1 
ATOM   5173 H HE2  . LYS A 1 348 ? 7.959  4.801   0.327   1.00 44.35 ? 348 LYS A HE2  1 
ATOM   5174 H HE3  . LYS A 1 348 ? 8.233  4.351   1.826   1.00 44.35 ? 348 LYS A HE3  1 
ATOM   5175 H HZ1  . LYS A 1 348 ? 6.480  3.201   0.957   1.00 49.95 ? 348 LYS A HZ1  1 
ATOM   5176 H HZ2  . LYS A 1 348 ? 5.999  4.008   2.060   1.00 49.95 ? 348 LYS A HZ2  1 
ATOM   5177 H HZ3  . LYS A 1 348 ? 5.746  4.423   0.695   1.00 49.95 ? 348 LYS A HZ3  1 
ATOM   5178 N N    . LYS A 1 349 ? 9.874  9.930   5.124   1.00 17.88 ? 349 LYS A N    1 
ATOM   5179 C CA   . LYS A 1 349 ? 9.498  10.934  6.090   1.00 18.77 ? 349 LYS A CA   1 
ATOM   5180 C C    . LYS A 1 349 ? 10.451 12.125  6.005   1.00 17.68 ? 349 LYS A C    1 
ATOM   5181 O O    . LYS A 1 349 ? 11.631 11.982  5.686   1.00 17.80 ? 349 LYS A O    1 
ATOM   5182 C CB   . LYS A 1 349 ? 9.564  10.327  7.486   1.00 19.29 ? 349 LYS A CB   1 
ATOM   5183 C CG   . LYS A 1 349 ? 8.297  9.588   7.840   1.00 22.16 ? 349 LYS A CG   1 
ATOM   5184 C CD   . LYS A 1 349 ? 8.438  8.607   9.011   1.00 20.87 ? 349 LYS A CD   1 
ATOM   5185 C CE   . LYS A 1 349 ? 7.176  7.769   9.158   1.00 22.44 ? 349 LYS A CE   1 
ATOM   5186 N NZ   . LYS A 1 349 ? 7.158  7.070   10.486  1.00 26.90 ? 349 LYS A NZ   1 
ATOM   5187 H H    . LYS A 1 349 ? 10.269 9.249   5.471   1.00 21.46 ? 349 LYS A H    1 
ATOM   5188 H HA   . LYS A 1 349 ? 8.597  11.251  5.920   1.00 22.53 ? 349 LYS A HA   1 
ATOM   5189 H HB2  . LYS A 1 349 ? 10.302 9.700   7.526   1.00 23.15 ? 349 LYS A HB2  1 
ATOM   5190 H HB3  . LYS A 1 349 ? 9.694  11.035  8.136   1.00 23.15 ? 349 LYS A HB3  1 
ATOM   5191 H HG2  . LYS A 1 349 ? 7.617  10.237  8.082   1.00 26.59 ? 349 LYS A HG2  1 
ATOM   5192 H HG3  . LYS A 1 349 ? 8.009  9.079   7.066   1.00 26.59 ? 349 LYS A HG3  1 
ATOM   5193 H HD2  . LYS A 1 349 ? 9.187  8.013   8.850   1.00 25.04 ? 349 LYS A HD2  1 
ATOM   5194 H HD3  . LYS A 1 349 ? 8.578  9.102   9.834   1.00 25.04 ? 349 LYS A HD3  1 
ATOM   5195 H HE2  . LYS A 1 349 ? 6.396  8.343   9.100   1.00 26.93 ? 349 LYS A HE2  1 
ATOM   5196 H HE3  . LYS A 1 349 ? 7.148  7.099   8.456   1.00 26.93 ? 349 LYS A HE3  1 
ATOM   5197 H HZ1  . LYS A 1 349 ? 6.410  6.595   10.570  1.00 32.28 ? 349 LYS A HZ1  1 
ATOM   5198 H HZ2  . LYS A 1 349 ? 7.857  6.522   10.551  1.00 32.28 ? 349 LYS A HZ2  1 
ATOM   5199 H HZ3  . LYS A 1 349 ? 7.198  7.667   11.144  1.00 32.28 ? 349 LYS A HZ3  1 
ATOM   5200 N N    . ALA A 1 350 ? 9.940  13.308  6.313   1.00 18.91 ? 350 ALA A N    1 
ATOM   5201 C CA   . ALA A 1 350 ? 10.768 14.505  6.289   1.00 18.36 ? 350 ALA A CA   1 
ATOM   5202 C C    . ALA A 1 350 ? 11.909 14.415  7.299   1.00 18.67 ? 350 ALA A C    1 
ATOM   5203 O O    . ALA A 1 350 ? 11.707 14.091  8.479   1.00 18.92 ? 350 ALA A O    1 
ATOM   5204 C CB   . ALA A 1 350 ? 9.921  15.734  6.587   1.00 21.04 ? 350 ALA A CB   1 
ATOM   5205 H H    . ALA A 1 350 ? 9.121  13.445  6.537   1.00 22.70 ? 350 ALA A H    1 
ATOM   5206 H HA   . ALA A 1 350 ? 11.154 14.593  5.404   1.00 22.03 ? 350 ALA A HA   1 
ATOM   5207 H HB1  . ALA A 1 350 ? 10.487 16.521  6.566   1.00 25.25 ? 350 ALA A HB1  1 
ATOM   5208 H HB2  . ALA A 1 350 ? 9.226  15.809  5.914   1.00 25.25 ? 350 ALA A HB2  1 
ATOM   5209 H HB3  . ALA A 1 350 ? 9.521  15.636  7.465   1.00 25.25 ? 350 ALA A HB3  1 
ATOM   5210 N N    . LEU A 1 351 ? 13.115 14.746  6.844   1.00 16.25 ? 351 LEU A N    1 
ATOM   5211 C CA   . LEU A 1 351 ? 14.316 14.668  7.671   1.00 15.16 ? 351 LEU A CA   1 
ATOM   5212 C C    . LEU A 1 351 ? 14.764 16.083  8.021   1.00 15.81 ? 351 LEU A C    1 
ATOM   5213 O O    . LEU A 1 351 ? 14.663 16.485  9.185   1.00 17.28 ? 351 LEU A O    1 
ATOM   5214 C CB   . LEU A 1 351 ? 15.391 13.908  6.896   1.00 15.66 ? 351 LEU A CB   1 
ATOM   5215 C CG   . LEU A 1 351 ? 16.793 13.888  7.487   1.00 13.26 ? 351 LEU A CG   1 
ATOM   5216 C CD1  . LEU A 1 351 ? 16.781 13.275  8.877   1.00 15.83 ? 351 LEU A CD1  1 
ATOM   5217 C CD2  . LEU A 1 351 ? 17.738 13.126  6.608   1.00 15.31 ? 351 LEU A CD2  1 
ATOM   5218 H H    . LEU A 1 351 ? 13.266 15.025  6.045   1.00 19.50 ? 351 LEU A H    1 
ATOM   5219 H HA   . LEU A 1 351 ? 14.146 14.193  8.499   1.00 18.19 ? 351 LEU A HA   1 
ATOM   5220 H HB2  . LEU A 1 351 ? 15.105 12.984  6.819   1.00 18.79 ? 351 LEU A HB2  1 
ATOM   5221 H HB3  . LEU A 1 351 ? 15.462 14.308  6.016   1.00 18.79 ? 351 LEU A HB3  1 
ATOM   5222 H HG   . LEU A 1 351 ? 17.106 14.804  7.552   1.00 15.92 ? 351 LEU A HG   1 
ATOM   5223 H HD11 . LEU A 1 351 ? 17.692 13.224  9.207   1.00 19.00 ? 351 LEU A HD11 1 
ATOM   5224 H HD12 . LEU A 1 351 ? 16.248 13.833  9.464   1.00 19.00 ? 351 LEU A HD12 1 
ATOM   5225 H HD13 . LEU A 1 351 ? 16.397 12.386  8.827   1.00 19.00 ? 351 LEU A HD13 1 
ATOM   5226 H HD21 . LEU A 1 351 ? 18.627 13.163  6.995   1.00 18.37 ? 351 LEU A HD21 1 
ATOM   5227 H HD22 . LEU A 1 351 ? 17.441 12.205  6.549   1.00 18.37 ? 351 LEU A HD22 1 
ATOM   5228 H HD23 . LEU A 1 351 ? 17.744 13.530  5.726   1.00 18.37 ? 351 LEU A HD23 1 
ATOM   5229 N N    . GLY A 1 352 ? 15.194 16.874  7.039   1.00 15.83 ? 352 GLY A N    1 
ATOM   5230 C CA   . GLY A 1 352 ? 15.653 18.221  7.272   1.00 17.47 ? 352 GLY A CA   1 
ATOM   5231 C C    . GLY A 1 352 ? 17.114 18.283  7.667   1.00 14.08 ? 352 GLY A C    1 
ATOM   5232 O O    . GLY A 1 352 ? 17.758 17.286  7.990   1.00 15.41 ? 352 GLY A O    1 
ATOM   5233 H H    . GLY A 1 352 ? 15.227 16.639  6.213   1.00 18.99 ? 352 GLY A H    1 
ATOM   5234 H HA2  . GLY A 1 352 ? 15.535 18.743  6.463   1.00 20.96 ? 352 GLY A HA2  1 
ATOM   5235 H HA3  . GLY A 1 352 ? 15.128 18.619  7.984   1.00 20.96 ? 352 GLY A HA3  1 
ATOM   5236 N N    . ALA A 1 353 ? 17.632 19.508  7.684   1.00 16.60 ? 353 ALA A N    1 
ATOM   5237 C CA   . ALA A 1 353 ? 19.056 19.646  7.923   1.00 16.44 ? 353 ALA A CA   1 
ATOM   5238 C C    . ALA A 1 353 ? 19.388 19.417  9.394   1.00 15.29 ? 353 ALA A C    1 
ATOM   5239 O O    . ALA A 1 353 ? 18.557 19.677  10.275  1.00 16.52 ? 353 ALA A O    1 
ATOM   5240 C CB   . ALA A 1 353 ? 19.525 21.039  7.540   1.00 20.33 ? 353 ALA A CB   1 
ATOM   5241 H H    . ALA A 1 353 ? 17.196 20.240  7.565   1.00 19.92 ? 353 ALA A H    1 
ATOM   5242 H HA   . ALA A 1 353 ? 19.528 18.989  7.388   1.00 19.73 ? 353 ALA A HA   1 
ATOM   5243 H HB1  . ALA A 1 353 ? 20.475 21.113  7.721   1.00 24.39 ? 353 ALA A HB1  1 
ATOM   5244 H HB2  . ALA A 1 353 ? 19.356 21.180  6.595   1.00 24.39 ? 353 ALA A HB2  1 
ATOM   5245 H HB3  . ALA A 1 353 ? 19.037 21.692  8.065   1.00 24.39 ? 353 ALA A HB3  1 
ATOM   5246 N N    . PRO A 1 354 ? 20.608 18.978  9.682   1.00 15.18 ? 354 PRO A N    1 
ATOM   5247 C CA   . PRO A 1 354 ? 21.025 18.887  11.095  1.00 15.74 ? 354 PRO A CA   1 
ATOM   5248 C C    . PRO A 1 354 ? 21.033 20.264  11.737  1.00 18.13 ? 354 PRO A C    1 
ATOM   5249 O O    . PRO A 1 354 ? 21.427 21.268  11.130  1.00 20.01 ? 354 PRO A O    1 
ATOM   5250 C CB   . PRO A 1 354 ? 22.429 18.286  11.031  1.00 18.51 ? 354 PRO A CB   1 
ATOM   5251 C CG   . PRO A 1 354 ? 22.902 18.528  9.625   1.00 19.08 ? 354 PRO A CG   1 
ATOM   5252 C CD   . PRO A 1 354 ? 21.655 18.502  8.764   1.00 15.56 ? 354 PRO A CD   1 
ATOM   5253 H HA   . PRO A 1 354 ? 20.446 18.287  11.590  1.00 18.89 ? 354 PRO A HA   1 
ATOM   5254 H HB2  . PRO A 1 354 ? 23.007 18.730  11.671  1.00 22.22 ? 354 PRO A HB2  1 
ATOM   5255 H HB3  . PRO A 1 354 ? 22.389 17.336  11.223  1.00 22.22 ? 354 PRO A HB3  1 
ATOM   5256 H HG2  . PRO A 1 354 ? 23.340 19.392  9.571   1.00 22.89 ? 354 PRO A HG2  1 
ATOM   5257 H HG3  . PRO A 1 354 ? 23.518 17.827  9.361   1.00 22.89 ? 354 PRO A HG3  1 
ATOM   5258 H HD2  . PRO A 1 354 ? 21.746 19.098  8.004   1.00 18.68 ? 354 PRO A HD2  1 
ATOM   5259 H HD3  . PRO A 1 354 ? 21.464 17.601  8.458   1.00 18.68 ? 354 PRO A HD3  1 
ATOM   5260 N N    . LEU A 1 355 ? 20.601 20.324  12.990  1.00 15.88 ? 355 LEU A N    1 
ATOM   5261 C CA   . LEU A 1 355 ? 20.626 21.561  13.749  1.00 17.14 ? 355 LEU A CA   1 
ATOM   5262 C C    . LEU A 1 355 ? 21.896 21.698  14.576  1.00 18.75 ? 355 LEU A C    1 
ATOM   5263 O O    . LEU A 1 355 ? 22.102 22.752  15.190  1.00 24.27 ? 355 LEU A O    1 
ATOM   5264 C CB   . LEU A 1 355 ? 19.382 21.643  14.636  1.00 19.29 ? 355 LEU A CB   1 
ATOM   5265 C CG   . LEU A 1 355 ? 18.060 21.685  13.862  1.00 25.23 ? 355 LEU A CG   1 
ATOM   5266 C CD1  . LEU A 1 355 ? 16.867 21.734  14.794  1.00 27.78 ? 355 LEU A CD1  1 
ATOM   5267 C CD2  . LEU A 1 355 ? 18.027 22.856  12.910  1.00 29.10 ? 355 LEU A CD2  1 
ATOM   5268 H H    . LEU A 1 355 ? 20.286 19.653  13.426  1.00 19.06 ? 355 LEU A H    1 
ATOM   5269 H HA   . LEU A 1 355 ? 20.592 22.323  13.150  1.00 20.57 ? 355 LEU A HA   1 
ATOM   5270 H HB2  . LEU A 1 355 ? 19.361 20.863  15.213  1.00 23.15 ? 355 LEU A HB2  1 
ATOM   5271 H HB3  . LEU A 1 355 ? 19.437 22.450  15.171  1.00 23.15 ? 355 LEU A HB3  1 
ATOM   5272 H HG   . LEU A 1 355 ? 17.994 20.868  13.344  1.00 30.27 ? 355 LEU A HG   1 
ATOM   5273 H HD11 . LEU A 1 355 ? 16.054 21.760  14.266  1.00 33.34 ? 355 LEU A HD11 1 
ATOM   5274 H HD12 . LEU A 1 355 ? 16.872 20.943  15.356  1.00 33.34 ? 355 LEU A HD12 1 
ATOM   5275 H HD13 . LEU A 1 355 ? 16.929 22.531  15.345  1.00 33.34 ? 355 LEU A HD13 1 
ATOM   5276 H HD21 . LEU A 1 355 ? 17.118 22.984  12.597  1.00 34.92 ? 355 LEU A HD21 1 
ATOM   5277 H HD22 . LEU A 1 355 ? 18.331 23.651  13.376  1.00 34.92 ? 355 LEU A HD22 1 
ATOM   5278 H HD23 . LEU A 1 355 ? 18.612 22.669  12.159  1.00 34.92 ? 355 LEU A HD23 1 
ATOM   5279 N N    . GLY A 1 356 ? 22.734 20.677  14.609  1.00 19.50 ? 356 GLY A N    1 
ATOM   5280 C CA   . GLY A 1 356 ? 23.985 20.704  15.348  1.00 20.25 ? 356 GLY A CA   1 
ATOM   5281 C C    . GLY A 1 356 ? 24.624 19.342  15.245  1.00 20.07 ? 356 GLY A C    1 
ATOM   5282 O O    . GLY A 1 356 ? 24.036 18.397  14.715  1.00 19.59 ? 356 GLY A O    1 
ATOM   5283 H H    . GLY A 1 356 ? 22.599 19.933  14.200  1.00 23.40 ? 356 GLY A H    1 
ATOM   5284 H HA2  . GLY A 1 356 ? 24.583 21.370  14.975  1.00 24.31 ? 356 GLY A HA2  1 
ATOM   5285 H HA3  . GLY A 1 356 ? 23.821 20.914  16.281  1.00 24.31 ? 356 GLY A HA3  1 
ATOM   5286 N N    . LYS A 1 357 ? 25.862 19.258  15.715  1.00 17.37 ? 357 LYS A N    1 
ATOM   5287 C CA   . LYS A 1 357 ? 26.544 17.984  15.753  1.00 18.45 ? 357 LYS A CA   1 
ATOM   5288 C C    . LYS A 1 357 ? 25.876 17.061  16.768  1.00 15.00 ? 357 LYS A C    1 
ATOM   5289 O O    . LYS A 1 357 ? 25.150 17.493  17.678  1.00 17.77 ? 357 LYS A O    1 
ATOM   5290 C CB   . LYS A 1 357 ? 28.001 18.170  16.162  1.00 19.75 ? 357 LYS A CB   1 
ATOM   5291 C CG   . LYS A 1 357 ? 28.856 18.970  15.196  1.00 28.71 ? 357 LYS A CG   1 
ATOM   5292 C CD   . LYS A 1 357 ? 28.468 18.757  13.749  1.00 37.24 ? 357 LYS A CD   1 
ATOM   5293 C CE   . LYS A 1 357 ? 29.362 19.559  12.820  1.00 36.79 ? 357 LYS A CE   1 
ATOM   5294 N NZ   . LYS A 1 357 ? 28.650 19.779  11.536  1.00 37.34 ? 357 LYS A NZ   1 
ATOM   5295 H H    . LYS A 1 357 ? 26.321 19.921  16.014  1.00 20.84 ? 357 LYS A H    1 
ATOM   5296 H HA   . LYS A 1 357 ? 26.510 17.580  14.872  1.00 22.14 ? 357 LYS A HA   1 
ATOM   5297 H HB2  . LYS A 1 357 ? 28.022 18.631  17.015  1.00 23.70 ? 357 LYS A HB2  1 
ATOM   5298 H HB3  . LYS A 1 357 ? 28.407 17.293  16.248  1.00 23.70 ? 357 LYS A HB3  1 
ATOM   5299 H HG2  . LYS A 1 357 ? 28.759 19.914  15.396  1.00 34.45 ? 357 LYS A HG2  1 
ATOM   5300 H HG3  . LYS A 1 357 ? 29.783 18.703  15.300  1.00 34.45 ? 357 LYS A HG3  1 
ATOM   5301 H HD2  . LYS A 1 357 ? 28.557 17.817  13.526  1.00 44.68 ? 357 LYS A HD2  1 
ATOM   5302 H HD3  . LYS A 1 357 ? 27.551 19.044  13.615  1.00 44.68 ? 357 LYS A HD3  1 
ATOM   5303 H HE2  . LYS A 1 357 ? 29.567 20.419  13.219  1.00 44.14 ? 357 LYS A HE2  1 
ATOM   5304 H HE3  . LYS A 1 357 ? 30.182 19.070  12.646  1.00 44.14 ? 357 LYS A HE3  1 
ATOM   5305 H HZ1  . LYS A 1 357 ? 29.169 20.235  10.975  1.00 44.81 ? 357 LYS A HZ1  1 
ATOM   5306 H HZ2  . LYS A 1 357 ? 28.440 18.998  11.166  1.00 44.81 ? 357 LYS A HZ2  1 
ATOM   5307 H HZ3  . LYS A 1 357 ? 27.902 20.241  11.678  1.00 44.81 ? 357 LYS A HZ3  1 
ATOM   5308 N N    . ALA A 1 358 ? 26.165 15.788  16.630  1.00 15.56 ? 358 ALA A N    1 
ATOM   5309 C CA   . ALA A 1 358 ? 25.707 14.819  17.603  1.00 14.58 ? 358 ALA A CA   1 
ATOM   5310 C C    . ALA A 1 358 ? 26.305 15.104  18.968  1.00 15.77 ? 358 ALA A C    1 
ATOM   5311 O O    . ALA A 1 358 ? 27.399 15.667  19.095  1.00 16.75 ? 358 ALA A O    1 
ATOM   5312 C CB   . ALA A 1 358 ? 26.125 13.427  17.162  1.00 15.52 ? 358 ALA A CB   1 
ATOM   5313 H H    . ALA A 1 358 ? 26.625 15.456  15.983  1.00 18.67 ? 358 ALA A H    1 
ATOM   5314 H HA   . ALA A 1 358 ? 24.740 14.862  17.675  1.00 17.49 ? 358 ALA A HA   1 
ATOM   5315 H HB1  . ALA A 1 358 ? 25.795 12.780  17.805  1.00 18.62 ? 358 ALA A HB1  1 
ATOM   5316 H HB2  . ALA A 1 358 ? 25.746 13.246  16.288  1.00 18.62 ? 358 ALA A HB2  1 
ATOM   5317 H HB3  . ALA A 1 358 ? 27.093 13.387  17.119  1.00 18.62 ? 358 ALA A HB3  1 
ATOM   5318 N N    . ILE A 1 359 ? 25.557 14.727  20.002  1.00 12.36 ? 359 ILE A N    1 
ATOM   5319 C CA   . ILE A 1 359 ? 25.986 14.773  21.402  1.00 12.80 ? 359 ILE A CA   1 
ATOM   5320 C C    . ILE A 1 359 ? 26.245 13.344  21.853  1.00 13.59 ? 359 ILE A C    1 
ATOM   5321 O O    . ILE A 1 359 ? 25.360 12.480  21.775  1.00 14.71 ? 359 ILE A O    1 
ATOM   5322 C CB   . ILE A 1 359 ? 24.900 15.413  22.279  1.00 14.79 ? 359 ILE A CB   1 
ATOM   5323 C CG1  . ILE A 1 359 ? 24.484 16.790  21.763  1.00 17.99 ? 359 ILE A CG1  1 
ATOM   5324 C CG2  . ILE A 1 359 ? 25.375 15.444  23.745  1.00 16.11 ? 359 ILE A CG2  1 
ATOM   5325 C CD1  . ILE A 1 359 ? 25.558 17.796  21.706  1.00 24.29 ? 359 ILE A CD1  1 
ATOM   5326 H H    . ILE A 1 359 ? 24.756 14.424  19.915  1.00 14.83 ? 359 ILE A H    1 
ATOM   5327 H HA   . ILE A 1 359 ? 26.809 15.282  21.478  1.00 15.36 ? 359 ILE A HA   1 
ATOM   5328 H HB   . ILE A 1 359 ? 24.099 14.869  22.231  1.00 17.75 ? 359 ILE A HB   1 
ATOM   5329 H HG12 . ILE A 1 359 ? 24.138 16.686  20.863  1.00 21.59 ? 359 ILE A HG12 1 
ATOM   5330 H HG13 . ILE A 1 359 ? 23.793 17.138  22.346  1.00 21.59 ? 359 ILE A HG13 1 
ATOM   5331 H HG21 . ILE A 1 359 ? 24.760 15.983  24.266  1.00 19.33 ? 359 ILE A HG21 1 
ATOM   5332 H HG22 . ILE A 1 359 ? 25.393 14.537  24.090  1.00 19.33 ? 359 ILE A HG22 1 
ATOM   5333 H HG23 . ILE A 1 359 ? 26.265 15.829  23.781  1.00 19.33 ? 359 ILE A HG23 1 
ATOM   5334 H HD11 . ILE A 1 359 ? 25.180 18.647  21.434  1.00 29.15 ? 359 ILE A HD11 1 
ATOM   5335 H HD12 . ILE A 1 359 ? 25.961 17.878  22.585  1.00 29.15 ? 359 ILE A HD12 1 
ATOM   5336 H HD13 . ILE A 1 359 ? 26.225 17.510  21.062  1.00 29.15 ? 359 ILE A HD13 1 
ATOM   5337 N N    . LYS A 1 360 ? 27.449 13.090  22.350  1.00 13.48 ? 360 LYS A N    1 
ATOM   5338 C CA   . LYS A 1 360 ? 27.840 11.772  22.841  1.00 13.45 ? 360 LYS A CA   1 
ATOM   5339 C C    . LYS A 1 360 ? 27.763 11.747  24.359  1.00 13.82 ? 360 LYS A C    1 
ATOM   5340 O O    . LYS A 1 360 ? 28.400 12.567  25.029  1.00 14.49 ? 360 LYS A O    1 
ATOM   5341 C CB   . LYS A 1 360 ? 29.258 11.432  22.382  1.00 13.03 ? 360 LYS A CB   1 
ATOM   5342 C CG   . LYS A 1 360 ? 29.738 10.057  22.823  1.00 13.62 ? 360 LYS A CG   1 
ATOM   5343 C CD   . LYS A 1 360 ? 31.193 9.809   22.404  1.00 14.24 ? 360 LYS A CD   1 
ATOM   5344 C CE   . LYS A 1 360 ? 31.652 8.388   22.685  1.00 13.15 ? 360 LYS A CE   1 
ATOM   5345 N NZ   . LYS A 1 360 ? 31.706 8.046   24.133  1.00 13.09 ? 360 LYS A NZ   1 
ATOM   5346 H H    . LYS A 1 360 ? 28.072 13.678  22.416  1.00 16.18 ? 360 LYS A H    1 
ATOM   5347 H HA   . LYS A 1 360 ? 27.231 11.101  22.495  1.00 16.14 ? 360 LYS A HA   1 
ATOM   5348 H HB2  . LYS A 1 360 ? 29.285 11.458  21.413  1.00 15.64 ? 360 LYS A HB2  1 
ATOM   5349 H HB3  . LYS A 1 360 ? 29.869 12.090  22.749  1.00 15.64 ? 360 LYS A HB3  1 
ATOM   5350 H HG2  . LYS A 1 360 ? 29.683 9.992   23.789  1.00 16.35 ? 360 LYS A HG2  1 
ATOM   5351 H HG3  . LYS A 1 360 ? 29.182 9.376   22.413  1.00 16.35 ? 360 LYS A HG3  1 
ATOM   5352 H HD2  . LYS A 1 360 ? 31.280 9.968   21.451  1.00 17.09 ? 360 LYS A HD2  1 
ATOM   5353 H HD3  . LYS A 1 360 ? 31.771 10.413  22.895  1.00 17.09 ? 360 LYS A HD3  1 
ATOM   5354 H HE2  . LYS A 1 360 ? 31.036 7.771   22.259  1.00 15.78 ? 360 LYS A HE2  1 
ATOM   5355 H HE3  . LYS A 1 360 ? 32.544 8.270   22.321  1.00 15.78 ? 360 LYS A HE3  1 
ATOM   5356 H HZ1  . LYS A 1 360 ? 32.019 7.220   24.239  1.00 15.70 ? 360 LYS A HZ1  1 
ATOM   5357 H HZ2  . LYS A 1 360 ? 32.241 8.615   24.560  1.00 15.70 ? 360 LYS A HZ2  1 
ATOM   5358 H HZ3  . LYS A 1 360 ? 30.891 8.095   24.487  1.00 15.70 ? 360 LYS A HZ3  1 
ATOM   5359 N N    . ASN A 1 361 ? 27.026 10.776  24.883  1.00 12.84 ? 361 ASN A N    1 
ATOM   5360 C CA   . ASN A 1 361 ? 26.841 10.541  26.315  1.00 12.87 ? 361 ASN A CA   1 
ATOM   5361 C C    . ASN A 1 361 ? 27.190 9.078   26.561  1.00 11.26 ? 361 ASN A C    1 
ATOM   5362 O O    . ASN A 1 361 ? 26.317 8.217   26.607  1.00 12.17 ? 361 ASN A O    1 
ATOM   5363 C CB   . ASN A 1 361 ? 25.380 10.833  26.693  1.00 14.87 ? 361 ASN A CB   1 
ATOM   5364 C CG   . ASN A 1 361 ? 25.040 10.390  28.096  1.00 17.82 ? 361 ASN A CG   1 
ATOM   5365 O OD1  . ASN A 1 361 ? 25.907 10.295  28.939  1.00 19.02 ? 361 ASN A OD1  1 
ATOM   5366 N ND2  . ASN A 1 361 ? 23.765 10.086  28.320  1.00 19.56 ? 361 ASN A ND2  1 
ATOM   5367 H H    . ASN A 1 361 ? 26.597 10.206  24.403  1.00 15.40 ? 361 ASN A H    1 
ATOM   5368 H HA   . ASN A 1 361 ? 27.432 11.105  26.837  1.00 15.45 ? 361 ASN A HA   1 
ATOM   5369 H HB2  . ASN A 1 361 ? 25.223 11.788  26.633  1.00 17.84 ? 361 ASN A HB2  1 
ATOM   5370 H HB3  . ASN A 1 361 ? 24.794 10.362  26.080  1.00 17.84 ? 361 ASN A HB3  1 
ATOM   5371 H HD21 . ASN A 1 361 ? 23.516 9.828   29.101  1.00 23.47 ? 361 ASN A HD21 1 
ATOM   5372 H HD22 . ASN A 1 361 ? 23.190 10.148  27.683  1.00 23.47 ? 361 ASN A HD22 1 
ATOM   5373 N N    . GLY A 1 362 ? 28.475 8.801   26.729  1.00 12.83 ? 362 GLY A N    1 
ATOM   5374 C CA   . GLY A 1 362 ? 28.884 7.405   26.860  1.00 12.87 ? 362 GLY A CA   1 
ATOM   5375 C C    . GLY A 1 362 ? 28.641 6.649   25.572  1.00 12.33 ? 362 GLY A C    1 
ATOM   5376 O O    . GLY A 1 362 ? 29.179 7.036   24.535  1.00 12.71 ? 362 GLY A O    1 
ATOM   5377 H H    . GLY A 1 362 ? 29.110 9.380   26.769  1.00 15.40 ? 362 GLY A H    1 
ATOM   5378 H HA2  . GLY A 1 362 ? 29.829 7.360   27.075  1.00 15.45 ? 362 GLY A HA2  1 
ATOM   5379 H HA3  . GLY A 1 362 ? 28.378 6.982   27.571  1.00 15.45 ? 362 GLY A HA3  1 
ATOM   5380 N N    . TYR A 1 363 ? 27.828 5.610   25.629  1.00 11.80 ? 363 TYR A N    1 
ATOM   5381 C CA   . TYR A 1 363 ? 27.445 4.852   24.450  1.00 10.72 ? 363 TYR A CA   1 
ATOM   5382 C C    . TYR A 1 363 ? 26.139 5.355   23.847  1.00 11.92 ? 363 TYR A C    1 
ATOM   5383 O O    . TYR A 1 363 ? 25.668 4.758   22.865  1.00 12.11 ? 363 TYR A O    1 
ATOM   5384 C CB   . TYR A 1 363 ? 27.315 3.389   24.827  1.00 11.84 ? 363 TYR A CB   1 
ATOM   5385 C CG   . TYR A 1 363 ? 28.590 2.704   25.238  1.00 11.58 ? 363 TYR A CG   1 
ATOM   5386 C CD1  . TYR A 1 363 ? 29.754 2.801   24.484  1.00 13.11 ? 363 TYR A CD1  1 
ATOM   5387 C CD2  . TYR A 1 363 ? 28.636 1.934   26.386  1.00 13.00 ? 363 TYR A CD2  1 
ATOM   5388 C CE1  . TYR A 1 363 ? 30.911 2.144   24.843  1.00 13.33 ? 363 TYR A CE1  1 
ATOM   5389 C CE2  . TYR A 1 363 ? 29.782 1.269   26.738  1.00 13.09 ? 363 TYR A CE2  1 
ATOM   5390 C CZ   . TYR A 1 363 ? 30.939 1.381   25.968  1.00 12.35 ? 363 TYR A CZ   1 
ATOM   5391 O OH   . TYR A 1 363 ? 32.077 0.720   26.356  1.00 13.98 ? 363 TYR A OH   1 
ATOM   5392 H H    . TYR A 1 363 ? 27.475 5.316   26.356  1.00 14.16 ? 363 TYR A H    1 
ATOM   5393 H HA   . TYR A 1 363 ? 28.131 4.928   23.768  1.00 12.87 ? 363 TYR A HA   1 
ATOM   5394 H HB2  . TYR A 1 363 ? 26.699 3.321   25.573  1.00 14.20 ? 363 TYR A HB2  1 
ATOM   5395 H HB3  . TYR A 1 363 ? 26.964 2.908   24.061  1.00 14.20 ? 363 TYR A HB3  1 
ATOM   5396 H HD1  . TYR A 1 363 ? 29.752 3.324   23.715  1.00 15.73 ? 363 TYR A HD1  1 
ATOM   5397 H HD2  . TYR A 1 363 ? 27.881 1.867   26.925  1.00 15.60 ? 363 TYR A HD2  1 
ATOM   5398 H HE1  . TYR A 1 363 ? 31.673 2.222   24.316  1.00 15.99 ? 363 TYR A HE1  1 
ATOM   5399 H HE2  . TYR A 1 363 ? 29.788 0.736   27.500  1.00 15.71 ? 363 TYR A HE2  1 
ATOM   5400 H HH   . TYR A 1 363 ? 32.700 0.879   25.816  1.00 16.78 ? 363 TYR A HH   1 
ATOM   5401 N N    . ILE A 1 364 ? 25.544 6.403   24.395  1.00 11.64 ? 364 ILE A N    1 
ATOM   5402 C CA   . ILE A 1 364 ? 24.316 7.000   23.875  1.00 11.60 ? 364 ILE A CA   1 
ATOM   5403 C C    . ILE A 1 364 ? 24.691 8.235   23.079  1.00 13.09 ? 364 ILE A C    1 
ATOM   5404 O O    . ILE A 1 364 ? 25.573 9.012   23.475  1.00 15.87 ? 364 ILE A O    1 
ATOM   5405 C CB   . ILE A 1 364 ? 23.343 7.314   25.021  1.00 12.57 ? 364 ILE A CB   1 
ATOM   5406 C CG1  . ILE A 1 364 ? 22.863 6.000   25.650  1.00 14.68 ? 364 ILE A CG1  1 
ATOM   5407 C CG2  . ILE A 1 364 ? 22.184 8.165   24.506  1.00 14.91 ? 364 ILE A CG2  1 
ATOM   5408 C CD1  . ILE A 1 364 ? 22.152 6.145   26.977  1.00 15.52 ? 364 ILE A CD1  1 
ATOM   5409 H H    . ILE A 1 364 ? 25.841 6.804   25.096  1.00 13.97 ? 364 ILE A H    1 
ATOM   5410 H HA   . ILE A 1 364 ? 23.868 6.386   23.272  1.00 13.92 ? 364 ILE A HA   1 
ATOM   5411 H HB   . ILE A 1 364 ? 23.793 7.829   25.709  1.00 15.09 ? 364 ILE A HB   1 
ATOM   5412 H HG12 . ILE A 1 364 ? 22.247 5.573   25.035  1.00 17.61 ? 364 ILE A HG12 1 
ATOM   5413 H HG13 . ILE A 1 364 ? 23.635 5.430   25.795  1.00 17.61 ? 364 ILE A HG13 1 
ATOM   5414 H HG21 . ILE A 1 364 ? 21.487 8.190   25.180  1.00 17.90 ? 364 ILE A HG21 1 
ATOM   5415 H HG22 . ILE A 1 364 ? 22.506 9.063   24.329  1.00 17.90 ? 364 ILE A HG22 1 
ATOM   5416 H HG23 . ILE A 1 364 ? 21.840 7.770   23.690  1.00 17.90 ? 364 ILE A HG23 1 
ATOM   5417 H HD11 . ILE A 1 364 ? 21.963 5.262   27.332  1.00 18.62 ? 364 ILE A HD11 1 
ATOM   5418 H HD12 . ILE A 1 364 ? 22.724 6.632   27.590  1.00 18.62 ? 364 ILE A HD12 1 
ATOM   5419 H HD13 . ILE A 1 364 ? 21.324 6.630   26.840  1.00 18.62 ? 364 ILE A HD13 1 
ATOM   5420 N N    . TYR A 1 365 ? 24.056 8.406   21.924  1.00 11.69 ? 365 TYR A N    1 
ATOM   5421 C CA   . TYR A 1 365 ? 24.223 9.606   21.112  1.00 11.68 ? 365 TYR A CA   1 
ATOM   5422 C C    . TYR A 1 365 ? 22.851 10.183  20.779  1.00 11.61 ? 365 TYR A C    1 
ATOM   5423 O O    . TYR A 1 365 ? 21.887 9.438   20.561  1.00 12.60 ? 365 TYR A O    1 
ATOM   5424 C CB   . TYR A 1 365 ? 24.923 9.322   19.808  1.00 13.02 ? 365 TYR A CB   1 
ATOM   5425 C CG   . TYR A 1 365 ? 26.308 8.747   19.896  1.00 10.31 ? 365 TYR A CG   1 
ATOM   5426 C CD1  . TYR A 1 365 ? 26.511 7.423   20.280  1.00 11.86 ? 365 TYR A CD1  1 
ATOM   5427 C CD2  . TYR A 1 365 ? 27.415 9.497   19.556  1.00 12.42 ? 365 TYR A CD2  1 
ATOM   5428 C CE1  . TYR A 1 365 ? 27.780 6.883   20.323  1.00 12.43 ? 365 TYR A CE1  1 
ATOM   5429 C CE2  . TYR A 1 365 ? 28.702 8.948   19.563  1.00 11.89 ? 365 TYR A CE2  1 
ATOM   5430 C CZ   . TYR A 1 365 ? 28.866 7.634   19.941  1.00 10.79 ? 365 TYR A CZ   1 
ATOM   5431 O OH   . TYR A 1 365 ? 30.129 7.079   19.969  1.00 13.47 ? 365 TYR A OH   1 
ATOM   5432 H H    . TYR A 1 365 ? 23.515 7.830   21.584  1.00 14.03 ? 365 TYR A H    1 
ATOM   5433 H HA   . TYR A 1 365 ? 24.743 10.249  21.619  1.00 14.02 ? 365 TYR A HA   1 
ATOM   5434 H HB2  . TYR A 1 365 ? 24.384 8.688   19.310  1.00 15.63 ? 365 TYR A HB2  1 
ATOM   5435 H HB3  . TYR A 1 365 ? 24.993 10.156  19.318  1.00 15.63 ? 365 TYR A HB3  1 
ATOM   5436 H HD1  . TYR A 1 365 ? 25.780 6.895   20.510  1.00 14.23 ? 365 TYR A HD1  1 
ATOM   5437 H HD2  . TYR A 1 365 ? 27.303 10.389  19.317  1.00 14.90 ? 365 TYR A HD2  1 
ATOM   5438 H HE1  . TYR A 1 365 ? 27.902 6.007   20.613  1.00 14.92 ? 365 TYR A HE1  1 
ATOM   5439 H HE2  . TYR A 1 365 ? 29.436 9.463   19.317  1.00 14.27 ? 365 TYR A HE2  1 
ATOM   5440 H HH   . TYR A 1 365 ? 30.694 7.635   19.689  1.00 16.17 ? 365 TYR A HH   1 
ATOM   5441 N N    . THR A 1 366 ? 22.780 11.502  20.704  1.00 11.60 ? 366 THR A N    1 
ATOM   5442 C CA   . THR A 1 366 ? 21.578 12.171  20.210  1.00 12.17 ? 366 THR A CA   1 
ATOM   5443 C C    . THR A 1 366 ? 21.962 13.186  19.143  1.00 13.15 ? 366 THR A C    1 
ATOM   5444 O O    . THR A 1 366 ? 23.081 13.704  19.102  1.00 12.93 ? 366 THR A O    1 
ATOM   5445 C CB   . THR A 1 366 ? 20.811 12.891  21.316  1.00 14.57 ? 366 THR A CB   1 
ATOM   5446 O OG1  . THR A 1 366 ? 21.690 13.823  21.934  1.00 17.96 ? 366 THR A OG1  1 
ATOM   5447 C CG2  . THR A 1 366 ? 20.271 11.888  22.322  1.00 15.46 ? 366 THR A CG2  1 
ATOM   5448 H H    . THR A 1 366 ? 23.414 12.036  20.934  1.00 13.92 ? 366 THR A H    1 
ATOM   5449 H HA   . THR A 1 366 ? 20.996 11.498  19.823  1.00 14.60 ? 366 THR A HA   1 
ATOM   5450 H HB   . THR A 1 366 ? 20.046 13.369  20.958  1.00 17.48 ? 366 THR A HB   1 
ATOM   5451 H HG1  . THR A 1 366 ? 22.297 13.415  22.346  1.00 21.55 ? 366 THR A HG1  1 
ATOM   5452 H HG21 . THR A 1 366 ? 19.702 12.338  22.966  1.00 18.56 ? 366 THR A HG21 1 
ATOM   5453 H HG22 . THR A 1 366 ? 19.753 11.207  21.866  1.00 18.56 ? 366 THR A HG22 1 
ATOM   5454 H HG23 . THR A 1 366 ? 21.005 11.463  22.793  1.00 18.56 ? 366 THR A HG23 1 
ATOM   5455 N N    . ARG A 1 367 ? 20.998 13.484  18.271  1.00 12.44 ? 367 ARG A N    1 
ATOM   5456 C CA   . ARG A 1 367 ? 21.195 14.549  17.299  1.00 11.50 ? 367 ARG A CA   1 
ATOM   5457 C C    . ARG A 1 367 ? 19.844 15.070  16.858  1.00 12.94 ? 367 ARG A C    1 
ATOM   5458 O O    . ARG A 1 367 ? 18.909 14.286  16.680  1.00 14.74 ? 367 ARG A O    1 
ATOM   5459 C CB   . ARG A 1 367 ? 22.029 14.090  16.106  1.00 11.33 ? 367 ARG A CB   1 
ATOM   5460 C CG   . ARG A 1 367 ? 22.569 15.232  15.291  1.00 12.29 ? 367 ARG A CG   1 
ATOM   5461 C CD   . ARG A 1 367 ? 23.450 14.734  14.177  1.00 11.66 ? 367 ARG A CD   1 
ATOM   5462 N NE   . ARG A 1 367 ? 24.097 15.822  13.471  1.00 13.02 ? 367 ARG A NE   1 
ATOM   5463 C CZ   . ARG A 1 367 ? 24.815 15.690  12.368  1.00 13.45 ? 367 ARG A CZ   1 
ATOM   5464 N NH1  . ARG A 1 367 ? 24.984 14.509  11.801  1.00 12.91 ? 367 ARG A NH1  1 
ATOM   5465 N NH2  . ARG A 1 367 ? 25.397 16.762  11.841  1.00 14.75 ? 367 ARG A NH2  1 
ATOM   5466 H H    . ARG A 1 367 ? 20.236 13.089  18.226  1.00 14.93 ? 367 ARG A H    1 
ATOM   5467 H HA   . ARG A 1 367 ? 21.673 15.281  17.718  1.00 13.80 ? 367 ARG A HA   1 
ATOM   5468 H HB2  . ARG A 1 367 ? 22.782 13.571  16.430  1.00 13.60 ? 367 ARG A HB2  1 
ATOM   5469 H HB3  . ARG A 1 367 ? 21.475 13.545  15.526  1.00 13.60 ? 367 ARG A HB3  1 
ATOM   5470 H HG2  . ARG A 1 367 ? 21.832 15.727  14.901  1.00 14.74 ? 367 ARG A HG2  1 
ATOM   5471 H HG3  . ARG A 1 367 ? 23.096 15.815  15.860  1.00 14.74 ? 367 ARG A HG3  1 
ATOM   5472 H HD2  . ARG A 1 367 ? 24.139 14.160  14.546  1.00 14.00 ? 367 ARG A HD2  1 
ATOM   5473 H HD3  . ARG A 1 367 ? 22.910 14.238  13.541  1.00 14.00 ? 367 ARG A HD3  1 
ATOM   5474 H HE   . ARG A 1 367 ? 24.007 16.614  13.793  1.00 15.62 ? 367 ARG A HE   1 
ATOM   5475 H HH11 . ARG A 1 367 ? 24.623 13.810  12.148  1.00 15.50 ? 367 ARG A HH11 1 
ATOM   5476 H HH12 . ARG A 1 367 ? 25.454 14.440  11.084  1.00 15.50 ? 367 ARG A HH12 1 
ATOM   5477 H HH21 . ARG A 1 367 ? 25.304 17.530  12.217  1.00 17.70 ? 367 ARG A HH21 1 
ATOM   5478 H HH22 . ARG A 1 367 ? 25.866 16.688  11.124  1.00 17.70 ? 367 ARG A HH22 1 
ATOM   5479 N N    . LYS A 1 368 ? 19.774 16.377  16.655  1.00 13.53 ? 368 LYS A N    1 
ATOM   5480 C CA   . LYS A 1 368 ? 18.570 17.050  16.180  1.00 15.69 ? 368 LYS A CA   1 
ATOM   5481 C C    . LYS A 1 368 ? 18.714 17.457  14.719  1.00 15.62 ? 368 LYS A C    1 
ATOM   5482 O O    . LYS A 1 368 ? 19.739 18.035  14.317  1.00 15.97 ? 368 LYS A O    1 
ATOM   5483 C CB   . LYS A 1 368 ? 18.267 18.290  17.025  1.00 19.93 ? 368 LYS A CB   1 
ATOM   5484 C CG   . LYS A 1 368 ? 18.096 18.010  18.501  1.00 28.27 ? 368 LYS A CG   1 
ATOM   5485 C CD   . LYS A 1 368 ? 17.921 19.293  19.299  1.00 35.79 ? 368 LYS A CD   1 
ATOM   5486 C CE   . LYS A 1 368 ? 18.208 19.101  20.789  1.00 41.04 ? 368 LYS A CE   1 
ATOM   5487 N NZ   . LYS A 1 368 ? 19.570 19.404  21.144  1.00 41.12 ? 368 LYS A NZ   1 
ATOM   5488 H H    . LYS A 1 368 ? 20.432 16.915  16.789  1.00 16.24 ? 368 LYS A H    1 
ATOM   5489 H HA   . LYS A 1 368 ? 17.829 16.427  16.247  1.00 18.83 ? 368 LYS A HA   1 
ATOM   5490 H HB2  . LYS A 1 368 ? 19.000 18.918  16.928  1.00 23.92 ? 368 LYS A HB2  1 
ATOM   5491 H HB3  . LYS A 1 368 ? 17.443 18.690  16.705  1.00 23.92 ? 368 LYS A HB3  1 
ATOM   5492 H HG2  . LYS A 1 368 ? 17.308 17.460  18.634  1.00 33.92 ? 368 LYS A HG2  1 
ATOM   5493 H HG3  . LYS A 1 368 ? 18.882 17.550  18.833  1.00 33.92 ? 368 LYS A HG3  1 
ATOM   5494 H HD2  . LYS A 1 368 ? 18.534 19.964  18.960  1.00 42.94 ? 368 LYS A HD2  1 
ATOM   5495 H HD3  . LYS A 1 368 ? 17.007 19.603  19.207  1.00 42.94 ? 368 LYS A HD3  1 
ATOM   5496 H HE2  . LYS A 1 368 ? 17.629 19.688  21.300  1.00 49.25 ? 368 LYS A HE2  1 
ATOM   5497 H HE3  . LYS A 1 368 ? 18.036 18.177  21.027  1.00 49.25 ? 368 LYS A HE3  1 
ATOM   5498 H HZ1  . LYS A 1 368 ? 19.696 19.267  22.014  1.00 49.35 ? 368 LYS A HZ1  1 
ATOM   5499 H HZ2  . LYS A 1 368 ? 20.127 18.883  20.686  1.00 49.35 ? 368 LYS A HZ2  1 
ATOM   5500 H HZ3  . LYS A 1 368 ? 19.751 20.255  20.956  1.00 49.35 ? 368 LYS A HZ3  1 
ATOM   5501 N N    . PHE A 1 369 ? 17.685 17.144  13.940  1.00 14.61 ? 369 PHE A N    1 
ATOM   5502 C CA   . PHE A 1 369 ? 17.482 17.618  12.572  1.00 14.14 ? 369 PHE A CA   1 
ATOM   5503 C C    . PHE A 1 369 ? 16.205 18.441  12.545  1.00 16.25 ? 369 PHE A C    1 
ATOM   5504 O O    . PHE A 1 369 ? 15.397 18.401  13.480  1.00 17.34 ? 369 PHE A O    1 
ATOM   5505 C CB   . PHE A 1 369 ? 17.367 16.442  11.585  1.00 14.73 ? 369 PHE A CB   1 
ATOM   5506 C CG   . PHE A 1 369 ? 18.620 15.612  11.483  1.00 13.37 ? 369 PHE A CG   1 
ATOM   5507 C CD1  . PHE A 1 369 ? 18.981 14.716  12.465  1.00 13.65 ? 369 PHE A CD1  1 
ATOM   5508 C CD2  . PHE A 1 369 ? 19.468 15.761  10.385  1.00 14.45 ? 369 PHE A CD2  1 
ATOM   5509 C CE1  . PHE A 1 369 ? 20.151 13.974  12.351  1.00 12.58 ? 369 PHE A CE1  1 
ATOM   5510 C CE2  . PHE A 1 369 ? 20.643 15.017  10.287  1.00 14.79 ? 369 PHE A CE2  1 
ATOM   5511 C CZ   . PHE A 1 369 ? 20.984 14.140  11.267  1.00 14.02 ? 369 PHE A CZ   1 
ATOM   5512 H H    . PHE A 1 369 ? 17.050 16.624  14.196  1.00 17.54 ? 369 PHE A H    1 
ATOM   5513 H HA   . PHE A 1 369 ? 18.232 18.166  12.293  1.00 16.96 ? 369 PHE A HA   1 
ATOM   5514 H HB2  . PHE A 1 369 ? 16.648 15.859  11.877  1.00 17.67 ? 369 PHE A HB2  1 
ATOM   5515 H HB3  . PHE A 1 369 ? 17.171 16.793  10.702  1.00 17.67 ? 369 PHE A HB3  1 
ATOM   5516 H HD1  . PHE A 1 369 ? 18.436 14.606  13.211  1.00 16.38 ? 369 PHE A HD1  1 
ATOM   5517 H HD2  . PHE A 1 369 ? 19.247 16.364  9.712   1.00 17.34 ? 369 PHE A HD2  1 
ATOM   5518 H HE1  . PHE A 1 369 ? 20.374 13.361  13.014  1.00 15.09 ? 369 PHE A HE1  1 
ATOM   5519 H HE2  . PHE A 1 369 ? 21.196 15.121  9.547   1.00 17.75 ? 369 PHE A HE2  1 
ATOM   5520 H HZ   . PHE A 1 369 ? 21.775 13.655  11.206  1.00 16.83 ? 369 PHE A HZ   1 
ATOM   5521 N N    . GLU A 1 370 ? 15.984 19.193  11.469  1.00 15.97 ? 370 GLU A N    1 
ATOM   5522 C CA   . GLU A 1 370 ? 14.818 20.074  11.436  1.00 17.45 ? 370 GLU A CA   1 
ATOM   5523 C C    . GLU A 1 370 ? 13.536 19.319  11.751  1.00 17.59 ? 370 GLU A C    1 
ATOM   5524 O O    . GLU A 1 370 ? 12.640 19.852  12.423  1.00 20.38 ? 370 GLU A O    1 
ATOM   5525 C CB   . GLU A 1 370 ? 14.724 20.759  10.080  1.00 19.12 ? 370 GLU A CB   1 
ATOM   5526 C CG   . GLU A 1 370 ? 15.705 21.894  9.961   1.00 23.80 ? 370 GLU A CG   1 
ATOM   5527 C CD   . GLU A 1 370 ? 15.785 22.513  8.580   1.00 28.39 ? 370 GLU A CD   1 
ATOM   5528 O OE1  . GLU A 1 370 ? 15.735 21.790  7.555   1.00 25.83 ? 370 GLU A OE1  1 
ATOM   5529 O OE2  . GLU A 1 370 ? 15.885 23.755  8.518   1.00 38.39 ? 370 GLU A OE2  1 
ATOM   5530 H H    . GLU A 1 370 ? 16.479 19.212  10.766  1.00 19.16 ? 370 GLU A H    1 
ATOM   5531 H HA   . GLU A 1 370 ? 14.926 20.761  12.112  1.00 20.94 ? 370 GLU A HA   1 
ATOM   5532 H HB2  . GLU A 1 370 ? 14.918 20.114  9.381   1.00 22.94 ? 370 GLU A HB2  1 
ATOM   5533 H HB3  . GLU A 1 370 ? 13.830 21.116  9.963   1.00 22.94 ? 370 GLU A HB3  1 
ATOM   5534 H HG2  . GLU A 1 370 ? 15.446 22.593  10.581  1.00 28.56 ? 370 GLU A HG2  1 
ATOM   5535 H HG3  . GLU A 1 370 ? 16.589 21.563  10.184  1.00 28.56 ? 370 GLU A HG3  1 
ATOM   5536 N N    . ASN A 1 371 ? 13.409 18.097  11.248  1.00 16.70 ? 371 ASN A N    1 
ATOM   5537 C CA   . ASN A 1 371 ? 12.170 17.341  11.337  1.00 17.08 ? 371 ASN A CA   1 
ATOM   5538 C C    . ASN A 1 371 ? 12.333 16.001  12.036  1.00 16.87 ? 371 ASN A C    1 
ATOM   5539 O O    . ASN A 1 371 ? 11.430 15.164  11.961  1.00 17.90 ? 371 ASN A O    1 
ATOM   5540 C CB   . ASN A 1 371 ? 11.554 17.137  9.953   1.00 17.64 ? 371 ASN A CB   1 
ATOM   5541 C CG   . ASN A 1 371 ? 11.449 18.414  9.180   1.00 21.24 ? 371 ASN A CG   1 
ATOM   5542 O OD1  . ASN A 1 371 ? 11.982 18.555  8.070   1.00 26.82 ? 371 ASN A OD1  1 
ATOM   5543 N ND2  . ASN A 1 371 ? 10.778 19.380  9.772   1.00 22.75 ? 371 ASN A ND2  1 
ATOM   5544 H H    . ASN A 1 371 ? 14.041 17.677  10.843  1.00 20.04 ? 371 ASN A H    1 
ATOM   5545 H HA   . ASN A 1 371 ? 11.552 17.866  11.870  1.00 20.49 ? 371 ASN A HA   1 
ATOM   5546 H HB2  . ASN A 1 371 ? 12.109 16.524  9.446   1.00 21.16 ? 371 ASN A HB2  1 
ATOM   5547 H HB3  . ASN A 1 371 ? 10.662 16.771  10.053  1.00 21.16 ? 371 ASN A HB3  1 
ATOM   5548 H HD21 . ASN A 1 371 ? 10.681 20.139  9.379   1.00 27.30 ? 371 ASN A HD21 1 
ATOM   5549 H HD22 . ASN A 1 371 ? 10.436 19.252  10.551  1.00 27.30 ? 371 ASN A HD22 1 
ATOM   5550 N N    . LEU A 1 372 ? 13.429 15.789  12.754  1.00 14.91 ? 372 LEU A N    1 
ATOM   5551 C CA   . LEU A 1 372 ? 13.688 14.496  13.361  1.00 14.08 ? 372 LEU A CA   1 
ATOM   5552 C C    . LEU A 1 372 ? 14.636 14.652  14.531  1.00 15.82 ? 372 LEU A C    1 
ATOM   5553 O O    . LEU A 1 372 ? 15.630 15.379  14.439  1.00 16.59 ? 372 LEU A O    1 
ATOM   5554 C CB   . LEU A 1 372 ? 14.337 13.564  12.320  1.00 14.69 ? 372 LEU A CB   1 
ATOM   5555 C CG   . LEU A 1 372 ? 14.942 12.253  12.828  1.00 14.72 ? 372 LEU A CG   1 
ATOM   5556 C CD1  . LEU A 1 372 ? 13.848 11.325  13.314  1.00 16.76 ? 372 LEU A CD1  1 
ATOM   5557 C CD2  . LEU A 1 372 ? 15.802 11.547  11.787  1.00 15.46 ? 372 LEU A CD2  1 
ATOM   5558 H H    . LEU A 1 372 ? 14.037 16.379  12.903  1.00 17.89 ? 372 LEU A H    1 
ATOM   5559 H HA   . LEU A 1 372 ? 12.857 14.123  13.695  1.00 16.89 ? 372 LEU A HA   1 
ATOM   5560 H HB2  . LEU A 1 372 ? 13.658 13.327  11.669  1.00 17.63 ? 372 LEU A HB2  1 
ATOM   5561 H HB3  . LEU A 1 372 ? 15.054 14.055  11.888  1.00 17.63 ? 372 LEU A HB3  1 
ATOM   5562 H HG   . LEU A 1 372 ? 15.531 12.476  13.565  1.00 17.66 ? 372 LEU A HG   1 
ATOM   5563 H HD11 . LEU A 1 372 ? 14.254 10.530  13.693  1.00 20.11 ? 372 LEU A HD11 1 
ATOM   5564 H HD12 . LEU A 1 372 ? 13.323 11.782  13.990  1.00 20.11 ? 372 LEU A HD12 1 
ATOM   5565 H HD13 . LEU A 1 372 ? 13.282 11.083  12.565  1.00 20.11 ? 372 LEU A HD13 1 
ATOM   5566 H HD21 . LEU A 1 372 ? 16.131 10.715  12.162  1.00 18.55 ? 372 LEU A HD21 1 
ATOM   5567 H HD22 . LEU A 1 372 ? 15.262 11.365  11.002  1.00 18.55 ? 372 LEU A HD22 1 
ATOM   5568 H HD23 . LEU A 1 372 ? 16.547 12.121  11.550  1.00 18.55 ? 372 LEU A HD23 1 
ATOM   5569 N N    . ASP A 1 373 ? 14.348 13.924  15.617  1.00 15.24 ? 373 ASP A N    1 
ATOM   5570 C CA   . ASP A 1 373 ? 15.265 13.761  16.745  1.00 14.97 ? 373 ASP A CA   1 
ATOM   5571 C C    . ASP A 1 373 ? 15.732 12.314  16.780  1.00 15.41 ? 373 ASP A C    1 
ATOM   5572 O O    . ASP A 1 373 ? 14.912 11.388  16.732  1.00 15.88 ? 373 ASP A O    1 
ATOM   5573 C CB   . ASP A 1 373 ? 14.565 14.065  18.066  1.00 18.45 ? 373 ASP A CB   1 
ATOM   5574 C CG   . ASP A 1 373 ? 14.103 15.498  18.166  1.00 25.04 ? 373 ASP A CG   1 
ATOM   5575 O OD1  . ASP A 1 373 ? 14.817 16.407  17.691  1.00 30.54 ? 373 ASP A OD1  1 
ATOM   5576 O OD2  . ASP A 1 373 ? 13.018 15.714  18.755  1.00 37.19 ? 373 ASP A OD2  1 
ATOM   5577 H H    . ASP A 1 373 ? 13.605 13.504  15.724  1.00 18.29 ? 373 ASP A H    1 
ATOM   5578 H HA   . ASP A 1 373 ? 16.021 14.359  16.635  1.00 17.96 ? 373 ASP A HA   1 
ATOM   5579 H HB2  . ASP A 1 373 ? 13.786 13.493  18.150  1.00 22.14 ? 373 ASP A HB2  1 
ATOM   5580 H HB3  . ASP A 1 373 ? 15.180 13.897  18.796  1.00 22.14 ? 373 ASP A HB3  1 
ATOM   5581 N N    . VAL A 1 374 ? 17.042 12.119  16.856  1.00 13.14 ? 374 VAL A N    1 
ATOM   5582 C CA   . VAL A 1 374 ? 17.677 10.812  16.852  1.00 12.11 ? 374 VAL A CA   1 
ATOM   5583 C C    . VAL A 1 374 ? 18.178 10.519  18.258  1.00 12.80 ? 374 VAL A C    1 
ATOM   5584 O O    . VAL A 1 374 ? 18.847 11.359  18.868  1.00 13.05 ? 374 VAL A O    1 
ATOM   5585 C CB   . VAL A 1 374 ? 18.865 10.779  15.881  1.00 11.84 ? 374 VAL A CB   1 
ATOM   5586 C CG1  . VAL A 1 374 ? 19.562 9.460   15.906  1.00 14.49 ? 374 VAL A CG1  1 
ATOM   5587 C CG2  . VAL A 1 374 ? 18.416 11.101  14.469  1.00 14.50 ? 374 VAL A CG2  1 
ATOM   5588 H H    . VAL A 1 374 ? 17.611 12.762  16.914  1.00 15.76 ? 374 VAL A H    1 
ATOM   5589 H HA   . VAL A 1 374 ? 17.022 10.145  16.594  1.00 14.54 ? 374 VAL A HA   1 
ATOM   5590 H HB   . VAL A 1 374 ? 19.498 11.456  16.169  1.00 14.21 ? 374 VAL A HB   1 
ATOM   5591 H HG11 . VAL A 1 374 ? 20.212 9.432   15.187  1.00 17.38 ? 374 VAL A HG11 1 
ATOM   5592 H HG12 . VAL A 1 374 ? 20.008 9.354   16.760  1.00 17.38 ? 374 VAL A HG12 1 
ATOM   5593 H HG13 . VAL A 1 374 ? 18.907 8.754   15.786  1.00 17.38 ? 374 VAL A HG13 1 
ATOM   5594 H HG21 . VAL A 1 374 ? 19.176 11.027  13.871  1.00 17.40 ? 374 VAL A HG21 1 
ATOM   5595 H HG22 . VAL A 1 374 ? 17.726 10.472  14.206  1.00 17.40 ? 374 VAL A HG22 1 
ATOM   5596 H HG23 . VAL A 1 374 ? 18.064 12.005  14.448  1.00 17.40 ? 374 VAL A HG23 1 
ATOM   5597 N N    . TRP A 1 375 ? 17.895 9.315   18.744  1.00 12.88 ? 375 TRP A N    1 
ATOM   5598 C CA   . TRP A 1 375 ? 18.473 8.795   19.982  1.00 11.66 ? 375 TRP A CA   1 
ATOM   5599 C C    . TRP A 1 375 ? 19.015 7.414   19.673  1.00 12.06 ? 375 TRP A C    1 
ATOM   5600 O O    . TRP A 1 375 ? 18.312 6.590   19.069  1.00 13.28 ? 375 TRP A O    1 
ATOM   5601 C CB   . TRP A 1 375 ? 17.411 8.719   21.057  1.00 14.75 ? 375 TRP A CB   1 
ATOM   5602 C CG   . TRP A 1 375 ? 17.866 8.157   22.382  1.00 14.85 ? 375 TRP A CG   1 
ATOM   5603 C CD1  . TRP A 1 375 ? 18.372 8.853   23.443  1.00 18.85 ? 375 TRP A CD1  1 
ATOM   5604 C CD2  . TRP A 1 375 ? 17.848 6.781   22.775  1.00 13.92 ? 375 TRP A CD2  1 
ATOM   5605 N NE1  . TRP A 1 375 ? 18.662 7.989   24.483  1.00 16.81 ? 375 TRP A NE1  1 
ATOM   5606 C CE2  . TRP A 1 375 ? 18.352 6.713   24.096  1.00 15.03 ? 375 TRP A CE2  1 
ATOM   5607 C CE3  . TRP A 1 375 ? 17.442 5.599   22.141  1.00 17.21 ? 375 TRP A CE3  1 
ATOM   5608 C CZ2  . TRP A 1 375 ? 18.450 5.495   24.800  1.00 17.15 ? 375 TRP A CZ2  1 
ATOM   5609 C CZ3  . TRP A 1 375 ? 17.536 4.387   22.851  1.00 18.25 ? 375 TRP A CZ3  1 
ATOM   5610 C CH2  . TRP A 1 375 ? 18.040 4.354   24.159  1.00 19.38 ? 375 TRP A CH2  1 
ATOM   5611 H H    . TRP A 1 375 ? 17.355 8.764   18.365  1.00 15.46 ? 375 TRP A H    1 
ATOM   5612 H HA   . TRP A 1 375 ? 19.195 9.356   20.305  1.00 13.99 ? 375 TRP A HA   1 
ATOM   5613 H HB2  . TRP A 1 375 ? 17.079 9.615   21.222  1.00 17.70 ? 375 TRP A HB2  1 
ATOM   5614 H HB3  . TRP A 1 375 ? 16.691 8.153   20.735  1.00 17.70 ? 375 TRP A HB3  1 
ATOM   5615 H HD1  . TRP A 1 375 ? 18.502 9.774   23.463  1.00 22.62 ? 375 TRP A HD1  1 
ATOM   5616 H HE1  . TRP A 1 375 ? 18.984 8.216   25.247  1.00 20.17 ? 375 TRP A HE1  1 
ATOM   5617 H HE3  . TRP A 1 375 ? 17.117 5.615   21.270  1.00 20.66 ? 375 TRP A HE3  1 
ATOM   5618 H HZ2  . TRP A 1 375 ? 18.781 5.467   25.669  1.00 20.58 ? 375 TRP A HZ2  1 
ATOM   5619 H HZ3  . TRP A 1 375 ? 17.260 3.596   22.446  1.00 21.90 ? 375 TRP A HZ3  1 
ATOM   5620 H HH2  . TRP A 1 375 ? 18.097 3.539   24.603  1.00 23.26 ? 375 TRP A HH2  1 
ATOM   5621 N N    . LEU A 1 376 ? 20.258 7.155   20.058  1.00 11.80 ? 376 LEU A N    1 
ATOM   5622 C CA   . LEU A 1 376 ? 20.969 5.927   19.727  1.00 12.08 ? 376 LEU A CA   1 
ATOM   5623 C C    . LEU A 1 376 ? 21.650 5.408   20.985  1.00 12.03 ? 376 LEU A C    1 
ATOM   5624 O O    . LEU A 1 376 ? 22.317 6.183   21.673  1.00 12.34 ? 376 LEU A O    1 
ATOM   5625 C CB   . LEU A 1 376 ? 22.036 6.217   18.660  1.00 11.50 ? 376 LEU A CB   1 
ATOM   5626 C CG   . LEU A 1 376 ? 23.035 5.114   18.356  1.00 11.76 ? 376 LEU A CG   1 
ATOM   5627 C CD1  . LEU A 1 376 ? 22.357 3.886   17.736  1.00 11.33 ? 376 LEU A CD1  1 
ATOM   5628 C CD2  . LEU A 1 376 ? 24.119 5.657   17.421  1.00 12.13 ? 376 LEU A CD2  1 
ATOM   5629 H H    . LEU A 1 376 ? 20.729 7.697   20.531  1.00 14.16 ? 376 LEU A H    1 
ATOM   5630 H HA   . LEU A 1 376 ? 20.351 5.254   19.400  1.00 14.50 ? 376 LEU A HA   1 
ATOM   5631 H HB2  . LEU A 1 376 ? 21.578 6.419   17.829  1.00 13.80 ? 376 LEU A HB2  1 
ATOM   5632 H HB3  . LEU A 1 376 ? 22.547 6.987   18.953  1.00 13.80 ? 376 LEU A HB3  1 
ATOM   5633 H HG   . LEU A 1 376 ? 23.442 4.820   19.186  1.00 14.11 ? 376 LEU A HG   1 
ATOM   5634 H HD11 . LEU A 1 376 ? 23.035 3.227   17.519  1.00 13.60 ? 376 LEU A HD11 1 
ATOM   5635 H HD12 . LEU A 1 376 ? 21.729 3.516   18.375  1.00 13.60 ? 376 LEU A HD12 1 
ATOM   5636 H HD13 . LEU A 1 376 ? 21.889 4.157   16.931  1.00 13.60 ? 376 LEU A HD13 1 
ATOM   5637 H HD21 . LEU A 1 376 ? 24.741 4.944   17.211  1.00 14.56 ? 376 LEU A HD21 1 
ATOM   5638 H HD22 . LEU A 1 376 ? 23.701 5.983   16.608  1.00 14.56 ? 376 LEU A HD22 1 
ATOM   5639 H HD23 . LEU A 1 376 ? 24.586 6.382   17.866  1.00 14.56 ? 376 LEU A HD23 1 
ATOM   5640 N N    . ASN A 1 377 ? 21.514 4.120   21.266  1.00 11.42 ? 377 ASN A N    1 
ATOM   5641 C CA   . ASN A 1 377 ? 22.211 3.493   22.394  1.00 11.74 ? 377 ASN A CA   1 
ATOM   5642 C C    . ASN A 1 377 ? 22.990 2.293   21.846  1.00 11.23 ? 377 ASN A C    1 
ATOM   5643 O O    . ASN A 1 377 ? 22.413 1.249   21.543  1.00 12.64 ? 377 ASN A O    1 
ATOM   5644 C CB   . ASN A 1 377 ? 21.231 3.079   23.486  1.00 12.14 ? 377 ASN A CB   1 
ATOM   5645 C CG   . ASN A 1 377 ? 21.923 2.616   24.739  1.00 14.73 ? 377 ASN A CG   1 
ATOM   5646 O OD1  . ASN A 1 377 ? 23.081 2.238   24.742  1.00 14.34 ? 377 ASN A OD1  1 
ATOM   5647 N ND2  . ASN A 1 377 ? 21.199 2.653   25.846  1.00 14.91 ? 377 ASN A ND2  1 
ATOM   5648 H H    . ASN A 1 377 ? 21.019 3.579   20.816  1.00 13.70 ? 377 ASN A H    1 
ATOM   5649 H HA   . ASN A 1 377 ? 22.843 4.121   22.778  1.00 14.09 ? 377 ASN A HA   1 
ATOM   5650 H HB2  . ASN A 1 377 ? 20.672 3.838   23.714  1.00 14.57 ? 377 ASN A HB2  1 
ATOM   5651 H HB3  . ASN A 1 377 ? 20.682 2.349   23.159  1.00 14.57 ? 377 ASN A HB3  1 
ATOM   5652 H HD21 . ASN A 1 377 ? 21.542 2.400   26.593  1.00 17.89 ? 377 ASN A HD21 1 
ATOM   5653 H HD22 . ASN A 1 377 ? 20.385 2.930   25.819  1.00 17.89 ? 377 ASN A HD22 1 
ATOM   5654 N N    . LEU A 1 378 ? 24.302 2.441   21.734  1.00 11.66 ? 378 LEU A N    1 
ATOM   5655 C CA   . LEU A 1 378 ? 25.135 1.349   21.219  1.00 12.29 ? 378 LEU A CA   1 
ATOM   5656 C C    . LEU A 1 378 ? 25.188 0.177   22.177  1.00 12.09 ? 378 LEU A C    1 
ATOM   5657 O O    . LEU A 1 378 ? 25.433 -0.945  21.745  1.00 14.75 ? 378 LEU A O    1 
ATOM   5658 C CB   . LEU A 1 378 ? 26.547 1.842   20.947  1.00 12.04 ? 378 LEU A CB   1 
ATOM   5659 C CG   . LEU A 1 378 ? 26.708 2.945   19.915  1.00 11.99 ? 378 LEU A CG   1 
ATOM   5660 C CD1  . LEU A 1 378 ? 28.177 3.299   19.842  1.00 12.46 ? 378 LEU A CD1  1 
ATOM   5661 C CD2  . LEU A 1 378 ? 26.194 2.510   18.586  1.00 13.81 ? 378 LEU A CD2  1 
ATOM   5662 H H    . LEU A 1 378 ? 24.737 3.152   21.945  1.00 13.99 ? 378 LEU A H    1 
ATOM   5663 H HA   . LEU A 1 378 ? 24.747 1.047   20.383  1.00 14.75 ? 378 LEU A HA   1 
ATOM   5664 H HB2  . LEU A 1 378 ? 26.911 2.179   21.780  1.00 14.45 ? 378 LEU A HB2  1 
ATOM   5665 H HB3  . LEU A 1 378 ? 27.071 1.087   20.637  1.00 14.45 ? 378 LEU A HB3  1 
ATOM   5666 H HG   . LEU A 1 378 ? 26.194 3.728   20.165  1.00 14.39 ? 378 LEU A HG   1 
ATOM   5667 H HD11 . LEU A 1 378 ? 28.308 3.962   19.147  1.00 14.95 ? 378 LEU A HD11 1 
ATOM   5668 H HD12 . LEU A 1 378 ? 28.458 3.658   20.699  1.00 14.95 ? 378 LEU A HD12 1 
ATOM   5669 H HD13 . LEU A 1 378 ? 28.685 2.499   19.637  1.00 14.95 ? 378 LEU A HD13 1 
ATOM   5670 H HD21 . LEU A 1 378 ? 26.411 3.187   17.926  1.00 16.57 ? 378 LEU A HD21 1 
ATOM   5671 H HD22 . LEU A 1 378 ? 26.611 1.668   18.346  1.00 16.57 ? 378 LEU A HD22 1 
ATOM   5672 H HD23 . LEU A 1 378 ? 25.232 2.398   18.641  1.00 16.57 ? 378 LEU A HD23 1 
ATOM   5673 N N    . GLU A 1 379 ? 25.007 0.425   23.476  1.00 13.14 ? 379 GLU A N    1 
ATOM   5674 C CA   . GLU A 1 379 ? 25.175 -0.633  24.467  1.00 14.18 ? 379 GLU A CA   1 
ATOM   5675 C C    . GLU A 1 379 ? 24.025 -1.628  24.407  1.00 14.75 ? 379 GLU A C    1 
ATOM   5676 O O    . GLU A 1 379 ? 24.244 -2.838  24.510  1.00 19.04 ? 379 GLU A O    1 
ATOM   5677 C CB   . GLU A 1 379 ? 25.278 0.000   25.851  1.00 14.91 ? 379 GLU A CB   1 
ATOM   5678 C CG   . GLU A 1 379 ? 25.648 -0.931  26.968  1.00 17.01 ? 379 GLU A CG   1 
ATOM   5679 C CD   . GLU A 1 379 ? 26.026 -0.195  28.235  1.00 18.68 ? 379 GLU A CD   1 
ATOM   5680 O OE1  . GLU A 1 379 ? 25.488 0.910   28.494  1.00 18.53 ? 379 GLU A OE1  1 
ATOM   5681 O OE2  . GLU A 1 379 ? 26.794 -0.769  29.023  1.00 22.90 ? 379 GLU A OE2  1 
ATOM   5682 H H    . GLU A 1 379 ? 24.788 1.190   23.805  1.00 15.77 ? 379 GLU A H    1 
ATOM   5683 H HA   . GLU A 1 379 ? 25.994 -1.123  24.290  1.00 17.02 ? 379 GLU A HA   1 
ATOM   5684 H HB2  . GLU A 1 379 ? 25.955 0.694   25.819  1.00 17.90 ? 379 GLU A HB2  1 
ATOM   5685 H HB3  . GLU A 1 379 ? 24.417 0.387   26.073  1.00 17.90 ? 379 GLU A HB3  1 
ATOM   5686 H HG2  . GLU A 1 379 ? 24.891 -1.503  27.168  1.00 20.41 ? 379 GLU A HG2  1 
ATOM   5687 H HG3  . GLU A 1 379 ? 26.408 -1.468  26.695  1.00 20.41 ? 379 GLU A HG3  1 
ATOM   5688 N N    . THR A 1 380 ? 22.805 -1.147  24.234  1.00 15.17 ? 380 THR A N    1 
ATOM   5689 C CA   . THR A 1 380 ? 21.631 -1.994  24.068  1.00 16.50 ? 380 THR A CA   1 
ATOM   5690 C C    . THR A 1 380 ? 21.319 -2.306  22.603  1.00 16.00 ? 380 THR A C    1 
ATOM   5691 O O    . THR A 1 380 ? 20.414 -3.100  22.322  1.00 17.26 ? 380 THR A O    1 
ATOM   5692 C CB   . THR A 1 380 ? 20.418 -1.293  24.697  1.00 17.41 ? 380 THR A CB   1 
ATOM   5693 O OG1  . THR A 1 380 ? 20.273 0.010   24.115  1.00 17.24 ? 380 THR A OG1  1 
ATOM   5694 C CG2  . THR A 1 380 ? 20.580 -1.127  26.187  1.00 19.22 ? 380 THR A CG2  1 
ATOM   5695 H H    . THR A 1 380 ? 22.623 -0.307  24.208  1.00 18.21 ? 380 THR A H    1 
ATOM   5696 H HA   . THR A 1 380 ? 21.780 -2.838  24.522  1.00 19.79 ? 380 THR A HA   1 
ATOM   5697 H HB   . THR A 1 380 ? 19.630 -1.835  24.536  1.00 20.89 ? 380 THR A HB   1 
ATOM   5698 H HG1  . THR A 1 380 ? 20.120 -0.058  23.292  1.00 20.68 ? 380 THR A HG1  1 
ATOM   5699 H HG21 . THR A 1 380 ? 19.785 -0.717  26.564  1.00 23.07 ? 380 THR A HG21 1 
ATOM   5700 H HG22 . THR A 1 380 ? 20.715 -1.992  26.605  1.00 23.07 ? 380 THR A HG22 1 
ATOM   5701 H HG23 . THR A 1 380 ? 21.345 -0.562  26.377  1.00 23.07 ? 380 THR A HG23 1 
ATOM   5702 N N    . GLN A 1 381 ? 22.019 -1.671  21.668  1.00 14.09 ? 381 GLN A N    1 
ATOM   5703 C CA   . GLN A 1 381 ? 21.800 -1.819  20.230  1.00 13.87 ? 381 GLN A CA   1 
ATOM   5704 C C    . GLN A 1 381 ? 20.363 -1.458  19.853  1.00 15.36 ? 381 GLN A C    1 
ATOM   5705 O O    . GLN A 1 381 ? 19.687 -2.184  19.126  1.00 16.58 ? 381 GLN A O    1 
ATOM   5706 C CB   . GLN A 1 381 ? 22.209 -3.197  19.702  1.00 16.40 ? 381 GLN A CB   1 
ATOM   5707 C CG   . GLN A 1 381 ? 23.634 -3.577  20.109  1.00 17.59 ? 381 GLN A CG   1 
ATOM   5708 C CD   . GLN A 1 381 ? 24.050 -4.923  19.598  1.00 23.95 ? 381 GLN A CD   1 
ATOM   5709 O OE1  . GLN A 1 381 ? 23.223 -5.734  19.186  1.00 37.23 ? 381 GLN A OE1  1 
ATOM   5710 N NE2  . GLN A 1 381 ? 25.347 -5.204  19.681  1.00 36.60 ? 381 GLN A NE2  1 
ATOM   5711 H H    . GLN A 1 381 ? 22.657 -1.122  21.849  1.00 16.91 ? 381 GLN A H    1 
ATOM   5712 H HA   . GLN A 1 381 ? 22.383 -1.185  19.783  1.00 16.64 ? 381 GLN A HA   1 
ATOM   5713 H HB2  . GLN A 1 381 ? 21.604 -3.866  20.058  1.00 19.69 ? 381 GLN A HB2  1 
ATOM   5714 H HB3  . GLN A 1 381 ? 22.164 -3.191  18.733  1.00 19.69 ? 381 GLN A HB3  1 
ATOM   5715 H HG2  . GLN A 1 381 ? 24.250 -2.919  19.752  1.00 21.10 ? 381 GLN A HG2  1 
ATOM   5716 H HG3  . GLN A 1 381 ? 23.690 -3.595  21.077  1.00 21.10 ? 381 GLN A HG3  1 
ATOM   5717 H HE21 . GLN A 1 381 ? 25.891 -4.627  20.014  1.00 43.92 ? 381 GLN A HE21 1 
ATOM   5718 H HE22 . GLN A 1 381 ? 25.642 -5.962  19.403  1.00 43.92 ? 381 GLN A HE22 1 
ATOM   5719 N N    . THR A 1 382 ? 19.929 -0.298  20.336  1.00 14.28 ? 382 THR A N    1 
ATOM   5720 C CA   . THR A 1 382 ? 18.593 0.217   20.062  1.00 15.24 ? 382 THR A CA   1 
ATOM   5721 C C    . THR A 1 382 ? 18.673 1.690   19.696  1.00 13.03 ? 382 THR A C    1 
ATOM   5722 O O    . THR A 1 382 ? 19.655 2.378   19.986  1.00 12.56 ? 382 THR A O    1 
ATOM   5723 C CB   . THR A 1 382 ? 17.656 0.049   21.264  1.00 15.79 ? 382 THR A CB   1 
ATOM   5724 O OG1  . THR A 1 382 ? 18.211 0.722   22.396  1.00 17.08 ? 382 THR A OG1  1 
ATOM   5725 C CG2  . THR A 1 382 ? 17.445 -1.427  21.613  1.00 18.12 ? 382 THR A CG2  1 
ATOM   5726 H H    . THR A 1 382 ? 20.400 0.219   20.835  1.00 17.14 ? 382 THR A H    1 
ATOM   5727 H HA   . THR A 1 382 ? 18.221 -0.270  19.311  1.00 18.28 ? 382 THR A HA   1 
ATOM   5728 H HB   . THR A 1 382 ? 16.791 0.427   21.042  1.00 18.95 ? 382 THR A HB   1 
ATOM   5729 H HG1  . THR A 1 382 ? 17.696 0.647   23.056  1.00 20.50 ? 382 THR A HG1  1 
ATOM   5730 H HG21 . THR A 1 382 ? 16.838 -1.507  22.365  1.00 21.74 ? 382 THR A HG21 1 
ATOM   5731 H HG22 . THR A 1 382 ? 17.068 -1.897  20.853  1.00 21.74 ? 382 THR A HG22 1 
ATOM   5732 H HG23 . THR A 1 382 ? 18.292 -1.837  21.848  1.00 21.74 ? 382 THR A HG23 1 
ATOM   5733 N N    . ALA A 1 383 ? 17.603 2.178   19.075  1.00 13.80 ? 383 ALA A N    1 
ATOM   5734 C CA   . ALA A 1 383 ? 17.514 3.591   18.730  1.00 13.14 ? 383 ALA A CA   1 
ATOM   5735 C C    . ALA A 1 383 ? 16.055 3.988   18.640  1.00 15.05 ? 383 ALA A C    1 
ATOM   5736 O O    . ALA A 1 383 ? 15.166 3.141   18.473  1.00 17.91 ? 383 ALA A O    1 
ATOM   5737 C CB   . ALA A 1 383 ? 18.164 3.896   17.383  1.00 13.12 ? 383 ALA A CB   1 
ATOM   5738 H H    . ALA A 1 383 ? 16.919 1.712   18.844  1.00 16.56 ? 383 ALA A H    1 
ATOM   5739 H HA   . ALA A 1 383 ? 17.957 4.097   19.429  1.00 15.77 ? 383 ALA A HA   1 
ATOM   5740 H HB1  . ALA A 1 383 ? 18.088 4.846   17.204  1.00 15.74 ? 383 ALA A HB1  1 
ATOM   5741 H HB2  . ALA A 1 383 ? 19.098 3.639   17.419  1.00 15.74 ? 383 ALA A HB2  1 
ATOM   5742 H HB3  . ALA A 1 383 ? 17.708 3.391   16.692  1.00 15.74 ? 383 ALA A HB3  1 
ATOM   5743 N N    . THR A 1 384 ? 15.808 5.283   18.734  1.00 14.13 ? 384 THR A N    1 
ATOM   5744 C CA   . THR A 1 384 ? 14.489 5.826   18.440  1.00 15.99 ? 384 THR A CA   1 
ATOM   5745 C C    . THR A 1 384 ? 14.652 6.972   17.458  1.00 16.84 ? 384 THR A C    1 
ATOM   5746 O O    . THR A 1 384 ? 15.548 7.820   17.606  1.00 17.31 ? 384 THR A O    1 
ATOM   5747 C CB   . THR A 1 384 ? 13.766 6.332   19.677  1.00 19.23 ? 384 THR A CB   1 
ATOM   5748 O OG1  . THR A 1 384 ? 14.522 7.371   20.276  1.00 25.83 ? 384 THR A OG1  1 
ATOM   5749 C CG2  . THR A 1 384 ? 13.585 5.209   20.652  1.00 17.22 ? 384 THR A CG2  1 
ATOM   5750 H H    . THR A 1 384 ? 16.390 5.872   18.967  1.00 16.95 ? 384 THR A H    1 
ATOM   5751 H HA   . THR A 1 384 ? 13.941 5.126   18.051  1.00 19.19 ? 384 THR A HA   1 
ATOM   5752 H HB   . THR A 1 384 ? 12.892 6.676   19.436  1.00 23.08 ? 384 THR A HB   1 
ATOM   5753 H HG1  . THR A 1 384 ? 14.164 7.607   20.998  1.00 30.99 ? 384 THR A HG1  1 
ATOM   5754 H HG21 . THR A 1 384 ? 13.106 5.524   21.435  1.00 20.67 ? 384 THR A HG21 1 
ATOM   5755 H HG22 . THR A 1 384 ? 13.079 4.491   20.241  1.00 20.67 ? 384 THR A HG22 1 
ATOM   5756 H HG23 . THR A 1 384 ? 14.450 4.868   20.928  1.00 20.67 ? 384 THR A HG23 1 
ATOM   5757 N N    . LEU A 1 385 ? 13.765 7.010   16.478  1.00 14.43 ? 385 LEU A N    1 
ATOM   5758 C CA   . LEU A 1 385 ? 13.658 8.102   15.522  1.00 15.33 ? 385 LEU A CA   1 
ATOM   5759 C C    . LEU A 1 385 ? 12.323 8.784   15.794  1.00 15.46 ? 385 LEU A C    1 
ATOM   5760 O O    . LEU A 1 385 ? 11.258 8.210   15.538  1.00 17.36 ? 385 LEU A O    1 
ATOM   5761 C CB   . LEU A 1 385 ? 13.745 7.569   14.102  1.00 15.50 ? 385 LEU A CB   1 
ATOM   5762 C CG   . LEU A 1 385 ? 15.044 6.843   13.737  1.00 14.08 ? 385 LEU A CG   1 
ATOM   5763 C CD1  . LEU A 1 385 ? 15.011 6.447   12.278  1.00 16.04 ? 385 LEU A CD1  1 
ATOM   5764 C CD2  . LEU A 1 385 ? 16.237 7.688   14.041  1.00 15.34 ? 385 LEU A CD2  1 
ATOM   5765 H H    . LEU A 1 385 ? 13.187 6.388   16.339  1.00 17.31 ? 385 LEU A H    1 
ATOM   5766 H HA   . LEU A 1 385 ? 14.374 8.746   15.640  1.00 18.39 ? 385 LEU A HA   1 
ATOM   5767 H HB2  . LEU A 1 385 ? 13.017 6.942   13.969  1.00 18.60 ? 385 LEU A HB2  1 
ATOM   5768 H HB3  . LEU A 1 385 ? 13.653 8.318   13.492  1.00 18.60 ? 385 LEU A HB3  1 
ATOM   5769 H HG   . LEU A 1 385 ? 15.125 6.038   14.273  1.00 16.89 ? 385 LEU A HG   1 
ATOM   5770 H HD11 . LEU A 1 385 ? 15.824 5.963   12.063  1.00 19.24 ? 385 LEU A HD11 1 
ATOM   5771 H HD12 . LEU A 1 385 ? 14.238 5.882   12.121  1.00 19.24 ? 385 LEU A HD12 1 
ATOM   5772 H HD13 . LEU A 1 385 ? 14.950 7.248   11.735  1.00 19.24 ? 385 LEU A HD13 1 
ATOM   5773 H HD21 . LEU A 1 385 ? 17.030 7.251   13.693  1.00 18.41 ? 385 LEU A HD21 1 
ATOM   5774 H HD22 . LEU A 1 385 ? 16.126 8.554   13.619  1.00 18.41 ? 385 LEU A HD22 1 
ATOM   5775 H HD23 . LEU A 1 385 ? 16.313 7.794   15.002  1.00 18.41 ? 385 LEU A HD23 1 
ATOM   5776 N N    . THR A 1 386 ? 12.363 10.004  16.319  1.00 15.29 ? 386 THR A N    1 
ATOM   5777 C CA   . THR A 1 386 ? 11.147 10.741  16.671  1.00 16.82 ? 386 THR A CA   1 
ATOM   5778 C C    . THR A 1 386 ? 10.922 11.776  15.581  1.00 16.75 ? 386 THR A C    1 
ATOM   5779 O O    . THR A 1 386 ? 11.594 12.809  15.540  1.00 17.48 ? 386 THR A O    1 
ATOM   5780 C CB   . THR A 1 386 ? 11.236 11.378  18.062  1.00 17.29 ? 386 THR A CB   1 
ATOM   5781 O OG1  . THR A 1 386 ? 11.511 10.345  19.024  1.00 19.18 ? 386 THR A OG1  1 
ATOM   5782 C CG2  . THR A 1 386 ? 9.952  12.076  18.454  1.00 20.85 ? 386 THR A CG2  1 
ATOM   5783 H H    . THR A 1 386 ? 13.089 10.433  16.484  1.00 18.35 ? 386 THR A H    1 
ATOM   5784 H HA   . THR A 1 386 ? 10.396 10.128  16.693  1.00 20.18 ? 386 THR A HA   1 
ATOM   5785 H HB   . THR A 1 386 ? 11.939 12.046  18.055  1.00 20.75 ? 386 THR A HB   1 
ATOM   5786 H HG1  . THR A 1 386 ? 12.275 10.023  18.889  1.00 23.02 ? 386 THR A HG1  1 
ATOM   5787 H HG21 . THR A 1 386 ? 10.018 12.405  19.364  1.00 25.02 ? 386 THR A HG21 1 
ATOM   5788 H HG22 . THR A 1 386 ? 9.787  12.824  17.860  1.00 25.02 ? 386 THR A HG22 1 
ATOM   5789 H HG23 . THR A 1 386 ? 9.208  11.457  18.397  1.00 25.02 ? 386 THR A HG23 1 
ATOM   5790 N N    . TRP A 1 387 ? 9.987  11.488  14.678  1.00 17.66 ? 387 TRP A N    1 
ATOM   5791 C CA   . TRP A 1 387 ? 9.730  12.321  13.512  1.00 17.21 ? 387 TRP A CA   1 
ATOM   5792 C C    . TRP A 1 387 ? 8.765  13.441  13.883  1.00 19.44 ? 387 TRP A C    1 
ATOM   5793 O O    . TRP A 1 387 ? 7.650  13.187  14.358  1.00 21.76 ? 387 TRP A O    1 
ATOM   5794 C CB   . TRP A 1 387 ? 9.125  11.450  12.401  1.00 18.03 ? 387 TRP A CB   1 
ATOM   5795 C CG   . TRP A 1 387 ? 9.995  10.287  11.976  1.00 17.72 ? 387 TRP A CG   1 
ATOM   5796 C CD1  . TRP A 1 387 ? 9.928  8.985   12.415  1.00 16.53 ? 387 TRP A CD1  1 
ATOM   5797 C CD2  . TRP A 1 387 ? 11.060 10.330  11.021  1.00 16.90 ? 387 TRP A CD2  1 
ATOM   5798 N NE1  . TRP A 1 387 ? 10.886 8.222   11.787  1.00 17.67 ? 387 TRP A NE1  1 
ATOM   5799 C CE2  . TRP A 1 387 ? 11.596 9.027   10.926  1.00 16.98 ? 387 TRP A CE2  1 
ATOM   5800 C CE3  . TRP A 1 387 ? 11.606 11.337  10.222  1.00 17.26 ? 387 TRP A CE3  1 
ATOM   5801 C CZ2  . TRP A 1 387 ? 12.653 8.713   10.046  1.00 17.02 ? 387 TRP A CZ2  1 
ATOM   5802 C CZ3  . TRP A 1 387 ? 12.670 11.019  9.366   1.00 16.96 ? 387 TRP A CZ3  1 
ATOM   5803 C CH2  . TRP A 1 387 ? 13.174 9.727   9.295   1.00 17.73 ? 387 TRP A CH2  1 
ATOM   5804 H H    . TRP A 1 387 ? 9.477  10.797  14.722  1.00 21.20 ? 387 TRP A H    1 
ATOM   5805 H HA   . TRP A 1 387 ? 10.553 12.726  13.196  1.00 20.65 ? 387 TRP A HA   1 
ATOM   5806 H HB2  . TRP A 1 387 ? 8.283  11.086  12.717  1.00 21.64 ? 387 TRP A HB2  1 
ATOM   5807 H HB3  . TRP A 1 387 ? 8.974  12.005  11.620  1.00 21.64 ? 387 TRP A HB3  1 
ATOM   5808 H HD1  . TRP A 1 387 ? 9.323  8.667   13.046  1.00 19.84 ? 387 TRP A HD1  1 
ATOM   5809 H HE1  . TRP A 1 387 ? 11.019 7.382   11.911  1.00 21.21 ? 387 TRP A HE1  1 
ATOM   5810 H HE3  . TRP A 1 387 ? 11.270 12.203  10.257  1.00 20.72 ? 387 TRP A HE3  1 
ATOM   5811 H HZ2  . TRP A 1 387 ? 12.984 7.846   9.981   1.00 20.42 ? 387 TRP A HZ2  1 
ATOM   5812 H HZ3  . TRP A 1 387 ? 13.045 11.685  8.837   1.00 20.35 ? 387 TRP A HZ3  1 
ATOM   5813 H HH2  . TRP A 1 387 ? 13.884 9.548   8.721   1.00 21.28 ? 387 TRP A HH2  1 
ATOM   5814 N N    . LYS A 1 388 ? 9.146  14.682  13.582  1.00 22.00 ? 388 LYS A N    1 
ATOM   5815 C CA   . LYS A 1 388 ? 8.400  15.871  14.019  1.00 22.99 ? 388 LYS A CA   1 
ATOM   5816 C C    . LYS A 1 388 ? 7.301  16.215  13.022  1.00 41.23 ? 388 LYS A C    1 
ATOM   5817 O O    . LYS A 1 388 ? 7.512  16.127  11.816  1.00 41.28 ? 388 LYS A O    1 
ATOM   5818 C CB   . LYS A 1 388 ? 9.404  17.027  14.108  1.00 37.76 ? 388 LYS A CB   1 
ATOM   5819 C CG   . LYS A 1 388 ? 10.497 16.842  15.191  1.00 37.10 ? 388 LYS A CG   1 
ATOM   5820 C CD   . LYS A 1 388 ? 11.663 17.869  15.029  1.00 37.59 ? 388 LYS A CD   1 
ATOM   5821 C CE   . LYS A 1 388 ? 12.861 17.592  15.981  1.00 38.58 ? 388 LYS A CE   1 
ATOM   5822 N NZ   . LYS A 1 388 ? 14.122 18.404  15.779  1.00 31.90 ? 388 LYS A NZ   1 
ATOM   5823 H H    . LYS A 1 388 ? 9.846  14.870  13.117  1.00 26.40 ? 388 LYS A H    1 
ATOM   5824 H HA   . LYS A 1 388 ? 7.975  15.723  14.878  1.00 27.58 ? 388 LYS A HA   1 
ATOM   5825 H HB2  . LYS A 1 388 ? 9.850  17.116  13.252  1.00 45.31 ? 388 LYS A HB2  1 
ATOM   5826 H HB3  . LYS A 1 388 ? 8.920  17.841  14.316  1.00 45.31 ? 388 LYS A HB3  1 
ATOM   5827 H HG2  . LYS A 1 388 ? 10.103 16.967  16.068  1.00 44.52 ? 388 LYS A HG2  1 
ATOM   5828 H HG3  . LYS A 1 388 ? 10.869 15.949  15.119  1.00 44.52 ? 388 LYS A HG3  1 
ATOM   5829 H HD2  . LYS A 1 388 ? 11.993 17.830  14.118  1.00 45.11 ? 388 LYS A HD2  1 
ATOM   5830 H HD3  . LYS A 1 388 ? 11.328 18.758  15.223  1.00 45.11 ? 388 LYS A HD3  1 
ATOM   5831 H HE2  . LYS A 1 388 ? 12.564 17.761  16.889  1.00 46.30 ? 388 LYS A HE2  1 
ATOM   5832 H HE3  . LYS A 1 388 ? 13.110 16.660  15.882  1.00 46.30 ? 388 LYS A HE3  1 
ATOM   5833 H HZ1  . LYS A 1 388 ? 14.741 18.156  16.369  1.00 38.28 ? 388 LYS A HZ1  1 
ATOM   5834 H HZ2  . LYS A 1 388 ? 14.438 18.275  14.957  1.00 38.28 ? 388 LYS A HZ2  1 
ATOM   5835 H HZ3  . LYS A 1 388 ? 13.948 19.269  15.889  1.00 38.28 ? 388 LYS A HZ3  1 
HETATM 5836 O O    . HOH B 2 .   ? 21.163 18.982  21.381  1.00 38.18 ? 401 HOH A O    1 
HETATM 5837 O O    . HOH B 2 .   ? 51.003 -21.563 -9.131  1.00 27.39 ? 402 HOH A O    1 
HETATM 5838 O O    . HOH B 2 .   ? 32.318 9.502   -18.114 1.00 11.15 ? 403 HOH A O    1 
HETATM 5839 O O    . HOH B 2 .   ? 43.347 2.754   14.599  1.00 10.76 ? 404 HOH A O    1 
HETATM 5840 O O    . HOH B 2 .   ? 35.953 19.197  -12.937 1.00 38.81 ? 405 HOH A O    1 
HETATM 5841 O O    . HOH B 2 .   ? 46.376 4.356   17.638  1.00 43.00 ? 406 HOH A O    1 
HETATM 5842 O O    . HOH B 2 .   ? 28.859 14.980  11.673  1.00 14.67 ? 407 HOH A O    1 
HETATM 5843 O O    . HOH B 2 .   ? 51.749 3.259   -16.069 1.00 37.49 ? 408 HOH A O    1 
HETATM 5844 O O    . HOH B 2 .   ? 54.552 4.133   -0.217  1.00 40.56 ? 409 HOH A O    1 
HETATM 5845 O O    . HOH B 2 .   ? 33.196 -17.280 9.275   1.00 42.18 ? 410 HOH A O    1 
HETATM 5846 O O    . HOH B 2 .   ? 45.242 -21.322 -10.337 1.00 37.57 ? 411 HOH A O    1 
HETATM 5847 O O    . HOH B 2 .   ? 26.501 -18.346 7.202   1.00 45.07 ? 412 HOH A O    1 
HETATM 5848 O O    . HOH B 2 .   ? 15.133 -9.138  -10.105 1.00 32.71 ? 413 HOH A O    1 
HETATM 5849 O O    . HOH B 2 .   ? 41.444 -0.192  -21.458 1.00 33.83 ? 414 HOH A O    1 
HETATM 5850 O O    . HOH B 2 .   ? 35.351 -10.658 15.795  1.00 32.44 ? 415 HOH A O    1 
HETATM 5851 O O    . HOH B 2 .   ? 34.945 -19.845 -2.578  1.00 28.35 ? 416 HOH A O    1 
HETATM 5852 O O    . HOH B 2 .   ? 33.497 -8.871  -12.994 1.00 18.08 ? 417 HOH A O    1 
HETATM 5853 O O    . HOH B 2 .   ? 22.520 5.924   -23.811 1.00 44.34 ? 418 HOH A O    1 
HETATM 5854 O O    . HOH B 2 .   ? 22.702 -16.509 5.505   1.00 18.38 ? 419 HOH A O    1 
HETATM 5855 O O    . HOH B 2 .   ? 10.337 0.509   -5.504  1.00 42.90 ? 420 HOH A O    1 
HETATM 5856 O O    . HOH B 2 .   ? 58.308 -6.249  -6.413  1.00 26.24 ? 421 HOH A O    1 
HETATM 5857 O O    . HOH B 2 .   ? 23.819 -14.783 1.474   1.00 32.04 ? 422 HOH A O    1 
HETATM 5858 O O    . HOH B 2 .   ? 32.004 -8.339  8.933   1.00 15.28 ? 423 HOH A O    1 
HETATM 5859 O O    . HOH B 2 .   ? 35.602 -8.607  20.116  1.00 24.83 ? 424 HOH A O    1 
HETATM 5860 O O    . HOH B 2 .   ? 33.400 -3.679  -11.937 1.00 12.82 ? 425 HOH A O    1 
HETATM 5861 O O    . HOH B 2 .   ? 50.067 -6.941  -5.977  1.00 24.98 ? 426 HOH A O    1 
HETATM 5862 O O    . HOH B 2 .   ? 19.373 -15.750 7.363   1.00 29.86 ? 427 HOH A O    1 
HETATM 5863 O O    . HOH B 2 .   ? 28.103 17.238  -10.806 1.00 37.52 ? 428 HOH A O    1 
HETATM 5864 O O    . HOH B 2 .   ? 55.975 -11.753 -4.643  1.00 23.94 ? 429 HOH A O    1 
HETATM 5865 O O    . HOH B 2 .   ? 11.179 -5.752  -12.094 1.00 25.78 ? 430 HOH A O    1 
HETATM 5866 O O    . HOH B 2 .   ? 59.744 -8.305  -3.185  1.00 22.53 ? 431 HOH A O    1 
HETATM 5867 O O    . HOH B 2 .   ? 20.391 -3.223  -19.654 1.00 28.71 ? 432 HOH A O    1 
HETATM 5868 O O    . HOH B 2 .   ? 42.274 1.790   16.563  1.00 20.07 ? 433 HOH A O    1 
HETATM 5869 O O    . HOH B 2 .   ? 37.632 -2.596  -16.587 1.00 20.05 ? 434 HOH A O    1 
HETATM 5870 O O    . HOH B 2 .   ? 51.457 9.516   -3.694  1.00 33.68 ? 435 HOH A O    1 
HETATM 5871 O O    . HOH B 2 .   ? 29.119 4.965   -20.374 1.00 20.51 ? 436 HOH A O    1 
HETATM 5872 O O    . HOH B 2 .   ? 56.156 1.011   1.076   1.00 27.01 ? 437 HOH A O    1 
HETATM 5873 O O    . HOH B 2 .   ? 15.515 19.791  4.079   1.00 34.82 ? 438 HOH A O    1 
HETATM 5874 O O    . HOH B 2 .   ? 9.918  6.072   14.782  1.00 22.38 ? 439 HOH A O    1 
HETATM 5875 O O    . HOH B 2 .   ? 50.272 3.256   5.422   1.00 28.10 ? 440 HOH A O    1 
HETATM 5876 O O    . HOH B 2 .   ? 28.384 -7.294  14.499  1.00 30.08 ? 441 HOH A O    1 
HETATM 5877 O O    . HOH B 2 .   ? 21.171 -11.838 0.861   1.00 20.82 ? 442 HOH A O    1 
HETATM 5878 O O    . HOH B 2 .   ? 49.585 6.092   -20.327 1.00 27.37 ? 443 HOH A O    1 
HETATM 5879 O O    . HOH B 2 .   ? 41.736 5.594   17.789  1.00 43.23 ? 444 HOH A O    1 
HETATM 5880 O O    . HOH B 2 .   ? 33.632 13.800  16.221  1.00 30.47 ? 445 HOH A O    1 
HETATM 5881 O O    . HOH B 2 .   ? 36.505 15.889  -2.813  1.00 27.51 ? 446 HOH A O    1 
HETATM 5882 O O    . HOH B 2 .   ? 37.898 17.463  2.201   1.00 41.83 ? 447 HOH A O    1 
HETATM 5883 O O    . HOH B 2 .   ? 27.216 -2.778  -23.522 1.00 32.84 ? 448 HOH A O    1 
HETATM 5884 O O    . HOH B 2 .   ? 29.128 -1.553  7.429   1.00 12.73 ? 449 HOH A O    1 
HETATM 5885 O O    . HOH B 2 .   ? 24.434 2.994   27.223  1.00 16.52 ? 450 HOH A O    1 
HETATM 5886 O O    . HOH B 2 .   ? 43.038 -15.458 -13.326 1.00 22.77 ? 451 HOH A O    1 
HETATM 5887 O O    . HOH B 2 .   ? 22.438 -9.930  4.158   1.00 15.29 ? 452 HOH A O    1 
HETATM 5888 O O    . HOH B 2 .   ? 39.827 -9.158  -12.437 1.00 12.41 ? 453 HOH A O    1 
HETATM 5889 O O    . HOH B 2 .   ? 35.849 -14.936 -15.980 1.00 19.45 ? 454 HOH A O    1 
HETATM 5890 O O    . HOH B 2 .   ? 32.643 -5.729  -2.775  1.00 22.51 ? 455 HOH A O    1 
HETATM 5891 O O    . HOH B 2 .   ? 40.900 -9.714  15.567  1.00 24.30 ? 456 HOH A O    1 
HETATM 5892 O O    . HOH B 2 .   ? 15.144 1.853   -1.160  1.00 22.73 ? 457 HOH A O    1 
HETATM 5893 O O    . HOH B 2 .   ? 43.828 7.593   -19.687 1.00 32.14 ? 458 HOH A O    1 
HETATM 5894 O O    . HOH B 2 .   ? 40.207 18.910  -13.205 1.00 41.50 ? 459 HOH A O    1 
HETATM 5895 O O    . HOH B 2 .   ? 37.696 -9.653  18.490  1.00 26.17 ? 460 HOH A O    1 
HETATM 5896 O O    . HOH B 2 .   ? 14.144 9.929   19.289  1.00 19.02 ? 461 HOH A O    1 
HETATM 5897 O O    . HOH B 2 .   ? 34.422 4.063   26.449  1.00 14.91 ? 462 HOH A O    1 
HETATM 5898 O O    . HOH B 2 .   ? 28.027 10.386  -16.985 1.00 32.23 ? 463 HOH A O    1 
HETATM 5899 O O    . HOH B 2 .   ? 21.519 -16.978 0.334   1.00 14.69 ? 464 HOH A O    1 
HETATM 5900 O O    . HOH B 2 .   ? 16.511 0.726   24.473  1.00 38.23 ? 465 HOH A O    1 
HETATM 5901 O O    . HOH B 2 .   ? 9.465  14.166  9.953   1.00 19.67 ? 466 HOH A O    1 
HETATM 5902 O O    . HOH B 2 .   ? 36.967 -4.319  3.780   1.00 14.64 ? 467 HOH A O    1 
HETATM 5903 O O    . HOH B 2 .   ? 13.678 10.269  5.391   1.00 17.22 ? 468 HOH A O    1 
HETATM 5904 O O    . HOH B 2 .   ? 20.302 2.218   -22.907 1.00 28.90 ? 469 HOH A O    1 
HETATM 5905 O O    . HOH B 2 .   ? 17.378 -0.127  1.972   1.00 20.00 ? 470 HOH A O    1 
HETATM 5906 O O    . HOH B 2 .   ? 15.330 -1.117  0.644   1.00 27.44 ? 471 HOH A O    1 
HETATM 5907 O O    . HOH B 2 .   ? 14.843 9.489   0.763   1.00 18.88 ? 472 HOH A O    1 
HETATM 5908 O O    . HOH B 2 .   ? 43.158 4.876   15.708  1.00 22.57 ? 473 HOH A O    1 
HETATM 5909 O O    . HOH B 2 .   ? 56.339 -10.025 -15.963 1.00 23.00 ? 474 HOH A O    1 
HETATM 5910 O O    . HOH B 2 .   ? 36.309 2.878   21.167  1.00 17.94 ? 475 HOH A O    1 
HETATM 5911 O O    . HOH B 2 .   ? 19.504 2.679   2.665   1.00 18.71 ? 476 HOH A O    1 
HETATM 5912 O O    . HOH B 2 .   ? 25.571 -2.958  16.797  1.00 17.33 ? 477 HOH A O    1 
HETATM 5913 O O    . HOH B 2 .   ? 33.587 -9.511  -11.314 1.00 28.27 ? 478 HOH A O    1 
HETATM 5914 O O    . HOH B 2 .   ? 55.351 2.412   -12.613 1.00 40.54 ? 479 HOH A O    1 
HETATM 5915 O O    . HOH B 2 .   ? 48.053 -14.279 -7.267  1.00 14.33 ? 480 HOH A O    1 
HETATM 5916 O O    . HOH B 2 .   ? 21.539 18.804  -5.153  1.00 30.80 ? 481 HOH A O    1 
HETATM 5917 O O    . HOH B 2 .   ? 17.275 -2.499  17.965  1.00 19.67 ? 482 HOH A O    1 
HETATM 5918 O O    . HOH B 2 .   ? 24.870 -4.402  14.520  1.00 17.75 ? 483 HOH A O    1 
HETATM 5919 O O    . HOH B 2 .   ? 32.293 8.354   18.984  1.00 12.89 ? 484 HOH A O    1 
HETATM 5920 O O    . HOH B 2 .   ? 39.071 -7.452  -10.385 1.00 13.68 ? 485 HOH A O    1 
HETATM 5921 O O    . HOH B 2 .   ? 20.219 -5.331  -0.538  1.00 13.96 ? 486 HOH A O    1 
HETATM 5922 O O    . HOH B 2 .   ? 16.521 -9.189  -17.312 1.00 33.57 ? 487 HOH A O    1 
HETATM 5923 O O    . HOH B 2 .   ? 24.009 15.321  -11.053 1.00 29.02 ? 488 HOH A O    1 
HETATM 5924 O O    . HOH B 2 .   ? 38.507 -4.993  -17.622 1.00 14.50 ? 489 HOH A O    1 
HETATM 5925 O O    . HOH B 2 .   ? 17.048 -12.391 3.105   1.00 17.90 ? 490 HOH A O    1 
HETATM 5926 O O    . HOH B 2 .   ? 55.931 -4.616  4.568   1.00 17.75 ? 491 HOH A O    1 
HETATM 5927 O O    . HOH B 2 .   ? 36.751 4.112   24.885  1.00 18.02 ? 492 HOH A O    1 
HETATM 5928 O O    . HOH B 2 .   ? 49.122 -5.987  2.729   1.00 12.83 ? 493 HOH A O    1 
HETATM 5929 O O    . HOH B 2 .   ? 40.984 1.492   19.926  1.00 26.29 ? 494 HOH A O    1 
HETATM 5930 O O    . HOH B 2 .   ? 10.175 -2.275  7.891   1.00 43.92 ? 495 HOH A O    1 
HETATM 5931 O O    . HOH B 2 .   ? 43.601 -8.328  9.923   1.00 32.73 ? 496 HOH A O    1 
HETATM 5932 O O    . HOH B 2 .   ? 40.869 13.849  -8.099  1.00 21.18 ? 497 HOH A O    1 
HETATM 5933 O O    . HOH B 2 .   ? 23.145 12.698  -8.300  1.00 16.37 ? 498 HOH A O    1 
HETATM 5934 O O    . HOH B 2 .   ? 16.392 22.487  5.016   1.00 37.39 ? 499 HOH A O    1 
HETATM 5935 O O    . HOH B 2 .   ? 54.101 -10.988 -19.909 1.00 14.96 ? 500 HOH A O    1 
HETATM 5936 O O    . HOH B 2 .   ? 50.506 0.515   5.389   1.00 21.14 ? 501 HOH A O    1 
HETATM 5937 O O    . HOH B 2 .   ? 30.875 12.367  -15.663 1.00 25.70 ? 502 HOH A O    1 
HETATM 5938 O O    . HOH B 2 .   ? 38.020 -11.365 -15.005 1.00 14.04 ? 503 HOH A O    1 
HETATM 5939 O O    . HOH B 2 .   ? 32.734 -8.998  13.689  1.00 21.30 ? 504 HOH A O    1 
HETATM 5940 O O    . HOH B 2 .   ? 32.097 14.105  -13.687 1.00 27.17 ? 505 HOH A O    1 
HETATM 5941 O O    . HOH B 2 .   ? 35.769 -13.578 -20.109 1.00 38.09 ? 506 HOH A O    1 
HETATM 5942 O O    . HOH B 2 .   ? 39.476 -1.528  0.796   1.00 11.08 ? 507 HOH A O    1 
HETATM 5943 O O    . HOH B 2 .   ? 19.269 -12.920 -12.642 1.00 20.44 ? 508 HOH A O    1 
HETATM 5944 O O    . HOH B 2 .   ? 53.469 -13.755 -21.393 1.00 22.76 ? 509 HOH A O    1 
HETATM 5945 O O    . HOH B 2 .   ? 31.525 -10.903 8.174   1.00 17.76 ? 510 HOH A O    1 
HETATM 5946 O O    . HOH B 2 .   ? 25.757 18.622  -5.555  1.00 29.25 ? 511 HOH A O    1 
HETATM 5947 O O    . HOH B 2 .   ? 16.630 -11.308 -15.680 1.00 26.91 ? 512 HOH A O    1 
HETATM 5948 O O    . HOH B 2 .   ? 37.962 -11.139 5.724   1.00 31.87 ? 513 HOH A O    1 
HETATM 5949 O O    . HOH B 2 .   ? 36.854 -5.211  -0.039  1.00 23.46 ? 514 HOH A O    1 
HETATM 5950 O O    . HOH B 2 .   ? 57.951 -11.966 -11.646 1.00 24.72 ? 515 HOH A O    1 
HETATM 5951 O O    . HOH B 2 .   ? 34.872 -6.576  0.894   1.00 22.51 ? 516 HOH A O    1 
HETATM 5952 O O    . HOH B 2 .   ? 57.482 -23.006 -9.649  1.00 26.97 ? 517 HOH A O    1 
HETATM 5953 O O    . HOH B 2 .   ? 26.938 -3.073  20.916  1.00 19.89 ? 518 HOH A O    1 
HETATM 5954 O O    . HOH B 2 .   ? 54.780 -11.873 -8.625  1.00 19.16 ? 519 HOH A O    1 
HETATM 5955 O O    . HOH B 2 .   ? 28.278 -3.642  4.380   1.00 13.67 ? 520 HOH A O    1 
HETATM 5956 O O    . HOH B 2 .   ? 48.892 -5.912  9.879   1.00 26.96 ? 521 HOH A O    1 
HETATM 5957 O O    . HOH B 2 .   ? 31.822 10.958  18.325  1.00 14.65 ? 522 HOH A O    1 
HETATM 5958 O O    . HOH B 2 .   ? 28.771 -16.769 -17.022 1.00 43.52 ? 523 HOH A O    1 
HETATM 5959 O O    . HOH B 2 .   ? 36.820 5.031   -23.437 1.00 24.51 ? 524 HOH A O    1 
HETATM 5960 O O    . HOH B 2 .   ? 37.585 -0.982  -18.880 1.00 21.85 ? 525 HOH A O    1 
HETATM 5961 O O    . HOH B 2 .   ? 53.915 -20.039 -11.849 1.00 32.43 ? 526 HOH A O    1 
HETATM 5962 O O    . HOH B 2 .   ? 26.850 21.488  16.971  1.00 35.44 ? 527 HOH A O    1 
HETATM 5963 O O    . HOH B 2 .   ? 27.245 14.401  26.711  1.00 24.15 ? 528 HOH A O    1 
HETATM 5964 O O    . HOH B 2 .   ? 17.886 12.947  0.143   1.00 19.84 ? 529 HOH A O    1 
HETATM 5965 O O    . HOH B 2 .   ? 56.534 -3.808  -16.539 1.00 14.82 ? 530 HOH A O    1 
HETATM 5966 O O    . HOH B 2 .   ? 31.028 -6.220  1.371   1.00 19.56 ? 531 HOH A O    1 
HETATM 5967 O O    . HOH B 2 .   ? 19.782 3.048   -0.042  1.00 15.83 ? 532 HOH A O    1 
HETATM 5968 O O    . HOH B 2 .   ? 38.736 8.801   -17.705 1.00 23.49 ? 533 HOH A O    1 
HETATM 5969 O O    . HOH B 2 .   ? 39.845 -14.886 -11.820 1.00 29.94 ? 534 HOH A O    1 
HETATM 5970 O O    . HOH B 2 .   ? 15.096 1.105   -18.880 1.00 29.72 ? 535 HOH A O    1 
HETATM 5971 O O    . HOH B 2 .   ? 28.844 -15.322 16.513  1.00 47.70 ? 536 HOH A O    1 
HETATM 5972 O O    . HOH B 2 .   ? 54.537 -12.867 -11.191 1.00 22.23 ? 537 HOH A O    1 
HETATM 5973 O O    . HOH B 2 .   ? 35.262 0.121   5.152   1.00 11.60 ? 538 HOH A O    1 
HETATM 5974 O O    . HOH B 2 .   ? 44.241 -16.149 1.388   1.00 31.48 ? 539 HOH A O    1 
HETATM 5975 O O    . HOH B 2 .   ? 15.816 -5.911  15.224  1.00 20.86 ? 540 HOH A O    1 
HETATM 5976 O O    . HOH B 2 .   ? 11.903 4.796   16.366  1.00 19.75 ? 541 HOH A O    1 
HETATM 5977 O O    . HOH B 2 .   ? 53.787 -7.188  8.156   1.00 25.48 ? 542 HOH A O    1 
HETATM 5978 O O    . HOH B 2 .   ? 57.721 -1.776  -8.544  1.00 29.48 ? 543 HOH A O    1 
HETATM 5979 O O    . HOH B 2 .   ? 21.960 -16.162 -14.824 1.00 26.89 ? 544 HOH A O    1 
HETATM 5980 O O    . HOH B 2 .   ? 4.762  -9.998  12.744  1.00 28.07 ? 545 HOH A O    1 
HETATM 5981 O O    . HOH B 2 .   ? 30.785 -9.041  -23.283 1.00 22.58 ? 546 HOH A O    1 
HETATM 5982 O O    . HOH B 2 .   ? 33.852 17.610  -7.496  1.00 28.17 ? 547 HOH A O    1 
HETATM 5983 O O    . HOH B 2 .   ? 30.244 17.513  4.092   1.00 17.70 ? 548 HOH A O    1 
HETATM 5984 O O    . HOH B 2 .   ? 21.256 -0.175  -22.226 1.00 27.63 ? 549 HOH A O    1 
HETATM 5985 O O    . HOH B 2 .   ? 36.864 10.822  -17.692 1.00 20.69 ? 550 HOH A O    1 
HETATM 5986 O O    . HOH B 2 .   ? 20.697 23.737  10.131  1.00 41.54 ? 551 HOH A O    1 
HETATM 5987 O O    . HOH B 2 .   ? 33.537 6.034   24.609  1.00 14.69 ? 552 HOH A O    1 
HETATM 5988 O O    . HOH B 2 .   ? 58.117 -10.847 -6.736  1.00 36.42 ? 553 HOH A O    1 
HETATM 5989 O O    . HOH B 2 .   ? 26.294 -4.474  25.381  1.00 40.59 ? 554 HOH A O    1 
HETATM 5990 O O    . HOH B 2 .   ? 32.421 10.245  -23.322 1.00 39.14 ? 555 HOH A O    1 
HETATM 5991 O O    . HOH B 2 .   ? 48.108 4.462   8.755   1.00 32.07 ? 556 HOH A O    1 
HETATM 5992 O O    . HOH B 2 .   ? 29.954 14.901  18.353  1.00 30.30 ? 557 HOH A O    1 
HETATM 5993 O O    . HOH B 2 .   ? 29.677 13.764  3.927   1.00 13.20 ? 558 HOH A O    1 
HETATM 5994 O O    . HOH B 2 .   ? 16.459 -15.159 -2.475  1.00 36.10 ? 559 HOH A O    1 
HETATM 5995 O O    . HOH B 2 .   ? 13.368 6.949   -11.491 1.00 29.41 ? 560 HOH A O    1 
HETATM 5996 O O    . HOH B 2 .   ? 12.352 18.388  19.045  1.00 36.76 ? 561 HOH A O    1 
HETATM 5997 O O    . HOH B 2 .   ? 58.030 -6.094  -9.904  1.00 23.24 ? 562 HOH A O    1 
HETATM 5998 O O    . HOH B 2 .   ? 19.925 -14.725 -6.647  1.00 24.84 ? 563 HOH A O    1 
HETATM 5999 O O    . HOH B 2 .   ? 27.073 13.466  -14.404 1.00 30.14 ? 564 HOH A O    1 
HETATM 6000 O O    . HOH B 2 .   ? 57.456 -13.243 -2.187  1.00 29.85 ? 565 HOH A O    1 
HETATM 6001 O O    . HOH B 2 .   ? 10.065 1.671   13.909  1.00 28.92 ? 566 HOH A O    1 
HETATM 6002 O O    . HOH B 2 .   ? 51.643 -13.700 -24.687 1.00 22.56 ? 567 HOH A O    1 
HETATM 6003 O O    . HOH B 2 .   ? 41.327 -12.804 -15.350 1.00 22.31 ? 568 HOH A O    1 
HETATM 6004 O O    . HOH B 2 .   ? 47.969 13.202  -8.068  1.00 31.69 ? 569 HOH A O    1 
HETATM 6005 O O    . HOH B 2 .   ? 55.556 -14.226 5.194   1.00 39.03 ? 570 HOH A O    1 
HETATM 6006 O O    . HOH B 2 .   ? 15.688 5.916   -4.072  1.00 23.86 ? 571 HOH A O    1 
HETATM 6007 O O    . HOH B 2 .   ? 53.139 -17.947 -0.090  1.00 27.51 ? 572 HOH A O    1 
HETATM 6008 O O    . HOH B 2 .   ? 27.447 -3.619  8.204   1.00 12.99 ? 573 HOH A O    1 
HETATM 6009 O O    . HOH B 2 .   ? 9.123  5.106   10.368  1.00 21.66 ? 574 HOH A O    1 
HETATM 6010 O O    . HOH B 2 .   ? 30.584 13.259  -11.599 1.00 23.06 ? 575 HOH A O    1 
HETATM 6011 O O    . HOH B 2 .   ? 30.945 -2.813  -12.731 1.00 13.54 ? 576 HOH A O    1 
HETATM 6012 O O    . HOH B 2 .   ? 51.288 -19.172 -13.880 1.00 38.89 ? 577 HOH A O    1 
HETATM 6013 O O    . HOH B 2 .   ? 38.725 13.519  -15.278 1.00 18.83 ? 578 HOH A O    1 
HETATM 6014 O O    . HOH B 2 .   ? 53.496 -11.525 7.935   1.00 31.93 ? 579 HOH A O    1 
HETATM 6015 O O    . HOH B 2 .   ? 53.508 4.346   2.148   1.00 33.47 ? 580 HOH A O    1 
HETATM 6016 O O    . HOH B 2 .   ? 22.012 -9.985  -1.865  1.00 14.38 ? 581 HOH A O    1 
HETATM 6017 O O    . HOH B 2 .   ? 27.533 14.665  14.204  1.00 15.06 ? 582 HOH A O    1 
HETATM 6018 O O    . HOH B 2 .   ? 19.617 -8.852  11.674  1.00 20.55 ? 583 HOH A O    1 
HETATM 6019 O O    . HOH B 2 .   ? 15.109 -9.694  -4.838  1.00 28.37 ? 584 HOH A O    1 
HETATM 6020 O O    . HOH B 2 .   ? 62.991 -6.591  5.237   1.00 27.96 ? 585 HOH A O    1 
HETATM 6021 O O    . HOH B 2 .   ? 18.286 24.835  9.463   1.00 45.63 ? 586 HOH A O    1 
HETATM 6022 O O    . HOH B 2 .   ? 11.343 0.814   18.513  1.00 34.41 ? 587 HOH A O    1 
HETATM 6023 O O    . HOH B 2 .   ? 42.530 -15.813 -18.156 1.00 25.48 ? 588 HOH A O    1 
HETATM 6024 O O    . HOH B 2 .   ? 31.579 -1.944  25.650  1.00 18.60 ? 589 HOH A O    1 
HETATM 6025 O O    . HOH B 2 .   ? 24.853 1.976   31.005  1.00 24.46 ? 590 HOH A O    1 
HETATM 6026 O O    . HOH B 2 .   ? 33.271 1.214   13.251  1.00 11.64 ? 591 HOH A O    1 
HETATM 6027 O O    . HOH B 2 .   ? 32.995 -9.245  20.156  1.00 41.06 ? 592 HOH A O    1 
HETATM 6028 O O    . HOH B 2 .   ? 17.494 20.364  -0.582  1.00 33.88 ? 593 HOH A O    1 
HETATM 6029 O O    . HOH B 2 .   ? 36.914 17.286  10.079  1.00 24.83 ? 594 HOH A O    1 
HETATM 6030 O O    . HOH B 2 .   ? 31.482 -16.898 -15.390 1.00 40.43 ? 595 HOH A O    1 
HETATM 6031 O O    . HOH B 2 .   ? 41.428 6.913   -20.964 1.00 36.42 ? 596 HOH A O    1 
HETATM 6032 O O    . HOH B 2 .   ? 49.879 -17.077 -13.631 1.00 21.51 ? 597 HOH A O    1 
HETATM 6033 O O    . HOH B 2 .   ? 9.923  -8.842  7.661   1.00 31.21 ? 598 HOH A O    1 
HETATM 6034 O O    . HOH B 2 .   ? 35.938 -8.363  11.570  1.00 21.26 ? 599 HOH A O    1 
HETATM 6035 O O    . HOH B 2 .   ? 17.568 -1.744  -1.854  1.00 24.71 ? 600 HOH A O    1 
HETATM 6036 O O    . HOH B 2 .   ? 13.239 -7.842  -3.451  1.00 43.34 ? 601 HOH A O    1 
HETATM 6037 O O    . HOH B 2 .   ? 40.476 12.667  -5.543  1.00 22.10 ? 602 HOH A O    1 
HETATM 6038 O O    . HOH B 2 .   ? 38.266 13.477  -8.564  1.00 20.47 ? 603 HOH A O    1 
HETATM 6039 O O    . HOH B 2 .   ? 53.625 2.376   5.519   1.00 34.77 ? 604 HOH A O    1 
HETATM 6040 O O    . HOH B 2 .   ? 39.476 5.902   -23.919 1.00 35.91 ? 605 HOH A O    1 
HETATM 6041 O O    . HOH B 2 .   ? 17.502 15.737  -16.414 1.00 41.66 ? 606 HOH A O    1 
HETATM 6042 O O    . HOH B 2 .   ? 26.875 19.400  6.268   1.00 20.18 ? 607 HOH A O    1 
HETATM 6043 O O    . HOH B 2 .   ? 28.444 -2.976  28.448  1.00 41.60 ? 608 HOH A O    1 
HETATM 6044 O O    . HOH B 2 .   ? 50.637 -4.191  0.102   1.00 35.27 ? 609 HOH A O    1 
HETATM 6045 O O    . HOH B 2 .   ? 54.660 5.618   -4.506  1.00 23.87 ? 610 HOH A O    1 
HETATM 6046 O O    . HOH B 2 .   ? 60.583 -3.555  -0.232  1.00 28.76 ? 611 HOH A O    1 
HETATM 6047 O O    . HOH B 2 .   ? 17.170 12.987  20.444  1.00 24.27 ? 612 HOH A O    1 
HETATM 6048 O O    . HOH B 2 .   ? 47.372 -17.142 -17.506 1.00 24.94 ? 613 HOH A O    1 
HETATM 6049 O O    . HOH B 2 .   ? 41.791 16.005  0.657   1.00 37.36 ? 614 HOH A O    1 
HETATM 6050 O O    . HOH B 2 .   ? 21.021 -12.315 -10.512 1.00 17.24 ? 615 HOH A O    1 
HETATM 6051 O O    . HOH B 2 .   ? 16.376 3.341   -19.763 1.00 22.18 ? 616 HOH A O    1 
HETATM 6052 O O    . HOH B 2 .   ? 54.183 -1.100  4.479   1.00 26.74 ? 617 HOH A O    1 
HETATM 6053 O O    . HOH B 2 .   ? 47.940 11.715  5.607   1.00 37.76 ? 618 HOH A O    1 
HETATM 6054 O O    . HOH B 2 .   ? 42.639 -7.193  -22.559 1.00 17.85 ? 619 HOH A O    1 
HETATM 6055 O O    . HOH B 2 .   ? 58.982 -15.339 -8.271  1.00 17.99 ? 620 HOH A O    1 
HETATM 6056 O O    . HOH B 2 .   ? 37.104 17.956  -4.747  1.00 34.27 ? 621 HOH A O    1 
HETATM 6057 O O    . HOH B 2 .   ? 8.785  11.416  0.563   1.00 34.96 ? 622 HOH A O    1 
HETATM 6058 O O    . HOH B 2 .   ? 39.342 14.227  5.119   1.00 38.57 ? 623 HOH A O    1 
HETATM 6059 O O    . HOH B 2 .   ? 51.519 3.896   -11.360 1.00 24.45 ? 624 HOH A O    1 
HETATM 6060 O O    . HOH B 2 .   ? 53.586 -16.468 5.994   1.00 42.55 ? 625 HOH A O    1 
HETATM 6061 O O    . HOH B 2 .   ? 45.724 11.408  2.412   1.00 28.93 ? 626 HOH A O    1 
HETATM 6062 O O    . HOH B 2 .   ? 30.547 -6.794  21.958  1.00 25.47 ? 627 HOH A O    1 
HETATM 6063 O O    . HOH B 2 .   ? 47.454 10.646  -14.299 1.00 29.77 ? 628 HOH A O    1 
HETATM 6064 O O    . HOH B 2 .   ? 21.158 -4.007  -17.109 1.00 19.00 ? 629 HOH A O    1 
HETATM 6065 O O    . HOH B 2 .   ? 20.204 -4.717  15.743  1.00 27.17 ? 630 HOH A O    1 
HETATM 6066 O O    . HOH B 2 .   ? 11.062 5.324   12.426  1.00 18.60 ? 631 HOH A O    1 
HETATM 6067 O O    . HOH B 2 .   ? 36.325 -2.514  5.795   1.00 13.26 ? 632 HOH A O    1 
HETATM 6068 O O    . HOH B 2 .   ? 13.291 1.498   16.957  1.00 21.86 ? 633 HOH A O    1 
HETATM 6069 O O    . HOH B 2 .   ? 45.183 -8.124  -23.295 1.00 20.66 ? 634 HOH A O    1 
HETATM 6070 O O    . HOH B 2 .   ? 33.977 0.863   8.399   1.00 11.86 ? 635 HOH A O    1 
HETATM 6071 O O    . HOH B 2 .   ? 38.404 6.996   14.916  1.00 17.35 ? 636 HOH A O    1 
HETATM 6072 O O    . HOH B 2 .   ? 24.701 20.010  18.927  1.00 34.98 ? 637 HOH A O    1 
HETATM 6073 O O    . HOH B 2 .   ? 26.825 -10.128 2.529   1.00 20.92 ? 638 HOH A O    1 
HETATM 6074 O O    . HOH B 2 .   ? 32.808 23.860  -5.856  1.00 38.69 ? 639 HOH A O    1 
HETATM 6075 O O    . HOH B 2 .   ? 26.420 -14.760 12.557  1.00 45.25 ? 640 HOH A O    1 
HETATM 6076 O O    . HOH B 2 .   ? 41.071 -5.293  22.701  1.00 25.33 ? 641 HOH A O    1 
HETATM 6077 O O    . HOH B 2 .   ? 26.103 20.478  9.818   1.00 33.70 ? 642 HOH A O    1 
HETATM 6078 O O    . HOH B 2 .   ? 28.513 17.969  20.354  1.00 36.72 ? 643 HOH A O    1 
HETATM 6079 O O    . HOH B 2 .   ? 28.715 -6.025  2.900   1.00 16.60 ? 644 HOH A O    1 
HETATM 6080 O O    . HOH B 2 .   ? 22.899 -7.505  5.479   1.00 13.70 ? 645 HOH A O    1 
HETATM 6081 O O    . HOH B 2 .   ? 27.194 3.410   -21.544 1.00 19.04 ? 646 HOH A O    1 
HETATM 6082 O O    . HOH B 2 .   ? 43.669 -13.790 2.894   1.00 25.21 ? 647 HOH A O    1 
HETATM 6083 O O    . HOH B 2 .   ? 9.017  -2.049  15.299  1.00 26.50 ? 648 HOH A O    1 
HETATM 6084 O O    . HOH B 2 .   ? 24.834 10.548  -19.887 1.00 34.78 ? 649 HOH A O    1 
HETATM 6085 O O    . HOH B 2 .   ? 57.931 -2.474  -13.384 1.00 21.53 ? 650 HOH A O    1 
HETATM 6086 O O    . HOH B 2 .   ? 56.603 -14.518 -12.035 1.00 29.89 ? 651 HOH A O    1 
HETATM 6087 O O    . HOH B 2 .   ? 43.790 2.405   -23.742 1.00 25.55 ? 652 HOH A O    1 
HETATM 6088 O O    . HOH B 2 .   ? 38.955 9.719   14.411  1.00 31.55 ? 653 HOH A O    1 
HETATM 6089 O O    . HOH B 2 .   ? 49.790 -22.084 -5.836  1.00 32.67 ? 654 HOH A O    1 
HETATM 6090 O O    . HOH B 2 .   ? 12.487 17.887  5.187   1.00 28.20 ? 655 HOH A O    1 
HETATM 6091 O O    . HOH B 2 .   ? 38.108 -12.864 -22.526 1.00 27.40 ? 656 HOH A O    1 
HETATM 6092 O O    . HOH B 2 .   ? 47.311 -14.942 4.183   1.00 27.95 ? 657 HOH A O    1 
HETATM 6093 O O    . HOH B 2 .   ? 39.027 -3.120  -19.609 1.00 24.13 ? 658 HOH A O    1 
HETATM 6094 O O    . HOH B 2 .   ? 58.062 -13.807 -6.339  1.00 22.21 ? 659 HOH A O    1 
HETATM 6095 O O    . HOH B 2 .   ? 19.522 -3.539  -2.459  1.00 23.10 ? 660 HOH A O    1 
HETATM 6096 O O    . HOH B 2 .   ? 10.668 1.209   -10.029 1.00 26.62 ? 661 HOH A O    1 
HETATM 6097 O O    . HOH B 2 .   ? 23.248 -5.273  23.349  1.00 34.87 ? 662 HOH A O    1 
HETATM 6098 O O    . HOH B 2 .   ? 51.275 12.072  -4.842  1.00 43.13 ? 663 HOH A O    1 
HETATM 6099 O O    . HOH B 2 .   ? 35.557 11.552  -21.893 1.00 38.16 ? 664 HOH A O    1 
HETATM 6100 O O    . HOH B 2 .   ? 11.719 -4.792  -18.386 1.00 29.81 ? 665 HOH A O    1 
HETATM 6101 O O    . HOH B 2 .   ? 26.358 4.832   27.981  1.00 13.33 ? 666 HOH A O    1 
HETATM 6102 O O    . HOH B 2 .   ? 55.748 1.155   -8.772  1.00 23.83 ? 667 HOH A O    1 
HETATM 6103 O O    . HOH B 2 .   ? 14.945 -10.461 -13.847 1.00 35.99 ? 668 HOH A O    1 
HETATM 6104 O O    . HOH B 2 .   ? 25.305 7.113   29.070  1.00 19.55 ? 669 HOH A O    1 
HETATM 6105 O O    . HOH B 2 .   ? 4.461  6.164   10.950  1.00 41.46 ? 670 HOH A O    1 
HETATM 6106 O O    . HOH B 2 .   ? 20.859 -12.276 9.616   1.00 16.79 ? 671 HOH A O    1 
HETATM 6107 O O    . HOH B 2 .   ? 43.500 -1.695  -20.041 1.00 17.99 ? 672 HOH A O    1 
HETATM 6108 O O    . HOH B 2 .   ? 32.675 -8.213  2.026   1.00 19.55 ? 673 HOH A O    1 
HETATM 6109 O O    . HOH B 2 .   ? 42.898 8.293   -6.411  1.00 23.40 ? 674 HOH A O    1 
HETATM 6110 O O    . HOH B 2 .   ? 25.000 -15.245 3.817   1.00 27.81 ? 675 HOH A O    1 
HETATM 6111 O O    . HOH B 2 .   ? 49.733 11.544  -13.277 1.00 38.87 ? 676 HOH A O    1 
HETATM 6112 O O    . HOH B 2 .   ? 33.759 -4.437  -0.756  1.00 26.36 ? 677 HOH A O    1 
HETATM 6113 O O    . HOH B 2 .   ? 24.407 20.649  5.637   1.00 27.19 ? 678 HOH A O    1 
HETATM 6114 O O    . HOH B 2 .   ? 26.193 -8.762  13.504  1.00 22.43 ? 679 HOH A O    1 
HETATM 6115 O O    . HOH B 2 .   ? 45.457 2.599   15.692  1.00 20.57 ? 680 HOH A O    1 
HETATM 6116 O O    . HOH B 2 .   ? 32.546 -11.745 13.801  1.00 36.24 ? 681 HOH A O    1 
HETATM 6117 O O    . HOH B 2 .   ? 38.876 -15.393 -14.517 1.00 37.01 ? 682 HOH A O    1 
HETATM 6118 O O    . HOH B 2 .   ? 20.726 -6.058  17.744  1.00 35.89 ? 683 HOH A O    1 
HETATM 6119 O O    . HOH B 2 .   ? 57.116 -1.053  -5.926  1.00 24.43 ? 684 HOH A O    1 
HETATM 6120 O O    . HOH B 2 .   ? 44.019 -5.893  20.308  1.00 40.15 ? 685 HOH A O    1 
HETATM 6121 O O    . HOH B 2 .   ? 18.375 -2.787  -18.585 1.00 39.64 ? 686 HOH A O    1 
HETATM 6122 O O    . HOH B 2 .   ? 52.071 8.361   -10.001 1.00 31.32 ? 687 HOH A O    1 
HETATM 6123 O O    . HOH B 2 .   ? 53.938 -13.951 -18.643 1.00 20.21 ? 688 HOH A O    1 
HETATM 6124 O O    . HOH B 2 .   ? 62.628 -19.918 -3.886  1.00 31.88 ? 689 HOH A O    1 
HETATM 6125 O O    . HOH B 2 .   ? 49.203 4.439   11.131  1.00 33.17 ? 690 HOH A O    1 
HETATM 6126 O O    . HOH B 2 .   ? 34.762 -8.040  8.989   1.00 17.45 ? 691 HOH A O    1 
HETATM 6127 O O    . HOH B 2 .   ? 35.019 0.796   11.124  1.00 13.73 ? 692 HOH A O    1 
HETATM 6128 O O    . HOH B 2 .   ? 21.645 10.963  26.515  1.00 21.93 ? 693 HOH A O    1 
HETATM 6129 O O    . HOH B 2 .   ? 18.213 -17.392 9.188   1.00 32.97 ? 694 HOH A O    1 
HETATM 6130 O O    . HOH B 2 .   ? 29.606 -1.412  -25.791 1.00 44.03 ? 695 HOH A O    1 
HETATM 6131 O O    . HOH B 2 .   ? 30.271 15.216  15.408  1.00 27.71 ? 696 HOH A O    1 
HETATM 6132 O O    . HOH B 2 .   ? 16.758 8.313   -3.344  1.00 24.94 ? 697 HOH A O    1 
HETATM 6133 O O    . HOH B 2 .   ? 6.824  -10.163 6.518   1.00 46.64 ? 698 HOH A O    1 
HETATM 6134 O O    . HOH B 2 .   ? 15.522 14.134  -0.556  1.00 40.95 ? 699 HOH A O    1 
HETATM 6135 O O    . HOH B 2 .   ? 37.771 -14.832 11.151  1.00 33.42 ? 700 HOH A O    1 
HETATM 6136 O O    . HOH B 2 .   ? 6.769  11.430  16.532  1.00 36.94 ? 701 HOH A O    1 
HETATM 6137 O O    . HOH B 2 .   ? 41.153 -3.483  -19.950 1.00 27.57 ? 702 HOH A O    1 
HETATM 6138 O O    . HOH B 2 .   ? 22.083 17.885  17.661  1.00 29.66 ? 703 HOH A O    1 
HETATM 6139 O O    . HOH B 2 .   ? 29.550 15.120  22.687  1.00 26.51 ? 704 HOH A O    1 
HETATM 6140 O O    . HOH B 2 .   ? 58.987 -0.033  -4.320  1.00 30.11 ? 705 HOH A O    1 
HETATM 6141 O O    . HOH B 2 .   ? 36.326 -2.926  23.922  1.00 19.86 ? 706 HOH A O    1 
HETATM 6142 O O    . HOH B 2 .   ? 21.688 20.070  19.202  1.00 40.09 ? 707 HOH A O    1 
HETATM 6143 O O    . HOH B 2 .   ? 29.532 -12.314 13.772  1.00 39.39 ? 708 HOH A O    1 
HETATM 6144 O O    . HOH B 2 .   ? 35.837 15.893  -8.679  1.00 28.64 ? 709 HOH A O    1 
HETATM 6145 O O    . HOH B 2 .   ? 29.290 12.270  18.635  1.00 16.39 ? 710 HOH A O    1 
HETATM 6146 O O    . HOH B 2 .   ? 8.834  -1.826  5.613   1.00 39.88 ? 711 HOH A O    1 
HETATM 6147 O O    . HOH B 2 .   ? 29.106 -4.016  22.829  1.00 19.19 ? 712 HOH A O    1 
HETATM 6148 O O    . HOH B 2 .   ? 49.277 -8.278  -23.440 1.00 15.99 ? 713 HOH A O    1 
HETATM 6149 O O    . HOH B 2 .   ? 28.573 -16.809 11.155  1.00 40.29 ? 714 HOH A O    1 
HETATM 6150 O O    . HOH B 2 .   ? 8.321  -0.249  -1.160  1.00 31.64 ? 715 HOH A O    1 
HETATM 6151 O O    . HOH B 2 .   ? 17.153 12.909  -17.252 1.00 35.40 ? 716 HOH A O    1 
HETATM 6152 O O    . HOH B 2 .   ? 12.722 13.951  21.113  1.00 36.25 ? 717 HOH A O    1 
HETATM 6153 O O    . HOH B 2 .   ? 47.637 -18.725 -1.240  1.00 25.65 ? 718 HOH A O    1 
HETATM 6154 O O    . HOH B 2 .   ? 7.920  9.434   15.205  1.00 24.68 ? 719 HOH A O    1 
HETATM 6155 O O    . HOH B 2 .   ? 57.376 -15.636 -0.865  1.00 28.68 ? 720 HOH A O    1 
HETATM 6156 O O    . HOH B 2 .   ? 31.545 -13.909 -22.865 1.00 42.25 ? 721 HOH A O    1 
HETATM 6157 O O    . HOH B 2 .   ? 17.273 11.248  -5.659  1.00 39.98 ? 722 HOH A O    1 
HETATM 6158 O O    . HOH B 2 .   ? 6.997  13.432  6.657   1.00 27.59 ? 723 HOH A O    1 
HETATM 6159 O O    . HOH B 2 .   ? 38.171 -9.065  24.462  1.00 45.29 ? 724 HOH A O    1 
HETATM 6160 O O    . HOH B 2 .   ? 19.116 20.132  1.608   1.00 21.57 ? 725 HOH A O    1 
HETATM 6161 O O    . HOH B 2 .   ? 18.240 1.172   25.946  1.00 41.49 ? 726 HOH A O    1 
HETATM 6162 O O    . HOH B 2 .   ? 18.522 -11.137 10.452  1.00 19.78 ? 727 HOH A O    1 
HETATM 6163 O O    . HOH B 2 .   ? 62.842 -15.399 2.201   1.00 20.56 ? 728 HOH A O    1 
HETATM 6164 O O    . HOH B 2 .   ? 9.125  0.860   6.962   1.00 27.14 ? 729 HOH A O    1 
HETATM 6165 O O    . HOH B 2 .   ? 35.141 -7.295  23.892  1.00 34.15 ? 730 HOH A O    1 
HETATM 6166 O O    . HOH B 2 .   ? 6.277  -10.227 10.523  1.00 24.49 ? 731 HOH A O    1 
HETATM 6167 O O    . HOH B 2 .   ? 18.237 10.002  -1.548  1.00 18.92 ? 732 HOH A O    1 
HETATM 6168 O O    . HOH B 2 .   ? 7.361  6.459   13.418  1.00 44.46 ? 733 HOH A O    1 
HETATM 6169 O O    . HOH B 2 .   ? 22.335 7.387   -21.764 1.00 33.90 ? 734 HOH A O    1 
HETATM 6170 O O    . HOH B 2 .   ? 34.668 15.689  14.529  1.00 38.40 ? 735 HOH A O    1 
HETATM 6171 O O    . HOH B 2 .   ? 26.973 -9.065  -1.292  1.00 18.03 ? 736 HOH A O    1 
HETATM 6172 O O    . HOH B 2 .   ? 40.934 10.222  -17.759 1.00 42.15 ? 737 HOH A O    1 
HETATM 6173 O O    . HOH B 2 .   ? 33.900 11.260  -17.943 1.00 20.42 ? 738 HOH A O    1 
HETATM 6174 O O    . HOH B 2 .   ? 19.203 20.335  -2.638  1.00 42.52 ? 739 HOH A O    1 
HETATM 6175 O O    . HOH B 2 .   ? 37.765 16.451  -7.367  1.00 33.37 ? 740 HOH A O    1 
HETATM 6176 O O    . HOH B 2 .   ? 16.450 -15.816 -5.478  1.00 38.72 ? 741 HOH A O    1 
HETATM 6177 O O    . HOH B 2 .   ? 29.308 -14.561 -18.850 1.00 42.80 ? 742 HOH A O    1 
HETATM 6178 O O    . HOH B 2 .   ? 9.913  -3.920  -15.739 1.00 23.68 ? 743 HOH A O    1 
HETATM 6179 O O    . HOH B 2 .   ? 6.940  -1.745  13.355  1.00 32.90 ? 744 HOH A O    1 
HETATM 6180 O O    . HOH B 2 .   ? 59.749 -24.971 -1.005  1.00 44.20 ? 745 HOH A O    1 
HETATM 6181 O O    . HOH B 2 .   ? 39.788 8.665   12.989  1.00 31.59 ? 746 HOH A O    1 
HETATM 6182 O O    . HOH B 2 .   ? 18.469 10.520  -8.253  1.00 35.29 ? 747 HOH A O    1 
HETATM 6183 O O    . HOH B 2 .   ? 24.119 -7.165  14.102  1.00 35.57 ? 748 HOH A O    1 
HETATM 6184 O O    . HOH B 2 .   ? 28.143 -16.748 -13.884 1.00 20.49 ? 749 HOH A O    1 
HETATM 6185 O O    . HOH B 2 .   ? 18.597 3.181   27.359  1.00 36.39 ? 750 HOH A O    1 
HETATM 6186 O O    . HOH B 2 .   ? 27.174 -7.608  19.209  1.00 38.66 ? 751 HOH A O    1 
HETATM 6187 O O    . HOH B 2 .   ? 13.916 8.359   23.104  1.00 38.55 ? 752 HOH A O    1 
HETATM 6188 O O    . HOH B 2 .   ? 50.575 -17.081 -22.537 1.00 47.46 ? 753 HOH A O    1 
HETATM 6189 O O    . HOH B 2 .   ? 30.240 16.238  -13.472 1.00 37.84 ? 754 HOH A O    1 
HETATM 6190 O O    . HOH B 2 .   ? 12.335 -7.622  -10.774 1.00 41.04 ? 755 HOH A O    1 
HETATM 6191 O O    . HOH B 2 .   ? 25.532 19.784  12.366  1.00 27.24 ? 756 HOH A O    1 
HETATM 6192 O O    . HOH B 2 .   ? 10.384 16.074  2.973   1.00 45.26 ? 757 HOH A O    1 
HETATM 6193 O O    . HOH B 2 .   ? 19.667 9.340   27.054  1.00 23.71 ? 758 HOH A O    1 
HETATM 6194 O O    . HOH B 2 .   ? 22.942 7.904   30.326  1.00 27.20 ? 759 HOH A O    1 
HETATM 6195 O O    . HOH B 2 .   ? 25.255 7.000   -24.413 1.00 38.81 ? 760 HOH A O    1 
HETATM 6196 O O    . HOH B 2 .   ? 9.153  -9.176  17.514  1.00 41.98 ? 761 HOH A O    1 
HETATM 6197 O O    . HOH B 2 .   ? 16.030 -0.030  17.597  1.00 20.91 ? 762 HOH A O    1 
HETATM 6198 O O    . HOH B 2 .   ? 14.665 26.221  7.115   1.00 38.84 ? 763 HOH A O    1 
HETATM 6199 O O    . HOH B 2 .   ? 14.723 -13.220 -7.174  1.00 44.87 ? 764 HOH A O    1 
HETATM 6200 O O    . HOH B 2 .   ? 24.661 24.429  15.797  1.00 49.77 ? 765 HOH A O    1 
HETATM 6201 O O    . HOH B 2 .   ? 51.485 -25.647 -10.136 1.00 39.75 ? 766 HOH A O    1 
HETATM 6202 O O    . HOH B 2 .   ? 38.688 14.903  -17.727 1.00 40.98 ? 767 HOH A O    1 
HETATM 6203 O O    . HOH B 2 .   ? 60.074 -0.838  -1.026  1.00 45.26 ? 768 HOH A O    1 
HETATM 6204 O O    . HOH B 2 .   ? 20.685 16.432  20.517  1.00 30.06 ? 769 HOH A O    1 
HETATM 6205 O O    . HOH B 2 .   ? 14.280 2.008   21.264  1.00 41.30 ? 770 HOH A O    1 
HETATM 6206 O O    . HOH B 2 .   ? 62.143 -21.107 -2.356  1.00 38.12 ? 771 HOH A O    1 
HETATM 6207 O O    . HOH B 2 .   ? 12.680 21.398  6.925   1.00 36.35 ? 772 HOH A O    1 
HETATM 6208 O O    . HOH B 2 .   ? 30.773 11.201  -18.394 1.00 25.18 ? 773 HOH A O    1 
HETATM 6209 O O    . HOH B 2 .   ? 37.821 -7.160  -1.962  1.00 16.30 ? 774 HOH A O    1 
HETATM 6210 O O    . HOH B 2 .   ? 41.460 10.450  13.918  1.00 44.19 ? 775 HOH A O    1 
HETATM 6211 O O    . HOH B 2 .   ? 61.342 -3.692  2.658   1.00 40.15 ? 776 HOH A O    1 
HETATM 6212 O O    . HOH B 2 .   ? 30.261 -9.049  15.173  1.00 31.18 ? 777 HOH A O    1 
HETATM 6213 O O    . HOH B 2 .   ? 21.891 -14.099 -22.280 1.00 18.53 ? 778 HOH A O    1 
HETATM 6214 O O    . HOH B 2 .   ? 20.194 13.174  -1.565  1.00 20.18 ? 779 HOH A O    1 
HETATM 6215 O O    . HOH B 2 .   ? 18.845 -5.006  20.300  1.00 37.62 ? 780 HOH A O    1 
HETATM 6216 O O    . HOH B 2 .   ? 39.140 -4.512  1.505   1.00 6.52  ? 781 HOH A O    1 
HETATM 6217 O O    . HOH B 2 .   ? 34.491 9.232   20.497  1.00 15.83 ? 782 HOH A O    1 
HETATM 6218 O O    . HOH B 2 .   ? 12.086 4.453   -6.623  1.00 39.59 ? 783 HOH A O    1 
HETATM 6219 O O    . HOH B 2 .   ? 8.848  1.812   -12.103 1.00 33.65 ? 784 HOH A O    1 
HETATM 6220 O O    . HOH B 2 .   ? 26.214 -10.880 15.109  1.00 41.95 ? 785 HOH A O    1 
HETATM 6221 O O    . HOH B 2 .   ? 8.527  14.279  3.051   1.00 40.69 ? 786 HOH A O    1 
HETATM 6222 O O    . HOH B 2 .   ? 40.466 -14.331 -13.913 1.00 44.09 ? 787 HOH A O    1 
HETATM 6223 O O    . HOH B 2 .   ? 24.309 22.596  11.918  1.00 45.30 ? 788 HOH A O    1 
HETATM 6224 O O    . HOH B 2 .   ? 50.889 -0.196  9.919   1.00 37.86 ? 789 HOH A O    1 
HETATM 6225 O O    . HOH B 2 .   ? 14.069 -0.293  20.012  1.00 36.20 ? 790 HOH A O    1 
HETATM 6226 O O    . HOH B 2 .   ? 17.897 -12.766 12.814  1.00 38.84 ? 791 HOH A O    1 
HETATM 6227 O O    . HOH B 2 .   ? 8.149  2.420   10.010  1.00 30.95 ? 792 HOH A O    1 
HETATM 6228 O O    . HOH B 2 .   ? 14.489 9.358   -11.217 1.00 33.03 ? 793 HOH A O    1 
HETATM 6229 O O    . HOH B 2 .   ? 40.848 -7.680  -24.645 1.00 32.71 ? 794 HOH A O    1 
HETATM 6230 O O    . HOH B 2 .   ? 50.988 10.763  -10.498 1.00 34.88 ? 795 HOH A O    1 
HETATM 6231 O O    . HOH B 2 .   ? 42.328 8.805   15.813  1.00 44.46 ? 796 HOH A O    1 
HETATM 6232 O O    . HOH B 2 .   ? 36.974 -9.936  -0.665  1.00 28.68 ? 797 HOH A O    1 
HETATM 6233 O O    . HOH B 2 .   ? 47.138 12.990  -2.102  1.00 40.97 ? 798 HOH A O    1 
HETATM 6234 O O    . HOH B 2 .   ? 17.720 -3.949  15.664  1.00 19.99 ? 799 HOH A O    1 
HETATM 6235 O O    . HOH B 2 .   ? 14.138 8.562   -1.850  1.00 34.94 ? 800 HOH A O    1 
HETATM 6236 O O    . HOH B 2 .   ? 23.324 21.687  3.601   1.00 40.02 ? 801 HOH A O    1 
HETATM 6237 O O    . HOH B 2 .   ? 8.252  7.387   16.913  1.00 39.64 ? 802 HOH A O    1 
HETATM 6238 O O    . HOH B 2 .   ? 11.844 3.482   -3.920  1.00 36.65 ? 803 HOH A O    1 
HETATM 6239 O O    . HOH B 2 .   ? 51.568 5.036   4.063   1.00 34.72 ? 804 HOH A O    1 
HETATM 6240 O O    . HOH B 2 .   ? 13.413 19.923  4.841   1.00 43.40 ? 805 HOH A O    1 
HETATM 6241 O O    . HOH B 2 .   ? 46.333 12.808  -15.844 1.00 38.79 ? 806 HOH A O    1 
HETATM 6242 O O    . HOH B 2 .   ? 26.519 7.660   31.191  1.00 37.65 ? 807 HOH A O    1 
HETATM 6243 O O    . HOH B 2 .   ? 53.094 8.084   -5.222  1.00 29.14 ? 808 HOH A O    1 
HETATM 6244 O O    . HOH B 2 .   ? 51.747 -21.292 -1.076  1.00 47.89 ? 809 HOH A O    1 
HETATM 6245 O O    . HOH B 2 .   ? 20.038 12.399  -8.662  1.00 25.80 ? 810 HOH A O    1 
HETATM 6246 O O    . HOH B 2 .   ? 55.869 3.086   -8.854  1.00 41.66 ? 811 HOH A O    1 
HETATM 6247 O O    . HOH B 2 .   ? 65.734 -6.118  2.178   1.00 36.21 ? 812 HOH A O    1 
HETATM 6248 O O    . HOH B 2 .   ? 17.755 1.060   -0.486  1.00 21.66 ? 813 HOH A O    1 
HETATM 6249 O O    . HOH B 2 .   ? 40.100 -14.920 -22.450 1.00 38.36 ? 814 HOH A O    1 
HETATM 6250 O O    . HOH B 2 .   ? 9.342  -6.074  -14.116 1.00 39.38 ? 815 HOH A O    1 
HETATM 6251 O O    . HOH B 2 .   ? 38.701 1.528   22.022  1.00 29.22 ? 816 HOH A O    1 
HETATM 6252 O O    . HOH B 2 .   ? 39.890 7.282   17.289  1.00 42.00 ? 817 HOH A O    1 
HETATM 6253 O O    . HOH B 2 .   ? 26.137 -0.330  -24.051 1.00 39.70 ? 818 HOH A O    1 
HETATM 6254 O O    . HOH B 2 .   ? 24.202 -17.154 -8.605  1.00 27.95 ? 819 HOH A O    1 
HETATM 6255 O O    . HOH B 2 .   ? 36.258 -10.122 22.248  1.00 37.82 ? 820 HOH A O    1 
HETATM 6256 O O    . HOH B 2 .   ? 23.797 -15.741 -3.907  1.00 27.87 ? 821 HOH A O    1 
HETATM 6257 O O    . HOH B 2 .   ? 14.861 -11.081 -11.613 1.00 40.68 ? 822 HOH A O    1 
HETATM 6258 O O    . HOH B 2 .   ? 36.089 -16.041 12.480  1.00 49.26 ? 823 HOH A O    1 
HETATM 6259 O O    . HOH B 2 .   ? 14.937 1.884   23.818  1.00 45.77 ? 824 HOH A O    1 
HETATM 6260 O O    . HOH B 2 .   ? 21.241 -16.055 -4.849  1.00 22.97 ? 825 HOH A O    1 
HETATM 6261 O O    . HOH B 2 .   ? 55.864 -24.940 -0.702  1.00 40.17 ? 826 HOH A O    1 
HETATM 6262 O O    . HOH B 2 .   ? 41.959 -15.567 -15.722 1.00 45.30 ? 827 HOH A O    1 
HETATM 6263 O O    . HOH B 2 .   ? 18.677 17.035  -4.711  1.00 37.58 ? 828 HOH A O    1 
HETATM 6264 O O    . HOH B 2 .   ? 11.336 3.537   -8.387  1.00 35.58 ? 829 HOH A O    1 
HETATM 6265 O O    . HOH B 2 .   ? 40.187 5.040   20.807  1.00 39.74 ? 830 HOH A O    1 
HETATM 6266 O O    . HOH B 2 .   ? 52.355 5.957   -19.917 1.00 45.65 ? 831 HOH A O    1 
HETATM 6267 O O    . HOH B 2 .   ? 53.489 9.176   -7.416  1.00 33.85 ? 832 HOH A O    1 
HETATM 6268 O O    . HOH B 2 .   ? 63.638 -4.719  -0.322  1.00 50.10 ? 833 HOH A O    1 
HETATM 6269 O O    . HOH B 2 .   ? 62.443 -23.340 -1.214  1.00 27.38 ? 834 HOH A O    1 
HETATM 6270 O O    . HOH B 2 .   ? 52.397 -6.556  10.240  1.00 38.73 ? 835 HOH A O    1 
HETATM 6271 O O    . HOH B 2 .   ? 37.089 -14.993 8.520   1.00 41.84 ? 836 HOH A O    1 
HETATM 6272 O O    . HOH B 2 .   ? 6.990  12.854  9.678   1.00 27.78 ? 837 HOH A O    1 
HETATM 6273 O O    . HOH B 2 .   ? 44.490 -17.635 -17.786 1.00 31.45 ? 838 HOH A O    1 
HETATM 6274 O O    . HOH B 2 .   ? 22.952 3.715   29.705  1.00 34.79 ? 839 HOH A O    1 
HETATM 6275 O O    . HOH B 2 .   ? 33.912 -17.179 -16.478 1.00 43.99 ? 840 HOH A O    1 
HETATM 6276 O O    . HOH B 2 .   ? 58.962 -3.700  -7.324  1.00 43.04 ? 841 HOH A O    1 
HETATM 6277 O O    . HOH B 2 .   ? 19.099 14.030  -4.075  1.00 32.41 ? 842 HOH A O    1 
HETATM 6278 O O    . HOH B 2 .   ? 39.286 2.875   24.473  1.00 26.55 ? 843 HOH A O    1 
HETATM 6279 O O    . HOH B 2 .   ? 59.684 -18.786 1.358   1.00 37.92 ? 844 HOH A O    1 
HETATM 6280 O O    . HOH B 2 .   ? 57.368 -5.707  -14.823 1.00 26.74 ? 845 HOH A O    1 
HETATM 6281 O O    . HOH B 2 .   ? 8.267  1.359   -3.415  1.00 48.55 ? 846 HOH A O    1 
HETATM 6282 O O    . HOH B 2 .   ? 27.218 -7.606  1.230   1.00 23.41 ? 847 HOH A O    1 
HETATM 6283 O O    . HOH B 2 .   ? 33.013 -8.441  22.851  1.00 47.89 ? 848 HOH A O    1 
HETATM 6284 O O    . HOH B 2 .   ? 14.741 11.804  21.005  1.00 27.29 ? 849 HOH A O    1 
HETATM 6285 O O    . HOH B 2 .   ? 16.339 -12.629 15.231  1.00 48.53 ? 850 HOH A O    1 
HETATM 6286 O O    . HOH B 2 .   ? 58.866 -5.078  -12.431 1.00 30.74 ? 851 HOH A O    1 
HETATM 6287 O O    . HOH B 2 .   ? 50.613 -16.320 -24.811 1.00 45.10 ? 852 HOH A O    1 
HETATM 6288 O O    . HOH B 2 .   ? 37.505 5.336   20.838  1.00 23.41 ? 853 HOH A O    1 
HETATM 6289 O O    . HOH B 2 .   ? 17.775 15.705  20.515  1.00 36.77 ? 854 HOH A O    1 
HETATM 6290 O O    . HOH B 2 .   ? 16.158 -4.336  19.609  1.00 34.19 ? 855 HOH A O    1 
HETATM 6291 O O    . HOH B 2 .   ? 19.811 2.335   -25.517 1.00 40.97 ? 856 HOH A O    1 
HETATM 6292 O O    . HOH B 2 .   ? 9.527  0.256   16.033  1.00 41.59 ? 857 HOH A O    1 
HETATM 6293 O O    . HOH B 2 .   ? 44.927 0.977   18.239  1.00 28.11 ? 858 HOH A O    1 
HETATM 6294 O O    . HOH B 2 .   ? 10.200 18.663  4.256   1.00 45.61 ? 859 HOH A O    1 
HETATM 6295 O O    . HOH B 2 .   ? 17.054 27.731  7.732   1.00 30.41 ? 860 HOH A O    1 
HETATM 6296 O O    . HOH B 2 .   ? 21.808 20.699  1.228   1.00 37.48 ? 861 HOH A O    1 
HETATM 6297 O O    . HOH B 2 .   ? 39.196 1.321   -25.706 1.00 38.63 ? 862 HOH A O    1 
HETATM 6298 O O    . HOH B 2 .   ? 7.662  -11.815 18.762  1.00 39.10 ? 863 HOH A O    1 
HETATM 6299 O O    . HOH B 2 .   ? 43.739 -9.281  14.490  1.00 46.55 ? 864 HOH A O    1 
HETATM 6300 O O    . HOH B 2 .   ? 40.988 -17.563 -19.706 1.00 50.12 ? 865 HOH A O    1 
HETATM 6301 O O    . HOH B 2 .   ? 15.707 6.604   27.242  1.00 43.41 ? 866 HOH A O    1 
HETATM 6302 O O    . HOH B 2 .   ? 14.442 -10.063 -7.720  1.00 29.51 ? 867 HOH A O    1 
HETATM 6303 O O    . HOH B 2 .   ? 35.276 13.508  18.284  1.00 30.83 ? 868 HOH A O    1 
HETATM 6304 O O    . HOH B 2 .   ? 16.537 -13.235 -12.079 1.00 32.04 ? 869 HOH A O    1 
HETATM 6305 O O    . HOH B 2 .   ? 56.473 0.329   3.770   1.00 30.86 ? 870 HOH A O    1 
HETATM 6306 O O    . HOH B 2 .   ? 25.325 -14.186 15.163  1.00 50.11 ? 871 HOH A O    1 
HETATM 6307 O O    . HOH B 2 .   ? 16.449 -13.657 -17.222 1.00 29.79 ? 872 HOH A O    1 
HETATM 6308 O O    . HOH B 2 .   ? 38.350 -1.112  23.170  1.00 24.99 ? 873 HOH A O    1 
HETATM 6309 O O    . HOH B 2 .   ? 54.721 6.538   -1.982  1.00 39.53 ? 874 HOH A O    1 
HETATM 6310 O O    . HOH B 2 .   ? 57.683 0.659   -12.296 1.00 41.81 ? 875 HOH A O    1 
HETATM 6311 O O    . HOH B 2 .   ? 57.644 -2.477  5.364   1.00 28.59 ? 876 HOH A O    1 
HETATM 6312 O O    . HOH B 2 .   ? 27.795 2.651   -24.079 1.00 29.97 ? 877 HOH A O    1 
HETATM 6313 O O    . HOH B 2 .   ? 47.351 -6.386  -23.312 1.00 20.78 ? 878 HOH A O    1 
HETATM 6314 O O    . HOH B 2 .   ? 40.136 8.677   -22.690 1.00 43.90 ? 879 HOH A O    1 
HETATM 6315 O O    . HOH B 2 .   ? 19.946 -15.417 -13.395 1.00 39.51 ? 880 HOH A O    1 
HETATM 6316 O O    . HOH B 2 .   ? 33.847 11.927  19.989  1.00 18.36 ? 881 HOH A O    1 
HETATM 6317 O O    . HOH B 2 .   ? 22.420 25.584  11.040  1.00 47.61 ? 882 HOH A O    1 
HETATM 6318 O O    . HOH B 2 .   ? 47.548 12.559  0.664   1.00 44.94 ? 883 HOH A O    1 
HETATM 6319 O O    . HOH B 2 .   ? 21.368 -14.573 11.038  1.00 30.71 ? 884 HOH A O    1 
HETATM 6320 O O    . HOH B 2 .   ? 28.890 -2.738  25.469  1.00 35.09 ? 885 HOH A O    1 
HETATM 6321 O O    . HOH B 2 .   ? 17.529 2.062   -22.050 1.00 25.88 ? 886 HOH A O    1 
HETATM 6322 O O    . HOH B 2 .   ? 55.420 -5.140  7.311   1.00 22.92 ? 887 HOH A O    1 
HETATM 6323 O O    . HOH B 2 .   ? 36.953 16.625  14.916  1.00 46.98 ? 888 HOH A O    1 
HETATM 6324 O O    . HOH B 2 .   ? 42.414 -4.390  -22.889 1.00 27.27 ? 889 HOH A O    1 
HETATM 6325 O O    . HOH B 2 .   ? 21.061 24.207  7.630   1.00 45.15 ? 890 HOH A O    1 
HETATM 6326 O O    . HOH B 2 .   ? 10.557 3.804   18.611  1.00 37.42 ? 891 HOH A O    1 
HETATM 6327 O O    . HOH B 2 .   ? 41.006 -12.897 3.013   1.00 29.65 ? 892 HOH A O    1 
HETATM 6328 O O    . HOH B 2 .   ? 10.859 -13.480 5.583   1.00 50.67 ? 893 HOH A O    1 
HETATM 6329 O O    . HOH B 2 .   ? 36.675 -16.958 -14.145 1.00 44.96 ? 894 HOH A O    1 
HETATM 6330 O O    . HOH B 2 .   ? 14.571 5.754   24.687  1.00 42.18 ? 895 HOH A O    1 
HETATM 6331 O O    . HOH B 2 .   ? 25.738 22.464  3.779   1.00 45.16 ? 896 HOH A O    1 
HETATM 6332 O O    . HOH B 2 .   ? 30.694 3.472   -24.495 1.00 37.47 ? 897 HOH A O    1 
HETATM 6333 O O    . HOH B 2 .   ? 55.917 5.009   3.767   1.00 30.94 ? 898 HOH A O    1 
HETATM 6334 O O    . HOH B 2 .   ? 16.277 -1.734  25.894  1.00 43.73 ? 899 HOH A O    1 
HETATM 6335 O O    . HOH B 2 .   ? 17.830 -20.531 9.020   1.00 35.97 ? 900 HOH A O    1 
HETATM 6336 O O    . HOH B 2 .   ? 18.429 5.487   28.543  1.00 39.31 ? 901 HOH A O    1 
HETATM 6337 O O    . HOH B 2 .   ? 12.417 27.060  8.448   1.00 34.64 ? 902 HOH A O    1 
HETATM 6338 O O    . HOH B 2 .   ? 37.375 12.186  -19.893 1.00 40.33 ? 903 HOH A O    1 
HETATM 6339 O O    . HOH B 2 .   ? 47.485 -17.720 -14.824 1.00 30.27 ? 904 HOH A O    1 
HETATM 6340 O O    . HOH B 2 .   ? 14.955 -6.116  17.975  1.00 40.92 ? 905 HOH A O    1 
HETATM 6341 O O    . HOH B 2 .   ? 51.300 -2.517  10.947  1.00 37.59 ? 906 HOH A O    1 
HETATM 6342 O O    . HOH B 2 .   ? 12.036 -9.774  -12.787 1.00 46.44 ? 907 HOH A O    1 
HETATM 6343 O O    . HOH B 2 .   ? 44.926 -17.569 -13.485 1.00 38.65 ? 908 HOH A O    1 
HETATM 6344 O O    . HOH B 2 .   ? 7.621  13.131  20.933  1.00 44.56 ? 909 HOH A O    1 
HETATM 6345 O O    . HOH B 2 .   ? 50.594 -20.282 -16.367 1.00 38.98 ? 910 HOH A O    1 
HETATM 6346 O O    . HOH B 2 .   ? 12.462 -10.330 -15.523 1.00 43.89 ? 911 HOH A O    1 
HETATM 6347 O O    . HOH B 2 .   ? 17.256 -2.168  28.014  1.00 46.60 ? 912 HOH A O    1 
HETATM 6348 O O    . HOH B 2 .   ? 17.280 -0.724  -21.921 1.00 38.30 ? 913 HOH A O    1 
HETATM 6349 O O    . HOH B 2 .   ? 43.877 -19.092 -15.284 1.00 41.53 ? 914 HOH A O    1 
HETATM 6350 O O    . HOH B 2 .   ? 16.022 2.668   -24.225 1.00 47.41 ? 915 HOH A O    1 
HETATM 6351 O O    . HOH B 2 .   ? 41.590 -21.985 -18.457 1.00 50.55 ? 916 HOH A O    1 
HETATM 6352 O O    . HOH B 2 .   ? 42.224 -24.378 -17.634 0.33 42.70 ? 917 HOH A 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   . ILE A 23  ? 0.6866 0.5429 0.8256 -0.1163 0.0670  -0.1001 23  ILE A N   
2    C CA  . ILE A 23  ? 0.6675 0.5303 0.7968 -0.1100 0.0650  -0.0889 23  ILE A CA  
3    C C   . ILE A 23  ? 0.6994 0.5293 0.8051 -0.1054 0.0774  -0.0691 23  ILE A C   
4    O O   . ILE A 23  ? 0.6931 0.4963 0.7822 -0.0997 0.0798  -0.0630 23  ILE A O   
5    C CB  . ILE A 23  ? 0.6665 0.5458 0.7905 -0.0994 0.0476  -0.0931 23  ILE A CB  
6    C CG1 . ILE A 23  ? 0.6525 0.5681 0.7966 -0.1009 0.0350  -0.1104 23  ILE A CG1 
7    C CG2 . ILE A 23  ? 0.6307 0.5114 0.7408 -0.0916 0.0464  -0.0793 23  ILE A CG2 
8    C CD1 . ILE A 23  ? 0.6560 0.5758 0.8013 -0.0973 0.0246  -0.1232 23  ILE A CD1 
19   N N   . ASP A 24  ? 0.6318 0.4650 0.7351 -0.1066 0.0849  -0.0594 24  ASP A N   
20   C CA  . ASP A 24  ? 0.6127 0.4201 0.6906 -0.0990 0.0945  -0.0397 24  ASP A CA  
21   C C   . ASP A 24  ? 0.5827 0.3933 0.6440 -0.0856 0.0834  -0.0322 24  ASP A C   
22   O O   . ASP A 24  ? 0.5460 0.3856 0.6126 -0.0824 0.0737  -0.0336 24  ASP A O   
23   C CB  . ASP A 24  ? 0.6138 0.4269 0.6956 -0.1050 0.1066  -0.0335 24  ASP A CB  
24   C CG  . ASP A 24  ? 0.6683 0.4576 0.7213 -0.0950 0.1157  -0.0132 24  ASP A CG  
25   O OD1 . ASP A 24  ? 0.6633 0.4306 0.6941 -0.0835 0.1134  -0.0042 24  ASP A OD1 
26   O OD2 . ASP A 24  ? 0.7406 0.5347 0.7926 -0.0972 0.1245  -0.0069 24  ASP A OD2 
31   N N   . TYR A 25  ? 0.5376 0.3257 0.5762 -0.0737 0.0819  -0.0228 25  TYR A N   
32   C CA  . TYR A 25  ? 0.4832 0.2822 0.5043 -0.0571 0.0686  -0.0150 25  TYR A CA  
33   C C   . TYR A 25  ? 0.4711 0.2571 0.4683 -0.0461 0.0741  0.0027  25  TYR A C   
34   O O   . TYR A 25  ? 0.4514 0.2457 0.4348 -0.0325 0.0639  0.0086  25  TYR A O   
35   C CB  . TYR A 25  ? 0.4894 0.2795 0.5036 -0.0493 0.0605  -0.0191 25  TYR A CB  
36   C CG  . TYR A 25  ? 0.4780 0.2849 0.5120 -0.0564 0.0517  -0.0371 25  TYR A CG  
37   C CD1 . TYR A 25  ? 0.4532 0.2921 0.4947 -0.0531 0.0378  -0.0436 25  TYR A CD1 
38   C CD2 . TYR A 25  ? 0.5525 0.3425 0.5966 -0.0655 0.0574  -0.0480 25  TYR A CD2 
39   C CE1 . TYR A 25  ? 0.4661 0.3205 0.5225 -0.0571 0.0291  -0.0599 25  TYR A CE1 
40   C CE2 . TYR A 25  ? 0.5502 0.3576 0.6117 -0.0708 0.0482  -0.0660 25  TYR A CE2 
41   C CZ  . TYR A 25  ? 0.5187 0.3588 0.5852 -0.0657 0.0337  -0.0716 25  TYR A CZ  
42   O OH  . TYR A 25  ? 0.5998 0.4571 0.6806 -0.0686 0.0240  -0.0893 25  TYR A OH  
52   N N   . SER A 26  ? 0.4650 0.2324 0.4573 -0.0516 0.0900  0.0106  26  SER A N   
53   C CA  . SER A 26  ? 0.4945 0.2442 0.4593 -0.0388 0.0960  0.0276  26  SER A CA  
54   C C   . SER A 26  ? 0.4600 0.2361 0.4182 -0.0289 0.0854  0.0324  26  SER A C   
55   O O   . SER A 26  ? 0.5090 0.2784 0.4447 -0.0139 0.0825  0.0429  26  SER A O   
56   C CB  . SER A 26  ? 0.5554 0.2850 0.5159 -0.0458 0.1147  0.0344  26  SER A CB  
57   O OG  . SER A 26  ? 0.5902 0.3382 0.5706 -0.0594 0.1204  0.0288  26  SER A OG  
63   N N   . ASN A 27  ? 0.4437 0.2496 0.4210 -0.0363 0.0790  0.0241  27  ASN A N   
64   C CA  . ASN A 27  ? 0.4108 0.2396 0.3830 -0.0283 0.0704  0.0277  27  ASN A CA  
65   C C   . ASN A 27  ? 0.3346 0.1858 0.3120 -0.0222 0.0533  0.0212  27  ASN A C   
66   O O   . ASN A 27  ? 0.3211 0.1924 0.2979 -0.0173 0.0456  0.0218  27  ASN A O   
67   C CB  . ASN A 27  ? 0.3946 0.2397 0.3817 -0.0386 0.0760  0.0242  27  ASN A CB  
68   C CG  . ASN A 27  ? 0.4663 0.2891 0.4494 -0.0460 0.0952  0.0306  27  ASN A CG  
69   O OD1 . ASN A 27  ? 0.5285 0.3292 0.4873 -0.0371 0.1032  0.0436  27  ASN A OD1 
70   N ND2 . ASN A 27  ? 0.4444 0.2720 0.4508 -0.0620 0.1035  0.0211  27  ASN A ND2 
77   N N   . TYR A 28  ? 0.3382 0.1848 0.3198 -0.0222 0.0482  0.0149  28  TYR A N   
78   C CA  . TYR A 28  ? 0.2859 0.1521 0.2726 -0.0175 0.0342  0.0084  28  TYR A CA  
79   C C   . TYR A 28  ? 0.2755 0.1424 0.2452 -0.0032 0.0279  0.0160  28  TYR A C   
80   O O   . TYR A 28  ? 0.3065 0.1557 0.2596 0.0048  0.0330  0.0249  28  TYR A O   
81   C CB  . TYR A 28  ? 0.3132 0.1734 0.3082 -0.0216 0.0319  -0.0012 28  TYR A CB  
82   C CG  . TYR A 28  ? 0.3034 0.1789 0.3204 -0.0332 0.0293  -0.0150 28  TYR A CG  
83   C CD1 . TYR A 28  ? 0.3868 0.2675 0.4181 -0.0446 0.0368  -0.0188 28  TYR A CD1 
84   C CD2 . TYR A 28  ? 0.3350 0.2201 0.3578 -0.0317 0.0196  -0.0249 28  TYR A CD2 
85   C CE1 . TYR A 28  ? 0.2957 0.1936 0.3487 -0.0539 0.0331  -0.0336 28  TYR A CE1 
86   C CE2 . TYR A 28  ? 0.3527 0.2529 0.3937 -0.0398 0.0157  -0.0386 28  TYR A CE2 
87   C CZ  . TYR A 28  ? 0.3477 0.2555 0.4046 -0.0506 0.0218  -0.0434 28  TYR A CZ  
88   O OH  . TYR A 28  ? 0.3308 0.2569 0.4074 -0.0575 0.0167  -0.0589 28  TYR A OH  
98   N N   . PRO A 29  ? 0.2465 0.1336 0.2204 0.0007  0.0173  0.0120  29  PRO A N   
99   C CA  . PRO A 29  ? 0.2410 0.1329 0.2038 0.0128  0.0110  0.0164  29  PRO A CA  
100  C C   . PRO A 29  ? 0.2490 0.1272 0.2044 0.0196  0.0102  0.0164  29  PRO A C   
101  O O   . PRO A 29  ? 0.2699 0.1358 0.2292 0.0149  0.0129  0.0119  29  PRO A O   
102  C CB  . PRO A 29  ? 0.2427 0.1581 0.2151 0.0119  0.0023  0.0107  29  PRO A CB  
103  C CG  . PRO A 29  ? 0.2888 0.2090 0.2744 0.0024  0.0021  0.0030  29  PRO A CG  
104  C CD  . PRO A 29  ? 0.2500 0.1572 0.2392 -0.0056 0.0111  0.0031  29  PRO A CD  
112  N N   . GLU A 30  ? 0.2562 0.1370 0.2011 0.0315  0.0062  0.0206  30  GLU A N   
113  C CA  . GLU A 30  ? 0.2502 0.1233 0.1895 0.0398  0.0038  0.0195  30  GLU A CA  
114  C C   . GLU A 30  ? 0.2336 0.1191 0.1847 0.0355  -0.0016 0.0107  30  GLU A C   
115  O O   . GLU A 30  ? 0.2282 0.1320 0.1883 0.0308  -0.0057 0.0072  30  GLU A O   
116  C CB  . GLU A 30  ? 0.2763 0.1581 0.2065 0.0535  -0.0011 0.0232  30  GLU A CB  
117  C CG  . GLU A 30  ? 0.3015 0.1724 0.2161 0.0614  0.0029  0.0319  30  GLU A CG  
118  C CD  . GLU A 30  ? 0.4423 0.2820 0.3425 0.0654  0.0114  0.0382  30  GLU A CD  
119  O OE1 . GLU A 30  ? 0.5169 0.3446 0.4148 0.0696  0.0114  0.0362  30  GLU A OE1 
120  O OE2 . GLU A 30  ? 0.5576 0.3829 0.4480 0.0642  0.0194  0.0454  30  GLU A OE2 
127  N N   . PHE A 31  ? 0.2491 0.1229 0.1978 0.0385  -0.0013 0.0076  31  PHE A N   
128  C CA  . PHE A 31  ? 0.2343 0.1183 0.1905 0.0368  -0.0061 -0.0005 31  PHE A CA  
129  C C   . PHE A 31  ? 0.2742 0.1492 0.2234 0.0465  -0.0068 -0.0017 31  PHE A C   
130  O O   . PHE A 31  ? 0.2932 0.1465 0.2348 0.0496  -0.0023 0.0003  31  PHE A O   
131  C CB  . PHE A 31  ? 0.2426 0.1222 0.2075 0.0261  -0.0047 -0.0078 31  PHE A CB  
132  C CG  . PHE A 31  ? 0.2329 0.1230 0.2019 0.0265  -0.0102 -0.0161 31  PHE A CG  
133  C CD1 . PHE A 31  ? 0.2135 0.1231 0.1878 0.0245  -0.0147 -0.0182 31  PHE A CD1 
134  C CD2 . PHE A 31  ? 0.2480 0.1275 0.2135 0.0304  -0.0103 -0.0210 31  PHE A CD2 
135  C CE1 . PHE A 31  ? 0.2064 0.1242 0.1807 0.0267  -0.0188 -0.0246 31  PHE A CE1 
136  C CE2 . PHE A 31  ? 0.2487 0.1381 0.2155 0.0321  -0.0150 -0.0284 31  PHE A CE2 
137  C CZ  . PHE A 31  ? 0.2378 0.1461 0.2082 0.0305  -0.0189 -0.0296 31  PHE A CZ  
147  N N   . SER A 32  ? 0.2672 0.1584 0.2193 0.0509  -0.0115 -0.0055 32  SER A N   
148  C CA  . SER A 32  ? 0.2765 0.1632 0.2241 0.0598  -0.0124 -0.0084 32  SER A CA  
149  C C   . SER A 32  ? 0.2502 0.1517 0.2034 0.0581  -0.0154 -0.0151 32  SER A C   
150  O O   . SER A 32  ? 0.2579 0.1765 0.2166 0.0546  -0.0172 -0.0150 32  SER A O   
151  C CB  . SER A 32  ? 0.3032 0.1972 0.2462 0.0718  -0.0140 -0.0041 32  SER A CB  
152  O OG  . SER A 32  ? 0.3151 0.2072 0.2550 0.0811  -0.0147 -0.0077 32  SER A OG  
158  N N   . TRP A 33  ? 0.2547 0.1476 0.2049 0.0614  -0.0152 -0.0207 33  TRP A N   
159  C CA  . TRP A 33  ? 0.2481 0.1534 0.1996 0.0630  -0.0171 -0.0266 33  TRP A CA  
160  C C   . TRP A 33  ? 0.2676 0.1852 0.2187 0.0726  -0.0169 -0.0257 33  TRP A C   
161  O O   . TRP A 33  ? 0.2596 0.1871 0.2110 0.0747  -0.0165 -0.0298 33  TRP A O   
162  C CB  . TRP A 33  ? 0.2780 0.1699 0.2260 0.0632  -0.0172 -0.0345 33  TRP A CB  
163  C CG  . TRP A 33  ? 0.2577 0.1432 0.2094 0.0533  -0.0182 -0.0400 33  TRP A CG  
164  C CD1 . TRP A 33  ? 0.2813 0.1476 0.2341 0.0486  -0.0160 -0.0434 33  TRP A CD1 
165  C CD2 . TRP A 33  ? 0.2447 0.1438 0.2005 0.0475  -0.0216 -0.0437 33  TRP A CD2 
166  N NE1 . TRP A 33  ? 0.2710 0.1412 0.2311 0.0392  -0.0182 -0.0506 33  TRP A NE1 
167  C CE2 . TRP A 33  ? 0.2486 0.1392 0.2096 0.0396  -0.0224 -0.0508 33  TRP A CE2 
168  C CE3 . TRP A 33  ? 0.2423 0.1590 0.1975 0.0487  -0.0234 -0.0421 33  TRP A CE3 
169  C CZ2 . TRP A 33  ? 0.2659 0.1682 0.2318 0.0343  -0.0266 -0.0570 33  TRP A CZ2 
170  C CZ3 . TRP A 33  ? 0.2251 0.1496 0.1821 0.0442  -0.0269 -0.0466 33  TRP A CZ3 
171  C CH2 . TRP A 33  ? 0.2597 0.1784 0.2222 0.0378  -0.0293 -0.0542 33  TRP A CH2 
182  N N   . ASP A 34  ? 0.2503 0.1683 0.2005 0.0795  -0.0168 -0.0211 34  ASP A N   
183  C CA  . ASP A 34  ? 0.2670 0.1981 0.2190 0.0897  -0.0169 -0.0226 34  ASP A CA  
184  C C   . ASP A 34  ? 0.2439 0.1983 0.2048 0.0861  -0.0161 -0.0245 34  ASP A C   
185  O O   . ASP A 34  ? 0.2393 0.2034 0.2023 0.0908  -0.0140 -0.0286 34  ASP A O   
186  C CB  . ASP A 34  ? 0.2956 0.2271 0.2455 0.0984  -0.0185 -0.0180 34  ASP A CB  
187  C CG  . ASP A 34  ? 0.3310 0.2368 0.2690 0.1059  -0.0175 -0.0156 34  ASP A CG  
188  O OD1 . ASP A 34  ? 0.4016 0.2894 0.3350 0.1036  -0.0154 -0.0187 34  ASP A OD1 
189  O OD2 . ASP A 34  ? 0.4321 0.3351 0.3644 0.1150  -0.0187 -0.0108 34  ASP A OD2 
194  N N   . THR A 35  ? 0.2353 0.1975 0.2013 0.0778  -0.0164 -0.0215 35  THR A N   
195  C CA  . THR A 35  ? 0.2100 0.1891 0.1832 0.0724  -0.0141 -0.0225 35  THR A CA  
196  C C   . THR A 35  ? 0.2036 0.1778 0.1755 0.0628  -0.0148 -0.0201 35  THR A C   
197  O O   . THR A 35  ? 0.2196 0.1812 0.1878 0.0600  -0.0170 -0.0185 35  THR A O   
198  C CB  . THR A 35  ? 0.2248 0.2226 0.2085 0.0741  -0.0141 -0.0225 35  THR A CB  
199  O OG1 . THR A 35  ? 0.2384 0.2333 0.2215 0.0729  -0.0176 -0.0186 35  THR A OG1 
200  C CG2 . THR A 35  ? 0.2356 0.2424 0.2225 0.0848  -0.0141 -0.0263 35  THR A CG2 
208  N N   . MET A 36  ? 0.1907 0.1744 0.1658 0.0580  -0.0122 -0.0200 36  MET A N   
209  C CA  . MET A 36  ? 0.1944 0.1742 0.1672 0.0510  -0.0131 -0.0183 36  MET A CA  
210  C C   . MET A 36  ? 0.1845 0.1603 0.1596 0.0470  -0.0163 -0.0153 36  MET A C   
211  O O   . MET A 36  ? 0.1995 0.1825 0.1799 0.0472  -0.0165 -0.0132 36  MET A O   
212  C CB  . MET A 36  ? 0.1906 0.1800 0.1665 0.0476  -0.0088 -0.0170 36  MET A CB  
213  C CG  . MET A 36  ? 0.1952 0.1793 0.1639 0.0446  -0.0090 -0.0161 36  MET A CG  
214  S SD  . MET A 36  ? 0.2126 0.1881 0.1686 0.0494  -0.0104 -0.0202 36  MET A SD  
215  C CE  . MET A 36  ? 0.2404 0.2214 0.1946 0.0549  -0.0032 -0.0213 36  MET A CE  
225  N N   . PRO A 37  ? 0.1823 0.1484 0.1542 0.0433  -0.0185 -0.0158 37  PRO A N   
226  C CA  . PRO A 37  ? 0.1741 0.1374 0.1488 0.0386  -0.0198 -0.0128 37  PRO A CA  
227  C C   . PRO A 37  ? 0.1707 0.1430 0.1489 0.0339  -0.0198 -0.0112 37  PRO A C   
228  O O   . PRO A 37  ? 0.1816 0.1547 0.1579 0.0323  -0.0204 -0.0131 37  PRO A O   
229  C CB  . PRO A 37  ? 0.1829 0.1343 0.1557 0.0355  -0.0209 -0.0160 37  PRO A CB  
230  C CG  . PRO A 37  ? 0.1966 0.1490 0.1657 0.0374  -0.0221 -0.0214 37  PRO A CG  
231  C CD  . PRO A 37  ? 0.2140 0.1719 0.1806 0.0437  -0.0198 -0.0206 37  PRO A CD  
239  N N   . LEU A 38  ? 0.1759 0.1544 0.1582 0.0330  -0.0195 -0.0083 38  LEU A N   
240  C CA  . LEU A 38  ? 0.1575 0.1442 0.1436 0.0293  -0.0188 -0.0074 38  LEU A CA  
241  C C   . LEU A 38  ? 0.1737 0.1596 0.1615 0.0254  -0.0202 -0.0055 38  LEU A C   
242  O O   . LEU A 38  ? 0.1876 0.1699 0.1745 0.0261  -0.0206 -0.0036 38  LEU A O   
243  C CB  . LEU A 38  ? 0.1737 0.1711 0.1656 0.0309  -0.0171 -0.0078 38  LEU A CB  
244  C CG  . LEU A 38  ? 0.1684 0.1699 0.1614 0.0343  -0.0143 -0.0102 38  LEU A CG  
245  C CD1 . LEU A 38  ? 0.2166 0.2323 0.2196 0.0346  -0.0126 -0.0128 38  LEU A CD1 
246  C CD2 . LEU A 38  ? 0.1968 0.1947 0.1853 0.0328  -0.0108 -0.0104 38  LEU A CD2 
258  N N   . TYR A 39  ? 0.1577 0.1462 0.1465 0.0222  -0.0202 -0.0057 39  TYR A N   
259  C CA  . TYR A 39  ? 0.1497 0.1398 0.1410 0.0188  -0.0210 -0.0047 39  TYR A CA  
260  C C   . TYR A 39  ? 0.1676 0.1644 0.1620 0.0179  -0.0198 -0.0042 39  TYR A C   
261  O O   . TYR A 39  ? 0.1650 0.1631 0.1595 0.0183  -0.0175 -0.0048 39  TYR A O   
262  C CB  . TYR A 39  ? 0.1783 0.1669 0.1687 0.0174  -0.0227 -0.0068 39  TYR A CB  
263  C CG  . TYR A 39  ? 0.1487 0.1409 0.1426 0.0146  -0.0236 -0.0070 39  TYR A CG  
264  C CD1 . TYR A 39  ? 0.1544 0.1466 0.1517 0.0116  -0.0226 -0.0059 39  TYR A CD1 
265  C CD2 . TYR A 39  ? 0.1557 0.1505 0.1484 0.0158  -0.0247 -0.0079 39  TYR A CD2 
266  C CE1 . TYR A 39  ? 0.1515 0.1485 0.1528 0.0093  -0.0227 -0.0067 39  TYR A CE1 
267  C CE2 . TYR A 39  ? 0.1465 0.1458 0.1429 0.0144  -0.0257 -0.0088 39  TYR A CE2 
268  C CZ  . TYR A 39  ? 0.1377 0.1392 0.1395 0.0107  -0.0246 -0.0085 39  TYR A CZ  
269  O OH  . TYR A 39  ? 0.1463 0.1536 0.1525 0.0096  -0.0249 -0.0099 39  TYR A OH  
279  N N   . MET A 40  ? 0.1430 0.1431 0.1397 0.0165  -0.0204 -0.0034 40  MET A N   
280  C CA  . MET A 40  ? 0.1486 0.1542 0.1489 0.0150  -0.0195 -0.0045 40  MET A CA  
281  C C   . MET A 40  ? 0.1366 0.1419 0.1369 0.0131  -0.0202 -0.0042 40  MET A C   
282  O O   . MET A 40  ? 0.1585 0.1630 0.1581 0.0126  -0.0209 -0.0032 40  MET A O   
283  C CB  . MET A 40  ? 0.1490 0.1618 0.1522 0.0166  -0.0203 -0.0059 40  MET A CB  
284  C CG  . MET A 40  ? 0.1610 0.1808 0.1699 0.0146  -0.0198 -0.0093 40  MET A CG  
285  S SD  . MET A 40  ? 0.1669 0.1844 0.1803 0.0107  -0.0149 -0.0114 40  MET A SD  
286  C CE  . MET A 40  ? 0.1993 0.2205 0.2158 0.0122  -0.0128 -0.0127 40  MET A CE  
296  N N   . HIS A 41  ? 0.1429 0.1480 0.1440 0.0123  -0.0189 -0.0051 41  HIS A N   
297  C CA  . HIS A 41  ? 0.1326 0.1374 0.1334 0.0121  -0.0196 -0.0054 41  HIS A CA  
298  C C   . HIS A 41  ? 0.1494 0.1540 0.1521 0.0112  -0.0174 -0.0069 41  HIS A C   
299  O O   . HIS A 41  ? 0.1566 0.1556 0.1576 0.0112  -0.0143 -0.0066 41  HIS A O   
300  C CB  . HIS A 41  ? 0.1564 0.1573 0.1533 0.0144  -0.0208 -0.0052 41  HIS A CB  
301  C CG  . HIS A 41  ? 0.1432 0.1466 0.1408 0.0157  -0.0227 -0.0065 41  HIS A CG  
302  N ND1 . HIS A 41  ? 0.1371 0.1456 0.1386 0.0148  -0.0251 -0.0086 41  HIS A ND1 
303  C CD2 . HIS A 41  ? 0.1623 0.1641 0.1582 0.0181  -0.0223 -0.0069 41  HIS A CD2 
304  C CE1 . HIS A 41  ? 0.1405 0.1532 0.1437 0.0169  -0.0265 -0.0106 41  HIS A CE1 
305  N NE2 . HIS A 41  ? 0.1575 0.1655 0.1564 0.0196  -0.0251 -0.0092 41  HIS A NE2 
313  N N   . VAL A 42  ? 0.1388 0.1483 0.1444 0.0103  -0.0180 -0.0089 42  VAL A N   
314  C CA  . VAL A 42  ? 0.1433 0.1538 0.1531 0.0084  -0.0160 -0.0125 42  VAL A CA  
315  C C   . VAL A 42  ? 0.1333 0.1472 0.1442 0.0085  -0.0170 -0.0153 42  VAL A C   
316  O O   . VAL A 42  ? 0.1401 0.1586 0.1490 0.0101  -0.0191 -0.0144 42  VAL A O   
317  C CB  . VAL A 42  ? 0.1810 0.1987 0.1957 0.0074  -0.0163 -0.0151 42  VAL A CB  
318  C CG1 . VAL A 42  ? 0.1942 0.2194 0.2071 0.0102  -0.0202 -0.0151 42  VAL A CG1 
319  C CG2 . VAL A 42  ? 0.2183 0.2387 0.2409 0.0039  -0.0136 -0.0211 42  VAL A CG2 
329  N N   . ARG A 43  ? 0.1392 0.1499 0.1533 0.0067  -0.0145 -0.0191 43  ARG A N   
330  C CA  . ARG A 43  ? 0.1357 0.1499 0.1518 0.0066  -0.0153 -0.0240 43  ARG A CA  
331  C C   . ARG A 43  ? 0.1411 0.1554 0.1651 0.0024  -0.0127 -0.0308 43  ARG A C   
332  O O   . ARG A 43  ? 0.1420 0.1517 0.1698 -0.0010 -0.0086 -0.0310 43  ARG A O   
333  C CB  . ARG A 43  ? 0.1423 0.1498 0.1543 0.0093  -0.0145 -0.0227 43  ARG A CB  
334  C CG  . ARG A 43  ? 0.1552 0.1486 0.1639 0.0099  -0.0104 -0.0206 43  ARG A CG  
335  C CD  . ARG A 43  ? 0.1637 0.1505 0.1678 0.0146  -0.0102 -0.0204 43  ARG A CD  
336  N NE  . ARG A 43  ? 0.1773 0.1667 0.1850 0.0135  -0.0101 -0.0265 43  ARG A NE  
337  C CZ  . ARG A 43  ? 0.1832 0.1629 0.1930 0.0111  -0.0061 -0.0309 43  ARG A CZ  
338  N NH1 . ARG A 43  ? 0.2178 0.1812 0.2246 0.0103  -0.0002 -0.0284 43  ARG A NH1 
339  N NH2 . ARG A 43  ? 0.1896 0.1753 0.2044 0.0094  -0.0072 -0.0384 43  ARG A NH2 
353  N N   . LYS A 44  ? 0.1422 0.1625 0.1692 0.0023  -0.0145 -0.0376 44  LYS A N   
354  C CA  . LYS A 44  ? 0.1505 0.1736 0.1875 -0.0024 -0.0129 -0.0472 44  LYS A CA  
355  C C   . LYS A 44  ? 0.1363 0.1598 0.1720 -0.0007 -0.0145 -0.0528 44  LYS A C   
356  O O   . LYS A 44  ? 0.1609 0.1896 0.1891 0.0046  -0.0182 -0.0502 44  LYS A O   
357  C CB  . LYS A 44  ? 0.1398 0.1794 0.1838 -0.0025 -0.0170 -0.0528 44  LYS A CB  
358  C CG  . LYS A 44  ? 0.1580 0.2035 0.2169 -0.0089 -0.0147 -0.0644 44  LYS A CG  
359  C CD  . LYS A 44  ? 0.1513 0.2177 0.2179 -0.0068 -0.0207 -0.0720 44  LYS A CD  
360  C CE  . LYS A 44  ? 0.1678 0.2437 0.2530 -0.0140 -0.0188 -0.0866 44  LYS A CE  
361  N NZ  . LYS A 44  ? 0.1753 0.2760 0.2683 -0.0096 -0.0271 -0.0967 44  LYS A NZ  
375  N N   . ASN A 45  ? 0.1605 0.1772 0.2030 -0.0052 -0.0105 -0.0603 45  ASN A N   
376  C CA  . ASN A 45  ? 0.1764 0.1921 0.2171 -0.0031 -0.0119 -0.0665 45  ASN A CA  
377  C C   . ASN A 45  ? 0.1518 0.1861 0.1960 -0.0013 -0.0185 -0.0764 45  ASN A C   
378  O O   . ASN A 45  ? 0.1802 0.2172 0.2194 0.0028  -0.0210 -0.0803 45  ASN A O   
379  C CB  . ASN A 45  ? 0.1926 0.1915 0.2385 -0.0083 -0.0048 -0.0716 45  ASN A CB  
380  C CG  . ASN A 45  ? 0.2035 0.1819 0.2399 -0.0058 0.0009  -0.0612 45  ASN A CG  
381  O OD1 . ASN A 45  ? 0.2411 0.2171 0.2681 0.0012  -0.0014 -0.0561 45  ASN A OD1 
382  N ND2 . ASN A 45  ? 0.2224 0.1879 0.2609 -0.0105 0.0083  -0.0581 45  ASN A ND2 
389  N N   . THR A 46  ? 0.1692 0.2171 0.2208 -0.0029 -0.0215 -0.0810 46  THR A N   
390  C CA  . THR A 46  ? 0.1731 0.2405 0.2266 0.0010  -0.0290 -0.0910 46  THR A CA  
391  C C   . THR A 46  ? 0.1511 0.2295 0.1987 0.0068  -0.0336 -0.0845 46  THR A C   
392  O O   . THR A 46  ? 0.1605 0.2317 0.2055 0.0059  -0.0307 -0.0742 46  THR A O   
393  C CB  . THR A 46  ? 0.1952 0.2711 0.2668 -0.0060 -0.0289 -0.1070 46  THR A CB  
394  O OG1 . THR A 46  ? 0.1947 0.2688 0.2772 -0.0127 -0.0240 -0.1053 46  THR A OG1 
395  C CG2 . THR A 46  ? 0.2104 0.2734 0.2869 -0.0114 -0.0240 -0.1146 46  THR A CG2 
403  N N   . ALA A 47  ? 0.1753 0.2705 0.2196 0.0137  -0.0410 -0.0912 47  ALA A N   
404  C CA  . ALA A 47  ? 0.1614 0.2647 0.1973 0.0212  -0.0452 -0.0848 47  ALA A CA  
405  C C   . ALA A 47  ? 0.1579 0.2654 0.2060 0.0171  -0.0442 -0.0856 47  ALA A C   
406  O O   . ALA A 47  ? 0.1664 0.2794 0.2318 0.0097  -0.0425 -0.0962 47  ALA A O   
407  C CB  . ALA A 47  ? 0.1756 0.2967 0.2050 0.0312  -0.0537 -0.0935 47  ALA A CB  
413  N N   . TYR A 48  ? 0.1729 0.2779 0.2123 0.0219  -0.0446 -0.0751 48  TYR A N   
414  C CA  . TYR A 48  ? 0.1655 0.2765 0.2146 0.0204  -0.0444 -0.0760 48  TYR A CA  
415  C C   . TYR A 48  ? 0.1863 0.3205 0.2426 0.0266  -0.0524 -0.0888 48  TYR A C   
416  O O   . TYR A 48  ? 0.1885 0.3314 0.2335 0.0367  -0.0592 -0.0912 48  TYR A O   
417  C CB  . TYR A 48  ? 0.1665 0.2675 0.2032 0.0249  -0.0430 -0.0621 48  TYR A CB  
418  C CG  . TYR A 48  ? 0.1567 0.2387 0.1891 0.0190  -0.0363 -0.0521 48  TYR A CG  
419  C CD1 . TYR A 48  ? 0.1495 0.2236 0.1904 0.0116  -0.0306 -0.0505 48  TYR A CD1 
420  C CD2 . TYR A 48  ? 0.1682 0.2413 0.1882 0.0214  -0.0354 -0.0449 48  TYR A CD2 
421  C CE1 . TYR A 48  ? 0.1455 0.2038 0.1810 0.0084  -0.0258 -0.0424 48  TYR A CE1 
422  C CE2 . TYR A 48  ? 0.1779 0.2372 0.1959 0.0170  -0.0304 -0.0378 48  TYR A CE2 
423  C CZ  . TYR A 48  ? 0.1323 0.1845 0.1574 0.0112  -0.0264 -0.0368 48  TYR A CZ  
424  O OH  . TYR A 48  ? 0.1578 0.1978 0.1791 0.0091  -0.0228 -0.0306 48  TYR A OH  
434  N N   . THR A 49  ? 0.1719 0.3173 0.2470 0.0214  -0.0515 -0.0974 49  THR A N   
435  C CA  . THR A 49  ? 0.1441 0.3107 0.2261 0.0283  -0.0576 -0.1083 49  THR A CA  
436  C C   . THR A 49  ? 0.1657 0.3330 0.2325 0.0410  -0.0618 -0.0991 49  THR A C   
437  O O   . THR A 49  ? 0.1719 0.3266 0.2286 0.0421  -0.0601 -0.0866 49  THR A O   
438  C CB  . THR A 49  ? 0.1626 0.3386 0.2688 0.0185  -0.0525 -0.1187 49  THR A CB  
439  O OG1 . THR A 49  ? 0.1702 0.3420 0.2802 0.0154  -0.0487 -0.1112 49  THR A OG1 
440  C CG2 . THR A 49  ? 0.2032 0.3737 0.3242 0.0051  -0.0459 -0.1268 49  THR A CG2 
448  N N   . ASP A 50  ? 0.1874 0.3675 0.2522 0.0508  -0.0662 -0.1054 50  ASP A N   
449  C CA  . ASP A 50  ? 0.2090 0.3876 0.2592 0.0633  -0.0692 -0.0974 50  ASP A CA  
450  C C   . ASP A 50  ? 0.2028 0.3794 0.2621 0.0588  -0.0659 -0.0931 50  ASP A C   
451  O O   . ASP A 50  ? 0.1895 0.3545 0.2349 0.0648  -0.0658 -0.0810 50  ASP A O   
452  C CB  . ASP A 50  ? 0.2145 0.4091 0.2638 0.0744  -0.0744 -0.1076 50  ASP A CB  
453  C CG  . ASP A 50  ? 0.3856 0.5754 0.4152 0.0896  -0.0773 -0.0990 50  ASP A CG  
454  O OD1 . ASP A 50  ? 0.4944 0.6973 0.5296 0.0959  -0.0801 -0.1065 50  ASP A OD1 
455  O OD2 . ASP A 50  ? 0.4212 0.5938 0.4296 0.0954  -0.0763 -0.0853 50  ASP A OD2 
460  N N   . GLU A 51  ? 0.1678 0.3548 0.2505 0.0482  -0.0620 -0.1029 51  GLU A N   
461  C CA  . GLU A 51  ? 0.1585 0.3447 0.2513 0.0434  -0.0575 -0.0995 51  GLU A CA  
462  C C   . GLU A 51  ? 0.1616 0.3261 0.2452 0.0381  -0.0523 -0.0856 51  GLU A C   
463  O O   . GLU A 51  ? 0.1652 0.3187 0.2407 0.0408  -0.0495 -0.0757 51  GLU A O   
464  C CB  . GLU A 51  ? 0.1748 0.3728 0.2938 0.0308  -0.0513 -0.1120 51  GLU A CB  
465  C CG  . GLU A 51  ? 0.2158 0.4132 0.3465 0.0246  -0.0443 -0.1088 51  GLU A CG  
466  C CD  . GLU A 51  ? 0.2772 0.4807 0.4325 0.0097  -0.0343 -0.1191 51  GLU A CD  
467  O OE1 . GLU A 51  ? 0.2998 0.5012 0.4631 0.0008  -0.0310 -0.1261 51  GLU A OE1 
468  O OE2 . GLU A 51  ? 0.3581 0.5668 0.5237 0.0073  -0.0286 -0.1197 51  GLU A OE2 
475  N N   . GLU A 52  ? 0.1623 0.3144 0.2435 0.0299  -0.0484 -0.0835 52  GLU A N   
476  C CA  . GLU A 52  ? 0.1454 0.2724 0.2143 0.0249  -0.0417 -0.0697 52  GLU A CA  
477  C C   . GLU A 52  ? 0.1431 0.2584 0.1902 0.0345  -0.0448 -0.0578 52  GLU A C   
478  O O   . GLU A 52  ? 0.1489 0.2486 0.1881 0.0334  -0.0406 -0.0475 52  GLU A O   
479  C CB  . GLU A 52  ? 0.1553 0.2732 0.2269 0.0159  -0.0374 -0.0713 52  GLU A CB  
480  C CG  . GLU A 52  ? 0.1663 0.2867 0.2573 0.0044  -0.0302 -0.0796 52  GLU A CG  
481  C CD  . GLU A 52  ? 0.1773 0.2884 0.2713 -0.0033 -0.0262 -0.0830 52  GLU A CD  
482  O OE1 . GLU A 52  ? 0.1699 0.2827 0.2565 0.0009  -0.0316 -0.0850 52  GLU A OE1 
483  O OE2 . GLU A 52  ? 0.2163 0.3181 0.3196 -0.0130 -0.0171 -0.0843 52  GLU A OE2 
490  N N   . ILE A 53  ? 0.1761 0.2981 0.2129 0.0441  -0.0514 -0.0595 53  ILE A N   
491  C CA  . ILE A 53  ? 0.1830 0.2921 0.1984 0.0532  -0.0523 -0.0478 53  ILE A CA  
492  C C   . ILE A 53  ? 0.2014 0.3084 0.2130 0.0601  -0.0529 -0.0433 53  ILE A C   
493  O O   . ILE A 53  ? 0.1877 0.2765 0.1875 0.0609  -0.0490 -0.0322 53  ILE A O   
494  C CB  . ILE A 53  ? 0.1920 0.3087 0.1948 0.0638  -0.0585 -0.0505 53  ILE A CB  
495  C CG1 . ILE A 53  ? 0.1924 0.3067 0.1957 0.0573  -0.0566 -0.0530 53  ILE A CG1 
496  C CG2 . ILE A 53  ? 0.2442 0.3470 0.2240 0.0749  -0.0581 -0.0384 53  ILE A CG2 
497  C CD1 . ILE A 53  ? 0.2056 0.2996 0.2005 0.0512  -0.0494 -0.0415 53  ILE A CD1 
509  N N   . ASN A 54  ? 0.1960 0.3218 0.2186 0.0651  -0.0576 -0.0527 54  ASN A N   
510  C CA  . ASN A 54  ? 0.2019 0.3260 0.2216 0.0723  -0.0580 -0.0491 54  ASN A CA  
511  C C   . ASN A 54  ? 0.1815 0.2915 0.2061 0.0624  -0.0502 -0.0430 54  ASN A C   
512  O O   . ASN A 54  ? 0.2216 0.3172 0.2353 0.0666  -0.0483 -0.0346 54  ASN A O   
513  C CB  . ASN A 54  ? 0.2124 0.3613 0.2465 0.0779  -0.0632 -0.0620 54  ASN A CB  
514  C CG  . ASN A 54  ? 0.2939 0.4486 0.3166 0.0882  -0.0679 -0.0663 54  ASN A CG  
515  O OD1 . ASN A 54  ? 0.3605 0.5023 0.3625 0.0956  -0.0687 -0.0582 54  ASN A OD1 
516  N ND2 . ASN A 54  ? 0.3335 0.5081 0.3701 0.0887  -0.0704 -0.0798 54  ASN A ND2 
523  N N   . TYR A 55  ? 0.1633 0.2756 0.2026 0.0498  -0.0453 -0.0474 55  TYR A N   
524  C CA  . TYR A 55  ? 0.1767 0.2752 0.2179 0.0416  -0.0379 -0.0416 55  TYR A CA  
525  C C   . TYR A 55  ? 0.1884 0.2651 0.2136 0.0405  -0.0356 -0.0302 55  TYR A C   
526  O O   . TYR A 55  ? 0.1826 0.2473 0.2011 0.0417  -0.0334 -0.0240 55  TYR A O   
527  C CB  . TYR A 55  ? 0.1802 0.2827 0.2366 0.0297  -0.0324 -0.0476 55  TYR A CB  
528  C CG  . TYR A 55  ? 0.1663 0.2549 0.2229 0.0222  -0.0243 -0.0422 55  TYR A CG  
529  C CD1 . TYR A 55  ? 0.2033 0.2933 0.2633 0.0232  -0.0209 -0.0419 55  TYR A CD1 
530  C CD2 . TYR A 55  ? 0.1672 0.2418 0.2196 0.0153  -0.0201 -0.0378 55  TYR A CD2 
531  C CE1 . TYR A 55  ? 0.2151 0.2922 0.2726 0.0177  -0.0134 -0.0370 55  TYR A CE1 
532  C CE2 . TYR A 55  ? 0.1663 0.2282 0.2160 0.0107  -0.0133 -0.0329 55  TYR A CE2 
533  C CZ  . TYR A 55  ? 0.1801 0.2431 0.2317 0.0119  -0.0100 -0.0325 55  TYR A CZ  
534  O OH  . TYR A 55  ? 0.2507 0.3010 0.2971 0.0088  -0.0032 -0.0276 55  TYR A OH  
544  N N   . LEU A 56  ? 0.1707 0.2431 0.1906 0.0383  -0.0361 -0.0285 56  LEU A N   
545  C CA  . LEU A 56  ? 0.1716 0.2266 0.1795 0.0368  -0.0335 -0.0194 56  LEU A CA  
546  C C   . LEU A 56  ? 0.2022 0.2476 0.1968 0.0449  -0.0343 -0.0127 56  LEU A C   
547  O O   . LEU A 56  ? 0.1889 0.2200 0.1784 0.0424  -0.0309 -0.0067 56  LEU A O   
548  C CB  . LEU A 56  ? 0.1893 0.2440 0.1938 0.0348  -0.0339 -0.0195 56  LEU A CB  
549  C CG  . LEU A 56  ? 0.1654 0.2232 0.1806 0.0265  -0.0317 -0.0246 56  LEU A CG  
550  C CD1 . LEU A 56  ? 0.2040 0.2625 0.2155 0.0261  -0.0325 -0.0257 56  LEU A CD1 
551  C CD2 . LEU A 56  ? 0.2107 0.2566 0.2270 0.0201  -0.0267 -0.0202 56  LEU A CD2 
563  N N   . ALA A 57  ? 0.2036 0.2558 0.1917 0.0551  -0.0387 -0.0140 57  ALA A N   
564  C CA  . ALA A 57  ? 0.2086 0.2480 0.1807 0.0644  -0.0385 -0.0066 57  ALA A CA  
565  C C   . ALA A 57  ? 0.2338 0.2668 0.2069 0.0666  -0.0373 -0.0051 57  ALA A C   
566  O O   . ALA A 57  ? 0.2633 0.2802 0.2233 0.0724  -0.0353 0.0017  57  ALA A O   
567  C CB  . ALA A 57  ? 0.2392 0.2887 0.2022 0.0777  -0.0443 -0.0090 57  ALA A CB  
573  N N   . SER A 58  ? 0.2098 0.2534 0.1973 0.0620  -0.0374 -0.0112 58  SER A N   
574  C CA  . SER A 58  ? 0.2238 0.2624 0.2124 0.0640  -0.0358 -0.0106 58  SER A CA  
575  C C   . SER A 58  ? 0.1994 0.2213 0.1859 0.0558  -0.0307 -0.0058 58  SER A C   
576  O O   . SER A 58  ? 0.2465 0.2614 0.2315 0.0578  -0.0293 -0.0052 58  SER A O   
577  C CB  . SER A 58  ? 0.2077 0.2656 0.2126 0.0629  -0.0366 -0.0194 58  SER A CB  
578  O OG  . SER A 58  ? 0.2241 0.2834 0.2392 0.0512  -0.0322 -0.0215 58  SER A OG  
584  N N   . PHE A 59  ? 0.1912 0.2079 0.1780 0.0474  -0.0285 -0.0037 59  PHE A N   
585  C CA  . PHE A 59  ? 0.2138 0.2178 0.1994 0.0405  -0.0250 -0.0009 59  PHE A CA  
586  C C   . PHE A 59  ? 0.2091 0.1971 0.1846 0.0413  -0.0229 0.0048  59  PHE A C   
587  O O   . PHE A 59  ? 0.2381 0.2245 0.2073 0.0438  -0.0226 0.0079  59  PHE A O   
588  C CB  . PHE A 59  ? 0.1976 0.2058 0.1895 0.0323  -0.0239 -0.0024 59  PHE A CB  
589  C CG  . PHE A 59  ? 0.1598 0.1779 0.1607 0.0298  -0.0232 -0.0071 59  PHE A CG  
590  C CD1 . PHE A 59  ? 0.1794 0.2109 0.1877 0.0303  -0.0244 -0.0117 59  PHE A CD1 
591  C CD2 . PHE A 59  ? 0.1692 0.1833 0.1711 0.0272  -0.0205 -0.0074 59  PHE A CD2 
592  C CE1 . PHE A 59  ? 0.1761 0.2159 0.1944 0.0267  -0.0217 -0.0165 59  PHE A CE1 
593  C CE2 . PHE A 59  ? 0.1998 0.2207 0.2085 0.0249  -0.0175 -0.0106 59  PHE A CE2 
594  C CZ  . PHE A 59  ? 0.1930 0.2263 0.2110 0.0237  -0.0173 -0.0151 59  PHE A CZ  
604  N N   . PRO A 60  ? 0.1954 0.1709 0.1690 0.0389  -0.0205 0.0058  60  PRO A N   
605  C CA  . PRO A 60  ? 0.2094 0.1683 0.1756 0.0378  -0.0166 0.0102  60  PRO A CA  
606  C C   . PRO A 60  ? 0.1939 0.1532 0.1637 0.0297  -0.0142 0.0109  60  PRO A C   
607  O O   . PRO A 60  ? 0.2239 0.1729 0.1880 0.0287  -0.0096 0.0151  60  PRO A O   
608  C CB  . PRO A 60  ? 0.2342 0.1820 0.2006 0.0367  -0.0153 0.0083  60  PRO A CB  
609  C CG  . PRO A 60  ? 0.2237 0.1838 0.1979 0.0347  -0.0183 0.0031  60  PRO A CG  
610  C CD  . PRO A 60  ? 0.2103 0.1857 0.1876 0.0383  -0.0208 0.0023  60  PRO A CD  
618  N N   . LEU A 61  ? 0.1915 0.1619 0.1699 0.0245  -0.0163 0.0070  61  LEU A N   
619  C CA  . LEU A 61  ? 0.1817 0.1543 0.1649 0.0177  -0.0147 0.0064  61  LEU A CA  
620  C C   . LEU A 61  ? 0.1898 0.1755 0.1778 0.0171  -0.0177 0.0039  61  LEU A C   
621  O O   . LEU A 61  ? 0.1760 0.1662 0.1670 0.0174  -0.0197 0.0012  61  LEU A O   
622  C CB  . LEU A 61  ? 0.1932 0.1614 0.1816 0.0124  -0.0142 0.0026  61  LEU A CB  
623  C CG  . LEU A 61  ? 0.1852 0.1578 0.1809 0.0059  -0.0129 0.0001  61  LEU A CG  
624  C CD1 . LEU A 61  ? 0.2012 0.1690 0.1954 0.0034  -0.0070 0.0039  61  LEU A CD1 
625  C CD2 . LEU A 61  ? 0.2134 0.1847 0.2155 0.0020  -0.0141 -0.0060 61  LEU A CD2 
637  N N   . ILE A 62  ? 0.1727 0.1628 0.1605 0.0162  -0.0168 0.0050  62  ILE A N   
638  C CA  . ILE A 62  ? 0.1628 0.1630 0.1544 0.0159  -0.0189 0.0025  62  ILE A CA  
639  C C   . ILE A 62  ? 0.1608 0.1632 0.1553 0.0120  -0.0173 0.0021  62  ILE A C   
640  O O   . ILE A 62  ? 0.1844 0.1843 0.1759 0.0115  -0.0140 0.0046  62  ILE A O   
641  C CB  . ILE A 62  ? 0.1684 0.1745 0.1563 0.0208  -0.0204 0.0026  62  ILE A CB  
642  C CG1 . ILE A 62  ? 0.1852 0.1919 0.1712 0.0260  -0.0223 0.0021  62  ILE A CG1 
643  C CG2 . ILE A 62  ? 0.1929 0.2083 0.1863 0.0192  -0.0220 -0.0016 62  ILE A CG2 
644  C CD1 . ILE A 62  ? 0.2938 0.2987 0.2704 0.0336  -0.0229 0.0050  62  ILE A CD1 
656  N N   . THR A 63  ? 0.1452 0.1518 0.1446 0.0102  -0.0188 -0.0009 63  THR A N   
657  C CA  . THR A 63  ? 0.1301 0.1414 0.1328 0.0085  -0.0182 -0.0024 63  THR A CA  
658  C C   . THR A 63  ? 0.1415 0.1573 0.1439 0.0103  -0.0192 -0.0039 63  THR A C   
659  O O   . THR A 63  ? 0.1449 0.1603 0.1483 0.0109  -0.0203 -0.0055 63  THR A O   
660  C CB  . THR A 63  ? 0.1361 0.1487 0.1432 0.0074  -0.0197 -0.0053 63  THR A CB  
661  O OG1 . THR A 63  ? 0.1515 0.1615 0.1612 0.0047  -0.0188 -0.0059 63  THR A OG1 
662  C CG2 . THR A 63  ? 0.1436 0.1627 0.1545 0.0075  -0.0196 -0.0075 63  THR A CG2 
670  N N   . LEU A 64  ? 0.1303 0.1499 0.1315 0.0108  -0.0178 -0.0039 64  LEU A N   
671  C CA  . LEU A 64  ? 0.1330 0.1572 0.1346 0.0122  -0.0188 -0.0071 64  LEU A CA  
672  C C   . LEU A 64  ? 0.1343 0.1597 0.1397 0.0116  -0.0185 -0.0092 64  LEU A C   
673  O O   . LEU A 64  ? 0.1504 0.1792 0.1574 0.0111  -0.0168 -0.0090 64  LEU A O   
674  C CB  . LEU A 64  ? 0.1420 0.1700 0.1381 0.0148  -0.0180 -0.0068 64  LEU A CB  
675  C CG  . LEU A 64  ? 0.1640 0.1914 0.1544 0.0182  -0.0193 -0.0050 64  LEU A CG  
676  C CD1 . LEU A 64  ? 0.1731 0.2036 0.1541 0.0234  -0.0187 -0.0041 64  LEU A CD1 
677  C CD2 . LEU A 64  ? 0.1749 0.2059 0.1701 0.0186  -0.0228 -0.0093 64  LEU A CD2 
689  N N   . GLU A 65  ? 0.1261 0.1482 0.1327 0.0122  -0.0196 -0.0110 65  GLU A N   
690  C CA  . GLU A 65  ? 0.1348 0.1556 0.1424 0.0142  -0.0198 -0.0126 65  GLU A CA  
691  C C   . GLU A 65  ? 0.1242 0.1490 0.1325 0.0157  -0.0191 -0.0156 65  GLU A C   
692  O O   . GLU A 65  ? 0.1370 0.1656 0.1441 0.0152  -0.0185 -0.0168 65  GLU A O   
693  C CB  . GLU A 65  ? 0.1583 0.1702 0.1635 0.0152  -0.0193 -0.0126 65  GLU A CB  
694  C CG  . GLU A 65  ? 0.1813 0.1890 0.1835 0.0174  -0.0203 -0.0105 65  GLU A CG  
695  C CD  . GLU A 65  ? 0.1752 0.1842 0.1763 0.0224  -0.0223 -0.0116 65  GLU A CD  
696  O OE1 . GLU A 65  ? 0.1920 0.2010 0.1908 0.0254  -0.0247 -0.0114 65  GLU A OE1 
697  O OE2 . GLU A 65  ? 0.1724 0.1837 0.1748 0.0244  -0.0221 -0.0137 65  GLU A OE2 
704  N N   . LYS A 66  ? 0.1269 0.1508 0.1357 0.0190  -0.0195 -0.0172 66  LYS A N   
705  C CA  . LYS A 66  ? 0.1408 0.1669 0.1499 0.0217  -0.0187 -0.0206 66  LYS A CA  
706  C C   . LYS A 66  ? 0.1332 0.1528 0.1405 0.0208  -0.0177 -0.0234 66  LYS A C   
707  O O   . LYS A 66  ? 0.1460 0.1595 0.1531 0.0181  -0.0171 -0.0228 66  LYS A O   
708  C CB  . LYS A 66  ? 0.1691 0.1938 0.1782 0.0274  -0.0199 -0.0217 66  LYS A CB  
709  C CG  . LYS A 66  ? 0.1763 0.1863 0.1792 0.0305  -0.0196 -0.0203 66  LYS A CG  
710  C CD  . LYS A 66  ? 0.2088 0.2160 0.2080 0.0389  -0.0214 -0.0206 66  LYS A CD  
711  C CE  . LYS A 66  ? 0.2350 0.2495 0.2353 0.0412  -0.0252 -0.0197 66  LYS A CE  
712  N NZ  . LYS A 66  ? 0.2100 0.2157 0.2048 0.0393  -0.0247 -0.0159 66  LYS A NZ  
726  N N   . SER A 67  ? 0.1430 0.1652 0.1502 0.0227  -0.0172 -0.0277 67  SER A N   
727  C CA  . SER A 67  ? 0.1534 0.1709 0.1607 0.0214  -0.0164 -0.0330 67  SER A CA  
728  C C   . SER A 67  ? 0.1437 0.1649 0.1528 0.0172  -0.0174 -0.0338 67  SER A C   
729  O O   . SER A 67  ? 0.1710 0.1862 0.1831 0.0138  -0.0163 -0.0352 67  SER A O   
730  C CB  . SER A 67  ? 0.1809 0.1833 0.1871 0.0226  -0.0141 -0.0338 67  SER A CB  
731  O OG  . SER A 67  ? 0.2668 0.2673 0.2707 0.0286  -0.0139 -0.0351 67  SER A OG  
737  N N   . GLN A 68  ? 0.1478 0.1792 0.1546 0.0180  -0.0190 -0.0328 68  GLN A N   
738  C CA  . GLN A 68  ? 0.1464 0.1826 0.1528 0.0167  -0.0208 -0.0325 68  GLN A CA  
739  C C   . GLN A 68  ? 0.1590 0.2027 0.1650 0.0183  -0.0233 -0.0403 68  GLN A C   
740  O O   . GLN A 68  ? 0.1662 0.2165 0.1655 0.0224  -0.0241 -0.0408 68  GLN A O   
741  C CB  . GLN A 68  ? 0.1437 0.1833 0.1453 0.0181  -0.0204 -0.0258 68  GLN A CB  
742  C CG  . GLN A 68  ? 0.1511 0.1924 0.1509 0.0182  -0.0222 -0.0237 68  GLN A CG  
743  C CD  . GLN A 68  ? 0.1528 0.1892 0.1580 0.0150  -0.0223 -0.0230 68  GLN A CD  
744  O OE1 . GLN A 68  ? 0.1761 0.2158 0.1846 0.0144  -0.0239 -0.0264 68  GLN A OE1 
745  N NE2 . GLN A 68  ? 0.1486 0.1785 0.1550 0.0133  -0.0206 -0.0192 68  GLN A NE2 
754  N N   . ALA A 69  ? 0.1569 0.2002 0.1702 0.0149  -0.0241 -0.0469 69  ALA A N   
755  C CA  . ALA A 69  ? 0.1773 0.2303 0.1934 0.0158  -0.0276 -0.0574 69  ALA A CA  
756  C C   . ALA A 69  ? 0.1796 0.2338 0.1918 0.0189  -0.0278 -0.0628 69  ALA A C   
757  O O   . ALA A 69  ? 0.1792 0.2440 0.1879 0.0231  -0.0317 -0.0697 69  ALA A O   
758  C CB  . ALA A 69  ? 0.1792 0.2441 0.1906 0.0204  -0.0320 -0.0569 69  ALA A CB  
764  N N   . GLN A 70  ? 0.1957 0.2391 0.2080 0.0181  -0.0240 -0.0605 70  GLN A N   
765  C CA  . GLN A 70  ? 0.1934 0.2379 0.2011 0.0223  -0.0237 -0.0645 70  GLN A CA  
766  C C   . GLN A 70  ? 0.2187 0.2646 0.2311 0.0213  -0.0254 -0.0776 70  GLN A C   
767  O O   . GLN A 70  ? 0.2181 0.2697 0.2251 0.0260  -0.0269 -0.0831 70  GLN A O   
768  C CB  . GLN A 70  ? 0.2177 0.2518 0.2246 0.0234  -0.0199 -0.0593 70  GLN A CB  
769  C CG  . GLN A 70  ? 0.2200 0.2390 0.2318 0.0207  -0.0170 -0.0627 70  GLN A CG  
770  C CD  . GLN A 70  ? 0.2089 0.2194 0.2253 0.0152  -0.0150 -0.0590 70  GLN A CD  
771  O OE1 . GLN A 70  ? 0.2309 0.2457 0.2466 0.0143  -0.0160 -0.0522 70  GLN A OE1 
772  N NE2 . GLN A 70  ? 0.2384 0.2356 0.2593 0.0113  -0.0110 -0.0636 70  GLN A NE2 
781  N N   . ASN A 71  ? 0.1955 0.2359 0.2183 0.0148  -0.0243 -0.0837 71  ASN A N   
782  C CA  . ASN A 71  ? 0.1933 0.2353 0.2233 0.0123  -0.0254 -0.0984 71  ASN A CA  
783  C C   . ASN A 71  ? 0.2167 0.2790 0.2468 0.0155  -0.0327 -0.1077 71  ASN A C   
784  O O   . ASN A 71  ? 0.2068 0.2748 0.2400 0.0162  -0.0355 -0.1214 71  ASN A O   
785  C CB  . ASN A 71  ? 0.2150 0.2435 0.2576 0.0031  -0.0200 -0.1028 71  ASN A CB  
786  C CG  . ASN A 71  ? 0.2303 0.2358 0.2689 0.0029  -0.0128 -0.0952 71  ASN A CG  
787  O OD1 . ASN A 71  ? 0.3345 0.3359 0.3636 0.0096  -0.0129 -0.0904 71  ASN A OD1 
788  N ND2 . ASN A 71  ? 0.2665 0.2574 0.3116 -0.0040 -0.0062 -0.0940 71  ASN A ND2 
795  N N   . THR A 72  ? 0.2049 0.2777 0.2305 0.0186  -0.0361 -0.1013 72  THR A N   
796  C CA  . THR A 72  ? 0.2162 0.3078 0.2376 0.0251  -0.0436 -0.1084 72  THR A CA  
797  C C   . THR A 72  ? 0.2243 0.3202 0.2267 0.0354  -0.0450 -0.1024 72  THR A C   
798  O O   . THR A 72  ? 0.2427 0.3501 0.2382 0.0423  -0.0500 -0.1116 72  THR A O   
799  C CB  . THR A 72  ? 0.2132 0.3125 0.2376 0.0251  -0.0461 -0.1042 72  THR A CB  
800  O OG1 . THR A 72  ? 0.1984 0.2963 0.2413 0.0155  -0.0439 -0.1109 72  THR A OG1 
801  C CG2 . THR A 72  ? 0.2270 0.3453 0.2434 0.0351  -0.0545 -0.1105 72  THR A CG2 
809  N N   . TYR A 73  ? 0.2219 0.3093 0.2159 0.0366  -0.0401 -0.0878 73  TYR A N   
810  C CA  . TYR A 73  ? 0.2353 0.3259 0.2122 0.0450  -0.0391 -0.0808 73  TYR A CA  
811  C C   . TYR A 73  ? 0.2173 0.3026 0.1905 0.0461  -0.0343 -0.0798 73  TYR A C   
812  O O   . TYR A 73  ? 0.2746 0.3639 0.2341 0.0529  -0.0322 -0.0760 73  TYR A O   
813  C CB  . TYR A 73  ? 0.2443 0.3309 0.2151 0.0456  -0.0363 -0.0667 73  TYR A CB  
814  C CG  . TYR A 73  ? 0.2498 0.3436 0.2207 0.0481  -0.0416 -0.0680 73  TYR A CG  
815  C CD1 . TYR A 73  ? 0.2612 0.3520 0.2445 0.0416  -0.0419 -0.0667 73  TYR A CD1 
816  C CD2 . TYR A 73  ? 0.2812 0.3857 0.2388 0.0585  -0.0467 -0.0715 73  TYR A CD2 
817  C CE1 . TYR A 73  ? 0.2842 0.3841 0.2686 0.0450  -0.0471 -0.0692 73  TYR A CE1 
818  C CE2 . TYR A 73  ? 0.3554 0.4685 0.3125 0.0632  -0.0526 -0.0738 73  TYR A CE2 
819  C CZ  . TYR A 73  ? 0.3316 0.4430 0.3032 0.0561  -0.0529 -0.0730 73  TYR A CZ  
820  O OH  . TYR A 73  ? 0.3939 0.5162 0.3655 0.0621  -0.0591 -0.0764 73  TYR A OH  
830  N N   . GLY A 74  ? 0.2164 0.2927 0.2003 0.0404  -0.0319 -0.0833 74  GLY A N   
831  C CA  . GLY A 74  ? 0.2143 0.2862 0.1959 0.0426  -0.0281 -0.0839 74  GLY A CA  
832  C C   . GLY A 74  ? 0.2282 0.2938 0.2106 0.0414  -0.0226 -0.0725 74  GLY A C   
833  O O   . GLY A 74  ? 0.2635 0.3255 0.2471 0.0432  -0.0197 -0.0737 74  GLY A O   
837  N N   . SER A 75  ? 0.1949 0.2599 0.1774 0.0389  -0.0216 -0.0627 75  SER A N   
838  C CA  . SER A 75  ? 0.1951 0.2572 0.1795 0.0376  -0.0171 -0.0535 75  SER A CA  
839  C C   . SER A 75  ? 0.1807 0.2402 0.1670 0.0335  -0.0174 -0.0457 75  SER A C   
840  O O   . SER A 75  ? 0.1795 0.2416 0.1619 0.0339  -0.0200 -0.0453 75  SER A O   
841  C CB  . SER A 75  ? 0.1973 0.2670 0.1739 0.0419  -0.0124 -0.0503 75  SER A CB  
842  O OG  . SER A 75  ? 0.2138 0.2874 0.1798 0.0441  -0.0114 -0.0454 75  SER A OG  
848  N N   . THR A 76  ? 0.1594 0.2150 0.1512 0.0309  -0.0151 -0.0401 76  THR A N   
849  C CA  . THR A 76  ? 0.1586 0.2116 0.1520 0.0274  -0.0149 -0.0330 76  THR A CA  
850  C C   . THR A 76  ? 0.1511 0.2081 0.1370 0.0285  -0.0118 -0.0274 76  THR A C   
851  O O   . THR A 76  ? 0.1541 0.2084 0.1371 0.0274  -0.0127 -0.0232 76  THR A O   
852  C CB  . THR A 76  ? 0.1583 0.2081 0.1587 0.0256  -0.0137 -0.0303 76  THR A CB  
853  O OG1 . THR A 76  ? 0.1698 0.2114 0.1734 0.0256  -0.0158 -0.0338 76  THR A OG1 
854  C CG2 . THR A 76  ? 0.1547 0.2024 0.1569 0.0220  -0.0134 -0.0242 76  THR A CG2 
862  N N   . GLU A 77  ? 0.1500 0.2122 0.1317 0.0309  -0.0071 -0.0268 77  GLU A N   
863  C CA  . GLU A 77  ? 0.1731 0.2355 0.1459 0.0318  -0.0017 -0.0201 77  GLU A CA  
864  C C   . GLU A 77  ? 0.1925 0.2540 0.1524 0.0370  -0.0049 -0.0199 77  GLU A C   
865  O O   . GLU A 77  ? 0.1976 0.2540 0.1513 0.0374  -0.0039 -0.0137 77  GLU A O   
866  C CB  . GLU A 77  ? 0.1926 0.2610 0.1629 0.0336  0.0055  -0.0202 77  GLU A CB  
867  C CG  . GLU A 77  ? 0.1935 0.2668 0.1782 0.0297  0.0085  -0.0217 77  GLU A CG  
868  C CD  . GLU A 77  ? 0.1615 0.2391 0.1514 0.0331  0.0049  -0.0295 77  GLU A CD  
869  O OE1 . GLU A 77  ? 0.1693 0.2425 0.1565 0.0354  -0.0012 -0.0339 77  GLU A OE1 
870  O OE2 . GLU A 77  ? 0.1636 0.2489 0.1610 0.0336  0.0087  -0.0316 77  GLU A OE2 
877  N N   . GLU A 78  ? 0.2003 0.2671 0.1564 0.0417  -0.0094 -0.0277 78  GLU A N   
878  C CA  . GLU A 78  ? 0.1971 0.2668 0.1418 0.0481  -0.0141 -0.0298 78  GLU A CA  
879  C C   . GLU A 78  ? 0.2095 0.2781 0.1614 0.0457  -0.0204 -0.0316 78  GLU A C   
880  O O   . GLU A 78  ? 0.2161 0.2853 0.1594 0.0505  -0.0227 -0.0290 78  GLU A O   
881  C CB  . GLU A 78  ? 0.2374 0.3152 0.1770 0.0539  -0.0177 -0.0399 78  GLU A CB  
882  C CG  . GLU A 78  ? 0.3146 0.3946 0.2434 0.0585  -0.0110 -0.0380 78  GLU A CG  
883  C CD  . GLU A 78  ? 0.4883 0.5666 0.3967 0.0661  -0.0067 -0.0298 78  GLU A CD  
884  O OE1 . GLU A 78  ? 0.5138 0.5899 0.4147 0.0669  0.0031  -0.0235 78  GLU A OE1 
885  O OE2 . GLU A 78  ? 0.5179 0.5961 0.4182 0.0711  -0.0120 -0.0292 78  GLU A OE2 
892  N N   . GLY A 79  ? 0.1843 0.2509 0.1509 0.0391  -0.0224 -0.0357 79  GLY A N   
893  C CA  . GLY A 79  ? 0.1781 0.2439 0.1522 0.0361  -0.0266 -0.0372 79  GLY A CA  
894  C C   . GLY A 79  ? 0.1955 0.2551 0.1676 0.0348  -0.0243 -0.0277 79  GLY A C   
895  O O   . GLY A 79  ? 0.1852 0.2463 0.1569 0.0366  -0.0276 -0.0276 79  GLY A O   
899  N N   . THR A 80  ? 0.1663 0.2199 0.1384 0.0319  -0.0187 -0.0207 80  THR A N   
900  C CA  . THR A 80  ? 0.1866 0.2333 0.1570 0.0301  -0.0157 -0.0126 80  THR A CA  
901  C C   . THR A 80  ? 0.1830 0.2277 0.1382 0.0369  -0.0143 -0.0076 80  THR A C   
902  O O   . THR A 80  ? 0.1961 0.2364 0.1481 0.0387  -0.0157 -0.0042 80  THR A O   
903  C CB  . THR A 80  ? 0.1596 0.2030 0.1351 0.0252  -0.0100 -0.0089 80  THR A CB  
904  O OG1 . THR A 80  ? 0.1652 0.2095 0.1520 0.0215  -0.0124 -0.0131 80  THR A OG1 
905  C CG2 . THR A 80  ? 0.1988 0.2345 0.1735 0.0224  -0.0063 -0.0022 80  THR A CG2 
913  N N   . LEU A 81  ? 0.1994 0.2461 0.1435 0.0418  -0.0110 -0.0067 81  LEU A N   
914  C CA  . LEU A 81  ? 0.2111 0.2534 0.1364 0.0503  -0.0085 -0.0007 81  LEU A CA  
915  C C   . LEU A 81  ? 0.2202 0.2686 0.1399 0.0584  -0.0173 -0.0052 81  LEU A C   
916  O O   . LEU A 81  ? 0.2493 0.2914 0.1585 0.0644  -0.0174 0.0004  81  LEU A O   
917  C CB  . LEU A 81  ? 0.2424 0.2865 0.1555 0.0548  -0.0028 0.0005  81  LEU A CB  
918  C CG  . LEU A 81  ? 0.2589 0.2978 0.1761 0.0478  0.0082  0.0059  81  LEU A CG  
919  C CD1 . LEU A 81  ? 0.2984 0.3428 0.2058 0.0526  0.0128  0.0043  81  LEU A CD1 
920  C CD2 . LEU A 81  ? 0.2769 0.3013 0.1870 0.0461  0.0169  0.0165  81  LEU A CD2 
932  N N   . ALA A 82  ? 0.2036 0.2642 0.1317 0.0587  -0.0247 -0.0163 82  ALA A N   
933  C CA  . ALA A 82  ? 0.2259 0.2968 0.1525 0.0659  -0.0335 -0.0235 82  ALA A CA  
934  C C   . ALA A 82  ? 0.2124 0.2814 0.1494 0.0624  -0.0359 -0.0224 82  ALA A C   
935  O O   . ALA A 82  ? 0.2360 0.3080 0.1659 0.0707  -0.0402 -0.0221 82  ALA A O   
936  C CB  . ALA A 82  ? 0.2325 0.3167 0.1696 0.0644  -0.0396 -0.0373 82  ALA A CB  
942  N N   . THR A 83  ? 0.1893 0.2538 0.1419 0.0515  -0.0334 -0.0222 83  THR A N   
943  C CA  . THR A 83  ? 0.2001 0.2627 0.1622 0.0479  -0.0348 -0.0214 83  THR A CA  
944  C C   . THR A 83  ? 0.2014 0.2524 0.1522 0.0518  -0.0313 -0.0110 83  THR A C   
945  O O   . THR A 83  ? 0.2036 0.2560 0.1531 0.0567  -0.0346 -0.0109 83  THR A O   
946  C CB  . THR A 83  ? 0.1746 0.2327 0.1515 0.0371  -0.0319 -0.0224 83  THR A CB  
947  O OG1 . THR A 83  ? 0.1861 0.2515 0.1720 0.0340  -0.0341 -0.0320 83  THR A OG1 
948  C CG2 . THR A 83  ? 0.1919 0.2473 0.1765 0.0339  -0.0323 -0.0212 83  THR A CG2 
956  N N   . ALA A 84  ? 0.1992 0.2388 0.1430 0.0494  -0.0241 -0.0028 84  ALA A N   
957  C CA  . ALA A 84  ? 0.2254 0.2509 0.1598 0.0513  -0.0190 0.0066  84  ALA A CA  
958  C C   . ALA A 84  ? 0.2289 0.2523 0.1445 0.0645  -0.0207 0.0100  84  ALA A C   
959  O O   . ALA A 84  ? 0.2345 0.2497 0.1442 0.0691  -0.0207 0.0145  84  ALA A O   
960  C CB  . ALA A 84  ? 0.2268 0.2422 0.1598 0.0450  -0.0097 0.0128  84  ALA A CB  
966  N N   . SER A 85  ? 0.2268 0.2571 0.1310 0.0721  -0.0223 0.0079  85  SER A N   
967  C CA  . SER A 85  ? 0.2731 0.3026 0.1563 0.0875  -0.0251 0.0105  85  SER A CA  
968  C C   . SER A 85  ? 0.2489 0.2903 0.1381 0.0939  -0.0352 0.0034  85  SER A C   
969  O O   . SER A 85  ? 0.2730 0.3076 0.1491 0.1046  -0.0363 0.0084  85  SER A O   
970  C CB  . SER A 85  ? 0.2688 0.3079 0.1407 0.0948  -0.0270 0.0063  85  SER A CB  
971  O OG  . SER A 85  ? 0.3324 0.3748 0.1836 0.1121  -0.0324 0.0065  85  SER A OG  
977  N N   . ALA A 86  ? 0.2344 0.2932 0.1439 0.0877  -0.0419 -0.0086 86  ALA A N   
978  C CA  . ALA A 86  ? 0.2385 0.3121 0.1574 0.0925  -0.0506 -0.0174 86  ALA A CA  
979  C C   . ALA A 86  ? 0.2301 0.2943 0.1546 0.0896  -0.0483 -0.0121 86  ALA A C   
980  O O   . ALA A 86  ? 0.2538 0.3228 0.1746 0.0997  -0.0532 -0.0134 86  ALA A O   
981  C CB  . ALA A 86  ? 0.2394 0.3313 0.1805 0.0839  -0.0555 -0.0315 86  ALA A CB  
987  N N   . ILE A 87  ? 0.2160 0.2679 0.1494 0.0770  -0.0414 -0.0070 87  ILE A N   
988  C CA  . ILE A 87  ? 0.2293 0.2711 0.1664 0.0743  -0.0389 -0.0022 87  ILE A CA  
989  C C   . ILE A 87  ? 0.2450 0.2710 0.1618 0.0853  -0.0361 0.0075  87  ILE A C   
990  O O   . ILE A 87  ? 0.2534 0.2783 0.1683 0.0923  -0.0388 0.0079  87  ILE A O   
991  C CB  . ILE A 87  ? 0.1959 0.2274 0.1430 0.0605  -0.0324 0.0011  87  ILE A CB  
992  C CG1 . ILE A 87  ? 0.1994 0.2428 0.1649 0.0512  -0.0345 -0.0074 87  ILE A CG1 
993  C CG2 . ILE A 87  ? 0.2285 0.2470 0.1758 0.0588  -0.0293 0.0064  87  ILE A CG2 
994  C CD1 . ILE A 87  ? 0.1924 0.2270 0.1643 0.0407  -0.0293 -0.0045 87  ILE A CD1 
1006 N N   . LYS A 88  ? 0.2575 0.2696 0.1584 0.0870  -0.0295 0.0157  88  LYS A N   
1007 C CA  . LYS A 88  ? 0.2799 0.2711 0.1602 0.0958  -0.0238 0.0266  88  LYS A CA  
1008 C C   . LYS A 88  ? 0.3268 0.3234 0.1904 0.1147  -0.0307 0.0259  88  LYS A C   
1009 O O   . LYS A 88  ? 0.3461 0.3279 0.1977 0.1228  -0.0281 0.0319  88  LYS A O   
1010 C CB  . LYS A 88  ? 0.3165 0.2919 0.1844 0.0923  -0.0131 0.0353  88  LYS A CB  
1011 C CG  . LYS A 88  ? 0.3043 0.2734 0.1885 0.0753  -0.0060 0.0360  88  LYS A CG  
1012 C CD  . LYS A 88  ? 0.3071 0.2580 0.1929 0.0712  -0.0008 0.0409  88  LYS A CD  
1013 C CE  . LYS A 88  ? 0.3267 0.2726 0.2273 0.0554  0.0063  0.0406  88  LYS A CE  
1014 N NZ  . LYS A 88  ? 0.3576 0.2828 0.2564 0.0522  0.0130  0.0454  88  LYS A NZ  
1028 N N   . LEU A 89  ? 0.3041 0.3218 0.1708 0.1195  -0.0382 0.0163  89  LEU A N   
1029 C CA  . LEU A 89  ? 0.3092 0.3344 0.1691 0.1325  -0.0425 0.0112  89  LEU A CA  
1030 C C   . LEU A 89  ? 0.3446 0.3794 0.2178 0.1342  -0.0480 0.0047  89  LEU A C   
1031 O O   . LEU A 89  ? 0.3742 0.4084 0.2383 0.1462  -0.0496 0.0037  89  LEU A O   
1032 C CB  . LEU A 89  ? 0.3267 0.3734 0.1913 0.1351  -0.0486 -0.0001 89  LEU A CB  
1033 C CG  . LEU A 89  ? 0.4047 0.4432 0.2511 0.1392  -0.0434 0.0055  89  LEU A CG  
1034 C CD1 . LEU A 89  ? 0.4625 0.5228 0.3172 0.1395  -0.0497 -0.0072 89  LEU A CD1 
1035 C CD2 . LEU A 89  ? 0.4523 0.4744 0.2741 0.1537  -0.0383 0.0139  89  LEU A CD2 
1047 N N   . LYS A 90  ? 0.3270 0.3707 0.2209 0.1233  -0.0506 0.0001  90  LYS A N   
1048 C CA  . LYS A 90  ? 0.2990 0.3517 0.2062 0.1241  -0.0544 -0.0058 90  LYS A CA  
1049 C C   . LYS A 90  ? 0.3491 0.3799 0.2493 0.1246  -0.0492 0.0044  90  LYS A C   
1050 O O   . LYS A 90  ? 0.3928 0.4233 0.2921 0.1317  -0.0505 0.0029  90  LYS A O   
1051 C CB  . LYS A 90  ? 0.2974 0.3703 0.2309 0.1123  -0.0584 -0.0163 90  LYS A CB  
1052 C CG  . LYS A 90  ? 0.4071 0.5033 0.3526 0.1111  -0.0636 -0.0299 90  LYS A CG  
1053 C CD  . LYS A 90  ? 0.4624 0.5697 0.4028 0.1239  -0.0679 -0.0370 90  LYS A CD  
1054 C CE  . LYS A 90  ? 0.5105 0.6388 0.4610 0.1232  -0.0725 -0.0507 90  LYS A CE  
1055 N NZ  . LYS A 90  ? 0.4912 0.6409 0.4681 0.1156  -0.0754 -0.0648 90  LYS A NZ  
1069 N N   . ASN A 91  ? 0.2497 0.3944 0.2634 0.1201  -0.0430 0.0033  91  ASN A N   
1070 C CA  . ASN A 91  ? 0.2382 0.3631 0.2473 0.1236  -0.0380 0.0084  91  ASN A CA  
1071 C C   . ASN A 91  ? 0.2469 0.3488 0.2442 0.1202  -0.0349 0.0142  91  ASN A C   
1072 O O   . ASN A 91  ? 0.2318 0.3251 0.2295 0.1098  -0.0320 0.0122  91  ASN A O   
1073 C CB  . ASN A 91  ? 0.2518 0.3776 0.2707 0.1179  -0.0340 0.0036  91  ASN A CB  
1074 C CG  . ASN A 91  ? 0.3345 0.4404 0.3484 0.1215  -0.0294 0.0070  91  ASN A CG  
1075 O OD1 . ASN A 91  ? 0.2934 0.3885 0.3001 0.1304  -0.0297 0.0126  91  ASN A OD1 
1076 N ND2 . ASN A 91  ? 0.4016 0.5034 0.4198 0.1154  -0.0253 0.0035  91  ASN A ND2 
1083 N N   . ASN A 92  ? 0.2409 0.3332 0.2282 0.1294  -0.0353 0.0220  92  ASN A N   
1084 C CA  A ASN A 92  ? 0.2711 0.3422 0.2487 0.1264  -0.0317 0.0284  92  ASN A CA  
1085 C CA  B ASN A 92  ? 0.2698 0.3408 0.2473 0.1263  -0.0317 0.0284  92  ASN A CA  
1086 C C   . ASN A 92  ? 0.2751 0.3253 0.2539 0.1220  -0.0263 0.0288  92  ASN A C   
1087 O O   . ASN A 92  ? 0.3224 0.3563 0.2963 0.1164  -0.0232 0.0321  92  ASN A O   
1088 C CB  A ASN A 92  ? 0.3183 0.3834 0.2855 0.1341  -0.0315 0.0367  92  ASN A CB  
1089 C CB  B ASN A 92  ? 0.3150 0.3796 0.2822 0.1341  -0.0314 0.0368  92  ASN A CB  
1090 C CG  A ASN A 92  ? 0.3180 0.3766 0.2856 0.1422  -0.0298 0.0401  92  ASN A CG  
1091 C CG  B ASN A 92  ? 0.3579 0.4383 0.3202 0.1343  -0.0353 0.0358  92  ASN A CG  
1092 O OD1 A ASN A 92  ? 0.4299 0.4787 0.4025 0.1429  -0.0274 0.0388  92  ASN A OD1 
1093 O OD1 B ASN A 92  ? 0.3740 0.4645 0.3386 0.1280  -0.0379 0.0304  92  ASN A OD1 
1094 N ND2 A ASN A 92  ? 0.4123 0.4761 0.3740 0.1490  -0.0312 0.0443  92  ASN A ND2 
1095 N ND2 B ASN A 92  ? 0.4047 0.4871 0.3603 0.1418  -0.0358 0.0405  92  ASN A ND2 
1108 N N   . LYS A 93  ? 0.2633 0.3150 0.2489 0.1243  -0.0254 0.0249  93  LYS A N   
1109 C CA  . LYS A 93  ? 0.2712 0.3044 0.2577 0.1210  -0.0210 0.0238  93  LYS A CA  
1110 C C   . LYS A 93  ? 0.2794 0.3141 0.2700 0.1092  -0.0193 0.0175  93  LYS A C   
1111 O O   . LYS A 93  ? 0.2738 0.2934 0.2637 0.1053  -0.0162 0.0162  93  LYS A O   
1112 C CB  . LYS A 93  ? 0.2732 0.3069 0.2639 0.1301  -0.0205 0.0220  93  LYS A CB  
1113 C CG  . LYS A 93  ? 0.3172 0.3423 0.3036 0.1414  -0.0206 0.0290  93  LYS A CG  
1114 C CD  . LYS A 93  ? 0.4094 0.4270 0.3997 0.1468  -0.0184 0.0263  93  LYS A CD  
1115 C CE  . LYS A 93  ? 0.4955 0.5074 0.4830 0.1549  -0.0184 0.0323  93  LYS A CE  
1116 N NZ  . LYS A 93  ? 0.5873 0.5773 0.5687 0.1540  -0.0157 0.0402  93  LYS A NZ  
1130 N N   . ALA A 94  ? 0.2056 0.2579 0.2010 0.1036  -0.0213 0.0133  94  ALA A N   
1131 C CA  . ALA A 94  ? 0.2069 0.2597 0.2057 0.0928  -0.0193 0.0088  94  ALA A CA  
1132 C C   . ALA A 94  ? 0.2108 0.2492 0.2033 0.0858  -0.0180 0.0114  94  ALA A C   
1133 O O   . ALA A 94  ? 0.2464 0.2838 0.2337 0.0868  -0.0196 0.0154  94  ALA A O   
1134 C CB  . ALA A 94  ? 0.2247 0.2985 0.2313 0.0886  -0.0216 0.0045  94  ALA A CB  
1140 N N   . LYS A 95  ? 0.1766 0.2050 0.1693 0.0794  -0.0151 0.0092  95  LYS A N   
1141 C CA  . LYS A 95  ? 0.1852 0.2015 0.1736 0.0724  -0.0138 0.0110  95  LYS A CA  
1142 C C   . LYS A 95  ? 0.1900 0.2155 0.1812 0.0639  -0.0140 0.0078  95  LYS A C   
1143 O O   . LYS A 95  ? 0.1870 0.2198 0.1835 0.0608  -0.0129 0.0038  95  LYS A O   
1144 C CB  . LYS A 95  ? 0.2048 0.2053 0.1922 0.0707  -0.0111 0.0097  95  LYS A CB  
1145 C CG  . LYS A 95  ? 0.1969 0.1844 0.1826 0.0783  -0.0104 0.0124  95  LYS A CG  
1146 C CD  . LYS A 95  ? 0.2481 0.2261 0.2293 0.0801  -0.0101 0.0197  95  LYS A CD  
1147 C CE  . LYS A 95  ? 0.2790 0.2413 0.2600 0.0869  -0.0085 0.0227  95  LYS A CE  
1148 N NZ  . LYS A 95  ? 0.3340 0.2857 0.3110 0.0885  -0.0068 0.0313  95  LYS A NZ  
1162 N N   . VAL A 96  ? 0.1748 0.1993 0.1626 0.0603  -0.0149 0.0099  96  VAL A N   
1163 C CA  . VAL A 96  ? 0.1681 0.2005 0.1588 0.0529  -0.0153 0.0068  96  VAL A CA  
1164 C C   . VAL A 96  ? 0.1773 0.1974 0.1641 0.0468  -0.0133 0.0082  96  VAL A C   
1165 O O   . VAL A 96  ? 0.1861 0.1977 0.1673 0.0481  -0.0129 0.0124  96  VAL A O   
1166 C CB  . VAL A 96  ? 0.1784 0.2236 0.1690 0.0550  -0.0190 0.0063  96  VAL A CB  
1167 C CG1 . VAL A 96  ? 0.1996 0.2506 0.1940 0.0471  -0.0193 0.0023  96  VAL A CG1 
1168 C CG2 . VAL A 96  ? 0.2019 0.2616 0.1983 0.0608  -0.0214 0.0040  96  VAL A CG2 
1178 N N   . LEU A 97  ? 0.1476 0.1675 0.1377 0.0405  -0.0116 0.0052  97  LEU A N   
1179 C CA  . LEU A 97  ? 0.1500 0.1603 0.1376 0.0348  -0.0100 0.0059  97  LEU A CA  
1180 C C   . LEU A 97  ? 0.1446 0.1610 0.1342 0.0293  -0.0104 0.0040  97  LEU A C   
1181 O O   . LEU A 97  ? 0.1587 0.1851 0.1540 0.0273  -0.0108 0.0010  97  LEU A O   
1182 C CB  . LEU A 97  ? 0.1539 0.1585 0.1428 0.0328  -0.0080 0.0039  97  LEU A CB  
1183 C CG  . LEU A 97  ? 0.1614 0.1596 0.1493 0.0381  -0.0076 0.0037  97  LEU A CG  
1184 C CD1 . LEU A 97  ? 0.1909 0.1853 0.1790 0.0359  -0.0062 0.0006  97  LEU A CD1 
1185 C CD2 . LEU A 97  ? 0.1971 0.1836 0.1816 0.0407  -0.0077 0.0073  97  LEU A CD2 
1197 N N   . TYR A 98  ? 0.1555 0.1655 0.1414 0.0264  -0.0098 0.0057  98  TYR A N   
1198 C CA  . TYR A 98  ? 0.1411 0.1546 0.1284 0.0214  -0.0098 0.0037  98  TYR A CA  
1199 C C   . TYR A 98  ? 0.1425 0.1506 0.1318 0.0164  -0.0076 0.0028  98  TYR A C   
1200 O O   . TYR A 98  ? 0.1614 0.1607 0.1480 0.0157  -0.0064 0.0046  98  TYR A O   
1201 C CB  . TYR A 98  ? 0.1793 0.1894 0.1608 0.0222  -0.0099 0.0063  98  TYR A CB  
1202 C CG  . TYR A 98  ? 0.1603 0.1738 0.1422 0.0183  -0.0102 0.0037  98  TYR A CG  
1203 C CD1 . TYR A 98  ? 0.1623 0.1856 0.1490 0.0168  -0.0122 -0.0011 98  TYR A CD1 
1204 C CD2 . TYR A 98  ? 0.1703 0.1776 0.1486 0.0164  -0.0084 0.0058  98  TYR A CD2 
1205 C CE1 . TYR A 98  ? 0.1737 0.1994 0.1611 0.0138  -0.0127 -0.0044 98  TYR A CE1 
1206 C CE2 . TYR A 98  ? 0.1712 0.1818 0.1494 0.0139  -0.0086 0.0031  98  TYR A CE2 
1207 C CZ  . TYR A 98  ? 0.1562 0.1754 0.1387 0.0127  -0.0109 -0.0023 98  TYR A CZ  
1208 O OH  . TYR A 98  ? 0.2093 0.2312 0.1922 0.0106  -0.0114 -0.0062 98  TYR A OH  
1218 N N   . TYR A 99  ? 0.1417 0.1553 0.1362 0.0130  -0.0071 0.0002  99  TYR A N   
1219 C CA  . TYR A 99  ? 0.1302 0.1394 0.1259 0.0091  -0.0048 0.0002  99  TYR A CA  
1220 C C   . TYR A 99  ? 0.1442 0.1482 0.1371 0.0066  -0.0047 0.0008  99  TYR A C   
1221 O O   . TYR A 99  ? 0.1404 0.1474 0.1332 0.0060  -0.0058 -0.0004 99  TYR A O   
1222 C CB  . TYR A 99  ? 0.1308 0.1467 0.1336 0.0061  -0.0036 -0.0016 99  TYR A CB  
1223 C CG  . TYR A 99  ? 0.1269 0.1390 0.1310 0.0028  -0.0010 -0.0006 99  TYR A CG  
1224 C CD1 . TYR A 99  ? 0.1405 0.1492 0.1448 -0.0002 -0.0009 -0.0011 99  TYR A CD1 
1225 C CD2 . TYR A 99  ? 0.1450 0.1574 0.1497 0.0035  0.0015  0.0010  99  TYR A CD2 
1226 C CE1 . TYR A 99  ? 0.1417 0.1466 0.1471 -0.0023 0.0015  0.0004  99  TYR A CE1 
1227 C CE2 . TYR A 99  ? 0.1432 0.1524 0.1479 0.0017  0.0039  0.0028  99  TYR A CE2 
1228 C CZ  . TYR A 99  ? 0.1444 0.1496 0.1496 -0.0011 0.0038  0.0027  99  TYR A CZ  
1229 O OH  . TYR A 99  ? 0.1681 0.1701 0.1732 -0.0020 0.0062  0.0050  99  TYR A OH  
1239 N N   . ARG A 100 ? 0.1396 0.1371 0.1309 0.0053  -0.0035 0.0020  100 ARG A N   
1240 C CA  . ARG A 100 ? 0.1406 0.1349 0.1311 0.0027  -0.0028 0.0022  100 ARG A CA  
1241 C C   . ARG A 100 ? 0.1431 0.1344 0.1345 0.0011  -0.0016 0.0024  100 ARG A C   
1242 O O   . ARG A 100 ? 0.1509 0.1396 0.1410 0.0025  -0.0018 0.0026  100 ARG A O   
1243 C CB  . ARG A 100 ? 0.1600 0.1502 0.1469 0.0038  -0.0030 0.0042  100 ARG A CB  
1244 C CG  . ARG A 100 ? 0.1608 0.1507 0.1471 0.0018  -0.0021 0.0043  100 ARG A CG  
1245 C CD  . ARG A 100 ? 0.1829 0.1789 0.1683 0.0026  -0.0032 0.0023  100 ARG A CD  
1246 N NE  . ARG A 100 ? 0.1781 0.1742 0.1613 0.0021  -0.0022 0.0022  100 ARG A NE  
1247 C CZ  . ARG A 100 ? 0.1610 0.1594 0.1459 0.0006  -0.0023 -0.0011 100 ARG A CZ  
1248 N NH1 . ARG A 100 ? 0.1637 0.1638 0.1538 -0.0014 -0.0029 -0.0044 100 ARG A NH1 
1249 N NH2 . ARG A 100 ? 0.1837 0.1828 0.1656 0.0013  -0.0012 -0.0012 100 ARG A NH2 
1263 N N   . ASN A 101 ? 0.1343 0.1262 0.1279 -0.0011 -0.0006 0.0020  101 ASN A N   
1264 C CA  . ASN A 101 ? 0.1312 0.1210 0.1250 -0.0016 0.0005  0.0029  101 ASN A CA  
1265 C C   . ASN A 101 ? 0.1335 0.1200 0.1261 -0.0023 0.0000  0.0031  101 ASN A C   
1266 O O   . ASN A 101 ? 0.1485 0.1350 0.1414 -0.0033 0.0003  0.0028  101 ASN A O   
1267 C CB  . ASN A 101 ? 0.1421 0.1330 0.1396 -0.0032 0.0024  0.0033  101 ASN A CB  
1268 C CG  . ASN A 101 ? 0.1215 0.1115 0.1183 -0.0021 0.0038  0.0055  101 ASN A CG  
1269 O OD1 . ASN A 101 ? 0.1425 0.1304 0.1376 -0.0015 0.0034  0.0060  101 ASN A OD1 
1270 N ND2 . ASN A 101 ? 0.1500 0.1425 0.1477 -0.0011 0.0057  0.0071  101 ASN A ND2 
1277 N N   . VAL A 102 ? 0.1411 0.1261 0.1328 -0.0015 -0.0007 0.0030  102 VAL A N   
1278 C CA  . VAL A 102 ? 0.1476 0.1308 0.1403 -0.0025 -0.0012 0.0028  102 VAL A CA  
1279 C C   . VAL A 102 ? 0.1504 0.1347 0.1447 -0.0032 -0.0003 0.0032  102 VAL A C   
1280 O O   . VAL A 102 ? 0.1672 0.1513 0.1633 -0.0043 -0.0001 0.0032  102 VAL A O   
1281 C CB  . VAL A 102 ? 0.1648 0.1466 0.1577 -0.0017 -0.0029 0.0012  102 VAL A CB  
1282 C CG1 . VAL A 102 ? 0.1659 0.1506 0.1577 0.0002  -0.0039 0.0001  102 VAL A CG1 
1283 C CG2 . VAL A 102 ? 0.1829 0.1628 0.1794 -0.0037 -0.0030 0.0009  102 VAL A CG2 
1293 N N   . VAL A 103 ? 0.1454 0.1306 0.1398 -0.0024 0.0005  0.0040  103 VAL A N   
1294 C CA  . VAL A 103 ? 0.1426 0.1277 0.1386 -0.0022 0.0015  0.0047  103 VAL A CA  
1295 C C   . VAL A 103 ? 0.1556 0.1394 0.1536 -0.0026 0.0035  0.0054  103 VAL A C   
1296 O O   . VAL A 103 ? 0.1657 0.1483 0.1655 -0.0025 0.0044  0.0053  103 VAL A O   
1297 C CB  . VAL A 103 ? 0.1707 0.1577 0.1660 0.0003  0.0004  0.0054  103 VAL A CB  
1298 C CG1 . VAL A 103 ? 0.1936 0.1824 0.1903 -0.0001 -0.0018 0.0032  103 VAL A CG1 
1299 C CG2 . VAL A 103 ? 0.1610 0.1492 0.1532 0.0026  0.0006  0.0067  103 VAL A CG2 
1309 N N   . ILE A 104 ? 0.1485 0.1324 0.1472 -0.0032 0.0045  0.0059  104 ILE A N   
1310 C CA  . ILE A 104 ? 0.1525 0.1345 0.1555 -0.0044 0.0068  0.0062  104 ILE A CA  
1311 C C   . ILE A 104 ? 0.1501 0.1327 0.1553 -0.0066 0.0060  0.0024  104 ILE A C   
1312 O O   . ILE A 104 ? 0.1594 0.1450 0.1634 -0.0070 0.0045  0.0008  104 ILE A O   
1313 C CB  . ILE A 104 ? 0.1494 0.1324 0.1540 -0.0043 0.0088  0.0088  104 ILE A CB  
1314 C CG1 . ILE A 104 ? 0.1682 0.1519 0.1686 -0.0008 0.0095  0.0126  104 ILE A CG1 
1315 C CG2 . ILE A 104 ? 0.1625 0.1428 0.1742 -0.0065 0.0116  0.0090  104 ILE A CG2 
1316 C CD1 . ILE A 104 ? 0.2088 0.1949 0.2092 0.0004  0.0121  0.0157  104 ILE A CD1 
1328 N N   . ASN A 105 ? 0.1516 0.1317 0.1601 -0.0073 0.0069  0.0005  105 ASN A N   
1329 C CA  . ASN A 105 ? 0.1467 0.1281 0.1569 -0.0087 0.0058  -0.0044 105 ASN A CA  
1330 C C   . ASN A 105 ? 0.1438 0.1252 0.1612 -0.0112 0.0066  -0.0067 105 ASN A C   
1331 O O   . ASN A 105 ? 0.1652 0.1430 0.1884 -0.0125 0.0079  -0.0091 105 ASN A O   
1332 C CB  . ASN A 105 ? 0.1549 0.1340 0.1650 -0.0075 0.0064  -0.0062 105 ASN A CB  
1333 C CG  . ASN A 105 ? 0.1601 0.1405 0.1716 -0.0081 0.0054  -0.0123 105 ASN A CG  
1334 O OD1 . ASN A 105 ? 0.1850 0.1621 0.1995 -0.0076 0.0065  -0.0149 105 ASN A OD1 
1335 N ND2 . ASN A 105 ? 0.1708 0.1565 0.1796 -0.0082 0.0032  -0.0150 105 ASN A ND2 
1342 N N   . TRP A 106 ? 0.1488 0.1344 0.1670 -0.0120 0.0059  -0.0062 106 TRP A N   
1343 C CA  . TRP A 106 ? 0.1469 0.1348 0.1736 -0.0149 0.0065  -0.0088 106 TRP A CA  
1344 C C   . TRP A 106 ? 0.1551 0.1460 0.1848 -0.0161 0.0037  -0.0164 106 TRP A C   
1345 O O   . TRP A 106 ? 0.1651 0.1583 0.1880 -0.0138 0.0013  -0.0187 106 TRP A O   
1346 C CB  . TRP A 106 ? 0.1729 0.1668 0.1993 -0.0146 0.0057  -0.0075 106 TRP A CB  
1347 C CG  . TRP A 106 ? 0.1929 0.1860 0.2157 -0.0127 0.0078  -0.0016 106 TRP A CG  
1348 C CD1 . TRP A 106 ? 0.2396 0.2343 0.2549 -0.0098 0.0062  0.0001  106 TRP A CD1 
1349 C CD2 . TRP A 106 ? 0.1934 0.1841 0.2196 -0.0130 0.0119  0.0032  106 TRP A CD2 
1350 N NE1 . TRP A 106 ? 0.2636 0.2578 0.2771 -0.0082 0.0084  0.0043  106 TRP A NE1 
1351 C CE2 . TRP A 106 ? 0.2045 0.1967 0.2236 -0.0097 0.0121  0.0069  106 TRP A CE2 
1352 C CE3 . TRP A 106 ? 0.1928 0.1797 0.2271 -0.0154 0.0157  0.0050  106 TRP A CE3 
1353 C CZ2 . TRP A 106 ? 0.2623 0.2542 0.2810 -0.0080 0.0157  0.0122  106 TRP A CZ2 
1354 C CZ3 . TRP A 106 ? 0.2455 0.2309 0.2798 -0.0139 0.0200  0.0117  106 TRP A CZ3 
1355 C CH2 . TRP A 106 ? 0.2467 0.2353 0.2722 -0.0098 0.0199  0.0152  106 TRP A CH2 
1366 N N   . GLY A 107 ? 0.1617 0.1531 0.2020 -0.0196 0.0043  -0.0203 107 GLY A N   
1367 C CA  . GLY A 107 ? 0.1607 0.1570 0.2049 -0.0207 0.0008  -0.0291 107 GLY A CA  
1368 C C   . GLY A 107 ? 0.1687 0.1756 0.2108 -0.0195 -0.0030 -0.0317 107 GLY A C   
1369 O O   . GLY A 107 ? 0.1751 0.1849 0.2134 -0.0179 -0.0027 -0.0267 107 GLY A O   
1373 N N   . ASN A 108 ? 0.1504 0.1634 0.1942 -0.0193 -0.0069 -0.0401 108 ASN A N   
1374 C CA  . ASN A 108 ? 0.1607 0.1855 0.2045 -0.0178 -0.0113 -0.0444 108 ASN A CA  
1375 C C   . ASN A 108 ? 0.1551 0.1839 0.1845 -0.0119 -0.0135 -0.0411 108 ASN A C   
1376 O O   . ASN A 108 ? 0.1937 0.2320 0.2216 -0.0093 -0.0169 -0.0427 108 ASN A O   
1377 C CB  . ASN A 108 ? 0.1882 0.2180 0.2425 -0.0208 -0.0104 -0.0431 108 ASN A CB  
1378 C CG  . ASN A 108 ? 0.2530 0.2786 0.3230 -0.0270 -0.0073 -0.0454 108 ASN A CG  
1379 O OD1 . ASN A 108 ? 0.3659 0.3856 0.4399 -0.0291 -0.0022 -0.0385 108 ASN A OD1 
1380 N ND2 . ASN A 108 ? 0.2529 0.2811 0.3315 -0.0295 -0.0101 -0.0552 108 ASN A ND2 
1387 N N   . TYR A 109 ? 0.1433 0.1657 0.1631 -0.0095 -0.0117 -0.0368 109 TYR A N   
1388 C CA  . TYR A 109 ? 0.1439 0.1694 0.1511 -0.0042 -0.0130 -0.0340 109 TYR A CA  
1389 C C   . TYR A 109 ? 0.1505 0.1786 0.1531 -0.0019 -0.0146 -0.0398 109 TYR A C   
1390 O O   . TYR A 109 ? 0.1673 0.1889 0.1695 -0.0027 -0.0121 -0.0399 109 TYR A O   
1391 C CB  . TYR A 109 ? 0.1579 0.1756 0.1590 -0.0033 -0.0095 -0.0254 109 TYR A CB  
1392 C CG  . TYR A 109 ? 0.1632 0.1790 0.1665 -0.0042 -0.0083 -0.0201 109 TYR A CG  
1393 C CD1 . TYR A 109 ? 0.1551 0.1746 0.1539 -0.0009 -0.0096 -0.0171 109 TYR A CD1 
1394 C CD2 . TYR A 109 ? 0.1630 0.1733 0.1724 -0.0075 -0.0055 -0.0180 109 TYR A CD2 
1395 C CE1 . TYR A 109 ? 0.1528 0.1706 0.1535 -0.0010 -0.0085 -0.0133 109 TYR A CE1 
1396 C CE2 . TYR A 109 ? 0.1422 0.1517 0.1525 -0.0074 -0.0043 -0.0137 109 TYR A CE2 
1397 C CZ  . TYR A 109 ? 0.1333 0.1467 0.1395 -0.0043 -0.0059 -0.0120 109 TYR A CZ  
1398 O OH  . TYR A 109 ? 0.1447 0.1575 0.1519 -0.0038 -0.0046 -0.0087 109 TYR A OH  
1408 N N   . LYS A 110 ? 0.1549 0.1933 0.1535 0.0018  -0.0187 -0.0449 110 LYS A N   
1409 C CA  . LYS A 110 ? 0.1705 0.2126 0.1637 0.0048  -0.0203 -0.0515 110 LYS A CA  
1410 C C   . LYS A 110 ? 0.1757 0.2131 0.1581 0.0081  -0.0166 -0.0451 110 LYS A C   
1411 O O   . LYS A 110 ? 0.1783 0.2139 0.1593 0.0088  -0.0154 -0.0488 110 LYS A O   
1412 C CB  . LYS A 110 ? 0.2186 0.2744 0.2078 0.0095  -0.0259 -0.0580 110 LYS A CB  
1413 C CG  . LYS A 110 ? 0.2446 0.3061 0.2225 0.0157  -0.0265 -0.0509 110 LYS A CG  
1414 C CD  . LYS A 110 ? 0.2616 0.3383 0.2342 0.0218  -0.0325 -0.0578 110 LYS A CD  
1415 C CE  . LYS A 110 ? 0.3708 0.4516 0.3315 0.0289  -0.0323 -0.0486 110 LYS A CE  
1416 N NZ  . LYS A 110 ? 0.4641 0.5427 0.4106 0.0343  -0.0286 -0.0421 110 LYS A NZ  
1430 N N   . ASN A 111 ? 0.1630 0.1986 0.1388 0.0103  -0.0144 -0.0357 111 ASN A N   
1431 C CA  . ASN A 111 ? 0.1724 0.2049 0.1398 0.0130  -0.0106 -0.0296 111 ASN A CA  
1432 C C   . ASN A 111 ? 0.1568 0.1798 0.1298 0.0088  -0.0069 -0.0273 111 ASN A C   
1433 O O   . ASN A 111 ? 0.1700 0.1918 0.1397 0.0102  -0.0042 -0.0266 111 ASN A O   
1434 C CB  . ASN A 111 ? 0.1971 0.2299 0.1575 0.0163  -0.0092 -0.0205 111 ASN A CB  
1435 C CG  . ASN A 111 ? 0.2246 0.2678 0.1778 0.0222  -0.0128 -0.0221 111 ASN A CG  
1436 O OD1 . ASN A 111 ? 0.2405 0.2921 0.1907 0.0251  -0.0158 -0.0296 111 ASN A OD1 
1437 N ND2 . ASN A 111 ? 0.2682 0.3111 0.2183 0.0247  -0.0127 -0.0153 111 ASN A ND2 
1444 N N   . ASP A 112 ? 0.1613 0.1785 0.1427 0.0043  -0.0066 -0.0260 112 ASP A N   
1445 C CA  . ASP A 112 ? 0.1511 0.1603 0.1373 0.0013  -0.0035 -0.0237 112 ASP A CA  
1446 C C   . ASP A 112 ? 0.1571 0.1647 0.1475 0.0005  -0.0035 -0.0306 112 ASP A C   
1447 O O   . ASP A 112 ? 0.1652 0.1692 0.1553 0.0010  -0.0010 -0.0296 112 ASP A O   
1448 C CB  . ASP A 112 ? 0.1566 0.1610 0.1495 -0.0023 -0.0032 -0.0208 112 ASP A CB  
1449 C CG  . ASP A 112 ? 0.1656 0.1698 0.1552 -0.0015 -0.0030 -0.0146 112 ASP A CG  
1450 O OD1 . ASP A 112 ? 0.1707 0.1774 0.1537 0.0015  -0.0030 -0.0118 112 ASP A OD1 
1451 O OD2 . ASP A 112 ? 0.1552 0.1564 0.1490 -0.0035 -0.0025 -0.0124 112 ASP A OD2 
1456 N N   . ASP A 113 ? 0.1654 0.1761 0.1610 -0.0007 -0.0064 -0.0382 113 ASP A N   
1457 C CA  . ASP A 113 ? 0.1768 0.1850 0.1780 -0.0016 -0.0066 -0.0459 113 ASP A CA  
1458 C C   . ASP A 113 ? 0.1768 0.1888 0.1696 0.0032  -0.0062 -0.0489 113 ASP A C   
1459 O O   . ASP A 113 ? 0.1883 0.1955 0.1829 0.0037  -0.0041 -0.0509 113 ASP A O   
1460 C CB  . ASP A 113 ? 0.1895 0.2018 0.1988 -0.0039 -0.0103 -0.0549 113 ASP A CB  
1461 C CG  . ASP A 113 ? 0.1892 0.1971 0.2098 -0.0092 -0.0094 -0.0524 113 ASP A CG  
1462 O OD1 . ASP A 113 ? 0.1993 0.2005 0.2204 -0.0105 -0.0059 -0.0444 113 ASP A OD1 
1463 O OD2 . ASP A 113 ? 0.2389 0.2511 0.2680 -0.0118 -0.0121 -0.0591 113 ASP A OD2 
1468 N N   . GLU A 114 ? 0.1774 0.1982 0.1604 0.0074  -0.0078 -0.0487 114 GLU A N   
1469 C CA  . GLU A 114 ? 0.1706 0.1964 0.1444 0.0127  -0.0067 -0.0506 114 GLU A CA  
1470 C C   . GLU A 114 ? 0.1721 0.1934 0.1434 0.0133  -0.0015 -0.0422 114 GLU A C   
1471 O O   . GLU A 114 ? 0.1906 0.2116 0.1607 0.0155  0.0007  -0.0447 114 GLU A O   
1472 C CB  . GLU A 114 ? 0.2153 0.2518 0.1787 0.0178  -0.0091 -0.0503 114 GLU A CB  
1473 C CG  . GLU A 114 ? 0.3035 0.3464 0.2551 0.0242  -0.0067 -0.0492 114 GLU A CG  
1474 C CD  . GLU A 114 ? 0.4601 0.5078 0.4103 0.0274  -0.0088 -0.0612 114 GLU A CD  
1475 O OE1 . GLU A 114 ? 0.4070 0.4591 0.3484 0.0327  -0.0057 -0.0606 114 GLU A OE1 
1476 O OE2 . GLU A 114 ? 0.4395 0.4868 0.3979 0.0247  -0.0131 -0.0714 114 GLU A OE2 
1483 N N   . PHE A 115 ? 0.1741 0.1924 0.1452 0.0114  0.0003  -0.0330 115 PHE A N   
1484 C CA  . PHE A 115 ? 0.1650 0.1800 0.1360 0.0111  0.0046  -0.0256 115 PHE A CA  
1485 C C   . PHE A 115 ? 0.1762 0.1848 0.1549 0.0090  0.0061  -0.0274 115 PHE A C   
1486 O O   . PHE A 115 ? 0.1743 0.1837 0.1525 0.0109  0.0091  -0.0265 115 PHE A O   
1487 C CB  . PHE A 115 ? 0.1819 0.1939 0.1535 0.0088  0.0052  -0.0176 115 PHE A CB  
1488 C CG  . PHE A 115 ? 0.1531 0.1619 0.1271 0.0075  0.0088  -0.0111 115 PHE A CG  
1489 C CD1 . PHE A 115 ? 0.1821 0.1949 0.1521 0.0100  0.0125  -0.0073 115 PHE A CD1 
1490 C CD2 . PHE A 115 ? 0.1764 0.1794 0.1571 0.0040  0.0086  -0.0088 115 PHE A CD2 
1491 C CE1 . PHE A 115 ? 0.1856 0.1966 0.1603 0.0081  0.0156  -0.0021 115 PHE A CE1 
1492 C CE2 . PHE A 115 ? 0.1778 0.1795 0.1616 0.0028  0.0110  -0.0041 115 PHE A CE2 
1493 C CZ  . PHE A 115 ? 0.1789 0.1846 0.1607 0.0044  0.0144  -0.0011 115 PHE A CZ  
1503 N N   . ILE A 116 ? 0.1593 0.1619 0.1454 0.0055  0.0044  -0.0294 116 ILE A N   
1504 C CA  . ILE A 116 ? 0.1651 0.1611 0.1583 0.0042  0.0059  -0.0299 116 ILE A CA  
1505 C C   . ILE A 116 ? 0.1790 0.1747 0.1733 0.0067  0.0061  -0.0377 116 ILE A C   
1506 O O   . ILE A 116 ? 0.1981 0.1909 0.1949 0.0083  0.0085  -0.0373 116 ILE A O   
1507 C CB  . ILE A 116 ? 0.1841 0.1738 0.1845 0.0003  0.0050  -0.0284 116 ILE A CB  
1508 C CG1 . ILE A 116 ? 0.1731 0.1632 0.1717 -0.0012 0.0050  -0.0211 116 ILE A CG1 
1509 C CG2 . ILE A 116 ? 0.1967 0.1789 0.2039 0.0000  0.0068  -0.0287 116 ILE A CG2 
1510 C CD1 . ILE A 116 ? 0.1994 0.1893 0.1965 -0.0003 0.0070  -0.0156 116 ILE A CD1 
1522 N N   . SER A 117 ? 0.1836 0.1830 0.1764 0.0076  0.0034  -0.0457 117 SER A N   
1523 C CA  . SER A 117 ? 0.1995 0.1990 0.1931 0.0104  0.0031  -0.0549 117 SER A CA  
1524 C C   . SER A 117 ? 0.2134 0.2183 0.1996 0.0156  0.0061  -0.0536 117 SER A C   
1525 O O   . SER A 117 ? 0.2403 0.2427 0.2288 0.0181  0.0077  -0.0581 117 SER A O   
1526 C CB  . SER A 117 ? 0.2347 0.2399 0.2274 0.0107  -0.0013 -0.0644 117 SER A CB  
1527 O OG  . SER A 117 ? 0.3908 0.4069 0.3718 0.0155  -0.0022 -0.0649 117 SER A OG  
1533 N N   . LYS A 118 ? 0.1944 0.2065 0.1722 0.0174  0.0074  -0.0473 118 LYS A N   
1534 C CA  . LYS A 118 ? 0.2061 0.2245 0.1777 0.0220  0.0113  -0.0448 118 LYS A CA  
1535 C C   . LYS A 118 ? 0.1850 0.2004 0.1614 0.0206  0.0151  -0.0369 118 LYS A C   
1536 O O   . LYS A 118 ? 0.2095 0.2299 0.1840 0.0239  0.0189  -0.0353 118 LYS A O   
1537 C CB  . LYS A 118 ? 0.2250 0.2525 0.1859 0.0249  0.0118  -0.0409 118 LYS A CB  
1538 C CG  . LYS A 118 ? 0.2455 0.2793 0.2000 0.0283  0.0077  -0.0500 118 LYS A CG  
1539 C CD  . LYS A 118 ? 0.3288 0.3722 0.2715 0.0328  0.0083  -0.0454 118 LYS A CD  
1540 C CE  . LYS A 118 ? 0.2941 0.3345 0.2380 0.0292  0.0082  -0.0360 118 LYS A CE  
1541 N NZ  . LYS A 118 ? 0.3170 0.3656 0.2506 0.0336  0.0061  -0.0347 118 LYS A NZ  
1555 N N   . ASN A 119 ? 0.1729 0.1816 0.1559 0.0160  0.0142  -0.0323 119 ASN A N   
1556 C CA  . ASN A 119 ? 0.1858 0.1933 0.1733 0.0145  0.0166  -0.0251 119 ASN A CA  
1557 C C   . ASN A 119 ? 0.1847 0.1838 0.1800 0.0119  0.0151  -0.0246 119 ASN A C   
1558 O O   . ASN A 119 ? 0.1785 0.1749 0.1757 0.0087  0.0140  -0.0198 119 ASN A O   
1559 C CB  . ASN A 119 ? 0.1742 0.1843 0.1592 0.0123  0.0172  -0.0177 119 ASN A CB  
1560 C CG  . ASN A 119 ? 0.1614 0.1793 0.1387 0.0153  0.0197  -0.0157 119 ASN A CG  
1561 O OD1 . ASN A 119 ? 0.1768 0.1998 0.1540 0.0172  0.0238  -0.0128 119 ASN A OD1 
1562 N ND2 . ASN A 119 ? 0.1690 0.1884 0.1398 0.0160  0.0175  -0.0168 119 ASN A ND2 
1569 N N   . PRO A 120 ? 0.1827 0.1773 0.1823 0.0138  0.0155  -0.0291 120 PRO A N   
1570 C CA  . PRO A 120 ? 0.2234 0.2098 0.2299 0.0123  0.0150  -0.0270 120 PRO A CA  
1571 C C   . PRO A 120 ? 0.1967 0.1850 0.2053 0.0120  0.0158  -0.0198 120 PRO A C   
1572 O O   . PRO A 120 ? 0.2053 0.1889 0.2169 0.0104  0.0147  -0.0162 120 PRO A O   
1573 C CB  . PRO A 120 ? 0.2323 0.2139 0.2427 0.0157  0.0160  -0.0328 120 PRO A CB  
1574 C CG  . PRO A 120 ? 0.2581 0.2477 0.2634 0.0196  0.0175  -0.0372 120 PRO A CG  
1575 C CD  . PRO A 120 ? 0.2286 0.2250 0.2265 0.0180  0.0165  -0.0365 120 PRO A CD  
1583 N N   . SER A 121 ? 0.2036 0.1996 0.2111 0.0135  0.0176  -0.0175 121 SER A N   
1584 C CA  . SER A 121 ? 0.2108 0.2101 0.2219 0.0127  0.0177  -0.0121 121 SER A CA  
1585 C C   . SER A 121 ? 0.2085 0.2077 0.2182 0.0087  0.0159  -0.0082 121 SER A C   
1586 O O   . SER A 121 ? 0.2338 0.2355 0.2470 0.0077  0.0152  -0.0048 121 SER A O   
1587 C CB  . SER A 121 ? 0.2386 0.2470 0.2513 0.0147  0.0207  -0.0112 121 SER A CB  
1588 O OG  . SER A 121 ? 0.2850 0.2981 0.2929 0.0133  0.0223  -0.0101 121 SER A OG  
1594 N N   . ALA A 122 ? 0.1630 0.1601 0.1681 0.0066  0.0148  -0.0092 122 ALA A N   
1595 C CA  . ALA A 122 ? 0.1579 0.1544 0.1616 0.0035  0.0132  -0.0059 122 ALA A CA  
1596 C C   . ALA A 122 ? 0.1670 0.1584 0.1729 0.0024  0.0111  -0.0046 122 ALA A C   
1597 O O   . ALA A 122 ? 0.1866 0.1779 0.1918 0.0004  0.0097  -0.0021 122 ALA A O   
1598 C CB  . ALA A 122 ? 0.1819 0.1788 0.1799 0.0028  0.0127  -0.0072 122 ALA A CB  
1604 N N   . LEU A 123 ? 0.1583 0.1452 0.1665 0.0039  0.0112  -0.0060 123 LEU A N   
1605 C CA  . LEU A 123 ? 0.1574 0.1396 0.1673 0.0035  0.0103  -0.0037 123 LEU A CA  
1606 C C   . LEU A 123 ? 0.1660 0.1497 0.1783 0.0061  0.0101  -0.0006 123 LEU A C   
1607 O O   . LEU A 123 ? 0.1814 0.1682 0.1961 0.0087  0.0110  -0.0012 123 LEU A O   
1608 C CB  . LEU A 123 ? 0.1777 0.1534 0.1900 0.0036  0.0112  -0.0063 123 LEU A CB  
1609 C CG  . LEU A 123 ? 0.1736 0.1492 0.1847 0.0010  0.0104  -0.0106 123 LEU A CG  
1610 C CD1 . LEU A 123 ? 0.2094 0.1783 0.2258 0.0004  0.0112  -0.0140 123 LEU A CD1 
1611 C CD2 . LEU A 123 ? 0.1788 0.1562 0.1876 -0.0015 0.0089  -0.0085 123 LEU A CD2 
1623 N N   . LEU A 124 ? 0.1543 0.1372 0.1658 0.0061  0.0089  0.0026  124 LEU A N   
1624 C CA  . LEU A 124 ? 0.1590 0.1451 0.1716 0.0093  0.0077  0.0053  124 LEU A CA  
1625 C C   . LEU A 124 ? 0.1477 0.1297 0.1623 0.0136  0.0093  0.0071  124 LEU A C   
1626 O O   . LEU A 124 ? 0.1625 0.1372 0.1773 0.0136  0.0111  0.0086  124 LEU A O   
1627 C CB  . LEU A 124 ? 0.1681 0.1546 0.1776 0.0088  0.0060  0.0076  124 LEU A CB  
1628 C CG  . LEU A 124 ? 0.1553 0.1471 0.1643 0.0124  0.0037  0.0095  124 LEU A CG  
1629 C CD1 . LEU A 124 ? 0.1798 0.1794 0.1923 0.0116  0.0016  0.0068  124 LEU A CD1 
1630 C CD2 . LEU A 124 ? 0.1688 0.1606 0.1733 0.0126  0.0025  0.0112  124 LEU A CD2 
1642 N N   . LYS A 125 ? 0.1626 0.1495 0.1798 0.0172  0.0089  0.0073  125 LYS A N   
1643 C CA  . LYS A 125 ? 0.1694 0.1530 0.1888 0.0225  0.0103  0.0094  125 LYS A CA  
1644 C C   . LYS A 125 ? 0.1994 0.1904 0.2191 0.0274  0.0080  0.0123  125 LYS A C   
1645 O O   . LYS A 125 ? 0.2039 0.2043 0.2246 0.0263  0.0052  0.0106  125 LYS A O   
1646 C CB  . LYS A 125 ? 0.1750 0.1583 0.1980 0.0235  0.0122  0.0055  125 LYS A CB  
1647 C CG  . LYS A 125 ? 0.1773 0.1546 0.1995 0.0196  0.0139  0.0015  125 LYS A CG  
1648 C CD  . LYS A 125 ? 0.2123 0.1891 0.2368 0.0217  0.0158  -0.0032 125 LYS A CD  
1649 C CE  . LYS A 125 ? 0.2231 0.1966 0.2457 0.0179  0.0162  -0.0081 125 LYS A CE  
1650 N NZ  . LYS A 125 ? 0.3047 0.2780 0.3284 0.0204  0.0178  -0.0139 125 LYS A NZ  
1664 N N   . ASN A 126 ? 0.1851 0.1720 0.2045 0.0331  0.0091  0.0166  126 ASN A N   
1665 C CA  . ASN A 126 ? 0.1882 0.1829 0.2071 0.0396  0.0066  0.0197  126 ASN A CA  
1666 C C   . ASN A 126 ? 0.1995 0.2012 0.2241 0.0433  0.0060  0.0173  126 ASN A C   
1667 O O   . ASN A 126 ? 0.1929 0.1943 0.2214 0.0406  0.0077  0.0132  126 ASN A O   
1668 C CB  . ASN A 126 ? 0.2308 0.2183 0.2459 0.0449  0.0086  0.0267  126 ASN A CB  
1669 C CG  . ASN A 126 ? 0.2486 0.2243 0.2672 0.0473  0.0130  0.0288  126 ASN A CG  
1670 O OD1 . ASN A 126 ? 0.2527 0.2281 0.2762 0.0479  0.0137  0.0249  126 ASN A OD1 
1671 N ND2 . ASN A 126 ? 0.3284 0.2944 0.3452 0.0492  0.0164  0.0351  126 ASN A ND2 
1678 N N   . GLN A 127 ? 0.2193 0.2289 0.2444 0.0502  0.0035  0.0198  127 GLN A N   
1679 C CA  . GLN A 127 ? 0.2343 0.2534 0.2661 0.0541  0.0025  0.0173  127 GLN A CA  
1680 C C   . GLN A 127 ? 0.2154 0.2259 0.2500 0.0581  0.0066  0.0181  127 GLN A C   
1681 O O   . GLN A 127 ? 0.2227 0.2401 0.2634 0.0602  0.0070  0.0149  127 GLN A O   
1682 C CB  . GLN A 127 ? 0.3059 0.3374 0.3381 0.0612  -0.0020 0.0192  127 GLN A CB  
1683 C CG  . GLN A 127 ? 0.3000 0.3451 0.3354 0.0570  -0.0067 0.0142  127 GLN A CG  
1684 C CD  . GLN A 127 ? 0.2835 0.3423 0.3189 0.0636  -0.0123 0.0144  127 GLN A CD  
1685 O OE1 . GLN A 127 ? 0.3526 0.4129 0.3856 0.0729  -0.0129 0.0189  127 GLN A OE1 
1686 N NE2 . GLN A 127 ? 0.2373 0.3062 0.2754 0.0592  -0.0168 0.0093  127 GLN A NE2 
1695 N N   . ASN A 128 ? 0.2370 0.2330 0.2685 0.0594  0.0100  0.0219  128 ASN A N   
1696 C CA  . ASN A 128 ? 0.2671 0.2522 0.3021 0.0617  0.0141  0.0211  128 ASN A CA  
1697 C C   . ASN A 128 ? 0.2620 0.2419 0.2981 0.0544  0.0161  0.0147  128 ASN A C   
1698 O O   . ASN A 128 ? 0.2822 0.2530 0.3212 0.0556  0.0192  0.0120  128 ASN A O   
1699 C CB  . ASN A 128 ? 0.3035 0.2740 0.3363 0.0652  0.0172  0.0277  128 ASN A CB  
1700 C CG  . ASN A 128 ? 0.2720 0.2422 0.3062 0.0758  0.0178  0.0333  128 ASN A CG  
1701 O OD1 . ASN A 128 ? 0.2806 0.2598 0.3187 0.0809  0.0163  0.0309  128 ASN A OD1 
1702 N ND2 . ASN A 128 ? 0.4161 0.3765 0.4472 0.0798  0.0202  0.0415  128 ASN A ND2 
1709 N N   . ASN A 129 ? 0.2216 0.2075 0.2555 0.0474  0.0143  0.0119  129 ASN A N   
1710 C CA  . ASN A 129 ? 0.2197 0.2022 0.2530 0.0409  0.0157  0.0067  129 ASN A CA  
1711 C C   . ASN A 129 ? 0.2175 0.1860 0.2497 0.0383  0.0180  0.0066  129 ASN A C   
1712 O O   . ASN A 129 ? 0.2619 0.2258 0.2952 0.0358  0.0195  0.0012  129 ASN A O   
1713 C CB  . ASN A 129 ? 0.2172 0.2046 0.2538 0.0420  0.0173  0.0013  129 ASN A CB  
1714 C CG  . ASN A 129 ? 0.2210 0.2129 0.2554 0.0356  0.0173  -0.0027 129 ASN A CG  
1715 O OD1 . ASN A 129 ? 0.2159 0.2137 0.2487 0.0316  0.0153  -0.0011 129 ASN A OD1 
1716 N ND2 . ASN A 129 ? 0.2367 0.2255 0.2704 0.0351  0.0196  -0.0078 129 ASN A ND2 
1723 N N   . GLU A 130 ? 0.2412 0.2040 0.2716 0.0389  0.0182  0.0124  130 GLU A N   
1724 C CA  . GLU A 130 ? 0.2674 0.2186 0.2986 0.0349  0.0205  0.0126  130 GLU A CA  
1725 C C   . GLU A 130 ? 0.2205 0.1749 0.2474 0.0294  0.0189  0.0140  130 GLU A C   
1726 O O   . GLU A 130 ? 0.2043 0.1668 0.2272 0.0303  0.0164  0.0168  130 GLU A O   
1727 C CB  . GLU A 130 ? 0.3200 0.2595 0.3542 0.0395  0.0238  0.0184  130 GLU A CB  
1728 C CG  . GLU A 130 ? 0.3754 0.3079 0.4153 0.0447  0.0261  0.0157  130 GLU A CG  
1729 C CD  . GLU A 130 ? 0.3250 0.2524 0.3690 0.0409  0.0269  0.0060  130 GLU A CD  
1730 O OE1 . GLU A 130 ? 0.4430 0.3666 0.4879 0.0343  0.0270  0.0021  130 GLU A OE1 
1731 O OE2 . GLU A 130 ? 0.2984 0.2266 0.3446 0.0453  0.0274  0.0017  130 GLU A OE2 
1738 N N   . LEU A 131 ? 0.1923 0.1407 0.2207 0.0241  0.0200  0.0109  131 LEU A N   
1739 C CA  . LEU A 131 ? 0.1919 0.1433 0.2170 0.0190  0.0187  0.0114  131 LEU A CA  
1740 C C   . LEU A 131 ? 0.1874 0.1376 0.2102 0.0209  0.0197  0.0190  131 LEU A C   
1741 O O   . LEU A 131 ? 0.2203 0.1631 0.2456 0.0243  0.0229  0.0243  131 LEU A O   
1742 C CB  . LEU A 131 ? 0.2165 0.1623 0.2453 0.0137  0.0198  0.0065  131 LEU A CB  
1743 C CG  . LEU A 131 ? 0.2046 0.1541 0.2330 0.0116  0.0182  -0.0016 131 LEU A CG  
1744 C CD1 . LEU A 131 ? 0.2937 0.2370 0.3271 0.0076  0.0189  -0.0071 131 LEU A CD1 
1745 C CD2 . LEU A 131 ? 0.2092 0.1682 0.2319 0.0095  0.0155  -0.0023 131 LEU A CD2 
1757 N N   . VAL A 132 ? 0.1940 0.1514 0.2119 0.0191  0.0174  0.0199  132 VAL A N   
1758 C CA  . VAL A 132 ? 0.2073 0.1649 0.2216 0.0205  0.0184  0.0261  132 VAL A CA  
1759 C C   . VAL A 132 ? 0.2165 0.1727 0.2318 0.0145  0.0192  0.0243  132 VAL A C   
1760 O O   . VAL A 132 ? 0.1968 0.1552 0.2129 0.0102  0.0173  0.0184  132 VAL A O   
1761 C CB  . VAL A 132 ? 0.2209 0.1886 0.2290 0.0243  0.0148  0.0277  132 VAL A CB  
1762 C CG1 . VAL A 132 ? 0.2468 0.2170 0.2551 0.0310  0.0140  0.0299  132 VAL A CG1 
1763 C CG2 . VAL A 132 ? 0.2159 0.1908 0.2227 0.0202  0.0111  0.0218  132 VAL A CG2 
1773 N N   . TYR A 133 ? 0.2195 0.1725 0.2350 0.0149  0.0224  0.0300  133 TYR A N   
1774 C CA  . TYR A 133 ? 0.2210 0.1724 0.2402 0.0094  0.0240  0.0287  133 TYR A CA  
1775 C C   . TYR A 133 ? 0.2500 0.2056 0.2648 0.0104  0.0254  0.0340  133 TYR A C   
1776 O O   . TYR A 133 ? 0.2612 0.2191 0.2701 0.0160  0.0260  0.0398  133 TYR A O   
1777 C CB  . TYR A 133 ? 0.2514 0.1926 0.2800 0.0073  0.0286  0.0300  133 TYR A CB  
1778 C CG  . TYR A 133 ? 0.2422 0.1778 0.2764 0.0062  0.0280  0.0239  133 TYR A CG  
1779 C CD1 . TYR A 133 ? 0.2508 0.1887 0.2873 0.0017  0.0252  0.0150  133 TYR A CD1 
1780 C CD2 . TYR A 133 ? 0.2867 0.2152 0.3234 0.0107  0.0303  0.0269  133 TYR A CD2 
1781 C CE1 . TYR A 133 ? 0.2479 0.1814 0.2888 0.0014  0.0248  0.0087  133 TYR A CE1 
1782 C CE2 . TYR A 133 ? 0.2937 0.2169 0.3356 0.0103  0.0300  0.0205  133 TYR A CE2 
1783 C CZ  . TYR A 133 ? 0.2563 0.1824 0.3001 0.0056  0.0272  0.0112  133 TYR A CZ  
1784 O OH  . TYR A 133 ? 0.3074 0.2290 0.3555 0.0061  0.0269  0.0042  133 TYR A OH  
1794 N N   . MET A 134 ? 0.2269 0.1842 0.2443 0.0056  0.0256  0.0314  134 MET A N   
1795 C CA  . MET A 134 ? 0.2440 0.2044 0.2601 0.0060  0.0286  0.0365  134 MET A CA  
1796 C C   . MET A 134 ? 0.2750 0.2283 0.2972 0.0066  0.0352  0.0441  134 MET A C   
1797 O O   . MET A 134 ? 0.2833 0.2282 0.3134 0.0047  0.0373  0.0435  134 MET A O   
1798 C CB  . MET A 134 ? 0.2770 0.2411 0.2968 0.0006  0.0274  0.0314  134 MET A CB  
1799 C CG  . MET A 134 ? 0.2524 0.2231 0.2657 0.0006  0.0221  0.0260  134 MET A CG  
1800 S SD  . MET A 134 ? 0.2732 0.2509 0.2761 0.0059  0.0208  0.0292  134 MET A SD  
1801 C CE  . MET A 134 ? 0.3470 0.3279 0.3527 0.0045  0.0249  0.0323  134 MET A CE  
1811 N N   . PRO A 135 ? 0.3260 0.2823 0.3446 0.0096  0.0390  0.0515  135 PRO A N   
1812 C CA  . PRO A 135 ? 0.3321 0.2815 0.3565 0.0107  0.0465  0.0607  135 PRO A CA  
1813 C C   . PRO A 135 ? 0.3322 0.2754 0.3717 0.0028  0.0500  0.0581  135 PRO A C   
1814 O O   . PRO A 135 ? 0.4045 0.3523 0.4484 -0.0027 0.0473  0.0508  135 PRO A O   
1815 C CB  . PRO A 135 ? 0.3850 0.3419 0.4019 0.0149  0.0497  0.0679  135 PRO A CB  
1816 C CG  . PRO A 135 ? 0.3571 0.3237 0.3620 0.0183  0.0427  0.0624  135 PRO A CG  
1817 C CD  . PRO A 135 ? 0.3364 0.3026 0.3456 0.0125  0.0370  0.0519  135 PRO A CD  
1825 N N   . ASN A 136 ? 0.4754 0.4083 0.5236 0.0026  0.0561  0.0641  136 ASN A N   
1826 C CA  . ASN A 136 ? 0.5857 0.5125 0.6507 -0.0050 0.0608  0.0631  136 ASN A CA  
1827 C C   . ASN A 136 ? 0.5633 0.4899 0.6360 -0.0115 0.0552  0.0499  136 ASN A C   
1828 O O   . ASN A 136 ? 0.6187 0.5492 0.7008 -0.0179 0.0550  0.0447  136 ASN A O   
1829 C CB  . ASN A 136 ? 0.5203 0.4536 0.5893 -0.0074 0.0660  0.0685  136 ASN A CB  
1830 C CG  . ASN A 136 ? 0.5800 0.5151 0.6393 0.0002  0.0717  0.0816  136 ASN A CG  
1831 O OD1 . ASN A 136 ? 0.6682 0.5962 0.7272 0.0045  0.0754  0.0885  136 ASN A OD1 
1832 N ND2 . ASN A 136 ? 0.6389 0.5857 0.6891 0.0028  0.0711  0.0831  136 ASN A ND2 
1839 N N   . GLY A 137 ? 0.4271 0.3501 0.4955 -0.0093 0.0506  0.0444  137 GLY A N   
1840 C CA  . GLY A 137 ? 0.4762 0.3983 0.5517 -0.0145 0.0462  0.0326  137 GLY A CA  
1841 C C   . GLY A 137 ? 0.4610 0.3841 0.5271 -0.0106 0.0406  0.0272  137 GLY A C   
1842 O O   . GLY A 137 ? 0.4410 0.3625 0.4992 -0.0044 0.0409  0.0325  137 GLY A O   
1846 N N   . SER A 138 ? 0.3575 0.2842 0.4253 -0.0140 0.0358  0.0167  138 SER A N   
1847 C CA  . SER A 138 ? 0.3350 0.2633 0.3959 -0.0112 0.0312  0.0108  138 SER A CA  
1848 C C   . SER A 138 ? 0.2286 0.1680 0.2812 -0.0118 0.0259  0.0059  138 SER A C   
1849 O O   . SER A 138 ? 0.2793 0.2212 0.3299 -0.0120 0.0223  -0.0015 138 SER A O   
1850 C CB  . SER A 138 ? 0.4716 0.3929 0.5418 -0.0136 0.0308  0.0023  138 SER A CB  
1851 O OG  . SER A 138 ? 0.5003 0.4228 0.5810 -0.0200 0.0308  -0.0033 138 SER A OG  
1857 N N   . THR A 139 ? 0.2448 0.1909 0.2926 -0.0118 0.0258  0.0102  139 THR A N   
1858 C CA  . THR A 139 ? 0.2233 0.1784 0.2629 -0.0115 0.0212  0.0068  139 THR A CA  
1859 C C   . THR A 139 ? 0.2103 0.1672 0.2403 -0.0068 0.0194  0.0093  139 THR A C   
1860 O O   . THR A 139 ? 0.2129 0.1697 0.2389 -0.0034 0.0209  0.0158  139 THR A O   
1861 C CB  . THR A 139 ? 0.2599 0.2212 0.2985 -0.0128 0.0215  0.0095  139 THR A CB  
1862 O OG1 . THR A 139 ? 0.2978 0.2588 0.3475 -0.0175 0.0236  0.0074  139 THR A OG1 
1863 C CG2 . THR A 139 ? 0.2397 0.2086 0.2711 -0.0124 0.0169  0.0056  139 THR A CG2 
1871 N N   . PRO A 140 ? 0.1813 0.1405 0.2079 -0.0061 0.0163  0.0044  140 PRO A N   
1872 C CA  . PRO A 140 ? 0.1753 0.1370 0.1955 -0.0023 0.0149  0.0062  140 PRO A CA  
1873 C C   . PRO A 140 ? 0.1559 0.1245 0.1698 -0.0024 0.0120  0.0060  140 PRO A C   
1874 O O   . PRO A 140 ? 0.1723 0.1434 0.1858 -0.0046 0.0113  0.0053  140 PRO A O   
1875 C CB  . PRO A 140 ? 0.1857 0.1460 0.2074 -0.0019 0.0142  0.0008  140 PRO A CB  
1876 C CG  . PRO A 140 ? 0.2040 0.1660 0.2280 -0.0056 0.0128  -0.0052 140 PRO A CG  
1877 C CD  . PRO A 140 ? 0.2031 0.1633 0.2322 -0.0086 0.0143  -0.0034 140 PRO A CD  
1885 N N   . PHE A 141 ? 0.1575 0.1292 0.1678 -0.0002 0.0104  0.0063  141 PHE A N   
1886 C CA  . PHE A 141 ? 0.1485 0.1253 0.1545 -0.0004 0.0080  0.0061  141 PHE A CA  
1887 C C   . PHE A 141 ? 0.1512 0.1308 0.1566 -0.0009 0.0070  0.0032  141 PHE A C   
1888 O O   . PHE A 141 ? 0.1593 0.1386 0.1665 0.0005  0.0078  0.0022  141 PHE A O   
1889 C CB  . PHE A 141 ? 0.1625 0.1418 0.1661 0.0027  0.0070  0.0093  141 PHE A CB  
1890 C CG  . PHE A 141 ? 0.1624 0.1403 0.1648 0.0047  0.0086  0.0135  141 PHE A CG  
1891 C CD1 . PHE A 141 ? 0.1758 0.1558 0.1755 0.0043  0.0084  0.0144  141 PHE A CD1 
1892 C CD2 . PHE A 141 ? 0.1726 0.1472 0.1766 0.0077  0.0109  0.0172  141 PHE A CD2 
1893 C CE1 . PHE A 141 ? 0.1798 0.1595 0.1778 0.0069  0.0107  0.0190  141 PHE A CE1 
1894 C CE2 . PHE A 141 ? 0.1971 0.1705 0.1996 0.0102  0.0134  0.0225  141 PHE A CE2 
1895 C CZ  . PHE A 141 ? 0.1868 0.1633 0.1860 0.0098  0.0133  0.0235  141 PHE A CZ  
1905 N N   . PHE A 142 ? 0.1549 0.1371 0.1579 -0.0024 0.0057  0.0023  142 PHE A N   
1906 C CA  . PHE A 142 ? 0.1546 0.1398 0.1570 -0.0027 0.0056  0.0014  142 PHE A CA  
1907 C C   . PHE A 142 ? 0.1595 0.1475 0.1640 -0.0016 0.0050  0.0027  142 PHE A C   
1908 O O   . PHE A 142 ? 0.1816 0.1703 0.1858 -0.0012 0.0033  0.0037  142 PHE A O   
1909 C CB  . PHE A 142 ? 0.1516 0.1379 0.1514 -0.0041 0.0047  0.0016  142 PHE A CB  
1910 C CG  . PHE A 142 ? 0.1640 0.1499 0.1618 -0.0046 0.0045  0.0000  142 PHE A CG  
1911 C CD1 . PHE A 142 ? 0.1915 0.1786 0.1886 -0.0042 0.0051  -0.0026 142 PHE A CD1 
1912 C CD2 . PHE A 142 ? 0.1857 0.1712 0.1825 -0.0051 0.0034  0.0006  142 PHE A CD2 
1913 C CE1 . PHE A 142 ? 0.2111 0.1997 0.2069 -0.0045 0.0040  -0.0052 142 PHE A CE1 
1914 C CE2 . PHE A 142 ? 0.2043 0.1914 0.2004 -0.0054 0.0027  -0.0012 142 PHE A CE2 
1915 C CZ  . PHE A 142 ? 0.2165 0.2053 0.2123 -0.0052 0.0027  -0.0042 142 PHE A CZ  
1925 N N   . ASP A 143 ? 0.1426 0.1335 0.1495 -0.0010 0.0061  0.0021  143 ASP A N   
1926 C CA  . ASP A 143 ? 0.1361 0.1317 0.1470 -0.0005 0.0052  0.0025  143 ASP A CA  
1927 C C   . ASP A 143 ? 0.1390 0.1364 0.1512 -0.0033 0.0053  0.0028  143 ASP A C   
1928 O O   . ASP A 143 ? 0.1405 0.1404 0.1544 -0.0042 0.0077  0.0032  143 ASP A O   
1929 C CB  . ASP A 143 ? 0.1532 0.1522 0.1677 0.0018  0.0067  0.0020  143 ASP A CB  
1930 C CG  . ASP A 143 ? 0.1503 0.1559 0.1704 0.0023  0.0052  0.0020  143 ASP A CG  
1931 O OD1 . ASP A 143 ? 0.1442 0.1514 0.1657 0.0003  0.0031  0.0016  143 ASP A OD1 
1932 O OD2 . ASP A 143 ? 0.1742 0.1838 0.1980 0.0051  0.0058  0.0017  143 ASP A OD2 
1937 N N   . ILE A 144 ? 0.1430 0.1390 0.1546 -0.0045 0.0032  0.0027  144 ILE A N   
1938 C CA  . ILE A 144 ? 0.1277 0.1231 0.1410 -0.0072 0.0035  0.0031  144 ILE A CA  
1939 C C   . ILE A 144 ? 0.1196 0.1196 0.1411 -0.0089 0.0035  0.0024  144 ILE A C   
1940 O O   . ILE A 144 ? 0.1508 0.1496 0.1760 -0.0117 0.0043  0.0030  144 ILE A O   
1941 C CB  . ILE A 144 ? 0.1388 0.1304 0.1491 -0.0074 0.0013  0.0025  144 ILE A CB  
1942 C CG1 . ILE A 144 ? 0.1550 0.1487 0.1662 -0.0060 -0.0019 0.0003  144 ILE A CG1 
1943 C CG2 . ILE A 144 ? 0.1674 0.1558 0.1716 -0.0063 0.0019  0.0034  144 ILE A CG2 
1944 C CD1 . ILE A 144 ? 0.1735 0.1644 0.1823 -0.0058 -0.0039 -0.0012 144 ILE A CD1 
1956 N N   . THR A 145 ? 0.1358 0.1413 0.1612 -0.0073 0.0026  0.0012  145 THR A N   
1957 C CA  . THR A 145 ? 0.1353 0.1473 0.1705 -0.0093 0.0029  0.0001  145 THR A CA  
1958 C C   . THR A 145 ? 0.1275 0.1414 0.1656 -0.0108 0.0078  0.0028  145 THR A C   
1959 O O   . THR A 145 ? 0.1487 0.1676 0.1962 -0.0134 0.0093  0.0029  145 THR A O   
1960 C CB  . THR A 145 ? 0.1401 0.1594 0.1793 -0.0064 0.0002  -0.0020 145 THR A CB  
1961 O OG1 . THR A 145 ? 0.1476 0.1682 0.1848 -0.0032 0.0025  -0.0006 145 THR A OG1 
1962 C CG2 . THR A 145 ? 0.1514 0.1700 0.1860 -0.0037 -0.0042 -0.0039 145 THR A CG2 
1970 N N   . LYS A 146 ? 0.1363 0.1473 0.1671 -0.0089 0.0104  0.0046  146 LYS A N   
1971 C CA  . LYS A 146 ? 0.1320 0.1460 0.1632 -0.0088 0.0153  0.0070  146 LYS A CA  
1972 C C   . LYS A 146 ? 0.1381 0.1480 0.1666 -0.0109 0.0177  0.0104  146 LYS A C   
1973 O O   . LYS A 146 ? 0.1417 0.1458 0.1627 -0.0102 0.0163  0.0107  146 LYS A O   
1974 C CB  . LYS A 146 ? 0.1369 0.1504 0.1613 -0.0049 0.0161  0.0059  146 LYS A CB  
1975 C CG  . LYS A 146 ? 0.1527 0.1694 0.1806 -0.0022 0.0145  0.0035  146 LYS A CG  
1976 C CD  . LYS A 146 ? 0.2033 0.2184 0.2264 0.0016  0.0158  0.0018  146 LYS A CD  
1977 C CE  . LYS A 146 ? 0.2121 0.2305 0.2401 0.0049  0.0149  0.0005  146 LYS A CE  
1978 N NZ  . LYS A 146 ? 0.3415 0.3586 0.3670 0.0087  0.0170  -0.0016 146 LYS A NZ  
1992 N N   . SER A 147 ? 0.1450 0.1582 0.1799 -0.0131 0.0218  0.0136  147 SER A N   
1993 C CA  . SER A 147 ? 0.1491 0.1574 0.1821 -0.0146 0.0247  0.0182  147 SER A CA  
1994 C C   . SER A 147 ? 0.1459 0.1522 0.1663 -0.0108 0.0262  0.0203  147 SER A C   
1995 O O   . SER A 147 ? 0.1616 0.1622 0.1768 -0.0105 0.0257  0.0224  147 SER A O   
1996 C CB  . SER A 147 ? 0.1892 0.2012 0.2324 -0.0178 0.0302  0.0225  147 SER A CB  
1997 O OG  . SER A 147 ? 0.1869 0.2063 0.2291 -0.0154 0.0349  0.0246  147 SER A OG  
2003 N N   . PHE A 148 ? 0.1435 0.1546 0.1588 -0.0073 0.0275  0.0189  148 PHE A N   
2004 C CA  . PHE A 148 ? 0.1488 0.1593 0.1525 -0.0035 0.0280  0.0193  148 PHE A CA  
2005 C C   . PHE A 148 ? 0.1391 0.1443 0.1376 -0.0029 0.0228  0.0156  148 PHE A C   
2006 O O   . PHE A 148 ? 0.1524 0.1563 0.1431 -0.0008 0.0221  0.0162  148 PHE A O   
2007 C CB  . PHE A 148 ? 0.1452 0.1623 0.1451 0.0003  0.0305  0.0173  148 PHE A CB  
2008 C CG  . PHE A 148 ? 0.1348 0.1517 0.1343 0.0019  0.0270  0.0108  148 PHE A CG  
2009 C CD1 . PHE A 148 ? 0.1352 0.1535 0.1429 0.0009  0.0260  0.0087  148 PHE A CD1 
2010 C CD2 . PHE A 148 ? 0.1496 0.1651 0.1411 0.0048  0.0247  0.0066  148 PHE A CD2 
2011 C CE1 . PHE A 148 ? 0.1517 0.1687 0.1588 0.0031  0.0237  0.0039  148 PHE A CE1 
2012 C CE2 . PHE A 148 ? 0.1691 0.1830 0.1617 0.0060  0.0223  0.0009  148 PHE A CE2 
2013 C CZ  . PHE A 148 ? 0.1701 0.1840 0.1703 0.0053  0.0221  0.0002  148 PHE A CZ  
2023 N N   . VAL A 149 ? 0.1365 0.1396 0.1393 -0.0045 0.0192  0.0120  149 VAL A N   
2024 C CA  . VAL A 149 ? 0.1385 0.1371 0.1379 -0.0044 0.0151  0.0093  149 VAL A CA  
2025 C C   . VAL A 149 ? 0.1471 0.1412 0.1468 -0.0061 0.0139  0.0117  149 VAL A C   
2026 O O   . VAL A 149 ? 0.1521 0.1438 0.1466 -0.0049 0.0123  0.0115  149 VAL A O   
2027 C CB  . VAL A 149 ? 0.1365 0.1345 0.1397 -0.0046 0.0126  0.0061  149 VAL A CB  
2028 C CG1 . VAL A 149 ? 0.1584 0.1521 0.1590 -0.0047 0.0094  0.0045  149 VAL A CG1 
2029 C CG2 . VAL A 149 ? 0.1443 0.1451 0.1473 -0.0022 0.0139  0.0036  149 VAL A CG2 
2039 N N   . GLN A 150 ? 0.1503 0.1436 0.1569 -0.0087 0.0146  0.0133  150 GLN A N   
2040 C CA  . GLN A 150 ? 0.1498 0.1378 0.1577 -0.0102 0.0139  0.0151  150 GLN A CA  
2041 C C   . GLN A 150 ? 0.1607 0.1468 0.1627 -0.0082 0.0165  0.0196  150 GLN A C   
2042 O O   . GLN A 150 ? 0.1658 0.1479 0.1639 -0.0069 0.0147  0.0200  150 GLN A O   
2043 C CB  . GLN A 150 ? 0.1662 0.1541 0.1845 -0.0137 0.0149  0.0156  150 GLN A CB  
2044 C CG  . GLN A 150 ? 0.1504 0.1413 0.1743 -0.0149 0.0114  0.0107  150 GLN A CG  
2045 C CD  . GLN A 150 ? 0.1849 0.1781 0.2204 -0.0185 0.0120  0.0100  150 GLN A CD  
2046 O OE1 . GLN A 150 ? 0.2440 0.2337 0.2848 -0.0211 0.0148  0.0128  150 GLN A OE1 
2047 N NE2 . GLN A 150 ? 0.1846 0.1838 0.2253 -0.0186 0.0095  0.0062  150 GLN A NE2 
2056 N N   . GLU A 151 ? 0.1651 0.1549 0.1660 -0.0072 0.0209  0.0233  151 GLU A N   
2057 C CA  . GLU A 151 ? 0.1759 0.1647 0.1701 -0.0042 0.0238  0.0288  151 GLU A CA  
2058 C C   . GLU A 151 ? 0.1645 0.1555 0.1487 -0.0001 0.0208  0.0262  151 GLU A C   
2059 O O   . GLU A 151 ? 0.1840 0.1726 0.1632 0.0024  0.0200  0.0287  151 GLU A O   
2060 C CB  . GLU A 151 ? 0.1854 0.1791 0.1797 -0.0033 0.0299  0.0338  151 GLU A CB  
2061 C CG  . GLU A 151 ? 0.2562 0.2495 0.2423 0.0010  0.0337  0.0411  151 GLU A CG  
2062 C CD  . GLU A 151 ? 0.3140 0.2987 0.3052 -0.0009 0.0359  0.0471  151 GLU A CD  
2063 O OE1 . GLU A 151 ? 0.3201 0.3003 0.3231 -0.0062 0.0354  0.0454  151 GLU A OE1 
2064 O OE2 . GLU A 151 ? 0.3284 0.3112 0.3121 0.0035  0.0379  0.0531  151 GLU A OE2 
2071 N N   . TYR A 152 ? 0.1612 0.1567 0.1433 0.0008  0.0189  0.0210  152 TYR A N   
2072 C CA  . TYR A 152 ? 0.1594 0.1574 0.1348 0.0036  0.0155  0.0169  152 TYR A CA  
2073 C C   . TYR A 152 ? 0.1628 0.1565 0.1392 0.0027  0.0119  0.0158  152 TYR A C   
2074 O O   . TYR A 152 ? 0.1757 0.1706 0.1470 0.0056  0.0103  0.0163  152 TYR A O   
2075 C CB  . TYR A 152 ? 0.1685 0.1697 0.1448 0.0035  0.0140  0.0106  152 TYR A CB  
2076 C CG  . TYR A 152 ? 0.1659 0.1689 0.1384 0.0052  0.0103  0.0057  152 TYR A CG  
2077 C CD1 . TYR A 152 ? 0.1719 0.1808 0.1369 0.0093  0.0099  0.0042  152 TYR A CD1 
2078 C CD2 . TYR A 152 ? 0.1594 0.1592 0.1359 0.0029  0.0071  0.0027  152 TYR A CD2 
2079 C CE1 . TYR A 152 ? 0.1764 0.1883 0.1396 0.0105  0.0059  -0.0011 152 TYR A CE1 
2080 C CE2 . TYR A 152 ? 0.1732 0.1756 0.1485 0.0037  0.0041  -0.0016 152 TYR A CE2 
2081 C CZ  . TYR A 152 ? 0.1649 0.1734 0.1342 0.0073  0.0031  -0.0040 152 TYR A CZ  
2082 O OH  . TYR A 152 ? 0.1801 0.1926 0.1495 0.0080  -0.0006 -0.0093 152 TYR A OH  
2092 N N   . TRP A 153 ? 0.1555 0.1454 0.1382 -0.0006 0.0105  0.0141  153 TRP A N   
2093 C CA  . TRP A 153 ? 0.1639 0.1508 0.1476 -0.0010 0.0074  0.0124  153 TRP A CA  
2094 C C   . TRP A 153 ? 0.1506 0.1335 0.1331 0.0002  0.0079  0.0164  153 TRP A C   
2095 O O   . TRP A 153 ? 0.1547 0.1380 0.1339 0.0026  0.0060  0.0162  153 TRP A O   
2096 C CB  . TRP A 153 ? 0.1674 0.1522 0.1567 -0.0038 0.0062  0.0101  153 TRP A CB  
2097 C CG  . TRP A 153 ? 0.1459 0.1292 0.1354 -0.0036 0.0036  0.0081  153 TRP A CG  
2098 C CD1 . TRP A 153 ? 0.1610 0.1462 0.1505 -0.0035 0.0022  0.0054  153 TRP A CD1 
2099 C CD2 . TRP A 153 ? 0.1497 0.1293 0.1401 -0.0034 0.0025  0.0088  153 TRP A CD2 
2100 N NE1 . TRP A 153 ? 0.1599 0.1440 0.1498 -0.0031 0.0008  0.0049  153 TRP A NE1 
2101 C CE2 . TRP A 153 ? 0.1524 0.1333 0.1423 -0.0027 0.0007  0.0065  153 TRP A CE2 
2102 C CE3 . TRP A 153 ? 0.1669 0.1421 0.1592 -0.0036 0.0033  0.0109  153 TRP A CE3 
2103 C CZ2 . TRP A 153 ? 0.1638 0.1425 0.1538 -0.0015 -0.0005 0.0060  153 TRP A CZ2 
2104 C CZ3 . TRP A 153 ? 0.1748 0.1465 0.1678 -0.0028 0.0017  0.0098  153 TRP A CZ3 
2105 C CH2 . TRP A 153 ? 0.1737 0.1477 0.1648 -0.0014 -0.0003 0.0071  153 TRP A CH2 
2116 N N   . LEU A 154 ? 0.1559 0.1351 0.1421 -0.0012 0.0106  0.0201  154 LEU A N   
2117 C CA  . LEU A 154 ? 0.1564 0.1297 0.1429 -0.0001 0.0117  0.0243  154 LEU A CA  
2118 C C   . LEU A 154 ? 0.1828 0.1582 0.1613 0.0048  0.0126  0.0283  154 LEU A C   
2119 O O   . LEU A 154 ? 0.1921 0.1649 0.1682 0.0077  0.0112  0.0295  154 LEU A O   
2120 C CB  . LEU A 154 ? 0.1765 0.1454 0.1703 -0.0033 0.0152  0.0276  154 LEU A CB  
2121 C CG  . LEU A 154 ? 0.1725 0.1393 0.1748 -0.0074 0.0131  0.0228  154 LEU A CG  
2122 C CD1 . LEU A 154 ? 0.2062 0.1721 0.2177 -0.0112 0.0165  0.0249  154 LEU A CD1 
2123 C CD2 . LEU A 154 ? 0.2073 0.1680 0.2108 -0.0068 0.0103  0.0205  154 LEU A CD2 
2135 N N   . LYS A 155 ? 0.1746 0.1553 0.1484 0.0066  0.0150  0.0305  155 LYS A N   
2136 C CA  . LYS A 155 ? 0.1951 0.1797 0.1599 0.0124  0.0155  0.0341  155 LYS A CA  
2137 C C   . LYS A 155 ? 0.1865 0.1765 0.1473 0.0150  0.0104  0.0286  155 LYS A C   
2138 O O   . LYS A 155 ? 0.2024 0.1943 0.1578 0.0200  0.0092  0.0310  155 LYS A O   
2139 C CB  . LYS A 155 ? 0.1994 0.1901 0.1592 0.0146  0.0191  0.0367  155 LYS A CB  
2140 C CG  . LYS A 155 ? 0.2620 0.2485 0.2241 0.0141  0.0255  0.0452  155 LYS A CG  
2141 C CD  . LYS A 155 ? 0.3092 0.2906 0.2675 0.0184  0.0273  0.0529  155 LYS A CD  
2142 C CE  . LYS A 155 ? 0.3446 0.3229 0.3041 0.0189  0.0349  0.0628  155 LYS A CE  
2143 N NZ  . LYS A 155 ? 0.3282 0.3002 0.2838 0.0237  0.0369  0.0711  155 LYS A NZ  
2157 N N   . SER A 156 ? 0.1796 0.1725 0.1436 0.0121  0.0075  0.0217  156 SER A N   
2158 C CA  . SER A 156 ? 0.1867 0.1849 0.1495 0.0135  0.0032  0.0164  156 SER A CA  
2159 C C   . SER A 156 ? 0.1977 0.1925 0.1623 0.0146  0.0015  0.0177  156 SER A C   
2160 O O   . SER A 156 ? 0.2393 0.2392 0.2008 0.0186  -0.0010 0.0171  156 SER A O   
2161 C CB  . SER A 156 ? 0.1991 0.1991 0.1667 0.0096  0.0015  0.0099  156 SER A CB  
2162 O OG  . SER A 156 ? 0.1869 0.1816 0.1609 0.0059  0.0015  0.0092  156 SER A OG  
2168 N N   . VAL A 157 ? 0.1758 0.1628 0.1454 0.0118  0.0028  0.0193  157 VAL A N   
2169 C CA  . VAL A 157 ? 0.1813 0.1645 0.1526 0.0133  0.0015  0.0199  157 VAL A CA  
2170 C C   . VAL A 157 ? 0.1924 0.1721 0.1596 0.0181  0.0031  0.0263  157 VAL A C   
2171 O O   . VAL A 157 ? 0.1944 0.1766 0.1590 0.0227  0.0011  0.0269  157 VAL A O   
2172 C CB  . VAL A 157 ? 0.1714 0.1478 0.1488 0.0094  0.0019  0.0184  157 VAL A CB  
2173 C CG1 . VAL A 157 ? 0.2014 0.1733 0.1801 0.0116  0.0009  0.0185  157 VAL A CG1 
2174 C CG2 . VAL A 157 ? 0.1857 0.1659 0.1661 0.0060  0.0005  0.0133  157 VAL A CG2 
2184 N N   . GLU A 158 ? 0.1900 0.1643 0.1573 0.0174  0.0071  0.0317  158 GLU A N   
2185 C CA  . GLU A 158 ? 0.2156 0.1846 0.1798 0.0219  0.0098  0.0393  158 GLU A CA  
2186 C C   . GLU A 158 ? 0.2117 0.1890 0.1665 0.0289  0.0087  0.0419  158 GLU A C   
2187 O O   . GLU A 158 ? 0.2205 0.1964 0.1721 0.0346  0.0082  0.0459  158 GLU A O   
2188 C CB  . GLU A 158 ? 0.2228 0.1854 0.1905 0.0190  0.0152  0.0450  158 GLU A CB  
2189 C CG  . GLU A 158 ? 0.2300 0.1844 0.2082 0.0127  0.0156  0.0419  158 GLU A CG  
2190 C CD  . GLU A 158 ? 0.3042 0.2559 0.2885 0.0081  0.0203  0.0451  158 GLU A CD  
2191 O OE1 . GLU A 158 ? 0.3102 0.2673 0.2904 0.0094  0.0236  0.0492  158 GLU A OE1 
2192 O OE2 . GLU A 158 ? 0.2842 0.2297 0.2783 0.0033  0.0206  0.0427  158 GLU A OE2 
2199 N N   . ASP A 159 ? 0.2047 0.1914 0.1550 0.0291  0.0079  0.0393  159 ASP A N   
2200 C CA  . ASP A 159 ? 0.2312 0.2278 0.1720 0.0363  0.0062  0.0405  159 ASP A CA  
2201 C C   . ASP A 159 ? 0.2228 0.2258 0.1640 0.0390  0.0006  0.0352  159 ASP A C   
2202 O O   . ASP A 159 ? 0.2560 0.2642 0.1910 0.0463  -0.0011 0.0380  159 ASP A O   
2203 C CB  . ASP A 159 ? 0.2386 0.2441 0.1751 0.0359  0.0061  0.0367  159 ASP A CB  
2204 C CG  . ASP A 159 ? 0.2565 0.2592 0.1901 0.0359  0.0123  0.0435  159 ASP A CG  
2205 O OD1 . ASP A 159 ? 0.3313 0.3272 0.2639 0.0381  0.0169  0.0528  159 ASP A OD1 
2206 O OD2 . ASP A 159 ? 0.2968 0.3047 0.2296 0.0340  0.0128  0.0395  159 ASP A OD2 
2211 N N   . MET A 160 ? 0.2091 0.2123 0.1579 0.0337  -0.0021 0.0280  160 MET A N   
2212 C CA  . MET A 160 ? 0.1954 0.2059 0.1465 0.0359  -0.0067 0.0232  160 MET A CA  
2213 C C   . MET A 160 ? 0.2093 0.2134 0.1614 0.0396  -0.0062 0.0277  160 MET A C   
2214 O O   . MET A 160 ? 0.2144 0.2250 0.1642 0.0457  -0.0090 0.0281  160 MET A O   
2215 C CB  . MET A 160 ? 0.1977 0.2102 0.1569 0.0294  -0.0085 0.0155  160 MET A CB  
2216 C CG  . MET A 160 ? 0.2205 0.2406 0.1839 0.0312  -0.0122 0.0115  160 MET A CG  
2217 S SD  . MET A 160 ? 0.2324 0.2690 0.1935 0.0354  -0.0172 0.0061  160 MET A SD  
2218 C CE  . MET A 160 ? 0.2744 0.3137 0.2404 0.0283  -0.0176 -0.0015 160 MET A CE  
2228 N N   . VAL A 161 ? 0.2040 0.1957 0.1602 0.0364  -0.0031 0.0305  161 VAL A N   
2229 C CA  . VAL A 161 ? 0.2186 0.2029 0.1764 0.0400  -0.0026 0.0338  161 VAL A CA  
2230 C C   . VAL A 161 ? 0.2243 0.2061 0.1753 0.0476  -0.0007 0.0423  161 VAL A C   
2231 O O   . VAL A 161 ? 0.2451 0.2250 0.1957 0.0534  -0.0016 0.0448  161 VAL A O   
2232 C CB  . VAL A 161 ? 0.2036 0.1757 0.1680 0.0346  -0.0001 0.0331  161 VAL A CB  
2233 C CG1 . VAL A 161 ? 0.2241 0.1869 0.1905 0.0385  0.0006  0.0358  161 VAL A CG1 
2234 C CG2 . VAL A 161 ? 0.2033 0.1794 0.1726 0.0292  -0.0022 0.0255  161 VAL A CG2 
2244 N N   . ALA A 162 ? 0.2220 0.2045 0.1673 0.0484  0.0021  0.0474  162 ALA A N   
2245 C CA  . ALA A 162 ? 0.2516 0.2318 0.1896 0.0562  0.0048  0.0570  162 ALA A CA  
2246 C C   . ALA A 162 ? 0.2471 0.2405 0.1775 0.0650  0.0004  0.0567  162 ALA A C   
2247 O O   . ALA A 162 ? 0.2842 0.2759 0.2081 0.0734  0.0021  0.0652  162 ALA A O   
2248 C CB  . ALA A 162 ? 0.2660 0.2452 0.1997 0.0549  0.0097  0.0626  162 ALA A CB  
2254 N N   . THR A 163 ? 0.2383 0.2450 0.1702 0.0636  -0.0050 0.0474  163 THR A N   
2255 C CA  . THR A 163 ? 0.2509 0.2724 0.1776 0.0715  -0.0102 0.0452  163 THR A CA  
2256 C C   . THR A 163 ? 0.2673 0.2876 0.1974 0.0767  -0.0121 0.0464  163 THR A C   
2257 O O   . THR A 163 ? 0.2416 0.2511 0.1790 0.0729  -0.0104 0.0459  163 THR A O   
2258 C CB  . THR A 163 ? 0.2377 0.2733 0.1679 0.0672  -0.0153 0.0339  163 THR A CB  
2259 O OG1 . THR A 163 ? 0.2356 0.2696 0.1768 0.0605  -0.0166 0.0273  163 THR A OG1 
2260 C CG2 . THR A 163 ? 0.2565 0.2925 0.1837 0.0625  -0.0133 0.0321  163 THR A CG2 
2268 N N   . PRO A 164 ? 0.2701 0.3019 0.1945 0.0863  -0.0159 0.0478  164 PRO A N   
2269 C CA  . PRO A 164 ? 0.2796 0.3078 0.2055 0.0935  -0.0163 0.0520  164 PRO A CA  
2270 C C   . PRO A 164 ? 0.2603 0.2919 0.1970 0.0901  -0.0193 0.0439  164 PRO A C   
2271 O O   . PRO A 164 ? 0.3226 0.3465 0.2622 0.0941  -0.0182 0.0469  164 PRO A O   
2272 C CB  . PRO A 164 ? 0.3064 0.3484 0.2224 0.1056  -0.0199 0.0558  164 PRO A CB  
2273 C CG  . PRO A 164 ? 0.3329 0.3901 0.2454 0.1032  -0.0236 0.0486  164 PRO A CG  
2274 C CD  . PRO A 164 ? 0.2778 0.3249 0.1926 0.0926  -0.0192 0.0473  164 PRO A CD  
2282 N N   . ASN A 165 ? 0.2274 0.2696 0.1706 0.0832  -0.0225 0.0341  165 ASN A N   
2283 C CA  . ASN A 165 ? 0.2251 0.2736 0.1786 0.0809  -0.0249 0.0272  165 ASN A CA  
2284 C C   . ASN A 165 ? 0.2073 0.2465 0.1684 0.0709  -0.0219 0.0233  165 ASN A C   
2285 O O   . ASN A 165 ? 0.2106 0.2556 0.1800 0.0684  -0.0231 0.0178  165 ASN A O   
2286 C CB  . ASN A 165 ? 0.2010 0.2705 0.1583 0.0815  -0.0308 0.0191  165 ASN A CB  
2287 C CG  . ASN A 165 ? 0.2290 0.3102 0.1786 0.0925  -0.0347 0.0221  165 ASN A CG  
2288 O OD1 . ASN A 165 ? 0.2499 0.3305 0.1977 0.1012  -0.0350 0.0271  165 ASN A OD1 
2289 N ND2 . ASN A 165 ? 0.2487 0.3406 0.1929 0.0932  -0.0378 0.0190  165 ASN A ND2 
2296 N N   . ILE A 166 ? 0.1970 0.2229 0.1555 0.0657  -0.0180 0.0263  166 ILE A N   
2297 C CA  . ILE A 166 ? 0.1872 0.2044 0.1517 0.0572  -0.0154 0.0231  166 ILE A CA  
2298 C C   . ILE A 166 ? 0.2061 0.2064 0.1698 0.0584  -0.0117 0.0284  166 ILE A C   
2299 O O   . ILE A 166 ? 0.2138 0.2058 0.1722 0.0611  -0.0092 0.0353  166 ILE A O   
2300 C CB  . ILE A 166 ? 0.2032 0.2201 0.1668 0.0500  -0.0144 0.0210  166 ILE A CB  
2301 C CG1 . ILE A 166 ? 0.2169 0.2493 0.1828 0.0485  -0.0182 0.0144  166 ILE A CG1 
2302 C CG2 . ILE A 166 ? 0.1857 0.1933 0.1542 0.0425  -0.0118 0.0188  166 ILE A CG2 
2303 C CD1 . ILE A 166 ? 0.2926 0.3316 0.2681 0.0445  -0.0195 0.0082  166 ILE A CD1 
2315 N N   . ASP A 167 ? 0.1935 0.1890 0.1629 0.0565  -0.0110 0.0250  167 ASP A N   
2316 C CA  . ASP A 167 ? 0.2010 0.1810 0.1713 0.0578  -0.0083 0.0278  167 ASP A CA  
2317 C C   . ASP A 167 ? 0.1984 0.1685 0.1716 0.0499  -0.0060 0.0256  167 ASP A C   
2318 O O   . ASP A 167 ? 0.2205 0.1771 0.1955 0.0499  -0.0038 0.0274  167 ASP A O   
2319 C CB  . ASP A 167 ? 0.2116 0.1930 0.1854 0.0628  -0.0094 0.0249  167 ASP A CB  
2320 C CG  . ASP A 167 ? 0.2376 0.2286 0.2092 0.0715  -0.0117 0.0274  167 ASP A CG  
2321 O OD1 . ASP A 167 ? 0.2602 0.2448 0.2270 0.0776  -0.0108 0.0345  167 ASP A OD1 
2322 O OD2 . ASP A 167 ? 0.2156 0.2214 0.1907 0.0727  -0.0144 0.0229  167 ASP A OD2 
2327 N N   . GLY A 168 ? 0.1882 0.1647 0.1628 0.0435  -0.0066 0.0215  168 GLY A N   
2328 C CA  . GLY A 168 ? 0.1831 0.1522 0.1605 0.0369  -0.0050 0.0191  168 GLY A CA  
2329 C C   . GLY A 168 ? 0.1764 0.1543 0.1551 0.0315  -0.0059 0.0149  168 GLY A C   
2330 O O   . GLY A 168 ? 0.1687 0.1569 0.1466 0.0317  -0.0074 0.0142  168 GLY A O   
2334 N N   . THR A 169 ? 0.1697 0.1434 0.1511 0.0268  -0.0051 0.0119  169 THR A N   
2335 C CA  . THR A 169 ? 0.1680 0.1475 0.1506 0.0218  -0.0053 0.0091  169 THR A CA  
2336 C C   . THR A 169 ? 0.1500 0.1298 0.1349 0.0207  -0.0053 0.0051  169 THR A C   
2337 O O   . THR A 169 ? 0.1668 0.1402 0.1521 0.0224  -0.0052 0.0036  169 THR A O   
2338 C CB  . THR A 169 ? 0.1713 0.1468 0.1533 0.0176  -0.0040 0.0110  169 THR A CB  
2339 O OG1 . THR A 169 ? 0.1798 0.1609 0.1629 0.0138  -0.0041 0.0086  169 THR A OG1 
2340 C CG2 . THR A 169 ? 0.1929 0.1589 0.1772 0.0156  -0.0029 0.0108  169 THR A CG2 
2348 N N   . PHE A 170 ? 0.1469 0.1342 0.1332 0.0182  -0.0051 0.0034  170 PHE A N   
2349 C CA  . PHE A 170 ? 0.1451 0.1339 0.1323 0.0172  -0.0044 0.0009  170 PHE A CA  
2350 C C   . PHE A 170 ? 0.1498 0.1375 0.1372 0.0126  -0.0038 0.0011  170 PHE A C   
2351 O O   . PHE A 170 ? 0.1523 0.1440 0.1411 0.0102  -0.0034 0.0019  170 PHE A O   
2352 C CB  . PHE A 170 ? 0.1775 0.1760 0.1673 0.0183  -0.0036 0.0002  170 PHE A CB  
2353 C CG  . PHE A 170 ? 0.1582 0.1596 0.1485 0.0167  -0.0017 -0.0005 170 PHE A CG  
2354 C CD1 . PHE A 170 ? 0.2018 0.2010 0.1892 0.0192  -0.0014 -0.0023 170 PHE A CD1 
2355 C CD2 . PHE A 170 ? 0.2025 0.2085 0.1961 0.0131  -0.0001 0.0006  170 PHE A CD2 
2356 C CE1 . PHE A 170 ? 0.2178 0.2208 0.2042 0.0189  0.0006  -0.0020 170 PHE A CE1 
2357 C CE2 . PHE A 170 ? 0.2045 0.2127 0.1983 0.0124  0.0023  0.0015  170 PHE A CE2 
2358 C CZ  . PHE A 170 ? 0.1980 0.2050 0.1875 0.0155  0.0027  0.0006  170 PHE A CZ  
2368 N N   . ILE A 171 ? 0.1426 0.1253 0.1292 0.0118  -0.0040 -0.0003 171 ILE A N   
2369 C CA  . ILE A 171 ? 0.1410 0.1230 0.1281 0.0083  -0.0038 -0.0001 171 ILE A CA  
2370 C C   . ILE A 171 ? 0.1407 0.1271 0.1270 0.0088  -0.0031 -0.0010 171 ILE A C   
2371 O O   . ILE A 171 ? 0.1506 0.1376 0.1349 0.0116  -0.0036 -0.0032 171 ILE A O   
2372 C CB  . ILE A 171 ? 0.1662 0.1416 0.1543 0.0070  -0.0047 -0.0012 171 ILE A CB  
2373 C CG1 . ILE A 171 ? 0.1762 0.1464 0.1652 0.0069  -0.0043 0.0013  171 ILE A CG1 
2374 C CG2 . ILE A 171 ? 0.1700 0.1466 0.1593 0.0040  -0.0046 -0.0011 171 ILE A CG2 
2375 C CD1 . ILE A 171 ? 0.2171 0.1903 0.2050 0.0060  -0.0032 0.0045  171 ILE A CD1 
2387 N N   . ASP A 172 ? 0.1420 0.1313 0.1295 0.0065  -0.0017 0.0008  172 ASP A N   
2388 C CA  . ASP A 172 ? 0.1476 0.1405 0.1345 0.0072  0.0000  0.0018  172 ASP A CA  
2389 C C   . ASP A 172 ? 0.1375 0.1287 0.1239 0.0058  -0.0002 0.0024  172 ASP A C   
2390 O O   . ASP A 172 ? 0.1386 0.1270 0.1266 0.0035  -0.0011 0.0022  172 ASP A O   
2391 C CB  . ASP A 172 ? 0.1467 0.1440 0.1374 0.0058  0.0024  0.0038  172 ASP A CB  
2392 C CG  . ASP A 172 ? 0.1945 0.1960 0.1853 0.0073  0.0054  0.0060  172 ASP A CG  
2393 O OD1 . ASP A 172 ? 0.1726 0.1750 0.1586 0.0108  0.0054  0.0058  172 ASP A OD1 
2394 O OD2 . ASP A 172 ? 0.2349 0.2388 0.2309 0.0050  0.0080  0.0080  172 ASP A OD2 
2399 N N   . ALA A 173 ? 0.1459 0.1398 0.1299 0.0081  0.0007  0.0034  173 ALA A N   
2400 C CA  . ALA A 173 ? 0.1316 0.1256 0.1145 0.0085  0.0005  0.0045  173 ALA A CA  
2401 C C   . ALA A 173 ? 0.1546 0.1480 0.1363 0.0093  -0.0031 0.0008  173 ALA A C   
2402 O O   . ALA A 173 ? 0.1597 0.1541 0.1417 0.0095  -0.0040 0.0009  173 ALA A O   
2403 C CB  . ALA A 173 ? 0.1511 0.1428 0.1379 0.0054  0.0020  0.0068  173 ALA A CB  
2409 N N   . ASN A 174 ? 0.1481 0.1402 0.1293 0.0101  -0.0051 -0.0030 174 ASN A N   
2410 C CA  . ASN A 174 ? 0.1484 0.1408 0.1297 0.0111  -0.0087 -0.0079 174 ASN A CA  
2411 C C   . ASN A 174 ? 0.1562 0.1547 0.1328 0.0153  -0.0098 -0.0085 174 ASN A C   
2412 O O   . ASN A 174 ? 0.1634 0.1642 0.1414 0.0155  -0.0127 -0.0113 174 ASN A O   
2413 C CB  . ASN A 174 ? 0.1580 0.1478 0.1389 0.0125  -0.0103 -0.0122 174 ASN A CB  
2414 C CG  . ASN A 174 ? 0.1442 0.1291 0.1277 0.0105  -0.0086 -0.0102 174 ASN A CG  
2415 O OD1 . ASN A 174 ? 0.1719 0.1519 0.1596 0.0073  -0.0089 -0.0099 174 ASN A OD1 
2416 N ND2 . ASN A 174 ? 0.1714 0.1584 0.1526 0.0125  -0.0066 -0.0081 174 ASN A ND2 
2423 N N   . ILE A 175 ? 0.1506 0.1528 0.1219 0.0191  -0.0075 -0.0058 175 ILE A N   
2424 C CA  . ILE A 175 ? 0.1629 0.1717 0.1278 0.0246  -0.0080 -0.0055 175 ILE A CA  
2425 C C   . ILE A 175 ? 0.1573 0.1672 0.1228 0.0245  -0.0072 -0.0010 175 ILE A C   
2426 O O   . ILE A 175 ? 0.1664 0.1814 0.1287 0.0284  -0.0098 -0.0024 175 ILE A O   
2427 C CB  . ILE A 175 ? 0.1592 0.1718 0.1185 0.0288  -0.0043 -0.0023 175 ILE A CB  
2428 C CG1 . ILE A 175 ? 0.1824 0.1951 0.1403 0.0307  -0.0060 -0.0082 175 ILE A CG1 
2429 C CG2 . ILE A 175 ? 0.2004 0.2201 0.1520 0.0352  -0.0034 0.0007  175 ILE A CG2 
2430 C CD1 . ILE A 175 ? 0.1993 0.2154 0.1545 0.0334  -0.0015 -0.0049 175 ILE A CD1 
2442 N N   . LYS A 176 ? 0.1620 0.1674 0.1320 0.0206  -0.0039 0.0037  176 LYS A N   
2443 C CA  . LYS A 176 ? 0.1667 0.1717 0.1384 0.0206  -0.0029 0.0075  176 LYS A CA  
2444 C C   . LYS A 176 ? 0.1581 0.1640 0.1334 0.0192  -0.0070 0.0033  176 LYS A C   
2445 O O   . LYS A 176 ? 0.1810 0.1904 0.1556 0.0221  -0.0080 0.0046  176 LYS A O   
2446 C CB  . LYS A 176 ? 0.1729 0.1725 0.1494 0.0166  0.0013  0.0118  176 LYS A CB  
2447 C CG  . LYS A 176 ? 0.1673 0.1673 0.1427 0.0176  0.0059  0.0166  176 LYS A CG  
2448 C CD  . LYS A 176 ? 0.1684 0.1635 0.1507 0.0131  0.0094  0.0193  176 LYS A CD  
2449 C CE  . LYS A 176 ? 0.1989 0.1948 0.1828 0.0134  0.0145  0.0243  176 LYS A CE  
2450 N NZ  . LYS A 176 ? 0.2153 0.2148 0.1988 0.0132  0.0147  0.0223  176 LYS A NZ  
2464 N N   . VAL A 177 ? 0.1540 0.1572 0.1338 0.0151  -0.0091 -0.0014 177 VAL A N   
2465 C CA  . VAL A 177 ? 0.1592 0.1642 0.1443 0.0133  -0.0126 -0.0056 177 VAL A CA  
2466 C C   . VAL A 177 ? 0.1665 0.1783 0.1494 0.0173  -0.0172 -0.0109 177 VAL A C   
2467 O O   . VAL A 177 ? 0.1729 0.1901 0.1587 0.0184  -0.0200 -0.0129 177 VAL A O   
2468 C CB  . VAL A 177 ? 0.1525 0.1522 0.1434 0.0080  -0.0126 -0.0080 177 VAL A CB  
2469 C CG1 . VAL A 177 ? 0.1710 0.1729 0.1689 0.0058  -0.0158 -0.0127 177 VAL A CG1 
2470 C CG2 . VAL A 177 ? 0.1677 0.1627 0.1604 0.0048  -0.0089 -0.0037 177 VAL A CG2 
2480 N N   . LEU A 178 ? 0.1564 0.1691 0.1347 0.0198  -0.0184 -0.0140 178 LEU A N   
2481 C CA  . LEU A 178 ? 0.1791 0.1977 0.1565 0.0228  -0.0237 -0.0218 178 LEU A CA  
2482 C C   . LEU A 178 ? 0.1814 0.2092 0.1497 0.0307  -0.0252 -0.0213 178 LEU A C   
2483 O O   . LEU A 178 ? 0.2007 0.2358 0.1685 0.0339  -0.0307 -0.0284 178 LEU A O   
2484 C CB  . LEU A 178 ? 0.1716 0.1858 0.1489 0.0220  -0.0244 -0.0268 178 LEU A CB  
2485 C CG  . LEU A 178 ? 0.1931 0.1987 0.1797 0.0151  -0.0235 -0.0277 178 LEU A CG  
2486 C CD1 . LEU A 178 ? 0.2204 0.2202 0.2058 0.0154  -0.0230 -0.0304 178 LEU A CD1 
2487 C CD2 . LEU A 178 ? 0.2446 0.2515 0.2409 0.0115  -0.0273 -0.0335 178 LEU A CD2 
2499 N N   . VAL A 179 ? 0.1737 0.2017 0.1352 0.0341  -0.0206 -0.0130 179 VAL A N   
2500 C CA  . VAL A 179 ? 0.1757 0.2122 0.1280 0.0424  -0.0210 -0.0100 179 VAL A CA  
2501 C C   . VAL A 179 ? 0.1844 0.2231 0.1406 0.0426  -0.0220 -0.0071 179 VAL A C   
2502 O O   . VAL A 179 ? 0.1803 0.2125 0.1400 0.0395  -0.0175 -0.0004 179 VAL A O   
2503 C CB  . VAL A 179 ? 0.1861 0.2208 0.1315 0.0454  -0.0144 -0.0012 179 VAL A CB  
2504 C CG1 . VAL A 179 ? 0.2060 0.2478 0.1426 0.0537  -0.0131 0.0050  179 VAL A CG1 
2505 C CG2 . VAL A 179 ? 0.2168 0.2518 0.1582 0.0465  -0.0137 -0.0046 179 VAL A CG2 
2515 N N   . PRO A 180 ? 0.1881 0.2356 0.1450 0.0459  -0.0279 -0.0128 180 PRO A N   
2516 C CA  . PRO A 180 ? 0.1954 0.2447 0.1591 0.0447  -0.0289 -0.0112 180 PRO A CA  
2517 C C   . PRO A 180 ? 0.2144 0.2619 0.1736 0.0491  -0.0241 -0.0006 180 PRO A C   
2518 O O   . PRO A 180 ? 0.2045 0.2476 0.1704 0.0459  -0.0221 0.0025  180 PRO A O   
2519 C CB  . PRO A 180 ? 0.2591 0.3208 0.2242 0.0486  -0.0367 -0.0199 180 PRO A CB  
2520 C CG  . PRO A 180 ? 0.2936 0.3567 0.2569 0.0481  -0.0402 -0.0287 180 PRO A CG  
2521 C CD  . PRO A 180 ? 0.2393 0.2952 0.1944 0.0489  -0.0346 -0.0232 180 PRO A CD  
2529 N N   . SER A 181 ? 0.2070 0.2571 0.1552 0.0564  -0.0216 0.0053  181 SER A N   
2530 C CA  . SER A 181 ? 0.2040 0.2513 0.1489 0.0607  -0.0165 0.0160  181 SER A CA  
2531 C C   . SER A 181 ? 0.2143 0.2487 0.1653 0.0540  -0.0097 0.0219  181 SER A C   
2532 O O   . SER A 181 ? 0.2216 0.2514 0.1744 0.0555  -0.0060 0.0290  181 SER A O   
2533 C CB  . SER A 181 ? 0.2188 0.2718 0.1508 0.0702  -0.0142 0.0222  181 SER A CB  
2534 O OG  . SER A 181 ? 0.2690 0.3188 0.1976 0.0681  -0.0107 0.0224  181 SER A OG  
2540 N N   . PHE A 182 ? 0.1924 0.2210 0.1470 0.0471  -0.0082 0.0189  182 PHE A N   
2541 C CA  . PHE A 182 ? 0.2019 0.2200 0.1619 0.0414  -0.0023 0.0238  182 PHE A CA  
2542 C C   . PHE A 182 ? 0.1926 0.2063 0.1606 0.0379  -0.0025 0.0235  182 PHE A C   
2543 O O   . PHE A 182 ? 0.2043 0.2121 0.1745 0.0383  0.0018  0.0296  182 PHE A O   
2544 C CB  . PHE A 182 ? 0.1987 0.2129 0.1611 0.0354  -0.0014 0.0202  182 PHE A CB  
2545 C CG  . PHE A 182 ? 0.2040 0.2097 0.1722 0.0301  0.0038  0.0243  182 PHE A CG  
2546 C CD1 . PHE A 182 ? 0.2213 0.2249 0.1880 0.0312  0.0095  0.0308  182 PHE A CD1 
2547 C CD2 . PHE A 182 ? 0.2034 0.2040 0.1790 0.0244  0.0034  0.0217  182 PHE A CD2 
2548 C CE1 . PHE A 182 ? 0.2256 0.2220 0.1996 0.0258  0.0137  0.0333  182 PHE A CE1 
2549 C CE2 . PHE A 182 ? 0.1953 0.1892 0.1762 0.0201  0.0073  0.0241  182 PHE A CE2 
2550 C CZ  . PHE A 182 ? 0.2048 0.1965 0.1856 0.0205  0.0122  0.0294  182 PHE A CZ  
2560 N N   . PHE A 183 ? 0.1773 0.1936 0.1507 0.0343  -0.0070 0.0164  183 PHE A N   
2561 C CA  . PHE A 183 ? 0.1800 0.1942 0.1605 0.0320  -0.0070 0.0161  183 PHE A CA  
2562 C C   . PHE A 183 ? 0.1705 0.1923 0.1508 0.0382  -0.0099 0.0166  183 PHE A C   
2563 O O   . PHE A 183 ? 0.1706 0.1900 0.1551 0.0389  -0.0082 0.0191  183 PHE A O   
2564 C CB  . PHE A 183 ? 0.1659 0.1792 0.1533 0.0251  -0.0089 0.0098  183 PHE A CB  
2565 C CG  . PHE A 183 ? 0.1673 0.1724 0.1563 0.0195  -0.0054 0.0105  183 PHE A CG  
2566 C CD1 . PHE A 183 ? 0.1757 0.1744 0.1669 0.0182  -0.0012 0.0142  183 PHE A CD1 
2567 C CD2 . PHE A 183 ? 0.1683 0.1725 0.1568 0.0162  -0.0064 0.0070  183 PHE A CD2 
2568 C CE1 . PHE A 183 ? 0.1733 0.1662 0.1660 0.0136  0.0012  0.0139  183 PHE A CE1 
2569 C CE2 . PHE A 183 ? 0.1717 0.1699 0.1613 0.0121  -0.0036 0.0078  183 PHE A CE2 
2570 C CZ  . PHE A 183 ? 0.1783 0.1717 0.1700 0.0108  -0.0001 0.0110  183 PHE A CZ  
2580 N N   . SER A 184 ? 0.1823 0.2139 0.1577 0.0436  -0.0144 0.0140  184 SER A N   
2581 C CA  . SER A 184 ? 0.1940 0.2343 0.1700 0.0499  -0.0178 0.0142  184 SER A CA  
2582 C C   . SER A 184 ? 0.2009 0.2374 0.1720 0.0566  -0.0134 0.0240  184 SER A C   
2583 O O   . SER A 184 ? 0.2175 0.2562 0.1919 0.0603  -0.0139 0.0259  184 SER A O   
2584 C CB  . SER A 184 ? 0.2128 0.2662 0.1853 0.0545  -0.0247 0.0078  184 SER A CB  
2585 O OG  . SER A 184 ? 0.2455 0.3020 0.2060 0.0620  -0.0241 0.0120  184 SER A OG  
2591 N N   . SER A 185 ? 0.2049 0.2349 0.1695 0.0580  -0.0083 0.0306  185 SER A N   
2592 C CA  . SER A 185 ? 0.2331 0.2569 0.1947 0.0633  -0.0027 0.0409  185 SER A CA  
2593 C C   . SER A 185 ? 0.2370 0.2491 0.2075 0.0583  0.0017  0.0430  185 SER A C   
2594 O O   . SER A 185 ? 0.2684 0.2746 0.2390 0.0629  0.0058  0.0507  185 SER A O   
2595 C CB  . SER A 185 ? 0.2458 0.2664 0.1999 0.0651  0.0022  0.0474  185 SER A CB  
2596 O OG  . SER A 185 ? 0.2714 0.2837 0.2305 0.0562  0.0055  0.0455  185 SER A OG  
2602 N N   . LYS A 186 ? 0.2137 0.2223 0.1914 0.0497  0.0009  0.0365  186 LYS A N   
2603 C CA  . LYS A 186 ? 0.1919 0.1909 0.1773 0.0451  0.0045  0.0366  186 LYS A CA  
2604 C C   . LYS A 186 ? 0.1971 0.2004 0.1887 0.0447  0.0014  0.0316  186 LYS A C   
2605 O O   . LYS A 186 ? 0.2290 0.2269 0.2250 0.0461  0.0039  0.0336  186 LYS A O   
2606 C CB  . LYS A 186 ? 0.2188 0.2117 0.2071 0.0365  0.0063  0.0332  186 LYS A CB  
2607 C CG  . LYS A 186 ? 0.2330 0.2219 0.2175 0.0360  0.0102  0.0379  186 LYS A CG  
2608 C CD  . LYS A 186 ? 0.2479 0.2341 0.2355 0.0283  0.0106  0.0334  186 LYS A CD  
2609 C CE  . LYS A 186 ? 0.2593 0.2424 0.2452 0.0275  0.0149  0.0379  186 LYS A CE  
2610 N NZ  . LYS A 186 ? 0.2985 0.2886 0.2758 0.0333  0.0144  0.0413  186 LYS A NZ  
2624 N N   . VAL A 187 ? 0.1811 0.1939 0.1742 0.0428  -0.0037 0.0250  187 VAL A N   
2625 C CA  . VAL A 187 ? 0.1772 0.1949 0.1781 0.0407  -0.0059 0.0200  187 VAL A CA  
2626 C C   . VAL A 187 ? 0.1801 0.2117 0.1825 0.0442  -0.0118 0.0160  187 VAL A C   
2627 O O   . VAL A 187 ? 0.1765 0.2143 0.1869 0.0420  -0.0136 0.0115  187 VAL A O   
2628 C CB  . VAL A 187 ? 0.1781 0.1921 0.1836 0.0320  -0.0048 0.0152  187 VAL A CB  
2629 C CG1 . VAL A 187 ? 0.2135 0.2158 0.2195 0.0293  0.0002  0.0176  187 VAL A CG1 
2630 C CG2 . VAL A 187 ? 0.1716 0.1872 0.1743 0.0282  -0.0070 0.0121  187 VAL A CG2 
2640 N N   . GLY A 188 ? 0.1778 0.2156 0.1732 0.0496  -0.0148 0.0170  188 GLY A N   
2641 C CA  . GLY A 188 ? 0.1696 0.2220 0.1664 0.0539  -0.0213 0.0122  188 GLY A CA  
2642 C C   . GLY A 188 ? 0.1596 0.2178 0.1591 0.0484  -0.0258 0.0038  188 GLY A C   
2643 O O   . GLY A 188 ? 0.1651 0.2161 0.1667 0.0409  -0.0238 0.0016  188 GLY A O   
2647 N N   . VAL A 189 ? 0.1772 0.2086 0.1661 0.0603  -0.0269 -0.0043 189 VAL A N   
2648 C CA  . VAL A 189 ? 0.1867 0.2254 0.1748 0.0548  -0.0318 -0.0104 189 VAL A CA  
2649 C C   . VAL A 189 ? 0.1730 0.2195 0.1757 0.0455  -0.0327 -0.0158 189 VAL A C   
2650 O O   . VAL A 189 ? 0.1739 0.2169 0.1777 0.0377  -0.0326 -0.0191 189 VAL A O   
2651 C CB  . VAL A 189 ? 0.2086 0.2581 0.1898 0.0627  -0.0404 -0.0122 189 VAL A CB  
2652 C CG1 . VAL A 189 ? 0.2451 0.3020 0.2302 0.0563  -0.0490 -0.0213 189 VAL A CG1 
2653 C CG2 . VAL A 189 ? 0.2437 0.2848 0.2061 0.0721  -0.0375 -0.0056 189 VAL A CG2 
2663 N N   . ASN A 190 ? 0.1577 0.2157 0.1718 0.0474  -0.0329 -0.0155 190 ASN A N   
2664 C CA  . ASN A 190 ? 0.1513 0.2201 0.1805 0.0398  -0.0320 -0.0175 190 ASN A CA  
2665 C C   . ASN A 190 ? 0.1602 0.2171 0.1868 0.0345  -0.0250 -0.0173 190 ASN A C   
2666 O O   . ASN A 190 ? 0.1554 0.2138 0.1879 0.0262  -0.0245 -0.0186 190 ASN A O   
2667 C CB  . ASN A 190 ? 0.1480 0.2328 0.1889 0.0458  -0.0304 -0.0151 190 ASN A CB  
2668 C CG  . ASN A 190 ? 0.1530 0.2544 0.2009 0.0513  -0.0384 -0.0148 190 ASN A CG  
2669 O OD1 . ASN A 190 ? 0.1645 0.2673 0.2099 0.0490  -0.0469 -0.0181 190 ASN A OD1 
2670 N ND2 . ASN A 190 ? 0.1569 0.2713 0.2125 0.0601  -0.0363 -0.0116 190 ASN A ND2 
2677 N N   . LYS A 191 ? 0.1451 0.1896 0.1638 0.0393  -0.0206 -0.0158 191 LYS A N   
2678 C CA  . LYS A 191 ? 0.1426 0.1766 0.1587 0.0353  -0.0163 -0.0167 191 LYS A CA  
2679 C C   . LYS A 191 ? 0.1586 0.1832 0.1703 0.0284  -0.0164 -0.0168 191 LYS A C   
2680 O O   . LYS A 191 ? 0.1491 0.1721 0.1625 0.0228  -0.0145 -0.0178 191 LYS A O   
2681 C CB  . LYS A 191 ? 0.1551 0.1762 0.1655 0.0419  -0.0146 -0.0168 191 LYS A CB  
2682 C CG  . LYS A 191 ? 0.1593 0.1705 0.1667 0.0394  -0.0129 -0.0197 191 LYS A CG  
2683 C CD  . LYS A 191 ? 0.1972 0.2204 0.2061 0.0414  -0.0098 -0.0216 191 LYS A CD  
2684 C CE  . LYS A 191 ? 0.2030 0.2155 0.2040 0.0426  -0.0097 -0.0258 191 LYS A CE  
2685 N NZ  . LYS A 191 ? 0.2426 0.2647 0.2393 0.0515  -0.0059 -0.0275 191 LYS A NZ  
2699 N N   . GLN A 192 ? 0.1572 0.1768 0.1625 0.0304  -0.0179 -0.0148 192 GLN A N   
2700 C CA  . GLN A 192 ? 0.1575 0.1707 0.1582 0.0261  -0.0170 -0.0146 192 GLN A CA  
2701 C C   . GLN A 192 ? 0.1527 0.1717 0.1572 0.0204  -0.0199 -0.0191 192 GLN A C   
2702 O O   . GLN A 192 ? 0.1531 0.1668 0.1575 0.0156  -0.0180 -0.0196 192 GLN A O   
2703 C CB  . GLN A 192 ? 0.1698 0.1797 0.1607 0.0321  -0.0169 -0.0107 192 GLN A CB  
2704 C CG  . GLN A 192 ? 0.1761 0.1804 0.1615 0.0306  -0.0137 -0.0090 192 GLN A CG  
2705 C CD  . GLN A 192 ? 0.1932 0.1998 0.1740 0.0292  -0.0180 -0.0158 192 GLN A CD  
2706 O OE1 . GLN A 192 ? 0.1997 0.2123 0.1797 0.0304  -0.0249 -0.0212 192 GLN A OE1 
2707 N NE2 . GLN A 192 ? 0.1940 0.1954 0.1728 0.0270  -0.0150 -0.0159 192 GLN A NE2 
2716 N N   . ALA A 193 ? 0.1596 0.1893 0.1696 0.0206  -0.0253 -0.0218 193 ALA A N   
2717 C CA  . ALA A 193 ? 0.1592 0.1923 0.1769 0.0137  -0.0298 -0.0257 193 ALA A CA  
2718 C C   . ALA A 193 ? 0.1543 0.1900 0.1829 0.0072  -0.0249 -0.0231 193 ALA A C   
2719 O O   . ALA A 193 ? 0.1601 0.1907 0.1917 0.0013  -0.0251 -0.0238 193 ALA A O   
2720 C CB  . ALA A 193 ? 0.1722 0.2175 0.1980 0.0141  -0.0388 -0.0291 193 ALA A CB  
2726 N N   . GLU A 194 ? 0.1445 0.1869 0.1767 0.0102  -0.0201 -0.0197 194 GLU A N   
2727 C CA  . GLU A 194 ? 0.1273 0.1735 0.1655 0.0074  -0.0145 -0.0164 194 GLU A CA  
2728 C C   . GLU A 194 ? 0.1429 0.1758 0.1712 0.0065  -0.0113 -0.0166 194 GLU A C   
2729 O O   . GLU A 194 ? 0.1442 0.1764 0.1753 0.0023  -0.0089 -0.0143 194 GLU A O   
2730 C CB  . GLU A 194 ? 0.1493 0.2058 0.1894 0.0146  -0.0107 -0.0142 194 GLU A CB  
2731 C CG  . GLU A 194 ? 0.1713 0.2471 0.2272 0.0150  -0.0127 -0.0118 194 GLU A CG  
2732 C CD  . GLU A 194 ? 0.3467 0.4307 0.4013 0.0257  -0.0112 -0.0113 194 GLU A CD  
2733 O OE1 . GLU A 194 ? 0.3156 0.3894 0.3572 0.0331  -0.0078 -0.0130 194 GLU A OE1 
2734 O OE2 . GLU A 194 ? 0.4099 0.5105 0.4776 0.0271  -0.0144 -0.0096 194 GLU A OE2 
2741 N N   . ILE A 195 ? 0.1360 0.1588 0.1545 0.0102  -0.0116 -0.0180 195 ILE A N   
2742 C CA  . ILE A 195 ? 0.1352 0.1476 0.1483 0.0086  -0.0100 -0.0177 195 ILE A CA  
2743 C C   . ILE A 195 ? 0.1393 0.1482 0.1528 0.0041  -0.0106 -0.0177 195 ILE A C   
2744 O O   . ILE A 195 ? 0.1524 0.1582 0.1659 0.0016  -0.0088 -0.0164 195 ILE A O   
2745 C CB  . ILE A 195 ? 0.1488 0.1526 0.1575 0.0118  -0.0106 -0.0172 195 ILE A CB  
2746 C CG1 . ILE A 195 ? 0.1465 0.1484 0.1543 0.0167  -0.0112 -0.0186 195 ILE A CG1 
2747 C CG2 . ILE A 195 ? 0.1598 0.1564 0.1681 0.0090  -0.0097 -0.0156 195 ILE A CG2 
2748 C CD1 . ILE A 195 ? 0.1690 0.1609 0.1763 0.0194  -0.0125 -0.0167 195 ILE A CD1 
2760 N N   . GLU A 196 ? 0.1456 0.1537 0.1573 0.0045  -0.0138 -0.0197 196 GLU A N   
2761 C CA  . GLU A 196 ? 0.1529 0.1547 0.1622 0.0025  -0.0156 -0.0218 196 GLU A CA  
2762 C C   . GLU A 196 ? 0.1567 0.1596 0.1757 -0.0038 -0.0166 -0.0216 196 GLU A C   
2763 O O   . GLU A 196 ? 0.1585 0.1538 0.1766 -0.0056 -0.0153 -0.0208 196 GLU A O   
2764 C CB  . GLU A 196 ? 0.1785 0.1790 0.1806 0.0067  -0.0204 -0.0258 196 GLU A CB  
2765 C CG  . GLU A 196 ? 0.2175 0.2088 0.2128 0.0078  -0.0232 -0.0302 196 GLU A CG  
2766 C CD  . GLU A 196 ? 0.2482 0.2382 0.2315 0.0151  -0.0290 -0.0356 196 GLU A CD  
2767 O OE1 . GLU A 196 ? 0.2935 0.2778 0.2751 0.0145  -0.0373 -0.0435 196 GLU A OE1 
2768 O OE2 . GLU A 196 ? 0.2631 0.2568 0.2381 0.0220  -0.0261 -0.0320 196 GLU A OE2 
2775 N N   . ASN A 197 ? 0.1448 0.1578 0.1751 -0.0068 -0.0184 -0.0207 197 ASN A N   
2776 C CA  . ASN A 197 ? 0.1506 0.1665 0.1946 -0.0136 -0.0179 -0.0169 197 ASN A CA  
2777 C C   . ASN A 197 ? 0.1406 0.1556 0.1823 -0.0130 -0.0105 -0.0108 197 ASN A C   
2778 O O   . ASN A 197 ? 0.1504 0.1595 0.1960 -0.0167 -0.0092 -0.0074 197 ASN A O   
2779 C CB  . ASN A 197 ? 0.1698 0.2021 0.2302 -0.0163 -0.0191 -0.0139 197 ASN A CB  
2780 C CG  . ASN A 197 ? 0.2704 0.3052 0.3370 -0.0181 -0.0292 -0.0201 197 ASN A CG  
2781 O OD1 . ASN A 197 ? 0.3353 0.3576 0.3958 -0.0190 -0.0362 -0.0269 197 ASN A OD1 
2782 N ND2 . ASN A 197 ? 0.3614 0.4130 0.4390 -0.0170 -0.0305 -0.0182 197 ASN A ND2 
2789 N N   . SER A 198 ? 0.1337 0.1538 0.1685 -0.0077 -0.0065 -0.0097 198 SER A N   
2790 C CA  . SER A 198 ? 0.1359 0.1559 0.1654 -0.0051 -0.0015 -0.0056 198 SER A CA  
2791 C C   . SER A 198 ? 0.1473 0.1555 0.1696 -0.0052 -0.0024 -0.0068 198 SER A C   
2792 O O   . SER A 198 ? 0.1570 0.1634 0.1785 -0.0053 0.0002  -0.0024 198 SER A O   
2793 C CB  . SER A 198 ? 0.1399 0.1646 0.1616 0.0019  0.0000  -0.0073 198 SER A CB  
2794 O OG  . SER A 198 ? 0.1514 0.1892 0.1797 0.0043  0.0024  -0.0050 198 SER A OG  
2800 N N   . TYR A 199 ? 0.1463 0.1480 0.1636 -0.0040 -0.0053 -0.0113 199 TYR A N   
2801 C CA  . TYR A 199 ? 0.1537 0.1474 0.1667 -0.0030 -0.0053 -0.0114 199 TYR A CA  
2802 C C   . TYR A 199 ? 0.1519 0.1389 0.1675 -0.0054 -0.0054 -0.0100 199 TYR A C   
2803 O O   . TYR A 199 ? 0.1580 0.1415 0.1723 -0.0043 -0.0035 -0.0067 199 TYR A O   
2804 C CB  . TYR A 199 ? 0.1459 0.1369 0.1549 -0.0003 -0.0066 -0.0140 199 TYR A CB  
2805 C CG  . TYR A 199 ? 0.1417 0.1272 0.1476 0.0023  -0.0052 -0.0131 199 TYR A CG  
2806 C CD1 . TYR A 199 ? 0.1575 0.1449 0.1656 0.0035  -0.0036 -0.0096 199 TYR A CD1 
2807 C CD2 . TYR A 199 ? 0.1678 0.1467 0.1692 0.0043  -0.0064 -0.0161 199 TYR A CD2 
2808 C CE1 . TYR A 199 ? 0.1607 0.1465 0.1683 0.0070  -0.0014 -0.0073 199 TYR A CE1 
2809 C CE2 . TYR A 199 ? 0.1635 0.1379 0.1605 0.0093  -0.0041 -0.0152 199 TYR A CE2 
2810 C CZ  . TYR A 199 ? 0.1575 0.1369 0.1585 0.0108  -0.0007 -0.0099 199 TYR A CZ  
2811 O OH  . TYR A 199 ? 0.1697 0.1476 0.1683 0.0170  0.0024  -0.0079 199 TYR A OH  
2821 N N   . PHE A 200 ? 0.1479 0.1320 0.1679 -0.0085 -0.0087 -0.0129 200 PHE A N   
2822 C CA  . PHE A 200 ? 0.1636 0.1368 0.1873 -0.0111 -0.0105 -0.0127 200 PHE A CA  
2823 C C   . PHE A 200 ? 0.1536 0.1291 0.1863 -0.0149 -0.0067 -0.0042 200 PHE A C   
2824 O O   . PHE A 200 ? 0.1870 0.1525 0.2202 -0.0149 -0.0058 -0.0011 200 PHE A O   
2825 C CB  . PHE A 200 ? 0.1804 0.1483 0.2078 -0.0139 -0.0179 -0.0195 200 PHE A CB  
2826 C CG  . PHE A 200 ? 0.1829 0.1447 0.1962 -0.0068 -0.0211 -0.0273 200 PHE A CG  
2827 C CD1 . PHE A 200 ? 0.2448 0.1966 0.2480 -0.0005 -0.0193 -0.0287 200 PHE A CD1 
2828 C CD2 . PHE A 200 ? 0.2207 0.1884 0.2306 -0.0048 -0.0252 -0.0319 200 PHE A CD2 
2829 C CE1 . PHE A 200 ? 0.2871 0.2355 0.2761 0.0083  -0.0203 -0.0341 200 PHE A CE1 
2830 C CE2 . PHE A 200 ? 0.2489 0.2120 0.2433 0.0039  -0.0272 -0.0375 200 PHE A CE2 
2831 C CZ  . PHE A 200 ? 0.2383 0.1924 0.2222 0.0106  -0.0240 -0.0381 200 PHE A CZ  
2841 N N   . SER A 201 ? 0.1485 0.1372 0.1879 -0.0168 -0.0037 0.0007  201 SER A N   
2842 C CA  . SER A 201 ? 0.1645 0.1584 0.2097 -0.0177 0.0023  0.0113  201 SER A CA  
2843 C C   . SER A 201 ? 0.1580 0.1497 0.1906 -0.0112 0.0054  0.0139  201 SER A C   
2844 O O   . SER A 201 ? 0.1693 0.1564 0.2032 -0.0108 0.0083  0.0213  201 SER A O   
2845 C CB  . SER A 201 ? 0.1741 0.1856 0.2251 -0.0170 0.0064  0.0158  201 SER A CB  
2846 O OG  . SER A 201 ? 0.2541 0.2736 0.3079 -0.0151 0.0141  0.0277  201 SER A OG  
2852 N N   . MET A 202 ? 0.1570 0.1516 0.1790 -0.0063 0.0039  0.0081  202 MET A N   
2853 C CA  . MET A 202 ? 0.1500 0.1440 0.1626 -0.0008 0.0041  0.0093  202 MET A CA  
2854 C C   . MET A 202 ? 0.1611 0.1444 0.1738 -0.0003 0.0030  0.0096  202 MET A C   
2855 O O   . MET A 202 ? 0.1679 0.1502 0.1776 0.0033  0.0044  0.0150  202 MET A O   
2856 C CB  . MET A 202 ? 0.1595 0.1576 0.1659 0.0024  0.0008  0.0028  202 MET A CB  
2857 C CG  . MET A 202 ? 0.1409 0.1475 0.1434 0.0055  0.0016  0.0016  202 MET A CG  
2858 S SD  . MET A 202 ? 0.1860 0.1913 0.1859 0.0069  -0.0036 -0.0071 202 MET A SD  
2859 C CE  . MET A 202 ? 0.2344 0.2376 0.2288 0.0105  -0.0092 -0.0094 202 MET A CE  
2869 N N   . MET A 203 ? 0.1591 0.1348 0.1733 -0.0018 0.0005  0.0040  203 MET A N   
2870 C CA  . MET A 203 ? 0.1584 0.1242 0.1705 0.0015  0.0001  0.0037  203 MET A CA  
2871 C C   . MET A 203 ? 0.1693 0.1240 0.1860 -0.0003 0.0010  0.0085  203 MET A C   
2872 O O   . MET A 203 ? 0.1857 0.1335 0.2002 0.0042  0.0020  0.0119  203 MET A O   
2873 C CB  . MET A 203 ? 0.1701 0.1308 0.1792 0.0033  -0.0021 -0.0037 203 MET A CB  
2874 C CG  . MET A 203 ? 0.1644 0.1352 0.1714 0.0052  -0.0017 -0.0054 203 MET A CG  
2875 S SD  . MET A 203 ? 0.1773 0.1570 0.1868 0.0089  -0.0006 -0.0008 203 MET A SD  
2876 C CE  . MET A 203 ? 0.1973 0.1853 0.2076 0.0055  -0.0032 -0.0008 203 MET A CE  
2886 N N   . SER A 204 ? 0.1786 0.1314 0.2041 -0.0070 0.0003  0.0100  204 SER A N   
2887 C CA  . SER A 204 ? 0.1847 0.1265 0.2194 -0.0106 0.0011  0.0171  204 SER A CA  
2888 C C   . SER A 204 ? 0.1923 0.1402 0.2252 -0.0069 0.0073  0.0293  204 SER A C   
2889 O O   . SER A 204 ? 0.2069 0.1434 0.2412 -0.0048 0.0087  0.0358  204 SER A O   
2890 C CB  . SER A 204 ? 0.2166 0.1602 0.2668 -0.0199 -0.0008 0.0185  204 SER A CB  
2891 O OG  . SER A 204 ? 0.3134 0.2482 0.3643 -0.0223 -0.0088 0.0067  204 SER A OG  
2897 N N   A ARG A 205 ? 0.1940 0.1589 0.2221 -0.0046 0.0106  0.0323  205 ARG A N   
2898 N N   B ARG A 205 ? 0.1938 0.1588 0.2219 -0.0046 0.0106  0.0322  205 ARG A N   
2899 C CA  A ARG A 205 ? 0.2006 0.1724 0.2225 0.0016  0.0156  0.0430  205 ARG A CA  
2900 C CA  B ARG A 205 ? 0.1995 0.1719 0.2211 0.0017  0.0156  0.0426  205 ARG A CA  
2901 C C   A ARG A 205 ? 0.2090 0.1768 0.2210 0.0092  0.0132  0.0413  205 ARG A C   
2902 C C   B ARG A 205 ? 0.2089 0.1771 0.2207 0.0092  0.0132  0.0413  205 ARG A C   
2903 O O   A ARG A 205 ? 0.2181 0.1817 0.2281 0.0138  0.0158  0.0507  205 ARG A O   
2904 O O   B ARG A 205 ? 0.2178 0.1818 0.2278 0.0137  0.0159  0.0508  205 ARG A O   
2905 C CB  A ARG A 205 ? 0.1946 0.1840 0.2091 0.0054  0.0183  0.0439  205 ARG A CB  
2906 C CB  B ARG A 205 ? 0.1970 0.1867 0.2112 0.0052  0.0177  0.0423  205 ARG A CB  
2907 C CG  A ARG A 205 ? 0.2386 0.2352 0.2385 0.0158  0.0199  0.0495  205 ARG A CG  
2908 C CG  B ARG A 205 ? 0.2233 0.2221 0.2483 0.0007  0.0227  0.0485  205 ARG A CG  
2909 C CD  A ARG A 205 ? 0.2272 0.2387 0.2195 0.0217  0.0255  0.0555  205 ARG A CD  
2910 C CD  B ARG A 205 ? 0.3013 0.3074 0.3269 0.0048  0.0314  0.0650  205 ARG A CD  
2911 N NE  A ARG A 205 ? 0.2586 0.2770 0.2316 0.0336  0.0231  0.0548  205 ARG A NE  
2912 N NE  B ARG A 205 ? 0.2920 0.3088 0.2970 0.0172  0.0331  0.0657  205 ARG A NE  
2913 C CZ  A ARG A 205 ? 0.2328 0.2635 0.1916 0.0430  0.0256  0.0559  205 ARG A CZ  
2914 C CZ  B ARG A 205 ? 0.2947 0.3254 0.2901 0.0236  0.0350  0.0630  205 ARG A CZ  
2915 N NH1 A ARG A 205 ? 0.2841 0.3237 0.2475 0.0423  0.0326  0.0597  205 ARG A NH1 
2916 N NH1 B ARG A 205 ? 0.2832 0.3207 0.2885 0.0190  0.0362  0.0598  205 ARG A NH1 
2917 N NH2 A ARG A 205 ? 0.2224 0.2574 0.1618 0.0546  0.0205  0.0527  205 ARG A NH2 
2918 N NH2 B ARG A 205 ? 0.2602 0.2976 0.2345 0.0363  0.0346  0.0625  205 ARG A NH2 
2945 N N   . LEU A 206 ? 0.1878 0.1582 0.1955 0.0108  0.0086  0.0312  206 LEU A N   
2946 C CA  . LEU A 206 ? 0.1887 0.1595 0.1918 0.0176  0.0062  0.0308  206 LEU A CA  
2947 C C   . LEU A 206 ? 0.2261 0.1815 0.2323 0.0197  0.0072  0.0335  206 LEU A C   
2948 O O   . LEU A 206 ? 0.2181 0.1725 0.2216 0.0267  0.0076  0.0393  206 LEU A O   
2949 C CB  . LEU A 206 ? 0.2449 0.2219 0.2486 0.0173  0.0022  0.0216  206 LEU A CB  
2950 C CG  . LEU A 206 ? 0.4008 0.3901 0.4025 0.0216  -0.0024 0.0204  206 LEU A CG  
2951 C CD1 . LEU A 206 ? 0.2704 0.2640 0.2774 0.0177  -0.0051 0.0131  206 LEU A CD1 
2952 C CD2 . LEU A 206 ? 0.2453 0.2425 0.2383 0.0248  -0.0041 0.0228  206 LEU A CD2 
2965 N N   . LYS A 207 ? 0.2073 0.1496 0.2184 0.0149  0.0066  0.0287  207 LYS A N   
2966 C CA  . LYS A 207 ? 0.2327 0.1562 0.2450 0.0183  0.0062  0.0290  207 LYS A CA  
2967 C C   . LYS A 207 ? 0.2487 0.1641 0.2639 0.0197  0.0093  0.0415  207 LYS A C   
2968 O O   . LYS A 207 ? 0.2675 0.1724 0.2805 0.0271  0.0097  0.0451  207 LYS A O   
2969 C CB  . LYS A 207 ? 0.2449 0.1540 0.2608 0.0128  0.0025  0.0201  207 LYS A CB  
2970 C CG  . LYS A 207 ? 0.2814 0.1670 0.2960 0.0177  0.0001  0.0172  207 LYS A CG  
2971 C CD  . LYS A 207 ? 0.3038 0.1735 0.3207 0.0127  -0.0066 0.0062  207 LYS A CD  
2972 C CE  . LYS A 207 ? 0.3437 0.1868 0.3556 0.0201  -0.0106 0.0002  207 LYS A CE  
2973 N NZ  . LYS A 207 ? 0.4790 0.3031 0.4935 0.0149  -0.0203 -0.0118 207 LYS A NZ  
2987 N N   . GLU A 208 ? 0.2335 0.1545 0.2541 0.0138  0.0125  0.0500  208 GLU A N   
2988 C CA  . GLU A 208 ? 0.2711 0.1869 0.2952 0.0154  0.0174  0.0654  208 GLU A CA  
2989 C C   . GLU A 208 ? 0.2530 0.1835 0.2647 0.0260  0.0198  0.0729  208 GLU A C   
2990 O O   . GLU A 208 ? 0.2773 0.2006 0.2863 0.0334  0.0215  0.0819  208 GLU A O   
2991 C CB  . GLU A 208 ? 0.2910 0.2120 0.3272 0.0061  0.0214  0.0733  208 GLU A CB  
2992 C CG  . GLU A 208 ? 0.4010 0.3088 0.4527 -0.0052 0.0166  0.0661  208 GLU A CG  
2993 C CD  . GLU A 208 ? 0.5466 0.4611 0.6170 -0.0149 0.0210  0.0780  208 GLU A CD  
2994 O OE1 . GLU A 208 ? 0.5823 0.5059 0.6539 -0.0118 0.0297  0.0951  208 GLU A OE1 
2995 O OE2 . GLU A 208 ? 0.5937 0.5073 0.6774 -0.0245 0.0160  0.0709  208 GLU A OE2 
3002 N N   . SER A 209 ? 0.2326 0.1827 0.2361 0.0278  0.0188  0.0686  209 SER A N   
3003 C CA  . SER A 209 ? 0.2393 0.2029 0.2299 0.0382  0.0188  0.0746  209 SER A CA  
3004 C C   . SER A 209 ? 0.2312 0.1954 0.2184 0.0458  0.0132  0.0702  209 SER A C   
3005 O O   . SER A 209 ? 0.2493 0.2194 0.2286 0.0556  0.0124  0.0778  209 SER A O   
3006 C CB  . SER A 209 ? 0.2644 0.2458 0.2463 0.0391  0.0171  0.0691  209 SER A CB  
3007 O OG  . SER A 209 ? 0.2704 0.2548 0.2547 0.0349  0.0108  0.0546  209 SER A OG  
3013 N N   . LEU A 210 ? 0.2387 0.1828 0.1973 -0.0002 0.0345  0.0058  210 LEU A N   
3014 C CA  . LEU A 210 ? 0.2233 0.1666 0.1792 0.0020  0.0283  0.0072  210 LEU A CA  
3015 C C   . LEU A 210 ? 0.2254 0.1656 0.1868 0.0030  0.0273  0.0093  210 LEU A C   
3016 O O   . LEU A 210 ? 0.2304 0.1722 0.1938 0.0058  0.0230  0.0097  210 LEU A O   
3017 C CB  . LEU A 210 ? 0.2331 0.1815 0.1913 0.0032  0.0241  0.0033  210 LEU A CB  
3018 C CG  . LEU A 210 ? 0.2568 0.2038 0.2061 0.0025  0.0258  0.0009  210 LEU A CG  
3019 C CD1 . LEU A 210 ? 0.2810 0.2302 0.2305 0.0031  0.0215  -0.0024 210 LEU A CD1 
3020 C CD2 . LEU A 210 ? 0.2956 0.2373 0.2300 0.0007  0.0263  0.0039  210 LEU A CD2 
3032 N N   . SER A 211 ? 0.2535 0.1878 0.2157 0.0005  0.0321  0.0109  211 SER A N   
3033 C CA  . SER A 211 ? 0.2719 0.1986 0.2364 0.0008  0.0327  0.0120  211 SER A CA  
3034 C C   . SER A 211 ? 0.2739 0.1946 0.2316 0.0063  0.0309  0.0180  211 SER A C   
3035 O O   . SER A 211 ? 0.3223 0.2365 0.2814 0.0089  0.0313  0.0188  211 SER A O   
3036 C CB  . SER A 211 ? 0.3061 0.2265 0.2713 -0.0049 0.0386  0.0122  211 SER A CB  
3037 O OG  . SER A 211 ? 0.3591 0.2737 0.3155 -0.0053 0.0424  0.0172  211 SER A OG  
3043 N N   . ASN A 212 ? 0.2675 0.1907 0.2175 0.0083  0.0293  0.0225  212 ASN A N   
3044 C CA  . ASN A 212 ? 0.3179 0.2407 0.2630 0.0142  0.0266  0.0297  212 ASN A CA  
3045 C C   . ASN A 212 ? 0.2738 0.2094 0.2205 0.0161  0.0196  0.0296  212 ASN A C   
3046 O O   . ASN A 212 ? 0.2997 0.2406 0.2421 0.0197  0.0161  0.0363  212 ASN A O   
3047 C CB  . ASN A 212 ? 0.3318 0.2495 0.2660 0.0143  0.0289  0.0363  212 ASN A CB  
3048 C CG  . ASN A 212 ? 0.4071 0.3107 0.3390 0.0120  0.0363  0.0374  212 ASN A CG  
3049 O OD1 . ASN A 212 ? 0.4562 0.3499 0.3904 0.0138  0.0391  0.0379  212 ASN A OD1 
3050 N ND2 . ASN A 212 ? 0.4814 0.3829 0.4076 0.0074  0.0401  0.0376  212 ASN A ND2 
3057 N N   . ASN A 213 ? 0.2354 0.1766 0.1879 0.0135  0.0176  0.0228  213 ASN A N   
3058 C CA  . ASN A 213 ? 0.2285 0.1801 0.1820 0.0134  0.0117  0.0215  213 ASN A CA  
3059 C C   . ASN A 213 ? 0.2142 0.1679 0.1776 0.0143  0.0110  0.0165  213 ASN A C   
3060 O O   . ASN A 213 ? 0.2423 0.1896 0.2107 0.0149  0.0145  0.0144  213 ASN A O   
3061 C CB  . ASN A 213 ? 0.2304 0.1835 0.1765 0.0083  0.0112  0.0180  213 ASN A CB  
3062 C CG  . ASN A 213 ? 0.2705 0.2217 0.2043 0.0067  0.0112  0.0228  213 ASN A CG  
3063 O OD1 . ASN A 213 ? 0.2731 0.2173 0.2017 0.0050  0.0164  0.0225  213 ASN A OD1 
3064 N ND2 . ASN A 213 ? 0.2612 0.2202 0.1902 0.0069  0.0054  0.0278  213 ASN A ND2 
3071 N N   . LEU A 214 ? 0.2036 0.1657 0.1687 0.0136  0.0064  0.0147  214 LEU A N   
3072 C CA  . LEU A 214 ? 0.1859 0.1506 0.1590 0.0144  0.0054  0.0103  214 LEU A CA  
3073 C C   . LEU A 214 ? 0.1905 0.1556 0.1637 0.0106  0.0055  0.0041  214 LEU A C   
3074 O O   . LEU A 214 ? 0.2003 0.1659 0.1663 0.0076  0.0044  0.0033  214 LEU A O   
3075 C CB  . LEU A 214 ? 0.2069 0.1812 0.1826 0.0168  0.0009  0.0135  214 LEU A CB  
3076 C CG  . LEU A 214 ? 0.2259 0.2012 0.2039 0.0232  0.0017  0.0205  214 LEU A CG  
3077 C CD1 . LEU A 214 ? 0.2779 0.2673 0.2594 0.0253  -0.0029 0.0250  214 LEU A CD1 
3078 C CD2 . LEU A 214 ? 0.2660 0.2314 0.2480 0.0267  0.0065  0.0182  214 LEU A CD2 
3090 N N   . ILE A 215 ? 0.1835 0.1475 0.1636 0.0108  0.0070  -0.0001 215 ILE A N   
3091 C CA  . ILE A 215 ? 0.1896 0.1554 0.1715 0.0092  0.0071  -0.0048 215 ILE A CA  
3092 C C   . ILE A 215 ? 0.1578 0.1273 0.1456 0.0106  0.0045  -0.0068 215 ILE A C   
3093 O O   . ILE A 215 ? 0.1715 0.1399 0.1644 0.0114  0.0054  -0.0079 215 ILE A O   
3094 C CB  . ILE A 215 ? 0.2063 0.1707 0.1918 0.0080  0.0113  -0.0069 215 ILE A CB  
3095 C CG1 . ILE A 215 ? 0.2309 0.1912 0.2114 0.0066  0.0150  -0.0043 215 ILE A CG1 
3096 C CG2 . ILE A 215 ? 0.2318 0.1987 0.2176 0.0083  0.0120  -0.0100 215 ILE A CG2 
3097 C CD1 . ILE A 215 ? 0.2865 0.2482 0.2724 0.0047  0.0197  -0.0057 215 ILE A CD1 
3109 N N   . LEU A 216 ? 0.1653 0.1377 0.1507 0.0101  0.0017  -0.0076 216 LEU A N   
3110 C CA  . LEU A 216 ? 0.1615 0.1373 0.1513 0.0111  -0.0005 -0.0094 216 LEU A CA  
3111 C C   . LEU A 216 ? 0.1615 0.1360 0.1504 0.0104  0.0003  -0.0127 216 LEU A C   
3112 O O   . LEU A 216 ? 0.1933 0.1640 0.1752 0.0090  0.0015  -0.0132 216 LEU A O   
3113 C CB  . LEU A 216 ? 0.1878 0.1685 0.1751 0.0103  -0.0040 -0.0066 216 LEU A CB  
3114 C CG  . LEU A 216 ? 0.1888 0.1742 0.1798 0.0111  -0.0060 -0.0071 216 LEU A CG  
3115 C CD1 . LEU A 216 ? 0.1995 0.1854 0.1966 0.0152  -0.0046 -0.0067 216 LEU A CD1 
3116 C CD2 . LEU A 216 ? 0.2285 0.2212 0.2169 0.0084  -0.0095 -0.0037 216 LEU A CD2 
3128 N N   . ALA A 217 ? 0.1648 0.1415 0.1592 0.0118  0.0001  -0.0148 217 ALA A N   
3129 C CA  . ALA A 217 ? 0.1584 0.1348 0.1527 0.0128  0.0012  -0.0166 217 ALA A CA  
3130 C C   . ALA A 217 ? 0.1542 0.1325 0.1497 0.0137  -0.0012 -0.0175 217 ALA A C   
3131 O O   . ALA A 217 ? 0.1612 0.1426 0.1605 0.0138  -0.0030 -0.0177 217 ALA A O   
3132 C CB  . ALA A 217 ? 0.2134 0.1935 0.2141 0.0137  0.0036  -0.0172 217 ALA A CB  
3138 N N   . ASN A 218 ? 0.1643 0.1388 0.1550 0.0144  -0.0005 -0.0180 218 ASN A N   
3139 C CA  . ASN A 218 ? 0.1628 0.1380 0.1537 0.0155  -0.0021 -0.0183 218 ASN A CA  
3140 C C   . ASN A 218 ? 0.1507 0.1317 0.1486 0.0186  -0.0018 -0.0185 218 ASN A C   
3141 O O   . ASN A 218 ? 0.1594 0.1399 0.1571 0.0219  0.0005  -0.0177 218 ASN A O   
3142 C CB  . ASN A 218 ? 0.1686 0.1347 0.1497 0.0149  -0.0005 -0.0184 218 ASN A CB  
3143 C CG  . ASN A 218 ? 0.1560 0.1206 0.1354 0.0158  -0.0014 -0.0182 218 ASN A CG  
3144 O OD1 . ASN A 218 ? 0.1726 0.1443 0.1580 0.0165  -0.0039 -0.0180 218 ASN A OD1 
3145 N ND2 . ASN A 218 ? 0.1827 0.1366 0.1525 0.0157  0.0010  -0.0183 218 ASN A ND2 
3152 N N   . ILE A 219 ? 0.1532 0.1398 0.1562 0.0177  -0.0041 -0.0192 219 ILE A N   
3153 C CA  . ILE A 219 ? 0.1717 0.1658 0.1810 0.0182  -0.0049 -0.0195 219 ILE A CA  
3154 C C   . ILE A 219 ? 0.1490 0.1463 0.1584 0.0180  -0.0079 -0.0202 219 ILE A C   
3155 O O   . ILE A 219 ? 0.1821 0.1858 0.1942 0.0196  -0.0092 -0.0192 219 ILE A O   
3156 C CB  . ILE A 219 ? 0.2210 0.2171 0.2343 0.0150  -0.0043 -0.0203 219 ILE A CB  
3157 C CG1 . ILE A 219 ? 0.2935 0.2887 0.3073 0.0156  -0.0009 -0.0190 219 ILE A CG1 
3158 C CG2 . ILE A 219 ? 0.2561 0.2601 0.2743 0.0123  -0.0064 -0.0213 219 ILE A CG2 
3159 C CD1 . ILE A 219 ? 0.2556 0.2588 0.2751 0.0178  0.0007  -0.0175 219 ILE A CD1 
3171 N N   . ILE A 220 ? 0.1376 0.1315 0.1442 0.0164  -0.0087 -0.0215 220 ILE A N   
3172 C CA  . ILE A 220 ? 0.1477 0.1434 0.1527 0.0158  -0.0107 -0.0227 220 ILE A CA  
3173 C C   . ILE A 220 ? 0.1601 0.1554 0.1618 0.0183  -0.0114 -0.0211 220 ILE A C   
3174 O O   . ILE A 220 ? 0.1587 0.1497 0.1571 0.0185  -0.0104 -0.0202 220 ILE A O   
3175 C CB  . ILE A 220 ? 0.1659 0.1569 0.1682 0.0145  -0.0097 -0.0243 220 ILE A CB  
3176 C CG1 . ILE A 220 ? 0.1983 0.1864 0.2016 0.0119  -0.0084 -0.0258 220 ILE A CG1 
3177 C CG2 . ILE A 220 ? 0.1907 0.1818 0.1887 0.0140  -0.0110 -0.0259 220 ILE A CG2 
3178 C CD1 . ILE A 220 ? 0.1945 0.1749 0.1939 0.0126  -0.0057 -0.0266 220 ILE A CD1 
3190 N N   . ARG A 221 ? 0.1551 0.1554 0.1572 0.0195  -0.0133 -0.0202 221 ARG A N   
3191 C CA  . ARG A 221 ? 0.1480 0.1468 0.1458 0.0223  -0.0137 -0.0181 221 ARG A CA  
3192 C C   . ARG A 221 ? 0.1583 0.1651 0.1568 0.0226  -0.0169 -0.0173 221 ARG A C   
3193 O O   . ARG A 221 ? 0.1682 0.1839 0.1724 0.0226  -0.0184 -0.0164 221 ARG A O   
3194 C CB  . ARG A 221 ? 0.1853 0.1795 0.1818 0.0259  -0.0112 -0.0155 221 ARG A CB  
3195 C CG  . ARG A 221 ? 0.1730 0.1619 0.1631 0.0289  -0.0105 -0.0128 221 ARG A CG  
3196 C CD  . ARG A 221 ? 0.1852 0.1670 0.1691 0.0255  -0.0099 -0.0137 221 ARG A CD  
3197 N NE  . ARG A 221 ? 0.2041 0.1792 0.1805 0.0270  -0.0088 -0.0112 221 ARG A NE  
3198 C CZ  . ARG A 221 ? 0.1899 0.1533 0.1589 0.0267  -0.0058 -0.0099 221 ARG A CZ  
3199 N NH1 . ARG A 221 ? 0.2034 0.1606 0.1706 0.0251  -0.0036 -0.0112 221 ARG A NH1 
3200 N NH2 . ARG A 221 ? 0.2185 0.1745 0.1797 0.0274  -0.0045 -0.0075 221 ARG A NH2 
3214 N N   . VAL A 222 ? 0.1563 0.1617 0.1491 0.0224  -0.0180 -0.0173 222 VAL A N   
3215 C CA  . VAL A 222 ? 0.1676 0.1810 0.1589 0.0221  -0.0218 -0.0163 222 VAL A CA  
3216 C C   . VAL A 222 ? 0.1765 0.1961 0.1710 0.0276  -0.0225 -0.0110 222 VAL A C   
3217 O O   . VAL A 222 ? 0.1890 0.2015 0.1798 0.0321  -0.0199 -0.0081 222 VAL A O   
3218 C CB  . VAL A 222 ? 0.1689 0.1779 0.1515 0.0211  -0.0220 -0.0171 222 VAL A CB  
3219 C CG1 . VAL A 222 ? 0.1922 0.2094 0.1714 0.0207  -0.0263 -0.0155 222 VAL A CG1 
3220 C CG2 . VAL A 222 ? 0.2001 0.2036 0.1798 0.0172  -0.0202 -0.0218 222 VAL A CG2 
3230 N N   . ARG A 223 ? 0.1684 0.2017 0.1695 0.0272  -0.0256 -0.0093 223 ARG A N   
3231 C CA  . ARG A 223 ? 0.1942 0.2372 0.2013 0.0341  -0.0256 -0.0030 223 ARG A CA  
3232 C C   . ARG A 223 ? 0.1700 0.2316 0.1812 0.0314  -0.0317 -0.0006 223 ARG A C   
3233 O O   . ARG A 223 ? 0.1780 0.2458 0.1917 0.0235  -0.0344 -0.0045 223 ARG A O   
3234 C CB  . ARG A 223 ? 0.1949 0.2396 0.2102 0.0366  -0.0219 -0.0022 223 ARG A CB  
3235 C CG  . ARG A 223 ? 0.2865 0.3145 0.2975 0.0377  -0.0165 -0.0046 223 ARG A CG  
3236 C CD  . ARG A 223 ? 0.2855 0.3026 0.2904 0.0452  -0.0121 -0.0008 223 ARG A CD  
3237 N NE  . ARG A 223 ? 0.2262 0.2523 0.2349 0.0536  -0.0115 0.0059  223 ARG A NE  
3238 C CZ  . ARG A 223 ? 0.2010 0.2155 0.2028 0.0613  -0.0068 0.0099  223 ARG A CZ  
3239 N NH1 . ARG A 223 ? 0.2547 0.2486 0.2452 0.0596  -0.0029 0.0071  223 ARG A NH1 
3240 N NH2 . ARG A 223 ? 0.2232 0.2468 0.2290 0.0705  -0.0059 0.0171  223 ARG A NH2 
3254 N N   . PRO A 224 ? 0.1875 0.2591 0.1998 0.0377  -0.0337 0.0062  224 PRO A N   
3255 C CA  . PRO A 224 ? 0.1711 0.2654 0.1893 0.0346  -0.0404 0.0097  224 PRO A CA  
3256 C C   . PRO A 224 ? 0.1768 0.2876 0.2089 0.0336  -0.0406 0.0117  224 PRO A C   
3257 O O   . PRO A 224 ? 0.1992 0.3277 0.2360 0.0256  -0.0464 0.0117  224 PRO A O   
3258 C CB  . PRO A 224 ? 0.2288 0.3291 0.2449 0.0438  -0.0416 0.0180  224 PRO A CB  
3259 C CG  . PRO A 224 ? 0.2653 0.3474 0.2780 0.0532  -0.0340 0.0199  224 PRO A CG  
3260 C CD  . PRO A 224 ? 0.2305 0.2930 0.2377 0.0473  -0.0301 0.0114  224 PRO A CD  
3268 N N   . GLU A 225 ? 0.1680 0.2730 0.2057 0.0402  -0.0341 0.0130  225 GLU A N   
3269 C CA  . GLU A 225 ? 0.1780 0.2992 0.2292 0.0399  -0.0331 0.0155  225 GLU A CA  
3270 C C   . GLU A 225 ? 0.2091 0.3274 0.2611 0.0283  -0.0338 0.0083  225 GLU A C   
3271 O O   . GLU A 225 ? 0.2642 0.3983 0.3272 0.0250  -0.0341 0.0101  225 GLU A O   
3272 C CB  . GLU A 225 ? 0.2151 0.3283 0.2694 0.0510  -0.0247 0.0190  225 GLU A CB  
3273 C CG  . GLU A 225 ? 0.2066 0.3176 0.2583 0.0640  -0.0217 0.0265  225 GLU A CG  
3274 C CD  . GLU A 225 ? 0.2120 0.2962 0.2484 0.0661  -0.0185 0.0233  225 GLU A CD  
3275 O OE1 . GLU A 225 ? 0.2289 0.3007 0.2575 0.0574  -0.0203 0.0160  225 GLU A OE1 
3276 O OE2 . GLU A 225 ? 0.2789 0.3541 0.3108 0.0768  -0.0133 0.0286  225 GLU A OE2 
3283 N N   . PHE A 226 ? 0.1769 0.2756 0.2180 0.0226  -0.0332 0.0009  226 PHE A N   
3284 C CA  . PHE A 226 ? 0.1730 0.2646 0.2129 0.0133  -0.0324 -0.0056 226 PHE A CA  
3285 C C   . PHE A 226 ? 0.1954 0.2865 0.2271 0.0030  -0.0378 -0.0102 226 PHE A C   
3286 O O   . PHE A 226 ? 0.1845 0.2620 0.2052 0.0030  -0.0378 -0.0135 226 PHE A O   
3287 C CB  . PHE A 226 ? 0.1896 0.2588 0.2224 0.0151  -0.0271 -0.0100 226 PHE A CB  
3288 C CG  . PHE A 226 ? 0.1850 0.2487 0.2211 0.0230  -0.0212 -0.0074 226 PHE A CG  
3289 C CD1 . PHE A 226 ? 0.2498 0.3261 0.2953 0.0288  -0.0191 -0.0020 226 PHE A CD1 
3290 C CD2 . PHE A 226 ? 0.2094 0.2551 0.2380 0.0242  -0.0177 -0.0105 226 PHE A CD2 
3291 C CE1 . PHE A 226 ? 0.2272 0.2936 0.2717 0.0359  -0.0125 -0.0006 226 PHE A CE1 
3292 C CE2 . PHE A 226 ? 0.2525 0.2902 0.2804 0.0296  -0.0125 -0.0091 226 PHE A CE2 
3293 C CZ  . PHE A 226 ? 0.2562 0.3025 0.2909 0.0354  -0.0096 -0.0046 226 PHE A CZ  
3303 N N   . GLU A 227 ? 0.2195 0.3244 0.2556 -0.0065 -0.0417 -0.0107 227 GLU A N   
3304 C CA  . GLU A 227 ? 0.2325 0.3350 0.2579 -0.0178 -0.0465 -0.0157 227 GLU A CA  
3305 C C   . GLU A 227 ? 0.2373 0.3135 0.2495 -0.0206 -0.0423 -0.0233 227 GLU A C   
3306 O O   . GLU A 227 ? 0.2411 0.3079 0.2405 -0.0241 -0.0438 -0.0272 227 GLU A O   
3307 C CB  . GLU A 227 ? 0.3222 0.4408 0.3536 -0.0297 -0.0503 -0.0158 227 GLU A CB  
3308 C CG  . GLU A 227 ? 0.4363 0.5583 0.4567 -0.0422 -0.0570 -0.0193 227 GLU A CG  
3309 C CD  . GLU A 227 ? 0.5010 0.6460 0.5250 -0.0397 -0.0641 -0.0125 227 GLU A CD  
3310 O OE1 . GLU A 227 ? 0.5486 0.7212 0.5866 -0.0415 -0.0683 -0.0059 227 GLU A OE1 
3311 O OE2 . GLU A 227 ? 0.5174 0.6540 0.5305 -0.0358 -0.0653 -0.0132 227 GLU A OE2 
3318 N N   . GLU A 228 ? 0.1857 0.2503 0.2005 -0.0183 -0.0366 -0.0250 228 GLU A N   
3319 C CA  . GLU A 228 ? 0.2105 0.2524 0.2146 -0.0192 -0.0321 -0.0306 228 GLU A CA  
3320 C C   . GLU A 228 ? 0.1917 0.2238 0.1966 -0.0089 -0.0276 -0.0291 228 GLU A C   
3321 O O   . GLU A 228 ? 0.2050 0.2224 0.2055 -0.0081 -0.0232 -0.0318 228 GLU A O   
3322 C CB  . GLU A 228 ? 0.2337 0.2683 0.2373 -0.0267 -0.0294 -0.0339 228 GLU A CB  
3323 C CG  . GLU A 228 ? 0.2982 0.3408 0.2994 -0.0398 -0.0337 -0.0360 228 GLU A CG  
3324 C CD  . GLU A 228 ? 0.4739 0.5084 0.4751 -0.0471 -0.0302 -0.0383 228 GLU A CD  
3325 O OE1 . GLU A 228 ? 0.5521 0.6031 0.5628 -0.0536 -0.0325 -0.0358 228 GLU A OE1 
3326 O OE2 . GLU A 228 ? 0.5591 0.5713 0.5508 -0.0463 -0.0248 -0.0421 228 GLU A OE2 
3333 N N   . ASN A 229 ? 0.1774 0.2171 0.1870 -0.0014 -0.0283 -0.0245 229 ASN A N   
3334 C CA  . ASN A 229 ? 0.1632 0.1932 0.1712 0.0063  -0.0247 -0.0233 229 ASN A CA  
3335 C C   . ASN A 229 ? 0.1549 0.1773 0.1660 0.0079  -0.0203 -0.0237 229 ASN A C   
3336 O O   . ASN A 229 ? 0.1658 0.1784 0.1732 0.0108  -0.0176 -0.0242 229 ASN A O   
3337 C CB  . ASN A 229 ? 0.1726 0.1926 0.1704 0.0063  -0.0243 -0.0257 229 ASN A CB  
3338 C CG  . ASN A 229 ? 0.1693 0.1967 0.1632 0.0062  -0.0284 -0.0241 229 ASN A CG  
3339 O OD1 . ASN A 229 ? 0.1794 0.2175 0.1785 0.0102  -0.0306 -0.0192 229 ASN A OD1 
3340 N ND2 . ASN A 229 ? 0.1933 0.2150 0.1772 0.0021  -0.0292 -0.0276 229 ASN A ND2 
3347 N N   . GLY A 230 ? 0.1628 0.1918 0.1809 0.0057  -0.0198 -0.0229 230 GLY A N   
3348 C CA  . GLY A 230 ? 0.1530 0.1766 0.1738 0.0072  -0.0157 -0.0226 230 GLY A CA  
3349 C C   . GLY A 230 ? 0.1889 0.2062 0.2080 0.0011  -0.0143 -0.0256 230 GLY A C   
3350 O O   . GLY A 230 ? 0.1799 0.1956 0.2021 0.0010  -0.0114 -0.0247 230 GLY A O   
3354 N N   . LEU A 231 ? 0.1806 0.1923 0.1932 -0.0040 -0.0155 -0.0290 231 LEU A N   
3355 C CA  . LEU A 231 ? 0.1985 0.1999 0.2068 -0.0096 -0.0130 -0.0319 231 LEU A CA  
3356 C C   . LEU A 231 ? 0.1951 0.2050 0.2099 -0.0156 -0.0132 -0.0310 231 LEU A C   
3357 O O   . LEU A 231 ? 0.2095 0.2106 0.2224 -0.0188 -0.0098 -0.0318 231 LEU A O   
3358 C CB  . LEU A 231 ? 0.2267 0.2192 0.2244 -0.0149 -0.0138 -0.0362 231 LEU A CB  
3359 C CG  . LEU A 231 ? 0.3093 0.2924 0.2992 -0.0098 -0.0123 -0.0374 231 LEU A CG  
3360 C CD1 . LEU A 231 ? 0.3246 0.2954 0.3018 -0.0150 -0.0112 -0.0421 231 LEU A CD1 
3361 C CD2 . LEU A 231 ? 0.3023 0.2777 0.2933 -0.0032 -0.0080 -0.0354 231 LEU A CD2 
3373 N N   . GLU A 232 ? 0.1744 0.2020 0.1969 -0.0174 -0.0169 -0.0287 232 GLU A N   
3374 C CA  . GLU A 232 ? 0.1871 0.2272 0.2177 -0.0237 -0.0172 -0.0270 232 GLU A CA  
3375 C C   . GLU A 232 ? 0.1824 0.2234 0.2197 -0.0188 -0.0126 -0.0239 232 GLU A C   
3376 O O   . GLU A 232 ? 0.2089 0.2582 0.2525 -0.0241 -0.0113 -0.0224 232 GLU A O   
3377 C CB  . GLU A 232 ? 0.2126 0.2757 0.2518 -0.0251 -0.0224 -0.0236 232 GLU A CB  
3378 C CG  . GLU A 232 ? 0.2031 0.2752 0.2483 -0.0135 -0.0225 -0.0188 232 GLU A CG  
3379 C CD  . GLU A 232 ? 0.1992 0.2670 0.2366 -0.0107 -0.0259 -0.0199 232 GLU A CD  
3380 O OE1 . GLU A 232 ? 0.1916 0.2420 0.2200 -0.0079 -0.0237 -0.0230 232 GLU A OE1 
3381 O OE2 . GLU A 232 ? 0.2410 0.3243 0.2814 -0.0115 -0.0308 -0.0171 232 GLU A OE2 
3388 N N   . TYR A 233 ? 0.1772 0.2099 0.2124 -0.0100 -0.0099 -0.0229 233 TYR A N   
3389 C CA  . TYR A 233 ? 0.1732 0.2043 0.2115 -0.0057 -0.0053 -0.0204 233 TYR A CA  
3390 C C   . TYR A 233 ? 0.1901 0.2043 0.2207 -0.0059 -0.0021 -0.0220 233 TYR A C   
3391 O O   . TYR A 233 ? 0.2106 0.2221 0.2415 -0.0032 0.0015  -0.0202 233 TYR A O   
3392 C CB  . TYR A 233 ? 0.1945 0.2284 0.2342 0.0035  -0.0044 -0.0177 233 TYR A CB  
3393 C CG  . TYR A 233 ? 0.1684 0.2183 0.2152 0.0061  -0.0070 -0.0148 233 TYR A CG  
3394 C CD1 . TYR A 233 ? 0.1653 0.2329 0.2228 0.0046  -0.0066 -0.0113 233 TYR A CD1 
3395 C CD2 . TYR A 233 ? 0.1760 0.2247 0.2192 0.0103  -0.0097 -0.0145 233 TYR A CD2 
3396 C CE1 . TYR A 233 ? 0.1750 0.2603 0.2402 0.0081  -0.0092 -0.0071 233 TYR A CE1 
3397 C CE2 . TYR A 233 ? 0.1825 0.2459 0.2316 0.0136  -0.0121 -0.0108 233 TYR A CE2 
3398 C CZ  . TYR A 233 ? 0.1774 0.2595 0.2377 0.0130  -0.0120 -0.0068 233 TYR A CZ  
3399 O OH  . TYR A 233 ? 0.2286 0.3280 0.2959 0.0175  -0.0146 -0.0016 233 TYR A OH  
3409 N N   . LEU A 234 ? 0.1841 0.1867 0.2072 -0.0085 -0.0028 -0.0250 234 LEU A N   
3410 C CA  . LEU A 234 ? 0.2227 0.2109 0.2392 -0.0059 0.0002  -0.0249 234 LEU A CA  
3411 C C   . LEU A 234 ? 0.2303 0.2121 0.2455 -0.0102 0.0039  -0.0242 234 LEU A C   
3412 O O   . LEU A 234 ? 0.2283 0.2001 0.2388 -0.0070 0.0066  -0.0226 234 LEU A O   
3413 C CB  . LEU A 234 ? 0.2631 0.2411 0.2722 -0.0052 -0.0003 -0.0272 234 LEU A CB  
3414 C CG  . LEU A 234 ? 0.2715 0.2525 0.2804 0.0007  -0.0024 -0.0266 234 LEU A CG  
3415 C CD1 . LEU A 234 ? 0.3134 0.2854 0.3154 0.0015  -0.0018 -0.0286 234 LEU A CD1 
3416 C CD2 . LEU A 234 ? 0.3605 0.3415 0.3701 0.0058  -0.0013 -0.0236 234 LEU A CD2 
3428 N N   . GLY A 235 ? 0.2270 0.2151 0.2461 -0.0175 0.0040  -0.0246 235 GLY A N   
3429 C CA  . GLY A 235 ? 0.2442 0.2251 0.2613 -0.0223 0.0081  -0.0237 235 GLY A CA  
3430 C C   . GLY A 235 ? 0.2276 0.2097 0.2467 -0.0174 0.0113  -0.0200 235 GLY A C   
3431 O O   . GLY A 235 ? 0.2532 0.2257 0.2680 -0.0193 0.0151  -0.0186 235 GLY A O   
3435 N N   . TYR A 236 ? 0.2000 0.1920 0.2238 -0.0114 0.0104  -0.0185 236 TYR A N   
3436 C CA  . TYR A 236 ? 0.2022 0.1936 0.2251 -0.0073 0.0138  -0.0158 236 TYR A CA  
3437 C C   . TYR A 236 ? 0.2051 0.1845 0.2192 -0.0029 0.0139  -0.0149 236 TYR A C   
3438 O O   . TYR A 236 ? 0.2037 0.1800 0.2140 -0.0012 0.0166  -0.0127 236 TYR A O   
3439 C CB  . TYR A 236 ? 0.2102 0.2128 0.2384 -0.0023 0.0139  -0.0147 236 TYR A CB  
3440 C CG  . TYR A 236 ? 0.2050 0.2236 0.2439 -0.0052 0.0148  -0.0133 236 TYR A CG  
3441 C CD1 . TYR A 236 ? 0.1870 0.2107 0.2296 -0.0069 0.0197  -0.0107 236 TYR A CD1 
3442 C CD2 . TYR A 236 ? 0.2475 0.2778 0.2930 -0.0064 0.0107  -0.0138 236 TYR A CD2 
3443 C CE1 . TYR A 236 ? 0.1933 0.2352 0.2476 -0.0097 0.0207  -0.0084 236 TYR A CE1 
3444 C CE2 . TYR A 236 ? 0.2587 0.3076 0.3153 -0.0093 0.0108  -0.0113 236 TYR A CE2 
3445 C CZ  . TYR A 236 ? 0.2154 0.2708 0.2772 -0.0108 0.0159  -0.0084 236 TYR A CZ  
3446 O OH  . TYR A 236 ? 0.2435 0.3210 0.3184 -0.0137 0.0162  -0.0049 236 TYR A OH  
3456 N N   . PHE A 237 ? 0.1734 0.1476 0.1842 -0.0010 0.0111  -0.0162 237 PHE A N   
3457 C CA  . PHE A 237 ? 0.1623 0.1318 0.1677 0.0038  0.0100  -0.0146 237 PHE A CA  
3458 C C   . PHE A 237 ? 0.1867 0.1470 0.1878 0.0050  0.0104  -0.0136 237 PHE A C   
3459 O O   . PHE A 237 ? 0.2134 0.1685 0.2139 0.0024  0.0113  -0.0156 237 PHE A O   
3460 C CB  . PHE A 237 ? 0.1653 0.1404 0.1721 0.0067  0.0067  -0.0159 237 PHE A CB  
3461 C CG  . PHE A 237 ? 0.1682 0.1507 0.1787 0.0072  0.0073  -0.0165 237 PHE A CG  
3462 C CD1 . PHE A 237 ? 0.2023 0.1839 0.2098 0.0084  0.0101  -0.0150 237 PHE A CD1 
3463 C CD2 . PHE A 237 ? 0.1756 0.1656 0.1916 0.0072  0.0054  -0.0179 237 PHE A CD2 
3464 C CE1 . PHE A 237 ? 0.2076 0.1943 0.2177 0.0106  0.0123  -0.0150 237 PHE A CE1 
3465 C CE2 . PHE A 237 ? 0.1966 0.1939 0.2165 0.0097  0.0068  -0.0170 237 PHE A CE2 
3466 C CZ  . PHE A 237 ? 0.1816 0.1765 0.1984 0.0118  0.0107  -0.0156 237 PHE A CZ  
3476 N N   . ASN A 238 ? 0.1684 0.1268 0.1657 0.0091  0.0100  -0.0102 238 ASN A N   
3477 C CA  . ASN A 238 ? 0.1789 0.1308 0.1732 0.0128  0.0108  -0.0079 238 ASN A CA  
3478 C C   . ASN A 238 ? 0.1735 0.1290 0.1697 0.0154  0.0086  -0.0095 238 ASN A C   
3479 O O   . ASN A 238 ? 0.1938 0.1434 0.1880 0.0190  0.0105  -0.0083 238 ASN A O   
3480 C CB  . ASN A 238 ? 0.1900 0.1423 0.1808 0.0165  0.0108  -0.0021 238 ASN A CB  
3481 C CG  . ASN A 238 ? 0.2163 0.1632 0.2034 0.0144  0.0138  0.0001  238 ASN A CG  
3482 O OD1 . ASN A 238 ? 0.1975 0.1487 0.1827 0.0129  0.0129  0.0011  238 ASN A OD1 
3483 N ND2 . ASN A 238 ? 0.2377 0.1734 0.2222 0.0138  0.0179  0.0007  238 ASN A ND2 
3490 N N   . GLY A 239 ? 0.1717 0.1355 0.1710 0.0143  0.0054  -0.0118 239 GLY A N   
3491 C CA  . GLY A 239 ? 0.1827 0.1496 0.1832 0.0161  0.0035  -0.0132 239 GLY A CA  
3492 C C   . GLY A 239 ? 0.1638 0.1379 0.1663 0.0148  0.0006  -0.0150 239 GLY A C   
3493 O O   . GLY A 239 ? 0.1716 0.1476 0.1741 0.0131  0.0005  -0.0153 239 GLY A O   
3497 N N   . SER A 240 ? 0.1593 0.1362 0.1622 0.0161  -0.0010 -0.0158 240 SER A N   
3498 C CA  . SER A 240 ? 0.1545 0.1359 0.1578 0.0153  -0.0033 -0.0171 240 SER A CA  
3499 C C   . SER A 240 ? 0.1449 0.1301 0.1470 0.0161  -0.0048 -0.0148 240 SER A C   
3500 O O   . SER A 240 ? 0.1504 0.1374 0.1534 0.0183  -0.0043 -0.0130 240 SER A O   
3501 C CB  . SER A 240 ? 0.1851 0.1674 0.1895 0.0148  -0.0041 -0.0200 240 SER A CB  
3502 O OG  . SER A 240 ? 0.1874 0.1731 0.1917 0.0150  -0.0057 -0.0203 240 SER A OG  
3508 N N   . TYR A 241 ? 0.1456 0.1315 0.1448 0.0142  -0.0061 -0.0147 241 TYR A N   
3509 C CA  . TYR A 241 ? 0.1413 0.1300 0.1381 0.0126  -0.0078 -0.0135 241 TYR A CA  
3510 C C   . TYR A 241 ? 0.1618 0.1494 0.1587 0.0134  -0.0079 -0.0157 241 TYR A C   
3511 O O   . TYR A 241 ? 0.1516 0.1371 0.1495 0.0146  -0.0073 -0.0177 241 TYR A O   
3512 C CB  . TYR A 241 ? 0.1572 0.1426 0.1475 0.0089  -0.0083 -0.0132 241 TYR A CB  
3513 C CG  . TYR A 241 ? 0.1486 0.1317 0.1329 0.0053  -0.0093 -0.0135 241 TYR A CG  
3514 C CD1 . TYR A 241 ? 0.1458 0.1223 0.1271 0.0065  -0.0079 -0.0157 241 TYR A CD1 
3515 C CD2 . TYR A 241 ? 0.1702 0.1563 0.1499 -0.0002 -0.0116 -0.0113 241 TYR A CD2 
3516 C CE1 . TYR A 241 ? 0.1595 0.1301 0.1329 0.0030  -0.0078 -0.0158 241 TYR A CE1 
3517 C CE2 . TYR A 241 ? 0.1590 0.1403 0.1308 -0.0055 -0.0121 -0.0119 241 TYR A CE2 
3518 C CZ  . TYR A 241 ? 0.1718 0.1434 0.1396 -0.0038 -0.0098 -0.0144 241 TYR A CZ  
3519 O OH  . TYR A 241 ? 0.1910 0.1541 0.1487 -0.0092 -0.0093 -0.0151 241 TYR A OH  
3529 N N   . LEU A 242 ? 0.1419 0.1324 0.1381 0.0127  -0.0088 -0.0146 242 LEU A N   
3530 C CA  . LEU A 242 ? 0.1429 0.1322 0.1377 0.0134  -0.0089 -0.0159 242 LEU A CA  
3531 C C   . LEU A 242 ? 0.1488 0.1365 0.1384 0.0098  -0.0095 -0.0146 242 LEU A C   
3532 O O   . LEU A 242 ? 0.1539 0.1468 0.1437 0.0067  -0.0103 -0.0122 242 LEU A O   
3533 C CB  . LEU A 242 ? 0.1579 0.1504 0.1552 0.0156  -0.0083 -0.0161 242 LEU A CB  
3534 C CG  . LEU A 242 ? 0.1558 0.1464 0.1551 0.0176  -0.0073 -0.0183 242 LEU A CG  
3535 C CD1 . LEU A 242 ? 0.2147 0.2057 0.2162 0.0190  -0.0056 -0.0166 242 LEU A CD1 
3536 C CD2 . LEU A 242 ? 0.2027 0.1924 0.1999 0.0185  -0.0069 -0.0203 242 LEU A CD2 
3548 N N   . GLU A 243 ? 0.1433 0.1245 0.1281 0.0103  -0.0089 -0.0155 243 GLU A N   
3549 C CA  . GLU A 243 ? 0.1533 0.1296 0.1311 0.0069  -0.0086 -0.0145 243 GLU A CA  
3550 C C   . GLU A 243 ? 0.1520 0.1253 0.1282 0.0104  -0.0079 -0.0145 243 GLU A C   
3551 O O   . GLU A 243 ? 0.1608 0.1364 0.1408 0.0149  -0.0082 -0.0153 243 GLU A O   
3552 C CB  . GLU A 243 ? 0.1609 0.1269 0.1298 0.0031  -0.0074 -0.0150 243 GLU A CB  
3553 C CG  . GLU A 243 ? 0.1779 0.1349 0.1436 0.0080  -0.0048 -0.0162 243 GLU A CG  
3554 C CD  . GLU A 243 ? 0.2187 0.1628 0.1736 0.0054  -0.0021 -0.0171 243 GLU A CD  
3555 O OE1 . GLU A 243 ? 0.2269 0.1692 0.1759 -0.0018 -0.0032 -0.0174 243 GLU A OE1 
3556 O OE2 . GLU A 243 ? 0.2316 0.1672 0.1829 0.0106  0.0016  -0.0174 243 GLU A OE2 
3563 N N   . GLY A 244 ? 0.1589 0.1277 0.1289 0.0077  -0.0072 -0.0131 244 GLY A N   
3564 C CA  . GLY A 244 ? 0.1617 0.1275 0.1288 0.0111  -0.0066 -0.0122 244 GLY A CA  
3565 C C   . GLY A 244 ? 0.1673 0.1425 0.1398 0.0135  -0.0079 -0.0125 244 GLY A C   
3566 O O   . GLY A 244 ? 0.1740 0.1487 0.1447 0.0169  -0.0083 -0.0119 244 GLY A O   
3570 N N   . PHE A 245 ? 0.1588 0.1417 0.1367 0.0121  -0.0082 -0.0130 245 PHE A N   
3571 C CA  . PHE A 245 ? 0.1509 0.1393 0.1318 0.0148  -0.0082 -0.0141 245 PHE A CA  
3572 C C   . PHE A 245 ? 0.1597 0.1478 0.1357 0.0150  -0.0073 -0.0129 245 PHE A C   
3573 O O   . PHE A 245 ? 0.1683 0.1572 0.1424 0.0173  -0.0077 -0.0142 245 PHE A O   
3574 C CB  . PHE A 245 ? 0.1585 0.1532 0.1450 0.0146  -0.0070 -0.0138 245 PHE A CB  
3575 C CG  . PHE A 245 ? 0.1460 0.1415 0.1339 0.0178  -0.0059 -0.0160 245 PHE A CG  
3576 C CD1 . PHE A 245 ? 0.1434 0.1360 0.1319 0.0187  -0.0071 -0.0187 245 PHE A CD1 
3577 C CD2 . PHE A 245 ? 0.1723 0.1708 0.1600 0.0196  -0.0029 -0.0152 245 PHE A CD2 
3578 C CE1 . PHE A 245 ? 0.1571 0.1474 0.1443 0.0200  -0.0056 -0.0212 245 PHE A CE1 
3579 C CE2 . PHE A 245 ? 0.1713 0.1664 0.1571 0.0225  -0.0006 -0.0177 245 PHE A CE2 
3580 C CZ  . PHE A 245 ? 0.1822 0.1720 0.1668 0.0220  -0.0021 -0.0211 245 PHE A CZ  
3590 N N   . ASP A 246 ? 0.1630 0.1498 0.1359 0.0115  -0.0061 -0.0104 246 ASP A N   
3591 C CA  . ASP A 246 ? 0.1708 0.1566 0.1382 0.0109  -0.0046 -0.0086 246 ASP A CA  
3592 C C   . ASP A 246 ? 0.1759 0.1514 0.1350 0.0107  -0.0047 -0.0069 246 ASP A C   
3593 O O   . ASP A 246 ? 0.2045 0.1767 0.1576 0.0085  -0.0029 -0.0044 246 ASP A O   
3594 C CB  . ASP A 246 ? 0.1843 0.1769 0.1540 0.0065  -0.0024 -0.0060 246 ASP A CB  
3595 C CG  . ASP A 246 ? 0.1745 0.1639 0.1420 -0.0002 -0.0029 -0.0043 246 ASP A CG  
3596 O OD1 . ASP A 246 ? 0.1941 0.1871 0.1603 -0.0061 -0.0015 -0.0014 246 ASP A OD1 
3597 O OD2 . ASP A 246 ? 0.1815 0.1649 0.1480 -0.0005 -0.0045 -0.0059 246 ASP A OD2 
3602 N N   . SER A 247 ? 0.1855 0.1555 0.1440 0.0135  -0.0059 -0.0076 247 SER A N   
3603 C CA  . SER A 247 ? 0.1900 0.1482 0.1402 0.0151  -0.0046 -0.0052 247 SER A CA  
3604 C C   . SER A 247 ? 0.2168 0.1768 0.1676 0.0222  -0.0063 -0.0042 247 SER A C   
3605 O O   . SER A 247 ? 0.2042 0.1656 0.1592 0.0257  -0.0071 -0.0047 247 SER A O   
3606 C CB  . SER A 247 ? 0.2176 0.1669 0.1651 0.0124  -0.0031 -0.0059 247 SER A CB  
3607 O OG  . SER A 247 ? 0.2548 0.1888 0.1915 0.0138  -0.0002 -0.0035 247 SER A OG  
3613 N N   . GLU A 248 ? 0.2084 0.1698 0.1548 0.0240  -0.0069 -0.0021 248 GLU A N   
3614 C CA  . GLU A 248 ? 0.1988 0.1667 0.1462 0.0293  -0.0099 -0.0006 248 GLU A CA  
3615 C C   . GLU A 248 ? 0.2001 0.1618 0.1441 0.0357  -0.0088 0.0040  248 GLU A C   
3616 O O   . GLU A 248 ? 0.2321 0.1798 0.1689 0.0360  -0.0049 0.0061  248 GLU A O   
3617 C CB  . GLU A 248 ? 0.2212 0.1924 0.1628 0.0286  -0.0108 0.0004  248 GLU A CB  
3618 C CG  . GLU A 248 ? 0.2178 0.1792 0.1489 0.0292  -0.0081 0.0050  248 GLU A CG  
3619 C CD  . GLU A 248 ? 0.2510 0.2061 0.1790 0.0229  -0.0042 0.0045  248 GLU A CD  
3620 O OE1 . GLU A 248 ? 0.2537 0.2128 0.1882 0.0187  -0.0037 0.0012  248 GLU A OE1 
3621 O OE2 . GLU A 248 ? 0.3445 0.2915 0.2633 0.0219  -0.0017 0.0081  248 GLU A OE2 
3628 N N   . ALA A 249 ? 0.2118 0.1840 0.1605 0.0407  -0.0122 0.0059  249 ALA A N   
3629 C CA  . ALA A 249 ? 0.2125 0.1835 0.1600 0.0491  -0.0113 0.0119  249 ALA A CA  
3630 C C   . ALA A 249 ? 0.2128 0.2011 0.1645 0.0518  -0.0170 0.0147  249 ALA A C   
3631 O O   . ALA A 249 ? 0.2180 0.2145 0.1699 0.0463  -0.0209 0.0111  249 ALA A O   
3632 C CB  . ALA A 249 ? 0.2484 0.2161 0.2013 0.0521  -0.0083 0.0114  249 ALA A CB  
3638 N N   . PHE A 250 ? 0.2294 0.2233 0.1834 0.0603  -0.0174 0.0213  250 PHE A N   
3639 C CA  . PHE A 250 ? 0.2225 0.2372 0.1823 0.0625  -0.0237 0.0250  250 PHE A CA  
3640 C C   . PHE A 250 ? 0.2379 0.2552 0.1885 0.0604  -0.0274 0.0268  250 PHE A C   
3641 O O   . PHE A 250 ? 0.2664 0.3007 0.2193 0.0578  -0.0340 0.0274  250 PHE A O   
3642 C CB  . PHE A 250 ? 0.2256 0.2552 0.1964 0.0561  -0.0279 0.0196  250 PHE A CB  
3643 C CG  . PHE A 250 ? 0.2065 0.2300 0.1839 0.0557  -0.0236 0.0159  250 PHE A CG  
3644 C CD1 . PHE A 250 ? 0.2385 0.2616 0.2208 0.0640  -0.0196 0.0206  250 PHE A CD1 
3645 C CD2 . PHE A 250 ? 0.2241 0.2413 0.2015 0.0478  -0.0228 0.0083  250 PHE A CD2 
3646 C CE1 . PHE A 250 ? 0.2468 0.2628 0.2329 0.0632  -0.0152 0.0170  250 PHE A CE1 
3647 C CE2 . PHE A 250 ? 0.2258 0.2376 0.2080 0.0472  -0.0192 0.0055  250 PHE A CE2 
3648 C CZ  . PHE A 250 ? 0.2313 0.2419 0.2170 0.0544  -0.0155 0.0095  250 PHE A CZ  
3658 N N   . GLY A 251 ? 0.2437 0.2443 0.1827 0.0608  -0.0234 0.0280  251 GLY A N   
3659 C CA  . GLY A 251 ? 0.2483 0.2497 0.1770 0.0587  -0.0259 0.0298  251 GLY A CA  
3660 C C   . GLY A 251 ? 0.2462 0.2485 0.1720 0.0490  -0.0273 0.0220  251 GLY A C   
3661 O O   . GLY A 251 ? 0.2626 0.2643 0.1783 0.0468  -0.0285 0.0227  251 GLY A O   
3665 N N   . MET A 252 ? 0.2149 0.2180 0.1484 0.0439  -0.0267 0.0150  252 MET A N   
3666 C CA  . MET A 252 ? 0.2124 0.2144 0.1427 0.0363  -0.0266 0.0080  252 MET A CA  
3667 C C   . MET A 252 ? 0.2322 0.2214 0.1557 0.0343  -0.0210 0.0072  252 MET A C   
3668 O O   . MET A 252 ? 0.2394 0.2188 0.1635 0.0356  -0.0168 0.0090  252 MET A O   
3669 C CB  . MET A 252 ? 0.2083 0.2143 0.1483 0.0323  -0.0270 0.0018  252 MET A CB  
3670 C CG  . MET A 252 ? 0.2113 0.2311 0.1596 0.0332  -0.0320 0.0029  252 MET A CG  
3671 S SD  . MET A 252 ? 0.2282 0.2503 0.1867 0.0279  -0.0317 -0.0041 252 MET A SD  
3672 C CE  . MET A 252 ? 0.2433 0.2602 0.1927 0.0207  -0.0312 -0.0110 252 MET A CE  
3682 N N   . SER A 253 ? 0.2180 0.2073 0.1345 0.0302  -0.0204 0.0042  253 SER A N   
3683 C CA  . SER A 253 ? 0.2246 0.2055 0.1373 0.0275  -0.0147 0.0032  253 SER A CA  
3684 C C   . SER A 253 ? 0.2075 0.1881 0.1301 0.0249  -0.0121 -0.0012 253 SER A C   
3685 O O   . SER A 253 ? 0.2018 0.1872 0.1315 0.0244  -0.0143 -0.0049 253 SER A O   
3686 C CB  . SER A 253 ? 0.2276 0.2091 0.1303 0.0249  -0.0136 0.0013  253 SER A CB  
3687 O OG  . SER A 253 ? 0.2432 0.2282 0.1477 0.0221  -0.0141 -0.0051 253 SER A OG  
3693 N N   . ASN A 254 ? 0.2055 0.1760 0.1572 0.0240  -0.0135 0.0251  254 ASN A N   
3694 C CA  . ASN A 254 ? 0.1929 0.1641 0.1525 0.0198  -0.0105 0.0187  254 ASN A CA  
3695 C C   . ASN A 254 ? 0.1835 0.1652 0.1441 0.0163  -0.0103 0.0134  254 ASN A C   
3696 O O   . ASN A 254 ? 0.1726 0.1589 0.1404 0.0158  -0.0106 0.0083  254 ASN A O   
3697 C CB  . ASN A 254 ? 0.2087 0.1696 0.1666 0.0152  -0.0058 0.0200  254 ASN A CB  
3698 C CG  . ASN A 254 ? 0.1922 0.1553 0.1584 0.0116  -0.0033 0.0140  254 ASN A CG  
3699 O OD1 . ASN A 254 ? 0.2143 0.1834 0.1815 0.0076  -0.0008 0.0112  254 ASN A OD1 
3700 N ND2 . ASN A 254 ? 0.2075 0.1665 0.1795 0.0138  -0.0042 0.0117  254 ASN A ND2 
3707 N N   . ALA A 255 ? 0.1899 0.1740 0.1419 0.0140  -0.0097 0.0146  255 ALA A N   
3708 C CA  . ALA A 255 ? 0.1846 0.1758 0.1357 0.0110  -0.0090 0.0090  255 ALA A CA  
3709 C C   . ALA A 255 ? 0.1799 0.1789 0.1339 0.0122  -0.0138 0.0057  255 ALA A C   
3710 O O   . ALA A 255 ? 0.1721 0.1735 0.1307 0.0102  -0.0131 0.0002  255 ALA A O   
3711 C CB  . ALA A 255 ? 0.2048 0.1965 0.1443 0.0090  -0.0070 0.0108  255 ALA A CB  
3717 N N   . GLU A 256 ? 0.1857 0.1891 0.1374 0.0152  -0.0186 0.0093  256 GLU A N   
3718 C CA  . GLU A 256 ? 0.1818 0.1955 0.1377 0.0152  -0.0234 0.0064  256 GLU A CA  
3719 C C   . GLU A 256 ? 0.1705 0.1857 0.1385 0.0164  -0.0230 0.0040  256 GLU A C   
3720 O O   . GLU A 256 ? 0.1648 0.1861 0.1374 0.0135  -0.0241 -0.0004 256 GLU A O   
3721 C CB  . GLU A 256 ? 0.1908 0.2119 0.1429 0.0190  -0.0289 0.0115  256 GLU A CB  
3722 C CG  . GLU A 256 ? 0.2034 0.2257 0.1418 0.0172  -0.0303 0.0132  256 GLU A CG  
3723 C CD  . GLU A 256 ? 0.2344 0.2631 0.1689 0.0113  -0.0320 0.0062  256 GLU A CD  
3724 O OE1 . GLU A 256 ? 0.2291 0.2561 0.1516 0.0088  -0.0311 0.0051  256 GLU A OE1 
3725 O OE2 . GLU A 256 ? 0.2472 0.2829 0.1895 0.0090  -0.0346 0.0017  256 GLU A OE2 
3732 N N   . TYR A 257 ? 0.1692 0.1777 0.1413 0.0202  -0.0210 0.0069  257 TYR A N   
3733 C CA  . TYR A 257 ? 0.1600 0.1697 0.1422 0.0218  -0.0201 0.0044  257 TYR A CA  
3734 C C   . TYR A 257 ? 0.1517 0.1596 0.1366 0.0172  -0.0169 -0.0009 257 TYR A C   
3735 O O   . TYR A 257 ? 0.1486 0.1617 0.1394 0.0161  -0.0173 -0.0039 257 TYR A O   
3736 C CB  . TYR A 257 ? 0.1639 0.1640 0.1470 0.0263  -0.0184 0.0077  257 TYR A CB  
3737 C CG  . TYR A 257 ? 0.1583 0.1613 0.1500 0.0302  -0.0184 0.0061  257 TYR A CG  
3738 C CD1 . TYR A 257 ? 0.1597 0.1723 0.1557 0.0355  -0.0216 0.0080  257 TYR A CD1 
3739 C CD2 . TYR A 257 ? 0.1615 0.1594 0.1570 0.0288  -0.0152 0.0025  257 TYR A CD2 
3740 C CE1 . TYR A 257 ? 0.1885 0.2054 0.1922 0.0395  -0.0209 0.0065  257 TYR A CE1 
3741 C CE2 . TYR A 257 ? 0.1587 0.1597 0.1606 0.0326  -0.0148 0.0008  257 TYR A CE2 
3742 C CZ  . TYR A 257 ? 0.1504 0.1607 0.1563 0.0379  -0.0173 0.0028  257 TYR A CZ  
3743 O OH  . TYR A 257 ? 0.1821 0.1971 0.1945 0.0420  -0.0161 0.0010  257 TYR A OH  
3753 N N   . LEU A 258 ? 0.1532 0.1544 0.1336 0.0147  -0.0135 -0.0016 258 LEU A N   
3754 C CA  . LEU A 258 ? 0.1471 0.1470 0.1295 0.0118  -0.0105 -0.0060 258 LEU A CA  
3755 C C   . LEU A 258 ? 0.1481 0.1515 0.1275 0.0088  -0.0114 -0.0097 258 LEU A C   
3756 O O   . LEU A 258 ? 0.1561 0.1592 0.1390 0.0075  -0.0104 -0.0130 258 LEU A O   
3757 C CB  . LEU A 258 ? 0.1559 0.1507 0.1355 0.0104  -0.0066 -0.0055 258 LEU A CB  
3758 C CG  . LEU A 258 ? 0.1488 0.1392 0.1334 0.0113  -0.0051 -0.0044 258 LEU A CG  
3759 C CD1 . LEU A 258 ? 0.1954 0.1818 0.1771 0.0088  -0.0021 -0.0021 258 LEU A CD1 
3760 C CD2 . LEU A 258 ? 0.1815 0.1736 0.1724 0.0112  -0.0040 -0.0082 258 LEU A CD2 
3772 N N   . VAL A 259 ? 0.1560 0.1617 0.1279 0.0075  -0.0135 -0.0093 259 VAL A N   
3773 C CA  . VAL A 259 ? 0.1598 0.1675 0.1277 0.0037  -0.0149 -0.0137 259 VAL A CA  
3774 C C   . VAL A 259 ? 0.1548 0.1677 0.1303 0.0022  -0.0174 -0.0152 259 VAL A C   
3775 O O   . VAL A 259 ? 0.1578 0.1679 0.1340 -0.0010 -0.0163 -0.0191 259 VAL A O   
3776 C CB  . VAL A 259 ? 0.1703 0.1818 0.1287 0.0026  -0.0182 -0.0127 259 VAL A CB  
3777 C CG1 . VAL A 259 ? 0.1841 0.1990 0.1390 -0.0024 -0.0214 -0.0178 259 VAL A CG1 
3778 C CG2 . VAL A 259 ? 0.1793 0.1856 0.1282 0.0029  -0.0145 -0.0122 259 VAL A CG2 
3788 N N   . GLU A 260 ? 0.1522 0.1728 0.1334 0.0048  -0.0206 -0.0117 260 GLU A N   
3789 C CA  . GLU A 260 ? 0.1699 0.1990 0.1590 0.0032  -0.0227 -0.0126 260 GLU A CA  
3790 C C   . GLU A 260 ? 0.1593 0.1843 0.1549 0.0038  -0.0190 -0.0137 260 GLU A C   
3791 O O   . GLU A 260 ? 0.1562 0.1833 0.1552 -0.0001 -0.0187 -0.0160 260 GLU A O   
3792 C CB  . GLU A 260 ? 0.1947 0.2347 0.1884 0.0075  -0.0267 -0.0083 260 GLU A CB  
3793 C CG  . GLU A 260 ? 0.1917 0.2456 0.1929 0.0046  -0.0298 -0.0093 260 GLU A CG  
3794 C CD  . GLU A 260 ? 0.1972 0.2654 0.2027 0.0094  -0.0345 -0.0050 260 GLU A CD  
3795 O OE1 . GLU A 260 ? 0.2673 0.3336 0.2667 0.0138  -0.0364 -0.0014 260 GLU A OE1 
3796 O OE2 . GLU A 260 ? 0.2070 0.2894 0.2219 0.0086  -0.0363 -0.0050 260 GLU A OE2 
3803 N N   . GLY A 261 ? 0.1405 0.1595 0.1373 0.0079  -0.0162 -0.0121 261 GLY A N   
3804 C CA  . GLY A 261 ? 0.1468 0.1627 0.1484 0.0086  -0.0132 -0.0133 261 GLY A CA  
3805 C C   . GLY A 261 ? 0.1414 0.1505 0.1397 0.0055  -0.0106 -0.0164 261 GLY A C   
3806 O O   . GLY A 261 ? 0.1492 0.1574 0.1504 0.0044  -0.0091 -0.0175 261 GLY A O   
3810 N N   . ILE A 262 ? 0.1363 0.1402 0.1279 0.0047  -0.0096 -0.0177 262 ILE A N   
3811 C CA  . ILE A 262 ? 0.1398 0.1365 0.1274 0.0033  -0.0069 -0.0207 262 ILE A CA  
3812 C C   . ILE A 262 ? 0.1451 0.1406 0.1312 -0.0014 -0.0080 -0.0232 262 ILE A C   
3813 O O   . ILE A 262 ? 0.1623 0.1518 0.1486 -0.0022 -0.0058 -0.0244 262 ILE A O   
3814 C CB  . ILE A 262 ? 0.1610 0.1541 0.1414 0.0039  -0.0052 -0.0218 262 ILE A CB  
3815 C CG1 . ILE A 262 ? 0.1514 0.1449 0.1345 0.0072  -0.0028 -0.0196 262 ILE A CG1 
3816 C CG2 . ILE A 262 ? 0.1746 0.1599 0.1490 0.0029  -0.0027 -0.0258 262 ILE A CG2 
3817 C CD1 . ILE A 262 ? 0.1692 0.1624 0.1463 0.0073  -0.0010 -0.0191 262 ILE A CD1 
3829 N N   . GLU A 263 ? 0.1556 0.1567 0.1399 -0.0050 -0.0116 -0.0238 263 GLU A N   
3830 C CA  . GLU A 263 ? 0.1640 0.1644 0.1469 -0.0114 -0.0130 -0.0267 263 GLU A CA  
3831 C C   . GLU A 263 ? 0.1663 0.1703 0.1574 -0.0129 -0.0123 -0.0251 263 GLU A C   
3832 O O   . GLU A 263 ? 0.1890 0.1857 0.1783 -0.0170 -0.0105 -0.0268 263 GLU A O   
3833 C CB  . GLU A 263 ? 0.1991 0.2087 0.1797 -0.0151 -0.0179 -0.0273 263 GLU A CB  
3834 C CG  . GLU A 263 ? 0.2575 0.2684 0.2371 -0.0236 -0.0202 -0.0307 263 GLU A CG  
3835 C CD  . GLU A 263 ? 0.3560 0.3804 0.3352 -0.0273 -0.0262 -0.0310 263 GLU A CD  
3836 O OE1 . GLU A 263 ? 0.3912 0.4190 0.3659 -0.0232 -0.0281 -0.0295 263 GLU A OE1 
3837 O OE2 . GLU A 263 ? 0.4028 0.4346 0.3855 -0.0347 -0.0290 -0.0327 263 GLU A OE2 
3844 N N   . ALA A 264 ? 0.1570 0.1713 0.1561 -0.0093 -0.0132 -0.0216 264 ALA A N   
3845 C CA  . ALA A 264 ? 0.1603 0.1800 0.1669 -0.0101 -0.0119 -0.0200 264 ALA A CA  
3846 C C   . ALA A 264 ? 0.1572 0.1662 0.1620 -0.0081 -0.0077 -0.0198 264 ALA A C   
3847 O O   . ALA A 264 ? 0.1645 0.1714 0.1704 -0.0116 -0.0058 -0.0195 264 ALA A O   
3848 C CB  . ALA A 264 ? 0.1691 0.2003 0.1832 -0.0046 -0.0129 -0.0168 264 ALA A CB  
3854 N N   . THR A 265 ? 0.1427 0.1462 0.1452 -0.0026 -0.0062 -0.0196 265 THR A N   
3855 C CA  . THR A 265 ? 0.1459 0.1423 0.1474 0.0003  -0.0030 -0.0191 265 THR A CA  
3856 C C   . THR A 265 ? 0.1624 0.1471 0.1574 -0.0021 -0.0011 -0.0208 265 THR A C   
3857 O O   . THR A 265 ? 0.1651 0.1446 0.1595 -0.0020 0.0012  -0.0196 265 THR A O   
3858 C CB  . THR A 265 ? 0.1501 0.1458 0.1515 0.0056  -0.0025 -0.0187 265 THR A CB  
3859 O OG1 . THR A 265 ? 0.1573 0.1602 0.1631 0.0078  -0.0040 -0.0172 265 THR A OG1 
3860 C CG2 . THR A 265 ? 0.1741 0.1660 0.1754 0.0089  -0.0002 -0.0180 265 THR A CG2 
3868 N N   . GLN A 266 ? 0.1584 0.1376 0.1475 -0.0039 -0.0016 -0.0236 266 GLN A N   
3869 C CA  . GLN A 266 ? 0.1631 0.1288 0.1445 -0.0061 0.0004  -0.0262 266 GLN A CA  
3870 C C   . GLN A 266 ? 0.1785 0.1410 0.1601 -0.0129 0.0004  -0.0259 266 GLN A C   
3871 O O   . GLN A 266 ? 0.1917 0.1425 0.1695 -0.0131 0.0033  -0.0253 266 GLN A O   
3872 C CB  . GLN A 266 ? 0.1826 0.1444 0.1567 -0.0078 -0.0006 -0.0302 266 GLN A CB  
3873 C CG  . GLN A 266 ? 0.1711 0.1336 0.1434 -0.0013 0.0010  -0.0303 266 GLN A CG  
3874 C CD  . GLN A 266 ? 0.1754 0.1369 0.1402 -0.0031 0.0001  -0.0337 266 GLN A CD  
3875 O OE1 . GLN A 266 ? 0.2005 0.1650 0.1630 -0.0088 -0.0032 -0.0353 266 GLN A OE1 
3876 N NE2 . GLN A 266 ? 0.1956 0.1546 0.1564 0.0017  0.0030  -0.0347 266 GLN A NE2 
3885 N N   . LYS A 267 ? 0.1802 0.1538 0.1665 -0.0187 -0.0026 -0.0260 267 LYS A N   
3886 C CA  . LYS A 267 ? 0.1905 0.1638 0.1783 -0.0269 -0.0024 -0.0256 267 LYS A CA  
3887 C C   . LYS A 267 ? 0.1818 0.1558 0.1739 -0.0249 0.0007  -0.0213 267 LYS A C   
3888 O O   . LYS A 267 ? 0.2001 0.1636 0.1885 -0.0291 0.0033  -0.0203 267 LYS A O   
3889 C CB  . LYS A 267 ? 0.1896 0.1796 0.1838 -0.0326 -0.0066 -0.0261 267 LYS A CB  
3890 C CG  . LYS A 267 ? 0.2649 0.2538 0.2529 -0.0368 -0.0102 -0.0306 267 LYS A CG  
3891 C CD  . LYS A 267 ? 0.3309 0.3402 0.3262 -0.0398 -0.0152 -0.0299 267 LYS A CD  
3892 C CE  . LYS A 267 ? 0.4007 0.4096 0.3884 -0.0445 -0.0193 -0.0344 267 LYS A CE  
3893 N NZ  . LYS A 267 ? 0.4869 0.5174 0.4815 -0.0457 -0.0250 -0.0330 267 LYS A NZ  
3907 N N   . ALA A 268 ? 0.1724 0.1574 0.1708 -0.0185 0.0006  -0.0187 268 ALA A N   
3908 C CA  . ALA A 268 ? 0.1728 0.1595 0.1739 -0.0163 0.0035  -0.0150 268 ALA A CA  
3909 C C   . ALA A 268 ? 0.1711 0.1427 0.1650 -0.0122 0.0064  -0.0138 268 ALA A C   
3910 O O   . ALA A 268 ? 0.1929 0.1579 0.1841 -0.0144 0.0092  -0.0110 268 ALA A O   
3911 C CB  . ALA A 268 ? 0.1638 0.1635 0.1714 -0.0099 0.0026  -0.0137 268 ALA A CB  
3917 N N   . ALA A 269 ? 0.1650 0.1315 0.1556 -0.0062 0.0060  -0.0155 269 ALA A N   
3918 C CA  . ALA A 269 ? 0.1836 0.1384 0.1684 -0.0007 0.0084  -0.0142 269 ALA A CA  
3919 C C   . ALA A 269 ? 0.2095 0.1470 0.1863 -0.0046 0.0106  -0.0146 269 ALA A C   
3920 O O   . ALA A 269 ? 0.2216 0.1490 0.1938 -0.0023 0.0132  -0.0113 269 ALA A O   
3921 C CB  . ALA A 269 ? 0.1683 0.1241 0.1528 0.0057  0.0077  -0.0161 269 ALA A CB  
3927 N N   . GLN A 270 ? 0.2015 0.1339 0.1751 -0.0105 0.0095  -0.0186 270 GLN A N   
3928 C CA  . GLN A 270 ? 0.2139 0.1269 0.1783 -0.0151 0.0115  -0.0202 270 GLN A CA  
3929 C C   . GLN A 270 ? 0.2530 0.1627 0.2177 -0.0232 0.0131  -0.0170 270 GLN A C   
3930 O O   . GLN A 270 ? 0.2928 0.1830 0.2489 -0.0261 0.0158  -0.0163 270 GLN A O   
3931 C CB  . GLN A 270 ? 0.2286 0.1382 0.1888 -0.0202 0.0095  -0.0263 270 GLN A CB  
3932 C CG  . GLN A 270 ? 0.2512 0.1599 0.2082 -0.0119 0.0096  -0.0291 270 GLN A CG  
3933 C CD  . GLN A 270 ? 0.2802 0.1913 0.2337 -0.0163 0.0071  -0.0346 270 GLN A CD  
3934 O OE1 . GLN A 270 ? 0.3319 0.2399 0.2824 -0.0257 0.0052  -0.0377 270 GLN A OE1 
3935 N NE2 . GLN A 270 ? 0.2589 0.1758 0.2123 -0.0099 0.0069  -0.0359 270 GLN A NE2 
3944 N N   . SER A 271 ? 0.2368 0.1644 0.2107 -0.0268 0.0118  -0.0147 271 SER A N   
3945 C CA  . SER A 271 ? 0.2413 0.1694 0.2167 -0.0346 0.0140  -0.0109 271 SER A CA  
3946 C C   . SER A 271 ? 0.2371 0.1615 0.2103 -0.0285 0.0175  -0.0049 271 SER A C   
3947 O O   . SER A 271 ? 0.2845 0.2080 0.2576 -0.0345 0.0202  -0.0008 271 SER A O   
3948 C CB  . SER A 271 ? 0.2740 0.2252 0.2607 -0.0402 0.0118  -0.0109 271 SER A CB  
3949 O OG  . SER A 271 ? 0.2662 0.2329 0.2599 -0.0327 0.0119  -0.0081 271 SER A OG  
3955 N N   . GLY A 272 ? 0.2334 0.1569 0.2050 -0.0175 0.0173  -0.0041 272 GLY A N   
3956 C CA  . GLY A 272 ? 0.2528 0.1736 0.2212 -0.0112 0.0197  0.0014  272 GLY A CA  
3957 C C   . GLY A 272 ? 0.2195 0.1596 0.1949 -0.0075 0.0189  0.0033  272 GLY A C   
3958 O O   . GLY A 272 ? 0.2462 0.1857 0.2182 -0.0032 0.0208  0.0078  272 GLY A O   
3962 N N   . LYS A 273 ? 0.2049 0.1607 0.1888 -0.0085 0.0163  -0.0001 273 LYS A N   
3963 C CA  . LYS A 273 ? 0.1866 0.1585 0.1762 -0.0042 0.0157  0.0005  273 LYS A CA  
3964 C C   . LYS A 273 ? 0.1906 0.1629 0.1788 0.0047  0.0139  -0.0006 273 LYS A C   
3965 O O   . LYS A 273 ? 0.1945 0.1619 0.1819 0.0071  0.0122  -0.0033 273 LYS A O   
3966 C CB  . LYS A 273 ? 0.2024 0.1888 0.2007 -0.0075 0.0136  -0.0025 273 LYS A CB  
3967 C CG  . LYS A 273 ? 0.2248 0.2175 0.2272 -0.0167 0.0150  -0.0013 273 LYS A CG  
3968 C CD  . LYS A 273 ? 0.2218 0.2232 0.2260 -0.0174 0.0187  0.0028  273 LYS A CD  
3969 C CE  . LYS A 273 ? 0.2554 0.2638 0.2645 -0.0280 0.0204  0.0042  273 LYS A CE  
3970 N NZ  . LYS A 273 ? 0.2553 0.2735 0.2662 -0.0296 0.0250  0.0086  273 LYS A NZ  
3984 N N   . ILE A 274 ? 0.1835 0.1627 0.1714 0.0093  0.0143  0.0013  274 ILE A N   
3985 C CA  . ILE A 274 ? 0.1659 0.1494 0.1542 0.0161  0.0119  -0.0006 274 ILE A CA  
3986 C C   . ILE A 274 ? 0.1551 0.1462 0.1501 0.0155  0.0094  -0.0050 274 ILE A C   
3987 O O   . ILE A 274 ? 0.1614 0.1597 0.1610 0.0125  0.0095  -0.0059 274 ILE A O   
3988 C CB  . ILE A 274 ? 0.1806 0.1709 0.1665 0.0197  0.0125  0.0014  274 ILE A CB  
3989 C CG1 . ILE A 274 ? 0.1892 0.1713 0.1669 0.0211  0.0149  0.0070  274 ILE A CG1 
3990 C CG2 . ILE A 274 ? 0.1899 0.1863 0.1769 0.0250  0.0094  -0.0015 274 ILE A CG2 
3991 C CD1 . ILE A 274 ? 0.2113 0.2008 0.1851 0.0236  0.0159  0.0093  274 ILE A CD1 
4003 N N   . ILE A 275 ? 0.1543 0.1445 0.1499 0.0188  0.0073  -0.0072 275 ILE A N   
4004 C CA  . ILE A 275 ? 0.1482 0.1440 0.1485 0.0186  0.0052  -0.0105 275 ILE A CA  
4005 C C   . ILE A 275 ? 0.1406 0.1405 0.1412 0.0227  0.0036  -0.0118 275 ILE A C   
4006 O O   . ILE A 275 ? 0.1580 0.1562 0.1566 0.0256  0.0033  -0.0111 275 ILE A O   
4007 C CB  . ILE A 275 ? 0.1510 0.1417 0.1512 0.0168  0.0046  -0.0121 275 ILE A CB  
4008 C CG1 . ILE A 275 ? 0.1743 0.1620 0.1741 0.0113  0.0052  -0.0119 275 ILE A CG1 
4009 C CG2 . ILE A 275 ? 0.1680 0.1632 0.1715 0.0174  0.0026  -0.0145 275 ILE A CG2 
4010 C CD1 . ILE A 275 ? 0.1956 0.1927 0.2008 0.0086  0.0041  -0.0124 275 ILE A CD1 
4022 N N   . THR A 276 ? 0.1351 0.1404 0.1381 0.0229  0.0026  -0.0137 276 THR A N   
4023 C CA  . THR A 276 ? 0.1396 0.1480 0.1428 0.0248  0.0007  -0.0159 276 THR A CA  
4024 C C   . THR A 276 ? 0.1414 0.1493 0.1478 0.0232  -0.0004 -0.0182 276 THR A C   
4025 O O   . THR A 276 ? 0.1447 0.1531 0.1521 0.0232  -0.0004 -0.0193 276 THR A O   
4026 C CB  . THR A 276 ? 0.1393 0.1514 0.1396 0.0267  0.0006  -0.0167 276 THR A CB  
4027 O OG1 . THR A 276 ? 0.1484 0.1618 0.1496 0.0264  0.0017  -0.0178 276 THR A OG1 
4028 C CG2 . THR A 276 ? 0.1437 0.1559 0.1394 0.0285  0.0018  -0.0133 276 THR A CG2 
4036 N N   . MET A 277 ? 0.1428 0.1494 0.1505 0.0222  -0.0009 -0.0183 277 MET A N   
4037 C CA  . MET A 277 ? 0.1333 0.1383 0.1427 0.0203  -0.0016 -0.0192 277 MET A CA  
4038 C C   . MET A 277 ? 0.1361 0.1422 0.1463 0.0195  -0.0028 -0.0212 277 MET A C   
4039 O O   . MET A 277 ? 0.1498 0.1595 0.1611 0.0190  -0.0032 -0.0216 277 MET A O   
4040 C CB  . MET A 277 ? 0.1565 0.1597 0.1656 0.0193  -0.0008 -0.0184 277 MET A CB  
4041 C CG  . MET A 277 ? 0.1639 0.1657 0.1734 0.0173  -0.0013 -0.0185 277 MET A CG  
4042 S SD  . MET A 277 ? 0.1660 0.1662 0.1732 0.0161  -0.0001 -0.0181 277 MET A SD  
4043 C CE  . MET A 277 ? 0.2218 0.2192 0.2267 0.0152  -0.0005 -0.0179 277 MET A CE  
4053 N N   . THR A 278 ? 0.1400 0.1433 0.1496 0.0193  -0.0033 -0.0226 278 THR A N   
4054 C CA  . THR A 278 ? 0.1356 0.1366 0.1449 0.0170  -0.0044 -0.0248 278 THR A CA  
4055 C C   . THR A 278 ? 0.1454 0.1421 0.1553 0.0146  -0.0040 -0.0233 278 THR A C   
4056 O O   . THR A 278 ? 0.1554 0.1498 0.1648 0.0160  -0.0035 -0.0213 278 THR A O   
4057 C CB  . THR A 278 ? 0.1539 0.1505 0.1602 0.0183  -0.0047 -0.0276 278 THR A CB  
4058 O OG1 . THR A 278 ? 0.1617 0.1526 0.1675 0.0206  -0.0039 -0.0266 278 THR A OG1 
4059 C CG2 . THR A 278 ? 0.1609 0.1623 0.1651 0.0211  -0.0045 -0.0286 278 THR A CG2 
4067 N N   . LEU A 279 ? 0.1383 0.1356 0.1493 0.0107  -0.0042 -0.0239 279 LEU A N   
4068 C CA  . LEU A 279 ? 0.1384 0.1315 0.1490 0.0077  -0.0033 -0.0219 279 LEU A CA  
4069 C C   . LEU A 279 ? 0.1394 0.1288 0.1497 0.0026  -0.0037 -0.0237 279 LEU A C   
4070 O O   . LEU A 279 ? 0.1474 0.1442 0.1607 -0.0005 -0.0044 -0.0257 279 LEU A O   
4071 C CB  . LEU A 279 ? 0.1451 0.1448 0.1577 0.0070  -0.0018 -0.0200 279 LEU A CB  
4072 C CG  . LEU A 279 ? 0.1473 0.1479 0.1586 0.0107  -0.0013 -0.0188 279 LEU A CG  
4073 C CD1 . LEU A 279 ? 0.1695 0.1757 0.1818 0.0110  0.0004  -0.0183 279 LEU A CD1 
4074 C CD2 . LEU A 279 ? 0.1782 0.1733 0.1865 0.0113  -0.0016 -0.0169 279 LEU A CD2 
4086 N N   . GLY A 280 ? 0.1490 0.1267 0.1556 0.0016  -0.0035 -0.0231 280 GLY A N   
4087 C CA  . GLY A 280 ? 0.1636 0.1339 0.1685 -0.0043 -0.0037 -0.0250 280 GLY A CA  
4088 C C   . GLY A 280 ? 0.1592 0.1330 0.1665 -0.0110 -0.0022 -0.0226 280 GLY A C   
4089 O O   . GLY A 280 ? 0.1657 0.1371 0.1714 -0.0108 -0.0004 -0.0183 280 GLY A O   
4093 N N   . LEU A 281 ? 0.1606 0.1416 0.1717 -0.0172 -0.0029 -0.0252 281 LEU A N   
4094 C CA  . LEU A 281 ? 0.1642 0.1503 0.1786 -0.0248 -0.0010 -0.0231 281 LEU A CA  
4095 C C   . LEU A 281 ? 0.1796 0.1486 0.1882 -0.0300 0.0006  -0.0208 281 LEU A C   
4096 O O   . LEU A 281 ? 0.2044 0.1734 0.2128 -0.0337 0.0034  -0.0164 281 LEU A O   
4097 C CB  . LEU A 281 ? 0.1637 0.1629 0.1842 -0.0308 -0.0027 -0.0268 281 LEU A CB  
4098 C CG  . LEU A 281 ? 0.1632 0.1812 0.1900 -0.0254 -0.0038 -0.0276 281 LEU A CG  
4099 C CD1 . LEU A 281 ? 0.1779 0.2072 0.2087 -0.0295 -0.0073 -0.0319 281 LEU A CD1 
4100 C CD2 . LEU A 281 ? 0.1668 0.1969 0.1986 -0.0245 -0.0006 -0.0238 281 LEU A CD2 
4112 N N   . GLY A 282 ? 0.2074 0.1604 0.2103 -0.0303 -0.0008 -0.0237 282 GLY A N   
4113 C CA  . GLY A 282 ? 0.2095 0.1424 0.2053 -0.0342 0.0008  -0.0213 282 GLY A CA  
4114 C C   . GLY A 282 ? 0.2105 0.1338 0.2009 -0.0256 0.0017  -0.0163 282 GLY A C   
4115 O O   . GLY A 282 ? 0.2010 0.1318 0.1930 -0.0173 0.0007  -0.0161 282 GLY A O   
4119 N N   . GLU A 283 ? 0.2369 0.1433 0.2206 -0.0280 0.0036  -0.0120 283 GLU A N   
4120 C CA  . GLU A 283 ? 0.2341 0.1324 0.2122 -0.0198 0.0040  -0.0062 283 GLU A CA  
4121 C C   . GLU A 283 ? 0.2388 0.1283 0.2138 -0.0100 0.0022  -0.0086 283 GLU A C   
4122 O O   . GLU A 283 ? 0.2688 0.1487 0.2417 -0.0105 0.0015  -0.0138 283 GLU A O   
4123 C CB  . GLU A 283 ? 0.3146 0.1952 0.2850 -0.0247 0.0065  -0.0003 283 GLU A CB  
4124 C CG  . GLU A 283 ? 0.3713 0.2606 0.3446 -0.0354 0.0094  0.0026  283 GLU A CG  
4125 C CD  . GLU A 283 ? 0.5165 0.4221 0.4919 -0.0320 0.0105  0.0067  283 GLU A CD  
4126 O OE1 . GLU A 283 ? 0.5438 0.4691 0.5272 -0.0328 0.0103  0.0035  283 GLU A OE1 
4127 O OE2 . GLU A 283 ? 0.5674 0.4654 0.5355 -0.0285 0.0114  0.0133  283 GLU A OE2 
4134 N N   . ALA A 284 ? 0.2504 0.1436 0.2247 -0.0010 0.0014  -0.0048 284 ALA A N   
4135 C CA  . ALA A 284 ? 0.2640 0.1508 0.2362 0.0090  0.0002  -0.0060 284 ALA A CA  
4136 C C   . ALA A 284 ? 0.2812 0.1432 0.2444 0.0108  0.0013  -0.0042 284 ALA A C   
4137 O O   . ALA A 284 ? 0.3261 0.1770 0.2836 0.0084  0.0025  0.0019  284 ALA A O   
4138 C CB  . ALA A 284 ? 0.2639 0.1616 0.2379 0.0172  -0.0012 -0.0017 284 ALA A CB  
4144 N N   . ILE A 285 ? 0.2903 0.1425 0.2512 0.0155  0.0011  -0.0094 285 ILE A N   
4145 C CA  . ILE A 285 ? 0.3738 0.2017 0.3255 0.0216  0.0023  -0.0075 285 ILE A CA  
4146 C C   . ILE A 285 ? 0.3616 0.1935 0.3131 0.0332  0.0013  -0.0005 285 ILE A C   
4147 O O   . ILE A 285 ? 0.3233 0.1758 0.2821 0.0385  -0.0003 -0.0005 285 ILE A O   
4148 C CB  . ILE A 285 ? 0.3441 0.1625 0.2930 0.0259  0.0026  -0.0156 285 ILE A CB  
4149 C CG1 . ILE A 285 ? 0.3819 0.1956 0.3296 0.0135  0.0027  -0.0228 285 ILE A CG1 
4150 C CG2 . ILE A 285 ? 0.3986 0.1915 0.3377 0.0351  0.0042  -0.0136 285 ILE A CG2 
4151 C CD1 . ILE A 285 ? 0.4838 0.2921 0.4283 0.0166  0.0027  -0.0319 285 ILE A CD1 
4163 N N   . ASP A 286 ? 0.4061 0.2187 0.3490 0.0368  0.0022  0.0059  286 ASP A N   
4164 C CA  . ASP A 286 ? 0.4404 0.2567 0.3824 0.0488  0.0007  0.0131  286 ASP A CA  
4165 C C   . ASP A 286 ? 0.3816 0.2106 0.3298 0.0605  -0.0005 0.0095  286 ASP A C   
4166 O O   . ASP A 286 ? 0.4245 0.2418 0.3702 0.0657  0.0011  0.0042  286 ASP A O   
4167 C CB  . ASP A 286 ? 0.4632 0.2509 0.3931 0.0527  0.0023  0.0194  286 ASP A CB  
4168 C CG  . ASP A 286 ? 0.5750 0.3590 0.4995 0.0462  0.0026  0.0281  286 ASP A CG  
4169 O OD1 . ASP A 286 ? 0.5839 0.3789 0.5120 0.0340  0.0033  0.0270  286 ASP A OD1 
4170 O OD2 . ASP A 286 ? 0.6748 0.4428 0.5903 0.0533  0.0028  0.0363  286 ASP A OD2 
4175 N N   . ASN A 287 ? 0.3690 0.2222 0.3249 0.0642  -0.0030 0.0121  287 ASN A N   
4176 C CA  . ASN A 287 ? 0.3734 0.2444 0.3374 0.0731  -0.0040 0.0092  287 ASN A CA  
4177 C C   . ASN A 287 ? 0.3642 0.2565 0.3337 0.0764  -0.0073 0.0150  287 ASN A C   
4178 O O   . ASN A 287 ? 0.3671 0.2723 0.3397 0.0680  -0.0086 0.0151  287 ASN A O   
4179 C CB  . ASN A 287 ? 0.3798 0.2625 0.3502 0.0662  -0.0031 0.0011  287 ASN A CB  
4180 C CG  . ASN A 287 ? 0.3600 0.2588 0.3377 0.0745  -0.0030 -0.0021 287 ASN A CG  
4181 O OD1 . ASN A 287 ? 0.3743 0.2848 0.3562 0.0832  -0.0045 0.0019  287 ASN A OD1 
4182 N ND2 . ASN A 287 ? 0.3400 0.2412 0.3194 0.0714  -0.0013 -0.0093 287 ASN A ND2 
4189 N N   . ASN A 288 ? 0.3715 0.2675 0.3418 0.0888  -0.0089 0.0194  288 ASN A N   
4190 C CA  . ASN A 288 ? 0.3865 0.3041 0.3619 0.0921  -0.0129 0.0246  288 ASN A CA  
4191 C C   . ASN A 288 ? 0.3723 0.3133 0.3592 0.0985  -0.0139 0.0217  288 ASN A C   
4192 O O   . ASN A 288 ? 0.3412 0.3000 0.3331 0.1046  -0.0174 0.0261  288 ASN A O   
4193 C CB  . ASN A 288 ? 0.4300 0.3375 0.3975 0.1006  -0.0149 0.0338  288 ASN A CB  
4194 C CG  . ASN A 288 ? 0.5193 0.4463 0.4883 0.0994  -0.0196 0.0393  288 ASN A CG  
4195 O OD1 . ASN A 288 ? 0.5102 0.4457 0.4798 0.0884  -0.0202 0.0376  288 ASN A OD1 
4196 N ND2 . ASN A 288 ? 0.5321 0.4662 0.5010 0.1112  -0.0230 0.0459  288 ASN A ND2 
4203 N N   . THR A 289 ? 0.3235 0.2663 0.3148 0.0966  -0.0109 0.0144  289 THR A N   
4204 C CA  . THR A 289 ? 0.3401 0.3040 0.3417 0.1026  -0.0107 0.0119  289 THR A CA  
4205 C C   . THR A 289 ? 0.2409 0.2263 0.2508 0.0929  -0.0119 0.0092  289 THR A C   
4206 O O   . THR A 289 ? 0.2745 0.2810 0.2939 0.0961  -0.0123 0.0085  289 THR A O   
4207 C CB  . THR A 289 ? 0.3149 0.2687 0.3153 0.1072  -0.0062 0.0056  289 THR A CB  
4208 O OG1 . THR A 289 ? 0.3116 0.2614 0.3106 0.0958  -0.0044 -0.0005 289 THR A OG1 
4209 C CG2 . THR A 289 ? 0.3750 0.3017 0.3651 0.1158  -0.0042 0.0067  289 THR A CG2 
4217 N N   . GLY A 290 ? 0.2490 0.2293 0.2555 0.0813  -0.0120 0.0074  290 GLY A N   
4218 C CA  . GLY A 290 ? 0.2248 0.2210 0.2375 0.0727  -0.0125 0.0045  290 GLY A CA  
4219 C C   . GLY A 290 ? 0.2071 0.2078 0.2240 0.0717  -0.0092 -0.0011 290 GLY A C   
4220 O O   . GLY A 290 ? 0.1994 0.2150 0.2223 0.0666  -0.0093 -0.0027 290 GLY A O   
4224 N N   . ILE A 291 ? 0.1559 0.2054 0.2442 0.0615  -0.0156 -0.0291 291 ILE A N   
4225 C CA  . ILE A 291 ? 0.1602 0.2132 0.2474 0.0553  -0.0050 -0.0379 291 ILE A CA  
4226 C C   . ILE A 291 ? 0.1810 0.2150 0.2537 0.0525  -0.0022 -0.0372 291 ILE A C   
4227 O O   . ILE A 291 ? 0.1882 0.2079 0.2605 0.0576  -0.0061 -0.0331 291 ILE A O   
4228 C CB  . ILE A 291 ? 0.1582 0.2238 0.2666 0.0610  0.0006  -0.0482 291 ILE A CB  
4229 C CG1 . ILE A 291 ? 0.1725 0.2596 0.3008 0.0646  -0.0035 -0.0498 291 ILE A CG1 
4230 C CG2 . ILE A 291 ? 0.1761 0.2458 0.2794 0.0533  0.0130  -0.0575 291 ILE A CG2 
4231 C CD1 . ILE A 291 ? 0.2061 0.3088 0.3594 0.0706  0.0027  -0.0611 291 ILE A CD1 
4243 N N   . ASP A 292 ? 0.1442 0.1778 0.2047 0.0441  0.0041  -0.0409 292 ASP A N   
4244 C CA  . ASP A 292 ? 0.1478 0.1671 0.1953 0.0402  0.0063  -0.0422 292 ASP A CA  
4245 C C   . ASP A 292 ? 0.1487 0.1573 0.1852 0.0376  0.0002  -0.0330 292 ASP A C   
4246 O O   . ASP A 292 ? 0.1587 0.1701 0.1952 0.0387  -0.0051 -0.0256 292 ASP A O   
4247 C CB  . ASP A 292 ? 0.1660 0.1766 0.2226 0.0462  0.0092  -0.0494 292 ASP A CB  
4248 C CG  . ASP A 292 ? 0.2469 0.2697 0.3157 0.0490  0.0166  -0.0600 292 ASP A CG  
4249 O OD1 . ASP A 292 ? 0.2300 0.2616 0.2904 0.0420  0.0231  -0.0646 292 ASP A OD1 
4250 O OD2 . ASP A 292 ? 0.3155 0.3395 0.4025 0.0583  0.0162  -0.0634 292 ASP A OD2 
4255 N N   . ASP A 293 ? 0.1592 0.1571 0.1864 0.0335  0.0011  -0.0341 293 ASP A N   
4256 C CA  . ASP A 293 ? 0.1530 0.1426 0.1721 0.0302  -0.0031 -0.0266 293 ASP A CA  
4257 C C   . ASP A 293 ? 0.1739 0.1515 0.1897 0.0269  -0.0018 -0.0302 293 ASP A C   
4258 O O   . ASP A 293 ? 0.1711 0.1484 0.1787 0.0209  -0.0027 -0.0298 293 ASP A O   
4259 C CB  . ASP A 293 ? 0.1636 0.1607 0.1732 0.0246  -0.0044 -0.0229 293 ASP A CB  
4260 C CG  . ASP A 293 ? 0.1480 0.1398 0.1525 0.0226  -0.0081 -0.0155 293 ASP A CG  
4261 O OD1 . ASP A 293 ? 0.1692 0.1536 0.1766 0.0259  -0.0100 -0.0108 293 ASP A OD1 
4262 O OD2 . ASP A 293 ? 0.1674 0.1622 0.1650 0.0180  -0.0088 -0.0140 293 ASP A OD2 
4267 N N   . GLN A 294 ? 0.2089 0.1766 0.2329 0.0312  -0.0001 -0.0340 294 GLN A N   
4268 C CA  . GLN A 294 ? 0.2262 0.1811 0.2492 0.0274  0.0013  -0.0385 294 GLN A CA  
4269 C C   . GLN A 294 ? 0.2001 0.1465 0.2201 0.0240  -0.0014 -0.0295 294 GLN A C   
4270 O O   . GLN A 294 ? 0.2155 0.1580 0.2367 0.0280  -0.0037 -0.0202 294 GLN A O   
4271 C CB  . GLN A 294 ? 0.2816 0.2253 0.3156 0.0337  0.0040  -0.0441 294 GLN A CB  
4272 C CG  . GLN A 294 ? 0.3871 0.3406 0.4276 0.0387  0.0081  -0.0533 294 GLN A CG  
4273 C CD  . GLN A 294 ? 0.4357 0.3971 0.4875 0.0477  0.0061  -0.0483 294 GLN A CD  
4274 O OE1 . GLN A 294 ? 0.3689 0.3320 0.4195 0.0494  0.0006  -0.0374 294 GLN A OE1 
4275 N NE2 . GLN A 294 ? 0.4826 0.4498 0.5463 0.0537  0.0105  -0.0574 294 GLN A NE2 
4284 N N   . ARG A 295 ? 0.2065 0.1514 0.2223 0.0164  -0.0013 -0.0324 295 ARG A N   
4285 C CA  . ARG A 295 ? 0.2021 0.1418 0.2167 0.0117  -0.0021 -0.0254 295 ARG A CA  
4286 C C   . ARG A 295 ? 0.2104 0.1363 0.2304 0.0067  0.0003  -0.0300 295 ARG A C   
4287 O O   . ARG A 295 ? 0.2259 0.1504 0.2481 0.0044  0.0014  -0.0409 295 ARG A O   
4288 C CB  . ARG A 295 ? 0.1813 0.1339 0.1902 0.0064  -0.0043 -0.0247 295 ARG A CB  
4289 C CG  . ARG A 295 ? 0.1776 0.1430 0.1808 0.0093  -0.0063 -0.0223 295 ARG A CG  
4290 C CD  . ARG A 295 ? 0.1779 0.1440 0.1809 0.0143  -0.0071 -0.0140 295 ARG A CD  
4291 N NE  . ARG A 295 ? 0.1827 0.1476 0.1828 0.0117  -0.0076 -0.0069 295 ARG A NE  
4292 C CZ  . ARG A 295 ? 0.1774 0.1465 0.1735 0.0139  -0.0092 -0.0006 295 ARG A CZ  
4293 N NH1 . ARG A 295 ? 0.1669 0.1415 0.1633 0.0188  -0.0112 0.0001  295 ARG A NH1 
4294 N NH2 . ARG A 295 ? 0.1868 0.1555 0.1791 0.0106  -0.0082 0.0040  295 ARG A NH2 
4308 N N   . GLU A 296 ? 0.1983 0.1138 0.2196 0.0041  0.0018  -0.0221 296 GLU A N   
4309 C CA  . GLU A 296 ? 0.2111 0.1151 0.2383 -0.0038 0.0049  -0.0258 296 GLU A CA  
4310 C C   . GLU A 296 ? 0.2014 0.1198 0.2296 -0.0118 0.0033  -0.0325 296 GLU A C   
4311 O O   . GLU A 296 ? 0.1871 0.1205 0.2106 -0.0115 0.0005  -0.0297 296 GLU A O   
4312 C CB  . GLU A 296 ? 0.2674 0.1581 0.2935 -0.0057 0.0080  -0.0141 296 GLU A CB  
4313 C CG  . GLU A 296 ? 0.3428 0.2176 0.3670 0.0030  0.0078  -0.0055 296 GLU A CG  
4314 C CD  . GLU A 296 ? 0.5598 0.4145 0.5924 0.0047  0.0102  -0.0108 296 GLU A CD  
4315 O OE1 . GLU A 296 ? 0.5476 0.3997 0.5870 -0.0021 0.0126  -0.0224 296 GLU A OE1 
4316 O OE2 . GLU A 296 ? 0.6039 0.4450 0.6366 0.0135  0.0092  -0.0037 296 GLU A OE2 
4323 N N   . ASP A 297 ? 0.2118 0.1251 0.2471 -0.0189 0.0045  -0.0419 297 ASP A N   
4324 C CA  . ASP A 297 ? 0.2051 0.1329 0.2440 -0.0265 0.0016  -0.0484 297 ASP A CA  
4325 C C   . ASP A 297 ? 0.2131 0.1470 0.2547 -0.0301 0.0034  -0.0397 297 ASP A C   
4326 O O   . ASP A 297 ? 0.2163 0.1375 0.2593 -0.0319 0.0089  -0.0315 297 ASP A O   
4327 C CB  . ASP A 297 ? 0.2207 0.1409 0.2690 -0.0345 0.0027  -0.0605 297 ASP A CB  
4328 C CG  . ASP A 297 ? 0.2296 0.1451 0.2742 -0.0312 0.0015  -0.0717 297 ASP A CG  
4329 O OD1 . ASP A 297 ? 0.2480 0.1743 0.2825 -0.0251 -0.0016 -0.0727 297 ASP A OD1 
4330 O OD2 . ASP A 297 ? 0.2472 0.1475 0.2987 -0.0349 0.0048  -0.0791 297 ASP A OD2 
4335 N N   . VAL A 298 ? 0.2062 0.1587 0.2479 -0.0309 -0.0009 -0.0411 298 VAL A N   
4336 C CA  . VAL A 298 ? 0.2073 0.1671 0.2536 -0.0341 0.0018  -0.0347 298 VAL A CA  
4337 C C   . VAL A 298 ? 0.2287 0.1848 0.2888 -0.0446 0.0066  -0.0389 298 VAL A C   
4338 O O   . VAL A 298 ? 0.2300 0.1870 0.2985 -0.0499 0.0042  -0.0495 298 VAL A O   
4339 C CB  . VAL A 298 ? 0.2513 0.2307 0.2965 -0.0312 -0.0040 -0.0356 298 VAL A CB  
4340 C CG1 . VAL A 298 ? 0.2551 0.2467 0.3090 -0.0355 -0.0098 -0.0460 298 VAL A CG1 
4341 C CG2 . VAL A 298 ? 0.2491 0.2347 0.2968 -0.0318 0.0001  -0.0283 298 VAL A CG2 
4351 N N   . ASP A 299 ? 0.2205 0.1714 0.2824 -0.0483 0.0140  -0.0306 299 ASP A N   
4352 C CA  . ASP A 299 ? 0.2662 0.2110 0.3406 -0.0594 0.0214  -0.0323 299 ASP A CA  
4353 C C   . ASP A 299 ? 0.2745 0.2270 0.3503 -0.0626 0.0282  -0.0251 299 ASP A C   
4354 O O   . ASP A 299 ? 0.3960 0.3336 0.4645 -0.0650 0.0365  -0.0152 299 ASP A O   
4355 C CB  . ASP A 299 ? 0.2976 0.2153 0.3683 -0.0613 0.0270  -0.0280 299 ASP A CB  
4356 C CG  . ASP A 299 ? 0.4714 0.3810 0.5574 -0.0744 0.0338  -0.0334 299 ASP A CG  
4357 O OD1 . ASP A 299 ? 0.5176 0.4445 0.6194 -0.0820 0.0319  -0.0444 299 ASP A OD1 
4358 O OD2 . ASP A 299 ? 0.6031 0.4882 0.6857 -0.0772 0.0408  -0.0263 299 ASP A OD2 
4363 N N   . LEU A 300 ? 0.2528 0.2281 0.3373 -0.0623 0.0247  -0.0302 300 LEU A N   
4364 C CA  . LEU A 300 ? 0.2255 0.2114 0.3120 -0.0637 0.0309  -0.0255 300 LEU A CA  
4365 C C   . LEU A 300 ? 0.2755 0.2814 0.3858 -0.0717 0.0322  -0.0354 300 LEU A C   
4366 O O   . LEU A 300 ? 0.2663 0.2850 0.3879 -0.0712 0.0230  -0.0453 300 LEU A O   
4367 C CB  . LEU A 300 ? 0.2326 0.2287 0.3086 -0.0531 0.0250  -0.0225 300 LEU A CB  
4368 C CG  . LEU A 300 ? 0.2319 0.2137 0.2869 -0.0447 0.0230  -0.0136 300 LEU A CG  
4369 C CD1 . LEU A 300 ? 0.2410 0.2337 0.2887 -0.0362 0.0174  -0.0124 300 LEU A CD1 
4370 C CD2 . LEU A 300 ? 0.2758 0.2421 0.3203 -0.0479 0.0324  -0.0033 300 LEU A CD2 
4382 N N   . ASN A 301 ? 0.2025 0.2125 0.3205 -0.0791 0.0434  -0.0330 301 ASN A N   
4383 C CA  . ASN A 301 ? 0.1856 0.2196 0.3296 -0.0853 0.0449  -0.0430 301 ASN A CA  
4384 C C   . ASN A 301 ? 0.1668 0.2215 0.3137 -0.0749 0.0369  -0.0456 301 ASN A C   
4385 O O   . ASN A 301 ? 0.1642 0.2131 0.2925 -0.0648 0.0319  -0.0396 301 ASN A O   
4386 C CB  . ASN A 301 ? 0.2166 0.2494 0.3694 -0.0973 0.0611  -0.0405 301 ASN A CB  
4387 C CG  . ASN A 301 ? 0.2190 0.2501 0.3561 -0.0938 0.0700  -0.0310 301 ASN A CG  
4388 O OD1 . ASN A 301 ? 0.2083 0.2502 0.3401 -0.0839 0.0647  -0.0310 301 ASN A OD1 
4389 N ND2 . ASN A 301 ? 0.2840 0.3014 0.4139 -0.1032 0.0845  -0.0236 301 ASN A ND2 
4396 N N   . ASP A 302 ? 0.1775 0.2564 0.3497 -0.0775 0.0353  -0.0552 302 ASP A N   
4397 C CA  . ASP A 302 ? 0.2027 0.2995 0.3796 -0.0664 0.0254  -0.0582 302 ASP A CA  
4398 C C   . ASP A 302 ? 0.1768 0.2713 0.3409 -0.0601 0.0321  -0.0510 302 ASP A C   
4399 O O   . ASP A 302 ? 0.1825 0.2772 0.3358 -0.0493 0.0241  -0.0484 302 ASP A O   
4400 C CB  . ASP A 302 ? 0.2371 0.3617 0.4471 -0.0696 0.0229  -0.0699 302 ASP A CB  
4401 C CG  . ASP A 302 ? 0.3023 0.4346 0.5261 -0.0739 0.0118  -0.0795 302 ASP A CG  
4402 O OD1 . ASP A 302 ? 0.4275 0.5447 0.6338 -0.0722 0.0044  -0.0779 302 ASP A OD1 
4403 O OD2 . ASP A 302 ? 0.3876 0.5380 0.6337 -0.0770 0.0105  -0.0874 302 ASP A OD2 
4408 N N   . GLU A 303 ? 0.1791 0.2712 0.3436 -0.0674 0.0471  -0.0480 303 GLU A N   
4409 C CA  . GLU A 303 ? 0.1845 0.2751 0.3356 -0.0625 0.0543  -0.0426 303 GLU A CA  
4410 C C   . GLU A 303 ? 0.1790 0.2479 0.2988 -0.0561 0.0506  -0.0323 303 GLU A C   
4411 O O   . GLU A 303 ? 0.1793 0.2489 0.2885 -0.0471 0.0466  -0.0304 303 GLU A O   
4412 C CB  . GLU A 303 ? 0.2332 0.3244 0.3882 -0.0736 0.0723  -0.0415 303 GLU A CB  
4413 C CG  . GLU A 303 ? 0.2958 0.4129 0.4856 -0.0801 0.0783  -0.0530 303 GLU A CG  
4414 C CD  . GLU A 303 ? 0.4027 0.5280 0.6162 -0.0871 0.0719  -0.0610 303 GLU A CD  
4415 O OE1 . GLU A 303 ? 0.2897 0.3970 0.4948 -0.0951 0.0738  -0.0571 303 GLU A OE1 
4416 O OE2 . GLU A 303 ? 0.3532 0.5007 0.5909 -0.0833 0.0640  -0.0707 303 GLU A OE2 
4423 N N   . GLU A 304 ? 0.1628 0.2126 0.2697 -0.0604 0.0516  -0.0262 304 GLU A N   
4424 C CA  . GLU A 304 ? 0.1715 0.2026 0.2521 -0.0540 0.0476  -0.0170 304 GLU A CA  
4425 C C   . GLU A 304 ? 0.1699 0.2035 0.2479 -0.0444 0.0336  -0.0195 304 GLU A C   
4426 O O   . GLU A 304 ? 0.1721 0.1995 0.2337 -0.0371 0.0297  -0.0146 304 GLU A O   
4427 C CB  . GLU A 304 ? 0.2050 0.2150 0.2764 -0.0600 0.0513  -0.0108 304 GLU A CB  
4428 C CG  . GLU A 304 ? 0.3206 0.3208 0.3888 -0.0705 0.0658  -0.0050 304 GLU A CG  
4429 C CD  . GLU A 304 ? 0.5177 0.4946 0.5812 -0.0765 0.0681  0.0004  304 GLU A CD  
4430 O OE1 . GLU A 304 ? 0.4127 0.3876 0.4883 -0.0780 0.0619  -0.0061 304 GLU A OE1 
4431 O OE2 . GLU A 304 ? 0.5603 0.5195 0.6067 -0.0797 0.0764  0.0112  304 GLU A OE2 
4438 N N   . LEU A 305 ? 0.1464 0.1887 0.2396 -0.0451 0.0259  -0.0272 305 LEU A N   
4439 C CA  . LEU A 305 ? 0.1515 0.1959 0.2396 -0.0367 0.0135  -0.0289 305 LEU A CA  
4440 C C   . LEU A 305 ? 0.1537 0.2087 0.2421 -0.0288 0.0101  -0.0291 305 LEU A C   
4441 O O   . LEU A 305 ? 0.1528 0.2020 0.2271 -0.0218 0.0047  -0.0254 305 LEU A O   
4442 C CB  . LEU A 305 ? 0.1657 0.2183 0.2679 -0.0394 0.0056  -0.0375 305 LEU A CB  
4443 C CG  . LEU A 305 ? 0.1684 0.2216 0.2617 -0.0319 -0.0067 -0.0389 305 LEU A CG  
4444 C CD1 . LEU A 305 ? 0.2174 0.2536 0.2903 -0.0286 -0.0074 -0.0334 305 LEU A CD1 
4445 C CD2 . LEU A 305 ? 0.2137 0.2770 0.3199 -0.0354 -0.0148 -0.0483 305 LEU A CD2 
4457 N N   . ASN A 306 ? 0.1446 0.2150 0.2505 -0.0301 0.0140  -0.0339 306 ASN A N   
4458 C CA  . ASN A 306 ? 0.1733 0.2520 0.2812 -0.0221 0.0115  -0.0348 306 ASN A CA  
4459 C C   . ASN A 306 ? 0.1410 0.2085 0.2292 -0.0195 0.0175  -0.0285 306 ASN A C   
4460 O O   . ASN A 306 ? 0.1509 0.2165 0.2315 -0.0122 0.0125  -0.0272 306 ASN A O   
4461 C CB  . ASN A 306 ? 0.1957 0.2940 0.3289 -0.0236 0.0159  -0.0424 306 ASN A CB  
4462 C CG  . ASN A 306 ? 0.3033 0.4170 0.4557 -0.0190 0.0036  -0.0490 306 ASN A CG  
4463 O OD1 . ASN A 306 ? 0.2795 0.3895 0.4233 -0.0114 -0.0080 -0.0468 306 ASN A OD1 
4464 N ND2 . ASN A 306 ? 0.3688 0.5007 0.5477 -0.0237 0.0060  -0.0569 306 ASN A ND2 
4471 N N   . LYS A 307 ? 0.1292 0.1885 0.2080 -0.0259 0.0278  -0.0243 307 LYS A N   
4472 C CA  . LYS A 307 ? 0.1461 0.1953 0.2040 -0.0235 0.0318  -0.0184 307 LYS A CA  
4473 C C   . LYS A 307 ? 0.1487 0.1857 0.1902 -0.0185 0.0232  -0.0132 307 LYS A C   
4474 O O   . LYS A 307 ? 0.1568 0.1911 0.1873 -0.0134 0.0209  -0.0115 307 LYS A O   
4475 C CB  . LYS A 307 ? 0.1863 0.2280 0.2347 -0.0314 0.0436  -0.0136 307 LYS A CB  
4476 C CG  . LYS A 307 ? 0.1978 0.2518 0.2590 -0.0369 0.0553  -0.0187 307 LYS A CG  
4477 C CD  . LYS A 307 ? 0.2669 0.3107 0.3117 -0.0447 0.0679  -0.0120 307 LYS A CD  
4478 C CE  . LYS A 307 ? 0.3520 0.4098 0.4104 -0.0513 0.0818  -0.0180 307 LYS A CE  
4479 N NZ  . LYS A 307 ? 0.4245 0.4906 0.4783 -0.0457 0.0847  -0.0228 307 LYS A NZ  
4493 N N   . ARG A 308 ? 0.1384 0.1686 0.1795 -0.0201 0.0188  -0.0117 308 ARG A N   
4494 C CA  . ARG A 308 ? 0.1433 0.1638 0.1715 -0.0155 0.0118  -0.0080 308 ARG A CA  
4495 C C   . ARG A 308 ? 0.1404 0.1669 0.1705 -0.0093 0.0036  -0.0110 308 ARG A C   
4496 O O   . ARG A 308 ? 0.1440 0.1657 0.1629 -0.0051 0.0006  -0.0081 308 ARG A O   
4497 C CB  . ARG A 308 ? 0.1589 0.1717 0.1891 -0.0189 0.0104  -0.0080 308 ARG A CB  
4498 C CG  . ARG A 308 ? 0.1639 0.1673 0.1834 -0.0145 0.0049  -0.0054 308 ARG A CG  
4499 C CD  . ARG A 308 ? 0.1745 0.1672 0.1801 -0.0126 0.0075  0.0020  308 ARG A CD  
4500 N NE  . ARG A 308 ? 0.1724 0.1582 0.1723 -0.0082 0.0026  0.0032  308 ARG A NE  
4501 C CZ  . ARG A 308 ? 0.1737 0.1557 0.1638 -0.0036 0.0008  0.0078  308 ARG A CZ  
4502 N NH1 . ARG A 308 ? 0.1817 0.1639 0.1634 -0.0030 0.0028  0.0122  308 ARG A NH1 
4503 N NH2 . ARG A 308 ? 0.1809 0.1602 0.1702 0.0004  -0.0032 0.0070  308 ARG A NH2 
4517 N N   . VAL A 309 ? 0.1266 0.1635 0.1709 -0.0089 -0.0002 -0.0163 309 VAL A N   
4518 C CA  . VAL A 309 ? 0.1324 0.1733 0.1774 -0.0027 -0.0081 -0.0176 309 VAL A CA  
4519 C C   . VAL A 309 ? 0.1295 0.1703 0.1710 0.0014  -0.0057 -0.0166 309 VAL A C   
4520 O O   . VAL A 309 ? 0.1333 0.1685 0.1655 0.0053  -0.0096 -0.0142 309 VAL A O   
4521 C CB  . VAL A 309 ? 0.1327 0.1858 0.1943 -0.0022 -0.0138 -0.0232 309 VAL A CB  
4522 C CG1 . VAL A 309 ? 0.1369 0.1928 0.1990 0.0052  -0.0218 -0.0229 309 VAL A CG1 
4523 C CG2 . VAL A 309 ? 0.1501 0.2021 0.2121 -0.0061 -0.0180 -0.0255 309 VAL A CG2 
4533 N N   . ASP A 310 ? 0.1287 0.1757 0.1780 -0.0002 0.0014  -0.0192 310 ASP A N   
4534 C CA  . ASP A 310 ? 0.1290 0.1757 0.1750 0.0033  0.0046  -0.0202 310 ASP A CA  
4535 C C   . ASP A 310 ? 0.1340 0.1699 0.1608 0.0031  0.0054  -0.0157 310 ASP A C   
4536 O O   . ASP A 310 ? 0.1333 0.1657 0.1549 0.0068  0.0029  -0.0159 310 ASP A O   
4537 C CB  . ASP A 310 ? 0.1329 0.1879 0.1878 0.0002  0.0145  -0.0245 310 ASP A CB  
4538 C CG  . ASP A 310 ? 0.1608 0.2303 0.2396 0.0021  0.0140  -0.0311 310 ASP A CG  
4539 O OD1 . ASP A 310 ? 0.1704 0.2433 0.2581 0.0071  0.0042  -0.0320 310 ASP A OD1 
4540 O OD2 . ASP A 310 ? 0.1711 0.2498 0.2602 -0.0015 0.0235  -0.0355 310 ASP A OD2 
4545 N N   . TYR A 311 ? 0.1364 0.1668 0.1536 -0.0011 0.0086  -0.0116 311 TYR A N   
4546 C CA  . TYR A 311 ? 0.1412 0.1635 0.1419 -0.0006 0.0081  -0.0073 311 TYR A CA  
4547 C C   . TYR A 311 ? 0.1357 0.1540 0.1326 0.0028  0.0006  -0.0059 311 TYR A C   
4548 O O   . TYR A 311 ? 0.1412 0.1574 0.1313 0.0046  -0.0011 -0.0059 311 TYR A O   
4549 C CB  . TYR A 311 ? 0.1466 0.1629 0.1396 -0.0046 0.0117  -0.0022 311 TYR A CB  
4550 C CG  . TYR A 311 ? 0.1532 0.1620 0.1304 -0.0031 0.0095  0.0029  311 TYR A CG  
4551 C CD1 . TYR A 311 ? 0.1767 0.1863 0.1429 -0.0025 0.0110  0.0026  311 TYR A CD1 
4552 C CD2 . TYR A 311 ? 0.1820 0.1841 0.1564 -0.0019 0.0054  0.0070  311 TYR A CD2 
4553 C CE1 . TYR A 311 ? 0.1907 0.1959 0.1438 -0.0009 0.0073  0.0067  311 TYR A CE1 
4554 C CE2 . TYR A 311 ? 0.1952 0.1926 0.1582 0.0007  0.0022  0.0114  311 TYR A CE2 
4555 C CZ  . TYR A 311 ? 0.2001 0.1998 0.1525 0.0011  0.0026  0.0114  311 TYR A CZ  
4556 O OH  . TYR A 311 ? 0.2290 0.2263 0.1707 0.0039  -0.0021 0.0153  311 TYR A OH  
4566 N N   . LEU A 312 ? 0.1356 0.1531 0.1368 0.0027  -0.0033 -0.0053 312 LEU A N   
4567 C CA  . LEU A 312 ? 0.1323 0.1464 0.1289 0.0050  -0.0086 -0.0041 312 LEU A CA  
4568 C C   . LEU A 312 ? 0.1244 0.1397 0.1230 0.0079  -0.0118 -0.0057 312 LEU A C   
4569 O O   . LEU A 312 ? 0.1395 0.1512 0.1321 0.0089  -0.0133 -0.0045 312 LEU A O   
4570 C CB  . LEU A 312 ? 0.1494 0.1620 0.1481 0.0038  -0.0109 -0.0043 312 LEU A CB  
4571 C CG  . LEU A 312 ? 0.1441 0.1515 0.1408 0.0015  -0.0079 -0.0023 312 LEU A CG  
4572 C CD1 . LEU A 312 ? 0.1665 0.1721 0.1668 0.0001  -0.0101 -0.0048 312 LEU A CD1 
4573 C CD2 . LEU A 312 ? 0.1575 0.1603 0.1454 0.0036  -0.0080 0.0013  312 LEU A CD2 
4585 N N   . LEU A 313 ? 0.1292 0.1493 0.1375 0.0094  -0.0128 -0.0082 313 LEU A N   
4586 C CA  . LEU A 313 ? 0.1326 0.1512 0.1428 0.0133  -0.0161 -0.0087 313 LEU A CA  
4587 C C   . LEU A 313 ? 0.1176 0.1328 0.1244 0.0138  -0.0125 -0.0100 313 LEU A C   
4588 O O   . LEU A 313 ? 0.1461 0.1552 0.1494 0.0153  -0.0145 -0.0091 313 LEU A O   
4589 C CB  . LEU A 313 ? 0.1317 0.1572 0.1556 0.0163  -0.0187 -0.0115 313 LEU A CB  
4590 C CG  . LEU A 313 ? 0.1295 0.1588 0.1564 0.0165  -0.0251 -0.0111 313 LEU A CG  
4591 C CD1 . LEU A 313 ? 0.1645 0.2036 0.2080 0.0202  -0.0285 -0.0147 313 LEU A CD1 
4592 C CD2 . LEU A 313 ? 0.1597 0.1813 0.1744 0.0181  -0.0308 -0.0069 313 LEU A CD2 
4604 N N   . ALA A 314 ? 0.1327 0.1513 0.1396 0.0119  -0.0068 -0.0124 314 ALA A N   
4605 C CA  . ALA A 314 ? 0.1387 0.1547 0.1402 0.0117  -0.0036 -0.0151 314 ALA A CA  
4606 C C   . ALA A 314 ? 0.1334 0.1444 0.1244 0.0101  -0.0060 -0.0128 314 ALA A C   
4607 O O   . ALA A 314 ? 0.1405 0.1475 0.1299 0.0104  -0.0067 -0.0149 314 ALA A O   
4608 C CB  . ALA A 314 ? 0.1408 0.1617 0.1404 0.0092  0.0032  -0.0176 314 ALA A CB  
4614 N N   . ILE A 315 ? 0.1361 0.1475 0.1217 0.0084  -0.0072 -0.0090 315 ILE A N   
4615 C CA  . ILE A 315 ? 0.1374 0.1468 0.1169 0.0075  -0.0098 -0.0075 315 ILE A CA  
4616 C C   . ILE A 315 ? 0.1424 0.1480 0.1242 0.0078  -0.0122 -0.0073 315 ILE A C   
4617 O O   . ILE A 315 ? 0.1470 0.1506 0.1271 0.0063  -0.0125 -0.0089 315 ILE A O   
4618 C CB  . ILE A 315 ? 0.1424 0.1526 0.1193 0.0072  -0.0108 -0.0037 315 ILE A CB  
4619 C CG1 . ILE A 315 ? 0.1550 0.1658 0.1260 0.0064  -0.0085 -0.0021 315 ILE A CG1 
4620 C CG2 . ILE A 315 ? 0.1631 0.1738 0.1384 0.0071  -0.0136 -0.0031 315 ILE A CG2 
4621 C CD1 . ILE A 315 ? 0.1840 0.1921 0.1540 0.0066  -0.0089 0.0022  315 ILE A CD1 
4633 N N   . PHE A 316 ? 0.1331 0.1374 0.1179 0.0092  -0.0140 -0.0052 316 PHE A N   
4634 C CA  . PHE A 316 ? 0.1345 0.1333 0.1179 0.0094  -0.0160 -0.0033 316 PHE A CA  
4635 C C   . PHE A 316 ? 0.1396 0.1324 0.1254 0.0104  -0.0156 -0.0049 316 PHE A C   
4636 O O   . PHE A 316 ? 0.1502 0.1369 0.1333 0.0083  -0.0151 -0.0043 316 PHE A O   
4637 C CB  . PHE A 316 ? 0.1465 0.1455 0.1306 0.0112  -0.0192 -0.0010 316 PHE A CB  
4638 C CG  . PHE A 316 ? 0.1360 0.1279 0.1159 0.0122  -0.0219 0.0023  316 PHE A CG  
4639 C CD1 . PHE A 316 ? 0.1577 0.1456 0.1295 0.0090  -0.0205 0.0047  316 PHE A CD1 
4640 C CD2 . PHE A 316 ? 0.1592 0.1482 0.1429 0.0163  -0.0256 0.0035  316 PHE A CD2 
4641 C CE1 . PHE A 316 ? 0.1726 0.1519 0.1373 0.0090  -0.0219 0.0092  316 PHE A CE1 
4642 C CE2 . PHE A 316 ? 0.1682 0.1481 0.1451 0.0177  -0.0289 0.0085  316 PHE A CE2 
4643 C CZ  . PHE A 316 ? 0.1624 0.1364 0.1282 0.0135  -0.0266 0.0118  316 PHE A CZ  
4653 N N   . LEU A 317 ? 0.1403 0.1345 0.1326 0.0135  -0.0151 -0.0076 317 LEU A N   
4654 C CA  . LEU A 317 ? 0.1493 0.1364 0.1459 0.0159  -0.0147 -0.0099 317 LEU A CA  
4655 C C   . LEU A 317 ? 0.1493 0.1336 0.1433 0.0127  -0.0113 -0.0147 317 LEU A C   
4656 O O   . LEU A 317 ? 0.1621 0.1368 0.1578 0.0129  -0.0110 -0.0163 317 LEU A O   
4657 C CB  . LEU A 317 ? 0.1459 0.1376 0.1530 0.0206  -0.0143 -0.0131 317 LEU A CB  
4658 C CG  . LEU A 317 ? 0.1531 0.1472 0.1654 0.0245  -0.0198 -0.0093 317 LEU A CG  
4659 C CD1 . LEU A 317 ? 0.1837 0.1878 0.2107 0.0283  -0.0186 -0.0142 317 LEU A CD1 
4660 C CD2 . LEU A 317 ? 0.1737 0.1564 0.1836 0.0279  -0.0249 -0.0042 317 LEU A CD2 
4672 N N   . ILE A 318 ? 0.1488 0.1404 0.1382 0.0097  -0.0095 -0.0171 318 ILE A N   
4673 C CA  . ILE A 318 ? 0.1541 0.1451 0.1397 0.0061  -0.0081 -0.0222 318 ILE A CA  
4674 C C   . ILE A 318 ? 0.1402 0.1267 0.1248 0.0023  -0.0097 -0.0204 318 ILE A C   
4675 O O   . ILE A 318 ? 0.1672 0.1506 0.1522 -0.0012 -0.0089 -0.0254 318 ILE A O   
4676 C CB  . ILE A 318 ? 0.1524 0.1526 0.1312 0.0046  -0.0075 -0.0233 318 ILE A CB  
4677 C CG1 . ILE A 318 ? 0.1693 0.1728 0.1482 0.0065  -0.0033 -0.0265 318 ILE A CG1 
4678 C CG2 . ILE A 318 ? 0.1881 0.1909 0.1616 0.0009  -0.0090 -0.0273 318 ILE A CG2 
4679 C CD1 . ILE A 318 ? 0.2012 0.2011 0.1838 0.0076  0.0002  -0.0342 318 ILE A CD1 
4691 N N   . CYS A 319 ? 0.1514 0.1378 0.1351 0.0022  -0.0112 -0.0143 319 CYS A N   
4692 C CA  . CYS A 319 ? 0.1609 0.1446 0.1438 -0.0022 -0.0108 -0.0125 319 CYS A CA  
4693 C C   . CYS A 319 ? 0.1573 0.1282 0.1395 -0.0025 -0.0101 -0.0081 319 CYS A C   
4694 O O   . CYS A 319 ? 0.1850 0.1503 0.1671 -0.0077 -0.0078 -0.0080 319 CYS A O   
4695 C CB  . CYS A 319 ? 0.1602 0.1520 0.1412 -0.0026 -0.0116 -0.0092 319 CYS A CB  
4696 S SG  . CYS A 319 ? 0.1715 0.1755 0.1523 -0.0014 -0.0134 -0.0116 319 CYS A SG  
4702 N N   . ALA A 320 ? 0.1712 0.1286 0.1386 0.0211  -0.0141 -0.0107 320 ALA A N   
4703 C CA  . ALA A 320 ? 0.1787 0.1352 0.1493 0.0217  -0.0126 -0.0078 320 ALA A CA  
4704 C C   . ALA A 320 ? 0.1657 0.1147 0.1374 0.0223  -0.0120 -0.0086 320 ALA A C   
4705 O O   . ALA A 320 ? 0.1908 0.1369 0.1615 0.0239  -0.0125 -0.0115 320 ALA A O   
4706 C CB  . ALA A 320 ? 0.1855 0.1463 0.1553 0.0244  -0.0117 -0.0066 320 ALA A CB  
4712 N N   . GLU A 321 ? 0.1860 0.1304 0.1585 0.0211  -0.0104 -0.0058 321 GLU A N   
4713 C CA  . GLU A 321 ? 0.2003 0.1343 0.1714 0.0217  -0.0088 -0.0050 321 GLU A CA  
4714 C C   . GLU A 321 ? 0.1958 0.1253 0.1613 0.0238  -0.0074 -0.0001 321 GLU A C   
4715 O O   . GLU A 321 ? 0.2005 0.1366 0.1648 0.0246  -0.0082 0.0017  321 GLU A O   
4716 C CB  . GLU A 321 ? 0.1964 0.1256 0.1724 0.0166  -0.0069 -0.0072 321 GLU A CB  
4717 C CG  . GLU A 321 ? 0.2063 0.1389 0.1867 0.0156  -0.0099 -0.0131 321 GLU A CG  
4718 C CD  . GLU A 321 ? 0.2446 0.1721 0.2220 0.0190  -0.0111 -0.0155 321 GLU A CD  
4719 O OE1 . GLU A 321 ? 0.2714 0.1905 0.2458 0.0213  -0.0095 -0.0134 321 GLU A OE1 
4720 O OE2 . GLU A 321 ? 0.2443 0.1749 0.2213 0.0196  -0.0138 -0.0199 321 GLU A OE2 
4727 N N   . LYS A 322 ? 0.2182 0.1348 0.1786 0.0247  -0.0057 0.0022  322 LYS A N   
4728 C CA  . LYS A 322 ? 0.2295 0.1385 0.1807 0.0269  -0.0046 0.0072  322 LYS A CA  
4729 C C   . LYS A 322 ? 0.2216 0.1351 0.1734 0.0222  -0.0016 0.0088  322 LYS A C   
4730 O O   . LYS A 322 ? 0.2103 0.1255 0.1688 0.0162  0.0018  0.0068  322 LYS A O   
4731 C CB  . LYS A 322 ? 0.2414 0.1317 0.1849 0.0269  -0.0017 0.0099  322 LYS A CB  
4732 C CG  . LYS A 322 ? 0.3309 0.2095 0.2600 0.0312  -0.0018 0.0156  322 LYS A CG  
4733 C CD  . LYS A 322 ? 0.3674 0.2239 0.2853 0.0327  0.0005  0.0187  322 LYS A CD  
4734 C CE  . LYS A 322 ? 0.4373 0.2806 0.3372 0.0394  -0.0017 0.0245  322 LYS A CE  
4735 N NZ  . LYS A 322 ? 0.5160 0.3336 0.4015 0.0417  0.0002  0.0284  322 LYS A NZ  
4749 N N   . TYR A 323 ? 0.2094 0.1256 0.1552 0.0253  -0.0031 0.0115  323 TYR A N   
4750 C CA  . TYR A 323 ? 0.2082 0.1286 0.1532 0.0221  -0.0005 0.0127  323 TYR A CA  
4751 C C   . TYR A 323 ? 0.2000 0.1355 0.1554 0.0197  -0.0022 0.0092  323 TYR A C   
4752 O O   . TYR A 323 ? 0.1894 0.1289 0.1474 0.0162  0.0002  0.0088  323 TYR A O   
4753 C CB  . TYR A 323 ? 0.2237 0.1339 0.1654 0.0164  0.0067  0.0146  323 TYR A CB  
4754 C CG  . TYR A 323 ? 0.2605 0.1519 0.1882 0.0184  0.0093  0.0191  323 TYR A CG  
4755 C CD1 . TYR A 323 ? 0.2877 0.1714 0.2002 0.0245  0.0067  0.0233  323 TYR A CD1 
4756 C CD2 . TYR A 323 ? 0.3046 0.1839 0.2327 0.0144  0.0141  0.0190  323 TYR A CD2 
4757 C CE1 . TYR A 323 ? 0.3385 0.2013 0.2342 0.0273  0.0085  0.0282  323 TYR A CE1 
4758 C CE2 . TYR A 323 ? 0.3686 0.2268 0.2811 0.0161  0.0170  0.0239  323 TYR A CE2 
4759 C CZ  . TYR A 323 ? 0.3665 0.2158 0.2617 0.0230  0.0139  0.0288  323 TYR A CZ  
4760 O OH  . TYR A 323 ? 0.4444 0.2695 0.3207 0.0259  0.0160  0.0342  323 TYR A OH  
4770 N N   . SER A 324 ? 0.1833 0.1260 0.1438 0.0218  -0.0060 0.0065  324 SER A N   
4771 C CA  . SER A 324 ? 0.1614 0.1152 0.1273 0.0207  -0.0080 0.0041  324 SER A CA  
4772 C C   . SER A 324 ? 0.1620 0.1214 0.1258 0.0243  -0.0106 0.0045  324 SER A C   
4773 O O   . SER A 324 ? 0.1891 0.1479 0.1516 0.0284  -0.0125 0.0042  324 SER A O   
4774 C CB  . SER A 324 ? 0.1692 0.1254 0.1392 0.0203  -0.0096 0.0007  324 SER A CB  
4775 O OG  . SER A 324 ? 0.1725 0.1256 0.1465 0.0172  -0.0087 -0.0015 324 SER A OG  
4781 N N   . TYR A 325 ? 0.1647 0.1302 0.1298 0.0227  -0.0108 0.0043  325 TYR A N   
4782 C CA  . TYR A 325 ? 0.1641 0.1355 0.1289 0.0251  -0.0131 0.0038  325 TYR A CA  
4783 C C   . TYR A 325 ? 0.1622 0.1402 0.1312 0.0222  -0.0131 0.0018  325 TYR A C   
4784 O O   . TYR A 325 ? 0.1686 0.1458 0.1387 0.0194  -0.0121 0.0018  325 TYR A O   
4785 C CB  . TYR A 325 ? 0.1685 0.1370 0.1269 0.0263  -0.0132 0.0059  325 TYR A CB  
4786 C CG  . TYR A 325 ? 0.1813 0.1390 0.1310 0.0289  -0.0124 0.0090  325 TYR A CG  
4787 C CD1 . TYR A 325 ? 0.1826 0.1320 0.1294 0.0254  -0.0076 0.0110  325 TYR A CD1 
4788 C CD2 . TYR A 325 ? 0.2003 0.1549 0.1445 0.0348  -0.0163 0.0094  325 TYR A CD2 
4789 C CE1 . TYR A 325 ? 0.2062 0.1424 0.1428 0.0270  -0.0056 0.0144  325 TYR A CE1 
4790 C CE2 . TYR A 325 ? 0.2142 0.1552 0.1471 0.0379  -0.0159 0.0129  325 TYR A CE2 
4791 C CZ  . TYR A 325 ? 0.2078 0.1383 0.1357 0.0336  -0.0099 0.0159  325 TYR A CZ  
4792 O OH  . TYR A 325 ? 0.2366 0.1505 0.1514 0.0355  -0.0080 0.0199  325 TYR A OH  
4802 N N   . VAL A 326 ? 0.1567 0.1409 0.1287 0.0228  -0.0141 -0.0003 326 VAL A N   
4803 C CA  . VAL A 326 ? 0.1542 0.1415 0.1282 0.0196  -0.0131 -0.0018 326 VAL A CA  
4804 C C   . VAL A 326 ? 0.1422 0.1346 0.1183 0.0192  -0.0140 -0.0031 326 VAL A C   
4805 O O   . VAL A 326 ? 0.1561 0.1525 0.1341 0.0220  -0.0160 -0.0046 326 VAL A O   
4806 C CB  . VAL A 326 ? 0.1483 0.1369 0.1239 0.0190  -0.0112 -0.0038 326 VAL A CB  
4807 C CG1 . VAL A 326 ? 0.1638 0.1591 0.1449 0.0212  -0.0113 -0.0068 326 VAL A CG1 
4808 C CG2 . VAL A 326 ? 0.1667 0.1535 0.1397 0.0153  -0.0093 -0.0042 326 VAL A CG2 
4818 N N   . TYR A 327 ? 0.1489 0.1404 0.1244 0.0162  -0.0133 -0.0032 327 TYR A N   
4819 C CA  . TYR A 327 ? 0.1459 0.1414 0.1240 0.0149  -0.0137 -0.0053 327 TYR A CA  
4820 C C   . TYR A 327 ? 0.1490 0.1420 0.1268 0.0108  -0.0112 -0.0060 327 TYR A C   
4821 O O   . TYR A 327 ? 0.1636 0.1503 0.1370 0.0098  -0.0114 -0.0044 327 TYR A O   
4822 C CB  . TYR A 327 ? 0.1760 0.1699 0.1514 0.0155  -0.0151 -0.0044 327 TYR A CB  
4823 C CG  . TYR A 327 ? 0.1873 0.1843 0.1645 0.0145  -0.0162 -0.0069 327 TYR A CG  
4824 C CD1 . TYR A 327 ? 0.1898 0.1931 0.1721 0.0145  -0.0175 -0.0104 327 TYR A CD1 
4825 C CD2 . TYR A 327 ? 0.2269 0.2208 0.2017 0.0139  -0.0163 -0.0066 327 TYR A CD2 
4826 C CE1 . TYR A 327 ? 0.2142 0.2202 0.1983 0.0137  -0.0193 -0.0137 327 TYR A CE1 
4827 C CE2 . TYR A 327 ? 0.2316 0.2273 0.2073 0.0132  -0.0175 -0.0093 327 TYR A CE2 
4828 C CZ  . TYR A 327 ? 0.1636 0.1650 0.1435 0.0130  -0.0190 -0.0127 327 TYR A CZ  
4829 O OH  . TYR A 327 ? 0.2373 0.2403 0.2183 0.0123  -0.0207 -0.0162 327 TYR A OH  
4839 N N   . LEU A 328 ? 0.1530 0.1503 0.1355 0.0088  -0.0088 -0.0089 328 LEU A N   
4840 C CA  . LEU A 328 ? 0.1537 0.1471 0.1348 0.0038  -0.0047 -0.0098 328 LEU A CA  
4841 C C   . LEU A 328 ? 0.1610 0.1570 0.1464 0.0017  -0.0055 -0.0124 328 LEU A C   
4842 O O   . LEU A 328 ? 0.1815 0.1870 0.1760 0.0019  -0.0064 -0.0166 328 LEU A O   
4843 C CB  . LEU A 328 ? 0.1666 0.1640 0.1520 0.0015  0.0002  -0.0127 328 LEU A CB  
4844 C CG  . LEU A 328 ? 0.2042 0.2005 0.1867 0.0041  0.0008  -0.0117 328 LEU A CG  
4845 C CD1 . LEU A 328 ? 0.2002 0.1993 0.1860 0.0006  0.0075  -0.0153 328 LEU A CD1 
4846 C CD2 . LEU A 328 ? 0.2054 0.1911 0.1767 0.0052  -0.0009 -0.0074 328 LEU A CD2 
4858 N N   . HIS A 329 ? 0.1617 0.1495 0.1413 0.0002  -0.0058 -0.0106 329 HIS A N   
4859 C CA  . HIS A 329 ? 0.1477 0.1373 0.1308 -0.0007 -0.0075 -0.0131 329 HIS A CA  
4860 C C   . HIS A 329 ? 0.1573 0.1378 0.1372 -0.0057 -0.0041 -0.0135 329 HIS A C   
4861 O O   . HIS A 329 ? 0.1694 0.1391 0.1406 -0.0075 -0.0013 -0.0105 329 HIS A O   
4862 C CB  . HIS A 329 ? 0.1625 0.1506 0.1419 0.0034  -0.0117 -0.0112 329 HIS A CB  
4863 C CG  . HIS A 329 ? 0.1683 0.1465 0.1406 0.0041  -0.0121 -0.0081 329 HIS A CG  
4864 N ND1 . HIS A 329 ? 0.1795 0.1495 0.1484 0.0025  -0.0122 -0.0084 329 HIS A ND1 
4865 C CD2 . HIS A 329 ? 0.1674 0.1423 0.1359 0.0065  -0.0132 -0.0055 329 HIS A CD2 
4866 C CE1 . HIS A 329 ? 0.1865 0.1488 0.1495 0.0049  -0.0141 -0.0061 329 HIS A CE1 
4867 N NE2 . HIS A 329 ? 0.1819 0.1478 0.1452 0.0071  -0.0148 -0.0046 329 HIS A NE2 
4875 N N   . ASP A 330 ? 0.1636 0.1473 0.1495 -0.0079 -0.0047 -0.0174 330 ASP A N   
4876 C CA  . ASP A 330 ? 0.1838 0.1574 0.1667 -0.0124 -0.0022 -0.0182 330 ASP A CA  
4877 C C   . ASP A 330 ? 0.1741 0.1459 0.1555 -0.0091 -0.0072 -0.0188 330 ASP A C   
4878 O O   . ASP A 330 ? 0.1861 0.1597 0.1727 -0.0113 -0.0078 -0.0232 330 ASP A O   
4879 C CB  . ASP A 330 ? 0.1837 0.1636 0.1775 -0.0187 0.0020  -0.0241 330 ASP A CB  
4880 C CG  . ASP A 330 ? 0.1952 0.1622 0.1855 -0.0249 0.0063  -0.0249 330 ASP A CG  
4881 O OD1 . ASP A 330 ? 0.2057 0.1561 0.1823 -0.0246 0.0072  -0.0197 330 ASP A OD1 
4882 O OD2 . ASP A 330 ? 0.1968 0.1697 0.1982 -0.0301 0.0086  -0.0311 330 ASP A OD2 
4887 N N   . GLY A 331 ? 0.1784 0.1473 0.1539 -0.0041 -0.0104 -0.0152 331 GLY A N   
4888 C CA  . GLY A 331 ? 0.1767 0.1456 0.1518 -0.0006 -0.0141 -0.0164 331 GLY A CA  
4889 C C   . GLY A 331 ? 0.1725 0.1533 0.1519 0.0025  -0.0165 -0.0185 331 GLY A C   
4890 O O   . GLY A 331 ? 0.1825 0.1714 0.1663 0.0021  -0.0165 -0.0199 331 GLY A O   
4894 N N   . TYR A 332 ? 0.1691 0.1500 0.1465 0.0059  -0.0186 -0.0191 332 TYR A N   
4895 C CA  . TYR A 332 ? 0.1786 0.1669 0.1554 0.0091  -0.0200 -0.0199 332 TYR A CA  
4896 C C   . TYR A 332 ? 0.1922 0.1841 0.1698 0.0094  -0.0222 -0.0250 332 TYR A C   
4897 O O   . TYR A 332 ? 0.2074 0.2036 0.1813 0.0126  -0.0239 -0.0258 332 TYR A O   
4898 C CB  . TYR A 332 ? 0.1847 0.1714 0.1584 0.0122  -0.0193 -0.0180 332 TYR A CB  
4899 C CG  . TYR A 332 ? 0.1715 0.1557 0.1452 0.0124  -0.0182 -0.0141 332 TYR A CG  
4900 C CD1 . TYR A 332 ? 0.1883 0.1734 0.1624 0.0112  -0.0176 -0.0119 332 TYR A CD1 
4901 C CD2 . TYR A 332 ? 0.1804 0.1625 0.1551 0.0142  -0.0181 -0.0139 332 TYR A CD2 
4902 C CE1 . TYR A 332 ? 0.1799 0.1624 0.1532 0.0116  -0.0171 -0.0090 332 TYR A CE1 
4903 C CE2 . TYR A 332 ? 0.1813 0.1620 0.1568 0.0147  -0.0181 -0.0116 332 TYR A CE2 
4904 C CZ  . TYR A 332 ? 0.1758 0.1561 0.1497 0.0134  -0.0178 -0.0090 332 TYR A CZ  
4905 O OH  . TYR A 332 ? 0.1905 0.1689 0.1642 0.0140  -0.0182 -0.0073 332 TYR A OH  
4915 N N   . LEU A 333 ? 0.1766 0.1652 0.1573 0.0063  -0.0224 -0.0284 333 LEU A N   
4916 C CA  . LEU A 333 ? 0.1659 0.1581 0.1485 0.0062  -0.0251 -0.0345 333 LEU A CA  
4917 C C   . LEU A 333 ? 0.1580 0.1582 0.1481 0.0039  -0.0266 -0.0381 333 LEU A C   
4918 O O   . LEU A 333 ? 0.1755 0.1745 0.1722 -0.0013 -0.0238 -0.0389 333 LEU A O   
4919 C CB  . LEU A 333 ? 0.1869 0.1711 0.1703 0.0038  -0.0245 -0.0374 333 LEU A CB  
4920 C CG  . LEU A 333 ? 0.1764 0.1635 0.1627 0.0029  -0.0274 -0.0448 333 LEU A CG  
4921 C CD1 . LEU A 333 ? 0.1971 0.1899 0.1772 0.0083  -0.0306 -0.0471 333 LEU A CD1 
4922 C CD2 . LEU A 333 ? 0.2189 0.1954 0.2052 0.0007  -0.0264 -0.0471 333 LEU A CD2 
4934 N N   . ALA A 334 ? 0.1644 0.1723 0.1534 0.0079  -0.0308 -0.0407 334 ALA A N   
4935 C CA  . ALA A 334 ? 0.1762 0.1937 0.1739 0.0075  -0.0335 -0.0448 334 ALA A CA  
4936 C C   . ALA A 334 ? 0.1825 0.2030 0.1924 0.0014  -0.0329 -0.0519 334 ALA A C   
4937 O O   . ALA A 334 ? 0.1904 0.2166 0.2112 -0.0025 -0.0307 -0.0542 334 ALA A O   
4938 C CB  . ALA A 334 ? 0.1812 0.2041 0.1731 0.0142  -0.0401 -0.0473 334 ALA A CB  
4944 N N   . THR A 335 ? 0.1737 0.1904 0.1826 0.0001  -0.0342 -0.0560 335 THR A N   
4945 C CA  . THR A 335 ? 0.1907 0.2100 0.2114 -0.0058 -0.0341 -0.0641 335 THR A CA  
4946 C C   . THR A 335 ? 0.1934 0.2030 0.2177 -0.0137 -0.0264 -0.0617 335 THR A C   
4947 O O   . THR A 335 ? 0.2226 0.2329 0.2575 -0.0204 -0.0243 -0.0681 335 THR A O   
4948 C CB  . THR A 335 ? 0.1807 0.1981 0.1977 -0.0039 -0.0386 -0.0698 335 THR A CB  
4949 O OG1 . THR A 335 ? 0.2095 0.2159 0.2143 -0.0015 -0.0365 -0.0643 335 THR A OG1 
4950 C CG2 . THR A 335 ? 0.2190 0.2461 0.2331 0.0029  -0.0468 -0.0745 335 THR A CG2 
4958 N N   . ASN A 336 ? 0.1823 0.1822 0.1976 -0.0133 -0.0222 -0.0532 336 ASN A N   
4959 C CA  . ASN A 336 ? 0.1885 0.1762 0.2026 -0.0197 -0.0154 -0.0499 336 ASN A CA  
4960 C C   . ASN A 336 ? 0.2078 0.1963 0.2214 -0.0209 -0.0110 -0.0449 336 ASN A C   
4961 O O   . ASN A 336 ? 0.2203 0.1960 0.2273 -0.0246 -0.0055 -0.0402 336 ASN A O   
4962 C CB  . ASN A 336 ? 0.2090 0.1814 0.2114 -0.0176 -0.0152 -0.0453 336 ASN A CB  
4963 C CG  . ASN A 336 ? 0.2168 0.1726 0.2158 -0.0241 -0.0095 -0.0436 336 ASN A CG  
4964 O OD1 . ASN A 336 ? 0.2465 0.2020 0.2534 -0.0315 -0.0055 -0.0483 336 ASN A OD1 
4965 N ND2 . ASN A 336 ? 0.2603 0.2017 0.2475 -0.0212 -0.0094 -0.0377 336 ASN A ND2 
4972 N N   . SER A 337 ? 0.1768 0.1786 0.1955 -0.0174 -0.0135 -0.0458 337 SER A N   
4973 C CA  . SER A 337 ? 0.1796 0.1829 0.1974 -0.0173 -0.0100 -0.0415 337 SER A CA  
4974 C C   . SER A 337 ? 0.2000 0.2145 0.2325 -0.0220 -0.0069 -0.0478 337 SER A C   
4975 O O   . SER A 337 ? 0.2051 0.2334 0.2488 -0.0198 -0.0119 -0.0548 337 SER A O   
4976 C CB  . SER A 337 ? 0.1798 0.1890 0.1928 -0.0094 -0.0150 -0.0380 337 SER A CB  
4977 O OG  . SER A 337 ? 0.1823 0.1953 0.1977 -0.0095 -0.0121 -0.0360 337 SER A OG  
4983 N N   . ALA A 338 ? 0.1929 0.2019 0.2251 -0.0276 0.0012  -0.0457 338 ALA A N   
4984 C CA  . ALA A 338 ? 0.2062 0.2266 0.2537 -0.0327 0.0062  -0.0523 338 ALA A CA  
4985 C C   . ALA A 338 ? 0.2038 0.2383 0.2575 -0.0264 0.0023  -0.0535 338 ALA A C   
4986 O O   . ALA A 338 ? 0.2675 0.3157 0.3379 -0.0288 0.0041  -0.0612 338 ALA A O   
4987 C CB  . ALA A 338 ? 0.2551 0.2625 0.2963 -0.0406 0.0173  -0.0488 338 ALA A CB  
4993 N N   . VAL A 339 ? 0.1707 0.2022 0.2129 -0.0187 -0.0026 -0.0468 339 VAL A N   
4994 C CA  . VAL A 339 ? 0.2050 0.2463 0.2507 -0.0125 -0.0061 -0.0471 339 VAL A CA  
4995 C C   . VAL A 339 ? 0.1894 0.2369 0.2339 -0.0041 -0.0162 -0.0483 339 VAL A C   
4996 O O   . VAL A 339 ? 0.2034 0.2576 0.2499 0.0021  -0.0203 -0.0488 339 VAL A O   
4997 C CB  . VAL A 339 ? 0.2112 0.2432 0.2448 -0.0111 -0.0025 -0.0392 339 VAL A CB  
4998 C CG1 . VAL A 339 ? 0.2309 0.2554 0.2631 -0.0192 0.0077  -0.0385 339 VAL A CG1 
4999 C CG2 . VAL A 339 ? 0.2077 0.2283 0.2259 -0.0072 -0.0060 -0.0316 339 VAL A CG2 
5009 N N   . TRP A 340 ? 0.2049 0.2493 0.2451 -0.0033 -0.0203 -0.0491 340 TRP A N   
5010 C CA  . TRP A 340 ? 0.2079 0.2566 0.2443 0.0045  -0.0293 -0.0507 340 TRP A CA  
5011 C C   . TRP A 340 ? 0.1823 0.2462 0.2335 0.0075  -0.0348 -0.0597 340 TRP A C   
5012 O O   . TRP A 340 ? 0.2030 0.2760 0.2705 0.0020  -0.0327 -0.0678 340 TRP A O   
5013 C CB  . TRP A 340 ? 0.2375 0.2811 0.2686 0.0035  -0.0316 -0.0520 340 TRP A CB  
5014 C CG  . TRP A 340 ? 0.2013 0.2481 0.2266 0.0108  -0.0403 -0.0547 340 TRP A CG  
5015 C CD1 . TRP A 340 ? 0.2291 0.2829 0.2607 0.0116  -0.0462 -0.0633 340 TRP A CD1 
5016 C CD2 . TRP A 340 ? 0.1909 0.2318 0.2005 0.0181  -0.0436 -0.0488 340 TRP A CD2 
5017 N NE1 . TRP A 340 ? 0.2134 0.2656 0.2324 0.0198  -0.0537 -0.0629 340 TRP A NE1 
5018 C CE2 . TRP A 340 ? 0.2036 0.2472 0.2085 0.0234  -0.0514 -0.0537 340 TRP A CE2 
5019 C CE3 . TRP A 340 ? 0.2074 0.2407 0.2066 0.0202  -0.0404 -0.0403 340 TRP A CE3 
5020 C CZ2 . TRP A 340 ? 0.2220 0.2589 0.2094 0.0307  -0.0553 -0.0495 340 TRP A CZ2 
5021 C CZ3 . TRP A 340 ? 0.2293 0.2569 0.2139 0.0265  -0.0436 -0.0366 340 TRP A CZ3 
5022 C CH2 . TRP A 340 ? 0.2236 0.2522 0.2012 0.0317  -0.0506 -0.0408 340 TRP A CH2 
5033 N N   . LEU A 341 ? 0.2130 0.2792 0.2587 0.0163  -0.0418 -0.0586 341 LEU A N   
5034 C CA  . LEU A 341 ? 0.2295 0.3090 0.2870 0.0223  -0.0493 -0.0667 341 LEU A CA  
5035 C C   . LEU A 341 ? 0.2618 0.3506 0.3349 0.0200  -0.0446 -0.0702 341 LEU A C   
5036 O O   . LEU A 341 ? 0.3358 0.4377 0.4224 0.0251  -0.0509 -0.0784 341 LEU A O   
5037 C CB  . LEU A 341 ? 0.2444 0.3344 0.3137 0.0220  -0.0558 -0.0776 341 LEU A CB  
5038 C CG  . LEU A 341 ? 0.2515 0.3339 0.3041 0.0274  -0.0632 -0.0760 341 LEU A CG  
5039 C CD1 . LEU A 341 ? 0.2765 0.3669 0.3397 0.0249  -0.0678 -0.0866 341 LEU A CD1 
5040 C CD2 . LEU A 341 ? 0.3431 0.4237 0.3837 0.0392  -0.0727 -0.0743 341 LEU A CD2 
5052 N N   . HIS A 342 ? 0.2298 0.3125 0.3013 0.0134  -0.0344 -0.0648 342 HIS A N   
5053 C CA  . HIS A 342 ? 0.2112 0.3023 0.2970 0.0101  -0.0281 -0.0689 342 HIS A CA  
5054 C C   . HIS A 342 ? 0.2213 0.3070 0.2979 0.0157  -0.0279 -0.0624 342 HIS A C   
5055 O O   . HIS A 342 ? 0.3819 0.4537 0.4408 0.0167  -0.0267 -0.0528 342 HIS A O   
5056 C CB  . HIS A 342 ? 0.2863 0.3719 0.3740 -0.0015 -0.0160 -0.0677 342 HIS A CB  
5057 C CG  . HIS A 342 ? 0.3372 0.4298 0.4374 -0.0062 -0.0071 -0.0718 342 HIS A CG  
5058 N ND1 . HIS A 342 ? 0.3637 0.4744 0.4876 -0.0078 -0.0067 -0.0840 342 HIS A ND1 
5059 C CD2 . HIS A 342 ? 0.3157 0.3999 0.4080 -0.0099 0.0019  -0.0664 342 HIS A CD2 
5060 C CE1 . HIS A 342 ? 0.3286 0.4420 0.4591 -0.0126 0.0034  -0.0857 342 HIS A CE1 
5061 N NE2 . HIS A 342 ? 0.3153 0.4119 0.4255 -0.0138 0.0087  -0.0748 342 HIS A NE2 
5069 N N   . GLN A 343 ? 0.1922 0.2891 0.2821 0.0191  -0.0287 -0.0685 343 GLN A N   
5070 C CA  . GLN A 343 ? 0.2218 0.3138 0.3050 0.0238  -0.0277 -0.0637 343 GLN A CA  
5071 C C   . GLN A 343 ? 0.2243 0.3215 0.3185 0.0169  -0.0168 -0.0671 343 GLN A C   
5072 O O   . GLN A 343 ? 0.2512 0.3640 0.3661 0.0155  -0.0151 -0.0776 343 GLN A O   
5073 C CB  . GLN A 343 ? 0.3127 0.4105 0.3988 0.0355  -0.0387 -0.0673 343 GLN A CB  
5074 C CG  . GLN A 343 ? 0.3846 0.4776 0.4662 0.0405  -0.0377 -0.0639 343 GLN A CG  
5075 C CD  . GLN A 343 ? 0.4639 0.5453 0.5285 0.0508  -0.0470 -0.0577 343 GLN A CD  
5076 O OE1 . GLN A 343 ? 0.4483 0.5142 0.4947 0.0499  -0.0445 -0.0479 343 GLN A OE1 
5077 N NE2 . GLN A 343 ? 0.4738 0.5617 0.5438 0.0606  -0.0576 -0.0639 343 GLN A NE2 
5086 N N   . PHE A 344 ? 0.1671 0.2513 0.2474 0.0127  -0.0093 -0.0591 344 PHE A N   
5087 C CA  . PHE A 344 ? 0.1637 0.2494 0.2490 0.0070  0.0014  -0.0612 344 PHE A CA  
5088 C C   . PHE A 344 ? 0.1447 0.2391 0.2390 0.0140  -0.0007 -0.0659 344 PHE A C   
5089 O O   . PHE A 344 ? 0.1551 0.2460 0.2428 0.0231  -0.0093 -0.0627 344 PHE A O   
5090 C CB  . PHE A 344 ? 0.1735 0.2416 0.2387 0.0029  0.0076  -0.0514 344 PHE A CB  
5091 C CG  . PHE A 344 ? 0.2110 0.2698 0.2684 -0.0046 0.0116  -0.0479 344 PHE A CG  
5092 C CD1 . PHE A 344 ? 0.1914 0.2522 0.2561 -0.0137 0.0209  -0.0525 344 PHE A CD1 
5093 C CD2 . PHE A 344 ? 0.2814 0.3287 0.3243 -0.0028 0.0066  -0.0404 344 PHE A CD2 
5094 C CE1 . PHE A 344 ? 0.2343 0.2843 0.2909 -0.0202 0.0243  -0.0492 344 PHE A CE1 
5095 C CE2 . PHE A 344 ? 0.2625 0.3008 0.2988 -0.0088 0.0096  -0.0378 344 PHE A CE2 
5096 C CZ  . PHE A 344 ? 0.2300 0.2688 0.2724 -0.0172 0.0181  -0.0420 344 PHE A CZ  
5106 N N   . ASP A 345 ? 0.1492 0.2533 0.2574 0.0095  0.0082  -0.0733 345 ASP A N   
5107 C CA  . ASP A 345 ? 0.1783 0.2913 0.2967 0.0161  0.0071  -0.0789 345 ASP A CA  
5108 C C   . ASP A 345 ? 0.1587 0.2566 0.2579 0.0209  0.0058  -0.0699 345 ASP A C   
5109 O O   . ASP A 345 ? 0.1705 0.2704 0.2719 0.0300  -0.0007 -0.0714 345 ASP A O   
5110 C CB  . ASP A 345 ? 0.1915 0.3160 0.3264 0.0089  0.0197  -0.0881 345 ASP A CB  
5111 C CG  . ASP A 345 ? 0.2982 0.4416 0.4586 0.0048  0.0206  -0.1002 345 ASP A CG  
5112 O OD1 . ASP A 345 ? 0.3086 0.4598 0.4770 0.0109  0.0087  -0.1036 345 ASP A OD1 
5113 O OD2 . ASP A 345 ? 0.4108 0.5612 0.5831 -0.0047 0.0337  -0.1069 345 ASP A OD2 
5118 N N   . GLN A 346 ? 0.1454 0.2277 0.2258 0.0151  0.0114  -0.0610 346 GLN A N   
5119 C CA  . GLN A 346 ? 0.1663 0.2345 0.2294 0.0184  0.0103  -0.0533 346 GLN A CA  
5120 C C   . GLN A 346 ? 0.1620 0.2240 0.2173 0.0266  -0.0008 -0.0480 346 GLN A C   
5121 O O   . GLN A 346 ? 0.2229 0.2750 0.2676 0.0303  -0.0026 -0.0433 346 GLN A O   
5122 C CB  . GLN A 346 ? 0.1607 0.2141 0.2062 0.0111  0.0163  -0.0458 346 GLN A CB  
5123 C CG  . GLN A 346 ? 0.1650 0.2176 0.2100 0.0028  0.0288  -0.0487 346 GLN A CG  
5124 C CD  . GLN A 346 ? 0.1666 0.2236 0.2193 -0.0052 0.0344  -0.0520 346 GLN A CD  
5125 O OE1 . GLN A 346 ? 0.1819 0.2496 0.2483 -0.0041 0.0293  -0.0562 346 GLN A OE1 
5126 N NE2 . GLN A 346 ? 0.2056 0.2533 0.2486 -0.0135 0.0453  -0.0506 346 GLN A NE2 
5135 N N   . TYR A 347 ? 0.1457 0.2117 0.2045 0.0289  -0.0078 -0.0486 347 TYR A N   
5136 C CA  . TYR A 347 ? 0.1595 0.2183 0.2089 0.0364  -0.0173 -0.0437 347 TYR A CA  
5137 C C   . TYR A 347 ? 0.1769 0.2425 0.2349 0.0464  -0.0250 -0.0492 347 TYR A C   
5138 O O   . TYR A 347 ? 0.2072 0.2629 0.2541 0.0535  -0.0321 -0.0446 347 TYR A O   
5139 C CB  . TYR A 347 ? 0.1656 0.2239 0.2118 0.0350  -0.0213 -0.0420 347 TYR A CB  
5140 C CG  . TYR A 347 ? 0.1656 0.2158 0.2025 0.0270  -0.0158 -0.0366 347 TYR A CG  
5141 C CD1 . TYR A 347 ? 0.1762 0.2176 0.2047 0.0223  -0.0091 -0.0321 347 TYR A CD1 
5142 C CD2 . TYR A 347 ? 0.1664 0.2169 0.2020 0.0250  -0.0185 -0.0362 347 TYR A CD2 
5143 C CE1 . TYR A 347 ? 0.1750 0.2082 0.1945 0.0166  -0.0060 -0.0275 347 TYR A CE1 
5144 C CE2 . TYR A 347 ? 0.1931 0.2358 0.2207 0.0190  -0.0145 -0.0318 347 TYR A CE2 
5145 C CZ  . TYR A 347 ? 0.1992 0.2333 0.2190 0.0150  -0.0086 -0.0274 347 TYR A CZ  
5146 O OH  . TYR A 347 ? 0.2333 0.2586 0.2445 0.0102  -0.0059 -0.0232 347 TYR A OH  
5156 N N   . LYS A 348 ? 0.1596 0.2407 0.2366 0.0471  -0.0235 -0.0592 348 LYS A N   
5157 C CA  . LYS A 348 ? 0.1693 0.2588 0.2573 0.0577  -0.0323 -0.0662 348 LYS A CA  
5158 C C   . LYS A 348 ? 0.1951 0.2843 0.2866 0.0617  -0.0296 -0.0688 348 LYS A C   
5159 O O   . LYS A 348 ? 0.2274 0.3169 0.3216 0.0724  -0.0380 -0.0718 348 LYS A O   
5160 C CB  . LYS A 348 ? 0.2050 0.3154 0.3167 0.0571  -0.0337 -0.0784 348 LYS A CB  
5161 C CG  . LYS A 348 ? 0.2751 0.3884 0.3870 0.0542  -0.0378 -0.0788 348 LYS A CG  
5162 C CD  . LYS A 348 ? 0.3215 0.4566 0.4603 0.0503  -0.0356 -0.0922 348 LYS A CD  
5163 C CE  . LYS A 348 ? 0.3761 0.5126 0.5155 0.0420  -0.0337 -0.0923 348 LYS A CE  
5164 N NZ  . LYS A 348 ? 0.4187 0.5766 0.5861 0.0376  -0.0316 -0.1063 348 LYS A NZ  
5178 N N   . LYS A 349 ? 0.1674 0.2547 0.2574 0.0541  -0.0185 -0.0677 349 LYS A N   
5179 C CA  . LYS A 349 ? 0.1771 0.2651 0.2711 0.0571  -0.0147 -0.0715 349 LYS A CA  
5180 C C   . LYS A 349 ? 0.1752 0.2451 0.2514 0.0630  -0.0195 -0.0633 349 LYS A C   
5181 O O   . LYS A 349 ? 0.1872 0.2429 0.2463 0.0603  -0.0206 -0.0538 349 LYS A O   
5182 C CB  . LYS A 349 ? 0.1835 0.2723 0.2770 0.0466  -0.0011 -0.0722 349 LYS A CB  
5183 C CG  . LYS A 349 ? 0.2062 0.3141 0.3215 0.0417  0.0061  -0.0833 349 LYS A CG  
5184 C CD  . LYS A 349 ? 0.1926 0.2976 0.3027 0.0292  0.0205  -0.0823 349 LYS A CD  
5185 C CE  . LYS A 349 ? 0.1987 0.3223 0.3316 0.0230  0.0284  -0.0935 349 LYS A CE  
5186 N NZ  . LYS A 349 ? 0.2592 0.3777 0.3853 0.0116  0.0445  -0.0932 349 LYS A NZ  
5200 N N   . ALA A 350 ? 0.1892 0.2593 0.2702 0.0707  -0.0218 -0.0678 350 ALA A N   
5201 C CA  . ALA A 350 ? 0.1934 0.2453 0.2587 0.0758  -0.0256 -0.0610 350 ALA A CA  
5202 C C   . ALA A 350 ? 0.2060 0.2462 0.2573 0.0674  -0.0175 -0.0544 350 ALA A C   
5203 O O   . ALA A 350 ? 0.2062 0.2516 0.2610 0.0616  -0.0086 -0.0580 350 ALA A O   
5204 C CB  . ALA A 350 ? 0.2235 0.2781 0.2980 0.0854  -0.0287 -0.0683 350 ALA A CB  
5210 N N   . LEU A 351 ? 0.1862 0.2101 0.2211 0.0671  -0.0206 -0.0453 351 LEU A N   
5211 C CA  . LEU A 351 ? 0.1802 0.1932 0.2027 0.0600  -0.0151 -0.0396 351 LEU A CA  
5212 C C   . LEU A 351 ? 0.1951 0.1950 0.2106 0.0644  -0.0167 -0.0383 351 LEU A C   
5213 O O   . LEU A 351 ? 0.2134 0.2133 0.2298 0.0632  -0.0120 -0.0421 351 LEU A O   
5214 C CB  . LEU A 351 ? 0.1920 0.1984 0.2045 0.0555  -0.0166 -0.0318 351 LEU A CB  
5215 C CG  . LEU A 351 ? 0.1695 0.1644 0.1701 0.0496  -0.0134 -0.0261 351 LEU A CG  
5216 C CD1 . LEU A 351 ? 0.2007 0.1995 0.2013 0.0437  -0.0065 -0.0287 351 LEU A CD1 
5217 C CD2 . LEU A 351 ? 0.1989 0.1898 0.1928 0.0461  -0.0150 -0.0200 351 LEU A CD2 
5229 N N   . GLY A 352 ? 0.2020 0.1896 0.2098 0.0696  -0.0229 -0.0336 352 GLY A N   
5230 C CA  . GLY A 352 ? 0.2301 0.2028 0.2308 0.0731  -0.0243 -0.0321 352 GLY A CA  
5231 C C   . GLY A 352 ? 0.1947 0.1557 0.1847 0.0659  -0.0208 -0.0265 352 GLY A C   
5232 O O   . GLY A 352 ? 0.2107 0.1758 0.1991 0.0586  -0.0173 -0.0244 352 GLY A O   
5236 N N   . ALA A 353 ? 0.2338 0.1797 0.2174 0.0683  -0.0221 -0.0247 353 ALA A N   
5237 C CA  . ALA A 353 ? 0.2378 0.1731 0.2137 0.0614  -0.0194 -0.0204 353 ALA A CA  
5238 C C   . ALA A 353 ? 0.2211 0.1611 0.1989 0.0564  -0.0153 -0.0245 353 ALA A C   
5239 O O   . ALA A 353 ? 0.2332 0.1789 0.2157 0.0592  -0.0138 -0.0306 353 ALA A O   
5240 C CB  . ALA A 353 ? 0.2957 0.2122 0.2645 0.0643  -0.0211 -0.0180 353 ALA A CB  
5246 N N   . PRO A 354 ? 0.2219 0.1592 0.1958 0.0496  -0.0135 -0.0219 354 PRO A N   
5247 C CA  . PRO A 354 ? 0.2290 0.1676 0.2016 0.0460  -0.0112 -0.0260 354 PRO A CA  
5248 C C   . PRO A 354 ? 0.2626 0.1918 0.2345 0.0488  -0.0116 -0.0300 354 PRO A C   
5249 O O   . PRO A 354 ? 0.2908 0.2080 0.2613 0.0503  -0.0133 -0.0281 354 PRO A O   
5250 C CB  . PRO A 354 ? 0.2659 0.2022 0.2355 0.0396  -0.0114 -0.0227 354 PRO A CB  
5251 C CG  . PRO A 354 ? 0.2752 0.2052 0.2444 0.0394  -0.0125 -0.0173 354 PRO A CG  
5252 C CD  . PRO A 354 ? 0.2292 0.1626 0.1996 0.0452  -0.0138 -0.0161 354 PRO A CD  
5260 N N   . LEU A 355 ? 0.2330 0.1659 0.2045 0.0494  -0.0096 -0.0359 355 LEU A N   
5261 C CA  . LEU A 355 ? 0.2522 0.1766 0.2226 0.0520  -0.0099 -0.0410 355 LEU A CA  
5262 C C   . LEU A 355 ? 0.2763 0.1945 0.2418 0.0469  -0.0107 -0.0426 355 LEU A C   
5263 O O   . LEU A 355 ? 0.3493 0.2592 0.3138 0.0482  -0.0114 -0.0472 355 LEU A O   
5264 C CB  . LEU A 355 ? 0.2761 0.2081 0.2488 0.0561  -0.0067 -0.0477 355 LEU A CB  
5265 C CG  . LEU A 355 ? 0.3458 0.2855 0.3272 0.0623  -0.0070 -0.0486 355 LEU A CG  
5266 C CD1 . LEU A 355 ? 0.3733 0.3226 0.3597 0.0656  -0.0026 -0.0568 355 LEU A CD1 
5267 C CD2 . LEU A 355 ? 0.3983 0.3265 0.3809 0.0682  -0.0118 -0.0467 355 LEU A CD2 
5279 N N   . GLY A 356 ? 0.2854 0.2073 0.2483 0.0418  -0.0111 -0.0397 356 GLY A N   
5280 C CA  . GLY A 356 ? 0.2973 0.2151 0.2572 0.0377  -0.0135 -0.0422 356 GLY A CA  
5281 C C   . GLY A 356 ? 0.2935 0.2176 0.2513 0.0339  -0.0144 -0.0387 356 GLY A C   
5282 O O   . GLY A 356 ? 0.2852 0.2162 0.2431 0.0341  -0.0125 -0.0348 356 GLY A O   
5286 N N   . LYS A 357 ? 0.2604 0.1820 0.2175 0.0308  -0.0180 -0.0410 357 LYS A N   
5287 C CA  . LYS A 357 ? 0.2732 0.1999 0.2280 0.0284  -0.0200 -0.0388 357 LYS A CA  
5288 C C   . LYS A 357 ? 0.2326 0.1616 0.1757 0.0300  -0.0189 -0.0396 357 LYS A C   
5289 O O   . LYS A 357 ? 0.2708 0.1973 0.2071 0.0323  -0.0168 -0.0434 357 LYS A O   
5290 C CB  . LYS A 357 ? 0.2894 0.2137 0.2474 0.0258  -0.0253 -0.0430 357 LYS A CB  
5291 C CG  . LYS A 357 ? 0.3996 0.3214 0.3699 0.0223  -0.0249 -0.0428 357 LYS A CG  
5292 C CD  . LYS A 357 ? 0.5059 0.4291 0.4799 0.0215  -0.0205 -0.0357 357 LYS A CD  
5293 C CE  . LYS A 357 ? 0.4990 0.4168 0.4820 0.0172  -0.0186 -0.0352 357 LYS A CE  
5294 N NZ  . LYS A 357 ? 0.5080 0.4218 0.4892 0.0183  -0.0142 -0.0285 357 LYS A NZ  
5308 N N   . ALA A 358 ? 0.2398 0.1721 0.1794 0.0285  -0.0198 -0.0361 358 ALA A N   
5309 C CA  . ALA A 358 ? 0.2323 0.1634 0.1581 0.0292  -0.0184 -0.0362 358 ALA A CA  
5310 C C   . ALA A 358 ? 0.2537 0.1774 0.1679 0.0308  -0.0228 -0.0417 358 ALA A C   
5311 O O   . ALA A 358 ? 0.2653 0.1870 0.1842 0.0308  -0.0290 -0.0454 358 ALA A O   
5312 C CB  . ALA A 358 ? 0.2441 0.1775 0.1681 0.0274  -0.0198 -0.0316 358 ALA A CB  
5318 N N   . ILE A 359 ? 0.1943 0.1255 0.1497 -0.0072 -0.0133 -0.0256 359 ILE A N   
5319 C CA  . ILE A 359 ? 0.2058 0.1290 0.1515 -0.0092 -0.0155 -0.0298 359 ILE A CA  
5320 C C   . ILE A 359 ? 0.2060 0.1496 0.1607 -0.0089 -0.0109 -0.0294 359 ILE A C   
5321 O O   . ILE A 359 ? 0.2145 0.1686 0.1759 -0.0020 -0.0048 -0.0307 359 ILE A O   
5322 C CB  . ILE A 359 ? 0.2417 0.1468 0.1737 0.0011  -0.0141 -0.0377 359 ILE A CB  
5323 C CG1 . ILE A 359 ? 0.2933 0.1744 0.2160 0.0044  -0.0192 -0.0387 359 ILE A CG1 
5324 C CG2 . ILE A 359 ? 0.2662 0.1621 0.1836 -0.0012 -0.0165 -0.0426 359 ILE A CG2 
5325 C CD1 . ILE A 359 ? 0.3835 0.2438 0.2956 -0.0078 -0.0299 -0.0356 359 ILE A CD1 
5337 N N   . LYS A 360 ? 0.2027 0.1517 0.1580 -0.0168 -0.0151 -0.0267 360 LYS A N   
5338 C CA  . LYS A 360 ? 0.1943 0.1596 0.1570 -0.0161 -0.0127 -0.0254 360 LYS A CA  
5339 C C   . LYS A 360 ? 0.2064 0.1628 0.1559 -0.0159 -0.0146 -0.0291 360 LYS A C   
5340 O O   . LYS A 360 ? 0.2228 0.1669 0.1606 -0.0223 -0.0217 -0.0301 360 LYS A O   
5341 C CB  . LYS A 360 ? 0.1799 0.1614 0.1538 -0.0229 -0.0161 -0.0190 360 LYS A CB  
5342 C CG  . LYS A 360 ? 0.1797 0.1762 0.1618 -0.0199 -0.0150 -0.0174 360 LYS A CG  
5343 C CD  . LYS A 360 ? 0.1766 0.1929 0.1716 -0.0241 -0.0180 -0.0110 360 LYS A CD  
5344 C CE  . LYS A 360 ? 0.1554 0.1851 0.1592 -0.0176 -0.0171 -0.0096 360 LYS A CE  
5345 N NZ  . LYS A 360 ? 0.1594 0.1823 0.1555 -0.0189 -0.0219 -0.0097 360 LYS A NZ  
5359 N N   . ASN A 361 ? 0.1916 0.1543 0.1418 -0.0101 -0.0091 -0.0302 361 ASN A N   
5360 C CA  . ASN A 361 ? 0.1981 0.1562 0.1349 -0.0094 -0.0090 -0.0325 361 ASN A CA  
5361 C C   . ASN A 361 ? 0.1699 0.1421 0.1158 -0.0101 -0.0086 -0.0271 361 ASN A C   
5362 O O   . ASN A 361 ? 0.1782 0.1562 0.1279 -0.0063 -0.0032 -0.0258 361 ASN A O   
5363 C CB  . ASN A 361 ? 0.2277 0.1811 0.1562 -0.0009 -0.0015 -0.0374 361 ASN A CB  
5364 C CG  . ASN A 361 ? 0.2692 0.2237 0.1841 0.0006  0.0013  -0.0384 361 ASN A CG  
5365 O OD1 . ASN A 361 ? 0.2892 0.2394 0.1939 -0.0048 -0.0045 -0.0376 361 ASN A OD1 
5366 N ND2 . ASN A 361 ? 0.2882 0.2511 0.2038 0.0073  0.0102  -0.0389 361 ASN A ND2 
5373 N N   . GLY A 362 ? 0.1867 0.1643 0.1366 -0.0153 -0.0154 -0.0231 362 GLY A N   
5374 C CA  . GLY A 362 ? 0.1805 0.1690 0.1397 -0.0138 -0.0163 -0.0179 362 GLY A CA  
5375 C C   . GLY A 362 ? 0.1660 0.1621 0.1404 -0.0090 -0.0122 -0.0170 362 GLY A C   
5376 O O   . GLY A 362 ? 0.1658 0.1680 0.1490 -0.0091 -0.0123 -0.0169 362 GLY A O   
5380 N N   . TYR A 363 ? 0.1591 0.1543 0.1349 -0.0057 -0.0091 -0.0159 363 TYR A N   
5381 C CA  . TYR A 363 ? 0.1413 0.1388 0.1273 -0.0017 -0.0067 -0.0163 363 TYR A CA  
5382 C C   . TYR A 363 ? 0.1573 0.1527 0.1430 -0.0010 -0.0015 -0.0193 363 TYR A C   
5383 O O   . TYR A 363 ? 0.1573 0.1534 0.1494 0.0011  -0.0006 -0.0199 363 TYR A O   
5384 C CB  . TYR A 363 ? 0.1562 0.1504 0.1432 -0.0003 -0.0091 -0.0124 363 TYR A CB  
5385 C CG  . TYR A 363 ? 0.1513 0.1477 0.1410 0.0021  -0.0151 -0.0088 363 TYR A CG  
5386 C CD1 . TYR A 363 ? 0.1642 0.1704 0.1634 0.0066  -0.0167 -0.0096 363 TYR A CD1 
5387 C CD2 . TYR A 363 ? 0.1731 0.1643 0.1565 0.0004  -0.0193 -0.0034 363 TYR A CD2 
5388 C CE1 . TYR A 363 ? 0.1631 0.1755 0.1678 0.0108  -0.0222 -0.0057 363 TYR A CE1 
5389 C CE2 . TYR A 363 ? 0.1724 0.1657 0.1594 0.0040  -0.0260 0.0007  363 TYR A CE2 
5390 C CZ  . TYR A 363 ? 0.1551 0.1601 0.1540 0.0101  -0.0275 -0.0007 363 TYR A CZ  
5391 O OH  . TYR A 363 ? 0.1718 0.1828 0.1767 0.0155  -0.0343 0.0040  363 TYR A OH  
5401 N N   . ILE A 364 ? 0.1574 0.1497 0.1353 -0.0018 0.0012  -0.0216 364 ILE A N   
5402 C CA  . ILE A 364 ? 0.1563 0.1489 0.1356 0.0009  0.0057  -0.0241 364 ILE A CA  
5403 C C   . ILE A 364 ? 0.1769 0.1649 0.1556 0.0015  0.0044  -0.0268 364 ILE A C   
5404 O O   . ILE A 364 ? 0.2164 0.1984 0.1882 -0.0015 0.0009  -0.0276 364 ILE A O   
5405 C CB  . ILE A 364 ? 0.1714 0.1643 0.1420 0.0026  0.0104  -0.0249 364 ILE A CB  
5406 C CG1 . ILE A 364 ? 0.1951 0.1948 0.1677 -0.0003 0.0117  -0.0193 364 ILE A CG1 
5407 C CG2 . ILE A 364 ? 0.1994 0.1946 0.1727 0.0081  0.0148  -0.0277 364 ILE A CG2 
5408 C CD1 . ILE A 364 ? 0.2078 0.2120 0.1698 0.0002  0.0170  -0.0181 364 ILE A CD1 
5420 N N   . TYR A 365 ? 0.1562 0.1465 0.1414 0.0039  0.0058  -0.0272 365 TYR A N   
5421 C CA  . TYR A 365 ? 0.1586 0.1432 0.1421 0.0041  0.0042  -0.0281 365 TYR A CA  
5422 C C   . TYR A 365 ? 0.1577 0.1411 0.1423 0.0097  0.0067  -0.0296 365 TYR A C   
5423 O O   . TYR A 365 ? 0.1647 0.1574 0.1568 0.0117  0.0091  -0.0285 365 TYR A O   
5424 C CB  . TYR A 365 ? 0.1714 0.1621 0.1613 0.0021  0.0026  -0.0258 365 TYR A CB  
5425 C CG  . TYR A 365 ? 0.1339 0.1315 0.1265 -0.0009 0.0008  -0.0238 365 TYR A CG  
5426 C CD1 . TYR A 365 ? 0.1508 0.1529 0.1469 0.0011  0.0010  -0.0237 365 TYR A CD1 
5427 C CD2 . TYR A 365 ? 0.1594 0.1601 0.1523 -0.0057 -0.0016 -0.0208 365 TYR A CD2 
5428 C CE1 . TYR A 365 ? 0.1539 0.1640 0.1543 0.0012  -0.0008 -0.0217 365 TYR A CE1 
5429 C CE2 . TYR A 365 ? 0.1464 0.1599 0.1456 -0.0073 -0.0027 -0.0179 365 TYR A CE2 
5430 C CZ  . TYR A 365 ? 0.1294 0.1478 0.1326 -0.0024 -0.0020 -0.0189 365 TYR A CZ  
5431 O OH  . TYR A 365 ? 0.1563 0.1886 0.1670 -0.0011 -0.0033 -0.0159 365 TYR A OH  
5441 N N   . THR A 366 ? 0.1638 0.1354 0.1414 0.0119  0.0049  -0.0312 366 THR A N   
5442 C CA  . THR A 366 ? 0.1708 0.1409 0.1506 0.0192  0.0061  -0.0319 366 THR A CA  
5443 C C   . THR A 366 ? 0.1879 0.1469 0.1648 0.0175  0.0009  -0.0297 366 THR A C   
5444 O O   . THR A 366 ? 0.1906 0.1400 0.1608 0.0106  -0.0032 -0.0282 366 THR A O   
5445 C CB  . THR A 366 ? 0.2062 0.1695 0.1778 0.0278  0.0093  -0.0367 366 THR A CB  
5446 O OG1 . THR A 366 ? 0.2613 0.2039 0.2171 0.0255  0.0050  -0.0401 366 THR A OG1 
5447 C CG2 . THR A 366 ? 0.2115 0.1899 0.1861 0.0290  0.0155  -0.0368 366 THR A CG2 
5455 N N   . ARG A 367 ? 0.1762 0.1379 0.1585 0.0229  0.0003  -0.0280 367 ARG A N   
5456 C CA  . ARG A 367 ? 0.1702 0.1191 0.1476 0.0220  -0.0052 -0.0245 367 ARG A CA  
5457 C C   . ARG A 367 ? 0.1869 0.1361 0.1688 0.0324  -0.0061 -0.0239 367 ARG A C   
5458 O O   . ARG A 367 ? 0.1996 0.1671 0.1932 0.0360  -0.0032 -0.0234 367 ARG A O   
5459 C CB  . ARG A 367 ? 0.1645 0.1216 0.1444 0.0132  -0.0070 -0.0193 367 ARG A CB  
5460 C CG  . ARG A 367 ? 0.1836 0.1275 0.1558 0.0084  -0.0127 -0.0136 367 ARG A CG  
5461 C CD  . ARG A 367 ? 0.1708 0.1279 0.1444 0.0004  -0.0122 -0.0083 367 ARG A CD  
5462 N NE  . ARG A 367 ? 0.1938 0.1410 0.1598 -0.0072 -0.0172 -0.0005 367 ARG A NE  
5463 C CZ  . ARG A 367 ? 0.1957 0.1548 0.1605 -0.0141 -0.0166 0.0062  367 ARG A CZ  
5464 N NH1 . ARG A 367 ? 0.1808 0.1599 0.1500 -0.0123 -0.0112 0.0041  367 ARG A NH1 
5465 N NH2 . ARG A 367 ? 0.2176 0.1675 0.1753 -0.0229 -0.0215 0.0152  367 ARG A NH2 
5479 N N   . LYS A 368 ? 0.2041 0.1327 0.1772 0.0364  -0.0113 -0.0231 368 LYS A N   
5480 C CA  . LYS A 368 ? 0.2309 0.1573 0.2079 0.0483  -0.0137 -0.0217 368 LYS A CA  
5481 C C   . LYS A 368 ? 0.2318 0.1539 0.2078 0.0433  -0.0208 -0.0135 368 LYS A C   
5482 O O   . LYS A 368 ? 0.2451 0.1514 0.2104 0.0337  -0.0256 -0.0094 368 LYS A O   
5483 C CB  . LYS A 368 ? 0.2969 0.1984 0.2620 0.0598  -0.0156 -0.0270 368 LYS A CB  
5484 C CG  . LYS A 368 ? 0.4027 0.3072 0.3641 0.0660  -0.0082 -0.0356 368 LYS A CG  
5485 C CD  . LYS A 368 ? 0.5139 0.3882 0.4576 0.0781  -0.0108 -0.0429 368 LYS A CD  
5486 C CE  . LYS A 368 ? 0.5858 0.4563 0.5173 0.0798  -0.0052 -0.0518 368 LYS A CE  
5487 N NZ  . LYS A 368 ? 0.5999 0.4473 0.5152 0.0657  -0.0120 -0.0528 368 LYS A NZ  
5501 N N   . PHE A 369 ? 0.2101 0.1480 0.1971 0.0488  -0.0220 -0.0102 369 PHE A N   
5502 C CA  . PHE A 369 ? 0.2058 0.1403 0.1910 0.0474  -0.0296 -0.0022 369 PHE A CA  
5503 C C   . PHE A 369 ? 0.2320 0.1627 0.2227 0.0631  -0.0336 -0.0010 369 PHE A C   
5504 O O   . PHE A 369 ? 0.2403 0.1792 0.2396 0.0751  -0.0286 -0.0065 369 PHE A O   
5505 C CB  . PHE A 369 ? 0.2034 0.1609 0.1954 0.0401  -0.0293 0.0007  369 PHE A CB  
5506 C CG  . PHE A 369 ? 0.1866 0.1485 0.1729 0.0279  -0.0253 -0.0007 369 PHE A CG  
5507 C CD1 . PHE A 369 ? 0.1860 0.1558 0.1768 0.0259  -0.0187 -0.0069 369 PHE A CD1 
5508 C CD2 . PHE A 369 ? 0.2045 0.1638 0.1806 0.0191  -0.0280 0.0051  369 PHE A CD2 
5509 C CE1 . PHE A 369 ? 0.1723 0.1466 0.1590 0.0172  -0.0155 -0.0078 369 PHE A CE1 
5510 C CE2 . PHE A 369 ? 0.2075 0.1747 0.1799 0.0105  -0.0232 0.0038  369 PHE A CE2 
5511 C CZ  . PHE A 369 ? 0.1935 0.1675 0.1718 0.0104  -0.0174 -0.0029 369 PHE A CZ  
5521 N N   . GLU A 370 ? 0.2334 0.1537 0.2197 0.0643  -0.0425 0.0069  370 GLU A N   
5522 C CA  . GLU A 370 ? 0.2523 0.1669 0.2440 0.0815  -0.0477 0.0087  370 GLU A CA  
5523 C C   . GLU A 370 ? 0.2357 0.1835 0.2492 0.0919  -0.0428 0.0063  370 GLU A C   
5524 O O   . GLU A 370 ? 0.2677 0.2176 0.2890 0.1095  -0.0408 0.0031  370 GLU A O   
5525 C CB  . GLU A 370 ? 0.2793 0.1827 0.2645 0.0795  -0.0591 0.0197  370 GLU A CB  
5526 C CG  . GLU A 370 ? 0.3579 0.2240 0.3224 0.0731  -0.0655 0.0237  370 GLU A CG  
5527 C CD  . GLU A 370 ? 0.4230 0.2779 0.3780 0.0672  -0.0766 0.0370  370 GLU A CD  
5528 O OE1 . GLU A 370 ? 0.3823 0.2592 0.3401 0.0590  -0.0773 0.0426  370 GLU A OE1 
5529 O OE2 . GLU A 370 ? 0.5650 0.3862 0.5073 0.0709  -0.0857 0.0419  370 GLU A OE2 
5536 N N   . ASN A 371 ? 0.2123 0.1864 0.2357 0.0815  -0.0413 0.0083  371 ASN A N   
5537 C CA  . ASN A 371 ? 0.1987 0.2061 0.2440 0.0869  -0.0396 0.0092  371 ASN A CA  
5538 C C   . ASN A 371 ? 0.1873 0.2140 0.2398 0.0775  -0.0312 0.0045  371 ASN A C   
5539 O O   . ASN A 371 ? 0.1851 0.2399 0.2549 0.0759  -0.0314 0.0071  371 ASN A O   
5540 C CB  . ASN A 371 ? 0.1995 0.2198 0.2508 0.0833  -0.0501 0.0179  371 ASN A CB  
5541 C CG  . ASN A 371 ? 0.2550 0.2546 0.2975 0.0912  -0.0598 0.0246  371 ASN A CG  
5542 O OD1 . ASN A 371 ? 0.3342 0.3221 0.3627 0.0815  -0.0672 0.0305  371 ASN A OD1 
5543 N ND2 . ASN A 371 ? 0.2741 0.2676 0.3227 0.1097  -0.0599 0.0238  371 ASN A ND2 
5550 N N   . LEU A 372 ? 0.1713 0.1838 0.2114 0.0707  -0.0249 -0.0014 372 LEU A N   
5551 C CA  . LEU A 372 ? 0.1545 0.1813 0.1991 0.0613  -0.0185 -0.0048 372 LEU A CA  
5552 C C   . LEU A 372 ? 0.1856 0.1970 0.2186 0.0606  -0.0114 -0.0114 372 LEU A C   
5553 O O   . LEU A 372 ? 0.2083 0.1960 0.2261 0.0582  -0.0135 -0.0126 372 LEU A O   
5554 C CB  . LEU A 372 ? 0.1643 0.1911 0.2029 0.0470  -0.0230 -0.0031 372 LEU A CB  
5555 C CG  . LEU A 372 ? 0.1632 0.1950 0.2010 0.0370  -0.0182 -0.0071 372 LEU A CG  
5556 C CD1 . LEU A 372 ? 0.1757 0.2307 0.2304 0.0360  -0.0169 -0.0056 372 LEU A CD1 
5557 C CD2 . LEU A 372 ? 0.1785 0.2040 0.2050 0.0269  -0.0220 -0.0075 372 LEU A CD2 
5569 N N   . ASP A 373 ? 0.1709 0.1971 0.2110 0.0609  -0.0039 -0.0143 373 ASP A N   
5570 C CA  . ASP A 373 ? 0.1749 0.1902 0.2038 0.0576  0.0021  -0.0199 373 ASP A CA  
5571 C C   . ASP A 373 ? 0.1761 0.2015 0.2080 0.0448  0.0033  -0.0191 373 ASP A C   
5572 O O   . ASP A 373 ? 0.1708 0.2167 0.2159 0.0417  0.0038  -0.0158 373 ASP A O   
5573 C CB  . ASP A 373 ? 0.2155 0.2387 0.2466 0.0692  0.0101  -0.0237 373 ASP A CB  
5574 C CG  . ASP A 373 ? 0.3056 0.3147 0.3311 0.0854  0.0090  -0.0266 373 ASP A CG  
5575 O OD1 . ASP A 373 ? 0.3892 0.3703 0.4009 0.0849  0.0024  -0.0276 373 ASP A OD1 
5576 O OD2 . ASP A 373 ? 0.4506 0.4770 0.4853 0.0992  0.0149  -0.0276 373 ASP A OD2 
5581 N N   . VAL A 374 ? 0.1560 0.1669 0.1762 0.0372  0.0029  -0.0214 374 VAL A N   
5582 C CA  . VAL A 374 ? 0.1414 0.1569 0.1620 0.0274  0.0032  -0.0214 374 VAL A CA  
5583 C C   . VAL A 374 ? 0.1525 0.1657 0.1681 0.0264  0.0084  -0.0242 374 VAL A C   
5584 O O   . VAL A 374 ? 0.1637 0.1634 0.1687 0.0286  0.0093  -0.0273 374 VAL A O   
5585 C CB  . VAL A 374 ? 0.1443 0.1494 0.1563 0.0214  -0.0007 -0.0213 374 VAL A CB  
5586 C CG1 . VAL A 374 ? 0.1771 0.1849 0.1884 0.0150  -0.0002 -0.0225 374 VAL A CG1 
5587 C CG2 . VAL A 374 ? 0.1773 0.1836 0.1900 0.0218  -0.0061 -0.0180 374 VAL A CG2 
5597 N N   . TRP A 375 ? 0.1479 0.1722 0.1694 0.0217  0.0103  -0.0225 375 TRP A N   
5598 C CA  . TRP A 375 ? 0.1351 0.1573 0.1507 0.0188  0.0138  -0.0235 375 TRP A CA  
5599 C C   . TRP A 375 ? 0.1398 0.1614 0.1570 0.0107  0.0103  -0.0217 375 TRP A C   
5600 O O   . TRP A 375 ? 0.1503 0.1789 0.1755 0.0069  0.0073  -0.0188 375 TRP A O   
5601 C CB  . TRP A 375 ? 0.1679 0.2047 0.1880 0.0224  0.0201  -0.0217 375 TRP A CB  
5602 C CG  . TRP A 375 ? 0.1720 0.2081 0.1841 0.0190  0.0237  -0.0214 375 TRP A CG  
5603 C CD1 . TRP A 375 ? 0.2305 0.2575 0.2284 0.0231  0.0269  -0.0257 375 TRP A CD1 
5604 C CD2 . TRP A 375 ? 0.1570 0.1993 0.1726 0.0102  0.0229  -0.0160 375 TRP A CD2 
5605 N NE1 . TRP A 375 ? 0.2053 0.2353 0.1980 0.0175  0.0287  -0.0229 375 TRP A NE1 
5606 C CE2 . TRP A 375 ? 0.1761 0.2150 0.1799 0.0096  0.0263  -0.0163 375 TRP A CE2 
5607 C CE3 . TRP A 375 ? 0.1935 0.2412 0.2192 0.0021  0.0182  -0.0108 375 TRP A CE3 
5608 C CZ2 . TRP A 375 ? 0.2023 0.2442 0.2052 0.0016  0.0255  -0.0102 375 TRP A CZ2 
5609 C CZ3 . TRP A 375 ? 0.2070 0.2548 0.2315 -0.0062 0.0169  -0.0053 375 TRP A CZ3 
5610 C CH2 . TRP A 375 ? 0.2257 0.2712 0.2394 -0.0062 0.0208  -0.0044 375 TRP A CH2 
5621 N N   . LEU A 376 ? 0.1422 0.1545 0.1517 0.0084  0.0095  -0.0233 376 LEU A N   
5622 C CA  . LEU A 376 ? 0.1471 0.1555 0.1564 0.0042  0.0059  -0.0228 376 LEU A CA  
5623 C C   . LEU A 376 ? 0.1491 0.1545 0.1535 0.0022  0.0067  -0.0215 376 LEU A C   
5624 O O   . LEU A 376 ? 0.1562 0.1586 0.1542 0.0036  0.0081  -0.0230 376 LEU A O   
5625 C CB  . LEU A 376 ? 0.1426 0.1459 0.1486 0.0055  0.0036  -0.0254 376 LEU A CB  
5626 C CG  . LEU A 376 ? 0.1477 0.1473 0.1518 0.0054  0.0011  -0.0264 376 LEU A CG  
5627 C CD1 . LEU A 376 ? 0.1433 0.1389 0.1484 0.0039  -0.0030 -0.0270 376 LEU A CD1 
5628 C CD2 . LEU A 376 ? 0.1526 0.1541 0.1542 0.0076  0.0015  -0.0279 376 LEU A CD2 
5640 N N   . ASN A 377 ? 0.1413 0.1452 0.1472 -0.0017 0.0041  -0.0184 377 ASN A N   
5641 C CA  . ASN A 377 ? 0.1487 0.1483 0.1493 -0.0036 0.0032  -0.0157 377 ASN A CA  
5642 C C   . ASN A 377 ? 0.1455 0.1352 0.1461 -0.0032 -0.0028 -0.0159 377 ASN A C   
5643 O O   . ASN A 377 ? 0.1648 0.1485 0.1669 -0.0066 -0.0069 -0.0138 377 ASN A O   
5644 C CB  . ASN A 377 ? 0.1516 0.1577 0.1519 -0.0083 0.0058  -0.0099 377 ASN A CB  
5645 C CG  . ASN A 377 ? 0.1888 0.1905 0.1805 -0.0104 0.0048  -0.0063 377 ASN A CG  
5646 O OD1 . ASN A 377 ? 0.1876 0.1808 0.1765 -0.0088 0.0001  -0.0071 377 ASN A OD1 
5647 N ND2 . ASN A 377 ? 0.1897 0.1998 0.1772 -0.0134 0.0094  -0.0016 377 ASN A ND2 
5654 N N   . LEU A 378 ? 0.1520 0.1400 0.1508 0.0012  -0.0040 -0.0183 378 LEU A N   
5655 C CA  . LEU A 378 ? 0.1627 0.1428 0.1614 0.0056  -0.0087 -0.0196 378 LEU A CA  
5656 C C   . LEU A 378 ? 0.1645 0.1347 0.1602 0.0036  -0.0135 -0.0146 378 LEU A C   
5657 O O   . LEU A 378 ? 0.2030 0.1604 0.1970 0.0070  -0.0190 -0.0154 378 LEU A O   
5658 C CB  . LEU A 378 ? 0.1564 0.1440 0.1570 0.0113  -0.0077 -0.0217 378 LEU A CB  
5659 C CG  . LEU A 378 ? 0.1522 0.1487 0.1548 0.0123  -0.0039 -0.0248 378 LEU A CG  
5660 C CD1 . LEU A 378 ? 0.1529 0.1608 0.1595 0.0155  -0.0035 -0.0239 378 LEU A CD1 
5661 C CD2 . LEU A 378 ? 0.1770 0.1695 0.1781 0.0151  -0.0041 -0.0288 378 LEU A CD2 
5673 N N   . GLU A 379 ? 0.1775 0.1515 0.1702 -0.0013 -0.0122 -0.0093 379 GLU A N   
5674 C CA  . GLU A 379 ? 0.1953 0.1601 0.1833 -0.0039 -0.0174 -0.0026 379 GLU A CA  
5675 C C   . GLU A 379 ? 0.2058 0.1612 0.1933 -0.0111 -0.0206 0.0022  379 GLU A C   
5676 O O   . GLU A 379 ? 0.2669 0.2056 0.2510 -0.0116 -0.0283 0.0059  379 GLU A O   
5677 C CB  . GLU A 379 ? 0.2041 0.1768 0.1858 -0.0076 -0.0147 0.0015  379 GLU A CB  
5678 C CG  . GLU A 379 ? 0.2355 0.2005 0.2104 -0.0103 -0.0205 0.0096  379 GLU A CG  
5679 C CD  . GLU A 379 ? 0.2572 0.2298 0.2227 -0.0125 -0.0189 0.0119  379 GLU A CD  
5680 O OE1 . GLU A 379 ? 0.2538 0.2352 0.2151 -0.0141 -0.0121 0.0083  379 GLU A OE1 
5681 O OE2 . GLU A 379 ? 0.3141 0.2818 0.2744 -0.0124 -0.0254 0.0175  379 GLU A OE2 
5688 N N   . THR A 380 ? 0.2066 0.1720 0.1978 -0.0169 -0.0159 0.0030  380 THR A N   
5689 C CA  . THR A 380 ? 0.2239 0.1852 0.2176 -0.0263 -0.0196 0.0088  380 THR A CA  
5690 C C   . THR A 380 ? 0.2194 0.1722 0.2165 -0.0252 -0.0243 0.0029  380 THR A C   
5691 O O   . THR A 380 ? 0.2370 0.1831 0.2358 -0.0343 -0.0303 0.0073  380 THR A O   
5692 C CB  . THR A 380 ? 0.2267 0.2098 0.2251 -0.0326 -0.0115 0.0140  380 THR A CB  
5693 O OG1 . THR A 380 ? 0.2188 0.2144 0.2217 -0.0257 -0.0049 0.0064  380 THR A OG1 
5694 C CG2 . THR A 380 ? 0.2498 0.2400 0.2406 -0.0345 -0.0071 0.0201  380 THR A CG2 
5702 N N   . GLN A 381 ? 0.1948 0.1485 0.1920 -0.0156 -0.0222 -0.0063 381 GLN A N   
5703 C CA  . GLN A 381 ? 0.1943 0.1414 0.1911 -0.0133 -0.0257 -0.0130 381 GLN A CA  
5704 C C   . GLN A 381 ? 0.2069 0.1657 0.2109 -0.0216 -0.0252 -0.0101 381 GLN A C   
5705 O O   . GLN A 381 ? 0.2259 0.1751 0.2291 -0.0275 -0.0329 -0.0100 381 GLN A O   
5706 C CB  . GLN A 381 ? 0.2381 0.1591 0.2261 -0.0111 -0.0356 -0.0159 381 GLN A CB  
5707 C CG  . GLN A 381 ? 0.2573 0.1701 0.2408 -0.0003 -0.0361 -0.0180 381 GLN A CG  
5708 C CD  . GLN A 381 ? 0.3505 0.2352 0.3241 0.0055  -0.0458 -0.0221 381 GLN A CD  
5709 O OE1 . GLN A 381 ? 0.5270 0.3927 0.4947 -0.0018 -0.0543 -0.0218 381 GLN A OE1 
5710 N NE2 . GLN A 381 ? 0.5128 0.3935 0.4842 0.0189  -0.0457 -0.0255 381 GLN A NE2 
5719 N N   . THR A 382 ? 0.1842 0.1635 0.1949 -0.0212 -0.0169 -0.0081 382 THR A N   
5720 C CA  . THR A 382 ? 0.1874 0.1836 0.2079 -0.0259 -0.0150 -0.0048 382 THR A CA  
5721 C C   . THR A 382 ? 0.1548 0.1626 0.1776 -0.0175 -0.0082 -0.0096 382 THR A C   
5722 O O   . THR A 382 ? 0.1517 0.1569 0.1688 -0.0109 -0.0041 -0.0135 382 THR A O   
5723 C CB  . THR A 382 ? 0.1871 0.1987 0.2143 -0.0338 -0.0114 0.0051  382 THR A CB  
5724 O OG1 . THR A 382 ? 0.2032 0.2204 0.2254 -0.0283 -0.0033 0.0049  382 THR A OG1 
5725 C CG2 . THR A 382 ? 0.2215 0.2203 0.2466 -0.0453 -0.0198 0.0127  382 THR A CG2 
5733 N N   . ALA A 383 ? 0.1574 0.1780 0.1888 -0.0186 -0.0084 -0.0083 383 ALA A N   
5734 C CA  . ALA A 383 ? 0.1455 0.1748 0.1790 -0.0105 -0.0034 -0.0115 383 ALA A CA  
5735 C C   . ALA A 383 ? 0.1584 0.2081 0.2054 -0.0114 -0.0024 -0.0065 383 ALA A C   
5736 O O   . ALA A 383 ? 0.1891 0.2468 0.2447 -0.0202 -0.0075 -0.0007 383 ALA A O   
5737 C CB  . ALA A 383 ? 0.1508 0.1699 0.1778 -0.0067 -0.0072 -0.0173 383 ALA A CB  
5743 N N   . THR A 384 ? 0.1431 0.2012 0.1925 -0.0024 0.0031  -0.0081 384 THR A N   
5744 C CA  . THR A 384 ? 0.1551 0.2338 0.2186 0.0006  0.0036  -0.0041 384 THR A CA  
5745 C C   . THR A 384 ? 0.1692 0.2411 0.2295 0.0090  0.0015  -0.0081 384 THR A C   
5746 O O   . THR A 384 ? 0.1838 0.2413 0.2327 0.0151  0.0044  -0.0130 384 THR A O   
5747 C CB  . THR A 384 ? 0.1875 0.2855 0.2577 0.0065  0.0132  -0.0011 384 THR A CB  
5748 O OG1 . THR A 384 ? 0.2797 0.3648 0.3368 0.0165  0.0190  -0.0078 384 THR A OG1 
5749 C CG2 . THR A 384 ? 0.1586 0.2648 0.2309 -0.0033 0.0154  0.0051  384 THR A CG2 
5757 N N   . LEU A 385 ? 0.1318 0.2143 0.2019 0.0080  -0.0046 -0.0047 385 LEU A N   
5758 C CA  . LEU A 385 ? 0.1449 0.2240 0.2136 0.0157  -0.0078 -0.0058 385 LEU A CA  
5759 C C   . LEU A 385 ? 0.1329 0.2359 0.2188 0.0242  -0.0054 -0.0009 385 LEU A C   
5760 O O   . LEU A 385 ? 0.1443 0.2692 0.2463 0.0190  -0.0096 0.0056  385 LEU A O   
5761 C CB  . LEU A 385 ? 0.1509 0.2230 0.2149 0.0088  -0.0179 -0.0057 385 LEU A CB  
5762 C CG  . LEU A 385 ? 0.1455 0.1967 0.1926 0.0034  -0.0194 -0.0112 385 LEU A CG  
5763 C CD1 . LEU A 385 ? 0.1750 0.2200 0.2143 -0.0009 -0.0288 -0.0122 385 LEU A CD1 
5764 C CD2 . LEU A 385 ? 0.1696 0.2077 0.2055 0.0093  -0.0134 -0.0151 385 LEU A CD2 
5776 N N   . THR A 386 ? 0.1330 0.2321 0.2157 0.0375  0.0006  -0.0038 386 THR A N   
5777 C CA  . THR A 386 ? 0.1399 0.2613 0.2378 0.0502  0.0044  -0.0005 386 THR A CA  
5778 C C   . THR A 386 ? 0.1417 0.2553 0.2393 0.0588  -0.0029 0.0003  386 THR A C   
5779 O O   . THR A 386 ? 0.1641 0.2533 0.2469 0.0665  -0.0029 -0.0043 386 THR A O   
5780 C CB  . THR A 386 ? 0.1484 0.2686 0.2401 0.0617  0.0157  -0.0054 386 THR A CB  
5781 O OG1 . THR A 386 ? 0.1708 0.2974 0.2606 0.0519  0.0213  -0.0047 386 THR A OG1 
5782 C CG2 . THR A 386 ? 0.1795 0.3258 0.2870 0.0779  0.0213  -0.0029 386 THR A CG2 
5790 N N   . TRP A 387 ? 0.1416 0.2747 0.2548 0.0560  -0.0109 0.0073  387 TRP A N   
5791 C CA  . TRP A 387 ? 0.1381 0.2649 0.2507 0.0621  -0.0201 0.0101  387 TRP A CA  
5792 C C   . TRP A 387 ? 0.1574 0.2982 0.2831 0.0819  -0.0171 0.0121  387 TRP A C   
5793 O O   . TRP A 387 ? 0.1679 0.3430 0.3159 0.0869  -0.0133 0.0169  387 TRP A O   
5794 C CB  . TRP A 387 ? 0.1403 0.2824 0.2626 0.0498  -0.0315 0.0166  387 TRP A CB  
5795 C CG  . TRP A 387 ? 0.1464 0.2729 0.2541 0.0328  -0.0352 0.0133  387 TRP A CG  
5796 C CD1 . TRP A 387 ? 0.1272 0.2616 0.2393 0.0201  -0.0347 0.0136  387 TRP A CD1 
5797 C CD2 . TRP A 387 ? 0.1522 0.2522 0.2377 0.0279  -0.0400 0.0093  387 TRP A CD2 
5798 N NE1 . TRP A 387 ? 0.1556 0.2671 0.2488 0.0098  -0.0393 0.0087  387 TRP A NE1 
5799 C CE2 . TRP A 387 ? 0.1583 0.2513 0.2355 0.0149  -0.0416 0.0058  387 TRP A CE2 
5800 C CE3 . TRP A 387 ? 0.1676 0.2496 0.2388 0.0333  -0.0431 0.0091  387 TRP A CE3 
5801 C CZ2 . TRP A 387 ? 0.1732 0.2446 0.2288 0.0096  -0.0449 0.0010  387 TRP A CZ2 
5802 C CZ3 . TRP A 387 ? 0.1768 0.2400 0.2274 0.0254  -0.0459 0.0060  387 TRP A CZ3 
5803 C CH2 . TRP A 387 ? 0.1903 0.2499 0.2336 0.0150  -0.0460 0.0013  387 TRP A CH2 
5814 N N   . LYS A 388 ? 0.2028 0.3179 0.3153 0.0935  -0.0197 0.0095  388 LYS A N   
5815 C CA  . LYS A 388 ? 0.2120 0.3303 0.3311 0.1159  -0.0169 0.0090  388 LYS A CA  
5816 C C   . LYS A 388 ? 0.4303 0.5685 0.5678 0.1235  -0.0270 0.0181  388 LYS A C   
5817 O O   . LYS A 388 ? 0.4358 0.5648 0.5677 0.1138  -0.0385 0.0229  388 LYS A O   
5818 C CB  . LYS A 388 ? 0.4224 0.4967 0.5157 0.1225  -0.0180 0.0025  388 LYS A CB  
5819 C CG  . LYS A 388 ? 0.4267 0.4812 0.5017 0.1164  -0.0093 -0.0064 388 LYS A CG  
5820 C CD  . LYS A 388 ? 0.4564 0.4664 0.5056 0.1156  -0.0143 -0.0104 388 LYS A CD  
5821 C CE  . LYS A 388 ? 0.4804 0.4730 0.5126 0.1060  -0.0082 -0.0178 388 LYS A CE  
5822 N NZ  . LYS A 388 ? 0.4162 0.3703 0.4256 0.0992  -0.0143 -0.0195 388 LYS A NZ  
# 
