data_8WZY
# 
_entry.id   8WZY 
# 
_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   8WZY         pdb_00008wzy 10.2210/pdb8wzy/pdb 
WWPDB D_1300042121 ?            ?                   
# 
_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       2024-11-13 
# 
_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                        8WZY 
_pdbx_database_status.recvd_initial_deposition_date   2023-11-02 
_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              danma@hbu.edu.cn 
_pdbx_contact_author.name_first         Dan 
_pdbx_contact_author.name_last          Ma 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-0593-397X 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Feng, R.' 1 0000-0003-3889-5631 
'Ma, D.'   2 0000-0003-0593-397X 
# 
_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                     'A novel amidohydrolase catalyzes the degradation of polyacrylamide by Klebsiella sp. PCX' 
_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 'Ma, D.'   1 0000-0003-0593-397X 
primary 'Feng, R.' 2 0000-0003-3889-5631 
# 
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 Dihydroorotase 40885.344 1   ? ? ? 
;Sequence reference for Klebsiella sp. PCX is not available in UniProt at the time of biocuration. Current sequence reference is from UniProt id A0A9Q5IKM4.
;
2 non-polymer syn 1,2-ETHANEDIOL 62.068    4   ? ? ? ? 
3 non-polymer syn 'ZINC ION'     65.409    2   ? ? ? ? 
4 water       nat water          18.015    139 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        Amidohydrolase 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   yes 
_entity_poly.pdbx_seq_one_letter_code       
;MFDLLLRRARLVDDTLTDIAIQDGKIAALGEISAPSRKTIDLQGNSYVSAGWIDSHVHCYPNSPIYHDEPDSVGIATGVT
TVIDAGSTGADDVDDFYQLTRKAVTEVYALLNISRVGLIAQNELANLANIDAEAVKQAVQRHPDFIVGL(KCX)ARMSSS
VVGENGITPLARAKTMQQENGDLPLMVHIGNNPPNLDEIAELLSRGDIITHCYNGKPNRILNPAGELRSSITRALHRGVR
LDVGHGTASFSFEVARRAIALGILPHTISSDIYCRNRIDGPVRSLALVMSKFLAIGMTLPQVIDCVTVSAAEGLRLSRKG
RLEAGFDADLTLFRLERQPTLLVDAEKESLQADNILVPLAAIRAGKGYLTEQGSAEHAFDF
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MFDLLLRRARLVDDTLTDIAIQDGKIAALGEISAPSRKTIDLQGNSYVSAGWIDSHVHCYPNSPIYHDEPDSVGIATGVT
TVIDAGSTGADDVDDFYQLTRKAVTEVYALLNISRVGLIAQNELANLANIDAEAVKQAVQRHPDFIVGLKARMSSSVVGE
NGITPLARAKTMQQENGDLPLMVHIGNNPPNLDEIAELLSRGDIITHCYNGKPNRILNPAGELRSSITRALHRGVRLDVG
HGTASFSFEVARRAIALGILPHTISSDIYCRNRIDGPVRSLALVMSKFLAIGMTLPQVIDCVTVSAAEGLRLSRKGRLEA
GFDADLTLFRLERQPTLLVDAEKESLQADNILVPLAAIRAGKGYLTEQGSAEHAFDF
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 1,2-ETHANEDIOL EDO 
3 'ZINC ION'     ZN  
4 water          HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   PHE n 
1 3   ASP n 
1 4   LEU n 
1 5   LEU n 
1 6   LEU n 
1 7   ARG n 
1 8   ARG n 
1 9   ALA n 
1 10  ARG n 
1 11  LEU n 
1 12  VAL n 
1 13  ASP n 
1 14  ASP n 
1 15  THR n 
1 16  LEU n 
1 17  THR n 
1 18  ASP n 
1 19  ILE n 
1 20  ALA n 
1 21  ILE n 
1 22  GLN n 
1 23  ASP n 
1 24  GLY n 
1 25  LYS n 
1 26  ILE n 
1 27  ALA n 
1 28  ALA n 
1 29  LEU n 
1 30  GLY n 
1 31  GLU n 
1 32  ILE n 
1 33  SER n 
1 34  ALA n 
1 35  PRO n 
1 36  SER n 
1 37  ARG n 
1 38  LYS n 
1 39  THR n 
1 40  ILE n 
1 41  ASP n 
1 42  LEU n 
1 43  GLN n 
1 44  GLY n 
1 45  ASN n 
1 46  SER n 
1 47  TYR n 
1 48  VAL n 
1 49  SER n 
1 50  ALA n 
1 51  GLY n 
1 52  TRP n 
1 53  ILE n 
1 54  ASP n 
1 55  SER n 
1 56  HIS n 
1 57  VAL n 
1 58  HIS n 
1 59  CYS n 
1 60  TYR n 
1 61  PRO n 
1 62  ASN n 
1 63  SER n 
1 64  PRO n 
1 65  ILE n 
1 66  TYR n 
1 67  HIS n 
1 68  ASP n 
1 69  GLU n 
1 70  PRO n 
1 71  ASP n 
1 72  SER n 
1 73  VAL n 
1 74  GLY n 
1 75  ILE n 
1 76  ALA n 
1 77  THR n 
1 78  GLY n 
1 79  VAL n 
1 80  THR n 
1 81  THR n 
1 82  VAL n 
1 83  ILE n 
1 84  ASP n 
1 85  ALA n 
1 86  GLY n 
1 87  SER n 
1 88  THR n 
1 89  GLY n 
1 90  ALA n 
1 91  ASP n 
1 92  ASP n 
1 93  VAL n 
1 94  ASP n 
1 95  ASP n 
1 96  PHE n 
1 97  TYR n 
1 98  GLN n 
1 99  LEU n 
1 100 THR n 
1 101 ARG n 
1 102 LYS n 
1 103 ALA n 
1 104 VAL n 
1 105 THR n 
1 106 GLU n 
1 107 VAL n 
1 108 TYR n 
1 109 ALA n 
1 110 LEU n 
1 111 LEU n 
1 112 ASN n 
1 113 ILE n 
1 114 SER n 
1 115 ARG n 
1 116 VAL n 
1 117 GLY n 
1 118 LEU n 
1 119 ILE n 
1 120 ALA n 
1 121 GLN n 
1 122 ASN n 
1 123 GLU n 
1 124 LEU n 
1 125 ALA n 
1 126 ASN n 
1 127 LEU n 
1 128 ALA n 
1 129 ASN n 
1 130 ILE n 
1 131 ASP n 
1 132 ALA n 
1 133 GLU n 
1 134 ALA n 
1 135 VAL n 
1 136 LYS n 
1 137 GLN n 
1 138 ALA n 
1 139 VAL n 
1 140 GLN n 
1 141 ARG n 
1 142 HIS n 
1 143 PRO n 
1 144 ASP n 
1 145 PHE n 
1 146 ILE n 
1 147 VAL n 
1 148 GLY n 
1 149 LEU n 
1 150 KCX n 
1 151 ALA n 
1 152 ARG n 
1 153 MET n 
1 154 SER n 
1 155 SER n 
1 156 SER n 
1 157 VAL n 
1 158 VAL n 
1 159 GLY n 
1 160 GLU n 
1 161 ASN n 
1 162 GLY n 
1 163 ILE n 
1 164 THR n 
1 165 PRO n 
1 166 LEU n 
1 167 ALA n 
1 168 ARG n 
1 169 ALA n 
1 170 LYS n 
1 171 THR n 
1 172 MET n 
1 173 GLN n 
1 174 GLN n 
1 175 GLU n 
1 176 ASN n 
1 177 GLY n 
1 178 ASP n 
1 179 LEU n 
1 180 PRO n 
1 181 LEU n 
1 182 MET n 
1 183 VAL n 
1 184 HIS n 
1 185 ILE n 
1 186 GLY n 
1 187 ASN n 
1 188 ASN n 
1 189 PRO n 
1 190 PRO n 
1 191 ASN n 
1 192 LEU n 
1 193 ASP n 
1 194 GLU n 
1 195 ILE n 
1 196 ALA n 
1 197 GLU n 
1 198 LEU n 
1 199 LEU n 
1 200 SER n 
1 201 ARG n 
1 202 GLY n 
1 203 ASP n 
1 204 ILE n 
1 205 ILE n 
1 206 THR n 
1 207 HIS n 
1 208 CYS n 
1 209 TYR n 
1 210 ASN n 
1 211 GLY n 
1 212 LYS n 
1 213 PRO n 
1 214 ASN n 
1 215 ARG n 
1 216 ILE n 
1 217 LEU n 
1 218 ASN n 
1 219 PRO n 
1 220 ALA n 
1 221 GLY n 
1 222 GLU n 
1 223 LEU n 
1 224 ARG n 
1 225 SER n 
1 226 SER n 
1 227 ILE n 
1 228 THR n 
1 229 ARG n 
1 230 ALA n 
1 231 LEU n 
1 232 HIS n 
1 233 ARG n 
1 234 GLY n 
1 235 VAL n 
1 236 ARG n 
1 237 LEU n 
1 238 ASP n 
1 239 VAL n 
1 240 GLY n 
1 241 HIS n 
1 242 GLY n 
1 243 THR n 
1 244 ALA n 
1 245 SER n 
1 246 PHE n 
1 247 SER n 
1 248 PHE n 
1 249 GLU n 
1 250 VAL n 
1 251 ALA n 
1 252 ARG n 
1 253 ARG n 
1 254 ALA n 
1 255 ILE n 
1 256 ALA n 
1 257 LEU n 
1 258 GLY n 
1 259 ILE n 
1 260 LEU n 
1 261 PRO n 
1 262 HIS n 
1 263 THR n 
1 264 ILE n 
1 265 SER n 
1 266 SER n 
1 267 ASP n 
1 268 ILE n 
1 269 TYR n 
1 270 CYS n 
1 271 ARG n 
1 272 ASN n 
1 273 ARG n 
1 274 ILE n 
1 275 ASP n 
1 276 GLY n 
1 277 PRO n 
1 278 VAL n 
1 279 ARG n 
1 280 SER n 
1 281 LEU n 
1 282 ALA n 
1 283 LEU n 
1 284 VAL n 
1 285 MET n 
1 286 SER n 
1 287 LYS n 
1 288 PHE n 
1 289 LEU n 
1 290 ALA n 
1 291 ILE n 
1 292 GLY n 
1 293 MET n 
1 294 THR n 
1 295 LEU n 
1 296 PRO n 
1 297 GLN n 
1 298 VAL n 
1 299 ILE n 
1 300 ASP n 
1 301 CYS n 
1 302 VAL n 
1 303 THR n 
1 304 VAL n 
1 305 SER n 
1 306 ALA n 
1 307 ALA n 
1 308 GLU n 
1 309 GLY n 
1 310 LEU n 
1 311 ARG n 
1 312 LEU n 
1 313 SER n 
1 314 ARG n 
1 315 LYS n 
1 316 GLY n 
1 317 ARG n 
1 318 LEU n 
1 319 GLU n 
1 320 ALA n 
1 321 GLY n 
1 322 PHE n 
1 323 ASP n 
1 324 ALA n 
1 325 ASP n 
1 326 LEU n 
1 327 THR n 
1 328 LEU n 
1 329 PHE n 
1 330 ARG n 
1 331 LEU n 
1 332 GLU n 
1 333 ARG n 
1 334 GLN n 
1 335 PRO n 
1 336 THR n 
1 337 LEU n 
1 338 LEU n 
1 339 VAL n 
1 340 ASP n 
1 341 ALA n 
1 342 GLU n 
1 343 LYS n 
1 344 GLU n 
1 345 SER n 
1 346 LEU n 
1 347 GLN n 
1 348 ALA n 
1 349 ASP n 
1 350 ASN n 
1 351 ILE n 
1 352 LEU n 
1 353 VAL n 
1 354 PRO n 
1 355 LEU n 
1 356 ALA n 
1 357 ALA n 
1 358 ILE n 
1 359 ARG n 
1 360 ALA n 
1 361 GLY n 
1 362 LYS n 
1 363 GLY n 
1 364 TYR n 
1 365 LEU n 
1 366 THR n 
1 367 GLU n 
1 368 GLN n 
1 369 GLY n 
1 370 SER n 
1 371 ALA n 
1 372 GLU n 
1 373 HIS n 
1 374 ALA n 
1 375 PHE n 
1 376 ASP n 
1 377 PHE 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                   377 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 A9P88_23745 
_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      'Klebsiella sp. PCX' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     2686364 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                     ?                 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE                    ?                 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE                  ?                 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'             ?                 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE                    ?                 'C3 H7 N O2 S'   121.158 
EDO non-polymer         . 1,2-ETHANEDIOL              'ETHYLENE GLYCOL' 'C2 H6 O2'       62.068  
GLN 'L-peptide linking' y GLUTAMINE                   ?                 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'             ?                 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE                     ?                 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE                   ?                 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER                       ?                 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE                  ?                 'C6 H13 N O2'    131.173 
KCX 'L-peptide linking' n 'LYSINE NZ-CARBOXYLIC ACID' ?                 'C7 H14 N2 O4'   190.197 
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 
ZN  non-polymer         . 'ZINC ION'                  ?                 'Zn 2'           65.409  
# 
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   MET 1   1   1   MET MET A . n 
A 1 2   PHE 2   2   2   PHE PHE A . n 
A 1 3   ASP 3   3   3   ASP ASP A . n 
A 1 4   LEU 4   4   4   LEU LEU A . n 
A 1 5   LEU 5   5   5   LEU LEU A . n 
A 1 6   LEU 6   6   6   LEU LEU A . n 
A 1 7   ARG 7   7   7   ARG ARG A . n 
A 1 8   ARG 8   8   8   ARG ARG A . n 
A 1 9   ALA 9   9   9   ALA ALA A . n 
A 1 10  ARG 10  10  10  ARG ARG A . n 
A 1 11  LEU 11  11  11  LEU LEU A . n 
A 1 12  VAL 12  12  12  VAL VAL A . n 
A 1 13  ASP 13  13  13  ASP ASP A . n 
A 1 14  ASP 14  14  14  ASP ASP A . n 
A 1 15  THR 15  15  15  THR THR A . n 
A 1 16  LEU 16  16  16  LEU LEU A . n 
A 1 17  THR 17  17  17  THR THR A . n 
A 1 18  ASP 18  18  18  ASP ASP A . n 
A 1 19  ILE 19  19  19  ILE ILE A . n 
A 1 20  ALA 20  20  20  ALA ALA A . n 
A 1 21  ILE 21  21  21  ILE ILE A . n 
A 1 22  GLN 22  22  22  GLN GLN A . n 
A 1 23  ASP 23  23  23  ASP ASP A . n 
A 1 24  GLY 24  24  24  GLY GLY A . n 
A 1 25  LYS 25  25  25  LYS LYS A . n 
A 1 26  ILE 26  26  26  ILE ILE A . n 
A 1 27  ALA 27  27  27  ALA ALA A . n 
A 1 28  ALA 28  28  28  ALA ALA A . n 
A 1 29  LEU 29  29  29  LEU LEU A . n 
A 1 30  GLY 30  30  30  GLY GLY A . n 
A 1 31  GLU 31  31  31  GLU GLU A . n 
A 1 32  ILE 32  32  32  ILE ILE A . n 
A 1 33  SER 33  33  33  SER SER A . n 
A 1 34  ALA 34  34  34  ALA ALA A . n 
A 1 35  PRO 35  35  35  PRO PRO A . n 
A 1 36  SER 36  36  36  SER SER A . n 
A 1 37  ARG 37  37  37  ARG ARG A . n 
A 1 38  LYS 38  38  38  LYS LYS A . n 
A 1 39  THR 39  39  39  THR THR A . n 
A 1 40  ILE 40  40  40  ILE ILE A . n 
A 1 41  ASP 41  41  41  ASP ASP A . n 
A 1 42  LEU 42  42  42  LEU LEU A . n 
A 1 43  GLN 43  43  43  GLN GLN A . n 
A 1 44  GLY 44  44  44  GLY GLY A . n 
A 1 45  ASN 45  45  45  ASN ASN A . n 
A 1 46  SER 46  46  46  SER SER A . n 
A 1 47  TYR 47  47  47  TYR TYR A . n 
A 1 48  VAL 48  48  48  VAL VAL A . n 
A 1 49  SER 49  49  49  SER SER A . n 
A 1 50  ALA 50  50  50  ALA ALA A . n 
A 1 51  GLY 51  51  51  GLY GLY A . n 
A 1 52  TRP 52  52  52  TRP TRP A . n 
A 1 53  ILE 53  53  53  ILE ILE A . n 
A 1 54  ASP 54  54  54  ASP ASP A . n 
A 1 55  SER 55  55  55  SER SER A . n 
A 1 56  HIS 56  56  56  HIS HIS A . n 
A 1 57  VAL 57  57  57  VAL VAL A . n 
A 1 58  HIS 58  58  58  HIS HIS A . n 
A 1 59  CYS 59  59  59  CYS CYS A . n 
A 1 60  TYR 60  60  60  TYR TYR A . n 
A 1 61  PRO 61  61  61  PRO PRO A . n 
A 1 62  ASN 62  62  62  ASN ASN A . n 
A 1 63  SER 63  63  63  SER SER A . n 
A 1 64  PRO 64  64  64  PRO PRO A . n 
A 1 65  ILE 65  65  65  ILE ILE A . n 
A 1 66  TYR 66  66  66  TYR TYR A . n 
A 1 67  HIS 67  67  67  HIS HIS A . n 
A 1 68  ASP 68  68  68  ASP ASP A . n 
A 1 69  GLU 69  69  69  GLU GLU A . n 
A 1 70  PRO 70  70  70  PRO PRO A . n 
A 1 71  ASP 71  71  71  ASP ASP A . n 
A 1 72  SER 72  72  72  SER SER A . n 
A 1 73  VAL 73  73  73  VAL VAL A . n 
A 1 74  GLY 74  74  74  GLY GLY A . n 
A 1 75  ILE 75  75  75  ILE ILE A . n 
A 1 76  ALA 76  76  76  ALA ALA A . n 
A 1 77  THR 77  77  77  THR THR A . n 
A 1 78  GLY 78  78  78  GLY GLY A . n 
A 1 79  VAL 79  79  79  VAL VAL A . n 
A 1 80  THR 80  80  80  THR THR A . n 
A 1 81  THR 81  81  81  THR THR A . n 
A 1 82  VAL 82  82  82  VAL VAL A . n 
A 1 83  ILE 83  83  83  ILE ILE A . n 
A 1 84  ASP 84  84  84  ASP ASP A . n 
A 1 85  ALA 85  85  85  ALA ALA A . n 
A 1 86  GLY 86  86  86  GLY GLY A . n 
A 1 87  SER 87  87  87  SER SER A . n 
A 1 88  THR 88  88  88  THR THR A . n 
A 1 89  GLY 89  89  89  GLY GLY A . n 
A 1 90  ALA 90  90  90  ALA ALA A . n 
A 1 91  ASP 91  91  91  ASP ASP A . n 
A 1 92  ASP 92  92  92  ASP ASP A . n 
A 1 93  VAL 93  93  93  VAL VAL A . n 
A 1 94  ASP 94  94  94  ASP ASP A . n 
A 1 95  ASP 95  95  95  ASP ASP A . n 
A 1 96  PHE 96  96  96  PHE PHE A . n 
A 1 97  TYR 97  97  97  TYR TYR A . n 
A 1 98  GLN 98  98  98  GLN GLN A . n 
A 1 99  LEU 99  99  99  LEU LEU A . n 
A 1 100 THR 100 100 100 THR THR A . n 
A 1 101 ARG 101 101 101 ARG ARG A . n 
A 1 102 LYS 102 102 102 LYS LYS A . n 
A 1 103 ALA 103 103 103 ALA ALA A . n 
A 1 104 VAL 104 104 104 VAL VAL A . n 
A 1 105 THR 105 105 105 THR THR A . n 
A 1 106 GLU 106 106 106 GLU GLU A . n 
A 1 107 VAL 107 107 107 VAL VAL A . n 
A 1 108 TYR 108 108 108 TYR TYR A . n 
A 1 109 ALA 109 109 109 ALA ALA A . n 
A 1 110 LEU 110 110 110 LEU LEU A . n 
A 1 111 LEU 111 111 111 LEU LEU A . n 
A 1 112 ASN 112 112 112 ASN ASN A . n 
A 1 113 ILE 113 113 113 ILE ILE A . n 
A 1 114 SER 114 114 114 SER SER A . n 
A 1 115 ARG 115 115 115 ARG ARG A . n 
A 1 116 VAL 116 116 116 VAL VAL A . n 
A 1 117 GLY 117 117 117 GLY GLY A . n 
A 1 118 LEU 118 118 118 LEU LEU A . n 
A 1 119 ILE 119 119 119 ILE ILE A . n 
A 1 120 ALA 120 120 120 ALA ALA A . n 
A 1 121 GLN 121 121 121 GLN GLN A . n 
A 1 122 ASN 122 122 122 ASN ASN A . n 
A 1 123 GLU 123 123 123 GLU GLU A . n 
A 1 124 LEU 124 124 124 LEU LEU A . n 
A 1 125 ALA 125 125 125 ALA ALA A . n 
A 1 126 ASN 126 126 126 ASN ASN A . n 
A 1 127 LEU 127 127 127 LEU LEU A . n 
A 1 128 ALA 128 128 128 ALA ALA A . n 
A 1 129 ASN 129 129 129 ASN ASN A . n 
A 1 130 ILE 130 130 130 ILE ILE A . n 
A 1 131 ASP 131 131 131 ASP ASP A . n 
A 1 132 ALA 132 132 132 ALA ALA A . n 
A 1 133 GLU 133 133 133 GLU GLU A . n 
A 1 134 ALA 134 134 134 ALA ALA A . n 
A 1 135 VAL 135 135 135 VAL VAL A . n 
A 1 136 LYS 136 136 136 LYS LYS A . n 
A 1 137 GLN 137 137 137 GLN GLN A . n 
A 1 138 ALA 138 138 138 ALA ALA A . n 
A 1 139 VAL 139 139 139 VAL VAL A . n 
A 1 140 GLN 140 140 140 GLN GLN A . n 
A 1 141 ARG 141 141 141 ARG ARG A . n 
A 1 142 HIS 142 142 142 HIS HIS A . n 
A 1 143 PRO 143 143 143 PRO PRO A . n 
A 1 144 ASP 144 144 144 ASP ASP A . n 
A 1 145 PHE 145 145 145 PHE PHE A . n 
A 1 146 ILE 146 146 146 ILE ILE A . n 
A 1 147 VAL 147 147 147 VAL VAL A . n 
A 1 148 GLY 148 148 148 GLY GLY A . n 
A 1 149 LEU 149 149 149 LEU LEU A . n 
A 1 150 KCX 150 150 150 KCX KCX A . n 
A 1 151 ALA 151 151 151 ALA ALA A . n 
A 1 152 ARG 152 152 152 ARG ARG A . n 
A 1 153 MET 153 153 153 MET MET A . n 
A 1 154 SER 154 154 154 SER SER A . n 
A 1 155 SER 155 155 155 SER SER 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 VAL 158 158 158 VAL VAL A . n 
A 1 159 GLY 159 159 159 GLY GLY A . n 
A 1 160 GLU 160 160 160 GLU GLU A . n 
A 1 161 ASN 161 161 161 ASN ASN A . n 
A 1 162 GLY 162 162 162 GLY GLY A . n 
A 1 163 ILE 163 163 163 ILE ILE A . n 
A 1 164 THR 164 164 164 THR THR A . n 
A 1 165 PRO 165 165 165 PRO PRO A . n 
A 1 166 LEU 166 166 166 LEU LEU A . n 
A 1 167 ALA 167 167 167 ALA ALA A . n 
A 1 168 ARG 168 168 168 ARG ARG A . n 
A 1 169 ALA 169 169 169 ALA ALA A . n 
A 1 170 LYS 170 170 170 LYS LYS A . n 
A 1 171 THR 171 171 171 THR THR A . n 
A 1 172 MET 172 172 172 MET MET A . n 
A 1 173 GLN 173 173 173 GLN GLN A . n 
A 1 174 GLN 174 174 174 GLN GLN A . n 
A 1 175 GLU 175 175 175 GLU GLU A . n 
A 1 176 ASN 176 176 176 ASN ASN A . n 
A 1 177 GLY 177 177 177 GLY GLY A . n 
A 1 178 ASP 178 178 178 ASP ASP A . n 
A 1 179 LEU 179 179 179 LEU LEU A . n 
A 1 180 PRO 180 180 180 PRO PRO A . n 
A 1 181 LEU 181 181 181 LEU LEU A . n 
A 1 182 MET 182 182 182 MET MET A . n 
A 1 183 VAL 183 183 183 VAL VAL A . n 
A 1 184 HIS 184 184 184 HIS HIS A . n 
A 1 185 ILE 185 185 185 ILE ILE A . n 
A 1 186 GLY 186 186 186 GLY GLY A . n 
A 1 187 ASN 187 187 187 ASN ASN A . n 
A 1 188 ASN 188 188 188 ASN ASN A . n 
A 1 189 PRO 189 189 189 PRO PRO A . n 
A 1 190 PRO 190 190 190 PRO PRO A . n 
A 1 191 ASN 191 191 191 ASN ASN A . n 
A 1 192 LEU 192 192 192 LEU LEU A . n 
A 1 193 ASP 193 193 193 ASP ASP 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 ALA 196 196 196 ALA ALA A . n 
A 1 197 GLU 197 197 197 GLU GLU A . n 
A 1 198 LEU 198 198 198 LEU LEU A . n 
A 1 199 LEU 199 199 199 LEU LEU A . n 
A 1 200 SER 200 200 200 SER SER A . n 
A 1 201 ARG 201 201 201 ARG ARG A . n 
A 1 202 GLY 202 202 ?   ?   ?   A . n 
A 1 203 ASP 203 203 203 ASP ASP A . n 
A 1 204 ILE 204 204 204 ILE ILE A . n 
A 1 205 ILE 205 205 205 ILE ILE A . n 
A 1 206 THR 206 206 206 THR THR A . n 
A 1 207 HIS 207 207 207 HIS HIS A . n 
A 1 208 CYS 208 208 208 CYS CYS A . n 
A 1 209 TYR 209 209 209 TYR TYR A . n 
A 1 210 ASN 210 210 210 ASN ASN A . n 
A 1 211 GLY 211 211 211 GLY GLY A . n 
A 1 212 LYS 212 212 212 LYS LYS A . n 
A 1 213 PRO 213 213 213 PRO PRO A . n 
A 1 214 ASN 214 214 214 ASN ASN A . n 
A 1 215 ARG 215 215 215 ARG ARG A . n 
A 1 216 ILE 216 216 216 ILE ILE A . n 
A 1 217 LEU 217 217 217 LEU LEU A . n 
A 1 218 ASN 218 218 218 ASN ASN A . n 
A 1 219 PRO 219 219 219 PRO PRO A . n 
A 1 220 ALA 220 220 220 ALA ALA A . n 
A 1 221 GLY 221 221 221 GLY GLY A . n 
A 1 222 GLU 222 222 222 GLU GLU A . n 
A 1 223 LEU 223 223 223 LEU LEU A . n 
A 1 224 ARG 224 224 224 ARG ARG A . n 
A 1 225 SER 225 225 225 SER SER A . n 
A 1 226 SER 226 226 226 SER SER A . n 
A 1 227 ILE 227 227 227 ILE ILE A . n 
A 1 228 THR 228 228 228 THR THR A . n 
A 1 229 ARG 229 229 229 ARG ARG A . n 
A 1 230 ALA 230 230 230 ALA ALA A . n 
A 1 231 LEU 231 231 231 LEU LEU A . n 
A 1 232 HIS 232 232 232 HIS HIS A . n 
A 1 233 ARG 233 233 233 ARG ARG A . n 
A 1 234 GLY 234 234 234 GLY GLY A . n 
A 1 235 VAL 235 235 235 VAL VAL A . n 
A 1 236 ARG 236 236 236 ARG ARG A . n 
A 1 237 LEU 237 237 237 LEU LEU A . n 
A 1 238 ASP 238 238 238 ASP ASP A . n 
A 1 239 VAL 239 239 239 VAL VAL A . n 
A 1 240 GLY 240 240 240 GLY GLY A . n 
A 1 241 HIS 241 241 241 HIS HIS A . n 
A 1 242 GLY 242 242 242 GLY GLY A . n 
A 1 243 THR 243 243 243 THR THR A . n 
A 1 244 ALA 244 244 244 ALA ALA A . n 
A 1 245 SER 245 245 245 SER SER A . n 
A 1 246 PHE 246 246 246 PHE PHE A . n 
A 1 247 SER 247 247 247 SER SER A . n 
A 1 248 PHE 248 248 248 PHE PHE A . n 
A 1 249 GLU 249 249 249 GLU GLU A . n 
A 1 250 VAL 250 250 250 VAL VAL A . n 
A 1 251 ALA 251 251 251 ALA ALA A . n 
A 1 252 ARG 252 252 252 ARG ARG A . n 
A 1 253 ARG 253 253 253 ARG ARG A . n 
A 1 254 ALA 254 254 254 ALA ALA A . n 
A 1 255 ILE 255 255 255 ILE ILE A . n 
A 1 256 ALA 256 256 256 ALA ALA A . n 
A 1 257 LEU 257 257 257 LEU LEU A . n 
A 1 258 GLY 258 258 258 GLY GLY A . n 
A 1 259 ILE 259 259 259 ILE ILE A . n 
A 1 260 LEU 260 260 260 LEU LEU A . n 
A 1 261 PRO 261 261 261 PRO PRO A . n 
A 1 262 HIS 262 262 262 HIS HIS A . n 
A 1 263 THR 263 263 263 THR THR A . n 
A 1 264 ILE 264 264 264 ILE ILE A . n 
A 1 265 SER 265 265 265 SER SER A . n 
A 1 266 SER 266 266 266 SER SER A . n 
A 1 267 ASP 267 267 267 ASP ASP A . n 
A 1 268 ILE 268 268 268 ILE ILE A . n 
A 1 269 TYR 269 269 269 TYR TYR A . n 
A 1 270 CYS 270 270 270 CYS CYS A . n 
A 1 271 ARG 271 271 271 ARG ARG A . n 
A 1 272 ASN 272 272 272 ASN ASN A . n 
A 1 273 ARG 273 273 273 ARG ARG A . n 
A 1 274 ILE 274 274 274 ILE ILE A . n 
A 1 275 ASP 275 275 275 ASP ASP A . n 
A 1 276 GLY 276 276 276 GLY GLY A . n 
A 1 277 PRO 277 277 277 PRO PRO A . n 
A 1 278 VAL 278 278 278 VAL VAL A . n 
A 1 279 ARG 279 279 279 ARG ARG A . n 
A 1 280 SER 280 280 280 SER SER A . n 
A 1 281 LEU 281 281 281 LEU LEU A . n 
A 1 282 ALA 282 282 282 ALA ALA A . n 
A 1 283 LEU 283 283 283 LEU LEU A . n 
A 1 284 VAL 284 284 284 VAL VAL A . n 
A 1 285 MET 285 285 285 MET MET A . n 
A 1 286 SER 286 286 286 SER SER A . n 
A 1 287 LYS 287 287 287 LYS LYS A . n 
A 1 288 PHE 288 288 288 PHE PHE A . n 
A 1 289 LEU 289 289 289 LEU LEU A . n 
A 1 290 ALA 290 290 290 ALA ALA A . n 
A 1 291 ILE 291 291 291 ILE ILE A . n 
A 1 292 GLY 292 292 292 GLY GLY A . n 
A 1 293 MET 293 293 293 MET MET A . n 
A 1 294 THR 294 294 294 THR THR A . n 
A 1 295 LEU 295 295 295 LEU LEU A . n 
A 1 296 PRO 296 296 296 PRO PRO A . n 
A 1 297 GLN 297 297 297 GLN GLN A . n 
A 1 298 VAL 298 298 298 VAL VAL A . n 
A 1 299 ILE 299 299 299 ILE ILE A . n 
A 1 300 ASP 300 300 300 ASP ASP A . n 
A 1 301 CYS 301 301 301 CYS CYS A . n 
A 1 302 VAL 302 302 302 VAL VAL A . n 
A 1 303 THR 303 303 303 THR THR A . n 
A 1 304 VAL 304 304 304 VAL VAL A . n 
A 1 305 SER 305 305 305 SER SER A . n 
A 1 306 ALA 306 306 306 ALA ALA A . n 
A 1 307 ALA 307 307 307 ALA ALA A . n 
A 1 308 GLU 308 308 308 GLU GLU A . n 
A 1 309 GLY 309 309 309 GLY GLY A . n 
A 1 310 LEU 310 310 310 LEU LEU A . n 
A 1 311 ARG 311 311 311 ARG ARG A . n 
A 1 312 LEU 312 312 312 LEU LEU A . n 
A 1 313 SER 313 313 313 SER SER A . n 
A 1 314 ARG 314 314 314 ARG ARG A . n 
A 1 315 LYS 315 315 315 LYS LYS A . n 
A 1 316 GLY 316 316 316 GLY GLY A . n 
A 1 317 ARG 317 317 317 ARG ARG A . n 
A 1 318 LEU 318 318 318 LEU LEU A . n 
A 1 319 GLU 319 319 319 GLU GLU A . n 
A 1 320 ALA 320 320 320 ALA ALA A . n 
A 1 321 GLY 321 321 321 GLY GLY A . n 
A 1 322 PHE 322 322 322 PHE PHE A . n 
A 1 323 ASP 323 323 323 ASP ASP A . n 
A 1 324 ALA 324 324 324 ALA ALA A . n 
A 1 325 ASP 325 325 325 ASP ASP A . n 
A 1 326 LEU 326 326 326 LEU LEU A . n 
A 1 327 THR 327 327 327 THR THR A . n 
A 1 328 LEU 328 328 328 LEU LEU A . n 
A 1 329 PHE 329 329 329 PHE PHE A . n 
A 1 330 ARG 330 330 330 ARG ARG A . n 
A 1 331 LEU 331 331 331 LEU LEU A . n 
A 1 332 GLU 332 332 332 GLU GLU A . n 
A 1 333 ARG 333 333 333 ARG ARG A . n 
A 1 334 GLN 334 334 334 GLN GLN A . n 
A 1 335 PRO 335 335 335 PRO PRO A . n 
A 1 336 THR 336 336 336 THR THR A . n 
A 1 337 LEU 337 337 337 LEU LEU A . n 
A 1 338 LEU 338 338 338 LEU LEU A . n 
A 1 339 VAL 339 339 339 VAL VAL A . n 
A 1 340 ASP 340 340 340 ASP ASP A . n 
A 1 341 ALA 341 341 341 ALA ALA A . n 
A 1 342 GLU 342 342 342 GLU GLU A . n 
A 1 343 LYS 343 343 343 LYS LYS A . n 
A 1 344 GLU 344 344 344 GLU GLU A . n 
A 1 345 SER 345 345 345 SER SER A . n 
A 1 346 LEU 346 346 346 LEU LEU A . n 
A 1 347 GLN 347 347 347 GLN GLN A . n 
A 1 348 ALA 348 348 348 ALA ALA A . n 
A 1 349 ASP 349 349 349 ASP ASP A . n 
A 1 350 ASN 350 350 350 ASN ASN A . n 
A 1 351 ILE 351 351 351 ILE ILE A . n 
A 1 352 LEU 352 352 352 LEU LEU A . n 
A 1 353 VAL 353 353 353 VAL VAL 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 ALA 356 356 356 ALA ALA A . n 
A 1 357 ALA 357 357 357 ALA ALA A . n 
A 1 358 ILE 358 358 358 ILE ILE A . n 
A 1 359 ARG 359 359 359 ARG ARG A . n 
A 1 360 ALA 360 360 360 ALA ALA A . n 
A 1 361 GLY 361 361 361 GLY GLY A . n 
A 1 362 LYS 362 362 362 LYS LYS A . n 
A 1 363 GLY 363 363 363 GLY GLY A . n 
A 1 364 TYR 364 364 364 TYR TYR A . n 
A 1 365 LEU 365 365 365 LEU LEU A . n 
A 1 366 THR 366 366 366 THR THR A . n 
A 1 367 GLU 367 367 367 GLU GLU A . n 
A 1 368 GLN 368 368 368 GLN GLN A . n 
A 1 369 GLY 369 369 369 GLY GLY A . n 
A 1 370 SER 370 370 370 SER SER A . n 
A 1 371 ALA 371 371 371 ALA ALA A . n 
A 1 372 GLU 372 372 372 GLU GLU A . n 
A 1 373 HIS 373 373 373 HIS HIS A . n 
A 1 374 ALA 374 374 374 ALA ALA A . n 
A 1 375 PHE 375 375 375 PHE PHE A . n 
A 1 376 ASP 376 376 376 ASP ASP A . n 
A 1 377 PHE 377 377 377 PHE PHE 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 EDO 1   401 401 EDO EDO A . 
C 2 EDO 1   402 402 EDO EDO A . 
D 2 EDO 1   403 403 EDO EDO A . 
E 2 EDO 1   404 404 EDO EDO A . 
F 3 ZN  1   405 1   ZN  ZN  A . 
G 3 ZN  1   406 2   ZN  ZN  A . 
H 4 HOH 1   501 126 HOH HOH A . 
H 4 HOH 2   502 24  HOH HOH A . 
H 4 HOH 3   503 142 HOH HOH A . 
H 4 HOH 4   504 27  HOH HOH A . 
H 4 HOH 5   505 11  HOH HOH A . 
H 4 HOH 6   506 2   HOH HOH A . 
H 4 HOH 7   507 21  HOH HOH A . 
H 4 HOH 8   508 115 HOH HOH A . 
H 4 HOH 9   509 125 HOH HOH A . 
H 4 HOH 10  510 128 HOH HOH A . 
H 4 HOH 11  511 25  HOH HOH A . 
H 4 HOH 12  512 94  HOH HOH A . 
H 4 HOH 13  513 152 HOH HOH A . 
H 4 HOH 14  514 89  HOH HOH A . 
H 4 HOH 15  515 72  HOH HOH A . 
H 4 HOH 16  516 88  HOH HOH A . 
H 4 HOH 17  517 80  HOH HOH A . 
H 4 HOH 18  518 16  HOH HOH A . 
H 4 HOH 19  519 69  HOH HOH A . 
H 4 HOH 20  520 103 HOH HOH A . 
H 4 HOH 21  521 19  HOH HOH A . 
H 4 HOH 22  522 33  HOH HOH A . 
H 4 HOH 23  523 22  HOH HOH A . 
H 4 HOH 24  524 32  HOH HOH A . 
H 4 HOH 25  525 81  HOH HOH A . 
H 4 HOH 26  526 47  HOH HOH A . 
H 4 HOH 27  527 7   HOH HOH A . 
H 4 HOH 28  528 41  HOH HOH A . 
H 4 HOH 29  529 160 HOH HOH A . 
H 4 HOH 30  530 51  HOH HOH A . 
H 4 HOH 31  531 118 HOH HOH A . 
H 4 HOH 32  532 167 HOH HOH A . 
H 4 HOH 33  533 138 HOH HOH A . 
H 4 HOH 34  534 60  HOH HOH A . 
H 4 HOH 35  535 42  HOH HOH A . 
H 4 HOH 36  536 92  HOH HOH A . 
H 4 HOH 37  537 20  HOH HOH A . 
H 4 HOH 38  538 76  HOH HOH A . 
H 4 HOH 39  539 3   HOH HOH A . 
H 4 HOH 40  540 17  HOH HOH A . 
H 4 HOH 41  541 28  HOH HOH A . 
H 4 HOH 42  542 36  HOH HOH A . 
H 4 HOH 43  543 98  HOH HOH A . 
H 4 HOH 44  544 85  HOH HOH A . 
H 4 HOH 45  545 26  HOH HOH A . 
H 4 HOH 46  546 63  HOH HOH A . 
H 4 HOH 47  547 8   HOH HOH A . 
H 4 HOH 48  548 15  HOH HOH A . 
H 4 HOH 49  549 46  HOH HOH A . 
H 4 HOH 50  550 95  HOH HOH A . 
H 4 HOH 51  551 55  HOH HOH A . 
H 4 HOH 52  552 90  HOH HOH A . 
H 4 HOH 53  553 104 HOH HOH A . 
H 4 HOH 54  554 114 HOH HOH A . 
H 4 HOH 55  555 4   HOH HOH A . 
H 4 HOH 56  556 132 HOH HOH A . 
H 4 HOH 57  557 29  HOH HOH A . 
H 4 HOH 58  558 31  HOH HOH A . 
H 4 HOH 59  559 23  HOH HOH A . 
H 4 HOH 60  560 56  HOH HOH A . 
H 4 HOH 61  561 10  HOH HOH A . 
H 4 HOH 62  562 35  HOH HOH A . 
H 4 HOH 63  563 6   HOH HOH A . 
H 4 HOH 64  564 1   HOH HOH A . 
H 4 HOH 65  565 65  HOH HOH A . 
H 4 HOH 66  566 101 HOH HOH A . 
H 4 HOH 67  567 53  HOH HOH A . 
H 4 HOH 68  568 139 HOH HOH A . 
H 4 HOH 69  569 83  HOH HOH A . 
H 4 HOH 70  570 34  HOH HOH A . 
H 4 HOH 71  571 99  HOH HOH A . 
H 4 HOH 72  572 75  HOH HOH A . 
H 4 HOH 73  573 12  HOH HOH A . 
H 4 HOH 74  574 30  HOH HOH A . 
H 4 HOH 75  575 100 HOH HOH A . 
H 4 HOH 76  576 13  HOH HOH A . 
H 4 HOH 77  577 123 HOH HOH A . 
H 4 HOH 78  578 50  HOH HOH A . 
H 4 HOH 79  579 157 HOH HOH A . 
H 4 HOH 80  580 177 HOH HOH A . 
H 4 HOH 81  581 119 HOH HOH A . 
H 4 HOH 82  582 9   HOH HOH A . 
H 4 HOH 83  583 86  HOH HOH A . 
H 4 HOH 84  584 67  HOH HOH A . 
H 4 HOH 85  585 131 HOH HOH A . 
H 4 HOH 86  586 113 HOH HOH A . 
H 4 HOH 87  587 122 HOH HOH A . 
H 4 HOH 88  588 54  HOH HOH A . 
H 4 HOH 89  589 79  HOH HOH A . 
H 4 HOH 90  590 109 HOH HOH A . 
H 4 HOH 91  591 146 HOH HOH A . 
H 4 HOH 92  592 112 HOH HOH A . 
H 4 HOH 93  593 52  HOH HOH A . 
H 4 HOH 94  594 153 HOH HOH A . 
H 4 HOH 95  595 37  HOH HOH A . 
H 4 HOH 96  596 44  HOH HOH A . 
H 4 HOH 97  597 82  HOH HOH A . 
H 4 HOH 98  598 5   HOH HOH A . 
H 4 HOH 99  599 71  HOH HOH A . 
H 4 HOH 100 600 64  HOH HOH A . 
H 4 HOH 101 601 39  HOH HOH A . 
H 4 HOH 102 602 48  HOH HOH A . 
H 4 HOH 103 603 49  HOH HOH A . 
H 4 HOH 104 604 105 HOH HOH A . 
H 4 HOH 105 605 135 HOH HOH A . 
H 4 HOH 106 606 107 HOH HOH A . 
H 4 HOH 107 607 93  HOH HOH A . 
H 4 HOH 108 608 18  HOH HOH A . 
H 4 HOH 109 609 165 HOH HOH A . 
H 4 HOH 110 610 14  HOH HOH A . 
H 4 HOH 111 611 111 HOH HOH A . 
H 4 HOH 112 612 143 HOH HOH A . 
H 4 HOH 113 613 171 HOH HOH A . 
H 4 HOH 114 614 172 HOH HOH A . 
H 4 HOH 115 615 170 HOH HOH A . 
H 4 HOH 116 616 121 HOH HOH A . 
H 4 HOH 117 617 161 HOH HOH A . 
H 4 HOH 118 618 68  HOH HOH A . 
H 4 HOH 119 619 168 HOH HOH A . 
H 4 HOH 120 620 57  HOH HOH A . 
H 4 HOH 121 621 134 HOH HOH A . 
H 4 HOH 122 622 116 HOH HOH A . 
H 4 HOH 123 623 96  HOH HOH A . 
H 4 HOH 124 624 149 HOH HOH A . 
H 4 HOH 125 625 136 HOH HOH A . 
H 4 HOH 126 626 164 HOH HOH A . 
H 4 HOH 127 627 175 HOH HOH A . 
H 4 HOH 128 628 169 HOH HOH A . 
H 4 HOH 129 629 73  HOH HOH A . 
H 4 HOH 130 630 151 HOH HOH A . 
H 4 HOH 131 631 150 HOH HOH A . 
H 4 HOH 132 632 148 HOH HOH A . 
H 4 HOH 133 633 77  HOH HOH A . 
H 4 HOH 134 634 174 HOH HOH A . 
H 4 HOH 135 635 162 HOH HOH A . 
H 4 HOH 136 636 74  HOH HOH A . 
H 4 HOH 137 637 176 HOH HOH A . 
H 4 HOH 138 638 144 HOH HOH A . 
H 4 HOH 139 639 173 HOH HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1   1 Y 1 A ARG 37  ? CG  ? A ARG 37  CG  
2   1 Y 1 A ARG 37  ? CD  ? A ARG 37  CD  
3   1 Y 1 A ARG 37  ? NE  ? A ARG 37  NE  
4   1 Y 1 A ARG 37  ? CZ  ? A ARG 37  CZ  
5   1 Y 1 A ARG 37  ? NH1 ? A ARG 37  NH1 
6   1 Y 1 A ARG 37  ? NH2 ? A ARG 37  NH2 
7   1 Y 1 A LEU 99  ? CG  ? A LEU 99  CG  
8   1 Y 1 A LEU 99  ? CD1 ? A LEU 99  CD1 
9   1 Y 1 A LEU 99  ? CD2 ? A LEU 99  CD2 
10  1 Y 1 A LYS 102 ? CG  ? A LYS 102 CG  
11  1 Y 1 A LYS 102 ? CD  ? A LYS 102 CD  
12  1 Y 1 A LYS 102 ? CE  ? A LYS 102 CE  
13  1 Y 1 A LYS 102 ? NZ  ? A LYS 102 NZ  
14  1 Y 1 A ARG 115 ? CG  ? A ARG 115 CG  
15  1 Y 1 A ARG 115 ? CD  ? A ARG 115 CD  
16  1 Y 1 A ARG 115 ? NE  ? A ARG 115 NE  
17  1 Y 1 A ARG 115 ? CZ  ? A ARG 115 CZ  
18  1 Y 1 A ARG 115 ? NH1 ? A ARG 115 NH1 
19  1 Y 1 A ARG 115 ? NH2 ? A ARG 115 NH2 
20  1 Y 1 A ILE 119 ? CG1 ? A ILE 119 CG1 
21  1 Y 1 A ILE 119 ? CG2 ? A ILE 119 CG2 
22  1 Y 1 A ILE 119 ? CD1 ? A ILE 119 CD1 
23  1 Y 1 A GLN 121 ? CG  ? A GLN 121 CG  
24  1 Y 1 A GLN 121 ? CD  ? A GLN 121 CD  
25  1 Y 1 A GLN 121 ? OE1 ? A GLN 121 OE1 
26  1 Y 1 A GLN 121 ? NE2 ? A GLN 121 NE2 
27  1 Y 1 A GLU 133 ? CG  ? A GLU 133 CG  
28  1 Y 1 A GLU 133 ? CD  ? A GLU 133 CD  
29  1 Y 1 A GLU 133 ? OE1 ? A GLU 133 OE1 
30  1 Y 1 A GLU 133 ? OE2 ? A GLU 133 OE2 
31  1 Y 1 A LYS 136 ? CG  ? A LYS 136 CG  
32  1 Y 1 A LYS 136 ? CD  ? A LYS 136 CD  
33  1 Y 1 A LYS 136 ? CE  ? A LYS 136 CE  
34  1 Y 1 A LYS 136 ? NZ  ? A LYS 136 NZ  
35  1 Y 1 A GLN 137 ? CG  ? A GLN 137 CG  
36  1 Y 1 A GLN 137 ? CD  ? A GLN 137 CD  
37  1 Y 1 A GLN 137 ? OE1 ? A GLN 137 OE1 
38  1 Y 1 A GLN 137 ? NE2 ? A GLN 137 NE2 
39  1 Y 1 A GLU 160 ? CG  ? A GLU 160 CG  
40  1 Y 1 A GLU 160 ? CD  ? A GLU 160 CD  
41  1 Y 1 A GLU 160 ? OE1 ? A GLU 160 OE1 
42  1 Y 1 A GLU 160 ? OE2 ? A GLU 160 OE2 
43  1 Y 1 A ASP 193 ? CG  ? A ASP 193 CG  
44  1 Y 1 A ASP 193 ? OD1 ? A ASP 193 OD1 
45  1 Y 1 A ASP 193 ? OD2 ? A ASP 193 OD2 
46  1 Y 1 A GLU 194 ? CG  ? A GLU 194 CG  
47  1 Y 1 A GLU 194 ? CD  ? A GLU 194 CD  
48  1 Y 1 A GLU 194 ? OE1 ? A GLU 194 OE1 
49  1 Y 1 A GLU 194 ? OE2 ? A GLU 194 OE2 
50  1 Y 1 A ARG 201 ? CG  ? A ARG 201 CG  
51  1 Y 1 A ARG 201 ? CD  ? A ARG 201 CD  
52  1 Y 1 A ARG 201 ? NE  ? A ARG 201 NE  
53  1 Y 1 A ARG 201 ? CZ  ? A ARG 201 CZ  
54  1 Y 1 A ARG 201 ? NH1 ? A ARG 201 NH1 
55  1 Y 1 A ARG 201 ? NH2 ? A ARG 201 NH2 
56  1 Y 1 A GLU 249 ? CG  ? A GLU 249 CG  
57  1 Y 1 A GLU 249 ? CD  ? A GLU 249 CD  
58  1 Y 1 A GLU 249 ? OE1 ? A GLU 249 OE1 
59  1 Y 1 A GLU 249 ? OE2 ? A GLU 249 OE2 
60  1 Y 1 A ARG 271 ? CG  ? A ARG 271 CG  
61  1 Y 1 A ARG 271 ? CD  ? A ARG 271 CD  
62  1 Y 1 A ARG 271 ? NE  ? A ARG 271 NE  
63  1 Y 1 A ARG 271 ? CZ  ? A ARG 271 CZ  
64  1 Y 1 A ARG 271 ? NH1 ? A ARG 271 NH1 
65  1 Y 1 A ARG 271 ? NH2 ? A ARG 271 NH2 
66  1 Y 1 A LEU 331 ? CG  ? A LEU 331 CG  
67  1 Y 1 A LEU 331 ? CD1 ? A LEU 331 CD1 
68  1 Y 1 A LEU 331 ? CD2 ? A LEU 331 CD2 
69  1 Y 1 A ARG 333 ? CG  ? A ARG 333 CG  
70  1 Y 1 A ARG 333 ? CD  ? A ARG 333 CD  
71  1 Y 1 A ARG 333 ? NE  ? A ARG 333 NE  
72  1 Y 1 A ARG 333 ? CZ  ? A ARG 333 CZ  
73  1 Y 1 A ARG 333 ? NH1 ? A ARG 333 NH1 
74  1 Y 1 A ARG 333 ? NH2 ? A ARG 333 NH2 
75  1 Y 1 A GLN 334 ? CG  ? A GLN 334 CG  
76  1 Y 1 A GLN 334 ? CD  ? A GLN 334 CD  
77  1 Y 1 A GLN 334 ? OE1 ? A GLN 334 OE1 
78  1 Y 1 A GLN 334 ? NE2 ? A GLN 334 NE2 
79  1 Y 1 A LEU 337 ? CG  ? A LEU 337 CG  
80  1 Y 1 A LEU 337 ? CD1 ? A LEU 337 CD1 
81  1 Y 1 A LEU 337 ? CD2 ? A LEU 337 CD2 
82  1 Y 1 A GLU 342 ? CG  ? A GLU 342 CG  
83  1 Y 1 A GLU 342 ? CD  ? A GLU 342 CD  
84  1 Y 1 A GLU 342 ? OE1 ? A GLU 342 OE1 
85  1 Y 1 A GLU 342 ? OE2 ? A GLU 342 OE2 
86  1 Y 1 A LYS 343 ? CG  ? A LYS 343 CG  
87  1 Y 1 A LYS 343 ? CD  ? A LYS 343 CD  
88  1 Y 1 A LYS 343 ? CE  ? A LYS 343 CE  
89  1 Y 1 A LYS 343 ? NZ  ? A LYS 343 NZ  
90  1 Y 1 A GLU 344 ? CG  ? A GLU 344 CG  
91  1 Y 1 A GLU 344 ? CD  ? A GLU 344 CD  
92  1 Y 1 A GLU 344 ? OE1 ? A GLU 344 OE1 
93  1 Y 1 A GLU 344 ? OE2 ? A GLU 344 OE2 
94  1 Y 1 A GLN 347 ? CG  ? A GLN 347 CG  
95  1 Y 1 A GLN 347 ? CD  ? A GLN 347 CD  
96  1 Y 1 A GLN 347 ? OE1 ? A GLN 347 OE1 
97  1 Y 1 A GLN 347 ? NE2 ? A GLN 347 NE2 
98  1 Y 1 A ASP 349 ? CG  ? A ASP 349 CG  
99  1 Y 1 A ASP 349 ? OD1 ? A ASP 349 OD1 
100 1 Y 1 A ASP 349 ? OD2 ? A ASP 349 OD2 
101 1 Y 1 A LYS 362 ? CG  ? A LYS 362 CG  
102 1 Y 1 A LYS 362 ? CD  ? A LYS 362 CD  
103 1 Y 1 A LYS 362 ? CE  ? A LYS 362 CE  
104 1 Y 1 A LYS 362 ? NZ  ? A LYS 362 NZ  
105 1 Y 1 A GLU 367 ? CG  ? A GLU 367 CG  
106 1 Y 1 A GLU 367 ? CD  ? A GLU 367 CD  
107 1 Y 1 A GLU 367 ? OE1 ? A GLU 367 OE1 
108 1 Y 1 A GLU 367 ? OE2 ? A GLU 367 OE2 
109 1 Y 1 A HIS 373 ? CG  ? A HIS 373 CG  
110 1 Y 1 A HIS 373 ? ND1 ? A HIS 373 ND1 
111 1 Y 1 A HIS 373 ? CD2 ? A HIS 373 CD2 
112 1 Y 1 A HIS 373 ? CE1 ? A HIS 373 CE1 
113 1 Y 1 A HIS 373 ? NE2 ? A HIS 373 NE2 
114 1 Y 1 A ASP 376 ? CG  ? A ASP 376 CG  
115 1 Y 1 A ASP 376 ? OD1 ? A ASP 376 OD1 
116 1 Y 1 A ASP 376 ? OD2 ? A ASP 376 OD2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? HKL-3000    ? ? ? 7.21     1 
? refinement        ? ? ? ? ? ? ? ? ? ? ? REFMAC      ? ? ? 5.8.0123 2 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? 3.27     3 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? HKL-3000    ? ? ? 7.21     4 
? phasing           ? ? ? ? ? ? ? ? ? ? ? PHASER      ? ? ? 2.7.0    5 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8WZY 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     179.745 
_cell.length_a_esd                 ? 
_cell.length_b                     42.002 
_cell.length_b_esd                 ? 
_cell.length_c                     43.557 
_cell.length_c_esd                 ? 
_cell.volume                       328840.083 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         8WZY 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                18 
_symmetry.space_group_name_Hall            'P 2 2ab (y,z,x)' 
_symmetry.space_group_name_H-M             'P 21 2 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8WZY 
_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             2.01 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          38.89 
_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    '0.2 M Calcium chloride dihydrate, 20% w/v Polyethylene glycol 3350' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            289.15 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-10-19 
_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 BL10U2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97918 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL10U2 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          26.15 
_reflns.entry_id                                       8WZY 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.87 
_reflns.d_resolution_low                               39.20 
_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                                     26948 
_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                           95.7 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                8.9 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          9.6 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   ? 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.126 
_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                                    1.87 
_reflns_shell.d_res_low                                     1.97 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             3105 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  ? 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  1.089 
_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                               29.51 
_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                                 8WZY 
_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                            1.87 
_refine.ls_d_res_low                             39.20 
_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                     26878 
_refine.ls_number_reflns_R_free                  1310 
_refine.ls_number_reflns_R_work                  25568 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    95.36 
_refine.ls_percent_reflns_R_free                 4.87 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2140 
_refine.ls_R_factor_R_free                       0.2601 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2116 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 25.43 
_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                            0.22 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.87 
_refine_hist.d_res_low                        39.20 
_refine_hist.number_atoms_solvent             139 
_refine_hist.number_atoms_total               2907 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        2750 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         18 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.005 ? ?   ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.763 ? ?   ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 6.175 ? 412 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.051 ? 461 ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.008 ? 500 ? 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' 1.87 1.95 . . 112 2162 74.00  . . . . 0.2740 . . . . . . . . . . . 0.3030 
'X-RAY DIFFRACTION' 1.95 2.04 . . 128 2678 92.00  . . . . 0.2522 . . . . . . . . . . . 0.3278 
'X-RAY DIFFRACTION' 2.04 2.14 . . 136 2922 99.00  . . . . 0.2273 . . . . . . . . . . . 0.3076 
'X-RAY DIFFRACTION' 2.14 2.28 . . 124 2932 99.00  . . . . 0.2295 . . . . . . . . . . . 0.2441 
'X-RAY DIFFRACTION' 2.28 2.45 . . 152 2946 100.00 . . . . 0.2334 . . . . . . . . . . . 0.2919 
'X-RAY DIFFRACTION' 2.45 2.70 . . 159 2940 100.00 . . . . 0.2305 . . . . . . . . . . . 0.3021 
'X-RAY DIFFRACTION' 2.70 3.09 . . 169 2965 100.00 . . . . 0.2370 . . . . . . . . . . . 0.2719 
'X-RAY DIFFRACTION' 3.09 3.86 . . 148 2951 100.00 . . . . 0.1986 . . . . . . . . . . . 0.2307 
'X-RAY DIFFRACTION' 3.92 4.50 . . 182 3072 99.00  . . . . 0.1792 . . . . . . . . . . . 0.2395 
# 
_struct.entry_id                     8WZY 
_struct.title                        'A novel amidohydrolase' 
_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        8WZY 
_struct_keywords.text            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 ? 
C N N 2 ? 
D N N 2 ? 
E N N 2 ? 
F N N 3 ? 
G N N 3 ? 
H N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A0A9Q5IKM4_9ENTR 
_struct_ref.pdbx_db_accession          A0A9Q5IKM4 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MFDLLLRRARLVDDTLTDIAIQDGKIAALGEISAPSRKTIDLQGNSYVSAGWIDSHVHCYPNSPIYHDEPDSVGIATGVT
TVIDAGSTGADDVDDFYQLTRKAVTEVYALLNISRVGLIAQNELANLANIDAEAVKQAVQRHPDFIVGLKARMSSSVVGE
NGITPLARAKTMQQENGDLPLMVHIGNNPPNLDEIAELLSRGDIITHCYNGKPNRILNPAGELRSSITRALHRGVRLDVG
HGTASFSFEVARRAIALGILPHTISSDIYCRNRIDGPVRSLALVMSKFLAIGMTLPQVIDCVTVSAAEGLRLSRKGRLEA
GFDADLTLFRLERQPTLLVDAEKESLQADNILVPLAAIRAGKGYLTEQGSAEHAFDF
;
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              8WZY 
_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                 377 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             A0A9Q5IKM4 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  377 
_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       377 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 210   ? 
1 MORE         -77   ? 
1 'SSA (A^2)'  13750 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H 
# 
_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 GLU A 69  ? GLY A 74  ? GLU A 69  GLY A 74  1 ? 6  
HELX_P HELX_P2  AA2 ILE A 75  ? THR A 77  ? ILE A 75  THR A 77  5 ? 3  
HELX_P HELX_P3  AA3 ASP A 92  ? ARG A 101 ? ASP A 92  ARG A 101 1 ? 10 
HELX_P HELX_P4  AA4 VAL A 116 ? ALA A 120 ? VAL A 116 ALA A 120 5 ? 5  
HELX_P HELX_P5  AA5 ASN A 126 ? ILE A 130 ? ASN A 126 ILE A 130 5 ? 5  
HELX_P HELX_P6  AA6 ASP A 131 ? HIS A 142 ? ASP A 131 HIS A 142 1 ? 12 
HELX_P HELX_P7  AA7 SER A 154 ? GLY A 159 ? SER A 154 GLY A 159 1 ? 6  
HELX_P HELX_P8  AA8 ILE A 163 ? ASN A 176 ? ILE A 163 ASN A 176 1 ? 14 
HELX_P HELX_P9  AA9 ASN A 191 ? LEU A 198 ? ASN A 191 LEU A 198 1 ? 8  
HELX_P HELX_P10 AB1 ARG A 224 ? GLY A 234 ? ARG A 224 GLY A 234 1 ? 11 
HELX_P HELX_P11 AB2 SER A 247 ? LEU A 257 ? SER A 247 LEU A 257 1 ? 11 
HELX_P HELX_P12 AB3 TYR A 269 ? ASP A 275 ? TYR A 269 ASP A 275 1 ? 7  
HELX_P HELX_P13 AB4 SER A 280 ? GLY A 292 ? SER A 280 GLY A 292 1 ? 13 
HELX_P HELX_P14 AB5 THR A 294 ? THR A 303 ? THR A 294 THR A 303 1 ? 10 
HELX_P HELX_P15 AB6 THR A 303 ? LEU A 310 ? THR A 303 LEU A 310 1 ? 8  
HELX_P HELX_P16 AB7 THR A 366 ? HIS A 373 ? THR A 366 HIS A 373 1 ? 8  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
covale1 covale both ? A LEU 149 C   ? ? ? 1_555 A KCX 150 N  ? ? A LEU 149 A KCX 150 1_555 ? ? ? ? ? ? ? 1.329 ? ? 
covale2 covale both ? A KCX 150 C   ? ? ? 1_555 A ALA 151 N  ? ? A KCX 150 A ALA 151 1_555 ? ? ? ? ? ? ? 1.326 ? ? 
metalc1 metalc ?    ? A HIS 56  NE2 ? ? ? 1_555 F ZN  .   ZN ? ? A HIS 56  A ZN  405 1_555 ? ? ? ? ? ? ? 2.256 ? ? 
metalc2 metalc ?    ? A HIS 58  NE2 ? ? ? 1_555 F ZN  .   ZN ? ? A HIS 58  A ZN  405 1_555 ? ? ? ? ? ? ? 2.234 ? ? 
metalc3 metalc ?    ? A KCX 150 OQ1 ? ? ? 1_555 F ZN  .   ZN ? ? A KCX 150 A ZN  405 1_555 ? ? ? ? ? ? ? 2.086 ? ? 
metalc4 metalc ?    ? A KCX 150 OQ2 ? ? ? 1_555 G ZN  .   ZN ? ? A KCX 150 A ZN  406 1_555 ? ? ? ? ? ? ? 1.992 ? ? 
metalc5 metalc ?    ? A HIS 184 ND1 ? ? ? 1_555 G ZN  .   ZN ? ? A HIS 184 A ZN  406 1_555 ? ? ? ? ? ? ? 2.279 ? ? 
metalc6 metalc ?    ? A HIS 207 NE2 ? ? ? 1_555 G ZN  .   ZN ? ? A HIS 207 A ZN  406 1_555 ? ? ? ? ? ? ? 2.231 ? ? 
metalc7 metalc ?    ? A ASP 267 OD1 ? ? ? 1_555 F ZN  .   ZN ? ? A ASP 267 A ZN  405 1_555 ? ? ? ? ? ? ? 2.324 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
covale ? ? 
metalc ? ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1 NE2 ? A HIS 56  ? A HIS 56  ? 1_555 ZN ? F ZN . ? A ZN 405 ? 1_555 NE2 ? A HIS 58  ? A HIS 58  ? 1_555 117.0 ? 
2 NE2 ? A HIS 56  ? A HIS 56  ? 1_555 ZN ? F ZN . ? A ZN 405 ? 1_555 OQ1 ? A KCX 150 ? A KCX 150 ? 1_555 97.3  ? 
3 NE2 ? A HIS 58  ? A HIS 58  ? 1_555 ZN ? F ZN . ? A ZN 405 ? 1_555 OQ1 ? A KCX 150 ? A KCX 150 ? 1_555 91.5  ? 
4 NE2 ? A HIS 56  ? A HIS 56  ? 1_555 ZN ? F ZN . ? A ZN 405 ? 1_555 OD1 ? A ASP 267 ? A ASP 267 ? 1_555 83.8  ? 
5 NE2 ? A HIS 58  ? A HIS 58  ? 1_555 ZN ? F ZN . ? A ZN 405 ? 1_555 OD1 ? A ASP 267 ? A ASP 267 ? 1_555 90.9  ? 
6 OQ1 ? A KCX 150 ? A KCX 150 ? 1_555 ZN ? F ZN . ? A ZN 405 ? 1_555 OD1 ? A ASP 267 ? A ASP 267 ? 1_555 176.6 ? 
7 OQ2 ? A KCX 150 ? A KCX 150 ? 1_555 ZN ? G ZN . ? A ZN 406 ? 1_555 ND1 ? A HIS 184 ? A HIS 184 ? 1_555 105.9 ? 
8 OQ2 ? A KCX 150 ? A KCX 150 ? 1_555 ZN ? G ZN . ? A ZN 406 ? 1_555 NE2 ? A HIS 207 ? A HIS 207 ? 1_555 102.4 ? 
9 ND1 ? A HIS 184 ? A HIS 184 ? 1_555 ZN ? G ZN . ? A ZN 406 ? 1_555 NE2 ? A HIS 207 ? A HIS 207 ? 1_555 92.6  ? 
# 
_pdbx_modification_feature.ordinal                            1 
_pdbx_modification_feature.label_comp_id                      KCX 
_pdbx_modification_feature.label_asym_id                      A 
_pdbx_modification_feature.label_seq_id                       150 
_pdbx_modification_feature.label_alt_id                       ? 
_pdbx_modification_feature.modified_residue_label_comp_id     . 
_pdbx_modification_feature.modified_residue_label_asym_id     . 
_pdbx_modification_feature.modified_residue_label_seq_id      . 
_pdbx_modification_feature.modified_residue_label_alt_id      . 
_pdbx_modification_feature.auth_comp_id                       KCX 
_pdbx_modification_feature.auth_asym_id                       A 
_pdbx_modification_feature.auth_seq_id                        150 
_pdbx_modification_feature.PDB_ins_code                       ? 
_pdbx_modification_feature.symmetry                           1_555 
_pdbx_modification_feature.modified_residue_auth_comp_id      . 
_pdbx_modification_feature.modified_residue_auth_asym_id      . 
_pdbx_modification_feature.modified_residue_auth_seq_id       . 
_pdbx_modification_feature.modified_residue_PDB_ins_code      . 
_pdbx_modification_feature.modified_residue_symmetry          . 
_pdbx_modification_feature.comp_id_linking_atom               . 
_pdbx_modification_feature.modified_residue_id_linking_atom   . 
_pdbx_modification_feature.modified_residue_id                LYS 
_pdbx_modification_feature.ref_pcm_id                         1 
_pdbx_modification_feature.ref_comp_id                        KCX 
_pdbx_modification_feature.type                               Carboxylation 
_pdbx_modification_feature.category                           'Named protein modification' 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 ASN 188 A . ? ASN 188 A PRO 189 A ? PRO 189 A 1 -2.41 
2 PRO 189 A . ? PRO 189 A PRO 190 A ? PRO 190 A 1 -1.75 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 4 ? 
AA3 ? 7 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? parallel      
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA3 1 2 ? parallel      
AA3 2 3 ? parallel      
AA3 3 4 ? parallel      
AA3 4 5 ? parallel      
AA3 5 6 ? parallel      
AA3 6 7 ? parallel      
# 
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 LYS A 25  ? GLY A 30  ? LYS A 25  GLY A 30  
AA1 2 LEU A 16  ? GLN A 22  ? LEU A 16  GLN A 22  
AA1 3 LEU A 4   ? ARG A 10  ? LEU A 4   ARG A 10  
AA1 4 THR A 39  ? ASP A 41  ? THR A 39  ASP A 41  
AA2 1 TYR A 47  ? ALA A 50  ? TYR A 47  ALA A 50  
AA2 2 LEU A 326 ? VAL A 339 ? LEU A 326 VAL A 339 
AA2 3 SER A 345 ? ARG A 359 ? SER A 345 ARG A 359 
AA2 4 LYS A 362 ? LEU A 365 ? LYS A 362 LEU A 365 
AA3 1 TRP A 52  ? VAL A 57  ? TRP A 52  VAL A 57  
AA3 2 VAL A 79  ? ALA A 85  ? VAL A 79  ALA A 85  
AA3 3 GLU A 106 ? ASN A 112 ? GLU A 106 ASN A 112 
AA3 4 ILE A 146 ? ARG A 152 ? ILE A 146 ARG A 152 
AA3 5 LEU A 181 ? HIS A 184 ? LEU A 181 HIS A 184 
AA3 6 ILE A 204 ? THR A 206 ? ILE A 204 THR A 206 
AA3 7 ARG A 236 ? LEU A 237 ? ARG A 236 LEU A 237 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O ALA A 27  ? O ALA A 27  N ALA A 20  ? N ALA A 20  
AA1 2 3 O ILE A 21  ? O ILE A 21  N LEU A 4   ? N LEU A 4   
AA1 3 4 N ARG A 7   ? N ARG A 7   O ILE A 40  ? O ILE A 40  
AA2 1 2 N TYR A 47  ? N TYR A 47  O PHE A 329 ? O PHE A 329 
AA2 2 3 N LEU A 328 ? N LEU A 328 O LEU A 355 ? O LEU A 355 
AA2 3 4 N ARG A 359 ? N ARG A 359 O LYS A 362 ? O LYS A 362 
AA3 1 2 N VAL A 57  ? N VAL A 57  O ALA A 85  ? O ALA A 85  
AA3 2 3 N ASP A 84  ? N ASP A 84  O LEU A 110 ? O LEU A 110 
AA3 3 4 N LEU A 111 ? N LEU A 111 O GLY A 148 ? O GLY A 148 
AA3 4 5 N LEU A 149 ? N LEU A 149 O MET A 182 ? O MET A 182 
AA3 5 6 N VAL A 183 ? N VAL A 183 O ILE A 204 ? O ILE A 204 
AA3 6 7 N ILE A 205 ? N ILE A 205 O ARG A 236 ? O ARG A 236 
# 
_pdbx_entry_details.entry_id                   8WZY 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     N 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 HIS A 56  ? ? -157.46 88.21  
2 1 ASN A 214 ? ? -89.29  37.27  
3 1 ARG A 279 ? ? 69.81   -54.91 
4 1 THR A 303 ? ? -128.83 -90.28 
5 1 PRO A 335 ? ? -38.38  126.04 
6 1 HIS A 373 ? ? 62.65   -96.65 
7 1 ALA A 374 ? ? 61.18   -61.17 
# 
_pdbx_struct_mod_residue.id               1 
_pdbx_struct_mod_residue.label_asym_id    A 
_pdbx_struct_mod_residue.label_comp_id    KCX 
_pdbx_struct_mod_residue.label_seq_id     150 
_pdbx_struct_mod_residue.auth_asym_id     A 
_pdbx_struct_mod_residue.auth_comp_id     KCX 
_pdbx_struct_mod_residue.auth_seq_id      150 
_pdbx_struct_mod_residue.PDB_ins_code     ? 
_pdbx_struct_mod_residue.parent_comp_id   LYS 
_pdbx_struct_mod_residue.details          'modified residue' 
# 
_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     639 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   H 
_pdbx_struct_special_symmetry.label_comp_id   HOH 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z           
2 x+1/2,-y,-z+1/2 
3 -x,y,-z         
4 -x+1/2,-y,z+1/2 
# 
_pdbx_refine_tls.id               1 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         24.0504 
_pdbx_refine_tls.origin_y         6.7597 
_pdbx_refine_tls.origin_z         5.1685 
_pdbx_refine_tls.T[1][1]          0.1875 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          -0.0244 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          -0.0192 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.1331 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          -0.0167 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.1586 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          1.7581 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          0.3673 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          0.1478 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          0.9288 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          0.0395 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          1.3483 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          0.0265 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          -0.0564 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          0.0187 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          -0.0337 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          -0.0181 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          0.0167 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          0.2154 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          -0.1530 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          -0.0061 
_pdbx_refine_tls.S[3][3]_esd      ? 
# 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.refine_tls_id       1 
_pdbx_refine_tls_group.beg_label_asym_id   A 
_pdbx_refine_tls_group.beg_label_seq_id    1 
_pdbx_refine_tls_group.beg_auth_asym_id    A 
_pdbx_refine_tls_group.beg_auth_seq_id     1 
_pdbx_refine_tls_group.beg_PDB_ins_code    ? 
_pdbx_refine_tls_group.end_label_asym_id   H 
_pdbx_refine_tls_group.end_label_seq_id    ? 
_pdbx_refine_tls_group.end_auth_asym_id    A 
_pdbx_refine_tls_group.end_auth_seq_id     377 
_pdbx_refine_tls_group.end_PDB_ins_code    ? 
_pdbx_refine_tls_group.selection           ? 
_pdbx_refine_tls_group.selection_details   all 
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      A 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       639 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   6.34 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
_pdbx_unobs_or_zero_occ_residues.id               1 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num    1 
_pdbx_unobs_or_zero_occ_residues.polymer_flag     Y 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag   1 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id     A 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id     GLY 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id      202 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code     ? 
_pdbx_unobs_or_zero_occ_residues.label_asym_id    A 
_pdbx_unobs_or_zero_occ_residues.label_comp_id    GLY 
_pdbx_unobs_or_zero_occ_residues.label_seq_id     202 
# 
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  
EDO C1   C  N N 88  
EDO O1   O  N N 89  
EDO C2   C  N N 90  
EDO O2   O  N N 91  
EDO H11  H  N N 92  
EDO H12  H  N N 93  
EDO HO1  H  N N 94  
EDO H21  H  N N 95  
EDO H22  H  N N 96  
EDO HO2  H  N N 97  
GLN N    N  N N 98  
GLN CA   C  N S 99  
GLN C    C  N N 100 
GLN O    O  N N 101 
GLN CB   C  N N 102 
GLN CG   C  N N 103 
GLN CD   C  N N 104 
GLN OE1  O  N N 105 
GLN NE2  N  N N 106 
GLN OXT  O  N N 107 
GLN H    H  N N 108 
GLN H2   H  N N 109 
GLN HA   H  N N 110 
GLN HB2  H  N N 111 
GLN HB3  H  N N 112 
GLN HG2  H  N N 113 
GLN HG3  H  N N 114 
GLN HE21 H  N N 115 
GLN HE22 H  N N 116 
GLN HXT  H  N N 117 
GLU N    N  N N 118 
GLU CA   C  N S 119 
GLU C    C  N N 120 
GLU O    O  N N 121 
GLU CB   C  N N 122 
GLU CG   C  N N 123 
GLU CD   C  N N 124 
GLU OE1  O  N N 125 
GLU OE2  O  N N 126 
GLU OXT  O  N N 127 
GLU H    H  N N 128 
GLU H2   H  N N 129 
GLU HA   H  N N 130 
GLU HB2  H  N N 131 
GLU HB3  H  N N 132 
GLU HG2  H  N N 133 
GLU HG3  H  N N 134 
GLU HE2  H  N N 135 
GLU HXT  H  N N 136 
GLY N    N  N N 137 
GLY CA   C  N N 138 
GLY C    C  N N 139 
GLY O    O  N N 140 
GLY OXT  O  N N 141 
GLY H    H  N N 142 
GLY H2   H  N N 143 
GLY HA2  H  N N 144 
GLY HA3  H  N N 145 
GLY HXT  H  N N 146 
HIS N    N  N N 147 
HIS CA   C  N S 148 
HIS C    C  N N 149 
HIS O    O  N N 150 
HIS CB   C  N N 151 
HIS CG   C  Y N 152 
HIS ND1  N  Y N 153 
HIS CD2  C  Y N 154 
HIS CE1  C  Y N 155 
HIS NE2  N  Y N 156 
HIS OXT  O  N N 157 
HIS H    H  N N 158 
HIS H2   H  N N 159 
HIS HA   H  N N 160 
HIS HB2  H  N N 161 
HIS HB3  H  N N 162 
HIS HD1  H  N N 163 
HIS HD2  H  N N 164 
HIS HE1  H  N N 165 
HIS HE2  H  N N 166 
HIS HXT  H  N N 167 
HOH O    O  N N 168 
HOH H1   H  N N 169 
HOH H2   H  N N 170 
ILE N    N  N N 171 
ILE CA   C  N S 172 
ILE C    C  N N 173 
ILE O    O  N N 174 
ILE CB   C  N S 175 
ILE CG1  C  N N 176 
ILE CG2  C  N N 177 
ILE CD1  C  N N 178 
ILE OXT  O  N N 179 
ILE H    H  N N 180 
ILE H2   H  N N 181 
ILE HA   H  N N 182 
ILE HB   H  N N 183 
ILE HG12 H  N N 184 
ILE HG13 H  N N 185 
ILE HG21 H  N N 186 
ILE HG22 H  N N 187 
ILE HG23 H  N N 188 
ILE HD11 H  N N 189 
ILE HD12 H  N N 190 
ILE HD13 H  N N 191 
ILE HXT  H  N N 192 
KCX N    N  N N 193 
KCX CA   C  N S 194 
KCX CB   C  N N 195 
KCX CG   C  N N 196 
KCX CD   C  N N 197 
KCX CE   C  N N 198 
KCX NZ   N  N N 199 
KCX C    C  N N 200 
KCX O    O  N N 201 
KCX CX   C  N N 202 
KCX OXT  O  N N 203 
KCX OQ1  O  N N 204 
KCX OQ2  O  N N 205 
KCX H    H  N N 206 
KCX H2   H  N N 207 
KCX HA   H  N N 208 
KCX HB2  H  N N 209 
KCX HB3  H  N N 210 
KCX HG2  H  N N 211 
KCX HG3  H  N N 212 
KCX HD2  H  N N 213 
KCX HD3  H  N N 214 
KCX HE2  H  N N 215 
KCX HE3  H  N N 216 
KCX HZ   H  N N 217 
KCX HXT  H  N N 218 
KCX HQ2  H  N N 219 
LEU N    N  N N 220 
LEU CA   C  N S 221 
LEU C    C  N N 222 
LEU O    O  N N 223 
LEU CB   C  N N 224 
LEU CG   C  N N 225 
LEU CD1  C  N N 226 
LEU CD2  C  N N 227 
LEU OXT  O  N N 228 
LEU H    H  N N 229 
LEU H2   H  N N 230 
LEU HA   H  N N 231 
LEU HB2  H  N N 232 
LEU HB3  H  N N 233 
LEU HG   H  N N 234 
LEU HD11 H  N N 235 
LEU HD12 H  N N 236 
LEU HD13 H  N N 237 
LEU HD21 H  N N 238 
LEU HD22 H  N N 239 
LEU HD23 H  N N 240 
LEU HXT  H  N N 241 
LYS N    N  N N 242 
LYS CA   C  N S 243 
LYS C    C  N N 244 
LYS O    O  N N 245 
LYS CB   C  N N 246 
LYS CG   C  N N 247 
LYS CD   C  N N 248 
LYS CE   C  N N 249 
LYS NZ   N  N N 250 
LYS OXT  O  N N 251 
LYS H    H  N N 252 
LYS H2   H  N N 253 
LYS HA   H  N N 254 
LYS HB2  H  N N 255 
LYS HB3  H  N N 256 
LYS HG2  H  N N 257 
LYS HG3  H  N N 258 
LYS HD2  H  N N 259 
LYS HD3  H  N N 260 
LYS HE2  H  N N 261 
LYS HE3  H  N N 262 
LYS HZ1  H  N N 263 
LYS HZ2  H  N N 264 
LYS HZ3  H  N N 265 
LYS HXT  H  N N 266 
MET N    N  N N 267 
MET CA   C  N S 268 
MET C    C  N N 269 
MET O    O  N N 270 
MET CB   C  N N 271 
MET CG   C  N N 272 
MET SD   S  N N 273 
MET CE   C  N N 274 
MET OXT  O  N N 275 
MET H    H  N N 276 
MET H2   H  N N 277 
MET HA   H  N N 278 
MET HB2  H  N N 279 
MET HB3  H  N N 280 
MET HG2  H  N N 281 
MET HG3  H  N N 282 
MET HE1  H  N N 283 
MET HE2  H  N N 284 
MET HE3  H  N N 285 
MET HXT  H  N N 286 
PHE N    N  N N 287 
PHE CA   C  N S 288 
PHE C    C  N N 289 
PHE O    O  N N 290 
PHE CB   C  N N 291 
PHE CG   C  Y N 292 
PHE CD1  C  Y N 293 
PHE CD2  C  Y N 294 
PHE CE1  C  Y N 295 
PHE CE2  C  Y N 296 
PHE CZ   C  Y N 297 
PHE OXT  O  N N 298 
PHE H    H  N N 299 
PHE H2   H  N N 300 
PHE HA   H  N N 301 
PHE HB2  H  N N 302 
PHE HB3  H  N N 303 
PHE HD1  H  N N 304 
PHE HD2  H  N N 305 
PHE HE1  H  N N 306 
PHE HE2  H  N N 307 
PHE HZ   H  N N 308 
PHE HXT  H  N N 309 
PRO N    N  N N 310 
PRO CA   C  N S 311 
PRO C    C  N N 312 
PRO O    O  N N 313 
PRO CB   C  N N 314 
PRO CG   C  N N 315 
PRO CD   C  N N 316 
PRO OXT  O  N N 317 
PRO H    H  N N 318 
PRO HA   H  N N 319 
PRO HB2  H  N N 320 
PRO HB3  H  N N 321 
PRO HG2  H  N N 322 
PRO HG3  H  N N 323 
PRO HD2  H  N N 324 
PRO HD3  H  N N 325 
PRO HXT  H  N N 326 
SER N    N  N N 327 
SER CA   C  N S 328 
SER C    C  N N 329 
SER O    O  N N 330 
SER CB   C  N N 331 
SER OG   O  N N 332 
SER OXT  O  N N 333 
SER H    H  N N 334 
SER H2   H  N N 335 
SER HA   H  N N 336 
SER HB2  H  N N 337 
SER HB3  H  N N 338 
SER HG   H  N N 339 
SER HXT  H  N N 340 
THR N    N  N N 341 
THR CA   C  N S 342 
THR C    C  N N 343 
THR O    O  N N 344 
THR CB   C  N R 345 
THR OG1  O  N N 346 
THR CG2  C  N N 347 
THR OXT  O  N N 348 
THR H    H  N N 349 
THR H2   H  N N 350 
THR HA   H  N N 351 
THR HB   H  N N 352 
THR HG1  H  N N 353 
THR HG21 H  N N 354 
THR HG22 H  N N 355 
THR HG23 H  N N 356 
THR HXT  H  N N 357 
TRP N    N  N N 358 
TRP CA   C  N S 359 
TRP C    C  N N 360 
TRP O    O  N N 361 
TRP CB   C  N N 362 
TRP CG   C  Y N 363 
TRP CD1  C  Y N 364 
TRP CD2  C  Y N 365 
TRP NE1  N  Y N 366 
TRP CE2  C  Y N 367 
TRP CE3  C  Y N 368 
TRP CZ2  C  Y N 369 
TRP CZ3  C  Y N 370 
TRP CH2  C  Y N 371 
TRP OXT  O  N N 372 
TRP H    H  N N 373 
TRP H2   H  N N 374 
TRP HA   H  N N 375 
TRP HB2  H  N N 376 
TRP HB3  H  N N 377 
TRP HD1  H  N N 378 
TRP HE1  H  N N 379 
TRP HE3  H  N N 380 
TRP HZ2  H  N N 381 
TRP HZ3  H  N N 382 
TRP HH2  H  N N 383 
TRP HXT  H  N N 384 
TYR N    N  N N 385 
TYR CA   C  N S 386 
TYR C    C  N N 387 
TYR O    O  N N 388 
TYR CB   C  N N 389 
TYR CG   C  Y N 390 
TYR CD1  C  Y N 391 
TYR CD2  C  Y N 392 
TYR CE1  C  Y N 393 
TYR CE2  C  Y N 394 
TYR CZ   C  Y N 395 
TYR OH   O  N N 396 
TYR OXT  O  N N 397 
TYR H    H  N N 398 
TYR H2   H  N N 399 
TYR HA   H  N N 400 
TYR HB2  H  N N 401 
TYR HB3  H  N N 402 
TYR HD1  H  N N 403 
TYR HD2  H  N N 404 
TYR HE1  H  N N 405 
TYR HE2  H  N N 406 
TYR HH   H  N N 407 
TYR HXT  H  N N 408 
VAL N    N  N N 409 
VAL CA   C  N S 410 
VAL C    C  N N 411 
VAL O    O  N N 412 
VAL CB   C  N N 413 
VAL CG1  C  N N 414 
VAL CG2  C  N N 415 
VAL OXT  O  N N 416 
VAL H    H  N N 417 
VAL H2   H  N N 418 
VAL HA   H  N N 419 
VAL HB   H  N N 420 
VAL HG11 H  N N 421 
VAL HG12 H  N N 422 
VAL HG13 H  N N 423 
VAL HG21 H  N N 424 
VAL HG22 H  N N 425 
VAL HG23 H  N N 426 
VAL HXT  H  N N 427 
ZN  ZN   ZN N N 428 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
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  
EDO C1  O1   sing N N 83  
EDO C1  C2   sing N N 84  
EDO C1  H11  sing N N 85  
EDO C1  H12  sing N N 86  
EDO O1  HO1  sing N N 87  
EDO C2  O2   sing N N 88  
EDO C2  H21  sing N N 89  
EDO C2  H22  sing N N 90  
EDO O2  HO2  sing N N 91  
GLN N   CA   sing N N 92  
GLN N   H    sing N N 93  
GLN N   H2   sing N N 94  
GLN CA  C    sing N N 95  
GLN CA  CB   sing N N 96  
GLN CA  HA   sing N N 97  
GLN C   O    doub N N 98  
GLN C   OXT  sing N N 99  
GLN CB  CG   sing N N 100 
GLN CB  HB2  sing N N 101 
GLN CB  HB3  sing N N 102 
GLN CG  CD   sing N N 103 
GLN CG  HG2  sing N N 104 
GLN CG  HG3  sing N N 105 
GLN CD  OE1  doub N N 106 
GLN CD  NE2  sing N N 107 
GLN NE2 HE21 sing N N 108 
GLN NE2 HE22 sing N N 109 
GLN OXT HXT  sing N N 110 
GLU N   CA   sing N N 111 
GLU N   H    sing N N 112 
GLU N   H2   sing N N 113 
GLU CA  C    sing N N 114 
GLU CA  CB   sing N N 115 
GLU CA  HA   sing N N 116 
GLU C   O    doub N N 117 
GLU C   OXT  sing N N 118 
GLU CB  CG   sing N N 119 
GLU CB  HB2  sing N N 120 
GLU CB  HB3  sing N N 121 
GLU CG  CD   sing N N 122 
GLU CG  HG2  sing N N 123 
GLU CG  HG3  sing N N 124 
GLU CD  OE1  doub N N 125 
GLU CD  OE2  sing N N 126 
GLU OE2 HE2  sing N N 127 
GLU OXT HXT  sing N N 128 
GLY N   CA   sing N N 129 
GLY N   H    sing N N 130 
GLY N   H2   sing N N 131 
GLY CA  C    sing N N 132 
GLY CA  HA2  sing N N 133 
GLY CA  HA3  sing N N 134 
GLY C   O    doub N N 135 
GLY C   OXT  sing N N 136 
GLY OXT HXT  sing N N 137 
HIS N   CA   sing N N 138 
HIS N   H    sing N N 139 
HIS N   H2   sing N N 140 
HIS CA  C    sing N N 141 
HIS CA  CB   sing N N 142 
HIS CA  HA   sing N N 143 
HIS C   O    doub N N 144 
HIS C   OXT  sing N N 145 
HIS CB  CG   sing N N 146 
HIS CB  HB2  sing N N 147 
HIS CB  HB3  sing N N 148 
HIS CG  ND1  sing Y N 149 
HIS CG  CD2  doub Y N 150 
HIS ND1 CE1  doub Y N 151 
HIS ND1 HD1  sing N N 152 
HIS CD2 NE2  sing Y N 153 
HIS CD2 HD2  sing N N 154 
HIS CE1 NE2  sing Y N 155 
HIS CE1 HE1  sing N N 156 
HIS NE2 HE2  sing N N 157 
HIS OXT HXT  sing N N 158 
HOH O   H1   sing N N 159 
HOH O   H2   sing N N 160 
ILE N   CA   sing N N 161 
ILE N   H    sing N N 162 
ILE N   H2   sing N N 163 
ILE CA  C    sing N N 164 
ILE CA  CB   sing N N 165 
ILE CA  HA   sing N N 166 
ILE C   O    doub N N 167 
ILE C   OXT  sing N N 168 
ILE CB  CG1  sing N N 169 
ILE CB  CG2  sing N N 170 
ILE CB  HB   sing N N 171 
ILE CG1 CD1  sing N N 172 
ILE CG1 HG12 sing N N 173 
ILE CG1 HG13 sing N N 174 
ILE CG2 HG21 sing N N 175 
ILE CG2 HG22 sing N N 176 
ILE CG2 HG23 sing N N 177 
ILE CD1 HD11 sing N N 178 
ILE CD1 HD12 sing N N 179 
ILE CD1 HD13 sing N N 180 
ILE OXT HXT  sing N N 181 
KCX N   CA   sing N N 182 
KCX N   H    sing N N 183 
KCX N   H2   sing N N 184 
KCX CA  CB   sing N N 185 
KCX CA  C    sing N N 186 
KCX CA  HA   sing N N 187 
KCX CB  CG   sing N N 188 
KCX CB  HB2  sing N N 189 
KCX CB  HB3  sing N N 190 
KCX CG  CD   sing N N 191 
KCX CG  HG2  sing N N 192 
KCX CG  HG3  sing N N 193 
KCX CD  CE   sing N N 194 
KCX CD  HD2  sing N N 195 
KCX CD  HD3  sing N N 196 
KCX CE  NZ   sing N N 197 
KCX CE  HE2  sing N N 198 
KCX CE  HE3  sing N N 199 
KCX NZ  CX   sing N N 200 
KCX NZ  HZ   sing N N 201 
KCX C   O    doub N N 202 
KCX C   OXT  sing N N 203 
KCX CX  OQ1  doub N N 204 
KCX CX  OQ2  sing N N 205 
KCX OXT HXT  sing N N 206 
KCX OQ2 HQ2  sing N N 207 
LEU N   CA   sing N N 208 
LEU N   H    sing N N 209 
LEU N   H2   sing N N 210 
LEU CA  C    sing N N 211 
LEU CA  CB   sing N N 212 
LEU CA  HA   sing N N 213 
LEU C   O    doub N N 214 
LEU C   OXT  sing N N 215 
LEU CB  CG   sing N N 216 
LEU CB  HB2  sing N N 217 
LEU CB  HB3  sing N N 218 
LEU CG  CD1  sing N N 219 
LEU CG  CD2  sing N N 220 
LEU CG  HG   sing N N 221 
LEU CD1 HD11 sing N N 222 
LEU CD1 HD12 sing N N 223 
LEU CD1 HD13 sing N N 224 
LEU CD2 HD21 sing N N 225 
LEU CD2 HD22 sing N N 226 
LEU CD2 HD23 sing N N 227 
LEU OXT HXT  sing N N 228 
LYS N   CA   sing N N 229 
LYS N   H    sing N N 230 
LYS N   H2   sing N N 231 
LYS CA  C    sing N N 232 
LYS CA  CB   sing N N 233 
LYS CA  HA   sing N N 234 
LYS C   O    doub N N 235 
LYS C   OXT  sing N N 236 
LYS CB  CG   sing N N 237 
LYS CB  HB2  sing N N 238 
LYS CB  HB3  sing N N 239 
LYS CG  CD   sing N N 240 
LYS CG  HG2  sing N N 241 
LYS CG  HG3  sing N N 242 
LYS CD  CE   sing N N 243 
LYS CD  HD2  sing N N 244 
LYS CD  HD3  sing N N 245 
LYS CE  NZ   sing N N 246 
LYS CE  HE2  sing N N 247 
LYS CE  HE3  sing N N 248 
LYS NZ  HZ1  sing N N 249 
LYS NZ  HZ2  sing N N 250 
LYS NZ  HZ3  sing N N 251 
LYS OXT HXT  sing N N 252 
MET N   CA   sing N N 253 
MET N   H    sing N N 254 
MET N   H2   sing N N 255 
MET CA  C    sing N N 256 
MET CA  CB   sing N N 257 
MET CA  HA   sing N N 258 
MET C   O    doub N N 259 
MET C   OXT  sing N N 260 
MET CB  CG   sing N N 261 
MET CB  HB2  sing N N 262 
MET CB  HB3  sing N N 263 
MET CG  SD   sing N N 264 
MET CG  HG2  sing N N 265 
MET CG  HG3  sing N N 266 
MET SD  CE   sing N N 267 
MET CE  HE1  sing N N 268 
MET CE  HE2  sing N N 269 
MET CE  HE3  sing N N 270 
MET OXT HXT  sing N N 271 
PHE N   CA   sing N N 272 
PHE N   H    sing N N 273 
PHE N   H2   sing N N 274 
PHE CA  C    sing N N 275 
PHE CA  CB   sing N N 276 
PHE CA  HA   sing N N 277 
PHE C   O    doub N N 278 
PHE C   OXT  sing N N 279 
PHE CB  CG   sing N N 280 
PHE CB  HB2  sing N N 281 
PHE CB  HB3  sing N N 282 
PHE CG  CD1  doub Y N 283 
PHE CG  CD2  sing Y N 284 
PHE CD1 CE1  sing Y N 285 
PHE CD1 HD1  sing N N 286 
PHE CD2 CE2  doub Y N 287 
PHE CD2 HD2  sing N N 288 
PHE CE1 CZ   doub Y N 289 
PHE CE1 HE1  sing N N 290 
PHE CE2 CZ   sing Y N 291 
PHE CE2 HE2  sing N N 292 
PHE CZ  HZ   sing N N 293 
PHE OXT HXT  sing N N 294 
PRO N   CA   sing N N 295 
PRO N   CD   sing N N 296 
PRO N   H    sing N N 297 
PRO CA  C    sing N N 298 
PRO CA  CB   sing N N 299 
PRO CA  HA   sing N N 300 
PRO C   O    doub N N 301 
PRO C   OXT  sing N N 302 
PRO CB  CG   sing N N 303 
PRO CB  HB2  sing N N 304 
PRO CB  HB3  sing N N 305 
PRO CG  CD   sing N N 306 
PRO CG  HG2  sing N N 307 
PRO CG  HG3  sing N N 308 
PRO CD  HD2  sing N N 309 
PRO CD  HD3  sing N N 310 
PRO OXT HXT  sing N N 311 
SER N   CA   sing N N 312 
SER N   H    sing N N 313 
SER N   H2   sing N N 314 
SER CA  C    sing N N 315 
SER CA  CB   sing N N 316 
SER CA  HA   sing N N 317 
SER C   O    doub N N 318 
SER C   OXT  sing N N 319 
SER CB  OG   sing N N 320 
SER CB  HB2  sing N N 321 
SER CB  HB3  sing N N 322 
SER OG  HG   sing N N 323 
SER OXT HXT  sing N N 324 
THR N   CA   sing N N 325 
THR N   H    sing N N 326 
THR N   H2   sing N N 327 
THR CA  C    sing N N 328 
THR CA  CB   sing N N 329 
THR CA  HA   sing N N 330 
THR C   O    doub N N 331 
THR C   OXT  sing N N 332 
THR CB  OG1  sing N N 333 
THR CB  CG2  sing N N 334 
THR CB  HB   sing N N 335 
THR OG1 HG1  sing N N 336 
THR CG2 HG21 sing N N 337 
THR CG2 HG22 sing N N 338 
THR CG2 HG23 sing N N 339 
THR OXT HXT  sing N N 340 
TRP N   CA   sing N N 341 
TRP N   H    sing N N 342 
TRP N   H2   sing N N 343 
TRP CA  C    sing N N 344 
TRP CA  CB   sing N N 345 
TRP CA  HA   sing N N 346 
TRP C   O    doub N N 347 
TRP C   OXT  sing N N 348 
TRP CB  CG   sing N N 349 
TRP CB  HB2  sing N N 350 
TRP CB  HB3  sing N N 351 
TRP CG  CD1  doub Y N 352 
TRP CG  CD2  sing Y N 353 
TRP CD1 NE1  sing Y N 354 
TRP CD1 HD1  sing N N 355 
TRP CD2 CE2  doub Y N 356 
TRP CD2 CE3  sing Y N 357 
TRP NE1 CE2  sing Y N 358 
TRP NE1 HE1  sing N N 359 
TRP CE2 CZ2  sing Y N 360 
TRP CE3 CZ3  doub Y N 361 
TRP CE3 HE3  sing N N 362 
TRP CZ2 CH2  doub Y N 363 
TRP CZ2 HZ2  sing N N 364 
TRP CZ3 CH2  sing Y N 365 
TRP CZ3 HZ3  sing N N 366 
TRP CH2 HH2  sing N N 367 
TRP OXT HXT  sing N N 368 
TYR N   CA   sing N N 369 
TYR N   H    sing N N 370 
TYR N   H2   sing N N 371 
TYR CA  C    sing N N 372 
TYR CA  CB   sing N N 373 
TYR CA  HA   sing N N 374 
TYR C   O    doub N N 375 
TYR C   OXT  sing N N 376 
TYR CB  CG   sing N N 377 
TYR CB  HB2  sing N N 378 
TYR CB  HB3  sing N N 379 
TYR CG  CD1  doub Y N 380 
TYR CG  CD2  sing Y N 381 
TYR CD1 CE1  sing Y N 382 
TYR CD1 HD1  sing N N 383 
TYR CD2 CE2  doub Y N 384 
TYR CD2 HD2  sing N N 385 
TYR CE1 CZ   doub Y N 386 
TYR CE1 HE1  sing N N 387 
TYR CE2 CZ   sing Y N 388 
TYR CE2 HE2  sing N N 389 
TYR CZ  OH   sing N N 390 
TYR OH  HH   sing N N 391 
TYR OXT HXT  sing N N 392 
VAL N   CA   sing N N 393 
VAL N   H    sing N N 394 
VAL N   H2   sing N N 395 
VAL CA  C    sing N N 396 
VAL CA  CB   sing N N 397 
VAL CA  HA   sing N N 398 
VAL C   O    doub N N 399 
VAL C   OXT  sing N N 400 
VAL CB  CG1  sing N N 401 
VAL CB  CG2  sing N N 402 
VAL CB  HB   sing N N 403 
VAL CG1 HG11 sing N N 404 
VAL CG1 HG12 sing N N 405 
VAL CG1 HG13 sing N N 406 
VAL CG2 HG21 sing N N 407 
VAL CG2 HG22 sing N N 408 
VAL CG2 HG23 sing N N 409 
VAL OXT HXT  sing N N 410 
# 
_pdbx_audit_support.funding_organization   'National Natural Science Foundation of China (NSFC)' 
_pdbx_audit_support.country                China 
_pdbx_audit_support.grant_number           32101371 
_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          ? 
# 
_space_group.name_H-M_alt     'P 21 2 21' 
_space_group.name_Hall        'P 2 2ab (y,z,x)' 
_space_group.IT_number        18 
_space_group.crystal_system   orthorhombic 
_space_group.id               1 
# 
_atom_sites.entry_id                    8WZY 
_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]   0.005563 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.023808 
_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]   0.022958 
_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 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C  ? ? 3.54356  2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N  ? ? 4.01032  2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O  ? ? 4.49882  3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S  ? ? 9.55732  6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
ZN ? ? 24.64596 5.25405 ? ? 2.14387  29.76375 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
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   . MET A 1 1   ? 57.688 12.085  9.381   1.00 41.59 ? 1   MET A N   1 
ATOM   2    C  CA  . MET A 1 1   ? 57.519 12.053  7.932   1.00 36.72 ? 1   MET A CA  1 
ATOM   3    C  C   . MET A 1 1   ? 56.140 11.460  7.590   1.00 34.81 ? 1   MET A C   1 
ATOM   4    O  O   . MET A 1 1   ? 55.780 10.391  8.087   1.00 33.07 ? 1   MET A O   1 
ATOM   5    C  CB  . MET A 1 1   ? 58.660 11.252  7.310   1.00 40.83 ? 1   MET A CB  1 
ATOM   6    C  CG  . MET A 1 1   ? 58.448 10.765  5.907   1.00 36.49 ? 1   MET A CG  1 
ATOM   7    S  SD  . MET A 1 1   ? 60.061 10.795  5.098   1.00 53.54 ? 1   MET A SD  1 
ATOM   8    C  CE  . MET A 1 1   ? 59.563 10.826  3.383   1.00 38.95 ? 1   MET A CE  1 
ATOM   9    N  N   . PHE A 1 2   ? 55.357 12.153  6.761   1.00 29.33 ? 2   PHE A N   1 
ATOM   10   C  CA  . PHE A 1 2   ? 53.969 11.749  6.564   1.00 31.82 ? 2   PHE A CA  1 
ATOM   11   C  C   . PHE A 1 2   ? 53.874 10.467  5.744   1.00 28.71 ? 2   PHE A C   1 
ATOM   12   O  O   . PHE A 1 2   ? 54.754 10.143  4.940   1.00 25.20 ? 2   PHE A O   1 
ATOM   13   C  CB  . PHE A 1 2   ? 53.156 12.864  5.889   1.00 28.59 ? 2   PHE A CB  1 
ATOM   14   C  CG  . PHE A 1 2   ? 53.031 14.118  6.719   1.00 27.69 ? 2   PHE A CG  1 
ATOM   15   C  CD1 . PHE A 1 2   ? 52.568 14.058  8.028   1.00 26.52 ? 2   PHE A CD1 1 
ATOM   16   C  CD2 . PHE A 1 2   ? 53.351 15.357  6.185   1.00 28.47 ? 2   PHE A CD2 1 
ATOM   17   C  CE1 . PHE A 1 2   ? 52.450 15.202  8.797   1.00 28.73 ? 2   PHE A CE1 1 
ATOM   18   C  CE2 . PHE A 1 2   ? 53.229 16.509  6.944   1.00 27.66 ? 2   PHE A CE2 1 
ATOM   19   C  CZ  . PHE A 1 2   ? 52.777 16.433  8.256   1.00 25.49 ? 2   PHE A CZ  1 
ATOM   20   N  N   . ASP A 1 3   ? 52.796 9.716   5.988   1.00 29.11 ? 3   ASP A N   1 
ATOM   21   C  CA  . ASP A 1 3   ? 52.495 8.552   5.162   1.00 27.53 ? 3   ASP A CA  1 
ATOM   22   C  C   . ASP A 1 3   ? 51.883 8.969   3.838   1.00 27.90 ? 3   ASP A C   1 
ATOM   23   O  O   . ASP A 1 3   ? 52.180 8.369   2.798   1.00 26.89 ? 3   ASP A O   1 
ATOM   24   C  CB  . ASP A 1 3   ? 51.540 7.594   5.888   1.00 25.03 ? 3   ASP A CB  1 
ATOM   25   C  CG  . ASP A 1 3   ? 52.201 6.872   7.050   1.00 31.14 ? 3   ASP A CG  1 
ATOM   26   O  OD1 . ASP A 1 3   ? 53.411 6.582   6.962   1.00 32.57 ? 3   ASP A OD1 1 
ATOM   27   O  OD2 . ASP A 1 3   ? 51.508 6.590   8.051   1.00 32.90 ? 3   ASP A OD2 1 
ATOM   28   N  N   . LEU A 1 4   ? 51.016 9.979   3.856   1.00 23.58 ? 4   LEU A N   1 
ATOM   29   C  CA  . LEU A 1 4   ? 50.381 10.409  2.618   1.00 25.39 ? 4   LEU A CA  1 
ATOM   30   C  C   . LEU A 1 4   ? 50.108 11.901  2.704   1.00 23.68 ? 4   LEU A C   1 
ATOM   31   O  O   . LEU A 1 4   ? 49.711 12.399  3.759   1.00 22.13 ? 4   LEU A O   1 
ATOM   32   C  CB  . LEU A 1 4   ? 49.082 9.634   2.363   1.00 24.11 ? 4   LEU A CB  1 
ATOM   33   C  CG  . LEU A 1 4   ? 48.250 10.048  1.146   1.00 24.60 ? 4   LEU A CG  1 
ATOM   34   C  CD1 . LEU A 1 4   ? 49.093 9.905   -0.107  1.00 25.22 ? 4   LEU A CD1 1 
ATOM   35   C  CD2 . LEU A 1 4   ? 46.975 9.211   1.030   1.00 23.86 ? 4   LEU A CD2 1 
ATOM   36   N  N   . LEU A 1 5   ? 50.330 12.614  1.599   1.00 24.63 ? 5   LEU A N   1 
ATOM   37   C  CA  . LEU A 1 5   ? 50.123 14.060  1.566   1.00 24.03 ? 5   LEU A CA  1 
ATOM   38   C  C   . LEU A 1 5   ? 49.370 14.426  0.297   1.00 23.71 ? 5   LEU A C   1 
ATOM   39   O  O   . LEU A 1 5   ? 49.838 14.142  -0.809  1.00 24.88 ? 5   LEU A O   1 
ATOM   40   C  CB  . LEU A 1 5   ? 51.455 14.820  1.644   1.00 23.64 ? 5   LEU A CB  1 
ATOM   41   C  CG  . LEU A 1 5   ? 51.413 16.352  1.551   1.00 25.76 ? 5   LEU A CG  1 
ATOM   42   C  CD1 . LEU A 1 5   ? 50.544 16.943  2.644   1.00 23.32 ? 5   LEU A CD1 1 
ATOM   43   C  CD2 . LEU A 1 5   ? 52.820 16.919  1.659   1.00 25.68 ? 5   LEU A CD2 1 
ATOM   44   N  N   . LEU A 1 6   ? 48.210 15.053  0.461   1.00 21.83 ? 6   LEU A N   1 
ATOM   45   C  CA  . LEU A 1 6   ? 47.408 15.538  -0.650  1.00 22.98 ? 6   LEU A CA  1 
ATOM   46   C  C   . LEU A 1 6   ? 47.609 17.042  -0.748  1.00 24.29 ? 6   LEU A C   1 
ATOM   47   O  O   . LEU A 1 6   ? 47.275 17.776  0.184   1.00 21.06 ? 6   LEU A O   1 
ATOM   48   C  CB  . LEU A 1 6   ? 45.932 15.213  -0.446  1.00 20.54 ? 6   LEU A CB  1 
ATOM   49   C  CG  . LEU A 1 6   ? 45.589 13.756  -0.146  1.00 24.99 ? 6   LEU A CG  1 
ATOM   50   C  CD1 . LEU A 1 6   ? 44.085 13.587  -0.026  1.00 23.95 ? 6   LEU A CD1 1 
ATOM   51   C  CD2 . LEU A 1 6   ? 46.149 12.853  -1.227  1.00 22.76 ? 6   LEU A CD2 1 
ATOM   52   N  N   . ARG A 1 7   ? 48.150 17.492  -1.867  1.00 23.73 ? 7   ARG A N   1 
ATOM   53   C  CA  . ARG A 1 7   ? 48.460 18.893  -2.070  1.00 23.12 ? 7   ARG A CA  1 
ATOM   54   C  C   . ARG A 1 7   ? 47.457 19.507  -3.032  1.00 24.56 ? 7   ARG A C   1 
ATOM   55   O  O   . ARG A 1 7   ? 47.057 18.875  -4.016  1.00 24.56 ? 7   ARG A O   1 
ATOM   56   C  CB  . ARG A 1 7   ? 49.876 19.053  -2.618  1.00 25.08 ? 7   ARG A CB  1 
ATOM   57   C  CG  . ARG A 1 7   ? 50.969 18.664  -1.645  1.00 26.86 ? 7   ARG A CG  1 
ATOM   58   C  CD  . ARG A 1 7   ? 52.313 19.203  -2.128  1.00 32.01 ? 7   ARG A CD  1 
ATOM   59   N  NE  . ARG A 1 7   ? 53.339 19.155  -1.092  1.00 33.66 ? 7   ARG A NE  1 
ATOM   60   C  CZ  . ARG A 1 7   ? 53.348 19.925  -0.010  1.00 34.82 ? 7   ARG A CZ  1 
ATOM   61   N  NH1 . ARG A 1 7   ? 52.394 20.818  0.214   1.00 31.28 ? 7   ARG A NH1 1 
ATOM   62   N  NH2 . ARG A 1 7   ? 54.343 19.800  0.869   1.00 32.38 ? 7   ARG A NH2 1 
ATOM   63   N  N   . ARG A 1 8   ? 47.048 20.740  -2.736  1.00 23.58 ? 8   ARG A N   1 
ATOM   64   C  CA  . ARG A 1 8   ? 46.155 21.502  -3.605  1.00 23.61 ? 8   ARG A CA  1 
ATOM   65   C  C   . ARG A 1 8   ? 44.823 20.780  -3.788  1.00 24.97 ? 8   ARG A C   1 
ATOM   66   O  O   . ARG A 1 8   ? 44.249 20.742  -4.881  1.00 23.41 ? 8   ARG A O   1 
ATOM   67   C  CB  . ARG A 1 8   ? 46.826 21.808  -4.946  1.00 23.90 ? 8   ARG A CB  1 
ATOM   68   C  CG  . ARG A 1 8   ? 47.879 22.916  -4.821  1.00 25.75 ? 8   ARG A CG  1 
ATOM   69   C  CD  . ARG A 1 8   ? 48.738 23.076  -6.070  1.00 28.67 ? 8   ARG A CD  1 
ATOM   70   N  NE  . ARG A 1 8   ? 49.804 22.083  -6.173  1.00 31.64 ? 8   ARG A NE  1 
ATOM   71   C  CZ  . ARG A 1 8   ? 50.963 22.144  -5.531  1.00 33.45 ? 8   ARG A CZ  1 
ATOM   72   N  NH1 . ARG A 1 8   ? 51.249 23.143  -4.712  1.00 33.06 ? 8   ARG A NH1 1 
ATOM   73   N  NH2 . ARG A 1 8   ? 51.862 21.180  -5.723  1.00 32.24 ? 8   ARG A NH2 1 
ATOM   74   N  N   . ALA A 1 9   ? 44.342 20.190  -2.702  1.00 23.00 ? 9   ALA A N   1 
ATOM   75   C  CA  . ALA A 1 9   ? 42.994 19.655  -2.651  1.00 24.37 ? 9   ALA A CA  1 
ATOM   76   C  C   . ALA A 1 9   ? 42.011 20.804  -2.524  1.00 23.54 ? 9   ALA A C   1 
ATOM   77   O  O   . ALA A 1 9   ? 42.337 21.869  -1.991  1.00 27.81 ? 9   ALA A O   1 
ATOM   78   C  CB  . ALA A 1 9   ? 42.837 18.699  -1.467  1.00 23.29 ? 9   ALA A CB  1 
ATOM   79   N  N   . ARG A 1 10  ? 40.804 20.596  -3.024  1.00 22.43 ? 10  ARG A N   1 
ATOM   80   C  CA  . ARG A 1 10  ? 39.756 21.590  -2.877  1.00 24.83 ? 10  ARG A CA  1 
ATOM   81   C  C   . ARG A 1 10  ? 38.766 21.122  -1.822  1.00 23.89 ? 10  ARG A C   1 
ATOM   82   O  O   . ARG A 1 10  ? 38.273 19.991  -1.882  1.00 20.30 ? 10  ARG A O   1 
ATOM   83   C  CB  . ARG A 1 10  ? 39.064 21.867  -4.211  1.00 25.70 ? 10  ARG A CB  1 
ATOM   84   C  CG  . ARG A 1 10  ? 38.626 23.309  -4.335  1.00 30.88 ? 10  ARG A CG  1 
ATOM   85   C  CD  . ARG A 1 10  ? 38.018 23.598  -5.690  1.00 33.94 ? 10  ARG A CD  1 
ATOM   86   N  NE  . ARG A 1 10  ? 39.066 23.786  -6.685  1.00 34.11 ? 10  ARG A NE  1 
ATOM   87   C  CZ  . ARG A 1 10  ? 39.893 24.823  -6.730  1.00 35.34 ? 10  ARG A CZ  1 
ATOM   88   N  NH1 . ARG A 1 10  ? 39.797 25.830  -5.872  1.00 35.99 ? 10  ARG A NH1 1 
ATOM   89   N  NH2 . ARG A 1 10  ? 40.835 24.860  -7.669  1.00 34.49 ? 10  ARG A NH2 1 
ATOM   90   N  N   . LEU A 1 11  ? 38.523 21.969  -0.828  1.00 25.55 ? 11  LEU A N   1 
ATOM   91   C  CA  . LEU A 1 11  ? 37.462 21.680  0.118   1.00 25.22 ? 11  LEU A CA  1 
ATOM   92   C  C   . LEU A 1 11  ? 36.129 22.099  -0.491  1.00 23.02 ? 11  LEU A C   1 
ATOM   93   O  O   . LEU A 1 11  ? 36.078 22.826  -1.482  1.00 25.44 ? 11  LEU A O   1 
ATOM   94   C  CB  . LEU A 1 11  ? 37.694 22.404  1.441   1.00 25.42 ? 11  LEU A CB  1 
ATOM   95   C  CG  . LEU A 1 11  ? 38.946 22.092  2.264   1.00 26.06 ? 11  LEU A CG  1 
ATOM   96   C  CD1 . LEU A 1 11  ? 38.970 22.965  3.510   1.00 28.70 ? 11  LEU A CD1 1 
ATOM   97   C  CD2 . LEU A 1 11  ? 39.053 20.611  2.635   1.00 22.44 ? 11  LEU A CD2 1 
ATOM   98   N  N   . VAL A 1 12  ? 35.031 21.655  0.125   1.00 25.07 ? 12  VAL A N   1 
ATOM   99   C  CA  . VAL A 1 12  ? 33.714 21.930  -0.442  1.00 23.19 ? 12  VAL A CA  1 
ATOM   100  C  C   . VAL A 1 12  ? 33.326 23.399  -0.387  1.00 29.14 ? 12  VAL A C   1 
ATOM   101  O  O   . VAL A 1 12  ? 32.339 23.792  -1.020  1.00 31.86 ? 12  VAL A O   1 
ATOM   102  C  CB  . VAL A 1 12  ? 32.635 21.070  0.240   1.00 26.90 ? 12  VAL A CB  1 
ATOM   103  C  CG1 . VAL A 1 12  ? 32.721 19.644  -0.286  1.00 22.52 ? 12  VAL A CG1 1 
ATOM   104  C  CG2 . VAL A 1 12  ? 32.801 21.113  1.750   1.00 29.75 ? 12  VAL A CG2 1 
ATOM   105  N  N   . ASP A 1 13  ? 34.065 24.227  0.337   1.00 28.06 ? 13  ASP A N   1 
ATOM   106  C  CA  . ASP A 1 13  ? 33.870 25.664  0.243   1.00 30.38 ? 13  ASP A CA  1 
ATOM   107  C  C   . ASP A 1 13  ? 34.714 26.276  -0.871  1.00 28.60 ? 13  ASP A C   1 
ATOM   108  O  O   . ASP A 1 13  ? 34.774 27.503  -0.987  1.00 31.20 ? 13  ASP A O   1 
ATOM   109  C  CB  . ASP A 1 13  ? 34.159 26.331  1.594   1.00 30.71 ? 13  ASP A CB  1 
ATOM   110  C  CG  . ASP A 1 13  ? 35.613 26.204  2.033   1.00 33.37 ? 13  ASP A CG  1 
ATOM   111  O  OD1 . ASP A 1 13  ? 36.451 25.679  1.270   1.00 28.74 ? 13  ASP A OD1 1 
ATOM   112  O  OD2 . ASP A 1 13  ? 35.914 26.637  3.168   1.00 32.94 ? 13  ASP A OD2 1 
ATOM   113  N  N   . ASP A 1 14  ? 35.365 25.428  -1.675  1.00 30.81 ? 14  ASP A N   1 
ATOM   114  C  CA  . ASP A 1 14  ? 36.187 25.743  -2.845  1.00 32.29 ? 14  ASP A CA  1 
ATOM   115  C  C   . ASP A 1 14  ? 37.552 26.330  -2.518  1.00 27.88 ? 14  ASP A C   1 
ATOM   116  O  O   . ASP A 1 14  ? 38.240 26.798  -3.429  1.00 29.05 ? 14  ASP A O   1 
ATOM   117  C  CB  . ASP A 1 14  ? 35.467 26.663  -3.838  1.00 32.16 ? 14  ASP A CB  1 
ATOM   118  C  CG  . ASP A 1 14  ? 34.717 25.882  -4.907  1.00 39.34 ? 14  ASP A CG  1 
ATOM   119  O  OD1 . ASP A 1 14  ? 34.014 24.907  -4.568  1.00 35.89 ? 14  ASP A OD1 1 
ATOM   120  O  OD2 . ASP A 1 14  ? 34.841 26.240  -6.098  1.00 49.13 ? 14  ASP A OD2 1 
ATOM   121  N  N   . THR A 1 15  ? 37.991 26.285  -1.268  1.00 26.35 ? 15  THR A N   1 
ATOM   122  C  CA  . THR A 1 15  ? 39.336 26.748  -0.961  1.00 27.91 ? 15  THR A CA  1 
ATOM   123  C  C   . THR A 1 15  ? 40.352 25.637  -1.206  1.00 25.68 ? 15  THR A C   1 
ATOM   124  O  O   . THR A 1 15  ? 40.033 24.447  -1.140  1.00 25.06 ? 15  THR A O   1 
ATOM   125  C  CB  . THR A 1 15  ? 39.417 27.259  0.481   1.00 26.93 ? 15  THR A CB  1 
ATOM   126  O  OG1 . THR A 1 15  ? 39.220 26.179  1.404   1.00 27.93 ? 15  THR A OG1 1 
ATOM   127  C  CG2 . THR A 1 15  ? 38.363 28.351  0.716   1.00 27.64 ? 15  THR A CG2 1 
ATOM   128  N  N   . LEU A 1 16  ? 41.577 26.039  -1.532  1.00 23.89 ? 16  LEU A N   1 
ATOM   129  C  CA  . LEU A 1 16  ? 42.662 25.095  -1.766  1.00 26.10 ? 16  LEU A CA  1 
ATOM   130  C  C   . LEU A 1 16  ? 43.396 24.828  -0.461  1.00 27.04 ? 16  LEU A C   1 
ATOM   131  O  O   . LEU A 1 16  ? 43.657 25.753  0.316   1.00 29.70 ? 16  LEU A O   1 
ATOM   132  C  CB  . LEU A 1 16  ? 43.647 25.643  -2.803  1.00 25.93 ? 16  LEU A CB  1 
ATOM   133  C  CG  . LEU A 1 16  ? 43.309 25.424  -4.275  1.00 30.63 ? 16  LEU A CG  1 
ATOM   134  C  CD1 . LEU A 1 16  ? 44.392 26.025  -5.153  1.00 31.42 ? 16  LEU A CD1 1 
ATOM   135  C  CD2 . LEU A 1 16  ? 43.100 23.948  -4.589  1.00 28.79 ? 16  LEU A CD2 1 
ATOM   136  N  N   . THR A 1 17  ? 43.742 23.568  -0.219  1.00 22.86 ? 17  THR A N   1 
ATOM   137  C  CA  . THR A 1 17  ? 44.465 23.255  1.006   1.00 24.01 ? 17  THR A CA  1 
ATOM   138  C  C   . THR A 1 17  ? 45.213 21.940  0.829   1.00 27.30 ? 17  THR A C   1 
ATOM   139  O  O   . THR A 1 17  ? 45.019 21.214  -0.152  1.00 22.80 ? 17  THR A O   1 
ATOM   140  C  CB  . THR A 1 17  ? 43.511 23.198  2.212   1.00 27.17 ? 17  THR A CB  1 
ATOM   141  O  OG1 . THR A 1 17  ? 44.260 23.386  3.420   1.00 32.68 ? 17  THR A OG1 1 
ATOM   142  C  CG2 . THR A 1 17  ? 42.795 21.853  2.273   1.00 26.12 ? 17  THR A CG2 1 
ATOM   143  N  N   . ASP A 1 18  ? 46.093 21.660  1.791   1.00 26.06 ? 18  ASP A N   1 
ATOM   144  C  CA  . ASP A 1 18  ? 46.863 20.428  1.860   1.00 26.37 ? 18  ASP A CA  1 
ATOM   145  C  C   . ASP A 1 18  ? 46.355 19.597  3.031   1.00 25.41 ? 18  ASP A C   1 
ATOM   146  O  O   . ASP A 1 18  ? 45.934 20.147  4.057   1.00 24.03 ? 18  ASP A O   1 
ATOM   147  C  CB  . ASP A 1 18  ? 48.358 20.706  2.066   1.00 28.25 ? 18  ASP A CB  1 
ATOM   148  C  CG  . ASP A 1 18  ? 48.956 21.617  1.003   1.00 30.92 ? 18  ASP A CG  1 
ATOM   149  O  OD1 . ASP A 1 18  ? 48.402 21.721  -0.114  1.00 26.69 ? 18  ASP A OD1 1 
ATOM   150  O  OD2 . ASP A 1 18  ? 49.983 22.256  1.314   1.00 32.02 ? 18  ASP A OD2 1 
ATOM   151  N  N   . ILE A 1 19  ? 46.412 18.270  2.875   1.00 22.03 ? 19  ILE A N   1 
ATOM   152  C  CA  . ILE A 1 19  ? 45.953 17.321  3.885   1.00 19.45 ? 19  ILE A CA  1 
ATOM   153  C  C   . ILE A 1 19  ? 47.030 16.260  4.095   1.00 21.69 ? 19  ILE A C   1 
ATOM   154  O  O   . ILE A 1 19  ? 47.331 15.481  3.179   1.00 22.13 ? 19  ILE A O   1 
ATOM   155  C  CB  . ILE A 1 19  ? 44.628 16.653  3.490   1.00 23.21 ? 19  ILE A CB  1 
ATOM   156  C  CG1 . ILE A 1 19  ? 43.574 17.704  3.144   1.00 21.31 ? 19  ILE A CG1 1 
ATOM   157  C  CG2 . ILE A 1 19  ? 44.146 15.749  4.625   1.00 20.58 ? 19  ILE A CG2 1 
ATOM   158  C  CD1 . ILE A 1 19  ? 42.314 17.121  2.578   1.00 24.52 ? 19  ILE A CD1 1 
ATOM   159  N  N   . ALA A 1 20  ? 47.585 16.208  5.302   1.00 21.63 ? 20  ALA A N   1 
ATOM   160  C  CA  . ALA A 1 20  ? 48.619 15.247  5.658   1.00 21.48 ? 20  ALA A CA  1 
ATOM   161  C  C   . ALA A 1 20  ? 48.031 14.150  6.534   1.00 21.46 ? 20  ALA A C   1 
ATOM   162  O  O   . ALA A 1 20  ? 47.299 14.441  7.495   1.00 20.90 ? 20  ALA A O   1 
ATOM   163  C  CB  . ALA A 1 20  ? 49.775 15.930  6.389   1.00 23.31 ? 20  ALA A CB  1 
ATOM   164  N  N   . ILE A 1 21  ? 48.415 12.909  6.225   1.00 20.83 ? 21  ILE A N   1 
ATOM   165  C  CA  . ILE A 1 21  ? 47.936 11.693  6.864   1.00 22.15 ? 21  ILE A CA  1 
ATOM   166  C  C   . ILE A 1 21  ? 49.140 10.925  7.392   1.00 25.06 ? 21  ILE A C   1 
ATOM   167  O  O   . ILE A 1 21  ? 50.115 10.685  6.659   1.00 22.80 ? 21  ILE A O   1 
ATOM   168  C  CB  . ILE A 1 21  ? 47.130 10.827  5.879   1.00 22.20 ? 21  ILE A CB  1 
ATOM   169  C  CG1 . ILE A 1 21  ? 45.808 11.513  5.534   1.00 22.18 ? 21  ILE A CG1 1 
ATOM   170  C  CG2 . ILE A 1 21  ? 46.891 9.430   6.439   1.00 25.22 ? 21  ILE A CG2 1 
ATOM   171  C  CD1 . ILE A 1 21  ? 45.420 11.356  4.064   1.00 24.66 ? 21  ILE A CD1 1 
ATOM   172  N  N   . GLN A 1 22  ? 49.052 10.518  8.652   1.00 24.40 ? 22  GLN A N   1 
ATOM   173  C  CA  . GLN A 1 22  ? 50.108 9.776   9.317   1.00 27.35 ? 22  GLN A CA  1 
ATOM   174  C  C   . GLN A 1 22  ? 49.458 8.712   10.189  1.00 27.89 ? 22  GLN A C   1 
ATOM   175  O  O   . GLN A 1 22  ? 48.579 9.024   11.001  1.00 24.57 ? 22  GLN A O   1 
ATOM   176  C  CB  . GLN A 1 22  ? 50.987 10.703  10.170  1.00 30.18 ? 22  GLN A CB  1 
ATOM   177  C  CG  . GLN A 1 22  ? 52.070 9.969   10.954  1.00 36.08 ? 22  GLN A CG  1 
ATOM   178  C  CD  . GLN A 1 22  ? 53.472 10.456  10.629  1.00 36.98 ? 22  GLN A CD  1 
ATOM   179  O  OE1 . GLN A 1 22  ? 53.673 11.203  9.678   1.00 40.18 ? 22  GLN A OE1 1 
ATOM   180  N  NE2 . GLN A 1 22  ? 54.451 10.022  11.418  1.00 39.70 ? 22  GLN A NE2 1 
ATOM   181  N  N   . ASP A 1 23  ? 49.875 7.461   9.998   1.00 29.32 ? 23  ASP A N   1 
ATOM   182  C  CA  . ASP A 1 23  ? 49.481 6.352   10.868  1.00 31.15 ? 23  ASP A CA  1 
ATOM   183  C  C   . ASP A 1 23  ? 47.962 6.191   10.907  1.00 27.81 ? 23  ASP A C   1 
ATOM   184  O  O   . ASP A 1 23  ? 47.354 6.071   11.971  1.00 24.91 ? 23  ASP A O   1 
ATOM   185  C  CB  . ASP A 1 23  ? 50.045 6.540   12.277  1.00 29.50 ? 23  ASP A CB  1 
ATOM   186  C  CG  . ASP A 1 23  ? 51.561 6.443   12.323  1.00 36.02 ? 23  ASP A CG  1 
ATOM   187  O  OD1 . ASP A 1 23  ? 52.150 5.635   11.570  1.00 36.97 ? 23  ASP A OD1 1 
ATOM   188  O  OD2 . ASP A 1 23  ? 52.165 7.176   13.133  1.00 39.66 ? 23  ASP A OD2 1 
ATOM   189  N  N   . GLY A 1 24  ? 47.344 6.216   9.726   1.00 26.63 ? 24  GLY A N   1 
ATOM   190  C  CA  . GLY A 1 24  ? 45.912 6.019   9.620   1.00 26.73 ? 24  GLY A CA  1 
ATOM   191  C  C   . GLY A 1 24  ? 45.041 7.124   10.175  1.00 26.69 ? 24  GLY A C   1 
ATOM   192  O  O   . GLY A 1 24  ? 43.828 6.930   10.280  1.00 26.62 ? 24  GLY A O   1 
ATOM   193  N  N   . LYS A 1 25  ? 45.615 8.283   10.516  1.00 24.97 ? 25  LYS A N   1 
ATOM   194  C  CA  . LYS A 1 25  ? 44.885 9.395   11.104  1.00 21.69 ? 25  LYS A CA  1 
ATOM   195  C  C   . LYS A 1 25  ? 45.160 10.648  10.284  1.00 21.69 ? 25  LYS A C   1 
ATOM   196  O  O   . LYS A 1 25  ? 46.190 10.762  9.619   1.00 22.17 ? 25  LYS A O   1 
ATOM   197  C  CB  . LYS A 1 25  ? 45.318 9.650   12.555  1.00 23.51 ? 25  LYS A CB  1 
ATOM   198  C  CG  . LYS A 1 25  ? 45.166 8.453   13.475  1.00 28.07 ? 25  LYS A CG  1 
ATOM   199  C  CD  . LYS A 1 25  ? 44.606 8.813   14.826  1.00 33.45 ? 25  LYS A CD  1 
ATOM   200  C  CE  . LYS A 1 25  ? 43.559 7.802   15.233  1.00 39.13 ? 25  LYS A CE  1 
ATOM   201  N  NZ  . LYS A 1 25  ? 44.148 6.433   15.383  1.00 40.93 ? 25  LYS A NZ  1 
ATOM   202  N  N   . ILE A 1 26  ? 44.236 11.601  10.334  1.00 20.12 ? 26  ILE A N   1 
ATOM   203  C  CA  . ILE A 1 26  ? 44.528 12.898  9.733   1.00 22.39 ? 26  ILE A CA  1 
ATOM   204  C  C   . ILE A 1 26  ? 45.562 13.599  10.603  1.00 21.95 ? 26  ILE A C   1 
ATOM   205  O  O   . ILE A 1 26  ? 45.359 13.784  11.809  1.00 23.35 ? 26  ILE A O   1 
ATOM   206  C  CB  . ILE A 1 26  ? 43.254 13.732  9.567   1.00 19.41 ? 26  ILE A CB  1 
ATOM   207  C  CG1 . ILE A 1 26  ? 42.273 12.994  8.650   1.00 19.82 ? 26  ILE A CG1 1 
ATOM   208  C  CG2 . ILE A 1 26  ? 43.595 15.092  8.975   1.00 20.29 ? 26  ILE A CG2 1 
ATOM   209  C  CD1 . ILE A 1 26  ? 40.873 13.529  8.695   1.00 25.84 ? 26  ILE A CD1 1 
ATOM   210  N  N   . ALA A 1 27  ? 46.701 13.940  10.008  1.00 20.34 ? 27  ALA A N   1 
ATOM   211  C  CA  . ALA A 1 27  ? 47.782 14.560  10.760  1.00 21.46 ? 27  ALA A CA  1 
ATOM   212  C  C   . ALA A 1 27  ? 47.678 16.076  10.765  1.00 25.22 ? 27  ALA A C   1 
ATOM   213  O  O   . ALA A 1 27  ? 47.924 16.717  11.802  1.00 23.74 ? 27  ALA A O   1 
ATOM   214  C  CB  . ALA A 1 27  ? 49.131 14.132  10.185  1.00 22.41 ? 27  ALA A CB  1 
ATOM   215  N  N   . ALA A 1 28  ? 47.322 16.662  9.623   1.00 23.01 ? 28  ALA A N   1 
ATOM   216  C  CA  . ALA A 1 28  ? 47.304 18.117  9.546   1.00 22.72 ? 28  ALA A CA  1 
ATOM   217  C  C   . ALA A 1 28  ? 46.520 18.564  8.321   1.00 24.48 ? 28  ALA A C   1 
ATOM   218  O  O   . ALA A 1 28  ? 46.388 17.825  7.342   1.00 21.58 ? 28  ALA A O   1 
ATOM   219  C  CB  . ALA A 1 28  ? 48.726 18.692  9.511   1.00 23.73 ? 28  ALA A CB  1 
ATOM   220  N  N   . LEU A 1 29  ? 45.991 19.790  8.401   1.00 25.66 ? 29  LEU A N   1 
ATOM   221  C  CA  . LEU A 1 29  ? 45.363 20.455  7.266   1.00 25.08 ? 29  LEU A CA  1 
ATOM   222  C  C   . LEU A 1 29  ? 45.845 21.894  7.189   1.00 25.56 ? 29  LEU A C   1 
ATOM   223  O  O   . LEU A 1 29  ? 46.026 22.557  8.214   1.00 27.16 ? 29  LEU A O   1 
ATOM   224  C  CB  . LEU A 1 29  ? 43.834 20.444  7.352   1.00 26.50 ? 29  LEU A CB  1 
ATOM   225  C  CG  . LEU A 1 29  ? 43.152 19.090  7.182   1.00 28.06 ? 29  LEU A CG  1 
ATOM   226  C  CD1 . LEU A 1 29  ? 42.812 18.528  8.544   1.00 30.78 ? 29  LEU A CD1 1 
ATOM   227  C  CD2 . LEU A 1 29  ? 41.901 19.247  6.329   1.00 28.40 ? 29  LEU A CD2 1 
ATOM   228  N  N   . GLY A 1 30  ? 46.045 22.369  5.966   1.00 26.81 ? 30  GLY A N   1 
ATOM   229  C  CA  . GLY A 1 30  ? 46.477 23.737  5.753   1.00 26.41 ? 30  GLY A CA  1 
ATOM   230  C  C   . GLY A 1 30  ? 47.619 23.832  4.764   1.00 32.87 ? 30  GLY A C   1 
ATOM   231  O  O   . GLY A 1 30  ? 47.681 23.054  3.807   1.00 28.91 ? 30  GLY A O   1 
ATOM   232  N  N   . GLU A 1 31  ? 48.522 24.787  4.983   1.00 32.02 ? 31  GLU A N   1 
ATOM   233  C  CA  . GLU A 1 31  ? 49.736 24.913  4.190   1.00 35.69 ? 31  GLU A CA  1 
ATOM   234  C  C   . GLU A 1 31  ? 50.809 24.049  4.839   1.00 33.58 ? 31  GLU A C   1 
ATOM   235  O  O   . GLU A 1 31  ? 51.188 24.291  5.990   1.00 31.11 ? 31  GLU A O   1 
ATOM   236  C  CB  . GLU A 1 31  ? 50.179 26.376  4.112   1.00 40.81 ? 31  GLU A CB  1 
ATOM   237  C  CG  . GLU A 1 31  ? 49.668 27.134  2.889   1.00 42.76 ? 31  GLU A CG  1 
ATOM   238  C  CD  . GLU A 1 31  ? 49.434 26.245  1.680   1.00 44.68 ? 31  GLU A CD  1 
ATOM   239  O  OE1 . GLU A 1 31  ? 50.401 25.598  1.216   1.00 48.48 ? 31  GLU A OE1 1 
ATOM   240  O  OE2 . GLU A 1 31  ? 48.277 26.181  1.203   1.00 44.28 ? 31  GLU A OE2 1 
ATOM   241  N  N   . ILE A 1 32  ? 51.285 23.037  4.116   1.00 32.99 ? 32  ILE A N   1 
ATOM   242  C  CA  . ILE A 1 32  ? 52.142 22.001  4.684   1.00 32.13 ? 32  ILE A CA  1 
ATOM   243  C  C   . ILE A 1 32  ? 53.426 21.889  3.873   1.00 33.89 ? 32  ILE A C   1 
ATOM   244  O  O   . ILE A 1 32  ? 53.385 21.728  2.648   1.00 32.05 ? 32  ILE A O   1 
ATOM   245  C  CB  . ILE A 1 32  ? 51.412 20.647  4.749   1.00 28.99 ? 32  ILE A CB  1 
ATOM   246  C  CG1 . ILE A 1 32  ? 50.147 20.790  5.600   1.00 27.77 ? 32  ILE A CG1 1 
ATOM   247  C  CG2 . ILE A 1 32  ? 52.333 19.569  5.299   1.00 31.38 ? 32  ILE A CG2 1 
ATOM   248  C  CD1 . ILE A 1 32  ? 49.251 19.574  5.589   1.00 25.02 ? 32  ILE A CD1 1 
ATOM   249  N  N   . SER A 1 33  ? 54.567 21.969  4.566   1.00 32.06 ? 33  SER A N   1 
ATOM   250  C  CA  . SER A 1 33  ? 55.875 21.816  3.946   1.00 34.93 ? 33  SER A CA  1 
ATOM   251  C  C   . SER A 1 33  ? 56.639 20.586  4.421   1.00 32.91 ? 33  SER A C   1 
ATOM   252  O  O   . SER A 1 33  ? 57.629 20.214  3.780   1.00 33.76 ? 33  SER A O   1 
ATOM   253  C  CB  . SER A 1 33  ? 56.733 23.070  4.196   1.00 36.34 ? 33  SER A CB  1 
ATOM   254  O  OG  . SER A 1 33  ? 57.020 23.230  5.576   1.00 35.52 ? 33  SER A OG  1 
ATOM   255  N  N   . ALA A 1 34  ? 56.216 19.949  5.517   1.00 34.82 ? 34  ALA A N   1 
ATOM   256  C  CA  . ALA A 1 34  ? 56.909 18.780  6.038   1.00 35.06 ? 34  ALA A CA  1 
ATOM   257  C  C   . ALA A 1 34  ? 56.940 17.670  4.985   1.00 31.75 ? 34  ALA A C   1 
ATOM   258  O  O   . ALA A 1 34  ? 56.092 17.633  4.089   1.00 32.39 ? 34  ALA A O   1 
ATOM   259  C  CB  . ALA A 1 34  ? 56.226 18.293  7.316   1.00 32.40 ? 34  ALA A CB  1 
ATOM   260  N  N   . PRO A 1 35  ? 57.908 16.756  5.070   1.00 34.29 ? 35  PRO A N   1 
ATOM   261  C  CA  . PRO A 1 35  ? 58.033 15.710  4.048   1.00 31.99 ? 35  PRO A CA  1 
ATOM   262  C  C   . PRO A 1 35  ? 56.995 14.607  4.210   1.00 32.02 ? 35  PRO A C   1 
ATOM   263  O  O   . PRO A 1 35  ? 56.404 14.408  5.275   1.00 31.12 ? 35  PRO A O   1 
ATOM   264  C  CB  . PRO A 1 35  ? 59.451 15.160  4.266   1.00 33.20 ? 35  PRO A CB  1 
ATOM   265  C  CG  . PRO A 1 35  ? 60.053 15.975  5.407   1.00 34.94 ? 35  PRO A CG  1 
ATOM   266  C  CD  . PRO A 1 35  ? 58.907 16.583  6.137   1.00 33.52 ? 35  PRO A CD  1 
ATOM   267  N  N   . SER A 1 36  ? 56.785 13.878  3.115   1.00 31.36 ? 36  SER A N   1 
ATOM   268  C  CA  . SER A 1 36  ? 55.842 12.767  3.073   1.00 30.22 ? 36  SER A CA  1 
ATOM   269  C  C   . SER A 1 36  ? 56.436 11.636  2.251   1.00 31.02 ? 36  SER A C   1 
ATOM   270  O  O   . SER A 1 36  ? 57.191 11.872  1.306   1.00 30.04 ? 36  SER A O   1 
ATOM   271  C  CB  . SER A 1 36  ? 54.499 13.179  2.462   1.00 29.04 ? 36  SER A CB  1 
ATOM   272  O  OG  . SER A 1 36  ? 53.702 12.049  2.143   1.00 27.98 ? 36  SER A OG  1 
ATOM   273  N  N   . ARG A 1 37  ? 56.075 10.400  2.610   1.00 30.46 ? 37  ARG A N   1 
ATOM   274  C  CA  . ARG A 1 37  ? 56.523 9.247   1.837   1.00 30.04 ? 37  ARG A CA  1 
ATOM   275  C  C   . ARG A 1 37  ? 55.820 9.162   0.491   1.00 29.12 ? 37  ARG A C   1 
ATOM   276  O  O   . ARG A 1 37  ? 56.341 8.530   -0.436  1.00 29.05 ? 37  ARG A O   1 
ATOM   277  C  CB  . ARG A 1 37  ? 56.295 7.954   2.625   1.00 32.78 ? 37  ARG A CB  1 
ATOM   278  N  N   . LYS A 1 38  ? 54.661 9.798   0.366   1.00 26.49 ? 38  LYS A N   1 
ATOM   279  C  CA  . LYS A 1 38  ? 53.883 9.776   -0.862  1.00 29.18 ? 38  LYS A CA  1 
ATOM   280  C  C   . LYS A 1 38  ? 53.114 11.084  -0.939  1.00 26.26 ? 38  LYS A C   1 
ATOM   281  O  O   . LYS A 1 38  ? 52.439 11.462  0.024   1.00 25.92 ? 38  LYS A O   1 
ATOM   282  C  CB  . LYS A 1 38  ? 52.923 8.582   -0.885  1.00 26.35 ? 38  LYS A CB  1 
ATOM   283  C  CG  . LYS A 1 38  ? 51.898 8.623   -2.005  1.00 32.82 ? 38  LYS A CG  1 
ATOM   284  C  CD  . LYS A 1 38  ? 52.460 8.010   -3.282  1.00 37.30 ? 38  LYS A CD  1 
ATOM   285  C  CE  . LYS A 1 38  ? 51.346 7.467   -4.166  1.00 45.13 ? 38  LYS A CE  1 
ATOM   286  N  NZ  . LYS A 1 38  ? 51.209 8.237   -5.437  1.00 45.14 ? 38  LYS A NZ  1 
ATOM   287  N  N   . THR A 1 39  ? 53.222 11.773  -2.069  1.00 24.90 ? 39  THR A N   1 
ATOM   288  C  CA  . THR A 1 39  ? 52.526 13.038  -2.242  1.00 26.14 ? 39  THR A CA  1 
ATOM   289  C  C   . THR A 1 39  ? 51.728 12.991  -3.535  1.00 28.04 ? 39  THR A C   1 
ATOM   290  O  O   . THR A 1 39  ? 52.231 12.527  -4.564  1.00 29.55 ? 39  THR A O   1 
ATOM   291  C  CB  . THR A 1 39  ? 53.515 14.216  -2.258  1.00 28.27 ? 39  THR A CB  1 
ATOM   292  O  OG1 . THR A 1 39  ? 54.277 14.215  -1.044  1.00 25.44 ? 39  THR A OG1 1 
ATOM   293  C  CG2 . THR A 1 39  ? 52.779 15.537  -2.382  1.00 24.99 ? 39  THR A CG2 1 
ATOM   294  N  N   . ILE A 1 40  ? 50.482 13.459  -3.472  1.00 23.64 ? 40  ILE A N   1 
ATOM   295  C  CA  . ILE A 1 40  ? 49.599 13.539  -4.629  1.00 28.05 ? 40  ILE A CA  1 
ATOM   296  C  C   . ILE A 1 40  ? 49.169 14.988  -4.804  1.00 26.26 ? 40  ILE A C   1 
ATOM   297  O  O   . ILE A 1 40  ? 48.700 15.623  -3.853  1.00 24.63 ? 40  ILE A O   1 
ATOM   298  C  CB  . ILE A 1 40  ? 48.370 12.629  -4.477  1.00 26.45 ? 40  ILE A CB  1 
ATOM   299  C  CG1 . ILE A 1 40  ? 48.798 11.171  -4.328  1.00 29.97 ? 40  ILE A CG1 1 
ATOM   300  C  CG2 . ILE A 1 40  ? 47.450 12.787  -5.678  1.00 31.63 ? 40  ILE A CG2 1 
ATOM   301  C  CD1 . ILE A 1 40  ? 47.660 10.248  -4.013  1.00 28.89 ? 40  ILE A CD1 1 
ATOM   302  N  N   . ASP A 1 41  ? 49.330 15.506  -6.013  1.00 29.04 ? 41  ASP A N   1 
ATOM   303  C  CA  . ASP A 1 41  ? 48.932 16.866  -6.354  1.00 25.10 ? 41  ASP A CA  1 
ATOM   304  C  C   . ASP A 1 41  ? 47.582 16.795  -7.062  1.00 27.23 ? 41  ASP A C   1 
ATOM   305  O  O   . ASP A 1 41  ? 47.504 16.346  -8.208  1.00 22.82 ? 41  ASP A O   1 
ATOM   306  C  CB  . ASP A 1 41  ? 49.993 17.524  -7.235  1.00 27.39 ? 41  ASP A CB  1 
ATOM   307  C  CG  . ASP A 1 41  ? 49.774 19.019  -7.403  1.00 28.89 ? 41  ASP A CG  1 
ATOM   308  O  OD1 . ASP A 1 41  ? 48.685 19.504  -7.040  1.00 25.83 ? 41  ASP A OD1 1 
ATOM   309  O  OD2 . ASP A 1 41  ? 50.692 19.706  -7.899  1.00 32.72 ? 41  ASP A OD2 1 
ATOM   310  N  N   . LEU A 1 42  ? 46.516 17.226  -6.379  1.00 24.22 ? 42  LEU A N   1 
ATOM   311  C  CA  . LEU A 1 42  ? 45.184 17.181  -6.977  1.00 25.30 ? 42  LEU A CA  1 
ATOM   312  C  C   . LEU A 1 42  ? 44.915 18.329  -7.946  1.00 25.82 ? 42  LEU A C   1 
ATOM   313  O  O   . LEU A 1 42  ? 43.873 18.318  -8.618  1.00 22.01 ? 42  LEU A O   1 
ATOM   314  C  CB  . LEU A 1 42  ? 44.123 17.146  -5.873  1.00 22.22 ? 42  LEU A CB  1 
ATOM   315  C  CG  . LEU A 1 42  ? 44.266 15.855  -5.052  1.00 26.31 ? 42  LEU A CG  1 
ATOM   316  C  CD1 . LEU A 1 42  ? 43.319 15.804  -3.868  1.00 23.29 ? 42  LEU A CD1 1 
ATOM   317  C  CD2 . LEU A 1 42  ? 44.020 14.666  -5.971  1.00 27.03 ? 42  LEU A CD2 1 
ATOM   318  N  N   . GLN A 1 43  ? 45.824 19.303  -8.025  1.00 25.30 ? 43  GLN A N   1 
ATOM   319  C  CA  . GLN A 1 43  ? 45.793 20.378  -9.026  1.00 25.10 ? 43  GLN A CA  1 
ATOM   320  C  C   . GLN A 1 43  ? 44.464 21.126  -9.054  1.00 24.04 ? 43  GLN A C   1 
ATOM   321  O  O   . GLN A 1 43  ? 43.981 21.541  -10.112 1.00 23.37 ? 43  GLN A O   1 
ATOM   322  C  CB  . GLN A 1 43  ? 46.144 19.846  -10.417 1.00 29.20 ? 43  GLN A CB  1 
ATOM   323  C  CG  . GLN A 1 43  ? 47.422 19.033  -10.450 1.00 29.28 ? 43  GLN A CG  1 
ATOM   324  C  CD  . GLN A 1 43  ? 47.676 18.401  -11.799 1.00 31.23 ? 43  GLN A CD  1 
ATOM   325  O  OE1 . GLN A 1 43  ? 48.458 18.922  -12.590 1.00 32.56 ? 43  GLN A OE1 1 
ATOM   326  N  NE2 . GLN A 1 43  ? 47.016 17.283  -12.072 1.00 35.59 ? 43  GLN A NE2 1 
ATOM   327  N  N   . GLY A 1 44  ? 43.879 21.321  -7.880  1.00 22.09 ? 44  GLY A N   1 
ATOM   328  C  CA  . GLY A 1 44  ? 42.633 22.048  -7.763  1.00 21.43 ? 44  GLY A CA  1 
ATOM   329  C  C   . GLY A 1 44  ? 41.461 21.456  -8.522  1.00 27.44 ? 44  GLY A C   1 
ATOM   330  O  O   . GLY A 1 44  ? 40.427 22.116  -8.653  1.00 26.60 ? 44  GLY A O   1 
ATOM   331  N  N   . ASN A 1 45  ? 41.586 20.218  -9.013  1.00 25.06 ? 45  ASN A N   1 
ATOM   332  C  CA  . ASN A 1 45  ? 40.579 19.643  -9.899  1.00 26.60 ? 45  ASN A CA  1 
ATOM   333  C  C   . ASN A 1 45  ? 39.812 18.495  -9.241  1.00 27.95 ? 45  ASN A C   1 
ATOM   334  O  O   . ASN A 1 45  ? 39.124 17.739  -9.932  1.00 29.05 ? 45  ASN A O   1 
ATOM   335  C  CB  . ASN A 1 45  ? 41.230 19.188  -11.212 1.00 25.74 ? 45  ASN A CB  1 
ATOM   336  C  CG  . ASN A 1 45  ? 40.221 18.974  -12.336 1.00 29.81 ? 45  ASN A CG  1 
ATOM   337  O  OD1 . ASN A 1 45  ? 39.392 19.844  -12.613 1.00 28.38 ? 45  ASN A OD1 1 
ATOM   338  N  ND2 . ASN A 1 45  ? 40.318 17.832  -13.017 1.00 31.20 ? 45  ASN A ND2 1 
ATOM   339  N  N   . SER A 1 46  ? 39.903 18.356  -7.919  1.00 23.59 ? 46  SER A N   1 
ATOM   340  C  CA  . SER A 1 46  ? 39.104 17.366  -7.211  1.00 25.57 ? 46  SER A CA  1 
ATOM   341  C  C   . SER A 1 46  ? 38.804 17.869  -5.809  1.00 25.25 ? 46  SER A C   1 
ATOM   342  O  O   . SER A 1 46  ? 39.691 18.396  -5.130  1.00 25.65 ? 46  SER A O   1 
ATOM   343  C  CB  . SER A 1 46  ? 39.815 16.006  -7.135  1.00 29.46 ? 46  SER A CB  1 
ATOM   344  O  OG  . SER A 1 46  ? 40.059 15.481  -8.429  1.00 32.63 ? 46  SER A OG  1 
ATOM   345  N  N   . TYR A 1 47  ? 37.554 17.709  -5.390  1.00 24.19 ? 47  TYR A N   1 
ATOM   346  C  CA  . TYR A 1 47  ? 37.205 17.931  -4.000  1.00 22.06 ? 47  TYR A CA  1 
ATOM   347  C  C   . TYR A 1 47  ? 37.694 16.775  -3.139  1.00 24.52 ? 47  TYR A C   1 
ATOM   348  O  O   . TYR A 1 47  ? 37.767 15.620  -3.582  1.00 25.03 ? 47  TYR A O   1 
ATOM   349  C  CB  . TYR A 1 47  ? 35.694 18.069  -3.822  1.00 23.85 ? 47  TYR A CB  1 
ATOM   350  C  CG  . TYR A 1 47  ? 35.063 19.257  -4.509  1.00 26.82 ? 47  TYR A CG  1 
ATOM   351  C  CD1 . TYR A 1 47  ? 35.241 20.540  -4.014  1.00 25.65 ? 47  TYR A CD1 1 
ATOM   352  C  CD2 . TYR A 1 47  ? 34.229 19.086  -5.609  1.00 25.63 ? 47  TYR A CD2 1 
ATOM   353  C  CE1 . TYR A 1 47  ? 34.649 21.625  -4.625  1.00 28.27 ? 47  TYR A CE1 1 
ATOM   354  C  CE2 . TYR A 1 47  ? 33.631 20.163  -6.222  1.00 27.70 ? 47  TYR A CE2 1 
ATOM   355  C  CZ  . TYR A 1 47  ? 33.843 21.430  -5.725  1.00 31.19 ? 47  TYR A CZ  1 
ATOM   356  O  OH  . TYR A 1 47  ? 33.253 22.515  -6.327  1.00 35.45 ? 47  TYR A OH  1 
ATOM   357  N  N   . VAL A 1 48  ? 38.011 17.100  -1.888  1.00 19.15 ? 48  VAL A N   1 
ATOM   358  C  CA  . VAL A 1 48  ? 38.276 16.121  -0.843  1.00 22.11 ? 48  VAL A CA  1 
ATOM   359  C  C   . VAL A 1 48  ? 37.375 16.451  0.333   1.00 20.72 ? 48  VAL A C   1 
ATOM   360  O  O   . VAL A 1 48  ? 37.279 17.614  0.743   1.00 20.48 ? 48  VAL A O   1 
ATOM   361  C  CB  . VAL A 1 48  ? 39.751 16.117  -0.403  1.00 23.04 ? 48  VAL A CB  1 
ATOM   362  C  CG1 . VAL A 1 48  ? 39.936 15.182  0.775   1.00 24.01 ? 48  VAL A CG1 1 
ATOM   363  C  CG2 . VAL A 1 48  ? 40.642 15.682  -1.538  1.00 21.64 ? 48  VAL A CG2 1 
ATOM   364  N  N   . SER A 1 49  ? 36.701 15.441  0.861   1.00 20.76 ? 49  SER A N   1 
ATOM   365  C  CA  . SER A 1 49  ? 35.941 15.617  2.086   1.00 21.57 ? 49  SER A CA  1 
ATOM   366  C  C   . SER A 1 49  ? 36.274 14.470  3.021   1.00 20.05 ? 49  SER A C   1 
ATOM   367  O  O   . SER A 1 49  ? 36.971 13.524  2.647   1.00 19.01 ? 49  SER A O   1 
ATOM   368  C  CB  . SER A 1 49  ? 34.431 15.681  1.811   1.00 23.80 ? 49  SER A CB  1 
ATOM   369  O  OG  . SER A 1 49  ? 33.939 14.410  1.419   1.00 18.52 ? 49  SER A OG  1 
ATOM   370  N  N   . ALA A 1 50  ? 35.785 14.562  4.259   1.00 19.93 ? 50  ALA A N   1 
ATOM   371  C  CA  . ALA A 1 50  ? 35.793 13.382  5.111   1.00 22.61 ? 50  ALA A CA  1 
ATOM   372  C  C   . ALA A 1 50  ? 35.107 12.232  4.378   1.00 15.63 ? 50  ALA A C   1 
ATOM   373  O  O   . ALA A 1 50  ? 34.231 12.446  3.530   1.00 16.23 ? 50  ALA A O   1 
ATOM   374  C  CB  . ALA A 1 50  ? 35.100 13.671  6.447   1.00 20.11 ? 50  ALA A CB  1 
ATOM   375  N  N   . GLY A 1 51  ? 35.548 11.009  4.672   1.00 20.67 ? 51  GLY A N   1 
ATOM   376  C  CA  . GLY A 1 51  ? 35.021 9.835   3.998   1.00 17.39 ? 51  GLY A CA  1 
ATOM   377  C  C   . GLY A 1 51  ? 33.513 9.799   4.116   1.00 17.28 ? 51  GLY A C   1 
ATOM   378  O  O   . GLY A 1 51  ? 32.984 10.001  5.210   1.00 18.11 ? 51  GLY A O   1 
ATOM   379  N  N   . TRP A 1 52  ? 32.806 9.606   3.005   1.00 13.30 ? 52  TRP A N   1 
ATOM   380  C  CA  . TRP A 1 52  ? 31.353 9.609   3.054   1.00 14.44 ? 52  TRP A CA  1 
ATOM   381  C  C   . TRP A 1 52  ? 30.837 8.431   3.873   1.00 17.57 ? 52  TRP A C   1 
ATOM   382  O  O   . TRP A 1 52  ? 31.390 7.327   3.835   1.00 16.72 ? 52  TRP A O   1 
ATOM   383  C  CB  . TRP A 1 52  ? 30.760 9.552   1.651   1.00 18.40 ? 52  TRP A CB  1 
ATOM   384  C  CG  . TRP A 1 52  ? 31.045 10.756  0.838   1.00 17.27 ? 52  TRP A CG  1 
ATOM   385  C  CD1 . TRP A 1 52  ? 31.599 11.935  1.266   1.00 18.55 ? 52  TRP A CD1 1 
ATOM   386  C  CD2 . TRP A 1 52  ? 30.775 10.922  -0.555  1.00 20.34 ? 52  TRP A CD2 1 
ATOM   387  N  NE1 . TRP A 1 52  ? 31.704 12.816  0.215   1.00 18.15 ? 52  TRP A NE1 1 
ATOM   388  C  CE2 . TRP A 1 52  ? 31.197 12.223  -0.911  1.00 19.69 ? 52  TRP A CE2 1 
ATOM   389  C  CE3 . TRP A 1 52  ? 30.223 10.095  -1.542  1.00 18.31 ? 52  TRP A CE3 1 
ATOM   390  C  CZ2 . TRP A 1 52  ? 31.078 12.715  -2.212  1.00 20.22 ? 52  TRP A CZ2 1 
ATOM   391  C  CZ3 . TRP A 1 52  ? 30.102 10.588  -2.832  1.00 23.30 ? 52  TRP A CZ3 1 
ATOM   392  C  CH2 . TRP A 1 52  ? 30.530 11.885  -3.154  1.00 23.17 ? 52  TRP A CH2 1 
ATOM   393  N  N   . ILE A 1 53  ? 29.771 8.687   4.617   1.00 17.69 ? 53  ILE A N   1 
ATOM   394  C  CA  . ILE A 1 53  ? 29.106 7.703   5.452   1.00 18.66 ? 53  ILE A CA  1 
ATOM   395  C  C   . ILE A 1 53  ? 27.699 7.533   4.906   1.00 18.65 ? 53  ILE A C   1 
ATOM   396  O  O   . ILE A 1 53  ? 26.968 8.520   4.765   1.00 16.70 ? 53  ILE A O   1 
ATOM   397  C  CB  . ILE A 1 53  ? 29.079 8.148   6.922   1.00 17.83 ? 53  ILE A CB  1 
ATOM   398  C  CG1 . ILE A 1 53  ? 30.506 8.305   7.450   1.00 17.45 ? 53  ILE A CG1 1 
ATOM   399  C  CG2 . ILE A 1 53  ? 28.292 7.170   7.772   1.00 19.79 ? 53  ILE A CG2 1 
ATOM   400  C  CD1 . ILE A 1 53  ? 30.588 9.048   8.774   1.00 19.89 ? 53  ILE A CD1 1 
ATOM   401  N  N   . ASP A 1 54  ? 27.329 6.291   4.589   1.00 19.33 ? 54  ASP A N   1 
ATOM   402  C  CA  . ASP A 1 54  ? 25.977 5.948   4.140   1.00 20.16 ? 54  ASP A CA  1 
ATOM   403  C  C   . ASP A 1 54  ? 25.262 5.289   5.316   1.00 20.89 ? 54  ASP A C   1 
ATOM   404  O  O   . ASP A 1 54  ? 25.555 4.143   5.669   1.00 17.73 ? 54  ASP A O   1 
ATOM   405  C  CB  . ASP A 1 54  ? 26.016 5.036   2.918   1.00 16.64 ? 54  ASP A CB  1 
ATOM   406  C  CG  . ASP A 1 54  ? 24.691 5.009   2.158   1.00 20.46 ? 54  ASP A CG  1 
ATOM   407  O  OD1 . ASP A 1 54  ? 23.646 5.360   2.749   1.00 19.61 ? 54  ASP A OD1 1 
ATOM   408  O  OD2 . ASP A 1 54  ? 24.687 4.592   0.977   1.00 20.69 ? 54  ASP A OD2 1 
ATOM   409  N  N   . SER A 1 55  ? 24.331 6.027   5.935   1.00 16.53 ? 55  SER A N   1 
ATOM   410  C  CA  . SER A 1 55  ? 23.691 5.609   7.177   1.00 20.04 ? 55  SER A CA  1 
ATOM   411  C  C   . SER A 1 55  ? 22.583 4.584   6.983   1.00 20.42 ? 55  SER A C   1 
ATOM   412  O  O   . SER A 1 55  ? 21.926 4.222   7.969   1.00 18.58 ? 55  SER A O   1 
ATOM   413  C  CB  . SER A 1 55  ? 23.124 6.825   7.919   1.00 20.44 ? 55  SER A CB  1 
ATOM   414  O  OG  . SER A 1 55  ? 23.983 7.948   7.806   1.00 23.20 ? 55  SER A OG  1 
ATOM   415  N  N   . HIS A 1 56  ? 22.363 4.104   5.759   1.00 15.91 ? 56  HIS A N   1 
ATOM   416  C  CA  . HIS A 1 56  ? 21.207 3.247   5.490   1.00 19.46 ? 56  HIS A CA  1 
ATOM   417  C  C   . HIS A 1 56  ? 21.514 2.425   4.236   1.00 17.93 ? 56  HIS A C   1 
ATOM   418  O  O   . HIS A 1 56  ? 21.181 2.835   3.126   1.00 20.14 ? 56  HIS A O   1 
ATOM   419  C  CB  . HIS A 1 56  ? 19.940 4.063   5.315   1.00 18.80 ? 56  HIS A CB  1 
ATOM   420  C  CG  . HIS A 1 56  ? 18.699 3.235   5.220   1.00 20.08 ? 56  HIS A CG  1 
ATOM   421  N  ND1 . HIS A 1 56  ? 17.457 3.708   5.583   1.00 20.92 ? 56  HIS A ND1 1 
ATOM   422  C  CD2 . HIS A 1 56  ? 18.510 1.963   4.799   1.00 22.75 ? 56  HIS A CD2 1 
ATOM   423  C  CE1 . HIS A 1 56  ? 16.556 2.761   5.397   1.00 20.42 ? 56  HIS A CE1 1 
ATOM   424  N  NE2 . HIS A 1 56  ? 17.171 1.692   4.923   1.00 22.15 ? 56  HIS A NE2 1 
ATOM   425  N  N   . VAL A 1 57  ? 22.144 1.266   4.429   1.00 18.41 ? 57  VAL A N   1 
ATOM   426  C  CA  . VAL A 1 57  ? 22.409 0.337   3.342   1.00 21.02 ? 57  VAL A CA  1 
ATOM   427  C  C   . VAL A 1 57  ? 21.910 -1.040  3.750   1.00 23.57 ? 57  VAL A C   1 
ATOM   428  O  O   . VAL A 1 57  ? 21.557 -1.284  4.905   1.00 20.43 ? 57  VAL A O   1 
ATOM   429  C  CB  . VAL A 1 57  ? 23.905 0.259   2.969   1.00 19.66 ? 57  VAL A CB  1 
ATOM   430  C  CG1 . VAL A 1 57  ? 24.472 1.644   2.654   1.00 21.20 ? 57  VAL A CG1 1 
ATOM   431  C  CG2 . VAL A 1 57  ? 24.695 -0.455  4.070   1.00 17.67 ? 57  VAL A CG2 1 
ATOM   432  N  N   . HIS A 1 58  ? 21.907 -1.954  2.777   1.00 18.38 ? 58  HIS A N   1 
ATOM   433  C  CA  . HIS A 1 58  ? 21.715 -3.379  3.044   1.00 21.02 ? 58  HIS A CA  1 
ATOM   434  C  C   . HIS A 1 58  ? 22.858 -4.135  2.387   1.00 24.45 ? 58  HIS A C   1 
ATOM   435  O  O   . HIS A 1 58  ? 22.839 -4.386  1.177   1.00 23.34 ? 58  HIS A O   1 
ATOM   436  C  CB  . HIS A 1 58  ? 20.371 -3.864  2.538   1.00 23.87 ? 58  HIS A CB  1 
ATOM   437  C  CG  . HIS A 1 58  ? 19.239 -3.222  3.250   1.00 21.77 ? 58  HIS A CG  1 
ATOM   438  N  ND1 . HIS A 1 58  ? 18.937 -3.508  4.562   1.00 24.78 ? 58  HIS A ND1 1 
ATOM   439  C  CD2 . HIS A 1 58  ? 18.392 -2.241  2.870   1.00 22.70 ? 58  HIS A CD2 1 
ATOM   440  C  CE1 . HIS A 1 58  ? 17.925 -2.757  4.951   1.00 21.31 ? 58  HIS A CE1 1 
ATOM   441  N  NE2 . HIS A 1 58  ? 17.573 -1.987  3.941   1.00 24.24 ? 58  HIS A NE2 1 
ATOM   442  N  N   . CYS A 1 59  ? 23.846 -4.501  3.189   1.00 24.61 ? 59  CYS A N   1 
ATOM   443  C  CA  . CYS A 1 59  ? 25.055 -5.113  2.665   1.00 26.47 ? 59  CYS A CA  1 
ATOM   444  C  C   . CYS A 1 59  ? 25.361 -6.440  3.351   1.00 24.72 ? 59  CYS A C   1 
ATOM   445  O  O   . CYS A 1 59  ? 26.529 -6.795  3.533   1.00 23.78 ? 59  CYS A O   1 
ATOM   446  C  CB  . CYS A 1 59  ? 26.228 -4.145  2.789   1.00 22.86 ? 59  CYS A CB  1 
ATOM   447  S  SG  . CYS A 1 59  ? 26.586 -3.673  4.504   1.00 23.05 ? 59  CYS A SG  1 
ATOM   448  N  N   . TYR A 1 60  ? 24.318 -7.166  3.761   1.00 20.25 ? 60  TYR A N   1 
ATOM   449  C  CA  . TYR A 1 60  ? 24.476 -8.512  4.291   1.00 27.41 ? 60  TYR A CA  1 
ATOM   450  C  C   . TYR A 1 60  ? 24.391 -9.488  3.123   1.00 24.77 ? 60  TYR A C   1 
ATOM   451  O  O   . TYR A 1 60  ? 23.294 -9.687  2.578   1.00 23.35 ? 60  TYR A O   1 
ATOM   452  C  CB  . TYR A 1 60  ? 23.402 -8.812  5.329   1.00 27.00 ? 60  TYR A CB  1 
ATOM   453  C  CG  . TYR A 1 60  ? 23.457 -10.206 5.892   1.00 28.55 ? 60  TYR A CG  1 
ATOM   454  C  CD1 . TYR A 1 60  ? 24.667 -10.806 6.206   1.00 29.14 ? 60  TYR A CD1 1 
ATOM   455  C  CD2 . TYR A 1 60  ? 22.290 -10.928 6.111   1.00 28.20 ? 60  TYR A CD2 1 
ATOM   456  C  CE1 . TYR A 1 60  ? 24.713 -12.088 6.720   1.00 28.66 ? 60  TYR A CE1 1 
ATOM   457  C  CE2 . TYR A 1 60  ? 22.323 -12.199 6.630   1.00 30.01 ? 60  TYR A CE2 1 
ATOM   458  C  CZ  . TYR A 1 60  ? 23.537 -12.777 6.929   1.00 31.35 ? 60  TYR A CZ  1 
ATOM   459  O  OH  . TYR A 1 60  ? 23.574 -14.046 7.441   1.00 33.21 ? 60  TYR A OH  1 
ATOM   460  N  N   . PRO A 1 61  ? 25.504 -10.081 2.685   1.00 26.74 ? 61  PRO A N   1 
ATOM   461  C  CA  . PRO A 1 61  ? 25.472 -10.874 1.443   1.00 27.20 ? 61  PRO A CA  1 
ATOM   462  C  C   . PRO A 1 61  ? 24.477 -12.015 1.456   1.00 26.55 ? 61  PRO A C   1 
ATOM   463  O  O   . PRO A 1 61  ? 24.032 -12.441 0.381   1.00 27.62 ? 61  PRO A O   1 
ATOM   464  C  CB  . PRO A 1 61  ? 26.912 -11.395 1.329   1.00 27.85 ? 61  PRO A CB  1 
ATOM   465  C  CG  . PRO A 1 61  ? 27.725 -10.384 2.058   1.00 30.60 ? 61  PRO A CG  1 
ATOM   466  C  CD  . PRO A 1 61  ? 26.868 -9.978  3.228   1.00 29.84 ? 61  PRO A CD  1 
ATOM   467  N  N   . ASN A 1 62  ? 24.126 -12.536 2.627   1.00 27.60 ? 62  ASN A N   1 
ATOM   468  C  CA  . ASN A 1 62  ? 23.270 -13.713 2.721   1.00 26.87 ? 62  ASN A CA  1 
ATOM   469  C  C   . ASN A 1 62  ? 21.799 -13.373 2.931   1.00 28.31 ? 62  ASN A C   1 
ATOM   470  O  O   . ASN A 1 62  ? 20.984 -14.287 3.066   1.00 31.42 ? 62  ASN A O   1 
ATOM   471  C  CB  . ASN A 1 62  ? 23.756 -14.637 3.842   1.00 29.50 ? 62  ASN A CB  1 
ATOM   472  C  CG  . ASN A 1 62  ? 25.065 -15.350 3.494   1.00 33.15 ? 62  ASN A CG  1 
ATOM   473  O  OD1 . ASN A 1 62  ? 25.240 -15.853 2.378   1.00 29.55 ? 62  ASN A OD1 1 
ATOM   474  N  ND2 . ASN A 1 62  ? 25.962 -15.448 4.471   1.00 35.34 ? 62  ASN A ND2 1 
ATOM   475  N  N   . SER A 1 63  ? 21.441 -12.095 2.946   1.00 29.25 ? 63  SER A N   1 
ATOM   476  C  CA  . SER A 1 63  ? 20.040 -11.702 3.065   1.00 29.40 ? 63  SER A CA  1 
ATOM   477  C  C   . SER A 1 63  ? 19.285 -12.113 1.805   1.00 30.15 ? 63  SER A C   1 
ATOM   478  O  O   . SER A 1 63  ? 19.747 -11.826 0.698   1.00 28.55 ? 63  SER A O   1 
ATOM   479  C  CB  . SER A 1 63  ? 19.941 -10.192 3.275   1.00 28.00 ? 63  SER A CB  1 
ATOM   480  O  OG  . SER A 1 63  ? 18.618 -9.806  3.584   1.00 30.50 ? 63  SER A OG  1 
ATOM   481  N  N   . PRO A 1 64  ? 18.126 -12.772 1.926   1.00 32.23 ? 64  PRO A N   1 
ATOM   482  C  CA  . PRO A 1 64  ? 17.494 -13.355 0.726   1.00 31.13 ? 64  PRO A CA  1 
ATOM   483  C  C   . PRO A 1 64  ? 17.091 -12.337 -0.336  1.00 32.79 ? 64  PRO A C   1 
ATOM   484  O  O   . PRO A 1 64  ? 17.248 -12.621 -1.530  1.00 33.11 ? 64  PRO A O   1 
ATOM   485  C  CB  . PRO A 1 64  ? 16.277 -14.101 1.300   1.00 33.11 ? 64  PRO A CB  1 
ATOM   486  C  CG  . PRO A 1 64  ? 16.030 -13.477 2.636   1.00 32.86 ? 64  PRO A CG  1 
ATOM   487  C  CD  . PRO A 1 64  ? 17.387 -13.095 3.156   1.00 34.88 ? 64  PRO A CD  1 
ATOM   488  N  N   . ILE A 1 65  ? 16.601 -11.156 0.046   1.00 30.13 ? 65  ILE A N   1 
ATOM   489  C  CA  . ILE A 1 65  ? 16.087 -10.170 -0.912  1.00 31.72 ? 65  ILE A CA  1 
ATOM   490  C  C   . ILE A 1 65  ? 16.990 -8.942  -0.993  1.00 30.76 ? 65  ILE A C   1 
ATOM   491  O  O   . ILE A 1 65  ? 17.485 -8.594  -2.069  1.00 26.32 ? 65  ILE A O   1 
ATOM   492  C  CB  . ILE A 1 65  ? 14.630 -9.770  -0.579  1.00 33.72 ? 65  ILE A CB  1 
ATOM   493  C  CG1 . ILE A 1 65  ? 13.700 -10.990 -0.608  1.00 31.44 ? 65  ILE A CG1 1 
ATOM   494  C  CG2 . ILE A 1 65  ? 14.134 -8.707  -1.561  1.00 31.18 ? 65  ILE A CG2 1 
ATOM   495  C  CD1 . ILE A 1 65  ? 13.834 -11.836 -1.851  1.00 31.40 ? 65  ILE A CD1 1 
ATOM   496  N  N   . TYR A 1 66  ? 17.206 -8.261  0.128   1.00 28.94 ? 66  TYR A N   1 
ATOM   497  C  CA  . TYR A 1 66  ? 17.983 -7.025  0.148   1.00 28.46 ? 66  TYR A CA  1 
ATOM   498  C  C   . TYR A 1 66  ? 19.401 -7.357  0.592   1.00 28.38 ? 66  TYR A C   1 
ATOM   499  O  O   . TYR A 1 66  ? 19.755 -7.238  1.764   1.00 27.60 ? 66  TYR A O   1 
ATOM   500  C  CB  . TYR A 1 66  ? 17.312 -5.979  1.031   1.00 30.58 ? 66  TYR A CB  1 
ATOM   501  C  CG  . TYR A 1 66  ? 15.830 -5.893  0.762   1.00 34.63 ? 66  TYR A CG  1 
ATOM   502  C  CD1 . TYR A 1 66  ? 15.355 -5.214  -0.354  1.00 35.56 ? 66  TYR A CD1 1 
ATOM   503  C  CD2 . TYR A 1 66  ? 14.905 -6.483  1.616   1.00 33.47 ? 66  TYR A CD2 1 
ATOM   504  C  CE1 . TYR A 1 66  ? 14.004 -5.138  -0.625  1.00 37.98 ? 66  TYR A CE1 1 
ATOM   505  C  CE2 . TYR A 1 66  ? 13.546 -6.401  1.356   1.00 37.44 ? 66  TYR A CE2 1 
ATOM   506  C  CZ  . TYR A 1 66  ? 13.104 -5.729  0.235   1.00 40.06 ? 66  TYR A CZ  1 
ATOM   507  O  OH  . TYR A 1 66  ? 11.757 -5.644  -0.036  1.00 47.89 ? 66  TYR A OH  1 
ATOM   508  N  N   . HIS A 1 67  ? 20.221 -7.768  -0.370  1.00 29.76 ? 67  HIS A N   1 
ATOM   509  C  CA  . HIS A 1 67  ? 21.606 -8.117  -0.115  1.00 28.40 ? 67  HIS A CA  1 
ATOM   510  C  C   . HIS A 1 67  ? 22.531 -7.300  -1.006  1.00 27.13 ? 67  HIS A C   1 
ATOM   511  O  O   . HIS A 1 67  ? 22.145 -6.822  -2.078  1.00 24.85 ? 67  HIS A O   1 
ATOM   512  C  CB  . HIS A 1 67  ? 21.850 -9.620  -0.325  1.00 28.55 ? 67  HIS A CB  1 
ATOM   513  C  CG  . HIS A 1 67  ? 21.537 -10.108 -1.707  1.00 29.78 ? 67  HIS A CG  1 
ATOM   514  N  ND1 . HIS A 1 67  ? 22.492 -10.202 -2.696  1.00 30.67 ? 67  HIS A ND1 1 
ATOM   515  C  CD2 . HIS A 1 67  ? 20.381 -10.548 -2.257  1.00 30.23 ? 67  HIS A CD2 1 
ATOM   516  C  CE1 . HIS A 1 67  ? 21.936 -10.674 -3.798  1.00 33.21 ? 67  HIS A CE1 1 
ATOM   517  N  NE2 . HIS A 1 67  ? 20.655 -10.891 -3.559  1.00 33.91 ? 67  HIS A NE2 1 
ATOM   518  N  N   . ASP A 1 68  ? 23.763 -7.141  -0.534  1.00 24.35 ? 68  ASP A N   1 
ATOM   519  C  CA  . ASP A 1 68  ? 24.837 -6.565  -1.332  1.00 22.24 ? 68  ASP A CA  1 
ATOM   520  C  C   . ASP A 1 68  ? 26.144 -6.840  -0.605  1.00 25.85 ? 68  ASP A C   1 
ATOM   521  O  O   . ASP A 1 68  ? 26.153 -7.253  0.558   1.00 26.81 ? 68  ASP A O   1 
ATOM   522  C  CB  . ASP A 1 68  ? 24.641 -5.064  -1.574  1.00 25.17 ? 68  ASP A CB  1 
ATOM   523  C  CG  . ASP A 1 68  ? 25.157 -4.627  -2.934  1.00 27.96 ? 68  ASP A CG  1 
ATOM   524  O  OD1 . ASP A 1 68  ? 26.030 -5.323  -3.494  1.00 25.68 ? 68  ASP A OD1 1 
ATOM   525  O  OD2 . ASP A 1 68  ? 24.687 -3.598  -3.452  1.00 26.06 ? 68  ASP A OD2 1 
ATOM   526  N  N   . GLU A 1 69  ? 27.255 -6.623  -1.315  1.00 25.97 ? 69  GLU A N   1 
ATOM   527  C  CA  . GLU A 1 69  ? 28.581 -6.730  -0.715  1.00 25.25 ? 69  GLU A CA  1 
ATOM   528  C  C   . GLU A 1 69  ? 28.981 -5.391  -0.105  1.00 25.74 ? 69  GLU A C   1 
ATOM   529  O  O   . GLU A 1 69  ? 28.816 -4.348  -0.756  1.00 22.15 ? 69  GLU A O   1 
ATOM   530  C  CB  . GLU A 1 69  ? 29.614 -7.140  -1.754  1.00 28.58 ? 69  GLU A CB  1 
ATOM   531  C  CG  . GLU A 1 69  ? 29.404 -8.520  -2.353  1.00 31.49 ? 69  GLU A CG  1 
ATOM   532  C  CD  . GLU A 1 69  ? 29.757 -9.641  -1.398  1.00 32.91 ? 69  GLU A CD  1 
ATOM   533  O  OE1 . GLU A 1 69  ? 30.574 -9.413  -0.476  1.00 35.72 ? 69  GLU A OE1 1 
ATOM   534  O  OE2 . GLU A 1 69  ? 29.233 -10.760 -1.585  1.00 38.03 ? 69  GLU A OE2 1 
ATOM   535  N  N   . PRO A 1 70  ? 29.503 -5.375  1.125   1.00 22.74 ? 70  PRO A N   1 
ATOM   536  C  CA  . PRO A 1 70  ? 29.914 -4.095  1.723   1.00 22.24 ? 70  PRO A CA  1 
ATOM   537  C  C   . PRO A 1 70  ? 30.797 -3.259  0.816   1.00 23.59 ? 70  PRO A C   1 
ATOM   538  O  O   . PRO A 1 70  ? 30.598 -2.043  0.717   1.00 20.53 ? 70  PRO A O   1 
ATOM   539  C  CB  . PRO A 1 70  ? 30.655 -4.527  2.995   1.00 24.29 ? 70  PRO A CB  1 
ATOM   540  C  CG  . PRO A 1 70  ? 30.006 -5.842  3.362   1.00 22.98 ? 70  PRO A CG  1 
ATOM   541  C  CD  . PRO A 1 70  ? 29.614 -6.503  2.072   1.00 24.75 ? 70  PRO A CD  1 
ATOM   542  N  N   . ASP A 1 71  ? 31.757 -3.874  0.128   1.00 23.44 ? 71  ASP A N   1 
ATOM   543  C  CA  . ASP A 1 71  ? 32.668 -3.057  -0.655  1.00 22.00 ? 71  ASP A CA  1 
ATOM   544  C  C   . ASP A 1 71  ? 32.041 -2.605  -1.968  1.00 27.86 ? 71  ASP A C   1 
ATOM   545  O  O   . ASP A 1 71  ? 32.483 -1.597  -2.536  1.00 23.88 ? 71  ASP A O   1 
ATOM   546  C  CB  . ASP A 1 71  ? 33.977 -3.812  -0.894  1.00 24.81 ? 71  ASP A CB  1 
ATOM   547  C  CG  . ASP A 1 71  ? 34.851 -3.865  0.359   1.00 25.62 ? 71  ASP A CG  1 
ATOM   548  O  OD1 . ASP A 1 71  ? 34.686 -2.993  1.243   1.00 23.02 ? 71  ASP A OD1 1 
ATOM   549  O  OD2 . ASP A 1 71  ? 35.676 -4.800  0.474   1.00 27.45 ? 71  ASP A OD2 1 
ATOM   550  N  N   . SER A 1 72  ? 31.002 -3.308  -2.443  1.00 24.94 ? 72  SER A N   1 
ATOM   551  C  CA  . SER A 1 72  ? 30.261 -2.813  -3.601  1.00 25.32 ? 72  SER A CA  1 
ATOM   552  C  C   . SER A 1 72  ? 29.467 -1.552  -3.271  1.00 21.77 ? 72  SER A C   1 
ATOM   553  O  O   . SER A 1 72  ? 29.297 -0.685  -4.136  1.00 23.25 ? 72  SER A O   1 
ATOM   554  C  CB  . SER A 1 72  ? 29.330 -3.896  -4.139  1.00 22.34 ? 72  SER A CB  1 
ATOM   555  O  OG  . SER A 1 72  ? 30.082 -4.989  -4.609  1.00 27.21 ? 72  SER A OG  1 
ATOM   556  N  N   . VAL A 1 73  ? 28.973 -1.419  -2.037  1.00 17.66 ? 73  VAL A N   1 
ATOM   557  C  CA  . VAL A 1 73  ? 28.268 -0.203  -1.648  1.00 18.82 ? 73  VAL A CA  1 
ATOM   558  C  C   . VAL A 1 73  ? 29.159 0.756   -0.882  1.00 22.59 ? 73  VAL A C   1 
ATOM   559  O  O   . VAL A 1 73  ? 28.736 1.876   -0.591  1.00 20.78 ? 73  VAL A O   1 
ATOM   560  C  CB  . VAL A 1 73  ? 26.998 -0.503  -0.827  1.00 22.87 ? 73  VAL A CB  1 
ATOM   561  C  CG1 . VAL A 1 73  ? 26.022 -1.327  -1.648  1.00 18.94 ? 73  VAL A CG1 1 
ATOM   562  C  CG2 . VAL A 1 73  ? 27.343 -1.181  0.509   1.00 20.52 ? 73  VAL A CG2 1 
ATOM   563  N  N   . GLY A 1 74  ? 30.382 0.351   -0.549  1.00 22.49 ? 74  GLY A N   1 
ATOM   564  C  CA  . GLY A 1 74  ? 31.309 1.223   0.143   1.00 21.51 ? 74  GLY A CA  1 
ATOM   565  C  C   . GLY A 1 74  ? 32.364 1.816   -0.770  1.00 19.85 ? 74  GLY A C   1 
ATOM   566  O  O   . GLY A 1 74  ? 32.039 2.595   -1.672  1.00 21.11 ? 74  GLY A O   1 
ATOM   567  N  N   . ILE A 1 75  ? 33.629 1.442   -0.535  1.00 20.65 ? 75  ILE A N   1 
ATOM   568  C  CA  . ILE A 1 75  ? 34.788 2.028   -1.217  1.00 20.40 ? 75  ILE A CA  1 
ATOM   569  C  C   . ILE A 1 75  ? 34.638 2.086   -2.724  1.00 22.40 ? 75  ILE A C   1 
ATOM   570  O  O   . ILE A 1 75  ? 35.124 3.029   -3.357  1.00 22.55 ? 75  ILE A O   1 
ATOM   571  C  CB  . ILE A 1 75  ? 36.073 1.274   -0.810  1.00 22.55 ? 75  ILE A CB  1 
ATOM   572  C  CG1 . ILE A 1 75  ? 36.675 1.888   0.448   1.00 23.65 ? 75  ILE A CG1 1 
ATOM   573  C  CG2 . ILE A 1 75  ? 37.087 1.203   -1.933  1.00 28.92 ? 75  ILE A CG2 1 
ATOM   574  C  CD1 . ILE A 1 75  ? 35.972 1.562   1.675   1.00 25.98 ? 75  ILE A CD1 1 
ATOM   575  N  N   . ALA A 1 76  ? 33.983 1.093   -3.333  1.00 21.12 ? 76  ALA A N   1 
ATOM   576  C  CA  . ALA A 1 76  ? 33.839 1.134   -4.785  1.00 27.29 ? 76  ALA A CA  1 
ATOM   577  C  C   . ALA A 1 76  ? 33.068 2.361   -5.252  1.00 22.26 ? 76  ALA A C   1 
ATOM   578  O  O   . ALA A 1 76  ? 33.248 2.783   -6.398  1.00 22.02 ? 76  ALA A O   1 
ATOM   579  C  CB  . ALA A 1 76  ? 33.164 -0.137  -5.305  1.00 21.85 ? 76  ALA A CB  1 
ATOM   580  N  N   . THR A 1 77  ? 32.230 2.949   -4.392  1.00 20.89 ? 77  THR A N   1 
ATOM   581  C  CA  . THR A 1 77  ? 31.509 4.177   -4.713  1.00 22.31 ? 77  THR A CA  1 
ATOM   582  C  C   . THR A 1 77  ? 32.038 5.387   -3.952  1.00 20.63 ? 77  THR A C   1 
ATOM   583  O  O   . THR A 1 77  ? 31.344 6.405   -3.869  1.00 21.65 ? 77  THR A O   1 
ATOM   584  C  CB  . THR A 1 77  ? 30.018 4.030   -4.404  1.00 22.08 ? 77  THR A CB  1 
ATOM   585  O  OG1 . THR A 1 77  ? 29.833 4.030   -2.980  1.00 20.76 ? 77  THR A OG1 1 
ATOM   586  C  CG2 . THR A 1 77  ? 29.471 2.732   -4.976  1.00 20.56 ? 77  THR A CG2 1 
ATOM   587  N  N   . GLY A 1 78  ? 33.222 5.291   -3.356  1.00 20.59 ? 78  GLY A N   1 
ATOM   588  C  CA  . GLY A 1 78  ? 33.769 6.396   -2.594  1.00 20.59 ? 78  GLY A CA  1 
ATOM   589  C  C   . GLY A 1 78  ? 33.318 6.480   -1.152  1.00 20.11 ? 78  GLY A C   1 
ATOM   590  O  O   . GLY A 1 78  ? 33.742 7.402   -0.441  1.00 22.01 ? 78  GLY A O   1 
ATOM   591  N  N   . VAL A 1 79  ? 32.492 5.548   -0.689  1.00 19.00 ? 79  VAL A N   1 
ATOM   592  C  CA  . VAL A 1 79  ? 31.916 5.600   0.652   1.00 16.23 ? 79  VAL A CA  1 
ATOM   593  C  C   . VAL A 1 79  ? 32.801 4.789   1.593   1.00 18.35 ? 79  VAL A C   1 
ATOM   594  O  O   . VAL A 1 79  ? 33.072 3.611   1.341   1.00 19.60 ? 79  VAL A O   1 
ATOM   595  C  CB  . VAL A 1 79  ? 30.475 5.065   0.647   1.00 19.52 ? 79  VAL A CB  1 
ATOM   596  C  CG1 . VAL A 1 79  ? 29.891 5.081   2.048   1.00 16.79 ? 79  VAL A CG1 1 
ATOM   597  C  CG2 . VAL A 1 79  ? 29.607 5.871   -0.323  1.00 18.03 ? 79  VAL A CG2 1 
ATOM   598  N  N   . THR A 1 80  ? 33.251 5.409   2.688   1.00 17.61 ? 80  THR A N   1 
ATOM   599  C  CA  . THR A 1 80  ? 34.221 4.750   3.556   1.00 18.48 ? 80  THR A CA  1 
ATOM   600  C  C   . THR A 1 80  ? 33.588 4.044   4.745   1.00 19.93 ? 80  THR A C   1 
ATOM   601  O  O   . THR A 1 80  ? 34.200 3.111   5.289   1.00 21.77 ? 80  THR A O   1 
ATOM   602  C  CB  . THR A 1 80  ? 35.259 5.753   4.054   1.00 22.31 ? 80  THR A CB  1 
ATOM   603  O  OG1 . THR A 1 80  ? 34.580 6.898   4.582   1.00 17.26 ? 80  THR A OG1 1 
ATOM   604  C  CG2 . THR A 1 80  ? 36.174 6.178   2.903   1.00 19.19 ? 80  THR A CG2 1 
ATOM   605  N  N   . THR A 1 81  ? 32.383 4.441   5.147   1.00 16.70 ? 81  THR A N   1 
ATOM   606  C  CA  . THR A 1 81  ? 31.638 3.736   6.184   1.00 18.16 ? 81  THR A CA  1 
ATOM   607  C  C   . THR A 1 81  ? 30.213 3.502   5.706   1.00 18.98 ? 81  THR A C   1 
ATOM   608  O  O   . THR A 1 81  ? 29.570 4.422   5.197   1.00 17.00 ? 81  THR A O   1 
ATOM   609  C  CB  . THR A 1 81  ? 31.628 4.520   7.499   1.00 18.98 ? 81  THR A CB  1 
ATOM   610  O  OG1 . THR A 1 81  ? 32.961 4.598   8.026   1.00 18.74 ? 81  THR A OG1 1 
ATOM   611  C  CG2 . THR A 1 81  ? 30.719 3.851   8.518   1.00 17.59 ? 81  THR A CG2 1 
ATOM   612  N  N   . VAL A 1 82  ? 29.716 2.277   5.877   1.00 19.76 ? 82  VAL A N   1 
ATOM   613  C  CA  . VAL A 1 82  ? 28.321 1.971   5.583   1.00 17.57 ? 82  VAL A CA  1 
ATOM   614  C  C   . VAL A 1 82  ? 27.677 1.431   6.852   1.00 20.26 ? 82  VAL A C   1 
ATOM   615  O  O   . VAL A 1 82  ? 28.331 0.769   7.665   1.00 22.08 ? 82  VAL A O   1 
ATOM   616  C  CB  . VAL A 1 82  ? 28.179 0.958   4.426   1.00 19.79 ? 82  VAL A CB  1 
ATOM   617  C  CG1 . VAL A 1 82  ? 28.663 1.562   3.112   1.00 20.09 ? 82  VAL A CG1 1 
ATOM   618  C  CG2 . VAL A 1 82  ? 28.920 -0.327  4.739   1.00 19.84 ? 82  VAL A CG2 1 
ATOM   619  N  N   . ILE A 1 83  ? 26.384 1.701   7.015   1.00 16.58 ? 83  ILE A N   1 
ATOM   620  C  CA  . ILE A 1 83  ? 25.639 1.274   8.198   1.00 18.66 ? 83  ILE A CA  1 
ATOM   621  C  C   . ILE A 1 83  ? 24.458 0.453   7.705   1.00 21.45 ? 83  ILE A C   1 
ATOM   622  O  O   . ILE A 1 83  ? 23.534 0.995   7.081   1.00 21.18 ? 83  ILE A O   1 
ATOM   623  C  CB  . ILE A 1 83  ? 25.173 2.452   9.066   1.00 19.13 ? 83  ILE A CB  1 
ATOM   624  C  CG1 . ILE A 1 83  ? 26.361 3.124   9.761   1.00 21.07 ? 83  ILE A CG1 1 
ATOM   625  C  CG2 . ILE A 1 83  ? 24.235 1.983   10.139  1.00 22.48 ? 83  ILE A CG2 1 
ATOM   626  C  CD1 . ILE A 1 83  ? 27.011 4.178   8.951   1.00 22.64 ? 83  ILE A CD1 1 
ATOM   627  N  N   . ASP A 1 84  ? 24.505 -0.855  7.959   1.00 18.55 ? 84  ASP A N   1 
ATOM   628  C  CA  . ASP A 1 84  ? 23.439 -1.754  7.535   1.00 22.03 ? 84  ASP A CA  1 
ATOM   629  C  C   . ASP A 1 84  ? 22.201 -1.525  8.388   1.00 22.07 ? 84  ASP A C   1 
ATOM   630  O  O   . ASP A 1 84  ? 22.260 -1.577  9.623   1.00 20.24 ? 84  ASP A O   1 
ATOM   631  C  CB  . ASP A 1 84  ? 23.898 -3.212  7.627   1.00 23.26 ? 84  ASP A CB  1 
ATOM   632  C  CG  . ASP A 1 84  ? 22.809 -4.200  7.220   1.00 23.33 ? 84  ASP A CG  1 
ATOM   633  O  OD1 . ASP A 1 84  ? 22.646 -4.464  6.007   1.00 23.56 ? 84  ASP A OD1 1 
ATOM   634  O  OD2 . ASP A 1 84  ? 22.110 -4.711  8.120   1.00 21.13 ? 84  ASP A OD2 1 
ATOM   635  N  N   . ALA A 1 85  ? 21.075 -1.277  7.722   1.00 22.25 ? 85  ALA A N   1 
ATOM   636  C  CA  . ALA A 1 85  ? 19.872 -0.782  8.386   1.00 22.02 ? 85  ALA A CA  1 
ATOM   637  C  C   . ALA A 1 85  ? 18.961 -1.949  8.762   1.00 22.59 ? 85  ALA A C   1 
ATOM   638  O  O   . ALA A 1 85  ? 17.842 -2.111  8.266   1.00 22.00 ? 85  ALA A O   1 
ATOM   639  C  CB  . ALA A 1 85  ? 19.157 0.226   7.498   1.00 19.64 ? 85  ALA A CB  1 
ATOM   640  N  N   . GLY A 1 86  ? 19.472 -2.775  9.667   1.00 19.63 ? 86  GLY A N   1 
ATOM   641  C  CA  . GLY A 1 86  ? 18.669 -3.861  10.193  1.00 24.23 ? 86  GLY A CA  1 
ATOM   642  C  C   . GLY A 1 86  ? 18.381 -4.997  9.239   1.00 24.81 ? 86  GLY A C   1 
ATOM   643  O  O   . GLY A 1 86  ? 17.291 -5.573  9.300   1.00 24.25 ? 86  GLY A O   1 
ATOM   644  N  N   . SER A 1 87  ? 19.335 -5.348  8.364   1.00 24.79 ? 87  SER A N   1 
ATOM   645  C  CA  . SER A 1 87  ? 19.186 -6.555  7.550   1.00 24.86 ? 87  SER A CA  1 
ATOM   646  C  C   . SER A 1 87  ? 19.196 -7.806  8.420   1.00 30.11 ? 87  SER A C   1 
ATOM   647  O  O   . SER A 1 87  ? 18.527 -8.798  8.097   1.00 25.53 ? 87  SER A O   1 
ATOM   648  C  CB  . SER A 1 87  ? 20.308 -6.644  6.512   1.00 25.69 ? 87  SER A CB  1 
ATOM   649  O  OG  . SER A 1 87  ? 20.352 -5.490  5.687   1.00 23.04 ? 87  SER A OG  1 
ATOM   650  N  N   . THR A 1 88  ? 19.946 -7.777  9.524   1.00 25.10 ? 88  THR A N   1 
ATOM   651  C  CA  . THR A 1 88  ? 20.025 -8.894  10.452  1.00 28.38 ? 88  THR A CA  1 
ATOM   652  C  C   . THR A 1 88  ? 19.481 -8.489  11.811  1.00 28.21 ? 88  THR A C   1 
ATOM   653  O  O   . THR A 1 88  ? 19.668 -7.353  12.255  1.00 27.63 ? 88  THR A O   1 
ATOM   654  C  CB  . THR A 1 88  ? 21.464 -9.394  10.642  1.00 28.36 ? 88  THR A CB  1 
ATOM   655  O  OG1 . THR A 1 88  ? 22.292 -8.316  11.098  1.00 27.09 ? 88  THR A OG1 1 
ATOM   656  C  CG2 . THR A 1 88  ? 22.025 -9.944  9.352   1.00 27.70 ? 88  THR A CG2 1 
ATOM   657  N  N   . GLY A 1 89  ? 18.817 -9.434  12.466  1.00 30.81 ? 89  GLY A N   1 
ATOM   658  C  CA  . GLY A 1 89  ? 18.600 -9.393  13.889  1.00 28.70 ? 89  GLY A CA  1 
ATOM   659  C  C   . GLY A 1 89  ? 19.635 -10.236 14.602  1.00 32.24 ? 89  GLY A C   1 
ATOM   660  O  O   . GLY A 1 89  ? 20.706 -10.538 14.064  1.00 32.58 ? 89  GLY A O   1 
ATOM   661  N  N   . ALA A 1 90  ? 19.297 -10.647 15.826  1.00 32.28 ? 90  ALA A N   1 
ATOM   662  C  CA  . ALA A 1 90  ? 20.216 -11.463 16.612  1.00 31.82 ? 90  ALA A CA  1 
ATOM   663  C  C   . ALA A 1 90  ? 20.507 -12.805 15.948  1.00 32.45 ? 90  ALA A C   1 
ATOM   664  O  O   . ALA A 1 90  ? 21.582 -13.376 16.162  1.00 32.02 ? 90  ALA A O   1 
ATOM   665  C  CB  . ALA A 1 90  ? 19.643 -11.673 18.011  1.00 32.46 ? 90  ALA A CB  1 
ATOM   666  N  N   . ASP A 1 91  ? 19.583 -13.302 15.127  1.00 34.59 ? 91  ASP A N   1 
ATOM   667  C  CA  . ASP A 1 91  ? 19.742 -14.615 14.515  1.00 36.57 ? 91  ASP A CA  1 
ATOM   668  C  C   . ASP A 1 91  ? 20.938 -14.662 13.567  1.00 34.54 ? 91  ASP A C   1 
ATOM   669  O  O   . ASP A 1 91  ? 21.677 -15.653 13.543  1.00 33.74 ? 91  ASP A O   1 
ATOM   670  C  CB  . ASP A 1 91  ? 18.454 -14.980 13.779  1.00 34.84 ? 91  ASP A CB  1 
ATOM   671  C  CG  . ASP A 1 91  ? 17.442 -15.648 14.683  1.00 38.99 ? 91  ASP A CG  1 
ATOM   672  O  OD1 . ASP A 1 91  ? 17.508 -15.418 15.909  1.00 37.32 ? 91  ASP A OD1 1 
ATOM   673  O  OD2 . ASP A 1 91  ? 16.568 -16.381 14.171  1.00 44.85 ? 91  ASP A OD2 1 
ATOM   674  N  N   . ASP A 1 92  ? 21.147 -13.614 12.770  1.00 30.60 ? 92  ASP A N   1 
ATOM   675  C  CA  . ASP A 1 92  ? 22.180 -13.647 11.741  1.00 32.61 ? 92  ASP A CA  1 
ATOM   676  C  C   . ASP A 1 92  ? 23.295 -12.630 11.960  1.00 35.26 ? 92  ASP A C   1 
ATOM   677  O  O   . ASP A 1 92  ? 24.158 -12.483 11.082  1.00 33.82 ? 92  ASP A O   1 
ATOM   678  C  CB  . ASP A 1 92  ? 21.561 -13.431 10.352  1.00 34.72 ? 92  ASP A CB  1 
ATOM   679  C  CG  . ASP A 1 92  ? 20.528 -14.492 9.992   1.00 39.94 ? 92  ASP A CG  1 
ATOM   680  O  OD1 . ASP A 1 92  ? 19.357 -14.366 10.414  1.00 42.98 ? 92  ASP A OD1 1 
ATOM   681  O  OD2 . ASP A 1 92  ? 20.889 -15.466 9.296   1.00 45.62 ? 92  ASP A OD2 1 
ATOM   682  N  N   . VAL A 1 93  ? 23.319 -11.927 13.096  1.00 30.53 ? 93  VAL A N   1 
ATOM   683  C  CA  . VAL A 1 93  ? 24.276 -10.829 13.222  1.00 30.31 ? 93  VAL A CA  1 
ATOM   684  C  C   . VAL A 1 93  ? 25.703 -11.353 13.363  1.00 30.47 ? 93  VAL A C   1 
ATOM   685  O  O   . VAL A 1 93  ? 26.653 -10.697 12.919  1.00 30.82 ? 93  VAL A O   1 
ATOM   686  C  CB  . VAL A 1 93  ? 23.888 -9.885  14.381  1.00 29.48 ? 93  VAL A CB  1 
ATOM   687  C  CG1 . VAL A 1 93  ? 24.158 -10.525 15.744  1.00 28.93 ? 93  VAL A CG1 1 
ATOM   688  C  CG2 . VAL A 1 93  ? 24.625 -8.563  14.255  1.00 29.85 ? 93  VAL A CG2 1 
ATOM   689  N  N   . ASP A 1 94  ? 25.886 -12.533 13.964  1.00 29.03 ? 94  ASP A N   1 
ATOM   690  C  CA  . ASP A 1 94  ? 27.232 -13.086 14.097  1.00 32.84 ? 94  ASP A CA  1 
ATOM   691  C  C   . ASP A 1 94  ? 27.844 -13.376 12.730  1.00 32.04 ? 94  ASP A C   1 
ATOM   692  O  O   . ASP A 1 94  ? 28.993 -13.003 12.460  1.00 32.96 ? 94  ASP A O   1 
ATOM   693  C  CB  . ASP A 1 94  ? 27.209 -14.359 14.944  1.00 33.70 ? 94  ASP A CB  1 
ATOM   694  C  CG  . ASP A 1 94  ? 26.644 -14.133 16.335  1.00 36.46 ? 94  ASP A CG  1 
ATOM   695  O  OD1 . ASP A 1 94  ? 26.504 -12.960 16.741  1.00 37.32 ? 94  ASP A OD1 1 
ATOM   696  O  OD2 . ASP A 1 94  ? 26.351 -15.137 17.024  1.00 37.43 ? 94  ASP A OD2 1 
ATOM   697  N  N   . ASP A 1 95  ? 27.091 -14.056 11.862  1.00 33.37 ? 95  ASP A N   1 
ATOM   698  C  CA  . ASP A 1 95  ? 27.591 -14.379 10.528  1.00 35.66 ? 95  ASP A CA  1 
ATOM   699  C  C   . ASP A 1 95  ? 27.872 -13.108 9.736   1.00 32.34 ? 95  ASP A C   1 
ATOM   700  O  O   . ASP A 1 95  ? 28.892 -13.005 9.037   1.00 33.85 ? 95  ASP A O   1 
ATOM   701  C  CB  . ASP A 1 95  ? 26.578 -15.284 9.810   1.00 36.40 ? 95  ASP A CB  1 
ATOM   702  C  CG  . ASP A 1 95  ? 26.958 -15.575 8.364   1.00 40.35 ? 95  ASP A CG  1 
ATOM   703  O  OD1 . ASP A 1 95  ? 26.073 -15.458 7.483   1.00 35.49 ? 95  ASP A OD1 1 
ATOM   704  O  OD2 . ASP A 1 95  ? 28.133 -15.929 8.112   1.00 39.65 ? 95  ASP A OD2 1 
ATOM   705  N  N   . PHE A 1 96  ? 26.985 -12.120 9.853   1.00 32.23 ? 96  PHE A N   1 
ATOM   706  C  CA  . PHE A 1 96  ? 27.221 -10.816 9.249   1.00 29.31 ? 96  PHE A CA  1 
ATOM   707  C  C   . PHE A 1 96  ? 28.562 -10.236 9.697   1.00 31.67 ? 96  PHE A C   1 
ATOM   708  O  O   . PHE A 1 96  ? 29.388 -9.836  8.868   1.00 32.11 ? 96  PHE A O   1 
ATOM   709  C  CB  . PHE A 1 96  ? 26.066 -9.884  9.622   1.00 28.60 ? 96  PHE A CB  1 
ATOM   710  C  CG  . PHE A 1 96  ? 26.022 -8.615  8.838   1.00 28.40 ? 96  PHE A CG  1 
ATOM   711  C  CD1 . PHE A 1 96  ? 26.655 -8.510  7.606   1.00 28.28 ? 96  PHE A CD1 1 
ATOM   712  C  CD2 . PHE A 1 96  ? 25.345 -7.511  9.340   1.00 24.56 ? 96  PHE A CD2 1 
ATOM   713  C  CE1 . PHE A 1 96  ? 26.604 -7.330  6.889   1.00 26.46 ? 96  PHE A CE1 1 
ATOM   714  C  CE2 . PHE A 1 96  ? 25.292 -6.334  8.635   1.00 26.50 ? 96  PHE A CE2 1 
ATOM   715  C  CZ  . PHE A 1 96  ? 25.924 -6.240  7.402   1.00 27.32 ? 96  PHE A CZ  1 
ATOM   716  N  N   . TYR A 1 97  ? 28.784 -10.175 11.014  1.00 30.89 ? 97  TYR A N   1 
ATOM   717  C  CA  . TYR A 1 97  ? 30.031 -9.646  11.563  1.00 32.54 ? 97  TYR A CA  1 
ATOM   718  C  C   . TYR A 1 97  ? 31.245 -10.384 10.999  1.00 33.57 ? 97  TYR A C   1 
ATOM   719  O  O   . TYR A 1 97  ? 32.235 -9.762  10.574  1.00 34.59 ? 97  TYR A O   1 
ATOM   720  C  CB  . TYR A 1 97  ? 29.980 -9.753  13.095  1.00 31.16 ? 97  TYR A CB  1 
ATOM   721  C  CG  . TYR A 1 97  ? 31.286 -9.468  13.812  1.00 33.48 ? 97  TYR A CG  1 
ATOM   722  C  CD1 . TYR A 1 97  ? 31.691 -8.164  14.084  1.00 32.92 ? 97  TYR A CD1 1 
ATOM   723  C  CD2 . TYR A 1 97  ? 32.107 -10.504 14.227  1.00 36.12 ? 97  TYR A CD2 1 
ATOM   724  C  CE1 . TYR A 1 97  ? 32.881 -7.909  14.750  1.00 33.38 ? 97  TYR A CE1 1 
ATOM   725  C  CE2 . TYR A 1 97  ? 33.299 -10.255 14.889  1.00 36.69 ? 97  TYR A CE2 1 
ATOM   726  C  CZ  . TYR A 1 97  ? 33.682 -8.964  15.144  1.00 33.84 ? 97  TYR A CZ  1 
ATOM   727  O  OH  . TYR A 1 97  ? 34.870 -8.734  15.802  1.00 38.01 ? 97  TYR A OH  1 
ATOM   728  N  N   . GLN A 1 98  ? 31.183 -11.719 10.993  1.00 31.80 ? 98  GLN A N   1 
ATOM   729  C  CA  . GLN A 1 98  ? 32.319 -12.518 10.538  1.00 35.79 ? 98  GLN A CA  1 
ATOM   730  C  C   . GLN A 1 98  ? 32.617 -12.277 9.065   1.00 32.69 ? 98  GLN A C   1 
ATOM   731  O  O   . GLN A 1 98  ? 33.785 -12.185 8.669   1.00 32.96 ? 98  GLN A O   1 
ATOM   732  C  CB  . GLN A 1 98  ? 32.061 -14.003 10.795  1.00 36.25 ? 98  GLN A CB  1 
ATOM   733  C  CG  . GLN A 1 98  ? 31.797 -14.351 12.255  1.00 40.78 ? 98  GLN A CG  1 
ATOM   734  C  CD  . GLN A 1 98  ? 33.002 -14.119 13.152  1.00 45.63 ? 98  GLN A CD  1 
ATOM   735  O  OE1 . GLN A 1 98  ? 34.142 -14.106 12.688  1.00 49.22 ? 98  GLN A OE1 1 
ATOM   736  N  NE2 . GLN A 1 98  ? 32.754 -13.944 14.446  1.00 45.44 ? 98  GLN A NE2 1 
ATOM   737  N  N   . LEU A 1 99  ? 31.580 -12.167 8.236   1.00 32.70 ? 99  LEU A N   1 
ATOM   738  C  CA  . LEU A 1 99  ? 31.814 -11.893 6.821   1.00 33.36 ? 99  LEU A CA  1 
ATOM   739  C  C   . LEU A 1 99  ? 32.377 -10.488 6.611   1.00 36.67 ? 99  LEU A C   1 
ATOM   740  O  O   . LEU A 1 99  ? 33.236 -10.280 5.744   1.00 36.39 ? 99  LEU A O   1 
ATOM   741  C  CB  . LEU A 1 99  ? 30.521 -12.087 6.028   1.00 31.52 ? 99  LEU A CB  1 
ATOM   742  N  N   . THR A 1 100 ? 31.917 -9.509  7.391   1.00 32.07 ? 100 THR A N   1 
ATOM   743  C  CA  . THR A 1 100 ? 32.404 -8.147  7.201   1.00 31.62 ? 100 THR A CA  1 
ATOM   744  C  C   . THR A 1 100 ? 33.812 -7.930  7.733   1.00 32.87 ? 100 THR A C   1 
ATOM   745  O  O   . THR A 1 100 ? 34.413 -6.899  7.414   1.00 28.94 ? 100 THR A O   1 
ATOM   746  C  CB  . THR A 1 100 ? 31.470 -7.133  7.865   1.00 29.84 ? 100 THR A CB  1 
ATOM   747  O  OG1 . THR A 1 100 ? 31.446 -7.367  9.282   1.00 34.08 ? 100 THR A OG1 1 
ATOM   748  C  CG2 . THR A 1 100 ? 30.074 -7.249  7.296   1.00 30.26 ? 100 THR A CG2 1 
ATOM   749  N  N   . ARG A 1 101 ? 34.340 -8.844  8.557   1.00 34.48 ? 101 ARG A N   1 
ATOM   750  C  CA  . ARG A 1 101 ? 35.714 -8.658  9.031   1.00 32.88 ? 101 ARG A CA  1 
ATOM   751  C  C   . ARG A 1 101 ? 36.701 -8.394  7.894   1.00 35.53 ? 101 ARG A C   1 
ATOM   752  O  O   . ARG A 1 101 ? 37.676 -7.656  8.082   1.00 36.78 ? 101 ARG A O   1 
ATOM   753  C  CB  . ARG A 1 101 ? 36.181 -9.859  9.860   1.00 37.25 ? 101 ARG A CB  1 
ATOM   754  C  CG  . ARG A 1 101 ? 35.274 -10.181 11.030  1.00 36.25 ? 101 ARG A CG  1 
ATOM   755  C  CD  . ARG A 1 101 ? 35.271 -9.027  12.031  1.00 35.59 ? 101 ARG A CD  1 
ATOM   756  N  NE  . ARG A 1 101 ? 34.213 -8.069  11.727  1.00 34.31 ? 101 ARG A NE  1 
ATOM   757  C  CZ  . ARG A 1 101 ? 34.286 -6.764  11.948  1.00 35.93 ? 101 ARG A CZ  1 
ATOM   758  N  NH1 . ARG A 1 101 ? 35.336 -6.221  12.552  1.00 33.51 ? 101 ARG A NH1 1 
ATOM   759  N  NH2 . ARG A 1 101 ? 33.275 -5.984  11.566  1.00 32.15 ? 101 ARG A NH2 1 
ATOM   760  N  N   . LYS A 1 102 ? 36.457 -8.948  6.704   1.00 30.55 ? 102 LYS A N   1 
ATOM   761  C  CA  . LYS A 1 102 ? 37.394 -8.766  5.599   1.00 32.46 ? 102 LYS A CA  1 
ATOM   762  C  C   . LYS A 1 102 ? 37.189 -7.473  4.813   1.00 32.23 ? 102 LYS A C   1 
ATOM   763  O  O   . LYS A 1 102 ? 38.112 -7.050  4.105   1.00 31.73 ? 102 LYS A O   1 
ATOM   764  C  CB  . LYS A 1 102 ? 37.313 -9.956  4.635   1.00 31.96 ? 102 LYS A CB  1 
ATOM   765  N  N   . ALA A 1 103 ? 36.021 -6.836  4.917   1.00 27.95 ? 103 ALA A N   1 
ATOM   766  C  CA  . ALA A 1 103 ? 35.708 -5.689  4.073   1.00 25.76 ? 103 ALA A CA  1 
ATOM   767  C  C   . ALA A 1 103 ? 36.709 -4.556  4.263   1.00 26.79 ? 103 ALA A C   1 
ATOM   768  O  O   . ALA A 1 103 ? 37.163 -4.277  5.377   1.00 26.34 ? 103 ALA A O   1 
ATOM   769  C  CB  . ALA A 1 103 ? 34.296 -5.175  4.370   1.00 27.68 ? 103 ALA A CB  1 
ATOM   770  N  N   . VAL A 1 104 ? 37.061 -3.901  3.155   1.00 25.13 ? 104 VAL A N   1 
ATOM   771  C  CA  . VAL A 1 104 ? 37.851 -2.681  3.255   1.00 25.87 ? 104 VAL A CA  1 
ATOM   772  C  C   . VAL A 1 104 ? 37.002 -1.563  3.847   1.00 25.35 ? 104 VAL A C   1 
ATOM   773  O  O   . VAL A 1 104 ? 37.460 -0.800  4.708   1.00 25.08 ? 104 VAL A O   1 
ATOM   774  C  CB  . VAL A 1 104 ? 38.424 -2.298  1.877   1.00 27.09 ? 104 VAL A CB  1 
ATOM   775  C  CG1 . VAL A 1 104 ? 39.130 -0.953  1.951   1.00 27.41 ? 104 VAL A CG1 1 
ATOM   776  C  CG2 . VAL A 1 104 ? 39.365 -3.377  1.367   1.00 25.19 ? 104 VAL A CG2 1 
ATOM   777  N  N   . THR A 1 105 ? 35.746 -1.469  3.412   1.00 25.22 ? 105 THR A N   1 
ATOM   778  C  CA  . THR A 1 105 ? 34.807 -0.515  3.987   1.00 23.84 ? 105 THR A CA  1 
ATOM   779  C  C   . THR A 1 105 ? 34.617 -0.771  5.474   1.00 23.31 ? 105 THR A C   1 
ATOM   780  O  O   . THR A 1 105 ? 34.556 -1.922  5.920   1.00 26.97 ? 105 THR A O   1 
ATOM   781  C  CB  . THR A 1 105 ? 33.456 -0.609  3.273   1.00 23.66 ? 105 THR A CB  1 
ATOM   782  O  OG1 . THR A 1 105 ? 33.653 -0.483  1.861   1.00 23.58 ? 105 THR A OG1 1 
ATOM   783  C  CG2 . THR A 1 105 ? 32.528 0.502   3.734   1.00 22.06 ? 105 THR A CG2 1 
ATOM   784  N  N   . GLU A 1 106 ? 34.543 0.311   6.246   1.00 22.38 ? 106 GLU A N   1 
ATOM   785  C  CA  . GLU A 1 106 ? 34.115 0.215   7.636   1.00 23.51 ? 106 GLU A CA  1 
ATOM   786  C  C   . GLU A 1 106 ? 32.622 -0.085  7.675   1.00 21.97 ? 106 GLU A C   1 
ATOM   787  O  O   . GLU A 1 106 ? 31.811 0.701   7.174   1.00 22.27 ? 106 GLU A O   1 
ATOM   788  C  CB  . GLU A 1 106 ? 34.405 1.513   8.385   1.00 25.70 ? 106 GLU A CB  1 
ATOM   789  C  CG  . GLU A 1 106 ? 34.192 1.366   9.886   1.00 26.35 ? 106 GLU A CG  1 
ATOM   790  C  CD  . GLU A 1 106 ? 35.481 1.057   10.613  1.00 28.95 ? 106 GLU A CD  1 
ATOM   791  O  OE1 . GLU A 1 106 ? 36.422 1.881   10.531  1.00 31.62 ? 106 GLU A OE1 1 
ATOM   792  O  OE2 . GLU A 1 106 ? 35.574 -0.031  11.217  1.00 30.95 ? 106 GLU A OE2 1 
ATOM   793  N  N   . VAL A 1 107 ? 32.253 -1.203  8.284   1.00 20.72 ? 107 VAL A N   1 
ATOM   794  C  CA  . VAL A 1 107 ? 30.875 -1.677  8.290   1.00 25.70 ? 107 VAL A CA  1 
ATOM   795  C  C   . VAL A 1 107 ? 30.377 -1.682  9.725   1.00 23.65 ? 107 VAL A C   1 
ATOM   796  O  O   . VAL A 1 107 ? 30.992 -2.304  10.600  1.00 22.98 ? 107 VAL A O   1 
ATOM   797  C  CB  . VAL A 1 107 ? 30.750 -3.081  7.678   1.00 20.21 ? 107 VAL A CB  1 
ATOM   798  C  CG1 . VAL A 1 107 ? 29.280 -3.503  7.629   1.00 21.52 ? 107 VAL A CG1 1 
ATOM   799  C  CG2 . VAL A 1 107 ? 31.377 -3.108  6.302   1.00 23.85 ? 107 VAL A CG2 1 
ATOM   800  N  N   . TYR A 1 108 ? 29.271 -0.991  9.963   1.00 20.14 ? 108 TYR A N   1 
ATOM   801  C  CA  . TYR A 1 108 ? 28.545 -1.078  11.216  1.00 19.86 ? 108 TYR A CA  1 
ATOM   802  C  C   . TYR A 1 108 ? 27.137 -1.545  10.899  1.00 19.58 ? 108 TYR A C   1 
ATOM   803  O  O   . TYR A 1 108 ? 26.686 -1.476  9.753   1.00 20.30 ? 108 TYR A O   1 
ATOM   804  C  CB  . TYR A 1 108 ? 28.473 0.268   11.944  1.00 21.79 ? 108 TYR A CB  1 
ATOM   805  C  CG  . TYR A 1 108 ? 29.811 0.855   12.290  1.00 23.01 ? 108 TYR A CG  1 
ATOM   806  C  CD1 . TYR A 1 108 ? 30.565 0.338   13.335  1.00 24.09 ? 108 TYR A CD1 1 
ATOM   807  C  CD2 . TYR A 1 108 ? 30.312 1.936   11.586  1.00 23.49 ? 108 TYR A CD2 1 
ATOM   808  C  CE1 . TYR A 1 108 ? 31.790 0.877   13.658  1.00 27.98 ? 108 TYR A CE1 1 
ATOM   809  C  CE2 . TYR A 1 108 ? 31.539 2.488   11.905  1.00 24.97 ? 108 TYR A CE2 1 
ATOM   810  C  CZ  . TYR A 1 108 ? 32.271 1.950   12.939  1.00 25.78 ? 108 TYR A CZ  1 
ATOM   811  O  OH  . TYR A 1 108 ? 33.491 2.488   13.267  1.00 28.47 ? 108 TYR A OH  1 
ATOM   812  N  N   . ALA A 1 109 ? 26.429 -1.995  11.917  1.00 21.26 ? 109 ALA A N   1 
ATOM   813  C  CA  . ALA A 1 109 ? 25.085 -2.501  11.703  1.00 23.45 ? 109 ALA A CA  1 
ATOM   814  C  C   . ALA A 1 109 ? 24.124 -1.894  12.707  1.00 23.02 ? 109 ALA A C   1 
ATOM   815  O  O   . ALA A 1 109 ? 24.460 -1.717  13.882  1.00 23.81 ? 109 ALA A O   1 
ATOM   816  C  CB  . ALA A 1 109 ? 25.039 -4.026  11.808  1.00 22.59 ? 109 ALA A CB  1 
ATOM   817  N  N   . LEU A 1 110 ? 22.936 -1.565  12.222  1.00 23.26 ? 110 LEU A N   1 
ATOM   818  C  CA  . LEU A 1 110 ? 21.769 -1.385  13.068  1.00 21.56 ? 110 LEU A CA  1 
ATOM   819  C  C   . LEU A 1 110 ? 21.121 -2.749  13.240  1.00 23.54 ? 110 LEU A C   1 
ATOM   820  O  O   . LEU A 1 110 ? 20.856 -3.436  12.247  1.00 24.54 ? 110 LEU A O   1 
ATOM   821  C  CB  . LEU A 1 110 ? 20.786 -0.416  12.416  1.00 24.13 ? 110 LEU A CB  1 
ATOM   822  C  CG  . LEU A 1 110 ? 21.280 1.008   12.193  1.00 23.01 ? 110 LEU A CG  1 
ATOM   823  C  CD1 . LEU A 1 110 ? 20.161 1.860   11.636  1.00 21.56 ? 110 LEU A CD1 1 
ATOM   824  C  CD2 . LEU A 1 110 ? 21.825 1.596   13.488  1.00 23.46 ? 110 LEU A CD2 1 
ATOM   825  N  N   . LEU A 1 111 ? 20.884 -3.157  14.486  1.00 19.54 ? 111 LEU A N   1 
ATOM   826  C  CA  . LEU A 1 111 ? 20.269 -4.458  14.739  1.00 23.03 ? 111 LEU A CA  1 
ATOM   827  C  C   . LEU A 1 111 ? 18.756 -4.337  14.621  1.00 25.24 ? 111 LEU A C   1 
ATOM   828  O  O   . LEU A 1 111 ? 18.138 -3.494  15.281  1.00 23.87 ? 111 LEU A O   1 
ATOM   829  C  CB  . LEU A 1 111 ? 20.661 -4.994  16.119  1.00 24.09 ? 111 LEU A CB  1 
ATOM   830  C  CG  . LEU A 1 111 ? 20.350 -6.477  16.346  1.00 25.03 ? 111 LEU A CG  1 
ATOM   831  C  CD1 . LEU A 1 111 ? 21.363 -7.333  15.620  1.00 26.92 ? 111 LEU A CD1 1 
ATOM   832  C  CD2 . LEU A 1 111 ? 20.341 -6.812  17.844  1.00 27.26 ? 111 LEU A CD2 1 
ATOM   833  N  N   . ASN A 1 112 ? 18.164 -5.158  13.758  1.00 24.01 ? 112 ASN A N   1 
ATOM   834  C  CA  . ASN A 1 112 ? 16.713 -5.215  13.662  1.00 24.55 ? 112 ASN A CA  1 
ATOM   835  C  C   . ASN A 1 112 ? 16.134 -5.653  15.003  1.00 30.09 ? 112 ASN A C   1 
ATOM   836  O  O   . ASN A 1 112 ? 16.650 -6.569  15.650  1.00 27.39 ? 112 ASN A O   1 
ATOM   837  C  CB  . ASN A 1 112 ? 16.316 -6.186  12.543  1.00 27.80 ? 112 ASN A CB  1 
ATOM   838  C  CG  . ASN A 1 112 ? 14.910 -5.944  12.002  1.00 30.87 ? 112 ASN A CG  1 
ATOM   839  O  OD1 . ASN A 1 112 ? 13.954 -5.754  12.755  1.00 29.48 ? 112 ASN A OD1 1 
ATOM   840  N  ND2 . ASN A 1 112 ? 14.793 -5.917  10.678  1.00 29.29 ? 112 ASN A ND2 1 
ATOM   841  N  N   . ILE A 1 113 ? 15.069 -4.975  15.440  1.00 29.08 ? 113 ILE A N   1 
ATOM   842  C  CA  . ILE A 1 113 ? 14.456 -5.367  16.701  1.00 31.78 ? 113 ILE A CA  1 
ATOM   843  C  C   . ILE A 1 113 ? 13.843 -6.755  16.609  1.00 30.71 ? 113 ILE A C   1 
ATOM   844  O  O   . ILE A 1 113 ? 13.616 -7.399  17.639  1.00 33.22 ? 113 ILE A O   1 
ATOM   845  C  CB  . ILE A 1 113 ? 13.409 -4.336  17.169  1.00 32.28 ? 113 ILE A CB  1 
ATOM   846  C  CG1 . ILE A 1 113 ? 12.195 -4.321  16.238  1.00 31.60 ? 113 ILE A CG1 1 
ATOM   847  C  CG2 . ILE A 1 113 ? 14.047 -2.955  17.301  1.00 27.16 ? 113 ILE A CG2 1 
ATOM   848  C  CD1 . ILE A 1 113 ? 11.090 -3.391  16.702  1.00 31.66 ? 113 ILE A CD1 1 
ATOM   849  N  N   . SER A 1 114 ? 13.586 -7.243  15.401  1.00 31.53 ? 114 SER A N   1 
ATOM   850  C  CA  . SER A 1 114 ? 13.080 -8.593  15.209  1.00 32.08 ? 114 SER A CA  1 
ATOM   851  C  C   . SER A 1 114 ? 14.246 -9.552  15.012  1.00 33.35 ? 114 SER A C   1 
ATOM   852  O  O   . SER A 1 114 ? 15.121 -9.313  14.170  1.00 29.99 ? 114 SER A O   1 
ATOM   853  C  CB  . SER A 1 114 ? 12.136 -8.652  14.012  1.00 34.89 ? 114 SER A CB  1 
ATOM   854  O  OG  . SER A 1 114 ? 11.813 -9.995  13.700  1.00 33.53 ? 114 SER A OG  1 
ATOM   855  N  N   . ARG A 1 115 ? 14.237 -10.647 15.779  1.00 32.60 ? 115 ARG A N   1 
ATOM   856  C  CA  . ARG A 1 115 ? 15.345 -11.596 15.764  1.00 31.34 ? 115 ARG A CA  1 
ATOM   857  C  C   . ARG A 1 115 ? 15.672 -12.088 14.359  1.00 33.66 ? 115 ARG A C   1 
ATOM   858  O  O   . ARG A 1 115 ? 16.844 -12.319 14.048  1.00 37.08 ? 115 ARG A O   1 
ATOM   859  C  CB  . ARG A 1 115 ? 15.021 -12.786 16.670  1.00 36.07 ? 115 ARG A CB  1 
ATOM   860  N  N   . VAL A 1 116 ? 14.664 -12.240 13.492  1.00 29.90 ? 116 VAL A N   1 
ATOM   861  C  CA  . VAL A 1 116 ? 14.898 -12.831 12.175  1.00 33.94 ? 116 VAL A CA  1 
ATOM   862  C  C   . VAL A 1 116 ? 15.357 -11.835 11.119  1.00 33.84 ? 116 VAL A C   1 
ATOM   863  O  O   . VAL A 1 116 ? 15.724 -12.260 10.013  1.00 35.21 ? 116 VAL A O   1 
ATOM   864  C  CB  . VAL A 1 116 ? 13.641 -13.557 11.658  1.00 32.97 ? 116 VAL A CB  1 
ATOM   865  C  CG1 . VAL A 1 116 ? 13.322 -14.738 12.556  1.00 34.67 ? 116 VAL A CG1 1 
ATOM   866  C  CG2 . VAL A 1 116 ? 12.471 -12.600 11.585  1.00 34.43 ? 116 VAL A CG2 1 
ATOM   867  N  N   . GLY A 1 117 ? 15.356 -10.535 11.415  1.00 31.25 ? 117 GLY A N   1 
ATOM   868  C  CA  . GLY A 1 117 ? 15.906 -9.559  10.474  1.00 32.26 ? 117 GLY A CA  1 
ATOM   869  C  C   . GLY A 1 117 ? 15.069 -9.433  9.211   1.00 32.19 ? 117 GLY A C   1 
ATOM   870  O  O   . GLY A 1 117 ? 13.838 -9.498  9.242   1.00 33.24 ? 117 GLY A O   1 
ATOM   871  N  N   . LEU A 1 118 ? 15.741 -9.237  8.075   1.00 29.62 ? 118 LEU A N   1 
ATOM   872  C  CA  . LEU A 1 118 ? 15.055 -9.184  6.789   1.00 33.88 ? 118 LEU A CA  1 
ATOM   873  C  C   . LEU A 1 118 ? 15.026 -10.536 6.086   1.00 38.01 ? 118 LEU A C   1 
ATOM   874  O  O   . LEU A 1 118 ? 14.901 -10.589 4.852   1.00 38.06 ? 118 LEU A O   1 
ATOM   875  C  CB  . LEU A 1 118 ? 15.691 -8.117  5.893   1.00 29.90 ? 118 LEU A CB  1 
ATOM   876  C  CG  . LEU A 1 118 ? 15.585 -6.693  6.454   1.00 29.35 ? 118 LEU A CG  1 
ATOM   877  C  CD1 . LEU A 1 118 ? 16.148 -5.646  5.486   1.00 28.39 ? 118 LEU A CD1 1 
ATOM   878  C  CD2 . LEU A 1 118 ? 14.140 -6.367  6.834   1.00 30.01 ? 118 LEU A CD2 1 
ATOM   879  N  N   . ILE A 1 119 ? 15.147 -11.635 6.842   1.00 36.28 ? 119 ILE A N   1 
ATOM   880  C  CA  . ILE A 1 119 ? 14.934 -12.967 6.279   1.00 40.90 ? 119 ILE A CA  1 
ATOM   881  C  C   . ILE A 1 119 ? 13.544 -13.068 5.666   1.00 45.06 ? 119 ILE A C   1 
ATOM   882  O  O   . ILE A 1 119 ? 13.352 -13.739 4.643   1.00 39.64 ? 119 ILE A O   1 
ATOM   883  C  CB  . ILE A 1 119 ? 15.148 -14.051 7.357   1.00 37.71 ? 119 ILE A CB  1 
ATOM   884  N  N   . ALA A 1 120 ? 12.558 -12.420 6.284   1.00 43.59 ? 120 ALA A N   1 
ATOM   885  C  CA  . ALA A 1 120 ? 11.212 -12.294 5.751   1.00 45.60 ? 120 ALA A CA  1 
ATOM   886  C  C   . ALA A 1 120 ? 10.852 -10.817 5.646   1.00 46.22 ? 120 ALA A C   1 
ATOM   887  O  O   . ALA A 1 120 ? 11.465 -9.961  6.291   1.00 43.41 ? 120 ALA A O   1 
ATOM   888  C  CB  . ALA A 1 120 ? 10.189 -13.026 6.630   1.00 41.58 ? 120 ALA A CB  1 
ATOM   889  N  N   . GLN A 1 121 ? 9.844  -10.524 4.822   1.00 50.15 ? 121 GLN A N   1 
ATOM   890  C  CA  . GLN A 1 121 ? 9.382  -9.151  4.639   1.00 46.57 ? 121 GLN A CA  1 
ATOM   891  C  C   . GLN A 1 121 ? 8.386  -8.707  5.706   1.00 42.67 ? 121 GLN A C   1 
ATOM   892  O  O   . GLN A 1 121 ? 8.002  -7.532  5.715   1.00 41.88 ? 121 GLN A O   1 
ATOM   893  C  CB  . GLN A 1 121 ? 8.757  -8.987  3.249   1.00 47.75 ? 121 GLN A CB  1 
ATOM   894  N  N   . ASN A 1 122 ? 7.965  -9.606  6.598   1.00 42.90 ? 122 ASN A N   1 
ATOM   895  C  CA  . ASN A 1 122 ? 6.998  -9.279  7.641   1.00 41.99 ? 122 ASN A CA  1 
ATOM   896  C  C   . ASN A 1 122 ? 7.579  -9.566  9.024   1.00 38.38 ? 122 ASN A C   1 
ATOM   897  O  O   . ASN A 1 122 ? 6.948  -10.233 9.849   1.00 37.03 ? 122 ASN A O   1 
ATOM   898  C  CB  . ASN A 1 122 ? 5.704  -10.065 7.411   1.00 36.79 ? 122 ASN A CB  1 
ATOM   899  C  CG  . ASN A 1 122 ? 5.894  -11.562 7.570   1.00 40.64 ? 122 ASN A CG  1 
ATOM   900  O  OD1 . ASN A 1 122 ? 6.899  -12.119 7.129   1.00 44.85 ? 122 ASN A OD1 1 
ATOM   901  N  ND2 . ASN A 1 122 ? 4.910  -12.227 8.166   1.00 38.88 ? 122 ASN A ND2 1 
ATOM   902  N  N   . GLU A 1 123 ? 8.776  -9.038  9.297   1.00 38.27 ? 123 GLU A N   1 
ATOM   903  C  CA  . GLU A 1 123 ? 9.536  -9.479  10.462  1.00 34.41 ? 123 GLU A CA  1 
ATOM   904  C  C   . GLU A 1 123 ? 8.938  -9.016  11.788  1.00 35.52 ? 123 GLU A C   1 
ATOM   905  O  O   . GLU A 1 123 ? 9.273  -9.587  12.833  1.00 33.92 ? 123 GLU A O   1 
ATOM   906  C  CB  . GLU A 1 123 ? 10.982 -9.008  10.334  1.00 35.09 ? 123 GLU A CB  1 
ATOM   907  C  CG  . GLU A 1 123 ? 11.201 -7.562  10.709  1.00 32.93 ? 123 GLU A CG  1 
ATOM   908  C  CD  . GLU A 1 123 ? 11.225 -6.659  9.495   1.00 34.54 ? 123 GLU A CD  1 
ATOM   909  O  OE1 . GLU A 1 123 ? 10.704 -7.079  8.440   1.00 35.50 ? 123 GLU A OE1 1 
ATOM   910  O  OE2 . GLU A 1 123 ? 11.771 -5.540  9.592   1.00 29.20 ? 123 GLU A OE2 1 
ATOM   911  N  N   . LEU A 1 124 ? 8.061  -8.014  11.782  1.00 33.47 ? 124 LEU A N   1 
ATOM   912  C  CA  . LEU A 1 124 ? 7.397  -7.566  12.999  1.00 34.57 ? 124 LEU A CA  1 
ATOM   913  C  C   . LEU A 1 124 ? 5.999  -8.157  13.161  1.00 41.66 ? 124 LEU A C   1 
ATOM   914  O  O   . LEU A 1 124 ? 5.301  -7.813  14.123  1.00 39.96 ? 124 LEU A O   1 
ATOM   915  C  CB  . LEU A 1 124 ? 7.325  -6.031  13.031  1.00 36.15 ? 124 LEU A CB  1 
ATOM   916  C  CG  . LEU A 1 124 ? 8.656  -5.265  13.013  1.00 35.31 ? 124 LEU A CG  1 
ATOM   917  C  CD1 . LEU A 1 124 ? 8.434  -3.759  13.132  1.00 31.94 ? 124 LEU A CD1 1 
ATOM   918  C  CD2 . LEU A 1 124 ? 9.597  -5.757  14.105  1.00 33.20 ? 124 LEU A CD2 1 
ATOM   919  N  N   . ALA A 1 125 ? 5.576  -9.046  12.252  1.00 38.19 ? 125 ALA A N   1 
ATOM   920  C  CA  . ALA A 1 125 ? 4.229  -9.605  12.334  1.00 42.22 ? 125 ALA A CA  1 
ATOM   921  C  C   . ALA A 1 125 ? 4.072  -10.517 13.540  1.00 42.41 ? 125 ALA A C   1 
ATOM   922  O  O   . ALA A 1 125 ? 2.980  -10.608 14.113  1.00 44.89 ? 125 ALA A O   1 
ATOM   923  C  CB  . ALA A 1 125 ? 3.887  -10.370 11.055  1.00 38.82 ? 125 ALA A CB  1 
ATOM   924  N  N   . ASN A 1 126 ? 5.142  -11.195 13.937  1.00 41.90 ? 126 ASN A N   1 
ATOM   925  C  CA  . ASN A 1 126 ? 5.126  -12.082 15.089  1.00 47.16 ? 126 ASN A CA  1 
ATOM   926  C  C   . ASN A 1 126 ? 5.819  -11.372 16.244  1.00 43.50 ? 126 ASN A C   1 
ATOM   927  O  O   . ASN A 1 126 ? 7.013  -11.066 16.159  1.00 42.79 ? 126 ASN A O   1 
ATOM   928  C  CB  . ASN A 1 126 ? 5.820  -13.405 14.763  1.00 43.88 ? 126 ASN A CB  1 
ATOM   929  C  CG  . ASN A 1 126 ? 5.568  -14.471 15.809  1.00 48.44 ? 126 ASN A CG  1 
ATOM   930  O  OD1 . ASN A 1 126 ? 5.358  -14.173 16.987  1.00 47.42 ? 126 ASN A OD1 1 
ATOM   931  N  ND2 . ASN A 1 126 ? 5.586  -15.728 15.381  1.00 51.00 ? 126 ASN A ND2 1 
ATOM   932  N  N   . LEU A 1 127 ? 5.069  -11.107 17.316  1.00 45.84 ? 127 LEU A N   1 
ATOM   933  C  CA  . LEU A 1 127 ? 5.661  -10.445 18.472  1.00 43.65 ? 127 LEU A CA  1 
ATOM   934  C  C   . LEU A 1 127 ? 6.757  -11.291 19.109  1.00 42.84 ? 127 LEU A C   1 
ATOM   935  O  O   . LEU A 1 127 ? 7.698  -10.740 19.688  1.00 43.99 ? 127 LEU A O   1 
ATOM   936  C  CB  . LEU A 1 127 ? 4.579  -10.106 19.496  1.00 47.49 ? 127 LEU A CB  1 
ATOM   937  C  CG  . LEU A 1 127 ? 3.734  -8.874  19.164  1.00 47.09 ? 127 LEU A CG  1 
ATOM   938  C  CD1 . LEU A 1 127 ? 2.510  -8.806  20.062  1.00 42.99 ? 127 LEU A CD1 1 
ATOM   939  C  CD2 . LEU A 1 127 ? 4.564  -7.603  19.278  1.00 44.39 ? 127 LEU A CD2 1 
ATOM   940  N  N   . ALA A 1 128 ? 6.669  -12.620 18.999  1.00 41.76 ? 128 ALA A N   1 
ATOM   941  C  CA  . ALA A 1 128 ? 7.686  -13.473 19.609  1.00 44.74 ? 128 ALA A CA  1 
ATOM   942  C  C   . ALA A 1 128 ? 9.074  -13.208 19.036  1.00 42.26 ? 128 ALA A C   1 
ATOM   943  O  O   . ALA A 1 128 ? 10.077 -13.406 19.730  1.00 41.50 ? 128 ALA A O   1 
ATOM   944  C  CB  . ALA A 1 128 ? 7.313  -14.945 19.440  1.00 46.55 ? 128 ALA A CB  1 
ATOM   945  N  N   . ASN A 1 129 ? 9.158  -12.764 17.779  1.00 42.41 ? 129 ASN A N   1 
ATOM   946  C  CA  . ASN A 1 129 ? 10.453 -12.458 17.186  1.00 40.01 ? 129 ASN A CA  1 
ATOM   947  C  C   . ASN A 1 129 ? 11.045 -11.156 17.707  1.00 38.45 ? 129 ASN A C   1 
ATOM   948  O  O   . ASN A 1 129 ? 12.263 -10.963 17.613  1.00 36.97 ? 129 ASN A O   1 
ATOM   949  C  CB  . ASN A 1 129 ? 10.342 -12.386 15.661  1.00 43.08 ? 129 ASN A CB  1 
ATOM   950  C  CG  . ASN A 1 129 ? 10.051 -13.728 15.040  1.00 43.95 ? 129 ASN A CG  1 
ATOM   951  O  OD1 . ASN A 1 129 ? 9.181  -13.846 14.182  1.00 45.25 ? 129 ASN A OD1 1 
ATOM   952  N  ND2 . ASN A 1 129 ? 10.752 -14.761 15.500  1.00 47.49 ? 129 ASN A ND2 1 
ATOM   953  N  N   . ILE A 1 130 ? 10.214 -10.257 18.230  1.00 39.32 ? 130 ILE A N   1 
ATOM   954  C  CA  . ILE A 1 130 ? 10.701 -9.006  18.797  1.00 39.64 ? 130 ILE A CA  1 
ATOM   955  C  C   . ILE A 1 130 ? 11.132 -9.310  20.225  1.00 41.47 ? 130 ILE A C   1 
ATOM   956  O  O   . ILE A 1 130 ? 10.390 -9.056  21.182  1.00 40.82 ? 130 ILE A O   1 
ATOM   957  C  CB  . ILE A 1 130 ? 9.634  -7.897  18.735  1.00 39.58 ? 130 ILE A CB  1 
ATOM   958  C  CG1 . ILE A 1 130 ? 9.057  -7.797  17.320  1.00 38.81 ? 130 ILE A CG1 1 
ATOM   959  C  CG2 . ILE A 1 130 ? 10.238 -6.561  19.128  1.00 38.71 ? 130 ILE A CG2 1 
ATOM   960  C  CD1 . ILE A 1 130 ? 7.661  -7.220  17.271  1.00 40.53 ? 130 ILE A CD1 1 
ATOM   961  N  N   . ASP A 1 131 ? 12.326 -9.880  20.366  1.00 41.39 ? 131 ASP A N   1 
ATOM   962  C  CA  . ASP A 1 131 ? 12.785 -10.480 21.613  1.00 38.93 ? 131 ASP A CA  1 
ATOM   963  C  C   . ASP A 1 131 ? 13.863 -9.598  22.229  1.00 37.84 ? 131 ASP A C   1 
ATOM   964  O  O   . ASP A 1 131 ? 14.925 -9.401  21.632  1.00 34.34 ? 131 ASP A O   1 
ATOM   965  C  CB  . ASP A 1 131 ? 13.306 -11.895 21.351  1.00 36.06 ? 131 ASP A CB  1 
ATOM   966  C  CG  . ASP A 1 131 ? 13.740 -12.613 22.619  1.00 42.60 ? 131 ASP A CG  1 
ATOM   967  O  OD1 . ASP A 1 131 ? 13.886 -13.860 22.574  1.00 46.42 ? 131 ASP A OD1 1 
ATOM   968  O  OD2 . ASP A 1 131 ? 13.956 -11.941 23.652  1.00 41.54 ? 131 ASP A OD2 1 
ATOM   969  N  N   . ALA A 1 132 ? 13.603 -9.113  23.448  1.00 38.79 ? 132 ALA A N   1 
ATOM   970  C  CA  . ALA A 1 132 ? 14.526 -8.184  24.091  1.00 39.79 ? 132 ALA A CA  1 
ATOM   971  C  C   . ALA A 1 132 ? 15.822 -8.874  24.504  1.00 38.68 ? 132 ALA A C   1 
ATOM   972  O  O   . ALA A 1 132 ? 16.907 -8.305  24.338  1.00 34.21 ? 132 ALA A O   1 
ATOM   973  C  CB  . ALA A 1 132 ? 13.856 -7.533  25.300  1.00 38.74 ? 132 ALA A CB  1 
ATOM   974  N  N   . GLU A 1 133 ? 15.734 -10.093 25.045  1.00 38.22 ? 133 GLU A N   1 
ATOM   975  C  CA  . GLU A 1 133 ? 16.931 -10.764 25.544  1.00 37.78 ? 133 GLU A CA  1 
ATOM   976  C  C   . GLU A 1 133 ? 17.880 -11.127 24.407  1.00 37.29 ? 133 GLU A C   1 
ATOM   977  O  O   . GLU A 1 133 ? 19.103 -11.034 24.560  1.00 38.48 ? 133 GLU A O   1 
ATOM   978  C  CB  . GLU A 1 133 ? 16.543 -12.008 26.342  1.00 42.52 ? 133 GLU A CB  1 
ATOM   979  N  N   . ALA A 1 134 ? 17.336 -11.542 23.259  1.00 36.40 ? 134 ALA A N   1 
ATOM   980  C  CA  . ALA A 1 134 ? 18.183 -11.824 22.106  1.00 33.65 ? 134 ALA A CA  1 
ATOM   981  C  C   . ALA A 1 134 ? 18.968 -10.588 21.694  1.00 32.61 ? 134 ALA A C   1 
ATOM   982  O  O   . ALA A 1 134 ? 20.162 -10.669 21.383  1.00 33.56 ? 134 ALA A O   1 
ATOM   983  C  CB  . ALA A 1 134 ? 17.334 -12.333 20.940  1.00 35.99 ? 134 ALA A CB  1 
ATOM   984  N  N   . VAL A 1 135 ? 18.322 -9.426  21.719  1.00 29.84 ? 135 VAL A N   1 
ATOM   985  C  CA  . VAL A 1 135 ? 19.004 -8.206  21.310  1.00 31.25 ? 135 VAL A CA  1 
ATOM   986  C  C   . VAL A 1 135 ? 20.011 -7.761  22.359  1.00 31.23 ? 135 VAL A C   1 
ATOM   987  O  O   . VAL A 1 135 ? 21.105 -7.297  22.023  1.00 32.54 ? 135 VAL A O   1 
ATOM   988  C  CB  . VAL A 1 135 ? 17.973 -7.123  20.994  1.00 32.61 ? 135 VAL A CB  1 
ATOM   989  C  CG1 . VAL A 1 135 ? 18.645 -5.753  20.913  1.00 34.04 ? 135 VAL A CG1 1 
ATOM   990  C  CG2 . VAL A 1 135 ? 17.328 -7.498  19.664  1.00 31.30 ? 135 VAL A CG2 1 
ATOM   991  N  N   . LYS A 1 136 ? 19.674 -7.902  23.642  1.00 33.42 ? 136 LYS A N   1 
ATOM   992  C  CA  . LYS A 1 136 ? 20.655 -7.619  24.684  1.00 30.20 ? 136 LYS A CA  1 
ATOM   993  C  C   . LYS A 1 136 ? 21.901 -8.474  24.494  1.00 32.33 ? 136 LYS A C   1 
ATOM   994  O  O   . LYS A 1 136 ? 23.029 -7.965  24.510  1.00 34.98 ? 136 LYS A O   1 
ATOM   995  C  CB  . LYS A 1 136 ? 20.042 -7.851  26.064  1.00 39.21 ? 136 LYS A CB  1 
ATOM   996  N  N   . GLN A 1 137 ? 21.709 -9.778  24.284  1.00 33.02 ? 137 GLN A N   1 
ATOM   997  C  CA  . GLN A 1 137 ? 22.842 -10.675 24.090  1.00 32.18 ? 137 GLN A CA  1 
ATOM   998  C  C   . GLN A 1 137 ? 23.640 -10.294 22.853  1.00 30.98 ? 137 GLN A C   1 
ATOM   999  O  O   . GLN A 1 137 ? 24.877 -10.271 22.888  1.00 31.49 ? 137 GLN A O   1 
ATOM   1000 C  CB  . GLN A 1 137 ? 22.354 -12.121 23.993  1.00 34.44 ? 137 GLN A CB  1 
ATOM   1001 N  N   . ALA A 1 138 ? 22.952 -9.985  21.747  1.00 32.83 ? 138 ALA A N   1 
ATOM   1002 C  CA  . ALA A 1 138 ? 23.649 -9.600  20.524  1.00 32.32 ? 138 ALA A CA  1 
ATOM   1003 C  C   . ALA A 1 138 ? 24.484 -8.348  20.736  1.00 32.92 ? 138 ALA A C   1 
ATOM   1004 O  O   . ALA A 1 138 ? 25.635 -8.277  20.289  1.00 31.44 ? 138 ALA A O   1 
ATOM   1005 C  CB  . ALA A 1 138 ? 22.648 -9.382  19.388  1.00 30.06 ? 138 ALA A CB  1 
ATOM   1006 N  N   . VAL A 1 139 ? 23.917 -7.349  21.419  1.00 29.45 ? 139 VAL A N   1 
ATOM   1007 C  CA  . VAL A 1 139 ? 24.627 -6.102  21.685  1.00 29.94 ? 139 VAL A CA  1 
ATOM   1008 C  C   . VAL A 1 139 ? 25.855 -6.356  22.543  1.00 31.41 ? 139 VAL A C   1 
ATOM   1009 O  O   . VAL A 1 139 ? 26.947 -5.846  22.262  1.00 33.49 ? 139 VAL A O   1 
ATOM   1010 C  CB  . VAL A 1 139 ? 23.671 -5.086  22.342  1.00 32.94 ? 139 VAL A CB  1 
ATOM   1011 C  CG1 . VAL A 1 139 ? 24.445 -3.955  23.008  1.00 30.76 ? 139 VAL A CG1 1 
ATOM   1012 C  CG2 . VAL A 1 139 ? 22.694 -4.537  21.293  1.00 28.58 ? 139 VAL A CG2 1 
ATOM   1013 N  N   . GLN A 1 140 ? 25.699 -7.147  23.604  1.00 33.58 ? 140 GLN A N   1 
ATOM   1014 C  CA  . GLN A 1 140 ? 26.847 -7.488  24.436  1.00 35.08 ? 140 GLN A CA  1 
ATOM   1015 C  C   . GLN A 1 140 ? 27.913 -8.219  23.630  1.00 36.45 ? 140 GLN A C   1 
ATOM   1016 O  O   . GLN A 1 140 ? 29.111 -8.047  23.881  1.00 37.23 ? 140 GLN A O   1 
ATOM   1017 C  CB  . GLN A 1 140 ? 26.386 -8.333  25.621  1.00 37.60 ? 140 GLN A CB  1 
ATOM   1018 C  CG  . GLN A 1 140 ? 25.599 -7.537  26.653  1.00 37.86 ? 140 GLN A CG  1 
ATOM   1019 C  CD  . GLN A 1 140 ? 26.409 -6.394  27.243  1.00 44.48 ? 140 GLN A CD  1 
ATOM   1020 O  OE1 . GLN A 1 140 ? 27.361 -6.616  27.995  1.00 46.40 ? 140 GLN A OE1 1 
ATOM   1021 N  NE2 . GLN A 1 140 ? 26.056 -5.162  26.874  1.00 42.30 ? 140 GLN A NE2 1 
ATOM   1022 N  N   . ARG A 1 141 ? 27.492 -9.011  22.641  1.00 34.60 ? 141 ARG A N   1 
ATOM   1023 C  CA  . ARG A 1 141 ? 28.426 -9.819  21.866  1.00 35.32 ? 141 ARG A CA  1 
ATOM   1024 C  C   . ARG A 1 141 ? 29.239 -8.963  20.899  1.00 34.63 ? 141 ARG A C   1 
ATOM   1025 O  O   . ARG A 1 141 ? 30.425 -9.231  20.671  1.00 33.09 ? 141 ARG A O   1 
ATOM   1026 C  CB  . ARG A 1 141 ? 27.653 -10.896 21.102  1.00 34.88 ? 141 ARG A CB  1 
ATOM   1027 C  CG  . ARG A 1 141 ? 28.207 -12.292 21.251  1.00 40.70 ? 141 ARG A CG  1 
ATOM   1028 C  CD  . ARG A 1 141 ? 27.139 -13.348 20.987  1.00 40.28 ? 141 ARG A CD  1 
ATOM   1029 N  NE  . ARG A 1 141 ? 26.320 -13.048 19.814  1.00 38.90 ? 141 ARG A NE  1 
ATOM   1030 C  CZ  . ARG A 1 141 ? 24.998 -12.938 19.826  1.00 37.20 ? 141 ARG A CZ  1 
ATOM   1031 N  NH1 . ARG A 1 141 ? 24.304 -13.065 20.946  1.00 35.62 ? 141 ARG A NH1 1 
ATOM   1032 N  NH2 . ARG A 1 141 ? 24.354 -12.709 18.683  1.00 37.15 ? 141 ARG A NH2 1 
ATOM   1033 N  N   . HIS A 1 142 ? 28.623 -7.935  20.318  1.00 32.57 ? 142 HIS A N   1 
ATOM   1034 C  CA  . HIS A 1 142 ? 29.269 -7.079  19.321  1.00 30.80 ? 142 HIS A CA  1 
ATOM   1035 C  C   . HIS A 1 142 ? 29.073 -5.624  19.718  1.00 32.14 ? 142 HIS A C   1 
ATOM   1036 O  O   . HIS A 1 142 ? 28.320 -4.885  19.074  1.00 29.27 ? 142 HIS A O   1 
ATOM   1037 C  CB  . HIS A 1 142 ? 28.708 -7.360  17.928  1.00 30.27 ? 142 HIS A CB  1 
ATOM   1038 C  CG  . HIS A 1 142 ? 28.790 -8.802  17.539  1.00 31.35 ? 142 HIS A CG  1 
ATOM   1039 N  ND1 . HIS A 1 142 ? 29.990 -9.465  17.392  1.00 34.02 ? 142 HIS A ND1 1 
ATOM   1040 C  CD2 . HIS A 1 142 ? 27.822 -9.721  17.307  1.00 32.60 ? 142 HIS A CD2 1 
ATOM   1041 C  CE1 . HIS A 1 142 ? 29.758 -10.725 17.068  1.00 37.33 ? 142 HIS A CE1 1 
ATOM   1042 N  NE2 . HIS A 1 142 ? 28.451 -10.907 17.011  1.00 34.31 ? 142 HIS A NE2 1 
ATOM   1043 N  N   . PRO A 1 143 ? 29.743 -5.181  20.789  1.00 34.35 ? 143 PRO A N   1 
ATOM   1044 C  CA  . PRO A 1 143 ? 29.504 -3.817  21.284  1.00 33.00 ? 143 PRO A CA  1 
ATOM   1045 C  C   . PRO A 1 143 ? 29.956 -2.731  20.327  1.00 31.59 ? 143 PRO A C   1 
ATOM   1046 O  O   . PRO A 1 143 ? 29.402 -1.628  20.362  1.00 30.52 ? 143 PRO A O   1 
ATOM   1047 C  CB  . PRO A 1 143 ? 30.294 -3.781  22.602  1.00 32.62 ? 143 PRO A CB  1 
ATOM   1048 C  CG  . PRO A 1 143 ? 31.363 -4.818  22.424  1.00 34.55 ? 143 PRO A CG  1 
ATOM   1049 C  CD  . PRO A 1 143 ? 30.715 -5.913  21.624  1.00 31.19 ? 143 PRO A CD  1 
ATOM   1050 N  N   . ASP A 1 144 ? 30.930 -2.996  19.463  1.00 30.40 ? 144 ASP A N   1 
ATOM   1051 C  CA  . ASP A 1 144 ? 31.396 -1.962  18.550  1.00 30.77 ? 144 ASP A CA  1 
ATOM   1052 C  C   . ASP A 1 144 ? 30.827 -2.092  17.144  1.00 29.81 ? 144 ASP A C   1 
ATOM   1053 O  O   . ASP A 1 144 ? 30.820 -1.103  16.404  1.00 28.74 ? 144 ASP A O   1 
ATOM   1054 C  CB  . ASP A 1 144 ? 32.927 -1.965  18.478  1.00 35.41 ? 144 ASP A CB  1 
ATOM   1055 C  CG  . ASP A 1 144 ? 33.567 -1.524  19.781  1.00 38.21 ? 144 ASP A CG  1 
ATOM   1056 O  OD1 . ASP A 1 144 ? 33.009 -0.621  20.445  1.00 39.55 ? 144 ASP A OD1 1 
ATOM   1057 O  OD2 . ASP A 1 144 ? 34.632 -2.069  20.133  1.00 42.22 ? 144 ASP A OD2 1 
ATOM   1058 N  N   . PHE A 1 145 ? 30.359 -3.278  16.761  1.00 28.07 ? 145 PHE A N   1 
ATOM   1059 C  CA  . PHE A 1 145 ? 29.790 -3.474  15.433  1.00 27.45 ? 145 PHE A CA  1 
ATOM   1060 C  C   . PHE A 1 145 ? 28.367 -2.936  15.355  1.00 24.37 ? 145 PHE A C   1 
ATOM   1061 O  O   . PHE A 1 145 ? 28.004 -2.269  14.378  1.00 23.01 ? 145 PHE A O   1 
ATOM   1062 C  CB  . PHE A 1 145 ? 29.843 -4.961  15.077  1.00 25.08 ? 145 PHE A CB  1 
ATOM   1063 C  CG  . PHE A 1 145 ? 29.265 -5.307  13.733  1.00 26.81 ? 145 PHE A CG  1 
ATOM   1064 C  CD1 . PHE A 1 145 ? 29.788 -4.761  12.570  1.00 24.87 ? 145 PHE A CD1 1 
ATOM   1065 C  CD2 . PHE A 1 145 ? 28.236 -6.235  13.629  1.00 26.30 ? 145 PHE A CD2 1 
ATOM   1066 C  CE1 . PHE A 1 145 ? 29.266 -5.102  11.327  1.00 27.35 ? 145 PHE A CE1 1 
ATOM   1067 C  CE2 . PHE A 1 145 ? 27.708 -6.582  12.391  1.00 26.17 ? 145 PHE A CE2 1 
ATOM   1068 C  CZ  . PHE A 1 145 ? 28.224 -6.023  11.239  1.00 23.28 ? 145 PHE A CZ  1 
ATOM   1069 N  N   . ILE A 1 146 ? 27.556 -3.205  16.372  1.00 23.53 ? 146 ILE A N   1 
ATOM   1070 C  CA  . ILE A 1 146 ? 26.169 -2.751  16.411  1.00 24.45 ? 146 ILE A CA  1 
ATOM   1071 C  C   . ILE A 1 146 ? 26.144 -1.329  16.956  1.00 25.27 ? 146 ILE A C   1 
ATOM   1072 O  O   . ILE A 1 146 ? 26.569 -1.083  18.089  1.00 21.59 ? 146 ILE A O   1 
ATOM   1073 C  CB  . ILE A 1 146 ? 25.300 -3.693  17.260  1.00 28.09 ? 146 ILE A CB  1 
ATOM   1074 C  CG1 . ILE A 1 146 ? 25.284 -5.104  16.647  1.00 24.99 ? 146 ILE A CG1 1 
ATOM   1075 C  CG2 . ILE A 1 146 ? 23.897 -3.126  17.445  1.00 22.74 ? 146 ILE A CG2 1 
ATOM   1076 C  CD1 . ILE A 1 146 ? 24.781 -6.195  17.605  1.00 26.66 ? 146 ILE A CD1 1 
ATOM   1077 N  N   . VAL A 1 147 ? 25.659 -0.389  16.144  1.00 20.23 ? 147 VAL A N   1 
ATOM   1078 C  CA  . VAL A 1 147 ? 25.646 1.023   16.514  1.00 22.56 ? 147 VAL A CA  1 
ATOM   1079 C  C   . VAL A 1 147 ? 24.248 1.549   16.786  1.00 23.65 ? 147 VAL A C   1 
ATOM   1080 O  O   . VAL A 1 147 ? 24.106 2.733   17.115  1.00 23.82 ? 147 VAL A O   1 
ATOM   1081 C  CB  . VAL A 1 147 ? 26.349 1.889   15.452  1.00 20.63 ? 147 VAL A CB  1 
ATOM   1082 C  CG1 . VAL A 1 147 ? 27.819 1.505   15.368  1.00 20.83 ? 147 VAL A CG1 1 
ATOM   1083 C  CG2 . VAL A 1 147 ? 25.649 1.774   14.091  1.00 21.75 ? 147 VAL A CG2 1 
ATOM   1084 N  N   . GLY A 1 148 ? 23.219 0.713   16.690  1.00 22.33 ? 148 GLY A N   1 
ATOM   1085 C  CA  . GLY A 1 148 ? 21.868 1.152   16.978  1.00 21.32 ? 148 GLY A CA  1 
ATOM   1086 C  C   . GLY A 1 148 ? 20.856 0.088   16.593  1.00 23.90 ? 148 GLY A C   1 
ATOM   1087 O  O   . GLY A 1 148 ? 21.210 -1.054  16.282  1.00 22.90 ? 148 GLY A O   1 
ATOM   1088 N  N   . LEU A 1 149 ? 19.588 0.491   16.612  1.00 21.44 ? 149 LEU A N   1 
ATOM   1089 C  CA  . LEU A 1 149 ? 18.475 -0.435  16.378  1.00 22.86 ? 149 LEU A CA  1 
ATOM   1090 C  C   . LEU A 1 149 ? 17.665 -0.009  15.164  1.00 21.30 ? 149 LEU A C   1 
ATOM   1091 O  O   . LEU A 1 149 ? 17.672 1.158   14.792  1.00 24.79 ? 149 LEU A O   1 
ATOM   1092 C  CB  . LEU A 1 149 ? 17.560 -0.513  17.606  1.00 23.44 ? 149 LEU A CB  1 
ATOM   1093 C  CG  . LEU A 1 149 ? 18.175 -0.782  18.982  1.00 26.26 ? 149 LEU A CG  1 
ATOM   1094 C  CD1 . LEU A 1 149 ? 17.135 -0.588  20.076  1.00 26.27 ? 149 LEU A CD1 1 
ATOM   1095 C  CD2 . LEU A 1 149 ? 18.767 -2.198  19.049  1.00 24.21 ? 149 LEU A CD2 1 
HETATM 1096 N  N   . KCX A 1 150 ? 16.972 -0.958  14.544  1.00 23.21 ? 150 KCX A N   1 
HETATM 1097 C  CA  . KCX A 1 150 ? 16.159 -0.647  13.369  1.00 22.27 ? 150 KCX A CA  1 
HETATM 1098 C  CB  . KCX A 1 150 ? 16.759 -1.275  12.098  1.00 26.34 ? 150 KCX A CB  1 
HETATM 1099 C  CG  . KCX A 1 150 ? 16.621 -0.452  10.801  1.00 25.76 ? 150 KCX A CG  1 
HETATM 1100 C  CD  . KCX A 1 150 ? 15.196 -0.097  10.453  1.00 26.73 ? 150 KCX A CD  1 
HETATM 1101 C  CE  . KCX A 1 150 ? 15.134 0.710   9.157   1.00 23.04 ? 150 KCX A CE  1 
HETATM 1102 N  NZ  . KCX A 1 150 ? 15.558 -0.166  8.023   1.00 20.45 ? 150 KCX A NZ  1 
HETATM 1103 C  C   . KCX A 1 150 ? 14.743 -1.162  13.580  1.00 24.67 ? 150 KCX A C   1 
HETATM 1104 O  O   . KCX A 1 150 ? 14.551 -2.315  13.957  1.00 25.02 ? 150 KCX A O   1 
HETATM 1105 C  CX  . KCX A 1 150 ? 15.037 -0.111  6.795   1.00 24.98 ? 150 KCX A CX  1 
HETATM 1106 O  OQ1 . KCX A 1 150 ? 15.473 -0.899  5.940   1.00 22.93 ? 150 KCX A OQ1 1 
HETATM 1107 O  OQ2 . KCX A 1 150 ? 14.136 0.689   6.490   1.00 22.43 ? 150 KCX A OQ2 1 
ATOM   1108 N  N   . ALA A 1 151 ? 13.751 -0.316  13.337  1.00 22.18 ? 151 ALA A N   1 
ATOM   1109 C  CA  . ALA A 1 151 ? 12.367 -0.773  13.376  1.00 24.81 ? 151 ALA A CA  1 
ATOM   1110 C  C   . ALA A 1 151 ? 11.644 -0.289  12.127  1.00 26.44 ? 151 ALA A C   1 
ATOM   1111 O  O   . ALA A 1 151 ? 11.569 0.912   11.888  1.00 23.81 ? 151 ALA A O   1 
ATOM   1112 C  CB  . ALA A 1 151 ? 11.662 -0.277  14.635  1.00 24.66 ? 151 ALA A CB  1 
ATOM   1113 N  N   . ARG A 1 152 ? 11.128 -1.219  11.319  1.00 27.14 ? 152 ARG A N   1 
ATOM   1114 C  CA  . ARG A 1 152 ? 10.409 -0.864  10.095  1.00 25.26 ? 152 ARG A CA  1 
ATOM   1115 C  C   . ARG A 1 152 ? 8.923  -0.802  10.413  1.00 29.42 ? 152 ARG A C   1 
ATOM   1116 O  O   . ARG A 1 152 ? 8.225  -1.821  10.401  1.00 32.02 ? 152 ARG A O   1 
ATOM   1117 C  CB  . ARG A 1 152 ? 10.705 -1.855  8.973   1.00 28.88 ? 152 ARG A CB  1 
ATOM   1118 C  CG  . ARG A 1 152 ? 12.190 -2.037  8.671   1.00 26.25 ? 152 ARG A CG  1 
ATOM   1119 C  CD  . ARG A 1 152 ? 12.398 -2.633  7.284   1.00 29.90 ? 152 ARG A CD  1 
ATOM   1120 N  NE  . ARG A 1 152 ? 11.763 -3.940  7.162   1.00 28.86 ? 152 ARG A NE  1 
ATOM   1121 C  CZ  . ARG A 1 152 ? 11.133 -4.374  6.081   1.00 35.23 ? 152 ARG A CZ  1 
ATOM   1122 N  NH1 . ARG A 1 152 ? 11.020 -3.621  4.995   1.00 26.06 ? 152 ARG A NH1 1 
ATOM   1123 N  NH2 . ARG A 1 152 ? 10.605 -5.595  6.088   1.00 33.97 ? 152 ARG A NH2 1 
ATOM   1124 N  N   . MET A 1 153 ? 8.423  0.401   10.676  1.00 28.35 ? 153 MET A N   1 
ATOM   1125 C  CA  . MET A 1 153 ? 7.071  0.557   11.199  1.00 28.95 ? 153 MET A CA  1 
ATOM   1126 C  C   . MET A 1 153 ? 6.146  0.918   10.042  1.00 30.13 ? 153 MET A C   1 
ATOM   1127 O  O   . MET A 1 153 ? 5.888  2.090   9.769   1.00 31.20 ? 153 MET A O   1 
ATOM   1128 C  CB  . MET A 1 153 ? 7.037  1.597   12.306  1.00 29.13 ? 153 MET A CB  1 
ATOM   1129 C  CG  . MET A 1 153 ? 7.999  1.232   13.423  1.00 28.22 ? 153 MET A CG  1 
ATOM   1130 S  SD  . MET A 1 153 ? 7.332  -0.072  14.445  1.00 31.70 ? 153 MET A SD  1 
ATOM   1131 C  CE  . MET A 1 153 ? 5.603  0.376   14.544  1.00 34.09 ? 153 MET A CE  1 
ATOM   1132 N  N   . SER A 1 154 ? 5.664  -0.104  9.345   1.00 28.47 ? 154 SER A N   1 
ATOM   1133 C  CA  . SER A 1 154 ? 4.736  0.092   8.241   1.00 31.21 ? 154 SER A CA  1 
ATOM   1134 C  C   . SER A 1 154 ? 3.804  -1.109  8.174   1.00 35.53 ? 154 SER A C   1 
ATOM   1135 O  O   . SER A 1 154 ? 3.988  -2.104  8.879   1.00 35.99 ? 154 SER A O   1 
ATOM   1136 C  CB  . SER A 1 154 ? 5.474  0.309   6.913   1.00 32.30 ? 154 SER A CB  1 
ATOM   1137 O  OG  . SER A 1 154 ? 6.403  -0.727  6.660   1.00 32.41 ? 154 SER A OG  1 
ATOM   1138 N  N   . SER A 1 155 ? 2.802  -1.008  7.297   1.00 37.58 ? 155 SER A N   1 
ATOM   1139 C  CA  . SER A 1 155 ? 1.690  -1.955  7.313   1.00 40.17 ? 155 SER A CA  1 
ATOM   1140 C  C   . SER A 1 155 ? 2.159  -3.384  7.052   1.00 38.81 ? 155 SER A C   1 
ATOM   1141 O  O   . SER A 1 155 ? 1.825  -4.304  7.806   1.00 42.03 ? 155 SER A O   1 
ATOM   1142 C  CB  . SER A 1 155 ? 0.635  -1.535  6.287   1.00 40.12 ? 155 SER A CB  1 
ATOM   1143 O  OG  . SER A 1 155 ? -0.270 -2.594  6.016   1.00 47.20 ? 155 SER A OG  1 
ATOM   1144 N  N   . SER A 1 156 ? 2.951  -3.587  5.996   1.00 40.37 ? 156 SER A N   1 
ATOM   1145 C  CA  . SER A 1 156 ? 3.367  -4.925  5.579   1.00 42.50 ? 156 SER A CA  1 
ATOM   1146 C  C   . SER A 1 156 ? 4.380  -5.570  6.524   1.00 44.39 ? 156 SER A C   1 
ATOM   1147 O  O   . SER A 1 156 ? 4.741  -6.738  6.309   1.00 40.42 ? 156 SER A O   1 
ATOM   1148 C  CB  . SER A 1 156 ? 3.940  -4.874  4.158   1.00 41.86 ? 156 SER A CB  1 
ATOM   1149 O  OG  . SER A 1 156 ? 5.219  -4.258  4.125   1.00 42.85 ? 156 SER A OG  1 
ATOM   1150 N  N   . VAL A 1 157 ? 4.832  -4.861  7.557   1.00 39.72 ? 157 VAL A N   1 
ATOM   1151 C  CA  . VAL A 1 157 ? 5.862  -5.350  8.464   1.00 38.23 ? 157 VAL A CA  1 
ATOM   1152 C  C   . VAL A 1 157 ? 5.286  -5.699  9.833   1.00 38.70 ? 157 VAL A C   1 
ATOM   1153 O  O   . VAL A 1 157 ? 5.626  -6.733  10.411  1.00 37.22 ? 157 VAL A O   1 
ATOM   1154 C  CB  . VAL A 1 157 ? 7.014  -4.330  8.593   1.00 32.37 ? 157 VAL A CB  1 
ATOM   1155 C  CG1 . VAL A 1 157 ? 8.157  -4.927  9.393   1.00 33.41 ? 157 VAL A CG1 1 
ATOM   1156 C  CG2 . VAL A 1 157 ? 7.484  -3.896  7.213   1.00 34.53 ? 157 VAL A CG2 1 
ATOM   1157 N  N   . VAL A 1 158 ? 4.416  -4.841  10.374  1.00 37.04 ? 158 VAL A N   1 
ATOM   1158 C  CA  . VAL A 1 158 ? 3.888  -5.087  11.716  1.00 36.38 ? 158 VAL A CA  1 
ATOM   1159 C  C   . VAL A 1 158 ? 2.725  -6.063  11.730  1.00 40.67 ? 158 VAL A C   1 
ATOM   1160 O  O   . VAL A 1 158 ? 2.344  -6.535  12.807  1.00 41.50 ? 158 VAL A O   1 
ATOM   1161 C  CB  . VAL A 1 158 ? 3.411  -3.795  12.402  1.00 35.88 ? 158 VAL A CB  1 
ATOM   1162 C  CG1 . VAL A 1 158 ? 4.597  -2.914  12.757  1.00 39.30 ? 158 VAL A CG1 1 
ATOM   1163 C  CG2 . VAL A 1 158 ? 2.420  -3.060  11.516  1.00 40.89 ? 158 VAL A CG2 1 
ATOM   1164 N  N   . GLY A 1 159 ? 2.151  -6.376  10.577  1.00 41.40 ? 159 GLY A N   1 
ATOM   1165 C  CA  . GLY A 1 159 ? 0.980  -7.238  10.562  1.00 44.22 ? 159 GLY A CA  1 
ATOM   1166 C  C   . GLY A 1 159 ? -0.153 -6.602  11.346  1.00 43.84 ? 159 GLY A C   1 
ATOM   1167 O  O   . GLY A 1 159 ? -0.609 -5.493  11.036  1.00 46.94 ? 159 GLY A O   1 
ATOM   1168 N  N   . GLU A 1 160 ? -0.605 -7.293  12.393  1.00 43.67 ? 160 GLU A N   1 
ATOM   1169 C  CA  . GLU A 1 160 ? -1.704 -6.827  13.227  1.00 44.65 ? 160 GLU A CA  1 
ATOM   1170 C  C   . GLU A 1 160 ? -1.228 -6.225  14.545  1.00 45.01 ? 160 GLU A C   1 
ATOM   1171 O  O   . GLU A 1 160 ? -2.031 -6.054  15.469  1.00 44.75 ? 160 GLU A O   1 
ATOM   1172 C  CB  . GLU A 1 160 ? -2.684 -7.972  13.495  1.00 47.84 ? 160 GLU A CB  1 
ATOM   1173 N  N   . ASN A 1 161 ? 0.059  -5.897  14.656  1.00 44.57 ? 161 ASN A N   1 
ATOM   1174 C  CA  . ASN A 1 161 ? 0.584  -5.355  15.901  1.00 41.90 ? 161 ASN A CA  1 
ATOM   1175 C  C   . ASN A 1 161 ? 0.581  -3.833  15.950  1.00 42.16 ? 161 ASN A C   1 
ATOM   1176 O  O   . ASN A 1 161 ? 0.736  -3.266  17.038  1.00 45.81 ? 161 ASN A O   1 
ATOM   1177 C  CB  . ASN A 1 161 ? 2.002  -5.881  16.149  1.00 44.15 ? 161 ASN A CB  1 
ATOM   1178 C  CG  . ASN A 1 161 ? 2.056  -7.396  16.202  1.00 44.32 ? 161 ASN A CG  1 
ATOM   1179 O  OD1 . ASN A 1 161 ? 1.274  -8.027  16.912  1.00 47.18 ? 161 ASN A OD1 1 
ATOM   1180 N  ND2 . ASN A 1 161 ? 2.973  -7.989  15.447  1.00 44.57 ? 161 ASN A ND2 1 
ATOM   1181 N  N   . GLY A 1 162 ? 0.413  -3.166  14.816  1.00 43.49 ? 162 GLY A N   1 
ATOM   1182 C  CA  . GLY A 1 162 ? 0.278  -1.718  14.821  1.00 43.27 ? 162 GLY A CA  1 
ATOM   1183 C  C   . GLY A 1 162 ? 1.490  -1.034  15.428  1.00 42.56 ? 162 GLY A C   1 
ATOM   1184 O  O   . GLY A 1 162 ? 2.625  -1.210  14.973  1.00 39.80 ? 162 GLY A O   1 
ATOM   1185 N  N   . ILE A 1 163 ? 1.250  -0.255  16.489  1.00 43.61 ? 163 ILE A N   1 
ATOM   1186 C  CA  . ILE A 1 163 ? 2.292  0.568   17.102  1.00 43.08 ? 163 ILE A CA  1 
ATOM   1187 C  C   . ILE A 1 163 ? 3.078  -0.171  18.176  1.00 37.63 ? 163 ILE A C   1 
ATOM   1188 O  O   . ILE A 1 163 ? 4.089  0.357   18.665  1.00 40.98 ? 163 ILE A O   1 
ATOM   1189 C  CB  . ILE A 1 163 ? 1.656  1.847   17.686  1.00 42.89 ? 163 ILE A CB  1 
ATOM   1190 C  CG1 . ILE A 1 163 ? 2.708  2.926   17.943  1.00 38.04 ? 163 ILE A CG1 1 
ATOM   1191 C  CG2 . ILE A 1 163 ? 0.889  1.527   18.953  1.00 42.91 ? 163 ILE A CG2 1 
ATOM   1192 C  CD1 . ILE A 1 163 ? 3.131  3.655   16.689  1.00 39.63 ? 163 ILE A CD1 1 
ATOM   1193 N  N   . THR A 1 164 ? 2.661  -1.382  18.546  1.00 40.79 ? 164 THR A N   1 
ATOM   1194 C  CA  . THR A 1 164 ? 3.315  -2.091  19.645  1.00 39.75 ? 164 THR A CA  1 
ATOM   1195 C  C   . THR A 1 164 ? 4.807  -2.331  19.425  1.00 39.26 ? 164 THR A C   1 
ATOM   1196 O  O   . THR A 1 164 ? 5.575  -2.155  20.388  1.00 36.17 ? 164 THR A O   1 
ATOM   1197 C  CB  . THR A 1 164 ? 2.584  -3.415  19.907  1.00 44.89 ? 164 THR A CB  1 
ATOM   1198 O  OG1 . THR A 1 164 ? 1.201  -3.150  20.167  1.00 45.20 ? 164 THR A OG1 1 
ATOM   1199 C  CG2 . THR A 1 164 ? 3.189  -4.132  21.105  1.00 45.10 ? 164 THR A CG2 1 
ATOM   1200 N  N   . PRO A 1 165 ? 5.284  -2.720  18.233  1.00 39.39 ? 165 PRO A N   1 
ATOM   1201 C  CA  . PRO A 1 165 ? 6.736  -2.925  18.076  1.00 36.81 ? 165 PRO A CA  1 
ATOM   1202 C  C   . PRO A 1 165 ? 7.580  -1.705  18.415  1.00 34.44 ? 165 PRO A C   1 
ATOM   1203 O  O   . PRO A 1 165 ? 8.651  -1.858  19.017  1.00 37.11 ? 165 PRO A O   1 
ATOM   1204 C  CB  . PRO A 1 165 ? 6.863  -3.320  16.600  1.00 34.98 ? 165 PRO A CB  1 
ATOM   1205 C  CG  . PRO A 1 165 ? 5.552  -3.992  16.304  1.00 36.89 ? 165 PRO A CG  1 
ATOM   1206 C  CD  . PRO A 1 165 ? 4.547  -3.167  17.035  1.00 35.36 ? 165 PRO A CD  1 
ATOM   1207 N  N   . LEU A 1 166 ? 7.129  -0.497  18.064  1.00 34.73 ? 166 LEU A N   1 
ATOM   1208 C  CA  . LEU A 1 166 ? 7.929  0.692   18.349  1.00 33.82 ? 166 LEU A CA  1 
ATOM   1209 C  C   . LEU A 1 166 ? 8.082  0.888   19.850  1.00 35.62 ? 166 LEU A C   1 
ATOM   1210 O  O   . LEU A 1 166 ? 9.186  1.153   20.345  1.00 34.49 ? 166 LEU A O   1 
ATOM   1211 C  CB  . LEU A 1 166 ? 7.304  1.924   17.692  1.00 35.37 ? 166 LEU A CB  1 
ATOM   1212 C  CG  . LEU A 1 166 ? 8.063  3.250   17.825  1.00 32.86 ? 166 LEU A CG  1 
ATOM   1213 C  CD1 . LEU A 1 166 ? 9.487  3.106   17.316  1.00 30.73 ? 166 LEU A CD1 1 
ATOM   1214 C  CD2 . LEU A 1 166 ? 7.349  4.355   17.075  1.00 32.93 ? 166 LEU A CD2 1 
ATOM   1215 N  N   . ALA A 1 167 ? 6.985  0.727   20.598  1.00 35.07 ? 167 ALA A N   1 
ATOM   1216 C  CA  . ALA A 1 167 ? 7.091  0.695   22.053  1.00 36.54 ? 167 ALA A CA  1 
ATOM   1217 C  C   . ALA A 1 167 ? 8.196  -0.260  22.480  1.00 36.30 ? 167 ALA A C   1 
ATOM   1218 O  O   . ALA A 1 167 ? 9.121  0.126   23.207  1.00 37.28 ? 167 ALA A O   1 
ATOM   1219 C  CB  . ALA A 1 167 ? 5.754  0.294   22.681  1.00 33.85 ? 167 ALA A CB  1 
ATOM   1220 N  N   . ARG A 1 168 ? 8.163  -1.493  21.962  1.00 36.75 ? 168 ARG A N   1 
ATOM   1221 C  CA  . ARG A 1 168 ? 9.199  -2.459  22.313  1.00 37.05 ? 168 ARG A CA  1 
ATOM   1222 C  C   . ARG A 1 168 ? 10.576 -1.922  21.950  1.00 35.16 ? 168 ARG A C   1 
ATOM   1223 O  O   . ARG A 1 168 ? 11.501 -1.940  22.775  1.00 34.09 ? 168 ARG A O   1 
ATOM   1224 C  CB  . ARG A 1 168 ? 8.930  -3.793  21.618  1.00 38.79 ? 168 ARG A CB  1 
ATOM   1225 C  CG  . ARG A 1 168 ? 7.811  -4.596  22.261  1.00 47.50 ? 168 ARG A CG  1 
ATOM   1226 C  CD  . ARG A 1 168 ? 8.108  -6.081  22.238  1.00 51.37 ? 168 ARG A CD  1 
ATOM   1227 N  NE  . ARG A 1 168 ? 6.895  -6.869  22.415  1.00 53.26 ? 168 ARG A NE  1 
ATOM   1228 C  CZ  . ARG A 1 168 ? 6.875  -8.176  22.632  1.00 53.35 ? 168 ARG A CZ  1 
ATOM   1229 N  NH1 . ARG A 1 168 ? 7.990  -8.887  22.675  1.00 53.58 ? 168 ARG A NH1 1 
ATOM   1230 N  NH2 . ARG A 1 168 ? 5.706  -8.788  22.798  1.00 52.87 ? 168 ARG A NH2 1 
ATOM   1231 N  N   . ALA A 1 169 ? 10.712 -1.384  20.732  1.00 33.70 ? 169 ALA A N   1 
ATOM   1232 C  CA  . ALA A 1 169 ? 11.997 -0.850  20.300  1.00 34.58 ? 169 ALA A CA  1 
ATOM   1233 C  C   . ALA A 1 169 ? 12.491 0.195   21.289  1.00 32.61 ? 169 ALA A C   1 
ATOM   1234 O  O   . ALA A 1 169 ? 13.658 0.176   21.703  1.00 31.78 ? 169 ALA A O   1 
ATOM   1235 C  CB  . ALA A 1 169 ? 11.884 -0.265  18.889  1.00 27.81 ? 169 ALA A CB  1 
ATOM   1236 N  N   . LYS A 1 170 ? 11.587 1.068   21.740  1.00 35.38 ? 170 LYS A N   1 
ATOM   1237 C  CA  . LYS A 1 170 ? 11.986 2.088   22.702  1.00 33.63 ? 170 LYS A CA  1 
ATOM   1238 C  C   . LYS A 1 170 ? 12.505 1.442   23.976  1.00 34.09 ? 170 LYS A C   1 
ATOM   1239 O  O   . LYS A 1 170 ? 13.607 1.761   24.442  1.00 38.32 ? 170 LYS A O   1 
ATOM   1240 C  CB  . LYS A 1 170 ? 10.819 3.028   22.997  1.00 35.68 ? 170 LYS A CB  1 
ATOM   1241 C  CG  . LYS A 1 170 ? 10.418 3.894   21.809  1.00 32.85 ? 170 LYS A CG  1 
ATOM   1242 C  CD  . LYS A 1 170 ? 11.532 4.882   21.438  1.00 31.54 ? 170 LYS A CD  1 
ATOM   1243 C  CE  . LYS A 1 170 ? 11.838 5.849   22.574  1.00 35.88 ? 170 LYS A CE  1 
ATOM   1244 N  NZ  . LYS A 1 170 ? 12.923 6.808   22.198  1.00 33.24 ? 170 LYS A NZ  1 
ATOM   1245 N  N   . THR A 1 171 ? 11.741 0.495   24.527  1.00 36.42 ? 171 THR A N   1 
ATOM   1246 C  CA  . THR A 1 171 ? 12.200 -0.226  25.709  1.00 34.35 ? 171 THR A CA  1 
ATOM   1247 C  C   . THR A 1 171 ? 13.567 -0.826  25.439  1.00 36.89 ? 171 THR A C   1 
ATOM   1248 O  O   . THR A 1 171 ? 14.513 -0.659  26.220  1.00 34.76 ? 171 THR A O   1 
ATOM   1249 C  CB  . THR A 1 171 ? 11.190 -1.314  26.075  1.00 37.52 ? 171 THR A CB  1 
ATOM   1250 O  OG1 . THR A 1 171 ? 9.978  -0.705  26.533  1.00 37.24 ? 171 THR A OG1 1 
ATOM   1251 C  CG2 . THR A 1 171 ? 11.744 -2.214  27.177  1.00 37.06 ? 171 THR A CG2 1 
ATOM   1252 N  N   . MET A 1 172 ? 13.703 -1.443  24.267  1.00 35.91 ? 172 MET A N   1 
ATOM   1253 C  CA  . MET A 1 172 ? 14.951 -2.075  23.875  1.00 33.69 ? 172 MET A CA  1 
ATOM   1254 C  C   . MET A 1 172 ? 16.081 -1.059  23.860  1.00 33.81 ? 172 MET A C   1 
ATOM   1255 O  O   . MET A 1 172 ? 17.175 -1.310  24.387  1.00 32.21 ? 172 MET A O   1 
ATOM   1256 C  CB  . MET A 1 172 ? 14.728 -2.702  22.504  1.00 34.86 ? 172 MET A CB  1 
ATOM   1257 C  CG  . MET A 1 172 ? 14.509 -4.190  22.530  1.00 34.65 ? 172 MET A CG  1 
ATOM   1258 S  SD  . MET A 1 172 ? 13.777 -4.596  20.946  1.00 35.69 ? 172 MET A SD  1 
ATOM   1259 C  CE  . MET A 1 172 ? 15.234 -5.094  20.113  1.00 35.54 ? 172 MET A CE  1 
ATOM   1260 N  N   . GLN A 1 173 ? 15.809 0.117   23.290  1.00 33.48 ? 173 GLN A N   1 
ATOM   1261 C  CA  . GLN A 1 173 ? 16.773 1.204   23.317  1.00 30.88 ? 173 GLN A CA  1 
ATOM   1262 C  C   . GLN A 1 173 ? 17.270 1.458   24.731  1.00 35.87 ? 173 GLN A C   1 
ATOM   1263 O  O   . GLN A 1 173 ? 18.482 1.453   24.992  1.00 33.32 ? 173 GLN A O   1 
ATOM   1264 C  CB  . GLN A 1 173 ? 16.130 2.464   22.757  1.00 32.74 ? 173 GLN A CB  1 
ATOM   1265 C  CG  . GLN A 1 173 ? 17.051 3.638   22.701  1.00 33.12 ? 173 GLN A CG  1 
ATOM   1266 C  CD  . GLN A 1 173 ? 16.407 4.794   21.996  1.00 35.28 ? 173 GLN A CD  1 
ATOM   1267 O  OE1 . GLN A 1 173 ? 15.258 5.136   22.281  1.00 34.13 ? 173 GLN A OE1 1 
ATOM   1268 N  NE2 . GLN A 1 173 ? 17.124 5.392   21.051  1.00 33.65 ? 173 GLN A NE2 1 
ATOM   1269 N  N   . GLN A 1 174 ? 16.329 1.649   25.667  1.00 32.99 ? 174 GLN A N   1 
ATOM   1270 C  CA  . GLN A 1 174 ? 16.700 1.956   27.043  1.00 37.29 ? 174 GLN A CA  1 
ATOM   1271 C  C   . GLN A 1 174 ? 17.597 0.882   27.629  1.00 36.38 ? 174 GLN A C   1 
ATOM   1272 O  O   . GLN A 1 174 ? 18.523 1.191   28.390  1.00 36.17 ? 174 GLN A O   1 
ATOM   1273 C  CB  . GLN A 1 174 ? 15.447 2.115   27.906  1.00 35.99 ? 174 GLN A CB  1 
ATOM   1274 C  CG  . GLN A 1 174 ? 14.791 3.478   27.791  1.00 43.03 ? 174 GLN A CG  1 
ATOM   1275 C  CD  . GLN A 1 174 ? 15.756 4.615   28.076  1.00 41.98 ? 174 GLN A CD  1 
ATOM   1276 O  OE1 . GLN A 1 174 ? 16.125 5.373   27.176  1.00 43.41 ? 174 GLN A OE1 1 
ATOM   1277 N  NE2 . GLN A 1 174 ? 16.160 4.747   29.332  1.00 39.80 ? 174 GLN A NE2 1 
ATOM   1278 N  N   . GLU A 1 175 ? 17.364 -0.376  27.266  1.00 36.52 ? 175 GLU A N   1 
ATOM   1279 C  CA  . GLU A 1 175 ? 18.101 -1.450  27.907  1.00 34.81 ? 175 GLU A CA  1 
ATOM   1280 C  C   . GLU A 1 175 ? 19.500 -1.624  27.341  1.00 37.51 ? 175 GLU A C   1 
ATOM   1281 O  O   . GLU A 1 175 ? 20.263 -2.440  27.872  1.00 36.23 ? 175 GLU A O   1 
ATOM   1282 C  CB  . GLU A 1 175 ? 17.327 -2.761  27.784  1.00 37.60 ? 175 GLU A CB  1 
ATOM   1283 C  CG  . GLU A 1 175 ? 15.929 -2.706  28.363  1.00 34.97 ? 175 GLU A CG  1 
ATOM   1284 C  CD  . GLU A 1 175 ? 15.218 -4.039  28.257  1.00 44.49 ? 175 GLU A CD  1 
ATOM   1285 O  OE1 . GLU A 1 175 ? 15.808 -4.982  27.687  1.00 46.72 ? 175 GLU A OE1 1 
ATOM   1286 O  OE2 . GLU A 1 175 ? 14.073 -4.147  28.741  1.00 43.20 ? 175 GLU A OE2 1 
ATOM   1287 N  N   . ASN A 1 176 ? 19.866 -0.881  26.293  1.00 35.37 ? 176 ASN A N   1 
ATOM   1288 C  CA  . ASN A 1 176 ? 21.165 -1.070  25.654  1.00 33.27 ? 176 ASN A CA  1 
ATOM   1289 C  C   . ASN A 1 176 ? 21.882 0.274   25.519  1.00 35.39 ? 176 ASN A C   1 
ATOM   1290 O  O   . ASN A 1 176 ? 22.263 0.703   24.430  1.00 37.92 ? 176 ASN A O   1 
ATOM   1291 C  CB  . ASN A 1 176 ? 21.000 -1.768  24.306  1.00 34.65 ? 176 ASN A CB  1 
ATOM   1292 C  CG  . ASN A 1 176 ? 20.487 -3.187  24.453  1.00 36.42 ? 176 ASN A CG  1 
ATOM   1293 O  OD1 . ASN A 1 176 ? 21.267 -4.137  24.511  1.00 38.91 ? 176 ASN A OD1 1 
ATOM   1294 N  ND2 . ASN A 1 176 ? 19.166 -3.340  24.510  1.00 37.27 ? 176 ASN A ND2 1 
ATOM   1295 N  N   . GLY A 1 177 ? 22.072 0.944   26.653  1.00 36.74 ? 177 GLY A N   1 
ATOM   1296 C  CA  . GLY A 1 177 ? 22.856 2.167   26.672  1.00 37.37 ? 177 GLY A CA  1 
ATOM   1297 C  C   . GLY A 1 177 ? 22.325 3.264   25.779  1.00 34.49 ? 177 GLY A C   1 
ATOM   1298 O  O   . GLY A 1 177 ? 23.104 4.096   25.304  1.00 36.52 ? 177 GLY A O   1 
ATOM   1299 N  N   . ASP A 1 178 ? 21.013 3.285   25.531  1.00 34.29 ? 178 ASP A N   1 
ATOM   1300 C  CA  . ASP A 1 178 ? 20.367 4.350   24.758  1.00 36.28 ? 178 ASP A CA  1 
ATOM   1301 C  C   . ASP A 1 178 ? 20.946 4.458   23.350  1.00 35.04 ? 178 ASP A C   1 
ATOM   1302 O  O   . ASP A 1 178 ? 21.223 5.552   22.849  1.00 32.36 ? 178 ASP A O   1 
ATOM   1303 C  CB  . ASP A 1 178 ? 20.455 5.691   25.490  1.00 40.59 ? 178 ASP A CB  1 
ATOM   1304 C  CG  . ASP A 1 178 ? 19.266 5.937   26.384  1.00 39.54 ? 178 ASP A CG  1 
ATOM   1305 O  OD1 . ASP A 1 178 ? 18.274 6.525   25.901  1.00 48.55 ? 178 ASP A OD1 1 
ATOM   1306 O  OD2 . ASP A 1 178 ? 19.311 5.525   27.560  1.00 47.13 ? 178 ASP A OD2 1 
ATOM   1307 N  N   . LEU A 1 179 ? 21.124 3.303   22.711  1.00 33.63 ? 179 LEU A N   1 
ATOM   1308 C  CA  . LEU A 1 179 ? 21.564 3.267   21.326  1.00 32.78 ? 179 LEU A CA  1 
ATOM   1309 C  C   . LEU A 1 179 ? 20.602 4.057   20.440  1.00 29.72 ? 179 LEU A C   1 
ATOM   1310 O  O   . LEU A 1 179 ? 19.393 4.083   20.692  1.00 29.68 ? 179 LEU A O   1 
ATOM   1311 C  CB  . LEU A 1 179 ? 21.633 1.827   20.822  1.00 31.41 ? 179 LEU A CB  1 
ATOM   1312 C  CG  . LEU A 1 179 ? 22.801 0.933   21.209  1.00 31.14 ? 179 LEU A CG  1 
ATOM   1313 C  CD1 . LEU A 1 179 ? 22.435 -0.499  20.862  1.00 28.96 ? 179 LEU A CD1 1 
ATOM   1314 C  CD2 . LEU A 1 179 ? 24.067 1.362   20.491  1.00 33.27 ? 179 LEU A CD2 1 
ATOM   1315 N  N   . PRO A 1 180 ? 21.111 4.702   19.390  1.00 27.39 ? 180 PRO A N   1 
ATOM   1316 C  CA  . PRO A 1 180 ? 20.219 5.330   18.410  1.00 26.74 ? 180 PRO A CA  1 
ATOM   1317 C  C   . PRO A 1 180 ? 19.244 4.320   17.822  1.00 26.53 ? 180 PRO A C   1 
ATOM   1318 O  O   . PRO A 1 180 ? 19.555 3.137   17.677  1.00 24.75 ? 180 PRO A O   1 
ATOM   1319 C  CB  . PRO A 1 180 ? 21.183 5.862   17.342  1.00 26.48 ? 180 PRO A CB  1 
ATOM   1320 C  CG  . PRO A 1 180 ? 22.481 6.024   18.062  1.00 26.55 ? 180 PRO A CG  1 
ATOM   1321 C  CD  . PRO A 1 180 ? 22.530 4.904   19.057  1.00 30.51 ? 180 PRO A CD  1 
ATOM   1322 N  N   . LEU A 1 181 ? 18.046 4.800   17.500  1.00 24.69 ? 181 LEU A N   1 
ATOM   1323 C  CA  . LEU A 1 181 ? 16.989 3.977   16.925  1.00 22.21 ? 181 LEU A CA  1 
ATOM   1324 C  C   . LEU A 1 181 ? 16.554 4.579   15.598  1.00 23.43 ? 181 LEU A C   1 
ATOM   1325 O  O   . LEU A 1 181 ? 16.135 5.741   15.554  1.00 23.84 ? 181 LEU A O   1 
ATOM   1326 C  CB  . LEU A 1 181 ? 15.795 3.881   17.868  1.00 23.48 ? 181 LEU A CB  1 
ATOM   1327 C  CG  . LEU A 1 181 ? 14.532 3.295   17.236  1.00 21.62 ? 181 LEU A CG  1 
ATOM   1328 C  CD1 . LEU A 1 181 ? 14.691 1.810   16.984  1.00 22.60 ? 181 LEU A CD1 1 
ATOM   1329 C  CD2 . LEU A 1 181 ? 13.315 3.572   18.117  1.00 23.36 ? 181 LEU A CD2 1 
ATOM   1330 N  N   . MET A 1 182 ? 16.630 3.784   14.533  1.00 20.26 ? 182 MET A N   1 
ATOM   1331 C  CA  . MET A 1 182 ? 16.165 4.183   13.209  1.00 22.13 ? 182 MET A CA  1 
ATOM   1332 C  C   . MET A 1 182 ? 14.800 3.565   12.934  1.00 20.57 ? 182 MET A C   1 
ATOM   1333 O  O   . MET A 1 182 ? 14.620 2.350   13.061  1.00 23.96 ? 182 MET A O   1 
ATOM   1334 C  CB  . MET A 1 182 ? 17.159 3.774   12.124  1.00 18.88 ? 182 MET A CB  1 
ATOM   1335 C  CG  . MET A 1 182 ? 16.703 4.149   10.737  1.00 22.17 ? 182 MET A CG  1 
ATOM   1336 S  SD  . MET A 1 182 ? 17.891 3.753   9.440   1.00 23.25 ? 182 MET A SD  1 
ATOM   1337 C  CE  . MET A 1 182 ? 18.926 5.203   9.537   1.00 22.32 ? 182 MET A CE  1 
ATOM   1338 N  N   . VAL A 1 183 ? 13.845 4.409   12.563  1.00 19.57 ? 183 VAL A N   1 
ATOM   1339 C  CA  . VAL A 1 183 ? 12.459 4.021   12.352  1.00 22.27 ? 183 VAL A CA  1 
ATOM   1340 C  C   . VAL A 1 183 ? 12.145 4.266   10.887  1.00 22.27 ? 183 VAL A C   1 
ATOM   1341 O  O   . VAL A 1 183 ? 12.272 5.396   10.403  1.00 21.11 ? 183 VAL A O   1 
ATOM   1342 C  CB  . VAL A 1 183 ? 11.506 4.816   13.257  1.00 22.42 ? 183 VAL A CB  1 
ATOM   1343 C  CG1 . VAL A 1 183 ? 10.074 4.352   13.059  1.00 23.09 ? 183 VAL A CG1 1 
ATOM   1344 C  CG2 . VAL A 1 183 ? 11.940 4.685   14.718  1.00 25.22 ? 183 VAL A CG2 1 
ATOM   1345 N  N   . HIS A 1 184 ? 11.761 3.211   10.184  1.00 21.78 ? 184 HIS A N   1 
ATOM   1346 C  CA  . HIS A 1 184 ? 11.305 3.325   8.810   1.00 24.87 ? 184 HIS A CA  1 
ATOM   1347 C  C   . HIS A 1 184 ? 9.817  3.662   8.802   1.00 25.86 ? 184 HIS A C   1 
ATOM   1348 O  O   . HIS A 1 184 ? 9.051  3.176   9.644   1.00 22.66 ? 184 HIS A O   1 
ATOM   1349 C  CB  . HIS A 1 184 ? 11.641 2.021   8.060   1.00 22.91 ? 184 HIS A CB  1 
ATOM   1350 C  CG  . HIS A 1 184 ? 10.538 1.437   7.227   1.00 23.78 ? 184 HIS A CG  1 
ATOM   1351 N  ND1 . HIS A 1 184 ? 10.773 0.940   5.964   1.00 22.99 ? 184 HIS A ND1 1 
ATOM   1352 C  CD2 . HIS A 1 184 ? 9.235  1.172   7.493   1.00 26.41 ? 184 HIS A CD2 1 
ATOM   1353 C  CE1 . HIS A 1 184 ? 9.654  0.449   5.466   1.00 25.18 ? 184 HIS A CE1 1 
ATOM   1354 N  NE2 . HIS A 1 184 ? 8.704  0.578   6.374   1.00 26.19 ? 184 HIS A NE2 1 
ATOM   1355 N  N   . ILE A 1 185 ? 9.418  4.523   7.864   1.00 21.96 ? 185 ILE A N   1 
ATOM   1356 C  CA  . ILE A 1 185 ? 8.025  4.906   7.679   1.00 24.78 ? 185 ILE A CA  1 
ATOM   1357 C  C   . ILE A 1 185 ? 7.652  4.728   6.212   1.00 28.15 ? 185 ILE A C   1 
ATOM   1358 O  O   . ILE A 1 185 ? 8.505  4.723   5.320   1.00 21.55 ? 185 ILE A O   1 
ATOM   1359 C  CB  . ILE A 1 185 ? 7.748  6.359   8.135   1.00 25.57 ? 185 ILE A CB  1 
ATOM   1360 C  CG1 . ILE A 1 185 ? 8.631  7.339   7.353   1.00 24.07 ? 185 ILE A CG1 1 
ATOM   1361 C  CG2 . ILE A 1 185 ? 7.962  6.503   9.635   1.00 25.73 ? 185 ILE A CG2 1 
ATOM   1362 C  CD1 . ILE A 1 185 ? 8.150  8.791   7.391   1.00 23.64 ? 185 ILE A CD1 1 
ATOM   1363 N  N   . GLY A 1 186 ? 6.351  4.580   5.973   1.00 29.64 ? 186 GLY A N   1 
ATOM   1364 C  CA  . GLY A 1 186 ? 5.839  4.418   4.627   1.00 32.20 ? 186 GLY A CA  1 
ATOM   1365 C  C   . GLY A 1 186 ? 4.330  4.304   4.587   1.00 31.97 ? 186 GLY A C   1 
ATOM   1366 O  O   . GLY A 1 186 ? 3.621  5.315   4.551   1.00 33.27 ? 186 GLY A O   1 
ATOM   1367 N  N   . ASN A 1 187 ? 3.823  3.079   4.600   1.00 32.31 ? 187 ASN A N   1 
ATOM   1368 C  CA  . ASN A 1 187 ? 2.389  2.849   4.563   1.00 31.60 ? 187 ASN A CA  1 
ATOM   1369 C  C   . ASN A 1 187 ? 1.835  2.728   5.981   1.00 37.66 ? 187 ASN A C   1 
ATOM   1370 O  O   . ASN A 1 187 ? 2.524  2.282   6.904   1.00 34.42 ? 187 ASN A O   1 
ATOM   1371 C  CB  . ASN A 1 187 ? 2.076  1.581   3.771   1.00 37.31 ? 187 ASN A CB  1 
ATOM   1372 C  CG  . ASN A 1 187 ? 2.070  1.819   2.271   1.00 38.80 ? 187 ASN A CG  1 
ATOM   1373 O  OD1 . ASN A 1 187 ? 1.413  2.734   1.774   1.00 40.29 ? 187 ASN A OD1 1 
ATOM   1374 N  ND2 . ASN A 1 187 ? 2.811  0.991   1.542   1.00 39.61 ? 187 ASN A ND2 1 
ATOM   1375 N  N   . ASN A 1 188 ? 0.580  3.130   6.143   1.00 36.06 ? 188 ASN A N   1 
ATOM   1376 C  CA  . ASN A 1 188 ? -0.141 3.011   7.400   1.00 39.30 ? 188 ASN A CA  1 
ATOM   1377 C  C   . ASN A 1 188 ? -1.121 1.850   7.326   1.00 41.72 ? 188 ASN A C   1 
ATOM   1378 O  O   . ASN A 1 188 ? -1.490 1.410   6.233   1.00 40.14 ? 188 ASN A O   1 
ATOM   1379 C  CB  . ASN A 1 188 ? -0.892 4.314   7.702   1.00 39.82 ? 188 ASN A CB  1 
ATOM   1380 C  CG  . ASN A 1 188 ? -1.920 4.650   6.641   1.00 43.28 ? 188 ASN A CG  1 
ATOM   1381 O  OD1 . ASN A 1 188 ? -1.617 4.669   5.444   1.00 40.06 ? 188 ASN A OD1 1 
ATOM   1382 N  ND2 . ASN A 1 188 ? -3.144 4.920   7.073   1.00 47.28 ? 188 ASN A ND2 1 
ATOM   1383 N  N   . PRO A 1 189 ? -1.560 1.301   8.470   1.00 41.61 ? 189 PRO A N   1 
ATOM   1384 C  CA  . PRO A 1 189 ? -1.199 1.621   9.862   1.00 41.18 ? 189 PRO A CA  1 
ATOM   1385 C  C   . PRO A 1 189 ? 0.189  1.106   10.228  1.00 41.79 ? 189 PRO A C   1 
ATOM   1386 O  O   . PRO A 1 189 ? 0.722  0.239   9.542   1.00 44.40 ? 189 PRO A O   1 
ATOM   1387 C  CB  . PRO A 1 189 ? -2.301 0.920   10.668  1.00 42.16 ? 189 PRO A CB  1 
ATOM   1388 C  CG  . PRO A 1 189 ? -2.676 -0.252  9.819   1.00 46.85 ? 189 PRO A CG  1 
ATOM   1389 C  CD  . PRO A 1 189 ? -2.613 0.270   8.411   1.00 44.59 ? 189 PRO A CD  1 
ATOM   1390 N  N   . PRO A 1 190 ? 0.814  1.624   11.297  1.00 42.76 ? 190 PRO A N   1 
ATOM   1391 C  CA  . PRO A 1 190 ? 0.339  2.693   12.187  1.00 44.30 ? 190 PRO A CA  1 
ATOM   1392 C  C   . PRO A 1 190 ? 0.374  4.053   11.502  1.00 41.87 ? 190 PRO A C   1 
ATOM   1393 O  O   . PRO A 1 190 ? 0.936  4.207   10.419  1.00 39.07 ? 190 PRO A O   1 
ATOM   1394 C  CB  . PRO A 1 190 ? 1.317  2.621   13.370  1.00 40.99 ? 190 PRO A CB  1 
ATOM   1395 C  CG  . PRO A 1 190 ? 2.579  2.066   12.772  1.00 40.92 ? 190 PRO A CG  1 
ATOM   1396 C  CD  . PRO A 1 190 ? 2.118  1.088   11.729  1.00 40.23 ? 190 PRO A CD  1 
ATOM   1397 N  N   . ASN A 1 191 ? -0.234 5.058   12.122  1.00 40.66 ? 191 ASN A N   1 
ATOM   1398 C  CA  . ASN A 1 191 ? -0.225 6.403   11.578  1.00 41.31 ? 191 ASN A CA  1 
ATOM   1399 C  C   . ASN A 1 191 ? 1.072  7.118   11.956  1.00 37.54 ? 191 ASN A C   1 
ATOM   1400 O  O   . ASN A 1 191 ? 1.725  6.782   12.948  1.00 37.38 ? 191 ASN A O   1 
ATOM   1401 C  CB  . ASN A 1 191 ? -1.427 7.192   12.095  1.00 40.13 ? 191 ASN A CB  1 
ATOM   1402 C  CG  . ASN A 1 191 ? -2.076 8.021   11.017  1.00 47.75 ? 191 ASN A CG  1 
ATOM   1403 O  OD1 . ASN A 1 191 ? -2.763 7.491   10.140  1.00 48.59 ? 191 ASN A OD1 1 
ATOM   1404 N  ND2 . ASN A 1 191 ? -1.827 9.325   11.045  1.00 49.60 ? 191 ASN A ND2 1 
ATOM   1405 N  N   . LEU A 1 192 ? 1.439  8.122   11.149  1.00 37.31 ? 192 LEU A N   1 
ATOM   1406 C  CA  . LEU A 1 192 ? 2.652  8.892   11.424  1.00 37.57 ? 192 LEU A CA  1 
ATOM   1407 C  C   . LEU A 1 192 ? 2.590  9.597   12.772  1.00 38.21 ? 192 LEU A C   1 
ATOM   1408 O  O   . LEU A 1 192 ? 3.618  9.733   13.446  1.00 35.10 ? 192 LEU A O   1 
ATOM   1409 C  CB  . LEU A 1 192 ? 2.902  9.928   10.324  1.00 36.46 ? 192 LEU A CB  1 
ATOM   1410 C  CG  . LEU A 1 192 ? 4.250  10.661  10.426  1.00 33.96 ? 192 LEU A CG  1 
ATOM   1411 C  CD1 . LEU A 1 192 ? 5.430  9.693   10.488  1.00 31.82 ? 192 LEU A CD1 1 
ATOM   1412 C  CD2 . LEU A 1 192 ? 4.440  11.679  9.310   1.00 32.61 ? 192 LEU A CD2 1 
ATOM   1413 N  N   . ASP A 1 193 ? 1.408  10.069  13.173  1.00 37.05 ? 193 ASP A N   1 
ATOM   1414 C  CA  . ASP A 1 193 ? 1.291  10.761  14.452  1.00 39.12 ? 193 ASP A CA  1 
ATOM   1415 C  C   . ASP A 1 193 ? 1.693  9.846   15.601  1.00 37.58 ? 193 ASP A C   1 
ATOM   1416 O  O   . ASP A 1 193 ? 2.504  10.221  16.458  1.00 37.48 ? 193 ASP A O   1 
ATOM   1417 C  CB  . ASP A 1 193 ? -0.139 11.274  14.640  1.00 40.71 ? 193 ASP A CB  1 
ATOM   1418 N  N   . GLU A 1 194 ? 1.141  8.627   15.621  1.00 37.56 ? 194 GLU A N   1 
ATOM   1419 C  CA  . GLU A 1 194 ? 1.430  7.696   16.706  1.00 37.48 ? 194 GLU A CA  1 
ATOM   1420 C  C   . GLU A 1 194 ? 2.908  7.332   16.742  1.00 36.82 ? 194 GLU A C   1 
ATOM   1421 O  O   . GLU A 1 194 ? 3.505  7.242   17.821  1.00 37.29 ? 194 GLU A O   1 
ATOM   1422 C  CB  . GLU A 1 194 ? 0.570  6.440   16.561  1.00 36.81 ? 194 GLU A CB  1 
ATOM   1423 N  N   . ILE A 1 195 ? 3.516  7.133   15.568  1.00 38.57 ? 195 ILE A N   1 
ATOM   1424 C  CA  . ILE A 1 195 ? 4.934  6.787   15.502  1.00 35.73 ? 195 ILE A CA  1 
ATOM   1425 C  C   . ILE A 1 195 ? 5.787  7.928   16.030  1.00 32.44 ? 195 ILE A C   1 
ATOM   1426 O  O   . ILE A 1 195 ? 6.640  7.733   16.904  1.00 33.92 ? 195 ILE A O   1 
ATOM   1427 C  CB  . ILE A 1 195 ? 5.337  6.429   14.061  1.00 33.14 ? 195 ILE A CB  1 
ATOM   1428 C  CG1 . ILE A 1 195 ? 4.651  5.147   13.600  1.00 36.80 ? 195 ILE A CG1 1 
ATOM   1429 C  CG2 . ILE A 1 195 ? 6.856  6.313   13.953  1.00 31.48 ? 195 ILE A CG2 1 
ATOM   1430 C  CD1 . ILE A 1 195 ? 4.924  4.816   12.144  1.00 33.70 ? 195 ILE A CD1 1 
ATOM   1431 N  N   . ALA A 1 196 ? 5.573  9.135   15.499  1.00 32.85 ? 196 ALA A N   1 
ATOM   1432 C  CA  . ALA A 1 196 ? 6.401  10.278  15.862  1.00 31.84 ? 196 ALA A CA  1 
ATOM   1433 C  C   . ALA A 1 196 ? 6.231  10.669  17.323  1.00 34.04 ? 196 ALA A C   1 
ATOM   1434 O  O   . ALA A 1 196 ? 7.169  11.195  17.930  1.00 32.77 ? 196 ALA A O   1 
ATOM   1435 C  CB  . ALA A 1 196 ? 6.080  11.468  14.959  1.00 32.28 ? 196 ALA A CB  1 
ATOM   1436 N  N   . GLU A 1 197 ? 5.057  10.426  17.910  1.00 32.39 ? 197 GLU A N   1 
ATOM   1437 C  CA  . GLU A 1 197 ? 4.877  10.796  19.309  1.00 36.44 ? 197 GLU A CA  1 
ATOM   1438 C  C   . GLU A 1 197 ? 5.776  9.979   20.231  1.00 36.08 ? 197 GLU A C   1 
ATOM   1439 O  O   . GLU A 1 197 ? 6.139  10.449  21.317  1.00 37.83 ? 197 GLU A O   1 
ATOM   1440 C  CB  . GLU A 1 197 ? 3.409  10.641  19.707  1.00 39.42 ? 197 GLU A CB  1 
ATOM   1441 C  CG  . GLU A 1 197 ? 2.976  11.591  20.816  1.00 49.65 ? 197 GLU A CG  1 
ATOM   1442 C  CD  . GLU A 1 197 ? 3.108  13.055  20.419  1.00 52.84 ? 197 GLU A CD  1 
ATOM   1443 O  OE1 . GLU A 1 197 ? 2.722  13.396  19.278  1.00 47.43 ? 197 GLU A OE1 1 
ATOM   1444 O  OE2 . GLU A 1 197 ? 3.599  13.860  21.246  1.00 54.76 ? 197 GLU A OE2 1 
ATOM   1445 N  N   . LEU A 1 198 ? 6.159  8.770   19.814  1.00 34.77 ? 198 LEU A N   1 
ATOM   1446 C  CA  . LEU A 1 198 ? 6.996  7.900   20.630  1.00 33.34 ? 198 LEU A CA  1 
ATOM   1447 C  C   . LEU A 1 198 ? 8.483  8.209   20.524  1.00 33.27 ? 198 LEU A C   1 
ATOM   1448 O  O   . LEU A 1 198 ? 9.265  7.626   21.281  1.00 33.78 ? 198 LEU A O   1 
ATOM   1449 C  CB  . LEU A 1 198 ? 6.764  6.435   20.248  1.00 34.18 ? 198 LEU A CB  1 
ATOM   1450 C  CG  . LEU A 1 198 ? 5.434  5.840   20.706  1.00 35.05 ? 198 LEU A CG  1 
ATOM   1451 C  CD1 . LEU A 1 198 ? 5.426  4.324   20.566  1.00 35.70 ? 198 LEU A CD1 1 
ATOM   1452 C  CD2 . LEU A 1 198 ? 5.172  6.254   22.143  1.00 36.80 ? 198 LEU A CD2 1 
ATOM   1453 N  N   . LEU A 1 199 ? 8.892  9.095   19.618  1.00 31.90 ? 199 LEU A N   1 
ATOM   1454 C  CA  . LEU A 1 199 ? 10.301 9.324   19.327  1.00 31.25 ? 199 LEU A CA  1 
ATOM   1455 C  C   . LEU A 1 199 ? 10.823 10.551  20.069  1.00 30.53 ? 199 LEU A C   1 
ATOM   1456 O  O   . LEU A 1 199 ? 10.066 11.444  20.457  1.00 34.62 ? 199 LEU A O   1 
ATOM   1457 C  CB  . LEU A 1 199 ? 10.520 9.490   17.819  1.00 30.45 ? 199 LEU A CB  1 
ATOM   1458 C  CG  . LEU A 1 199 ? 9.995  8.335   16.960  1.00 27.99 ? 199 LEU A CG  1 
ATOM   1459 C  CD1 . LEU A 1 199 ? 10.305 8.560   15.482  1.00 22.88 ? 199 LEU A CD1 1 
ATOM   1460 C  CD2 . LEU A 1 199 ? 10.557 7.004   17.440  1.00 28.26 ? 199 LEU A CD2 1 
ATOM   1461 N  N   . SER A 1 200 ? 12.138 10.581  20.269  1.00 30.42 ? 200 SER A N   1 
ATOM   1462 C  CA  . SER A 1 200 ? 12.773 11.665  21.011  1.00 30.75 ? 200 SER A CA  1 
ATOM   1463 C  C   . SER A 1 200 ? 14.198 11.838  20.495  1.00 30.87 ? 200 SER A C   1 
ATOM   1464 O  O   . SER A 1 200 ? 14.604 11.206  19.515  1.00 29.57 ? 200 SER A O   1 
ATOM   1465 C  CB  . SER A 1 200 ? 12.732 11.380  22.516  1.00 34.86 ? 200 SER A CB  1 
ATOM   1466 O  OG  . SER A 1 200 ? 13.583 10.294  22.828  1.00 38.78 ? 200 SER A OG  1 
ATOM   1467 N  N   . ARG A 1 201 ? 14.965 12.692  21.171  1.00 28.52 ? 201 ARG A N   1 
ATOM   1468 C  CA  . ARG A 1 201 ? 16.329 13.025  20.749  1.00 27.70 ? 201 ARG A CA  1 
ATOM   1469 C  C   . ARG A 1 201 ? 17.195 11.784  20.509  1.00 29.54 ? 201 ARG A C   1 
ATOM   1470 O  O   . ARG A 1 201 ? 17.200 10.862  21.325  1.00 31.44 ? 201 ARG A O   1 
ATOM   1471 C  CB  . ARG A 1 201 ? 16.997 13.924  21.792  1.00 31.61 ? 201 ARG A CB  1 
ATOM   1472 N  N   . ASP A 1 203 ? 16.752 9.572   18.052  1.00 24.42 ? 203 ASP A N   1 
ATOM   1473 C  CA  . ASP A 1 203 ? 15.934 8.753   17.175  1.00 24.66 ? 203 ASP A CA  1 
ATOM   1474 C  C   . ASP A 1 203 ? 15.926 9.361   15.773  1.00 24.51 ? 203 ASP A C   1 
ATOM   1475 O  O   . ASP A 1 203 ? 15.960 10.583  15.614  1.00 25.35 ? 203 ASP A O   1 
ATOM   1476 C  CB  . ASP A 1 203 ? 14.507 8.635   17.709  1.00 25.27 ? 203 ASP A CB  1 
ATOM   1477 C  CG  . ASP A 1 203 ? 14.445 7.963   19.074  1.00 30.28 ? 203 ASP A CG  1 
ATOM   1478 O  OD1 . ASP A 1 203 ? 15.415 7.281   19.462  1.00 29.91 ? 203 ASP A OD1 1 
ATOM   1479 O  OD2 . ASP A 1 203 ? 13.412 8.108   19.754  1.00 27.63 ? 203 ASP A OD2 1 
ATOM   1480 N  N   . ILE A 1 204 ? 15.862 8.502   14.758  1.00 22.74 ? 204 ILE A N   1 
ATOM   1481 C  CA  . ILE A 1 204 ? 16.008 8.900   13.364  1.00 22.37 ? 204 ILE A CA  1 
ATOM   1482 C  C   . ILE A 1 204 ? 14.855 8.309   12.569  1.00 22.16 ? 204 ILE A C   1 
ATOM   1483 O  O   . ILE A 1 204 ? 14.687 7.088   12.544  1.00 19.28 ? 204 ILE A O   1 
ATOM   1484 C  CB  . ILE A 1 204 ? 17.340 8.411   12.772  1.00 25.81 ? 204 ILE A CB  1 
ATOM   1485 C  CG1 . ILE A 1 204 ? 18.530 8.938   13.582  1.00 24.67 ? 204 ILE A CG1 1 
ATOM   1486 C  CG2 . ILE A 1 204 ? 17.418 8.724   11.280  1.00 23.79 ? 204 ILE A CG2 1 
ATOM   1487 C  CD1 . ILE A 1 204 ? 19.763 8.064   13.473  1.00 23.11 ? 204 ILE A CD1 1 
ATOM   1488 N  N   . ILE A 1 205 ? 14.103 9.156   11.876  1.00 19.12 ? 205 ILE A N   1 
ATOM   1489 C  CA  . ILE A 1 205 ? 13.099 8.687   10.930  1.00 21.27 ? 205 ILE A CA  1 
ATOM   1490 C  C   . ILE A 1 205 ? 13.745 8.617   9.557   1.00 19.93 ? 205 ILE A C   1 
ATOM   1491 O  O   . ILE A 1 205 ? 14.190 9.638   9.021   1.00 20.85 ? 205 ILE A O   1 
ATOM   1492 C  CB  . ILE A 1 205 ? 11.871 9.608   10.902  1.00 20.23 ? 205 ILE A CB  1 
ATOM   1493 C  CG1 . ILE A 1 205 ? 11.155 9.599   12.252  1.00 21.49 ? 205 ILE A CG1 1 
ATOM   1494 C  CG2 . ILE A 1 205 ? 10.922 9.193   9.769   1.00 18.39 ? 205 ILE A CG2 1 
ATOM   1495 C  CD1 . ILE A 1 205 ? 10.196 10.754  12.434  1.00 24.09 ? 205 ILE A CD1 1 
ATOM   1496 N  N   . THR A 1 206 ? 13.801 7.424   8.986   1.00 18.98 ? 206 THR A N   1 
ATOM   1497 C  CA  . THR A 1 206 ? 14.311 7.262   7.633   1.00 19.23 ? 206 THR A CA  1 
ATOM   1498 C  C   . THR A 1 206 ? 13.150 7.154   6.639   1.00 23.44 ? 206 THR A C   1 
ATOM   1499 O  O   . THR A 1 206 ? 11.980 7.065   7.024   1.00 23.93 ? 206 THR A O   1 
ATOM   1500 C  CB  . THR A 1 206 ? 15.258 6.055   7.563   1.00 20.12 ? 206 THR A CB  1 
ATOM   1501 O  OG1 . THR A 1 206 ? 15.983 6.081   6.324   1.00 17.25 ? 206 THR A OG1 1 
ATOM   1502 C  CG2 . THR A 1 206 ? 14.500 4.732   7.702   1.00 18.45 ? 206 THR A CG2 1 
ATOM   1503 N  N   . HIS A 1 207 ? 13.492 7.184   5.340   1.00 19.34 ? 207 HIS A N   1 
ATOM   1504 C  CA  . HIS A 1 207 ? 12.523 7.391   4.251   1.00 19.60 ? 207 HIS A CA  1 
ATOM   1505 C  C   . HIS A 1 207 ? 11.756 8.694   4.434   1.00 21.28 ? 207 HIS A C   1 
ATOM   1506 O  O   . HIS A 1 207 ? 10.556 8.769   4.166   1.00 20.92 ? 207 HIS A O   1 
ATOM   1507 C  CB  . HIS A 1 207 ? 11.551 6.214   4.104   1.00 19.30 ? 207 HIS A CB  1 
ATOM   1508 C  CG  . HIS A 1 207 ? 12.225 4.886   4.083   1.00 18.45 ? 207 HIS A CG  1 
ATOM   1509 N  ND1 . HIS A 1 207 ? 13.405 4.669   3.405   1.00 19.37 ? 207 HIS A ND1 1 
ATOM   1510 C  CD2 . HIS A 1 207 ? 11.897 3.708   4.657   1.00 25.39 ? 207 HIS A CD2 1 
ATOM   1511 C  CE1 . HIS A 1 207 ? 13.771 3.411   3.557   1.00 20.01 ? 207 HIS A CE1 1 
ATOM   1512 N  NE2 . HIS A 1 207 ? 12.871 2.807   4.308   1.00 20.73 ? 207 HIS A NE2 1 
ATOM   1513 N  N   . CYS A 1 208 ? 12.459 9.735   4.887   1.00 19.71 ? 208 CYS A N   1 
ATOM   1514 C  CA  . CYS A 1 208 ? 11.788 10.937  5.364   1.00 21.58 ? 208 CYS A CA  1 
ATOM   1515 C  C   . CYS A 1 208 ? 11.069 11.715  4.268   1.00 23.75 ? 208 CYS A C   1 
ATOM   1516 O  O   . CYS A 1 208 ? 10.255 12.588  4.590   1.00 21.75 ? 208 CYS A O   1 
ATOM   1517 C  CB  . CYS A 1 208 ? 12.793 11.844  6.068   1.00 20.11 ? 208 CYS A CB  1 
ATOM   1518 S  SG  . CYS A 1 208 ? 14.041 12.589  4.997   1.00 22.68 ? 208 CYS A SG  1 
ATOM   1519 N  N   . TYR A 1 209 ? 11.339 11.437  2.998   1.00 21.60 ? 209 TYR A N   1 
ATOM   1520 C  CA  . TYR A 1 209 ? 10.650 12.115  1.909   1.00 21.00 ? 209 TYR A CA  1 
ATOM   1521 C  C   . TYR A 1 209 ? 9.855  11.127  1.062   1.00 21.11 ? 209 TYR A C   1 
ATOM   1522 O  O   . TYR A 1 209 ? 9.709  11.319  -0.146  1.00 21.22 ? 209 TYR A O   1 
ATOM   1523 C  CB  . TYR A 1 209 ? 11.637 12.892  1.037   1.00 23.16 ? 209 TYR A CB  1 
ATOM   1524 C  CG  . TYR A 1 209 ? 12.367 14.008  1.755   1.00 23.33 ? 209 TYR A CG  1 
ATOM   1525 C  CD1 . TYR A 1 209 ? 11.674 14.943  2.521   1.00 23.82 ? 209 TYR A CD1 1 
ATOM   1526 C  CD2 . TYR A 1 209 ? 13.743 14.143  1.649   1.00 24.68 ? 209 TYR A CD2 1 
ATOM   1527 C  CE1 . TYR A 1 209 ? 12.336 15.963  3.175   1.00 25.98 ? 209 TYR A CE1 1 
ATOM   1528 C  CE2 . TYR A 1 209 ? 14.417 15.172  2.308   1.00 24.53 ? 209 TYR A CE2 1 
ATOM   1529 C  CZ  . TYR A 1 209 ? 13.701 16.077  3.064   1.00 25.11 ? 209 TYR A CZ  1 
ATOM   1530 O  OH  . TYR A 1 209 ? 14.352 17.100  3.716   1.00 26.98 ? 209 TYR A OH  1 
ATOM   1531 N  N   . ASN A 1 210 ? 9.360  10.054  1.676   1.00 23.68 ? 210 ASN A N   1 
ATOM   1532 C  CA  . ASN A 1 210 ? 8.483  9.128   0.969   1.00 24.23 ? 210 ASN A CA  1 
ATOM   1533 C  C   . ASN A 1 210 ? 7.184  9.818   0.574   1.00 24.40 ? 210 ASN A C   1 
ATOM   1534 O  O   . ASN A 1 210 ? 6.735  10.765  1.226   1.00 24.24 ? 210 ASN A O   1 
ATOM   1535 C  CB  . ASN A 1 210 ? 8.167  7.907   1.834   1.00 23.56 ? 210 ASN A CB  1 
ATOM   1536 C  CG  . ASN A 1 210 ? 7.148  8.212   2.920   1.00 26.03 ? 210 ASN A CG  1 
ATOM   1537 O  OD1 . ASN A 1 210 ? 5.940  8.184   2.681   1.00 26.47 ? 210 ASN A OD1 1 
ATOM   1538 N  ND2 . ASN A 1 210 ? 7.634  8.506   4.124   1.00 26.27 ? 210 ASN A ND2 1 
ATOM   1539 N  N   . GLY A 1 211 ? 6.580  9.331   -0.510  1.00 22.06 ? 211 GLY A N   1 
ATOM   1540 C  CA  . GLY A 1 211 ? 5.301  9.810   -0.986  1.00 24.39 ? 211 GLY A CA  1 
ATOM   1541 C  C   . GLY A 1 211 ? 4.127  8.941   -0.594  1.00 27.58 ? 211 GLY A C   1 
ATOM   1542 O  O   . GLY A 1 211 ? 3.037  9.096   -1.164  1.00 27.18 ? 211 GLY A O   1 
ATOM   1543 N  N   . LYS A 1 212 ? 4.316  8.031   0.355   1.00 25.64 ? 212 LYS A N   1 
ATOM   1544 C  CA  . LYS A 1 212 ? 3.273  7.138   0.841   1.00 29.18 ? 212 LYS A CA  1 
ATOM   1545 C  C   . LYS A 1 212 ? 2.383  7.880   1.839   1.00 29.55 ? 212 LYS A C   1 
ATOM   1546 O  O   . LYS A 1 212 ? 2.644  9.034   2.176   1.00 27.40 ? 212 LYS A O   1 
ATOM   1547 C  CB  . LYS A 1 212 ? 3.935  5.896   1.436   1.00 27.32 ? 212 LYS A CB  1 
ATOM   1548 C  CG  . LYS A 1 212 ? 4.768  5.132   0.404   1.00 31.68 ? 212 LYS A CG  1 
ATOM   1549 C  CD  . LYS A 1 212 ? 5.409  3.869   0.976   1.00 35.69 ? 212 LYS A CD  1 
ATOM   1550 C  CE  . LYS A 1 212 ? 5.866  2.932   -0.144  1.00 39.45 ? 212 LYS A CE  1 
ATOM   1551 N  NZ  . LYS A 1 212 ? 6.875  1.941   0.324   1.00 45.88 ? 212 LYS A NZ  1 
ATOM   1552 N  N   . PRO A 1 213 ? 1.288  7.265   2.307   1.00 29.95 ? 213 PRO A N   1 
ATOM   1553 C  CA  . PRO A 1 213 ? 0.383  8.010   3.205   1.00 28.12 ? 213 PRO A CA  1 
ATOM   1554 C  C   . PRO A 1 213 ? 1.037  8.530   4.476   1.00 30.12 ? 213 PRO A C   1 
ATOM   1555 O  O   . PRO A 1 213 ? 0.587  9.555   5.007   1.00 30.04 ? 213 PRO A O   1 
ATOM   1556 C  CB  . PRO A 1 213 ? -0.720 6.990   3.511   1.00 33.44 ? 213 PRO A CB  1 
ATOM   1557 C  CG  . PRO A 1 213 ? -0.745 6.106   2.320   1.00 31.59 ? 213 PRO A CG  1 
ATOM   1558 C  CD  . PRO A 1 213 ? 0.674  6.004   1.842   1.00 30.08 ? 213 PRO A CD  1 
ATOM   1559 N  N   . ASN A 1 214 ? 2.080  7.873   4.984   1.00 27.51 ? 214 ASN A N   1 
ATOM   1560 C  CA  . ASN A 1 214 ? 2.765  8.347   6.187   1.00 28.69 ? 214 ASN A CA  1 
ATOM   1561 C  C   . ASN A 1 214 ? 3.892  9.312   5.849   1.00 30.44 ? 214 ASN A C   1 
ATOM   1562 O  O   . ASN A 1 214 ? 4.958  9.303   6.473   1.00 31.58 ? 214 ASN A O   1 
ATOM   1563 C  CB  . ASN A 1 214 ? 3.281  7.163   6.996   1.00 32.22 ? 214 ASN A CB  1 
ATOM   1564 C  CG  . ASN A 1 214 ? 2.320  6.750   8.096   1.00 34.64 ? 214 ASN A CG  1 
ATOM   1565 O  OD1 . ASN A 1 214 ? 1.308  7.411   8.332   1.00 33.84 ? 214 ASN A OD1 1 
ATOM   1566 N  ND2 . ASN A 1 214 ? 2.622  5.641   8.761   1.00 35.30 ? 214 ASN A ND2 1 
ATOM   1567 N  N   . ARG A 1 215 ? 3.672  10.149  4.840   1.00 28.42 ? 215 ARG A N   1 
ATOM   1568 C  CA  . ARG A 1 215 ? 4.598  11.208  4.481   1.00 25.61 ? 215 ARG A CA  1 
ATOM   1569 C  C   . ARG A 1 215 ? 4.575  12.319  5.527   1.00 28.64 ? 215 ARG A C   1 
ATOM   1570 O  O   . ARG A 1 215 ? 3.606  12.490  6.272   1.00 25.43 ? 215 ARG A O   1 
ATOM   1571 C  CB  . ARG A 1 215 ? 4.234  11.775  3.108   1.00 27.08 ? 215 ARG A CB  1 
ATOM   1572 C  CG  . ARG A 1 215 ? 2.759  12.140  2.943   1.00 27.37 ? 215 ARG A CG  1 
ATOM   1573 C  CD  . ARG A 1 215 ? 2.610  12.918  1.658   1.00 29.07 ? 215 ARG A CD  1 
ATOM   1574 N  NE  . ARG A 1 215 ? 2.358  12.024  0.535   1.00 25.14 ? 215 ARG A NE  1 
ATOM   1575 C  CZ  . ARG A 1 215 ? 1.757  12.386  -0.589  1.00 27.18 ? 215 ARG A CZ  1 
ATOM   1576 N  NH1 . ARG A 1 215 ? 1.384  13.639  -0.801  1.00 26.73 ? 215 ARG A NH1 1 
ATOM   1577 N  NH2 . ARG A 1 215 ? 1.557  11.477  -1.539  1.00 26.33 ? 215 ARG A NH2 1 
ATOM   1578 N  N   . ILE A 1 216 ? 5.670  13.085  5.583   1.00 25.53 ? 216 ILE A N   1 
ATOM   1579 C  CA  . ILE A 1 216 ? 5.778  14.125  6.605   1.00 28.26 ? 216 ILE A CA  1 
ATOM   1580 C  C   . ILE A 1 216 ? 4.972  15.373  6.282   1.00 29.35 ? 216 ILE A C   1 
ATOM   1581 O  O   . ILE A 1 216 ? 4.897  16.277  7.125   1.00 30.11 ? 216 ILE A O   1 
ATOM   1582 C  CB  . ILE A 1 216 ? 7.237  14.548  6.849   1.00 24.86 ? 216 ILE A CB  1 
ATOM   1583 C  CG1 . ILE A 1 216 ? 7.858  15.116  5.573   1.00 26.45 ? 216 ILE A CG1 1 
ATOM   1584 C  CG2 . ILE A 1 216 ? 8.054  13.380  7.396   1.00 25.30 ? 216 ILE A CG2 1 
ATOM   1585 C  CD1 . ILE A 1 216 ? 9.307  15.556  5.751   1.00 24.02 ? 216 ILE A CD1 1 
ATOM   1586 N  N   . LEU A 1 217 ? 4.383  15.458  5.091   1.00 26.18 ? 217 LEU A N   1 
ATOM   1587 C  CA  . LEU A 1 217 ? 3.529  16.577  4.698   1.00 29.52 ? 217 LEU A CA  1 
ATOM   1588 C  C   . LEU A 1 217 ? 2.062  16.174  4.785   1.00 31.23 ? 217 LEU A C   1 
ATOM   1589 O  O   . LEU A 1 217 ? 1.704  15.047  4.431   1.00 29.22 ? 217 LEU A O   1 
ATOM   1590 C  CB  . LEU A 1 217 ? 3.849  17.015  3.269   1.00 28.52 ? 217 LEU A CB  1 
ATOM   1591 C  CG  . LEU A 1 217 ? 5.292  17.418  2.975   1.00 26.40 ? 217 LEU A CG  1 
ATOM   1592 C  CD1 . LEU A 1 217 ? 5.481  17.635  1.477   1.00 27.34 ? 217 LEU A CD1 1 
ATOM   1593 C  CD2 . LEU A 1 217 ? 5.649  18.677  3.742   1.00 27.68 ? 217 LEU A CD2 1 
ATOM   1594 N  N   . ASN A 1 218 ? 1.210  17.095  5.236   1.00 27.89 ? 218 ASN A N   1 
ATOM   1595 C  CA  . ASN A 1 218 ? -0.226 16.837  5.242   1.00 31.49 ? 218 ASN A CA  1 
ATOM   1596 C  C   . ASN A 1 218 ? -0.776 17.083  3.840   1.00 32.06 ? 218 ASN A C   1 
ATOM   1597 O  O   . ASN A 1 218 ? -0.047 17.519  2.947   1.00 29.38 ? 218 ASN A O   1 
ATOM   1598 C  CB  . ASN A 1 218 ? -0.910 17.675  6.333   1.00 34.27 ? 218 ASN A CB  1 
ATOM   1599 C  CG  . ASN A 1 218 ? -0.831 19.184  6.100   1.00 34.42 ? 218 ASN A CG  1 
ATOM   1600 O  OD1 . ASN A 1 218 ? -0.759 19.667  4.970   1.00 32.84 ? 218 ASN A OD1 1 
ATOM   1601 N  ND2 . ASN A 1 218 ? -0.850 19.937  7.197   1.00 37.57 ? 218 ASN A ND2 1 
ATOM   1602 N  N   . PRO A 1 219 ? -2.049 16.765  3.587   1.00 31.27 ? 219 PRO A N   1 
ATOM   1603 C  CA  . PRO A 1 219 ? -2.576 16.963  2.226   1.00 32.01 ? 219 PRO A CA  1 
ATOM   1604 C  C   . PRO A 1 219 ? -2.629 18.415  1.793   1.00 32.86 ? 219 PRO A C   1 
ATOM   1605 O  O   . PRO A 1 219 ? -2.784 18.680  0.596   1.00 34.57 ? 219 PRO A O   1 
ATOM   1606 C  CB  . PRO A 1 219 ? -3.977 16.346  2.299   1.00 33.41 ? 219 PRO A CB  1 
ATOM   1607 C  CG  . PRO A 1 219 ? -3.861 15.314  3.362   1.00 32.79 ? 219 PRO A CG  1 
ATOM   1608 C  CD  . PRO A 1 219 ? -2.973 15.948  4.399   1.00 32.01 ? 219 PRO A CD  1 
ATOM   1609 N  N   . ALA A 1 220 ? -2.509 19.366  2.716   1.00 36.35 ? 220 ALA A N   1 
ATOM   1610 C  CA  . ALA A 1 220 ? -2.474 20.774  2.346   1.00 36.02 ? 220 ALA A CA  1 
ATOM   1611 C  C   . ALA A 1 220 ? -1.080 21.244  1.956   1.00 34.46 ? 220 ALA A C   1 
ATOM   1612 O  O   . ALA A 1 220 ? -0.906 22.430  1.661   1.00 37.28 ? 220 ALA A O   1 
ATOM   1613 C  CB  . ALA A 1 220 ? -3.014 21.638  3.492   1.00 36.72 ? 220 ALA A CB  1 
ATOM   1614 N  N   . GLY A 1 221 ? -0.090 20.351  1.945   1.00 34.43 ? 221 GLY A N   1 
ATOM   1615 C  CA  . GLY A 1 221 ? 1.262  20.713  1.576   1.00 33.60 ? 221 GLY A CA  1 
ATOM   1616 C  C   . GLY A 1 221 ? 2.094  21.301  2.692   1.00 35.95 ? 221 GLY A C   1 
ATOM   1617 O  O   . GLY A 1 221 ? 3.164  21.857  2.418   1.00 36.46 ? 221 GLY A O   1 
ATOM   1618 N  N   . GLU A 1 222 ? 1.645  21.192  3.938   1.00 34.59 ? 222 GLU A N   1 
ATOM   1619 C  CA  . GLU A 1 222 ? 2.374  21.703  5.086   1.00 34.21 ? 222 GLU A CA  1 
ATOM   1620 C  C   . GLU A 1 222 ? 2.934  20.550  5.909   1.00 33.53 ? 222 GLU A C   1 
ATOM   1621 O  O   . GLU A 1 222 ? 2.539  19.392  5.753   1.00 27.75 ? 222 GLU A O   1 
ATOM   1622 C  CB  . GLU A 1 222 ? 1.473  22.579  5.960   1.00 36.41 ? 222 GLU A CB  1 
ATOM   1623 C  CG  . GLU A 1 222 ? 0.648  23.574  5.170   1.00 38.82 ? 222 GLU A CG  1 
ATOM   1624 C  CD  . GLU A 1 222 ? 1.136  24.991  5.357   1.00 40.81 ? 222 GLU A CD  1 
ATOM   1625 O  OE1 . GLU A 1 222 ? 2.268  25.161  5.869   1.00 45.09 ? 222 GLU A OE1 1 
ATOM   1626 O  OE2 . GLU A 1 222 ? 0.389  25.927  4.999   1.00 51.85 ? 222 GLU A OE2 1 
ATOM   1627 N  N   . LEU A 1 223 ? 3.873  20.875  6.793   1.00 31.95 ? 223 LEU A N   1 
ATOM   1628 C  CA  . LEU A 1 223 ? 4.463  19.844  7.631   1.00 31.46 ? 223 LEU A CA  1 
ATOM   1629 C  C   . LEU A 1 223 ? 3.448  19.371  8.660   1.00 32.85 ? 223 LEU A C   1 
ATOM   1630 O  O   . LEU A 1 223 ? 2.678  20.165  9.207   1.00 33.60 ? 223 LEU A O   1 
ATOM   1631 C  CB  . LEU A 1 223 ? 5.718  20.367  8.331   1.00 31.21 ? 223 LEU A CB  1 
ATOM   1632 C  CG  . LEU A 1 223 ? 6.714  19.310  8.818   1.00 29.97 ? 223 LEU A CG  1 
ATOM   1633 C  CD1 . LEU A 1 223 ? 7.274  18.486  7.655   1.00 28.68 ? 223 LEU A CD1 1 
ATOM   1634 C  CD2 . LEU A 1 223 ? 7.834  19.942  9.631   1.00 31.82 ? 223 LEU A CD2 1 
ATOM   1635 N  N   . ARG A 1 224 ? 3.425  18.064  8.909   1.00 31.63 ? 224 ARG A N   1 
ATOM   1636 C  CA  . ARG A 1 224 ? 2.574  17.559  9.976   1.00 37.57 ? 224 ARG A CA  1 
ATOM   1637 C  C   . ARG A 1 224 ? 3.054  18.116  11.307  1.00 34.73 ? 224 ARG A C   1 
ATOM   1638 O  O   . ARG A 1 224 ? 4.258  18.215  11.555  1.00 33.49 ? 224 ARG A O   1 
ATOM   1639 C  CB  . ARG A 1 224 ? 2.578  16.029  9.996   1.00 37.07 ? 224 ARG A CB  1 
ATOM   1640 C  CG  . ARG A 1 224 ? 2.318  15.411  8.639   1.00 34.53 ? 224 ARG A CG  1 
ATOM   1641 C  CD  . ARG A 1 224 ? 1.093  14.536  8.640   1.00 38.58 ? 224 ARG A CD  1 
ATOM   1642 N  NE  . ARG A 1 224 ? 1.211  13.504  7.617   1.00 41.98 ? 224 ARG A NE  1 
ATOM   1643 C  CZ  . ARG A 1 224 ? 0.818  12.246  7.764   1.00 39.46 ? 224 ARG A CZ  1 
ATOM   1644 N  NH1 . ARG A 1 224 ? 0.274  11.818  8.893   1.00 44.25 ? 224 ARG A NH1 1 
ATOM   1645 N  NH2 . ARG A 1 224 ? 0.987  11.395  6.757   1.00 35.99 ? 224 ARG A NH2 1 
ATOM   1646 N  N   . SER A 1 225 ? 2.102  18.509  12.156  1.00 34.63 ? 225 SER A N   1 
ATOM   1647 C  CA  . SER A 1 225 ? 2.470  19.073  13.449  1.00 37.23 ? 225 SER A CA  1 
ATOM   1648 C  C   . SER A 1 225 ? 3.206  18.058  14.316  1.00 37.40 ? 225 SER A C   1 
ATOM   1649 O  O   . SER A 1 225 ? 4.065  18.439  15.124  1.00 36.61 ? 225 SER A O   1 
ATOM   1650 C  CB  . SER A 1 225 ? 1.225  19.605  14.161  1.00 38.60 ? 225 SER A CB  1 
ATOM   1651 O  OG  . SER A 1 225 ? 0.224  18.609  14.266  1.00 43.87 ? 225 SER A OG  1 
ATOM   1652 N  N   . SER A 1 226 ? 2.905  16.766  14.157  1.00 35.41 ? 226 SER A N   1 
ATOM   1653 C  CA  . SER A 1 226 ? 3.657  15.752  14.887  1.00 36.65 ? 226 SER A CA  1 
ATOM   1654 C  C   . SER A 1 226 ? 5.128  15.773  14.486  1.00 32.47 ? 226 SER A C   1 
ATOM   1655 O  O   . SER A 1 226 ? 6.015  15.631  15.335  1.00 30.98 ? 226 SER A O   1 
ATOM   1656 C  CB  . SER A 1 226 ? 3.052  14.367  14.654  1.00 37.48 ? 226 SER A CB  1 
ATOM   1657 O  OG  . SER A 1 226 ? 3.139  13.993  13.292  1.00 34.23 ? 226 SER A OG  1 
ATOM   1658 N  N   . ILE A 1 227 ? 5.409  15.988  13.199  1.00 32.51 ? 227 ILE A N   1 
ATOM   1659 C  CA  . ILE A 1 227 ? 6.796  16.032  12.754  1.00 30.69 ? 227 ILE A CA  1 
ATOM   1660 C  C   . ILE A 1 227 ? 7.472  17.304  13.249  1.00 31.14 ? 227 ILE A C   1 
ATOM   1661 O  O   . ILE A 1 227 ? 8.657  17.292  13.598  1.00 28.86 ? 227 ILE A O   1 
ATOM   1662 C  CB  . ILE A 1 227 ? 6.874  15.900  11.224  1.00 29.00 ? 227 ILE A CB  1 
ATOM   1663 C  CG1 . ILE A 1 227 ? 6.284  14.562  10.779  1.00 30.44 ? 227 ILE A CG1 1 
ATOM   1664 C  CG2 . ILE A 1 227 ? 8.312  16.010  10.750  1.00 26.96 ? 227 ILE A CG2 1 
ATOM   1665 C  CD1 . ILE A 1 227 ? 6.907  13.367  11.456  1.00 28.59 ? 227 ILE A CD1 1 
ATOM   1666 N  N   . THR A 1 228 ? 6.733  18.416  13.295  1.00 33.04 ? 228 THR A N   1 
ATOM   1667 C  CA  . THR A 1 228 ? 7.285  19.649  13.855  1.00 33.28 ? 228 THR A CA  1 
ATOM   1668 C  C   . THR A 1 228 ? 7.683  19.467  15.318  1.00 32.04 ? 228 THR A C   1 
ATOM   1669 O  O   . THR A 1 228 ? 8.793  19.837  15.720  1.00 32.84 ? 228 THR A O   1 
ATOM   1670 C  CB  . THR A 1 228 ? 6.278  20.794  13.708  1.00 35.53 ? 228 THR A CB  1 
ATOM   1671 O  OG1 . THR A 1 228 ? 5.593  20.669  12.458  1.00 33.00 ? 228 THR A OG1 1 
ATOM   1672 C  CG2 . THR A 1 228 ? 6.979  22.149  13.768  1.00 39.98 ? 228 THR A CG2 1 
ATOM   1673 N  N   . ARG A 1 229 ? 6.793  18.891  16.133  1.00 32.63 ? 229 ARG A N   1 
ATOM   1674 C  CA  . ARG A 1 229 ? 7.145  18.664  17.535  1.00 31.08 ? 229 ARG A CA  1 
ATOM   1675 C  C   . ARG A 1 229 ? 8.284  17.657  17.675  1.00 34.34 ? 229 ARG A C   1 
ATOM   1676 O  O   . ARG A 1 229 ? 9.135  17.799  18.565  1.00 34.79 ? 229 ARG A O   1 
ATOM   1677 C  CB  . ARG A 1 229 ? 5.933  18.195  18.334  1.00 35.25 ? 229 ARG A CB  1 
ATOM   1678 C  CG  . ARG A 1 229 ? 4.679  18.995  18.123  1.00 36.12 ? 229 ARG A CG  1 
ATOM   1679 C  CD  . ARG A 1 229 ? 3.644  18.600  19.153  1.00 39.54 ? 229 ARG A CD  1 
ATOM   1680 N  NE  . ARG A 1 229 ? 2.776  17.555  18.626  1.00 41.97 ? 229 ARG A NE  1 
ATOM   1681 C  CZ  . ARG A 1 229 ? 1.772  17.772  17.787  1.00 44.45 ? 229 ARG A CZ  1 
ATOM   1682 N  NH1 . ARG A 1 229 ? 1.452  18.994  17.394  1.00 43.68 ? 229 ARG A NH1 1 
ATOM   1683 N  NH2 . ARG A 1 229 ? 1.071  16.735  17.331  1.00 45.14 ? 229 ARG A NH2 1 
ATOM   1684 N  N   . ALA A 1 230 ? 8.318  16.632  16.817  1.00 30.36 ? 230 ALA A N   1 
ATOM   1685 C  CA  . ALA A 1 230 ? 9.400  15.655  16.886  1.00 31.29 ? 230 ALA A CA  1 
ATOM   1686 C  C   . ALA A 1 230 ? 10.743 16.316  16.614  1.00 31.04 ? 230 ALA A C   1 
ATOM   1687 O  O   . ALA A 1 230 ? 11.714 16.103  17.351  1.00 28.27 ? 230 ALA A O   1 
ATOM   1688 C  CB  . ALA A 1 230 ? 9.148  14.517  15.897  1.00 28.69 ? 230 ALA A CB  1 
ATOM   1689 N  N   . LEU A 1 231 ? 10.813 17.127  15.553  1.00 28.33 ? 231 LEU A N   1 
ATOM   1690 C  CA  . LEU A 1 231 ? 12.009 17.922  15.289  1.00 28.32 ? 231 LEU A CA  1 
ATOM   1691 C  C   . LEU A 1 231 ? 12.346 18.820  16.473  1.00 31.31 ? 231 LEU A C   1 
ATOM   1692 O  O   . LEU A 1 231 ? 13.522 19.003  16.808  1.00 29.28 ? 231 LEU A O   1 
ATOM   1693 C  CB  . LEU A 1 231 ? 11.812 18.761  14.026  1.00 29.39 ? 231 LEU A CB  1 
ATOM   1694 C  CG  . LEU A 1 231 ? 11.654 18.039  12.681  1.00 28.93 ? 231 LEU A CG  1 
ATOM   1695 C  CD1 . LEU A 1 231 ? 11.360 19.039  11.574  1.00 28.62 ? 231 LEU A CD1 1 
ATOM   1696 C  CD2 . LEU A 1 231 ? 12.902 17.251  12.347  1.00 28.24 ? 231 LEU A CD2 1 
ATOM   1697 N  N   . HIS A 1 232 ? 11.324 19.393  17.117  1.00 28.93 ? 232 HIS A N   1 
ATOM   1698 C  CA  . HIS A 1 232 ? 11.570 20.224  18.294  1.00 35.03 ? 232 HIS A CA  1 
ATOM   1699 C  C   . HIS A 1 232 ? 12.255 19.417  19.392  1.00 34.58 ? 232 HIS A C   1 
ATOM   1700 O  O   . HIS A 1 232 ? 13.130 19.934  20.096  1.00 34.92 ? 232 HIS A O   1 
ATOM   1701 C  CB  . HIS A 1 232 ? 10.254 20.827  18.801  1.00 31.65 ? 232 HIS A CB  1 
ATOM   1702 C  CG  . HIS A 1 232 ? 10.415 21.800  19.934  1.00 40.57 ? 232 HIS A CG  1 
ATOM   1703 N  ND1 . HIS A 1 232 ? 11.153 21.526  21.067  1.00 43.53 ? 232 HIS A ND1 1 
ATOM   1704 C  CD2 . HIS A 1 232 ? 9.911  23.046  20.112  1.00 43.95 ? 232 HIS A CD2 1 
ATOM   1705 C  CE1 . HIS A 1 232 ? 11.110 22.563  21.885  1.00 44.70 ? 232 HIS A CE1 1 
ATOM   1706 N  NE2 . HIS A 1 232 ? 10.361 23.499  21.330  1.00 47.83 ? 232 HIS A NE2 1 
ATOM   1707 N  N   . ARG A 1 233 ? 11.882 18.143  19.539  1.00 33.54 ? 233 ARG A N   1 
ATOM   1708 C  CA  . ARG A 1 233 ? 12.454 17.280  20.567  1.00 32.59 ? 233 ARG A CA  1 
ATOM   1709 C  C   . ARG A 1 233 ? 13.821 16.714  20.191  1.00 33.32 ? 233 ARG A C   1 
ATOM   1710 O  O   . ARG A 1 233 ? 14.475 16.107  21.048  1.00 31.57 ? 233 ARG A O   1 
ATOM   1711 C  CB  . ARG A 1 233 ? 11.502 16.121  20.879  1.00 33.13 ? 233 ARG A CB  1 
ATOM   1712 C  CG  . ARG A 1 233 ? 10.183 16.530  21.503  1.00 34.67 ? 233 ARG A CG  1 
ATOM   1713 C  CD  . ARG A 1 233 ? 9.472  15.320  22.097  1.00 35.39 ? 233 ARG A CD  1 
ATOM   1714 N  NE  . ARG A 1 233 ? 9.227  14.303  21.081  1.00 36.02 ? 233 ARG A NE  1 
ATOM   1715 C  CZ  . ARG A 1 233 ? 8.213  14.317  20.227  1.00 35.19 ? 233 ARG A CZ  1 
ATOM   1716 N  NH1 . ARG A 1 233 ? 7.293  15.265  20.262  1.00 34.85 ? 233 ARG A NH1 1 
ATOM   1717 N  NH2 . ARG A 1 233 ? 8.122  13.355  19.314  1.00 34.42 ? 233 ARG A NH2 1 
ATOM   1718 N  N   . GLY A 1 234 ? 14.266 16.882  18.946  1.00 30.29 ? 234 GLY A N   1 
ATOM   1719 C  CA  . GLY A 1 234 ? 15.576 16.422  18.532  1.00 29.82 ? 234 GLY A CA  1 
ATOM   1720 C  C   . GLY A 1 234 ? 15.575 15.224  17.610  1.00 28.62 ? 234 GLY A C   1 
ATOM   1721 O  O   . GLY A 1 234 ? 16.655 14.715  17.285  1.00 23.01 ? 234 GLY A O   1 
ATOM   1722 N  N   . VAL A 1 235 ? 14.404 14.753  17.181  1.00 27.90 ? 235 VAL A N   1 
ATOM   1723 C  CA  . VAL A 1 235 ? 14.339 13.664  16.213  1.00 26.90 ? 235 VAL A CA  1 
ATOM   1724 C  C   . VAL A 1 235 ? 14.905 14.146  14.880  1.00 26.69 ? 235 VAL A C   1 
ATOM   1725 O  O   . VAL A 1 235 ? 14.721 15.307  14.488  1.00 24.13 ? 235 VAL A O   1 
ATOM   1726 C  CB  . VAL A 1 235 ? 12.884 13.173  16.092  1.00 26.51 ? 235 VAL A CB  1 
ATOM   1727 C  CG1 . VAL A 1 235 ? 12.736 12.095  15.020  1.00 27.21 ? 235 VAL A CG1 1 
ATOM   1728 C  CG2 . VAL A 1 235 ? 12.390 12.665  17.448  1.00 28.26 ? 235 VAL A CG2 1 
ATOM   1729 N  N   . ARG A 1 236 ? 15.630 13.270  14.192  1.00 24.99 ? 236 ARG A N   1 
ATOM   1730 C  CA  . ARG A 1 236 ? 16.299 13.625  12.950  1.00 25.29 ? 236 ARG A CA  1 
ATOM   1731 C  C   . ARG A 1 236 ? 15.686 12.887  11.767  1.00 24.23 ? 236 ARG A C   1 
ATOM   1732 O  O   . ARG A 1 236 ? 15.122 11.799  11.911  1.00 24.60 ? 236 ARG A O   1 
ATOM   1733 C  CB  . ARG A 1 236 ? 17.796 13.320  13.027  1.00 25.63 ? 236 ARG A CB  1 
ATOM   1734 C  CG  . ARG A 1 236 ? 18.483 13.984  14.208  1.00 29.75 ? 236 ARG A CG  1 
ATOM   1735 C  CD  . ARG A 1 236 ? 18.228 15.491  14.182  1.00 30.70 ? 236 ARG A CD  1 
ATOM   1736 N  NE  . ARG A 1 236 ? 19.366 16.306  14.600  1.00 39.58 ? 236 ARG A NE  1 
ATOM   1737 C  CZ  . ARG A 1 236 ? 20.084 16.135  15.705  1.00 43.51 ? 236 ARG A CZ  1 
ATOM   1738 N  NH1 . ARG A 1 236 ? 19.752 15.239  16.624  1.00 43.40 ? 236 ARG A NH1 1 
ATOM   1739 N  NH2 . ARG A 1 236 ? 21.151 16.904  15.909  1.00 43.92 ? 236 ARG A NH2 1 
ATOM   1740 N  N   . LEU A 1 237 ? 15.817 13.488  10.590  1.00 22.05 ? 237 LEU A N   1 
ATOM   1741 C  CA  . LEU A 1 237 ? 15.305 12.918  9.351   1.00 21.50 ? 237 LEU A CA  1 
ATOM   1742 C  C   . LEU A 1 237 ? 16.458 12.355  8.532   1.00 20.00 ? 237 LEU A C   1 
ATOM   1743 O  O   . LEU A 1 237 ? 17.440 13.060  8.274   1.00 20.87 ? 237 LEU A O   1 
ATOM   1744 C  CB  . LEU A 1 237 ? 14.562 13.973  8.538   1.00 24.57 ? 237 LEU A CB  1 
ATOM   1745 C  CG  . LEU A 1 237 ? 13.418 14.682  9.251   1.00 24.14 ? 237 LEU A CG  1 
ATOM   1746 C  CD1 . LEU A 1 237 ? 12.789 15.703  8.314   1.00 26.30 ? 237 LEU A CD1 1 
ATOM   1747 C  CD2 . LEU A 1 237 ? 12.387 13.670  9.714   1.00 21.44 ? 237 LEU A CD2 1 
ATOM   1748 N  N   . ASP A 1 238 ? 16.330 11.097  8.117   1.00 20.19 ? 238 ASP A N   1 
ATOM   1749 C  CA  . ASP A 1 238 ? 17.265 10.459  7.198   1.00 21.04 ? 238 ASP A CA  1 
ATOM   1750 C  C   . ASP A 1 238 ? 16.538 10.113  5.903   1.00 19.07 ? 238 ASP A C   1 
ATOM   1751 O  O   . ASP A 1 238 ? 15.371 9.710   5.928   1.00 20.40 ? 238 ASP A O   1 
ATOM   1752 C  CB  . ASP A 1 238 ? 17.876 9.204   7.834   1.00 20.72 ? 238 ASP A CB  1 
ATOM   1753 C  CG  . ASP A 1 238 ? 18.814 8.460   6.896   1.00 20.61 ? 238 ASP A CG  1 
ATOM   1754 O  OD1 . ASP A 1 238 ? 19.949 8.940   6.694   1.00 21.91 ? 238 ASP A OD1 1 
ATOM   1755 O  OD2 . ASP A 1 238 ? 18.444 7.364   6.412   1.00 21.22 ? 238 ASP A OD2 1 
ATOM   1756 N  N   . VAL A 1 239 ? 17.225 10.270  4.770   1.00 18.39 ? 239 VAL A N   1 
ATOM   1757 C  CA  . VAL A 1 239 ? 16.543 10.182  3.480   1.00 19.37 ? 239 VAL A CA  1 
ATOM   1758 C  C   . VAL A 1 239 ? 16.180 8.739   3.160   1.00 18.25 ? 239 VAL A C   1 
ATOM   1759 O  O   . VAL A 1 239 ? 15.023 8.433   2.850   1.00 18.05 ? 239 VAL A O   1 
ATOM   1760 C  CB  . VAL A 1 239 ? 17.402 10.807  2.367   1.00 19.43 ? 239 VAL A CB  1 
ATOM   1761 C  CG1 . VAL A 1 239 ? 16.799 10.487  0.992   1.00 20.17 ? 239 VAL A CG1 1 
ATOM   1762 C  CG2 . VAL A 1 239 ? 17.529 12.310  2.584   1.00 17.18 ? 239 VAL A CG2 1 
ATOM   1763 N  N   . GLY A 1 240 ? 17.158 7.832   3.223   1.00 18.74 ? 240 GLY A N   1 
ATOM   1764 C  CA  . GLY A 1 240 ? 16.923 6.434   2.882   1.00 17.75 ? 240 GLY A CA  1 
ATOM   1765 C  C   . GLY A 1 240 ? 16.167 6.240   1.583   1.00 20.16 ? 240 GLY A C   1 
ATOM   1766 O  O   . GLY A 1 240 ? 15.113 5.594   1.565   1.00 22.60 ? 240 GLY A O   1 
ATOM   1767 N  N   . HIS A 1 241 ? 16.704 6.800   0.493   1.00 19.46 ? 241 HIS A N   1 
ATOM   1768 C  CA  . HIS A 1 241 ? 16.069 6.851   -0.825  1.00 20.53 ? 241 HIS A CA  1 
ATOM   1769 C  C   . HIS A 1 241 ? 15.320 5.578   -1.200  1.00 21.23 ? 241 HIS A C   1 
ATOM   1770 O  O   . HIS A 1 241 ? 14.093 5.592   -1.360  1.00 20.56 ? 241 HIS A O   1 
ATOM   1771 C  CB  . HIS A 1 241 ? 17.135 7.142   -1.888  1.00 20.16 ? 241 HIS A CB  1 
ATOM   1772 C  CG  . HIS A 1 241 ? 16.577 7.522   -3.225  1.00 20.85 ? 241 HIS A CG  1 
ATOM   1773 N  ND1 . HIS A 1 241 ? 15.805 6.665   -3.978  1.00 23.99 ? 241 HIS A ND1 1 
ATOM   1774 C  CD2 . HIS A 1 241 ? 16.724 8.647   -3.966  1.00 17.39 ? 241 HIS A CD2 1 
ATOM   1775 C  CE1 . HIS A 1 241 ? 15.476 7.258   -5.114  1.00 25.72 ? 241 HIS A CE1 1 
ATOM   1776 N  NE2 . HIS A 1 241 ? 16.025 8.460   -5.132  1.00 22.38 ? 241 HIS A NE2 1 
ATOM   1777 N  N   . GLY A 1 242 ? 16.057 4.482   -1.384  1.00 20.98 ? 242 GLY A N   1 
ATOM   1778 C  CA  . GLY A 1 242 ? 15.451 3.198   -1.647  1.00 19.88 ? 242 GLY A CA  1 
ATOM   1779 C  C   . GLY A 1 242 ? 14.740 3.106   -2.984  1.00 23.87 ? 242 GLY A C   1 
ATOM   1780 O  O   . GLY A 1 242 ? 14.812 3.990   -3.842  1.00 21.66 ? 242 GLY A O   1 
ATOM   1781 N  N   . THR A 1 243 ? 14.031 1.989   -3.144  1.00 20.91 ? 243 THR A N   1 
ATOM   1782 C  CA  . THR A 1 243 ? 13.296 1.747   -4.380  1.00 24.27 ? 243 THR A CA  1 
ATOM   1783 C  C   . THR A 1 243 ? 11.953 2.465   -4.393  1.00 28.53 ? 243 THR A C   1 
ATOM   1784 O  O   . THR A 1 243 ? 11.505 2.913   -5.458  1.00 29.51 ? 243 THR A O   1 
ATOM   1785 C  CB  . THR A 1 243 ? 13.097 0.240   -4.587  1.00 26.10 ? 243 THR A CB  1 
ATOM   1786 O  OG1 . THR A 1 243 ? 14.374 -0.383  -4.788  1.00 25.49 ? 243 THR A OG1 1 
ATOM   1787 C  CG2 . THR A 1 243 ? 12.221 -0.026  -5.802  1.00 23.57 ? 243 THR A CG2 1 
ATOM   1788 N  N   . ALA A 1 244 ? 11.308 2.608   -3.232  1.00 27.83 ? 244 ALA A N   1 
ATOM   1789 C  CA  . ALA A 1 244 ? 9.974  3.193   -3.187  1.00 30.85 ? 244 ALA A CA  1 
ATOM   1790 C  C   . ALA A 1 244 ? 9.822  4.248   -2.092  1.00 30.19 ? 244 ALA A C   1 
ATOM   1791 O  O   . ALA A 1 244 ? 8.691  4.566   -1.714  1.00 30.89 ? 244 ALA A O   1 
ATOM   1792 C  CB  . ALA A 1 244 ? 8.913  2.100   -3.020  1.00 30.51 ? 244 ALA A CB  1 
ATOM   1793 N  N   . SER A 1 245 ? 10.923 4.835   -1.606  1.00 25.94 ? 245 SER A N   1 
ATOM   1794 C  CA  . SER A 1 245 ? 10.868 5.700   -0.431  1.00 24.31 ? 245 SER A CA  1 
ATOM   1795 C  C   . SER A 1 245 ? 11.307 7.142   -0.672  1.00 23.97 ? 245 SER A C   1 
ATOM   1796 O  O   . SER A 1 245 ? 11.494 7.877   0.302   1.00 25.37 ? 245 SER A O   1 
ATOM   1797 C  CB  . SER A 1 245 ? 11.717 5.109   0.698   1.00 24.66 ? 245 SER A CB  1 
ATOM   1798 O  OG  . SER A 1 245 ? 11.172 3.894   1.162   1.00 27.24 ? 245 SER A OG  1 
ATOM   1799 N  N   . PHE A 1 246 ? 11.476 7.582   -1.918  1.00 22.55 ? 246 PHE A N   1 
ATOM   1800 C  CA  . PHE A 1 246 ? 11.857 8.969   -2.176  1.00 25.19 ? 246 PHE A CA  1 
ATOM   1801 C  C   . PHE A 1 246 ? 10.991 9.573   -3.272  1.00 27.37 ? 246 PHE A C   1 
ATOM   1802 O  O   . PHE A 1 246 ? 10.944 9.053   -4.389  1.00 26.76 ? 246 PHE A O   1 
ATOM   1803 C  CB  . PHE A 1 246 ? 13.334 9.084   -2.559  1.00 27.23 ? 246 PHE A CB  1 
ATOM   1804 C  CG  . PHE A 1 246 ? 13.746 10.482  -2.929  1.00 22.85 ? 246 PHE A CG  1 
ATOM   1805 C  CD1 . PHE A 1 246 ? 13.959 11.437  -1.957  1.00 24.14 ? 246 PHE A CD1 1 
ATOM   1806 C  CD2 . PHE A 1 246 ? 13.899 10.843  -4.259  1.00 26.67 ? 246 PHE A CD2 1 
ATOM   1807 C  CE1 . PHE A 1 246 ? 14.331 12.728  -2.300  1.00 26.00 ? 246 PHE A CE1 1 
ATOM   1808 C  CE2 . PHE A 1 246 ? 14.268 12.138  -4.611  1.00 29.17 ? 246 PHE A CE2 1 
ATOM   1809 C  CZ  . PHE A 1 246 ? 14.481 13.079  -3.632  1.00 25.58 ? 246 PHE A CZ  1 
ATOM   1810 N  N   . SER A 1 247 ? 10.355 10.699  -2.964  1.00 26.67 ? 247 SER A N   1 
ATOM   1811 C  CA  . SER A 1 247 ? 9.573  11.470  -3.922  1.00 28.27 ? 247 SER A CA  1 
ATOM   1812 C  C   . SER A 1 247 ? 10.238 12.824  -4.135  1.00 26.80 ? 247 SER A C   1 
ATOM   1813 O  O   . SER A 1 247 ? 10.450 13.568  -3.171  1.00 24.54 ? 247 SER A O   1 
ATOM   1814 C  CB  . SER A 1 247 ? 8.140  11.651  -3.428  1.00 26.88 ? 247 SER A CB  1 
ATOM   1815 O  OG  . SER A 1 247 ? 7.487  12.706  -4.118  1.00 26.81 ? 247 SER A OG  1 
ATOM   1816 N  N   . PHE A 1 248 ? 10.571 13.134  -5.395  1.00 27.56 ? 248 PHE A N   1 
ATOM   1817 C  CA  . PHE A 1 248 ? 11.081 14.462  -5.739  1.00 28.37 ? 248 PHE A CA  1 
ATOM   1818 C  C   . PHE A 1 248 ? 10.128 15.561  -5.281  1.00 28.46 ? 248 PHE A C   1 
ATOM   1819 O  O   . PHE A 1 248 ? 10.565 16.596  -4.770  1.00 26.99 ? 248 PHE A O   1 
ATOM   1820 C  CB  . PHE A 1 248 ? 11.300 14.580  -7.250  1.00 30.21 ? 248 PHE A CB  1 
ATOM   1821 C  CG  . PHE A 1 248 ? 12.688 14.216  -7.712  1.00 34.14 ? 248 PHE A CG  1 
ATOM   1822 C  CD1 . PHE A 1 248 ? 13.809 14.809  -7.144  1.00 33.08 ? 248 PHE A CD1 1 
ATOM   1823 C  CD2 . PHE A 1 248 ? 12.868 13.307  -8.747  1.00 33.80 ? 248 PHE A CD2 1 
ATOM   1824 C  CE1 . PHE A 1 248 ? 15.090 14.479  -7.584  1.00 33.14 ? 248 PHE A CE1 1 
ATOM   1825 C  CE2 . PHE A 1 248 ? 14.141 12.971  -9.191  1.00 30.54 ? 248 PHE A CE2 1 
ATOM   1826 C  CZ  . PHE A 1 248 ? 15.253 13.557  -8.611  1.00 31.44 ? 248 PHE A CZ  1 
ATOM   1827 N  N   . GLU A 1 249 ? 8.823  15.362  -5.469  1.00 27.00 ? 249 GLU A N   1 
ATOM   1828 C  CA  . GLU A 1 249 ? 7.867  16.424  -5.160  1.00 27.62 ? 249 GLU A CA  1 
ATOM   1829 C  C   . GLU A 1 249 ? 7.743  16.635  -3.655  1.00 27.98 ? 249 GLU A C   1 
ATOM   1830 O  O   . GLU A 1 249 ? 7.691  17.782  -3.183  1.00 28.41 ? 249 GLU A O   1 
ATOM   1831 C  CB  . GLU A 1 249 ? 6.509  16.104  -5.786  1.00 27.56 ? 249 GLU A CB  1 
ATOM   1832 N  N   . VAL A 1 250 ? 7.723  15.542  -2.883  1.00 25.09 ? 250 VAL A N   1 
ATOM   1833 C  CA  . VAL A 1 250 ? 7.716  15.668  -1.429  1.00 24.52 ? 250 VAL A CA  1 
ATOM   1834 C  C   . VAL A 1 250 ? 8.974  16.380  -0.959  1.00 26.61 ? 250 VAL A C   1 
ATOM   1835 O  O   . VAL A 1 250 ? 8.921  17.255  -0.087  1.00 24.60 ? 250 VAL A O   1 
ATOM   1836 C  CB  . VAL A 1 250 ? 7.585  14.288  -0.760  1.00 24.72 ? 250 VAL A CB  1 
ATOM   1837 C  CG1 . VAL A 1 250 ? 7.777  14.422  0.751   1.00 24.51 ? 250 VAL A CG1 1 
ATOM   1838 C  CG2 . VAL A 1 250 ? 6.237  13.648  -1.084  1.00 22.32 ? 250 VAL A CG2 1 
ATOM   1839 N  N   . ALA A 1 251 ? 10.124 16.009  -1.524  1.00 22.77 ? 251 ALA A N   1 
ATOM   1840 C  CA  . ALA A 1 251 ? 11.387 16.575  -1.066  1.00 25.68 ? 251 ALA A CA  1 
ATOM   1841 C  C   . ALA A 1 251 ? 11.491 18.050  -1.421  1.00 24.94 ? 251 ALA A C   1 
ATOM   1842 O  O   . ALA A 1 251 ? 11.945 18.855  -0.605  1.00 27.60 ? 251 ALA A O   1 
ATOM   1843 C  CB  . ALA A 1 251 ? 12.559 15.794  -1.659  1.00 23.31 ? 251 ALA A CB  1 
ATOM   1844 N  N   . ARG A 1 252 ? 11.094 18.417  -2.641  1.00 28.37 ? 252 ARG A N   1 
ATOM   1845 C  CA  . ARG A 1 252 ? 11.050 19.824  -3.033  1.00 27.49 ? 252 ARG A CA  1 
ATOM   1846 C  C   . ARG A 1 252 ? 10.174 20.632  -2.086  1.00 28.43 ? 252 ARG A C   1 
ATOM   1847 O  O   . ARG A 1 252 ? 10.557 21.722  -1.641  1.00 31.27 ? 252 ARG A O   1 
ATOM   1848 C  CB  . ARG A 1 252 ? 10.522 19.946  -4.462  1.00 30.39 ? 252 ARG A CB  1 
ATOM   1849 C  CG  . ARG A 1 252 ? 11.568 19.857  -5.546  1.00 33.02 ? 252 ARG A CG  1 
ATOM   1850 C  CD  . ARG A 1 252 ? 11.090 20.562  -6.809  1.00 35.77 ? 252 ARG A CD  1 
ATOM   1851 N  NE  . ARG A 1 252 ? 11.106 19.665  -7.958  1.00 43.51 ? 252 ARG A NE  1 
ATOM   1852 C  CZ  . ARG A 1 252 ? 12.184 19.384  -8.678  1.00 43.92 ? 252 ARG A CZ  1 
ATOM   1853 N  NH1 . ARG A 1 252 ? 13.361 19.926  -8.404  1.00 42.56 ? 252 ARG A NH1 1 
ATOM   1854 N  NH2 . ARG A 1 252 ? 12.080 18.532  -9.695  1.00 40.57 ? 252 ARG A NH2 1 
ATOM   1855 N  N   . ARG A 1 253 ? 8.979  20.123  -1.778  1.00 30.53 ? 253 ARG A N   1 
ATOM   1856 C  CA  . ARG A 1 253 ? 8.081  20.893  -0.927  1.00 28.27 ? 253 ARG A CA  1 
ATOM   1857 C  C   . ARG A 1 253 ? 8.631  21.010  0.493   1.00 31.58 ? 253 ARG A C   1 
ATOM   1858 O  O   . ARG A 1 253 ? 8.625  22.100  1.078   1.00 32.39 ? 253 ARG A O   1 
ATOM   1859 C  CB  . ARG A 1 253 ? 6.689  20.263  -0.935  1.00 30.77 ? 253 ARG A CB  1 
ATOM   1860 C  CG  . ARG A 1 253 ? 5.700  20.928  -0.007  1.00 33.63 ? 253 ARG A CG  1 
ATOM   1861 C  CD  . ARG A 1 253 ? 5.554  22.404  -0.347  1.00 36.79 ? 253 ARG A CD  1 
ATOM   1862 N  NE  . ARG A 1 253 ? 4.563  23.062  0.495   1.00 37.23 ? 253 ARG A NE  1 
ATOM   1863 C  CZ  . ARG A 1 253 ? 4.361  24.371  0.526   1.00 41.31 ? 253 ARG A CZ  1 
ATOM   1864 N  NH1 . ARG A 1 253 ? 5.122  25.202  -0.169  1.00 45.94 ? 253 ARG A NH1 1 
ATOM   1865 N  NH2 . ARG A 1 253 ? 3.371  24.858  1.270   1.00 39.61 ? 253 ARG A NH2 1 
ATOM   1866 N  N   . ALA A 1 254 ? 9.134  19.910  1.060   1.00 32.34 ? 254 ALA A N   1 
ATOM   1867 C  CA  . ALA A 1 254 ? 9.687  19.982  2.410   1.00 32.32 ? 254 ALA A CA  1 
ATOM   1868 C  C   . ALA A 1 254 ? 10.892 20.915  2.463   1.00 31.99 ? 254 ALA A C   1 
ATOM   1869 O  O   . ALA A 1 254 ? 11.046 21.684  3.418   1.00 31.59 ? 254 ALA A O   1 
ATOM   1870 C  CB  . ALA A 1 254 ? 10.062 18.588  2.906   1.00 29.69 ? 254 ALA A CB  1 
ATOM   1871 N  N   . ILE A 1 255 ? 11.750 20.872  1.440   1.00 31.84 ? 255 ILE A N   1 
ATOM   1872 C  CA  . ILE A 1 255 ? 12.912 21.749  1.395   1.00 31.39 ? 255 ILE A CA  1 
ATOM   1873 C  C   . ILE A 1 255 ? 12.490 23.212  1.247   1.00 33.20 ? 255 ILE A C   1 
ATOM   1874 O  O   . ILE A 1 255 ? 13.147 24.113  1.785   1.00 33.52 ? 255 ILE A O   1 
ATOM   1875 C  CB  . ILE A 1 255 ? 13.853 21.278  0.264   1.00 33.92 ? 255 ILE A CB  1 
ATOM   1876 C  CG1 . ILE A 1 255 ? 14.596 20.004  0.695   1.00 31.22 ? 255 ILE A CG1 1 
ATOM   1877 C  CG2 . ILE A 1 255 ? 14.837 22.366  -0.140  1.00 36.62 ? 255 ILE A CG2 1 
ATOM   1878 C  CD1 . ILE A 1 255 ? 15.224 19.211  -0.447  1.00 31.04 ? 255 ILE A CD1 1 
ATOM   1879 N  N   . ALA A 1 256 ? 11.383 23.483  0.549   1.00 35.94 ? 256 ALA A N   1 
ATOM   1880 C  CA  . ALA A 1 256 ? 10.885 24.855  0.499   1.00 31.61 ? 256 ALA A CA  1 
ATOM   1881 C  C   . ALA A 1 256 ? 10.314 25.295  1.843   1.00 34.94 ? 256 ALA A C   1 
ATOM   1882 O  O   . ALA A 1 256 ? 10.285 26.495  2.145   1.00 34.88 ? 256 ALA A O   1 
ATOM   1883 C  CB  . ALA A 1 256 ? 9.829  25.000  -0.598  1.00 36.06 ? 256 ALA A CB  1 
ATOM   1884 N  N   . LEU A 1 257 ? 9.851  24.354  2.657   1.00 31.40 ? 257 LEU A N   1 
ATOM   1885 C  CA  . LEU A 1 257 ? 9.369  24.691  3.989   1.00 34.86 ? 257 LEU A CA  1 
ATOM   1886 C  C   . LEU A 1 257 ? 10.496 24.813  5.004   1.00 33.42 ? 257 LEU A C   1 
ATOM   1887 O  O   . LEU A 1 257 ? 10.221 24.974  6.197   1.00 35.44 ? 257 LEU A O   1 
ATOM   1888 C  CB  . LEU A 1 257 ? 8.346  23.651  4.462   1.00 33.61 ? 257 LEU A CB  1 
ATOM   1889 C  CG  . LEU A 1 257 ? 6.989  23.651  3.755   1.00 31.32 ? 257 LEU A CG  1 
ATOM   1890 C  CD1 . LEU A 1 257 ? 6.141  22.472  4.208   1.00 34.65 ? 257 LEU A CD1 1 
ATOM   1891 C  CD2 . LEU A 1 257 ? 6.241  24.968  3.965   1.00 33.88 ? 257 LEU A CD2 1 
ATOM   1892 N  N   . GLY A 1 258 ? 11.749 24.745  4.561   1.00 33.15 ? 258 GLY A N   1 
ATOM   1893 C  CA  . GLY A 1 258 ? 12.870 24.787  5.476   1.00 31.31 ? 258 GLY A CA  1 
ATOM   1894 C  C   . GLY A 1 258 ? 13.126 23.495  6.212   1.00 34.94 ? 258 GLY A C   1 
ATOM   1895 O  O   . GLY A 1 258 ? 13.783 23.509  7.258   1.00 33.48 ? 258 GLY A O   1 
ATOM   1896 N  N   . ILE A 1 259 ? 12.630 22.372  5.699   1.00 29.56 ? 259 ILE A N   1 
ATOM   1897 C  CA  . ILE A 1 259 ? 12.790 21.088  6.367   1.00 30.54 ? 259 ILE A CA  1 
ATOM   1898 C  C   . ILE A 1 259 ? 13.800 20.255  5.590   1.00 31.45 ? 259 ILE A C   1 
ATOM   1899 O  O   . ILE A 1 259 ? 13.424 19.398  4.782   1.00 31.42 ? 259 ILE A O   1 
ATOM   1900 C  CB  . ILE A 1 259 ? 11.440 20.356  6.495   1.00 31.12 ? 259 ILE A CB  1 
ATOM   1901 C  CG1 . ILE A 1 259 ? 10.393 21.276  7.121   1.00 30.49 ? 259 ILE A CG1 1 
ATOM   1902 C  CG2 . ILE A 1 259 ? 11.589 19.117  7.353   1.00 31.09 ? 259 ILE A CG2 1 
ATOM   1903 C  CD1 . ILE A 1 259 ? 10.818 21.862  8.451   1.00 31.30 ? 259 ILE A CD1 1 
ATOM   1904 N  N   . LEU A 1 260 ? 15.092 20.514  5.816   1.00 27.49 ? 260 LEU A N   1 
ATOM   1905 C  CA  . LEU A 1 260 ? 16.162 19.814  5.127   1.00 28.33 ? 260 LEU A CA  1 
ATOM   1906 C  C   . LEU A 1 260 ? 16.488 18.509  5.841   1.00 26.35 ? 260 LEU A C   1 
ATOM   1907 O  O   . LEU A 1 260 ? 16.263 18.383  7.047   1.00 26.78 ? 260 LEU A O   1 
ATOM   1908 C  CB  . LEU A 1 260 ? 17.416 20.679  5.066   1.00 25.90 ? 260 LEU A CB  1 
ATOM   1909 C  CG  . LEU A 1 260 ? 17.329 21.967  4.251   1.00 32.85 ? 260 LEU A CG  1 
ATOM   1910 C  CD1 . LEU A 1 260 ? 18.699 22.602  4.150   1.00 28.41 ? 260 LEU A CD1 1 
ATOM   1911 C  CD2 . LEU A 1 260 ? 16.754 21.699  2.879   1.00 34.27 ? 260 LEU A CD2 1 
ATOM   1912 N  N   . PRO A 1 261 ? 17.036 17.525  5.125   1.00 24.35 ? 261 PRO A N   1 
ATOM   1913 C  CA  . PRO A 1 261 ? 17.409 16.276  5.789   1.00 24.17 ? 261 PRO A CA  1 
ATOM   1914 C  C   . PRO A 1 261 ? 18.592 16.506  6.709   1.00 26.24 ? 261 PRO A C   1 
ATOM   1915 O  O   . PRO A 1 261 ? 19.479 17.317  6.425   1.00 24.08 ? 261 PRO A O   1 
ATOM   1916 C  CB  . PRO A 1 261 ? 17.765 15.342  4.626   1.00 24.00 ? 261 PRO A CB  1 
ATOM   1917 C  CG  . PRO A 1 261 ? 18.236 16.260  3.550   1.00 26.51 ? 261 PRO A CG  1 
ATOM   1918 C  CD  . PRO A 1 261 ? 17.412 17.521  3.697   1.00 26.32 ? 261 PRO A CD  1 
ATOM   1919 N  N   . HIS A 1 262 ? 18.574 15.823  7.847   1.00 21.58 ? 262 HIS A N   1 
ATOM   1920 C  CA  . HIS A 1 262 ? 19.773 15.799  8.672   1.00 22.41 ? 262 HIS A CA  1 
ATOM   1921 C  C   . HIS A 1 262 ? 20.853 14.969  7.990   1.00 23.34 ? 262 HIS A C   1 
ATOM   1922 O  O   . HIS A 1 262 ? 21.991 15.425  7.820   1.00 19.90 ? 262 HIS A O   1 
ATOM   1923 C  CB  . HIS A 1 262 ? 19.448 15.258  10.064  1.00 24.29 ? 262 HIS A CB  1 
ATOM   1924 C  CG  . HIS A 1 262 ? 20.584 15.375  11.034  1.00 28.43 ? 262 HIS A CG  1 
ATOM   1925 N  ND1 . HIS A 1 262 ? 21.225 14.280  11.574  1.00 27.11 ? 262 HIS A ND1 1 
ATOM   1926 C  CD2 . HIS A 1 262 ? 21.206 16.464  11.546  1.00 28.35 ? 262 HIS A CD2 1 
ATOM   1927 C  CE1 . HIS A 1 262 ? 22.186 14.690  12.384  1.00 28.10 ? 262 HIS A CE1 1 
ATOM   1928 N  NE2 . HIS A 1 262 ? 22.193 16.011  12.386  1.00 27.39 ? 262 HIS A NE2 1 
ATOM   1929 N  N   . THR A 1 263 ? 20.502 13.761  7.551   1.00 17.50 ? 263 THR A N   1 
ATOM   1930 C  CA  . THR A 1 263 ? 21.428 12.907  6.823   1.00 20.81 ? 263 THR A CA  1 
ATOM   1931 C  C   . THR A 1 263 ? 20.812 12.468  5.502   1.00 19.57 ? 263 THR A C   1 
ATOM   1932 O  O   . THR A 1 263 ? 19.594 12.299  5.385   1.00 20.86 ? 263 THR A O   1 
ATOM   1933 C  CB  . THR A 1 263 ? 21.845 11.669  7.641   1.00 23.20 ? 263 THR A CB  1 
ATOM   1934 O  OG1 . THR A 1 263 ? 20.704 10.846  7.917   1.00 22.30 ? 263 THR A OG1 1 
ATOM   1935 C  CG2 . THR A 1 263 ? 22.514 12.088  8.943   1.00 23.60 ? 263 THR A CG2 1 
ATOM   1936 N  N   . ILE A 1 264 ? 21.675 12.307  4.502   1.00 17.42 ? 264 ILE A N   1 
ATOM   1937 C  CA  . ILE A 1 264 ? 21.309 11.718  3.221   1.00 20.50 ? 264 ILE A CA  1 
ATOM   1938 C  C   . ILE A 1 264 ? 21.850 10.298  3.183   1.00 20.02 ? 264 ILE A C   1 
ATOM   1939 O  O   . ILE A 1 264 ? 23.022 10.060  3.506   1.00 19.86 ? 264 ILE A O   1 
ATOM   1940 C  CB  . ILE A 1 264 ? 21.862 12.538  2.046   1.00 19.12 ? 264 ILE A CB  1 
ATOM   1941 C  CG1 . ILE A 1 264 ? 21.164 13.891  1.962   1.00 22.27 ? 264 ILE A CG1 1 
ATOM   1942 C  CG2 . ILE A 1 264 ? 21.715 11.766  0.741   1.00 20.53 ? 264 ILE A CG2 1 
ATOM   1943 C  CD1 . ILE A 1 264 ? 21.812 14.835  0.961   1.00 24.46 ? 264 ILE A CD1 1 
ATOM   1944 N  N   . SER A 1 265 ? 21.001 9.358   2.791   1.00 16.71 ? 265 SER A N   1 
ATOM   1945 C  CA  . SER A 1 265 ? 21.358 7.952   2.741   1.00 18.52 ? 265 SER A CA  1 
ATOM   1946 C  C   . SER A 1 265 ? 20.567 7.315   1.609   1.00 18.95 ? 265 SER A C   1 
ATOM   1947 O  O   . SER A 1 265 ? 19.563 7.861   1.151   1.00 18.97 ? 265 SER A O   1 
ATOM   1948 C  CB  . SER A 1 265 ? 21.069 7.252   4.070   1.00 20.34 ? 265 SER A CB  1 
ATOM   1949 O  OG  . SER A 1 265 ? 19.670 7.218   4.297   1.00 18.36 ? 265 SER A OG  1 
ATOM   1950 N  N   . SER A 1 266 ? 21.023 6.143   1.172   1.00 16.98 ? 266 SER A N   1 
ATOM   1951 C  CA  . SER A 1 266 ? 20.617 5.595   -0.115  1.00 21.16 ? 266 SER A CA  1 
ATOM   1952 C  C   . SER A 1 266 ? 19.556 4.510   -0.024  1.00 19.80 ? 266 SER A C   1 
ATOM   1953 O  O   . SER A 1 266 ? 18.773 4.360   -0.968  1.00 21.48 ? 266 SER A O   1 
ATOM   1954 C  CB  . SER A 1 266 ? 21.837 5.022   -0.841  1.00 20.00 ? 266 SER A CB  1 
ATOM   1955 O  OG  . SER A 1 266 ? 22.410 3.993   -0.057  1.00 21.74 ? 266 SER A OG  1 
ATOM   1956 N  N   . ASP A 1 267 ? 19.515 3.759   1.080   1.00 18.14 ? 267 ASP A N   1 
ATOM   1957 C  CA  . ASP A 1 267 ? 18.722 2.527   1.177   1.00 20.20 ? 267 ASP A CA  1 
ATOM   1958 C  C   . ASP A 1 267 ? 19.054 1.595   0.014   1.00 21.21 ? 267 ASP A C   1 
ATOM   1959 O  O   . ASP A 1 267 ? 18.181 1.037   -0.654  1.00 19.05 ? 267 ASP A O   1 
ATOM   1960 C  CB  . ASP A 1 267 ? 17.226 2.827   1.248   1.00 19.86 ? 267 ASP A CB  1 
ATOM   1961 C  CG  . ASP A 1 267 ? 16.397 1.593   1.568   1.00 22.59 ? 267 ASP A CG  1 
ATOM   1962 O  OD1 . ASP A 1 267 ? 16.966 0.599   2.072   1.00 21.06 ? 267 ASP A OD1 1 
ATOM   1963 O  OD2 . ASP A 1 267 ? 15.186 1.595   1.266   1.00 24.52 ? 267 ASP A OD2 1 
ATOM   1964 N  N   . ILE A 1 268 ? 20.346 1.416   -0.205  1.00 20.16 ? 268 ILE A N   1 
ATOM   1965 C  CA  . ILE A 1 268 ? 20.858 0.736   -1.382  1.00 20.02 ? 268 ILE A CA  1 
ATOM   1966 C  C   . ILE A 1 268 ? 20.987 -0.756  -1.103  1.00 22.97 ? 268 ILE A C   1 
ATOM   1967 O  O   . ILE A 1 268 ? 21.338 -1.184  0.005   1.00 17.47 ? 268 ILE A O   1 
ATOM   1968 C  CB  . ILE A 1 268 ? 22.204 1.361   -1.804  1.00 19.96 ? 268 ILE A CB  1 
ATOM   1969 C  CG1 . ILE A 1 268 ? 22.642 0.887   -3.188  1.00 22.47 ? 268 ILE A CG1 1 
ATOM   1970 C  CG2 . ILE A 1 268 ? 23.287 1.081   -0.765  1.00 19.01 ? 268 ILE A CG2 1 
ATOM   1971 C  CD1 . ILE A 1 268 ? 23.803 1.723   -3.765  1.00 20.53 ? 268 ILE A CD1 1 
ATOM   1972 N  N   . TYR A 1 269 ? 20.666 -1.556  -2.111  1.00 21.06 ? 269 TYR A N   1 
ATOM   1973 C  CA  . TYR A 1 269 ? 21.045 -2.960  -2.136  1.00 23.46 ? 269 TYR A CA  1 
ATOM   1974 C  C   . TYR A 1 269 ? 21.331 -3.299  -3.590  1.00 26.57 ? 269 TYR A C   1 
ATOM   1975 O  O   . TYR A 1 269 ? 21.263 -2.431  -4.465  1.00 21.82 ? 269 TYR A O   1 
ATOM   1976 C  CB  . TYR A 1 269 ? 19.978 -3.843  -1.480  1.00 22.78 ? 269 TYR A CB  1 
ATOM   1977 C  CG  . TYR A 1 269 ? 18.747 -4.073  -2.308  1.00 24.88 ? 269 TYR A CG  1 
ATOM   1978 C  CD1 . TYR A 1 269 ? 17.804 -3.067  -2.472  1.00 25.55 ? 269 TYR A CD1 1 
ATOM   1979 C  CD2 . TYR A 1 269 ? 18.494 -5.314  -2.882  1.00 29.27 ? 269 TYR A CD2 1 
ATOM   1980 C  CE1 . TYR A 1 269 ? 16.667 -3.271  -3.211  1.00 24.61 ? 269 TYR A CE1 1 
ATOM   1981 C  CE2 . TYR A 1 269 ? 17.349 -5.534  -3.622  1.00 33.42 ? 269 TYR A CE2 1 
ATOM   1982 C  CZ  . TYR A 1 269 ? 16.439 -4.506  -3.788  1.00 32.68 ? 269 TYR A CZ  1 
ATOM   1983 O  OH  . TYR A 1 269 ? 15.297 -4.716  -4.530  1.00 34.59 ? 269 TYR A OH  1 
ATOM   1984 N  N   . CYS A 1 270 ? 21.674 -4.562  -3.848  1.00 25.57 ? 270 CYS A N   1 
ATOM   1985 C  CA  . CYS A 1 270 ? 22.228 -4.895  -5.158  1.00 23.98 ? 270 CYS A CA  1 
ATOM   1986 C  C   . CYS A 1 270 ? 21.276 -4.505  -6.286  1.00 27.18 ? 270 CYS A C   1 
ATOM   1987 O  O   . CYS A 1 270 ? 21.712 -3.958  -7.307  1.00 28.98 ? 270 CYS A O   1 
ATOM   1988 C  CB  . CYS A 1 270 ? 22.594 -6.384  -5.220  1.00 25.40 ? 270 CYS A CB  1 
ATOM   1989 S  SG  . CYS A 1 270 ? 21.231 -7.541  -5.026  1.00 34.55 ? 270 CYS A SG  1 
ATOM   1990 N  N   . ARG A 1 271 ? 19.968 -4.721  -6.104  1.00 26.48 ? 271 ARG A N   1 
ATOM   1991 C  CA  . ARG A 1 271 ? 19.036 -4.504  -7.209  1.00 29.67 ? 271 ARG A CA  1 
ATOM   1992 C  C   . ARG A 1 271 ? 18.882 -3.019  -7.529  1.00 28.80 ? 271 ARG A C   1 
ATOM   1993 O  O   . ARG A 1 271 ? 19.013 -2.613  -8.691  1.00 27.78 ? 271 ARG A O   1 
ATOM   1994 C  CB  . ARG A 1 271 ? 17.675 -5.140  -6.909  1.00 28.63 ? 271 ARG A CB  1 
ATOM   1995 N  N   . ASN A 1 272 ? 18.609 -2.182  -6.526  1.00 26.53 ? 272 ASN A N   1 
ATOM   1996 C  CA  . ASN A 1 272 ? 18.433 -0.775  -6.869  1.00 25.73 ? 272 ASN A CA  1 
ATOM   1997 C  C   . ASN A 1 272 ? 19.762 -0.051  -7.075  1.00 25.29 ? 272 ASN A C   1 
ATOM   1998 O  O   . ASN A 1 272 ? 19.766 1.074   -7.588  1.00 24.93 ? 272 ASN A O   1 
ATOM   1999 C  CB  . ASN A 1 272 ? 17.521 -0.069  -5.845  1.00 23.96 ? 272 ASN A CB  1 
ATOM   2000 C  CG  . ASN A 1 272 ? 18.134 0.069   -4.460  1.00 22.85 ? 272 ASN A CG  1 
ATOM   2001 O  OD1 . ASN A 1 272 ? 19.353 0.076   -4.284  1.00 19.89 ? 272 ASN A OD1 1 
ATOM   2002 N  ND2 . ASN A 1 272 ? 17.270 0.174   -3.459  1.00 21.35 ? 272 ASN A ND2 1 
ATOM   2003 N  N   . ARG A 1 273 ? 20.890 -0.688  -6.752  1.00 24.71 ? 273 ARG A N   1 
ATOM   2004 C  CA  . ARG A 1 273 ? 22.174 -0.183  -7.230  1.00 22.06 ? 273 ARG A CA  1 
ATOM   2005 C  C   . ARG A 1 273 ? 22.334 -0.455  -8.721  1.00 29.12 ? 273 ARG A C   1 
ATOM   2006 O  O   . ARG A 1 273 ? 22.552 0.470   -9.513  1.00 23.28 ? 273 ARG A O   1 
ATOM   2007 C  CB  . ARG A 1 273 ? 23.325 -0.812  -6.438  1.00 24.87 ? 273 ARG A CB  1 
ATOM   2008 C  CG  . ARG A 1 273 ? 24.715 -0.508  -6.994  1.00 25.44 ? 273 ARG A CG  1 
ATOM   2009 C  CD  . ARG A 1 273 ? 25.807 -0.958  -6.037  1.00 25.98 ? 273 ARG A CD  1 
ATOM   2010 N  NE  . ARG A 1 273 ? 25.789 -2.401  -5.805  1.00 26.86 ? 273 ARG A NE  1 
ATOM   2011 C  CZ  . ARG A 1 273 ? 26.314 -3.292  -6.636  1.00 25.99 ? 273 ARG A CZ  1 
ATOM   2012 N  NH1 . ARG A 1 273 ? 26.927 -2.922  -7.745  1.00 27.27 ? 273 ARG A NH1 1 
ATOM   2013 N  NH2 . ARG A 1 273 ? 26.230 -4.585  -6.340  1.00 28.43 ? 273 ARG A NH2 1 
ATOM   2014 N  N   . ILE A 1 274 ? 22.195 -1.718  -9.127  1.00 26.76 ? 274 ILE A N   1 
ATOM   2015 C  CA  . ILE A 1 274 ? 22.460 -2.079  -10.514 1.00 31.36 ? 274 ILE A CA  1 
ATOM   2016 C  C   . ILE A 1 274 ? 21.331 -1.608  -11.432 1.00 31.13 ? 274 ILE A C   1 
ATOM   2017 O  O   . ILE A 1 274 ? 21.586 -1.106  -12.532 1.00 34.98 ? 274 ILE A O   1 
ATOM   2018 C  CB  . ILE A 1 274 ? 22.698 -3.598  -10.613 1.00 31.05 ? 274 ILE A CB  1 
ATOM   2019 C  CG1 . ILE A 1 274 ? 23.940 -3.984  -9.805  1.00 26.85 ? 274 ILE A CG1 1 
ATOM   2020 C  CG2 . ILE A 1 274 ? 22.861 -4.029  -12.058 1.00 34.75 ? 274 ILE A CG2 1 
ATOM   2021 C  CD1 . ILE A 1 274 ? 23.906 -5.404  -9.244  1.00 29.30 ? 274 ILE A CD1 1 
ATOM   2022 N  N   . ASP A 1 275 ? 20.077 -1.727  -10.988 0.91 29.76 ? 275 ASP A N   1 
ATOM   2023 C  CA  . ASP A 1 275 ? 18.900 -1.502  -11.824 0.91 33.32 ? 275 ASP A CA  1 
ATOM   2024 C  C   . ASP A 1 275 ? 18.024 -0.347  -11.370 0.91 36.31 ? 275 ASP A C   1 
ATOM   2025 O  O   . ASP A 1 275 ? 17.478 0.373   -12.213 0.91 32.57 ? 275 ASP A O   1 
ATOM   2026 C  CB  . ASP A 1 275 ? 18.020 -2.760  -11.856 0.91 35.15 ? 275 ASP A CB  1 
ATOM   2027 C  CG  . ASP A 1 275 ? 18.738 -3.968  -12.409 0.91 37.33 ? 275 ASP A CG  1 
ATOM   2028 O  OD1 . ASP A 1 275 ? 19.768 -3.799  -13.096 0.91 38.49 ? 275 ASP A OD1 1 
ATOM   2029 O  OD2 . ASP A 1 275 ? 18.262 -5.092  -12.156 0.91 42.02 ? 275 ASP A OD2 1 
ATOM   2030 N  N   . GLY A 1 276 ? 17.845 -0.178  -10.058 1.00 38.70 ? 276 GLY A N   1 
ATOM   2031 C  CA  . GLY A 1 276 ? 16.819 0.680   -9.513  1.00 27.97 ? 276 GLY A CA  1 
ATOM   2032 C  C   . GLY A 1 276 ? 17.186 2.143   -9.545  1.00 32.42 ? 276 GLY A C   1 
ATOM   2033 O  O   . GLY A 1 276 ? 18.197 2.550   -10.131 1.00 36.78 ? 276 GLY A O   1 
ATOM   2034 N  N   . PRO A 1 277 ? 16.364 2.971   -8.898  1.00 27.64 ? 277 PRO A N   1 
ATOM   2035 C  CA  . PRO A 1 277 ? 16.573 4.421   -8.948  1.00 31.57 ? 277 PRO A CA  1 
ATOM   2036 C  C   . PRO A 1 277 ? 17.653 4.939   -8.010  1.00 25.36 ? 277 PRO A C   1 
ATOM   2037 O  O   . PRO A 1 277 ? 17.897 6.152   -7.996  1.00 28.69 ? 277 PRO A O   1 
ATOM   2038 C  CB  . PRO A 1 277 ? 15.191 4.968   -8.557  1.00 27.83 ? 277 PRO A CB  1 
ATOM   2039 C  CG  . PRO A 1 277 ? 14.629 3.927   -7.656  1.00 25.69 ? 277 PRO A CG  1 
ATOM   2040 C  CD  . PRO A 1 277 ? 15.179 2.601   -8.103  1.00 27.61 ? 277 PRO A CD  1 
ATOM   2041 N  N   . VAL A 1 278 ? 18.318 4.079   -7.238  1.00 22.74 ? 278 VAL A N   1 
ATOM   2042 C  CA  . VAL A 1 278 ? 19.267 4.556   -6.236  1.00 25.81 ? 278 VAL A CA  1 
ATOM   2043 C  C   . VAL A 1 278 ? 20.648 4.736   -6.854  1.00 23.71 ? 278 VAL A C   1 
ATOM   2044 O  O   . VAL A 1 278 ? 21.216 5.831   -6.806  1.00 22.36 ? 278 VAL A O   1 
ATOM   2045 C  CB  . VAL A 1 278 ? 19.317 3.608   -5.025  1.00 22.50 ? 278 VAL A CB  1 
ATOM   2046 C  CG1 . VAL A 1 278 ? 20.405 4.042   -4.062  1.00 23.99 ? 278 VAL A CG1 1 
ATOM   2047 C  CG2 . VAL A 1 278 ? 17.978 3.607   -4.318  1.00 23.71 ? 278 VAL A CG2 1 
ATOM   2048 N  N   . ARG A 1 279 ? 21.199 3.652   -7.406  1.00 23.80 ? 279 ARG A N   1 
ATOM   2049 C  CA  . ARG A 1 279 ? 22.479 3.607   -8.115  1.00 24.90 ? 279 ARG A CA  1 
ATOM   2050 C  C   . ARG A 1 279 ? 23.695 3.799   -7.208  1.00 23.87 ? 279 ARG A C   1 
ATOM   2051 O  O   . ARG A 1 279 ? 24.591 2.946   -7.202  1.00 23.45 ? 279 ARG A O   1 
ATOM   2052 C  CB  . ARG A 1 279 ? 22.490 4.622   -9.267  1.00 24.43 ? 279 ARG A CB  1 
ATOM   2053 C  CG  . ARG A 1 279 ? 21.527 4.217   -10.374 1.00 27.18 ? 279 ARG A CG  1 
ATOM   2054 C  CD  . ARG A 1 279 ? 21.370 5.275   -11.459 1.00 32.88 ? 279 ARG A CD  1 
ATOM   2055 N  NE  . ARG A 1 279 ? 20.439 4.881   -12.517 1.00 30.46 ? 279 ARG A NE  1 
ATOM   2056 C  CZ  . ARG A 1 279 ? 20.485 3.756   -13.224 1.00 34.74 ? 279 ARG A CZ  1 
ATOM   2057 N  NH1 . ARG A 1 279 ? 21.488 2.900   -13.114 1.00 35.01 ? 279 ARG A NH1 1 
ATOM   2058 N  NH2 . ARG A 1 279 ? 19.507 3.496   -14.089 1.00 37.38 ? 279 ARG A NH2 1 
ATOM   2059 N  N   . SER A 1 280 ? 23.745 4.886   -6.441  1.00 22.43 ? 280 SER A N   1 
ATOM   2060 C  CA  . SER A 1 280 ? 24.871 5.153   -5.551  1.00 19.53 ? 280 SER A CA  1 
ATOM   2061 C  C   . SER A 1 280 ? 24.498 6.298   -4.628  1.00 22.22 ? 280 SER A C   1 
ATOM   2062 O  O   . SER A 1 280 ? 23.576 7.066   -4.912  1.00 22.01 ? 280 SER A O   1 
ATOM   2063 C  CB  . SER A 1 280 ? 26.148 5.503   -6.316  1.00 17.97 ? 280 SER A CB  1 
ATOM   2064 O  OG  . SER A 1 280 ? 26.048 6.788   -6.910  1.00 20.34 ? 280 SER A OG  1 
ATOM   2065 N  N   . LEU A 1 281 ? 25.245 6.415   -3.524  1.00 20.95 ? 281 LEU A N   1 
ATOM   2066 C  CA  . LEU A 1 281 ? 25.056 7.560   -2.636  1.00 17.77 ? 281 LEU A CA  1 
ATOM   2067 C  C   . LEU A 1 281 ? 25.387 8.856   -3.357  1.00 22.03 ? 281 LEU A C   1 
ATOM   2068 O  O   . LEU A 1 281 ? 24.739 9.883   -3.131  1.00 19.23 ? 281 LEU A O   1 
ATOM   2069 C  CB  . LEU A 1 281 ? 25.923 7.419   -1.388  1.00 20.51 ? 281 LEU A CB  1 
ATOM   2070 C  CG  . LEU A 1 281 ? 25.698 8.494   -0.331  1.00 20.23 ? 281 LEU A CG  1 
ATOM   2071 C  CD1 . LEU A 1 281 ? 24.270 8.393   0.203   1.00 17.98 ? 281 LEU A CD1 1 
ATOM   2072 C  CD2 . LEU A 1 281 ? 26.730 8.374   0.785   1.00 17.06 ? 281 LEU A CD2 1 
ATOM   2073 N  N   . ALA A 1 282 ? 26.393 8.821   -4.237  1.00 19.91 ? 282 ALA A N   1 
ATOM   2074 C  CA  . ALA A 1 282 ? 26.732 10.001  -5.024  1.00 21.43 ? 282 ALA A CA  1 
ATOM   2075 C  C   . ALA A 1 282 ? 25.539 10.490  -5.840  1.00 19.40 ? 282 ALA A C   1 
ATOM   2076 O  O   . ALA A 1 282 ? 25.289 11.698  -5.918  1.00 20.20 ? 282 ALA A O   1 
ATOM   2077 C  CB  . ALA A 1 282 ? 27.919 9.694   -5.939  1.00 23.34 ? 282 ALA A CB  1 
ATOM   2078 N  N   . LEU A 1 283 ? 24.768 9.570   -6.434  1.00 18.74 ? 283 LEU A N   1 
ATOM   2079 C  CA  . LEU A 1 283 ? 23.644 9.997   -7.267  1.00 22.83 ? 283 LEU A CA  1 
ATOM   2080 C  C   . LEU A 1 283 ? 22.491 10.542  -6.423  1.00 21.57 ? 283 LEU A C   1 
ATOM   2081 O  O   . LEU A 1 283 ? 21.825 11.509  -6.819  1.00 21.94 ? 283 LEU A O   1 
ATOM   2082 C  CB  . LEU A 1 283 ? 23.167 8.847   -8.158  1.00 21.22 ? 283 LEU A CB  1 
ATOM   2083 C  CG  . LEU A 1 283 ? 23.733 8.781   -9.583  1.00 29.42 ? 283 LEU A CG  1 
ATOM   2084 C  CD1 . LEU A 1 283 ? 23.095 9.843   -10.487 1.00 28.37 ? 283 LEU A CD1 1 
ATOM   2085 C  CD2 . LEU A 1 283 ? 25.239 8.905   -9.614  1.00 28.05 ? 283 LEU A CD2 1 
ATOM   2086 N  N   . VAL A 1 284 ? 22.241 9.937   -5.261  1.00 21.45 ? 284 VAL A N   1 
ATOM   2087 C  CA  . VAL A 1 284 ? 21.240 10.467  -4.334  1.00 21.15 ? 284 VAL A CA  1 
ATOM   2088 C  C   . VAL A 1 284 ? 21.614 11.886  -3.890  1.00 20.08 ? 284 VAL A C   1 
ATOM   2089 O  O   . VAL A 1 284 ? 20.790 12.822  -3.925  1.00 21.06 ? 284 VAL A O   1 
ATOM   2090 C  CB  . VAL A 1 284 ? 21.092 9.517   -3.132  1.00 19.35 ? 284 VAL A CB  1 
ATOM   2091 C  CG1 . VAL A 1 284 ? 20.202 10.136  -2.061  1.00 18.58 ? 284 VAL A CG1 1 
ATOM   2092 C  CG2 . VAL A 1 284 ? 20.549 8.153   -3.588  1.00 20.86 ? 284 VAL A CG2 1 
ATOM   2093 N  N   . MET A 1 285 ? 22.865 12.057  -3.444  1.00 18.96 ? 285 MET A N   1 
ATOM   2094 C  CA  . MET A 1 285 ? 23.368 13.388  -3.114  1.00 21.91 ? 285 MET A CA  1 
ATOM   2095 C  C   . MET A 1 285 ? 23.156 14.360  -4.269  1.00 19.94 ? 285 MET A C   1 
ATOM   2096 O  O   . MET A 1 285 ? 22.762 15.518  -4.060  1.00 21.30 ? 285 MET A O   1 
ATOM   2097 C  CB  . MET A 1 285 ? 24.854 13.309  -2.741  1.00 19.29 ? 285 MET A CB  1 
ATOM   2098 C  CG  . MET A 1 285 ? 25.142 12.551  -1.457  1.00 19.79 ? 285 MET A CG  1 
ATOM   2099 S  SD  . MET A 1 285 ? 26.863 11.991  -1.303  1.00 22.71 ? 285 MET A SD  1 
ATOM   2100 C  CE  . MET A 1 285 ? 27.735 13.548  -1.323  1.00 22.40 ? 285 MET A CE  1 
ATOM   2101 N  N   . SER A 1 286 ? 23.421 13.905  -5.498  1.00 19.36 ? 286 SER A N   1 
ATOM   2102 C  CA  . SER A 1 286 ? 23.257 14.771  -6.660  1.00 21.15 ? 286 SER A CA  1 
ATOM   2103 C  C   . SER A 1 286 ? 21.809 15.208  -6.821  1.00 22.13 ? 286 SER A C   1 
ATOM   2104 O  O   . SER A 1 286 ? 21.541 16.338  -7.245  1.00 21.37 ? 286 SER A O   1 
ATOM   2105 C  CB  . SER A 1 286 ? 23.744 14.055  -7.922  1.00 20.23 ? 286 SER A CB  1 
ATOM   2106 O  OG  . SER A 1 286 ? 25.141 13.823  -7.844  1.00 19.30 ? 286 SER A OG  1 
ATOM   2107 N  N   . LYS A 1 287 ? 20.863 14.313  -6.517  1.00 24.12 ? 287 LYS A N   1 
ATOM   2108 C  CA  . LYS A 1 287 ? 19.455 14.703  -6.559  1.00 25.00 ? 287 LYS A CA  1 
ATOM   2109 C  C   . LYS A 1 287 ? 19.187 15.849  -5.597  1.00 24.12 ? 287 LYS A C   1 
ATOM   2110 O  O   . LYS A 1 287 ? 18.432 16.781  -5.909  1.00 26.39 ? 287 LYS A O   1 
ATOM   2111 C  CB  . LYS A 1 287 ? 18.562 13.510  -6.222  1.00 24.94 ? 287 LYS A CB  1 
ATOM   2112 C  CG  . LYS A 1 287 ? 18.536 12.457  -7.306  1.00 25.92 ? 287 LYS A CG  1 
ATOM   2113 C  CD  . LYS A 1 287 ? 17.851 11.188  -6.839  1.00 25.24 ? 287 LYS A CD  1 
ATOM   2114 C  CE  . LYS A 1 287 ? 17.205 10.464  -8.001  1.00 27.98 ? 287 LYS A CE  1 
ATOM   2115 N  NZ  . LYS A 1 287 ? 17.245 8.990   -7.777  1.00 29.40 ? 287 LYS A NZ  1 
ATOM   2116 N  N   . PHE A 1 288 ? 19.814 15.810  -4.424  1.00 22.48 ? 288 PHE A N   1 
ATOM   2117 C  CA  . PHE A 1 288 ? 19.574 16.920  -3.496  1.00 22.59 ? 288 PHE A CA  1 
ATOM   2118 C  C   . PHE A 1 288 ? 20.269 18.207  -3.943  1.00 24.92 ? 288 PHE A C   1 
ATOM   2119 O  O   . PHE A 1 288 ? 19.757 19.311  -3.695  1.00 21.01 ? 288 PHE A O   1 
ATOM   2120 C  CB  . PHE A 1 288 ? 19.974 16.503  -2.087  1.00 24.32 ? 288 PHE A CB  1 
ATOM   2121 C  CG  . PHE A 1 288 ? 18.996 15.558  -1.494  1.00 25.08 ? 288 PHE A CG  1 
ATOM   2122 C  CD1 . PHE A 1 288 ? 17.788 16.020  -0.999  1.00 25.38 ? 288 PHE A CD1 1 
ATOM   2123 C  CD2 . PHE A 1 288 ? 19.224 14.196  -1.538  1.00 24.43 ? 288 PHE A CD2 1 
ATOM   2124 C  CE1 . PHE A 1 288 ? 16.854 15.140  -0.499  1.00 25.44 ? 288 PHE A CE1 1 
ATOM   2125 C  CE2 . PHE A 1 288 ? 18.293 13.318  -1.042  1.00 24.33 ? 288 PHE A CE2 1 
ATOM   2126 C  CZ  . PHE A 1 288 ? 17.107 13.792  -0.524  1.00 24.75 ? 288 PHE A CZ  1 
ATOM   2127 N  N   . LEU A 1 289 ? 21.408 18.091  -4.631  1.00 22.90 ? 289 LEU A N   1 
ATOM   2128 C  CA  . LEU A 1 289 ? 21.998 19.270  -5.270  1.00 23.34 ? 289 LEU A CA  1 
ATOM   2129 C  C   . LEU A 1 289 ? 21.060 19.855  -6.322  1.00 25.68 ? 289 LEU A C   1 
ATOM   2130 O  O   . LEU A 1 289 ? 20.957 21.080  -6.466  1.00 26.21 ? 289 LEU A O   1 
ATOM   2131 C  CB  . LEU A 1 289 ? 23.340 18.921  -5.913  1.00 23.16 ? 289 LEU A CB  1 
ATOM   2132 C  CG  . LEU A 1 289 ? 24.542 18.691  -5.006  1.00 23.94 ? 289 LEU A CG  1 
ATOM   2133 C  CD1 . LEU A 1 289 ? 25.705 18.236  -5.856  1.00 22.04 ? 289 LEU A CD1 1 
ATOM   2134 C  CD2 . LEU A 1 289 ? 24.893 19.978  -4.252  1.00 23.73 ? 289 LEU A CD2 1 
ATOM   2135 N  N   . ALA A 1 290 ? 20.377 18.987  -7.074  1.00 22.89 ? 290 ALA A N   1 
ATOM   2136 C  CA  . ALA A 1 290 ? 19.459 19.443  -8.110  1.00 26.50 ? 290 ALA A CA  1 
ATOM   2137 C  C   . ALA A 1 290 ? 18.224 20.109  -7.520  1.00 27.83 ? 290 ALA A C   1 
ATOM   2138 O  O   . ALA A 1 290 ? 17.668 21.028  -8.135  1.00 27.56 ? 290 ALA A O   1 
ATOM   2139 C  CB  . ALA A 1 290 ? 19.043 18.273  -9.004  1.00 24.16 ? 290 ALA A CB  1 
ATOM   2140 N  N   . ILE A 1 291 ? 17.765 19.646  -6.354  1.00 26.36 ? 291 ILE A N   1 
ATOM   2141 C  CA  . ILE A 1 291 ? 16.642 20.305  -5.692  1.00 28.96 ? 291 ILE A CA  1 
ATOM   2142 C  C   . ILE A 1 291 ? 17.039 21.665  -5.126  1.00 33.28 ? 291 ILE A C   1 
ATOM   2143 O  O   . ILE A 1 291 ? 16.170 22.522  -4.914  1.00 36.00 ? 291 ILE A O   1 
ATOM   2144 C  CB  . ILE A 1 291 ? 16.052 19.412  -4.582  1.00 31.16 ? 291 ILE A CB  1 
ATOM   2145 C  CG1 . ILE A 1 291 ? 15.719 18.026  -5.116  1.00 34.29 ? 291 ILE A CG1 1 
ATOM   2146 C  CG2 . ILE A 1 291 ? 14.775 20.008  -4.021  1.00 35.38 ? 291 ILE A CG2 1 
ATOM   2147 C  CD1 . ILE A 1 291 ? 15.259 17.079  -4.019  1.00 31.15 ? 291 ILE A CD1 1 
ATOM   2148 N  N   . GLY A 1 292 ? 18.329 21.900  -4.877  1.00 25.19 ? 292 GLY A N   1 
ATOM   2149 C  CA  . GLY A 1 292 ? 18.763 23.239  -4.527  1.00 31.12 ? 292 GLY A CA  1 
ATOM   2150 C  C   . GLY A 1 292 ? 19.639 23.365  -3.297  1.00 31.78 ? 292 GLY A C   1 
ATOM   2151 O  O   . GLY A 1 292 ? 20.083 24.470  -2.969  1.00 31.60 ? 292 GLY A O   1 
ATOM   2152 N  N   . MET A 1 293 ? 19.894 22.264  -2.597  1.00 27.57 ? 293 MET A N   1 
ATOM   2153 C  CA  . MET A 1 293 ? 20.828 22.313  -1.478  1.00 26.60 ? 293 MET A CA  1 
ATOM   2154 C  C   . MET A 1 293 ? 22.243 22.603  -1.978  1.00 25.59 ? 293 MET A C   1 
ATOM   2155 O  O   . MET A 1 293 ? 22.616 22.240  -3.095  1.00 24.94 ? 293 MET A O   1 
ATOM   2156 C  CB  . MET A 1 293 ? 20.782 21.001  -0.695  1.00 24.46 ? 293 MET A CB  1 
ATOM   2157 C  CG  . MET A 1 293 ? 19.456 20.755  0.013   1.00 24.36 ? 293 MET A CG  1 
ATOM   2158 S  SD  . MET A 1 293 ? 19.419 19.175  0.888   1.00 27.85 ? 293 MET A SD  1 
ATOM   2159 C  CE  . MET A 1 293 ? 20.675 19.411  2.151   1.00 23.72 ? 293 MET A CE  1 
ATOM   2160 N  N   . THR A 1 294 ? 23.026 23.294  -1.150  1.00 23.90 ? 294 THR A N   1 
ATOM   2161 C  CA  . THR A 1 294 ? 24.406 23.591  -1.505  1.00 23.05 ? 294 THR A CA  1 
ATOM   2162 C  C   . THR A 1 294 ? 25.282 22.353  -1.335  1.00 25.52 ? 294 THR A C   1 
ATOM   2163 O  O   . THR A 1 294 ? 24.929 21.392  -0.643  1.00 20.68 ? 294 THR A O   1 
ATOM   2164 C  CB  . THR A 1 294 ? 24.974 24.727  -0.646  1.00 24.09 ? 294 THR A CB  1 
ATOM   2165 O  OG1 . THR A 1 294 ? 25.166 24.262  0.696   1.00 25.62 ? 294 THR A OG1 1 
ATOM   2166 C  CG2 . THR A 1 294 ? 24.054 25.932  -0.641  1.00 22.47 ? 294 THR A CG2 1 
ATOM   2167 N  N   . LEU A 1 295 ? 26.454 22.390  -1.968  1.00 24.74 ? 295 LEU A N   1 
ATOM   2168 C  CA  . LEU A 1 295 ? 27.392 21.283  -1.797  1.00 24.77 ? 295 LEU A CA  1 
ATOM   2169 C  C   . LEU A 1 295 ? 27.837 21.110  -0.343  1.00 22.41 ? 295 LEU A C   1 
ATOM   2170 O  O   . LEU A 1 295 ? 27.852 19.959  0.135   1.00 21.88 ? 295 LEU A O   1 
ATOM   2171 C  CB  . LEU A 1 295 ? 28.593 21.469  -2.735  1.00 26.93 ? 295 LEU A CB  1 
ATOM   2172 C  CG  . LEU A 1 295 ? 29.579 20.299  -2.757  1.00 24.55 ? 295 LEU A CG  1 
ATOM   2173 C  CD1 . LEU A 1 295 ? 28.868 19.027  -3.202  1.00 21.89 ? 295 LEU A CD1 1 
ATOM   2174 C  CD2 . LEU A 1 295 ? 30.773 20.593  -3.635  1.00 24.59 ? 295 LEU A CD2 1 
ATOM   2175 N  N   . PRO A 1 296 ? 28.194 22.165  0.407   1.00 23.45 ? 296 PRO A N   1 
ATOM   2176 C  CA  . PRO A 1 296 ? 28.491 21.956  1.837   1.00 22.03 ? 296 PRO A CA  1 
ATOM   2177 C  C   . PRO A 1 296 ? 27.370 21.265  2.601   1.00 22.78 ? 296 PRO A C   1 
ATOM   2178 O  O   . PRO A 1 296 ? 27.650 20.417  3.459   1.00 21.57 ? 296 PRO A O   1 
ATOM   2179 C  CB  . PRO A 1 296 ? 28.733 23.383  2.350   1.00 21.76 ? 296 PRO A CB  1 
ATOM   2180 C  CG  . PRO A 1 296 ? 29.241 24.114  1.164   1.00 24.22 ? 296 PRO A CG  1 
ATOM   2181 C  CD  . PRO A 1 296 ? 28.476 23.559  0.001   1.00 22.78 ? 296 PRO A CD  1 
ATOM   2182 N  N   . GLN A 1 297 ? 26.108 21.578  2.297   1.00 21.45 ? 297 GLN A N   1 
ATOM   2183 C  CA  . GLN A 1 297 ? 24.998 20.949  3.016   1.00 20.59 ? 297 GLN A CA  1 
ATOM   2184 C  C   . GLN A 1 297 ? 24.923 19.456  2.723   1.00 19.63 ? 297 GLN A C   1 
ATOM   2185 O  O   . GLN A 1 297 ? 24.781 18.637  3.638   1.00 19.25 ? 297 GLN A O   1 
ATOM   2186 C  CB  . GLN A 1 297 ? 23.680 21.623  2.647   1.00 18.92 ? 297 GLN A CB  1 
ATOM   2187 C  CG  . GLN A 1 297 ? 23.481 22.963  3.280   1.00 22.82 ? 297 GLN A CG  1 
ATOM   2188 C  CD  . GLN A 1 297 ? 22.231 23.633  2.784   1.00 23.19 ? 297 GLN A CD  1 
ATOM   2189 O  OE1 . GLN A 1 297 ? 21.910 23.580  1.595   1.00 21.39 ? 297 GLN A OE1 1 
ATOM   2190 N  NE2 . GLN A 1 297 ? 21.501 24.255  3.694   1.00 23.77 ? 297 GLN A NE2 1 
ATOM   2191 N  N   . VAL A 1 298 ? 25.004 19.085  1.445   1.00 18.59 ? 298 VAL A N   1 
ATOM   2192 C  CA  . VAL A 1 298 ? 24.927 17.675  1.068   1.00 18.70 ? 298 VAL A CA  1 
ATOM   2193 C  C   . VAL A 1 298 ? 26.093 16.891  1.674   1.00 18.21 ? 298 VAL A C   1 
ATOM   2194 O  O   . VAL A 1 298 ? 25.920 15.786  2.226   1.00 19.73 ? 298 VAL A O   1 
ATOM   2195 C  CB  . VAL A 1 298 ? 24.884 17.568  -0.466  1.00 21.62 ? 298 VAL A CB  1 
ATOM   2196 C  CG1 . VAL A 1 298 ? 24.970 16.138  -0.889  1.00 20.21 ? 298 VAL A CG1 1 
ATOM   2197 C  CG2 . VAL A 1 298 ? 23.613 18.233  -1.007  1.00 21.81 ? 298 VAL A CG2 1 
ATOM   2198 N  N   . ILE A 1 299 ? 27.294 17.475  1.622   1.00 18.09 ? 299 ILE A N   1 
ATOM   2199 C  CA  . ILE A 1 299 ? 28.467 16.806  2.178   1.00 19.72 ? 299 ILE A CA  1 
ATOM   2200 C  C   . ILE A 1 299 ? 28.338 16.660  3.690   1.00 19.11 ? 299 ILE A C   1 
ATOM   2201 O  O   . ILE A 1 299 ? 28.691 15.618  4.256   1.00 22.32 ? 299 ILE A O   1 
ATOM   2202 C  CB  . ILE A 1 299 ? 29.749 17.560  1.787   1.00 18.43 ? 299 ILE A CB  1 
ATOM   2203 C  CG1 . ILE A 1 299 ? 29.989 17.443  0.283   1.00 20.69 ? 299 ILE A CG1 1 
ATOM   2204 C  CG2 . ILE A 1 299 ? 30.943 17.035  2.590   1.00 24.56 ? 299 ILE A CG2 1 
ATOM   2205 C  CD1 . ILE A 1 299 ? 29.998 16.032  -0.253  1.00 22.15 ? 299 ILE A CD1 1 
ATOM   2206 N  N   . ASP A 1 300 ? 27.831 17.693  4.368   1.00 21.35 ? 300 ASP A N   1 
ATOM   2207 C  CA  . ASP A 1 300 ? 27.533 17.576  5.793   1.00 18.24 ? 300 ASP A CA  1 
ATOM   2208 C  C   . ASP A 1 300 ? 26.560 16.432  6.048   1.00 19.57 ? 300 ASP A C   1 
ATOM   2209 O  O   . ASP A 1 300 ? 26.738 15.647  6.990   1.00 17.91 ? 300 ASP A O   1 
ATOM   2210 C  CB  . ASP A 1 300 ? 26.945 18.888  6.314   1.00 20.91 ? 300 ASP A CB  1 
ATOM   2211 C  CG  . ASP A 1 300 ? 28.005 19.855  6.789   1.00 26.74 ? 300 ASP A CG  1 
ATOM   2212 O  OD1 . ASP A 1 300 ? 29.206 19.559  6.626   1.00 25.24 ? 300 ASP A OD1 1 
ATOM   2213 O  OD2 . ASP A 1 300 ? 27.634 20.921  7.320   1.00 33.76 ? 300 ASP A OD2 1 
ATOM   2214 N  N   . CYS A 1 301 ? 25.533 16.319  5.207   1.00 16.57 ? 301 CYS A N   1 
ATOM   2215 C  CA  . CYS A 1 301 ? 24.562 15.243  5.354   1.00 18.40 ? 301 CYS A CA  1 
ATOM   2216 C  C   . CYS A 1 301 ? 25.183 13.865  5.254   1.00 19.08 ? 301 CYS A C   1 
ATOM   2217 O  O   . CYS A 1 301 ? 24.570 12.899  5.725   1.00 18.59 ? 301 CYS A O   1 
ATOM   2218 C  CB  . CYS A 1 301 ? 23.476 15.356  4.291   1.00 20.40 ? 301 CYS A CB  1 
ATOM   2219 S  SG  . CYS A 1 301 ? 22.389 16.692  4.586   1.00 20.40 ? 301 CYS A SG  1 
ATOM   2220 N  N   . VAL A 1 302 ? 26.343 13.726  4.611   1.00 17.36 ? 302 VAL A N   1 
ATOM   2221 C  CA  . VAL A 1 302 ? 26.945 12.395  4.513   1.00 19.00 ? 302 VAL A CA  1 
ATOM   2222 C  C   . VAL A 1 302 ? 28.256 12.285  5.295   1.00 20.18 ? 302 VAL A C   1 
ATOM   2223 O  O   . VAL A 1 302 ? 28.942 11.259  5.206   1.00 18.69 ? 302 VAL A O   1 
ATOM   2224 C  CB  . VAL A 1 302 ? 27.139 11.971  3.047   1.00 17.07 ? 302 VAL A CB  1 
ATOM   2225 C  CG1 . VAL A 1 302 ? 25.812 12.091  2.293   1.00 16.21 ? 302 VAL A CG1 1 
ATOM   2226 C  CG2 . VAL A 1 302 ? 28.236 12.779  2.379   1.00 17.30 ? 302 VAL A CG2 1 
ATOM   2227 N  N   . THR A 1 303 ? 28.612 13.297  6.085   1.00 17.32 ? 303 THR A N   1 
ATOM   2228 C  CA  . THR A 1 303 ? 29.838 13.226  6.875   1.00 19.29 ? 303 THR A CA  1 
ATOM   2229 C  C   . THR A 1 303 ? 29.573 13.556  8.339   1.00 18.85 ? 303 THR A C   1 
ATOM   2230 O  O   . THR A 1 303 ? 29.273 12.655  9.130   1.00 19.46 ? 303 THR A O   1 
ATOM   2231 C  CB  . THR A 1 303 ? 30.912 14.163  6.316   1.00 19.61 ? 303 THR A CB  1 
ATOM   2232 O  OG1 . THR A 1 303 ? 30.380 15.493  6.185   1.00 18.50 ? 303 THR A OG1 1 
ATOM   2233 C  CG2 . THR A 1 303 ? 31.420 13.660  4.959   1.00 19.61 ? 303 THR A CG2 1 
ATOM   2234 N  N   . VAL A 1 304 ? 29.681 14.838  8.709   1.00 16.91 ? 304 VAL A N   1 
ATOM   2235 C  CA  . VAL A 1 304 ? 29.637 15.205  10.125  1.00 19.68 ? 304 VAL A CA  1 
ATOM   2236 C  C   . VAL A 1 304 ? 28.274 14.870  10.724  1.00 21.44 ? 304 VAL A C   1 
ATOM   2237 O  O   . VAL A 1 304 ? 28.188 14.364  11.848  1.00 21.03 ? 304 VAL A O   1 
ATOM   2238 C  CB  . VAL A 1 304 ? 30.001 16.693  10.322  1.00 23.10 ? 304 VAL A CB  1 
ATOM   2239 C  CG1 . VAL A 1 304 ? 29.062 17.609  9.551   1.00 24.36 ? 304 VAL A CG1 1 
ATOM   2240 C  CG2 . VAL A 1 304 ? 30.014 17.054  11.797  1.00 25.17 ? 304 VAL A CG2 1 
ATOM   2241 N  N   . SER A 1 305 ? 27.193 15.114  9.973   1.00 19.78 ? 305 SER A N   1 
ATOM   2242 C  CA  . SER A 1 305 ? 25.853 14.857  10.492  1.00 21.74 ? 305 SER A CA  1 
ATOM   2243 C  C   . SER A 1 305 ? 25.597 13.366  10.635  1.00 22.42 ? 305 SER A C   1 
ATOM   2244 O  O   . SER A 1 305 ? 25.006 12.921  11.628  1.00 21.17 ? 305 SER A O   1 
ATOM   2245 C  CB  . SER A 1 305 ? 24.807 15.488  9.576   1.00 21.85 ? 305 SER A CB  1 
ATOM   2246 O  OG  . SER A 1 305 ? 24.925 16.896  9.597   1.00 22.49 ? 305 SER A OG  1 
ATOM   2247 N  N   . ALA A 1 306 ? 26.037 12.579  9.654   1.00 18.36 ? 306 ALA A N   1 
ATOM   2248 C  CA  . ALA A 1 306 ? 25.894 11.135  9.751   1.00 19.67 ? 306 ALA A CA  1 
ATOM   2249 C  C   . ALA A 1 306 ? 26.677 10.591  10.933  1.00 21.71 ? 306 ALA A C   1 
ATOM   2250 O  O   . ALA A 1 306 ? 26.168 9.760   11.690  1.00 22.05 ? 306 ALA A O   1 
ATOM   2251 C  CB  . ALA A 1 306 ? 26.354 10.473  8.454   1.00 18.00 ? 306 ALA A CB  1 
ATOM   2252 N  N   . ALA A 1 307 ? 27.917 11.052  11.109  1.00 17.14 ? 307 ALA A N   1 
ATOM   2253 C  CA  . ALA A 1 307 ? 28.724 10.569  12.222  1.00 19.67 ? 307 ALA A CA  1 
ATOM   2254 C  C   . ALA A 1 307 ? 28.126 10.985  13.562  1.00 21.84 ? 307 ALA A C   1 
ATOM   2255 O  O   . ALA A 1 307 ? 28.123 10.198  14.514  1.00 22.62 ? 307 ALA A O   1 
ATOM   2256 C  CB  . ALA A 1 307 ? 30.160 11.069  12.086  1.00 20.22 ? 307 ALA A CB  1 
ATOM   2257 N  N   . GLU A 1 308 ? 27.611 12.213  13.662  1.00 22.35 ? 308 GLU A N   1 
ATOM   2258 C  CA  . GLU A 1 308 ? 26.968 12.625  14.907  1.00 23.70 ? 308 GLU A CA  1 
ATOM   2259 C  C   . GLU A 1 308 ? 25.727 11.790  15.191  1.00 25.48 ? 308 GLU A C   1 
ATOM   2260 O  O   . GLU A 1 308 ? 25.522 11.343  16.326  1.00 26.11 ? 308 GLU A O   1 
ATOM   2261 C  CB  . GLU A 1 308 ? 26.611 14.114  14.870  1.00 23.70 ? 308 GLU A CB  1 
ATOM   2262 C  CG  . GLU A 1 308 ? 27.806 15.029  15.050  1.00 28.73 ? 308 GLU A CG  1 
ATOM   2263 C  CD  . GLU A 1 308 ? 27.532 16.473  14.648  1.00 30.82 ? 308 GLU A CD  1 
ATOM   2264 O  OE1 . GLU A 1 308 ? 26.379 16.801  14.290  1.00 30.12 ? 308 GLU A OE1 1 
ATOM   2265 O  OE2 . GLU A 1 308 ? 28.476 17.288  14.717  1.00 33.24 ? 308 GLU A OE2 1 
ATOM   2266 N  N   . GLY A 1 309 ? 24.898 11.554  14.172  1.00 24.56 ? 309 GLY A N   1 
ATOM   2267 C  CA  . GLY A 1 309 ? 23.631 10.878  14.400  1.00 25.32 ? 309 GLY A CA  1 
ATOM   2268 C  C   . GLY A 1 309 ? 23.779 9.436   14.836  1.00 24.30 ? 309 GLY A C   1 
ATOM   2269 O  O   . GLY A 1 309 ? 22.899 8.896   15.509  1.00 26.71 ? 309 GLY A O   1 
ATOM   2270 N  N   . LEU A 1 310 ? 24.878 8.786   14.454  1.00 25.58 ? 310 LEU A N   1 
ATOM   2271 C  CA  . LEU A 1 310 ? 25.139 7.411   14.858  1.00 24.82 ? 310 LEU A CA  1 
ATOM   2272 C  C   . LEU A 1 310 ? 26.284 7.316   15.856  1.00 24.02 ? 310 LEU A C   1 
ATOM   2273 O  O   . LEU A 1 310 ? 26.758 6.211   16.135  1.00 24.21 ? 310 LEU A O   1 
ATOM   2274 C  CB  . LEU A 1 310 ? 25.417 6.550   13.622  1.00 20.71 ? 310 LEU A CB  1 
ATOM   2275 C  CG  . LEU A 1 310 ? 24.131 6.250   12.847  1.00 24.60 ? 310 LEU A CG  1 
ATOM   2276 C  CD1 . LEU A 1 310 ? 24.389 5.378   11.633  1.00 26.14 ? 310 LEU A CD1 1 
ATOM   2277 C  CD2 . LEU A 1 310 ? 23.090 5.596   13.758  1.00 23.98 ? 310 LEU A CD2 1 
ATOM   2278 N  N   . ARG A 1 311 ? 26.742 8.456   16.387  1.00 22.53 ? 311 ARG A N   1 
ATOM   2279 C  CA  . ARG A 1 311 ? 27.772 8.515   17.432  1.00 25.59 ? 311 ARG A CA  1 
ATOM   2280 C  C   . ARG A 1 311 ? 29.069 7.828   16.999  1.00 23.33 ? 311 ARG A C   1 
ATOM   2281 O  O   . ARG A 1 311 ? 29.712 7.126   17.784  1.00 23.60 ? 311 ARG A O   1 
ATOM   2282 C  CB  . ARG A 1 311 ? 27.253 7.922   18.745  1.00 27.41 ? 311 ARG A CB  1 
ATOM   2283 C  CG  . ARG A 1 311 ? 25.877 8.438   19.117  1.00 27.95 ? 311 ARG A CG  1 
ATOM   2284 C  CD  . ARG A 1 311 ? 25.439 7.991   20.496  1.00 36.62 ? 311 ARG A CD  1 
ATOM   2285 N  NE  . ARG A 1 311 ? 24.037 8.330   20.707  1.00 40.08 ? 311 ARG A NE  1 
ATOM   2286 C  CZ  . ARG A 1 311 ? 23.297 7.891   21.715  1.00 40.83 ? 311 ARG A CZ  1 
ATOM   2287 N  NH1 . ARG A 1 311 ? 23.805 7.116   22.659  1.00 42.48 ? 311 ARG A NH1 1 
ATOM   2288 N  NH2 . ARG A 1 311 ? 22.016 8.244   21.778  1.00 40.95 ? 311 ARG A NH2 1 
ATOM   2289 N  N   . LEU A 1 312 ? 29.459 8.036   15.742  1.00 20.92 ? 312 LEU A N   1 
ATOM   2290 C  CA  . LEU A 1 312 ? 30.711 7.499   15.203  1.00 22.06 ? 312 LEU A CA  1 
ATOM   2291 C  C   . LEU A 1 312 ? 31.806 8.517   15.494  1.00 21.84 ? 312 LEU A C   1 
ATOM   2292 O  O   . LEU A 1 312 ? 32.105 9.392   14.681  1.00 22.70 ? 312 LEU A O   1 
ATOM   2293 C  CB  . LEU A 1 312 ? 30.577 7.201   13.713  1.00 22.54 ? 312 LEU A CB  1 
ATOM   2294 C  CG  . LEU A 1 312 ? 29.247 6.559   13.312  1.00 20.83 ? 312 LEU A CG  1 
ATOM   2295 C  CD1 . LEU A 1 312 ? 29.084 6.485   11.785  1.00 21.87 ? 312 LEU A CD1 1 
ATOM   2296 C  CD2 . LEU A 1 312 ? 29.136 5.192   13.954  1.00 22.39 ? 312 LEU A CD2 1 
ATOM   2297 N  N   . SER A 1 313 ? 32.442 8.360   16.660  1.00 23.81 ? 313 SER A N   1 
ATOM   2298 C  CA  . SER A 1 313 ? 33.174 9.465   17.282  1.00 23.34 ? 313 SER A CA  1 
ATOM   2299 C  C   . SER A 1 313 ? 34.359 9.944   16.443  1.00 24.25 ? 313 SER A C   1 
ATOM   2300 O  O   . SER A 1 313 ? 34.663 11.142  16.436  1.00 24.58 ? 313 SER A O   1 
ATOM   2301 C  CB  . SER A 1 313 ? 33.646 9.060   18.678  1.00 25.82 ? 313 SER A CB  1 
ATOM   2302 O  OG  . SER A 1 313 ? 34.541 7.956   18.613  1.00 32.99 ? 313 SER A OG  1 
ATOM   2303 N  N   . ARG A 1 314 ? 35.060 9.039   15.759  1.00 20.57 ? 314 ARG A N   1 
ATOM   2304 C  CA  . ARG A 1 314 ? 36.254 9.424   15.007  1.00 21.89 ? 314 ARG A CA  1 
ATOM   2305 C  C   . ARG A 1 314 ? 36.031 9.466   13.500  1.00 22.71 ? 314 ARG A C   1 
ATOM   2306 O  O   . ARG A 1 314 ? 37.003 9.581   12.742  1.00 21.53 ? 314 ARG A O   1 
ATOM   2307 C  CB  . ARG A 1 314 ? 37.422 8.495   15.332  1.00 21.73 ? 314 ARG A CB  1 
ATOM   2308 C  CG  . ARG A 1 314 ? 37.602 8.217   16.829  1.00 25.80 ? 314 ARG A CG  1 
ATOM   2309 C  CD  . ARG A 1 314 ? 37.724 9.516   17.615  1.00 29.17 ? 314 ARG A CD  1 
ATOM   2310 N  NE  . ARG A 1 314 ? 38.897 10.299  17.234  1.00 30.10 ? 314 ARG A NE  1 
ATOM   2311 C  CZ  . ARG A 1 314 ? 39.139 11.534  17.654  1.00 33.02 ? 314 ARG A CZ  1 
ATOM   2312 N  NH1 . ARG A 1 314 ? 38.286 12.175  18.438  1.00 32.45 ? 314 ARG A NH1 1 
ATOM   2313 N  NH2 . ARG A 1 314 ? 40.262 12.143  17.276  1.00 31.95 ? 314 ARG A NH2 1 
ATOM   2314 N  N   . LYS A 1 315 ? 34.790 9.379   13.043  1.00 20.39 ? 315 LYS A N   1 
ATOM   2315 C  CA  . LYS A 1 315 ? 34.480 9.453   11.622  1.00 19.92 ? 315 LYS A CA  1 
ATOM   2316 C  C   . LYS A 1 315 ? 33.812 10.787  11.299  1.00 18.63 ? 315 LYS A C   1 
ATOM   2317 O  O   . LYS A 1 315 ? 33.407 11.538  12.189  1.00 19.52 ? 315 LYS A O   1 
ATOM   2318 C  CB  . LYS A 1 315 ? 33.581 8.279   11.197  1.00 20.67 ? 315 LYS A CB  1 
ATOM   2319 C  CG  . LYS A 1 315 ? 34.051 6.902   11.684  1.00 20.55 ? 315 LYS A CG  1 
ATOM   2320 C  CD  . LYS A 1 315 ? 35.251 6.427   10.881  1.00 20.03 ? 315 LYS A CD  1 
ATOM   2321 C  CE  . LYS A 1 315 ? 35.311 4.917   10.735  1.00 24.93 ? 315 LYS A CE  1 
ATOM   2322 N  NZ  . LYS A 1 315 ? 36.693 4.468   10.408  1.00 27.66 ? 315 LYS A NZ  1 
ATOM   2323 N  N   . GLY A 1 316 ? 33.723 11.088  10.001  1.00 18.64 ? 316 GLY A N   1 
ATOM   2324 C  CA  . GLY A 1 316 ? 32.912 12.184  9.510   1.00 19.89 ? 316 GLY A CA  1 
ATOM   2325 C  C   . GLY A 1 316 ? 33.513 13.571  9.596   1.00 21.16 ? 316 GLY A C   1 
ATOM   2326 O  O   . GLY A 1 316 ? 32.876 14.527  9.140   1.00 19.87 ? 316 GLY A O   1 
ATOM   2327 N  N   . ARG A 1 317 ? 34.709 13.729  10.155  1.00 23.01 ? 317 ARG A N   1 
ATOM   2328 C  CA  . ARG A 1 317 ? 35.283 15.053  10.345  1.00 24.15 ? 317 ARG A CA  1 
ATOM   2329 C  C   . ARG A 1 317 ? 36.659 15.141  9.711   1.00 25.40 ? 317 ARG A C   1 
ATOM   2330 O  O   . ARG A 1 317 ? 37.524 14.296  9.967   1.00 25.32 ? 317 ARG A O   1 
ATOM   2331 C  CB  . ARG A 1 317 ? 35.356 15.419  11.832  1.00 25.72 ? 317 ARG A CB  1 
ATOM   2332 C  CG  . ARG A 1 317 ? 33.994 15.495  12.511  1.00 27.89 ? 317 ARG A CG  1 
ATOM   2333 C  CD  . ARG A 1 317 ? 33.833 14.396  13.529  1.00 28.39 ? 317 ARG A CD  1 
ATOM   2334 N  NE  . ARG A 1 317 ? 32.738 14.627  14.466  1.00 33.91 ? 317 ARG A NE  1 
ATOM   2335 C  CZ  . ARG A 1 317 ? 32.046 13.653  15.044  1.00 31.17 ? 317 ARG A CZ  1 
ATOM   2336 N  NH1 . ARG A 1 317 ? 32.288 12.381  14.770  1.00 21.28 ? 317 ARG A NH1 1 
ATOM   2337 N  NH2 . ARG A 1 317 ? 31.082 13.963  15.909  1.00 28.58 ? 317 ARG A NH2 1 
ATOM   2338 N  N   . LEU A 1 318 ? 36.851 16.178  8.891   1.00 25.25 ? 318 LEU A N   1 
ATOM   2339 C  CA  . LEU A 1 318 ? 38.155 16.510  8.313   1.00 28.65 ? 318 LEU A CA  1 
ATOM   2340 C  C   . LEU A 1 318 ? 38.933 17.371  9.310   1.00 26.47 ? 318 LEU A C   1 
ATOM   2341 O  O   . LEU A 1 318 ? 39.127 18.575  9.131   1.00 27.16 ? 318 LEU A O   1 
ATOM   2342 C  CB  . LEU A 1 318 ? 37.982 17.224  6.977   1.00 26.96 ? 318 LEU A CB  1 
ATOM   2343 C  CG  . LEU A 1 318 ? 38.606 16.593  5.729   1.00 29.39 ? 318 LEU A CG  1 
ATOM   2344 C  CD1 . LEU A 1 318 ? 38.527 17.561  4.553   1.00 27.58 ? 318 LEU A CD1 1 
ATOM   2345 C  CD2 . LEU A 1 318 ? 40.034 16.150  5.984   1.00 28.59 ? 318 LEU A CD2 1 
ATOM   2346 N  N   . GLU A 1 319 ? 39.354 16.725  10.399  1.00 24.63 ? 319 GLU A N   1 
ATOM   2347 C  CA  . GLU A 1 319 ? 40.082 17.390  11.472  1.00 24.26 ? 319 GLU A CA  1 
ATOM   2348 C  C   . GLU A 1 319 ? 41.280 16.554  11.892  1.00 23.83 ? 319 GLU A C   1 
ATOM   2349 O  O   . GLU A 1 319 ? 41.255 15.323  11.824  1.00 21.31 ? 319 GLU A O   1 
ATOM   2350 C  CB  . GLU A 1 319 ? 39.210 17.635  12.717  1.00 26.98 ? 319 GLU A CB  1 
ATOM   2351 C  CG  . GLU A 1 319 ? 37.746 17.958  12.481  1.00 31.46 ? 319 GLU A CG  1 
ATOM   2352 C  CD  . GLU A 1 319 ? 37.483 19.439  12.306  1.00 33.98 ? 319 GLU A CD  1 
ATOM   2353 O  OE1 . GLU A 1 319 ? 36.466 19.926  12.851  1.00 37.16 ? 319 GLU A OE1 1 
ATOM   2354 O  OE2 . GLU A 1 319 ? 38.280 20.113  11.616  1.00 42.00 ? 319 GLU A OE2 1 
ATOM   2355 N  N   . ALA A 1 320 ? 42.319 17.240  12.363  1.00 21.98 ? 320 ALA A N   1 
ATOM   2356 C  CA  . ALA A 1 320 ? 43.509 16.558  12.843  1.00 22.62 ? 320 ALA A CA  1 
ATOM   2357 C  C   . ALA A 1 320 ? 43.163 15.569  13.949  1.00 24.86 ? 320 ALA A C   1 
ATOM   2358 O  O   . ALA A 1 320 ? 42.410 15.880  14.877  1.00 22.40 ? 320 ALA A O   1 
ATOM   2359 C  CB  . ALA A 1 320 ? 44.528 17.575  13.352  1.00 22.59 ? 320 ALA A CB  1 
ATOM   2360 N  N   . GLY A 1 321 ? 43.731 14.370  13.850  1.00 23.77 ? 321 GLY A N   1 
ATOM   2361 C  CA  . GLY A 1 321 ? 43.556 13.349  14.854  1.00 24.18 ? 321 GLY A CA  1 
ATOM   2362 C  C   . GLY A 1 321 ? 42.413 12.392  14.596  1.00 25.48 ? 321 GLY A C   1 
ATOM   2363 O  O   . GLY A 1 321 ? 42.365 11.326  15.218  1.00 25.89 ? 321 GLY A O   1 
ATOM   2364 N  N   . PHE A 1 322 ? 41.494 12.734  13.700  1.00 23.92 ? 322 PHE A N   1 
ATOM   2365 C  CA  . PHE A 1 322 ? 40.419 11.816  13.371  1.00 26.01 ? 322 PHE A CA  1 
ATOM   2366 C  C   . PHE A 1 322 ? 40.906 10.767  12.373  1.00 23.58 ? 322 PHE A C   1 
ATOM   2367 O  O   . PHE A 1 322 ? 42.007 10.858  11.825  1.00 25.48 ? 322 PHE A O   1 
ATOM   2368 C  CB  . PHE A 1 322 ? 39.212 12.585  12.835  1.00 23.86 ? 322 PHE A CB  1 
ATOM   2369 C  CG  . PHE A 1 322 ? 38.460 13.320  13.904  1.00 26.76 ? 322 PHE A CG  1 
ATOM   2370 C  CD1 . PHE A 1 322 ? 38.964 14.501  14.432  1.00 26.51 ? 322 PHE A CD1 1 
ATOM   2371 C  CD2 . PHE A 1 322 ? 37.270 12.816  14.410  1.00 26.83 ? 322 PHE A CD2 1 
ATOM   2372 C  CE1 . PHE A 1 322 ? 38.290 15.179  15.434  1.00 27.04 ? 322 PHE A CE1 1 
ATOM   2373 C  CE2 . PHE A 1 322 ? 36.590 13.491  15.419  1.00 27.13 ? 322 PHE A CE2 1 
ATOM   2374 C  CZ  . PHE A 1 322 ? 37.100 14.673  15.926  1.00 30.62 ? 322 PHE A CZ  1 
ATOM   2375 N  N   . ASP A 1 323 ? 40.073 9.751   12.153  1.00 22.54 ? 323 ASP A N   1 
ATOM   2376 C  CA  . ASP A 1 323 ? 40.427 8.669   11.243  1.00 19.19 ? 323 ASP A CA  1 
ATOM   2377 C  C   . ASP A 1 323 ? 40.674 9.202   9.837   1.00 23.83 ? 323 ASP A C   1 
ATOM   2378 O  O   . ASP A 1 323 ? 39.965 10.088  9.351   1.00 21.54 ? 323 ASP A O   1 
ATOM   2379 C  CB  . ASP A 1 323 ? 39.322 7.617   11.207  1.00 23.19 ? 323 ASP A CB  1 
ATOM   2380 C  CG  . ASP A 1 323 ? 39.271 6.774   12.468  1.00 25.96 ? 323 ASP A CG  1 
ATOM   2381 O  OD1 . ASP A 1 323 ? 40.196 6.876   13.300  1.00 25.18 ? 323 ASP A OD1 1 
ATOM   2382 O  OD2 . ASP A 1 323 ? 38.312 5.988   12.613  1.00 27.59 ? 323 ASP A OD2 1 
ATOM   2383 N  N   . ALA A 1 324 ? 41.686 8.646   9.172   1.00 20.86 ? 324 ALA A N   1 
ATOM   2384 C  CA  . ALA A 1 324 ? 42.043 9.096   7.829   1.00 22.44 ? 324 ALA A CA  1 
ATOM   2385 C  C   . ALA A 1 324 ? 41.153 8.423   6.779   1.00 19.58 ? 324 ALA A C   1 
ATOM   2386 O  O   . ALA A 1 324 ? 41.618 7.740   5.870   1.00 22.31 ? 324 ALA A O   1 
ATOM   2387 C  CB  . ALA A 1 324 ? 43.520 8.842   7.558   1.00 22.91 ? 324 ALA A CB  1 
ATOM   2388 N  N   . ASP A 1 325 ? 39.845 8.647   6.920   1.00 18.46 ? 325 ASP A N   1 
ATOM   2389 C  CA  . ASP A 1 325 ? 38.860 8.275   5.910   1.00 20.37 ? 325 ASP A CA  1 
ATOM   2390 C  C   . ASP A 1 325 ? 38.509 9.527   5.115   1.00 20.26 ? 325 ASP A C   1 
ATOM   2391 O  O   . ASP A 1 325 ? 38.024 10.513  5.682   1.00 18.86 ? 325 ASP A O   1 
ATOM   2392 C  CB  . ASP A 1 325 ? 37.592 7.688   6.531   1.00 21.96 ? 325 ASP A CB  1 
ATOM   2393 C  CG  . ASP A 1 325 ? 37.836 6.383   7.267   1.00 22.27 ? 325 ASP A CG  1 
ATOM   2394 O  OD1 . ASP A 1 325 ? 38.962 5.838   7.217   1.00 23.11 ? 325 ASP A OD1 1 
ATOM   2395 O  OD2 . ASP A 1 325 ? 36.871 5.885   7.878   1.00 26.68 ? 325 ASP A OD2 1 
ATOM   2396 N  N   . LEU A 1 326 ? 38.755 9.485   3.813   1.00 18.79 ? 326 LEU A N   1 
ATOM   2397 C  CA  . LEU A 1 326 ? 38.533 10.623  2.931   1.00 20.30 ? 326 LEU A CA  1 
ATOM   2398 C  C   . LEU A 1 326 ? 37.825 10.164  1.667   1.00 20.36 ? 326 LEU A C   1 
ATOM   2399 O  O   . LEU A 1 326 ? 37.993 9.028   1.228   1.00 19.84 ? 326 LEU A O   1 
ATOM   2400 C  CB  . LEU A 1 326 ? 39.859 11.300  2.544   1.00 18.22 ? 326 LEU A CB  1 
ATOM   2401 C  CG  . LEU A 1 326 ? 40.785 11.674  3.690   1.00 20.66 ? 326 LEU A CG  1 
ATOM   2402 C  CD1 . LEU A 1 326 ? 42.096 12.164  3.125   1.00 25.63 ? 326 LEU A CD1 1 
ATOM   2403 C  CD2 . LEU A 1 326 ? 40.131 12.762  4.489   1.00 22.64 ? 326 LEU A CD2 1 
ATOM   2404 N  N   . THR A 1 327 ? 37.046 11.061  1.069   1.00 19.57 ? 327 THR A N   1 
ATOM   2405 C  CA  . THR A 1 327 ? 36.475 10.819  -0.252  1.00 19.49 ? 327 THR A CA  1 
ATOM   2406 C  C   . THR A 1 327 ? 36.978 11.885  -1.212  1.00 17.97 ? 327 THR A C   1 
ATOM   2407 O  O   . THR A 1 327 ? 36.894 13.079  -0.911  1.00 18.94 ? 327 THR A O   1 
ATOM   2408 C  CB  . THR A 1 327 ? 34.940 10.816  -0.217  1.00 19.64 ? 327 THR A CB  1 
ATOM   2409 O  OG1 . THR A 1 327 ? 34.481 9.787   0.671   1.00 18.23 ? 327 THR A OG1 1 
ATOM   2410 C  CG2 . THR A 1 327 ? 34.369 10.581  -1.608  1.00 17.40 ? 327 THR A CG2 1 
ATOM   2411 N  N   . LEU A 1 328 ? 37.504 11.452  -2.357  1.00 20.80 ? 328 LEU A N   1 
ATOM   2412 C  CA  . LEU A 1 328 ? 37.955 12.342  -3.422  1.00 18.87 ? 328 LEU A CA  1 
ATOM   2413 C  C   . LEU A 1 328 ? 36.961 12.238  -4.566  1.00 20.16 ? 328 LEU A C   1 
ATOM   2414 O  O   . LEU A 1 328 ? 36.706 11.137  -5.074  1.00 21.51 ? 328 LEU A O   1 
ATOM   2415 C  CB  . LEU A 1 328 ? 39.365 11.981  -3.906  1.00 19.73 ? 328 LEU A CB  1 
ATOM   2416 C  CG  . LEU A 1 328 ? 40.578 12.364  -3.054  1.00 22.73 ? 328 LEU A CG  1 
ATOM   2417 C  CD1 . LEU A 1 328 ? 40.484 11.801  -1.654  1.00 22.04 ? 328 LEU A CD1 1 
ATOM   2418 C  CD2 . LEU A 1 328 ? 41.899 11.942  -3.721  1.00 22.16 ? 328 LEU A CD2 1 
ATOM   2419 N  N   . PHE A 1 329 ? 36.409 13.376  -4.969  1.00 22.80 ? 329 PHE A N   1 
ATOM   2420 C  CA  . PHE A 1 329 ? 35.297 13.357  -5.908  1.00 23.87 ? 329 PHE A CA  1 
ATOM   2421 C  C   . PHE A 1 329 ? 35.323 14.621  -6.756  1.00 24.70 ? 329 PHE A C   1 
ATOM   2422 O  O   . PHE A 1 329 ? 36.089 15.549  -6.505  1.00 21.90 ? 329 PHE A O   1 
ATOM   2423 C  CB  . PHE A 1 329 ? 33.953 13.189  -5.175  1.00 22.21 ? 329 PHE A CB  1 
ATOM   2424 C  CG  . PHE A 1 329 ? 33.619 14.305  -4.212  1.00 22.39 ? 329 PHE A CG  1 
ATOM   2425 C  CD1 . PHE A 1 329 ? 34.113 14.298  -2.913  1.00 21.94 ? 329 PHE A CD1 1 
ATOM   2426 C  CD2 . PHE A 1 329 ? 32.776 15.336  -4.595  1.00 22.22 ? 329 PHE A CD2 1 
ATOM   2427 C  CE1 . PHE A 1 329 ? 33.791 15.315  -2.017  1.00 21.90 ? 329 PHE A CE1 1 
ATOM   2428 C  CE2 . PHE A 1 329 ? 32.446 16.359  -3.708  1.00 24.05 ? 329 PHE A CE2 1 
ATOM   2429 C  CZ  . PHE A 1 329 ? 32.953 16.348  -2.419  1.00 22.77 ? 329 PHE A CZ  1 
ATOM   2430 N  N   . ARG A 1 330 ? 34.489 14.632  -7.790  1.00 24.59 ? 330 ARG A N   1 
ATOM   2431 C  CA  . ARG A 1 330 ? 34.376 15.768  -8.687  1.00 24.68 ? 330 ARG A CA  1 
ATOM   2432 C  C   . ARG A 1 330 ? 32.903 16.083  -8.899  1.00 27.60 ? 330 ARG A C   1 
ATOM   2433 O  O   . ARG A 1 330 ? 32.049 15.196  -8.820  1.00 24.85 ? 330 ARG A O   1 
ATOM   2434 C  CB  . ARG A 1 330 ? 35.058 15.486  -10.042 1.00 31.18 ? 330 ARG A CB  1 
ATOM   2435 C  CG  . ARG A 1 330 ? 36.561 15.718  -10.035 1.00 31.26 ? 330 ARG A CG  1 
ATOM   2436 C  CD  . ARG A 1 330 ? 37.161 15.742  -11.442 1.00 33.50 ? 330 ARG A CD  1 
ATOM   2437 N  NE  . ARG A 1 330 ? 36.298 16.393  -12.425 1.00 38.21 ? 330 ARG A NE  1 
ATOM   2438 C  CZ  . ARG A 1 330 ? 36.193 17.707  -12.595 1.00 39.83 ? 330 ARG A CZ  1 
ATOM   2439 N  NH1 . ARG A 1 330 ? 36.839 18.561  -11.813 1.00 36.07 ? 330 ARG A NH1 1 
ATOM   2440 N  NH2 . ARG A 1 330 ? 35.411 18.178  -13.566 1.00 36.80 ? 330 ARG A NH2 1 
ATOM   2441 N  N   . LEU A 1 331 ? 32.611 17.363  -9.137  1.00 23.61 ? 331 LEU A N   1 
ATOM   2442 C  CA  . LEU A 1 331 ? 31.296 17.793  -9.608  1.00 26.30 ? 331 LEU A CA  1 
ATOM   2443 C  C   . LEU A 1 331 ? 31.441 18.028  -11.104 1.00 32.47 ? 331 LEU A C   1 
ATOM   2444 O  O   . LEU A 1 331 ? 31.960 19.058  -11.536 1.00 35.69 ? 331 LEU A O   1 
ATOM   2445 C  CB  . LEU A 1 331 ? 30.815 19.042  -8.879  1.00 29.98 ? 331 LEU A CB  1 
ATOM   2446 N  N   . GLU A 1 332 ? 31.005 17.060  -11.896 1.00 33.30 ? 332 GLU A N   1 
ATOM   2447 C  CA  . GLU A 1 332 ? 31.232 17.095  -13.331 1.00 36.53 ? 332 GLU A CA  1 
ATOM   2448 C  C   . GLU A 1 332 ? 29.962 17.490  -14.064 1.00 34.28 ? 332 GLU A C   1 
ATOM   2449 O  O   . GLU A 1 332 ? 28.865 17.036  -13.724 1.00 35.34 ? 332 GLU A O   1 
ATOM   2450 C  CB  . GLU A 1 332 ? 31.743 15.744  -13.834 1.00 37.10 ? 332 GLU A CB  1 
ATOM   2451 C  CG  . GLU A 1 332 ? 33.214 15.514  -13.526 1.00 37.30 ? 332 GLU A CG  1 
ATOM   2452 C  CD  . GLU A 1 332 ? 33.627 14.078  -13.726 1.00 39.20 ? 332 GLU A CD  1 
ATOM   2453 O  OE1 . GLU A 1 332 ? 33.210 13.483  -14.743 1.00 40.73 ? 332 GLU A OE1 1 
ATOM   2454 O  OE2 . GLU A 1 332 ? 34.385 13.553  -12.884 1.00 35.23 ? 332 GLU A OE2 1 
ATOM   2455 N  N   . ARG A 1 333 ? 30.118 18.362  -15.051 1.00 33.85 ? 333 ARG A N   1 
ATOM   2456 C  CA  . ARG A 1 333 ? 29.017 18.736  -15.927 1.00 36.16 ? 333 ARG A CA  1 
ATOM   2457 C  C   . ARG A 1 333 ? 28.739 17.557  -16.847 1.00 39.62 ? 333 ARG A C   1 
ATOM   2458 O  O   . ARG A 1 333 ? 29.490 17.293  -17.789 1.00 39.78 ? 333 ARG A O   1 
ATOM   2459 C  CB  . ARG A 1 333 ? 29.360 19.997  -16.714 1.00 37.56 ? 333 ARG A CB  1 
ATOM   2460 N  N   . GLN A 1 334 ? 27.666 16.825  -16.552 1.00 37.02 ? 334 GLN A N   1 
ATOM   2461 C  CA  . GLN A 1 334 ? 27.284 15.651  -17.335 1.00 42.28 ? 334 GLN A CA  1 
ATOM   2462 C  C   . GLN A 1 334 ? 25.774 15.509  -17.249 1.00 43.68 ? 334 GLN A C   1 
ATOM   2463 O  O   . GLN A 1 334 ? 25.244 14.919  -16.298 1.00 42.46 ? 334 GLN A O   1 
ATOM   2464 C  CB  . GLN A 1 334 ? 27.979 14.383  -16.839 1.00 40.04 ? 334 GLN A CB  1 
ATOM   2465 N  N   . PRO A 1 335 ? 25.036 16.103  -18.212 1.00 45.64 ? 335 PRO A N   1 
ATOM   2466 C  CA  . PRO A 1 335 ? 23.582 15.914  -18.290 1.00 44.72 ? 335 PRO A CA  1 
ATOM   2467 C  C   . PRO A 1 335 ? 23.125 14.501  -17.959 1.00 44.58 ? 335 PRO A C   1 
ATOM   2468 O  O   . PRO A 1 335 ? 23.606 13.531  -18.554 1.00 40.80 ? 335 PRO A O   1 
ATOM   2469 C  CB  . PRO A 1 335 ? 23.300 16.263  -19.751 1.00 46.58 ? 335 PRO A CB  1 
ATOM   2470 C  CG  . PRO A 1 335 ? 24.318 17.388  -20.058 1.00 44.61 ? 335 PRO A CG  1 
ATOM   2471 C  CD  . PRO A 1 335 ? 25.440 17.274  -19.010 1.00 44.05 ? 335 PRO A CD  1 
ATOM   2472 N  N   . THR A 1 336 ? 22.198 14.378  -17.009 1.00 42.96 ? 336 THR A N   1 
ATOM   2473 C  CA  . THR A 1 336 ? 21.803 13.084  -16.470 1.00 44.06 ? 336 THR A CA  1 
ATOM   2474 C  C   . THR A 1 336 ? 20.349 13.154  -16.022 1.00 38.13 ? 336 THR A C   1 
ATOM   2475 O  O   . THR A 1 336 ? 19.905 14.179  -15.500 1.00 40.07 ? 336 THR A O   1 
ATOM   2476 C  CB  . THR A 1 336 ? 22.704 12.684  -15.288 1.00 48.32 ? 336 THR A CB  1 
ATOM   2477 O  OG1 . THR A 1 336 ? 24.077 12.694  -15.704 1.00 49.45 ? 336 THR A OG1 1 
ATOM   2478 C  CG2 . THR A 1 336 ? 22.344 11.291  -14.761 1.00 38.57 ? 336 THR A CG2 1 
ATOM   2479 N  N   . LEU A 1 337 ? 19.610 12.068  -16.226 1.00 39.03 ? 337 LEU A N   1 
ATOM   2480 C  CA  . LEU A 1 337 ? 18.244 11.969  -15.727 1.00 33.59 ? 337 LEU A CA  1 
ATOM   2481 C  C   . LEU A 1 337 ? 18.267 11.271  -14.374 1.00 36.02 ? 337 LEU A C   1 
ATOM   2482 O  O   . LEU A 1 337 ? 18.707 10.121  -14.270 1.00 38.04 ? 337 LEU A O   1 
ATOM   2483 C  CB  . LEU A 1 337 ? 17.346 11.212  -16.706 1.00 34.71 ? 337 LEU A CB  1 
ATOM   2484 N  N   . LEU A 1 338 ? 17.807 11.967  -13.341 1.00 33.53 ? 338 LEU A N   1 
ATOM   2485 C  CA  . LEU A 1 338 ? 17.683 11.411  -12.003 1.00 30.48 ? 338 LEU A CA  1 
ATOM   2486 C  C   . LEU A 1 338 ? 16.234 10.990  -11.794 1.00 33.32 ? 338 LEU A C   1 
ATOM   2487 O  O   . LEU A 1 338 ? 15.317 11.786  -12.017 1.00 31.00 ? 338 LEU A O   1 
ATOM   2488 C  CB  . LEU A 1 338 ? 18.105 12.444  -10.962 1.00 32.29 ? 338 LEU A CB  1 
ATOM   2489 C  CG  . LEU A 1 338 ? 19.411 13.186  -11.278 1.00 32.56 ? 338 LEU A CG  1 
ATOM   2490 C  CD1 . LEU A 1 338 ? 19.710 14.241  -10.226 1.00 30.02 ? 338 LEU A CD1 1 
ATOM   2491 C  CD2 . LEU A 1 338 ? 20.583 12.219  -11.408 1.00 34.31 ? 338 LEU A CD2 1 
ATOM   2492 N  N   . VAL A 1 339 ? 16.025 9.738   -11.395 1.00 32.97 ? 339 VAL A N   1 
ATOM   2493 C  CA  . VAL A 1 339 ? 14.687 9.166   -11.265 1.00 33.47 ? 339 VAL A CA  1 
ATOM   2494 C  C   . VAL A 1 339 ? 14.438 8.850   -9.799  1.00 31.52 ? 339 VAL A C   1 
ATOM   2495 O  O   . VAL A 1 339 ? 15.274 8.214   -9.145  1.00 30.12 ? 339 VAL A O   1 
ATOM   2496 C  CB  . VAL A 1 339 ? 14.516 7.907   -12.137 1.00 31.03 ? 339 VAL A CB  1 
ATOM   2497 C  CG1 . VAL A 1 339 ? 13.061 7.468   -12.150 1.00 33.63 ? 339 VAL A CG1 1 
ATOM   2498 C  CG2 . VAL A 1 339 ? 15.000 8.176   -13.556 1.00 33.68 ? 339 VAL A CG2 1 
ATOM   2499 N  N   . ASP A 1 340 ? 13.292 9.293   -9.284  1.00 32.87 ? 340 ASP A N   1 
ATOM   2500 C  CA  . ASP A 1 340 ? 12.940 9.037   -7.895  1.00 35.70 ? 340 ASP A CA  1 
ATOM   2501 C  C   . ASP A 1 340 ? 12.126 7.747   -7.795  1.00 36.35 ? 340 ASP A C   1 
ATOM   2502 O  O   . ASP A 1 340 ? 12.004 6.981   -8.755  1.00 39.04 ? 340 ASP A O   1 
ATOM   2503 C  CB  . ASP A 1 340 ? 12.197 10.232  -7.287  1.00 33.30 ? 340 ASP A CB  1 
ATOM   2504 C  CG  . ASP A 1 340 ? 10.813 10.470  -7.905  1.00 36.88 ? 340 ASP A CG  1 
ATOM   2505 O  OD1 . ASP A 1 340 ? 10.376 9.703   -8.797  1.00 37.66 ? 340 ASP A OD1 1 
ATOM   2506 O  OD2 . ASP A 1 340 ? 10.153 11.445  -7.476  1.00 34.07 ? 340 ASP A OD2 1 
ATOM   2507 N  N   . ALA A 1 341 ? 11.536 7.513   -6.622  1.00 35.26 ? 341 ALA A N   1 
ATOM   2508 C  CA  . ALA A 1 341 ? 10.772 6.299   -6.376  1.00 33.83 ? 341 ALA A CA  1 
ATOM   2509 C  C   . ALA A 1 341 ? 9.383  6.336   -6.995  1.00 39.06 ? 341 ALA A C   1 
ATOM   2510 O  O   . ALA A 1 341 ? 8.786  5.273   -7.206  1.00 43.98 ? 341 ALA A O   1 
ATOM   2511 C  CB  . ALA A 1 341 ? 10.659 6.058   -4.872  1.00 31.97 ? 341 ALA A CB  1 
ATOM   2512 N  N   . GLU A 1 342 ? 8.854  7.526   -7.285  1.00 37.54 ? 342 GLU A N   1 
ATOM   2513 C  CA  . GLU A 1 342 ? 7.570  7.677   -7.955  1.00 39.41 ? 342 GLU A CA  1 
ATOM   2514 C  C   . GLU A 1 342 ? 7.697  7.641   -9.473  1.00 40.17 ? 342 GLU A C   1 
ATOM   2515 O  O   . GLU A 1 342 ? 6.753  8.028   -10.173 1.00 40.25 ? 342 GLU A O   1 
ATOM   2516 C  CB  . GLU A 1 342 ? 6.897  8.980   -7.516  1.00 44.04 ? 342 GLU A CB  1 
ATOM   2517 N  N   . LYS A 1 343 ? 8.840  7.184   -9.990  1.00 39.50 ? 343 LYS A N   1 
ATOM   2518 C  CA  . LYS A 1 343 ? 9.125  7.146   -11.425 1.00 41.79 ? 343 LYS A CA  1 
ATOM   2519 C  C   . LYS A 1 343 ? 9.066  8.537   -12.059 1.00 42.18 ? 343 LYS A C   1 
ATOM   2520 O  O   . LYS A 1 343 ? 8.715  8.682   -13.231 1.00 43.95 ? 343 LYS A O   1 
ATOM   2521 C  CB  . LYS A 1 343 ? 8.185  6.183   -12.160 1.00 41.36 ? 343 LYS A CB  1 
ATOM   2522 N  N   . GLU A 1 344 ? 9.412  9.577   -11.305 1.00 40.74 ? 344 GLU A N   1 
ATOM   2523 C  CA  . GLU A 1 344 ? 9.467  10.933  -11.836 1.00 42.22 ? 344 GLU A CA  1 
ATOM   2524 C  C   . GLU A 1 344 ? 10.907 11.275  -12.196 1.00 40.02 ? 344 GLU A C   1 
ATOM   2525 O  O   . GLU A 1 344 ? 11.821 11.051  -11.396 1.00 38.25 ? 344 GLU A O   1 
ATOM   2526 C  CB  . GLU A 1 344 ? 8.915  11.946  -10.832 1.00 42.52 ? 344 GLU A CB  1 
ATOM   2527 N  N   . SER A 1 345 ? 11.106 11.809  -13.395 1.00 41.06 ? 345 SER A N   1 
ATOM   2528 C  CA  . SER A 1 345 ? 12.435 12.138  -13.886 1.00 39.89 ? 345 SER A CA  1 
ATOM   2529 C  C   . SER A 1 345 ? 12.758 13.604  -13.627 1.00 39.23 ? 345 SER A C   1 
ATOM   2530 O  O   . SER A 1 345 ? 11.869 14.455  -13.553 1.00 40.16 ? 345 SER A O   1 
ATOM   2531 C  CB  . SER A 1 345 ? 12.554 11.837  -15.381 1.00 39.55 ? 345 SER A CB  1 
ATOM   2532 O  OG  . SER A 1 345 ? 13.888 11.494  -15.718 1.00 40.18 ? 345 SER A OG  1 
ATOM   2533 N  N   . LEU A 1 346 ? 14.050 13.890  -13.489 1.00 34.64 ? 346 LEU A N   1 
ATOM   2534 C  CA  . LEU A 1 346 ? 14.533 15.250  -13.301 1.00 33.37 ? 346 LEU A CA  1 
ATOM   2535 C  C   . LEU A 1 346 ? 15.864 15.380  -14.022 1.00 34.65 ? 346 LEU A C   1 
ATOM   2536 O  O   . LEU A 1 346 ? 16.802 14.632  -13.733 1.00 31.75 ? 346 LEU A O   1 
ATOM   2537 C  CB  . LEU A 1 346 ? 14.686 15.580  -11.815 1.00 35.17 ? 346 LEU A CB  1 
ATOM   2538 C  CG  . LEU A 1 346 ? 15.297 16.937  -11.479 1.00 36.51 ? 346 LEU A CG  1 
ATOM   2539 C  CD1 . LEU A 1 346 ? 14.541 18.055  -12.186 1.00 38.64 ? 346 LEU A CD1 1 
ATOM   2540 C  CD2 . LEU A 1 346 ? 15.297 17.147  -9.975  1.00 37.01 ? 346 LEU A CD2 1 
ATOM   2541 N  N   . GLN A 1 347 ? 15.941 16.308  -14.971 1.00 31.60 ? 347 GLN A N   1 
ATOM   2542 C  CA  . GLN A 1 347 ? 17.182 16.540  -15.692 1.00 33.29 ? 347 GLN A CA  1 
ATOM   2543 C  C   . GLN A 1 347 ? 18.125 17.365  -14.828 1.00 35.54 ? 347 GLN A C   1 
ATOM   2544 O  O   . GLN A 1 347 ? 17.737 18.405  -14.288 1.00 36.33 ? 347 GLN A O   1 
ATOM   2545 C  CB  . GLN A 1 347 ? 16.907 17.249  -17.021 1.00 30.47 ? 347 GLN A CB  1 
ATOM   2546 N  N   . ALA A 1 348 ? 19.356 16.887  -14.674 1.00 37.89 ? 348 ALA A N   1 
ATOM   2547 C  CA  . ALA A 1 348 ? 20.375 17.577  -13.899 1.00 36.18 ? 348 ALA A CA  1 
ATOM   2548 C  C   . ALA A 1 348 ? 21.599 17.776  -14.775 1.00 38.87 ? 348 ALA A C   1 
ATOM   2549 O  O   . ALA A 1 348 ? 21.929 16.917  -15.599 1.00 41.69 ? 348 ALA A O   1 
ATOM   2550 C  CB  . ALA A 1 348 ? 20.747 16.791  -12.641 1.00 35.32 ? 348 ALA A CB  1 
ATOM   2551 N  N   . ASP A 1 349 ? 22.261 18.919  -14.605 1.00 40.04 ? 349 ASP A N   1 
ATOM   2552 C  CA  . ASP A 1 349 ? 23.433 19.234  -15.408 1.00 40.31 ? 349 ASP A CA  1 
ATOM   2553 C  C   . ASP A 1 349 ? 24.727 18.766  -14.761 1.00 38.64 ? 349 ASP A C   1 
ATOM   2554 O  O   . ASP A 1 349 ? 25.704 18.506  -15.473 1.00 37.66 ? 349 ASP A O   1 
ATOM   2555 C  CB  . ASP A 1 349 ? 23.509 20.743  -15.670 1.00 44.44 ? 349 ASP A CB  1 
ATOM   2556 N  N   . ASN A 1 350 ? 24.754 18.651  -13.434 1.00 35.01 ? 350 ASN A N   1 
ATOM   2557 C  CA  . ASN A 1 350 ? 25.947 18.269  -12.695 1.00 34.88 ? 350 ASN A CA  1 
ATOM   2558 C  C   . ASN A 1 350 ? 25.650 17.064  -11.819 1.00 33.95 ? 350 ASN A C   1 
ATOM   2559 O  O   . ASN A 1 350 ? 24.539 16.922  -11.295 1.00 32.84 ? 350 ASN A O   1 
ATOM   2560 C  CB  . ASN A 1 350 ? 26.463 19.419  -11.822 1.00 36.56 ? 350 ASN A CB  1 
ATOM   2561 C  CG  . ASN A 1 350 ? 26.223 20.775  -12.440 1.00 41.58 ? 350 ASN A CG  1 
ATOM   2562 O  OD1 . ASN A 1 350 ? 26.542 21.003  -13.606 1.00 45.05 ? 350 ASN A OD1 1 
ATOM   2563 N  ND2 . ASN A 1 350 ? 25.657 21.689  -11.660 1.00 45.35 ? 350 ASN A ND2 1 
ATOM   2564 N  N   . ILE A 1 351 ? 26.646 16.193  -11.666 1.00 30.38 ? 351 ILE A N   1 
ATOM   2565 C  CA  . ILE A 1 351 ? 26.538 15.039  -10.785 1.00 26.55 ? 351 ILE A CA  1 
ATOM   2566 C  C   . ILE A 1 351 ? 27.868 14.855  -10.067 1.00 26.76 ? 351 ILE A C   1 
ATOM   2567 O  O   . ILE A 1 351 ? 28.936 15.172  -10.601 1.00 27.04 ? 351 ILE A O   1 
ATOM   2568 C  CB  . ILE A 1 351 ? 26.132 13.749  -11.542 1.00 30.85 ? 351 ILE A CB  1 
ATOM   2569 C  CG1 . ILE A 1 351 ? 27.122 13.432  -12.661 1.00 32.55 ? 351 ILE A CG1 1 
ATOM   2570 C  CG2 . ILE A 1 351 ? 24.725 13.869  -12.114 1.00 32.84 ? 351 ILE A CG2 1 
ATOM   2571 C  CD1 . ILE A 1 351 ? 27.296 11.948  -12.899 1.00 31.58 ? 351 ILE A CD1 1 
ATOM   2572 N  N   . LEU A 1 352 ? 27.794 14.366  -8.835  1.00 25.31 ? 352 LEU A N   1 
ATOM   2573 C  CA  . LEU A 1 352 ? 28.994 14.018  -8.090  1.00 22.98 ? 352 LEU A CA  1 
ATOM   2574 C  C   . LEU A 1 352 ? 29.574 12.719  -8.637  1.00 25.82 ? 352 LEU A C   1 
ATOM   2575 O  O   . LEU A 1 352 ? 28.856 11.728  -8.801  1.00 25.03 ? 352 LEU A O   1 
ATOM   2576 C  CB  . LEU A 1 352 ? 28.674 13.870  -6.604  1.00 21.37 ? 352 LEU A CB  1 
ATOM   2577 C  CG  . LEU A 1 352 ? 28.232 15.151  -5.906  1.00 23.26 ? 352 LEU A CG  1 
ATOM   2578 C  CD1 . LEU A 1 352 ? 27.503 14.823  -4.626  1.00 22.21 ? 352 LEU A CD1 1 
ATOM   2579 C  CD2 . LEU A 1 352 ? 29.417 16.081  -5.642  1.00 23.83 ? 352 LEU A CD2 1 
ATOM   2580 N  N   . VAL A 1 353 ? 30.871 12.722  -8.912  1.00 24.82 ? 353 VAL A N   1 
ATOM   2581 C  CA  . VAL A 1 353 ? 31.577 11.560  -9.430  1.00 22.78 ? 353 VAL A CA  1 
ATOM   2582 C  C   . VAL A 1 353 ? 32.687 11.198  -8.449  1.00 25.37 ? 353 VAL A C   1 
ATOM   2583 O  O   . VAL A 1 353 ? 33.713 11.874  -8.377  1.00 22.33 ? 353 VAL A O   1 
ATOM   2584 C  CB  . VAL A 1 353 ? 32.138 11.829  -10.839 1.00 27.47 ? 353 VAL A CB  1 
ATOM   2585 C  CG1 . VAL A 1 353 ? 33.074 10.717  -11.270 1.00 26.70 ? 353 VAL A CG1 1 
ATOM   2586 C  CG2 . VAL A 1 353 ? 30.993 11.989  -11.835 1.00 25.24 ? 353 VAL A CG2 1 
ATOM   2587 N  N   . PRO A 1 354 ? 32.510 10.132  -7.665  1.00 27.45 ? 354 PRO A N   1 
ATOM   2588 C  CA  . PRO A 1 354 ? 33.560 9.735   -6.718  1.00 23.19 ? 354 PRO A CA  1 
ATOM   2589 C  C   . PRO A 1 354 ? 34.760 9.156   -7.455  1.00 22.38 ? 354 PRO A C   1 
ATOM   2590 O  O   . PRO A 1 354 ? 34.624 8.277   -8.312  1.00 24.58 ? 354 PRO A O   1 
ATOM   2591 C  CB  . PRO A 1 354 ? 32.869 8.684   -5.836  1.00 25.60 ? 354 PRO A CB  1 
ATOM   2592 C  CG  . PRO A 1 354 ? 31.757 8.166   -6.663  1.00 29.96 ? 354 PRO A CG  1 
ATOM   2593 C  CD  . PRO A 1 354 ? 31.305 9.293   -7.547  1.00 26.58 ? 354 PRO A CD  1 
ATOM   2594 N  N   . LEU A 1 355 ? 35.940 9.680   -7.135  1.00 20.63 ? 355 LEU A N   1 
ATOM   2595 C  CA  . LEU A 1 355 ? 37.169 9.283   -7.808  1.00 23.23 ? 355 LEU A CA  1 
ATOM   2596 C  C   . LEU A 1 355 ? 38.016 8.343   -6.978  1.00 25.23 ? 355 LEU A C   1 
ATOM   2597 O  O   . LEU A 1 355 ? 38.721 7.496   -7.541  1.00 24.34 ? 355 LEU A O   1 
ATOM   2598 C  CB  . LEU A 1 355 ? 38.010 10.515  -8.159  1.00 23.51 ? 355 LEU A CB  1 
ATOM   2599 C  CG  . LEU A 1 355 ? 37.425 11.475  -9.186  1.00 27.58 ? 355 LEU A CG  1 
ATOM   2600 C  CD1 . LEU A 1 355 ? 38.384 12.638  -9.408  1.00 28.71 ? 355 LEU A CD1 1 
ATOM   2601 C  CD2 . LEU A 1 355 ? 37.154 10.734  -10.477 1.00 28.45 ? 355 LEU A CD2 1 
ATOM   2602 N  N   . ALA A 1 356 ? 37.969 8.481   -5.656  1.00 22.11 ? 356 ALA A N   1 
ATOM   2603 C  CA  . ALA A 1 356 ? 38.756 7.599   -4.807  1.00 26.40 ? 356 ALA A CA  1 
ATOM   2604 C  C   . ALA A 1 356 ? 38.199 7.613   -3.395  1.00 20.44 ? 356 ALA A C   1 
ATOM   2605 O  O   . ALA A 1 356 ? 37.584 8.590   -2.962  1.00 23.59 ? 356 ALA A O   1 
ATOM   2606 C  CB  . ALA A 1 356 ? 40.237 8.001   -4.792  1.00 24.81 ? 356 ALA A CB  1 
ATOM   2607 N  N   . ALA A 1 357 ? 38.423 6.511   -2.687  1.00 23.45 ? 357 ALA A N   1 
ATOM   2608 C  CA  . ALA A 1 357 ? 38.175 6.427   -1.256  1.00 22.99 ? 357 ALA A CA  1 
ATOM   2609 C  C   . ALA A 1 357 ? 39.502 6.188   -0.556  1.00 24.12 ? 357 ALA A C   1 
ATOM   2610 O  O   . ALA A 1 357 ? 40.279 5.328   -0.979  1.00 23.90 ? 357 ALA A O   1 
ATOM   2611 C  CB  . ALA A 1 357 ? 37.190 5.303   -0.919  1.00 21.53 ? 357 ALA A CB  1 
ATOM   2612 N  N   . ILE A 1 358 ? 39.763 6.945   0.502   1.00 19.81 ? 358 ILE A N   1 
ATOM   2613 C  CA  . ILE A 1 358 ? 40.909 6.715   1.367   1.00 19.80 ? 358 ILE A CA  1 
ATOM   2614 C  C   . ILE A 1 358 ? 40.372 6.143   2.669   1.00 19.96 ? 358 ILE A C   1 
ATOM   2615 O  O   . ILE A 1 358 ? 39.463 6.710   3.286   1.00 20.22 ? 358 ILE A O   1 
ATOM   2616 C  CB  . ILE A 1 358 ? 41.721 7.998   1.594   1.00 22.67 ? 358 ILE A CB  1 
ATOM   2617 C  CG1 . ILE A 1 358 ? 42.389 8.422   0.278   1.00 23.43 ? 358 ILE A CG1 1 
ATOM   2618 C  CG2 . ILE A 1 358 ? 42.763 7.778   2.681   1.00 21.42 ? 358 ILE A CG2 1 
ATOM   2619 C  CD1 . ILE A 1 358 ? 43.047 9.773   0.339   1.00 23.88 ? 358 ILE A CD1 1 
ATOM   2620 N  N   . ARG A 1 359 ? 40.888 4.986   3.052   1.00 23.29 ? 359 ARG A N   1 
ATOM   2621 C  CA  . ARG A 1 359 ? 40.393 4.270   4.212   1.00 24.60 ? 359 ARG A CA  1 
ATOM   2622 C  C   . ARG A 1 359 ? 41.578 3.903   5.090   1.00 24.14 ? 359 ARG A C   1 
ATOM   2623 O  O   . ARG A 1 359 ? 42.489 3.192   4.650   1.00 21.96 ? 359 ARG A O   1 
ATOM   2624 C  CB  . ARG A 1 359 ? 39.592 3.043   3.784   1.00 21.56 ? 359 ARG A CB  1 
ATOM   2625 C  CG  . ARG A 1 359 ? 39.243 2.182   4.923   1.00 29.10 ? 359 ARG A CG  1 
ATOM   2626 C  CD  . ARG A 1 359 ? 37.854 2.498   5.443   1.00 25.75 ? 359 ARG A CD  1 
ATOM   2627 N  NE  . ARG A 1 359 ? 37.580 1.554   6.513   1.00 27.28 ? 359 ARG A NE  1 
ATOM   2628 C  CZ  . ARG A 1 359 ? 38.056 1.671   7.743   1.00 28.93 ? 359 ARG A CZ  1 
ATOM   2629 N  NH1 . ARG A 1 359 ? 38.713 2.755   8.128   1.00 26.90 ? 359 ARG A NH1 1 
ATOM   2630 N  NH2 . ARG A 1 359 ? 37.887 0.665   8.602   1.00 31.01 ? 359 ARG A NH2 1 
ATOM   2631 N  N   . ALA A 1 360 ? 41.578 4.427   6.318   1.00 25.72 ? 360 ALA A N   1 
ATOM   2632 C  CA  . ALA A 1 360 ? 42.685 4.233   7.255   1.00 24.53 ? 360 ALA A CA  1 
ATOM   2633 C  C   . ALA A 1 360 ? 44.010 4.691   6.650   1.00 22.26 ? 360 ALA A C   1 
ATOM   2634 O  O   . ALA A 1 360 ? 45.066 4.119   6.925   1.00 28.13 ? 360 ALA A O   1 
ATOM   2635 C  CB  . ALA A 1 360 ? 42.772 2.772   7.710   1.00 27.33 ? 360 ALA A CB  1 
ATOM   2636 N  N   . GLY A 1 361 ? 43.955 5.719   5.802   1.00 24.23 ? 361 GLY A N   1 
ATOM   2637 C  CA  . GLY A 1 361 ? 45.128 6.254   5.147   1.00 22.28 ? 361 GLY A CA  1 
ATOM   2638 C  C   . GLY A 1 361 ? 45.548 5.545   3.876   1.00 26.29 ? 361 GLY A C   1 
ATOM   2639 O  O   . GLY A 1 361 ? 46.568 5.923   3.289   1.00 28.22 ? 361 GLY A O   1 
ATOM   2640 N  N   . LYS A 1 362 ? 44.804 4.539   3.425   1.00 22.13 ? 362 LYS A N   1 
ATOM   2641 C  CA  . LYS A 1 362 ? 45.146 3.809   2.207   1.00 26.16 ? 362 LYS A CA  1 
ATOM   2642 C  C   . LYS A 1 362 ? 44.164 4.170   1.099   1.00 24.81 ? 362 LYS A C   1 
ATOM   2643 O  O   . LYS A 1 362 ? 42.950 4.118   1.304   1.00 22.44 ? 362 LYS A O   1 
ATOM   2644 C  CB  . LYS A 1 362 ? 45.139 2.300   2.458   1.00 28.06 ? 362 LYS A CB  1 
ATOM   2645 N  N   . GLY A 1 363 ? 44.685 4.526   -0.074  1.00 24.93 ? 363 GLY A N   1 
ATOM   2646 C  CA  . GLY A 1 363 ? 43.836 4.953   -1.174  1.00 25.05 ? 363 GLY A CA  1 
ATOM   2647 C  C   . GLY A 1 363 ? 43.368 3.816   -2.074  1.00 28.90 ? 363 GLY A C   1 
ATOM   2648 O  O   . GLY A 1 363 ? 44.084 2.847   -2.308  1.00 25.85 ? 363 GLY A O   1 
ATOM   2649 N  N   . TYR A 1 364 ? 42.140 3.961   -2.582  1.00 26.49 ? 364 TYR A N   1 
ATOM   2650 C  CA  . TYR A 1 364 ? 41.533 3.030   -3.532  1.00 28.13 ? 364 TYR A CA  1 
ATOM   2651 C  C   . TYR A 1 364 ? 40.789 3.843   -4.584  1.00 28.90 ? 364 TYR A C   1 
ATOM   2652 O  O   . TYR A 1 364 ? 39.788 4.498   -4.269  1.00 24.50 ? 364 TYR A O   1 
ATOM   2653 C  CB  . TYR A 1 364 ? 40.576 2.055   -2.840  1.00 29.56 ? 364 TYR A CB  1 
ATOM   2654 C  CG  . TYR A 1 364 ? 41.179 1.320   -1.671  1.00 28.10 ? 364 TYR A CG  1 
ATOM   2655 C  CD1 . TYR A 1 364 ? 41.109 1.842   -0.389  1.00 25.85 ? 364 TYR A CD1 1 
ATOM   2656 C  CD2 . TYR A 1 364 ? 41.839 0.113   -1.853  1.00 30.51 ? 364 TYR A CD2 1 
ATOM   2657 C  CE1 . TYR A 1 364 ? 41.667 1.175   0.682   1.00 29.49 ? 364 TYR A CE1 1 
ATOM   2658 C  CE2 . TYR A 1 364 ? 42.403 -0.559  -0.788  1.00 29.69 ? 364 TYR A CE2 1 
ATOM   2659 C  CZ  . TYR A 1 364 ? 42.310 -0.021  0.479   1.00 28.34 ? 364 TYR A CZ  1 
ATOM   2660 O  OH  . TYR A 1 364 ? 42.867 -0.682  1.549   1.00 30.68 ? 364 TYR A OH  1 
ATOM   2661 N  N   . LEU A 1 365 ? 41.277 3.814   -5.824  1.00 29.91 ? 365 LEU A N   1 
ATOM   2662 C  CA  . LEU A 1 365 ? 40.557 4.439   -6.926  1.00 26.69 ? 365 LEU A CA  1 
ATOM   2663 C  C   . LEU A 1 365 ? 39.231 3.724   -7.159  1.00 28.14 ? 365 LEU A C   1 
ATOM   2664 O  O   . LEU A 1 365 ? 39.138 2.499   -7.031  1.00 29.18 ? 365 LEU A O   1 
ATOM   2665 C  CB  . LEU A 1 365 ? 41.389 4.399   -8.213  1.00 28.83 ? 365 LEU A CB  1 
ATOM   2666 C  CG  . LEU A 1 365 ? 42.634 5.275   -8.324  1.00 29.74 ? 365 LEU A CG  1 
ATOM   2667 C  CD1 . LEU A 1 365 ? 43.450 4.896   -9.549  1.00 34.95 ? 365 LEU A CD1 1 
ATOM   2668 C  CD2 . LEU A 1 365 ? 42.237 6.744   -8.378  1.00 29.97 ? 365 LEU A CD2 1 
ATOM   2669 N  N   . THR A 1 366 ? 38.200 4.498   -7.492  1.00 24.29 ? 366 THR A N   1 
ATOM   2670 C  CA  . THR A 1 366 ? 36.971 3.927   -8.020  1.00 26.11 ? 366 THR A CA  1 
ATOM   2671 C  C   . THR A 1 366 ? 37.154 3.622   -9.503  1.00 28.96 ? 366 THR A C   1 
ATOM   2672 O  O   . THR A 1 366 ? 38.180 3.945   -10.109 1.00 27.54 ? 366 THR A O   1 
ATOM   2673 C  CB  . THR A 1 366 ? 35.794 4.883   -7.851  1.00 25.30 ? 366 THR A CB  1 
ATOM   2674 O  OG1 . THR A 1 366 ? 35.984 6.009   -8.717  1.00 25.55 ? 366 THR A OG1 1 
ATOM   2675 C  CG2 . THR A 1 366 ? 35.681 5.367   -6.406  1.00 23.24 ? 366 THR A CG2 1 
ATOM   2676 N  N   . GLU A 1 367 ? 36.126 3.024   -10.107 1.00 24.66 ? 367 GLU A N   1 
ATOM   2677 C  CA  . GLU A 1 367 ? 36.171 2.769   -11.541 1.00 30.59 ? 367 GLU A CA  1 
ATOM   2678 C  C   . GLU A 1 367 ? 36.397 4.066   -12.309 1.00 29.54 ? 367 GLU A C   1 
ATOM   2679 O  O   . GLU A 1 367 ? 37.297 4.155   -13.150 1.00 27.50 ? 367 GLU A O   1 
ATOM   2680 C  CB  . GLU A 1 367 ? 34.880 2.077   -11.987 1.00 29.46 ? 367 GLU A CB  1 
ATOM   2681 N  N   . GLN A 1 368 ? 35.615 5.101   -11.987 1.00 30.64 ? 368 GLN A N   1 
ATOM   2682 C  CA  . GLN A 1 368 ? 35.765 6.403   -12.635 1.00 30.33 ? 368 GLN A CA  1 
ATOM   2683 C  C   . GLN A 1 368 ? 37.121 7.031   -12.329 1.00 32.02 ? 368 GLN A C   1 
ATOM   2684 O  O   . GLN A 1 368 ? 37.711 7.698   -13.187 1.00 32.67 ? 368 GLN A O   1 
ATOM   2685 C  CB  . GLN A 1 368 ? 34.634 7.325   -12.184 1.00 29.14 ? 368 GLN A CB  1 
ATOM   2686 C  CG  . GLN A 1 368 ? 33.249 6.709   -12.322 1.00 31.17 ? 368 GLN A CG  1 
ATOM   2687 C  CD  . GLN A 1 368 ? 32.650 6.301   -10.985 1.00 33.97 ? 368 GLN A CD  1 
ATOM   2688 O  OE1 . GLN A 1 368 ? 33.176 5.411   -10.310 1.00 32.55 ? 368 GLN A OE1 1 
ATOM   2689 N  NE2 . GLN A 1 368 ? 31.560 6.953   -10.589 1.00 31.81 ? 368 GLN A NE2 1 
ATOM   2690 N  N   . GLY A 1 369 ? 37.626 6.836   -11.108 1.00 26.19 ? 369 GLY A N   1 
ATOM   2691 C  CA  . GLY A 1 369 ? 38.947 7.345   -10.777 1.00 29.10 ? 369 GLY A CA  1 
ATOM   2692 C  C   . GLY A 1 369 ? 40.048 6.693   -11.593 1.00 32.54 ? 369 GLY A C   1 
ATOM   2693 O  O   . GLY A 1 369 ? 41.009 7.354   -12.000 1.00 33.88 ? 369 GLY A O   1 
ATOM   2694 N  N   . SER A 1 370 ? 39.936 5.383   -11.828 1.00 29.64 ? 370 SER A N   1 
ATOM   2695 C  CA  . SER A 1 370 ? 40.896 4.720   -12.703 1.00 30.50 ? 370 SER A CA  1 
ATOM   2696 C  C   . SER A 1 370 ? 40.760 5.216   -14.138 1.00 33.50 ? 370 SER A C   1 
ATOM   2697 O  O   . SER A 1 370 ? 41.768 5.486   -14.805 1.00 34.79 ? 370 SER A O   1 
ATOM   2698 C  CB  . SER A 1 370 ? 40.713 3.205   -12.638 1.00 29.17 ? 370 SER A CB  1 
ATOM   2699 O  OG  . SER A 1 370 ? 40.801 2.749   -11.304 1.00 36.10 ? 370 SER A OG  1 
ATOM   2700 N  N   . ALA A 1 371 ? 39.522 5.352   -14.620 1.00 32.71 ? 371 ALA A N   1 
ATOM   2701 C  CA  . ALA A 1 371 ? 39.292 5.811   -15.988 1.00 35.76 ? 371 ALA A CA  1 
ATOM   2702 C  C   . ALA A 1 371 ? 39.914 7.183   -16.222 1.00 36.95 ? 371 ALA A C   1 
ATOM   2703 O  O   . ALA A 1 371 ? 40.693 7.371   -17.163 1.00 41.87 ? 371 ALA A O   1 
ATOM   2704 C  CB  . ALA A 1 371 ? 37.791 5.837   -16.285 1.00 33.91 ? 371 ALA A CB  1 
ATOM   2705 N  N   . GLU A 1 372 ? 39.593 8.155   -15.365 1.00 36.33 ? 372 GLU A N   1 
ATOM   2706 C  CA  . GLU A 1 372 ? 40.150 9.496   -15.512 1.00 38.03 ? 372 GLU A CA  1 
ATOM   2707 C  C   . GLU A 1 372 ? 41.652 9.546   -15.254 1.00 39.87 ? 372 GLU A C   1 
ATOM   2708 O  O   . GLU A 1 372 ? 42.289 10.539  -15.625 1.00 36.51 ? 372 GLU A O   1 
ATOM   2709 C  CB  . GLU A 1 372 ? 39.414 10.471  -14.582 1.00 38.44 ? 372 GLU A CB  1 
ATOM   2710 C  CG  . GLU A 1 372 ? 37.961 10.704  -14.994 1.00 34.12 ? 372 GLU A CG  1 
ATOM   2711 C  CD  . GLU A 1 372 ? 37.228 11.740  -14.150 1.00 40.04 ? 372 GLU A CD  1 
ATOM   2712 O  OE1 . GLU A 1 372 ? 37.870 12.669  -13.604 1.00 37.89 ? 372 GLU A OE1 1 
ATOM   2713 O  OE2 . GLU A 1 372 ? 35.987 11.629  -14.055 1.00 37.41 ? 372 GLU A OE2 1 
ATOM   2714 N  N   . HIS A 1 373 ? 42.226 8.492   -14.665 1.00 38.20 ? 373 HIS A N   1 
ATOM   2715 C  CA  . HIS A 1 373 ? 43.630 8.447   -14.268 1.00 38.84 ? 373 HIS A CA  1 
ATOM   2716 C  C   . HIS A 1 373 ? 43.921 9.509   -13.213 1.00 43.14 ? 373 HIS A C   1 
ATOM   2717 O  O   . HIS A 1 373 ? 43.686 9.284   -12.019 1.00 46.93 ? 373 HIS A O   1 
ATOM   2718 C  CB  . HIS A 1 373 ? 44.552 8.621   -15.478 1.00 41.01 ? 373 HIS A CB  1 
ATOM   2719 N  N   . ALA A 1 374 ? 44.434 10.662  -13.650 1.00 43.54 ? 374 ALA A N   1 
ATOM   2720 C  CA  . ALA A 1 374 ? 44.727 11.808  -12.790 1.00 42.66 ? 374 ALA A CA  1 
ATOM   2721 C  C   . ALA A 1 374 ? 45.761 11.479  -11.718 1.00 42.99 ? 374 ALA A C   1 
ATOM   2722 O  O   . ALA A 1 374 ? 46.832 12.094  -11.679 1.00 42.45 ? 374 ALA A O   1 
ATOM   2723 C  CB  . ALA A 1 374 ? 43.450 12.352  -12.138 1.00 41.81 ? 374 ALA A CB  1 
ATOM   2724 N  N   . PHE A 1 375 ? 45.458 10.526  -10.840 1.00 42.76 ? 375 PHE A N   1 
ATOM   2725 C  CA  . PHE A 1 375 ? 46.376 10.191  -9.763  1.00 41.66 ? 375 PHE A CA  1 
ATOM   2726 C  C   . PHE A 1 375 ? 46.230 8.717   -9.425  1.00 41.55 ? 375 PHE A C   1 
ATOM   2727 O  O   . PHE A 1 375 ? 45.238 8.073   -9.774  1.00 38.47 ? 375 PHE A O   1 
ATOM   2728 C  CB  . PHE A 1 375 ? 46.130 11.061  -8.522  1.00 39.32 ? 375 PHE A CB  1 
ATOM   2729 C  CG  . PHE A 1 375 ? 44.686 11.143  -8.105  1.00 38.76 ? 375 PHE A CG  1 
ATOM   2730 C  CD1 . PHE A 1 375 ? 44.149 10.210  -7.229  1.00 35.55 ? 375 PHE A CD1 1 
ATOM   2731 C  CD2 . PHE A 1 375 ? 43.863 12.147  -8.595  1.00 39.07 ? 375 PHE A CD2 1 
ATOM   2732 C  CE1 . PHE A 1 375 ? 42.815 10.281  -6.844  1.00 30.53 ? 375 PHE A CE1 1 
ATOM   2733 C  CE2 . PHE A 1 375 ? 42.535 12.223  -8.215  1.00 35.93 ? 375 PHE A CE2 1 
ATOM   2734 C  CZ  . PHE A 1 375 ? 42.010 11.286  -7.335  1.00 32.40 ? 375 PHE A CZ  1 
ATOM   2735 N  N   . ASP A 1 376 ? 47.245 8.189   -8.746  1.00 42.37 ? 376 ASP A N   1 
ATOM   2736 C  CA  . ASP A 1 376 ? 47.266 6.797   -8.326  1.00 41.91 ? 376 ASP A CA  1 
ATOM   2737 C  C   . ASP A 1 376 ? 47.913 6.710   -6.951  1.00 43.28 ? 376 ASP A C   1 
ATOM   2738 O  O   . ASP A 1 376 ? 48.666 7.595   -6.538  1.00 42.76 ? 376 ASP A O   1 
ATOM   2739 C  CB  . ASP A 1 376 ? 48.018 5.913   -9.328  1.00 40.78 ? 376 ASP A CB  1 
ATOM   2740 N  N   . PHE A 1 377 ? 47.618 5.621   -6.252  1.00 44.65 ? 377 PHE A N   1 
ATOM   2741 C  CA  . PHE A 1 377 ? 48.096 5.424   -4.889  1.00 41.86 ? 377 PHE A CA  1 
ATOM   2742 C  C   . PHE A 1 377 ? 49.233 4.408   -4.834  1.00 45.43 ? 377 PHE A C   1 
ATOM   2743 O  O   . PHE A 1 377 ? 50.224 4.543   -5.549  1.00 46.74 ? 377 PHE A O   1 
ATOM   2744 C  CB  . PHE A 1 377 ? 46.936 4.976   -4.006  1.00 37.14 ? 377 PHE A CB  1 
ATOM   2745 C  CG  . PHE A 1 377 ? 45.931 6.054   -3.767  1.00 34.09 ? 377 PHE A CG  1 
ATOM   2746 C  CD1 . PHE A 1 377 ? 46.235 7.140   -2.962  1.00 33.13 ? 377 PHE A CD1 1 
ATOM   2747 C  CD2 . PHE A 1 377 ? 44.701 6.017   -4.401  1.00 33.42 ? 377 PHE A CD2 1 
ATOM   2748 C  CE1 . PHE A 1 377 ? 45.310 8.143   -2.755  1.00 27.61 ? 377 PHE A CE1 1 
ATOM   2749 C  CE2 . PHE A 1 377 ? 43.774 7.019   -4.203  1.00 29.19 ? 377 PHE A CE2 1 
ATOM   2750 C  CZ  . PHE A 1 377 ? 44.076 8.087   -3.386  1.00 28.52 ? 377 PHE A CZ  1 
HETATM 2751 C  C1  . EDO B 2 .   ? 17.935 26.667  -3.032  1.00 38.82 ? 401 EDO A C1  1 
HETATM 2752 O  O1  . EDO B 2 .   ? 16.613 26.952  -3.500  1.00 40.97 ? 401 EDO A O1  1 
HETATM 2753 C  C2  . EDO B 2 .   ? 18.961 27.238  -4.007  1.00 37.97 ? 401 EDO A C2  1 
HETATM 2754 O  O2  . EDO B 2 .   ? 20.224 26.619  -3.752  1.00 39.70 ? 401 EDO A O2  1 
HETATM 2755 C  C1  . EDO C 2 .   ? -0.652 13.770  12.131  1.00 50.29 ? 402 EDO A C1  1 
HETATM 2756 O  O1  . EDO C 2 .   ? 0.497  12.920  12.010  1.00 47.86 ? 402 EDO A O1  1 
HETATM 2757 C  C2  . EDO C 2 .   ? -0.394 14.821  13.207  1.00 44.28 ? 402 EDO A C2  1 
HETATM 2758 O  O2  . EDO C 2 .   ? 0.629  15.714  12.760  1.00 38.25 ? 402 EDO A O2  1 
HETATM 2759 C  C1  . EDO D 2 .   ? 31.174 22.982  -11.732 1.00 40.04 ? 403 EDO A C1  1 
HETATM 2760 O  O1  . EDO D 2 .   ? 31.113 21.829  -10.888 1.00 44.10 ? 403 EDO A O1  1 
HETATM 2761 C  C2  . EDO D 2 .   ? 30.251 22.760  -12.921 1.00 46.68 ? 403 EDO A C2  1 
HETATM 2762 O  O2  . EDO D 2 .   ? 30.566 21.503  -13.529 1.00 42.02 ? 403 EDO A O2  1 
HETATM 2763 C  C1  . EDO E 2 .   ? 43.773 1.768   -7.082  1.00 37.86 ? 404 EDO A C1  1 
HETATM 2764 O  O1  . EDO E 2 .   ? 42.879 1.600   -5.977  1.00 38.52 ? 404 EDO A O1  1 
HETATM 2765 C  C2  . EDO E 2 .   ? 44.860 2.764   -6.700  1.00 39.34 ? 404 EDO A C2  1 
HETATM 2766 O  O2  . EDO E 2 .   ? 46.033 2.518   -7.489  1.00 42.50 ? 404 EDO A O2  1 
HETATM 2767 ZN ZN  . ZN  F 3 .   ? 16.241 -0.204  4.129   1.00 25.55 ? 405 ZN  A ZN  1 
HETATM 2768 ZN ZN  . ZN  G 3 .   ? 12.820 0.685   4.995   1.00 28.90 ? 406 ZN  A ZN  1 
HETATM 2769 O  O   . HOH H 4 .   ? 39.567 13.921  -12.805 1.00 38.05 ? 501 HOH A O   1 
HETATM 2770 O  O   . HOH H 4 .   ? 9.684  17.855  -8.385  1.00 37.85 ? 502 HOH A O   1 
HETATM 2771 O  O   . HOH H 4 .   ? 37.299 4.567   14.197  1.00 31.86 ? 503 HOH A O   1 
HETATM 2772 O  O   . HOH H 4 .   ? 55.992 15.611  -0.195  1.00 30.93 ? 504 HOH A O   1 
HETATM 2773 O  O   . HOH H 4 .   ? 21.383 -7.001  3.514   1.00 23.26 ? 505 HOH A O   1 
HETATM 2774 O  O   . HOH H 4 .   ? 24.361 8.891   5.624   1.00 19.80 ? 506 HOH A O   1 
HETATM 2775 O  O   . HOH H 4 .   ? 14.393 -2.550  -5.891  1.00 26.80 ? 507 HOH A O   1 
HETATM 2776 O  O   . HOH H 4 .   ? 24.153 17.375  13.408  1.00 39.74 ? 508 HOH A O   1 
HETATM 2777 O  O   . HOH H 4 .   ? 15.588 17.623  14.918  1.00 34.93 ? 509 HOH A O   1 
HETATM 2778 O  O   . HOH H 4 .   ? 52.711 3.247   10.992  1.00 44.48 ? 510 HOH A O   1 
HETATM 2779 O  O   . HOH H 4 .   ? 29.133 0.362   21.885  1.00 28.82 ? 511 HOH A O   1 
HETATM 2780 O  O   . HOH H 4 .   ? 47.397 23.903  -0.913  1.00 29.47 ? 512 HOH A O   1 
HETATM 2781 O  O   . HOH H 4 .   ? 33.760 16.639  8.022   1.00 32.24 ? 513 HOH A O   1 
HETATM 2782 O  O   . HOH H 4 .   ? 8.262  25.938  7.518   1.00 36.49 ? 514 HOH A O   1 
HETATM 2783 O  O   . HOH H 4 .   ? 15.709 19.761  17.883  1.00 34.75 ? 515 HOH A O   1 
HETATM 2784 O  O   . HOH H 4 .   ? 6.184  11.947  23.391  1.00 45.45 ? 516 HOH A O   1 
HETATM 2785 O  O   . HOH H 4 .   ? 31.594 17.748  6.076   1.00 33.58 ? 517 HOH A O   1 
HETATM 2786 O  O   . HOH H 4 .   ? 22.929 17.792  8.130   1.00 23.55 ? 518 HOH A O   1 
HETATM 2787 O  O   . HOH H 4 .   ? 12.436 2.015   -0.053  1.00 29.51 ? 519 HOH A O   1 
HETATM 2788 O  O   . HOH H 4 .   ? 40.589 0.435   -6.089  1.00 36.10 ? 520 HOH A O   1 
HETATM 2789 O  O   . HOH H 4 .   ? 48.505 6.192   7.428   1.00 26.27 ? 521 HOH A O   1 
HETATM 2790 O  O   . HOH H 4 .   ? 34.324 6.664   7.305   1.00 22.33 ? 522 HOH A O   1 
HETATM 2791 O  O   . HOH H 4 .   ? -1.179 11.269  4.233   1.00 28.47 ? 523 HOH A O   1 
HETATM 2792 O  O   . HOH H 4 .   ? 17.432 -9.352  17.071  1.00 30.78 ? 524 HOH A O   1 
HETATM 2793 O  O   . HOH H 4 .   ? 36.900 -10.334 15.517  1.00 36.81 ? 525 HOH A O   1 
HETATM 2794 O  O   . HOH H 4 .   ? 37.409 2.766   -4.574  1.00 28.60 ? 526 HOH A O   1 
HETATM 2795 O  O   . HOH H 4 .   ? 13.100 9.610   1.422   1.00 24.34 ? 527 HOH A O   1 
HETATM 2796 O  O   . HOH H 4 .   ? 26.322 3.303   -0.607  1.00 23.96 ? 528 HOH A O   1 
HETATM 2797 O  O   . HOH H 4 .   ? 29.923 -6.107  28.230  1.00 48.12 ? 529 HOH A O   1 
HETATM 2798 O  O   . HOH H 4 .   ? 26.066 4.504   18.005  1.00 29.43 ? 530 HOH A O   1 
HETATM 2799 O  O   . HOH H 4 .   ? 29.049 -7.282  -5.423  1.00 31.84 ? 531 HOH A O   1 
HETATM 2800 O  O   . HOH H 4 .   ? 37.754 -1.371  11.886  1.00 39.89 ? 532 HOH A O   1 
HETATM 2801 O  O   . HOH H 4 .   ? 28.007 6.970   -8.717  1.00 26.09 ? 533 HOH A O   1 
HETATM 2802 O  O   . HOH H 4 .   ? 11.974 -3.964  11.741  1.00 31.29 ? 534 HOH A O   1 
HETATM 2803 O  O   . HOH H 4 .   ? 0.681  13.886  -3.371  1.00 32.62 ? 535 HOH A O   1 
HETATM 2804 O  O   . HOH H 4 .   ? 25.877 18.855  11.165  1.00 35.00 ? 536 HOH A O   1 
HETATM 2805 O  O   . HOH H 4 .   ? 35.359 20.820  -14.059 1.00 31.77 ? 537 HOH A O   1 
HETATM 2806 O  O   . HOH H 4 .   ? 35.558 19.269  1.989   1.00 25.74 ? 538 HOH A O   1 
HETATM 2807 O  O   . HOH H 4 .   ? 4.600  3.672   8.009   1.00 27.95 ? 539 HOH A O   1 
HETATM 2808 O  O   . HOH H 4 .   ? 21.585 -5.494  10.645  1.00 23.51 ? 540 HOH A O   1 
HETATM 2809 O  O   . HOH H 4 .   ? 30.600 -13.622 16.047  1.00 34.06 ? 541 HOH A O   1 
HETATM 2810 O  O   . HOH H 4 .   ? 29.947 -0.785  -6.759  1.00 26.30 ? 542 HOH A O   1 
HETATM 2811 O  O   . HOH H 4 .   ? 17.092 -8.493  -4.743  1.00 44.93 ? 543 HOH A O   1 
HETATM 2812 O  O   . HOH H 4 .   ? 30.068 -6.657  25.999  1.00 40.95 ? 544 HOH A O   1 
HETATM 2813 O  O   . HOH H 4 .   ? 36.537 10.946  7.912   1.00 20.13 ? 545 HOH A O   1 
HETATM 2814 O  O   . HOH H 4 .   ? 49.545 21.227  -11.648 1.00 33.14 ? 546 HOH A O   1 
HETATM 2815 O  O   . HOH H 4 .   ? 23.475 19.612  5.816   1.00 17.46 ? 547 HOH A O   1 
HETATM 2816 O  O   . HOH H 4 .   ? 20.717 19.666  5.818   1.00 23.18 ? 548 HOH A O   1 
HETATM 2817 O  O   . HOH H 4 .   ? 34.313 1.543   -8.580  1.00 31.93 ? 549 HOH A O   1 
HETATM 2818 O  O   . HOH H 4 .   ? 21.390 -13.025 20.769  1.00 34.83 ? 550 HOH A O   1 
HETATM 2819 O  O   . HOH H 4 .   ? 28.663 6.910   -3.954  1.00 25.83 ? 551 HOH A O   1 
HETATM 2820 O  O   . HOH H 4 .   ? 26.181 -7.865  -4.482  1.00 31.12 ? 552 HOH A O   1 
HETATM 2821 O  O   . HOH H 4 .   ? 12.253 8.527   24.441  1.00 40.66 ? 553 HOH A O   1 
HETATM 2822 O  O   . HOH H 4 .   ? 14.169 4.722   24.761  1.00 38.51 ? 554 HOH A O   1 
HETATM 2823 O  O   . HOH H 4 .   ? 27.138 4.483   -2.719  1.00 22.20 ? 555 HOH A O   1 
HETATM 2824 O  O   . HOH H 4 .   ? 4.554  23.442  7.509   1.00 35.90 ? 556 HOH A O   1 
HETATM 2825 O  O   . HOH H 4 .   ? 8.757  4.248   2.617   1.00 26.77 ? 557 HOH A O   1 
HETATM 2826 O  O   . HOH H 4 .   ? 18.650 -10.772 6.168   1.00 33.77 ? 558 HOH A O   1 
HETATM 2827 O  O   . HOH H 4 .   ? 30.096 11.450  16.479  1.00 28.64 ? 559 HOH A O   1 
HETATM 2828 O  O   . HOH H 4 .   ? 16.139 -9.632  2.384   1.00 32.85 ? 560 HOH A O   1 
HETATM 2829 O  O   . HOH H 4 .   ? 23.666 8.986   10.816  1.00 22.79 ? 561 HOH A O   1 
HETATM 2830 O  O   . HOH H 4 .   ? 34.880 18.947  -9.203  1.00 30.40 ? 562 HOH A O   1 
HETATM 2831 O  O   . HOH H 4 .   ? 34.138 9.400   7.657   1.00 21.15 ? 563 HOH A O   1 
HETATM 2832 O  O   . HOH H 4 .   ? 7.569  12.228  3.438   1.00 23.67 ? 564 HOH A O   1 
HETATM 2833 O  O   . HOH H 4 .   ? 45.978 25.248  8.963   1.00 31.94 ? 565 HOH A O   1 
HETATM 2834 O  O   . HOH H 4 .   ? 28.482 9.257   -10.063 1.00 25.91 ? 566 HOH A O   1 
HETATM 2835 O  O   . HOH H 4 .   ? 4.842  11.870  -4.596  1.00 30.38 ? 567 HOH A O   1 
HETATM 2836 O  O   . HOH H 4 .   ? 50.594 14.083  -8.096  1.00 30.85 ? 568 HOH A O   1 
HETATM 2837 O  O   . HOH H 4 .   ? 14.594 -0.154  -1.386  1.00 31.49 ? 569 HOH A O   1 
HETATM 2838 O  O   . HOH H 4 .   ? 7.922  7.460   -2.164  1.00 28.73 ? 570 HOH A O   1 
HETATM 2839 O  O   . HOH H 4 .   ? 42.297 0.292   4.168   1.00 31.06 ? 571 HOH A O   1 
HETATM 2840 O  O   . HOH H 4 .   ? 41.816 28.882  -1.722  1.00 31.79 ? 572 HOH A O   1 
HETATM 2841 O  O   . HOH H 4 .   ? 40.780 8.869   15.267  1.00 27.19 ? 573 HOH A O   1 
HETATM 2842 O  O   . HOH H 4 .   ? 5.709  14.212  18.028  1.00 36.04 ? 574 HOH A O   1 
HETATM 2843 O  O   . HOH H 4 .   ? 43.460 11.281  17.879  1.00 38.61 ? 575 HOH A O   1 
HETATM 2844 O  O   . HOH H 4 .   ? 37.017 11.502  10.446  1.00 22.04 ? 576 HOH A O   1 
HETATM 2845 O  O   . HOH H 4 .   ? 32.726 4.964   14.524  1.00 27.86 ? 577 HOH A O   1 
HETATM 2846 O  O   . HOH H 4 .   ? 47.558 4.621   -0.268  1.00 29.65 ? 578 HOH A O   1 
HETATM 2847 O  O   . HOH H 4 .   ? 27.766 -0.245  -8.453  1.00 34.30 ? 579 HOH A O   1 
HETATM 2848 O  O   . HOH H 4 .   ? 41.554 15.021  17.514  1.00 34.50 ? 580 HOH A O   1 
HETATM 2849 O  O   . HOH H 4 .   ? 7.882  13.269  -7.250  1.00 33.01 ? 581 HOH A O   1 
HETATM 2850 O  O   . HOH H 4 .   ? 6.644  19.930  -4.840  1.00 27.72 ? 582 HOH A O   1 
HETATM 2851 O  O   . HOH H 4 .   ? 34.563 17.037  5.183   1.00 29.16 ? 583 HOH A O   1 
HETATM 2852 O  O   . HOH H 4 .   ? 56.404 15.075  8.130   1.00 34.29 ? 584 HOH A O   1 
HETATM 2853 O  O   . HOH H 4 .   ? 37.763 -4.864  13.485  1.00 44.10 ? 585 HOH A O   1 
HETATM 2854 O  O   . HOH H 4 .   ? 39.859 3.606   10.692  1.00 29.29 ? 586 HOH A O   1 
HETATM 2855 O  O   . HOH H 4 .   ? 39.489 -5.690  6.864   1.00 35.10 ? 587 HOH A O   1 
HETATM 2856 O  O   . HOH H 4 .   ? 37.431 -2.300  7.542   1.00 27.68 ? 588 HOH A O   1 
HETATM 2857 O  O   . HOH H 4 .   ? 40.314 -0.940  5.449   1.00 29.14 ? 589 HOH A O   1 
HETATM 2858 O  O   . HOH H 4 .   ? 49.891 25.202  -3.081  1.00 26.60 ? 590 HOH A O   1 
HETATM 2859 O  O   . HOH H 4 .   ? 42.501 4.449   11.217  1.00 32.08 ? 591 HOH A O   1 
HETATM 2860 O  O   . HOH H 4 .   ? 47.001 12.957  14.138  1.00 24.31 ? 592 HOH A O   1 
HETATM 2861 O  O   . HOH H 4 .   ? -1.316 16.412  -0.718  1.00 30.64 ? 593 HOH A O   1 
HETATM 2862 O  O   . HOH H 4 .   ? 28.106 -5.398  -9.008  1.00 29.82 ? 594 HOH A O   1 
HETATM 2863 O  O   . HOH H 4 .   ? 26.999 24.920  -3.523  1.00 27.38 ? 595 HOH A O   1 
HETATM 2864 O  O   . HOH H 4 .   ? 47.998 26.639  7.314   1.00 30.91 ? 596 HOH A O   1 
HETATM 2865 O  O   . HOH H 4 .   ? 22.242 23.941  6.609   1.00 25.57 ? 597 HOH A O   1 
HETATM 2866 O  O   . HOH H 4 .   ? 25.455 -9.634  -2.353  1.00 26.83 ? 598 HOH A O   1 
HETATM 2867 O  O   . HOH H 4 .   ? 20.187 25.721  0.281   1.00 28.62 ? 599 HOH A O   1 
HETATM 2868 O  O   . HOH H 4 .   ? 27.684 -14.749 0.896   1.00 28.44 ? 600 HOH A O   1 
HETATM 2869 O  O   . HOH H 4 .   ? 18.074 7.520   -10.848 1.00 29.41 ? 601 HOH A O   1 
HETATM 2870 O  O   . HOH H 4 .   ? 5.592  0.773   3.586   1.00 32.18 ? 602 HOH A O   1 
HETATM 2871 O  O   . HOH H 4 .   ? 12.892 -1.685  3.498   1.00 36.20 ? 603 HOH A O   1 
HETATM 2872 O  O   . HOH H 4 .   ? 41.269 15.168  -11.248 1.00 37.24 ? 604 HOH A O   1 
HETATM 2873 O  O   . HOH H 4 .   ? 34.820 5.937   15.447  1.00 26.23 ? 605 HOH A O   1 
HETATM 2874 O  O   . HOH H 4 .   ? 38.324 20.639  6.888   1.00 37.83 ? 606 HOH A O   1 
HETATM 2875 O  O   . HOH H 4 .   ? 20.430 -7.591  -7.343  1.00 34.03 ? 607 HOH A O   1 
HETATM 2876 O  O   . HOH H 4 .   ? 16.312 16.608  10.976  1.00 23.04 ? 608 HOH A O   1 
HETATM 2877 O  O   . HOH H 4 .   ? 53.798 5.705   3.445   1.00 38.13 ? 609 HOH A O   1 
HETATM 2878 O  O   . HOH H 4 .   ? 48.519 21.921  -9.106  1.00 30.57 ? 610 HOH A O   1 
HETATM 2879 O  O   . HOH H 4 .   ? 4.526  -1.142  4.061   1.00 32.34 ? 611 HOH A O   1 
HETATM 2880 O  O   . HOH H 4 .   ? 54.474 21.586  -3.929  1.00 38.93 ? 612 HOH A O   1 
HETATM 2881 O  O   . HOH H 4 .   ? 46.105 -0.809  1.051   1.00 41.12 ? 613 HOH A O   1 
HETATM 2882 O  O   . HOH H 4 .   ? 32.198 -5.697  18.104  1.00 22.99 ? 614 HOH A O   1 
HETATM 2883 O  O   . HOH H 4 .   ? 34.660 23.213  3.502   1.00 31.33 ? 615 HOH A O   1 
HETATM 2884 O  O   . HOH H 4 .   ? 3.678  9.784   -4.442  1.00 33.40 ? 616 HOH A O   1 
HETATM 2885 O  O   . HOH H 4 .   ? 50.913 5.175   2.909   1.00 38.89 ? 617 HOH A O   1 
HETATM 2886 O  O   . HOH H 4 .   ? 15.166 -1.787  -8.623  1.00 34.26 ? 618 HOH A O   1 
HETATM 2887 O  O   . HOH H 4 .   ? -1.064 18.359  10.820  1.00 36.07 ? 619 HOH A O   1 
HETATM 2888 O  O   . HOH H 4 .   ? 7.365  22.420  -3.930  1.00 31.10 ? 620 HOH A O   1 
HETATM 2889 O  O   . HOH H 4 .   ? 8.465  11.747  23.729  1.00 43.62 ? 621 HOH A O   1 
HETATM 2890 O  O   . HOH H 4 .   ? 37.335 -0.193  -5.363  1.00 36.72 ? 622 HOH A O   1 
HETATM 2891 O  O   . HOH H 4 .   ? 36.718 -0.159  -7.733  1.00 34.07 ? 623 HOH A O   1 
HETATM 2892 O  O   . HOH H 4 .   ? 31.307 3.894   16.874  1.00 25.72 ? 624 HOH A O   1 
HETATM 2893 O  O   . HOH H 4 .   ? 36.735 20.336  -8.187  1.00 35.65 ? 625 HOH A O   1 
HETATM 2894 O  O   . HOH H 4 .   ? 41.649 9.884   20.000  1.00 40.89 ? 626 HOH A O   1 
HETATM 2895 O  O   . HOH H 4 .   ? 11.568 -1.249  1.667   1.00 40.10 ? 627 HOH A O   1 
HETATM 2896 O  O   . HOH H 4 .   ? 26.633 -17.929 13.271  1.00 36.75 ? 628 HOH A O   1 
HETATM 2897 O  O   . HOH H 4 .   ? 21.282 19.381  9.553   1.00 29.64 ? 629 HOH A O   1 
HETATM 2898 O  O   . HOH H 4 .   ? 22.619 20.141  12.118  1.00 47.22 ? 630 HOH A O   1 
HETATM 2899 O  O   . HOH H 4 .   ? 14.488 20.681  10.355  1.00 31.99 ? 631 HOH A O   1 
HETATM 2900 O  O   . HOH H 4 .   ? 10.511 6.507   25.814  1.00 37.25 ? 632 HOH A O   1 
HETATM 2901 O  O   . HOH H 4 .   ? 4.081  19.138  -5.558  1.00 34.37 ? 633 HOH A O   1 
HETATM 2902 O  O   . HOH H 4 .   ? -3.050 14.143  15.014  1.00 53.09 ? 634 HOH A O   1 
HETATM 2903 O  O   . HOH H 4 .   ? 40.160 30.820  -1.993  1.00 42.23 ? 635 HOH A O   1 
HETATM 2904 O  O   . HOH H 4 .   ? 30.673 27.131  -8.644  1.00 52.87 ? 636 HOH A O   1 
HETATM 2905 O  O   . HOH H 4 .   ? 38.898 -12.654 9.554   1.00 40.48 ? 637 HOH A O   1 
HETATM 2906 O  O   . HOH H 4 .   ? 57.064 21.708  -4.296  1.00 48.99 ? 638 HOH A O   1 
HETATM 2907 O  O   . HOH H 4 .   ? 0.000  -11.891 21.779  0.50 49.39 ? 639 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   . MET A 1   ? 0.3456 0.6102 0.6246 0.0401  -0.0317 -0.0193 1   MET A N   
2    C  CA  . MET A 1   ? 0.2867 0.5446 0.5637 0.0415  -0.0192 -0.0201 1   MET A CA  
3    C  C   . MET A 1   ? 0.2814 0.5073 0.5340 0.0457  -0.0167 -0.0196 1   MET A C   
4    O  O   . MET A 1   ? 0.2658 0.4806 0.5100 0.0556  -0.0217 -0.0180 1   MET A O   
5    C  CB  . MET A 1   ? 0.3253 0.6051 0.6210 0.0530  -0.0144 -0.0202 1   MET A CB  
6    C  CG  . MET A 1   ? 0.2748 0.5465 0.5653 0.0588  -0.0022 -0.0218 1   MET A CG  
7    S  SD  . MET A 1   ? 0.4684 0.7780 0.7878 0.0620  0.0061  -0.0237 1   MET A SD  
8    C  CE  . MET A 1   ? 0.2915 0.5899 0.5984 0.0606  0.0218  -0.0259 1   MET A CE  
9    N  N   . PHE A 2   ? 0.2207 0.4317 0.4621 0.0378  -0.0095 -0.0204 2   PHE A N   
10   C  CA  . PHE A 2   ? 0.2695 0.4516 0.4881 0.0396  -0.0085 -0.0200 2   PHE A CA  
11   C  C   . PHE A 2   ? 0.2344 0.4087 0.4476 0.0520  -0.0031 -0.0204 2   PHE A C   
12   O  O   . PHE A 2   ? 0.1809 0.3704 0.4063 0.0574  0.0035  -0.0217 2   PHE A O   
13   C  CB  . PHE A 2   ? 0.2358 0.4052 0.4452 0.0281  -0.0031 -0.0202 2   PHE A CB  
14   C  CG  . PHE A 2   ? 0.2231 0.3937 0.4355 0.0161  -0.0085 -0.0211 2   PHE A CG  
15   C  CD1 . PHE A 2   ? 0.2125 0.3771 0.4183 0.0156  -0.0178 -0.0224 2   PHE A CD1 
16   C  CD2 . PHE A 2   ? 0.2279 0.4049 0.4490 0.0051  -0.0042 -0.0208 2   PHE A CD2 
17   C  CE1 . PHE A 2   ? 0.2392 0.4049 0.4474 0.0047  -0.0224 -0.0251 2   PHE A CE1 
18   C  CE2 . PHE A 2   ? 0.2168 0.3928 0.4413 -0.0059 -0.0092 -0.0228 2   PHE A CE2 
19   C  CZ  . PHE A 2   ? 0.1934 0.3637 0.4114 -0.0058 -0.0182 -0.0258 2   PHE A CZ  
20   N  N   . ASP A 3   ? 0.2534 0.4042 0.4485 0.0563  -0.0060 -0.0197 3   ASP A N   
21   C  CA  . ASP A 3   ? 0.2402 0.3784 0.4273 0.0663  -0.0009 -0.0210 3   ASP A CA  
22   C  C   . ASP A 3   ? 0.2513 0.3806 0.4281 0.0611  0.0088  -0.0228 3   ASP A C   
23   O  O   . ASP A 3   ? 0.2377 0.3690 0.4151 0.0673  0.0165  -0.0256 3   ASP A O   
24   C  CB  . ASP A 3   ? 0.2213 0.3372 0.3927 0.0714  -0.0076 -0.0192 3   ASP A CB  
25   C  CG  . ASP A 3   ? 0.2931 0.4167 0.4734 0.0792  -0.0170 -0.0162 3   ASP A CG  
26   O  OD1 . ASP A 3   ? 0.2985 0.4417 0.4972 0.0865  -0.0165 -0.0166 3   ASP A OD1 
27   O  OD2 . ASP A 3   ? 0.3232 0.4346 0.4923 0.0780  -0.0248 -0.0129 3   ASP A OD2 
28   N  N   . LEU A 4   ? 0.2030 0.3227 0.3702 0.0501  0.0083  -0.0214 4   LEU A N   
29   C  CA  . LEU A 4   ? 0.2323 0.3435 0.3891 0.0449  0.0163  -0.0215 4   LEU A CA  
30   C  C   . LEU A 4   ? 0.2097 0.3221 0.3681 0.0321  0.0157  -0.0190 4   LEU A C   
31   O  O   . LEU A 4   ? 0.1919 0.2994 0.3496 0.0277  0.0086  -0.0186 4   LEU A O   
32   C  CB  . LEU A 4   ? 0.2309 0.3178 0.3674 0.0479  0.0159  -0.0222 4   LEU A CB  
33   C  CG  . LEU A 4   ? 0.2447 0.3218 0.3682 0.0422  0.0224  -0.0217 4   LEU A CG  
34   C  CD1 . LEU A 4   ? 0.2462 0.3372 0.3749 0.0444  0.0319  -0.0237 4   LEU A CD1 
35   C  CD2 . LEU A 4   ? 0.2491 0.3038 0.3538 0.0449  0.0207  -0.0228 4   LEU A CD2 
36   N  N   . LEU A 5   ? 0.2189 0.3377 0.3794 0.0261  0.0233  -0.0175 5   LEU A N   
37   C  CA  . LEU A 5   ? 0.2105 0.3288 0.3738 0.0139  0.0230  -0.0143 5   LEU A CA  
38   C  C   . LEU A 5   ? 0.2139 0.3220 0.3648 0.0095  0.0293  -0.0111 5   LEU A C   
39   O  O   . LEU A 5   ? 0.2258 0.3430 0.3763 0.0108  0.0372  -0.0106 5   LEU A O   
40   C  CB  . LEU A 5   ? 0.1908 0.3326 0.3746 0.0083  0.0247  -0.0135 5   LEU A CB  
41   C  CG  . LEU A 5   ? 0.2160 0.3574 0.4053 -0.0052 0.0248  -0.0099 5   LEU A CG  
42   C  CD1 . LEU A 5   ? 0.1920 0.3175 0.3766 -0.0092 0.0165  -0.0114 5   LEU A CD1 
43   C  CD2 . LEU A 5   ? 0.1996 0.3659 0.4101 -0.0107 0.0263  -0.0096 5   LEU A CD2 
44   N  N   . LEU A 6   ? 0.1994 0.2899 0.3403 0.0043  0.0258  -0.0090 6   LEU A N   
45   C  CA  . LEU A 6   ? 0.2210 0.3016 0.3507 -0.0006 0.0299  -0.0046 6   LEU A CA  
46   C  C   . LEU A 6   ? 0.2336 0.3166 0.3727 -0.0116 0.0300  0.0004  6   LEU A C   
47   O  O   . LEU A 6   ? 0.1935 0.2693 0.3373 -0.0156 0.0239  -0.0005 6   LEU A O   
48   C  CB  . LEU A 6   ? 0.2022 0.2621 0.3160 0.0017  0.0256  -0.0052 6   LEU A CB  
49   C  CG  . LEU A 6   ? 0.2640 0.3175 0.3682 0.0113  0.0240  -0.0098 6   LEU A CG  
50   C  CD1 . LEU A 6   ? 0.2620 0.2967 0.3514 0.0111  0.0202  -0.0096 6   LEU A CD1 
51   C  CD2 . LEU A 6   ? 0.2345 0.2952 0.3351 0.0166  0.0312  -0.0116 6   LEU A CD2 
52   N  N   . ARG A 7   ? 0.2225 0.3152 0.3640 -0.0169 0.0369  0.0053  7   ARG A N   
53   C  CA  . ARG A 7   ? 0.2107 0.3058 0.3620 -0.0282 0.0375  0.0113  7   ARG A CA  
54   C  C   . ARG A 7   ? 0.2378 0.3185 0.3767 -0.0331 0.0388  0.0188  7   ARG A C   
55   O  O   . ARG A 7   ? 0.2428 0.3226 0.3678 -0.0299 0.0431  0.0204  7   ARG A O   
56   C  CB  . ARG A 7   ? 0.2233 0.3419 0.3877 -0.0324 0.0444  0.0132  7   ARG A CB  
57   C  CG  . ARG A 7   ? 0.2348 0.3704 0.4153 -0.0288 0.0422  0.0071  7   ARG A CG  
58   C  CD  . ARG A 7   ? 0.2865 0.4461 0.4835 -0.0362 0.0483  0.0101  7   ARG A CD  
59   N  NE  . ARG A 7   ? 0.2956 0.4722 0.5113 -0.0356 0.0444  0.0052  7   ARG A NE  
60   C  CZ  . ARG A 7   ? 0.3089 0.4809 0.5333 -0.0414 0.0366  0.0036  7   ARG A CZ  
61   N  NH1 . ARG A 7   ? 0.2735 0.4239 0.4913 -0.0477 0.0324  0.0058  7   ARG A NH1 
62   N  NH2 . ARG A 7   ? 0.2664 0.4569 0.5072 -0.0408 0.0330  -0.0007 7   ARG A NH2 
63   N  N   . ARG A 8   ? 0.2273 0.2969 0.3717 -0.0407 0.0346  0.0230  8   ARG A N   
64   C  CA  . ARG A 8   ? 0.2351 0.2911 0.3710 -0.0458 0.0347  0.0318  8   ARG A CA  
65   C  C   . ARG A 8   ? 0.2626 0.3050 0.3813 -0.0384 0.0322  0.0303  8   ARG A C   
66   O  O   . ARG A 8   ? 0.2481 0.2870 0.3545 -0.0394 0.0345  0.0366  8   ARG A O   
67   C  CB  . ARG A 8   ? 0.2351 0.3034 0.3697 -0.0526 0.0425  0.0406  8   ARG A CB  
68   C  CG  . ARG A 8   ? 0.2496 0.3268 0.4020 -0.0634 0.0439  0.0450  8   ARG A CG  
69   C  CD  . ARG A 8   ? 0.2808 0.3754 0.4330 -0.0705 0.0528  0.0531  8   ARG A CD  
70   N  NE  . ARG A 8   ? 0.3093 0.4276 0.4653 -0.0657 0.0593  0.0465  8   ARG A NE  
71   C  CZ  . ARG A 8   ? 0.3206 0.4557 0.4946 -0.0676 0.0602  0.0421  8   ARG A CZ  
72   N  NH1 . ARG A 8   ? 0.3120 0.4430 0.5010 -0.0752 0.0551  0.0429  8   ARG A NH1 
73   N  NH2 . ARG A 8   ? 0.2967 0.4538 0.4743 -0.0616 0.0663  0.0364  8   ARG A NH2 
74   N  N   . ALA A 9   ? 0.2401 0.2761 0.3578 -0.0317 0.0271  0.0222  9   ALA A N   
75   C  CA  . ALA A 9   ? 0.2665 0.2888 0.3706 -0.0262 0.0236  0.0205  9   ALA A CA  
76   C  C   . ALA A 9   ? 0.2602 0.2676 0.3667 -0.0302 0.0188  0.0249  9   ALA A C   
77   O  O   . ALA A 9   ? 0.3107 0.3155 0.4304 -0.0354 0.0166  0.0256  9   ALA A O   
78   C  CB  . ALA A 9   ? 0.2536 0.2747 0.3566 -0.0189 0.0198  0.0113  9   ALA A CB  
79   N  N   . ARG A 10  ? 0.2533 0.2510 0.3478 -0.0276 0.0170  0.0276  10  ARG A N   
80   C  CA  . ARG A 10  ? 0.2873 0.2711 0.3849 -0.0293 0.0120  0.0313  10  ARG A CA  
81   C  C   . ARG A 10  ? 0.2787 0.2551 0.3738 -0.0234 0.0073  0.0231  10  ARG A C   
82   O  O   . ARG A 10  ? 0.2368 0.2143 0.3201 -0.0184 0.0075  0.0198  10  ARG A O   
83   C  CB  . ARG A 10  ? 0.3028 0.2827 0.3908 -0.0314 0.0125  0.0417  10  ARG A CB  
84   C  CG  . ARG A 10  ? 0.3691 0.3377 0.4667 -0.0360 0.0088  0.0496  10  ARG A CG  
85   C  CD  . ARG A 10  ? 0.4117 0.3779 0.4997 -0.0384 0.0086  0.0619  10  ARG A CD  
86   N  NE  . ARG A 10  ? 0.4113 0.3876 0.4969 -0.0452 0.0143  0.0699  10  ARG A NE  
87   C  CZ  . ARG A 10  ? 0.4229 0.3990 0.5209 -0.0527 0.0156  0.0760  10  ARG A CZ  
88   N  NH1 . ARG A 10  ? 0.4300 0.3940 0.5435 -0.0543 0.0113  0.0747  10  ARG A NH1 
89   N  NH2 . ARG A 10  ? 0.4092 0.3975 0.5037 -0.0593 0.0218  0.0832  10  ARG A NH2 
90   N  N   . LEU A 11  ? 0.2983 0.2679 0.4047 -0.0243 0.0034  0.0193  11  LEU A N   
91   C  CA  . LEU A 11  ? 0.2968 0.2603 0.4010 -0.0195 -0.0006 0.0122  11  LEU A CA  
92   C  C   . LEU A 11  ? 0.2733 0.2274 0.3740 -0.0181 -0.0032 0.0175  11  LEU A C   
93   O  O   . LEU A 11  ? 0.3046 0.2551 0.4070 -0.0212 -0.0029 0.0269  11  LEU A O   
94   C  CB  . LEU A 11  ? 0.2959 0.2572 0.4126 -0.0209 -0.0034 0.0044  11  LEU A CB  
95   C  CG  . LEU A 11  ? 0.2988 0.2706 0.4207 -0.0225 -0.0026 -0.0017 11  LEU A CG  
96   C  CD1 . LEU A 11  ? 0.3296 0.2981 0.4627 -0.0249 -0.0060 -0.0097 11  LEU A CD1 
97   C  CD2 . LEU A 11  ? 0.2540 0.2336 0.3650 -0.0172 -0.0020 -0.0058 11  LEU A CD2 
98   N  N   . VAL A 12  ? 0.3016 0.2527 0.3983 -0.0135 -0.0059 0.0121  12  VAL A N   
99   C  CA  . VAL A 12  ? 0.2805 0.2256 0.3748 -0.0115 -0.0087 0.0169  12  VAL A CA  
100  C  C   . VAL A 12  ? 0.3544 0.2900 0.4629 -0.0124 -0.0116 0.0200  12  VAL A C   
101  O  O   . VAL A 12  ? 0.3903 0.3211 0.4991 -0.0106 -0.0144 0.0262  12  VAL A O   
102  C  CB  . VAL A 12  ? 0.3294 0.2757 0.4170 -0.0070 -0.0106 0.0100  12  VAL A CB  
103  C  CG1 . VAL A 12  ? 0.2773 0.2292 0.3491 -0.0061 -0.0085 0.0104  12  VAL A CG1 
104  C  CG2 . VAL A 12  ? 0.3630 0.3104 0.4571 -0.0060 -0.0111 -0.0006 12  VAL A CG2 
105  N  N   . ASP A 13  ? 0.3376 0.2699 0.4586 -0.0152 -0.0115 0.0158  13  ASP A N   
106  C  CA  . ASP A 13  ? 0.3661 0.2870 0.5014 -0.0169 -0.0140 0.0196  13  ASP A CA  
107  C  C   . ASP A 13  ? 0.3435 0.2623 0.4807 -0.0232 -0.0125 0.0318  13  ASP A C   
108  O  O   . ASP A 13  ? 0.3759 0.2839 0.5257 -0.0261 -0.0144 0.0364  13  ASP A O   
109  C  CB  . ASP A 13  ? 0.3673 0.2843 0.5154 -0.0177 -0.0149 0.0080  13  ASP A CB  
110  C  CG  . ASP A 13  ? 0.3980 0.3221 0.5480 -0.0232 -0.0124 0.0043  13  ASP A CG  
111  O  OD1 . ASP A 13  ? 0.3388 0.2708 0.4823 -0.0262 -0.0094 0.0109  13  ASP A OD1 
112  O  OD2 . ASP A 13  ? 0.3900 0.3131 0.5485 -0.0246 -0.0134 -0.0060 13  ASP A OD2 
113  N  N   . ASP A 14  ? 0.3721 0.3013 0.4972 -0.0254 -0.0087 0.0368  14  ASP A N   
114  C  CA  . ASP A 14  ? 0.3906 0.3227 0.5136 -0.0317 -0.0058 0.0485  14  ASP A CA  
115  C  C   . ASP A 14  ? 0.3301 0.2649 0.4642 -0.0386 -0.0032 0.0475  14  ASP A C   
116  O  O   . ASP A 14  ? 0.3441 0.2809 0.4790 -0.0452 -0.0006 0.0578  14  ASP A O   
117  C  CB  . ASP A 14  ? 0.3917 0.3140 0.5164 -0.0331 -0.0091 0.0618  14  ASP A CB  
118  C  CG  . ASP A 14  ? 0.4863 0.4143 0.5944 -0.0305 -0.0094 0.0686  14  ASP A CG  
119  O  OD1 . ASP A 14  ? 0.4439 0.3761 0.5437 -0.0249 -0.0101 0.0610  14  ASP A OD1 
120  O  OD2 . ASP A 14  ? 0.6117 0.5404 0.7145 -0.0350 -0.0090 0.0816  14  ASP A OD2 
121  N  N   . THR A 15  ? 0.3076 0.2441 0.4495 -0.0381 -0.0036 0.0357  15  THR A N   
122  C  CA  . THR A 15  ? 0.3221 0.2640 0.4745 -0.0452 -0.0014 0.0343  15  THR A CA  
123  C  C   . THR A 15  ? 0.2903 0.2503 0.4351 -0.0454 0.0036  0.0331  15  THR A C   
124  O  O   . THR A 15  ? 0.2843 0.2506 0.4173 -0.0390 0.0045  0.0288  15  THR A O   
125  C  CB  . THR A 15  ? 0.3072 0.2443 0.4716 -0.0453 -0.0046 0.0220  15  THR A CB  
126  O  OG1 . THR A 15  ? 0.3196 0.2650 0.4766 -0.0392 -0.0050 0.0113  15  THR A OG1 
127  C  CG2 . THR A 15  ? 0.3195 0.2381 0.4925 -0.0438 -0.0090 0.0218  15  THR A CG2 
128  N  N   . LEU A 16  ? 0.2623 0.2306 0.4147 -0.0529 0.0070  0.0371  16  LEU A N   
129  C  CA  . LEU A 16  ? 0.2852 0.2724 0.4340 -0.0529 0.0121  0.0356  16  LEU A CA  
130  C  C   . LEU A 16  ? 0.2914 0.2869 0.4492 -0.0521 0.0104  0.0242  16  LEU A C   
131  O  O   . LEU A 16  ? 0.3224 0.3129 0.4931 -0.0571 0.0073  0.0204  16  LEU A O   
132  C  CB  . LEU A 16  ? 0.2787 0.2744 0.4320 -0.0619 0.0172  0.0459  16  LEU A CB  
133  C  CG  . LEU A 16  ? 0.3422 0.3395 0.4820 -0.0626 0.0211  0.0571  16  LEU A CG  
134  C  CD1 . LEU A 16  ? 0.3469 0.3548 0.4922 -0.0728 0.0266  0.0669  16  LEU A CD1 
135  C  CD2 . LEU A 16  ? 0.3208 0.3277 0.4451 -0.0543 0.0241  0.0522  16  LEU A CD2 
136  N  N   . THR A 17  ? 0.2366 0.2444 0.3877 -0.0459 0.0122  0.0188  17  THR A N   
137  C  CA  . THR A 17  ? 0.2453 0.2626 0.4043 -0.0448 0.0098  0.0093  17  THR A CA  
138  C  C   . THR A 17  ? 0.2831 0.3169 0.4374 -0.0391 0.0133  0.0075  17  THR A C   
139  O  O   . THR A 17  ? 0.2290 0.2647 0.3725 -0.0353 0.0176  0.0115  17  THR A O   
140  C  CB  . THR A 17  ? 0.2898 0.2966 0.4460 -0.0403 0.0039  0.0009  17  THR A CB  
141  O  OG1 . THR A 17  ? 0.3535 0.3682 0.5199 -0.0428 0.0006  -0.0072 17  THR A OG1 
142  C  CG2 . THR A 17  ? 0.2815 0.2881 0.4227 -0.0312 0.0038  -0.0016 17  THR A CG2 
143  N  N   . ASP A 18  ? 0.2602 0.3063 0.4235 -0.0385 0.0112  0.0011  18  ASP A N   
144  C  CA  . ASP A 18  ? 0.2594 0.3211 0.4216 -0.0318 0.0132  -0.0016 18  ASP A CA  
145  C  C   . ASP A 18  ? 0.2507 0.3085 0.4065 -0.0246 0.0075  -0.0085 18  ASP A C   
146  O  O   . ASP A 18  ? 0.2346 0.2858 0.3926 -0.0270 0.0021  -0.0131 18  ASP A O   
147  C  CB  . ASP A 18  ? 0.2708 0.3527 0.4498 -0.0366 0.0145  -0.0024 18  ASP A CB  
148  C  CG  . ASP A 18  ? 0.3001 0.3877 0.4870 -0.0458 0.0202  0.0050  18  ASP A CG  
149  O  OD1 . ASP A 18  ? 0.2523 0.3322 0.4297 -0.0467 0.0245  0.0117  18  ASP A OD1 
150  O  OD2 . ASP A 18  ? 0.3044 0.4049 0.5072 -0.0532 0.0200  0.0046  18  ASP A OD2 
151  N  N   . ILE A 19  ? 0.2091 0.2710 0.3568 -0.0160 0.0090  -0.0095 19  ILE A N   
152  C  CA  . ILE A 19  ? 0.1802 0.2381 0.3205 -0.0090 0.0039  -0.0142 19  ILE A CA  
153  C  C   . ILE A 19  ? 0.2019 0.2750 0.3472 -0.0024 0.0042  -0.0156 19  ILE A C   
154  O  O   . ILE A 19  ? 0.2072 0.2840 0.3495 0.0027  0.0094  -0.0139 19  ILE A O   
155  C  CB  . ILE A 19  ? 0.2389 0.2809 0.3621 -0.0044 0.0044  -0.0133 19  ILE A CB  
156  C  CG1 . ILE A 19  ? 0.2203 0.2490 0.3403 -0.0099 0.0042  -0.0110 19  ILE A CG1 
157  C  CG2 . ILE A 19  ? 0.2094 0.2473 0.3254 0.0010  -0.0010 -0.0173 19  ILE A CG2 
158  C  CD1 . ILE A 19  ? 0.2702 0.2863 0.3751 -0.0063 0.0049  -0.0093 19  ILE A CD1 
159  N  N   . ALA A 20  ? 0.1957 0.2777 0.3486 -0.0021 -0.0017 -0.0190 20  ALA A N   
160  C  CA  . ALA A 20  ? 0.1864 0.2836 0.3462 0.0049  -0.0031 -0.0198 20  ALA A CA  
161  C  C   . ALA A 20  ? 0.1926 0.2816 0.3413 0.0122  -0.0087 -0.0210 20  ALA A C   
162  O  O   . ALA A 20  ? 0.1902 0.2714 0.3324 0.0092  -0.0140 -0.0230 20  ALA A O   
163  C  CB  . ALA A 20  ? 0.1974 0.3135 0.3746 -0.0004 -0.0067 -0.0215 20  ALA A CB  
164  N  N   . ILE A 21  ? 0.1841 0.2756 0.3315 0.0217  -0.0073 -0.0199 21  ILE A N   
165  C  CA  . ILE A 21  ? 0.2075 0.2896 0.3444 0.0294  -0.0119 -0.0195 21  ILE A CA  
166  C  C   . ILE A 21  ? 0.2352 0.3330 0.3840 0.0369  -0.0155 -0.0188 21  ILE A C   
167  O  O   . ILE A 21  ? 0.1984 0.3090 0.3589 0.0413  -0.0108 -0.0189 21  ILE A O   
168  C  CB  . ILE A 21  ? 0.2181 0.2840 0.3415 0.0343  -0.0069 -0.0189 21  ILE A CB  
169  C  CG1 . ILE A 21  ? 0.2268 0.2777 0.3381 0.0274  -0.0052 -0.0188 21  ILE A CG1 
170  C  CG2 . ILE A 21  ? 0.2619 0.3189 0.3775 0.0428  -0.0112 -0.0179 21  ILE A CG2 
171  C  CD1 . ILE A 21  ? 0.2630 0.3068 0.3673 0.0280  0.0022  -0.0182 21  ILE A CD1 
172  N  N   . GLN A 22  ? 0.2279 0.3257 0.3736 0.0386  -0.0239 -0.0178 22  GLN A N   
173  C  CA  . GLN A 22  ? 0.2567 0.3690 0.4133 0.0460  -0.0295 -0.0158 22  GLN A CA  
174  C  C   . GLN A 22  ? 0.2724 0.3716 0.4157 0.0512  -0.0362 -0.0124 22  GLN A C   
175  O  O   . GLN A 22  ? 0.2371 0.3282 0.3684 0.0450  -0.0403 -0.0124 22  GLN A O   
176  C  CB  . GLN A 22  ? 0.2810 0.4145 0.4513 0.0395  -0.0348 -0.0170 22  GLN A CB  
177  C  CG  . GLN A 22  ? 0.3460 0.4969 0.5280 0.0471  -0.0423 -0.0141 22  GLN A CG  
178  C  CD  . GLN A 22  ? 0.3411 0.5181 0.5460 0.0466  -0.0406 -0.0154 22  GLN A CD  
179  O  OE1 . GLN A 22  ? 0.3781 0.5591 0.5895 0.0415  -0.0326 -0.0179 22  GLN A OE1 
180  N  NE2 . GLN A 22  ? 0.3650 0.5609 0.5824 0.0518  -0.0483 -0.0131 22  GLN A NE2 
181  N  N   . ASP A 23  ? 0.2906 0.3872 0.4362 0.0624  -0.0369 -0.0096 23  ASP A N   
182  C  CA  . ASP A 23  ? 0.3208 0.4062 0.4565 0.0679  -0.0442 -0.0046 23  ASP A CA  
183  C  C   . ASP A 23  ? 0.2933 0.3556 0.4080 0.0629  -0.0432 -0.0043 23  ASP A C   
184  O  O   . ASP A 23  ? 0.2617 0.3192 0.3656 0.0591  -0.0495 -0.0013 23  ASP A O   
185  C  CB  . ASP A 23  ? 0.2930 0.3942 0.4337 0.0660  -0.0545 -0.0012 23  ASP A CB  
186  C  CG  . ASP A 23  ? 0.3604 0.4852 0.5228 0.0727  -0.0572 -0.0003 23  ASP A CG  
187  O  OD1 . ASP A 23  ? 0.3692 0.4942 0.5411 0.0834  -0.0536 0.0002  23  ASP A OD1 
188  O  OD2 . ASP A 23  ? 0.3973 0.5415 0.5679 0.0671  -0.0629 -0.0006 23  ASP A OD2 
189  N  N   . GLY A 24  ? 0.2843 0.3342 0.3932 0.0622  -0.0350 -0.0075 24  GLY A N   
190  C  CA  . GLY A 24  ? 0.2984 0.3280 0.3892 0.0578  -0.0336 -0.0075 24  GLY A CA  
191  C  C   . GLY A 24  ? 0.3002 0.3301 0.3839 0.0469  -0.0346 -0.0093 24  GLY A C   
192  O  O   . GLY A 24  ? 0.3088 0.3244 0.3783 0.0433  -0.0344 -0.0089 24  GLY A O   
193  N  N   . LYS A 25  ? 0.2696 0.3155 0.3635 0.0416  -0.0355 -0.0118 25  LYS A N   
194  C  CA  . LYS A 25  ? 0.2295 0.2759 0.3187 0.0320  -0.0365 -0.0150 25  LYS A CA  
195  C  C   . LYS A 25  ? 0.2242 0.2766 0.3234 0.0269  -0.0309 -0.0188 25  LYS A C   
196  O  O   . LYS A 25  ? 0.2226 0.2854 0.3344 0.0294  -0.0280 -0.0187 25  LYS A O   
197  C  CB  . LYS A 25  ? 0.2475 0.3070 0.3388 0.0290  -0.0445 -0.0148 25  LYS A CB  
198  C  CG  . LYS A 25  ? 0.3097 0.3653 0.3914 0.0333  -0.0511 -0.0091 25  LYS A CG  
199  C  CD  . LYS A 25  ? 0.3798 0.4395 0.4518 0.0263  -0.0567 -0.0099 25  LYS A CD  
200  C  CE  . LYS A 25  ? 0.4623 0.5073 0.5172 0.0270  -0.0583 -0.0050 25  LYS A CE  
201  N  NZ  . LYS A 25  ? 0.4862 0.5279 0.5411 0.0356  -0.0631 0.0033  25  LYS A NZ  
202  N  N   . ILE A 26  ? 0.2080 0.2542 0.3024 0.0196  -0.0295 -0.0219 26  ILE A N   
203  C  CA  . ILE A 26  ? 0.2317 0.2827 0.3363 0.0138  -0.0256 -0.0247 26  ILE A CA  
204  C  C   . ILE A 26  ? 0.2163 0.2843 0.3335 0.0098  -0.0301 -0.0273 26  ILE A C   
205  O  O   . ILE A 26  ? 0.2341 0.3054 0.3477 0.0066  -0.0357 -0.0300 26  ILE A O   
206  C  CB  . ILE A 26  ? 0.2003 0.2392 0.2981 0.0082  -0.0234 -0.0271 26  ILE A CB  
207  C  CG1 . ILE A 26  ? 0.2143 0.2387 0.3002 0.0117  -0.0196 -0.0243 26  ILE A CG1 
208  C  CG2 . ILE A 26  ? 0.2066 0.2486 0.3158 0.0021  -0.0202 -0.0287 26  ILE A CG2 
209  C  CD1 . ILE A 26  ? 0.2967 0.3103 0.3748 0.0078  -0.0190 -0.0261 26  ILE A CD1 
210  N  N   . ALA A 27  ? 0.1869 0.2673 0.3186 0.0096  -0.0276 -0.0267 27  ALA A N   
211  C  CA  . ALA A 27  ? 0.1905 0.2890 0.3358 0.0053  -0.0320 -0.0291 27  ALA A CA  
212  C  C   . ALA A 27  ? 0.2360 0.3341 0.3880 -0.0051 -0.0308 -0.0336 27  ALA A C   
213  O  O   . ALA A 27  ? 0.2134 0.3191 0.3693 -0.0109 -0.0362 -0.0384 27  ALA A O   
214  C  CB  . ALA A 27  ? 0.1922 0.3071 0.3520 0.0100  -0.0302 -0.0263 27  ALA A CB  
215  N  N   . ALA A 28  ? 0.2108 0.2996 0.3638 -0.0076 -0.0242 -0.0321 28  ALA A N   
216  C  CA  . ALA A 28  ? 0.2051 0.2917 0.3663 -0.0173 -0.0232 -0.0352 28  ALA A CA  
217  C  C   . ALA A 28  ? 0.2338 0.3053 0.3909 -0.0184 -0.0169 -0.0316 28  ALA A C   
218  O  O   . ALA A 28  ? 0.2001 0.2685 0.3515 -0.0130 -0.0123 -0.0268 28  ALA A O   
219  C  CB  . ALA A 28  ? 0.2057 0.3109 0.3851 -0.0226 -0.0236 -0.0355 28  ALA A CB  
220  N  N   . LEU A 29  ? 0.2511 0.3129 0.4111 -0.0255 -0.0170 -0.0344 29  LEU A N   
221  C  CA  . LEU A 29  ? 0.2484 0.2971 0.4075 -0.0279 -0.0121 -0.0299 29  LEU A CA  
222  C  C   . LEU A 29  ? 0.2499 0.2981 0.4231 -0.0377 -0.0120 -0.0308 29  LEU A C   
223  O  O   . LEU A 29  ? 0.2675 0.3174 0.4470 -0.0427 -0.0164 -0.0379 29  LEU A O   
224  C  CB  . LEU A 29  ? 0.2762 0.3078 0.4230 -0.0251 -0.0127 -0.0312 29  LEU A CB  
225  C  CG  . LEU A 29  ? 0.3019 0.3302 0.4339 -0.0169 -0.0120 -0.0290 29  LEU A CG  
226  C  CD1 . LEU A 29  ? 0.3378 0.3682 0.4633 -0.0145 -0.0171 -0.0347 29  LEU A CD1 
227  C  CD2 . LEU A 29  ? 0.3139 0.3274 0.4377 -0.0157 -0.0094 -0.0256 29  LEU A CD2 
228  N  N   . GLY A 30  ? 0.2652 0.3108 0.4426 -0.0410 -0.0070 -0.0236 30  GLY A N   
229  C  CA  . GLY A 30  ? 0.2567 0.2994 0.4474 -0.0511 -0.0065 -0.0225 30  GLY A CA  
230  C  C   . GLY A 30  ? 0.3311 0.3871 0.5308 -0.0556 -0.0014 -0.0153 30  GLY A C   
231  O  O   . GLY A 30  ? 0.2816 0.3424 0.4743 -0.0508 0.0035  -0.0093 30  GLY A O   
232  N  N   . GLU A 31  ? 0.3129 0.3756 0.5280 -0.0656 -0.0023 -0.0163 31  GLU A N   
233  C  CA  . GLU A 31  ? 0.3502 0.4298 0.5762 -0.0714 0.0025  -0.0101 31  GLU A CA  
234  C  C   . GLU A 31  ? 0.3131 0.4168 0.5457 -0.0678 0.0009  -0.0147 31  GLU A C   
235  O  O   . GLU A 31  ? 0.2775 0.3874 0.5174 -0.0708 -0.0052 -0.0222 31  GLU A O   
236  C  CB  . GLU A 31  ? 0.4117 0.4866 0.6523 -0.0849 0.0021  -0.0083 31  GLU A CB  
237  C  CG  . GLU A 31  ? 0.4424 0.5018 0.6805 -0.0897 0.0065  0.0023  31  GLU A CG  
238  C  CD  . GLU A 31  ? 0.4695 0.5332 0.6948 -0.0829 0.0128  0.0106  31  GLU A CD  
239  O  OE1 . GLU A 31  ? 0.5095 0.5946 0.7380 -0.0822 0.0177  0.0128  31  GLU A OE1 
240  O  OE2 . GLU A 31  ? 0.4744 0.5211 0.6869 -0.0781 0.0129  0.0142  31  GLU A OE2 
241  N  N   . ILE A 32  ? 0.3020 0.4196 0.5320 -0.0611 0.0060  -0.0107 32  ILE A N   
242  C  CA  . ILE A 32  ? 0.2824 0.4210 0.5173 -0.0541 0.0042  -0.0145 32  ILE A CA  
243  C  C   . ILE A 32  ? 0.2923 0.4546 0.5407 -0.0567 0.0105  -0.0103 32  ILE A C   
244  O  O   . ILE A 32  ? 0.2705 0.4329 0.5143 -0.0559 0.0183  -0.0042 32  ILE A O   
245  C  CB  . ILE A 32  ? 0.2503 0.3821 0.4691 -0.0407 0.0037  -0.0156 32  ILE A CB  
246  C  CG1 . ILE A 32  ? 0.2459 0.3571 0.4523 -0.0392 -0.0022 -0.0199 32  ILE A CG1 
247  C  CG2 . ILE A 32  ? 0.2716 0.4238 0.4968 -0.0327 0.0014  -0.0183 32  ILE A CG2 
248  C  CD1 . ILE A 32  ? 0.2198 0.3212 0.4094 -0.0281 -0.0024 -0.0199 32  ILE A CD1 
249  N  N   . SER A 33  ? 0.2563 0.4404 0.5213 -0.0599 0.0072  -0.0137 33  SER A N   
250  C  CA  . SER A 33  ? 0.2783 0.4896 0.5591 -0.0619 0.0128  -0.0108 33  SER A CA  
251  C  C   . SER A 33  ? 0.2434 0.4764 0.5307 -0.0503 0.0107  -0.0142 33  SER A C   
252  O  O   . SER A 33  ? 0.2425 0.4986 0.5418 -0.0484 0.0167  -0.0122 33  SER A O   
253  C  CB  . SER A 33  ? 0.2860 0.5089 0.5857 -0.0774 0.0113  -0.0107 33  SER A CB  
254  O  OG  . SER A 33  ? 0.2713 0.5000 0.5782 -0.0794 0.0016  -0.0181 33  SER A OG  
255  N  N   . ALA A 34  ? 0.2720 0.4988 0.5521 -0.0425 0.0024  -0.0188 34  ALA A N   
256  C  CA  . ALA A 34  ? 0.2668 0.5121 0.5532 -0.0310 -0.0010 -0.0208 34  ALA A CA  
257  C  C   . ALA A 34  ? 0.2259 0.4732 0.5072 -0.0191 0.0072  -0.0182 34  ALA A C   
258  O  O   . ALA A 34  ? 0.2449 0.4741 0.5116 -0.0183 0.0133  -0.0158 34  ALA A O   
259  C  CB  . ALA A 34  ? 0.2409 0.4743 0.5157 -0.0253 -0.0109 -0.0245 34  ALA A CB  
260  N  N   . PRO A 35  ? 0.2464 0.5162 0.5404 -0.0095 0.0072  -0.0191 35  PRO A N   
261  C  CA  . PRO A 35  ? 0.2172 0.4900 0.5083 0.0021  0.0156  -0.0184 35  PRO A CA  
262  C  C   . PRO A 35  ? 0.2321 0.4812 0.5035 0.0141  0.0131  -0.0194 35  PRO A C   
263  O  O   . PRO A 35  ? 0.2277 0.4641 0.4907 0.0160  0.0040  -0.0202 35  PRO A O   
264  C  CB  . PRO A 35  ? 0.2138 0.5194 0.5283 0.0088  0.0150  -0.0198 35  PRO A CB  
265  C  CG  . PRO A 35  ? 0.2262 0.5464 0.5550 -0.0007 0.0056  -0.0205 35  PRO A CG  
266  C  CD  . PRO A 35  ? 0.2230 0.5162 0.5343 -0.0078 -0.0012 -0.0212 35  PRO A CD  
267  N  N   . SER A 36  ? 0.2280 0.4720 0.4916 0.0216  0.0217  -0.0195 36  SER A N   
268  C  CA  . SER A 36  ? 0.2271 0.4486 0.4724 0.0324  0.0206  -0.0207 36  SER A CA  
269  C  C   . SER A 36  ? 0.2323 0.4638 0.4825 0.0450  0.0279  -0.0235 36  SER A C   
270  O  O   . SER A 36  ? 0.2103 0.4604 0.4706 0.0431  0.0371  -0.0241 36  SER A O   
271  C  CB  . SER A 36  ? 0.2280 0.4236 0.4519 0.0264  0.0237  -0.0192 36  SER A CB  
272  O  OG  . SER A 36  ? 0.2260 0.4032 0.4337 0.0363  0.0248  -0.0208 36  SER A OG  
273  N  N   . ARG A 37  ? 0.2321 0.4506 0.4749 0.0576  0.0240  -0.0252 37  ARG A N   
274  C  CA  . ARG A 37  ? 0.2239 0.4472 0.4701 0.0708  0.0308  -0.0292 37  ARG A CA  
275  C  C   . ARG A 37  ? 0.2222 0.4324 0.4517 0.0690  0.0410  -0.0314 37  ARG A C   
276  O  O   . ARG A 37  ? 0.2168 0.4367 0.4504 0.0764  0.0499  -0.0360 37  ARG A O   
277  C  CB  . ARG A 37  ? 0.2643 0.4741 0.5072 0.0843  0.0230  -0.0298 37  ARG A CB  
278  N  N   . LYS A 38  ? 0.2020 0.3917 0.4130 0.0593  0.0399  -0.0286 38  LYS A N   
279  C  CA  . LYS A 38  ? 0.2461 0.4229 0.4395 0.0565  0.0480  -0.0296 38  LYS A CA  
280  C  C   . LYS A 38  ? 0.2153 0.3830 0.3996 0.0420  0.0467  -0.0242 38  LYS A C   
281  O  O   . LYS A 38  ? 0.2169 0.3713 0.3967 0.0382  0.0381  -0.0219 38  LYS A O   
282  C  CB  . LYS A 38  ? 0.2244 0.3763 0.4003 0.0654  0.0458  -0.0329 38  LYS A CB  
283  C  CG  . LYS A 38  ? 0.3186 0.4548 0.4736 0.0607  0.0517  -0.0336 38  LYS A CG  
284  C  CD  . LYS A 38  ? 0.3718 0.5188 0.5267 0.0663  0.0629  -0.0396 38  LYS A CD  
285  C  CE  . LYS A 38  ? 0.4856 0.6120 0.6172 0.0663  0.0661  -0.0427 38  LYS A CE  
286  N  NZ  . LYS A 38  ? 0.4861 0.6205 0.6087 0.0566  0.0747  -0.0409 38  LYS A NZ  
287  N  N   . THR A 39  ? 0.1963 0.3717 0.3783 0.0342  0.0552  -0.0221 39  THR A N   
288  C  CA  . THR A 39  ? 0.2175 0.3836 0.3922 0.0209  0.0541  -0.0160 39  THR A CA  
289  C  C   . THR A 39  ? 0.2513 0.4068 0.4072 0.0184  0.0607  -0.0146 39  THR A C   
290  O  O   . THR A 39  ? 0.2669 0.4345 0.4215 0.0213  0.0698  -0.0172 39  THR A O   
291  C  CB  . THR A 39  ? 0.2315 0.4186 0.4241 0.0105  0.0563  -0.0119 39  THR A CB  
292  O  OG1 . THR A 39  ? 0.1860 0.3847 0.3960 0.0127  0.0494  -0.0139 39  THR A OG1 
293  C  CG2 . THR A 39  ? 0.1964 0.3706 0.3826 -0.0027 0.0543  -0.0053 39  THR A CG2 
294  N  N   . ILE A 40  ? 0.2076 0.3418 0.3490 0.0131  0.0561  -0.0109 40  ILE A N   
295  C  CA  . ILE A 40  ? 0.2730 0.3968 0.3960 0.0095  0.0605  -0.0083 40  ILE A CA  
296  C  C   . ILE A 40  ? 0.2520 0.3710 0.3745 -0.0030 0.0588  0.0004  40  ILE A C   
297  O  O   . ILE A 40  ? 0.2337 0.3419 0.3601 -0.0062 0.0511  0.0022  40  ILE A O   
298  C  CB  . ILE A 40  ? 0.2660 0.3675 0.3715 0.0158  0.0561  -0.0118 40  ILE A CB  
299  C  CG1 . ILE A 40  ? 0.3097 0.4130 0.4160 0.0281  0.0575  -0.0200 40  ILE A CG1 
300  C  CG2 . ILE A 40  ? 0.3406 0.4335 0.4276 0.0110  0.0596  -0.0087 40  ILE A CG2 
301  C  CD1 . ILE A 40  ? 0.3085 0.3894 0.3997 0.0335  0.0523  -0.0232 40  ILE A CD1 
302  N  N   . ASP A 41  ? 0.2862 0.4132 0.4041 -0.0099 0.0660  0.0057  41  ASP A N   
303  C  CA  . ASP A 41  ? 0.2384 0.3598 0.3553 -0.0218 0.0647  0.0155  41  ASP A CA  
304  C  C   . ASP A 41  ? 0.2782 0.3820 0.3743 -0.0224 0.0632  0.0190  41  ASP A C   
305  O  O   . ASP A 41  ? 0.2249 0.3339 0.3080 -0.0222 0.0695  0.0193  41  ASP A O   
306  C  CB  . ASP A 41  ? 0.2577 0.4002 0.3827 -0.0303 0.0732  0.0212  41  ASP A CB  
307  C  CG  . ASP A 41  ? 0.2777 0.4140 0.4062 -0.0432 0.0710  0.0323  41  ASP A CG  
308  O  OD1 . ASP A 41  ? 0.2481 0.3631 0.3704 -0.0445 0.0636  0.0355  41  ASP A OD1 
309  O  OD2 . ASP A 41  ? 0.3174 0.4701 0.4556 -0.0521 0.0767  0.0380  41  ASP A OD2 
310  N  N   . LEU A 42  ? 0.2476 0.3321 0.3407 -0.0231 0.0548  0.0208  42  LEU A N   
311  C  CA  . LEU A 42  ? 0.2722 0.3413 0.3477 -0.0235 0.0522  0.0242  42  LEU A CA  
312  C  C   . LEU A 42  ? 0.2804 0.3486 0.3520 -0.0334 0.0536  0.0360  42  LEU A C   
313  O  O   . LEU A 42  ? 0.2403 0.2989 0.2970 -0.0342 0.0517  0.0402  42  LEU A O   
314  C  CB  . LEU A 42  ? 0.2395 0.2904 0.3143 -0.0197 0.0432  0.0213  42  LEU A CB  
315  C  CG  . LEU A 42  ? 0.2915 0.3420 0.3661 -0.0101 0.0418  0.0112  42  LEU A CG  
316  C  CD1 . LEU A 42  ? 0.2583 0.2939 0.3326 -0.0073 0.0335  0.0083  42  LEU A CD1 
317  C  CD2 . LEU A 42  ? 0.3057 0.3565 0.3647 -0.0049 0.0463  0.0072  42  LEU A CD2 
318  N  N   . GLN A 43  ? 0.2661 0.3442 0.3509 -0.0414 0.0563  0.0421  43  GLN A N   
319  C  CA  . GLN A 43  ? 0.2641 0.3434 0.3461 -0.0519 0.0586  0.0549  43  GLN A CA  
320  C  C   . GLN A 43  ? 0.2597 0.3184 0.3355 -0.0540 0.0509  0.0624  43  GLN A C   
321  O  O   . GLN A 43  ? 0.2556 0.3122 0.3201 -0.0591 0.0516  0.0725  43  GLN A O   
322  C  CB  . GLN A 43  ? 0.3157 0.4103 0.3836 -0.0536 0.0676  0.0571  43  GLN A CB  
323  C  CG  . GLN A 43  ? 0.3071 0.4235 0.3820 -0.0498 0.0759  0.0485  43  GLN A CG  
324  C  CD  . GLN A 43  ? 0.3319 0.4632 0.3915 -0.0502 0.0853  0.0480  43  GLN A CD  
325  O  OE1 . GLN A 43  ? 0.3424 0.4907 0.4039 -0.0585 0.0927  0.0547  43  GLN A OE1 
326  N  NE2 . GLN A 43  ? 0.3944 0.5198 0.4383 -0.0420 0.0853  0.0399  43  GLN A NE2 
327  N  N   . GLY A 44  ? 0.2371 0.2814 0.3206 -0.0502 0.0434  0.0577  44  GLY A N   
328  C  CA  . GLY A 44  ? 0.2358 0.2614 0.3170 -0.0509 0.0360  0.0633  44  GLY A CA  
329  C  C   . GLY A 44  ? 0.3200 0.3399 0.3826 -0.0471 0.0342  0.0652  44  GLY A C   
330  O  O   . GLY A 44  ? 0.3144 0.3214 0.3751 -0.0481 0.0284  0.0719  44  GLY A O   
331  N  N   . ASN A 45  ? 0.2912 0.3203 0.3407 -0.0426 0.0388  0.0590  45  ASN A N   
332  C  CA  . ASN A 45  ? 0.3181 0.3441 0.3485 -0.0408 0.0378  0.0608  45  ASN A CA  
333  C  C   . ASN A 45  ? 0.3397 0.3584 0.3638 -0.0322 0.0344  0.0497  45  ASN A C   
334  O  O   . ASN A 45  ? 0.3592 0.3773 0.3672 -0.0304 0.0343  0.0480  45  ASN A O   
335  C  CB  . ASN A 45  ? 0.3062 0.3481 0.3238 -0.0442 0.0461  0.0630  45  ASN A CB  
336  C  CG  . ASN A 45  ? 0.3651 0.4051 0.3626 -0.0458 0.0444  0.0683  45  ASN A CG  
337  O  OD1 . ASN A 45  ? 0.3503 0.3817 0.3464 -0.0496 0.0384  0.0791  45  ASN A OD1 
338  N  ND2 . ASN A 45  ? 0.3849 0.4334 0.3670 -0.0432 0.0496  0.0608  45  ASN A ND2 
339  N  N   . SER A 46  ? 0.2824 0.2957 0.3182 -0.0277 0.0312  0.0422  46  SER A N   
340  C  CA  . SER A 46  ? 0.3119 0.3172 0.3423 -0.0208 0.0274  0.0334  46  SER A CA  
341  C  C   . SER A 46  ? 0.3064 0.3031 0.3500 -0.0190 0.0216  0.0304  46  SER A C   
342  O  O   . SER A 46  ? 0.3055 0.3060 0.3629 -0.0205 0.0223  0.0293  46  SER A O   
343  C  CB  . SER A 46  ? 0.3605 0.3727 0.3863 -0.0152 0.0321  0.0237  46  SER A CB  
344  O  OG  . SER A 46  ? 0.4023 0.4227 0.4149 -0.0164 0.0381  0.0243  46  SER A OG  
345  N  N   . TYR A 47  ? 0.2977 0.2842 0.3371 -0.0163 0.0161  0.0287  47  TYR A N   
346  C  CA  . TYR A 47  ? 0.2697 0.2497 0.3190 -0.0138 0.0115  0.0235  47  TYR A CA  
347  C  C   . TYR A 47  ? 0.3001 0.2830 0.3484 -0.0089 0.0124  0.0143  47  TYR A C   
348  O  O   . TYR A 47  ? 0.3096 0.2944 0.3471 -0.0058 0.0149  0.0111  47  TYR A O   
349  C  CB  . TYR A 47  ? 0.2966 0.2674 0.3423 -0.0124 0.0060  0.0241  47  TYR A CB  
350  C  CG  . TYR A 47  ? 0.3345 0.3009 0.3836 -0.0159 0.0033  0.0336  47  TYR A CG  
351  C  CD1 . TYR A 47  ? 0.3163 0.2779 0.3804 -0.0181 0.0013  0.0364  47  TYR A CD1 
352  C  CD2 . TYR A 47  ? 0.3234 0.2896 0.3607 -0.0167 0.0020  0.0397  47  TYR A CD2 
353  C  CE1 . TYR A 47  ? 0.3502 0.3056 0.4185 -0.0205 -0.0018 0.0458  47  TYR A CE1 
354  C  CE2 . TYR A 47  ? 0.3497 0.3120 0.3906 -0.0192 -0.0015 0.0497  47  TYR A CE2 
355  C  CZ  . TYR A 47  ? 0.3906 0.3467 0.4475 -0.0207 -0.0034 0.0531  47  TYR A CZ  
356  O  OH  . TYR A 47  ? 0.4450 0.3952 0.5067 -0.0226 -0.0073 0.0638  47  TYR A OH  
357  N  N   . VAL A 48  ? 0.2286 0.2110 0.2881 -0.0082 0.0099  0.0100  48  VAL A N   
358  C  CA  . VAL A 48  ? 0.2658 0.2496 0.3249 -0.0036 0.0087  0.0026  48  VAL A CA  
359  C  C   . VAL A 48  ? 0.2493 0.2264 0.3115 -0.0032 0.0034  -0.0008 48  VAL A C   
360  O  O   . VAL A 48  ? 0.2435 0.2187 0.3158 -0.0063 0.0015  -0.0001 48  VAL A O   
361  C  CB  . VAL A 48  ? 0.2705 0.2648 0.3401 -0.0033 0.0108  0.0004  48  VAL A CB  
362  C  CG1 . VAL A 48  ? 0.2825 0.2776 0.3520 0.0016  0.0080  -0.0058 48  VAL A CG1 
363  C  CG2 . VAL A 48  ? 0.2507 0.2540 0.3176 -0.0029 0.0170  0.0025  48  VAL A CG2 
364  N  N   . SER A 49  ? 0.2540 0.2273 0.3075 0.0001  0.0014  -0.0047 49  SER A N   
365  C  CA  . SER A 49  ? 0.2647 0.2346 0.3205 0.0003  -0.0027 -0.0088 49  SER A CA  
366  C  C   . SER A 49  ? 0.2463 0.2180 0.2976 0.0035  -0.0039 -0.0131 49  SER A C   
367  O  O   . SER A 49  ? 0.2339 0.2074 0.2810 0.0064  -0.0019 -0.0129 49  SER A O   
368  C  CB  . SER A 49  ? 0.2970 0.2606 0.3468 0.0000  -0.0046 -0.0076 49  SER A CB  
369  O  OG  . SER A 49  ? 0.2353 0.1962 0.2721 0.0017  -0.0043 -0.0079 49  SER A OG  
370  N  N   . ALA A 50  ? 0.2444 0.2158 0.2970 0.0031  -0.0072 -0.0170 50  ALA A N   
371  C  CA  . ALA A 50  ? 0.2808 0.2520 0.3262 0.0055  -0.0092 -0.0192 50  ALA A CA  
372  C  C   . ALA A 50  ? 0.1990 0.1630 0.2319 0.0071  -0.0082 -0.0173 50  ALA A C   
373  O  O   . ALA A 50  ? 0.2091 0.1692 0.2382 0.0056  -0.0073 -0.0155 50  ALA A O   
374  C  CB  . ALA A 50  ? 0.2486 0.2211 0.2944 0.0036  -0.0124 -0.0232 50  ALA A CB  
375  N  N   . GLY A 51  ? 0.2654 0.2274 0.2925 0.0103  -0.0088 -0.0176 51  GLY A N   
376  C  CA  . GLY A 51  ? 0.2305 0.1840 0.2462 0.0116  -0.0080 -0.0169 51  GLY A CA  
377  C  C   . GLY A 51  ? 0.2330 0.1817 0.2418 0.0079  -0.0097 -0.0169 51  GLY A C   
378  O  O   . GLY A 51  ? 0.2424 0.1933 0.2522 0.0059  -0.0122 -0.0181 51  GLY A O   
379  N  N   . TRP A 52  ? 0.1862 0.1306 0.1886 0.0065  -0.0083 -0.0159 52  TRP A N   
380  C  CA  . TRP A 52  ? 0.2029 0.1453 0.2006 0.0028  -0.0102 -0.0158 52  TRP A CA  
381  C  C   . TRP A 52  ? 0.2471 0.1839 0.2366 0.0015  -0.0123 -0.0166 52  TRP A C   
382  O  O   . TRP A 52  ? 0.2406 0.1705 0.2243 0.0037  -0.0122 -0.0167 52  TRP A O   
383  C  CB  . TRP A 52  ? 0.2558 0.1958 0.2474 0.0012  -0.0091 -0.0142 52  TRP A CB  
384  C  CG  . TRP A 52  ? 0.2375 0.1828 0.2359 0.0012  -0.0077 -0.0115 52  TRP A CG  
385  C  CD1 . TRP A 52  ? 0.2480 0.1984 0.2584 0.0018  -0.0074 -0.0106 52  TRP A CD1 
386  C  CD2 . TRP A 52  ? 0.2779 0.2236 0.2712 -0.0003 -0.0066 -0.0086 52  TRP A CD2 
387  N  NE1 . TRP A 52  ? 0.2412 0.1938 0.2546 0.0008  -0.0062 -0.0065 52  TRP A NE1 
388  C  CE2 . TRP A 52  ? 0.2650 0.2156 0.2676 -0.0004 -0.0058 -0.0048 52  TRP A CE2 
389  C  CE3 . TRP A 52  ? 0.2575 0.1998 0.2386 -0.0021 -0.0065 -0.0089 52  TRP A CE3 
390  C  CZ2 . TRP A 52  ? 0.2720 0.2248 0.2716 -0.0023 -0.0049 0.0001  52  TRP A CZ2 
391  C  CZ3 . TRP A 52  ? 0.3206 0.2664 0.2983 -0.0039 -0.0058 -0.0052 52  TRP A CZ3 
392  C  CH2 . TRP A 52  ? 0.3142 0.2654 0.3007 -0.0039 -0.0050 -0.0001 52  TRP A CH2 
393  N  N   . ILE A 53  ? 0.2474 0.1875 0.2374 -0.0020 -0.0141 -0.0171 53  ILE A N   
394  C  CA  . ILE A 53  ? 0.2632 0.1999 0.2457 -0.0051 -0.0159 -0.0169 53  ILE A CA  
395  C  C   . ILE A 53  ? 0.2647 0.2012 0.2429 -0.0096 -0.0164 -0.0168 53  ILE A C   
396  O  O   . ILE A 53  ? 0.2351 0.1795 0.2200 -0.0106 -0.0164 -0.0174 53  ILE A O   
397  C  CB  . ILE A 53  ? 0.2489 0.1933 0.2355 -0.0062 -0.0171 -0.0181 53  ILE A CB  
398  C  CG1 . ILE A 53  ? 0.2420 0.1881 0.2331 -0.0022 -0.0176 -0.0181 53  ILE A CG1 
399  C  CG2 . ILE A 53  ? 0.2772 0.2196 0.2551 -0.0107 -0.0187 -0.0167 53  ILE A CG2 
400  C  CD1 . ILE A 53  ? 0.2678 0.2239 0.2640 -0.0035 -0.0187 -0.0206 53  ILE A CD1 
401  N  N   . ASP A 54  ? 0.2797 0.2071 0.2477 -0.0123 -0.0172 -0.0160 54  ASP A N   
402  C  CA  . ASP A 54  ? 0.2916 0.2194 0.2550 -0.0180 -0.0183 -0.0160 54  ASP A CA  
403  C  C   . ASP A 54  ? 0.3019 0.2302 0.2615 -0.0232 -0.0195 -0.0150 54  ASP A C   
404  O  O   . ASP A 54  ? 0.2681 0.1857 0.2199 -0.0246 -0.0205 -0.0134 54  ASP A O   
405  C  CB  . ASP A 54  ? 0.2536 0.1708 0.2077 -0.0189 -0.0182 -0.0167 54  ASP A CB  
406  C  CG  . ASP A 54  ? 0.3017 0.2228 0.2529 -0.0247 -0.0198 -0.0170 54  ASP A CG  
407  O  OD1 . ASP A 54  ? 0.2864 0.2168 0.2421 -0.0285 -0.0210 -0.0163 54  ASP A OD1 
408  O  OD2 . ASP A 54  ? 0.3086 0.2245 0.2530 -0.0256 -0.0198 -0.0183 54  ASP A OD2 
409  N  N   . SER A 55  ? 0.2405 0.1814 0.2063 -0.0259 -0.0194 -0.0159 55  SER A N   
410  C  CA  . SER A 55  ? 0.2841 0.2299 0.2473 -0.0311 -0.0196 -0.0151 55  SER A CA  
411  C  C   . SER A 55  ? 0.2925 0.2352 0.2483 -0.0391 -0.0207 -0.0135 55  SER A C   
412  O  O   . SER A 55  ? 0.2680 0.2163 0.2214 -0.0449 -0.0205 -0.0121 55  SER A O   
413  C  CB  . SER A 55  ? 0.2803 0.2425 0.2538 -0.0307 -0.0182 -0.0182 55  SER A CB  
414  O  OG  . SER A 55  ? 0.3116 0.2761 0.2939 -0.0242 -0.0174 -0.0204 55  SER A OG  
415  N  N   . HIS A 56  ? 0.2393 0.1742 0.1909 -0.0403 -0.0218 -0.0137 56  HIS A N   
416  C  CA  . HIS A 56  ? 0.2866 0.2203 0.2325 -0.0489 -0.0232 -0.0130 56  HIS A CA  
417  C  C   . HIS A 56  ? 0.2750 0.1937 0.2126 -0.0492 -0.0245 -0.0140 56  HIS A C   
418  O  O   . HIS A 56  ? 0.3011 0.2239 0.2402 -0.0488 -0.0252 -0.0159 56  HIS A O   
419  C  CB  . HIS A 56  ? 0.2692 0.2210 0.2241 -0.0518 -0.0233 -0.0143 56  HIS A CB  
420  C  CG  . HIS A 56  ? 0.2858 0.2404 0.2368 -0.0618 -0.0247 -0.0136 56  HIS A CG  
421  N  ND1 . HIS A 56  ? 0.2873 0.2608 0.2467 -0.0661 -0.0244 -0.0142 56  HIS A ND1 
422  C  CD2 . HIS A 56  ? 0.3277 0.2687 0.2680 -0.0686 -0.0266 -0.0127 56  HIS A CD2 
423  C  CE1 . HIS A 56  ? 0.2829 0.2559 0.2371 -0.0758 -0.0259 -0.0131 56  HIS A CE1 
424  N  NE2 . HIS A 56  ? 0.3157 0.2679 0.2579 -0.0779 -0.0275 -0.0123 56  HIS A NE2 
425  N  N   . VAL A 57  ? 0.2898 0.1912 0.2187 -0.0498 -0.0251 -0.0130 57  VAL A N   
426  C  CA  . VAL A 57  ? 0.3309 0.2163 0.2513 -0.0505 -0.0259 -0.0156 57  VAL A CA  
427  C  C   . VAL A 57  ? 0.3709 0.2422 0.2827 -0.0587 -0.0278 -0.0138 57  VAL A C   
428  O  O   . VAL A 57  ? 0.3302 0.2038 0.2421 -0.0632 -0.0283 -0.0093 57  VAL A O   
429  C  CB  . VAL A 57  ? 0.3175 0.1923 0.2370 -0.0409 -0.0243 -0.0172 57  VAL A CB  
430  C  CG1 . VAL A 57  ? 0.3295 0.2179 0.2580 -0.0338 -0.0223 -0.0179 57  VAL A CG1 
431  C  CG2 . VAL A 57  ? 0.2965 0.1603 0.2145 -0.0383 -0.0248 -0.0137 57  VAL A CG2 
432  N  N   . HIS A 58  ? 0.3127 0.1690 0.2165 -0.0612 -0.0288 -0.0175 58  HIS A N   
433  C  CA  . HIS A 58  ? 0.3556 0.1920 0.2510 -0.0678 -0.0307 -0.0164 58  HIS A CA  
434  C  C   . HIS A 58  ? 0.4077 0.2233 0.2981 -0.0606 -0.0301 -0.0205 58  HIS A C   
435  O  O   . HIS A 58  ? 0.3971 0.2071 0.2826 -0.0609 -0.0297 -0.0273 58  HIS A O   
436  C  CB  . HIS A 58  ? 0.3926 0.2305 0.2838 -0.0800 -0.0328 -0.0183 58  HIS A CB  
437  C  CG  . HIS A 58  ? 0.3567 0.2161 0.2544 -0.0868 -0.0330 -0.0144 58  HIS A CG  
438  N  ND1 . HIS A 58  ? 0.3940 0.2553 0.2924 -0.0919 -0.0329 -0.0082 58  HIS A ND1 
439  C  CD2 . HIS A 58  ? 0.3587 0.2402 0.2637 -0.0884 -0.0331 -0.0158 58  HIS A CD2 
440  C  CE1 . HIS A 58  ? 0.3399 0.2242 0.2455 -0.0965 -0.0322 -0.0071 58  HIS A CE1 
441  N  NE2 . HIS A 58  ? 0.3713 0.2677 0.2819 -0.0940 -0.0325 -0.0116 58  HIS A NE2 
442  N  N   . CYS A 59  ? 0.4128 0.2180 0.3044 -0.0541 -0.0300 -0.0168 59  CYS A N   
443  C  CA  . CYS A 59  ? 0.4425 0.2307 0.3325 -0.0449 -0.0290 -0.0208 59  CYS A CA  
444  C  C   . CYS A 59  ? 0.4296 0.1941 0.3157 -0.0455 -0.0317 -0.0168 59  CYS A C   
445  O  O   . CYS A 59  ? 0.4203 0.1743 0.3092 -0.0356 -0.0315 -0.0163 59  CYS A O   
446  C  CB  . CYS A 59  ? 0.3899 0.1901 0.2884 -0.0333 -0.0265 -0.0204 59  CYS A CB  
447  S  SG  . CYS A 59  ? 0.3870 0.1969 0.2919 -0.0311 -0.0282 -0.0109 59  CYS A SG  
448  N  N   . TYR A 60  ? 0.3775 0.1340 0.2580 -0.0573 -0.0344 -0.0132 60  TYR A N   
449  C  CA  . TYR A 60  ? 0.4784 0.2090 0.3541 -0.0597 -0.0375 -0.0088 60  TYR A CA  
450  C  C   . TYR A 60  ? 0.4542 0.1630 0.3238 -0.0616 -0.0375 -0.0181 60  TYR A C   
451  O  O   . TYR A 60  ? 0.4377 0.1473 0.3021 -0.0731 -0.0382 -0.0218 60  TYR A O   
452  C  CB  . TYR A 60  ? 0.4735 0.2065 0.3459 -0.0728 -0.0400 0.0003  60  TYR A CB  
453  C  CG  . TYR A 60  ? 0.5041 0.2095 0.3711 -0.0773 -0.0437 0.0067  60  TYR A CG  
454  C  CD1 . TYR A 60  ? 0.5173 0.2041 0.3860 -0.0663 -0.0455 0.0097  60  TYR A CD1 
455  C  CD2 . TYR A 60  ? 0.5032 0.2032 0.3652 -0.0920 -0.0455 0.0102  60  TYR A CD2 
456  C  CE1 . TYR A 60  ? 0.5176 0.1857 0.3857 -0.0681 -0.0482 0.0163  60  TYR A CE1 
457  C  CE2 . TYR A 60  ? 0.5323 0.2145 0.3934 -0.0942 -0.0478 0.0166  60  TYR A CE2 
458  C  CZ  . TYR A 60  ? 0.5538 0.2193 0.4178 -0.0822 -0.0492 0.0198  60  TYR A CZ  
459  O  OH  . TYR A 60  ? 0.5835 0.2307 0.4476 -0.0842 -0.0517 0.0267  60  TYR A OH  
460  N  N   . PRO A 61  ? 0.4850 0.1757 0.3554 -0.0508 -0.0367 -0.0230 61  PRO A N   
461  C  CA  . PRO A 61  ? 0.4945 0.1756 0.3633 -0.0503 -0.0346 -0.0340 61  PRO A CA  
462  C  C   . PRO A 61  ? 0.4910 0.1608 0.3569 -0.0618 -0.0368 -0.0333 61  PRO A C   
463  O  O   . PRO A 61  ? 0.5064 0.1737 0.3692 -0.0659 -0.0356 -0.0429 61  PRO A O   
464  C  CB  . PRO A 61  ? 0.5048 0.1733 0.3800 -0.0352 -0.0327 -0.0370 61  PRO A CB  
465  C  CG  . PRO A 61  ? 0.5347 0.2139 0.4141 -0.0267 -0.0329 -0.0308 61  PRO A CG  
466  C  CD  . PRO A 61  ? 0.5223 0.2114 0.4002 -0.0367 -0.0363 -0.0193 61  PRO A CD  
467  N  N   . ASN A 62  ? 0.5063 0.1695 0.3728 -0.0674 -0.0400 -0.0221 62  ASN A N   
468  C  CA  . ASN A 62  ? 0.5019 0.1524 0.3665 -0.0781 -0.0421 -0.0204 62  ASN A CA  
469  C  C   . ASN A 62  ? 0.5165 0.1821 0.3769 -0.0939 -0.0434 -0.0169 62  ASN A C   
470  O  O   . ASN A 62  ? 0.5590 0.2167 0.4181 -0.1043 -0.0452 -0.0148 62  ASN A O   
471  C  CB  . ASN A 62  ? 0.5399 0.1731 0.4078 -0.0754 -0.0447 -0.0096 62  ASN A CB  
472  C  CG  . ASN A 62  ? 0.5900 0.2052 0.4643 -0.0608 -0.0435 -0.0142 62  ASN A CG  
473  O  OD1 . ASN A 62  ? 0.5467 0.1535 0.4224 -0.0578 -0.0410 -0.0264 62  ASN A OD1 
474  N  ND2 . ASN A 62  ? 0.6179 0.2280 0.4969 -0.0521 -0.0455 -0.0046 62  ASN A ND2 
475  N  N   . SER A 63  ? 0.5213 0.2092 0.3810 -0.0960 -0.0426 -0.0166 63  SER A N   
476  C  CA  . SER A 63  ? 0.5177 0.2236 0.3759 -0.1101 -0.0435 -0.0144 63  SER A CA  
477  C  C   . SER A 63  ? 0.5275 0.2344 0.3836 -0.1164 -0.0435 -0.0245 63  SER A C   
478  O  O   . SER A 63  ? 0.5075 0.2151 0.3622 -0.1097 -0.0419 -0.0343 63  SER A O   
479  C  CB  . SER A 63  ? 0.4914 0.2207 0.3515 -0.1090 -0.0424 -0.0132 63  SER A CB  
480  O  OG  . SER A 63  ? 0.5162 0.2652 0.3776 -0.1219 -0.0431 -0.0100 63  SER A OG  
481  N  N   . PRO A 64  ? 0.5537 0.2618 0.4090 -0.1296 -0.0453 -0.0223 64  PRO A N   
482  C  CA  . PRO A 64  ? 0.5413 0.2471 0.3944 -0.1355 -0.0460 -0.0322 64  PRO A CA  
483  C  C   . PRO A 64  ? 0.5555 0.2829 0.4076 -0.1358 -0.0456 -0.0399 64  PRO A C   
484  O  O   . PRO A 64  ? 0.5623 0.2849 0.4110 -0.1338 -0.0454 -0.0503 64  PRO A O   
485  C  CB  . PRO A 64  ? 0.5659 0.2725 0.4196 -0.1504 -0.0482 -0.0261 64  PRO A CB  
486  C  CG  . PRO A 64  ? 0.5574 0.2776 0.4134 -0.1536 -0.0479 -0.0141 64  PRO A CG  
487  C  CD  . PRO A 64  ? 0.5861 0.2972 0.4421 -0.1400 -0.0467 -0.0109 64  PRO A CD  
488  N  N   . ILE A 65  ? 0.5128 0.2641 0.3680 -0.1381 -0.0456 -0.0352 65  ILE A N   
489  C  CA  . ILE A 65  ? 0.5253 0.2989 0.3810 -0.1392 -0.0461 -0.0407 65  ILE A CA  
490  C  C   . ILE A 65  ? 0.5101 0.2917 0.3668 -0.1280 -0.0442 -0.0413 65  ILE A C   
491  O  O   . ILE A 65  ? 0.4549 0.2374 0.3078 -0.1219 -0.0434 -0.0488 65  ILE A O   
492  C  CB  . ILE A 65  ? 0.5407 0.3386 0.4018 -0.1514 -0.0481 -0.0361 65  ILE A CB  
493  C  CG1 . ILE A 65  ? 0.5146 0.3054 0.3746 -0.1633 -0.0500 -0.0362 65  ILE A CG1 
494  C  CG2 . ILE A 65  ? 0.4999 0.3218 0.3631 -0.1512 -0.0495 -0.0407 65  ILE A CG2 
495  C  CD1 . ILE A 65  ? 0.5210 0.2972 0.3751 -0.1634 -0.0511 -0.0465 65  ILE A CD1 
496  N  N   . TYR A 66  ? 0.4834 0.2715 0.3447 -0.1258 -0.0434 -0.0335 66  TYR A N   
497  C  CA  . TYR A 66  ? 0.4714 0.2724 0.3374 -0.1138 -0.0410 -0.0328 66  TYR A CA  
498  C  C   . TYR A 66  ? 0.4772 0.2591 0.3422 -0.1022 -0.0388 -0.0316 66  TYR A C   
499  O  O   . TYR A 66  ? 0.4656 0.2481 0.3349 -0.0990 -0.0381 -0.0239 66  TYR A O   
500  C  CB  . TYR A 66  ? 0.4859 0.3138 0.3623 -0.1150 -0.0404 -0.0257 66  TYR A CB  
501  C  CG  . TYR A 66  ? 0.5305 0.3760 0.4095 -0.1276 -0.0430 -0.0261 66  TYR A CG  
502  C  CD1 . TYR A 66  ? 0.5362 0.3980 0.4170 -0.1274 -0.0446 -0.0308 66  TYR A CD1 
503  C  CD2 . TYR A 66  ? 0.5147 0.3622 0.3948 -0.1400 -0.0440 -0.0212 66  TYR A CD2 
504  C  CE1 . TYR A 66  ? 0.5596 0.4394 0.4441 -0.1385 -0.0477 -0.0310 66  TYR A CE1 
505  C  CE2 . TYR A 66  ? 0.5574 0.4236 0.4416 -0.1518 -0.0463 -0.0218 66  TYR A CE2 
506  C  CZ  . TYR A 66  ? 0.5841 0.4667 0.4711 -0.1505 -0.0484 -0.0269 66  TYR A CZ  
507  O  OH  . TYR A 66  ? 0.6740 0.5781 0.5674 -0.1601 -0.0509 -0.0269 66  TYR A OH  
508  N  N   . HIS A 67  ? 0.5016 0.2681 0.3610 -0.0957 -0.0377 -0.0396 67  HIS A N   
509  C  CA  . HIS A 67  ? 0.4898 0.2394 0.3497 -0.0836 -0.0356 -0.0398 67  HIS A CA  
510  C  C   . HIS A 67  ? 0.4699 0.2292 0.3316 -0.0719 -0.0320 -0.0456 67  HIS A C   
511  O  O   . HIS A 67  ? 0.4382 0.2092 0.2967 -0.0741 -0.0316 -0.0513 67  HIS A O   
512  C  CB  . HIS A 67  ? 0.5019 0.2251 0.3576 -0.0844 -0.0363 -0.0436 67  HIS A CB  
513  C  CG  . HIS A 67  ? 0.5198 0.2411 0.3707 -0.0872 -0.0356 -0.0546 67  HIS A CG  
514  N  ND1 . HIS A 67  ? 0.5339 0.2491 0.3824 -0.0776 -0.0324 -0.0642 67  HIS A ND1 
515  C  CD2 . HIS A 67  ? 0.5251 0.2507 0.3729 -0.0988 -0.0378 -0.0578 67  HIS A CD2 
516  C  CE1 . HIS A 67  ? 0.5677 0.2832 0.4109 -0.0835 -0.0327 -0.0731 67  HIS A CE1 
517  N  NE2 . HIS A 67  ? 0.5747 0.2962 0.4175 -0.0962 -0.0363 -0.0693 67  HIS A NE2 
518  N  N   . ASP A 68  ? 0.4343 0.1896 0.3012 -0.0599 -0.0297 -0.0433 68  ASP A N   
519  C  CA  . ASP A 68  ? 0.4049 0.1663 0.2738 -0.0486 -0.0257 -0.0487 68  ASP A CA  
520  C  C   . ASP A 68  ? 0.4520 0.2033 0.3271 -0.0370 -0.0244 -0.0458 68  ASP A C   
521  O  O   . ASP A 68  ? 0.4657 0.2093 0.3436 -0.0378 -0.0270 -0.0381 68  ASP A O   
522  C  CB  . ASP A 68  ? 0.4310 0.2199 0.3054 -0.0472 -0.0243 -0.0462 68  ASP A CB  
523  C  CG  . ASP A 68  ? 0.4654 0.2609 0.3362 -0.0425 -0.0210 -0.0536 68  ASP A CG  
524  O  OD1 . ASP A 68  ? 0.4423 0.2239 0.3093 -0.0366 -0.0182 -0.0607 68  ASP A OD1 
525  O  OD2 . ASP A 68  ? 0.4345 0.2492 0.3065 -0.0446 -0.0210 -0.0523 68  ASP A OD2 
526  N  N   . GLU A 69  ? 0.4522 0.2049 0.3295 -0.0265 -0.0203 -0.0517 69  GLU A N   
527  C  CA  . GLU A 69  ? 0.4419 0.1901 0.3275 -0.0144 -0.0190 -0.0492 69  GLU A CA  
528  C  C   . GLU A 69  ? 0.4371 0.2087 0.3322 -0.0102 -0.0181 -0.0424 69  GLU A C   
529  O  O   . GLU A 69  ? 0.3853 0.1750 0.2813 -0.0111 -0.0157 -0.0441 69  GLU A O   
530  C  CB  . GLU A 69  ? 0.4866 0.2275 0.3717 -0.0050 -0.0144 -0.0595 69  GLU A CB  
531  C  CG  . GLU A 69  ? 0.5349 0.2500 0.4115 -0.0073 -0.0148 -0.0683 69  GLU A CG  
532  C  CD  . GLU A 69  ? 0.5593 0.2511 0.4399 -0.0036 -0.0182 -0.0637 69  GLU A CD  
533  O  OE1 . GLU A 69  ? 0.5908 0.2858 0.4807 0.0047  -0.0193 -0.0561 69  GLU A OE1 
534  O  OE2 . GLU A 69  ? 0.6294 0.3074 0.5083 -0.0092 -0.0196 -0.0665 69  GLU A OE2 
535  N  N   . PRO A 70  ? 0.3967 0.1683 0.2989 -0.0059 -0.0202 -0.0346 70  PRO A N   
536  C  CA  . PRO A 70  ? 0.3802 0.1735 0.2913 -0.0024 -0.0195 -0.0294 70  PRO A CA  
537  C  C   . PRO A 70  ? 0.3911 0.1976 0.3075 0.0048  -0.0147 -0.0345 70  PRO A C   
538  O  O   . PRO A 70  ? 0.3450 0.1698 0.2651 0.0030  -0.0136 -0.0328 70  PRO A O   
539  C  CB  . PRO A 70  ? 0.4063 0.1936 0.3229 0.0030  -0.0226 -0.0224 70  PRO A CB  
540  C  CG  . PRO A 70  ? 0.3998 0.1649 0.3086 -0.0029 -0.0263 -0.0199 70  PRO A CG  
541  C  CD  . PRO A 70  ? 0.4290 0.1809 0.3304 -0.0056 -0.0242 -0.0293 70  PRO A CD  
542  N  N   . ASP A 71  ? 0.3919 0.1898 0.3091 0.0128  -0.0117 -0.0407 71  ASP A N   
543  C  CA  . ASP A 71  ? 0.3667 0.1796 0.2895 0.0192  -0.0066 -0.0446 71  ASP A CA  
544  C  C   . ASP A 71  ? 0.4414 0.2613 0.3559 0.0135  -0.0035 -0.0501 71  ASP A C   
545  O  O   . ASP A 71  ? 0.3843 0.2207 0.3025 0.0154  0.0000  -0.0503 71  ASP A O   
546  C  CB  . ASP A 71  ? 0.4032 0.2080 0.3314 0.0305  -0.0037 -0.0496 71  ASP A CB  
547  C  CG  . ASP A 71  ? 0.4092 0.2154 0.3490 0.0378  -0.0068 -0.0426 71  ASP A CG  
548  O  OD1 . ASP A 71  ? 0.3704 0.1896 0.3146 0.0347  -0.0095 -0.0352 71  ASP A OD1 
549  O  OD2 . ASP A 71  ? 0.4347 0.2290 0.3791 0.0466  -0.0069 -0.0446 71  ASP A OD2 
550  N  N   . SER A 72  ? 0.4119 0.2203 0.3152 0.0058  -0.0053 -0.0538 72  SER A N   
551  C  CA  . SER A 72  ? 0.4166 0.2341 0.3114 -0.0009 -0.0040 -0.0575 72  SER A CA  
552  C  C   . SER A 72  ? 0.3644 0.1996 0.2630 -0.0066 -0.0064 -0.0499 72  SER A C   
553  O  O   . SER A 72  ? 0.3793 0.2281 0.2761 -0.0084 -0.0048 -0.0501 72  SER A O   
554  C  CB  . SER A 72  ? 0.3882 0.1898 0.2707 -0.0085 -0.0061 -0.0637 72  SER A CB  
555  O  OG  . SER A 72  ? 0.4566 0.2414 0.3358 -0.0026 -0.0032 -0.0726 72  SER A OG  
556  N  N   . VAL A 73  ? 0.3106 0.1460 0.2145 -0.0092 -0.0102 -0.0431 73  VAL A N   
557  C  CA  . VAL A 73  ? 0.3178 0.1700 0.2272 -0.0132 -0.0120 -0.0371 73  VAL A CA  
558  C  C   . VAL A 73  ? 0.3580 0.2210 0.2792 -0.0068 -0.0108 -0.0325 73  VAL A C   
559  O  O   . VAL A 73  ? 0.3286 0.2051 0.2558 -0.0087 -0.0117 -0.0286 73  VAL A O   
560  C  CB  . VAL A 73  ? 0.3704 0.2205 0.2781 -0.0216 -0.0164 -0.0334 73  VAL A CB  
561  C  CG1 . VAL A 73  ? 0.3269 0.1688 0.2238 -0.0296 -0.0181 -0.0379 73  VAL A CG1 
562  C  CG2 . VAL A 73  ? 0.3431 0.1832 0.2535 -0.0198 -0.0181 -0.0296 73  VAL A CG2 
563  N  N   . GLY A 74  ? 0.3571 0.2147 0.2826 0.0009  -0.0090 -0.0334 74  GLY A N   
564  C  CA  . GLY A 74  ? 0.3372 0.2060 0.2742 0.0065  -0.0082 -0.0298 74  GLY A CA  
565  C  C   . GLY A 74  ? 0.3116 0.1894 0.2530 0.0119  -0.0034 -0.0324 74  GLY A C   
566  O  O   . GLY A 74  ? 0.3253 0.2120 0.2648 0.0089  -0.0016 -0.0326 74  GLY A O   
567  N  N   . ILE A 75  ? 0.3201 0.1966 0.2678 0.0198  -0.0015 -0.0337 75  ILE A N   
568  C  CA  . ILE A 75  ? 0.3108 0.1988 0.2655 0.0251  0.0035  -0.0356 75  ILE A CA  
569  C  C   . ILE A 75  ? 0.3382 0.2286 0.2844 0.0230  0.0081  -0.0404 75  ILE A C   
570  O  O   . ILE A 75  ? 0.3343 0.2382 0.2843 0.0230  0.0117  -0.0393 75  ILE A O   
571  C  CB  . ILE A 75  ? 0.3366 0.2213 0.2989 0.0345  0.0046  -0.0376 75  ILE A CB  
572  C  CG1 . ILE A 75  ? 0.3434 0.2374 0.3178 0.0368  0.0015  -0.0319 75  ILE A CG1 
573  C  CG2 . ILE A 75  ? 0.4144 0.3055 0.3790 0.0400  0.0114  -0.0435 75  ILE A CG2 
574  C  CD1 . ILE A 75  ? 0.3762 0.2627 0.3482 0.0336  -0.0045 -0.0273 75  ILE A CD1 
575  N  N   . ALA A 76  ? 0.3302 0.2078 0.2645 0.0206  0.0079  -0.0456 76  ALA A N   
576  C  CA  . ALA A 76  ? 0.4104 0.2917 0.3348 0.0180  0.0120  -0.0507 76  ALA A CA  
577  C  C   . ALA A 76  ? 0.3432 0.2373 0.2655 0.0109  0.0108  -0.0452 76  ALA A C   
578  O  O   . ALA A 76  ? 0.3389 0.2418 0.2558 0.0094  0.0145  -0.0466 76  ALA A O   
579  C  CB  . ALA A 76  ? 0.3513 0.2161 0.2626 0.0152  0.0111  -0.0581 76  ALA A CB  
580  N  N   . THR A 77  ? 0.3238 0.2196 0.2505 0.0069  0.0057  -0.0389 77  THR A N   
581  C  CA  . THR A 77  ? 0.3375 0.2449 0.2654 0.0017  0.0039  -0.0331 77  THR A CA  
582  C  C   . THR A 77  ? 0.3082 0.2255 0.2502 0.0039  0.0038  -0.0271 77  THR A C   
583  O  O   . THR A 77  ? 0.3176 0.2416 0.2635 0.0004  0.0012  -0.0220 77  THR A O   
584  C  CB  . THR A 77  ? 0.3373 0.2409 0.2607 -0.0049 -0.0016 -0.0314 77  THR A CB  
585  O  OG1 . THR A 77  ? 0.3188 0.2196 0.2503 -0.0041 -0.0045 -0.0286 77  THR A OG1 
586  C  CG2 . THR A 77  ? 0.3264 0.2183 0.2366 -0.0083 -0.0023 -0.0379 77  THR A CG2 
587  N  N   . GLY A 78  ? 0.3045 0.2227 0.2550 0.0098  0.0061  -0.0280 78  GLY A N   
588  C  CA  . GLY A 78  ? 0.2970 0.2245 0.2609 0.0111  0.0056  -0.0234 78  GLY A CA  
589  C  C   . GLY A 78  ? 0.2899 0.2147 0.2595 0.0106  0.0010  -0.0214 78  GLY A C   
590  O  O   . GLY A 78  ? 0.3079 0.2401 0.2882 0.0112  0.0003  -0.0188 78  GLY A O   
591  N  N   . VAL A 79  ? 0.2815 0.1965 0.2440 0.0087  -0.0021 -0.0228 79  VAL A N   
592  C  CA  . VAL A 79  ? 0.2457 0.1597 0.2114 0.0068  -0.0061 -0.0207 79  VAL A CA  
593  C  C   . VAL A 79  ? 0.2733 0.1822 0.2415 0.0116  -0.0070 -0.0211 79  VAL A C   
594  O  O   . VAL A 79  ? 0.2947 0.1929 0.2570 0.0142  -0.0066 -0.0234 79  VAL A O   
595  C  CB  . VAL A 79  ? 0.2921 0.2002 0.2492 0.0009  -0.0090 -0.0208 79  VAL A CB  
596  C  CG1 . VAL A 79  ? 0.2564 0.1655 0.2162 -0.0016 -0.0122 -0.0187 79  VAL A CG1 
597  C  CG2 . VAL A 79  ? 0.2716 0.1864 0.2272 -0.0031 -0.0090 -0.0197 79  VAL A CG2 
598  N  N   . THR A 80  ? 0.2585 0.1748 0.2356 0.0128  -0.0087 -0.0189 80  THR A N   
599  C  CA  . THR A 80  ? 0.2692 0.1834 0.2497 0.0177  -0.0103 -0.0182 80  THR A CA  
600  C  C   . THR A 80  ? 0.2914 0.1992 0.2667 0.0151  -0.0147 -0.0156 80  THR A C   
601  O  O   . THR A 80  ? 0.3171 0.2182 0.2917 0.0191  -0.0169 -0.0139 80  THR A O   
602  C  CB  . THR A 80  ? 0.3091 0.2365 0.3020 0.0203  -0.0101 -0.0174 80  THR A CB  
603  O  OG1 . THR A 80  ? 0.2416 0.1764 0.2379 0.0153  -0.0113 -0.0167 80  THR A OG1 
604  C  CG2 . THR A 80  ? 0.2658 0.1992 0.2642 0.0234  -0.0053 -0.0192 80  THR A CG2 
605  N  N   . THR A 81  ? 0.2508 0.1608 0.2227 0.0087  -0.0161 -0.0147 81  THR A N   
606  C  CA  . THR A 81  ? 0.2732 0.1782 0.2386 0.0045  -0.0195 -0.0120 81  THR A CA  
607  C  C   . THR A 81  ? 0.2875 0.1884 0.2454 -0.0022 -0.0193 -0.0127 81  THR A C   
608  O  O   . THR A 81  ? 0.2587 0.1676 0.2197 -0.0046 -0.0178 -0.0143 81  THR A O   
609  C  CB  . THR A 81  ? 0.2780 0.1949 0.2482 0.0026  -0.0214 -0.0106 81  THR A CB  
610  O  OG1 . THR A 81  ? 0.2715 0.1926 0.2480 0.0081  -0.0228 -0.0096 81  THR A OG1 
611  C  CG2 . THR A 81  ? 0.2642 0.1782 0.2261 -0.0032 -0.0241 -0.0075 81  THR A CG2 
612  N  N   . VAL A 82  ? 0.3044 0.1930 0.2535 -0.0054 -0.0211 -0.0109 82  VAL A N   
613  C  CA  . VAL A 82  ? 0.2797 0.1657 0.2222 -0.0132 -0.0215 -0.0113 82  VAL A CA  
614  C  C   . VAL A 82  ? 0.3155 0.2007 0.2535 -0.0190 -0.0241 -0.0069 82  VAL A C   
615  O  O   . VAL A 82  ? 0.3414 0.2201 0.2773 -0.0170 -0.0262 -0.0030 82  VAL A O   
616  C  CB  . VAL A 82  ? 0.3153 0.1866 0.2501 -0.0139 -0.0210 -0.0140 82  VAL A CB  
617  C  CG1 . VAL A 82  ? 0.3169 0.1922 0.2542 -0.0096 -0.0179 -0.0182 82  VAL A CG1 
618  C  CG2 . VAL A 82  ? 0.3230 0.1774 0.2535 -0.0104 -0.0225 -0.0124 82  VAL A CG2 
619  N  N   . ILE A 83  ? 0.2667 0.1596 0.2035 -0.0265 -0.0239 -0.0070 83  ILE A N   
620  C  CA  . ILE A 83  ? 0.2937 0.1894 0.2261 -0.0336 -0.0254 -0.0030 83  ILE A CA  
621  C  C   . ILE A 83  ? 0.3335 0.2224 0.2592 -0.0421 -0.0260 -0.0027 83  ILE A C   
622  O  O   . ILE A 83  ? 0.3259 0.2242 0.2548 -0.0454 -0.0249 -0.0058 83  ILE A O   
623  C  CB  . ILE A 83  ? 0.2908 0.2063 0.2297 -0.0352 -0.0240 -0.0043 83  ILE A CB  
624  C  CG1 . ILE A 83  ? 0.3117 0.2329 0.2558 -0.0286 -0.0243 -0.0045 83  ILE A CG1 
625  C  CG2 . ILE A 83  ? 0.3334 0.2540 0.2667 -0.0438 -0.0245 -0.0008 83  ILE A CG2 
626  C  CD1 . ILE A 83  ? 0.3271 0.2526 0.2805 -0.0219 -0.0226 -0.0088 83  ILE A CD1 
627  N  N   . ASP A 84  ? 0.3051 0.1774 0.2223 -0.0456 -0.0281 0.0013  84  ASP A N   
628  C  CA  . ASP A 84  ? 0.3543 0.2180 0.2649 -0.0550 -0.0291 0.0017  84  ASP A CA  
629  C  C   . ASP A 84  ? 0.3496 0.2287 0.2604 -0.0647 -0.0286 0.0044  84  ASP A C   
630  O  O   . ASP A 84  ? 0.3253 0.2095 0.2343 -0.0670 -0.0289 0.0094  84  ASP A O   
631  C  CB  . ASP A 84  ? 0.3807 0.2200 0.2830 -0.0559 -0.0317 0.0055  84  ASP A CB  
632  C  CG  . ASP A 84  ? 0.3876 0.2160 0.2829 -0.0671 -0.0330 0.0056  84  ASP A CG  
633  O  OD1 . ASP A 84  ? 0.3937 0.2142 0.2872 -0.0673 -0.0328 -0.0006 84  ASP A OD1 
634  O  OD2 . ASP A 84  ? 0.3611 0.1895 0.2523 -0.0764 -0.0343 0.0118  84  ASP A OD2 
635  N  N   . ALA A 85  ? 0.3481 0.2362 0.2612 -0.0706 -0.0279 0.0010  85  ALA A N   
636  C  CA  . ALA A 85  ? 0.3370 0.2454 0.2541 -0.0781 -0.0264 0.0017  85  ALA A CA  
637  C  C   . ALA A 85  ? 0.3488 0.2511 0.2584 -0.0909 -0.0276 0.0062  85  ALA A C   
638  O  O   . ALA A 85  ? 0.3387 0.2475 0.2496 -0.0990 -0.0279 0.0046  85  ALA A O   
639  C  CB  . ALA A 85  ? 0.2985 0.2228 0.2249 -0.0766 -0.0254 -0.0038 85  ALA A CB  
640  N  N   . GLY A 86  ? 0.3181 0.2079 0.2200 -0.0930 -0.0289 0.0128  86  GLY A N   
641  C  CA  . GLY A 86  ? 0.3809 0.2643 0.2753 -0.1060 -0.0301 0.0190  86  GLY A CA  
642  C  C   . GLY A 86  ? 0.3974 0.2592 0.2861 -0.1120 -0.0327 0.0183  86  GLY A C   
643  O  O   . GLY A 86  ? 0.3904 0.2543 0.2767 -0.1248 -0.0331 0.0203  86  GLY A O   
644  N  N   . SER A 87  ? 0.4045 0.2463 0.2912 -0.1035 -0.0344 0.0147  87  SER A N   
645  C  CA  . SER A 87  ? 0.4157 0.2333 0.2956 -0.1089 -0.0369 0.0131  87  SER A CA  
646  C  C   . SER A 87  ? 0.4915 0.2893 0.3634 -0.1166 -0.0395 0.0223  87  SER A C   
647  O  O   . SER A 87  ? 0.4401 0.2232 0.3069 -0.1275 -0.0414 0.0228  87  SER A O   
648  C  CB  . SER A 87  ? 0.4316 0.2331 0.3112 -0.0970 -0.0372 0.0066  87  SER A CB  
649  O  OG  . SER A 87  ? 0.3902 0.2092 0.2762 -0.0904 -0.0350 -0.0004 87  SER A OG  
650  N  N   . THR A 88  ? 0.4286 0.2256 0.2994 -0.1118 -0.0400 0.0299  88  THR A N   
651  C  CA  . THR A 88  ? 0.4788 0.2578 0.3417 -0.1184 -0.0431 0.0409  88  THR A CA  
652  C  C   . THR A 88  ? 0.4699 0.2707 0.3313 -0.1260 -0.0416 0.0491  88  THR A C   
653  O  O   . THR A 88  ? 0.4529 0.2774 0.3194 -0.1200 -0.0389 0.0468  88  THR A O   
654  C  CB  . THR A 88  ? 0.4862 0.2437 0.3478 -0.1062 -0.0461 0.0446  88  THR A CB  
655  O  OG1 . THR A 88  ? 0.4621 0.2380 0.3292 -0.0949 -0.0446 0.0438  88  THR A OG1 
656  C  CG2 . THR A 88  ? 0.4851 0.2198 0.3476 -0.0990 -0.0469 0.0360  88  THR A CG2 
657  N  N   . GLY A 89  ? 0.5081 0.3005 0.3621 -0.1396 -0.0432 0.0585  89  GLY A N   
658  C  CA  . GLY A 89  ? 0.4785 0.2844 0.3274 -0.1464 -0.0427 0.0692  89  GLY A CA  
659  C  C   . GLY A 89  ? 0.5335 0.3163 0.3751 -0.1422 -0.0476 0.0806  89  GLY A C   
660  O  O   . GLY A 89  ? 0.5440 0.3061 0.3877 -0.1300 -0.0507 0.0784  89  GLY A O   
661  N  N   . ALA A 90  ? 0.5353 0.3227 0.3686 -0.1527 -0.0485 0.0933  90  ALA A N   
662  C  CA  . ALA A 90  ? 0.5380 0.3062 0.3647 -0.1489 -0.0540 0.1059  90  ALA A CA  
663  C  C   . ALA A 90  ? 0.5554 0.2927 0.3849 -0.1445 -0.0577 0.1058  90  ALA A C   
664  O  O   . ALA A 90  ? 0.5557 0.2752 0.3858 -0.1340 -0.0621 0.1111  90  ALA A O   
665  C  CB  . ALA A 90  ? 0.5431 0.3284 0.3619 -0.1602 -0.0535 0.1176  90  ALA A CB  
666  N  N   . ASP A 91  ? 0.5834 0.3153 0.4155 -0.1520 -0.0559 0.0992  91  ASP A N   
667  C  CA  . ASP A 91  ? 0.6172 0.3208 0.4516 -0.1497 -0.0586 0.0983  91  ASP A CA  
668  C  C   . ASP A 91  ? 0.5959 0.2804 0.4362 -0.1330 -0.0600 0.0900  91  ASP A C   
669  O  O   . ASP A 91  ? 0.5927 0.2542 0.4352 -0.1255 -0.0632 0.0933  91  ASP A O   
670  C  CB  . ASP A 91  ? 0.5940 0.2999 0.4299 -0.1618 -0.0561 0.0915  91  ASP A CB  
671  C  CG  . ASP A 91  ? 0.6459 0.3583 0.4772 -0.1771 -0.0560 0.1017  91  ASP A CG  
672  O  OD1 . ASP A 91  ? 0.6221 0.3476 0.4482 -0.1803 -0.0562 0.1125  91  ASP A OD1 
673  O  OD2 . ASP A 91  ? 0.7218 0.4277 0.5545 -0.1863 -0.0556 0.0988  91  ASP A OD2 
674  N  N   . ASP A 92  ? 0.5416 0.2359 0.3853 -0.1269 -0.0575 0.0790  92  ASP A N   
675  C  CA  . ASP A 92  ? 0.5702 0.2491 0.4197 -0.1119 -0.0578 0.0694  92  ASP A CA  
676  C  C   . ASP A 92  ? 0.6005 0.2873 0.4521 -0.0994 -0.0583 0.0691  92  ASP A C   
677  O  O   . ASP A 92  ? 0.5830 0.2616 0.4402 -0.0867 -0.0578 0.0602  92  ASP A O   
678  C  CB  . ASP A 92  ? 0.5954 0.2763 0.4476 -0.1142 -0.0546 0.0549  92  ASP A CB  
679  C  CG  . ASP A 92  ? 0.6648 0.3367 0.5158 -0.1259 -0.0546 0.0538  92  ASP A CG  
680  O  OD1 . ASP A 92  ? 0.6992 0.3863 0.5474 -0.1399 -0.0536 0.0575  92  ASP A OD1 
681  O  OD2 . ASP A 92  ? 0.7432 0.3934 0.5968 -0.1210 -0.0554 0.0488  92  ASP A OD2 
682  N  N   . VAL A 93  ? 0.5363 0.2400 0.3838 -0.1026 -0.0592 0.0783  93  VAL A N   
683  C  CA  . VAL A 93  ? 0.5246 0.2480 0.3791 -0.0888 -0.0577 0.0739  93  VAL A CA  
684  C  C   . VAL A 93  ? 0.5317 0.2367 0.3893 -0.0747 -0.0624 0.0784  93  VAL A C   
685  O  O   . VAL A 93  ? 0.5308 0.2434 0.3967 -0.0612 -0.0611 0.0710  93  VAL A O   
686  C  CB  . VAL A 93  ? 0.5045 0.2590 0.3568 -0.0942 -0.0559 0.0787  93  VAL A CB  
687  C  CG1 . VAL A 93  ? 0.5019 0.2514 0.3458 -0.0984 -0.0608 0.0948  93  VAL A CG1 
688  C  CG2 . VAL A 93  ? 0.4988 0.2755 0.3597 -0.0821 -0.0533 0.0703  93  VAL A CG2 
689  N  N   . ASP A 94  ? 0.5218 0.2060 0.3753 -0.0767 -0.0674 0.0899  94  ASP A N   
690  C  CA  . ASP A 94  ? 0.5721 0.2432 0.4324 -0.0615 -0.0714 0.0934  94  ASP A CA  
691  C  C   . ASP A 94  ? 0.5636 0.2202 0.4334 -0.0497 -0.0689 0.0799  94  ASP A C   
692  O  O   . ASP A 94  ? 0.5724 0.2302 0.4498 -0.0353 -0.0695 0.0761  94  ASP A O   
693  C  CB  . ASP A 94  ? 0.5881 0.2461 0.4463 -0.0649 -0.0753 0.1063  94  ASP A CB  
694  C  CG  . ASP A 94  ? 0.6208 0.2954 0.4689 -0.0767 -0.0774 0.1198  94  ASP A CG  
695  O  OD1 . ASP A 94  ? 0.6258 0.3226 0.4695 -0.0800 -0.0762 0.1195  94  ASP A OD1 
696  O  OD2 . ASP A 94  ? 0.6374 0.3031 0.4818 -0.0829 -0.0798 0.1305  94  ASP A OD2 
697  N  N   . ASP A 95  ? 0.5847 0.2293 0.4541 -0.0558 -0.0658 0.0724  95  ASP A N   
698  C  CA  . ASP A 95  ? 0.6152 0.2477 0.4921 -0.0460 -0.0627 0.0587  95  ASP A CA  
699  C  C   . ASP A 95  ? 0.5675 0.2150 0.4463 -0.0403 -0.0591 0.0475  95  ASP A C   
700  O  O   . ASP A 95  ? 0.5848 0.2297 0.4715 -0.0266 -0.0574 0.0395  95  ASP A O   
701  C  CB  . ASP A 95  ? 0.6297 0.2492 0.5041 -0.0562 -0.0606 0.0530  95  ASP A CB  
702  C  CG  . ASP A 95  ? 0.6811 0.2906 0.5614 -0.0482 -0.0567 0.0375  95  ASP A CG  
703  O  OD1 . ASP A 95  ? 0.6196 0.2323 0.4964 -0.0565 -0.0538 0.0280  95  ASP A OD1 
704  O  OD2 . ASP A 95  ? 0.6726 0.2728 0.5612 -0.0339 -0.0565 0.0347  95  ASP A OD2 
705  N  N   . PHE A 96  ? 0.5625 0.2271 0.4351 -0.0506 -0.0576 0.0469  96  PHE A N   
706  C  CA  . PHE A 96  ? 0.5159 0.2039 0.3938 -0.0447 -0.0531 0.0371  96  PHE A CA  
707  C  C   . PHE A 96  ? 0.5393 0.2385 0.4256 -0.0304 -0.0539 0.0391  96  PHE A C   
708  O  O   . PHE A 96  ? 0.5412 0.2440 0.4348 -0.0192 -0.0510 0.0301  96  PHE A O   
709  C  CB  . PHE A 96  ? 0.4992 0.2133 0.3742 -0.0564 -0.0505 0.0377  96  PHE A CB  
710  C  CG  . PHE A 96  ? 0.4871 0.2241 0.3680 -0.0524 -0.0457 0.0272  96  PHE A CG  
711  C  CD1 . PHE A 96  ? 0.4859 0.2176 0.3709 -0.0432 -0.0432 0.0168  96  PHE A CD1 
712  C  CD2 . PHE A 96  ? 0.4289 0.1930 0.3112 -0.0579 -0.0435 0.0279  96  PHE A CD2 
713  C  CE1 . PHE A 96  ? 0.4544 0.2068 0.3442 -0.0404 -0.0391 0.0088  96  PHE A CE1 
714  C  CE2 . PHE A 96  ? 0.4451 0.2283 0.3335 -0.0541 -0.0396 0.0193  96  PHE A CE2 
715  C  CZ  . PHE A 96  ? 0.4563 0.2334 0.3481 -0.0456 -0.0377 0.0106  96  PHE A CZ  
716  N  N   . TYR A 97  ? 0.5274 0.2340 0.4123 -0.0314 -0.0578 0.0511  97  TYR A N   
717  C  CA  . TYR A 97  ? 0.5416 0.2606 0.4342 -0.0193 -0.0596 0.0540  97  TYR A CA  
718  C  C   . TYR A 97  ? 0.5585 0.2581 0.4591 -0.0048 -0.0615 0.0516  97  TYR A C   
719  O  O   . TYR A 97  ? 0.5641 0.2755 0.4747 0.0068  -0.0593 0.0451  97  TYR A O   
720  C  CB  . TYR A 97  ? 0.5237 0.2495 0.4107 -0.0245 -0.0648 0.0685  97  TYR A CB  
721  C  CG  . TYR A 97  ? 0.5476 0.2830 0.4415 -0.0130 -0.0689 0.0739  97  TYR A CG  
722  C  CD1 . TYR A 97  ? 0.5292 0.2931 0.4285 -0.0097 -0.0667 0.0694  97  TYR A CD1 
723  C  CD2 . TYR A 97  ? 0.5869 0.3029 0.4826 -0.0055 -0.0755 0.0836  97  TYR A CD2 
724  C  CE1 . TYR A 97  ? 0.5294 0.3036 0.4353 -0.0002 -0.0710 0.0741  97  TYR A CE1 
725  C  CE2 . TYR A 97  ? 0.5881 0.3150 0.4910 0.0050  -0.0801 0.0890  97  TYR A CE2 
726  C  CZ  . TYR A 97  ? 0.5404 0.2970 0.4482 0.0072  -0.0779 0.0840  97  TYR A CZ  
727  O  OH  . TYR A 97  ? 0.5868 0.3553 0.5021 0.0168  -0.0830 0.0891  97  TYR A OH  
728  N  N   . GLN A 98  ? 0.5472 0.2170 0.4443 -0.0055 -0.0653 0.0566  98  GLN A N   
729  C  CA  . GLN A 98  ? 0.5986 0.2548 0.5066 0.0090  -0.0657 0.0535  98  GLN A CA  
730  C  C   . GLN A 98  ? 0.5575 0.2134 0.4713 0.0160  -0.0591 0.0369  98  GLN A C   
731  O  O   . GLN A 98  ? 0.5561 0.2154 0.4809 0.0301  -0.0576 0.0319  98  GLN A O   
732  C  CB  . GLN A 98  ? 0.6114 0.2468 0.5191 0.0059  -0.0675 0.0598  98  GLN A CB  
733  C  CG  . GLN A 98  ? 0.6707 0.3065 0.5720 -0.0012 -0.0737 0.0771  98  GLN A CG  
734  C  CD  . GLN A 98  ? 0.7268 0.3722 0.6347 0.0102  -0.0791 0.0864  98  GLN A CD  
735  O  OE1 . GLN A 98  ? 0.7680 0.4141 0.6882 0.0251  -0.0784 0.0809  98  GLN A OE1 
736  N  NE2 . GLN A 98  ? 0.7238 0.3789 0.6238 0.0028  -0.0843 0.1005  98  GLN A NE2 
737  N  N   . LEU A 99  ? 0.5606 0.2147 0.4671 0.0060  -0.0549 0.0284  99  LEU A N   
738  C  CA  . LEU A 99  ? 0.5672 0.2233 0.4770 0.0114  -0.0487 0.0130  99  LEU A CA  
739  C  C   . LEU A 99  ? 0.5991 0.2803 0.5138 0.0175  -0.0457 0.0086  99  LEU A C   
740  O  O   . LEU A 99  ? 0.5918 0.2769 0.5138 0.0280  -0.0415 -0.0007 99  LEU A O   
741  C  CB  . LEU A 99  ? 0.5483 0.2001 0.4491 -0.0017 -0.0458 0.0059  99  LEU A CB  
742  N  N   . THR A 100 ? 0.5338 0.2376 0.4469 0.0106  -0.0463 0.0148  100 THR A N   
743  C  CA  . THR A 100 ? 0.5166 0.2481 0.4368 0.0151  -0.0424 0.0104  100 THR A CA  
744  C  C   . THR A 100 ? 0.5257 0.2659 0.4573 0.0278  -0.0444 0.0140  100 THR A C   
745  O  O   . THR A 100 ? 0.4666 0.2272 0.4058 0.0328  -0.0409 0.0092  100 THR A O   
746  C  CB  . THR A 100 ? 0.4883 0.2408 0.4045 0.0044  -0.0423 0.0144  100 THR A CB  
747  O  OG1 . THR A 100 ? 0.5425 0.2961 0.4563 0.0012  -0.0476 0.0263  100 THR A OG1 
748  C  CG2 . THR A 100 ? 0.4981 0.2465 0.4053 -0.0079 -0.0404 0.0106  100 THR A CG2 
749  N  N   . ARG A 101 ? 0.5503 0.2763 0.4836 0.0326  -0.0503 0.0230  101 ARG A N   
750  C  CA  . ARG A 101 ? 0.5225 0.2586 0.4681 0.0453  -0.0529 0.0264  101 ARG A CA  
751  C  C   . ARG A 101 ? 0.5505 0.2924 0.5073 0.0570  -0.0472 0.0149  101 ARG A C   
752  O  O   . ARG A 101 ? 0.5558 0.3180 0.5236 0.0643  -0.0467 0.0147  101 ARG A O   
753  C  CB  . ARG A 101 ? 0.5840 0.3003 0.5309 0.0507  -0.0605 0.0375  101 ARG A CB  
754  C  CG  . ARG A 101 ? 0.5771 0.2882 0.5120 0.0385  -0.0661 0.0505  101 ARG A CG  
755  C  CD  . ARG A 101 ? 0.5592 0.2996 0.4933 0.0338  -0.0675 0.0557  101 ARG A CD  
756  N  NE  . ARG A 101 ? 0.5403 0.2955 0.4679 0.0226  -0.0618 0.0490  101 ARG A NE  
757  C  CZ  . ARG A 101 ? 0.5509 0.3326 0.4817 0.0211  -0.0592 0.0455  101 ARG A CZ  
758  N  NH1 . ARG A 101 ? 0.5119 0.3100 0.4512 0.0283  -0.0619 0.0481  101 ARG A NH1 
759  N  NH2 . ARG A 101 ? 0.5012 0.2932 0.4274 0.0120  -0.0542 0.0393  101 ARG A NH2 
760  N  N   . LYS A 102 ? 0.4935 0.2198 0.4475 0.0580  -0.0425 0.0048  102 LYS A N   
761  C  CA  . LYS A 102 ? 0.5125 0.2450 0.4760 0.0688  -0.0364 -0.0065 102 LYS A CA  
762  C  C   . LYS A 102 ? 0.5021 0.2577 0.4648 0.0642  -0.0297 -0.0140 102 LYS A C   
763  O  O   . LYS A 102 ? 0.4885 0.2567 0.4605 0.0725  -0.0247 -0.0210 102 LYS A O   
764  C  CB  . LYS A 102 ? 0.5160 0.2219 0.4765 0.0726  -0.0340 -0.0155 102 LYS A CB  
765  N  N   . ALA A 103 ? 0.4490 0.2111 0.4018 0.0514  -0.0295 -0.0124 103 ALA A N   
766  C  CA  . ALA A 103 ? 0.4156 0.1959 0.3672 0.0469  -0.0238 -0.0190 103 ALA A CA  
767  C  C   . ALA A 103 ? 0.4165 0.2213 0.3800 0.0527  -0.0220 -0.0182 103 ALA A C   
768  O  O   . ALA A 103 ? 0.4059 0.2195 0.3755 0.0546  -0.0264 -0.0107 103 ALA A O   
769  C  CB  . ALA A 103 ? 0.4420 0.2264 0.3835 0.0333  -0.0252 -0.0157 103 ALA A CB  
770  N  N   . VAL A 104 ? 0.3906 0.2070 0.3571 0.0547  -0.0156 -0.0260 104 VAL A N   
771  C  CA  . VAL A 104 ? 0.3885 0.2288 0.3657 0.0573  -0.0135 -0.0252 104 VAL A CA  
772  C  C   . VAL A 104 ? 0.3790 0.2314 0.3529 0.0474  -0.0154 -0.0205 104 VAL A C   
773  O  O   . VAL A 104 ? 0.3681 0.2350 0.3498 0.0478  -0.0177 -0.0161 104 VAL A O   
774  C  CB  . VAL A 104 ? 0.3999 0.2492 0.3802 0.0610  -0.0058 -0.0338 104 VAL A CB  
775  C  CG1 . VAL A 104 ? 0.3924 0.2659 0.3833 0.0613  -0.0035 -0.0322 104 VAL A CG1 
776  C  CG2 . VAL A 104 ? 0.3773 0.2169 0.3629 0.0722  -0.0032 -0.0398 104 VAL A CG2 
777  N  N   . THR A 105 ? 0.3826 0.2298 0.3458 0.0385  -0.0146 -0.0220 105 THR A N   
778  C  CA  . THR A 105 ? 0.3626 0.2199 0.3233 0.0297  -0.0164 -0.0182 105 THR A CA  
779  C  C   . THR A 105 ? 0.3566 0.2124 0.3168 0.0276  -0.0222 -0.0109 105 THR A C   
780  O  O   . THR A 105 ? 0.4096 0.2499 0.3652 0.0285  -0.0255 -0.0076 105 THR A O   
781  C  CB  . THR A 105 ? 0.3661 0.2170 0.3159 0.0212  -0.0154 -0.0209 105 THR A CB  
782  O  OG1 . THR A 105 ? 0.3652 0.2173 0.3133 0.0229  -0.0104 -0.0275 105 THR A OG1 
783  C  CG2 . THR A 105 ? 0.3414 0.2055 0.2915 0.0137  -0.0164 -0.0180 105 THR A CG2 
784  N  N   . GLU A 106 ? 0.3380 0.2098 0.3025 0.0244  -0.0233 -0.0083 106 GLU A N   
785  C  CA  . GLU A 106 ? 0.3528 0.2262 0.3141 0.0200  -0.0281 -0.0021 106 GLU A CA  
786  C  C   . GLU A 106 ? 0.3392 0.2057 0.2899 0.0104  -0.0284 -0.0012 106 GLU A C   
787  O  O   . GLU A 106 ? 0.3407 0.2147 0.2909 0.0055  -0.0257 -0.0046 106 GLU A O   
788  C  CB  . GLU A 106 ? 0.3716 0.2646 0.3402 0.0188  -0.0286 -0.0018 106 GLU A CB  
789  C  CG  . GLU A 106 ? 0.3799 0.2767 0.3446 0.0150  -0.0335 0.0041  106 GLU A CG  
790  C  CD  . GLU A 106 ? 0.4096 0.3099 0.3803 0.0219  -0.0377 0.0082  106 GLU A CD  
791  O  OE1 . GLU A 106 ? 0.4355 0.3490 0.4168 0.0261  -0.0368 0.0054  106 GLU A OE1 
792  O  OE2 . GLU A 106 ? 0.4403 0.3299 0.4058 0.0231  -0.0421 0.0147  106 GLU A OE2 
793  N  N   . VAL A 107 ? 0.3304 0.1834 0.2736 0.0076  -0.0320 0.0039  107 VAL A N   
794  C  CA  . VAL A 107 ? 0.3992 0.2446 0.3326 -0.0021 -0.0323 0.0051  107 VAL A CA  
795  C  C   . VAL A 107 ? 0.3727 0.2243 0.3018 -0.0085 -0.0356 0.0122  107 VAL A C   
796  O  O   . VAL A 107 ? 0.3664 0.2128 0.2942 -0.0060 -0.0397 0.0188  107 VAL A O   
797  C  CB  . VAL A 107 ? 0.3397 0.1617 0.2666 -0.0020 -0.0332 0.0049  107 VAL A CB  
798  C  CG1 . VAL A 107 ? 0.3613 0.1774 0.2790 -0.0137 -0.0335 0.0057  107 VAL A CG1 
799  C  CG2 . VAL A 107 ? 0.3862 0.2034 0.3166 0.0050  -0.0294 -0.0031 107 VAL A CG2 
800  N  N   . TYR A 108 ? 0.3247 0.1885 0.2520 -0.0166 -0.0339 0.0108  108 TYR A N   
801  C  CA  . TYR A 108 ? 0.3209 0.1914 0.2423 -0.0246 -0.0357 0.0164  108 TYR A CA  
802  C  C   . TYR A 108 ? 0.3210 0.1869 0.2358 -0.0345 -0.0345 0.0163  108 TYR A C   
803  O  O   . TYR A 108 ? 0.3309 0.1933 0.2470 -0.0351 -0.0323 0.0109  108 TYR A O   
804  C  CB  . TYR A 108 ? 0.3360 0.2291 0.2626 -0.0254 -0.0342 0.0136  108 TYR A CB  
805  C  CG  . TYR A 108 ? 0.3467 0.2470 0.2805 -0.0172 -0.0356 0.0130  108 TYR A CG  
806  C  CD1 . TYR A 108 ? 0.3617 0.2613 0.2925 -0.0154 -0.0402 0.0197  108 TYR A CD1 
807  C  CD2 . TYR A 108 ? 0.3466 0.2554 0.2906 -0.0119 -0.0328 0.0063  108 TYR A CD2 
808  C  CE1 . TYR A 108 ? 0.4055 0.3138 0.3438 -0.0085 -0.0420 0.0190  108 TYR A CE1 
809  C  CE2 . TYR A 108 ? 0.3602 0.2767 0.3117 -0.0056 -0.0341 0.0055  108 TYR A CE2 
810  C  CZ  . TYR A 108 ? 0.3712 0.2881 0.3202 -0.0038 -0.0388 0.0115  108 TYR A CZ  
811  O  OH  . TYR A 108 ? 0.3993 0.3259 0.3566 0.0019  -0.0407 0.0107  108 TYR A OH  
812  N  N   . ALA A 109 ? 0.3442 0.2120 0.2518 -0.0431 -0.0360 0.0226  109 ALA A N   
813  C  CA  . ALA A 109 ? 0.3746 0.2396 0.2767 -0.0538 -0.0350 0.0232  109 ALA A CA  
814  C  C   . ALA A 109 ? 0.3625 0.2484 0.2636 -0.0622 -0.0331 0.0244  109 ALA A C   
815  O  O   . ALA A 109 ? 0.3705 0.2653 0.2689 -0.0627 -0.0341 0.0287  109 ALA A O   
816  C  CB  . ALA A 109 ? 0.3746 0.2162 0.2677 -0.0584 -0.0385 0.0305  109 ALA A CB  
817  N  N   . LEU A 110 ? 0.3617 0.2568 0.2651 -0.0685 -0.0302 0.0200  110 LEU A N   
818  C  CA  . LEU A 110 ? 0.3352 0.2474 0.2368 -0.0786 -0.0280 0.0216  110 LEU A CA  
819  C  C   . LEU A 110 ? 0.3681 0.2664 0.2599 -0.0896 -0.0300 0.0291  110 LEU A C   
820  O  O   . LEU A 110 ? 0.3864 0.2691 0.2770 -0.0917 -0.0312 0.0280  110 LEU A O   
821  C  CB  . LEU A 110 ? 0.3589 0.2882 0.2699 -0.0796 -0.0245 0.0136  110 LEU A CB  
822  C  CG  . LEU A 110 ? 0.3368 0.2789 0.2586 -0.0698 -0.0226 0.0063  110 LEU A CG  
823  C  CD1 . LEU A 110 ? 0.3099 0.2682 0.2412 -0.0714 -0.0199 0.0002  110 LEU A CD1 
824  C  CD2 . LEU A 110 ? 0.3386 0.2927 0.2602 -0.0677 -0.0218 0.0067  110 LEU A CD2 
825  N  N   . LEU A 111 ? 0.3183 0.2217 0.2024 -0.0972 -0.0304 0.0370  111 LEU A N   
826  C  CA  . LEU A 111 ? 0.3703 0.2599 0.2450 -0.1090 -0.0324 0.0458  111 LEU A CA  
827  C  C   . LEU A 111 ? 0.3921 0.2978 0.2691 -0.1208 -0.0287 0.0431  111 LEU A C   
828  O  O   . LEU A 111 ? 0.3648 0.2966 0.2455 -0.1236 -0.0246 0.0402  111 LEU A O   
829  C  CB  . LEU A 111 ? 0.3875 0.2759 0.2520 -0.1131 -0.0348 0.0572  111 LEU A CB  
830  C  CG  . LEU A 111 ? 0.4101 0.2766 0.2643 -0.1236 -0.0383 0.0687  111 LEU A CG  
831  C  CD1 . LEU A 111 ? 0.4448 0.2797 0.2985 -0.1150 -0.0433 0.0707  111 LEU A CD1 
832  C  CD2 . LEU A 111 ? 0.4394 0.3134 0.2827 -0.1314 -0.0396 0.0809  111 LEU A CD2 
833  N  N   . ASN A 112 ? 0.3818 0.2729 0.2575 -0.1274 -0.0301 0.0431  112 ASN A N   
834  C  CA  . ASN A 112 ? 0.3829 0.2890 0.2610 -0.1401 -0.0275 0.0419  112 ASN A CA  
835  C  C   . ASN A 112 ? 0.4521 0.3686 0.3226 -0.1526 -0.0259 0.0513  112 ASN A C   
836  O  O   . ASN A 112 ? 0.4273 0.3262 0.2873 -0.1560 -0.0291 0.0617  112 ASN A O   
837  C  CB  . ASN A 112 ? 0.4317 0.3168 0.3079 -0.1460 -0.0304 0.0409  112 ASN A CB  
838  C  CG  . ASN A 112 ? 0.4620 0.3659 0.3452 -0.1556 -0.0282 0.0358  112 ASN A CG  
839  O  OD1 . ASN A 112 ? 0.4363 0.3624 0.3215 -0.1652 -0.0250 0.0382  112 ASN A OD1 
840  N  ND2 . ASN A 112 ? 0.4430 0.3399 0.3302 -0.1527 -0.0299 0.0284  112 ASN A ND2 
841  N  N   . ILE A 113 ? 0.4274 0.3737 0.3036 -0.1591 -0.0209 0.0480  113 ILE A N   
842  C  CA  . ILE A 113 ? 0.4598 0.4194 0.3284 -0.1722 -0.0184 0.0565  113 ILE A CA  
843  C  C   . ILE A 113 ? 0.4546 0.3968 0.3153 -0.1875 -0.0209 0.0658  113 ILE A C   
844  O  O   . ILE A 113 ? 0.4894 0.4327 0.3401 -0.1988 -0.0205 0.0767  113 ILE A O   
845  C  CB  . ILE A 113 ? 0.4504 0.4478 0.3282 -0.1755 -0.0116 0.0495  113 ILE A CB  
846  C  CG1 . ILE A 113 ? 0.4348 0.4424 0.3234 -0.1820 -0.0102 0.0438  113 ILE A CG1 
847  C  CG2 . ILE A 113 ? 0.3781 0.3899 0.2638 -0.1606 -0.0094 0.0399  113 ILE A CG2 
848  C  CD1 . ILE A 113 ? 0.4192 0.4649 0.3190 -0.1852 -0.0035 0.0372  113 ILE A CD1 
849  N  N   . SER A 114 ? 0.4694 0.3949 0.3338 -0.1888 -0.0237 0.0620  114 SER A N   
850  C  CA  . SER A 114 ? 0.4857 0.3904 0.3431 -0.2032 -0.0267 0.0696  114 SER A CA  
851  C  C   . SER A 114 ? 0.5177 0.3835 0.3661 -0.1974 -0.0327 0.0757  114 SER A C   
852  O  O   . SER A 114 ? 0.4787 0.3304 0.3305 -0.1834 -0.0349 0.0687  114 SER A O   
853  C  CB  . SER A 114 ? 0.5173 0.4254 0.3832 -0.2085 -0.0269 0.0612  114 SER A CB  
854  O  OG  . SER A 114 ? 0.5086 0.3954 0.3698 -0.2142 -0.0305 0.0647  114 SER A OG  
855  N  N   . ARG A 115 ? 0.5148 0.3684 0.3554 -0.2027 -0.0351 0.0863  115 ARG A N   
856  C  CA  . ARG A 115 ? 0.5120 0.3321 0.3467 -0.1946 -0.0408 0.0923  115 ARG A CA  
857  C  C   . ARG A 115 ? 0.5483 0.3432 0.3873 -0.1876 -0.0436 0.0834  115 ARG A C   
858  O  O   . ARG A 115 ? 0.5994 0.3720 0.4377 -0.1753 -0.0469 0.0831  115 ARG A O   
859  C  CB  . ARG A 115 ? 0.5768 0.3887 0.4048 -0.2035 -0.0429 0.1043  115 ARG A CB  
860  N  N   . VAL A 116 ? 0.4974 0.2975 0.3414 -0.1945 -0.0423 0.0758  116 VAL A N   
861  C  CA  . VAL A 116 ? 0.5552 0.3326 0.4018 -0.1891 -0.0448 0.0671  116 VAL A CA  
862  C  C   . VAL A 116 ? 0.5508 0.3323 0.4025 -0.1789 -0.0439 0.0554  116 VAL A C   
863  O  O   . VAL A 116 ? 0.5739 0.3373 0.4267 -0.1727 -0.0456 0.0475  116 VAL A O   
864  C  CB  . VAL A 116 ? 0.5415 0.3211 0.3902 -0.2014 -0.0447 0.0642  116 VAL A CB  
865  C  CG1 . VAL A 116 ? 0.5685 0.3370 0.4119 -0.2108 -0.0463 0.0757  116 VAL A CG1 
866  C  CG2 . VAL A 116 ? 0.5464 0.3605 0.4012 -0.2095 -0.0409 0.0597  116 VAL A CG2 
867  N  N   . GLY A 117 ? 0.5091 0.3141 0.3641 -0.1772 -0.0410 0.0536  117 GLY A N   
868  C  CA  . GLY A 117 ? 0.5183 0.3282 0.3793 -0.1649 -0.0402 0.0430  117 GLY A CA  
869  C  C   . GLY A 117 ? 0.5139 0.3297 0.3794 -0.1695 -0.0403 0.0330  117 GLY A C   
870  O  O   . GLY A 117 ? 0.5203 0.3537 0.3892 -0.1808 -0.0391 0.0329  117 GLY A O   
871  N  N   . LEU A 118 ? 0.4844 0.2897 0.3512 -0.1586 -0.0413 0.0240  118 LEU A N   
872  C  CA  . LEU A 118 ? 0.5358 0.3460 0.4054 -0.1617 -0.0420 0.0146  118 LEU A CA  
873  C  C   . LEU A 118 ? 0.5975 0.3842 0.4625 -0.1634 -0.0442 0.0119  118 LEU A C   
874  O  O   . LEU A 118 ? 0.5987 0.3834 0.4640 -0.1615 -0.0449 0.0026  118 LEU A O   
875  C  CB  . LEU A 118 ? 0.4808 0.2998 0.3553 -0.1478 -0.0409 0.0062  118 LEU A CB  
876  C  CG  . LEU A 118 ? 0.4604 0.3102 0.3445 -0.1410 -0.0376 0.0070  118 LEU A CG  
877  C  CD1 . LEU A 118 ? 0.4437 0.3019 0.3332 -0.1280 -0.0368 -0.0004 118 LEU A CD1 
878  C  CD2 . LEU A 118 ? 0.4578 0.3341 0.3482 -0.1529 -0.0365 0.0085  118 LEU A CD2 
879  N  N   . ILE A 119 ? 0.5828 0.3520 0.4435 -0.1672 -0.0453 0.0197  119 ILE A N   
880  C  CA  . ILE A 119 ? 0.6492 0.3975 0.5073 -0.1712 -0.0472 0.0172  119 ILE A CA  
881  C  C   . ILE A 119 ? 0.6958 0.4598 0.5566 -0.1833 -0.0474 0.0128  119 ILE A C   
882  O  O   . ILE A 119 ? 0.6312 0.3840 0.4910 -0.1848 -0.0489 0.0051  119 ILE A O   
883  C  CB  . ILE A 119 ? 0.6161 0.3462 0.4706 -0.1747 -0.0486 0.0283  119 ILE A CB  
884  N  N   . ALA A 120 ? 0.6666 0.4580 0.5315 -0.1921 -0.0459 0.0171  120 ALA A N   
885  C  CA  . ALA A 120 ? 0.6833 0.4960 0.5532 -0.2024 -0.0461 0.0132  120 ALA A CA  
886  C  C   . ALA A 120 ? 0.6781 0.5222 0.5558 -0.1996 -0.0443 0.0102  120 ALA A C   
887  O  O   . ALA A 120 ? 0.6397 0.4908 0.5188 -0.1931 -0.0423 0.0130  120 ALA A O   
888  C  CB  . ALA A 120 ? 0.6302 0.4491 0.5004 -0.2166 -0.0457 0.0213  120 ALA A CB  
889  N  N   . GLN A 121 ? 0.7195 0.5828 0.6032 -0.2046 -0.0452 0.0045  121 GLN A N   
890  C  CA  . GLN A 121 ? 0.6605 0.5550 0.5541 -0.2018 -0.0442 0.0017  121 GLN A CA  
891  C  C   . GLN A 121 ? 0.5987 0.5220 0.5007 -0.2097 -0.0411 0.0074  121 GLN A C   
892  O  O   . GLN A 121 ? 0.5759 0.5268 0.4885 -0.2065 -0.0397 0.0053  121 GLN A O   
893  C  CB  . GLN A 121 ? 0.6711 0.5753 0.5680 -0.2024 -0.0472 -0.0064 121 GLN A CB  
894  N  N   . ASN A 122 ? 0.6044 0.5229 0.5027 -0.2196 -0.0399 0.0145  122 ASN A N   
895  C  CA  . ASN A 122 ? 0.5811 0.5279 0.4864 -0.2277 -0.0362 0.0198  122 ASN A CA  
896  C  C   . ASN A 122 ? 0.5407 0.4789 0.4387 -0.2292 -0.0334 0.0289  122 ASN A C   
897  O  O   . ASN A 122 ? 0.5230 0.4653 0.4186 -0.2396 -0.0319 0.0358  122 ASN A O   
898  C  CB  . ASN A 122 ? 0.5114 0.4669 0.4196 -0.2406 -0.0372 0.0202  122 ASN A CB  
899  C  CG  . ASN A 122 ? 0.5740 0.4989 0.4711 -0.2479 -0.0393 0.0249  122 ASN A CG  
900  O  OD1 . ASN A 122 ? 0.6403 0.5344 0.5292 -0.2418 -0.0419 0.0233  122 ASN A OD1 
901  N  ND2 . ASN A 122 ? 0.5485 0.4822 0.4467 -0.2608 -0.0382 0.0302  122 ASN A ND2 
902  N  N   . GLU A 123 ? 0.5441 0.4716 0.4384 -0.2189 -0.0330 0.0295  123 GLU A N   
903  C  CA  . GLU A 123 ? 0.5032 0.4160 0.3881 -0.2190 -0.0320 0.0387  123 GLU A CA  
904  C  C   . GLU A 123 ? 0.5070 0.4479 0.3946 -0.2257 -0.0270 0.0446  123 GLU A C   
905  O  O   . GLU A 123 ? 0.4927 0.4247 0.3714 -0.2293 -0.0264 0.0539  123 GLU A O   
906  C  CB  . GLU A 123 ? 0.5191 0.4142 0.4001 -0.2059 -0.0331 0.0373  123 GLU A CB  
907  C  CG  . GLU A 123 ? 0.4809 0.4007 0.3695 -0.1987 -0.0296 0.0342  123 GLU A CG  
908  C  CD  . GLU A 123 ? 0.4952 0.4240 0.3930 -0.1879 -0.0305 0.0236  123 GLU A CD  
909  O  OE1 . GLU A 123 ? 0.5090 0.4322 0.4075 -0.1937 -0.0336 0.0191  123 GLU A OE1 
910  O  OE2 . GLU A 123 ? 0.4215 0.3625 0.3254 -0.1742 -0.0283 0.0199  123 GLU A OE2 
911  N  N   . LEU A 124 ? 0.4654 0.4409 0.3653 -0.2269 -0.0233 0.0394  124 LEU A N   
912  C  CA  . LEU A 124 ? 0.4681 0.4737 0.3717 -0.2328 -0.0175 0.0430  124 LEU A CA  
913  C  C   . LEU A 124 ? 0.5510 0.5734 0.4584 -0.2452 -0.0161 0.0449  124 LEU A C   
914  O  O   . LEU A 124 ? 0.5190 0.5692 0.4302 -0.2504 -0.0108 0.0468  124 LEU A O   
915  C  CB  . LEU A 124 ? 0.4736 0.5093 0.3907 -0.2250 -0.0134 0.0354  124 LEU A CB  
916  C  CG  . LEU A 124 ? 0.4674 0.4917 0.3825 -0.2091 -0.0139 0.0324  124 LEU A CG  
917  C  CD1 . LEU A 124 ? 0.4097 0.4646 0.3394 -0.1973 -0.0096 0.0238  124 LEU A CD1 
918  C  CD2 . LEU A 124 ? 0.4511 0.4585 0.3518 -0.2090 -0.0135 0.0413  124 LEU A CD2 
919  N  N   . ALA A 125 ? 0.5127 0.5195 0.4190 -0.2501 -0.0205 0.0438  125 ALA A N   
920  C  CA  . ALA A 125 ? 0.5569 0.5798 0.4675 -0.2624 -0.0195 0.0452  125 ALA A CA  
921  C  C   . ALA A 125 ? 0.5644 0.5820 0.4650 -0.2729 -0.0178 0.0558  125 ALA A C   
922  O  O   . ALA A 125 ? 0.5861 0.6282 0.4912 -0.2827 -0.0143 0.0579  125 ALA A O   
923  C  CB  . ALA A 125 ? 0.5194 0.5253 0.4304 -0.2655 -0.0249 0.0411  125 ALA A CB  
924  N  N   . ASN A 126 ? 0.5725 0.5594 0.4601 -0.2708 -0.0205 0.0627  126 ASN A N   
925  C  CA  . ASN A 126 ? 0.6451 0.6243 0.5224 -0.2797 -0.0199 0.0741  126 ASN A CA  
926  C  C   . ASN A 126 ? 0.5968 0.5869 0.4691 -0.2745 -0.0164 0.0784  126 ASN A C   
927  O  O   . ASN A 126 ? 0.5949 0.5679 0.4628 -0.2638 -0.0183 0.0783  126 ASN A O   
928  C  CB  . ASN A 126 ? 0.6209 0.5581 0.4882 -0.2805 -0.0259 0.0796  126 ASN A CB  
929  C  CG  . ASN A 126 ? 0.6842 0.6135 0.5429 -0.2917 -0.0262 0.0918  126 ASN A CG  
930  O  OD1 . ASN A 126 ? 0.6655 0.6152 0.5212 -0.2959 -0.0224 0.0981  126 ASN A OD1 
931  N  ND2 . ASN A 126 ? 0.7277 0.6275 0.5825 -0.2968 -0.0307 0.0950  126 ASN A ND2 
932  N  N   . LEU A 127 ? 0.6164 0.6359 0.4895 -0.2820 -0.0110 0.0817  127 LEU A N   
933  C  CA  . LEU A 127 ? 0.5861 0.6187 0.4537 -0.2779 -0.0073 0.0851  127 LEU A CA  
934  C  C   . LEU A 127 ? 0.5912 0.5931 0.4436 -0.2769 -0.0118 0.0965  127 LEU A C   
935  O  O   . LEU A 127 ? 0.6076 0.6092 0.4547 -0.2691 -0.0112 0.0983  127 LEU A O   
936  C  CB  . LEU A 127 ? 0.6211 0.6914 0.4919 -0.2867 -0.0005 0.0856  127 LEU A CB  
937  C  CG  . LEU A 127 ? 0.5981 0.7055 0.4857 -0.2829 0.0054  0.0733  127 LEU A CG  
938  C  CD1 . LEU A 127 ? 0.5333 0.6753 0.4247 -0.2927 0.0117  0.0736  127 LEU A CD1 
939  C  CD2 . LEU A 127 ? 0.5595 0.6765 0.4506 -0.2698 0.0083  0.0664  127 LEU A CD2 
940  N  N   . ALA A 128 ? 0.5882 0.5642 0.4344 -0.2841 -0.0165 0.1043  128 ALA A N   
941  C  CA  . ALA A 128 ? 0.6398 0.5866 0.4736 -0.2822 -0.0212 0.1158  128 ALA A CA  
942  C  C   . ALA A 128 ? 0.6173 0.5391 0.4495 -0.2672 -0.0253 0.1131  128 ALA A C   
943  O  O   . ALA A 128 ? 0.6150 0.5231 0.4387 -0.2618 -0.0279 0.1212  128 ALA A O   
944  C  CB  . ALA A 128 ? 0.6722 0.5940 0.5024 -0.2919 -0.0255 0.1232  128 ALA A CB  
945  N  N   . ASN A 129 ? 0.6182 0.5347 0.4587 -0.2602 -0.0260 0.1021  129 ASN A N   
946  C  CA  . ASN A 129 ? 0.5954 0.4899 0.4350 -0.2460 -0.0293 0.0987  129 ASN A CA  
947  C  C   . ASN A 129 ? 0.5687 0.4832 0.4089 -0.2381 -0.0258 0.0963  129 ASN A C   
948  O  O   . ASN A 129 ? 0.5571 0.4540 0.3938 -0.2269 -0.0287 0.0971  129 ASN A O   
949  C  CB  . ASN A 129 ? 0.6352 0.5189 0.4828 -0.2414 -0.0310 0.0874  129 ASN A CB  
950  C  CG  . ASN A 129 ? 0.6554 0.5131 0.5014 -0.2468 -0.0351 0.0887  129 ASN A CG  
951  O  OD1 . ASN A 129 ? 0.6679 0.5312 0.5201 -0.2521 -0.0349 0.0816  129 ASN A OD1 
952  N  ND2 . ASN A 129 ? 0.7121 0.5421 0.5503 -0.2458 -0.0390 0.0979  129 ASN A ND2 
953  N  N   . ILE A 130 ? 0.5658 0.5170 0.4112 -0.2430 -0.0195 0.0925  130 ILE A N   
954  C  CA  . ILE A 130 ? 0.5624 0.5349 0.4087 -0.2363 -0.0152 0.0892  130 ILE A CA  
955  C  C   . ILE A 130 ? 0.5888 0.5640 0.4228 -0.2389 -0.0153 0.1002  130 ILE A C   
956  O  O   . ILE A 130 ? 0.5714 0.5751 0.4043 -0.2465 -0.0102 0.1013  130 ILE A O   
957  C  CB  . ILE A 130 ? 0.5443 0.5561 0.4036 -0.2389 -0.0080 0.0789  130 ILE A CB  
958  C  CG1 . ILE A 130 ? 0.5312 0.5406 0.4028 -0.2378 -0.0095 0.0697  130 ILE A CG1 
959  C  CG2 . ILE A 130 ? 0.5260 0.5567 0.3882 -0.2303 -0.0035 0.0733  130 ILE A CG2 
960  C  CD1 . ILE A 130 ? 0.5364 0.5820 0.4214 -0.2433 -0.0041 0.0626  130 ILE A CD1 
961  N  N   . ASP A 131 ? 0.6004 0.5467 0.4255 -0.2321 -0.0213 0.1079  131 ASP A N   
962  C  CA  . ASP A 131 ? 0.5746 0.5169 0.3878 -0.2346 -0.0238 0.1204  131 ASP A CA  
963  C  C   . ASP A 131 ? 0.5599 0.5098 0.3681 -0.2247 -0.0236 0.1206  131 ASP A C   
964  O  O   . ASP A 131 ? 0.5219 0.4521 0.3309 -0.2132 -0.0275 0.1189  131 ASP A O   
965  C  CB  . ASP A 131 ? 0.5525 0.4565 0.3609 -0.2337 -0.0314 0.1298  131 ASP A CB  
966  C  CG  . ASP A 131 ? 0.6407 0.5398 0.4380 -0.2366 -0.0347 0.1440  131 ASP A CG  
967  O  OD1 . ASP A 131 ? 0.6991 0.5712 0.4935 -0.2388 -0.0399 0.1527  131 ASP A OD1 
968  O  OD2 . ASP A 131 ? 0.6216 0.5434 0.4133 -0.2363 -0.0323 0.1462  131 ASP A OD2 
969  N  N   . ALA A 132 ? 0.5641 0.5426 0.3670 -0.2292 -0.0194 0.1224  132 ALA A N   
970  C  CA  . ALA A 132 ? 0.5744 0.5651 0.3724 -0.2206 -0.0187 0.1207  132 ALA A CA  
971  C  C   . ALA A 132 ? 0.5721 0.5370 0.3607 -0.2135 -0.0272 0.1323  132 ALA A C   
972  O  O   . ALA A 132 ? 0.5178 0.4763 0.3057 -0.2020 -0.0299 0.1302  132 ALA A O   
973  C  CB  . ALA A 132 ? 0.5493 0.5783 0.3442 -0.2273 -0.0119 0.1178  132 ALA A CB  
974  N  N   . GLU A 133 ? 0.5731 0.5236 0.3554 -0.2199 -0.0317 0.1447  133 GLU A N   
975  C  CA  . GLU A 133 ? 0.5772 0.5061 0.3522 -0.2128 -0.0397 0.1563  133 GLU A CA  
976  C  C   . GLU A 133 ? 0.5804 0.4751 0.3612 -0.2005 -0.0456 0.1553  133 GLU A C   
977  O  O   . GLU A 133 ? 0.5996 0.4838 0.3785 -0.1891 -0.0509 0.1588  133 GLU A O   
978  C  CB  . GLU A 133 ? 0.6421 0.5633 0.4100 -0.2229 -0.0427 0.1700  133 GLU A CB  
979  N  N   . ALA A 134 ? 0.5721 0.4505 0.3606 -0.2023 -0.0449 0.1498  134 ALA A N   
980  C  CA  . ALA A 134 ? 0.5453 0.3931 0.3401 -0.1903 -0.0494 0.1462  134 ALA A CA  
981  C  C   . ALA A 134 ? 0.5285 0.3840 0.3264 -0.1790 -0.0483 0.1375  134 ALA A C   
982  O  O   . ALA A 134 ? 0.5464 0.3829 0.3459 -0.1661 -0.0536 0.1387  134 ALA A O   
983  C  CB  . ALA A 134 ? 0.5770 0.4116 0.3790 -0.1953 -0.0478 0.1391  134 ALA A CB  
984  N  N   . VAL A 135 ? 0.4832 0.3676 0.2830 -0.1832 -0.0414 0.1288  135 VAL A N   
985  C  CA  . VAL A 135 ? 0.4937 0.3904 0.3032 -0.1680 -0.0397 0.1153  135 VAL A CA  
986  C  C   . VAL A 135 ? 0.4921 0.3993 0.2953 -0.1610 -0.0425 0.1197  135 VAL A C   
987  O  O   . VAL A 135 ? 0.5083 0.4100 0.3179 -0.1462 -0.0454 0.1142  135 VAL A O   
988  C  CB  . VAL A 135 ? 0.4978 0.4240 0.3172 -0.1704 -0.0316 0.1010  135 VAL A CB  
989  C  CG1 . VAL A 135 ? 0.5073 0.4505 0.3356 -0.1558 -0.0296 0.0882  135 VAL A CG1 
990  C  CG2 . VAL A 135 ? 0.4831 0.3950 0.3110 -0.1724 -0.0311 0.0950  135 VAL A CG2 
991  N  N   . LYS A 136 ? 0.5187 0.4422 0.3091 -0.1721 -0.0416 0.1296  136 LYS A N   
992  C  CA  . LYS A 136 ? 0.4776 0.4099 0.2598 -0.1669 -0.0456 0.1354  136 LYS A CA  
993  C  C   . LYS A 136 ? 0.5156 0.4166 0.2964 -0.1572 -0.0553 0.1461  136 LYS A C   
994  O  O   . LYS A 136 ? 0.5472 0.4492 0.3326 -0.1437 -0.0590 0.1423  136 LYS A O   
995  C  CB  . LYS A 136 ? 0.5882 0.5421 0.3594 -0.1793 -0.0435 0.1432  136 LYS A CB  
996  N  N   . GLN A 137 ? 0.5324 0.4085 0.3139 -0.1604 -0.0588 0.1546  137 GLN A N   
997  C  CA  . GLN A 137 ? 0.5305 0.3775 0.3147 -0.1493 -0.0672 0.1625  137 GLN A CA  
998  C  C   . GLN A 137 ? 0.5179 0.3478 0.3116 -0.1357 -0.0689 0.1538  137 GLN A C   
999  O  O   . GLN A 137 ? 0.5261 0.3477 0.3227 -0.1229 -0.0748 0.1563  137 GLN A O   
1000 C  CB  . GLN A 137 ? 0.5667 0.3906 0.3513 -0.1554 -0.0693 0.1707  137 GLN A CB  
1001 N  N   . ALA A 138 ? 0.5395 0.3670 0.3407 -0.1372 -0.0635 0.1416  138 ALA A N   
1002 C  CA  . ALA A 138 ? 0.5319 0.3493 0.3469 -0.1220 -0.0632 0.1285  138 ALA A CA  
1003 C  C   . ALA A 138 ? 0.5298 0.3698 0.3513 -0.1102 -0.0622 0.1196  138 ALA A C   
1004 O  O   . ALA A 138 ? 0.5118 0.3418 0.3410 -0.0961 -0.0657 0.1168  138 ALA A O   
1005 C  CB  . ALA A 138 ? 0.5008 0.3185 0.3229 -0.1264 -0.0572 0.1160  138 ALA A CB  
1006 N  N   . VAL A 139 ? 0.4762 0.3472 0.2954 -0.1159 -0.0571 0.1145  139 VAL A N   
1007 C  CA  . VAL A 139 ? 0.4732 0.3662 0.2984 -0.1064 -0.0559 0.1052  139 VAL A CA  
1008 C  C   . VAL A 139 ? 0.4942 0.3849 0.3143 -0.1001 -0.0634 0.1153  139 VAL A C   
1009 O  O   . VAL A 139 ? 0.5172 0.4088 0.3463 -0.0873 -0.0659 0.1098  139 VAL A O   
1010 C  CB  . VAL A 139 ? 0.5011 0.4264 0.3241 -0.1149 -0.0488 0.0977  139 VAL A CB  
1011 C  CG1 . VAL A 139 ? 0.4656 0.4128 0.2906 -0.1078 -0.0489 0.0911  139 VAL A CG1 
1012 C  CG2 . VAL A 139 ? 0.4406 0.3709 0.2742 -0.1161 -0.0419 0.0847  139 VAL A CG2 
1013 N  N   . GLN A 140 ? 0.5271 0.4160 0.3329 -0.1095 -0.0676 0.1309  140 GLN A N   
1014 C  CA  . GLN A 140 ? 0.5487 0.4351 0.3492 -0.1039 -0.0762 0.1427  140 GLN A CA  
1015 C  C   . GLN A 140 ? 0.5724 0.4299 0.3827 -0.0903 -0.0826 0.1460  140 GLN A C   
1016 O  O   . GLN A 140 ? 0.5800 0.4399 0.3948 -0.0793 -0.0883 0.1479  140 GLN A O   
1017 C  CB  . GLN A 140 ? 0.5865 0.4732 0.3691 -0.1175 -0.0798 0.1609  140 GLN A CB  
1018 C  CG  . GLN A 140 ? 0.5820 0.5027 0.3538 -0.1295 -0.0740 0.1578  140 GLN A CG  
1019 C  CD  . GLN A 140 ? 0.6567 0.6030 0.4302 -0.1221 -0.0747 0.1493  140 GLN A CD  
1020 O  OE1 . GLN A 140 ? 0.6824 0.6303 0.4502 -0.1182 -0.0827 0.1591  140 GLN A OE1 
1021 N  NE2 . GLN A 140 ? 0.6195 0.5853 0.4023 -0.1196 -0.0669 0.1306  140 GLN A NE2 
1022 N  N   . ARG A 141 ? 0.5563 0.3877 0.3706 -0.0908 -0.0814 0.1454  141 ARG A N   
1023 C  CA  . ARG A 141 ? 0.5722 0.3745 0.3953 -0.0782 -0.0867 0.1479  141 ARG A CA  
1024 C  C   . ARG A 141 ? 0.5563 0.3643 0.3952 -0.0635 -0.0840 0.1321  141 ARG A C   
1025 O  O   . ARG A 141 ? 0.5375 0.3351 0.3847 -0.0502 -0.0891 0.1338  141 ARG A O   
1026 C  CB  . ARG A 141 ? 0.5767 0.3500 0.3984 -0.0847 -0.0857 0.1502  141 ARG A CB  
1027 C  CG  . ARG A 141 ? 0.6576 0.4063 0.4824 -0.0792 -0.0913 0.1602  141 ARG A CG  
1028 C  CD  . ARG A 141 ? 0.6586 0.3909 0.4810 -0.0900 -0.0885 0.1619  141 ARG A CD  
1029 N  NE  . ARG A 141 ? 0.6417 0.3693 0.4671 -0.0945 -0.0824 0.1489  141 ARG A NE  
1030 C  CZ  . ARG A 141 ? 0.6189 0.3560 0.4384 -0.1097 -0.0774 0.1469  141 ARG A CZ  
1031 N  NH1 . ARG A 141 ? 0.5968 0.3495 0.4070 -0.1221 -0.0768 0.1563  141 ARG A NH1 
1032 N  NH2 . ARG A 141 ? 0.6185 0.3510 0.4422 -0.1123 -0.0727 0.1348  141 ARG A NH2 
1033 N  N   . HIS A 142 ? 0.5229 0.3476 0.3667 -0.0655 -0.0761 0.1173  142 HIS A N   
1034 C  CA  . HIS A 142 ? 0.4940 0.3241 0.3520 -0.0535 -0.0727 0.1028  142 HIS A CA  
1035 C  C   . HIS A 142 ? 0.4998 0.3613 0.3599 -0.0553 -0.0680 0.0932  142 HIS A C   
1036 O  O   . HIS A 142 ? 0.4591 0.3295 0.3235 -0.0581 -0.0613 0.0819  142 HIS A O   
1037 C  CB  . HIS A 142 ? 0.4912 0.3045 0.3546 -0.0532 -0.0681 0.0938  142 HIS A CB  
1038 C  CG  . HIS A 142 ? 0.5165 0.2973 0.3774 -0.0526 -0.0722 0.1015  142 HIS A CG  
1039 N  ND1 . HIS A 142 ? 0.5542 0.3175 0.4210 -0.0401 -0.0777 0.1059  142 HIS A ND1 
1040 C  CD2 . HIS A 142 ? 0.5408 0.3032 0.3947 -0.0631 -0.0718 0.1055  142 HIS A CD2 
1041 C  CE1 . HIS A 142 ? 0.6071 0.3407 0.4706 -0.0423 -0.0805 0.1118  142 HIS A CE1 
1042 N  NE2 . HIS A 142 ? 0.5721 0.3041 0.4273 -0.0568 -0.0770 0.1117  142 HIS A NE2 
1043 N  N   . PRO A 143 ? 0.5231 0.4016 0.3803 -0.0538 -0.0718 0.0973  143 PRO A N   
1044 C  CA  . PRO A 143 ? 0.4961 0.4036 0.3542 -0.0567 -0.0674 0.0876  143 PRO A CA  
1045 C  C   . PRO A 143 ? 0.4710 0.3853 0.3441 -0.0475 -0.0632 0.0728  143 PRO A C   
1046 O  O   . PRO A 143 ? 0.4504 0.3830 0.3262 -0.0507 -0.0577 0.0625  143 PRO A O   
1047 C  CB  . PRO A 143 ? 0.4891 0.4100 0.3402 -0.0566 -0.0740 0.0962  143 PRO A CB  
1048 C  CG  . PRO A 143 ? 0.5196 0.4194 0.3738 -0.0473 -0.0820 0.1070  143 PRO A CG  
1049 C  CD  . PRO A 143 ? 0.4866 0.3589 0.3395 -0.0497 -0.0808 0.1112  143 PRO A CD  
1050 N  N   . ASP A 144 ? 0.4572 0.3575 0.3405 -0.0361 -0.0654 0.0715  144 ASP A N   
1051 C  CA  . ASP A 144 ? 0.4550 0.3624 0.3519 -0.0283 -0.0613 0.0587  144 ASP A CA  
1052 C  C   . ASP A 144 ? 0.4457 0.3394 0.3477 -0.0271 -0.0562 0.0519  144 ASP A C   
1053 O  O   . ASP A 144 ? 0.4264 0.3285 0.3373 -0.0241 -0.0515 0.0414  144 ASP A O   
1054 C  CB  . ASP A 144 ? 0.5107 0.4176 0.4172 -0.0165 -0.0662 0.0600  144 ASP A CB  
1055 C  CG  . ASP A 144 ? 0.5407 0.4667 0.4442 -0.0174 -0.0713 0.0641  144 ASP A CG  
1056 O  OD1 . ASP A 144 ? 0.5529 0.4978 0.4520 -0.0247 -0.0685 0.0589  144 ASP A OD1 
1057 O  OD2 . ASP A 144 ? 0.5917 0.5146 0.4978 -0.0106 -0.0782 0.0718  144 ASP A OD2 
1058 N  N   . PHE A 145 ? 0.4326 0.3051 0.3289 -0.0299 -0.0572 0.0577  145 PHE A N   
1059 C  CA  . PHE A 145 ? 0.4279 0.2876 0.3273 -0.0299 -0.0529 0.0508  145 PHE A CA  
1060 C  C   . PHE A 145 ? 0.3864 0.2571 0.2824 -0.0404 -0.0478 0.0460  145 PHE A C   
1061 O  O   . PHE A 145 ? 0.3658 0.2405 0.2682 -0.0390 -0.0434 0.0367  145 PHE A O   
1062 C  CB  . PHE A 145 ? 0.4087 0.2406 0.3035 -0.0293 -0.0563 0.0578  145 PHE A CB  
1063 C  CG  . PHE A 145 ? 0.4350 0.2524 0.3313 -0.0302 -0.0525 0.0505  145 PHE A CG  
1064 C  CD1 . PHE A 145 ? 0.4069 0.2255 0.3123 -0.0217 -0.0490 0.0403  145 PHE A CD1 
1065 C  CD2 . PHE A 145 ? 0.4364 0.2387 0.3241 -0.0402 -0.0527 0.0542  145 PHE A CD2 
1066 C  CE1 . PHE A 145 ? 0.4426 0.2489 0.3476 -0.0230 -0.0459 0.0335  145 PHE A CE1 
1067 C  CE2 . PHE A 145 ? 0.4389 0.2283 0.3272 -0.0417 -0.0499 0.0469  145 PHE A CE2 
1068 C  CZ  . PHE A 145 ? 0.3988 0.1904 0.2952 -0.0330 -0.0466 0.0364  145 PHE A CZ  
1069 N  N   . ILE A 146 ? 0.3769 0.2539 0.2632 -0.0508 -0.0484 0.0525  146 ILE A N   
1070 C  CA  . ILE A 146 ? 0.3849 0.2750 0.2690 -0.0610 -0.0435 0.0483  146 ILE A CA  
1071 C  C   . ILE A 146 ? 0.3849 0.3012 0.2741 -0.0599 -0.0402 0.0408  146 ILE A C   
1072 O  O   . ILE A 146 ? 0.3357 0.2638 0.2207 -0.0607 -0.0423 0.0442  146 ILE A O   
1073 C  CB  . ILE A 146 ? 0.4362 0.3230 0.3080 -0.0736 -0.0448 0.0586  146 ILE A CB  
1074 C  CG1 . ILE A 146 ? 0.4081 0.2656 0.2757 -0.0751 -0.0481 0.0653  146 ILE A CG1 
1075 C  CG2 . ILE A 146 ? 0.3623 0.2683 0.2335 -0.0839 -0.0391 0.0539  146 ILE A CG2 
1076 C  CD1 . ILE A 146 ? 0.4363 0.2855 0.2913 -0.0865 -0.0513 0.0790  146 ILE A CD1 
1077 N  N   . VAL A 147 ? 0.3151 0.2399 0.2134 -0.0581 -0.0356 0.0305  147 VAL A N   
1078 C  CA  . VAL A 147 ? 0.3351 0.2816 0.2406 -0.0559 -0.0324 0.0220  147 VAL A CA  
1079 C  C   . VAL A 147 ? 0.3431 0.3063 0.2491 -0.0640 -0.0275 0.0173  147 VAL A C   
1080 O  O   . VAL A 147 ? 0.3372 0.3180 0.2500 -0.0623 -0.0244 0.0092  147 VAL A O   
1081 C  CB  . VAL A 147 ? 0.3070 0.2519 0.2249 -0.0460 -0.0313 0.0140  147 VAL A CB  
1082 C  CG1 . VAL A 147 ? 0.3127 0.2468 0.2318 -0.0377 -0.0356 0.0177  147 VAL A CG1 
1083 C  CG2 . VAL A 147 ? 0.3227 0.2590 0.2446 -0.0461 -0.0289 0.0106  147 VAL A CG2 
1084 N  N   . GLY A 148 ? 0.3298 0.2887 0.2300 -0.0728 -0.0267 0.0218  148 GLY A N   
1085 C  CA  . GLY A 148 ? 0.3102 0.2875 0.2122 -0.0807 -0.0218 0.0177  148 GLY A CA  
1086 C  C   . GLY A 148 ? 0.3474 0.3163 0.2442 -0.0904 -0.0217 0.0232  148 GLY A C   
1087 O  O   . GLY A 148 ? 0.3444 0.2916 0.2343 -0.0919 -0.0256 0.0308  148 GLY A O   
1088 N  N   . LEU A 149 ? 0.3089 0.2953 0.2104 -0.0968 -0.0173 0.0187  149 LEU A N   
1089 C  CA  . LEU A 149 ? 0.3292 0.3127 0.2267 -0.1082 -0.0168 0.0234  149 LEU A CA  
1090 C  C   . LEU A 149 ? 0.3042 0.2918 0.2132 -0.1070 -0.0152 0.0162  149 LEU A C   
1091 O  O   . LEU A 149 ? 0.3407 0.3400 0.2610 -0.0991 -0.0132 0.0077  149 LEU A O   
1092 C  CB  . LEU A 149 ? 0.3313 0.3359 0.2234 -0.1197 -0.0129 0.0263  149 LEU A CB  
1093 C  CG  . LEU A 149 ? 0.3702 0.3778 0.2498 -0.1226 -0.0139 0.0335  149 LEU A CG  
1094 C  CD1 . LEU A 149 ? 0.3625 0.3970 0.2385 -0.1336 -0.0083 0.0333  149 LEU A CD1 
1095 C  CD2 . LEU A 149 ? 0.3572 0.3382 0.2243 -0.1265 -0.0199 0.0469  149 LEU A CD2 
1096 N  N   . KCX A 150 ? 0.3328 0.3103 0.2388 -0.1153 -0.0167 0.0198  150 KCX A N   
1097 C  CA  . KCX A 150 ? 0.3160 0.2983 0.2318 -0.1153 -0.0162 0.0137  150 KCX A CA  
1098 C  CB  . KCX A 150 ? 0.3771 0.3337 0.2900 -0.1112 -0.0205 0.0139  150 KCX A CB  
1099 C  CG  . KCX A 150 ? 0.3648 0.3258 0.2881 -0.1039 -0.0207 0.0061  150 KCX A CG  
1100 C  CD  . KCX A 150 ? 0.3675 0.3487 0.2996 -0.1104 -0.0192 0.0028  150 KCX A CD  
1101 C  CE  . KCX A 150 ? 0.3165 0.3011 0.2580 -0.1027 -0.0206 -0.0031 150 KCX A CE  
1102 N  NZ  . KCX A 150 ? 0.2940 0.2556 0.2273 -0.1033 -0.0244 -0.0026 150 KCX A NZ  
1103 C  C   . KCX A 150 ? 0.3421 0.3375 0.2580 -0.1293 -0.0143 0.0160  150 KCX A C   
1104 O  O   . KCX A 150 ? 0.3536 0.3377 0.2592 -0.1399 -0.0157 0.0239  150 KCX A O   
1105 C  CX  . KCX A 150 ? 0.3500 0.3129 0.2861 -0.1043 -0.0267 -0.0058 150 KCX A CX  
1106 O  OQ1 . KCX A 150 ? 0.3335 0.2765 0.2611 -0.1051 -0.0293 -0.0064 150 KCX A OQ1 
1107 O  OQ2 . KCX A 150 ? 0.3071 0.2909 0.2542 -0.1044 -0.0265 -0.0085 150 KCX A OQ2 
1108 N  N   . ALA A 151 ? 0.2983 0.3175 0.2269 -0.1294 -0.0112 0.0094  151 ALA A N   
1109 C  CA  . ALA A 151 ? 0.3257 0.3598 0.2572 -0.1425 -0.0095 0.0107  151 ALA A CA  
1110 C  C   . ALA A 151 ? 0.3393 0.3818 0.2836 -0.1399 -0.0110 0.0046  151 ALA A C   
1111 O  O   . ALA A 151 ? 0.2969 0.3543 0.2537 -0.1300 -0.0095 -0.0022 151 ALA A O   
1112 C  CB  . ALA A 151 ? 0.3129 0.3759 0.2480 -0.1474 -0.0035 0.0097  151 ALA A CB  
1113 N  N   . ARG A 152 ? 0.3528 0.3848 0.2937 -0.1488 -0.0145 0.0070  152 ARG A N   
1114 C  CA  . ARG A 152 ? 0.3226 0.3631 0.2740 -0.1478 -0.0170 0.0019  152 ARG A CA  
1115 C  C   . ARG A 152 ? 0.3620 0.4318 0.3239 -0.1584 -0.0143 0.0012  152 ARG A C   
1116 O  O   . ARG A 152 ? 0.3971 0.4651 0.3543 -0.1728 -0.0155 0.0052  152 ARG A O   
1117 C  CB  . ARG A 152 ? 0.3804 0.3946 0.3224 -0.1515 -0.0224 0.0032  152 ARG A CB  
1118 C  CG  . ARG A 152 ? 0.3598 0.3457 0.2920 -0.1413 -0.0244 0.0037  152 ARG A CG  
1119 C  CD  . ARG A 152 ? 0.4143 0.3806 0.3411 -0.1416 -0.0290 0.0011  152 ARG A CD  
1120 N  NE  . ARG A 152 ? 0.4076 0.3623 0.3267 -0.1564 -0.0314 0.0039  152 ARG A NE  
1121 C  CZ  . ARG A 152 ? 0.4892 0.4416 0.4079 -0.1632 -0.0350 0.0004  152 ARG A CZ  
1122 N  NH1 . ARG A 152 ? 0.3677 0.3297 0.2927 -0.1564 -0.0369 -0.0053 152 ARG A NH1 
1123 N  NH2 . ARG A 152 ? 0.4797 0.4197 0.3913 -0.1777 -0.0370 0.0029  152 ARG A NH2 
1124 N  N   . MET A 153 ? 0.3343 0.4312 0.3115 -0.1513 -0.0108 -0.0042 153 MET A N   
1125 C  CA  . MET A 153 ? 0.3274 0.4562 0.3165 -0.1598 -0.0069 -0.0056 153 MET A CA  
1126 C  C   . MET A 153 ? 0.3325 0.4760 0.3362 -0.1591 -0.0106 -0.0093 153 MET A C   
1127 O  O   . MET A 153 ? 0.3350 0.4959 0.3546 -0.1479 -0.0101 -0.0147 153 MET A O   
1128 C  CB  . MET A 153 ? 0.3195 0.4705 0.3170 -0.1526 -0.0002 -0.0102 153 MET A CB  
1129 C  CG  . MET A 153 ? 0.3179 0.4550 0.2994 -0.1537 0.0025  -0.0062 153 MET A CG  
1130 S  SD  . MET A 153 ? 0.3642 0.5068 0.3336 -0.1740 0.0056  0.0025  153 MET A SD  
1131 C  CE  . MET A 153 ? 0.3736 0.5587 0.3631 -0.1811 0.0106  -0.0027 153 MET A CE  
1132 N  N   . SER A 154 ? 0.3159 0.4514 0.3143 -0.1711 -0.0150 -0.0061 154 SER A N   
1133 C  CA  . SER A 154 ? 0.3415 0.4920 0.3521 -0.1728 -0.0197 -0.0088 154 SER A CA  
1134 C  C   . SER A 154 ? 0.3963 0.5503 0.4034 -0.1919 -0.0213 -0.0053 154 SER A C   
1135 O  O   . SER A 154 ? 0.4118 0.5504 0.4050 -0.2010 -0.0190 -0.0001 154 SER A O   
1136 C  CB  . SER A 154 ? 0.3637 0.4936 0.3699 -0.1633 -0.0261 -0.0104 154 SER A CB  
1137 O  OG  . SER A 154 ? 0.3830 0.4788 0.3696 -0.1673 -0.0284 -0.0076 154 SER A OG  
1138 N  N   . SER A 155 ? 0.4135 0.5830 0.4312 -0.1925 -0.0249 -0.0073 155 SER A N   
1139 C  CA  . SER A 155 ? 0.4444 0.6206 0.4612 -0.2046 -0.0249 -0.0046 155 SER A CA  
1140 C  C   . SER A 155 ? 0.4456 0.5871 0.4418 -0.2141 -0.0279 -0.0006 155 SER A C   
1141 O  O   . SER A 155 ? 0.4904 0.6273 0.4791 -0.2248 -0.0250 0.0041  155 SER A O   
1142 C  CB  . SER A 155 ? 0.4315 0.6294 0.4635 -0.2025 -0.0296 -0.0077 155 SER A CB  
1143 O  OG  . SER A 155 ? 0.5225 0.7201 0.5507 -0.2149 -0.0314 -0.0055 155 SER A OG  
1144 N  N   . SER A 156 ? 0.4768 0.5933 0.4638 -0.2098 -0.0334 -0.0025 156 SER A N   
1145 C  CA  . SER A 156 ? 0.5207 0.6041 0.4902 -0.2169 -0.0365 -0.0006 156 SER A CA  
1146 C  C   . SER A 156 ? 0.5581 0.6153 0.5131 -0.2185 -0.0336 0.0044  156 SER A C   
1147 O  O   . SER A 156 ? 0.5219 0.5505 0.4635 -0.2237 -0.0358 0.0064  156 SER A O   
1148 C  CB  . SER A 156 ? 0.5199 0.5865 0.4841 -0.2105 -0.0425 -0.0054 156 SER A CB  
1149 O  OG  . SER A 156 ? 0.5388 0.5911 0.4982 -0.1996 -0.0423 -0.0068 156 SER A OG  
1150 N  N   . VAL A 157 ? 0.4949 0.5614 0.4528 -0.2140 -0.0289 0.0062  157 VAL A N   
1151 C  CA  . VAL A 157 ? 0.4883 0.5317 0.4328 -0.2144 -0.0268 0.0116  157 VAL A CA  
1152 C  C   . VAL A 157 ? 0.4900 0.5470 0.4334 -0.2237 -0.0215 0.0180  157 VAL A C   
1153 O  O   . VAL A 157 ? 0.4828 0.5185 0.4130 -0.2302 -0.0217 0.0249  157 VAL A O   
1154 C  CB  . VAL A 157 ? 0.4149 0.4549 0.3603 -0.2021 -0.0260 0.0090  157 VAL A CB  
1155 C  CG1 . VAL A 157 ? 0.4420 0.4550 0.3726 -0.2000 -0.0249 0.0150  157 VAL A CG1 
1156 C  CG2 . VAL A 157 ? 0.4451 0.4752 0.3918 -0.1911 -0.0307 0.0028  157 VAL A CG2 
1157 N  N   . VAL A 158 ? 0.4523 0.5454 0.4098 -0.2238 -0.0168 0.0158  158 VAL A N   
1158 C  CA  . VAL A 158 ? 0.4391 0.5481 0.3949 -0.2321 -0.0109 0.0210  158 VAL A CA  
1159 C  C   . VAL A 158 ? 0.4919 0.6063 0.4471 -0.2449 -0.0113 0.0245  158 VAL A C   
1160 O  O   . VAL A 158 ? 0.5017 0.6234 0.4517 -0.2536 -0.0073 0.0304  158 VAL A O   
1161 C  CB  . VAL A 158 ? 0.4150 0.5619 0.3863 -0.2265 -0.0044 0.0160  158 VAL A CB  
1162 C  CG1 . VAL A 158 ? 0.4602 0.6026 0.4304 -0.2160 -0.0027 0.0136  158 VAL A CG1 
1163 C  CG2 . VAL A 158 ? 0.4636 0.6358 0.4542 -0.2219 -0.0058 0.0088  158 VAL A CG2 
1164 N  N   . GLY A 159 ? 0.5004 0.6123 0.4603 -0.2468 -0.0161 0.0211  159 GLY A N   
1165 C  CA  . GLY A 159 ? 0.5331 0.6529 0.4942 -0.2595 -0.0165 0.0237  159 GLY A CA  
1166 C  C   . GLY A 159 ? 0.5102 0.6704 0.4852 -0.2624 -0.0103 0.0227  159 GLY A C   
1167 O  O   . GLY A 159 ? 0.5348 0.7221 0.5265 -0.2541 -0.0090 0.0162  159 GLY A O   
1168 N  N   . GLU A 160 ? 0.5087 0.6735 0.4773 -0.2735 -0.0065 0.0291  160 GLU A N   
1169 C  CA  . GLU A 160 ? 0.5045 0.7073 0.4846 -0.2773 0.0000  0.0281  160 GLU A CA  
1170 C  C   . GLU A 160 ? 0.5064 0.7209 0.4829 -0.2735 0.0069  0.0294  160 GLU A C   
1171 O  O   . GLU A 160 ? 0.4923 0.7345 0.4735 -0.2784 0.0131  0.0297  160 GLU A O   
1172 C  CB  . GLU A 160 ? 0.5455 0.7503 0.5219 -0.2935 -0.0001 0.0339  160 GLU A CB  
1173 N  N   . ASN A 161 ? 0.5102 0.7051 0.4783 -0.2650 0.0061  0.0297  161 ASN A N   
1174 C  CA  . ASN A 161 ? 0.4747 0.6795 0.4378 -0.2617 0.0122  0.0308  161 ASN A CA  
1175 C  C   . ASN A 161 ? 0.4634 0.6957 0.4429 -0.2484 0.0168  0.0206  161 ASN A C   
1176 O  O   . ASN A 161 ? 0.5044 0.7534 0.4829 -0.2460 0.0233  0.0190  161 ASN A O   
1177 C  CB  . ASN A 161 ? 0.5213 0.6904 0.4659 -0.2604 0.0089  0.0376  161 ASN A CB  
1178 C  CG  . ASN A 161 ? 0.5381 0.6784 0.4674 -0.2721 0.0043  0.0477  161 ASN A CG  
1179 O  OD1 . ASN A 161 ? 0.5720 0.7226 0.4979 -0.2834 0.0066  0.0530  161 ASN A OD1 
1180 N  ND2 . ASN A 161 ? 0.5563 0.6603 0.4769 -0.2691 -0.0022 0.0499  161 ASN A ND2 
1181 N  N   . GLY A 162 ? 0.4737 0.7108 0.4680 -0.2397 0.0134  0.0137  162 GLY A N   
1182 C  CA  . GLY A 162 ? 0.4557 0.7198 0.4686 -0.2265 0.0173  0.0040  162 GLY A CA  
1183 C  C   . GLY A 162 ? 0.4509 0.7080 0.4583 -0.2180 0.0201  0.0019  162 GLY A C   
1184 O  O   . GLY A 162 ? 0.4287 0.6572 0.4263 -0.2150 0.0154  0.0045  162 GLY A O   
1185 N  N   . ILE A 163 ? 0.4533 0.7369 0.4667 -0.2141 0.0281  -0.0033 163 ILE A N   
1186 C  CA  . ILE A 163 ? 0.4477 0.7305 0.4586 -0.2052 0.0317  -0.0075 163 ILE A CA  
1187 C  C   . ILE A 163 ? 0.3917 0.6586 0.3793 -0.2134 0.0335  0.0009  163 ILE A C   
1188 O  O   . ILE A 163 ? 0.4378 0.6994 0.4198 -0.2071 0.0354  -0.0011 163 ILE A O   
1189 C  CB  . ILE A 163 ? 0.4273 0.7458 0.4566 -0.1952 0.0394  -0.0193 163 ILE A CB  
1190 C  CG1 . ILE A 163 ? 0.3655 0.6821 0.3978 -0.1822 0.0416  -0.0268 163 ILE A CG1 
1191 C  CG2 . ILE A 163 ? 0.4226 0.7621 0.4456 -0.2038 0.0466  -0.0185 163 ILE A CG2 
1192 C  CD1 . ILE A 163 ? 0.3873 0.6877 0.4309 -0.1664 0.0345  -0.0311 163 ILE A CD1 
1193 N  N   . THR A 164 ? 0.4392 0.6975 0.4131 -0.2269 0.0322  0.0105  164 THR A N   
1194 C  CA  . THR A 164 ? 0.4377 0.6827 0.3900 -0.2344 0.0331  0.0197  164 THR A CA  
1195 C  C   . THR A 164 ? 0.4471 0.6584 0.3860 -0.2307 0.0280  0.0253  164 THR A C   
1196 O  O   . THR A 164 ? 0.4122 0.6225 0.3395 -0.2293 0.0306  0.0276  164 THR A O   
1197 C  CB  . THR A 164 ? 0.5083 0.7468 0.4504 -0.2492 0.0311  0.0298  164 THR A CB  
1198 O  OG1 . THR A 164 ? 0.4968 0.7689 0.4518 -0.2528 0.0363  0.0245  164 THR A OG1 
1199 C  CG2 . THR A 164 ? 0.5220 0.7487 0.4430 -0.2565 0.0313  0.0401  164 THR A CG2 
1200 N  N   . PRO A 165 ? 0.4579 0.6415 0.3970 -0.2286 0.0208  0.0273  165 PRO A N   
1201 C  CA  . PRO A 165 ? 0.4410 0.5907 0.3671 -0.2212 0.0155  0.0315  165 PRO A CA  
1202 C  C   . PRO A 165 ? 0.4082 0.5631 0.3375 -0.2038 0.0175  0.0231  165 PRO A C   
1203 O  O   . PRO A 165 ? 0.4520 0.5904 0.3675 -0.2000 0.0158  0.0278  165 PRO A O   
1204 C  CB  . PRO A 165 ? 0.4247 0.5498 0.3547 -0.2182 0.0081  0.0305  165 PRO A CB  
1205 C  CG  . PRO A 165 ? 0.4434 0.5799 0.3785 -0.2311 0.0082  0.0323  165 PRO A CG  
1206 C  CD  . PRO A 165 ? 0.4061 0.5836 0.3537 -0.2312 0.0159  0.0262  165 PRO A CD  
1207 N  N   . LEU A 166 ? 0.3982 0.5756 0.3459 -0.1933 0.0206  0.0111  166 LEU A N   
1208 C  CA  . LEU A 166 ? 0.3843 0.5646 0.3359 -0.1773 0.0222  0.0026  166 LEU A CA  
1209 C  C   . LEU A 166 ? 0.4047 0.6017 0.3468 -0.1809 0.0284  0.0027  166 LEU A C   
1210 O  O   . LEU A 166 ? 0.3978 0.5827 0.3302 -0.1736 0.0270  0.0028  166 LEU A O   
1211 C  CB  . LEU A 166 ? 0.3896 0.5903 0.3640 -0.1661 0.0242  -0.0097 166 LEU A CB  
1212 C  CG  . LEU A 166 ? 0.3550 0.5570 0.3366 -0.1492 0.0254  -0.0195 166 LEU A CG  
1213 C  CD1 . LEU A 166 ? 0.3429 0.5108 0.3139 -0.1409 0.0187  -0.0157 166 LEU A CD1 
1214 C  CD2 . LEU A 166 ? 0.3423 0.5617 0.3473 -0.1389 0.0263  -0.0295 166 LEU A CD2 
1215 N  N   . ALA A 167 ? 0.3873 0.6135 0.3315 -0.1930 0.0353  0.0028  167 ALA A N   
1216 C  CA  . ALA A 167 ? 0.4050 0.6471 0.3362 -0.1997 0.0412  0.0048  167 ALA A CA  
1217 C  C   . ALA A 167 ? 0.4196 0.6321 0.3276 -0.2043 0.0354  0.0182  167 ALA A C   
1218 O  O   . ALA A 167 ? 0.4364 0.6456 0.3346 -0.1980 0.0353  0.0171  167 ALA A O   
1219 C  CB  . ALA A 167 ? 0.3603 0.6322 0.2937 -0.2145 0.0480  0.0066  167 ALA A CB  
1220 N  N   . ARG A 168 ? 0.4358 0.6246 0.3359 -0.2141 0.0298  0.0305  168 ARG A N   
1221 C  CA  . ARG A 168 ? 0.4563 0.6150 0.3364 -0.2175 0.0236  0.0439  168 ARG A CA  
1222 C  C   . ARG A 168 ? 0.4400 0.5768 0.3192 -0.2002 0.0182  0.0399  168 ARG A C   
1223 O  O   . ARG A 168 ? 0.4327 0.5635 0.2990 -0.1976 0.0166  0.0443  168 ARG A O   
1224 C  CB  . ARG A 168 ? 0.4884 0.6220 0.3636 -0.2289 0.0182  0.0553  168 ARG A CB  
1225 C  CG  . ARG A 168 ? 0.5956 0.7418 0.4674 -0.2422 0.0198  0.0610  168 ARG A CG  
1226 C  CD  . ARG A 168 ? 0.6602 0.7731 0.5185 -0.2496 0.0122  0.0750  168 ARG A CD  
1227 N  NE  . ARG A 168 ? 0.6808 0.8026 0.5403 -0.2618 0.0130  0.0787  168 ARG A NE  
1228 C  CZ  . ARG A 168 ? 0.6929 0.7925 0.5418 -0.2706 0.0079  0.0906  168 ARG A CZ  
1229 N  NH1 . ARG A 168 ? 0.7107 0.7771 0.5480 -0.2674 0.0013  0.1000  168 ARG A NH1 
1230 N  NH2 . ARG A 168 ? 0.6821 0.7933 0.5333 -0.2823 0.0096  0.0930  168 ARG A NH2 
1231 N  N   . ALA A 169 ? 0.4200 0.5472 0.3133 -0.1884 0.0154  0.0314  169 ALA A N   
1232 C  CA  . ALA A 169 ? 0.4374 0.5451 0.3314 -0.1725 0.0107  0.0274  169 ALA A CA  
1233 C  C   . ALA A 169 ? 0.4067 0.5325 0.3000 -0.1652 0.0146  0.0202  169 ALA A C   
1234 O  O   . ALA A 169 ? 0.4039 0.5161 0.2874 -0.1596 0.0108  0.0235  169 ALA A O   
1235 C  CB  . ALA A 169 ? 0.3482 0.4500 0.2585 -0.1621 0.0086  0.0187  169 ALA A CB  
1236 N  N   . LYS A 170 ? 0.4276 0.5854 0.3312 -0.1660 0.0221  0.0101  170 LYS A N   
1237 C  CA  . LYS A 170 ? 0.3997 0.5754 0.3027 -0.1597 0.0264  0.0011  170 LYS A CA  
1238 C  C   . LYS A 170 ? 0.4126 0.5887 0.2941 -0.1686 0.0260  0.0108  170 LYS A C   
1239 O  O   . LYS A 170 ? 0.4711 0.6397 0.3450 -0.1618 0.0229  0.0103  170 LYS A O   
1240 C  CB  . LYS A 170 ? 0.4090 0.6195 0.3270 -0.1597 0.0352  -0.0118 170 LYS A CB  
1241 C  CG  . LYS A 170 ? 0.3653 0.5768 0.3059 -0.1482 0.0349  -0.0220 170 LYS A CG  
1242 C  CD  . LYS A 170 ? 0.3517 0.5487 0.2978 -0.1323 0.0314  -0.0296 170 LYS A CD  
1243 C  CE  . LYS A 170 ? 0.4011 0.6161 0.3461 -0.1281 0.0366  -0.0402 170 LYS A CE  
1244 N  NZ  . LYS A 170 ? 0.3706 0.5708 0.3217 -0.1139 0.0330  -0.0474 170 LYS A NZ  
1245 N  N   . THR A 171 ? 0.4427 0.6272 0.3141 -0.1844 0.0284  0.0210  171 THR A N   
1246 C  CA  . THR A 171 ? 0.4240 0.6077 0.2735 -0.1942 0.0272  0.0331  171 THR A CA  
1247 C  C   . THR A 171 ? 0.4710 0.6201 0.3106 -0.1880 0.0172  0.0432  171 THR A C   
1248 O  O   . THR A 171 ? 0.4480 0.5961 0.2765 -0.1846 0.0145  0.0454  171 THR A O   
1249 C  CB  . THR A 171 ? 0.4644 0.6555 0.3056 -0.2130 0.0299  0.0452  171 THR A CB  
1250 O  OG1 . THR A 171 ? 0.4455 0.6721 0.2975 -0.2166 0.0387  0.0344  171 THR A OG1 
1251 C  CG2 . THR A 171 ? 0.4683 0.6497 0.2901 -0.2196 0.0247  0.0593  171 THR A CG2 
1252 N  N   . MET A 172 ? 0.4658 0.5876 0.3111 -0.1852 0.0117  0.0477  172 MET A N   
1253 C  CA  . MET A 172 ? 0.4510 0.5394 0.2895 -0.1784 0.0027  0.0564  172 MET A CA  
1254 C  C   . MET A 172 ? 0.4514 0.5387 0.2945 -0.1629 0.0006  0.0472  172 MET A C   
1255 O  O   . MET A 172 ? 0.4382 0.5145 0.2709 -0.1595 -0.0048 0.0540  172 MET A O   
1256 C  CB  . MET A 172 ? 0.4712 0.5354 0.3178 -0.1774 -0.0010 0.0581  172 MET A CB  
1257 C  CG  . MET A 172 ? 0.4793 0.5229 0.3145 -0.1902 -0.0049 0.0737  172 MET A CG  
1258 S  SD  . MET A 172 ? 0.4932 0.5215 0.3412 -0.1914 -0.0061 0.0694  172 MET A SD  
1259 C  CE  . MET A 172 ? 0.5053 0.4941 0.3509 -0.1783 -0.0148 0.0725  172 MET A CE  
1260 N  N   . GLN A 173 ? 0.4375 0.5375 0.2971 -0.1537 0.0047  0.0319  173 GLN A N   
1261 C  CA  . GLN A 173 ? 0.4021 0.5036 0.2675 -0.1403 0.0036  0.0220  173 GLN A CA  
1262 C  C   . GLN A 173 ? 0.4645 0.5815 0.3170 -0.1432 0.0044  0.0227  173 GLN A C   
1263 O  O   . GLN A 173 ? 0.4380 0.5437 0.2843 -0.1371 -0.0014 0.0261  173 GLN A O   
1264 C  CB  . GLN A 173 ? 0.4139 0.5319 0.2983 -0.1330 0.0092  0.0061  173 GLN A CB  
1265 C  CG  . GLN A 173 ? 0.4160 0.5342 0.3082 -0.1200 0.0083  -0.0046 173 GLN A CG  
1266 C  CD  . GLN A 173 ? 0.4330 0.5623 0.3450 -0.1124 0.0127  -0.0183 173 GLN A CD  
1267 O  OE1 . GLN A 173 ? 0.4088 0.5605 0.3274 -0.1168 0.0192  -0.0244 173 GLN A OE1 
1268 N  NE2 . GLN A 173 ? 0.4139 0.5282 0.3363 -0.1009 0.0093  -0.0225 173 GLN A NE2 
1269 N  N   . GLN A 174 ? 0.4203 0.5649 0.2681 -0.1529 0.0115  0.0198  174 GLN A N   
1270 C  CA  . GLN A 174 ? 0.4732 0.6363 0.3074 -0.1566 0.0131  0.0189  174 GLN A CA  
1271 C  C   . GLN A 174 ? 0.4735 0.6204 0.2885 -0.1616 0.0051  0.0363  174 GLN A C   
1272 O  O   . GLN A 174 ? 0.4724 0.6233 0.2785 -0.1585 0.0018  0.0362  174 GLN A O   
1273 C  CB  . GLN A 174 ? 0.4470 0.6425 0.2778 -0.1682 0.0226  0.0146  174 GLN A CB  
1274 C  CG  . GLN A 174 ? 0.5225 0.7413 0.3710 -0.1612 0.0308  -0.0058 174 GLN A CG  
1275 C  CD  . GLN A 174 ? 0.5075 0.7282 0.3593 -0.1497 0.0296  -0.0185 174 GLN A CD  
1276 O  OE1 . GLN A 174 ? 0.5241 0.7332 0.3921 -0.1372 0.0277  -0.0273 174 GLN A OE1 
1277 N  NE2 . GLN A 174 ? 0.4800 0.7161 0.3159 -0.1546 0.0305  -0.0193 174 GLN A NE2 
1278 N  N   . GLU A 175 ? 0.4837 0.6112 0.2927 -0.1689 0.0014  0.0515  175 GLU A N   
1279 C  CA  . GLU A 175 ? 0.4731 0.5855 0.2641 -0.1744 -0.0061 0.0696  175 GLU A CA  
1280 C  C   . GLU A 175 ? 0.5154 0.6006 0.3093 -0.1614 -0.0155 0.0733  175 GLU A C   
1281 O  O   . GLU A 175 ? 0.5079 0.5801 0.2887 -0.1633 -0.0228 0.0879  175 GLU A O   
1282 C  CB  . GLU A 175 ? 0.5150 0.6151 0.2987 -0.1878 -0.0067 0.0848  175 GLU A CB  
1283 C  CG  . GLU A 175 ? 0.4722 0.5999 0.2565 -0.2003 0.0021  0.0814  175 GLU A CG  
1284 C  CD  . GLU A 175 ? 0.5981 0.7114 0.3807 -0.2114 -0.0003 0.0946  175 GLU A CD  
1285 O  OE1 . GLU A 175 ? 0.6382 0.7190 0.4178 -0.2097 -0.0081 0.1061  175 GLU A OE1 
1286 O  OE2 . GLU A 175 ? 0.5741 0.7082 0.3589 -0.2213 0.0055  0.0928  175 GLU A OE2 
1287 N  N   . ASN A 176 ? 0.4853 0.5623 0.2962 -0.1484 -0.0154 0.0610  176 ASN A N   
1288 C  CA  . ASN A 176 ? 0.4655 0.5178 0.2807 -0.1363 -0.0234 0.0640  176 ASN A CA  
1289 C  C   . ASN A 176 ? 0.4852 0.5478 0.3116 -0.1243 -0.0225 0.0490  176 ASN A C   
1290 O  O   . ASN A 176 ? 0.5166 0.5671 0.3572 -0.1139 -0.0231 0.0417  176 ASN A O   
1291 C  CB  . ASN A 176 ? 0.4889 0.5148 0.3130 -0.1333 -0.0253 0.0669  176 ASN A CB  
1292 C  CG  . ASN A 176 ? 0.5202 0.5308 0.3329 -0.1450 -0.0278 0.0827  176 ASN A CG  
1293 O  OD1 . ASN A 176 ? 0.5615 0.5497 0.3673 -0.1435 -0.0351 0.0954  176 ASN A OD1 
1294 N  ND2 . ASN A 176 ? 0.5270 0.5499 0.3391 -0.1569 -0.0217 0.0821  176 ASN A ND2 
1295 N  N   . GLY A 177 ? 0.4972 0.5824 0.3164 -0.1266 -0.0210 0.0443  177 GLY A N   
1296 C  CA  . GLY A 177 ? 0.4993 0.5931 0.3275 -0.1167 -0.0211 0.0308  177 GLY A CA  
1297 C  C   . GLY A 177 ? 0.4550 0.5534 0.3019 -0.1100 -0.0148 0.0146  177 GLY A C   
1298 O  O   . GLY A 177 ? 0.4784 0.5727 0.3365 -0.0998 -0.0164 0.0059  177 GLY A O   
1299 N  N   . ASP A 178 ? 0.4482 0.5554 0.2994 -0.1156 -0.0080 0.0109  178 ASP A N   
1300 C  CA  . ASP A 178 ? 0.4648 0.5792 0.3343 -0.1095 -0.0021 -0.0039 178 ASP A CA  
1301 C  C   . ASP A 178 ? 0.4523 0.5438 0.3351 -0.0989 -0.0060 -0.0046 178 ASP A C   
1302 O  O   . ASP A 178 ? 0.4134 0.5063 0.3098 -0.0900 -0.0047 -0.0159 178 ASP A O   
1303 C  CB  . ASP A 178 ? 0.5108 0.6468 0.3848 -0.1063 0.0022  -0.0194 178 ASP A CB  
1304 C  CG  . ASP A 178 ? 0.4897 0.6530 0.3597 -0.1151 0.0105  -0.0257 178 ASP A CG  
1305 O  OD1 . ASP A 178 ? 0.5958 0.7687 0.4801 -0.1132 0.0167  -0.0354 178 ASP A OD1 
1306 O  OD2 . ASP A 178 ? 0.5872 0.7634 0.4400 -0.1240 0.0107  -0.0207 178 ASP A OD2 
1307 N  N   . LEU A 179 ? 0.4432 0.5132 0.3215 -0.1003 -0.0106 0.0076  179 LEU A N   
1308 C  CA  . LEU A 179 ? 0.4357 0.4850 0.3249 -0.0915 -0.0135 0.0071  179 LEU A CA  
1309 C  C   . LEU A 179 ? 0.3896 0.4460 0.2938 -0.0889 -0.0083 -0.0031 179 LEU A C   
1310 O  O   . LEU A 179 ? 0.3836 0.4552 0.2889 -0.0960 -0.0034 -0.0055 179 LEU A O   
1311 C  CB  . LEU A 179 ? 0.4285 0.4551 0.3099 -0.0951 -0.0179 0.0202  179 LEU A CB  
1312 C  CG  . LEU A 179 ? 0.4339 0.4441 0.3050 -0.0934 -0.0250 0.0317  179 LEU A CG  
1313 C  CD1 . LEU A 179 ? 0.4156 0.4058 0.2790 -0.0999 -0.0278 0.0437  179 LEU A CD1 
1314 C  CD2 . LEU A 179 ? 0.4618 0.4604 0.3421 -0.0807 -0.0286 0.0279  179 LEU A CD2 
1315 N  N   . PRO A 180 ? 0.3593 0.4058 0.2757 -0.0790 -0.0096 -0.0087 180 PRO A N   
1316 C  CA  . PRO A 180 ? 0.3450 0.3956 0.2754 -0.0763 -0.0062 -0.0157 180 PRO A CA  
1317 C  C   . PRO A 180 ? 0.3452 0.3902 0.2727 -0.0837 -0.0062 -0.0093 180 PRO A C   
1318 O  O   . PRO A 180 ? 0.3316 0.3598 0.2488 -0.0877 -0.0099 0.0005  180 PRO A O   
1319 C  CB  . PRO A 180 ? 0.3437 0.3795 0.2831 -0.0656 -0.0092 -0.0183 180 PRO A CB  
1320 C  CG  . PRO A 180 ? 0.3470 0.3804 0.2814 -0.0621 -0.0122 -0.0176 180 PRO A CG  
1321 C  CD  . PRO A 180 ? 0.4026 0.4357 0.3210 -0.0701 -0.0142 -0.0081 180 PRO A CD  
1322 N  N   . LEU A 181 ? 0.3137 0.3732 0.2512 -0.0857 -0.0021 -0.0151 181 LEU A N   
1323 C  CA  . LEU A 181 ? 0.2828 0.3412 0.2199 -0.0936 -0.0019 -0.0105 181 LEU A CA  
1324 C  C   . LEU A 181 ? 0.2938 0.3510 0.2453 -0.0874 -0.0023 -0.0157 181 LEU A C   
1325 O  O   . LEU A 181 ? 0.2894 0.3620 0.2543 -0.0818 0.0007  -0.0244 181 LEU A O   
1326 C  CB  . LEU A 181 ? 0.2914 0.3733 0.2272 -0.1038 0.0034  -0.0113 181 LEU A CB  
1327 C  CG  . LEU A 181 ? 0.2648 0.3516 0.2049 -0.1120 0.0043  -0.0089 181 LEU A CG  
1328 C  CD1 . LEU A 181 ? 0.2889 0.3543 0.2155 -0.1206 -0.0001 0.0027  181 LEU A CD1 
1329 C  CD2 . LEU A 181 ? 0.2755 0.3923 0.2198 -0.1197 0.0110  -0.0129 181 LEU A CD2 
1330 N  N   . MET A 182 ? 0.2608 0.2999 0.2092 -0.0885 -0.0062 -0.0106 182 MET A N   
1331 C  CA  . MET A 182 ? 0.2812 0.3193 0.2404 -0.0845 -0.0075 -0.0140 182 MET A CA  
1332 C  C   . MET A 182 ? 0.2578 0.3053 0.2185 -0.0946 -0.0069 -0.0121 182 MET A C   
1333 O  O   . MET A 182 ? 0.3077 0.3455 0.2574 -0.1043 -0.0083 -0.0054 182 MET A O   
1334 C  CB  . MET A 182 ? 0.2496 0.2634 0.2043 -0.0791 -0.0120 -0.0111 182 MET A CB  
1335 C  CG  . MET A 182 ? 0.2885 0.3018 0.2519 -0.0758 -0.0136 -0.0138 182 MET A CG  
1336 S  SD  . MET A 182 ? 0.3126 0.3005 0.2700 -0.0695 -0.0176 -0.0119 182 MET A SD  
1337 C  CE  . MET A 182 ? 0.2966 0.2881 0.2635 -0.0572 -0.0163 -0.0163 182 MET A CE  
1338 N  N   . VAL A 183 ? 0.2339 0.3004 0.2094 -0.0925 -0.0050 -0.0178 183 VAL A N   
1339 C  CA  . VAL A 183 ? 0.2612 0.3429 0.2419 -0.1016 -0.0042 -0.0173 183 VAL A CA  
1340 C  C   . VAL A 183 ? 0.2596 0.3378 0.2487 -0.0976 -0.0083 -0.0185 183 VAL A C   
1341 O  O   . VAL A 183 ? 0.2393 0.3226 0.2403 -0.0871 -0.0087 -0.0231 183 VAL A O   
1342 C  CB  . VAL A 183 ? 0.2491 0.3609 0.2418 -0.1023 0.0017  -0.0233 183 VAL A CB  
1343 C  CG1 . VAL A 183 ? 0.2493 0.3793 0.2486 -0.1125 0.0026  -0.0223 183 VAL A CG1 
1344 C  CG2 . VAL A 183 ? 0.2864 0.4026 0.2690 -0.1057 0.0058  -0.0228 183 VAL A CG2 
1345 N  N   . HIS A 184 ? 0.2588 0.3276 0.2410 -0.1063 -0.0117 -0.0142 184 HIS A N   
1346 C  CA  . HIS A 184 ? 0.2961 0.3645 0.2844 -0.1049 -0.0160 -0.0152 184 HIS A CA  
1347 C  C   . HIS A 184 ? 0.2943 0.3911 0.2973 -0.1098 -0.0149 -0.0175 184 HIS A C   
1348 O  O   . HIS A 184 ? 0.2490 0.3597 0.2520 -0.1197 -0.0116 -0.0164 184 HIS A O   
1349 C  CB  . HIS A 184 ? 0.2842 0.3286 0.2577 -0.1121 -0.0202 -0.0110 184 HIS A CB  
1350 C  CG  . HIS A 184 ? 0.2923 0.3433 0.2679 -0.1219 -0.0235 -0.0106 184 HIS A CG  
1351 N  ND1 . HIS A 184 ? 0.2900 0.3248 0.2588 -0.1226 -0.0284 -0.0108 184 HIS A ND1 
1352 C  CD2 . HIS A 184 ? 0.3165 0.3881 0.2990 -0.1325 -0.0227 -0.0103 184 HIS A CD2 
1353 C  CE1 . HIS A 184 ? 0.3133 0.3585 0.2848 -0.1331 -0.0311 -0.0109 184 HIS A CE1 
1354 N  NE2 . HIS A 184 ? 0.3156 0.3834 0.2962 -0.1392 -0.0278 -0.0103 184 HIS A NE2 
1355 N  N   . ILE A 185 ? 0.2372 0.3438 0.2534 -0.1025 -0.0177 -0.0202 185 ILE A N   
1356 C  CA  . ILE A 185 ? 0.2581 0.3924 0.2909 -0.1052 -0.0180 -0.0222 185 ILE A CA  
1357 C  C   . ILE A 185 ? 0.3013 0.4330 0.3354 -0.1064 -0.0250 -0.0203 185 ILE A C   
1358 O  O   . ILE A 185 ? 0.2272 0.3388 0.2527 -0.1015 -0.0287 -0.0190 185 ILE A O   
1359 C  CB  . ILE A 185 ? 0.2550 0.4096 0.3071 -0.0934 -0.0145 -0.0277 185 ILE A CB  
1360 C  CG1 . ILE A 185 ? 0.2393 0.3803 0.2947 -0.0798 -0.0177 -0.0283 185 ILE A CG1 
1361 C  CG2 . ILE A 185 ? 0.2553 0.4168 0.3057 -0.0939 -0.0073 -0.0310 185 ILE A CG2 
1362 C  CD1 . ILE A 185 ? 0.2204 0.3799 0.2980 -0.0680 -0.0167 -0.0330 185 ILE A CD1 
1363 N  N   . GLY A 186 ? 0.3090 0.4634 0.3539 -0.1136 -0.0266 -0.0205 186 GLY A N   
1364 C  CA  . GLY A 186 ? 0.3399 0.4966 0.3868 -0.1161 -0.0339 -0.0190 186 GLY A CA  
1365 C  C   . GLY A 186 ? 0.3220 0.5090 0.3837 -0.1244 -0.0352 -0.0194 186 GLY A C   
1366 O  O   . GLY A 186 ? 0.3235 0.5350 0.4057 -0.1166 -0.0355 -0.0213 186 GLY A O   
1367 N  N   . ASN A 187 ? 0.3296 0.5154 0.3826 -0.1402 -0.0362 -0.0177 187 ASN A N   
1368 C  CA  . ASN A 187 ? 0.3062 0.5216 0.3730 -0.1504 -0.0376 -0.0180 187 ASN A CA  
1369 C  C   . ASN A 187 ? 0.3744 0.6086 0.4478 -0.1566 -0.0294 -0.0190 187 ASN A C   
1370 O  O   . ASN A 187 ? 0.3431 0.5615 0.4032 -0.1594 -0.0241 -0.0178 187 ASN A O   
1371 C  CB  . ASN A 187 ? 0.3864 0.5908 0.4403 -0.1657 -0.0433 -0.0160 187 ASN A CB  
1372 C  CG  . ASN A 187 ? 0.4066 0.6078 0.4599 -0.1616 -0.0520 -0.0160 187 ASN A CG  
1373 O  OD1 . ASN A 187 ? 0.4116 0.6366 0.4825 -0.1543 -0.0556 -0.0162 187 ASN A OD1 
1374 N  ND2 . ASN A 187 ? 0.4335 0.6052 0.4664 -0.1658 -0.0554 -0.0158 187 ASN A ND2 
1375 N  N   . ASN A 188 ? 0.3361 0.6044 0.4298 -0.1577 -0.0282 -0.0208 188 ASN A N   
1376 C  CA  . ASN A 188 ? 0.3685 0.6564 0.4682 -0.1624 -0.0197 -0.0219 188 ASN A CA  
1377 C  C   . ASN A 188 ? 0.4003 0.6907 0.4941 -0.1767 -0.0203 -0.0182 188 ASN A C   
1378 O  O   . ASN A 188 ? 0.3828 0.6676 0.4746 -0.1803 -0.0275 -0.0165 188 ASN A O   
1379 C  CB  . ASN A 188 ? 0.3551 0.6765 0.4814 -0.1501 -0.0165 -0.0273 188 ASN A CB  
1380 C  CG  . ASN A 188 ? 0.3875 0.7265 0.5304 -0.1464 -0.0233 -0.0268 188 ASN A CG  
1381 O  OD1 . ASN A 188 ? 0.3520 0.6787 0.4913 -0.1442 -0.0320 -0.0243 188 ASN A OD1 
1382 N  ND2 . ASN A 188 ? 0.4226 0.7908 0.5831 -0.1458 -0.0196 -0.0290 188 ASN A ND2 
1383 N  N   . PRO A 189 ? 0.3976 0.6960 0.4874 -0.1856 -0.0131 -0.0170 189 PRO A N   
1384 C  CA  . PRO A 189 ? 0.3904 0.6957 0.4787 -0.1841 -0.0041 -0.0186 189 PRO A CA  
1385 C  C   . PRO A 189 ? 0.4160 0.6893 0.4825 -0.1870 -0.0037 -0.0153 189 PRO A C   
1386 O  O   . PRO A 189 ? 0.4637 0.7086 0.5148 -0.1927 -0.0094 -0.0110 189 PRO A O   
1387 C  CB  . PRO A 189 ? 0.3970 0.7197 0.4851 -0.1960 0.0013  -0.0164 189 PRO A CB  
1388 C  CG  . PRO A 189 ? 0.4649 0.7721 0.5432 -0.2078 -0.0053 -0.0113 189 PRO A CG  
1389 C  CD  . PRO A 189 ? 0.4343 0.7385 0.5214 -0.1992 -0.0137 -0.0136 189 PRO A CD  
1390 N  N   . PRO A 190 ? 0.4277 0.7045 0.4925 -0.1827 0.0028  -0.0175 190 PRO A N   
1391 C  CA  . PRO A 190 ? 0.4313 0.7392 0.5128 -0.1745 0.0106  -0.0244 190 PRO A CA  
1392 C  C   . PRO A 190 ? 0.3893 0.7094 0.4920 -0.1580 0.0080  -0.0314 190 PRO A C   
1393 O  O   . PRO A 190 ? 0.3611 0.6618 0.4617 -0.1516 0.0004  -0.0300 190 PRO A O   
1394 C  CB  . PRO A 190 ? 0.3975 0.6956 0.4643 -0.1762 0.0165  -0.0238 190 PRO A CB  
1395 C  CG  . PRO A 190 ? 0.4164 0.6741 0.4641 -0.1750 0.0100  -0.0184 190 PRO A CG  
1396 C  CD  . PRO A 190 ? 0.4123 0.6598 0.4565 -0.1860 0.0030  -0.0133 190 PRO A CD  
1397 N  N   . ASN A 191 ? 0.3585 0.7066 0.4798 -0.1487 0.0142  -0.0388 191 ASN A N   
1398 C  CA  . ASN A 191 ? 0.3558 0.7148 0.4988 -0.1317 0.0120  -0.0455 191 ASN A CA  
1399 C  C   . ASN A 191 ? 0.3193 0.6542 0.4530 -0.1187 0.0138  -0.0487 191 ASN A C   
1400 O  O   . ASN A 191 ? 0.3259 0.6511 0.4434 -0.1230 0.0191  -0.0486 191 ASN A O   
1401 C  CB  . ASN A 191 ? 0.3225 0.7144 0.4878 -0.1243 0.0178  -0.0523 191 ASN A CB  
1402 C  CG  . ASN A 191 ? 0.4073 0.8111 0.5959 -0.1124 0.0112  -0.0537 191 ASN A CG  
1403 O  OD1 . ASN A 191 ? 0.4165 0.8227 0.6070 -0.1183 0.0047  -0.0482 191 ASN A OD1 
1404 N  ND2 . ASN A 191 ? 0.4230 0.8325 0.6289 -0.0955 0.0123  -0.0607 191 ASN A ND2 
1405 N  N   . LEU A 192 ? 0.3158 0.6419 0.4601 -0.1031 0.0088  -0.0509 192 LEU A N   
1406 C  CA  . LEU A 192 ? 0.3284 0.6325 0.4664 -0.0907 0.0099  -0.0542 192 LEU A CA  
1407 C  C   . LEU A 192 ? 0.3286 0.6497 0.4734 -0.0859 0.0196  -0.0637 192 LEU A C   
1408 O  O   . LEU A 192 ? 0.2995 0.6036 0.4306 -0.0834 0.0225  -0.0657 192 LEU A O   
1409 C  CB  . LEU A 192 ? 0.3130 0.6082 0.4641 -0.0755 0.0032  -0.0545 192 LEU A CB  
1410 C  CG  . LEU A 192 ? 0.2926 0.5615 0.4361 -0.0642 0.0032  -0.0565 192 LEU A CG  
1411 C  CD1 . LEU A 192 ? 0.2847 0.5238 0.4006 -0.0720 0.0019  -0.0506 192 LEU A CD1 
1412 C  CD2 . LEU A 192 ? 0.2739 0.5344 0.4306 -0.0506 -0.0035 -0.0552 192 LEU A CD2 
1413 N  N   . ASP A 193 ? 0.2951 0.6509 0.4616 -0.0843 0.0247  -0.0704 193 ASP A N   
1414 C  CA  . ASP A 193 ? 0.3129 0.6872 0.4864 -0.0796 0.0347  -0.0814 193 ASP A CA  
1415 C  C   . ASP A 193 ? 0.3022 0.6739 0.4519 -0.0936 0.0409  -0.0794 193 ASP A C   
1416 O  O   . ASP A 193 ? 0.3071 0.6701 0.4467 -0.0898 0.0453  -0.0846 193 ASP A O   
1417 C  CB  . ASP A 193 ? 0.3107 0.7244 0.5115 -0.0765 0.0393  -0.0887 193 ASP A CB  
1418 N  N   . GLU A 194 ? 0.3027 0.6814 0.4428 -0.1104 0.0408  -0.0714 194 GLU A N   
1419 C  CA  . GLU A 194 ? 0.3098 0.6868 0.4276 -0.1248 0.0462  -0.0674 194 GLU A CA  
1420 C  C   . GLU A 194 ? 0.3224 0.6611 0.4156 -0.1240 0.0419  -0.0615 194 GLU A C   
1421 O  O   . GLU A 194 ? 0.3341 0.6702 0.4126 -0.1269 0.0468  -0.0627 194 GLU A O   
1422 C  CB  . GLU A 194 ? 0.3016 0.6847 0.4124 -0.1417 0.0449  -0.0580 194 GLU A CB  
1423 N  N   . ILE A 195 ? 0.3553 0.6659 0.4442 -0.1201 0.0327  -0.0554 195 ILE A N   
1424 C  CA  . ILE A 195 ? 0.3381 0.6134 0.4061 -0.1184 0.0285  -0.0500 195 ILE A CA  
1425 C  C   . ILE A 195 ? 0.2972 0.5677 0.3675 -0.1047 0.0312  -0.0585 195 ILE A C   
1426 O  O   . ILE A 195 ? 0.3248 0.5852 0.3788 -0.1068 0.0334  -0.0578 195 ILE A O   
1427 C  CB  . ILE A 195 ? 0.3148 0.5646 0.3799 -0.1161 0.0190  -0.0435 195 ILE A CB  
1428 C  CG1 . ILE A 195 ? 0.3634 0.6129 0.4219 -0.1316 0.0159  -0.0353 195 ILE A CG1 
1429 C  CG2 . ILE A 195 ? 0.3108 0.5268 0.3586 -0.1109 0.0154  -0.0401 195 ILE A CG2 
1430 C  CD1 . ILE A 195 ? 0.3321 0.5599 0.3883 -0.1299 0.0069  -0.0307 195 ILE A CD1 
1431 N  N   . ALA A 196 ? 0.2933 0.5707 0.3843 -0.0907 0.0304  -0.0662 196 ALA A N   
1432 C  CA  . ALA A 196 ? 0.2818 0.5514 0.3767 -0.0776 0.0320  -0.0745 196 ALA A CA  
1433 C  C   . ALA A 196 ? 0.3028 0.5934 0.3973 -0.0788 0.0413  -0.0842 196 ALA A C   
1434 O  O   . ALA A 196 ? 0.2925 0.5727 0.3799 -0.0735 0.0428  -0.0893 196 ALA A O   
1435 C  CB  . ALA A 196 ? 0.2784 0.5509 0.3971 -0.0630 0.0289  -0.0797 196 ALA A CB  
1436 N  N   . GLU A 197 ? 0.2693 0.5906 0.3710 -0.0863 0.0478  -0.0873 197 GLU A N   
1437 C  CA  . GLU A 197 ? 0.3137 0.6571 0.4138 -0.0880 0.0575  -0.0974 197 GLU A CA  
1438 C  C   . GLU A 197 ? 0.3227 0.6537 0.3944 -0.0986 0.0585  -0.0913 197 GLU A C   
1439 O  O   . GLU A 197 ? 0.3441 0.6834 0.4097 -0.0973 0.0643  -0.0998 197 GLU A O   
1440 C  CB  . GLU A 197 ? 0.3341 0.7155 0.4480 -0.0948 0.0648  -0.1013 197 GLU A CB  
1441 C  CG  . GLU A 197 ? 0.4506 0.8603 0.5757 -0.0890 0.0753  -0.1175 197 GLU A CG  
1442 C  CD  . GLU A 197 ? 0.4845 0.8910 0.6323 -0.0696 0.0745  -0.1298 197 GLU A CD  
1443 O  OE1 . GLU A 197 ? 0.4112 0.8134 0.5774 -0.0614 0.0683  -0.1272 197 GLU A OE1 
1444 O  OE2 . GLU A 197 ? 0.5100 0.9152 0.6556 -0.0627 0.0789  -0.1414 197 GLU A OE2 
1445 N  N   . LEU A 198 ? 0.3186 0.6293 0.3730 -0.1088 0.0526  -0.0771 198 LEU A N   
1446 C  CA  . LEU A 198 ? 0.3137 0.6111 0.3419 -0.1187 0.0523  -0.0691 198 LEU A CA  
1447 C  C   . LEU A 198 ? 0.3260 0.5943 0.3438 -0.1100 0.0468  -0.0684 198 LEU A C   
1448 O  O   . LEU A 198 ? 0.3425 0.6012 0.3400 -0.1163 0.0461  -0.0627 198 LEU A O   
1449 C  CB  . LEU A 198 ? 0.3323 0.6188 0.3475 -0.1331 0.0481  -0.0541 198 LEU A CB  
1450 C  CG  . LEU A 198 ? 0.3326 0.6483 0.3510 -0.1471 0.0542  -0.0522 198 LEU A CG  
1451 C  CD1 . LEU A 198 ? 0.3518 0.6519 0.3527 -0.1632 0.0501  -0.0366 198 LEU A CD1 
1452 C  CD2 . LEU A 198 ? 0.3464 0.6902 0.3614 -0.1504 0.0642  -0.0601 198 LEU A CD2 
1453 N  N   . LEU A 199 ? 0.3086 0.5636 0.3400 -0.0964 0.0426  -0.0732 199 LEU A N   
1454 C  CA  . LEU A 199 ? 0.3124 0.5393 0.3355 -0.0889 0.0368  -0.0713 199 LEU A CA  
1455 C  C   . LEU A 199 ? 0.2996 0.5324 0.3280 -0.0797 0.0405  -0.0842 199 LEU A C   
1456 O  O   . LEU A 199 ? 0.3389 0.5939 0.3828 -0.0750 0.0466  -0.0963 199 LEU A O   
1457 C  CB  . LEU A 199 ? 0.3057 0.5127 0.3385 -0.0811 0.0297  -0.0673 199 LEU A CB  
1458 C  CG  . LEU A 199 ? 0.2784 0.4786 0.3067 -0.0899 0.0255  -0.0564 199 LEU A CG  
1459 C  CD1 . LEU A 199 ? 0.2174 0.3988 0.2531 -0.0819 0.0186  -0.0534 199 LEU A CD1 
1460 C  CD2 . LEU A 199 ? 0.2942 0.4802 0.2994 -0.1014 0.0237  -0.0457 199 LEU A CD2 
1461 N  N   . SER A 200 ? 0.3089 0.5219 0.3250 -0.0772 0.0367  -0.0822 200 SER A N   
1462 C  CA  . SER A 200 ? 0.3111 0.5274 0.3298 -0.0701 0.0393  -0.0943 200 SER A CA  
1463 C  C   . SER A 200 ? 0.3235 0.5122 0.3372 -0.0639 0.0322  -0.0904 200 SER A C   
1464 O  O   . SER A 200 ? 0.3148 0.4837 0.3250 -0.0638 0.0262  -0.0797 200 SER A O   
1465 C  CB  . SER A 200 ? 0.3621 0.5969 0.3653 -0.0791 0.0450  -0.0976 200 SER A CB  
1466 O  OG  . SER A 200 ? 0.4240 0.6445 0.4050 -0.0872 0.0402  -0.0848 200 SER A OG  
1467 N  N   . ARG A 201 ? 0.2938 0.4825 0.3072 -0.0592 0.0333  -0.0999 201 ARG A N   
1468 C  CA  . ARG A 201 ? 0.2918 0.4576 0.3032 -0.0532 0.0272  -0.0979 201 ARG A CA  
1469 C  C   . ARG A 201 ? 0.3270 0.4750 0.3206 -0.0587 0.0211  -0.0830 201 ARG A C   
1470 O  O   . ARG A 201 ? 0.3546 0.5084 0.3317 -0.0678 0.0216  -0.0769 201 ARG A O   
1471 C  CB  . ARG A 201 ? 0.3397 0.5117 0.3495 -0.0510 0.0294  -0.1102 201 ARG A CB  
1472 N  N   . ASP A 203 ? 0.2745 0.3907 0.2625 -0.0640 0.0120  -0.0564 203 ASP A N   
1473 C  CA  . ASP A 203 ? 0.2784 0.3913 0.2672 -0.0685 0.0106  -0.0492 203 ASP A CA  
1474 C  C   . ASP A 203 ? 0.2752 0.3783 0.2778 -0.0600 0.0076  -0.0503 203 ASP A C   
1475 O  O   . ASP A 203 ? 0.2797 0.3872 0.2964 -0.0515 0.0088  -0.0583 203 ASP A O   
1476 C  CB  . ASP A 203 ? 0.2766 0.4138 0.2697 -0.0757 0.0161  -0.0522 203 ASP A CB  
1477 C  CG  . ASP A 203 ? 0.3416 0.4899 0.3191 -0.0859 0.0194  -0.0496 203 ASP A CG  
1478 O  OD1 . ASP A 203 ? 0.3469 0.4809 0.3086 -0.0888 0.0159  -0.0423 203 ASP A OD1 
1479 O  OD2 . ASP A 203 ? 0.2987 0.4711 0.2800 -0.0911 0.0255  -0.0545 203 ASP A OD2 
1480 N  N   . ILE A 204 ? 0.2587 0.3483 0.2570 -0.0626 0.0036  -0.0421 204 ILE A N   
1481 C  CA  . ILE A 204 ? 0.2548 0.3333 0.2619 -0.0558 0.0000  -0.0412 204 ILE A CA  
1482 C  C   . ILE A 204 ? 0.2494 0.3331 0.2595 -0.0612 -0.0012 -0.0376 204 ILE A C   
1483 O  O   . ILE A 204 ? 0.2190 0.2963 0.2171 -0.0700 -0.0026 -0.0312 204 ILE A O   
1484 C  CB  . ILE A 204 ? 0.3097 0.3644 0.3067 -0.0531 -0.0043 -0.0354 204 ILE A CB  
1485 C  CG1 . ILE A 204 ? 0.2973 0.3484 0.2917 -0.0486 -0.0038 -0.0385 204 ILE A CG1 
1486 C  CG2 . ILE A 204 ? 0.2851 0.3300 0.2888 -0.0477 -0.0076 -0.0338 204 ILE A CG2 
1487 C  CD1 . ILE A 204 ? 0.2882 0.3204 0.2696 -0.0489 -0.0074 -0.0317 204 ILE A CD1 
1488 N  N   . ILE A 205 ? 0.2022 0.2961 0.2283 -0.0560 -0.0015 -0.0413 205 ILE A N   
1489 C  CA  . ILE A 205 ? 0.2265 0.3253 0.2565 -0.0602 -0.0041 -0.0377 205 ILE A CA  
1490 C  C   . ILE A 205 ? 0.2169 0.2967 0.2439 -0.0561 -0.0095 -0.0333 205 ILE A C   
1491 O  O   . ILE A 205 ? 0.2268 0.3028 0.2627 -0.0468 -0.0109 -0.0351 205 ILE A O   
1492 C  CB  . ILE A 205 ? 0.1987 0.3214 0.2488 -0.0566 -0.0022 -0.0434 205 ILE A CB  
1493 C  CG1 . ILE A 205 ? 0.2065 0.3510 0.2592 -0.0616 0.0043  -0.0486 205 ILE A CG1 
1494 C  CG2 . ILE A 205 ? 0.1719 0.2998 0.2269 -0.0603 -0.0064 -0.0391 205 ILE A CG2 
1495 C  CD1 . ILE A 205 ? 0.2242 0.3921 0.2991 -0.0546 0.0075  -0.0570 205 ILE A CD1 
1496 N  N   . THR A 206 ? 0.2131 0.2807 0.2274 -0.0633 -0.0125 -0.0277 206 THR A N   
1497 C  CA  . THR A 206 ? 0.2230 0.2748 0.2331 -0.0605 -0.0170 -0.0244 206 THR A CA  
1498 C  C   . THR A 206 ? 0.2707 0.3329 0.2871 -0.0641 -0.0204 -0.0232 206 THR A C   
1499 O  O   . THR A 206 ? 0.2681 0.3490 0.2920 -0.0696 -0.0192 -0.0244 206 THR A O   
1500 C  CB  . THR A 206 ? 0.2476 0.2773 0.2398 -0.0647 -0.0183 -0.0204 206 THR A CB  
1501 O  OG1 . THR A 206 ? 0.2174 0.2323 0.2058 -0.0600 -0.0214 -0.0189 206 THR A OG1 
1502 C  CG2 . THR A 206 ? 0.2297 0.2585 0.2128 -0.0769 -0.0190 -0.0173 206 THR A CG2 
1503 N  N   . HIS A 207 ? 0.2232 0.2748 0.2367 -0.0613 -0.0246 -0.0208 207 HIS A N   
1504 C  CA  . HIS A 207 ? 0.2203 0.2830 0.2412 -0.0624 -0.0290 -0.0194 207 HIS A CA  
1505 C  C   . HIS A 207 ? 0.2278 0.3112 0.2694 -0.0552 -0.0286 -0.0216 207 HIS A C   
1506 O  O   . HIS A 207 ? 0.2138 0.3155 0.2657 -0.0579 -0.0308 -0.0215 207 HIS A O   
1507 C  CB  . HIS A 207 ? 0.2167 0.2848 0.2318 -0.0748 -0.0308 -0.0183 207 HIS A CB  
1508 C  CG  . HIS A 207 ? 0.2194 0.2659 0.2156 -0.0820 -0.0309 -0.0169 207 HIS A CG  
1509 N  ND1 . HIS A 207 ? 0.2419 0.2670 0.2269 -0.0778 -0.0321 -0.0161 207 HIS A ND1 
1510 C  CD2 . HIS A 207 ? 0.3117 0.3541 0.2990 -0.0930 -0.0299 -0.0158 207 HIS A CD2 
1511 C  CE1 . HIS A 207 ? 0.2603 0.2687 0.2312 -0.0847 -0.0319 -0.0154 207 HIS A CE1 
1512 N  NE2 . HIS A 207 ? 0.2663 0.2836 0.2379 -0.0943 -0.0309 -0.0147 207 HIS A NE2 
1513 N  N   . CYS A 208 ? 0.2067 0.2870 0.2553 -0.0457 -0.0261 -0.0239 208 CYS A N   
1514 C  CA  . CYS A 208 ? 0.2177 0.3157 0.2866 -0.0385 -0.0244 -0.0278 208 CYS A CA  
1515 C  C   . CYS A 208 ? 0.2373 0.3449 0.3202 -0.0330 -0.0298 -0.0247 208 CYS A C   
1516 O  O   . CYS A 208 ? 0.1998 0.3247 0.3019 -0.0273 -0.0291 -0.0278 208 CYS A O   
1517 C  CB  . CYS A 208 ? 0.2008 0.2903 0.2729 -0.0304 -0.0209 -0.0316 208 CYS A CB  
1518 S  SG  . CYS A 208 ? 0.2408 0.3102 0.3108 -0.0224 -0.0244 -0.0272 208 CYS A SG  
1519 N  N   . TYR A 209 ? 0.2162 0.3139 0.2906 -0.0343 -0.0351 -0.0189 209 TYR A N   
1520 C  CA  . TYR A 209 ? 0.2015 0.3090 0.2874 -0.0299 -0.0412 -0.0143 209 TYR A CA  
1521 C  C   . TYR A 209 ? 0.2030 0.3178 0.2813 -0.0395 -0.0462 -0.0112 209 TYR A C   
1522 O  O   . TYR A 209 ? 0.2045 0.3199 0.2819 -0.0385 -0.0524 -0.0058 209 TYR A O   
1523 C  CB  . TYR A 209 ? 0.2348 0.3267 0.3183 -0.0227 -0.0439 -0.0095 209 TYR A CB  
1524 C  CG  . TYR A 209 ? 0.2360 0.3210 0.3294 -0.0135 -0.0401 -0.0125 209 TYR A CG  
1525 C  CD1 . TYR A 209 ? 0.2308 0.3295 0.3448 -0.0068 -0.0382 -0.0171 209 TYR A CD1 
1526 C  CD2 . TYR A 209 ? 0.2630 0.3286 0.3461 -0.0116 -0.0383 -0.0113 209 TYR A CD2 
1527 C  CE1 . TYR A 209 ? 0.2577 0.3488 0.3805 0.0010  -0.0349 -0.0212 209 TYR A CE1 
1528 C  CE2 . TYR A 209 ? 0.2600 0.3194 0.3525 -0.0043 -0.0352 -0.0145 209 TYR A CE2 
1529 C  CZ  . TYR A 209 ? 0.2570 0.3284 0.3688 0.0017  -0.0337 -0.0196 209 TYR A CZ  
1530 O  OH  . TYR A 209 ? 0.2800 0.3442 0.4010 0.0083  -0.0307 -0.0241 209 TYR A OH  
1531 N  N   . ASN A 210 ? 0.2358 0.3560 0.3078 -0.0495 -0.0437 -0.0142 210 ASN A N   
1532 C  CA  . ASN A 210 ? 0.2416 0.3705 0.3085 -0.0599 -0.0485 -0.0122 210 ASN A CA  
1533 C  C   . ASN A 210 ? 0.2281 0.3833 0.3155 -0.0570 -0.0531 -0.0106 210 ASN A C   
1534 O  O   . ASN A 210 ? 0.2148 0.3846 0.3217 -0.0489 -0.0507 -0.0129 210 ASN A O   
1535 C  CB  . ASN A 210 ? 0.2358 0.3654 0.2940 -0.0718 -0.0445 -0.0153 210 ASN A CB  
1536 C  CG  . ASN A 210 ? 0.2532 0.4072 0.3285 -0.0725 -0.0404 -0.0188 210 ASN A CG  
1537 O  OD1 . ASN A 210 ? 0.2473 0.4238 0.3347 -0.0765 -0.0433 -0.0185 210 ASN A OD1 
1538 N  ND2 . ASN A 210 ? 0.2569 0.4081 0.3333 -0.0689 -0.0336 -0.0225 210 ASN A ND2 
1539 N  N   . GLY A 211 ? 0.1977 0.3595 0.2811 -0.0634 -0.0601 -0.0071 211 GLY A N   
1540 C  CA  . GLY A 211 ? 0.2120 0.4006 0.3140 -0.0622 -0.0660 -0.0047 211 GLY A CA  
1541 C  C   . GLY A 211 ? 0.2440 0.4531 0.3507 -0.0741 -0.0659 -0.0075 211 GLY A C   
1542 O  O   . GLY A 211 ? 0.2268 0.4591 0.3467 -0.0756 -0.0721 -0.0052 211 GLY A O   
1543 N  N   . LYS A 212 ? 0.2252 0.4270 0.3218 -0.0829 -0.0594 -0.0117 212 LYS A N   
1544 C  CA  . LYS A 212 ? 0.2631 0.4828 0.3629 -0.0960 -0.0582 -0.0138 212 LYS A CA  
1545 C  C   . LYS A 212 ? 0.2503 0.4981 0.3745 -0.0909 -0.0534 -0.0171 212 LYS A C   
1546 O  O   . LYS A 212 ? 0.2179 0.4679 0.3551 -0.0770 -0.0510 -0.0185 212 LYS A O   
1547 C  CB  . LYS A 212 ? 0.2540 0.4516 0.3323 -0.1071 -0.0534 -0.0155 212 LYS A CB  
1548 C  CG  . LYS A 212 ? 0.3257 0.4964 0.3815 -0.1115 -0.0578 -0.0138 212 LYS A CG  
1549 C  CD  . LYS A 212 ? 0.3909 0.5381 0.4270 -0.1216 -0.0536 -0.0152 212 LYS A CD  
1550 C  CE  . LYS A 212 ? 0.4521 0.5781 0.4687 -0.1285 -0.0587 -0.0152 212 LYS A CE  
1551 N  NZ  . LYS A 212 ? 0.5496 0.6461 0.5474 -0.1327 -0.0546 -0.0163 212 LYS A NZ  
1552 N  N   . PRO A 213 ? 0.2451 0.5159 0.3771 -0.1019 -0.0519 -0.0188 213 PRO A N   
1553 C  CA  . PRO A 213 ? 0.2034 0.5047 0.3604 -0.0964 -0.0468 -0.0229 213 PRO A CA  
1554 C  C   . PRO A 213 ? 0.2309 0.5254 0.3883 -0.0889 -0.0371 -0.0279 213 PRO A C   
1555 O  O   . PRO A 213 ? 0.2162 0.5302 0.3951 -0.0781 -0.0336 -0.0323 213 PRO A O   
1556 C  CB  . PRO A 213 ? 0.2625 0.5859 0.4221 -0.1131 -0.0458 -0.0234 213 PRO A CB  
1557 C  CG  . PRO A 213 ? 0.2476 0.5599 0.3927 -0.1238 -0.0546 -0.0191 213 PRO A CG  
1558 C  CD  . PRO A 213 ? 0.2487 0.5231 0.3711 -0.1192 -0.0559 -0.0173 213 PRO A CD  
1559 N  N   . ASN A 214 ? 0.2140 0.4821 0.3490 -0.0938 -0.0330 -0.0278 214 ASN A N   
1560 C  CA  . ASN A 214 ? 0.2316 0.4933 0.3651 -0.0874 -0.0247 -0.0325 214 ASN A CA  
1561 C  C   . ASN A 214 ? 0.2616 0.5018 0.3933 -0.0729 -0.0261 -0.0325 214 ASN A C   
1562 O  O   . ASN A 214 ? 0.2867 0.5074 0.4057 -0.0708 -0.0220 -0.0340 214 ASN A O   
1563 C  CB  . ASN A 214 ? 0.2886 0.5353 0.4003 -0.1002 -0.0199 -0.0314 214 ASN A CB  
1564 C  CG  . ASN A 214 ? 0.3084 0.5811 0.4267 -0.1102 -0.0131 -0.0341 214 ASN A CG  
1565 O  OD1 . ASN A 214 ? 0.2808 0.5840 0.4211 -0.1065 -0.0109 -0.0383 214 ASN A OD1 
1566 N  ND2 . ASN A 214 ? 0.3268 0.5879 0.4264 -0.1232 -0.0099 -0.0313 214 ASN A ND2 
1567 N  N   . ARG A 215 ? 0.2303 0.4745 0.3750 -0.0633 -0.0326 -0.0302 215 ARG A N   
1568 C  CA  . ARG A 215 ? 0.1998 0.4267 0.3465 -0.0496 -0.0342 -0.0295 215 ARG A CA  
1569 C  C   . ARG A 215 ? 0.2293 0.4657 0.3931 -0.0386 -0.0277 -0.0369 215 ARG A C   
1570 O  O   . ARG A 215 ? 0.1749 0.4370 0.3545 -0.0388 -0.0232 -0.0424 215 ARG A O   
1571 C  CB  . ARG A 215 ? 0.2140 0.4447 0.3702 -0.0436 -0.0434 -0.0234 215 ARG A CB  
1572 C  CG  . ARG A 215 ? 0.1985 0.4623 0.3792 -0.0418 -0.0465 -0.0238 215 ARG A CG  
1573 C  CD  . ARG A 215 ? 0.2166 0.4811 0.4068 -0.0331 -0.0561 -0.0168 215 ARG A CD  
1574 N  NE  . ARG A 215 ? 0.1714 0.4355 0.3482 -0.0437 -0.0639 -0.0106 215 ARG A NE  
1575 C  CZ  . ARG A 215 ? 0.1903 0.4663 0.3761 -0.0408 -0.0735 -0.0041 215 ARG A CZ  
1576 N  NH1 . ARG A 215 ? 0.1733 0.4603 0.3819 -0.0268 -0.0770 -0.0015 215 ARG A NH1 
1577 N  NH2 . ARG A 215 ? 0.1845 0.4603 0.3556 -0.0522 -0.0800 0.0000  215 ARG A NH2 
1578 N  N   . ILE A 216 ? 0.1979 0.4136 0.3585 -0.0292 -0.0268 -0.0378 216 ILE A N   
1579 C  CA  . ILE A 216 ? 0.2260 0.4471 0.4007 -0.0194 -0.0205 -0.0462 216 ILE A CA  
1580 C  C   . ILE A 216 ? 0.2250 0.4623 0.4279 -0.0065 -0.0231 -0.0481 216 ILE A C   
1581 O  O   . ILE A 216 ? 0.2275 0.4714 0.4451 0.0023  -0.0177 -0.0568 216 ILE A O   
1582 C  CB  . ILE A 216 ? 0.1959 0.3899 0.3588 -0.0144 -0.0187 -0.0473 216 ILE A CB  
1583 C  CG1 . ILE A 216 ? 0.2222 0.3981 0.3848 -0.0077 -0.0261 -0.0396 216 ILE A CG1 
1584 C  CG2 . ILE A 216 ? 0.2147 0.3944 0.3524 -0.0254 -0.0154 -0.0464 216 ILE A CG2 
1585 C  CD1 . ILE A 216 ? 0.2031 0.3539 0.3556 -0.0035 -0.0244 -0.0402 216 ILE A CD1 
1586 N  N   . LEU A 217 ? 0.1801 0.4236 0.3909 -0.0048 -0.0315 -0.0404 217 LEU A N   
1587 C  CA  . LEU A 217 ? 0.2076 0.4676 0.4465 0.0076  -0.0355 -0.0403 217 LEU A CA  
1588 C  C   . LEU A 217 ? 0.2127 0.5067 0.4672 0.0033  -0.0358 -0.0419 217 LEU A C   
1589 O  O   . LEU A 217 ? 0.1892 0.4896 0.4313 -0.0098 -0.0382 -0.0377 217 LEU A O   
1590 C  CB  . LEU A 217 ? 0.1999 0.4459 0.4379 0.0128  -0.0457 -0.0291 217 LEU A CB  
1591 C  CG  . LEU A 217 ? 0.1886 0.4025 0.4118 0.0162  -0.0462 -0.0258 217 LEU A CG  
1592 C  CD1 . LEU A 217 ? 0.2051 0.4094 0.4243 0.0181  -0.0562 -0.0134 217 LEU A CD1 
1593 C  CD2 . LEU A 217 ? 0.2017 0.4092 0.4409 0.0287  -0.0416 -0.0330 217 LEU A CD2 
1594 N  N   . ASN A 218 ? 0.1536 0.4696 0.4363 0.0142  -0.0335 -0.0483 218 ASN A N   
1595 C  CA  . ASN A 218 ? 0.1809 0.5327 0.4828 0.0116  -0.0343 -0.0495 218 ASN A CA  
1596 C  C   . ASN A 218 ? 0.1824 0.5406 0.4951 0.0157  -0.0467 -0.0386 218 ASN A C   
1597 O  O   . ASN A 218 ? 0.1587 0.4937 0.4640 0.0209  -0.0536 -0.0306 218 ASN A O   
1598 C  CB  . ASN A 218 ? 0.1997 0.5746 0.5280 0.0219  -0.0259 -0.0619 218 ASN A CB  
1599 C  CG  . ASN A 218 ? 0.1959 0.5642 0.5478 0.0416  -0.0288 -0.0636 218 ASN A CG  
1600 O  OD1 . ASN A 218 ? 0.1773 0.5357 0.5347 0.0484  -0.0390 -0.0535 218 ASN A OD1 
1601 N  ND2 . ASN A 218 ? 0.2307 0.6024 0.5946 0.0502  -0.0196 -0.0762 218 ASN A ND2 
1602 N  N   . PRO A 219 ? 0.1563 0.5468 0.4852 0.0122  -0.0500 -0.0374 219 PRO A N   
1603 C  CA  . PRO A 219 ? 0.1602 0.5583 0.4980 0.0152  -0.0630 -0.0262 219 PRO A CA  
1604 C  C   . PRO A 219 ? 0.1638 0.5593 0.5255 0.0348  -0.0685 -0.0231 219 PRO A C   
1605 O  O   . PRO A 219 ? 0.1848 0.5793 0.5495 0.0381  -0.0801 -0.0117 219 PRO A O   
1606 C  CB  . PRO A 219 ? 0.1621 0.5945 0.5126 0.0070  -0.0634 -0.0270 219 PRO A CB  
1607 C  CG  . PRO A 219 ? 0.1595 0.5931 0.4933 -0.0075 -0.0526 -0.0346 219 PRO A CG  
1608 C  CD  . PRO A 219 ? 0.1543 0.5743 0.4878 0.0010  -0.0432 -0.0440 219 PRO A CD  
1609 N  N   . ALA A 220 ? 0.2029 0.5968 0.5816 0.0475  -0.0610 -0.0326 220 ALA A N   
1610 C  CA  . ALA A 220 ? 0.1965 0.5789 0.5934 0.0655  -0.0651 -0.0284 220 ALA A CA  
1611 C  C   . ALA A 220 ? 0.1936 0.5396 0.5762 0.0695  -0.0680 -0.0242 220 ALA A C   
1612 O  O   . ALA A 220 ? 0.2292 0.5619 0.6254 0.0836  -0.0714 -0.0205 220 ALA A O   
1613 C  CB  . ALA A 220 ? 0.1971 0.5865 0.6118 0.0763  -0.0544 -0.0392 220 ALA A CB  
1614 N  N   . GLY A 221 ? 0.2112 0.5359 0.5611 0.0562  -0.0653 -0.0228 221 GLY A N   
1615 C  CA  . GLY A 221 ? 0.2186 0.5075 0.5504 0.0578  -0.0665 -0.0177 221 GLY A CA  
1616 C  C   . GLY A 221 ? 0.2543 0.5257 0.5858 0.0633  -0.0568 -0.0288 221 GLY A C   
1617 O  O   . GLY A 221 ? 0.2731 0.5164 0.5959 0.0670  -0.0581 -0.0250 221 GLY A O   
1618 N  N   . GLU A 222 ? 0.2286 0.5167 0.5689 0.0630  -0.0470 -0.0423 222 GLU A N   
1619 C  CA  . GLU A 222 ? 0.2288 0.5033 0.5678 0.0671  -0.0375 -0.0545 222 GLU A CA  
1620 C  C   . GLU A 222 ? 0.2302 0.5014 0.5423 0.0522  -0.0295 -0.0598 222 GLU A C   
1621 O  O   . GLU A 222 ? 0.1573 0.4405 0.4566 0.0397  -0.0301 -0.0562 222 GLU A O   
1622 C  CB  . GLU A 222 ? 0.2390 0.5353 0.6090 0.0793  -0.0317 -0.0673 222 GLU A CB  
1623 C  CG  . GLU A 222 ? 0.2606 0.5611 0.6531 0.0924  -0.0392 -0.0596 222 GLU A CG  
1624 C  CD  . GLU A 222 ? 0.2915 0.5669 0.6921 0.1058  -0.0379 -0.0622 222 GLU A CD  
1625 O  OE1 . GLU A 222 ? 0.3570 0.6101 0.7463 0.1043  -0.0336 -0.0683 222 GLU A OE1 
1626 O  OE2 . GLU A 222 ? 0.4246 0.7027 0.8428 0.1171  -0.0414 -0.0582 222 GLU A OE2 
1627 N  N   . LEU A 223 ? 0.2187 0.4728 0.5224 0.0535  -0.0226 -0.0682 223 LEU A N   
1628 C  CA  . LEU A 223 ? 0.2221 0.4724 0.5009 0.0404  -0.0156 -0.0725 223 LEU A CA  
1629 C  C   . LEU A 223 ? 0.2271 0.5081 0.5131 0.0355  -0.0076 -0.0822 223 LEU A C   
1630 O  O   . LEU A 223 ? 0.2220 0.5223 0.5324 0.0451  -0.0035 -0.0919 223 LEU A O   
1631 C  CB  . LEU A 223 ? 0.2301 0.4566 0.4990 0.0431  -0.0109 -0.0791 223 LEU A CB  
1632 C  CG  . LEU A 223 ? 0.2290 0.4419 0.4678 0.0302  -0.0074 -0.0782 223 LEU A CG  
1633 C  CD1 . LEU A 223 ? 0.2246 0.4210 0.4441 0.0228  -0.0147 -0.0645 223 LEU A CD1 
1634 C  CD2 . LEU A 223 ? 0.2603 0.4552 0.4935 0.0337  -0.0028 -0.0863 223 LEU A CD2 
1635 N  N   . ARG A 224 ? 0.2166 0.5029 0.4821 0.0205  -0.0054 -0.0795 224 ARG A N   
1636 C  CA  . ARG A 224 ? 0.2812 0.5958 0.5504 0.0137  0.0031  -0.0879 224 ARG A CA  
1637 C  C   . ARG A 224 ? 0.2459 0.5593 0.5145 0.0175  0.0127  -0.1013 224 ARG A C   
1638 O  O   . ARG A 224 ? 0.2441 0.5322 0.4961 0.0171  0.0133  -0.1017 224 ARG A O   
1639 C  CB  . ARG A 224 ? 0.2826 0.5981 0.5278 -0.0042 0.0033  -0.0811 224 ARG A CB  
1640 C  CG  . ARG A 224 ? 0.2531 0.5646 0.4941 -0.0094 -0.0066 -0.0687 224 ARG A CG  
1641 C  CD  . ARG A 224 ? 0.2932 0.6333 0.5392 -0.0204 -0.0063 -0.0672 224 ARG A CD  
1642 N  NE  . ARG A 224 ? 0.3459 0.6744 0.5747 -0.0315 -0.0141 -0.0564 224 ARG A NE  
1643 C  CZ  . ARG A 224 ? 0.3158 0.6517 0.5318 -0.0476 -0.0130 -0.0535 224 ARG A CZ  
1644 N  NH1 . ARG A 224 ? 0.3694 0.7254 0.5867 -0.0556 -0.0045 -0.0592 224 ARG A NH1 
1645 N  NH2 . ARG A 224 ? 0.2814 0.6038 0.4823 -0.0565 -0.0205 -0.0450 224 ARG A NH2 
1646 N  N   . SER A 225 ? 0.2286 0.5711 0.5162 0.0213  0.0203  -0.1128 225 SER A N   
1647 C  CA  . SER A 225 ? 0.2610 0.6054 0.5483 0.0248  0.0300  -0.1274 225 SER A CA  
1648 C  C   . SER A 225 ? 0.2755 0.6130 0.5323 0.0100  0.0350  -0.1269 225 SER A C   
1649 O  O   . SER A 225 ? 0.2729 0.5982 0.5199 0.0115  0.0394  -0.1347 225 SER A O   
1650 C  CB  . SER A 225 ? 0.2637 0.6342 0.5689 0.0303  0.0368  -0.1373 225 SER A CB  
1651 O  OG  . SER A 225 ? 0.3232 0.7184 0.6254 0.0188  0.0389  -0.1327 225 SER A OG  
1652 N  N   . SER A 226 ? 0.2533 0.5975 0.4947 -0.0046 0.0339  -0.1174 226 SER A N   
1653 C  CA  . SER A 226 ? 0.2820 0.6162 0.4942 -0.0183 0.0371  -0.1145 226 SER A CA  
1654 C  C   . SER A 226 ? 0.2475 0.5448 0.4414 -0.0168 0.0314  -0.1085 226 SER A C   
1655 O  O   . SER A 226 ? 0.2378 0.5245 0.4145 -0.0205 0.0351  -0.1118 226 SER A O   
1656 C  CB  . SER A 226 ? 0.2929 0.6375 0.4936 -0.0340 0.0357  -0.1043 226 SER A CB  
1657 O  OG  . SER A 226 ? 0.2576 0.5864 0.4565 -0.0347 0.0257  -0.0926 226 SER A OG  
1658 N  N   . ILE A 227 ? 0.2527 0.5319 0.4506 -0.0111 0.0225  -0.1000 227 ILE A N   
1659 C  CA  . ILE A 227 ? 0.2459 0.4923 0.4280 -0.0096 0.0176  -0.0944 227 ILE A CA  
1660 C  C   . ILE A 227 ? 0.2518 0.4885 0.4426 0.0018  0.0201  -0.1044 227 ILE A C   
1661 O  O   . ILE A 227 ? 0.2348 0.4518 0.4101 0.0003  0.0203  -0.1047 227 ILE A O   
1662 C  CB  . ILE A 227 ? 0.2289 0.4609 0.4119 -0.0077 0.0080  -0.0825 227 ILE A CB  
1663 C  CG1 . ILE A 227 ? 0.2485 0.4879 0.4204 -0.0206 0.0054  -0.0739 227 ILE A CG1 
1664 C  CG2 . ILE A 227 ? 0.2186 0.4190 0.3868 -0.0057 0.0038  -0.0773 227 ILE A CG2 
1665 C  CD1 . ILE A 227 ? 0.2366 0.4667 0.3829 -0.0335 0.0084  -0.0711 227 ILE A CD1 
1666 N  N   . THR A 228 ? 0.2628 0.5131 0.4794 0.0134  0.0219  -0.1130 228 THR A N   
1667 C  CA  . THR A 228 ? 0.2655 0.5070 0.4920 0.0238  0.0250  -0.1245 228 THR A CA  
1668 C  C   . THR A 228 ? 0.2520 0.5003 0.4649 0.0178  0.0335  -0.1356 228 THR A C   
1669 O  O   . THR A 228 ? 0.2716 0.5016 0.4746 0.0187  0.0337  -0.1393 228 THR A O   
1670 C  CB  . THR A 228 ? 0.2783 0.5350 0.5365 0.0374  0.0258  -0.1325 228 THR A CB  
1671 O  OG1 . THR A 228 ? 0.2414 0.5016 0.5109 0.0401  0.0181  -0.1209 228 THR A OG1 
1672 C  CG2 . THR A 228 ? 0.3373 0.5743 0.6073 0.0496  0.0251  -0.1402 228 THR A CG2 
1673 N  N   . ARG A 229 ? 0.2506 0.5266 0.4625 0.0108  0.0405  -0.1406 229 ARG A N   
1674 C  CA  . ARG A 229 ? 0.2332 0.5177 0.4299 0.0038  0.0485  -0.1501 229 ARG A CA  
1675 C  C   . ARG A 229 ? 0.2910 0.5560 0.4577 -0.0075 0.0454  -0.1400 229 ARG A C   
1676 O  O   . ARG A 229 ? 0.3032 0.5618 0.4568 -0.0097 0.0483  -0.1461 229 ARG A O   
1677 C  CB  . ARG A 229 ? 0.2729 0.5927 0.4737 -0.0026 0.0569  -0.1560 229 ARG A CB  
1678 C  CG  . ARG A 229 ? 0.2658 0.6091 0.4977 0.0080  0.0598  -0.1644 229 ARG A CG  
1679 C  CD  . ARG A 229 ? 0.3013 0.6720 0.5291 0.0005  0.0678  -0.1697 229 ARG A CD  
1680 N  NE  . ARG A 229 ? 0.3265 0.7136 0.5545 -0.0090 0.0661  -0.1583 229 ARG A NE  
1681 C  CZ  . ARG A 229 ? 0.3482 0.7445 0.5963 -0.0031 0.0621  -0.1543 229 ARG A CZ  
1682 N  NH1 . ARG A 229 ? 0.3327 0.7242 0.6030 0.0129  0.0597  -0.1598 229 ARG A NH1 
1683 N  NH2 . ARG A 229 ? 0.3534 0.7631 0.5989 -0.0138 0.0600  -0.1437 229 ARG A NH2 
1684 N  N   . ALA A 230 ? 0.2473 0.5030 0.4033 -0.0147 0.0394  -0.1250 230 ALA A N   
1685 C  CA  . ALA A 230 ? 0.2745 0.5104 0.4041 -0.0241 0.0361  -0.1153 230 ALA A CA  
1686 C  C   . ALA A 230 ? 0.2814 0.4906 0.4073 -0.0172 0.0318  -0.1156 230 ALA A C   
1687 O  O   . ALA A 230 ? 0.2547 0.4552 0.3642 -0.0213 0.0327  -0.1168 230 ALA A O   
1688 C  CB  . ALA A 230 ? 0.2465 0.4757 0.3679 -0.0317 0.0303  -0.1007 230 ALA A CB  
1689 N  N   . LEU A 231 ? 0.2460 0.4430 0.3875 -0.0071 0.0268  -0.1139 231 LEU A N   
1690 C  CA  . LEU A 231 ? 0.2536 0.4272 0.3952 -0.0004 0.0234  -0.1150 231 LEU A CA  
1691 C  C   . LEU A 231 ? 0.2886 0.4670 0.4341 0.0032  0.0290  -0.1301 231 LEU A C   
1692 O  O   . LEU A 231 ? 0.2714 0.4346 0.4064 0.0023  0.0278  -0.1315 231 LEU A O   
1693 C  CB  . LEU A 231 ? 0.2642 0.4278 0.4246 0.0097  0.0178  -0.1110 231 LEU A CB  
1694 C  CG  . LEU A 231 ? 0.2624 0.4183 0.4185 0.0070  0.0110  -0.0963 231 LEU A CG  
1695 C  CD1 . LEU A 231 ? 0.2539 0.4036 0.4299 0.0176  0.0058  -0.0932 231 LEU A CD1 
1696 C  CD2 . LEU A 231 ? 0.2681 0.4026 0.4022 0.0008  0.0074  -0.0873 231 LEU A CD2 
1697 N  N   . HIS A 232 ? 0.2459 0.4465 0.4067 0.0072  0.0353  -0.1423 232 HIS A N   
1698 C  CA  . HIS A 232 ? 0.3201 0.5270 0.4838 0.0101  0.0414  -0.1588 232 HIS A CA  
1699 C  C   . HIS A 232 ? 0.3218 0.5323 0.4599 -0.0013 0.0443  -0.1594 232 HIS A C   
1700 O  O   . HIS A 232 ? 0.3305 0.5339 0.4625 -0.0009 0.0453  -0.1679 232 HIS A O   
1701 C  CB  . HIS A 232 ? 0.2617 0.4951 0.4459 0.0159  0.0486  -0.1721 232 HIS A CB  
1702 C  CG  . HIS A 232 ? 0.3705 0.6105 0.5603 0.0204  0.0554  -0.1916 232 HIS A CG  
1703 N  ND1 . HIS A 232 ? 0.4142 0.6565 0.5833 0.0122  0.0590  -0.1979 232 HIS A ND1 
1704 C  CD2 . HIS A 232 ? 0.4057 0.6474 0.6167 0.0312  0.0576  -0.2043 232 HIS A CD2 
1705 C  CE1 . HIS A 232 ? 0.4256 0.6707 0.6022 0.0170  0.0629  -0.2137 232 HIS A CE1 
1706 N  NE2 . HIS A 232 ? 0.4584 0.7001 0.6587 0.0280  0.0612  -0.2162 232 HIS A NE2 
1707 N  N   . ARG A 233 ? 0.3103 0.5311 0.4330 -0.0119 0.0450  -0.1499 233 ARG A N   
1708 C  CA  . ARG A 233 ? 0.3051 0.5299 0.4031 -0.0232 0.0471  -0.1479 233 ARG A CA  
1709 C  C   . ARG A 233 ? 0.3288 0.5279 0.4094 -0.0265 0.0397  -0.1363 233 ARG A C   
1710 O  O   . ARG A 233 ? 0.3130 0.5127 0.3738 -0.0344 0.0401  -0.1344 233 ARG A O   
1711 C  CB  . ARG A 233 ? 0.3084 0.5531 0.3973 -0.0340 0.0506  -0.1412 233 ARG A CB  
1712 C  CG  . ARG A 233 ? 0.3127 0.5887 0.4159 -0.0329 0.0594  -0.1533 233 ARG A CG  
1713 C  CD  . ARG A 233 ? 0.3198 0.6162 0.4089 -0.0468 0.0636  -0.1466 233 ARG A CD  
1714 N  NE  . ARG A 233 ? 0.3322 0.6187 0.4178 -0.0522 0.0576  -0.1302 233 ARG A NE  
1715 C  CZ  . ARG A 233 ? 0.3127 0.6082 0.4160 -0.0495 0.0567  -0.1278 233 ARG A CZ  
1716 N  NH1 . ARG A 233 ? 0.2938 0.6094 0.4210 -0.0407 0.0615  -0.1397 233 ARG A NH1 
1717 N  NH2 . ARG A 233 ? 0.3088 0.5930 0.4061 -0.0555 0.0505  -0.1135 233 ARG A NH2 
1718 N  N   . GLY A 234 ? 0.2952 0.4732 0.3826 -0.0208 0.0332  -0.1282 234 GLY A N   
1719 C  CA  . GLY A 234 ? 0.3014 0.4566 0.3750 -0.0228 0.0269  -0.1184 234 GLY A CA  
1720 C  C   . GLY A 234 ? 0.2929 0.4378 0.3568 -0.0278 0.0221  -0.1028 234 GLY A C   
1721 O  O   . GLY A 234 ? 0.2317 0.3587 0.2837 -0.0294 0.0174  -0.0947 234 GLY A O   
1722 N  N   . VAL A 235 ? 0.2783 0.4345 0.3475 -0.0302 0.0232  -0.0991 235 VAL A N   
1723 C  CA  . VAL A 235 ? 0.2718 0.4174 0.3330 -0.0351 0.0184  -0.0858 235 VAL A CA  
1724 C  C   . VAL A 235 ? 0.2730 0.3991 0.3419 -0.0273 0.0126  -0.0811 235 VAL A C   
1725 O  O   . VAL A 235 ? 0.2347 0.3612 0.3210 -0.0184 0.0125  -0.0868 235 VAL A O   
1726 C  CB  . VAL A 235 ? 0.2584 0.4234 0.3257 -0.0400 0.0210  -0.0844 235 VAL A CB  
1727 C  CG1 . VAL A 235 ? 0.2733 0.4272 0.3333 -0.0454 0.0157  -0.0720 235 VAL A CG1 
1728 C  CG2 . VAL A 235 ? 0.2769 0.4621 0.3349 -0.0491 0.0273  -0.0881 235 VAL A CG2 
1729 N  N   . ARG A 236 ? 0.2617 0.3702 0.3175 -0.0306 0.0079  -0.0708 236 ARG A N   
1730 C  CA  . ARG A 236 ? 0.2702 0.3606 0.3300 -0.0245 0.0030  -0.0658 236 ARG A CA  
1731 C  C   . ARG A 236 ? 0.2583 0.3457 0.3167 -0.0273 -0.0006 -0.0573 236 ARG A C   
1732 O  O   . ARG A 236 ? 0.2644 0.3568 0.3135 -0.0356 -0.0003 -0.0533 236 ARG A O   
1733 C  CB  . ARG A 236 ? 0.2847 0.3574 0.3317 -0.0249 0.0006  -0.0622 236 ARG A CB  
1734 C  CG  . ARG A 236 ? 0.3358 0.4120 0.3826 -0.0234 0.0033  -0.0705 236 ARG A CG  
1735 C  CD  . ARG A 236 ? 0.3401 0.4206 0.4059 -0.0153 0.0049  -0.0799 236 ARG A CD  
1736 N  NE  . ARG A 236 ? 0.4547 0.5270 0.5222 -0.0120 0.0045  -0.0854 236 ARG A NE  
1737 C  CZ  . ARG A 236 ? 0.5071 0.5821 0.5642 -0.0157 0.0057  -0.0895 236 ARG A CZ  
1738 N  NH1 . ARG A 236 ? 0.5063 0.5926 0.5502 -0.0228 0.0079  -0.0889 236 ARG A NH1 
1739 N  NH2 . ARG A 236 ? 0.5139 0.5809 0.5741 -0.0129 0.0044  -0.0940 236 ARG A NH2 
1740 N  N   . LEU A 237 ? 0.2306 0.3095 0.2977 -0.0211 -0.0044 -0.0543 237 LEU A N   
1741 C  CA  . LEU A 237 ? 0.2251 0.3011 0.2907 -0.0232 -0.0085 -0.0469 237 LEU A CA  
1742 C  C   . LEU A 237 ? 0.2175 0.2728 0.2697 -0.0239 -0.0119 -0.0401 237 LEU A C   
1743 O  O   . LEU A 237 ? 0.2313 0.2758 0.2858 -0.0182 -0.0126 -0.0402 237 LEU A O   
1744 C  CB  . LEU A 237 ? 0.2555 0.3385 0.3397 -0.0159 -0.0108 -0.0473 237 LEU A CB  
1745 C  CG  . LEU A 237 ? 0.2370 0.3414 0.3386 -0.0128 -0.0074 -0.0550 237 LEU A CG  
1746 C  CD1 . LEU A 237 ? 0.2567 0.3652 0.3775 -0.0042 -0.0111 -0.0535 237 LEU A CD1 
1747 C  CD2 . LEU A 237 ? 0.1987 0.3199 0.2959 -0.0218 -0.0051 -0.0550 237 LEU A CD2 
1748 N  N   . ASP A 238 ? 0.2260 0.2760 0.2650 -0.0311 -0.0136 -0.0349 238 ASP A N   
1749 C  CA  . ASP A 238 ? 0.2469 0.2787 0.2740 -0.0316 -0.0165 -0.0294 238 ASP A CA  
1750 C  C   . ASP A 238 ? 0.2218 0.2543 0.2485 -0.0340 -0.0203 -0.0253 238 ASP A C   
1751 O  O   . ASP A 238 ? 0.2337 0.2784 0.2629 -0.0393 -0.0209 -0.0253 238 ASP A O   
1752 C  CB  . ASP A 238 ? 0.2515 0.2735 0.2623 -0.0377 -0.0156 -0.0275 238 ASP A CB  
1753 C  CG  . ASP A 238 ? 0.2600 0.2635 0.2594 -0.0376 -0.0181 -0.0231 238 ASP A CG  
1754 O  OD1 . ASP A 238 ? 0.2792 0.2742 0.2791 -0.0317 -0.0180 -0.0231 238 ASP A OD1 
1755 O  OD2 . ASP A 238 ? 0.2728 0.2706 0.2628 -0.0437 -0.0198 -0.0204 238 ASP A OD2 
1756 N  N   . VAL A 239 ? 0.2182 0.2392 0.2415 -0.0306 -0.0230 -0.0218 239 VAL A N   
1757 C  CA  . VAL A 239 ? 0.2294 0.2533 0.2531 -0.0321 -0.0271 -0.0181 239 VAL A CA  
1758 C  C   . VAL A 239 ? 0.2213 0.2409 0.2311 -0.0412 -0.0285 -0.0169 239 VAL A C   
1759 O  O   . VAL A 239 ? 0.2142 0.2451 0.2267 -0.0464 -0.0308 -0.0164 239 VAL A O   
1760 C  CB  . VAL A 239 ? 0.2337 0.2479 0.2566 -0.0265 -0.0291 -0.0145 239 VAL A CB  
1761 C  CG1 . VAL A 239 ? 0.2439 0.2603 0.2621 -0.0297 -0.0337 -0.0104 239 VAL A CG1 
1762 C  CG2 . VAL A 239 ? 0.1983 0.2170 0.2373 -0.0184 -0.0286 -0.0150 239 VAL A CG2 
1763 N  N   . GLY A 240 ? 0.2377 0.2408 0.2334 -0.0433 -0.0273 -0.0166 240 GLY A N   
1764 C  CA  . GLY A 240 ? 0.2325 0.2272 0.2148 -0.0516 -0.0288 -0.0159 240 GLY A CA  
1765 C  C   . GLY A 240 ? 0.2623 0.2610 0.2426 -0.0554 -0.0330 -0.0148 240 GLY A C   
1766 O  O   . GLY A 240 ? 0.2911 0.2971 0.2705 -0.0635 -0.0348 -0.0150 240 GLY A O   
1767 N  N   . HIS A 241 ? 0.2550 0.2501 0.2344 -0.0502 -0.0346 -0.0132 241 HIS A N   
1768 C  CA  . HIS A 241 ? 0.2672 0.2682 0.2447 -0.0527 -0.0392 -0.0113 241 HIS A CA  
1769 C  C   . HIS A 241 ? 0.2799 0.2794 0.2471 -0.0632 -0.0417 -0.0132 241 HIS A C   
1770 O  O   . HIS A 241 ? 0.2643 0.2790 0.2377 -0.0683 -0.0451 -0.0126 241 HIS A O   
1771 C  CB  . HIS A 241 ? 0.2684 0.2593 0.2383 -0.0479 -0.0392 -0.0097 241 HIS A CB  
1772 C  CG  . HIS A 241 ? 0.2746 0.2741 0.2435 -0.0490 -0.0441 -0.0065 241 HIS A CG  
1773 N  ND1 . HIS A 241 ? 0.3164 0.3188 0.2762 -0.0573 -0.0480 -0.0078 241 HIS A ND1 
1774 C  CD2 . HIS A 241 ? 0.2268 0.2323 0.2016 -0.0434 -0.0462 -0.0014 241 HIS A CD2 
1775 C  CE1 . HIS A 241 ? 0.3353 0.3469 0.2951 -0.0566 -0.0525 -0.0038 241 HIS A CE1 
1776 N  NE2 . HIS A 241 ? 0.2895 0.3025 0.2582 -0.0481 -0.0515 0.0009  241 HIS A NE2 
1777 N  N   . GLY A 242 ? 0.2878 0.2690 0.2402 -0.0664 -0.0404 -0.0158 242 GLY A N   
1778 C  CA  . GLY A 242 ? 0.2792 0.2548 0.2213 -0.0769 -0.0425 -0.0184 242 GLY A CA  
1779 C  C   . GLY A 242 ? 0.3288 0.3118 0.2663 -0.0820 -0.0476 -0.0190 242 GLY A C   
1780 O  O   . GLY A 242 ? 0.2971 0.2884 0.2374 -0.0770 -0.0497 -0.0165 242 GLY A O   
1781 N  N   . THR A 243 ? 0.2948 0.2747 0.2249 -0.0929 -0.0500 -0.0220 243 THR A N   
1782 C  CA  . THR A 243 ? 0.3368 0.3243 0.2612 -0.0998 -0.0555 -0.0236 243 THR A CA  
1783 C  C   . THR A 243 ? 0.3770 0.3911 0.3160 -0.1023 -0.0601 -0.0199 243 THR A C   
1784 O  O   . THR A 243 ? 0.3853 0.4116 0.3244 -0.1026 -0.0653 -0.0183 243 THR A O   
1785 C  CB  . THR A 243 ? 0.3696 0.3418 0.2803 -0.1112 -0.0566 -0.0293 243 THR A CB  
1786 O  OG1 . THR A 243 ? 0.3744 0.3222 0.2721 -0.1072 -0.0529 -0.0334 243 THR A OG1 
1787 C  CG2 . THR A 243 ? 0.3361 0.3185 0.2409 -0.1200 -0.0630 -0.0319 243 THR A CG2 
1788 N  N   . ALA A 244 ? 0.3603 0.3850 0.3122 -0.1036 -0.0582 -0.0183 244 ALA A N   
1789 C  CA  . ALA A 244 ? 0.3842 0.4359 0.3520 -0.1060 -0.0620 -0.0158 244 ALA A CA  
1790 C  C   . ALA A 244 ? 0.3655 0.4303 0.3514 -0.0975 -0.0583 -0.0133 244 ALA A C   
1791 O  O   . ALA A 244 ? 0.3618 0.4491 0.3626 -0.0999 -0.0596 -0.0125 244 ALA A O   
1792 C  CB  . ALA A 244 ? 0.3786 0.4362 0.3445 -0.1207 -0.0643 -0.0182 244 ALA A CB  
1793 N  N   . SER A 245 ? 0.3155 0.3686 0.3015 -0.0875 -0.0536 -0.0128 245 SER A N   
1794 C  CA  . SER A 245 ? 0.2867 0.3494 0.2877 -0.0805 -0.0493 -0.0125 245 SER A CA  
1795 C  C   . SER A 245 ? 0.2773 0.3440 0.2895 -0.0678 -0.0495 -0.0100 245 SER A C   
1796 O  O   . SER A 245 ? 0.2903 0.3606 0.3132 -0.0613 -0.0455 -0.0111 245 SER A O   
1797 C  CB  . SER A 245 ? 0.2991 0.3458 0.2920 -0.0813 -0.0434 -0.0144 245 SER A CB  
1798 O  OG  . SER A 245 ? 0.3347 0.3794 0.3207 -0.0932 -0.0429 -0.0155 245 SER A OG  
1799 N  N   . PHE A 246 ? 0.2605 0.3263 0.2701 -0.0645 -0.0542 -0.0066 246 PHE A N   
1800 C  CA  . PHE A 246 ? 0.2893 0.3578 0.3100 -0.0533 -0.0549 -0.0028 246 PHE A CA  
1801 C  C   . PHE A 246 ? 0.3090 0.3933 0.3376 -0.0521 -0.0623 0.0024  246 PHE A C   
1802 O  O   . PHE A 246 ? 0.3061 0.3886 0.3220 -0.0575 -0.0668 0.0043  246 PHE A O   
1803 C  CB  . PHE A 246 ? 0.3259 0.3741 0.3346 -0.0488 -0.0523 -0.0019 246 PHE A CB  
1804 C  CG  . PHE A 246 ? 0.2665 0.3159 0.2856 -0.0389 -0.0534 0.0030  246 PHE A CG  
1805 C  CD1 . PHE A 246 ? 0.2775 0.3282 0.3113 -0.0313 -0.0500 0.0018  246 PHE A CD1 
1806 C  CD2 . PHE A 246 ? 0.3168 0.3660 0.3305 -0.0379 -0.0581 0.0088  246 PHE A CD2 
1807 C  CE1 . PHE A 246 ? 0.2981 0.3477 0.3422 -0.0228 -0.0513 0.0065  246 PHE A CE1 
1808 C  CE2 . PHE A 246 ? 0.3452 0.3945 0.3686 -0.0295 -0.0594 0.0149  246 PHE A CE2 
1809 C  CZ  . PHE A 246 ? 0.2948 0.3432 0.3340 -0.0220 -0.0561 0.0137  246 PHE A CZ  
1810 N  N   . SER A 247 ? 0.2882 0.3876 0.3376 -0.0444 -0.0637 0.0047  247 SER A N   
1811 C  CA  . SER A 247 ? 0.2997 0.4144 0.3600 -0.0408 -0.0714 0.0112  247 SER A CA  
1812 C  C   . SER A 247 ? 0.2803 0.3882 0.3496 -0.0292 -0.0717 0.0165  247 SER A C   
1813 O  O   . SER A 247 ? 0.2478 0.3540 0.3305 -0.0218 -0.0671 0.0137  247 SER A O   
1814 C  CB  . SER A 247 ? 0.2670 0.4068 0.3474 -0.0410 -0.0735 0.0099  247 SER A CB  
1815 O  OG  . SER A 247 ? 0.2558 0.4101 0.3526 -0.0334 -0.0805 0.0167  247 SER A OG  
1816 N  N   . PHE A 248 ? 0.2940 0.3980 0.3552 -0.0284 -0.0770 0.0241  248 PHE A N   
1817 C  CA  . PHE A 248 ? 0.3030 0.4015 0.3735 -0.0185 -0.0786 0.0314  248 PHE A CA  
1818 C  C   . PHE A 248 ? 0.2901 0.4035 0.3879 -0.0094 -0.0815 0.0334  248 PHE A C   
1819 O  O   . PHE A 248 ? 0.2697 0.3755 0.3803 -0.0005 -0.0789 0.0338  248 PHE A O   
1820 C  CB  . PHE A 248 ? 0.3309 0.4283 0.3887 -0.0206 -0.0852 0.0408  248 PHE A CB  
1821 C  CG  . PHE A 248 ? 0.3940 0.4724 0.4307 -0.0235 -0.0808 0.0407  248 PHE A CG  
1822 C  CD1 . PHE A 248 ? 0.3848 0.4479 0.4241 -0.0179 -0.0746 0.0399  248 PHE A CD1 
1823 C  CD2 . PHE A 248 ? 0.3973 0.4746 0.4123 -0.0320 -0.0829 0.0409  248 PHE A CD2 
1824 C  CE1 . PHE A 248 ? 0.3964 0.4447 0.4181 -0.0204 -0.0704 0.0398  248 PHE A CE1 
1825 C  CE2 . PHE A 248 ? 0.3673 0.4290 0.3640 -0.0340 -0.0782 0.0399  248 PHE A CE2 
1826 C  CZ  . PHE A 248 ? 0.3819 0.4299 0.3826 -0.0281 -0.0718 0.0397  248 PHE A CZ  
1827 N  N   . GLU A 249 ? 0.2611 0.3959 0.3688 -0.0115 -0.0870 0.0341  249 GLU A N   
1828 C  CA  . GLU A 249 ? 0.2543 0.4052 0.3899 -0.0016 -0.0904 0.0364  249 GLU A CA  
1829 C  C   . GLU A 249 ? 0.2533 0.4063 0.4036 0.0027  -0.0822 0.0260  249 GLU A C   
1830 O  O   . GLU A 249 ? 0.2521 0.4049 0.4224 0.0138  -0.0812 0.0256  249 GLU A O   
1831 C  CB  . GLU A 249 ? 0.2426 0.4188 0.3857 -0.0053 -0.0988 0.0399  249 GLU A CB  
1832 N  N   . VAL A 250 ? 0.2197 0.3739 0.3598 -0.0061 -0.0761 0.0174  250 VAL A N   
1833 C  CA  . VAL A 250 ? 0.2086 0.3646 0.3585 -0.0034 -0.0677 0.0077  250 VAL A CA  
1834 C  C   . VAL A 250 ? 0.2431 0.3774 0.3907 0.0032  -0.0627 0.0059  250 VAL A C   
1835 O  O   . VAL A 250 ? 0.2114 0.3475 0.3759 0.0114  -0.0588 0.0006  250 VAL A O   
1836 C  CB  . VAL A 250 ? 0.2150 0.3736 0.3508 -0.0155 -0.0627 0.0010  250 VAL A CB  
1837 C  CG1 . VAL A 250 ? 0.2103 0.3688 0.3522 -0.0133 -0.0537 -0.0082 250 VAL A CG1 
1838 C  CG2 . VAL A 250 ? 0.1746 0.3571 0.3161 -0.0227 -0.0673 0.0017  250 VAL A CG2 
1839 N  N   . ALA A 251 ? 0.2079 0.3223 0.3351 -0.0006 -0.0624 0.0094  251 ALA A N   
1840 C  CA  . ALA A 251 ? 0.2522 0.3472 0.3763 0.0039  -0.0575 0.0076  251 ALA A CA  
1841 C  C   . ALA A 251 ? 0.2385 0.3295 0.3796 0.0147  -0.0608 0.0130  251 ALA A C   
1842 O  O   . ALA A 251 ? 0.2712 0.3548 0.4228 0.0210  -0.0566 0.0081  251 ALA A O   
1843 C  CB  . ALA A 251 ? 0.2362 0.3135 0.3359 -0.0026 -0.0565 0.0102  251 ALA A CB  
1844 N  N   . ARG A 252 ? 0.2798 0.3749 0.4234 0.0164  -0.0688 0.0234  252 ARG A N   
1845 C  CA  . ARG A 252 ? 0.2639 0.3555 0.4252 0.0266  -0.0732 0.0305  252 ARG A CA  
1846 C  C   . ARG A 252 ? 0.2629 0.3659 0.4512 0.0359  -0.0718 0.0238  252 ARG A C   
1847 O  O   . ARG A 252 ? 0.2978 0.3903 0.5001 0.0443  -0.0699 0.0221  252 ARG A O   
1848 C  CB  . ARG A 252 ? 0.2987 0.3978 0.4583 0.0262  -0.0830 0.0435  252 ARG A CB  
1849 C  CG  . ARG A 252 ? 0.3438 0.4279 0.4828 0.0215  -0.0850 0.0527  252 ARG A CG  
1850 C  CD  . ARG A 252 ? 0.3750 0.4650 0.5192 0.0249  -0.0951 0.0672  252 ARG A CD  
1851 N  NE  . ARG A 252 ? 0.4789 0.5740 0.6004 0.0153  -0.0993 0.0729  252 ARG A NE  
1852 C  CZ  . ARG A 252 ? 0.4957 0.5778 0.5954 0.0096  -0.0976 0.0769  252 ARG A CZ  
1853 N  NH1 . ARG A 252 ? 0.4851 0.5490 0.5831 0.0120  -0.0920 0.0772  252 ARG A NH1 
1854 N  NH2 . ARG A 252 ? 0.4577 0.5465 0.5372 0.0010  -0.1013 0.0801  252 ARG A NH2 
1855 N  N   . ARG A 253 ? 0.2794 0.4046 0.4761 0.0344  -0.0725 0.0195  253 ARG A N   
1856 C  CA  . ARG A 253 ? 0.2370 0.3762 0.4608 0.0439  -0.0707 0.0124  253 ARG A CA  
1857 C  C   . ARG A 253 ? 0.2809 0.4130 0.5060 0.0450  -0.0606 -0.0008 253 ARG A C   
1858 O  O   . ARG A 253 ? 0.2860 0.4146 0.5301 0.0550  -0.0585 -0.0060 253 ARG A O   
1859 C  CB  . ARG A 253 ? 0.2564 0.4239 0.4888 0.0408  -0.0732 0.0108  253 ARG A CB  
1860 C  CG  . ARG A 253 ? 0.2770 0.4632 0.5377 0.0501  -0.0701 0.0020  253 ARG A CG  
1861 C  CD  . ARG A 253 ? 0.3106 0.4917 0.5953 0.0649  -0.0752 0.0070  253 ARG A CD  
1862 N  NE  . ARG A 253 ? 0.3003 0.5002 0.6142 0.0752  -0.0722 -0.0024 253 ARG A NE  
1863 C  CZ  . ARG A 253 ? 0.3450 0.5407 0.6840 0.0896  -0.0746 -0.0022 253 ARG A CZ  
1864 N  NH1 . ARG A 253 ? 0.4119 0.5837 0.7501 0.0948  -0.0798 0.0076  253 ARG A NH1 
1865 N  NH2 . ARG A 253 ? 0.3077 0.5236 0.6739 0.0990  -0.0715 -0.0120 253 ARG A NH2 
1866 N  N   . ALA A 254 ? 0.2983 0.4274 0.5032 0.0348  -0.0547 -0.0066 254 ALA A N   
1867 C  CA  . ALA A 254 ? 0.3002 0.4236 0.5041 0.0350  -0.0459 -0.0183 254 ALA A CA  
1868 C  C   . ALA A 254 ? 0.3037 0.4041 0.5077 0.0404  -0.0448 -0.0180 254 ALA A C   
1869 O  O   . ALA A 254 ? 0.2954 0.3933 0.5116 0.0464  -0.0400 -0.0273 254 ALA A O   
1870 C  CB  . ALA A 254 ? 0.2747 0.3976 0.4558 0.0229  -0.0411 -0.0219 254 ALA A CB  
1871 N  N   . ILE A 255 ? 0.3117 0.3959 0.5023 0.0378  -0.0489 -0.0078 255 ILE A N   
1872 C  CA  . ILE A 255 ? 0.3129 0.3760 0.5037 0.0416  -0.0481 -0.0061 255 ILE A CA  
1873 C  C   . ILE A 255 ? 0.3283 0.3890 0.5443 0.0531  -0.0517 -0.0041 255 ILE A C   
1874 O  O   . ILE A 255 ? 0.3342 0.3812 0.5584 0.0578  -0.0489 -0.0089 255 ILE A O   
1875 C  CB  . ILE A 255 ? 0.3562 0.4060 0.5265 0.0353  -0.0512 0.0047  255 ILE A CB  
1876 C  CG1 . ILE A 255 ? 0.3308 0.3769 0.4785 0.0259  -0.0460 -0.0001 255 ILE A CG1 
1877 C  CG2 . ILE A 255 ? 0.3953 0.4263 0.5697 0.0395  -0.0525 0.0104  255 ILE A CG2 
1878 C  CD1 . ILE A 255 ? 0.3380 0.3768 0.4648 0.0191  -0.0486 0.0085  255 ILE A CD1 
1879 N  N   . ALA A 256 ? 0.3540 0.4278 0.5836 0.0580  -0.0582 0.0026  256 ALA A N   
1880 C  CA  . ALA A 256 ? 0.2910 0.3629 0.5472 0.0704  -0.0618 0.0041  256 ALA A CA  
1881 C  C   . ALA A 256 ? 0.3236 0.4051 0.5990 0.0771  -0.0553 -0.0118 256 ALA A C   
1882 O  O   . ALA A 256 ? 0.3188 0.3918 0.6147 0.0872  -0.0554 -0.0154 256 ALA A O   
1883 C  CB  . ALA A 256 ? 0.3393 0.4248 0.6059 0.0744  -0.0712 0.0162  256 ALA A CB  
1884 N  N   . LEU A 257 ? 0.2751 0.3739 0.5441 0.0715  -0.0496 -0.0217 257 LEU A N   
1885 C  CA  . LEU A 257 ? 0.3103 0.4202 0.5942 0.0764  -0.0422 -0.0377 257 LEU A CA  
1886 C  C   . LEU A 257 ? 0.3005 0.3950 0.5742 0.0733  -0.0348 -0.0481 257 LEU A C   
1887 O  O   . LEU A 257 ? 0.3205 0.4244 0.6018 0.0754  -0.0278 -0.0626 257 LEU A O   
1888 C  CB  . LEU A 257 ? 0.2860 0.4233 0.5679 0.0707  -0.0389 -0.0431 257 LEU A CB  
1889 C  CG  . LEU A 257 ? 0.2439 0.4033 0.5427 0.0750  -0.0452 -0.0368 257 LEU A CG  
1890 C  CD1 . LEU A 257 ? 0.2795 0.4646 0.5723 0.0659  -0.0415 -0.0414 257 LEU A CD1 
1891 C  CD2 . LEU A 257 ? 0.2632 0.4291 0.5949 0.0905  -0.0463 -0.0416 257 LEU A CD2 
1892 N  N   . GLY A 258 ? 0.3098 0.3829 0.5667 0.0682  -0.0362 -0.0414 258 GLY A N   
1893 C  CA  . GLY A 258 ? 0.2943 0.3545 0.5408 0.0644  -0.0302 -0.0504 258 GLY A CA  
1894 C  C   . GLY A 258 ? 0.3445 0.4133 0.5698 0.0540  -0.0248 -0.0557 258 GLY A C   
1895 O  O   . GLY A 258 ? 0.3293 0.3942 0.5486 0.0515  -0.0192 -0.0658 258 GLY A O   
1896 N  N   . ILE A 259 ? 0.2766 0.3565 0.4899 0.0474  -0.0268 -0.0489 259 ILE A N   
1897 C  CA  . ILE A 259 ? 0.2931 0.3802 0.4869 0.0373  -0.0222 -0.0526 259 ILE A CA  
1898 C  C   . ILE A 259 ? 0.3172 0.3893 0.4886 0.0297  -0.0249 -0.0429 259 ILE A C   
1899 O  O   . ILE A 259 ? 0.3184 0.3949 0.4804 0.0246  -0.0284 -0.0352 259 ILE A O   
1900 C  CB  . ILE A 259 ? 0.2913 0.4024 0.4888 0.0343  -0.0216 -0.0538 259 ILE A CB  
1901 C  CG1 . ILE A 259 ? 0.2692 0.3972 0.4923 0.0434  -0.0190 -0.0633 259 ILE A CG1 
1902 C  CG2 . ILE A 259 ? 0.2951 0.4125 0.4738 0.0236  -0.0164 -0.0580 259 ILE A CG2 
1903 C  CD1 . ILE A 259 ? 0.2786 0.4049 0.5056 0.0462  -0.0117 -0.0774 259 ILE A CD1 
1904 N  N   . LEU A 260 ? 0.2753 0.3303 0.4388 0.0290  -0.0233 -0.0439 260 LEU A N   
1905 C  CA  . LEU A 260 ? 0.2970 0.3383 0.4413 0.0231  -0.0250 -0.0359 260 LEU A CA  
1906 C  C   . LEU A 260 ? 0.2772 0.3212 0.4029 0.0147  -0.0213 -0.0393 260 LEU A C   
1907 O  O   . LEU A 260 ? 0.2794 0.3320 0.4060 0.0135  -0.0168 -0.0482 260 LEU A O   
1908 C  CB  . LEU A 260 ? 0.2715 0.2953 0.4173 0.0257  -0.0249 -0.0353 260 LEU A CB  
1909 C  CG  . LEU A 260 ? 0.3567 0.3725 0.5189 0.0330  -0.0291 -0.0295 260 LEU A CG  
1910 C  CD1 . LEU A 260 ? 0.3070 0.3052 0.4673 0.0326  -0.0287 -0.0278 260 LEU A CD1 
1911 C  CD2 . LEU A 260 ? 0.3745 0.3934 0.5343 0.0327  -0.0350 -0.0173 260 LEU A CD2 
1912 N  N   . PRO A 261 ? 0.2601 0.2966 0.3685 0.0090  -0.0231 -0.0322 261 PRO A N   
1913 C  CA  . PRO A 261 ? 0.2635 0.2997 0.3550 0.0017  -0.0202 -0.0344 261 PRO A CA  
1914 C  C   . PRO A 261 ? 0.2939 0.3217 0.3815 0.0020  -0.0169 -0.0395 261 PRO A C   
1915 O  O   . PRO A 261 ? 0.2685 0.2859 0.3605 0.0058  -0.0176 -0.0385 261 PRO A O   
1916 C  CB  . PRO A 261 ? 0.2692 0.2969 0.3458 -0.0028 -0.0233 -0.0261 261 PRO A CB  
1917 C  CG  . PRO A 261 ? 0.3018 0.3211 0.3842 0.0022  -0.0264 -0.0201 261 PRO A CG  
1918 C  CD  . PRO A 261 ? 0.2899 0.3171 0.3930 0.0090  -0.0276 -0.0221 261 PRO A CD  
1919 N  N   . HIS A 262 ? 0.2354 0.2691 0.3153 -0.0024 -0.0136 -0.0447 262 HIS A N   
1920 C  CA  . HIS A 262 ? 0.2507 0.2773 0.3236 -0.0034 -0.0116 -0.0481 262 HIS A CA  
1921 C  C   . HIS A 262 ? 0.2715 0.2848 0.3304 -0.0059 -0.0135 -0.0410 262 HIS A C   
1922 O  O   . HIS A 262 ? 0.2309 0.2348 0.2903 -0.0036 -0.0139 -0.0402 262 HIS A O   
1923 C  CB  . HIS A 262 ? 0.2727 0.3104 0.3397 -0.0079 -0.0080 -0.0543 262 HIS A CB  
1924 C  CG  . HIS A 262 ? 0.3285 0.3621 0.3898 -0.0086 -0.0066 -0.0585 262 HIS A CG  
1925 N  ND1 . HIS A 262 ? 0.3180 0.3486 0.3633 -0.0139 -0.0067 -0.0556 262 HIS A ND1 
1926 C  CD2 . HIS A 262 ? 0.3252 0.3571 0.3950 -0.0048 -0.0056 -0.0653 262 HIS A CD2 
1927 C  CE1 . HIS A 262 ? 0.3314 0.3607 0.3757 -0.0132 -0.0062 -0.0600 262 HIS A CE1 
1928 N  NE2 . HIS A 262 ? 0.3174 0.3474 0.3760 -0.0083 -0.0054 -0.0666 262 HIS A NE2 
1929 N  N   . THR A 263 ? 0.2017 0.2141 0.2490 -0.0107 -0.0146 -0.0361 263 THR A N   
1930 C  CA  . THR A 263 ? 0.2522 0.2519 0.2867 -0.0124 -0.0161 -0.0305 263 THR A CA  
1931 C  C   . THR A 263 ? 0.2381 0.2361 0.2693 -0.0140 -0.0187 -0.0251 263 THR A C   
1932 O  O   . THR A 263 ? 0.2503 0.2577 0.2845 -0.0164 -0.0197 -0.0251 263 THR A O   
1933 C  CB  . THR A 263 ? 0.2880 0.2846 0.3088 -0.0173 -0.0151 -0.0304 263 THR A CB  
1934 O  OG1 . THR A 263 ? 0.2758 0.2794 0.2919 -0.0231 -0.0149 -0.0300 263 THR A OG1 
1935 C  CG2 . THR A 263 ? 0.2916 0.2913 0.3140 -0.0163 -0.0132 -0.0353 263 THR A CG2 
1936 N  N   . ILE A 264 ? 0.2164 0.2038 0.2416 -0.0128 -0.0198 -0.0208 264 ILE A N   
1937 C  CA  . ILE A 264 ? 0.2588 0.2434 0.2766 -0.0152 -0.0222 -0.0163 264 ILE A CA  
1938 C  C   . ILE A 264 ? 0.2611 0.2362 0.2635 -0.0192 -0.0216 -0.0161 264 ILE A C   
1939 O  O   . ILE A 264 ? 0.2631 0.2302 0.2613 -0.0173 -0.0199 -0.0166 264 ILE A O   
1940 C  CB  . ILE A 264 ? 0.2416 0.2222 0.2626 -0.0114 -0.0235 -0.0119 264 ILE A CB  
1941 C  CG1 . ILE A 264 ? 0.2736 0.2619 0.3107 -0.0074 -0.0252 -0.0109 264 ILE A CG1 
1942 C  CG2 . ILE A 264 ? 0.2645 0.2418 0.2739 -0.0147 -0.0255 -0.0081 264 ILE A CG2 
1943 C  CD1 . ILE A 264 ? 0.3017 0.2848 0.3429 -0.0040 -0.0265 -0.0053 264 ILE A CD1 
1944 N  N   . SER A 265 ? 0.2215 0.1972 0.2164 -0.0247 -0.0233 -0.0153 265 SER A N   
1945 C  CA  . SER A 265 ? 0.2528 0.2174 0.2336 -0.0289 -0.0230 -0.0155 265 SER A CA  
1946 C  C   . SER A 265 ? 0.2607 0.2248 0.2344 -0.0338 -0.0257 -0.0145 265 SER A C   
1947 O  O   . SER A 265 ? 0.2550 0.2304 0.2353 -0.0350 -0.0281 -0.0133 265 SER A O   
1948 C  CB  . SER A 265 ? 0.2765 0.2418 0.2546 -0.0330 -0.0220 -0.0168 265 SER A CB  
1949 O  OG  . SER A 265 ? 0.2460 0.2234 0.2281 -0.0382 -0.0229 -0.0173 265 SER A OG  
1950 N  N   . SER A 266 ? 0.2444 0.1956 0.2053 -0.0366 -0.0257 -0.0153 266 SER A N   
1951 C  CA  . SER A 266 ? 0.3011 0.2496 0.2534 -0.0406 -0.0279 -0.0156 266 SER A CA  
1952 C  C   . SER A 266 ? 0.2863 0.2338 0.2322 -0.0496 -0.0301 -0.0170 266 SER A C   
1953 O  O   . SER A 266 ? 0.3070 0.2595 0.2498 -0.0543 -0.0332 -0.0173 266 SER A O   
1954 C  CB  . SER A 266 ? 0.2945 0.2290 0.2366 -0.0377 -0.0260 -0.0174 266 SER A CB  
1955 O  OG  . SER A 266 ? 0.3226 0.2442 0.2592 -0.0381 -0.0245 -0.0191 266 SER A OG  
1956 N  N   . ASP A 267 ? 0.2677 0.2098 0.2116 -0.0530 -0.0290 -0.0173 267 ASP A N   
1957 C  CA  . ASP A 267 ? 0.2983 0.2348 0.2344 -0.0627 -0.0307 -0.0181 267 ASP A CA  
1958 C  C   . ASP A 267 ? 0.3203 0.2419 0.2438 -0.0650 -0.0320 -0.0213 267 ASP A C   
1959 O  O   . ASP A 267 ? 0.2943 0.2169 0.2127 -0.0729 -0.0348 -0.0231 267 ASP A O   
1960 C  CB  . ASP A 267 ? 0.2855 0.2403 0.2289 -0.0693 -0.0330 -0.0173 267 ASP A CB  
1961 C  CG  . ASP A 267 ? 0.3235 0.2742 0.2605 -0.0807 -0.0343 -0.0175 267 ASP A CG  
1962 O  OD1 . ASP A 267 ? 0.3129 0.2463 0.2411 -0.0830 -0.0333 -0.0172 267 ASP A OD1 
1963 O  OD2 . ASP A 267 ? 0.3421 0.3065 0.2831 -0.0877 -0.0369 -0.0177 267 ASP A OD2 
1964 N  N   . ILE A 268 ? 0.3129 0.2214 0.2317 -0.0583 -0.0297 -0.0227 268 ILE A N   
1965 C  CA  . ILE A 268 ? 0.3189 0.2149 0.2269 -0.0581 -0.0296 -0.0272 268 ILE A CA  
1966 C  C   . ILE A 268 ? 0.3662 0.2419 0.2648 -0.0626 -0.0298 -0.0299 268 ILE A C   
1967 O  O   . ILE A 268 ? 0.2986 0.1663 0.1989 -0.0616 -0.0291 -0.0272 268 ILE A O   
1968 C  CB  . ILE A 268 ? 0.3182 0.2126 0.2276 -0.0480 -0.0262 -0.0277 268 ILE A CB  
1969 C  CG1 . ILE A 268 ? 0.3561 0.2432 0.2546 -0.0478 -0.0253 -0.0330 268 ILE A CG1 
1970 C  CG2 . ILE A 268 ? 0.3084 0.1931 0.2207 -0.0420 -0.0237 -0.0266 268 ILE A CG2 
1971 C  CD1 . ILE A 268 ? 0.3292 0.2208 0.2301 -0.0392 -0.0217 -0.0326 268 ILE A CD1 
1972 N  N   . TYR A 269 ? 0.3481 0.2153 0.2367 -0.0682 -0.0313 -0.0352 269 TYR A N   
1973 C  CA  . TYR A 269 ? 0.3895 0.2333 0.2688 -0.0705 -0.0312 -0.0396 269 TYR A CA  
1974 C  C   . TYR A 269 ? 0.4342 0.2720 0.3034 -0.0703 -0.0306 -0.0478 269 TYR A C   
1975 O  O   . TYR A 269 ? 0.3690 0.2218 0.2382 -0.0685 -0.0304 -0.0483 269 TYR A O   
1976 C  CB  . TYR A 269 ? 0.3835 0.2213 0.2608 -0.0821 -0.0343 -0.0377 269 TYR A CB  
1977 C  CG  . TYR A 269 ? 0.4092 0.2540 0.2820 -0.0932 -0.0378 -0.0412 269 TYR A CG  
1978 C  CD1 . TYR A 269 ? 0.4070 0.2767 0.2871 -0.0960 -0.0398 -0.0382 269 TYR A CD1 
1979 C  CD2 . TYR A 269 ? 0.4744 0.3011 0.3366 -0.1012 -0.0397 -0.0475 269 TYR A CD2 
1980 C  CE1 . TYR A 269 ? 0.3932 0.2717 0.2703 -0.1062 -0.0438 -0.0407 269 TYR A CE1 
1981 C  CE2 . TYR A 269 ? 0.5257 0.3603 0.3838 -0.1125 -0.0436 -0.0510 269 TYR A CE2 
1982 C  CZ  . TYR A 269 ? 0.5048 0.3664 0.3705 -0.1150 -0.0458 -0.0472 269 TYR A CZ  
1983 O  OH  . TYR A 269 ? 0.5266 0.3984 0.3893 -0.1262 -0.0504 -0.0502 269 TYR A OH  
1984 N  N   . CYS A 270 ? 0.4319 0.2475 0.2923 -0.0719 -0.0302 -0.0541 270 CYS A N   
1985 C  CA  . CYS A 270 ? 0.4171 0.2261 0.2678 -0.0694 -0.0281 -0.0636 270 CYS A CA  
1986 C  C   . CYS A 270 ? 0.4548 0.2790 0.2990 -0.0773 -0.0309 -0.0666 270 CYS A C   
1987 O  O   . CYS A 270 ? 0.4761 0.3094 0.3158 -0.0735 -0.0289 -0.0697 270 CYS A O   
1988 C  CB  . CYS A 270 ? 0.4471 0.2281 0.2901 -0.0705 -0.0276 -0.0712 270 CYS A CB  
1989 S  SG  . CYS A 270 ? 0.5693 0.3372 0.4063 -0.0864 -0.0330 -0.0728 270 CYS A SG  
1990 N  N   . ARG A 271 ? 0.4442 0.2736 0.2884 -0.0887 -0.0358 -0.0646 271 ARG A N   
1991 C  CA  . ARG A 271 ? 0.4820 0.3255 0.3197 -0.0970 -0.0396 -0.0679 271 ARG A CA  
1992 C  C   . ARG A 271 ? 0.4601 0.3293 0.3049 -0.0925 -0.0403 -0.0610 271 ARG A C   
1993 O  O   . ARG A 271 ? 0.4466 0.3248 0.2842 -0.0918 -0.0405 -0.0637 271 ARG A O   
1994 C  CB  . ARG A 271 ? 0.4686 0.3128 0.3064 -0.1108 -0.0449 -0.0675 271 ARG A CB  
1995 N  N   . ASN A 272 ? 0.4227 0.3040 0.2814 -0.0895 -0.0406 -0.0520 272 ASN A N   
1996 C  CA  . ASN A 272 ? 0.4027 0.3061 0.2690 -0.0850 -0.0416 -0.0458 272 ASN A CA  
1997 C  C   . ASN A 272 ? 0.3970 0.2994 0.2646 -0.0736 -0.0367 -0.0444 272 ASN A C   
1998 O  O   . ASN A 272 ? 0.3860 0.3038 0.2576 -0.0701 -0.0374 -0.0395 272 ASN A O   
1999 C  CB  . ASN A 272 ? 0.3701 0.2889 0.2516 -0.0863 -0.0439 -0.0382 272 ASN A CB  
2000 C  CG  . ASN A 272 ? 0.3550 0.2675 0.2456 -0.0801 -0.0400 -0.0347 272 ASN A CG  
2001 O  OD1 . ASN A 272 ? 0.3217 0.2232 0.2108 -0.0721 -0.0359 -0.0355 272 ASN A OD1 
2002 N  ND2 . ASN A 272 ? 0.3301 0.2513 0.2299 -0.0842 -0.0413 -0.0310 272 ASN A ND2 
2003 N  N   . ARG A 273 ? 0.3964 0.2814 0.2609 -0.0680 -0.0320 -0.0484 273 ARG A N   
2004 C  CA  . ARG A 273 ? 0.3632 0.2481 0.2268 -0.0588 -0.0271 -0.0491 273 ARG A CA  
2005 C  C   . ARG A 273 ? 0.4571 0.3428 0.3063 -0.0612 -0.0264 -0.0558 273 ARG A C   
2006 O  O   . ARG A 273 ? 0.3790 0.2785 0.2270 -0.0590 -0.0257 -0.0525 273 ARG A O   
2007 C  CB  . ARG A 273 ? 0.4036 0.2717 0.2696 -0.0516 -0.0227 -0.0514 273 ARG A CB  
2008 C  CG  . ARG A 273 ? 0.4112 0.2791 0.2762 -0.0426 -0.0170 -0.0539 273 ARG A CG  
2009 C  CD  . ARG A 273 ? 0.4200 0.2753 0.2917 -0.0345 -0.0137 -0.0543 273 ARG A CD  
2010 N  NE  . ARG A 273 ? 0.4403 0.2746 0.3059 -0.0364 -0.0143 -0.0605 273 ARG A NE  
2011 C  CZ  . ARG A 273 ? 0.4365 0.2584 0.2928 -0.0348 -0.0114 -0.0702 273 ARG A CZ  
2012 N  NH1 . ARG A 273 ? 0.4516 0.2818 0.3028 -0.0314 -0.0072 -0.0749 273 ARG A NH1 
2013 N  NH2 . ARG A 273 ? 0.4759 0.2764 0.3281 -0.0367 -0.0126 -0.0753 273 ARG A NH2 
2014 N  N   . ILE A 274 ? 0.4361 0.3069 0.2737 -0.0665 -0.0266 -0.0653 274 ILE A N   
2015 C  CA  . ILE A 274 ? 0.4995 0.3700 0.3219 -0.0685 -0.0250 -0.0740 274 ILE A CA  
2016 C  C   . ILE A 274 ? 0.4929 0.3811 0.3088 -0.0774 -0.0308 -0.0719 274 ILE A C   
2017 O  O   . ILE A 274 ? 0.5407 0.4404 0.3480 -0.0771 -0.0299 -0.0725 274 ILE A O   
2018 C  CB  . ILE A 274 ? 0.5067 0.3536 0.3196 -0.0709 -0.0233 -0.0861 274 ILE A CB  
2019 C  CG1 . ILE A 274 ? 0.4562 0.2875 0.2766 -0.0602 -0.0178 -0.0871 274 ILE A CG1 
2020 C  CG2 . ILE A 274 ? 0.5591 0.4062 0.3551 -0.0742 -0.0216 -0.0973 274 ILE A CG2 
2021 C  CD1 . ILE A 274 ? 0.4965 0.3019 0.3149 -0.0623 -0.0185 -0.0936 274 ILE A CD1 
2022 N  N   . ASP A 275 ? 0.4726 0.3652 0.2930 -0.0856 -0.0371 -0.0686 275 ASP A N   
2023 C  CA  . ASP A 275 ? 0.5141 0.4229 0.3289 -0.0950 -0.0438 -0.0677 275 ASP A CA  
2024 C  C   . ASP A 275 ? 0.5402 0.4697 0.3698 -0.0949 -0.0487 -0.0556 275 ASP A C   
2025 O  O   . ASP A 275 ? 0.4874 0.4351 0.3148 -0.0973 -0.0533 -0.0511 275 ASP A O   
2026 C  CB  . ASP A 275 ? 0.5432 0.4415 0.3507 -0.1067 -0.0478 -0.0759 275 ASP A CB  
2027 C  CG  . ASP A 275 ? 0.5831 0.4596 0.3756 -0.1077 -0.0438 -0.0896 275 ASP A CG  
2028 O  OD1 . ASP A 275 ? 0.6007 0.4759 0.3858 -0.1008 -0.0385 -0.0938 275 ASP A OD1 
2029 O  OD2 . ASP A 275 ? 0.6466 0.5102 0.4399 -0.1132 -0.0450 -0.0946 275 ASP A OD2 
2030 N  N   . GLY A 276 ? 0.5662 0.4936 0.4106 -0.0922 -0.0481 -0.0505 276 GLY A N   
2031 C  CA  . GLY A 276 ? 0.4193 0.3650 0.2784 -0.0933 -0.0526 -0.0417 276 GLY A CA  
2032 C  C   . GLY A 276 ? 0.4678 0.4269 0.3372 -0.0841 -0.0519 -0.0327 276 GLY A C   
2033 O  O   . GLY A 276 ? 0.5258 0.4823 0.3896 -0.0781 -0.0483 -0.0323 276 GLY A O   
2034 N  N   . PRO A 277 ? 0.3970 0.3709 0.2824 -0.0829 -0.0551 -0.0255 277 PRO A N   
2035 C  CA  . PRO A 277 ? 0.4390 0.4249 0.3357 -0.0745 -0.0554 -0.0168 277 PRO A CA  
2036 C  C   . PRO A 277 ? 0.3605 0.3374 0.2657 -0.0652 -0.0491 -0.0151 277 PRO A C   
2037 O  O   . PRO A 277 ? 0.3967 0.3813 0.3120 -0.0585 -0.0490 -0.0084 277 PRO A O   
2038 C  CB  . PRO A 277 ? 0.3804 0.3849 0.2923 -0.0769 -0.0611 -0.0117 277 PRO A CB  
2039 C  CG  . PRO A 277 ? 0.3548 0.3538 0.2676 -0.0837 -0.0604 -0.0171 277 PRO A CG  
2040 C  CD  . PRO A 277 ? 0.3915 0.3719 0.2858 -0.0895 -0.0583 -0.0254 277 PRO A CD  
2041 N  N   . VAL A 278 ? 0.3337 0.2946 0.2357 -0.0647 -0.0444 -0.0205 278 VAL A N   
2042 C  CA  . VAL A 278 ? 0.3716 0.3263 0.2826 -0.0565 -0.0394 -0.0188 278 VAL A CA  
2043 C  C   . VAL A 278 ? 0.3497 0.2970 0.2541 -0.0507 -0.0349 -0.0196 278 VAL A C   
2044 O  O   . VAL A 278 ? 0.3281 0.2806 0.2407 -0.0445 -0.0333 -0.0145 278 VAL A O   
2045 C  CB  . VAL A 278 ? 0.3334 0.2763 0.2451 -0.0584 -0.0372 -0.0225 278 VAL A CB  
2046 C  CG1 . VAL A 278 ? 0.3517 0.2889 0.2709 -0.0503 -0.0326 -0.0210 278 VAL A CG1 
2047 C  CG2 . VAL A 278 ? 0.3422 0.2961 0.2626 -0.0642 -0.0406 -0.0207 278 VAL A CG2 
2048 N  N   . ARG A 279 ? 0.3597 0.2947 0.2500 -0.0528 -0.0325 -0.0266 279 ARG A N   
2049 C  CA  . ARG A 279 ? 0.3782 0.3073 0.2607 -0.0481 -0.0275 -0.0294 279 ARG A CA  
2050 C  C   . ARG A 279 ? 0.3646 0.2866 0.2556 -0.0399 -0.0224 -0.0289 279 ARG A C   
2051 O  O   . ARG A 279 ? 0.3654 0.2751 0.2506 -0.0372 -0.0183 -0.0349 279 ARG A O   
2052 C  CB  . ARG A 279 ? 0.3684 0.3114 0.2483 -0.0478 -0.0287 -0.0240 279 ARG A CB  
2053 C  CG  . ARG A 279 ? 0.4054 0.3549 0.2727 -0.0560 -0.0337 -0.0261 279 ARG A CG  
2054 C  CD  . ARG A 279 ? 0.4732 0.4381 0.3379 -0.0564 -0.0364 -0.0184 279 ARG A CD  
2055 N  NE  . ARG A 279 ? 0.4440 0.4172 0.2960 -0.0648 -0.0421 -0.0202 279 ARG A NE  
2056 C  CZ  . ARG A 279 ? 0.5061 0.4728 0.3411 -0.0705 -0.0411 -0.0302 279 ARG A CZ  
2057 N  NH1 . ARG A 279 ? 0.5170 0.4682 0.3451 -0.0679 -0.0343 -0.0395 279 ARG A NH1 
2058 N  NH2 . ARG A 279 ? 0.5397 0.5159 0.3646 -0.0789 -0.0475 -0.0314 279 ARG A NH2 
2059 N  N   . SER A 280 ? 0.3392 0.2687 0.2442 -0.0358 -0.0226 -0.0223 280 SER A N   
2060 C  CA  . SER A 280 ? 0.3012 0.2261 0.2148 -0.0289 -0.0185 -0.0217 280 SER A CA  
2061 C  C   . SER A 280 ? 0.3274 0.2611 0.2560 -0.0269 -0.0203 -0.0159 280 SER A C   
2062 O  O   . SER A 280 ? 0.3196 0.2636 0.2529 -0.0289 -0.0239 -0.0116 280 SER A O   
2063 C  CB  . SER A 280 ? 0.2820 0.2078 0.1931 -0.0243 -0.0138 -0.0219 280 SER A CB  
2064 O  OG  . SER A 280 ? 0.3065 0.2443 0.2222 -0.0241 -0.0147 -0.0150 280 SER A OG  
2065 N  N   . LEU A 281 ? 0.3099 0.2398 0.2464 -0.0224 -0.0180 -0.0161 281 LEU A N   
2066 C  CA  . LEU A 281 ? 0.2622 0.2000 0.2129 -0.0200 -0.0189 -0.0123 281 LEU A CA  
2067 C  C   . LEU A 281 ? 0.3116 0.2569 0.2684 -0.0174 -0.0186 -0.0073 281 LEU A C   
2068 O  O   . LEU A 281 ? 0.2703 0.2231 0.2375 -0.0169 -0.0210 -0.0036 281 LEU A O   
2069 C  CB  . LEU A 281 ? 0.2967 0.2298 0.2529 -0.0162 -0.0166 -0.0139 281 LEU A CB  
2070 C  CG  . LEU A 281 ? 0.2861 0.2268 0.2557 -0.0144 -0.0174 -0.0121 281 LEU A CG  
2071 C  CD1 . LEU A 281 ? 0.2552 0.2014 0.2268 -0.0187 -0.0202 -0.0124 281 LEU A CD1 
2072 C  CD2 . LEU A 281 ? 0.2459 0.1832 0.2192 -0.0110 -0.0155 -0.0138 281 LEU A CD2 
2073 N  N   . ALA A 282 ? 0.2874 0.2308 0.2384 -0.0158 -0.0154 -0.0072 282 ALA A N   
2074 C  CA  . ALA A 282 ? 0.3029 0.2531 0.2582 -0.0148 -0.0150 -0.0012 282 ALA A CA  
2075 C  C   . ALA A 282 ? 0.2753 0.2327 0.2289 -0.0182 -0.0198 0.0039  282 ALA A C   
2076 O  O   . ALA A 282 ? 0.2803 0.2432 0.2440 -0.0169 -0.0220 0.0103  282 ALA A O   
2077 C  CB  . ALA A 282 ? 0.3304 0.2794 0.2772 -0.0139 -0.0101 -0.0023 282 ALA A CB  
2078 N  N   . LEU A 283 ? 0.2710 0.2284 0.2128 -0.0227 -0.0221 0.0011  283 LEU A N   
2079 C  CA  . LEU A 283 ? 0.3203 0.2867 0.2604 -0.0261 -0.0275 0.0062  283 LEU A CA  
2080 C  C   . LEU A 283 ? 0.2978 0.2701 0.2518 -0.0255 -0.0319 0.0083  283 LEU A C   
2081 O  O   . LEU A 283 ? 0.2971 0.2779 0.2588 -0.0248 -0.0362 0.0151  283 LEU A O   
2082 C  CB  . LEU A 283 ? 0.3058 0.2716 0.2291 -0.0320 -0.0290 0.0016  283 LEU A CB  
2083 C  CG  . LEU A 283 ? 0.4135 0.3819 0.3224 -0.0341 -0.0273 0.0025  283 LEU A CG  
2084 C  CD1 . LEU A 283 ? 0.3958 0.3764 0.3059 -0.0358 -0.0326 0.0126  283 LEU A CD1 
2085 C  CD2 . LEU A 283 ? 0.3979 0.3615 0.3063 -0.0299 -0.0203 0.0014  283 LEU A CD2 
2086 N  N   . VAL A 284 ? 0.2962 0.2648 0.2540 -0.0257 -0.0310 0.0028  284 VAL A N   
2087 C  CA  . VAL A 284 ? 0.2854 0.2612 0.2572 -0.0248 -0.0336 0.0036  284 VAL A CA  
2088 C  C   . VAL A 284 ? 0.2659 0.2439 0.2531 -0.0187 -0.0329 0.0075  284 VAL A C   
2089 O  O   . VAL A 284 ? 0.2716 0.2578 0.2708 -0.0167 -0.0365 0.0116  284 VAL A O   
2090 C  CB  . VAL A 284 ? 0.2645 0.2356 0.2353 -0.0268 -0.0316 -0.0027 284 VAL A CB  
2091 C  CG1 . VAL A 284 ? 0.2466 0.2270 0.2322 -0.0255 -0.0328 -0.0029 284 VAL A CG1 
2092 C  CG2 . VAL A 284 ? 0.2892 0.2570 0.2463 -0.0338 -0.0332 -0.0062 284 VAL A CG2 
2093 N  N   . MET A 285 ? 0.2539 0.2243 0.2420 -0.0157 -0.0285 0.0060  285 MET A N   
2094 C  CA  . MET A 285 ? 0.2867 0.2574 0.2885 -0.0111 -0.0278 0.0092  285 MET A CA  
2095 C  C   . MET A 285 ? 0.2595 0.2340 0.2642 -0.0105 -0.0310 0.0178  285 MET A C   
2096 O  O   . MET A 285 ? 0.2711 0.2481 0.2902 -0.0071 -0.0333 0.0216  285 MET A O   
2097 C  CB  . MET A 285 ? 0.2563 0.2198 0.2566 -0.0093 -0.0229 0.0068  285 MET A CB  
2098 C  CG  . MET A 285 ? 0.2640 0.2240 0.2638 -0.0090 -0.0207 0.0000  285 MET A CG  
2099 S  SD  . MET A 285 ? 0.3052 0.2582 0.2995 -0.0073 -0.0160 -0.0026 285 MET A SD  
2100 C  CE  . MET A 285 ? 0.2961 0.2511 0.3039 -0.0047 -0.0147 0.0013  285 MET A CE  
2101 N  N   . SER A 286 ? 0.2568 0.2314 0.2475 -0.0136 -0.0311 0.0210  286 SER A N   
2102 C  CA  . SER A 286 ? 0.2779 0.2569 0.2687 -0.0140 -0.0345 0.0307  286 SER A CA  
2103 C  C   . SER A 286 ? 0.2848 0.2724 0.2836 -0.0135 -0.0413 0.0349  286 SER A C   
2104 O  O   . SER A 286 ? 0.2711 0.2613 0.2795 -0.0110 -0.0450 0.0435  286 SER A O   
2105 C  CB  . SER A 286 ? 0.2724 0.2521 0.2443 -0.0184 -0.0330 0.0318  286 SER A CB  
2106 O  OG  . SER A 286 ? 0.2639 0.2378 0.2315 -0.0178 -0.0265 0.0288  286 SER A OG  
2107 N  N   . LYS A 287 ? 0.3095 0.3020 0.3051 -0.0161 -0.0432 0.0294  287 LYS A N   
2108 C  CA  . LYS A 287 ? 0.3135 0.3170 0.3193 -0.0153 -0.0495 0.0326  287 LYS A CA  
2109 C  C   . LYS A 287 ? 0.2950 0.2990 0.3223 -0.0087 -0.0497 0.0330  287 LYS A C   
2110 O  O   . LYS A 287 ? 0.3174 0.3280 0.3574 -0.0050 -0.0549 0.0396  287 LYS A O   
2111 C  CB  . LYS A 287 ? 0.3129 0.3217 0.3129 -0.0202 -0.0504 0.0256  287 LYS A CB  
2112 C  CG  . LYS A 287 ? 0.3318 0.3410 0.3120 -0.0271 -0.0519 0.0248  287 LYS A CG  
2113 C  CD  . LYS A 287 ? 0.3248 0.3353 0.2990 -0.0329 -0.0519 0.0169  287 LYS A CD  
2114 C  CE  . LYS A 287 ? 0.3620 0.3788 0.3223 -0.0401 -0.0567 0.0173  287 LYS A CE  
2115 N  NZ  . LYS A 287 ? 0.3871 0.3958 0.3342 -0.0467 -0.0542 0.0083  287 LYS A NZ  
2116 N  N   . PHE A 288 ? 0.2749 0.2723 0.3069 -0.0067 -0.0444 0.0259  288 PHE A N   
2117 C  CA  . PHE A 288 ? 0.2695 0.2673 0.3214 -0.0006 -0.0442 0.0246  288 PHE A CA  
2118 C  C   . PHE A 288 ? 0.2986 0.2892 0.3588 0.0032  -0.0450 0.0320  288 PHE A C   
2119 O  O   . PHE A 288 ? 0.2430 0.2346 0.3207 0.0086  -0.0476 0.0343  288 PHE A O   
2120 C  CB  . PHE A 288 ? 0.2920 0.2866 0.3454 -0.0005 -0.0388 0.0146  288 PHE A CB  
2121 C  CG  . PHE A 288 ? 0.2995 0.3028 0.3505 -0.0037 -0.0389 0.0088  288 PHE A CG  
2122 C  CD1 . PHE A 288 ? 0.2945 0.3094 0.3603 -0.0010 -0.0409 0.0070  288 PHE A CD1 
2123 C  CD2 . PHE A 288 ? 0.2979 0.2982 0.3323 -0.0096 -0.0371 0.0058  288 PHE A CD2 
2124 C  CE1 . PHE A 288 ? 0.2926 0.3176 0.3564 -0.0052 -0.0407 0.0023  288 PHE A CE1 
2125 C  CE2 . PHE A 288 ? 0.2949 0.3026 0.3270 -0.0139 -0.0375 0.0016  288 PHE A CE2 
2126 C  CZ  . PHE A 288 ? 0.2910 0.3118 0.3376 -0.0122 -0.0392 0.0001  288 PHE A CZ  
2127 N  N   . LEU A 289 ? 0.2794 0.2629 0.3280 0.0004  -0.0426 0.0358  289 LEU A N   
2128 C  CA  . LEU A 289 ? 0.2848 0.2626 0.3396 0.0021  -0.0439 0.0452  289 LEU A CA  
2129 C  C   . LEU A 289 ? 0.3113 0.2951 0.3694 0.0032  -0.0511 0.0562  289 LEU A C   
2130 O  O   . LEU A 289 ? 0.3146 0.2945 0.3868 0.0072  -0.0543 0.0636  289 LEU A O   
2131 C  CB  . LEU A 289 ? 0.2889 0.2615 0.3294 -0.0022 -0.0395 0.0475  289 LEU A CB  
2132 C  CG  . LEU A 289 ? 0.3010 0.2670 0.3417 -0.0023 -0.0331 0.0397  289 LEU A CG  
2133 C  CD1 . LEU A 289 ? 0.2820 0.2468 0.3085 -0.0063 -0.0292 0.0424  289 LEU A CD1 
2134 C  CD2 . LEU A 289 ? 0.2943 0.2539 0.3533 0.0012  -0.0328 0.0398  289 LEU A CD2 
2135 N  N   . ALA A 290 ? 0.2771 0.2701 0.3224 -0.0006 -0.0543 0.0576  290 ALA A N   
2136 C  CA  . ALA A 290 ? 0.3195 0.3208 0.3664 -0.0002 -0.0621 0.0685  290 ALA A CA  
2137 C  C   . ALA A 290 ? 0.3270 0.3349 0.3954 0.0064  -0.0671 0.0684  290 ALA A C   
2138 O  O   . ALA A 290 ? 0.3194 0.3301 0.3978 0.0101  -0.0737 0.0791  290 ALA A O   
2139 C  CB  . ALA A 290 ? 0.2934 0.3040 0.3206 -0.0068 -0.0643 0.0682  290 ALA A CB  
2140 N  N   . ILE A 291 ? 0.3049 0.3162 0.3803 0.0079  -0.0640 0.0568  291 ILE A N   
2141 C  CA  . ILE A 291 ? 0.3280 0.3470 0.4253 0.0147  -0.0672 0.0549  291 ILE A CA  
2142 C  C   . ILE A 291 ? 0.3799 0.3882 0.4962 0.0220  -0.0661 0.0557  291 ILE A C   
2143 O  O   . ILE A 291 ? 0.4062 0.4189 0.5427 0.0293  -0.0702 0.0574  291 ILE A O   
2144 C  CB  . ILE A 291 ? 0.3527 0.3801 0.4513 0.0132  -0.0634 0.0421  291 ILE A CB  
2145 C  CG1 . ILE A 291 ? 0.3961 0.4311 0.4758 0.0049  -0.0643 0.0407  291 ILE A CG1 
2146 C  CG2 . ILE A 291 ? 0.3945 0.4343 0.5154 0.0198  -0.0664 0.0398  291 ILE A CG2 
2147 C  CD1 . ILE A 291 ? 0.3544 0.3955 0.4335 0.0017  -0.0601 0.0294  291 ILE A CD1 
2148 N  N   . GLY A 292 ? 0.2838 0.2781 0.3952 0.0204  -0.0609 0.0543  292 GLY A N   
2149 C  CA  . GLY A 292 ? 0.3572 0.3397 0.4856 0.0259  -0.0608 0.0564  292 GLY A CA  
2150 C  C   . GLY A 292 ? 0.3673 0.3408 0.4994 0.0261  -0.0538 0.0449  292 GLY A C   
2151 O  O   . GLY A 292 ? 0.3642 0.3266 0.5099 0.0296  -0.0534 0.0453  292 GLY A O   
2152 N  N   . MET A 293 ? 0.3164 0.2942 0.4368 0.0221  -0.0487 0.0348  293 MET A N   
2153 C  CA  . MET A 293 ? 0.3062 0.2767 0.4279 0.0214  -0.0427 0.0250  293 MET A CA  
2154 C  C   . MET A 293 ? 0.2994 0.2586 0.4141 0.0177  -0.0407 0.0305  293 MET A C   
2155 O  O   . MET A 293 ? 0.2956 0.2548 0.3974 0.0138  -0.0418 0.0393  293 MET A O   
2156 C  CB  . MET A 293 ? 0.2806 0.2584 0.3902 0.0176  -0.0386 0.0153  293 MET A CB  
2157 C  CG  . MET A 293 ? 0.2725 0.2628 0.3902 0.0201  -0.0393 0.0086  293 MET A CG  
2158 S  SD  . MET A 293 ? 0.3197 0.3170 0.4216 0.0141  -0.0348 -0.0005 293 MET A SD  
2159 C  CE  . MET A 293 ? 0.2702 0.2589 0.3724 0.0139  -0.0293 -0.0092 293 MET A CE  
2160 N  N   . THR A 294 ? 0.2778 0.2285 0.4016 0.0186  -0.0376 0.0248  294 THR A N   
2161 C  CA  . THR A 294 ? 0.2716 0.2133 0.3909 0.0145  -0.0353 0.0291  294 THR A CA  
2162 C  C   . THR A 294 ? 0.3072 0.2528 0.4095 0.0096  -0.0307 0.0245  294 THR A C   
2163 O  O   . THR A 294 ? 0.2460 0.1980 0.3418 0.0095  -0.0290 0.0165  294 THR A O   
2164 C  CB  . THR A 294 ? 0.2828 0.2145 0.4181 0.0162  -0.0339 0.0238  294 THR A CB  
2165 O  OG1 . THR A 294 ? 0.3009 0.2365 0.4359 0.0161  -0.0301 0.0099  294 THR A OG1 
2166 C  CG2 . THR A 294 ? 0.2576 0.1840 0.4122 0.0225  -0.0383 0.0260  294 THR A CG2 
2167 N  N   . LEU A 295 ? 0.3009 0.2425 0.3966 0.0055  -0.0286 0.0301  295 LEU A N   
2168 C  CA  . LEU A 295 ? 0.3047 0.2496 0.3868 0.0021  -0.0241 0.0255  295 LEU A CA  
2169 C  C   . LEU A 295 ? 0.2732 0.2182 0.3600 0.0029  -0.0214 0.0139  295 LEU A C   
2170 O  O   . LEU A 295 ? 0.2684 0.2180 0.3451 0.0024  -0.0197 0.0081  295 LEU A O   
2171 C  CB  . LEU A 295 ? 0.3345 0.2775 0.4113 -0.0020 -0.0217 0.0332  295 LEU A CB  
2172 C  CG  . LEU A 295 ? 0.3072 0.2547 0.3708 -0.0045 -0.0170 0.0291  295 LEU A CG  
2173 C  CD1 . LEU A 295 ? 0.2769 0.2293 0.3254 -0.0043 -0.0175 0.0276  295 LEU A CD1 
2174 C  CD2 . LEU A 295 ? 0.3085 0.2565 0.3694 -0.0084 -0.0138 0.0360  295 LEU A CD2 
2175 N  N   . PRO A 296 ? 0.2834 0.2231 0.3844 0.0037  -0.0213 0.0101  296 PRO A N   
2176 C  CA  . PRO A 296 ? 0.2638 0.2057 0.3676 0.0040  -0.0194 -0.0016 296 PRO A CA  
2177 C  C   . PRO A 296 ? 0.2722 0.2207 0.3727 0.0065  -0.0198 -0.0085 296 PRO A C   
2178 O  O   . PRO A 296 ? 0.2578 0.2110 0.3510 0.0053  -0.0180 -0.0151 296 PRO A O   
2179 C  CB  . PRO A 296 ? 0.2573 0.1916 0.3781 0.0046  -0.0202 -0.0045 296 PRO A CB  
2180 C  CG  . PRO A 296 ? 0.2896 0.2170 0.4136 0.0024  -0.0212 0.0070  296 PRO A CG  
2181 C  CD  . PRO A 296 ? 0.2735 0.2044 0.3877 0.0034  -0.0230 0.0163  296 PRO A CD  
2182 N  N   . GLN A 297 ? 0.2529 0.2031 0.3590 0.0097  -0.0224 -0.0065 297 GLN A N   
2183 C  CA  . GLN A 297 ? 0.2398 0.1986 0.3441 0.0113  -0.0224 -0.0131 297 GLN A CA  
2184 C  C   . GLN A 297 ? 0.2317 0.1956 0.3186 0.0080  -0.0217 -0.0114 297 GLN A C   
2185 O  O   . GLN A 297 ? 0.2274 0.1961 0.3080 0.0066  -0.0200 -0.0178 297 GLN A O   
2186 C  CB  . GLN A 297 ? 0.2139 0.1753 0.3298 0.0157  -0.0256 -0.0106 297 GLN A CB  
2187 C  CG  . GLN A 297 ? 0.2584 0.2153 0.3932 0.0202  -0.0259 -0.0160 297 GLN A CG  
2188 C  CD  . GLN A 297 ? 0.2579 0.2172 0.4060 0.0259  -0.0296 -0.0122 297 GLN A CD  
2189 O  OE1 . GLN A 297 ? 0.2361 0.1952 0.3814 0.0260  -0.0333 -0.0011 297 GLN A OE1 
2190 N  NE2 . GLN A 297 ? 0.2592 0.2219 0.4218 0.0308  -0.0288 -0.0217 297 GLN A NE2 
2191 N  N   . VAL A 298 ? 0.2219 0.1841 0.3003 0.0065  -0.0231 -0.0028 298 VAL A N   
2192 C  CA  . VAL A 298 ? 0.2278 0.1928 0.2899 0.0033  -0.0225 -0.0020 298 VAL A CA  
2193 C  C   . VAL A 298 ? 0.2252 0.1876 0.2789 0.0015  -0.0192 -0.0061 298 VAL A C   
2194 O  O   . VAL A 298 ? 0.2470 0.2112 0.2916 -0.0002 -0.0184 -0.0100 298 VAL A O   
2195 C  CB  . VAL A 298 ? 0.2675 0.2316 0.3222 0.0019  -0.0244 0.0071  298 VAL A CB  
2196 C  CG1 . VAL A 298 ? 0.2552 0.2200 0.2928 -0.0015 -0.0234 0.0064  298 VAL A CG1 
2197 C  CG2 . VAL A 298 ? 0.2657 0.2342 0.3287 0.0040  -0.0290 0.0120  298 VAL A CG2 
2198 N  N   . ILE A 299 ? 0.2238 0.1820 0.2815 0.0016  -0.0176 -0.0050 299 ILE A N   
2199 C  CA  . ILE A 299 ? 0.2465 0.2040 0.2986 0.0006  -0.0150 -0.0085 299 ILE A CA  
2200 C  C   . ILE A 299 ? 0.2369 0.1975 0.2916 0.0009  -0.0148 -0.0164 299 ILE A C   
2201 O  O   . ILE A 299 ? 0.2802 0.2418 0.3262 0.0000  -0.0141 -0.0189 299 ILE A O   
2202 C  CB  . ILE A 299 ? 0.2291 0.1840 0.2870 0.0000  -0.0134 -0.0055 299 ILE A CB  
2203 C  CG1 . ILE A 299 ? 0.2604 0.2143 0.3116 -0.0012 -0.0127 0.0025  299 ILE A CG1 
2204 C  CG2 . ILE A 299 ? 0.3067 0.2635 0.3630 -0.0003 -0.0115 -0.0100 299 ILE A CG2 
2205 C  CD1 . ILE A 299 ? 0.2836 0.2385 0.3195 -0.0017 -0.0114 0.0023  299 ILE A CD1 
2206 N  N   . ASP A 300 ? 0.2608 0.2229 0.3274 0.0021  -0.0156 -0.0205 300 ASP A N   
2207 C  CA  . ASP A 300 ? 0.2193 0.1866 0.2871 0.0019  -0.0151 -0.0288 300 ASP A CA  
2208 C  C   . ASP A 300 ? 0.2379 0.2100 0.2956 0.0005  -0.0152 -0.0294 300 ASP A C   
2209 O  O   . ASP A 300 ? 0.2184 0.1935 0.2687 -0.0014 -0.0145 -0.0327 300 ASP A O   
2210 C  CB  . ASP A 300 ? 0.2479 0.2162 0.3306 0.0040  -0.0154 -0.0341 300 ASP A CB  
2211 C  CG  . ASP A 300 ? 0.3198 0.2845 0.4116 0.0036  -0.0150 -0.0380 300 ASP A CG  
2212 O  OD1 . ASP A 300 ? 0.3030 0.2658 0.3904 0.0016  -0.0146 -0.0354 300 ASP A OD1 
2213 O  OD2 . ASP A 300 ? 0.4050 0.3688 0.5090 0.0053  -0.0151 -0.0441 300 ASP A OD2 
2214 N  N   . CYS A 301 ? 0.1998 0.1729 0.2570 0.0008  -0.0164 -0.0254 301 CYS A N   
2215 C  CA  . CYS A 301 ? 0.2243 0.2022 0.2728 -0.0017 -0.0167 -0.0257 301 CYS A CA  
2216 C  C   . CYS A 301 ? 0.2395 0.2126 0.2730 -0.0045 -0.0163 -0.0235 301 CYS A C   
2217 O  O   . CYS A 301 ? 0.2351 0.2106 0.2608 -0.0077 -0.0164 -0.0245 301 CYS A O   
2218 C  CB  . CYS A 301 ? 0.2480 0.2283 0.2987 -0.0013 -0.0189 -0.0211 301 CYS A CB  
2219 S  SG  . CYS A 301 ? 0.2394 0.2273 0.3085 0.0028  -0.0199 -0.0241 301 CYS A SG  
2220 N  N   . VAL A 302 ? 0.2211 0.1874 0.2509 -0.0036 -0.0158 -0.0204 302 VAL A N   
2221 C  CA  . VAL A 302 ? 0.2479 0.2090 0.2650 -0.0049 -0.0154 -0.0191 302 VAL A CA  
2222 C  C   . VAL A 302 ? 0.2631 0.2229 0.2807 -0.0035 -0.0145 -0.0209 302 VAL A C   
2223 O  O   . VAL A 302 ? 0.2485 0.2035 0.2580 -0.0031 -0.0143 -0.0197 302 VAL A O   
2224 C  CB  . VAL A 302 ? 0.2274 0.1833 0.2378 -0.0049 -0.0153 -0.0148 302 VAL A CB  
2225 C  CG1 . VAL A 302 ? 0.2157 0.1747 0.2255 -0.0069 -0.0172 -0.0127 302 VAL A CG1 
2226 C  CG2 . VAL A 302 ? 0.2289 0.1836 0.2447 -0.0026 -0.0138 -0.0124 302 VAL A CG2 
2227 N  N   . THR A 303 ? 0.2221 0.1864 0.2495 -0.0026 -0.0144 -0.0243 303 THR A N   
2228 C  CA  . THR A 303 ? 0.2464 0.2119 0.2748 -0.0018 -0.0144 -0.0262 303 THR A CA  
2229 C  C   . THR A 303 ? 0.2377 0.2099 0.2685 -0.0034 -0.0151 -0.0317 303 THR A C   
2230 O  O   . THR A 303 ? 0.2477 0.2218 0.2698 -0.0052 -0.0158 -0.0320 303 THR A O   
2231 C  CB  . THR A 303 ? 0.2475 0.2124 0.2851 -0.0003 -0.0135 -0.0251 303 THR A CB  
2232 O  OG1 . THR A 303 ? 0.2297 0.1954 0.2780 -0.0005 -0.0135 -0.0266 303 THR A OG1 
2233 C  CG2 . THR A 303 ? 0.2506 0.2110 0.2834 0.0009  -0.0120 -0.0199 303 THR A CG2 
2234 N  N   . VAL A 304 ? 0.2082 0.1839 0.2503 -0.0030 -0.0148 -0.0363 304 VAL A N   
2235 C  CA  . VAL A 304 ? 0.2402 0.2233 0.2841 -0.0046 -0.0151 -0.0432 304 VAL A CA  
2236 C  C   . VAL A 304 ? 0.2622 0.2508 0.3016 -0.0064 -0.0143 -0.0460 304 VAL A C   
2237 O  O   . VAL A 304 ? 0.2573 0.2523 0.2896 -0.0091 -0.0146 -0.0486 304 VAL A O   
2238 C  CB  . VAL A 304 ? 0.2786 0.2626 0.3363 -0.0041 -0.0148 -0.0489 304 VAL A CB  
2239 C  CG1 . VAL A 304 ? 0.2927 0.2729 0.3600 -0.0021 -0.0139 -0.0488 304 VAL A CG1 
2240 C  CG2 . VAL A 304 ? 0.3019 0.2942 0.3602 -0.0063 -0.0151 -0.0578 304 VAL A CG2 
2241 N  N   . SER A 305 ? 0.2402 0.2278 0.2835 -0.0054 -0.0135 -0.0447 305 SER A N   
2242 C  CA  . SER A 305 ? 0.2631 0.2585 0.3045 -0.0073 -0.0123 -0.0475 305 SER A CA  
2243 C  C   . SER A 305 ? 0.2767 0.2717 0.3036 -0.0110 -0.0129 -0.0427 305 SER A C   
2244 O  O   . SER A 305 ? 0.2600 0.2629 0.2813 -0.0146 -0.0119 -0.0451 305 SER A O   
2245 C  CB  . SER A 305 ? 0.2612 0.2568 0.3120 -0.0048 -0.0122 -0.0465 305 SER A CB  
2246 O  OG  . SER A 305 ? 0.2648 0.2597 0.3301 -0.0013 -0.0118 -0.0512 305 SER A OG  
2247 N  N   . ALA A 306 ? 0.2306 0.2161 0.2510 -0.0106 -0.0142 -0.0361 306 ALA A N   
2248 C  CA  . ALA A 306 ? 0.2528 0.2345 0.2601 -0.0140 -0.0150 -0.0317 306 ALA A CA  
2249 C  C   . ALA A 306 ? 0.2806 0.2635 0.2809 -0.0155 -0.0160 -0.0317 306 ALA A C   
2250 O  O   . ALA A 306 ? 0.2870 0.2725 0.2784 -0.0199 -0.0163 -0.0301 306 ALA A O   
2251 C  CB  . ALA A 306 ? 0.2370 0.2074 0.2395 -0.0125 -0.0159 -0.0264 306 ALA A CB  
2252 N  N   . ALA A 307 ? 0.2216 0.2036 0.2259 -0.0124 -0.0169 -0.0327 307 ALA A N   
2253 C  CA  . ALA A 307 ? 0.2548 0.2396 0.2532 -0.0135 -0.0188 -0.0321 307 ALA A CA  
2254 C  C   . ALA A 307 ? 0.2786 0.2757 0.2757 -0.0173 -0.0181 -0.0375 307 ALA A C   
2255 O  O   . ALA A 307 ? 0.2906 0.2911 0.2775 -0.0208 -0.0195 -0.0350 307 ALA A O   
2256 C  CB  . ALA A 307 ? 0.2598 0.2437 0.2648 -0.0097 -0.0201 -0.0327 307 ALA A CB  
2257 N  N   . GLU A 308 ? 0.2794 0.2833 0.2866 -0.0167 -0.0158 -0.0449 308 GLU A N   
2258 C  CA  . GLU A 308 ? 0.2924 0.3093 0.2986 -0.0201 -0.0141 -0.0519 308 GLU A CA  
2259 C  C   . GLU A 308 ? 0.3161 0.3380 0.3140 -0.0247 -0.0124 -0.0494 308 GLU A C   
2260 O  O   . GLU A 308 ? 0.3242 0.3550 0.3127 -0.0295 -0.0121 -0.0499 308 GLU A O   
2261 C  CB  . GLU A 308 ? 0.2861 0.3076 0.3067 -0.0175 -0.0116 -0.0613 308 GLU A CB  
2262 C  CG  . GLU A 308 ? 0.3480 0.3678 0.3760 -0.0155 -0.0131 -0.0658 308 GLU A CG  
2263 C  CD  . GLU A 308 ? 0.3696 0.3877 0.4137 -0.0122 -0.0114 -0.0730 308 GLU A CD  
2264 O  OE1 . GLU A 308 ? 0.3583 0.3778 0.4084 -0.0105 -0.0091 -0.0749 308 GLU A OE1 
2265 O  OE2 . GLU A 308 ? 0.3987 0.4141 0.4501 -0.0114 -0.0126 -0.0767 308 GLU A OE2 
2266 N  N   . GLY A 309 ? 0.3051 0.3223 0.3058 -0.0242 -0.0115 -0.0463 309 GLY A N   
2267 C  CA  . GLY A 309 ? 0.3144 0.3382 0.3096 -0.0294 -0.0097 -0.0447 309 GLY A CA  
2268 C  C   . GLY A 309 ? 0.3082 0.3273 0.2879 -0.0349 -0.0116 -0.0367 309 GLY A C   
2269 O  O   . GLY A 309 ? 0.3379 0.3656 0.3111 -0.0412 -0.0100 -0.0357 309 GLY A O   
2270 N  N   . LEU A 310 ? 0.3306 0.3364 0.3051 -0.0325 -0.0150 -0.0307 310 LEU A N   
2271 C  CA  . LEU A 310 ? 0.3278 0.3263 0.2888 -0.0365 -0.0176 -0.0225 310 LEU A CA  
2272 C  C   . LEU A 310 ? 0.3188 0.3191 0.2748 -0.0356 -0.0205 -0.0209 310 LEU A C   
2273 O  O   . LEU A 310 ? 0.3272 0.3192 0.2734 -0.0370 -0.0238 -0.0129 310 LEU A O   
2274 C  CB  . LEU A 310 ? 0.2823 0.2634 0.2412 -0.0343 -0.0195 -0.0168 310 LEU A CB  
2275 C  CG  . LEU A 310 ? 0.3317 0.3119 0.2909 -0.0382 -0.0178 -0.0165 310 LEU A CG  
2276 C  CD1 . LEU A 310 ? 0.3582 0.3214 0.3137 -0.0367 -0.0197 -0.0124 310 LEU A CD1 
2277 C  CD2 . LEU A 310 ? 0.3239 0.3119 0.2752 -0.0471 -0.0168 -0.0140 310 LEU A CD2 
2278 N  N   . ARG A 311 ? 0.2941 0.3048 0.2570 -0.0333 -0.0198 -0.0283 311 ARG A N   
2279 C  CA  . ARG A 311 ? 0.3325 0.3488 0.2910 -0.0333 -0.0229 -0.0281 311 ARG A CA  
2280 C  C   . ARG A 311 ? 0.3082 0.3125 0.2658 -0.0285 -0.0275 -0.0209 311 ARG A C   
2281 O  O   . ARG A 311 ? 0.3141 0.3190 0.2635 -0.0296 -0.0316 -0.0150 311 ARG A O   
2282 C  CB  . ARG A 311 ? 0.3565 0.3832 0.3016 -0.0408 -0.0232 -0.0253 311 ARG A CB  
2283 C  CG  . ARG A 311 ? 0.3585 0.3985 0.3048 -0.0456 -0.0177 -0.0322 311 ARG A CG  
2284 C  CD  . ARG A 311 ? 0.4683 0.5220 0.4010 -0.0537 -0.0171 -0.0304 311 ARG A CD  
2285 N  NE  . ARG A 311 ? 0.5070 0.5740 0.4418 -0.0583 -0.0110 -0.0364 311 ARG A NE  
2286 C  CZ  . ARG A 311 ? 0.5157 0.5964 0.4394 -0.0667 -0.0086 -0.0348 311 ARG A CZ  
2287 N  NH1 . ARG A 311 ? 0.5411 0.6235 0.4494 -0.0720 -0.0121 -0.0266 311 ARG A NH1 
2288 N  NH2 . ARG A 311 ? 0.5110 0.6051 0.4397 -0.0700 -0.0025 -0.0411 311 ARG A NH2 
2289 N  N   . LEU A 312 ? 0.2781 0.2724 0.2445 -0.0230 -0.0268 -0.0213 312 LEU A N   
2290 C  CA  . LEU A 312 ? 0.2951 0.2799 0.2633 -0.0174 -0.0299 -0.0164 312 LEU A CA  
2291 C  C   . LEU A 312 ? 0.2861 0.2797 0.2639 -0.0144 -0.0312 -0.0213 312 LEU A C   
2292 O  O   . LEU A 312 ? 0.2937 0.2864 0.2823 -0.0113 -0.0290 -0.0257 312 LEU A O   
2293 C  CB  . LEU A 312 ? 0.3042 0.2761 0.2760 -0.0139 -0.0279 -0.0150 312 LEU A CB  
2294 C  CG  . LEU A 312 ? 0.2869 0.2528 0.2519 -0.0183 -0.0261 -0.0130 312 LEU A CG  
2295 C  CD1 . LEU A 312 ? 0.3021 0.2580 0.2709 -0.0154 -0.0241 -0.0134 312 LEU A CD1 
2296 C  CD2 . LEU A 312 ? 0.3128 0.2719 0.2657 -0.0218 -0.0290 -0.0054 312 LEU A CD2 
2297 N  N   . SER A 313 ? 0.3098 0.3118 0.2829 -0.0159 -0.0351 -0.0199 313 SER A N   
2298 C  CA  . SER A 313 ? 0.2974 0.3119 0.2777 -0.0161 -0.0363 -0.0268 313 SER A CA  
2299 C  C   . SER A 313 ? 0.3054 0.3174 0.2986 -0.0106 -0.0368 -0.0278 313 SER A C   
2300 O  O   . SER A 313 ? 0.3042 0.3225 0.3073 -0.0113 -0.0356 -0.0352 313 SER A O   
2301 C  CB  . SER A 313 ? 0.3283 0.3534 0.2994 -0.0193 -0.0414 -0.0240 313 SER A CB  
2302 O  OG  . SER A 313 ? 0.4221 0.4410 0.3904 -0.0152 -0.0464 -0.0141 313 SER A OG  
2303 N  N   . ARG A 314 ? 0.2614 0.2648 0.2554 -0.0056 -0.0385 -0.0207 314 ARG A N   
2304 C  CA  . ARG A 314 ? 0.2738 0.2777 0.2801 -0.0007 -0.0385 -0.0214 314 ARG A CA  
2305 C  C   . ARG A 314 ? 0.2862 0.2795 0.2974 0.0025  -0.0337 -0.0212 314 ARG A C   
2306 O  O   . ARG A 314 ? 0.2682 0.2615 0.2883 0.0066  -0.0329 -0.0206 314 ARG A O   
2307 C  CB  . ARG A 314 ? 0.2712 0.2769 0.2776 0.0039  -0.0436 -0.0148 314 ARG A CB  
2308 C  CG  . ARG A 314 ? 0.3220 0.3380 0.3205 0.0007  -0.0496 -0.0124 314 ARG A CG  
2309 C  CD  . ARG A 314 ? 0.3582 0.3891 0.3609 -0.0046 -0.0500 -0.0210 314 ARG A CD  
2310 N  NE  . ARG A 314 ? 0.3627 0.4007 0.3802 -0.0024 -0.0506 -0.0247 314 ARG A NE  
2311 C  CZ  . ARG A 314 ? 0.3940 0.4422 0.4184 -0.0068 -0.0506 -0.0332 314 ARG A CZ  
2312 N  NH1 . ARG A 314 ? 0.3874 0.4399 0.4058 -0.0126 -0.0495 -0.0402 314 ARG A NH1 
2313 N  NH2 . ARG A 314 ? 0.3736 0.4282 0.4120 -0.0055 -0.0514 -0.0354 314 ARG A NH2 
2314 N  N   . LYS A 315 ? 0.2611 0.2469 0.2667 0.0003  -0.0306 -0.0217 315 LYS A N   
2315 C  CA  . LYS A 315 ? 0.2571 0.2342 0.2658 0.0023  -0.0266 -0.0215 315 LYS A CA  
2316 C  C   . LYS A 315 ? 0.2374 0.2176 0.2530 -0.0003 -0.0236 -0.0269 315 LYS A C   
2317 O  O   . LYS A 315 ? 0.2455 0.2331 0.2630 -0.0035 -0.0241 -0.0317 315 LYS A O   
2318 C  CB  . LYS A 315 ? 0.2739 0.2397 0.2717 0.0018  -0.0261 -0.0174 315 LYS A CB  
2319 C  CG  . LYS A 315 ? 0.2770 0.2368 0.2671 0.0040  -0.0296 -0.0116 315 LYS A CG  
2320 C  CD  . LYS A 315 ? 0.2700 0.2253 0.2657 0.0109  -0.0295 -0.0098 315 LYS A CD  
2321 C  CE  . LYS A 315 ? 0.3391 0.2809 0.3271 0.0140  -0.0314 -0.0047 315 LYS A CE  
2322 N  NZ  . LYS A 315 ? 0.3713 0.3128 0.3667 0.0220  -0.0323 -0.0034 315 LYS A NZ  
2323 N  N   . GLY A 316 ? 0.2380 0.2126 0.2578 0.0014  -0.0207 -0.0261 316 GLY A N   
2324 C  CA  . GLY A 316 ? 0.2517 0.2265 0.2774 -0.0003 -0.0184 -0.0290 316 GLY A CA  
2325 C  C   . GLY A 316 ? 0.2619 0.2418 0.3002 -0.0009 -0.0180 -0.0329 316 GLY A C   
2326 O  O   . GLY A 316 ? 0.2441 0.2223 0.2887 -0.0017 -0.0165 -0.0346 316 GLY A O   
2327 N  N   . ARG A 317 ? 0.2817 0.2676 0.3248 -0.0007 -0.0197 -0.0340 317 ARG A N   
2328 C  CA  . ARG A 317 ? 0.2906 0.2811 0.3459 -0.0027 -0.0197 -0.0384 317 ARG A CA  
2329 C  C   . ARG A 317 ? 0.3031 0.2961 0.3658 -0.0015 -0.0192 -0.0354 317 ARG A C   
2330 O  O   . ARG A 317 ? 0.3014 0.2989 0.3619 0.0007  -0.0209 -0.0331 317 ARG A O   
2331 C  CB  . ARG A 317 ? 0.3076 0.3065 0.3632 -0.0057 -0.0224 -0.0451 317 ARG A CB  
2332 C  CG  . ARG A 317 ? 0.3369 0.3361 0.3866 -0.0074 -0.0218 -0.0495 317 ARG A CG  
2333 C  CD  . ARG A 317 ? 0.3457 0.3500 0.3828 -0.0084 -0.0241 -0.0481 317 ARG A CD  
2334 N  NE  . ARG A 317 ? 0.4156 0.4251 0.4479 -0.0115 -0.0232 -0.0540 317 ARG A NE  
2335 C  CZ  . ARG A 317 ? 0.3841 0.3959 0.4042 -0.0132 -0.0236 -0.0513 317 ARG A CZ  
2336 N  NH1 . ARG A 317 ? 0.2635 0.2700 0.2750 -0.0119 -0.0253 -0.0427 317 ARG A NH1 
2337 N  NH2 . ARG A 317 ? 0.3500 0.3692 0.3668 -0.0164 -0.0220 -0.0574 317 ARG A NH2 
2338 N  N   . LEU A 318 ? 0.2988 0.2895 0.3711 -0.0030 -0.0170 -0.0350 318 LEU A N   
2339 C  CA  . LEU A 318 ? 0.3372 0.3326 0.4187 -0.0035 -0.0158 -0.0326 318 LEU A CA  
2340 C  C   . LEU A 318 ? 0.3035 0.3071 0.3951 -0.0074 -0.0185 -0.0381 318 LEU A C   
2341 O  O   . LEU A 318 ? 0.3093 0.3114 0.4113 -0.0114 -0.0178 -0.0401 318 LEU A O   
2342 C  CB  . LEU A 318 ? 0.3162 0.3056 0.4023 -0.0046 -0.0123 -0.0283 318 LEU A CB  
2343 C  CG  . LEU A 318 ? 0.3476 0.3380 0.4312 -0.0024 -0.0088 -0.0222 318 LEU A CG  
2344 C  CD1 . LEU A 318 ? 0.3242 0.3107 0.4130 -0.0054 -0.0059 -0.0176 318 LEU A CD1 
2345 C  CD2 . LEU A 318 ? 0.3319 0.3333 0.4211 -0.0011 -0.0089 -0.0224 318 LEU A CD2 
2346 N  N   . GLU A 319 ? 0.2788 0.2904 0.3666 -0.0068 -0.0221 -0.0405 319 GLU A N   
2347 C  CA  . GLU A 319 ? 0.2685 0.2899 0.3635 -0.0109 -0.0256 -0.0465 319 GLU A CA  
2348 C  C   . GLU A 319 ? 0.2586 0.2921 0.3546 -0.0088 -0.0289 -0.0439 319 GLU A C   
2349 O  O   . GLU A 319 ? 0.2298 0.2625 0.3174 -0.0036 -0.0295 -0.0390 319 GLU A O   
2350 C  CB  . GLU A 319 ? 0.3047 0.3268 0.3935 -0.0133 -0.0280 -0.0538 319 GLU A CB  
2351 C  CG  . GLU A 319 ? 0.3663 0.3780 0.4508 -0.0128 -0.0252 -0.0558 319 GLU A CG  
2352 C  CD  . GLU A 319 ? 0.3963 0.4025 0.4923 -0.0161 -0.0237 -0.0615 319 GLU A CD  
2353 O  OE1 . GLU A 319 ? 0.4379 0.4412 0.5328 -0.0166 -0.0232 -0.0680 319 GLU A OE1 
2354 O  OE2 . GLU A 319 ? 0.4948 0.4993 0.6016 -0.0180 -0.0229 -0.0592 319 GLU A OE2 
2355 N  N   . ALA A 320 ? 0.2279 0.2724 0.3349 -0.0128 -0.0314 -0.0473 320 ALA A N   
2356 C  CA  . ALA A 320 ? 0.2301 0.2890 0.3405 -0.0108 -0.0354 -0.0451 320 ALA A CA  
2357 C  C   . ALA A 320 ? 0.2617 0.3236 0.3594 -0.0082 -0.0403 -0.0444 320 ALA A C   
2358 O  O   . ALA A 320 ? 0.2334 0.2943 0.3235 -0.0118 -0.0423 -0.0497 320 ALA A O   
2359 C  CB  . ALA A 320 ? 0.2209 0.2924 0.3450 -0.0174 -0.0383 -0.0502 320 ALA A CB  
2360 N  N   . GLY A 321 ? 0.2474 0.3130 0.3429 -0.0018 -0.0422 -0.0378 321 GLY A N   
2361 C  CA  . GLY A 321 ? 0.2555 0.3236 0.3397 0.0008  -0.0476 -0.0348 321 GLY A CA  
2362 C  C   . GLY A 321 ? 0.2817 0.3349 0.3515 0.0043  -0.0454 -0.0306 321 GLY A C   
2363 O  O   . GLY A 321 ? 0.2899 0.3429 0.3508 0.0074  -0.0496 -0.0256 321 GLY A O   
2364 N  N   . PHE A 322 ? 0.2668 0.3076 0.3344 0.0036  -0.0396 -0.0320 322 PHE A N   
2365 C  CA  . PHE A 322 ? 0.3019 0.3294 0.3568 0.0062  -0.0376 -0.0282 322 PHE A CA  
2366 C  C   . PHE A 322 ? 0.2729 0.2943 0.3286 0.0132  -0.0358 -0.0224 322 PHE A C   
2367 O  O   . PHE A 322 ? 0.2910 0.3192 0.3580 0.0163  -0.0348 -0.0216 322 PHE A O   
2368 C  CB  . PHE A 322 ? 0.2784 0.2970 0.3312 0.0027  -0.0329 -0.0320 322 PHE A CB  
2369 C  CG  . PHE A 322 ? 0.3151 0.3375 0.3644 -0.0028 -0.0342 -0.0384 322 PHE A CG  
2370 C  CD1 . PHE A 322 ? 0.3059 0.3370 0.3645 -0.0070 -0.0354 -0.0452 322 PHE A CD1 
2371 C  CD2 . PHE A 322 ? 0.3214 0.3397 0.3585 -0.0042 -0.0340 -0.0382 322 PHE A CD2 
2372 C  CE1 . PHE A 322 ? 0.3124 0.3473 0.3677 -0.0118 -0.0362 -0.0529 322 PHE A CE1 
2373 C  CE2 . PHE A 322 ? 0.3242 0.3483 0.3582 -0.0091 -0.0344 -0.0452 322 PHE A CE2 
2374 C  CZ  . PHE A 322 ? 0.3628 0.3949 0.4058 -0.0125 -0.0353 -0.0531 322 PHE A CZ  
2375 N  N   . ASP A 323 ? 0.2678 0.2768 0.3119 0.0155  -0.0351 -0.0188 323 ASP A N   
2376 C  CA  . ASP A 323 ? 0.2283 0.2292 0.2717 0.0222  -0.0333 -0.0147 323 ASP A CA  
2377 C  C   . ASP A 323 ? 0.2850 0.2848 0.3358 0.0233  -0.0270 -0.0167 323 ASP A C   
2378 O  O   . ASP A 323 ? 0.2570 0.2541 0.3075 0.0187  -0.0237 -0.0193 323 ASP A O   
2379 C  CB  . ASP A 323 ? 0.2885 0.2746 0.3178 0.0225  -0.0333 -0.0116 323 ASP A CB  
2380 C  CG  . ASP A 323 ? 0.3264 0.3124 0.3477 0.0224  -0.0395 -0.0069 323 ASP A CG  
2381 O  OD1 . ASP A 323 ? 0.3107 0.3086 0.3375 0.0237  -0.0443 -0.0056 323 ASP A OD1 
2382 O  OD2 . ASP A 323 ? 0.3547 0.3294 0.3642 0.0207  -0.0399 -0.0039 323 ASP A OD2 
2383 N  N   . ALA A 324 ? 0.2442 0.2466 0.3017 0.0295  -0.0254 -0.0152 324 ALA A N   
2384 C  CA  . ALA A 324 ? 0.2617 0.2655 0.3255 0.0302  -0.0190 -0.0168 324 ALA A CA  
2385 C  C   . ALA A 324 ? 0.2341 0.2232 0.2867 0.0315  -0.0149 -0.0165 324 ALA A C   
2386 O  O   . ALA A 324 ? 0.2692 0.2560 0.3223 0.0367  -0.0113 -0.0168 324 ALA A O   
2387 C  CB  . ALA A 324 ? 0.2592 0.2753 0.3359 0.0360  -0.0181 -0.0164 324 ALA A CB  
2388 N  N   . ASP A 325 ? 0.2260 0.2064 0.2689 0.0265  -0.0155 -0.0168 325 ASP A N   
2389 C  CA  . ASP A 325 ? 0.2574 0.2260 0.2903 0.0256  -0.0122 -0.0169 325 ASP A CA  
2390 C  C   . ASP A 325 ? 0.2538 0.2257 0.2902 0.0209  -0.0087 -0.0176 325 ASP A C   
2391 O  O   . ASP A 325 ? 0.2341 0.2089 0.2736 0.0163  -0.0104 -0.0184 325 ASP A O   
2392 C  CB  . ASP A 325 ? 0.2850 0.2434 0.3061 0.0228  -0.0152 -0.0160 325 ASP A CB  
2393 C  CG  . ASP A 325 ? 0.2926 0.2449 0.3087 0.0267  -0.0190 -0.0135 325 ASP A CG  
2394 O  OD1 . ASP A 325 ? 0.3003 0.2551 0.3225 0.0330  -0.0194 -0.0128 325 ASP A OD1 
2395 O  OD2 . ASP A 325 ? 0.3540 0.2990 0.3607 0.0234  -0.0217 -0.0118 325 ASP A OD2 
2396 N  N   . LEU A 326 ? 0.2357 0.2070 0.2714 0.0221  -0.0039 -0.0175 326 LEU A N   
2397 C  CA  . LEU A 326 ? 0.2528 0.2271 0.2914 0.0178  -0.0008 -0.0163 326 LEU A CA  
2398 C  C   . LEU A 326 ? 0.2596 0.2266 0.2873 0.0174  0.0023  -0.0157 326 LEU A C   
2399 O  O   . LEU A 326 ? 0.2569 0.2192 0.2777 0.0213  0.0039  -0.0175 326 LEU A O   
2400 C  CB  . LEU A 326 ? 0.2183 0.2048 0.2692 0.0179  0.0024  -0.0156 326 LEU A CB  
2401 C  CG  . LEU A 326 ? 0.2420 0.2383 0.3048 0.0181  -0.0007 -0.0167 326 LEU A CG  
2402 C  CD1 . LEU A 326 ? 0.2965 0.3058 0.3713 0.0180  0.0032  -0.0160 326 LEU A CD1 
2403 C  CD2 . LEU A 326 ? 0.2664 0.2616 0.3322 0.0126  -0.0041 -0.0174 326 LEU A CD2 
2404 N  N   . THR A 327 ? 0.2504 0.2164 0.2766 0.0128  0.0028  -0.0134 327 THR A N   
2405 C  CA  . THR A 327 ? 0.2540 0.2163 0.2702 0.0115  0.0054  -0.0121 327 THR A CA  
2406 C  C   . THR A 327 ? 0.2305 0.2003 0.2518 0.0086  0.0089  -0.0082 327 THR A C   
2407 O  O   . THR A 327 ? 0.2391 0.2113 0.2693 0.0053  0.0074  -0.0052 327 THR A O   
2408 C  CB  . THR A 327 ? 0.2609 0.2160 0.2695 0.0085  0.0020  -0.0114 327 THR A CB  
2409 O  OG1 . THR A 327 ? 0.2469 0.1954 0.2502 0.0100  -0.0008 -0.0143 327 THR A OG1 
2410 C  CG2 . THR A 327 ? 0.2368 0.1898 0.2347 0.0065  0.0039  -0.0099 327 THR A CG2 
2411 N  N   . LEU A 328 ? 0.2671 0.2403 0.2828 0.0095  0.0138  -0.0083 328 LEU A N   
2412 C  CA  . LEU A 328 ? 0.2394 0.2206 0.2571 0.0057  0.0178  -0.0035 328 LEU A CA  
2413 C  C   . LEU A 328 ? 0.2615 0.2389 0.2654 0.0027  0.0180  -0.0010 328 LEU A C   
2414 O  O   . LEU A 328 ? 0.2838 0.2576 0.2758 0.0047  0.0194  -0.0054 328 LEU A O   
2415 C  CB  . LEU A 328 ? 0.2454 0.2373 0.2670 0.0083  0.0241  -0.0056 328 LEU A CB  
2416 C  CG  . LEU A 328 ? 0.2749 0.2760 0.3127 0.0097  0.0245  -0.0063 328 LEU A CG  
2417 C  CD1 . LEU A 328 ? 0.2667 0.2625 0.3084 0.0140  0.0193  -0.0103 328 LEU A CD1 
2418 C  CD2 . LEU A 328 ? 0.2620 0.2763 0.3039 0.0126  0.0315  -0.0086 328 LEU A CD2 
2419 N  N   . PHE A 329 ? 0.2942 0.2721 0.2999 -0.0020 0.0161  0.0060  329 PHE A N   
2420 C  CA  . PHE A 329 ? 0.3129 0.2878 0.3065 -0.0049 0.0142  0.0094  329 PHE A CA  
2421 C  C   . PHE A 329 ? 0.3209 0.3005 0.3170 -0.0099 0.0145  0.0190  329 PHE A C   
2422 O  O   . PHE A 329 ? 0.2803 0.2634 0.2884 -0.0116 0.0159  0.0228  329 PHE A O   
2423 C  CB  . PHE A 329 ? 0.2949 0.2615 0.2874 -0.0043 0.0080  0.0079  329 PHE A CB  
2424 C  CG  . PHE A 329 ? 0.2932 0.2578 0.2996 -0.0048 0.0041  0.0106  329 PHE A CG  
2425 C  CD1 . PHE A 329 ? 0.2846 0.2484 0.3008 -0.0024 0.0035  0.0060  329 PHE A CD1 
2426 C  CD2 . PHE A 329 ? 0.2904 0.2540 0.3000 -0.0073 0.0006  0.0173  329 PHE A CD2 
2427 C  CE1 . PHE A 329 ? 0.2806 0.2428 0.3088 -0.0030 0.0003  0.0066  329 PHE A CE1 
2428 C  CE2 . PHE A 329 ? 0.3100 0.2707 0.3333 -0.0070 -0.0027 0.0183  329 PHE A CE2 
2429 C  CZ  . PHE A 329 ? 0.2911 0.2510 0.3232 -0.0050 -0.0025 0.0122  329 PHE A CZ  
2430 N  N   . ARG A 330 ? 0.3234 0.3032 0.3077 -0.0128 0.0130  0.0235  330 ARG A N   
2431 C  CA  . ARG A 330 ? 0.3232 0.3067 0.3078 -0.0178 0.0123  0.0345  330 ARG A CA  
2432 C  C   . ARG A 330 ? 0.3630 0.3417 0.3440 -0.0188 0.0052  0.0393  330 ARG A C   
2433 O  O   . ARG A 330 ? 0.3318 0.3079 0.3044 -0.0172 0.0026  0.0339  330 ARG A O   
2434 C  CB  . ARG A 330 ? 0.4065 0.3999 0.3782 -0.0212 0.0184  0.0368  330 ARG A CB  
2435 C  CG  . ARG A 330 ? 0.4020 0.4039 0.3817 -0.0220 0.0255  0.0364  330 ARG A CG  
2436 C  CD  . ARG A 330 ? 0.4303 0.4443 0.3983 -0.0268 0.0318  0.0409  330 ARG A CD  
2437 N  NE  . ARG A 330 ? 0.4931 0.5074 0.4511 -0.0323 0.0280  0.0518  330 ARG A NE  
2438 C  CZ  . ARG A 330 ? 0.5116 0.5246 0.4771 -0.0370 0.0249  0.0646  330 ARG A CZ  
2439 N  NH1 . ARG A 330 ? 0.4590 0.4692 0.4425 -0.0375 0.0251  0.0673  330 ARG A NH1 
2440 N  NH2 . ARG A 330 ? 0.4764 0.4904 0.4315 -0.0414 0.0209  0.0752  330 ARG A NH2 
2441 N  N   . LEU A 331 ? 0.3102 0.2878 0.2990 -0.0213 0.0018  0.0497  331 LEU A N   
2442 C  CA  . LEU A 331 ? 0.3457 0.3216 0.3318 -0.0221 -0.0050 0.0568  331 LEU A CA  
2443 C  C   . LEU A 331 ? 0.4257 0.4090 0.3988 -0.0274 -0.0040 0.0666  331 LEU A C   
2444 O  O   . LEU A 331 ? 0.4645 0.4488 0.4427 -0.0309 -0.0032 0.0769  331 LEU A O   
2445 C  CB  . LEU A 331 ? 0.3888 0.3575 0.3930 -0.0204 -0.0101 0.0619  331 LEU A CB  
2446 N  N   . GLU A 332 ? 0.4404 0.4290 0.3958 -0.0288 -0.0038 0.0634  332 GLU A N   
2447 C  CA  . GLU A 332 ? 0.4835 0.4814 0.4230 -0.0344 -0.0018 0.0707  332 GLU A CA  
2448 C  C   . GLU A 332 ? 0.4564 0.4564 0.3896 -0.0367 -0.0102 0.0803  332 GLU A C   
2449 O  O   . GLU A 332 ? 0.4707 0.4682 0.4037 -0.0343 -0.0158 0.0759  332 GLU A O   
2450 C  CB  . GLU A 332 ? 0.4944 0.4981 0.4171 -0.0350 0.0047  0.0595  332 GLU A CB  
2451 C  CG  . GLU A 332 ? 0.4942 0.5007 0.4221 -0.0335 0.0137  0.0534  332 GLU A CG  
2452 C  CD  . GLU A 332 ? 0.5216 0.5305 0.4373 -0.0313 0.0195  0.0398  332 GLU A CD  
2453 O  OE1 . GLU A 332 ? 0.5454 0.5593 0.4429 -0.0344 0.0198  0.0378  332 GLU A OE1 
2454 O  OE2 . GLU A 332 ? 0.4694 0.4753 0.3939 -0.0265 0.0236  0.0310  332 GLU A OE2 
2455 N  N   . ARG A 333 ? 0.4506 0.4560 0.3794 -0.0416 -0.0112 0.0942  333 ARG A N   
2456 C  CA  . ARG A 333 ? 0.4811 0.4909 0.4020 -0.0442 -0.0195 0.1052  333 ARG A CA  
2457 C  C   . ARG A 333 ? 0.5294 0.5491 0.4267 -0.0478 -0.0184 0.0984  333 ARG A C   
2458 O  O   . ARG A 333 ? 0.5338 0.5625 0.4153 -0.0529 -0.0123 0.0991  333 ARG A O   
2459 C  CB  . ARG A 333 ? 0.4976 0.5096 0.4197 -0.0490 -0.0210 0.1233  333 ARG A CB  
2460 N  N   . GLN A 334 ? 0.4976 0.5161 0.3928 -0.0456 -0.0237 0.0909  334 GLN A N   
2461 C  CA  . GLN A 334 ? 0.5690 0.5949 0.4427 -0.0494 -0.0235 0.0826  334 GLN A CA  
2462 C  C   . GLN A 334 ? 0.5857 0.6129 0.4611 -0.0489 -0.0337 0.0837  334 GLN A C   
2463 O  O   . GLN A 334 ? 0.5696 0.5904 0.4533 -0.0452 -0.0350 0.0739  334 GLN A O   
2464 C  CB  . GLN A 334 ? 0.5436 0.5649 0.4127 -0.0473 -0.0153 0.0650  334 GLN A CB  
2465 N  N   . PRO A 335 ? 0.6097 0.6462 0.4783 -0.0526 -0.0415 0.0967  335 PRO A N   
2466 C  CA  . PRO A 335 ? 0.5961 0.6378 0.4653 -0.0528 -0.0517 0.0979  335 PRO A CA  
2467 C  C   . PRO A 335 ? 0.5973 0.6380 0.4587 -0.0539 -0.0507 0.0810  335 PRO A C   
2468 O  O   . PRO A 335 ? 0.5551 0.5979 0.3972 -0.0584 -0.0453 0.0714  335 PRO A O   
2469 C  CB  . PRO A 335 ? 0.6210 0.6763 0.4726 -0.0595 -0.0571 0.1106  335 PRO A CB  
2470 C  CG  . PRO A 335 ? 0.5955 0.6488 0.4507 -0.0599 -0.0531 0.1241  335 PRO A CG  
2471 C  CD  . PRO A 335 ? 0.5884 0.6296 0.4557 -0.0556 -0.0428 0.1141  335 PRO A CD  
2472 N  N   . THR A 336 ? 0.5729 0.6100 0.4495 -0.0501 -0.0555 0.0771  336 THR A N   
2473 C  CA  . THR A 336 ? 0.5894 0.6227 0.4619 -0.0513 -0.0540 0.0618  336 THR A CA  
2474 C  C   . THR A 336 ? 0.5085 0.5472 0.3931 -0.0505 -0.0632 0.0634  336 THR A C   
2475 O  O   . THR A 336 ? 0.5263 0.5658 0.4302 -0.0452 -0.0674 0.0722  336 THR A O   
2476 C  CB  . THR A 336 ? 0.6449 0.6646 0.5265 -0.0464 -0.0454 0.0515  336 THR A CB  
2477 O  OG1 . THR A 336 ? 0.6628 0.6799 0.5360 -0.0466 -0.0370 0.0506  336 THR A OG1 
2478 C  CG2 . THR A 336 ? 0.5250 0.5390 0.4013 -0.0482 -0.0440 0.0369  336 THR A CG2 
2479 N  N   . LEU A 337 ? 0.5220 0.5648 0.3961 -0.0558 -0.0660 0.0545  337 LEU A N   
2480 C  CA  . LEU A 337 ? 0.4469 0.4965 0.3330 -0.0560 -0.0736 0.0541  337 LEU A CA  
2481 C  C   . LEU A 337 ? 0.4780 0.5165 0.3740 -0.0535 -0.0686 0.0425  337 LEU A C   
2482 O  O   . LEU A 337 ? 0.5105 0.5404 0.3944 -0.0570 -0.0634 0.0309  337 LEU A O   
2483 C  CB  . LEU A 337 ? 0.4625 0.5242 0.3323 -0.0646 -0.0805 0.0516  337 LEU A CB  
2484 N  N   . LEU A 338 ? 0.4391 0.4777 0.3571 -0.0475 -0.0702 0.0458  338 LEU A N   
2485 C  CA  . LEU A 338 ? 0.3996 0.4307 0.3277 -0.0457 -0.0663 0.0364  338 LEU A CA  
2486 C  C   . LEU A 338 ? 0.4298 0.4724 0.3639 -0.0496 -0.0729 0.0344  338 LEU A C   
2487 O  O   . LEU A 338 ? 0.3920 0.4480 0.3380 -0.0476 -0.0801 0.0426  338 LEU A O   
2488 C  CB  . LEU A 338 ? 0.4179 0.4434 0.3657 -0.0373 -0.0632 0.0399  338 LEU A CB  
2489 C  CG  . LEU A 338 ? 0.4245 0.4423 0.3703 -0.0338 -0.0585 0.0451  338 LEU A CG  
2490 C  CD1 . LEU A 338 ? 0.3872 0.3996 0.3536 -0.0264 -0.0564 0.0477  338 LEU A CD1 
2491 C  CD2 . LEU A 338 ? 0.4554 0.4632 0.3851 -0.0363 -0.0507 0.0367  338 LEU A CD2 
2492 N  N   . VAL A 339 ? 0.4295 0.4673 0.3560 -0.0553 -0.0708 0.0239  339 VAL A N   
2493 C  CA  . VAL A 339 ? 0.4309 0.4799 0.3610 -0.0613 -0.0765 0.0210  339 VAL A CA  
2494 C  C   . VAL A 339 ? 0.4032 0.4478 0.3464 -0.0598 -0.0726 0.0153  339 VAL A C   
2495 O  O   . VAL A 339 ? 0.3926 0.4217 0.3303 -0.0595 -0.0658 0.0088  339 VAL A O   
2496 C  CB  . VAL A 339 ? 0.4074 0.4553 0.3163 -0.0717 -0.0783 0.0137  339 VAL A CB  
2497 C  CG1 . VAL A 339 ? 0.4338 0.4967 0.3475 -0.0790 -0.0856 0.0125  339 VAL A CG1 
2498 C  CG2 . VAL A 339 ? 0.4454 0.4966 0.3378 -0.0732 -0.0803 0.0181  339 VAL A CG2 
2499 N  N   . ASP A 340 ? 0.4096 0.4690 0.3703 -0.0588 -0.0769 0.0181  340 ASP A N   
2500 C  CA  . ASP A 340 ? 0.4415 0.5003 0.4145 -0.0582 -0.0731 0.0130  340 ASP A CA  
2501 C  C   . ASP A 340 ? 0.4510 0.5132 0.4170 -0.0692 -0.0748 0.0064  340 ASP A C   
2502 O  O   . ASP A 340 ? 0.4906 0.5517 0.4409 -0.0770 -0.0781 0.0041  340 ASP A O   
2503 C  CB  . ASP A 340 ? 0.3982 0.4717 0.3955 -0.0506 -0.0754 0.0181  340 ASP A CB  
2504 C  CG  . ASP A 340 ? 0.4329 0.5287 0.4395 -0.0532 -0.0842 0.0227  340 ASP A CG  
2505 O  OD1 . ASP A 340 ? 0.4455 0.5466 0.4390 -0.0619 -0.0890 0.0220  340 ASP A OD1 
2506 O  OD2 . ASP A 340 ? 0.3859 0.4947 0.4139 -0.0460 -0.0863 0.0266  340 ASP A OD2 
2507 N  N   . ALA A 341 ? 0.4318 0.4985 0.4094 -0.0706 -0.0724 0.0032  341 ALA A N   
2508 C  CA  . ALA A 341 ? 0.4147 0.4837 0.3872 -0.0819 -0.0734 -0.0023 341 ALA A CA  
2509 C  C   . ALA A 341 ? 0.4707 0.5630 0.4504 -0.0880 -0.0815 0.0001  341 ALA A C   
2510 O  O   . ALA A 341 ? 0.5352 0.6292 0.5068 -0.0995 -0.0839 -0.0043 341 ALA A O   
2511 C  CB  . ALA A 341 ? 0.3886 0.4559 0.3704 -0.0820 -0.0676 -0.0055 341 ALA A CB  
2512 N  N   . GLU A 342 ? 0.4403 0.5502 0.4358 -0.0805 -0.0861 0.0070  342 GLU A N   
2513 C  CA  . GLU A 342 ? 0.4531 0.5872 0.4572 -0.0847 -0.0949 0.0106  342 GLU A CA  
2514 C  C   . GLU A 342 ? 0.4674 0.6028 0.4561 -0.0879 -0.1020 0.0143  342 GLU A C   
2515 O  O   . GLU A 342 ? 0.4588 0.6154 0.4550 -0.0891 -0.1107 0.0196  342 GLU A O   
2516 C  CB  . GLU A 342 ? 0.4965 0.6497 0.5271 -0.0741 -0.0970 0.0165  342 GLU A CB  
2517 N  N   . LYS A 343 ? 0.4730 0.5874 0.4404 -0.0892 -0.0984 0.0114  343 LYS A N   
2518 C  CA  . LYS A 343 ? 0.5078 0.6224 0.4576 -0.0923 -0.1035 0.0140  343 LYS A CA  
2519 C  C   . LYS A 343 ? 0.5055 0.6322 0.4648 -0.0831 -0.1089 0.0260  343 LYS A C   
2520 O  O   . LYS A 343 ? 0.5268 0.6652 0.4779 -0.0866 -0.1167 0.0312  343 LYS A O   
2521 C  CB  . LYS A 343 ? 0.5018 0.6279 0.4416 -0.1057 -0.1105 0.0096  343 LYS A CB  
2522 N  N   . GLU A 344 ? 0.4827 0.6063 0.4590 -0.0717 -0.1052 0.0308  344 GLU A N   
2523 C  CA  . GLU A 344 ? 0.4958 0.6264 0.4819 -0.0624 -0.1098 0.0427  344 GLU A CA  
2524 C  C   . GLU A 344 ? 0.4788 0.5902 0.4516 -0.0584 -0.1042 0.0451  344 GLU A C   
2525 O  O   . GLU A 344 ? 0.4627 0.5570 0.4335 -0.0560 -0.0954 0.0390  344 GLU A O   
2526 C  CB  . GLU A 344 ? 0.4872 0.6262 0.5020 -0.0523 -0.1096 0.0461  344 GLU A CB  
2527 N  N   . SER A 345 ? 0.4936 0.6094 0.4571 -0.0582 -0.1096 0.0543  345 SER A N   
2528 C  CA  . SER A 345 ? 0.4882 0.5892 0.4382 -0.0558 -0.1045 0.0575  345 SER A CA  
2529 C  C   . SER A 345 ? 0.4748 0.5732 0.4425 -0.0450 -0.1047 0.0684  345 SER A C   
2530 O  O   . SER A 345 ? 0.4760 0.5868 0.4629 -0.0396 -0.1116 0.0764  345 SER A O   
2531 C  CB  . SER A 345 ? 0.4896 0.5967 0.4164 -0.0632 -0.1093 0.0612  345 SER A CB  
2532 O  OG  . SER A 345 ? 0.5090 0.6007 0.4171 -0.0647 -0.1011 0.0570  345 SER A OG  
2533 N  N   . LEU A 346 ? 0.4240 0.5060 0.3861 -0.0419 -0.0970 0.0684  346 LEU A N   
2534 C  CA  . LEU A 346 ? 0.4050 0.4813 0.3817 -0.0331 -0.0965 0.0783  346 LEU A CA  
2535 C  C   . LEU A 346 ? 0.4304 0.4961 0.3900 -0.0350 -0.0915 0.0819  346 LEU A C   
2536 O  O   . LEU A 346 ? 0.4013 0.4558 0.3494 -0.0375 -0.0831 0.0723  346 LEU A O   
2537 C  CB  . LEU A 346 ? 0.4241 0.4916 0.4206 -0.0260 -0.0906 0.0718  346 LEU A CB  
2538 C  CG  . LEU A 346 ? 0.4390 0.4972 0.4508 -0.0175 -0.0890 0.0793  346 LEU A CG  
2539 C  CD1 . LEU A 346 ? 0.4587 0.5267 0.4829 -0.0129 -0.0987 0.0937  346 LEU A CD1 
2540 C  CD2 . LEU A 346 ? 0.4413 0.4935 0.4715 -0.0116 -0.0835 0.0706  346 LEU A CD2 
2541 N  N   . GLN A 347 ? 0.3908 0.4608 0.3489 -0.0340 -0.0968 0.0961  347 GLN A N   
2542 C  CA  . GLN A 347 ? 0.4199 0.4823 0.3627 -0.0365 -0.0919 0.1010  347 GLN A CA  
2543 C  C   . GLN A 347 ? 0.4484 0.4959 0.4059 -0.0299 -0.0852 0.1020  347 GLN A C   
2544 O  O   . GLN A 347 ? 0.4519 0.4973 0.4310 -0.0228 -0.0886 0.1084  347 GLN A O   
2545 C  CB  . GLN A 347 ? 0.3832 0.4563 0.3181 -0.0389 -0.1003 0.1174  347 GLN A CB  
2546 N  N   . ALA A 348 ? 0.4851 0.5227 0.4318 -0.0320 -0.0756 0.0947  348 ALA A N   
2547 C  CA  . ALA A 348 ? 0.4638 0.4884 0.4225 -0.0273 -0.0690 0.0946  348 ALA A CA  
2548 C  C   . ALA A 348 ? 0.5034 0.5257 0.4476 -0.0314 -0.0640 0.1004  348 ALA A C   
2549 O  O   . ALA A 348 ? 0.5446 0.5720 0.4674 -0.0375 -0.0613 0.0966  348 ALA A O   
2550 C  CB  . ALA A 348 ? 0.4542 0.4705 0.4173 -0.0254 -0.0618 0.0793  348 ALA A CB  
2551 N  N   . ASP A 349 ? 0.5168 0.5316 0.4729 -0.0285 -0.0625 0.1092  349 ASP A N   
2552 C  CA  . ASP A 349 ? 0.5244 0.5382 0.4688 -0.0330 -0.0574 0.1162  349 ASP A CA  
2553 C  C   . ASP A 349 ? 0.5061 0.5125 0.4497 -0.0330 -0.0467 0.1051  349 ASP A C   
2554 O  O   . ASP A 349 ? 0.4974 0.5069 0.4265 -0.0378 -0.0406 0.1056  349 ASP A O   
2555 C  CB  . ASP A 349 ? 0.5738 0.5833 0.5312 -0.0314 -0.0618 0.1332  349 ASP A CB  
2556 N  N   . ASN A 350 ? 0.4578 0.4559 0.4165 -0.0278 -0.0443 0.0952  350 ASN A N   
2557 C  CA  . ASN A 350 ? 0.4578 0.4494 0.4183 -0.0270 -0.0354 0.0854  350 ASN A CA  
2558 C  C   . ASN A 350 ? 0.4471 0.4368 0.4060 -0.0249 -0.0334 0.0704  350 ASN A C   
2559 O  O   . ASN A 350 ? 0.4305 0.4210 0.3962 -0.0226 -0.0386 0.0677  350 ASN A O   
2560 C  CB  . ASN A 350 ? 0.4751 0.4576 0.4562 -0.0234 -0.0344 0.0887  350 ASN A CB  
2561 C  CG  . ASN A 350 ? 0.5366 0.5177 0.5256 -0.0239 -0.0398 0.1048  350 ASN A CG  
2562 O  OD1 . ASN A 350 ? 0.5828 0.5692 0.5597 -0.0290 -0.0400 0.1153  350 ASN A OD1 
2563 N  ND2 . ASN A 350 ? 0.5800 0.5538 0.5894 -0.0186 -0.0443 0.1070  350 ASN A ND2 
2564 N  N   . ILE A 351 ? 0.4054 0.3931 0.3558 -0.0258 -0.0260 0.0611  351 ILE A N   
2565 C  CA  . ILE A 351 ? 0.3587 0.3422 0.3078 -0.0239 -0.0238 0.0479  351 ILE A CA  
2566 C  C   . ILE A 351 ? 0.3616 0.3397 0.3154 -0.0215 -0.0164 0.0417  351 ILE A C   
2567 O  O   . ILE A 351 ? 0.3652 0.3457 0.3165 -0.0229 -0.0116 0.0450  351 ILE A O   
2568 C  CB  . ILE A 351 ? 0.4185 0.4056 0.3481 -0.0278 -0.0239 0.0415  351 ILE A CB  
2569 C  CG1 . ILE A 351 ? 0.4439 0.4351 0.3576 -0.0312 -0.0181 0.0415  351 ILE A CG1 
2570 C  CG2 . ILE A 351 ? 0.4425 0.4366 0.3688 -0.0305 -0.0322 0.0468  351 ILE A CG2 
2571 C  CD1 . ILE A 351 ? 0.4374 0.4266 0.3357 -0.0327 -0.0143 0.0289  351 ILE A CD1 
2572 N  N   . LEU A 352 ? 0.3425 0.3150 0.3039 -0.0182 -0.0158 0.0333  352 LEU A N   
2573 C  CA  . LEU A 352 ? 0.3131 0.2816 0.2785 -0.0157 -0.0099 0.0269  352 LEU A CA  
2574 C  C   . LEU A 352 ? 0.3542 0.3227 0.3043 -0.0165 -0.0052 0.0195  352 LEU A C   
2575 O  O   . LEU A 352 ? 0.3483 0.3147 0.2881 -0.0178 -0.0070 0.0143  352 LEU A O   
2576 C  CB  . LEU A 352 ? 0.2907 0.2540 0.2672 -0.0123 -0.0114 0.0209  352 LEU A CB  
2577 C  CG  . LEU A 352 ? 0.3093 0.2720 0.3024 -0.0106 -0.0149 0.0253  352 LEU A CG  
2578 C  CD1 . LEU A 352 ? 0.2945 0.2551 0.2942 -0.0084 -0.0170 0.0188  352 LEU A CD1 
2579 C  CD2 . LEU A 352 ? 0.3135 0.2750 0.3172 -0.0098 -0.0117 0.0280  352 LEU A CD2 
2580 N  N   . VAL A 353 ? 0.3409 0.3118 0.2905 -0.0157 0.0010  0.0187  353 VAL A N   
2581 C  CA  . VAL A 353 ? 0.3188 0.2902 0.2564 -0.0151 0.0065  0.0108  353 VAL A CA  
2582 C  C   . VAL A 353 ? 0.3493 0.3179 0.2967 -0.0101 0.0107  0.0049  353 VAL A C   
2583 O  O   . VAL A 353 ? 0.3060 0.2800 0.2624 -0.0094 0.0143  0.0079  353 VAL A O   
2584 C  CB  . VAL A 353 ? 0.3786 0.3596 0.3057 -0.0188 0.0108  0.0150  353 VAL A CB  
2585 C  CG1 . VAL A 353 ? 0.3714 0.3539 0.2892 -0.0168 0.0181  0.0052  353 VAL A CG1 
2586 C  CG2 . VAL A 353 ? 0.3533 0.3377 0.2680 -0.0238 0.0058  0.0204  353 VAL A CG2 
2587 N  N   . PRO A 354 ? 0.3787 0.3392 0.3250 -0.0070 0.0098  -0.0029 354 PRO A N   
2588 C  CA  . PRO A 354 ? 0.3224 0.2808 0.2778 -0.0019 0.0127  -0.0076 354 PRO A CA  
2589 C  C   . PRO A 354 ? 0.3120 0.2752 0.2632 0.0007  0.0198  -0.0122 354 PRO A C   
2590 O  O   . PRO A 354 ? 0.3449 0.3063 0.2828 0.0003  0.0221  -0.0176 354 PRO A O   
2591 C  CB  . PRO A 354 ? 0.3575 0.3051 0.3101 -0.0002 0.0091  -0.0132 354 PRO A CB  
2592 C  CG  . PRO A 354 ? 0.4183 0.3629 0.3571 -0.0045 0.0067  -0.0144 354 PRO A CG  
2593 C  CD  . PRO A 354 ? 0.3730 0.3263 0.3106 -0.0087 0.0053  -0.0067 354 PRO A CD  
2594 N  N   . LEU A 355 ? 0.2834 0.2539 0.2466 0.0031  0.0234  -0.0108 355 LEU A N   
2595 C  CA  . LEU A 355 ? 0.3137 0.2926 0.2762 0.0058  0.0309  -0.0148 355 LEU A CA  
2596 C  C   . LEU A 355 ? 0.3375 0.3135 0.3075 0.0133  0.0324  -0.0219 355 LEU A C   
2597 O  O   . LEU A 355 ? 0.3268 0.3052 0.2930 0.0174  0.0380  -0.0287 355 LEU A O   
2598 C  CB  . LEU A 355 ? 0.3098 0.3019 0.2815 0.0026  0.0344  -0.0076 355 LEU A CB  
2599 C  CG  . LEU A 355 ? 0.3624 0.3589 0.3266 -0.0047 0.0338  0.0011  355 LEU A CG  
2600 C  CD1 . LEU A 355 ? 0.3692 0.3773 0.3443 -0.0083 0.0375  0.0086  355 LEU A CD1 
2601 C  CD2 . LEU A 355 ? 0.3787 0.3779 0.3244 -0.0064 0.0373  -0.0026 355 LEU A CD2 
2602 N  N   . ALA A 356 ? 0.2960 0.2673 0.2766 0.0153  0.0276  -0.0206 356 ALA A N   
2603 C  CA  . ALA A 356 ? 0.3488 0.3176 0.3366 0.0225  0.0277  -0.0257 356 ALA A CA  
2604 C  C   . ALA A 356 ? 0.2743 0.2350 0.2671 0.0228  0.0207  -0.0238 356 ALA A C   
2605 O  O   . ALA A 356 ? 0.3128 0.2745 0.3090 0.0181  0.0171  -0.0190 356 ALA A O   
2606 C  CB  . ALA A 356 ? 0.3192 0.3026 0.3207 0.0256  0.0326  -0.0256 356 ALA A CB  
2607 N  N   . ALA A 357 ? 0.3149 0.2678 0.3082 0.0283  0.0189  -0.0277 357 ALA A N   
2608 C  CA  . ALA A 357 ? 0.3090 0.2570 0.3074 0.0291  0.0129  -0.0258 357 ALA A CA  
2609 C  C   . ALA A 357 ? 0.3168 0.2718 0.3278 0.0356  0.0131  -0.0265 357 ALA A C   
2610 O  O   . ALA A 357 ? 0.3136 0.2686 0.3258 0.0421  0.0165  -0.0306 357 ALA A O   
2611 C  CB  . ALA A 357 ? 0.2995 0.2317 0.2870 0.0290  0.0092  -0.0277 357 ALA A CB  
2612 N  N   . ILE A 358 ? 0.2565 0.2185 0.2775 0.0342  0.0095  -0.0232 358 ILE A N   
2613 C  CA  . ILE A 358 ? 0.2500 0.2195 0.2829 0.0397  0.0077  -0.0232 358 ILE A CA  
2614 C  C   . ILE A 358 ? 0.2561 0.2166 0.2856 0.0402  0.0009  -0.0215 358 ILE A C   
2615 O  O   . ILE A 358 ? 0.2615 0.2196 0.2873 0.0344  -0.0025 -0.0196 358 ILE A O   
2616 C  CB  . ILE A 358 ? 0.2763 0.2621 0.3229 0.0367  0.0085  -0.0212 358 ILE A CB  
2617 C  CG1 . ILE A 358 ? 0.2815 0.2772 0.3314 0.0361  0.0159  -0.0219 358 ILE A CG1 
2618 C  CG2 . ILE A 358 ? 0.2536 0.2482 0.3123 0.0414  0.0048  -0.0209 358 ILE A CG2 
2619 C  CD1 . ILE A 358 ? 0.2783 0.2883 0.3408 0.0309  0.0170  -0.0191 358 ILE A CD1 
2620 N  N   . ARG A 359 ? 0.2997 0.2550 0.3301 0.0473  -0.0010 -0.0221 359 ARG A N   
2621 C  CA  . ARG A 359 ? 0.3213 0.2668 0.3466 0.0476  -0.0075 -0.0192 359 ARG A CA  
2622 C  C   . ARG A 359 ? 0.3092 0.2624 0.3457 0.0544  -0.0112 -0.0171 359 ARG A C   
2623 O  O   . ARG A 359 ? 0.2791 0.2332 0.3222 0.0627  -0.0091 -0.0190 359 ARG A O   
2624 C  CB  . ARG A 359 ? 0.2934 0.2199 0.3060 0.0486  -0.0074 -0.0206 359 ARG A CB  
2625 C  CG  . ARG A 359 ? 0.3940 0.3099 0.4020 0.0492  -0.0137 -0.0164 359 ARG A CG  
2626 C  CD  . ARG A 359 ? 0.3564 0.2676 0.3542 0.0400  -0.0163 -0.0141 359 ARG A CD  
2627 N  NE  . ARG A 359 ? 0.3809 0.2821 0.3734 0.0401  -0.0220 -0.0093 359 ARG A NE  
2628 C  CZ  . ARG A 359 ? 0.3979 0.3066 0.3947 0.0410  -0.0270 -0.0046 359 ARG A CZ  
2629 N  NH1 . ARG A 359 ? 0.3631 0.2894 0.3696 0.0408  -0.0272 -0.0052 359 ARG A NH1 
2630 N  NH2 . ARG A 359 ? 0.4296 0.3279 0.4207 0.0416  -0.0322 0.0010  359 ARG A NH2 
2631 N  N   . ALA A 360 ? 0.3257 0.2862 0.3652 0.0511  -0.0167 -0.0136 360 ALA A N   
2632 C  CA  . ALA A 360 ? 0.3035 0.2747 0.3538 0.0563  -0.0216 -0.0108 360 ALA A CA  
2633 C  C   . ALA A 360 ? 0.2640 0.2518 0.3300 0.0609  -0.0177 -0.0134 360 ALA A C   
2634 O  O   . ALA A 360 ? 0.3324 0.3274 0.4090 0.0688  -0.0199 -0.0123 360 ALA A O   
2635 C  CB  . ALA A 360 ? 0.3446 0.3029 0.3910 0.0634  -0.0261 -0.0072 360 ALA A CB  
2636 N  N   . GLY A 361 ? 0.2857 0.2805 0.3542 0.0557  -0.0119 -0.0164 361 GLY A N   
2637 C  CA  . GLY A 361 ? 0.2507 0.2624 0.3335 0.0578  -0.0071 -0.0185 361 GLY A CA  
2638 C  C   . GLY A 361 ? 0.3019 0.3117 0.3853 0.0644  0.0000  -0.0221 361 GLY A C   
2639 O  O   . GLY A 361 ? 0.3169 0.3428 0.4126 0.0664  0.0049  -0.0239 361 GLY A O   
2640 N  N   . LYS A 362 ? 0.2595 0.2512 0.3303 0.0673  0.0010  -0.0238 362 LYS A N   
2641 C  CA  . LYS A 362 ? 0.3118 0.3006 0.3817 0.0735  0.0081  -0.0290 362 LYS A CA  
2642 C  C   . LYS A 362 ? 0.3018 0.2830 0.3578 0.0665  0.0133  -0.0314 362 LYS A C   
2643 O  O   . LYS A 362 ? 0.2808 0.2480 0.3239 0.0610  0.0101  -0.0298 362 LYS A O   
2644 C  CB  . LYS A 362 ? 0.3423 0.3150 0.4090 0.0827  0.0052  -0.0303 362 LYS A CB  
2645 N  N   . GLY A 363 ? 0.2989 0.2908 0.3574 0.0663  0.0212  -0.0348 363 GLY A N   
2646 C  CA  . GLY A 363 ? 0.3062 0.2938 0.3516 0.0592  0.0257  -0.0359 363 GLY A CA  
2647 C  C   . GLY A 363 ? 0.3641 0.3377 0.3964 0.0627  0.0292  -0.0422 363 GLY A C   
2648 O  O   . GLY A 363 ? 0.3244 0.2970 0.3609 0.0717  0.0320  -0.0477 363 GLY A O   
2649 N  N   . TYR A 364 ? 0.3422 0.3053 0.3591 0.0555  0.0286  -0.0418 364 TYR A N   
2650 C  CA  . TYR A 364 ? 0.3720 0.3223 0.3744 0.0560  0.0315  -0.0482 364 TYR A CA  
2651 C  C   . TYR A 364 ? 0.3841 0.3387 0.3751 0.0470  0.0344  -0.0468 364 TYR A C   
2652 O  O   . TYR A 364 ? 0.3312 0.2822 0.3176 0.0399  0.0297  -0.0413 364 TYR A O   
2653 C  CB  . TYR A 364 ? 0.4002 0.3291 0.3940 0.0562  0.0251  -0.0484 364 TYR A CB  
2654 C  CG  . TYR A 364 ? 0.3801 0.3035 0.3839 0.0641  0.0204  -0.0469 364 TYR A CG  
2655 C  CD1 . TYR A 364 ? 0.3484 0.2750 0.3588 0.0620  0.0140  -0.0396 364 TYR A CD1 
2656 C  CD2 . TYR A 364 ? 0.4124 0.3276 0.4192 0.0738  0.0223  -0.0529 364 TYR A CD2 
2657 C  CE1 . TYR A 364 ? 0.3930 0.3160 0.4116 0.0687  0.0090  -0.0371 364 TYR A CE1 
2658 C  CE2 . TYR A 364 ? 0.4004 0.3105 0.4171 0.0815  0.0172  -0.0501 364 TYR A CE2 
2659 C  CZ  . TYR A 364 ? 0.3801 0.2946 0.4020 0.0786  0.0103  -0.0416 364 TYR A CZ  
2660 O  OH  . TYR A 364 ? 0.4082 0.3188 0.4386 0.0857  0.0044  -0.0376 364 TYR A OH  
2661 N  N   . LEU A 365 ? 0.3952 0.3588 0.3823 0.0475  0.0421  -0.0516 365 LEU A N   
2662 C  CA  . LEU A 365 ? 0.3576 0.3249 0.3315 0.0391  0.0445  -0.0500 365 LEU A CA  
2663 C  C   . LEU A 365 ? 0.3872 0.3372 0.3447 0.0355  0.0405  -0.0529 365 LEU A C   
2664 O  O   . LEU A 365 ? 0.4064 0.3425 0.3597 0.0403  0.0398  -0.0600 365 LEU A O   
2665 C  CB  . LEU A 365 ? 0.3811 0.3623 0.3520 0.0403  0.0541  -0.0554 365 LEU A CB  
2666 C  CG  . LEU A 365 ? 0.3806 0.3834 0.3660 0.0408  0.0596  -0.0518 365 LEU A CG  
2667 C  CD1 . LEU A 365 ? 0.4435 0.4595 0.4251 0.0434  0.0700  -0.0595 365 LEU A CD1 
2668 C  CD2 . LEU A 365 ? 0.3807 0.3909 0.3669 0.0311  0.0573  -0.0408 365 LEU A CD2 
2669 N  N   . THR A 366 ? 0.3410 0.2917 0.2902 0.0269  0.0373  -0.0471 366 THR A N   
2670 C  CA  . THR A 366 ? 0.3733 0.3126 0.3063 0.0220  0.0344  -0.0501 366 THR A CA  
2671 C  C   . THR A 366 ? 0.4118 0.3570 0.3315 0.0204  0.0409  -0.0566 366 THR A C   
2672 O  O   . THR A 366 ? 0.3880 0.3471 0.3112 0.0226  0.0480  -0.0579 366 THR A O   
2673 C  CB  . THR A 366 ? 0.3635 0.3038 0.2941 0.0142  0.0283  -0.0414 366 THR A CB  
2674 O  OG1 . THR A 366 ? 0.3622 0.3169 0.2919 0.0098  0.0312  -0.0356 366 THR A OG1 
2675 C  CG2 . THR A 366 ? 0.3337 0.2715 0.2777 0.0154  0.0230  -0.0356 366 THR A CG2 
2676 N  N   . GLU A 367 ? 0.3656 0.3017 0.2696 0.0157  0.0386  -0.0609 367 GLU A N   
2677 C  CA  . GLU A 367 ? 0.4437 0.3863 0.3325 0.0127  0.0441  -0.0675 367 GLU A CA  
2678 C  C   . GLU A 367 ? 0.4243 0.3862 0.3118 0.0074  0.0469  -0.0589 367 GLU A C   
2679 O  O   . GLU A 367 ? 0.3950 0.3698 0.2800 0.0085  0.0549  -0.0622 367 GLU A O   
2680 C  CB  . GLU A 367 ? 0.4388 0.3696 0.3110 0.0064  0.0393  -0.0721 367 GLU A CB  
2681 N  N   . GLN A 368 ? 0.4366 0.4007 0.3271 0.0018  0.0405  -0.0474 368 GLN A N   
2682 C  CA  . GLN A 368 ? 0.4273 0.4070 0.3180 -0.0035 0.0419  -0.0371 368 GLN A CA  
2683 C  C   . GLN A 368 ? 0.4400 0.4308 0.3459 0.0004  0.0478  -0.0339 368 GLN A C   
2684 O  O   . GLN A 368 ? 0.4441 0.4496 0.3476 -0.0030 0.0532  -0.0298 368 GLN A O   
2685 C  CB  . GLN A 368 ? 0.4121 0.3891 0.3062 -0.0084 0.0332  -0.0261 368 GLN A CB  
2686 C  CG  . GLN A 368 ? 0.4448 0.4125 0.3271 -0.0123 0.0267  -0.0289 368 GLN A CG  
2687 C  CD  . GLN A 368 ? 0.4816 0.4360 0.3731 -0.0097 0.0209  -0.0301 368 GLN A CD  
2688 O  OE1 . GLN A 368 ? 0.4652 0.4105 0.3610 -0.0042 0.0229  -0.0373 368 GLN A OE1 
2689 N  NE2 . GLN A 368 ? 0.4533 0.4071 0.3483 -0.0134 0.0139  -0.0227 368 GLN A NE2 
2690 N  N   . GLY A 369 ? 0.3629 0.3479 0.2844 0.0067  0.0465  -0.0353 369 GLY A N   
2691 C  CA  . GLY A 369 ? 0.3906 0.3873 0.3277 0.0102  0.0515  -0.0334 369 GLY A CA  
2692 C  C   . GLY A 369 ? 0.4315 0.4387 0.3662 0.0144  0.0612  -0.0421 369 GLY A C   
2693 O  O   . GLY A 369 ? 0.4406 0.4645 0.3820 0.0132  0.0675  -0.0389 369 GLY A O   
2694 N  N   . SER A 370 ? 0.4009 0.3986 0.3268 0.0193  0.0630  -0.0538 370 SER A N   
2695 C  CA  . SER A 370 ? 0.4095 0.4172 0.3321 0.0238  0.0729  -0.0641 370 SER A CA  
2696 C  C   . SER A 370 ? 0.4482 0.4699 0.3546 0.0156  0.0782  -0.0626 370 SER A C   
2697 O  O   . SER A 370 ? 0.4577 0.4978 0.3663 0.0158  0.0872  -0.0639 370 SER A O   
2698 C  CB  . SER A 370 ? 0.4002 0.3913 0.3168 0.0307  0.0730  -0.0776 370 SER A CB  
2699 O  OG  . SER A 370 ? 0.4878 0.4656 0.4182 0.0375  0.0673  -0.0771 370 SER A OG  
2700 N  N   . ALA A 371 ? 0.4460 0.4609 0.3360 0.0081  0.0727  -0.0592 371 ALA A N   
2701 C  CA  . ALA A 371 ? 0.4860 0.5141 0.3584 -0.0003 0.0763  -0.0565 371 ALA A CA  
2702 C  C   . ALA A 371 ? 0.4925 0.5386 0.3727 -0.0055 0.0792  -0.0432 371 ALA A C   
2703 O  O   . ALA A 371 ? 0.5508 0.6146 0.4256 -0.0079 0.0882  -0.0443 371 ALA A O   
2704 C  CB  . ALA A 371 ? 0.4710 0.4893 0.3279 -0.0075 0.0675  -0.0529 371 ALA A CB  
2705 N  N   . GLU A 372 ? 0.4820 0.5235 0.3750 -0.0075 0.0721  -0.0310 372 GLU A N   
2706 C  CA  . GLU A 372 ? 0.4959 0.5512 0.3977 -0.0130 0.0740  -0.0179 372 GLU A CA  
2707 C  C   . GLU A 372 ? 0.5094 0.5782 0.4272 -0.0086 0.0825  -0.0210 372 GLU A C   
2708 O  O   . GLU A 372 ? 0.4602 0.5437 0.3834 -0.0144 0.0864  -0.0117 372 GLU A O   
2709 C  CB  . GLU A 372 ? 0.5009 0.5457 0.4138 -0.0154 0.0640  -0.0062 372 GLU A CB  
2710 C  CG  . GLU A 372 ? 0.4536 0.4903 0.3525 -0.0209 0.0559  -0.0003 372 GLU A CG  
2711 C  CD  . GLU A 372 ? 0.5275 0.5554 0.4385 -0.0227 0.0469  0.0109  372 GLU A CD  
2712 O  OE1 . GLU A 372 ? 0.4939 0.5249 0.4209 -0.0232 0.0474  0.0177  372 GLU A OE1 
2713 O  OE2 . GLU A 372 ? 0.4993 0.5179 0.4041 -0.0238 0.0392  0.0122  372 GLU A OE2 
2714 N  N   . HIS A 373 ? 0.4869 0.5516 0.4129 0.0011  0.0851  -0.0333 373 HIS A N   
2715 C  CA  . HIS A 373 ? 0.4846 0.5624 0.4289 0.0069  0.0919  -0.0368 373 HIS A CA  
2716 C  C   . HIS A 373 ? 0.5322 0.6107 0.4962 0.0050  0.0868  -0.0261 373 HIS A C   
2717 O  O   . HIS A 373 ? 0.5812 0.6466 0.5554 0.0101  0.0798  -0.0271 373 HIS A O   
2718 C  CB  . HIS A 373 ? 0.5059 0.6072 0.4452 0.0035  0.1037  -0.0384 373 HIS A CB  
2719 N  N   . ALA A 374 ? 0.5307 0.6243 0.4994 -0.0029 0.0902  -0.0159 374 ALA A N   
2720 C  CA  . ALA A 374 ? 0.5133 0.6078 0.4998 -0.0067 0.0858  -0.0057 374 ALA A CA  
2721 C  C   . ALA A 374 ? 0.5087 0.6084 0.5165 0.0009  0.0865  -0.0115 374 ALA A C   
2722 O  O   . ALA A 374 ? 0.4913 0.6080 0.5136 -0.0018 0.0912  -0.0081 374 ALA A O   
2723 C  CB  . ALA A 374 ? 0.5099 0.5848 0.4940 -0.0096 0.0746  0.0014  374 ALA A CB  
2724 N  N   . PHE A 375 ? 0.5096 0.5954 0.5196 0.0099  0.0815  -0.0194 375 PHE A N   
2725 C  CA  . PHE A 375 ? 0.4877 0.5779 0.5172 0.0176  0.0806  -0.0238 375 PHE A CA  
2726 C  C   . PHE A 375 ? 0.4913 0.5700 0.5173 0.0287  0.0795  -0.0349 375 PHE A C   
2727 O  O   . PHE A 375 ? 0.4629 0.5264 0.4722 0.0293  0.0773  -0.0385 375 PHE A O   
2728 C  CB  . PHE A 375 ? 0.4565 0.5392 0.4982 0.0144  0.0716  -0.0165 375 PHE A CB  
2729 C  CG  . PHE A 375 ? 0.4602 0.5216 0.4908 0.0124  0.0629  -0.0137 375 PHE A CG  
2730 C  CD1 . PHE A 375 ? 0.4252 0.4717 0.4539 0.0194  0.0571  -0.0193 375 PHE A CD1 
2731 C  CD2 . PHE A 375 ? 0.4682 0.5252 0.4910 0.0035  0.0605  -0.0048 375 PHE A CD2 
2732 C  CE1 . PHE A 375 ? 0.3705 0.3998 0.3898 0.0170  0.0497  -0.0168 375 PHE A CE1 
2733 C  CE2 . PHE A 375 ? 0.4369 0.4766 0.4515 0.0023  0.0528  -0.0026 375 PHE A CE2 
2734 C  CZ  . PHE A 375 ? 0.3971 0.4240 0.4101 0.0088  0.0477  -0.0090 375 PHE A CZ  
2735 N  N   . ASP A 376 ? 0.4936 0.5799 0.5362 0.0374  0.0806  -0.0400 376 ASP A N   
2736 C  CA  . ASP A 376 ? 0.4916 0.5666 0.5343 0.0489  0.0791  -0.0496 376 ASP A CA  
2737 C  C   . ASP A 376 ? 0.5018 0.5785 0.5641 0.0552  0.0731  -0.0482 376 ASP A C   
2738 O  O   . ASP A 376 ? 0.4848 0.5773 0.5624 0.0518  0.0730  -0.0428 376 ASP A O   
2739 C  CB  . ASP A 376 ? 0.4740 0.5600 0.5152 0.0559  0.0896  -0.0603 376 ASP A CB  
2740 N  N   . PHE A 377 ? 0.5249 0.5854 0.5863 0.0638  0.0679  -0.0528 377 PHE A N   
2741 C  CA  . PHE A 377 ? 0.4845 0.5444 0.5615 0.0698  0.0607  -0.0506 377 PHE A CA  
2742 C  C   . PHE A 377 ? 0.5222 0.5909 0.6132 0.0829  0.0642  -0.0579 377 PHE A C   
2743 O  O   . PHE A 377 ? 0.5286 0.6183 0.6292 0.0851  0.0728  -0.0615 377 PHE A O   
2744 C  CB  . PHE A 377 ? 0.4363 0.4719 0.5030 0.0695  0.0511  -0.0484 377 PHE A CB  
2745 C  CG  . PHE A 377 ? 0.4023 0.4320 0.4608 0.0582  0.0464  -0.0410 377 PHE A CG  
2746 C  CD1 . PHE A 377 ? 0.3830 0.4224 0.4533 0.0531  0.0425  -0.0347 377 PHE A CD1 
2747 C  CD2 . PHE A 377 ? 0.4047 0.4204 0.4448 0.0527  0.0462  -0.0410 377 PHE A CD2 
2748 C  CE1 . PHE A 377 ? 0.3172 0.3504 0.3813 0.0437  0.0385  -0.0289 377 PHE A CE1 
2749 C  CE2 . PHE A 377 ? 0.3544 0.3657 0.3891 0.0434  0.0419  -0.0343 377 PHE A CE2 
2750 C  CZ  . PHE A 377 ? 0.3390 0.3584 0.3860 0.0394  0.0383  -0.0285 377 PHE A CZ  
2751 C  C1  . EDO B .   ? 0.4399 0.4032 0.6319 0.0478  -0.0649 0.0524  401 EDO A C1  
2752 O  O1  . EDO B .   ? 0.4592 0.4333 0.6642 0.0544  -0.0718 0.0585  401 EDO A O1  
2753 C  C2  . EDO B .   ? 0.4362 0.3850 0.6215 0.0437  -0.0668 0.0661  401 EDO A C2  
2754 O  O2  . EDO B .   ? 0.4652 0.4093 0.6339 0.0359  -0.0601 0.0611  401 EDO A O2  
2755 C  C1  . EDO C .   ? 0.4144 0.8259 0.6704 -0.0382 0.0224  -0.0906 402 EDO A C1  
2756 O  O1  . EDO C .   ? 0.4048 0.7837 0.6300 -0.0475 0.0195  -0.0828 402 EDO A O1  
2757 C  C2  . EDO C .   ? 0.3349 0.7489 0.5986 -0.0266 0.0310  -0.1036 402 EDO A C2  
2758 O  O2  . EDO C .   ? 0.2675 0.6540 0.5318 -0.0139 0.0265  -0.1043 402 EDO A O2  
2759 C  C1  . EDO D .   ? 0.5141 0.4796 0.5277 -0.0344 -0.0172 0.1120  403 EDO A C1  
2760 O  O1  . EDO D .   ? 0.5657 0.5332 0.5769 -0.0300 -0.0145 0.0960  403 EDO A O1  
2761 C  C2  . EDO D .   ? 0.6011 0.5734 0.5991 -0.0361 -0.0221 0.1210  403 EDO A C2  
2762 O  O2  . EDO D .   ? 0.5450 0.5287 0.5229 -0.0385 -0.0169 0.1138  403 EDO A O2  
2763 C  C1  . EDO E .   ? 0.4883 0.4633 0.4869 0.0694  0.0587  -0.0733 404 EDO A C1  
2764 O  O1  . EDO E .   ? 0.5031 0.4607 0.4996 0.0673  0.0489  -0.0677 404 EDO A O1  
2765 C  C2  . EDO E .   ? 0.4935 0.4909 0.5102 0.0699  0.0606  -0.0673 404 EDO A C2  
2766 O  O2  . EDO E .   ? 0.5253 0.5397 0.5498 0.0762  0.0703  -0.0745 404 EDO A O2  
2767 ZN ZN  . ZN  F .   ? 0.3685 0.3051 0.2971 -0.0936 -0.0313 -0.0121 405 ZN  A ZN  
2768 ZN ZN  . ZN  G .   ? 0.3831 0.3790 0.3359 -0.1107 -0.0308 -0.0114 406 ZN  A ZN  
2769 O  O   . HOH H .   ? 0.4832 0.5247 0.4377 -0.0239 0.0526  0.0246  501 HOH A O   
2770 O  O   . HOH H .   ? 0.4024 0.5250 0.5105 0.0022  -0.1042 0.0670  502 HOH A O   
2771 O  O   . HOH H .   ? 0.4184 0.3846 0.4076 0.0158  -0.0467 0.0054  503 HOH A O   
2772 O  O   . HOH H .   ? 0.2325 0.4657 0.4769 -0.0001 0.0464  -0.0115 504 HOH A O   
2773 O  O   . HOH H .   ? 0.4104 0.1876 0.2859 -0.0842 -0.0364 -0.0132 505 HOH A O   
2774 O  O   . HOH H .   ? 0.2678 0.2275 0.2571 -0.0182 -0.0177 -0.0194 506 HOH A O   
2775 O  O   . HOH H .   ? 0.4089 0.3278 0.2815 -0.1217 -0.0553 -0.0458 507 HOH A O   
2776 O  O   . HOH H .   ? 0.4740 0.4978 0.5382 -0.0062 -0.0058 -0.0765 508 HOH A O   
2777 O  O   . HOH H .   ? 0.3671 0.4852 0.4747 -0.0039 0.0140  -0.1030 509 HOH A O   
2778 O  O   . HOH H .   ? 0.4671 0.5769 0.6460 0.1080  -0.0541 0.0050  510 HOH A O   
2779 O  O   . HOH H .   ? 0.4148 0.3919 0.2884 -0.0571 -0.0535 0.0500  511 HOH A O   
2780 O  O   . HOH H .   ? 0.2958 0.3493 0.4746 -0.0611 0.0233  0.0238  512 HOH A O   
2781 O  O   . HOH H .   ? 0.3946 0.3705 0.4599 -0.0025 -0.0146 -0.0345 513 HOH A O   
2782 O  O   . HOH H .   ? 0.3080 0.4467 0.6316 0.0909  -0.0208 -0.0840 514 HOH A O   
2783 O  O   . HOH H .   ? 0.3528 0.4943 0.4733 0.0016  0.0271  -0.1412 515 HOH A O   
2784 O  O   . HOH H .   ? 0.4287 0.8016 0.4968 -0.0907 0.0791  -0.1259 516 HOH A O   
2785 O  O   . HOH H .   ? 0.4138 0.3783 0.4840 -0.0010 -0.0131 -0.0280 517 HOH A O   
2786 O  O   . HOH H .   ? 0.2717 0.2694 0.3537 0.0040  -0.0133 -0.0472 518 HOH A O   
2787 O  O   . HOH H .   ? 0.3877 0.3914 0.3422 -0.1005 -0.0452 -0.0179 519 HOH A O   
2788 O  O   . HOH H .   ? 0.4943 0.4150 0.4624 0.0594  0.0410  -0.0709 520 HOH A O   
2789 O  O   . HOH H .   ? 0.2709 0.3306 0.3967 0.0700  -0.0205 -0.0136 521 HOH A O   
2790 O  O   . HOH H .   ? 0.3044 0.2438 0.3001 0.0124  -0.0188 -0.0143 522 HOH A O   
2791 O  O   . HOH H .   ? 0.1634 0.5258 0.3927 -0.0598 -0.0410 -0.0330 523 HOH A O   
2792 O  O   . HOH H .   ? 0.4963 0.3432 0.3298 -0.1708 -0.0390 0.0923  524 HOH A O   
2793 O  O   . HOH H .   ? 0.5751 0.3148 0.5089 0.0420  -0.0922 0.0967  525 HOH A O   
2794 O  O   . HOH H .   ? 0.4040 0.3210 0.3617 0.0342  0.0232  -0.0472 526 HOH A O   
2795 O  O   . HOH H .   ? 0.2772 0.3365 0.3113 -0.0438 -0.0385 -0.0127 527 HOH A O   
2796 O  O   . HOH H .   ? 0.3611 0.2578 0.2916 -0.0204 -0.0163 -0.0236 528 HOH A O   
2797 O  O   . HOH H .   ? 0.6992 0.6506 0.4786 -0.0949 -0.0967 0.1597  529 HOH A O   
2798 O  O   . HOH H .   ? 0.3998 0.3963 0.3219 -0.0504 -0.0265 -0.0002 530 HOH A O   
2799 O  O   . HOH H .   ? 0.5345 0.2805 0.3947 -0.0125 -0.0060 -0.0876 531 HOH A O   
2800 O  O   . HOH H .   ? 0.5515 0.4358 0.5283 0.0395  -0.0506 0.0237  532 HOH A O   
2801 O  O   . HOH H .   ? 0.3817 0.3241 0.2855 -0.0209 -0.0056 -0.0164 533 HOH A O   
2802 O  O   . HOH H .   ? 0.4329 0.4122 0.3439 -0.1657 -0.0200 0.0226  534 HOH A O   
2803 O  O   . HOH H .   ? 0.2436 0.5432 0.4526 -0.0267 -0.0987 0.0159  535 HOH A O   
2804 O  O   . HOH H .   ? 0.4171 0.4139 0.4989 0.0004  -0.0103 -0.0669 536 HOH A O   
2805 O  O   . HOH H .   ? 0.4093 0.4176 0.3803 -0.0509 0.0147  0.1038  537 HOH A O   
2806 O  O   . HOH H .   ? 0.3103 0.2736 0.3941 -0.0078 -0.0052 -0.0039 538 HOH A O   
2807 O  O   . HOH H .   ? 0.2719 0.4654 0.3247 -0.1346 -0.0167 -0.0212 539 HOH A O   
2808 O  O   . HOH H .   ? 0.3930 0.2249 0.2755 -0.0896 -0.0366 0.0289  540 HOH A O   
2809 O  O   . HOH H .   ? 0.5833 0.2534 0.4573 -0.0288 -0.0859 0.1167  541 HOH A O   
2810 O  O   . HOH H .   ? 0.4210 0.2763 0.3018 -0.0076 0.0031  -0.0628 542 HOH A O   
2811 O  O   . HOH H .   ? 0.6902 0.4845 0.5324 -0.1240 -0.0449 -0.0654 543 HOH A O   
2812 O  O   . HOH H .   ? 0.6138 0.5245 0.4175 -0.0803 -0.0935 0.1504  544 HOH A O   
2813 O  O   . HOH H .   ? 0.2520 0.2270 0.2860 0.0102  -0.0171 -0.0214 545 HOH A O   
2814 O  O   . HOH H .   ? 0.3374 0.4880 0.4337 -0.0761 0.0888  0.0700  546 HOH A O   
2815 O  O   . HOH H .   ? 0.1945 0.1745 0.2942 0.0106  -0.0180 -0.0345 547 HOH A O   
2816 O  O   . HOH H .   ? 0.2562 0.2554 0.3692 0.0150  -0.0196 -0.0370 548 HOH A O   
2817 O  O   . HOH H .   ? 0.4703 0.3729 0.3700 0.0133  0.0257  -0.0632 549 HOH A O   
2818 O  O   . HOH H .   ? 0.5813 0.3565 0.3854 -0.1535 -0.0652 0.1498  550 HOH A O   
2819 O  O   . HOH H .   ? 0.3710 0.2980 0.3122 -0.0097 -0.0073 -0.0173 551 HOH A O   
2820 O  O   . HOH H .   ? 0.5316 0.2683 0.3826 -0.0395 -0.0180 -0.0781 552 HOH A O   
2821 O  O   . HOH H .   ? 0.4453 0.6989 0.4006 -0.1133 0.0483  -0.0730 553 HOH A O   
2822 O  O   . HOH H .   ? 0.4565 0.6530 0.3538 -0.1376 0.0298  -0.0233 554 HOH A O   
2823 O  O   . HOH H .   ? 0.3357 0.2430 0.2649 -0.0163 -0.0125 -0.0241 555 HOH A O   
2824 O  O   . HOH H .   ? 0.2657 0.4965 0.6018 0.0792  -0.0190 -0.0825 556 HOH A O   
2825 O  O   . HOH H .   ? 0.3039 0.3960 0.3171 -0.1024 -0.0406 -0.0161 557 HOH A O   
2826 O  O   . HOH H .   ? 0.5622 0.2995 0.4215 -0.1294 -0.0450 0.0118  558 HOH A O   
2827 O  O   . HOH H .   ? 0.3599 0.3775 0.3509 -0.0207 -0.0236 -0.0439 559 HOH A O   
2828 O  O   . HOH H .   ? 0.5346 0.3151 0.3986 -0.1423 -0.0447 -0.0170 560 HOH A O   
2829 O  O   . HOH H .   ? 0.2962 0.2850 0.2845 -0.0270 -0.0146 -0.0278 561 HOH A O   
2830 O  O   . HOH H .   ? 0.3882 0.3716 0.3952 -0.0271 0.0097  0.0588  562 HOH A O   
2831 O  O   . HOH H .   ? 0.2779 0.2358 0.2898 0.0076  -0.0173 -0.0191 563 HOH A O   
2832 O  O   . HOH H .   ? 0.2032 0.3698 0.3263 -0.0338 -0.0376 -0.0234 564 HOH A O   
2833 O  O   . HOH H .   ? 0.3266 0.3610 0.5260 -0.0595 -0.0202 -0.0482 565 HOH A O   
2834 O  O   . HOH H .   ? 0.3713 0.3334 0.2796 -0.0223 -0.0048 -0.0003 566 HOH A O   
2835 O  O   . HOH H .   ? 0.2792 0.4820 0.3933 -0.0457 -0.0913 0.0170  567 HOH A O   
2836 O  O   . HOH H .   ? 0.3012 0.4596 0.4115 -0.0029 0.0857  -0.0021 568 HOH A O   
2837 O  O   . HOH H .   ? 0.4439 0.3909 0.3619 -0.1022 -0.0447 -0.0248 569 HOH A O   
2838 O  O   . HOH H .   ? 0.3099 0.4333 0.3484 -0.0777 -0.0646 -0.0054 570 HOH A O   
2839 O  O   . HOH H .   ? 0.4099 0.3280 0.4421 0.0761  -0.0101 -0.0217 571 HOH A O   
2840 O  O   . HOH H .   ? 0.3619 0.3053 0.5406 -0.0683 0.0029  0.0487  572 HOH A O   
2841 O  O   . HOH H .   ? 0.3237 0.3518 0.3577 0.0133  -0.0503 -0.0135 573 HOH A O   
2842 O  O   . HOH H .   ? 0.3008 0.6216 0.4469 -0.0444 0.0516  -0.1193 574 HOH A O   
2843 O  O   . HOH H .   ? 0.4426 0.5249 0.4995 0.0021  -0.0646 -0.0257 575 HOH A O   
2844 O  O   . HOH H .   ? 0.2699 0.2598 0.3077 0.0064  -0.0240 -0.0259 576 HOH A O   
2845 O  O   . HOH H .   ? 0.3790 0.3382 0.3414 -0.0071 -0.0376 0.0000  577 HOH A O   
2846 O  O   . HOH H .   ? 0.3339 0.3652 0.4275 0.0788  0.0284  -0.0382 578 HOH A O   
2847 O  O   . HOH H .   ? 0.5241 0.3936 0.3854 -0.0249 -0.0028 -0.0628 579 HOH A O   
2848 O  O   . HOH H .   ? 0.3911 0.4635 0.4562 -0.0154 -0.0513 -0.0535 580 HOH A O   
2849 O  O   . HOH H .   ? 0.3424 0.4931 0.4188 -0.0334 -0.0974 0.0361  581 HOH A O   
2850 O  O   . HOH H .   ? 0.2278 0.3935 0.4321 0.0322  -0.0990 0.0467  582 HOH A O   
2851 O  O   . HOH H .   ? 0.3566 0.3255 0.4259 -0.0018 -0.0103 -0.0215 583 HOH A O   
2852 O  O   . HOH H .   ? 0.2653 0.5057 0.5317 0.0079  -0.0185 -0.0233 584 HOH A O   
2853 O  O   . HOH H .   ? 0.6253 0.4631 0.5871 0.0443  -0.0669 0.0495  585 HOH A O   
2854 O  O   . HOH H .   ? 0.3811 0.3339 0.3977 0.0396  -0.0379 0.0012  586 HOH A O   
2855 O  O   . HOH H .   ? 0.5119 0.3190 0.5027 0.0770  -0.0362 0.0004  587 HOH A O   
2856 O  O   . HOH H .   ? 0.4074 0.2589 0.3854 0.0484  -0.0327 0.0012  588 HOH A O   
2857 O  O   . HOH H .   ? 0.4041 0.2897 0.4133 0.0673  -0.0199 -0.0136 589 HOH A O   
2858 O  O   . HOH H .   ? 0.2414 0.3291 0.4402 -0.0844 0.0385  0.0433  590 HOH A O   
2859 O  O   . HOH H .   ? 0.3964 0.3817 0.4408 0.0482  -0.0419 0.0007  591 HOH A O   
2860 O  O   . HOH H .   ? 0.2341 0.3357 0.3536 0.0090  -0.0514 -0.0285 592 HOH A O   
2861 O  O   . HOH H .   ? 0.1713 0.5263 0.4665 0.0065  -0.0857 -0.0002 593 HOH A O   
2862 O  O   . HOH H .   ? 0.5016 0.2957 0.3357 -0.0258 0.0000  -0.1005 594 HOH A O   
2863 O  O   . HOH H .   ? 0.3338 0.2586 0.4478 0.0040  -0.0336 0.0527  595 HOH A O   
2864 O  O   . HOH H .   ? 0.3009 0.3457 0.5278 -0.0765 -0.0143 -0.0354 596 HOH A O   
2865 O  O   . HOH H .   ? 0.2806 0.2511 0.4396 0.0271  -0.0196 -0.0494 597 HOH A O   
2866 O  O   . HOH H .   ? 0.4858 0.1909 0.3426 -0.0477 -0.0256 -0.0652 598 HOH A O   
2867 O  O   . HOH H .   ? 0.3181 0.2721 0.4972 0.0389  -0.0442 0.0138  599 HOH A O   
2868 O  O   . HOH H .   ? 0.5259 0.1439 0.4107 -0.0280 -0.0328 -0.0446 600 HOH A O   
2869 O  O   . HOH H .   ? 0.4046 0.4078 0.3049 -0.0586 -0.0555 0.0034  601 HOH A O   
2870 O  O   . HOH H .   ? 0.3660 0.4837 0.3728 -0.1535 -0.0416 -0.0144 602 HOH A O   
2871 O  O   . HOH H .   ? 0.4961 0.4538 0.4254 -0.1258 -0.0372 -0.0125 603 HOH A O   
2872 O  O   . HOH H .   ? 0.4586 0.5068 0.4497 -0.0237 0.0543  0.0286  604 HOH A O   
2873 O  O   . HOH H .   ? 0.3478 0.3259 0.3227 -0.0014 -0.0428 -0.0023 605 HOH A O   
2874 O  O   . HOH H .   ? 0.4465 0.4293 0.5618 -0.0154 -0.0124 -0.0320 606 HOH A O   
2875 O  O   . HOH H .   ? 0.5622 0.3454 0.3855 -0.0947 -0.0344 -0.0863 607 HOH A O   
2876 O  O   . HOH H .   ? 0.2322 0.3101 0.3330 -0.0022 -0.0022 -0.0694 608 HOH A O   
2877 O  O   . HOH H .   ? 0.3690 0.5109 0.5688 0.0979  0.0114  -0.0288 609 HOH A O   
2878 O  O   . HOH H .   ? 0.3107 0.4239 0.4268 -0.0700 0.0689  0.0636  610 HOH A O   
2879 O  O   . HOH H .   ? 0.3716 0.4879 0.3692 -0.1806 -0.0418 -0.0117 611 HOH A O   
2880 O  O   . HOH H .   ? 0.3517 0.5502 0.5772 -0.0673 0.0638  0.0273  612 HOH A O   
2881 O  O   . HOH H .   ? 0.5151 0.4626 0.5847 0.1085  0.0126  -0.0443 613 HOH A O   
2882 O  O   . HOH H .   ? 0.3809 0.2225 0.2703 -0.0202 -0.0743 0.0855  614 HOH A O   
2883 O  O   . HOH H .   ? 0.3746 0.3187 0.4971 -0.0128 -0.0116 -0.0113 615 HOH A O   
2884 O  O   . HOH H .   ? 0.3162 0.5348 0.4181 -0.0694 -0.0920 0.0097  616 HOH A O   
2885 O  O   . HOH H .   ? 0.4133 0.4987 0.5658 0.0904  0.0119  -0.0291 617 HOH A O   
2886 O  O   . HOH H .   ? 0.5067 0.4344 0.3604 -0.1156 -0.0575 -0.0522 618 HOH A O   
2887 O  O   . HOH H .   ? 0.2122 0.6136 0.5447 0.0245  0.0124  -0.1032 619 HOH A O   
2888 O  O   . HOH H .   ? 0.2670 0.4083 0.5062 0.0552  -0.0952 0.0462  620 HOH A O   
2889 O  O   . HOH H .   ? 0.4303 0.7599 0.4671 -0.0901 0.0702  -0.1187 621 HOH A O   
2890 O  O   . HOH H .   ? 0.5232 0.4075 0.4644 0.0423  0.0258  -0.0653 622 HOH A O   
2891 O  O   . HOH H .   ? 0.4953 0.3858 0.4133 0.0342  0.0333  -0.0755 623 HOH A O   
2892 O  O   . HOH H .   ? 0.3575 0.3240 0.2957 -0.0212 -0.0417 0.0094  624 HOH A O   
2893 O  O   . HOH H .   ? 0.4454 0.4297 0.4795 -0.0310 0.0140  0.0604  625 HOH A O   
2894 O  O   . HOH H .   ? 0.4854 0.5636 0.5046 -0.0035 -0.0711 -0.0185 626 HOH A O   
2895 O  O   . HOH H .   ? 0.5364 0.5150 0.4722 -0.1306 -0.0433 -0.0173 627 HOH A O   
2896 O  O   . HOH H .   ? 0.6456 0.2371 0.5136 -0.0667 -0.0737 0.0988  628 HOH A O   
2897 O  O   . HOH H .   ? 0.3351 0.3492 0.4419 0.0100  -0.0098 -0.0637 629 HOH A O   
2898 O  O   . HOH H .   ? 0.5568 0.5752 0.6620 0.0070  -0.0050 -0.0842 630 HOH A O   
2899 O  O   . HOH H .   ? 0.3188 0.4075 0.4894 0.0271  -0.0031 -0.0850 631 HOH A O   
2900 O  O   . HOH H .   ? 0.3982 0.6872 0.3298 -0.1448 0.0573  -0.0560 632 HOH A O   
2901 O  O   . HOH H .   ? 0.2881 0.5071 0.5109 0.0271  -0.1119 0.0504  633 HOH A O   
2902 O  O   . HOH H .   ? 0.4251 0.8962 0.6957 -0.0400 0.0472  -0.1112 634 HOH A O   
2903 O  O   . HOH H .   ? 0.5028 0.4088 0.6930 -0.0681 -0.0052 0.0584  635 HOH A O   
2904 O  O   . HOH H .   ? 0.6669 0.5841 0.7577 -0.0249 -0.0296 0.1149  636 HOH A O   
2905 O  O   . HOH H .   ? 0.6259 0.3081 0.6041 0.0857  -0.0640 0.0399  637 HOH A O   
2906 O  O   . HOH H .   ? 0.4488 0.7040 0.7087 -0.0759 0.0750  0.0273  638 HOH A O   
2907 O  O   . HOH H .   ? 0.6080 0.7871 0.4815 0.0000  0.0283  0.0000  639 HOH A O   
# 
