data_8YOQ
# 
_entry.id   8YOQ 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.399 
_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   8YOQ         pdb_00008yoq 10.2210/pdb8yoq/pdb 
WWPDB D_1300046043 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-01-08 
# 
_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                        8YOQ 
_pdbx_database_status.recvd_initial_deposition_date   2024-03-13 
_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              wfeng@bit.edu.cn 
_pdbx_contact_author.name_first         Feng 
_pdbx_contact_author.name_last          Wang 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-9403-4337 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Lan, H.Y.'   1 ? 
'Gao, Y.'     2 ? 
'Hong, T.'    3 ? 
'Zhao, Z.Z.'  4 ? 
'Chang, Z.H.' 5 ? 
'Wang, Y.F.'  6 ? 
'Wang, F.'    7 ? 
# 
_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                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Cell Discov' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2056-5968 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            10 
_citation.language                  ? 
_citation.page_first                88 
_citation.page_last                 88 
_citation.title                     'Structural insight into 6-OH-FAD-dependent activation of hFSP1 for ferroptosis suppression.' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s41421-024-00723-7 
_citation.pdbx_database_id_PubMed   39160155 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Lan, H.'   1 0009-0009-6083-0704 
primary 'Gao, Y.'   2 ?                   
primary 'Hong, T.'  3 ?                   
primary 'Chang, Z.' 4 ?                   
primary 'Zhao, Z.'  5 ?                   
primary 'Wang, Y.'  6 ?                   
primary 'Wang, F.'  7 ?                   
# 
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 'Ferroptosis suppressor protein 1'                          40035.066 1   1.6.5.- ? ? ? 
2 non-polymer syn '6-HYDROXY-FLAVIN-ADENINE DINUCLEOTIDE'                     801.549   1   ?       ? ? ? 
3 non-polymer syn 'NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE' 745.421   1   ?       ? ? ? 
4 non-polymer syn 'SULFATE ION'                                               96.063    1   ?       ? ? ? 
5 water       nat water                                                       18.015    310 ?       ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        
'FSP1,Apoptosis-inducing factor homologous mitochondrion-associated inducer of death,AMID,p53-responsive gene 3 protein' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;PHMGALHVVIVGGGFGGIAAASQLQALNVPFMLVDMKDSFHHNVAALRASVETGFAKKTFISYSVTFKDNFRQGLVVGID
LKNQMVLLQGGEALPFSHLILATGSTGPFPGKFNEVSSQQAAIQAYEDMVRQVQRSRFIVVVGGGSAGVEMAAEIKTEYP
EKEVTLIHSQVALADKELLPSVRQEVKEILLRKGVQLLLSERVSNLEELPLNEYREYIKVQTDKGTEVATNLVILCTGIK
INSSAYRKAFESRLASSGALRVNEHLQVEGHSNVYAIGDCADVRTPKMAYLAGLHANIAVANIVNSVKQRPLQAYKPGAL
TFLLSMGRNDGVGQISGFYVGRLMVRLTKSRDLFVSTSWKTMRQSPP
;
_entity_poly.pdbx_seq_one_letter_code_can   
;PHMGALHVVIVGGGFGGIAAASQLQALNVPFMLVDMKDSFHHNVAALRASVETGFAKKTFISYSVTFKDNFRQGLVVGID
LKNQMVLLQGGEALPFSHLILATGSTGPFPGKFNEVSSQQAAIQAYEDMVRQVQRSRFIVVVGGGSAGVEMAAEIKTEYP
EKEVTLIHSQVALADKELLPSVRQEVKEILLRKGVQLLLSERVSNLEELPLNEYREYIKVQTDKGTEVATNLVILCTGIK
INSSAYRKAFESRLASSGALRVNEHLQVEGHSNVYAIGDCADVRTPKMAYLAGLHANIAVANIVNSVKQRPLQAYKPGAL
TFLLSMGRNDGVGQISGFYVGRLMVRLTKSRDLFVSTSWKTMRQSPP
;
_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 '6-HYDROXY-FLAVIN-ADENINE DINUCLEOTIDE'                     6FA 
3 'NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE' NDP 
4 'SULFATE ION'                                               SO4 
5 water                                                       HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   PRO n 
1 2   HIS n 
1 3   MET n 
1 4   GLY n 
1 5   ALA n 
1 6   LEU n 
1 7   HIS n 
1 8   VAL n 
1 9   VAL n 
1 10  ILE n 
1 11  VAL n 
1 12  GLY n 
1 13  GLY n 
1 14  GLY n 
1 15  PHE n 
1 16  GLY n 
1 17  GLY n 
1 18  ILE n 
1 19  ALA n 
1 20  ALA n 
1 21  ALA n 
1 22  SER n 
1 23  GLN n 
1 24  LEU n 
1 25  GLN n 
1 26  ALA n 
1 27  LEU n 
1 28  ASN n 
1 29  VAL n 
1 30  PRO n 
1 31  PHE n 
1 32  MET n 
1 33  LEU n 
1 34  VAL n 
1 35  ASP n 
1 36  MET n 
1 37  LYS n 
1 38  ASP n 
1 39  SER n 
1 40  PHE n 
1 41  HIS n 
1 42  HIS n 
1 43  ASN n 
1 44  VAL n 
1 45  ALA n 
1 46  ALA n 
1 47  LEU n 
1 48  ARG n 
1 49  ALA n 
1 50  SER n 
1 51  VAL n 
1 52  GLU n 
1 53  THR n 
1 54  GLY n 
1 55  PHE n 
1 56  ALA n 
1 57  LYS n 
1 58  LYS n 
1 59  THR n 
1 60  PHE n 
1 61  ILE n 
1 62  SER n 
1 63  TYR n 
1 64  SER n 
1 65  VAL n 
1 66  THR n 
1 67  PHE n 
1 68  LYS n 
1 69  ASP n 
1 70  ASN n 
1 71  PHE n 
1 72  ARG n 
1 73  GLN n 
1 74  GLY n 
1 75  LEU n 
1 76  VAL n 
1 77  VAL n 
1 78  GLY n 
1 79  ILE n 
1 80  ASP n 
1 81  LEU n 
1 82  LYS n 
1 83  ASN n 
1 84  GLN n 
1 85  MET n 
1 86  VAL n 
1 87  LEU n 
1 88  LEU n 
1 89  GLN n 
1 90  GLY n 
1 91  GLY n 
1 92  GLU n 
1 93  ALA n 
1 94  LEU n 
1 95  PRO n 
1 96  PHE n 
1 97  SER n 
1 98  HIS n 
1 99  LEU n 
1 100 ILE n 
1 101 LEU n 
1 102 ALA n 
1 103 THR n 
1 104 GLY n 
1 105 SER n 
1 106 THR n 
1 107 GLY n 
1 108 PRO n 
1 109 PHE n 
1 110 PRO n 
1 111 GLY n 
1 112 LYS n 
1 113 PHE n 
1 114 ASN n 
1 115 GLU n 
1 116 VAL n 
1 117 SER n 
1 118 SER n 
1 119 GLN n 
1 120 GLN n 
1 121 ALA n 
1 122 ALA n 
1 123 ILE n 
1 124 GLN n 
1 125 ALA n 
1 126 TYR n 
1 127 GLU n 
1 128 ASP n 
1 129 MET n 
1 130 VAL n 
1 131 ARG n 
1 132 GLN n 
1 133 VAL n 
1 134 GLN n 
1 135 ARG n 
1 136 SER n 
1 137 ARG n 
1 138 PHE n 
1 139 ILE n 
1 140 VAL n 
1 141 VAL n 
1 142 VAL n 
1 143 GLY n 
1 144 GLY n 
1 145 GLY n 
1 146 SER n 
1 147 ALA n 
1 148 GLY n 
1 149 VAL n 
1 150 GLU n 
1 151 MET n 
1 152 ALA n 
1 153 ALA n 
1 154 GLU n 
1 155 ILE n 
1 156 LYS n 
1 157 THR n 
1 158 GLU n 
1 159 TYR n 
1 160 PRO n 
1 161 GLU n 
1 162 LYS n 
1 163 GLU n 
1 164 VAL n 
1 165 THR n 
1 166 LEU n 
1 167 ILE n 
1 168 HIS n 
1 169 SER n 
1 170 GLN n 
1 171 VAL n 
1 172 ALA n 
1 173 LEU n 
1 174 ALA n 
1 175 ASP n 
1 176 LYS n 
1 177 GLU n 
1 178 LEU n 
1 179 LEU n 
1 180 PRO n 
1 181 SER n 
1 182 VAL n 
1 183 ARG n 
1 184 GLN n 
1 185 GLU n 
1 186 VAL n 
1 187 LYS n 
1 188 GLU n 
1 189 ILE n 
1 190 LEU n 
1 191 LEU n 
1 192 ARG n 
1 193 LYS n 
1 194 GLY n 
1 195 VAL n 
1 196 GLN n 
1 197 LEU n 
1 198 LEU n 
1 199 LEU n 
1 200 SER n 
1 201 GLU n 
1 202 ARG n 
1 203 VAL n 
1 204 SER n 
1 205 ASN n 
1 206 LEU n 
1 207 GLU n 
1 208 GLU n 
1 209 LEU n 
1 210 PRO n 
1 211 LEU n 
1 212 ASN n 
1 213 GLU n 
1 214 TYR n 
1 215 ARG n 
1 216 GLU n 
1 217 TYR n 
1 218 ILE n 
1 219 LYS n 
1 220 VAL n 
1 221 GLN n 
1 222 THR n 
1 223 ASP n 
1 224 LYS n 
1 225 GLY n 
1 226 THR n 
1 227 GLU n 
1 228 VAL n 
1 229 ALA n 
1 230 THR n 
1 231 ASN n 
1 232 LEU n 
1 233 VAL n 
1 234 ILE n 
1 235 LEU n 
1 236 CYS n 
1 237 THR n 
1 238 GLY n 
1 239 ILE n 
1 240 LYS n 
1 241 ILE n 
1 242 ASN n 
1 243 SER n 
1 244 SER n 
1 245 ALA n 
1 246 TYR n 
1 247 ARG n 
1 248 LYS n 
1 249 ALA n 
1 250 PHE n 
1 251 GLU n 
1 252 SER n 
1 253 ARG n 
1 254 LEU n 
1 255 ALA n 
1 256 SER n 
1 257 SER n 
1 258 GLY n 
1 259 ALA n 
1 260 LEU n 
1 261 ARG n 
1 262 VAL n 
1 263 ASN n 
1 264 GLU n 
1 265 HIS n 
1 266 LEU n 
1 267 GLN n 
1 268 VAL n 
1 269 GLU n 
1 270 GLY n 
1 271 HIS n 
1 272 SER n 
1 273 ASN n 
1 274 VAL n 
1 275 TYR n 
1 276 ALA n 
1 277 ILE n 
1 278 GLY n 
1 279 ASP n 
1 280 CYS n 
1 281 ALA n 
1 282 ASP n 
1 283 VAL n 
1 284 ARG n 
1 285 THR n 
1 286 PRO n 
1 287 LYS n 
1 288 MET n 
1 289 ALA n 
1 290 TYR n 
1 291 LEU n 
1 292 ALA n 
1 293 GLY n 
1 294 LEU n 
1 295 HIS n 
1 296 ALA n 
1 297 ASN n 
1 298 ILE n 
1 299 ALA n 
1 300 VAL n 
1 301 ALA n 
1 302 ASN n 
1 303 ILE n 
1 304 VAL n 
1 305 ASN n 
1 306 SER n 
1 307 VAL n 
1 308 LYS n 
1 309 GLN n 
1 310 ARG n 
1 311 PRO n 
1 312 LEU n 
1 313 GLN n 
1 314 ALA n 
1 315 TYR n 
1 316 LYS n 
1 317 PRO n 
1 318 GLY n 
1 319 ALA n 
1 320 LEU n 
1 321 THR n 
1 322 PHE n 
1 323 LEU n 
1 324 LEU n 
1 325 SER n 
1 326 MET n 
1 327 GLY n 
1 328 ARG n 
1 329 ASN n 
1 330 ASP n 
1 331 GLY n 
1 332 VAL n 
1 333 GLY n 
1 334 GLN n 
1 335 ILE n 
1 336 SER n 
1 337 GLY n 
1 338 PHE n 
1 339 TYR n 
1 340 VAL n 
1 341 GLY n 
1 342 ARG n 
1 343 LEU n 
1 344 MET n 
1 345 VAL n 
1 346 ARG n 
1 347 LEU n 
1 348 THR n 
1 349 LYS n 
1 350 SER n 
1 351 ARG n 
1 352 ASP n 
1 353 LEU n 
1 354 PHE n 
1 355 VAL n 
1 356 SER n 
1 357 THR n 
1 358 SER n 
1 359 TRP n 
1 360 LYS n 
1 361 THR n 
1 362 MET n 
1 363 ARG n 
1 364 GLN n 
1 365 SER n 
1 366 PRO n 
1 367 PRO 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                   367 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'AIFM2, AMID, PRG3' 
_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      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_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 
6FA non-polymer         . '6-HYDROXY-FLAVIN-ADENINE DINUCLEOTIDE'                     ? 'C27 H33 N9 O16 P2' 801.549 
ALA 'L-peptide linking' y ALANINE                                                     ? 'C3 H7 N O2'        89.093  
ARG 'L-peptide linking' y ARGININE                                                    ? 'C6 H15 N4 O2 1'    175.209 
ASN 'L-peptide linking' y ASPARAGINE                                                  ? 'C4 H8 N2 O3'       132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                                             ? 'C4 H7 N O4'        133.103 
CYS 'L-peptide linking' y CYSTEINE                                                    ? 'C3 H7 N O2 S'      121.158 
GLN 'L-peptide linking' y GLUTAMINE                                                   ? 'C5 H10 N2 O3'      146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                                             ? 'C5 H9 N O4'        147.129 
GLY 'peptide linking'   y GLYCINE                                                     ? 'C2 H5 N O2'        75.067  
HIS 'L-peptide linking' y HISTIDINE                                                   ? 'C6 H10 N3 O2 1'    156.162 
HOH non-polymer         . WATER                                                       ? 'H2 O'              18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                                  ? 'C6 H13 N O2'       131.173 
LEU 'L-peptide linking' y LEUCINE                                                     ? 'C6 H13 N O2'       131.173 
LYS 'L-peptide linking' y LYSINE                                                      ? 'C6 H15 N2 O2 1'    147.195 
MET 'L-peptide linking' y METHIONINE                                                  ? 'C5 H11 N O2 S'     149.211 
NDP non-polymer         . 'NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE' ? 'C21 H30 N7 O17 P3' 745.421 
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 
SO4 non-polymer         . 'SULFATE ION'                                               ? 'O4 S -2'           96.063  
THR 'L-peptide linking' y THREONINE                                                   ? 'C4 H9 N O3'        119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                                  ? 'C11 H12 N2 O2'     204.225 
TYR 'L-peptide linking' y TYROSINE                                                    ? 'C9 H11 N O3'       181.189 
VAL 'L-peptide linking' y VALINE                                                      ? 'C5 H11 N O2'       117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   PRO 1   7   7   PRO PRO A . n 
A 1 2   HIS 2   8   8   HIS HIS A . n 
A 1 3   MET 3   9   9   MET MET A . n 
A 1 4   GLY 4   10  10  GLY GLY A . n 
A 1 5   ALA 5   11  11  ALA ALA A . n 
A 1 6   LEU 6   12  12  LEU LEU A . n 
A 1 7   HIS 7   13  13  HIS HIS A . n 
A 1 8   VAL 8   14  14  VAL VAL A . n 
A 1 9   VAL 9   15  15  VAL VAL A . n 
A 1 10  ILE 10  16  16  ILE ILE A . n 
A 1 11  VAL 11  17  17  VAL VAL A . n 
A 1 12  GLY 12  18  18  GLY GLY A . n 
A 1 13  GLY 13  19  19  GLY GLY A . n 
A 1 14  GLY 14  20  20  GLY GLY A . n 
A 1 15  PHE 15  21  21  PHE PHE A . n 
A 1 16  GLY 16  22  22  GLY GLY A . n 
A 1 17  GLY 17  23  23  GLY GLY A . n 
A 1 18  ILE 18  24  24  ILE ILE A . n 
A 1 19  ALA 19  25  25  ALA ALA A . n 
A 1 20  ALA 20  26  26  ALA ALA A . n 
A 1 21  ALA 21  27  27  ALA ALA A . n 
A 1 22  SER 22  28  28  SER SER A . n 
A 1 23  GLN 23  29  29  GLN GLN A . n 
A 1 24  LEU 24  30  30  LEU LEU A . n 
A 1 25  GLN 25  31  31  GLN GLN A . n 
A 1 26  ALA 26  32  32  ALA ALA A . n 
A 1 27  LEU 27  33  33  LEU LEU A . n 
A 1 28  ASN 28  34  34  ASN ASN A . n 
A 1 29  VAL 29  35  35  VAL VAL A . n 
A 1 30  PRO 30  36  36  PRO PRO A . n 
A 1 31  PHE 31  37  37  PHE PHE A . n 
A 1 32  MET 32  38  38  MET MET A . n 
A 1 33  LEU 33  39  39  LEU LEU A . n 
A 1 34  VAL 34  40  40  VAL VAL A . n 
A 1 35  ASP 35  41  41  ASP ASP A . n 
A 1 36  MET 36  42  42  MET MET A . n 
A 1 37  LYS 37  43  43  LYS LYS A . n 
A 1 38  ASP 38  44  44  ASP ASP A . n 
A 1 39  SER 39  45  45  SER SER A . n 
A 1 40  PHE 40  46  46  PHE PHE A . n 
A 1 41  HIS 41  47  47  HIS HIS A . n 
A 1 42  HIS 42  48  48  HIS HIS A . n 
A 1 43  ASN 43  49  49  ASN ASN A . n 
A 1 44  VAL 44  50  50  VAL VAL A . n 
A 1 45  ALA 45  51  51  ALA ALA A . n 
A 1 46  ALA 46  52  52  ALA ALA A . n 
A 1 47  LEU 47  53  53  LEU LEU A . n 
A 1 48  ARG 48  54  54  ARG ARG A . n 
A 1 49  ALA 49  55  55  ALA ALA A . n 
A 1 50  SER 50  56  56  SER SER A . n 
A 1 51  VAL 51  57  57  VAL VAL A . n 
A 1 52  GLU 52  58  58  GLU GLU A . n 
A 1 53  THR 53  59  59  THR THR A . n 
A 1 54  GLY 54  60  60  GLY GLY A . n 
A 1 55  PHE 55  61  61  PHE PHE A . n 
A 1 56  ALA 56  62  62  ALA ALA A . n 
A 1 57  LYS 57  63  63  LYS LYS A . n 
A 1 58  LYS 58  64  64  LYS LYS A . n 
A 1 59  THR 59  65  65  THR THR A . n 
A 1 60  PHE 60  66  66  PHE PHE A . n 
A 1 61  ILE 61  67  67  ILE ILE A . n 
A 1 62  SER 62  68  68  SER SER A . n 
A 1 63  TYR 63  69  69  TYR TYR A . n 
A 1 64  SER 64  70  70  SER SER A . n 
A 1 65  VAL 65  71  71  VAL VAL A . n 
A 1 66  THR 66  72  72  THR THR A . n 
A 1 67  PHE 67  73  73  PHE PHE A . n 
A 1 68  LYS 68  74  74  LYS LYS A . n 
A 1 69  ASP 69  75  75  ASP ASP A . n 
A 1 70  ASN 70  76  76  ASN ASN A . n 
A 1 71  PHE 71  77  77  PHE PHE A . n 
A 1 72  ARG 72  78  78  ARG ARG A . n 
A 1 73  GLN 73  79  79  GLN GLN A . n 
A 1 74  GLY 74  80  80  GLY GLY A . n 
A 1 75  LEU 75  81  81  LEU LEU A . n 
A 1 76  VAL 76  82  82  VAL VAL A . n 
A 1 77  VAL 77  83  83  VAL VAL A . n 
A 1 78  GLY 78  84  84  GLY GLY A . n 
A 1 79  ILE 79  85  85  ILE ILE A . n 
A 1 80  ASP 80  86  86  ASP ASP A . n 
A 1 81  LEU 81  87  87  LEU LEU A . n 
A 1 82  LYS 82  88  88  LYS LYS A . n 
A 1 83  ASN 83  89  89  ASN ASN A . n 
A 1 84  GLN 84  90  90  GLN GLN A . n 
A 1 85  MET 85  91  91  MET MET A . n 
A 1 86  VAL 86  92  92  VAL VAL A . n 
A 1 87  LEU 87  93  93  LEU LEU A . n 
A 1 88  LEU 88  94  94  LEU LEU A . n 
A 1 89  GLN 89  95  95  GLN GLN A . n 
A 1 90  GLY 90  96  96  GLY GLY A . n 
A 1 91  GLY 91  97  97  GLY GLY A . n 
A 1 92  GLU 92  98  98  GLU GLU A . n 
A 1 93  ALA 93  99  99  ALA ALA A . n 
A 1 94  LEU 94  100 100 LEU LEU A . n 
A 1 95  PRO 95  101 101 PRO PRO A . n 
A 1 96  PHE 96  102 102 PHE PHE A . n 
A 1 97  SER 97  103 103 SER SER A . n 
A 1 98  HIS 98  104 104 HIS HIS A . n 
A 1 99  LEU 99  105 105 LEU LEU A . n 
A 1 100 ILE 100 106 106 ILE ILE A . n 
A 1 101 LEU 101 107 107 LEU LEU A . n 
A 1 102 ALA 102 108 108 ALA ALA A . n 
A 1 103 THR 103 109 109 THR THR A . n 
A 1 104 GLY 104 110 110 GLY GLY A . n 
A 1 105 SER 105 111 111 SER SER A . n 
A 1 106 THR 106 112 112 THR THR A . n 
A 1 107 GLY 107 113 113 GLY GLY A . n 
A 1 108 PRO 108 114 114 PRO PRO A . n 
A 1 109 PHE 109 115 115 PHE PHE A . n 
A 1 110 PRO 110 116 116 PRO PRO A . n 
A 1 111 GLY 111 117 117 GLY GLY A . n 
A 1 112 LYS 112 118 118 LYS LYS A . n 
A 1 113 PHE 113 119 119 PHE PHE A . n 
A 1 114 ASN 114 120 120 ASN ASN A . n 
A 1 115 GLU 115 121 121 GLU GLU A . n 
A 1 116 VAL 116 122 122 VAL VAL A . n 
A 1 117 SER 117 123 123 SER SER A . n 
A 1 118 SER 118 124 124 SER SER A . n 
A 1 119 GLN 119 125 125 GLN GLN A . n 
A 1 120 GLN 120 126 126 GLN GLN A . n 
A 1 121 ALA 121 127 127 ALA ALA A . n 
A 1 122 ALA 122 128 128 ALA ALA A . n 
A 1 123 ILE 123 129 129 ILE ILE A . n 
A 1 124 GLN 124 130 130 GLN GLN A . n 
A 1 125 ALA 125 131 131 ALA ALA A . n 
A 1 126 TYR 126 132 132 TYR TYR A . n 
A 1 127 GLU 127 133 133 GLU GLU A . n 
A 1 128 ASP 128 134 134 ASP ASP A . n 
A 1 129 MET 129 135 135 MET MET A . n 
A 1 130 VAL 130 136 136 VAL VAL A . n 
A 1 131 ARG 131 137 137 ARG ARG A . n 
A 1 132 GLN 132 138 138 GLN GLN A . n 
A 1 133 VAL 133 139 139 VAL VAL A . n 
A 1 134 GLN 134 140 140 GLN GLN A . n 
A 1 135 ARG 135 141 141 ARG ARG A . n 
A 1 136 SER 136 142 142 SER SER A . n 
A 1 137 ARG 137 143 143 ARG ARG A . n 
A 1 138 PHE 138 144 144 PHE PHE A . n 
A 1 139 ILE 139 145 145 ILE ILE A . n 
A 1 140 VAL 140 146 146 VAL VAL A . n 
A 1 141 VAL 141 147 147 VAL VAL A . n 
A 1 142 VAL 142 148 148 VAL VAL A . n 
A 1 143 GLY 143 149 149 GLY GLY A . n 
A 1 144 GLY 144 150 150 GLY GLY A . n 
A 1 145 GLY 145 151 151 GLY GLY A . n 
A 1 146 SER 146 152 152 SER SER A . n 
A 1 147 ALA 147 153 153 ALA ALA A . n 
A 1 148 GLY 148 154 154 GLY GLY A . n 
A 1 149 VAL 149 155 155 VAL VAL A . n 
A 1 150 GLU 150 156 156 GLU GLU A . n 
A 1 151 MET 151 157 157 MET MET A . n 
A 1 152 ALA 152 158 158 ALA ALA A . n 
A 1 153 ALA 153 159 159 ALA ALA A . n 
A 1 154 GLU 154 160 160 GLU GLU A . n 
A 1 155 ILE 155 161 161 ILE ILE A . n 
A 1 156 LYS 156 162 162 LYS LYS A . n 
A 1 157 THR 157 163 163 THR THR A . n 
A 1 158 GLU 158 164 164 GLU GLU A . n 
A 1 159 TYR 159 165 165 TYR TYR A . n 
A 1 160 PRO 160 166 166 PRO PRO A . n 
A 1 161 GLU 161 167 167 GLU GLU A . n 
A 1 162 LYS 162 168 168 LYS LYS A . n 
A 1 163 GLU 163 169 169 GLU GLU A . n 
A 1 164 VAL 164 170 170 VAL VAL A . n 
A 1 165 THR 165 171 171 THR THR A . n 
A 1 166 LEU 166 172 172 LEU LEU A . n 
A 1 167 ILE 167 173 173 ILE ILE A . n 
A 1 168 HIS 168 174 174 HIS HIS A . n 
A 1 169 SER 169 175 175 SER SER A . n 
A 1 170 GLN 170 176 176 GLN GLN A . n 
A 1 171 VAL 171 177 177 VAL VAL A . n 
A 1 172 ALA 172 178 178 ALA ALA A . n 
A 1 173 LEU 173 179 179 LEU LEU A . n 
A 1 174 ALA 174 180 180 ALA ALA A . n 
A 1 175 ASP 175 181 181 ASP ASP A . n 
A 1 176 LYS 176 182 182 LYS LYS A . n 
A 1 177 GLU 177 183 183 GLU GLU A . n 
A 1 178 LEU 178 184 184 LEU LEU A . n 
A 1 179 LEU 179 185 185 LEU LEU A . n 
A 1 180 PRO 180 186 186 PRO PRO A . n 
A 1 181 SER 181 187 187 SER SER A . n 
A 1 182 VAL 182 188 188 VAL VAL A . n 
A 1 183 ARG 183 189 189 ARG ARG A . n 
A 1 184 GLN 184 190 190 GLN GLN A . n 
A 1 185 GLU 185 191 191 GLU GLU A . n 
A 1 186 VAL 186 192 192 VAL VAL A . n 
A 1 187 LYS 187 193 193 LYS LYS A . n 
A 1 188 GLU 188 194 194 GLU GLU A . n 
A 1 189 ILE 189 195 195 ILE ILE A . n 
A 1 190 LEU 190 196 196 LEU LEU A . n 
A 1 191 LEU 191 197 197 LEU LEU A . n 
A 1 192 ARG 192 198 198 ARG ARG A . n 
A 1 193 LYS 193 199 199 LYS LYS A . n 
A 1 194 GLY 194 200 200 GLY GLY A . n 
A 1 195 VAL 195 201 201 VAL VAL A . n 
A 1 196 GLN 196 202 202 GLN GLN A . n 
A 1 197 LEU 197 203 203 LEU LEU A . n 
A 1 198 LEU 198 204 204 LEU LEU A . n 
A 1 199 LEU 199 205 205 LEU LEU A . n 
A 1 200 SER 200 206 206 SER SER A . n 
A 1 201 GLU 201 207 207 GLU GLU A . n 
A 1 202 ARG 202 208 208 ARG ARG A . n 
A 1 203 VAL 203 209 209 VAL VAL A . n 
A 1 204 SER 204 210 210 SER SER A . n 
A 1 205 ASN 205 211 211 ASN ASN A . n 
A 1 206 LEU 206 212 212 LEU LEU A . n 
A 1 207 GLU 207 213 213 GLU GLU A . n 
A 1 208 GLU 208 214 214 GLU GLU A . n 
A 1 209 LEU 209 215 215 LEU LEU A . n 
A 1 210 PRO 210 216 216 PRO PRO A . n 
A 1 211 LEU 211 217 217 LEU LEU A . n 
A 1 212 ASN 212 218 218 ASN ASN A . n 
A 1 213 GLU 213 219 219 GLU GLU A . n 
A 1 214 TYR 214 220 220 TYR TYR A . n 
A 1 215 ARG 215 221 221 ARG ARG A . n 
A 1 216 GLU 216 222 222 GLU GLU A . n 
A 1 217 TYR 217 223 223 TYR TYR A . n 
A 1 218 ILE 218 224 224 ILE ILE A . n 
A 1 219 LYS 219 225 225 LYS LYS A . n 
A 1 220 VAL 220 226 226 VAL VAL A . n 
A 1 221 GLN 221 227 227 GLN GLN A . n 
A 1 222 THR 222 228 228 THR THR A . n 
A 1 223 ASP 223 229 229 ASP ASP A . n 
A 1 224 LYS 224 230 230 LYS LYS A . n 
A 1 225 GLY 225 231 231 GLY GLY A . n 
A 1 226 THR 226 232 232 THR THR A . n 
A 1 227 GLU 227 233 233 GLU GLU A . n 
A 1 228 VAL 228 234 234 VAL VAL A . n 
A 1 229 ALA 229 235 235 ALA ALA A . n 
A 1 230 THR 230 236 236 THR THR A . n 
A 1 231 ASN 231 237 237 ASN ASN A . n 
A 1 232 LEU 232 238 238 LEU LEU A . n 
A 1 233 VAL 233 239 239 VAL VAL A . n 
A 1 234 ILE 234 240 240 ILE ILE A . n 
A 1 235 LEU 235 241 241 LEU LEU A . n 
A 1 236 CYS 236 242 242 CYS CYS A . n 
A 1 237 THR 237 243 243 THR THR A . n 
A 1 238 GLY 238 244 244 GLY GLY A . n 
A 1 239 ILE 239 245 245 ILE ILE A . n 
A 1 240 LYS 240 246 246 LYS LYS A . n 
A 1 241 ILE 241 247 247 ILE ILE A . n 
A 1 242 ASN 242 248 248 ASN ASN A . n 
A 1 243 SER 243 249 249 SER SER A . n 
A 1 244 SER 244 250 250 SER SER A . n 
A 1 245 ALA 245 251 251 ALA ALA A . n 
A 1 246 TYR 246 252 252 TYR TYR A . n 
A 1 247 ARG 247 253 253 ARG ARG A . n 
A 1 248 LYS 248 254 254 LYS LYS A . n 
A 1 249 ALA 249 255 255 ALA ALA A . n 
A 1 250 PHE 250 256 256 PHE PHE A . n 
A 1 251 GLU 251 257 257 GLU GLU A . n 
A 1 252 SER 252 258 258 SER SER A . n 
A 1 253 ARG 253 259 259 ARG ARG A . n 
A 1 254 LEU 254 260 260 LEU LEU A . n 
A 1 255 ALA 255 261 261 ALA ALA A . n 
A 1 256 SER 256 262 262 SER SER A . n 
A 1 257 SER 257 263 263 SER SER A . n 
A 1 258 GLY 258 264 264 GLY GLY A . n 
A 1 259 ALA 259 265 265 ALA ALA A . n 
A 1 260 LEU 260 266 266 LEU LEU A . n 
A 1 261 ARG 261 267 267 ARG ARG A . n 
A 1 262 VAL 262 268 268 VAL VAL A . n 
A 1 263 ASN 263 269 269 ASN ASN A . n 
A 1 264 GLU 264 270 270 GLU GLU A . n 
A 1 265 HIS 265 271 271 HIS HIS A . n 
A 1 266 LEU 266 272 272 LEU LEU A . n 
A 1 267 GLN 267 273 273 GLN GLN A . n 
A 1 268 VAL 268 274 274 VAL VAL A . n 
A 1 269 GLU 269 275 275 GLU GLU A . n 
A 1 270 GLY 270 276 276 GLY GLY A . n 
A 1 271 HIS 271 277 277 HIS HIS A . n 
A 1 272 SER 272 278 278 SER SER A . n 
A 1 273 ASN 273 279 279 ASN ASN A . n 
A 1 274 VAL 274 280 280 VAL VAL A . n 
A 1 275 TYR 275 281 281 TYR TYR A . n 
A 1 276 ALA 276 282 282 ALA ALA A . n 
A 1 277 ILE 277 283 283 ILE ILE A . n 
A 1 278 GLY 278 284 284 GLY GLY A . n 
A 1 279 ASP 279 285 285 ASP ASP A . n 
A 1 280 CYS 280 286 286 CYS CYS A . n 
A 1 281 ALA 281 287 287 ALA ALA A . n 
A 1 282 ASP 282 288 288 ASP ASP A . n 
A 1 283 VAL 283 289 289 VAL VAL A . n 
A 1 284 ARG 284 290 290 ARG ARG A . n 
A 1 285 THR 285 291 291 THR THR A . n 
A 1 286 PRO 286 292 292 PRO PRO A . n 
A 1 287 LYS 287 293 293 LYS LYS A . n 
A 1 288 MET 288 294 294 MET MET A . n 
A 1 289 ALA 289 295 295 ALA ALA A . n 
A 1 290 TYR 290 296 296 TYR TYR A . n 
A 1 291 LEU 291 297 297 LEU LEU A . n 
A 1 292 ALA 292 298 298 ALA ALA A . n 
A 1 293 GLY 293 299 299 GLY GLY A . n 
A 1 294 LEU 294 300 300 LEU LEU A . n 
A 1 295 HIS 295 301 301 HIS HIS A . n 
A 1 296 ALA 296 302 302 ALA ALA A . n 
A 1 297 ASN 297 303 303 ASN ASN A . n 
A 1 298 ILE 298 304 304 ILE ILE A . n 
A 1 299 ALA 299 305 305 ALA ALA A . n 
A 1 300 VAL 300 306 306 VAL VAL A . n 
A 1 301 ALA 301 307 307 ALA ALA A . n 
A 1 302 ASN 302 308 308 ASN ASN A . n 
A 1 303 ILE 303 309 309 ILE ILE A . n 
A 1 304 VAL 304 310 310 VAL VAL A . n 
A 1 305 ASN 305 311 311 ASN ASN A . n 
A 1 306 SER 306 312 312 SER SER A . n 
A 1 307 VAL 307 313 313 VAL VAL A . n 
A 1 308 LYS 308 314 314 LYS LYS A . n 
A 1 309 GLN 309 315 315 GLN GLN A . n 
A 1 310 ARG 310 316 316 ARG ARG A . n 
A 1 311 PRO 311 317 317 PRO PRO A . n 
A 1 312 LEU 312 318 318 LEU LEU A . n 
A 1 313 GLN 313 319 319 GLN GLN A . n 
A 1 314 ALA 314 320 320 ALA ALA A . n 
A 1 315 TYR 315 321 321 TYR TYR A . n 
A 1 316 LYS 316 322 322 LYS LYS A . n 
A 1 317 PRO 317 323 323 PRO PRO A . n 
A 1 318 GLY 318 324 324 GLY GLY A . n 
A 1 319 ALA 319 325 325 ALA ALA A . n 
A 1 320 LEU 320 326 326 LEU LEU A . n 
A 1 321 THR 321 327 327 THR THR A . n 
A 1 322 PHE 322 328 328 PHE PHE A . n 
A 1 323 LEU 323 329 329 LEU LEU A . n 
A 1 324 LEU 324 330 330 LEU LEU A . n 
A 1 325 SER 325 331 331 SER SER A . n 
A 1 326 MET 326 332 332 MET MET A . n 
A 1 327 GLY 327 333 333 GLY GLY A . n 
A 1 328 ARG 328 334 334 ARG ARG A . n 
A 1 329 ASN 329 335 335 ASN ASN A . n 
A 1 330 ASP 330 336 336 ASP ASP A . n 
A 1 331 GLY 331 337 337 GLY GLY A . n 
A 1 332 VAL 332 338 338 VAL VAL A . n 
A 1 333 GLY 333 339 339 GLY GLY A . n 
A 1 334 GLN 334 340 340 GLN GLN A . n 
A 1 335 ILE 335 341 341 ILE ILE A . n 
A 1 336 SER 336 342 342 SER SER A . n 
A 1 337 GLY 337 343 343 GLY GLY A . n 
A 1 338 PHE 338 344 344 PHE PHE A . n 
A 1 339 TYR 339 345 345 TYR TYR A . n 
A 1 340 VAL 340 346 346 VAL VAL A . n 
A 1 341 GLY 341 347 347 GLY GLY A . n 
A 1 342 ARG 342 348 348 ARG ARG A . n 
A 1 343 LEU 343 349 349 LEU LEU A . n 
A 1 344 MET 344 350 350 MET MET A . n 
A 1 345 VAL 345 351 351 VAL VAL A . n 
A 1 346 ARG 346 352 352 ARG ARG A . n 
A 1 347 LEU 347 353 353 LEU LEU A . n 
A 1 348 THR 348 354 354 THR THR A . n 
A 1 349 LYS 349 355 355 LYS LYS A . n 
A 1 350 SER 350 356 356 SER SER A . n 
A 1 351 ARG 351 357 357 ARG ARG A . n 
A 1 352 ASP 352 358 358 ASP ASP A . n 
A 1 353 LEU 353 359 359 LEU LEU A . n 
A 1 354 PHE 354 360 360 PHE PHE A . n 
A 1 355 VAL 355 361 361 VAL VAL A . n 
A 1 356 SER 356 362 362 SER SER A . n 
A 1 357 THR 357 363 363 THR THR A . n 
A 1 358 SER 358 364 364 SER SER A . n 
A 1 359 TRP 359 365 365 TRP TRP A . n 
A 1 360 LYS 360 366 366 LYS LYS A . n 
A 1 361 THR 361 367 367 THR THR A . n 
A 1 362 MET 362 368 368 MET MET A . n 
A 1 363 ARG 363 369 369 ARG ARG A . n 
A 1 364 GLN 364 370 370 GLN GLN A . n 
A 1 365 SER 365 371 371 SER SER A . n 
A 1 366 PRO 366 372 372 PRO PRO A . n 
A 1 367 PRO 367 373 373 PRO PRO A . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 6FA ? ? 6FA ? ? 'SUBJECT OF INVESTIGATION' ? 
2 NDP ? ? NDP ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 6FA 1   401 401 6FA 6FA A . 
C 3 NDP 1   402 402 NDP NDP A . 
D 4 SO4 1   403 1   SO4 SO4 A . 
E 5 HOH 1   501 88  HOH HOH A . 
E 5 HOH 2   502 127 HOH HOH A . 
E 5 HOH 3   503 116 HOH HOH A . 
E 5 HOH 4   504 236 HOH HOH A . 
E 5 HOH 5   505 38  HOH HOH A . 
E 5 HOH 6   506 99  HOH HOH A . 
E 5 HOH 7   507 224 HOH HOH A . 
E 5 HOH 8   508 221 HOH HOH A . 
E 5 HOH 9   509 143 HOH HOH A . 
E 5 HOH 10  510 234 HOH HOH A . 
E 5 HOH 11  511 276 HOH HOH A . 
E 5 HOH 12  512 310 HOH HOH A . 
E 5 HOH 13  513 290 HOH HOH A . 
E 5 HOH 14  514 260 HOH HOH A . 
E 5 HOH 15  515 50  HOH HOH A . 
E 5 HOH 16  516 169 HOH HOH A . 
E 5 HOH 17  517 298 HOH HOH A . 
E 5 HOH 18  518 278 HOH HOH A . 
E 5 HOH 19  519 230 HOH HOH A . 
E 5 HOH 20  520 98  HOH HOH A . 
E 5 HOH 21  521 291 HOH HOH A . 
E 5 HOH 22  522 183 HOH HOH A . 
E 5 HOH 23  523 68  HOH HOH A . 
E 5 HOH 24  524 95  HOH HOH A . 
E 5 HOH 25  525 64  HOH HOH A . 
E 5 HOH 26  526 113 HOH HOH A . 
E 5 HOH 27  527 165 HOH HOH A . 
E 5 HOH 28  528 61  HOH HOH A . 
E 5 HOH 29  529 213 HOH HOH A . 
E 5 HOH 30  530 244 HOH HOH A . 
E 5 HOH 31  531 110 HOH HOH A . 
E 5 HOH 32  532 107 HOH HOH A . 
E 5 HOH 33  533 86  HOH HOH A . 
E 5 HOH 34  534 14  HOH HOH A . 
E 5 HOH 35  535 26  HOH HOH A . 
E 5 HOH 36  536 84  HOH HOH A . 
E 5 HOH 37  537 12  HOH HOH A . 
E 5 HOH 38  538 55  HOH HOH A . 
E 5 HOH 39  539 53  HOH HOH A . 
E 5 HOH 40  540 35  HOH HOH A . 
E 5 HOH 41  541 225 HOH HOH A . 
E 5 HOH 42  542 173 HOH HOH A . 
E 5 HOH 43  543 155 HOH HOH A . 
E 5 HOH 44  544 111 HOH HOH A . 
E 5 HOH 45  545 25  HOH HOH A . 
E 5 HOH 46  546 33  HOH HOH A . 
E 5 HOH 47  547 42  HOH HOH A . 
E 5 HOH 48  548 22  HOH HOH A . 
E 5 HOH 49  549 101 HOH HOH A . 
E 5 HOH 50  550 265 HOH HOH A . 
E 5 HOH 51  551 1   HOH HOH A . 
E 5 HOH 52  552 54  HOH HOH A . 
E 5 HOH 53  553 28  HOH HOH A . 
E 5 HOH 54  554 37  HOH HOH A . 
E 5 HOH 55  555 112 HOH HOH A . 
E 5 HOH 56  556 52  HOH HOH A . 
E 5 HOH 57  557 108 HOH HOH A . 
E 5 HOH 58  558 196 HOH HOH A . 
E 5 HOH 59  559 115 HOH HOH A . 
E 5 HOH 60  560 65  HOH HOH A . 
E 5 HOH 61  561 7   HOH HOH A . 
E 5 HOH 62  562 186 HOH HOH A . 
E 5 HOH 63  563 60  HOH HOH A . 
E 5 HOH 64  564 266 HOH HOH A . 
E 5 HOH 65  565 149 HOH HOH A . 
E 5 HOH 66  566 250 HOH HOH A . 
E 5 HOH 67  567 238 HOH HOH A . 
E 5 HOH 68  568 4   HOH HOH A . 
E 5 HOH 69  569 252 HOH HOH A . 
E 5 HOH 70  570 226 HOH HOH A . 
E 5 HOH 71  571 124 HOH HOH A . 
E 5 HOH 72  572 63  HOH HOH A . 
E 5 HOH 73  573 187 HOH HOH A . 
E 5 HOH 74  574 5   HOH HOH A . 
E 5 HOH 75  575 70  HOH HOH A . 
E 5 HOH 76  576 305 HOH HOH A . 
E 5 HOH 77  577 171 HOH HOH A . 
E 5 HOH 78  578 80  HOH HOH A . 
E 5 HOH 79  579 161 HOH HOH A . 
E 5 HOH 80  580 206 HOH HOH A . 
E 5 HOH 81  581 303 HOH HOH A . 
E 5 HOH 82  582 74  HOH HOH A . 
E 5 HOH 83  583 16  HOH HOH A . 
E 5 HOH 84  584 29  HOH HOH A . 
E 5 HOH 85  585 43  HOH HOH A . 
E 5 HOH 86  586 2   HOH HOH A . 
E 5 HOH 87  587 122 HOH HOH A . 
E 5 HOH 88  588 109 HOH HOH A . 
E 5 HOH 89  589 162 HOH HOH A . 
E 5 HOH 90  590 215 HOH HOH A . 
E 5 HOH 91  591 117 HOH HOH A . 
E 5 HOH 92  592 85  HOH HOH A . 
E 5 HOH 93  593 56  HOH HOH A . 
E 5 HOH 94  594 15  HOH HOH A . 
E 5 HOH 95  595 21  HOH HOH A . 
E 5 HOH 96  596 283 HOH HOH A . 
E 5 HOH 97  597 147 HOH HOH A . 
E 5 HOH 98  598 194 HOH HOH A . 
E 5 HOH 99  599 166 HOH HOH A . 
E 5 HOH 100 600 289 HOH HOH A . 
E 5 HOH 101 601 3   HOH HOH A . 
E 5 HOH 102 602 17  HOH HOH A . 
E 5 HOH 103 603 19  HOH HOH A . 
E 5 HOH 104 604 275 HOH HOH A . 
E 5 HOH 105 605 172 HOH HOH A . 
E 5 HOH 106 606 306 HOH HOH A . 
E 5 HOH 107 607 24  HOH HOH A . 
E 5 HOH 108 608 78  HOH HOH A . 
E 5 HOH 109 609 148 HOH HOH A . 
E 5 HOH 110 610 270 HOH HOH A . 
E 5 HOH 111 611 67  HOH HOH A . 
E 5 HOH 112 612 180 HOH HOH A . 
E 5 HOH 113 613 93  HOH HOH A . 
E 5 HOH 114 614 32  HOH HOH A . 
E 5 HOH 115 615 46  HOH HOH A . 
E 5 HOH 116 616 308 HOH HOH A . 
E 5 HOH 117 617 123 HOH HOH A . 
E 5 HOH 118 618 102 HOH HOH A . 
E 5 HOH 119 619 262 HOH HOH A . 
E 5 HOH 120 620 212 HOH HOH A . 
E 5 HOH 121 621 267 HOH HOH A . 
E 5 HOH 122 622 39  HOH HOH A . 
E 5 HOH 123 623 77  HOH HOH A . 
E 5 HOH 124 624 118 HOH HOH A . 
E 5 HOH 125 625 11  HOH HOH A . 
E 5 HOH 126 626 189 HOH HOH A . 
E 5 HOH 127 627 208 HOH HOH A . 
E 5 HOH 128 628 9   HOH HOH A . 
E 5 HOH 129 629 136 HOH HOH A . 
E 5 HOH 130 630 27  HOH HOH A . 
E 5 HOH 131 631 175 HOH HOH A . 
E 5 HOH 132 632 135 HOH HOH A . 
E 5 HOH 133 633 192 HOH HOH A . 
E 5 HOH 134 634 31  HOH HOH A . 
E 5 HOH 135 635 20  HOH HOH A . 
E 5 HOH 136 636 51  HOH HOH A . 
E 5 HOH 137 637 18  HOH HOH A . 
E 5 HOH 138 638 10  HOH HOH A . 
E 5 HOH 139 639 271 HOH HOH A . 
E 5 HOH 140 640 45  HOH HOH A . 
E 5 HOH 141 641 176 HOH HOH A . 
E 5 HOH 142 642 203 HOH HOH A . 
E 5 HOH 143 643 181 HOH HOH A . 
E 5 HOH 144 644 103 HOH HOH A . 
E 5 HOH 145 645 90  HOH HOH A . 
E 5 HOH 146 646 160 HOH HOH A . 
E 5 HOH 147 647 8   HOH HOH A . 
E 5 HOH 148 648 297 HOH HOH A . 
E 5 HOH 149 649 299 HOH HOH A . 
E 5 HOH 150 650 134 HOH HOH A . 
E 5 HOH 151 651 36  HOH HOH A . 
E 5 HOH 152 652 105 HOH HOH A . 
E 5 HOH 153 653 247 HOH HOH A . 
E 5 HOH 154 654 82  HOH HOH A . 
E 5 HOH 155 655 138 HOH HOH A . 
E 5 HOH 156 656 6   HOH HOH A . 
E 5 HOH 157 657 188 HOH HOH A . 
E 5 HOH 158 658 13  HOH HOH A . 
E 5 HOH 159 659 89  HOH HOH A . 
E 5 HOH 160 660 76  HOH HOH A . 
E 5 HOH 161 661 209 HOH HOH A . 
E 5 HOH 162 662 66  HOH HOH A . 
E 5 HOH 163 663 83  HOH HOH A . 
E 5 HOH 164 664 207 HOH HOH A . 
E 5 HOH 165 665 23  HOH HOH A . 
E 5 HOH 166 666 280 HOH HOH A . 
E 5 HOH 167 667 259 HOH HOH A . 
E 5 HOH 168 668 41  HOH HOH A . 
E 5 HOH 169 669 150 HOH HOH A . 
E 5 HOH 170 670 191 HOH HOH A . 
E 5 HOH 171 671 97  HOH HOH A . 
E 5 HOH 172 672 233 HOH HOH A . 
E 5 HOH 173 673 219 HOH HOH A . 
E 5 HOH 174 674 300 HOH HOH A . 
E 5 HOH 175 675 197 HOH HOH A . 
E 5 HOH 176 676 199 HOH HOH A . 
E 5 HOH 177 677 133 HOH HOH A . 
E 5 HOH 178 678 96  HOH HOH A . 
E 5 HOH 179 679 253 HOH HOH A . 
E 5 HOH 180 680 145 HOH HOH A . 
E 5 HOH 181 681 71  HOH HOH A . 
E 5 HOH 182 682 126 HOH HOH A . 
E 5 HOH 183 683 239 HOH HOH A . 
E 5 HOH 184 684 106 HOH HOH A . 
E 5 HOH 185 685 229 HOH HOH A . 
E 5 HOH 186 686 40  HOH HOH A . 
E 5 HOH 187 687 302 HOH HOH A . 
E 5 HOH 188 688 57  HOH HOH A . 
E 5 HOH 189 689 157 HOH HOH A . 
E 5 HOH 190 690 242 HOH HOH A . 
E 5 HOH 191 691 294 HOH HOH A . 
E 5 HOH 192 692 34  HOH HOH A . 
E 5 HOH 193 693 87  HOH HOH A . 
E 5 HOH 194 694 142 HOH HOH A . 
E 5 HOH 195 695 140 HOH HOH A . 
E 5 HOH 196 696 75  HOH HOH A . 
E 5 HOH 197 697 119 HOH HOH A . 
E 5 HOH 198 698 125 HOH HOH A . 
E 5 HOH 199 699 201 HOH HOH A . 
E 5 HOH 200 700 151 HOH HOH A . 
E 5 HOH 201 701 69  HOH HOH A . 
E 5 HOH 202 702 146 HOH HOH A . 
E 5 HOH 203 703 174 HOH HOH A . 
E 5 HOH 204 704 248 HOH HOH A . 
E 5 HOH 205 705 58  HOH HOH A . 
E 5 HOH 206 706 168 HOH HOH A . 
E 5 HOH 207 707 132 HOH HOH A . 
E 5 HOH 208 708 139 HOH HOH A . 
E 5 HOH 209 709 121 HOH HOH A . 
E 5 HOH 210 710 48  HOH HOH A . 
E 5 HOH 211 711 62  HOH HOH A . 
E 5 HOH 212 712 130 HOH HOH A . 
E 5 HOH 213 713 59  HOH HOH A . 
E 5 HOH 214 714 92  HOH HOH A . 
E 5 HOH 215 715 193 HOH HOH A . 
E 5 HOH 216 716 205 HOH HOH A . 
E 5 HOH 217 717 179 HOH HOH A . 
E 5 HOH 218 718 195 HOH HOH A . 
E 5 HOH 219 719 240 HOH HOH A . 
E 5 HOH 220 720 49  HOH HOH A . 
E 5 HOH 221 721 47  HOH HOH A . 
E 5 HOH 222 722 131 HOH HOH A . 
E 5 HOH 223 723 296 HOH HOH A . 
E 5 HOH 224 724 73  HOH HOH A . 
E 5 HOH 225 725 154 HOH HOH A . 
E 5 HOH 226 726 137 HOH HOH A . 
E 5 HOH 227 727 170 HOH HOH A . 
E 5 HOH 228 728 120 HOH HOH A . 
E 5 HOH 229 729 232 HOH HOH A . 
E 5 HOH 230 730 264 HOH HOH A . 
E 5 HOH 231 731 258 HOH HOH A . 
E 5 HOH 232 732 257 HOH HOH A . 
E 5 HOH 233 733 81  HOH HOH A . 
E 5 HOH 234 734 249 HOH HOH A . 
E 5 HOH 235 735 228 HOH HOH A . 
E 5 HOH 236 736 245 HOH HOH A . 
E 5 HOH 237 737 223 HOH HOH A . 
E 5 HOH 238 738 217 HOH HOH A . 
E 5 HOH 239 739 293 HOH HOH A . 
E 5 HOH 240 740 30  HOH HOH A . 
E 5 HOH 241 741 128 HOH HOH A . 
E 5 HOH 242 742 44  HOH HOH A . 
E 5 HOH 243 743 141 HOH HOH A . 
E 5 HOH 244 744 273 HOH HOH A . 
E 5 HOH 245 745 218 HOH HOH A . 
E 5 HOH 246 746 220 HOH HOH A . 
E 5 HOH 247 747 235 HOH HOH A . 
E 5 HOH 248 748 94  HOH HOH A . 
E 5 HOH 249 749 285 HOH HOH A . 
E 5 HOH 250 750 282 HOH HOH A . 
E 5 HOH 251 751 254 HOH HOH A . 
E 5 HOH 252 752 153 HOH HOH A . 
E 5 HOH 253 753 237 HOH HOH A . 
E 5 HOH 254 754 277 HOH HOH A . 
E 5 HOH 255 755 214 HOH HOH A . 
E 5 HOH 256 756 167 HOH HOH A . 
E 5 HOH 257 757 268 HOH HOH A . 
E 5 HOH 258 758 255 HOH HOH A . 
E 5 HOH 259 759 177 HOH HOH A . 
E 5 HOH 260 760 198 HOH HOH A . 
E 5 HOH 261 761 129 HOH HOH A . 
E 5 HOH 262 762 222 HOH HOH A . 
E 5 HOH 263 763 246 HOH HOH A . 
E 5 HOH 264 764 158 HOH HOH A . 
E 5 HOH 265 765 144 HOH HOH A . 
E 5 HOH 266 766 269 HOH HOH A . 
E 5 HOH 267 767 182 HOH HOH A . 
E 5 HOH 268 768 184 HOH HOH A . 
E 5 HOH 269 769 284 HOH HOH A . 
E 5 HOH 270 770 200 HOH HOH A . 
E 5 HOH 271 771 231 HOH HOH A . 
E 5 HOH 272 772 159 HOH HOH A . 
E 5 HOH 273 773 163 HOH HOH A . 
E 5 HOH 274 774 91  HOH HOH A . 
E 5 HOH 275 775 190 HOH HOH A . 
E 5 HOH 276 776 156 HOH HOH A . 
E 5 HOH 277 777 274 HOH HOH A . 
E 5 HOH 278 778 164 HOH HOH A . 
E 5 HOH 279 779 243 HOH HOH A . 
E 5 HOH 280 780 227 HOH HOH A . 
E 5 HOH 281 781 104 HOH HOH A . 
E 5 HOH 282 782 202 HOH HOH A . 
E 5 HOH 283 783 286 HOH HOH A . 
E 5 HOH 284 784 279 HOH HOH A . 
E 5 HOH 285 785 185 HOH HOH A . 
E 5 HOH 286 786 204 HOH HOH A . 
E 5 HOH 287 787 295 HOH HOH A . 
E 5 HOH 288 788 281 HOH HOH A . 
E 5 HOH 289 789 241 HOH HOH A . 
E 5 HOH 290 790 152 HOH HOH A . 
E 5 HOH 291 791 210 HOH HOH A . 
E 5 HOH 292 792 114 HOH HOH A . 
E 5 HOH 293 793 304 HOH HOH A . 
E 5 HOH 294 794 263 HOH HOH A . 
E 5 HOH 295 795 261 HOH HOH A . 
E 5 HOH 296 796 100 HOH HOH A . 
E 5 HOH 297 797 301 HOH HOH A . 
E 5 HOH 298 798 287 HOH HOH A . 
E 5 HOH 299 799 178 HOH HOH A . 
E 5 HOH 300 800 307 HOH HOH A . 
E 5 HOH 301 801 79  HOH HOH A . 
E 5 HOH 302 802 256 HOH HOH A . 
E 5 HOH 303 803 216 HOH HOH A . 
E 5 HOH 304 804 72  HOH HOH A . 
E 5 HOH 305 805 288 HOH HOH A . 
E 5 HOH 306 806 309 HOH HOH A . 
E 5 HOH 307 807 211 HOH HOH A . 
E 5 HOH 308 808 272 HOH HOH A . 
E 5 HOH 309 809 251 HOH HOH A . 
E 5 HOH 310 810 292 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 GLN 29  ? CD  ? A GLN 23  CD  
2  1 Y 1 A GLN 29  ? OE1 ? A GLN 23  OE1 
3  1 Y 1 A GLN 29  ? NE2 ? A GLN 23  NE2 
4  1 Y 1 A ARG 78  ? NE  ? A ARG 72  NE  
5  1 Y 1 A ARG 78  ? CZ  ? A ARG 72  CZ  
6  1 Y 1 A ARG 78  ? NH1 ? A ARG 72  NH1 
7  1 Y 1 A ARG 78  ? NH2 ? A ARG 72  NH2 
8  1 Y 1 A LYS 88  ? CG  ? A LYS 82  CG  
9  1 Y 1 A LYS 88  ? CD  ? A LYS 82  CD  
10 1 Y 1 A LYS 88  ? CE  ? A LYS 82  CE  
11 1 Y 1 A LYS 88  ? NZ  ? A LYS 82  NZ  
12 1 Y 1 A GLU 121 ? CD  ? A GLU 115 CD  
13 1 Y 1 A GLU 121 ? OE1 ? A GLU 115 OE1 
14 1 Y 1 A GLU 121 ? OE2 ? A GLU 115 OE2 
15 1 Y 1 A ARG 137 ? CZ  ? A ARG 131 CZ  
16 1 Y 1 A ARG 137 ? NH1 ? A ARG 131 NH1 
17 1 Y 1 A ARG 137 ? NH2 ? A ARG 131 NH2 
18 1 Y 1 A LYS 182 ? CG  ? A LYS 176 CG  
19 1 Y 1 A LYS 182 ? CD  ? A LYS 176 CD  
20 1 Y 1 A LYS 182 ? CE  ? A LYS 176 CE  
21 1 Y 1 A LYS 182 ? NZ  ? A LYS 176 NZ  
22 1 Y 1 A GLU 213 ? CD  ? A GLU 207 CD  
23 1 Y 1 A GLU 213 ? OE1 ? A GLU 207 OE1 
24 1 Y 1 A GLU 213 ? OE2 ? A GLU 207 OE2 
25 1 Y 1 A GLU 214 ? CG  ? A GLU 208 CG  
26 1 Y 1 A GLU 214 ? CD  ? A GLU 208 CD  
27 1 Y 1 A GLU 214 ? OE1 ? A GLU 208 OE1 
28 1 Y 1 A GLU 214 ? OE2 ? A GLU 208 OE2 
29 1 Y 1 A GLU 219 ? CD  ? A GLU 213 CD  
30 1 Y 1 A GLU 219 ? OE1 ? A GLU 213 OE1 
31 1 Y 1 A GLU 219 ? OE2 ? A GLU 213 OE2 
32 1 Y 1 A GLU 222 ? OE1 ? A GLU 216 OE1 
33 1 Y 1 A GLU 222 ? OE2 ? A GLU 216 OE2 
34 1 Y 1 A LYS 225 ? CE  ? A LYS 219 CE  
35 1 Y 1 A LYS 225 ? NZ  ? A LYS 219 NZ  
36 1 Y 1 A LYS 230 ? CG  ? A LYS 224 CG  
37 1 Y 1 A LYS 230 ? CD  ? A LYS 224 CD  
38 1 Y 1 A LYS 230 ? CE  ? A LYS 224 CE  
39 1 Y 1 A LYS 230 ? NZ  ? A LYS 224 NZ  
40 1 Y 1 A LYS 246 ? CE  ? A LYS 240 CE  
41 1 Y 1 A LYS 246 ? NZ  ? A LYS 240 NZ  
42 1 Y 1 A ARG 253 ? CD  ? A ARG 247 CD  
43 1 Y 1 A ARG 253 ? NE  ? A ARG 247 NE  
44 1 Y 1 A ARG 253 ? CZ  ? A ARG 247 CZ  
45 1 Y 1 A ARG 253 ? NH1 ? A ARG 247 NH1 
46 1 Y 1 A ARG 253 ? NH2 ? A ARG 247 NH2 
47 1 Y 1 A LYS 254 ? CG  ? A LYS 248 CG  
48 1 Y 1 A LYS 254 ? CD  ? A LYS 248 CD  
49 1 Y 1 A LYS 254 ? CE  ? A LYS 248 CE  
50 1 Y 1 A LYS 254 ? NZ  ? A LYS 248 NZ  
51 1 Y 1 A GLU 257 ? CD  ? A GLU 251 CD  
52 1 Y 1 A GLU 257 ? OE1 ? A GLU 251 OE1 
53 1 Y 1 A GLU 257 ? OE2 ? A GLU 251 OE2 
54 1 Y 1 A VAL 289 ? CG1 ? A VAL 283 CG1 
55 1 Y 1 A VAL 289 ? CG2 ? A VAL 283 CG2 
56 1 Y 1 A ARG 290 ? CG  ? A ARG 284 CG  
57 1 Y 1 A ARG 290 ? CD  ? A ARG 284 CD  
58 1 Y 1 A ARG 290 ? NE  ? A ARG 284 NE  
59 1 Y 1 A ARG 290 ? CZ  ? A ARG 284 CZ  
60 1 Y 1 A ARG 290 ? NH1 ? A ARG 284 NH1 
61 1 Y 1 A ARG 290 ? NH2 ? A ARG 284 NH2 
62 1 Y 1 A THR 291 ? OG1 ? A THR 285 OG1 
63 1 Y 1 A THR 291 ? CG2 ? A THR 285 CG2 
64 1 Y 1 A LYS 293 ? CE  ? A LYS 287 CE  
65 1 Y 1 A LYS 293 ? NZ  ? A LYS 287 NZ  
66 1 Y 1 A ARG 316 ? CD  ? A ARG 310 CD  
67 1 Y 1 A ARG 316 ? NE  ? A ARG 310 NE  
68 1 Y 1 A ARG 316 ? CZ  ? A ARG 310 CZ  
69 1 Y 1 A ARG 316 ? NH1 ? A ARG 310 NH1 
70 1 Y 1 A ARG 316 ? NH2 ? A ARG 310 NH2 
71 1 Y 1 A ASP 358 ? CG  ? A ASP 352 CG  
72 1 Y 1 A ASP 358 ? OD1 ? A ASP 352 OD1 
73 1 Y 1 A ASP 358 ? OD2 ? A ASP 352 OD2 
74 1 Y 1 A LYS 366 ? CD  ? A LYS 360 CD  
75 1 Y 1 A LYS 366 ? CE  ? A LYS 360 CE  
76 1 Y 1 A LYS 366 ? NZ  ? A LYS 360 NZ  
77 1 Y 1 A ARG 369 ? CZ  ? A ARG 363 CZ  
78 1 Y 1 A ARG 369 ? NH1 ? A ARG 363 NH1 
79 1 Y 1 A ARG 369 ? NH2 ? A ARG 363 NH2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? '(1.20.1_4487: ???)' 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? HKL-3000 ? ? ? .                    2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? HKL-3000 ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  120.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8YOQ 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     60.302 
_cell.length_a_esd                 ? 
_cell.length_b                     60.302 
_cell.length_b_esd                 ? 
_cell.length_c                     194.721 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        6 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         8YOQ 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                154 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 32 2 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8YOQ 
_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             2.55 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          51.82 
_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, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              7.7 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.1 M Sodium chloride, 0.12 M Lithium sulfate, 0.1 M Sodium HEPES, 16.5% PEG 6000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291.15 
# 
_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         2021-10-04 
_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   0.987 
_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 BL17U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.987 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL17U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          17.50 
_reflns.entry_id                                       8YOQ 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.78 
_reflns.d_resolution_low                               46.021 
_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                                     40126 
_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                           94.33 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                18.9 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          19.6 
_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                                0.301 
_reflns.pdbx_Rpim_I_all                                0.069 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.997 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_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                                    1.80 
_reflns_shell.d_res_low                                     1.806 
_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                             3915 
_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                                  0.704 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 8YOQ 
_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                            1.79 
_refine.ls_d_res_low                             32.45 
_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                     37747 
_refine.ls_number_reflns_R_free                  1963 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    94.33 
_refine.ls_percent_reflns_R_free                 5.20 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1957 
_refine.ls_R_factor_R_free                       0.2187 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1944 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.35 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      8YOX 
_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                 22.20 
_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                            0.18 
_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                       1.79 
_refine_hist.d_res_low                        32.45 
_refine_hist.number_atoms_solvent             310 
_refine_hist.number_atoms_total               3151 
_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        2734 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         107 
_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' ? 0.008  ? ?    ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.927  ? ?    ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 13.605 ? 1050 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.055  ? 461  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.006  ? 495  ? 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' 1.79 1.83 . . 89  1383 52.00  . . . . 0.21   . . . . . . . . . . . 0.2359 
'X-RAY DIFFRACTION' 1.83 1.88 . . 109 1909 72.00  . . . . 0.2412 . . . . . . . . . . . 0.2731 
'X-RAY DIFFRACTION' 1.88 1.94 . . 140 2541 96.00  . . . . 0.2532 . . . . . . . . . . . 0.3050 
'X-RAY DIFFRACTION' 1.94 2.00 . . 152 2657 100.00 . . . . 0.2291 . . . . . . . . . . . 0.2663 
'X-RAY DIFFRACTION' 2.00 2.07 . . 128 2693 100.00 . . . . 0.2240 . . . . . . . . . . . 0.2392 
'X-RAY DIFFRACTION' 2.07 2.15 . . 160 2668 100.00 . . . . 0.2100 . . . . . . . . . . . 0.2464 
'X-RAY DIFFRACTION' 2.15 2.25 . . 145 2659 100.00 . . . . 0.2146 . . . . . . . . . . . 0.2526 
'X-RAY DIFFRACTION' 2.25 2.37 . . 140 2686 100.00 . . . . 0.2033 . . . . . . . . . . . 0.2522 
'X-RAY DIFFRACTION' 2.37 2.52 . . 153 2708 100.00 . . . . 0.2040 . . . . . . . . . . . 0.2214 
'X-RAY DIFFRACTION' 2.52 2.71 . . 165 2679 100.00 . . . . 0.1919 . . . . . . . . . . . 0.2353 
'X-RAY DIFFRACTION' 2.71 2.98 . . 125 2745 100.00 . . . . 0.1995 . . . . . . . . . . . 0.2035 
'X-RAY DIFFRACTION' 2.98 3.42 . . 158 2726 100.00 . . . . 0.1843 . . . . . . . . . . . 0.2233 
'X-RAY DIFFRACTION' 3.42 4.30 . . 142 2802 100.00 . . . . 0.1665 . . . . . . . . . . . 0.1720 
# 
_struct.entry_id                     8YOQ 
_struct.title                        'Crystal structure of hFSP1 with both 6-OH-FAD and NADP (hFSP1-6-OH-FAD-NADP)' 
_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        8YOQ 
_struct_keywords.text            'Flavoprotein, 6-OH-FAD, Redox, NADP, OXIDOREDUCTASE' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
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 3 ? 
D N N 4 ? 
E N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    FSP1_HUMAN 
_struct_ref.pdbx_db_accession          Q9BRQ8 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;GALHVVIVGGGFGGIAAASQLQALNVPFMLVDMKDSFHHNVAALRASVETGFAKKTFISYSVTFKDNFRQGLVVGIDLKN
QMVLLQGGEALPFSHLILATGSTGPFPGKFNEVSSQQAAIQAYEDMVRQVQRSRFIVVVGGGSAGVEMAAEIKTEYPEKE
VTLIHSQVALADKELLPSVRQEVKEILLRKGVQLLLSERVSNLEELPLNEYREYIKVQTDKGTEVATNLVILCTGIKINS
SAYRKAFESRLASSGALRVNEHLQVEGHSNVYAIGDCADVRTPKMAYLAGLHANIAVANIVNSVKQRPLQAYKPGALTFL
LSMGRNDGVGQISGFYVGRLMVRLTKSRDLFVSTSWKTMRQSPP
;
_struct_ref.pdbx_align_begin           10 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              8YOQ 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 4 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 367 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q9BRQ8 
_struct_ref_seq.db_align_beg                  10 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  373 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       10 
_struct_ref_seq.pdbx_auth_seq_align_end       373 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 8YOQ PRO A 1 ? UNP Q9BRQ8 ? ? 'expression tag'        7 1 
1 8YOQ HIS A 2 ? UNP Q9BRQ8 ? ? 'expression tag'        8 2 
1 8YOQ MET A 3 ? UNP Q9BRQ8 ? ? 'initiating methionine' 9 3 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly   ?    monomeric 1 
2 software_defined_assembly PISA dimeric   2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
2 'ABSA (A^2)' 6870  ? 
2 MORE         -51   ? 
2 'SSA (A^2)'  28480 ? 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1   A,B,C,D,E 
2 1,2 A,B,C,D,E 
# 
_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                ? 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z  1.0000000000  0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000  0.0000000000 
2 'crystal symmetry operation' 4_555 y,x,-z -0.5000000000 0.8660254038 0.0000000000 0.0000000000 0.8660254038 0.5000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 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 GLY A 14  ? ASN A 28  ? GLY A 20  ASN A 34  1 ? 15 
HELX_P HELX_P2  AA2 ASN A 43  ? ALA A 46  ? ASN A 49  ALA A 52  5 ? 4  
HELX_P HELX_P3  AA3 LEU A 47  ? VAL A 51  ? LEU A 53  VAL A 57  5 ? 5  
HELX_P HELX_P4  AA4 PHE A 55  ? LYS A 58  ? PHE A 61  LYS A 64  5 ? 4  
HELX_P HELX_P5  AA5 TYR A 63  ? LYS A 68  ? TYR A 69  LYS A 74  1 ? 6  
HELX_P HELX_P6  AA6 SER A 118 ? SER A 136 ? SER A 124 SER A 142 1 ? 19 
HELX_P HELX_P7  AA7 GLY A 145 ? TYR A 159 ? GLY A 151 TYR A 165 1 ? 15 
HELX_P HELX_P8  AA8 LEU A 179 ? GLY A 194 ? LEU A 185 GLY A 200 1 ? 16 
HELX_P HELX_P9  AA9 ASN A 205 ? LEU A 209 ? ASN A 211 LEU A 215 5 ? 5  
HELX_P HELX_P10 AB1 PHE A 250 ? LEU A 254 ? PHE A 256 LEU A 260 5 ? 5  
HELX_P HELX_P11 AB2 GLY A 278 ? ALA A 281 ? GLY A 284 ALA A 287 5 ? 4  
HELX_P HELX_P12 AB3 MET A 288 ? LYS A 308 ? MET A 294 LYS A 314 1 ? 21 
HELX_P HELX_P13 AB4 GLY A 341 ? LYS A 349 ? GLY A 347 LYS A 355 1 ? 9  
HELX_P HELX_P14 AB5 PHE A 354 ? MET A 362 ? PHE A 360 MET A 368 1 ? 9  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          PHE 
_struct_mon_prot_cis.label_seq_id           109 
_struct_mon_prot_cis.label_asym_id          A 
_struct_mon_prot_cis.label_alt_id           . 
_struct_mon_prot_cis.pdbx_PDB_ins_code      ? 
_struct_mon_prot_cis.auth_comp_id           PHE 
_struct_mon_prot_cis.auth_seq_id            115 
_struct_mon_prot_cis.auth_asym_id           A 
_struct_mon_prot_cis.pdbx_label_comp_id_2   PRO 
_struct_mon_prot_cis.pdbx_label_seq_id_2    110 
_struct_mon_prot_cis.pdbx_label_asym_id_2   A 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2    ? 
_struct_mon_prot_cis.pdbx_auth_comp_id_2    PRO 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     116 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    A 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       6.02 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 2 ? 
AA3 ? 3 ? 
AA4 ? 2 ? 
AA5 ? 4 ? 
AA6 ? 2 ? 
AA7 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel      
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA1 4 5 ? parallel      
AA2 1 2 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA5 1 2 ? parallel      
AA5 2 3 ? parallel      
AA5 3 4 ? parallel      
AA6 1 2 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA7 2 3 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 PHE A 71  ? GLN A 73  ? PHE A 77  GLN A 79  
AA1 2 PHE A 31  ? ASP A 35  ? PHE A 37  ASP A 41  
AA1 3 VAL A 8   ? VAL A 11  ? VAL A 14  VAL A 17  
AA1 4 HIS A 98  ? LEU A 101 ? HIS A 104 LEU A 107 
AA1 5 VAL A 274 ? ALA A 276 ? VAL A 280 ALA A 282 
AA2 1 SER A 39  ? HIS A 41  ? SER A 45  HIS A 47  
AA2 2 PHE A 60  ? SER A 62  ? PHE A 66  SER A 68  
AA3 1 VAL A 76  ? ASP A 80  ? VAL A 82  ASP A 86  
AA3 2 MET A 85  ? LEU A 88  ? MET A 91  LEU A 94  
AA3 3 ALA A 93  ? PRO A 95  ? ALA A 99  PRO A 101 
AA4 1 SER A 105 ? THR A 106 ? SER A 111 THR A 112 
AA4 2 LYS A 240 ? ILE A 241 ? LYS A 246 ILE A 247 
AA5 1 GLN A 196 ? LEU A 198 ? GLN A 202 LEU A 204 
AA5 2 GLU A 163 ? ILE A 167 ? GLU A 169 ILE A 173 
AA5 3 PHE A 138 ? VAL A 142 ? PHE A 144 VAL A 148 
AA5 4 LEU A 232 ? LEU A 235 ? LEU A 238 LEU A 241 
AA6 1 ILE A 218 ? GLN A 221 ? ILE A 224 GLN A 227 
AA6 2 GLU A 227 ? THR A 230 ? GLU A 233 THR A 236 
AA7 1 PHE A 322 ? SER A 325 ? PHE A 328 SER A 331 
AA7 2 GLY A 331 ? ILE A 335 ? GLY A 337 ILE A 341 
AA7 3 PHE A 338 ? VAL A 340 ? PHE A 344 VAL A 346 
# 
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 ARG A 72  ? O ARG A 78  N LEU A 33  ? N LEU A 39  
AA1 2 3 O VAL A 34  ? O VAL A 40  N ILE A 10  ? N ILE A 16  
AA1 3 4 N VAL A 9   ? N VAL A 15  O ILE A 100 ? O ILE A 106 
AA1 4 5 N LEU A 101 ? N LEU A 107 O TYR A 275 ? O TYR A 281 
AA2 1 2 N PHE A 40  ? N PHE A 46  O ILE A 61  ? O ILE A 67  
AA3 1 2 N ASP A 80  ? N ASP A 86  O MET A 85  ? O MET A 91  
AA3 2 3 N VAL A 86  ? N VAL A 92  O LEU A 94  ? O LEU A 100 
AA4 1 2 N THR A 106 ? N THR A 112 O LYS A 240 ? O LYS A 246 
AA5 1 2 O GLN A 196 ? O GLN A 202 N VAL A 164 ? N VAL A 170 
AA5 2 3 O THR A 165 ? O THR A 171 N VAL A 141 ? N VAL A 147 
AA5 3 4 N VAL A 142 ? N VAL A 148 O ILE A 234 ? O ILE A 240 
AA6 1 2 N VAL A 220 ? N VAL A 226 O VAL A 228 ? O VAL A 234 
AA7 1 2 N PHE A 322 ? N PHE A 328 O GLN A 334 ? O GLN A 340 
AA7 2 3 N GLY A 333 ? N GLY A 339 O VAL A 340 ? O VAL A 346 
# 
_pdbx_entry_details.entry_id                   8YOQ 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1  1 O   A HOH 772 ? ? O A HOH 810 ? ? 1.85 
2  1 O   A GLU 275 ? ? O A HOH 501 ? ? 1.85 
3  1 O   A HOH 717 ? ? O A HOH 736 ? ? 1.94 
4  1 O   A HOH 701 ? ? O A HOH 715 ? ? 1.99 
5  1 O   A SER 312 ? ? O A HOH 502 ? ? 2.00 
6  1 O   A HOH 570 ? ? O A HOH 690 ? ? 2.02 
7  1 OE1 A GLN 315 ? ? O A HOH 502 ? ? 2.03 
8  1 OG  A SER 278 ? ? O A HOH 503 ? ? 2.07 
9  1 O   A GLN 273 ? ? O A HOH 504 ? ? 2.09 
10 1 O   A HOH 504 ? ? O A HOH 673 ? ? 2.10 
11 1 O   A HOH 796 ? ? O A HOH 808 ? ? 2.10 
12 1 OD1 A ASP 181 ? ? O A HOH 505 ? ? 2.12 
13 1 N   A LYS 254 ? ? O A HOH 506 ? ? 2.15 
14 1 ND1 A HIS 8   ? ? O A HOH 507 ? ? 2.19 
15 1 O   A HOH 753 ? ? O A HOH 800 ? ? 2.19 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    O 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    HOH 
_pdbx_validate_symm_contact.auth_seq_id_1     722 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    O 
_pdbx_validate_symm_contact.auth_asym_id_2    A 
_pdbx_validate_symm_contact.auth_comp_id_2    HOH 
_pdbx_validate_symm_contact.auth_seq_id_2     771 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   4_555 
_pdbx_validate_symm_contact.dist              2.10 
# 
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 LYS A 74  ? ? 56.76   -128.44 
2 1 ALA A 108 ? ? -143.92 53.05   
3 1 ALA A 180 ? ? 60.16   -171.97 
4 1 SER A 263 ? ? -57.20  -9.28   
5 1 ARG A 290 ? ? 68.05   -10.65  
6 1 SER A 342 ? ? 30.90   60.37   
# 
loop_
_pdbx_struct_special_symmetry.id 
_pdbx_struct_special_symmetry.PDB_model_num 
_pdbx_struct_special_symmetry.auth_asym_id 
_pdbx_struct_special_symmetry.auth_comp_id 
_pdbx_struct_special_symmetry.auth_seq_id 
_pdbx_struct_special_symmetry.PDB_ins_code 
_pdbx_struct_special_symmetry.label_asym_id 
_pdbx_struct_special_symmetry.label_comp_id 
_pdbx_struct_special_symmetry.label_seq_id 
1 1 A HOH 534 ? E HOH . 
2 1 A HOH 746 ? E HOH . 
3 1 A HOH 781 ? E HOH . 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z          
2 -y,x-y,z+2/3   
3 -x+y,-x,z+1/3  
4 x-y,-y,-z+1/3  
5 -x,-x+y,-z+2/3 
6 y,x,-z         
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1 'X-RAY DIFFRACTION' ? refined -29.7051 -16.7750 18.0635 0.1058 ? -0.0183 ? 0.0075  ? 0.1422 ? 0.0473 ? 0.1198 ? 0.0083 ? -0.0314 
? -0.0197 ? 0.1158 ? -0.0278 ? 0.0247 ? 0.0433 ? 0.0262  ? 0.0319  ? 0.0632 ? 0.0456  ? 0.1172  ? -0.0373 ? -0.1794 ? -0.0000 ? 
2 'X-RAY DIFFRACTION' ? refined -10.2226 1.6901   11.3047 0.1553 ? -0.0063 ? -0.0218 ? 0.0541 ? 0.0056 ? 0.1471 ? 0.0231 ? -0.0030 
? -0.0139 ? 0.0124 ? 0.0035  ? 0.0183 ? 0.0650 ? 0.0007  ? 0.0725  ? 0.0529 ? -0.0562 ? -0.0640 ? -0.1154 ? -0.0353 ? -0.0006 ? 
3 'X-RAY DIFFRACTION' ? refined -24.9103 -4.3668  23.5976 0.3884 ? -0.0615 ? 0.0290  ? 0.0156 ? 0.0850 ? 0.0577 ? 0.1719 ? -0.0535 
? 0.0418  ? 0.0248 ? -0.0009 ? 0.0183 ? 0.1130 ? -0.0669 ? 0.1001  ? 0.2263 ? -0.1802 ? 0.0398  ? 0.0088  ? -0.0405 ? -0.1360 ? 
4 'X-RAY DIFFRACTION' ? refined -13.9859 -20.4170 22.7135 0.1390 ? -0.0561 ? -0.0889 ? 0.1402 ? 0.0586 ? 0.0962 ? 0.0739 ? -0.1134 
? 0.0437  ? 0.2151 ? -0.0760 ? 0.0582 ? 0.1132 ? -0.0273 ? -0.0932 ? 0.0460 ? -0.0871 ? -0.1765 ? 0.1146  ? 0.0220  ? 0.0252  ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 7 through 164 )
;
2 'X-RAY DIFFRACTION' 2 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 165 through 214 )
;
3 'X-RAY DIFFRACTION' 3 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 215 through 294 )
;
4 'X-RAY DIFFRACTION' 4 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 295 through 373 )
;
# 
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 
6FA N1     N N N 1   
6FA C2     C N N 2   
6FA O2     O N N 3   
6FA N3     N N N 4   
6FA C4     C N N 5   
6FA O4     O N N 6   
6FA C4A    C N N 7   
6FA N5     N N N 8   
6FA C5A    C Y N 9   
6FA C6     C Y N 10  
6FA O6     O N N 11  
6FA C7     C Y N 12  
6FA C7M    C N N 13  
6FA C8     C Y N 14  
6FA C8M    C N N 15  
6FA C9     C Y N 16  
6FA C9A    C Y N 17  
6FA N10    N N N 18  
6FA C10    C N N 19  
6FA "C1'"  C N N 20  
6FA "C2'"  C N S 21  
6FA "O2'"  O N N 22  
6FA "C3'"  C N S 23  
6FA "O3'"  O N N 24  
6FA "C4'"  C N R 25  
6FA "O4'"  O N N 26  
6FA "C5'"  C N N 27  
6FA "O5'"  O N N 28  
6FA P      P N R 29  
6FA O1P    O N N 30  
6FA O2P    O N N 31  
6FA O3P    O N N 32  
6FA PA     P N S 33  
6FA O1A    O N N 34  
6FA O2A    O N N 35  
6FA O5B    O N N 36  
6FA C5B    C N N 37  
6FA C4B    C N R 38  
6FA O4B    O N N 39  
6FA C3B    C N S 40  
6FA O3B    O N N 41  
6FA C2B    C N R 42  
6FA O2B    O N N 43  
6FA C1B    C N R 44  
6FA N9A    N Y N 45  
6FA C8A    C Y N 46  
6FA N7A    N Y N 47  
6FA C5X    C Y N 48  
6FA C6A    C Y N 49  
6FA N6A    N N N 50  
6FA N1A    N Y N 51  
6FA C2A    C Y N 52  
6FA N3A    N Y N 53  
6FA C4X    C Y N 54  
6FA HN3    H N N 55  
6FA HO6    H N N 56  
6FA HM71   H N N 57  
6FA HM72   H N N 58  
6FA HM73   H N N 59  
6FA HM81   H N N 60  
6FA HM82   H N N 61  
6FA HM83   H N N 62  
6FA H9     H N N 63  
6FA "H1'1" H N N 64  
6FA "H1'2" H N N 65  
6FA "H2'"  H N N 66  
6FA "HO2'" H N N 67  
6FA "H3'"  H N N 68  
6FA "HO3'" H N N 69  
6FA "H4'"  H N N 70  
6FA "HO4'" H N N 71  
6FA "H5'1" H N N 72  
6FA "H5'2" H N N 73  
6FA HOP2   H N N 74  
6FA HOA2   H N N 75  
6FA H51A   H N N 76  
6FA H52A   H N N 77  
6FA H4B    H N N 78  
6FA H3B    H N N 79  
6FA HO3A   H N N 80  
6FA H2B    H N N 81  
6FA HO2A   H N N 82  
6FA H1B    H N N 83  
6FA H8A    H N N 84  
6FA H61A   H N N 85  
6FA H62A   H N N 86  
6FA H2A    H N N 87  
ALA N      N N N 88  
ALA CA     C N S 89  
ALA C      C N N 90  
ALA O      O N N 91  
ALA CB     C N N 92  
ALA OXT    O N N 93  
ALA H      H N N 94  
ALA H2     H N N 95  
ALA HA     H N N 96  
ALA HB1    H N N 97  
ALA HB2    H N N 98  
ALA HB3    H N N 99  
ALA HXT    H N N 100 
ARG N      N N N 101 
ARG CA     C N S 102 
ARG C      C N N 103 
ARG O      O N N 104 
ARG CB     C N N 105 
ARG CG     C N N 106 
ARG CD     C N N 107 
ARG NE     N N N 108 
ARG CZ     C N N 109 
ARG NH1    N N N 110 
ARG NH2    N N N 111 
ARG OXT    O N N 112 
ARG H      H N N 113 
ARG H2     H N N 114 
ARG HA     H N N 115 
ARG HB2    H N N 116 
ARG HB3    H N N 117 
ARG HG2    H N N 118 
ARG HG3    H N N 119 
ARG HD2    H N N 120 
ARG HD3    H N N 121 
ARG HE     H N N 122 
ARG HH11   H N N 123 
ARG HH12   H N N 124 
ARG HH21   H N N 125 
ARG HH22   H N N 126 
ARG HXT    H N N 127 
ASN N      N N N 128 
ASN CA     C N S 129 
ASN C      C N N 130 
ASN O      O N N 131 
ASN CB     C N N 132 
ASN CG     C N N 133 
ASN OD1    O N N 134 
ASN ND2    N N N 135 
ASN OXT    O N N 136 
ASN H      H N N 137 
ASN H2     H N N 138 
ASN HA     H N N 139 
ASN HB2    H N N 140 
ASN HB3    H N N 141 
ASN HD21   H N N 142 
ASN HD22   H N N 143 
ASN HXT    H N N 144 
ASP N      N N N 145 
ASP CA     C N S 146 
ASP C      C N N 147 
ASP O      O N N 148 
ASP CB     C N N 149 
ASP CG     C N N 150 
ASP OD1    O N N 151 
ASP OD2    O N N 152 
ASP OXT    O N N 153 
ASP H      H N N 154 
ASP H2     H N N 155 
ASP HA     H N N 156 
ASP HB2    H N N 157 
ASP HB3    H N N 158 
ASP HD2    H N N 159 
ASP HXT    H N N 160 
CYS N      N N N 161 
CYS CA     C N R 162 
CYS C      C N N 163 
CYS O      O N N 164 
CYS CB     C N N 165 
CYS SG     S N N 166 
CYS OXT    O N N 167 
CYS H      H N N 168 
CYS H2     H N N 169 
CYS HA     H N N 170 
CYS HB2    H N N 171 
CYS HB3    H N N 172 
CYS HG     H N N 173 
CYS HXT    H N N 174 
GLN N      N N N 175 
GLN CA     C N S 176 
GLN C      C N N 177 
GLN O      O N N 178 
GLN CB     C N N 179 
GLN CG     C N N 180 
GLN CD     C N N 181 
GLN OE1    O N N 182 
GLN NE2    N N N 183 
GLN OXT    O N N 184 
GLN H      H N N 185 
GLN H2     H N N 186 
GLN HA     H N N 187 
GLN HB2    H N N 188 
GLN HB3    H N N 189 
GLN HG2    H N N 190 
GLN HG3    H N N 191 
GLN HE21   H N N 192 
GLN HE22   H N N 193 
GLN HXT    H N N 194 
GLU N      N N N 195 
GLU CA     C N S 196 
GLU C      C N N 197 
GLU O      O N N 198 
GLU CB     C N N 199 
GLU CG     C N N 200 
GLU CD     C N N 201 
GLU OE1    O N N 202 
GLU OE2    O N N 203 
GLU OXT    O N N 204 
GLU H      H N N 205 
GLU H2     H N N 206 
GLU HA     H N N 207 
GLU HB2    H N N 208 
GLU HB3    H N N 209 
GLU HG2    H N N 210 
GLU HG3    H N N 211 
GLU HE2    H N N 212 
GLU HXT    H N N 213 
GLY N      N N N 214 
GLY CA     C N N 215 
GLY C      C N N 216 
GLY O      O N N 217 
GLY OXT    O N N 218 
GLY H      H N N 219 
GLY H2     H N N 220 
GLY HA2    H N N 221 
GLY HA3    H N N 222 
GLY HXT    H N N 223 
HIS N      N N N 224 
HIS CA     C N S 225 
HIS C      C N N 226 
HIS O      O N N 227 
HIS CB     C N N 228 
HIS CG     C Y N 229 
HIS ND1    N Y N 230 
HIS CD2    C Y N 231 
HIS CE1    C Y N 232 
HIS NE2    N Y N 233 
HIS OXT    O N N 234 
HIS H      H N N 235 
HIS H2     H N N 236 
HIS HA     H N N 237 
HIS HB2    H N N 238 
HIS HB3    H N N 239 
HIS HD1    H N N 240 
HIS HD2    H N N 241 
HIS HE1    H N N 242 
HIS HE2    H N N 243 
HIS HXT    H N N 244 
HOH O      O N N 245 
HOH H1     H N N 246 
HOH H2     H N N 247 
ILE N      N N N 248 
ILE CA     C N S 249 
ILE C      C N N 250 
ILE O      O N N 251 
ILE CB     C N S 252 
ILE CG1    C N N 253 
ILE CG2    C N N 254 
ILE CD1    C N N 255 
ILE OXT    O N N 256 
ILE H      H N N 257 
ILE H2     H N N 258 
ILE HA     H N N 259 
ILE HB     H N N 260 
ILE HG12   H N N 261 
ILE HG13   H N N 262 
ILE HG21   H N N 263 
ILE HG22   H N N 264 
ILE HG23   H N N 265 
ILE HD11   H N N 266 
ILE HD12   H N N 267 
ILE HD13   H N N 268 
ILE HXT    H N N 269 
LEU N      N N N 270 
LEU CA     C N S 271 
LEU C      C N N 272 
LEU O      O N N 273 
LEU CB     C N N 274 
LEU CG     C N N 275 
LEU CD1    C N N 276 
LEU CD2    C N N 277 
LEU OXT    O N N 278 
LEU H      H N N 279 
LEU H2     H N N 280 
LEU HA     H N N 281 
LEU HB2    H N N 282 
LEU HB3    H N N 283 
LEU HG     H N N 284 
LEU HD11   H N N 285 
LEU HD12   H N N 286 
LEU HD13   H N N 287 
LEU HD21   H N N 288 
LEU HD22   H N N 289 
LEU HD23   H N N 290 
LEU HXT    H N N 291 
LYS N      N N N 292 
LYS CA     C N S 293 
LYS C      C N N 294 
LYS O      O N N 295 
LYS CB     C N N 296 
LYS CG     C N N 297 
LYS CD     C N N 298 
LYS CE     C N N 299 
LYS NZ     N N N 300 
LYS OXT    O N N 301 
LYS H      H N N 302 
LYS H2     H N N 303 
LYS HA     H N N 304 
LYS HB2    H N N 305 
LYS HB3    H N N 306 
LYS HG2    H N N 307 
LYS HG3    H N N 308 
LYS HD2    H N N 309 
LYS HD3    H N N 310 
LYS HE2    H N N 311 
LYS HE3    H N N 312 
LYS HZ1    H N N 313 
LYS HZ2    H N N 314 
LYS HZ3    H N N 315 
LYS HXT    H N N 316 
MET N      N N N 317 
MET CA     C N S 318 
MET C      C N N 319 
MET O      O N N 320 
MET CB     C N N 321 
MET CG     C N N 322 
MET SD     S N N 323 
MET CE     C N N 324 
MET OXT    O N N 325 
MET H      H N N 326 
MET H2     H N N 327 
MET HA     H N N 328 
MET HB2    H N N 329 
MET HB3    H N N 330 
MET HG2    H N N 331 
MET HG3    H N N 332 
MET HE1    H N N 333 
MET HE2    H N N 334 
MET HE3    H N N 335 
MET HXT    H N N 336 
NDP PA     P N S 337 
NDP O1A    O N N 338 
NDP O2A    O N N 339 
NDP O5B    O N N 340 
NDP C5B    C N N 341 
NDP C4B    C N R 342 
NDP O4B    O N N 343 
NDP C3B    C N R 344 
NDP O3B    O N N 345 
NDP C2B    C N R 346 
NDP O2B    O N N 347 
NDP C1B    C N R 348 
NDP N9A    N Y N 349 
NDP C8A    C Y N 350 
NDP N7A    N Y N 351 
NDP C5A    C Y N 352 
NDP C6A    C Y N 353 
NDP N6A    N N N 354 
NDP N1A    N Y N 355 
NDP C2A    C Y N 356 
NDP N3A    N Y N 357 
NDP C4A    C Y N 358 
NDP O3     O N N 359 
NDP PN     P N S 360 
NDP O1N    O N N 361 
NDP O2N    O N N 362 
NDP O5D    O N N 363 
NDP C5D    C N N 364 
NDP C4D    C N R 365 
NDP O4D    O N N 366 
NDP C3D    C N S 367 
NDP O3D    O N N 368 
NDP C2D    C N R 369 
NDP O2D    O N N 370 
NDP C1D    C N R 371 
NDP N1N    N N N 372 
NDP C2N    C N N 373 
NDP C3N    C N N 374 
NDP C7N    C N N 375 
NDP O7N    O N N 376 
NDP N7N    N N N 377 
NDP C4N    C N N 378 
NDP C5N    C N N 379 
NDP C6N    C N N 380 
NDP P2B    P N N 381 
NDP O1X    O N N 382 
NDP O2X    O N N 383 
NDP O3X    O N N 384 
NDP HOA2   H N N 385 
NDP H51A   H N N 386 
NDP H52A   H N N 387 
NDP H4B    H N N 388 
NDP H3B    H N N 389 
NDP HO3A   H N N 390 
NDP H2B    H N N 391 
NDP H1B    H N N 392 
NDP H8A    H N N 393 
NDP H61A   H N N 394 
NDP H62A   H N N 395 
NDP H2A    H N N 396 
NDP H21N   H N N 397 
NDP H51N   H N N 398 
NDP H52N   H N N 399 
NDP H4D    H N N 400 
NDP H3D    H N N 401 
NDP HO3N   H N N 402 
NDP H2D    H N N 403 
NDP HO2N   H N N 404 
NDP H1D    H N N 405 
NDP H2N    H N N 406 
NDP H71N   H N N 407 
NDP H72N   H N N 408 
NDP H41N   H N N 409 
NDP H42N   H N N 410 
NDP H5N    H N N 411 
NDP H6N    H N N 412 
NDP HOP2   H N N 413 
NDP HOP3   H N N 414 
PHE N      N N N 415 
PHE CA     C N S 416 
PHE C      C N N 417 
PHE O      O N N 418 
PHE CB     C N N 419 
PHE CG     C Y N 420 
PHE CD1    C Y N 421 
PHE CD2    C Y N 422 
PHE CE1    C Y N 423 
PHE CE2    C Y N 424 
PHE CZ     C Y N 425 
PHE OXT    O N N 426 
PHE H      H N N 427 
PHE H2     H N N 428 
PHE HA     H N N 429 
PHE HB2    H N N 430 
PHE HB3    H N N 431 
PHE HD1    H N N 432 
PHE HD2    H N N 433 
PHE HE1    H N N 434 
PHE HE2    H N N 435 
PHE HZ     H N N 436 
PHE HXT    H N N 437 
PRO N      N N N 438 
PRO CA     C N S 439 
PRO C      C N N 440 
PRO O      O N N 441 
PRO CB     C N N 442 
PRO CG     C N N 443 
PRO CD     C N N 444 
PRO OXT    O N N 445 
PRO H      H N N 446 
PRO HA     H N N 447 
PRO HB2    H N N 448 
PRO HB3    H N N 449 
PRO HG2    H N N 450 
PRO HG3    H N N 451 
PRO HD2    H N N 452 
PRO HD3    H N N 453 
PRO HXT    H N N 454 
SER N      N N N 455 
SER CA     C N S 456 
SER C      C N N 457 
SER O      O N N 458 
SER CB     C N N 459 
SER OG     O N N 460 
SER OXT    O N N 461 
SER H      H N N 462 
SER H2     H N N 463 
SER HA     H N N 464 
SER HB2    H N N 465 
SER HB3    H N N 466 
SER HG     H N N 467 
SER HXT    H N N 468 
SO4 S      S N N 469 
SO4 O1     O N N 470 
SO4 O2     O N N 471 
SO4 O3     O N N 472 
SO4 O4     O N N 473 
THR N      N N N 474 
THR CA     C N S 475 
THR C      C N N 476 
THR O      O N N 477 
THR CB     C N R 478 
THR OG1    O N N 479 
THR CG2    C N N 480 
THR OXT    O N N 481 
THR H      H N N 482 
THR H2     H N N 483 
THR HA     H N N 484 
THR HB     H N N 485 
THR HG1    H N N 486 
THR HG21   H N N 487 
THR HG22   H N N 488 
THR HG23   H N N 489 
THR HXT    H N N 490 
TRP N      N N N 491 
TRP CA     C N S 492 
TRP C      C N N 493 
TRP O      O N N 494 
TRP CB     C N N 495 
TRP CG     C Y N 496 
TRP CD1    C Y N 497 
TRP CD2    C Y N 498 
TRP NE1    N Y N 499 
TRP CE2    C Y N 500 
TRP CE3    C Y N 501 
TRP CZ2    C Y N 502 
TRP CZ3    C Y N 503 
TRP CH2    C Y N 504 
TRP OXT    O N N 505 
TRP H      H N N 506 
TRP H2     H N N 507 
TRP HA     H N N 508 
TRP HB2    H N N 509 
TRP HB3    H N N 510 
TRP HD1    H N N 511 
TRP HE1    H N N 512 
TRP HE3    H N N 513 
TRP HZ2    H N N 514 
TRP HZ3    H N N 515 
TRP HH2    H N N 516 
TRP HXT    H N N 517 
TYR N      N N N 518 
TYR CA     C N S 519 
TYR C      C N N 520 
TYR O      O N N 521 
TYR CB     C N N 522 
TYR CG     C Y N 523 
TYR CD1    C Y N 524 
TYR CD2    C Y N 525 
TYR CE1    C Y N 526 
TYR CE2    C Y N 527 
TYR CZ     C Y N 528 
TYR OH     O N N 529 
TYR OXT    O N N 530 
TYR H      H N N 531 
TYR H2     H N N 532 
TYR HA     H N N 533 
TYR HB2    H N N 534 
TYR HB3    H N N 535 
TYR HD1    H N N 536 
TYR HD2    H N N 537 
TYR HE1    H N N 538 
TYR HE2    H N N 539 
TYR HH     H N N 540 
TYR HXT    H N N 541 
VAL N      N N N 542 
VAL CA     C N S 543 
VAL C      C N N 544 
VAL O      O N N 545 
VAL CB     C N N 546 
VAL CG1    C N N 547 
VAL CG2    C N N 548 
VAL OXT    O N N 549 
VAL H      H N N 550 
VAL H2     H N N 551 
VAL HA     H N N 552 
VAL HB     H N N 553 
VAL HG11   H N N 554 
VAL HG12   H N N 555 
VAL HG13   H N N 556 
VAL HG21   H N N 557 
VAL HG22   H N N 558 
VAL HG23   H N N 559 
VAL HXT    H N N 560 
# 
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 
6FA N1    C2     sing N N 1   
6FA N1    C10    doub N N 2   
6FA C2    O2     doub N N 3   
6FA C2    N3     sing N N 4   
6FA N3    C4     sing N N 5   
6FA N3    HN3    sing N N 6   
6FA C4    O4     doub N N 7   
6FA C4    C4A    sing N N 8   
6FA C4A   N5     doub N N 9   
6FA C4A   C10    sing N N 10  
6FA N5    C5A    sing N N 11  
6FA C5A   C6     doub Y N 12  
6FA C5A   C9A    sing Y N 13  
6FA C6    O6     sing N N 14  
6FA C6    C7     sing Y N 15  
6FA O6    HO6    sing N N 16  
6FA C7    C7M    sing N N 17  
6FA C7    C8     doub Y N 18  
6FA C7M   HM71   sing N N 19  
6FA C7M   HM72   sing N N 20  
6FA C7M   HM73   sing N N 21  
6FA C8    C8M    sing N N 22  
6FA C8    C9     sing Y N 23  
6FA C8M   HM81   sing N N 24  
6FA C8M   HM82   sing N N 25  
6FA C8M   HM83   sing N N 26  
6FA C9    C9A    doub Y N 27  
6FA C9    H9     sing N N 28  
6FA C9A   N10    sing N N 29  
6FA N10   C10    sing N N 30  
6FA N10   "C1'"  sing N N 31  
6FA "C1'" "C2'"  sing N N 32  
6FA "C1'" "H1'1" sing N N 33  
6FA "C1'" "H1'2" sing N N 34  
6FA "C2'" "O2'"  sing N N 35  
6FA "C2'" "C3'"  sing N N 36  
6FA "C2'" "H2'"  sing N N 37  
6FA "O2'" "HO2'" sing N N 38  
6FA "C3'" "O3'"  sing N N 39  
6FA "C3'" "C4'"  sing N N 40  
6FA "C3'" "H3'"  sing N N 41  
6FA "O3'" "HO3'" sing N N 42  
6FA "C4'" "O4'"  sing N N 43  
6FA "C4'" "C5'"  sing N N 44  
6FA "C4'" "H4'"  sing N N 45  
6FA "O4'" "HO4'" sing N N 46  
6FA "C5'" "O5'"  sing N N 47  
6FA "C5'" "H5'1" sing N N 48  
6FA "C5'" "H5'2" sing N N 49  
6FA "O5'" P      sing N N 50  
6FA P     O1P    doub N N 51  
6FA P     O2P    sing N N 52  
6FA P     O3P    sing N N 53  
6FA O2P   HOP2   sing N N 54  
6FA O3P   PA     sing N N 55  
6FA PA    O1A    doub N N 56  
6FA PA    O2A    sing N N 57  
6FA PA    O5B    sing N N 58  
6FA O2A   HOA2   sing N N 59  
6FA O5B   C5B    sing N N 60  
6FA C5B   C4B    sing N N 61  
6FA C5B   H51A   sing N N 62  
6FA C5B   H52A   sing N N 63  
6FA C4B   O4B    sing N N 64  
6FA C4B   C3B    sing N N 65  
6FA C4B   H4B    sing N N 66  
6FA O4B   C1B    sing N N 67  
6FA C3B   O3B    sing N N 68  
6FA C3B   C2B    sing N N 69  
6FA C3B   H3B    sing N N 70  
6FA O3B   HO3A   sing N N 71  
6FA C2B   O2B    sing N N 72  
6FA C2B   C1B    sing N N 73  
6FA C2B   H2B    sing N N 74  
6FA O2B   HO2A   sing N N 75  
6FA C1B   N9A    sing N N 76  
6FA C1B   H1B    sing N N 77  
6FA N9A   C8A    sing Y N 78  
6FA N9A   C4X    sing Y N 79  
6FA C8A   N7A    doub Y N 80  
6FA C8A   H8A    sing N N 81  
6FA N7A   C5X    sing Y N 82  
6FA C5X   C6A    sing Y N 83  
6FA C5X   C4X    doub Y N 84  
6FA C6A   N6A    sing N N 85  
6FA C6A   N1A    doub Y N 86  
6FA N6A   H61A   sing N N 87  
6FA N6A   H62A   sing N N 88  
6FA N1A   C2A    sing Y N 89  
6FA C2A   N3A    doub Y N 90  
6FA C2A   H2A    sing N N 91  
6FA N3A   C4X    sing Y N 92  
ALA N     CA     sing N N 93  
ALA N     H      sing N N 94  
ALA N     H2     sing N N 95  
ALA CA    C      sing N N 96  
ALA CA    CB     sing N N 97  
ALA CA    HA     sing N N 98  
ALA C     O      doub N N 99  
ALA C     OXT    sing N N 100 
ALA CB    HB1    sing N N 101 
ALA CB    HB2    sing N N 102 
ALA CB    HB3    sing N N 103 
ALA OXT   HXT    sing N N 104 
ARG N     CA     sing N N 105 
ARG N     H      sing N N 106 
ARG N     H2     sing N N 107 
ARG CA    C      sing N N 108 
ARG CA    CB     sing N N 109 
ARG CA    HA     sing N N 110 
ARG C     O      doub N N 111 
ARG C     OXT    sing N N 112 
ARG CB    CG     sing N N 113 
ARG CB    HB2    sing N N 114 
ARG CB    HB3    sing N N 115 
ARG CG    CD     sing N N 116 
ARG CG    HG2    sing N N 117 
ARG CG    HG3    sing N N 118 
ARG CD    NE     sing N N 119 
ARG CD    HD2    sing N N 120 
ARG CD    HD3    sing N N 121 
ARG NE    CZ     sing N N 122 
ARG NE    HE     sing N N 123 
ARG CZ    NH1    sing N N 124 
ARG CZ    NH2    doub N N 125 
ARG NH1   HH11   sing N N 126 
ARG NH1   HH12   sing N N 127 
ARG NH2   HH21   sing N N 128 
ARG NH2   HH22   sing N N 129 
ARG OXT   HXT    sing N N 130 
ASN N     CA     sing N N 131 
ASN N     H      sing N N 132 
ASN N     H2     sing N N 133 
ASN CA    C      sing N N 134 
ASN CA    CB     sing N N 135 
ASN CA    HA     sing N N 136 
ASN C     O      doub N N 137 
ASN C     OXT    sing N N 138 
ASN CB    CG     sing N N 139 
ASN CB    HB2    sing N N 140 
ASN CB    HB3    sing N N 141 
ASN CG    OD1    doub N N 142 
ASN CG    ND2    sing N N 143 
ASN ND2   HD21   sing N N 144 
ASN ND2   HD22   sing N N 145 
ASN OXT   HXT    sing N N 146 
ASP N     CA     sing N N 147 
ASP N     H      sing N N 148 
ASP N     H2     sing N N 149 
ASP CA    C      sing N N 150 
ASP CA    CB     sing N N 151 
ASP CA    HA     sing N N 152 
ASP C     O      doub N N 153 
ASP C     OXT    sing N N 154 
ASP CB    CG     sing N N 155 
ASP CB    HB2    sing N N 156 
ASP CB    HB3    sing N N 157 
ASP CG    OD1    doub N N 158 
ASP CG    OD2    sing N N 159 
ASP OD2   HD2    sing N N 160 
ASP OXT   HXT    sing N N 161 
CYS N     CA     sing N N 162 
CYS N     H      sing N N 163 
CYS N     H2     sing N N 164 
CYS CA    C      sing N N 165 
CYS CA    CB     sing N N 166 
CYS CA    HA     sing N N 167 
CYS C     O      doub N N 168 
CYS C     OXT    sing N N 169 
CYS CB    SG     sing N N 170 
CYS CB    HB2    sing N N 171 
CYS CB    HB3    sing N N 172 
CYS SG    HG     sing N N 173 
CYS OXT   HXT    sing N N 174 
GLN N     CA     sing N N 175 
GLN N     H      sing N N 176 
GLN N     H2     sing N N 177 
GLN CA    C      sing N N 178 
GLN CA    CB     sing N N 179 
GLN CA    HA     sing N N 180 
GLN C     O      doub N N 181 
GLN C     OXT    sing N N 182 
GLN CB    CG     sing N N 183 
GLN CB    HB2    sing N N 184 
GLN CB    HB3    sing N N 185 
GLN CG    CD     sing N N 186 
GLN CG    HG2    sing N N 187 
GLN CG    HG3    sing N N 188 
GLN CD    OE1    doub N N 189 
GLN CD    NE2    sing N N 190 
GLN NE2   HE21   sing N N 191 
GLN NE2   HE22   sing N N 192 
GLN OXT   HXT    sing N N 193 
GLU N     CA     sing N N 194 
GLU N     H      sing N N 195 
GLU N     H2     sing N N 196 
GLU CA    C      sing N N 197 
GLU CA    CB     sing N N 198 
GLU CA    HA     sing N N 199 
GLU C     O      doub N N 200 
GLU C     OXT    sing N N 201 
GLU CB    CG     sing N N 202 
GLU CB    HB2    sing N N 203 
GLU CB    HB3    sing N N 204 
GLU CG    CD     sing N N 205 
GLU CG    HG2    sing N N 206 
GLU CG    HG3    sing N N 207 
GLU CD    OE1    doub N N 208 
GLU CD    OE2    sing N N 209 
GLU OE2   HE2    sing N N 210 
GLU OXT   HXT    sing N N 211 
GLY N     CA     sing N N 212 
GLY N     H      sing N N 213 
GLY N     H2     sing N N 214 
GLY CA    C      sing N N 215 
GLY CA    HA2    sing N N 216 
GLY CA    HA3    sing N N 217 
GLY C     O      doub N N 218 
GLY C     OXT    sing N N 219 
GLY OXT   HXT    sing N N 220 
HIS N     CA     sing N N 221 
HIS N     H      sing N N 222 
HIS N     H2     sing N N 223 
HIS CA    C      sing N N 224 
HIS CA    CB     sing N N 225 
HIS CA    HA     sing N N 226 
HIS C     O      doub N N 227 
HIS C     OXT    sing N N 228 
HIS CB    CG     sing N N 229 
HIS CB    HB2    sing N N 230 
HIS CB    HB3    sing N N 231 
HIS CG    ND1    sing Y N 232 
HIS CG    CD2    doub Y N 233 
HIS ND1   CE1    doub Y N 234 
HIS ND1   HD1    sing N N 235 
HIS CD2   NE2    sing Y N 236 
HIS CD2   HD2    sing N N 237 
HIS CE1   NE2    sing Y N 238 
HIS CE1   HE1    sing N N 239 
HIS NE2   HE2    sing N N 240 
HIS OXT   HXT    sing N N 241 
HOH O     H1     sing N N 242 
HOH O     H2     sing N N 243 
ILE N     CA     sing N N 244 
ILE N     H      sing N N 245 
ILE N     H2     sing N N 246 
ILE CA    C      sing N N 247 
ILE CA    CB     sing N N 248 
ILE CA    HA     sing N N 249 
ILE C     O      doub N N 250 
ILE C     OXT    sing N N 251 
ILE CB    CG1    sing N N 252 
ILE CB    CG2    sing N N 253 
ILE CB    HB     sing N N 254 
ILE CG1   CD1    sing N N 255 
ILE CG1   HG12   sing N N 256 
ILE CG1   HG13   sing N N 257 
ILE CG2   HG21   sing N N 258 
ILE CG2   HG22   sing N N 259 
ILE CG2   HG23   sing N N 260 
ILE CD1   HD11   sing N N 261 
ILE CD1   HD12   sing N N 262 
ILE CD1   HD13   sing N N 263 
ILE OXT   HXT    sing N N 264 
LEU N     CA     sing N N 265 
LEU N     H      sing N N 266 
LEU N     H2     sing N N 267 
LEU CA    C      sing N N 268 
LEU CA    CB     sing N N 269 
LEU CA    HA     sing N N 270 
LEU C     O      doub N N 271 
LEU C     OXT    sing N N 272 
LEU CB    CG     sing N N 273 
LEU CB    HB2    sing N N 274 
LEU CB    HB3    sing N N 275 
LEU CG    CD1    sing N N 276 
LEU CG    CD2    sing N N 277 
LEU CG    HG     sing N N 278 
LEU CD1   HD11   sing N N 279 
LEU CD1   HD12   sing N N 280 
LEU CD1   HD13   sing N N 281 
LEU CD2   HD21   sing N N 282 
LEU CD2   HD22   sing N N 283 
LEU CD2   HD23   sing N N 284 
LEU OXT   HXT    sing N N 285 
LYS N     CA     sing N N 286 
LYS N     H      sing N N 287 
LYS N     H2     sing N N 288 
LYS CA    C      sing N N 289 
LYS CA    CB     sing N N 290 
LYS CA    HA     sing N N 291 
LYS C     O      doub N N 292 
LYS C     OXT    sing N N 293 
LYS CB    CG     sing N N 294 
LYS CB    HB2    sing N N 295 
LYS CB    HB3    sing N N 296 
LYS CG    CD     sing N N 297 
LYS CG    HG2    sing N N 298 
LYS CG    HG3    sing N N 299 
LYS CD    CE     sing N N 300 
LYS CD    HD2    sing N N 301 
LYS CD    HD3    sing N N 302 
LYS CE    NZ     sing N N 303 
LYS CE    HE2    sing N N 304 
LYS CE    HE3    sing N N 305 
LYS NZ    HZ1    sing N N 306 
LYS NZ    HZ2    sing N N 307 
LYS NZ    HZ3    sing N N 308 
LYS OXT   HXT    sing N N 309 
MET N     CA     sing N N 310 
MET N     H      sing N N 311 
MET N     H2     sing N N 312 
MET CA    C      sing N N 313 
MET CA    CB     sing N N 314 
MET CA    HA     sing N N 315 
MET C     O      doub N N 316 
MET C     OXT    sing N N 317 
MET CB    CG     sing N N 318 
MET CB    HB2    sing N N 319 
MET CB    HB3    sing N N 320 
MET CG    SD     sing N N 321 
MET CG    HG2    sing N N 322 
MET CG    HG3    sing N N 323 
MET SD    CE     sing N N 324 
MET CE    HE1    sing N N 325 
MET CE    HE2    sing N N 326 
MET CE    HE3    sing N N 327 
MET OXT   HXT    sing N N 328 
NDP PA    O1A    doub N N 329 
NDP PA    O2A    sing N N 330 
NDP PA    O5B    sing N N 331 
NDP PA    O3     sing N N 332 
NDP O2A   HOA2   sing N N 333 
NDP O5B   C5B    sing N N 334 
NDP C5B   C4B    sing N N 335 
NDP C5B   H51A   sing N N 336 
NDP C5B   H52A   sing N N 337 
NDP C4B   O4B    sing N N 338 
NDP C4B   C3B    sing N N 339 
NDP C4B   H4B    sing N N 340 
NDP O4B   C1B    sing N N 341 
NDP C3B   O3B    sing N N 342 
NDP C3B   C2B    sing N N 343 
NDP C3B   H3B    sing N N 344 
NDP O3B   HO3A   sing N N 345 
NDP C2B   O2B    sing N N 346 
NDP C2B   C1B    sing N N 347 
NDP C2B   H2B    sing N N 348 
NDP O2B   P2B    sing N N 349 
NDP C1B   N9A    sing N N 350 
NDP C1B   H1B    sing N N 351 
NDP N9A   C8A    sing Y N 352 
NDP N9A   C4A    sing Y N 353 
NDP C8A   N7A    doub Y N 354 
NDP C8A   H8A    sing N N 355 
NDP N7A   C5A    sing Y N 356 
NDP C5A   C6A    sing Y N 357 
NDP C5A   C4A    doub Y N 358 
NDP C6A   N6A    sing N N 359 
NDP C6A   N1A    doub Y N 360 
NDP N6A   H61A   sing N N 361 
NDP N6A   H62A   sing N N 362 
NDP N1A   C2A    sing Y N 363 
NDP C2A   N3A    doub Y N 364 
NDP C2A   H2A    sing N N 365 
NDP N3A   C4A    sing Y N 366 
NDP O3    PN     sing N N 367 
NDP PN    O1N    doub N N 368 
NDP PN    O2N    sing N N 369 
NDP PN    O5D    sing N N 370 
NDP O2N   H21N   sing N N 371 
NDP O5D   C5D    sing N N 372 
NDP C5D   C4D    sing N N 373 
NDP C5D   H51N   sing N N 374 
NDP C5D   H52N   sing N N 375 
NDP C4D   O4D    sing N N 376 
NDP C4D   C3D    sing N N 377 
NDP C4D   H4D    sing N N 378 
NDP O4D   C1D    sing N N 379 
NDP C3D   O3D    sing N N 380 
NDP C3D   C2D    sing N N 381 
NDP C3D   H3D    sing N N 382 
NDP O3D   HO3N   sing N N 383 
NDP C2D   O2D    sing N N 384 
NDP C2D   C1D    sing N N 385 
NDP C2D   H2D    sing N N 386 
NDP O2D   HO2N   sing N N 387 
NDP C1D   N1N    sing N N 388 
NDP C1D   H1D    sing N N 389 
NDP N1N   C2N    sing N N 390 
NDP N1N   C6N    sing N N 391 
NDP C2N   C3N    doub N N 392 
NDP C2N   H2N    sing N N 393 
NDP C3N   C7N    sing N N 394 
NDP C3N   C4N    sing N N 395 
NDP C7N   O7N    doub N N 396 
NDP C7N   N7N    sing N N 397 
NDP N7N   H71N   sing N N 398 
NDP N7N   H72N   sing N N 399 
NDP C4N   C5N    sing N N 400 
NDP C4N   H41N   sing N N 401 
NDP C4N   H42N   sing N N 402 
NDP C5N   C6N    doub N N 403 
NDP C5N   H5N    sing N N 404 
NDP C6N   H6N    sing N N 405 
NDP P2B   O1X    doub N N 406 
NDP P2B   O2X    sing N N 407 
NDP P2B   O3X    sing N N 408 
NDP O2X   HOP2   sing N N 409 
NDP O3X   HOP3   sing N N 410 
PHE N     CA     sing N N 411 
PHE N     H      sing N N 412 
PHE N     H2     sing N N 413 
PHE CA    C      sing N N 414 
PHE CA    CB     sing N N 415 
PHE CA    HA     sing N N 416 
PHE C     O      doub N N 417 
PHE C     OXT    sing N N 418 
PHE CB    CG     sing N N 419 
PHE CB    HB2    sing N N 420 
PHE CB    HB3    sing N N 421 
PHE CG    CD1    doub Y N 422 
PHE CG    CD2    sing Y N 423 
PHE CD1   CE1    sing Y N 424 
PHE CD1   HD1    sing N N 425 
PHE CD2   CE2    doub Y N 426 
PHE CD2   HD2    sing N N 427 
PHE CE1   CZ     doub Y N 428 
PHE CE1   HE1    sing N N 429 
PHE CE2   CZ     sing Y N 430 
PHE CE2   HE2    sing N N 431 
PHE CZ    HZ     sing N N 432 
PHE OXT   HXT    sing N N 433 
PRO N     CA     sing N N 434 
PRO N     CD     sing N N 435 
PRO N     H      sing N N 436 
PRO CA    C      sing N N 437 
PRO CA    CB     sing N N 438 
PRO CA    HA     sing N N 439 
PRO C     O      doub N N 440 
PRO C     OXT    sing N N 441 
PRO CB    CG     sing N N 442 
PRO CB    HB2    sing N N 443 
PRO CB    HB3    sing N N 444 
PRO CG    CD     sing N N 445 
PRO CG    HG2    sing N N 446 
PRO CG    HG3    sing N N 447 
PRO CD    HD2    sing N N 448 
PRO CD    HD3    sing N N 449 
PRO OXT   HXT    sing N N 450 
SER N     CA     sing N N 451 
SER N     H      sing N N 452 
SER N     H2     sing N N 453 
SER CA    C      sing N N 454 
SER CA    CB     sing N N 455 
SER CA    HA     sing N N 456 
SER C     O      doub N N 457 
SER C     OXT    sing N N 458 
SER CB    OG     sing N N 459 
SER CB    HB2    sing N N 460 
SER CB    HB3    sing N N 461 
SER OG    HG     sing N N 462 
SER OXT   HXT    sing N N 463 
SO4 S     O1     doub N N 464 
SO4 S     O2     doub N N 465 
SO4 S     O3     sing N N 466 
SO4 S     O4     sing N N 467 
THR N     CA     sing N N 468 
THR N     H      sing N N 469 
THR N     H2     sing N N 470 
THR CA    C      sing N N 471 
THR CA    CB     sing N N 472 
THR CA    HA     sing N N 473 
THR C     O      doub N N 474 
THR C     OXT    sing N N 475 
THR CB    OG1    sing N N 476 
THR CB    CG2    sing N N 477 
THR CB    HB     sing N N 478 
THR OG1   HG1    sing N N 479 
THR CG2   HG21   sing N N 480 
THR CG2   HG22   sing N N 481 
THR CG2   HG23   sing N N 482 
THR OXT   HXT    sing N N 483 
TRP N     CA     sing N N 484 
TRP N     H      sing N N 485 
TRP N     H2     sing N N 486 
TRP CA    C      sing N N 487 
TRP CA    CB     sing N N 488 
TRP CA    HA     sing N N 489 
TRP C     O      doub N N 490 
TRP C     OXT    sing N N 491 
TRP CB    CG     sing N N 492 
TRP CB    HB2    sing N N 493 
TRP CB    HB3    sing N N 494 
TRP CG    CD1    doub Y N 495 
TRP CG    CD2    sing Y N 496 
TRP CD1   NE1    sing Y N 497 
TRP CD1   HD1    sing N N 498 
TRP CD2   CE2    doub Y N 499 
TRP CD2   CE3    sing Y N 500 
TRP NE1   CE2    sing Y N 501 
TRP NE1   HE1    sing N N 502 
TRP CE2   CZ2    sing Y N 503 
TRP CE3   CZ3    doub Y N 504 
TRP CE3   HE3    sing N N 505 
TRP CZ2   CH2    doub Y N 506 
TRP CZ2   HZ2    sing N N 507 
TRP CZ3   CH2    sing Y N 508 
TRP CZ3   HZ3    sing N N 509 
TRP CH2   HH2    sing N N 510 
TRP OXT   HXT    sing N N 511 
TYR N     CA     sing N N 512 
TYR N     H      sing N N 513 
TYR N     H2     sing N N 514 
TYR CA    C      sing N N 515 
TYR CA    CB     sing N N 516 
TYR CA    HA     sing N N 517 
TYR C     O      doub N N 518 
TYR C     OXT    sing N N 519 
TYR CB    CG     sing N N 520 
TYR CB    HB2    sing N N 521 
TYR CB    HB3    sing N N 522 
TYR CG    CD1    doub Y N 523 
TYR CG    CD2    sing Y N 524 
TYR CD1   CE1    sing Y N 525 
TYR CD1   HD1    sing N N 526 
TYR CD2   CE2    doub Y N 527 
TYR CD2   HD2    sing N N 528 
TYR CE1   CZ     doub Y N 529 
TYR CE1   HE1    sing N N 530 
TYR CE2   CZ     sing Y N 531 
TYR CE2   HE2    sing N N 532 
TYR CZ    OH     sing N N 533 
TYR OH    HH     sing N N 534 
TYR OXT   HXT    sing N N 535 
VAL N     CA     sing N N 536 
VAL N     H      sing N N 537 
VAL N     H2     sing N N 538 
VAL CA    C      sing N N 539 
VAL CA    CB     sing N N 540 
VAL CA    HA     sing N N 541 
VAL C     O      doub N N 542 
VAL C     OXT    sing N N 543 
VAL CB    CG1    sing N N 544 
VAL CB    CG2    sing N N 545 
VAL CB    HB     sing N N 546 
VAL CG1   HG11   sing N N 547 
VAL CG1   HG12   sing N N 548 
VAL CG1   HG13   sing N N 549 
VAL CG2   HG21   sing N N 550 
VAL CG2   HG22   sing N N 551 
VAL CG2   HG23   sing N N 552 
VAL OXT   HXT    sing N N 553 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'National Natural Science Foundation of China (NSFC)' China 32071269 1 
'National Natural Science Foundation of China (NSFC)' China 31770827 2 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   8YOX 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'P 32 2 1' 
_space_group.name_Hall        
;P 32 2"
;
_space_group.IT_number        154 
_space_group.crystal_system   trigonal 
_space_group.id               1 
# 
_atom_sites.entry_id                    8YOQ 
_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]   0.016583 
_atom_sites.fract_transf_matrix[1][2]   0.009574 
_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]   0.019149 
_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]   0.005136 
_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.
;
? 
H   ? ? ?       ?       ? ? ?        ?        ? ? ?   ? ? 
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.
;
? 
O1- ? ? 5.12366 3.84317 ? ? 3.49406  27.47979 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
P   ? ? 9.51135 5.44231 ? ? 1.42069  35.72801 ? ? 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.
;
? 
# 
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     . PRO A 1 1   ? -45.823 -26.054 41.950  1.00 33.75 ?  7   PRO A N     1 
ATOM   2    C CA    . PRO A 1 1   ? -44.871 -26.741 42.833  1.00 30.77 ?  7   PRO A CA    1 
ATOM   3    C C     . PRO A 1 1   ? -44.173 -27.907 42.125  1.00 27.38 ?  7   PRO A C     1 
ATOM   4    O O     . PRO A 1 1   ? -44.845 -28.799 41.614  1.00 23.40 ?  7   PRO A O     1 
ATOM   5    C CB    . PRO A 1 1   ? -45.758 -27.246 43.981  1.00 32.94 ?  7   PRO A CB    1 
ATOM   6    C CG    . PRO A 1 1   ? -47.140 -27.365 43.376  1.00 32.77 ?  7   PRO A CG    1 
ATOM   7    C CD    . PRO A 1 1   ? -47.221 -26.230 42.388  1.00 40.95 ?  7   PRO A CD    1 
ATOM   8    N N     . HIS A 1 2   ? -42.844 -27.913 42.079  1.00 27.56 ?  8   HIS A N     1 
ATOM   9    C CA    . HIS A 1 2   ? -42.161 -29.018 41.419  1.00 24.04 ?  8   HIS A CA    1 
ATOM   10   C C     . HIS A 1 2   ? -41.925 -30.210 42.341  1.00 23.75 ?  8   HIS A C     1 
ATOM   11   O O     . HIS A 1 2   ? -41.555 -31.285 41.847  1.00 17.94 ?  8   HIS A O     1 
ATOM   12   C CB    . HIS A 1 2   ? -40.836 -28.533 40.828  1.00 29.27 ?  8   HIS A CB    1 
ATOM   13   C CG    . HIS A 1 2   ? -41.020 -27.540 39.727  1.00 35.54 ?  8   HIS A CG    1 
ATOM   14   N ND1   . HIS A 1 2   ? -41.215 -27.918 38.415  1.00 32.58 ?  8   HIS A ND1   1 
ATOM   15   C CD2   . HIS A 1 2   ? -41.097 -26.188 39.749  1.00 36.48 ?  8   HIS A CD2   1 
ATOM   16   C CE1   . HIS A 1 2   ? -41.383 -26.840 37.672  1.00 37.15 ?  8   HIS A CE1   1 
ATOM   17   N NE2   . HIS A 1 2   ? -41.315 -25.778 38.458  1.00 40.57 ?  8   HIS A NE2   1 
ATOM   18   N N     . MET A 1 3   ? -42.138 -30.040 43.656  1.00 19.99 ?  9   MET A N     1 
ATOM   19   C CA    . MET A 1 3   ? -41.987 -31.110 44.651  1.00 16.62 ?  9   MET A CA    1 
ATOM   20   C C     . MET A 1 3   ? -40.648 -31.829 44.527  1.00 16.11 ?  9   MET A C     1 
ATOM   21   O O     . MET A 1 3   ? -40.568 -33.060 44.577  1.00 17.56 ?  9   MET A O     1 
ATOM   22   C CB    . MET A 1 3   ? -43.149 -32.092 44.568  1.00 15.01 ?  9   MET A CB    1 
ATOM   23   C CG    . MET A 1 3   ? -44.503 -31.394 44.773  1.00 15.27 ?  9   MET A CG    1 
ATOM   24   S SD    . MET A 1 3   ? -45.900 -32.531 44.890  1.00 23.43 ?  9   MET A SD    1 
ATOM   25   C CE    . MET A 1 3   ? -47.269 -31.378 44.935  1.00 45.81 ?  9   MET A CE    1 
ATOM   26   N N     . GLY A 1 4   ? -39.579 -31.054 44.394  1.00 17.10 ?  10  GLY A N     1 
ATOM   27   C CA    . GLY A 1 4   ? -38.245 -31.600 44.337  1.00 17.14 ?  10  GLY A CA    1 
ATOM   28   C C     . GLY A 1 4   ? -37.740 -31.948 42.949  1.00 19.88 ?  10  GLY A C     1 
ATOM   29   O O     . GLY A 1 4   ? -36.528 -32.090 42.771  1.00 21.54 ?  10  GLY A O     1 
ATOM   30   N N     . ALA A 1 5   ? -38.622 -32.099 41.968  1.00 16.45 ?  11  ALA A N     1 
ATOM   31   C CA    . ALA A 1 5   ? -38.186 -32.432 40.618  1.00 19.54 ?  11  ALA A CA    1 
ATOM   32   C C     . ALA A 1 5   ? -37.497 -31.235 39.964  1.00 20.68 ?  11  ALA A C     1 
ATOM   33   O O     . ALA A 1 5   ? -37.730 -30.078 40.326  1.00 19.97 ?  11  ALA A O     1 
ATOM   34   C CB    . ALA A 1 5   ? -39.377 -32.892 39.782  1.00 17.87 ?  11  ALA A CB    1 
ATOM   35   N N     . LEU A 1 6   ? -36.608 -31.526 39.014  1.00 21.01 ?  12  LEU A N     1 
ATOM   36   C CA    . LEU A 1 6   ? -35.893 -30.489 38.279  1.00 21.96 ?  12  LEU A CA    1 
ATOM   37   C C     . LEU A 1 6   ? -36.653 -30.124 37.019  1.00 22.00 ?  12  LEU A C     1 
ATOM   38   O O     . LEU A 1 6   ? -37.133 -30.998 36.288  1.00 20.15 ?  12  LEU A O     1 
ATOM   39   C CB    . LEU A 1 6   ? -34.489 -30.951 37.877  1.00 19.74 ?  12  LEU A CB    1 
ATOM   40   C CG    . LEU A 1 6   ? -33.426 -31.198 38.937  1.00 24.10 ?  12  LEU A CG    1 
ATOM   41   C CD1   . LEU A 1 6   ? -32.102 -31.510 38.248  1.00 22.68 ?  12  LEU A CD1   1 
ATOM   42   C CD2   . LEU A 1 6   ? -33.284 -29.994 39.862  1.00 25.82 ?  12  LEU A CD2   1 
ATOM   43   N N     . HIS A 1 7   ? -36.750 -28.826 36.756  1.00 20.35 ?  13  HIS A N     1 
ATOM   44   C CA    . HIS A 1 7   ? -37.144 -28.345 35.437  1.00 22.75 ?  13  HIS A CA    1 
ATOM   45   C C     . HIS A 1 7   ? -36.370 -27.059 35.206  1.00 22.04 ?  13  HIS A C     1 
ATOM   46   O O     . HIS A 1 7   ? -36.648 -26.044 35.849  1.00 21.20 ?  13  HIS A O     1 
ATOM   47   C CB    . HIS A 1 7   ? -38.651 -28.117 35.301  1.00 27.61 ?  13  HIS A CB    1 
ATOM   48   C CG    . HIS A 1 7   ? -39.085 -27.924 33.877  1.00 39.93 ?  13  HIS A CG    1 
ATOM   49   N ND1   . HIS A 1 7   ? -39.557 -26.721 33.393  1.00 50.52 ?  13  HIS A ND1   1 
ATOM   50   C CD2   . HIS A 1 7   ? -39.064 -28.769 32.818  1.00 47.52 ?  13  HIS A CD2   1 
ATOM   51   C CE1   . HIS A 1 7   ? -39.834 -26.842 32.106  1.00 53.95 ?  13  HIS A CE1   1 
ATOM   52   N NE2   . HIS A 1 7   ? -39.540 -28.074 31.731  1.00 48.51 ?  13  HIS A NE2   1 
ATOM   53   N N     . VAL A 1 8   ? -35.380 -27.118 34.325  1.00 18.09 ?  14  VAL A N     1 
ATOM   54   C CA    . VAL A 1 8   ? -34.507 -25.985 34.068  1.00 18.38 ?  14  VAL A CA    1 
ATOM   55   C C     . VAL A 1 8   ? -35.058 -25.226 32.872  1.00 19.62 ?  14  VAL A C     1 
ATOM   56   O O     . VAL A 1 8   ? -35.437 -25.826 31.864  1.00 18.39 ?  14  VAL A O     1 
ATOM   57   C CB    . VAL A 1 8   ? -33.063 -26.449 33.823  1.00 15.32 ?  14  VAL A CB    1 
ATOM   58   C CG1   . VAL A 1 8   ? -32.138 -25.234 33.662  1.00 14.10 ?  14  VAL A CG1   1 
ATOM   59   C CG2   . VAL A 1 8   ? -32.588 -27.309 34.990  1.00 14.76 ?  14  VAL A CG2   1 
ATOM   60   N N     . VAL A 1 9   ? -35.153 -23.911 32.990  1.00 16.82 ?  15  VAL A N     1 
ATOM   61   C CA    . VAL A 1 9   ? -35.519 -23.075 31.854  1.00 19.47 ?  15  VAL A CA    1 
ATOM   62   C C     . VAL A 1 9   ? -34.296 -22.268 31.473  1.00 16.36 ?  15  VAL A C     1 
ATOM   63   O O     . VAL A 1 9   ? -33.636 -21.673 32.340  1.00 16.01 ?  15  VAL A O     1 
ATOM   64   C CB    . VAL A 1 9   ? -36.733 -22.177 32.158  1.00 20.60 ?  15  VAL A CB    1 
ATOM   65   C CG1   . VAL A 1 9   ? -37.019 -21.248 30.972  1.00 20.65 ?  15  VAL A CG1   1 
ATOM   66   C CG2   . VAL A 1 9   ? -37.946 -23.043 32.448  1.00 23.51 ?  15  VAL A CG2   1 
ATOM   67   N N     . ILE A 1 10  ? -33.952 -22.311 30.186  1.00 15.77 ?  16  ILE A N     1 
ATOM   68   C CA    . ILE A 1 10  ? -32.847 -21.542 29.626  1.00 14.86 ?  16  ILE A CA    1 
ATOM   69   C C     . ILE A 1 10  ? -33.468 -20.432 28.788  1.00 15.72 ?  16  ILE A C     1 
ATOM   70   O O     . ILE A 1 10  ? -34.230 -20.709 27.859  1.00 15.23 ?  16  ILE A O     1 
ATOM   71   C CB    . ILE A 1 10  ? -31.920 -22.416 28.761  1.00 14.52 ?  16  ILE A CB    1 
ATOM   72   C CG1   . ILE A 1 10  ? -31.394 -23.627 29.541  1.00 12.16 ?  16  ILE A CG1   1 
ATOM   73   C CG2   . ILE A 1 10  ? -30.743 -21.585 28.209  1.00 12.77 ?  16  ILE A CG2   1 
ATOM   74   C CD1   . ILE A 1 10  ? -30.742 -24.660 28.612  1.00 13.90 ?  16  ILE A CD1   1 
ATOM   75   N N     . VAL A 1 11  ? -33.160 -19.181 29.113  1.00 17.70 ?  17  VAL A N     1 
ATOM   76   C CA    . VAL A 1 11  ? -33.645 -18.048 28.336  1.00 15.94 ?  17  VAL A CA    1 
ATOM   77   C C     . VAL A 1 11  ? -32.499 -17.588 27.454  1.00 12.81 ?  17  VAL A C     1 
ATOM   78   O O     . VAL A 1 11  ? -31.515 -17.023 27.942  1.00 15.15 ?  17  VAL A O     1 
ATOM   79   C CB    . VAL A 1 11  ? -34.166 -16.917 29.228  1.00 19.44 ?  17  VAL A CB    1 
ATOM   80   C CG1   . VAL A 1 11  ? -34.650 -15.734 28.360  1.00 19.31 ?  17  VAL A CG1   1 
ATOM   81   C CG2   . VAL A 1 11  ? -35.307 -17.436 30.101  1.00 20.67 ?  17  VAL A CG2   1 
ATOM   82   N N     . GLY A 1 12  ? -32.618 -17.859 26.159  1.00 15.28 ?  18  GLY A N     1 
ATOM   83   C CA    . GLY A 1 12  ? -31.609 -17.466 25.193  1.00 14.45 ?  18  GLY A CA    1 
ATOM   84   C C     . GLY A 1 12  ? -30.890 -18.656 24.597  1.00 13.82 ?  18  GLY A C     1 
ATOM   85   O O     . GLY A 1 12  ? -30.263 -19.434 25.325  1.00 13.79 ?  18  GLY A O     1 
ATOM   86   N N     . GLY A 1 13  ? -30.962 -18.809 23.277  1.00 12.72 ?  19  GLY A N     1 
ATOM   87   C CA    . GLY A 1 13  ? -30.299 -19.919 22.618  1.00 10.02 ?  19  GLY A CA    1 
ATOM   88   C C     . GLY A 1 13  ? -29.073 -19.510 21.828  1.00 10.97 ?  19  GLY A C     1 
ATOM   89   O O     . GLY A 1 13  ? -28.960 -19.813 20.634  1.00 13.02 ?  19  GLY A O     1 
ATOM   90   N N     . GLY A 1 14  ? -28.165 -18.796 22.470  1.00 11.69 ?  20  GLY A N     1 
ATOM   91   C CA    . GLY A 1 14  ? -26.900 -18.421 21.869  1.00 9.51  ?  20  GLY A CA    1 
ATOM   92   C C     . GLY A 1 14  ? -25.848 -19.460 22.172  1.00 9.62  ?  20  GLY A C     1 
ATOM   93   O O     . GLY A 1 14  ? -26.147 -20.622 22.447  1.00 10.26 ?  20  GLY A O     1 
ATOM   94   N N     . PHE A 1 15  ? -24.590 -19.027 22.129  1.00 9.62  ?  21  PHE A N     1 
ATOM   95   C CA    . PHE A 1 15  ? -23.496 -19.929 22.465  1.00 9.08  ?  21  PHE A CA    1 
ATOM   96   C C     . PHE A 1 15  ? -23.675 -20.504 23.867  1.00 12.00 ?  21  PHE A C     1 
ATOM   97   O O     . PHE A 1 15  ? -23.485 -21.710 24.087  1.00 10.55 ?  21  PHE A O     1 
ATOM   98   C CB    . PHE A 1 15  ? -22.168 -19.187 22.346  1.00 11.07 ?  21  PHE A CB    1 
ATOM   99   C CG    . PHE A 1 15  ? -21.732 -18.970 20.934  1.00 11.12 ?  21  PHE A CG    1 
ATOM   100  C CD1   . PHE A 1 15  ? -21.026 -19.954 20.255  1.00 11.52 ?  21  PHE A CD1   1 
ATOM   101  C CD2   . PHE A 1 15  ? -22.044 -17.795 20.277  1.00 11.20 ?  21  PHE A CD2   1 
ATOM   102  C CE1   . PHE A 1 15  ? -20.616 -19.757 18.924  1.00 10.68 ?  21  PHE A CE1   1 
ATOM   103  C CE2   . PHE A 1 15  ? -21.637 -17.603 18.947  1.00 9.56  ?  21  PHE A CE2   1 
ATOM   104  C CZ    . PHE A 1 15  ? -20.935 -18.586 18.291  1.00 10.50 ?  21  PHE A CZ    1 
ATOM   105  N N     . GLY A 1 16  ? -24.076 -19.668 24.819  1.00 9.08  ?  22  GLY A N     1 
ATOM   106  C CA    . GLY A 1 16  ? -24.292 -20.175 26.171  1.00 11.92 ?  22  GLY A CA    1 
ATOM   107  C C     . GLY A 1 16  ? -25.480 -21.115 26.249  1.00 10.04 ?  22  GLY A C     1 
ATOM   108  O O     . GLY A 1 16  ? -25.391 -22.211 26.816  1.00 11.42 ?  22  GLY A O     1 
ATOM   109  N N     . GLY A 1 17  ? -26.611 -20.701 25.673  1.00 10.62 ?  23  GLY A N     1 
ATOM   110  C CA    . GLY A 1 17  ? -27.822 -21.500 25.781  1.00 11.30 ?  23  GLY A CA    1 
ATOM   111  C C     . GLY A 1 17  ? -27.723 -22.863 25.117  1.00 11.44 ?  23  GLY A C     1 
ATOM   112  O O     . GLY A 1 17  ? -28.208 -23.854 25.662  1.00 12.76 ?  23  GLY A O     1 
ATOM   113  N N     . ILE A 1 18  ? -27.130 -22.937 23.913  1.00 11.30 ?  24  ILE A N     1 
ATOM   114  C CA    . ILE A 1 18  ? -27.071 -24.254 23.283  1.00 10.18 ?  24  ILE A CA    1 
ATOM   115  C C     . ILE A 1 18  ? -26.089 -25.163 24.018  1.00 10.67 ?  24  ILE A C     1 
ATOM   116  O O     . ILE A 1 18  ? -26.264 -26.388 24.039  1.00 10.93 ?  24  ILE A O     1 
ATOM   117  C CB    . ILE A 1 18  ? -26.738 -24.168 21.774  1.00 9.12  ?  24  ILE A CB    1 
ATOM   118  C CG1   . ILE A 1 18  ? -25.319 -23.644 21.518  1.00 9.63  ?  24  ILE A CG1   1 
ATOM   119  C CG2   . ILE A 1 18  ? -27.795 -23.322 21.046  1.00 10.70 ?  24  ILE A CG2   1 
ATOM   120  C CD1   . ILE A 1 18  ? -24.814 -23.911 20.050  1.00 10.14 ?  24  ILE A CD1   1 
ATOM   121  N N     . ALA A 1 19  ? -25.048 -24.606 24.627  1.00 10.15 ?  25  ALA A N     1 
ATOM   122  C CA    . ALA A 1 19  ? -24.163 -25.452 25.419  1.00 9.45  ?  25  ALA A CA    1 
ATOM   123  C C     . ALA A 1 19  ? -24.885 -26.001 26.638  1.00 12.29 ?  25  ALA A C     1 
ATOM   124  O O     . ALA A 1 19  ? -24.749 -27.188 26.969  1.00 11.39 ?  25  ALA A O     1 
ATOM   125  C CB    . ALA A 1 19  ? -22.924 -24.663 25.846  1.00 11.42 ?  25  ALA A CB    1 
ATOM   126  N N     . ALA A 1 20  ? -25.654 -25.151 27.321  1.00 10.01 ?  26  ALA A N     1 
ATOM   127  C CA    . ALA A 1 20  ? -26.398 -25.609 28.493  1.00 11.78 ?  26  ALA A CA    1 
ATOM   128  C C     . ALA A 1 20  ? -27.457 -26.632 28.109  1.00 10.85 ?  26  ALA A C     1 
ATOM   129  O O     . ALA A 1 20  ? -27.609 -27.660 28.780  1.00 10.76 ?  26  ALA A O     1 
ATOM   130  C CB    . ALA A 1 20  ? -27.037 -24.425 29.214  1.00 9.25  ?  26  ALA A CB    1 
ATOM   131  N N     . ALA A 1 21  ? -28.202 -26.372 27.028  1.00 12.77 ?  27  ALA A N     1 
ATOM   132  C CA    . ALA A 1 21  ? -29.228 -27.317 26.608  1.00 10.74 ?  27  ALA A CA    1 
ATOM   133  C C     . ALA A 1 21  ? -28.621 -28.652 26.198  1.00 11.22 ?  27  ALA A C     1 
ATOM   134  O O     . ALA A 1 21  ? -29.193 -29.716 26.472  1.00 11.56 ?  27  ALA A O     1 
ATOM   135  C CB    . ALA A 1 21  ? -30.035 -26.731 25.444  1.00 11.02 ?  27  ALA A CB    1 
ATOM   136  N N     . SER A 1 22  ? -27.504 -28.616 25.476  1.00 10.14 ?  28  SER A N     1 
ATOM   137  C CA    . SER A 1 22  ? -26.863 -29.853 25.052  1.00 13.78 ?  28  SER A CA    1 
ATOM   138  C C     . SER A 1 22  ? -26.471 -30.706 26.249  1.00 15.15 ?  28  SER A C     1 
ATOM   139  O O     . SER A 1 22  ? -26.595 -31.934 26.216  1.00 15.49 ?  28  SER A O     1 
ATOM   140  C CB    . SER A 1 22  ? -25.632 -29.543 24.193  1.00 17.46 ?  28  SER A CB    1 
ATOM   141  O OG    . SER A 1 22  ? -24.965 -30.748 23.855  1.00 25.82 ?  28  SER A OG    1 
ATOM   142  N N     . GLN A 1 23  ? -25.998 -30.073 27.323  1.00 14.97 ?  29  GLN A N     1 
ATOM   143  C CA    . GLN A 1 23  ? -25.558 -30.852 28.476  1.00 15.53 ?  29  GLN A CA    1 
ATOM   144  C C     . GLN A 1 23  ? -26.748 -31.360 29.287  1.00 15.49 ?  29  GLN A C     1 
ATOM   145  O O     . GLN A 1 23  ? -26.748 -32.516 29.706  1.00 17.16 ?  29  GLN A O     1 
ATOM   146  C CB    . GLN A 1 23  ? -24.611 -30.036 29.349  1.00 16.72 ?  29  GLN A CB    1 
ATOM   147  C CG    . GLN A 1 23  ? -23.330 -29.632 28.631  1.00 25.97 ?  29  GLN A CG    1 
ATOM   148  N N     . LEU A 1 24  ? -27.793 -30.539 29.472  1.00 12.83 ?  30  LEU A N     1 
ATOM   149  C CA    . LEU A 1 24  ? -29.001 -31.024 30.150  1.00 11.85 ?  30  LEU A CA    1 
ATOM   150  C C     . LEU A 1 24  ? -29.646 -32.157 29.371  1.00 13.55 ?  30  LEU A C     1 
ATOM   151  O O     . LEU A 1 24  ? -30.110 -33.146 29.957  1.00 13.18 ?  30  LEU A O     1 
ATOM   152  C CB    . LEU A 1 24  ? -29.995 -29.879 30.352  1.00 13.34 ?  30  LEU A CB    1 
ATOM   153  C CG    . LEU A 1 24  ? -29.501 -28.829 31.345  1.00 14.86 ?  30  LEU A CG    1 
ATOM   154  C CD1   . LEU A 1 24  ? -30.235 -27.540 31.118  1.00 13.19 ?  30  LEU A CD1   1 
ATOM   155  C CD2   . LEU A 1 24  ? -29.717 -29.319 32.783  1.00 15.33 ?  30  LEU A CD2   1 
ATOM   156  N N     . GLN A 1 25  ? -29.670 -32.035 28.039  1.00 13.45 ?  31  GLN A N     1 
ATOM   157  C CA    . GLN A 1 25  ? -30.171 -33.115 27.201  1.00 14.23 ?  31  GLN A CA    1 
ATOM   158  C C     . GLN A 1 25  ? -29.367 -34.399 27.405  1.00 17.52 ?  31  GLN A C     1 
ATOM   159  O O     . GLN A 1 25  ? -29.945 -35.488 27.505  1.00 17.88 ?  31  GLN A O     1 
ATOM   160  C CB    . GLN A 1 25  ? -30.132 -32.696 25.735  1.00 13.76 ?  31  GLN A CB    1 
ATOM   161  C CG    . GLN A 1 25  ? -30.890 -33.640 24.834  1.00 19.72 ?  31  GLN A CG    1 
ATOM   162  C CD    . GLN A 1 25  ? -30.796 -33.209 23.396  1.00 22.86 ?  31  GLN A CD    1 
ATOM   163  O OE1   . GLN A 1 25  ? -29.702 -33.094 22.844  1.00 25.96 ?  31  GLN A OE1   1 
ATOM   164  N NE2   . GLN A 1 25  ? -31.925 -32.908 22.802  1.00 21.34 ?  31  GLN A NE2   1 
ATOM   165  N N     . ALA A 1 26  ? -28.036 -34.298 27.463  1.00 16.68 ?  32  ALA A N     1 
ATOM   166  C CA    . ALA A 1 26  ? -27.217 -35.497 27.668  1.00 17.67 ?  32  ALA A CA    1 
ATOM   167  C C     . ALA A 1 26  ? -27.422 -36.098 29.054  1.00 21.45 ?  32  ALA A C     1 
ATOM   168  O O     . ALA A 1 26  ? -27.275 -37.313 29.240  1.00 22.56 ?  32  ALA A O     1 
ATOM   169  C CB    . ALA A 1 26  ? -25.739 -35.169 27.452  1.00 22.72 ?  32  ALA A CB    1 
ATOM   170  N N     . LEU A 1 27  ? -27.762 -35.277 30.035  1.00 18.79 ?  33  LEU A N     1 
ATOM   171  C CA    . LEU A 1 27  ? -28.006 -35.761 31.386  1.00 18.22 ?  33  LEU A CA    1 
ATOM   172  C C     . LEU A 1 27  ? -29.435 -36.239 31.606  1.00 18.57 ?  33  LEU A C     1 
ATOM   173  O O     . LEU A 1 27  ? -29.744 -36.729 32.701  1.00 19.41 ?  33  LEU A O     1 
ATOM   174  C CB    . LEU A 1 27  ? -27.694 -34.658 32.400  1.00 17.94 ?  33  LEU A CB    1 
ATOM   175  C CG    . LEU A 1 27  ? -26.262 -34.153 32.521  1.00 23.24 ?  33  LEU A CG    1 
ATOM   176  C CD1   . LEU A 1 27  ? -26.238 -32.886 33.370  1.00 22.47 ?  33  LEU A CD1   1 
ATOM   177  C CD2   . LEU A 1 27  ? -25.373 -35.230 33.128  1.00 25.32 ?  33  LEU A CD2   1 
ATOM   178  N N     . ASN A 1 28  ? -30.309 -36.099 30.607  1.00 16.45 ?  34  ASN A N     1 
ATOM   179  C CA    . ASN A 1 28  ? -31.729 -36.434 30.708  1.00 18.26 ?  34  ASN A CA    1 
ATOM   180  C C     . ASN A 1 28  ? -32.421 -35.630 31.813  1.00 20.90 ?  34  ASN A C     1 
ATOM   181  O O     . ASN A 1 28  ? -33.335 -36.126 32.482  1.00 18.72 ?  34  ASN A O     1 
ATOM   182  C CB    . ASN A 1 28  ? -31.940 -37.946 30.908  1.00 20.37 ?  34  ASN A CB    1 
ATOM   183  C CG    . ASN A 1 28  ? -33.290 -38.422 30.382  1.00 26.23 ?  34  ASN A CG    1 
ATOM   184  O OD1   . ASN A 1 28  ? -33.912 -37.758 29.547  1.00 32.40 ?  34  ASN A OD1   1 
ATOM   185  N ND2   . ASN A 1 28  ? -33.754 -39.574 30.870  1.00 27.68 ?  34  ASN A ND2   1 
ATOM   186  N N     . VAL A 1 29  ? -32.007 -34.381 31.998  1.00 16.16 ?  35  VAL A N     1 
ATOM   187  C CA    . VAL A 1 29  ? -32.628 -33.493 32.981  1.00 16.38 ?  35  VAL A CA    1 
ATOM   188  C C     . VAL A 1 29  ? -33.745 -32.743 32.261  1.00 19.05 ?  35  VAL A C     1 
ATOM   189  O O     . VAL A 1 29  ? -33.498 -32.167 31.188  1.00 15.82 ?  35  VAL A O     1 
ATOM   190  C CB    . VAL A 1 29  ? -31.595 -32.530 33.596  1.00 19.30 ?  35  VAL A CB    1 
ATOM   191  C CG1   . VAL A 1 29  ? -32.278 -31.454 34.446  1.00 16.54 ?  35  VAL A CG1   1 
ATOM   192  C CG2   . VAL A 1 29  ? -30.549 -33.303 34.420  1.00 15.67 ?  35  VAL A CG2   1 
ATOM   193  N N     . PRO A 1 30  ? -34.974 -32.723 32.778  1.00 16.05 ?  36  PRO A N     1 
ATOM   194  C CA    . PRO A 1 30  ? -36.044 -31.982 32.090  1.00 17.38 ?  36  PRO A CA    1 
ATOM   195  C C     . PRO A 1 30  ? -35.684 -30.508 31.968  1.00 18.22 ?  36  PRO A C     1 
ATOM   196  O O     . PRO A 1 30  ? -35.205 -29.889 32.922  1.00 14.00 ?  36  PRO A O     1 
ATOM   197  C CB    . PRO A 1 30  ? -37.261 -32.192 33.000  1.00 22.20 ?  36  PRO A CB    1 
ATOM   198  C CG    . PRO A 1 30  ? -36.973 -33.496 33.694  1.00 21.14 ?  36  PRO A CG    1 
ATOM   199  C CD    . PRO A 1 30  ? -35.483 -33.460 33.948  1.00 18.13 ?  36  PRO A CD    1 
ATOM   200  N N     . PHE A 1 31  ? -35.912 -29.940 30.783  1.00 17.33 ?  37  PHE A N     1 
ATOM   201  C CA    . PHE A 1 31  ? -35.562 -28.540 30.584  1.00 16.56 ?  37  PHE A CA    1 
ATOM   202  C C     . PHE A 1 31  ? -36.314 -28.009 29.377  1.00 17.80 ?  37  PHE A C     1 
ATOM   203  O O     . PHE A 1 31  ? -36.836 -28.773 28.564  1.00 16.01 ?  37  PHE A O     1 
ATOM   204  C CB    . PHE A 1 31  ? -34.043 -28.350 30.386  1.00 16.00 ?  37  PHE A CB    1 
ATOM   205  C CG    . PHE A 1 31  ? -33.564 -28.733 29.020  1.00 14.45 ?  37  PHE A CG    1 
ATOM   206  C CD1   . PHE A 1 31  ? -33.338 -30.060 28.704  1.00 14.46 ?  37  PHE A CD1   1 
ATOM   207  C CD2   . PHE A 1 31  ? -33.367 -27.761 28.037  1.00 14.66 ?  37  PHE A CD2   1 
ATOM   208  C CE1   . PHE A 1 31  ? -32.913 -30.428 27.420  1.00 14.84 ?  37  PHE A CE1   1 
ATOM   209  C CE2   . PHE A 1 31  ? -32.942 -28.116 26.746  1.00 13.41 ?  37  PHE A CE2   1 
ATOM   210  C CZ    . PHE A 1 31  ? -32.722 -29.436 26.437  1.00 14.04 ?  37  PHE A CZ    1 
ATOM   211  N N     . MET A 1 32  ? -36.359 -26.686 29.273  1.00 15.56 ?  38  MET A N     1 
ATOM   212  C CA    . MET A 1 32  ? -36.894 -26.011 28.098  1.00 17.25 ?  38  MET A CA    1 
ATOM   213  C C     . MET A 1 32  ? -35.939 -24.895 27.705  1.00 15.43 ?  38  MET A C     1 
ATOM   214  O O     . MET A 1 32  ? -35.570 -24.064 28.542  1.00 17.12 ?  38  MET A O     1 
ATOM   215  C CB    . MET A 1 32  ? -38.291 -25.446 28.376  1.00 20.57 ?  38  MET A CB    1 
ATOM   216  C CG    . MET A 1 32  ? -39.021 -24.892 27.151  1.00 24.44 ?  38  MET A CG    1 
ATOM   217  S SD    . MET A 1 32  ? -39.525 -26.180 25.986  1.00 30.63 ?  38  MET A SD    1 
ATOM   218  C CE    . MET A 1 32  ? -40.626 -27.134 27.039  1.00 34.15 ?  38  MET A CE    1 
ATOM   219  N N     . LEU A 1 33  ? -35.509 -24.902 26.455  1.00 14.63 ?  39  LEU A N     1 
ATOM   220  C CA    . LEU A 1 33  ? -34.720 -23.814 25.900  1.00 15.62 ?  39  LEU A CA    1 
ATOM   221  C C     . LEU A 1 33  ? -35.654 -22.873 25.154  1.00 15.34 ?  39  LEU A C     1 
ATOM   222  O O     . LEU A 1 33  ? -36.401 -23.307 24.277  1.00 14.55 ?  39  LEU A O     1 
ATOM   223  C CB    . LEU A 1 33  ? -33.640 -24.353 24.959  1.00 14.36 ?  39  LEU A CB    1 
ATOM   224  C CG    . LEU A 1 33  ? -32.906 -23.326 24.099  1.00 16.90 ?  39  LEU A CG    1 
ATOM   225  C CD1   . LEU A 1 33  ? -32.045 -22.434 24.976  1.00 14.17 ?  39  LEU A CD1   1 
ATOM   226  C CD2   . LEU A 1 33  ? -32.058 -24.034 23.044  1.00 13.45 ?  39  LEU A CD2   1 
ATOM   227  N N     . VAL A 1 34  ? -35.615 -21.590 25.504  1.00 16.61 ?  40  VAL A N     1 
ATOM   228  C CA    . VAL A 1 34  ? -36.453 -20.584 24.868  1.00 17.29 ?  40  VAL A CA    1 
ATOM   229  C C     . VAL A 1 34  ? -35.562 -19.636 24.078  1.00 15.28 ?  40  VAL A C     1 
ATOM   230  O O     . VAL A 1 34  ? -34.560 -19.134 24.605  1.00 17.12 ?  40  VAL A O     1 
ATOM   231  C CB    . VAL A 1 34  ? -37.289 -19.807 25.898  1.00 17.08 ?  40  VAL A CB    1 
ATOM   232  C CG1   . VAL A 1 34  ? -38.222 -18.836 25.166  1.00 19.38 ?  40  VAL A CG1   1 
ATOM   233  C CG2   . VAL A 1 34  ? -38.079 -20.764 26.749  1.00 20.29 ?  40  VAL A CG2   1 
ATOM   234  N N     . ASP A 1 35  ? -35.914 -19.404 22.815  1.00 16.17 ?  41  ASP A N     1 
ATOM   235  C CA    . ASP A 1 35  ? -35.269 -18.370 22.017  1.00 16.22 ?  41  ASP A CA    1 
ATOM   236  C C     . ASP A 1 35  ? -36.301 -17.713 21.110  1.00 17.52 ?  41  ASP A C     1 
ATOM   237  O O     . ASP A 1 35  ? -37.241 -18.363 20.653  1.00 18.26 ?  41  ASP A O     1 
ATOM   238  C CB    . ASP A 1 35  ? -34.141 -18.935 21.148  1.00 14.62 ?  41  ASP A CB    1 
ATOM   239  C CG    . ASP A 1 35  ? -33.216 -17.850 20.645  1.00 15.23 ?  41  ASP A CG    1 
ATOM   240  O OD1   . ASP A 1 35  ? -32.342 -17.434 21.426  1.00 15.76 ?  41  ASP A OD1   1 
ATOM   241  O OD2   . ASP A 1 35  ? -33.372 -17.416 19.483  1.00 15.80 -1 41  ASP A OD2   1 
ATOM   242  N N     . MET A 1 36  ? -36.098 -16.421 20.818  1.00 18.38 ?  42  MET A N     1 
ATOM   243  C CA    . MET A 1 36  ? -37.031 -15.722 19.940  1.00 19.27 ?  42  MET A CA    1 
ATOM   244  C C     . MET A 1 36  ? -36.913 -16.182 18.487  1.00 19.86 ?  42  MET A C     1 
ATOM   245  O O     . MET A 1 36  ? -37.901 -16.108 17.744  1.00 21.12 ?  42  MET A O     1 
ATOM   246  C CB    . MET A 1 36  ? -36.826 -14.203 20.047  1.00 21.13 ?  42  MET A CB    1 
ATOM   247  C CG    . MET A 1 36  ? -35.527 -13.690 19.436  1.00 22.51 ?  42  MET A CG    1 
ATOM   248  S SD    . MET A 1 36  ? -35.376 -11.888 19.544  1.00 27.43 ?  42  MET A SD    1 
ATOM   249  C CE    . MET A 1 36  ? -35.167 -11.649 21.298  1.00 23.60 ?  42  MET A CE    1 
ATOM   250  N N     . LYS A 1 37  ? -35.746 -16.674 18.060  1.00 15.98 ?  43  LYS A N     1 
ATOM   251  C CA    . LYS A 1 37  ? -35.551 -17.157 16.697  1.00 17.83 ?  43  LYS A CA    1 
ATOM   252  C C     . LYS A 1 37  ? -35.849 -18.646 16.611  1.00 18.08 ?  43  LYS A C     1 
ATOM   253  O O     . LYS A 1 37  ? -35.909 -19.338 17.624  1.00 15.62 ?  43  LYS A O     1 
ATOM   254  C CB    . LYS A 1 37  ? -34.120 -16.940 16.201  1.00 15.55 ?  43  LYS A CB    1 
ATOM   255  C CG    . LYS A 1 37  ? -33.508 -15.576 16.453  1.00 18.45 ?  43  LYS A CG    1 
ATOM   256  C CD    . LYS A 1 37  ? -32.083 -15.545 15.901  1.00 16.87 ?  43  LYS A CD    1 
ATOM   257  C CE    . LYS A 1 37  ? -31.005 -15.749 16.977  1.00 16.05 ?  43  LYS A CE    1 
ATOM   258  N NZ    . LYS A 1 37  ? -31.135 -17.043 17.705  1.00 12.94 ?  43  LYS A NZ    1 
ATOM   259  N N     . ASP A 1 38  ? -35.975 -19.152 15.379  1.00 15.80 ?  44  ASP A N     1 
ATOM   260  C CA    . ASP A 1 38  ? -36.092 -20.598 15.183  1.00 18.43 ?  44  ASP A CA    1 
ATOM   261  C C     . ASP A 1 38  ? -34.748 -21.289 14.987  1.00 15.59 ?  44  ASP A C     1 
ATOM   262  O O     . ASP A 1 38  ? -34.710 -22.523 14.904  1.00 13.66 ?  44  ASP A O     1 
ATOM   263  C CB    . ASP A 1 38  ? -37.042 -20.934 14.011  1.00 18.13 ?  44  ASP A CB    1 
ATOM   264  C CG    . ASP A 1 38  ? -36.402 -20.775 12.608  1.00 26.38 ?  44  ASP A CG    1 
ATOM   265  O OD1   . ASP A 1 38  ? -35.228 -20.335 12.479  1.00 25.95 ?  44  ASP A OD1   1 
ATOM   266  O OD2   . ASP A 1 38  ? -37.100 -21.096 11.601  1.00 22.43 -1 44  ASP A OD2   1 
ATOM   267  N N     . SER A 1 39  ? -33.644 -20.545 14.937  1.00 16.11 ?  45  SER A N     1 
ATOM   268  C CA    . SER A 1 39  ? -32.342 -21.170 14.736  1.00 12.81 ?  45  SER A CA    1 
ATOM   269  C C     . SER A 1 39  ? -31.256 -20.429 15.513  1.00 12.80 ?  45  SER A C     1 
ATOM   270  O O     . SER A 1 39  ? -31.324 -19.209 15.712  1.00 12.97 ?  45  SER A O     1 
ATOM   271  C CB    . SER A 1 39  ? -31.987 -21.214 13.244  1.00 18.03 ?  45  SER A CB    1 
ATOM   272  O OG    . SER A 1 39  ? -32.217 -19.952 12.654  1.00 23.64 ?  45  SER A OG    1 
ATOM   273  N N     . PHE A 1 40  ? -30.264 -21.197 15.955  1.00 10.75 ?  46  PHE A N     1 
ATOM   274  C CA    . PHE A 1 40  ? -29.033 -20.648 16.527  1.00 9.66  ?  46  PHE A CA    1 
ATOM   275  C C     . PHE A 1 40  ? -28.247 -19.869 15.476  1.00 9.10  ?  46  PHE A C     1 
ATOM   276  O O     . PHE A 1 40  ? -28.147 -20.289 14.326  1.00 9.45  ?  46  PHE A O     1 
ATOM   277  C CB    . PHE A 1 40  ? -28.184 -21.800 17.073  1.00 10.32 ?  46  PHE A CB    1 
ATOM   278  C CG    . PHE A 1 40  ? -26.748 -21.416 17.368  1.00 10.45 ?  46  PHE A CG    1 
ATOM   279  C CD1   . PHE A 1 40  ? -26.420 -20.770 18.548  1.00 9.76  ?  46  PHE A CD1   1 
ATOM   280  C CD2   . PHE A 1 40  ? -25.741 -21.696 16.458  1.00 9.42  ?  46  PHE A CD2   1 
ATOM   281  C CE1   . PHE A 1 40  ? -25.108 -20.399 18.809  1.00 11.02 ?  46  PHE A CE1   1 
ATOM   282  C CE2   . PHE A 1 40  ? -24.432 -21.332 16.717  1.00 8.89  ?  46  PHE A CE2   1 
ATOM   283  C CZ    . PHE A 1 40  ? -24.120 -20.713 17.898  1.00 9.55  ?  46  PHE A CZ    1 
ATOM   284  N N     . HIS A 1 41  ? -27.684 -18.731 15.865  1.00 9.03  ?  47  HIS A N     1 
ATOM   285  C CA    . HIS A 1 41  ? -26.897 -17.897 14.965  1.00 9.21  ?  47  HIS A CA    1 
ATOM   286  C C     . HIS A 1 41  ? -25.442 -17.911 15.408  1.00 10.39 ?  47  HIS A C     1 
ATOM   287  O O     . HIS A 1 41  ? -25.127 -17.421 16.497  1.00 8.98  ?  47  HIS A O     1 
ATOM   288  C CB    . HIS A 1 41  ? -27.409 -16.464 14.957  1.00 9.08  ?  47  HIS A CB    1 
ATOM   289  C CG    . HIS A 1 41  ? -26.713 -15.587 13.964  1.00 8.92  ?  47  HIS A CG    1 
ATOM   290  N ND1   . HIS A 1 41  ? -26.607 -14.223 14.121  1.00 11.43 ?  47  HIS A ND1   1 
ATOM   291  C CD2   . HIS A 1 41  ? -26.109 -15.881 12.786  1.00 9.59  ?  47  HIS A CD2   1 
ATOM   292  C CE1   . HIS A 1 41  ? -25.967 -13.711 13.079  1.00 10.49 ?  47  HIS A CE1   1 
ATOM   293  N NE2   . HIS A 1 41  ? -25.648 -14.699 12.259  1.00 9.97  ?  47  HIS A NE2   1 
ATOM   294  N N     . HIS A 1 42  ? -24.559 -18.431 14.557  1.00 9.10  ?  48  HIS A N     1 
ATOM   295  C CA    . HIS A 1 42  ? -23.121 -18.415 14.825  1.00 9.08  ?  48  HIS A CA    1 
ATOM   296  C C     . HIS A 1 42  ? -22.621 -17.019 14.457  1.00 10.07 ?  48  HIS A C     1 
ATOM   297  O O     . HIS A 1 42  ? -22.059 -16.773 13.389  1.00 9.66  ?  48  HIS A O     1 
ATOM   298  C CB    . HIS A 1 42  ? -22.414 -19.519 14.048  1.00 8.35  ?  48  HIS A CB    1 
ATOM   299  C CG    . HIS A 1 42  ? -20.982 -19.710 14.425  1.00 10.42 ?  48  HIS A CG    1 
ATOM   300  N ND1   . HIS A 1 42  ? -20.580 -20.608 15.394  1.00 10.62 ?  48  HIS A ND1   1 
ATOM   301  C CD2   . HIS A 1 42  ? -19.857 -19.091 13.989  1.00 10.99 ?  48  HIS A CD2   1 
ATOM   302  C CE1   . HIS A 1 42  ? -19.264 -20.544 15.526  1.00 12.10 ?  48  HIS A CE1   1 
ATOM   303  N NE2   . HIS A 1 42  ? -18.802 -19.629 14.689  1.00 9.50  ?  48  HIS A NE2   1 
ATOM   304  N N     . ASN A 1 43  ? -22.880 -16.064 15.349  1.00 7.92  ?  49  ASN A N     1 
ATOM   305  C CA    . ASN A 1 43  ? -22.737 -14.671 14.943  1.00 10.39 ?  49  ASN A CA    1 
ATOM   306  C C     . ASN A 1 43  ? -21.280 -14.244 14.829  1.00 10.33 ?  49  ASN A C     1 
ATOM   307  O O     . ASN A 1 43  ? -21.000 -13.166 14.276  1.00 9.53  ?  49  ASN A O     1 
ATOM   308  C CB    . ASN A 1 43  ? -23.512 -13.751 15.905  1.00 11.68 ?  49  ASN A CB    1 
ATOM   309  C CG    . ASN A 1 43  ? -23.141 -13.965 17.362  1.00 12.41 ?  49  ASN A CG    1 
ATOM   310  O OD1   . ASN A 1 43  ? -22.097 -14.521 17.668  1.00 15.12 ?  49  ASN A OD1   1 
ATOM   311  N ND2   . ASN A 1 43  ? -24.004 -13.517 18.270  1.00 16.32 ?  49  ASN A ND2   1 
ATOM   312  N N     . VAL A 1 44  ? -20.348 -15.067 15.322  1.00 8.91  ?  50  VAL A N     1 
ATOM   313  C CA    . VAL A 1 44  ? -18.931 -14.800 15.088  1.00 10.15 ?  50  VAL A CA    1 
ATOM   314  C C     . VAL A 1 44  ? -18.642 -14.737 13.595  1.00 10.96 ?  50  VAL A C     1 
ATOM   315  O O     . VAL A 1 44  ? -17.734 -14.019 13.153  1.00 11.65 ?  50  VAL A O     1 
ATOM   316  C CB    . VAL A 1 44  ? -18.075 -15.867 15.804  1.00 10.81 ?  50  VAL A CB    1 
ATOM   317  C CG1   . VAL A 1 44  ? -16.605 -15.696 15.459  1.00 13.31 ?  50  VAL A CG1   1 
ATOM   318  C CG2   . VAL A 1 44  ? -18.273 -15.777 17.306  1.00 11.29 ?  50  VAL A CG2   1 
ATOM   319  N N     . ALA A 1 45  ? -19.438 -15.431 12.785  1.00 9.05  ?  51  ALA A N     1 
ATOM   320  C CA    . ALA A 1 45  ? -19.229 -15.461 11.344  1.00 8.16  ?  51  ALA A CA    1 
ATOM   321  C C     . ALA A 1 45  ? -20.174 -14.544 10.584  1.00 9.58  ?  51  ALA A C     1 
ATOM   322  O O     . ALA A 1 45  ? -20.249 -14.633 9.356   1.00 9.89  ?  51  ALA A O     1 
ATOM   323  C CB    . ALA A 1 45  ? -19.374 -16.892 10.834  1.00 7.89  ?  51  ALA A CB    1 
ATOM   324  N N     . ALA A 1 46  ? -20.895 -13.663 11.282  1.00 8.36  ?  52  ALA A N     1 
ATOM   325  C CA    . ALA A 1 46  ? -21.908 -12.835 10.628  1.00 9.94  ?  52  ALA A CA    1 
ATOM   326  C C     . ALA A 1 46  ? -21.313 -11.869 9.613   1.00 9.07  ?  52  ALA A C     1 
ATOM   327  O O     . ALA A 1 46  ? -21.980 -11.522 8.631   1.00 8.80  ?  52  ALA A O     1 
ATOM   328  C CB    . ALA A 1 46  ? -22.697 -12.057 11.685  1.00 9.52  ?  52  ALA A CB    1 
ATOM   329  N N     . LEU A 1 47  ? -20.094 -11.384 9.848   1.00 9.07  ?  53  LEU A N     1 
ATOM   330  C CA    . LEU A 1 47  ? -19.507 -10.438 8.911   1.00 8.89  ?  53  LEU A CA    1 
ATOM   331  C C     . LEU A 1 47  ? -19.036 -11.143 7.639   1.00 9.87  ?  53  LEU A C     1 
ATOM   332  O O     . LEU A 1 47  ? -19.258 -10.645 6.530   1.00 11.55 ?  53  LEU A O     1 
ATOM   333  C CB    . LEU A 1 47  ? -18.366 -9.668  9.584   1.00 9.96  ?  53  LEU A CB    1 
ATOM   334  C CG    . LEU A 1 47  ? -18.711 -9.002  10.927  1.00 11.35 ?  53  LEU A CG    1 
ATOM   335  C CD1   . LEU A 1 47  ? -17.552 -8.124  11.423  1.00 13.67 ?  53  LEU A CD1   1 
ATOM   336  C CD2   . LEU A 1 47  ? -19.998 -8.182  10.824  1.00 11.44 ?  53  LEU A CD2   1 
ATOM   337  N N     . ARG A 1 48  ? -18.432 -12.324 7.765   1.00 9.04  ?  54  ARG A N     1 
ATOM   338  C CA    . ARG A 1 48  ? -18.146 -13.135 6.581   1.00 9.25  ?  54  ARG A CA    1 
ATOM   339  C C     . ARG A 1 48  ? -19.425 -13.488 5.824   1.00 9.06  ?  54  ARG A C     1 
ATOM   340  O O     . ARG A 1 48  ? -19.437 -13.515 4.585   1.00 10.35 ?  54  ARG A O     1 
ATOM   341  C CB    . ARG A 1 48  ? -17.386 -14.382 7.008   1.00 10.95 ?  54  ARG A CB    1 
ATOM   342  C CG    . ARG A 1 48  ? -17.032 -15.417 5.938   1.00 14.31 ?  54  ARG A CG    1 
ATOM   343  C CD    . ARG A 1 48  ? -15.726 -15.170 5.202   1.00 14.78 ?  54  ARG A CD    1 
ATOM   344  N NE    . ARG A 1 48  ? -14.638 -14.633 6.012   1.00 12.21 ?  54  ARG A NE    1 
ATOM   345  C CZ    . ARG A 1 48  ? -13.719 -15.343 6.654   1.00 13.94 ?  54  ARG A CZ    1 
ATOM   346  N NH1   . ARG A 1 48  ? -13.710 -16.673 6.615   1.00 10.12 ?  54  ARG A NH1   1 
ATOM   347  N NH2   . ARG A 1 48  ? -12.788 -14.698 7.361   1.00 9.87  ?  54  ARG A NH2   1 
ATOM   348  N N     . ALA A 1 49  ? -20.510 -13.762 6.540   1.00 8.60  ?  55  ALA A N     1 
ATOM   349  C CA    . ALA A 1 49  ? -21.790 -14.019 5.884   1.00 7.76  ?  55  ALA A CA    1 
ATOM   350  C C     . ALA A 1 49  ? -22.373 -12.776 5.227   1.00 10.00 ?  55  ALA A C     1 
ATOM   351  O O     . ALA A 1 49  ? -23.316 -12.890 4.437   1.00 10.13 ?  55  ALA A O     1 
ATOM   352  C CB    . ALA A 1 49  ? -22.796 -14.595 6.884   1.00 9.98  ?  55  ALA A CB    1 
ATOM   353  N N     . SER A 1 50  ? -21.832 -11.605 5.516   1.00 9.99  ?  56  SER A N     1 
ATOM   354  C CA    . SER A 1 50  ? -22.233 -10.378 4.847   1.00 11.31 ?  56  SER A CA    1 
ATOM   355  C C     . SER A 1 50  ? -21.467 -10.093 3.563   1.00 10.73 ?  56  SER A C     1 
ATOM   356  O O     . SER A 1 50  ? -21.809 -9.126  2.874   1.00 9.78  ?  56  SER A O     1 
ATOM   357  C CB    . SER A 1 50  ? -22.050 -9.187  5.793   1.00 10.88 ?  56  SER A CB    1 
ATOM   358  O OG    . SER A 1 50  ? -22.994 -9.263  6.833   1.00 11.40 ?  56  SER A OG    1 
ATOM   359  N N     . VAL A 1 51  ? -20.432 -10.873 3.233   1.00 10.31 ?  57  VAL A N     1 
ATOM   360  C CA    . VAL A 1 51  ? -19.605 -10.568 2.069   1.00 11.57 ?  57  VAL A CA    1 
ATOM   361  C C     . VAL A 1 51  ? -19.438 -11.760 1.132   1.00 14.73 ?  57  VAL A C     1 
ATOM   362  O O     . VAL A 1 51  ? -18.987 -11.581 -0.003  1.00 14.16 ?  57  VAL A O     1 
ATOM   363  C CB    . VAL A 1 51  ? -18.204 -10.037 2.459   1.00 11.63 ?  57  VAL A CB    1 
ATOM   364  C CG1   . VAL A 1 51  ? -18.300 -8.692  3.185   1.00 12.97 ?  57  VAL A CG1   1 
ATOM   365  C CG2   . VAL A 1 51  ? -17.410 -11.059 3.292   1.00 12.28 ?  57  VAL A CG2   1 
ATOM   366  N N     . GLU A 1 52  ? -19.760 -12.976 1.580   1.00 10.63 ?  58  GLU A N     1 
ATOM   367  C CA    . GLU A 1 52  ? -19.476 -14.181 0.794   1.00 14.30 ?  58  GLU A CA    1 
ATOM   368  C C     . GLU A 1 52  ? -20.782 -14.855 0.378   1.00 11.98 ?  58  GLU A C     1 
ATOM   369  O O     . GLU A 1 52  ? -21.550 -15.310 1.235   1.00 11.93 ?  58  GLU A O     1 
ATOM   370  C CB    . GLU A 1 52  ? -18.587 -15.159 1.574   1.00 13.38 ?  58  GLU A CB    1 
ATOM   371  C CG    . GLU A 1 52  ? -18.326 -16.475 0.802   1.00 16.73 ?  58  GLU A CG    1 
ATOM   372  C CD    . GLU A 1 52  ? -17.523 -17.530 1.575   1.00 22.47 ?  58  GLU A CD    1 
ATOM   373  O OE1   . GLU A 1 52  ? -16.889 -17.206 2.614   1.00 19.72 ?  58  GLU A OE1   1 
ATOM   374  O OE2   . GLU A 1 52  ? -17.519 -18.707 1.129   1.00 25.41 -1 58  GLU A OE2   1 
ATOM   375  N N     . THR A 1 53  ? -21.036 -14.907 -0.935  1.00 12.73 ?  59  THR A N     1 
ATOM   376  C CA    . THR A 1 53  ? -22.242 -15.548 -1.437  1.00 12.96 ?  59  THR A CA    1 
ATOM   377  C C     . THR A 1 53  ? -22.287 -17.002 -0.974  1.00 14.13 ?  59  THR A C     1 
ATOM   378  O O     . THR A 1 53  ? -21.277 -17.711 -1.037  1.00 14.12 ?  59  THR A O     1 
ATOM   379  C CB    . THR A 1 53  ? -22.276 -15.475 -2.974  1.00 16.33 ?  59  THR A CB    1 
ATOM   380  O OG1   . THR A 1 53  ? -22.218 -14.102 -3.398  1.00 17.95 ?  59  THR A OG1   1 
ATOM   381  C CG2   . THR A 1 53  ? -23.576 -16.081 -3.498  1.00 18.60 ?  59  THR A CG2   1 
ATOM   382  N N     . GLY A 1 54  ? -23.453 -17.433 -0.487  1.00 12.48 ?  60  GLY A N     1 
ATOM   383  C CA    . GLY A 1 54  ? -23.683 -18.817 -0.120  1.00 16.21 ?  60  GLY A CA    1 
ATOM   384  C C     . GLY A 1 54  ? -23.190 -19.221 1.252   1.00 15.48 ?  60  GLY A C     1 
ATOM   385  O O     . GLY A 1 54  ? -23.356 -20.386 1.634   1.00 15.35 ?  60  GLY A O     1 
ATOM   386  N N     . PHE A 1 55  ? -22.592 -18.304 2.007   1.00 11.69 ?  61  PHE A N     1 
ATOM   387  C CA    . PHE A 1 55  ? -22.019 -18.652 3.300   1.00 13.31 ?  61  PHE A CA    1 
ATOM   388  C C     . PHE A 1 55  ? -23.052 -18.617 4.421   1.00 10.43 ?  61  PHE A C     1 
ATOM   389  O O     . PHE A 1 55  ? -22.917 -19.340 5.415   1.00 10.72 ?  61  PHE A O     1 
ATOM   390  C CB    . PHE A 1 55  ? -20.871 -17.690 3.613   1.00 11.31 ?  61  PHE A CB    1 
ATOM   391  C CG    . PHE A 1 55  ? -20.106 -18.051 4.848   1.00 11.48 ?  61  PHE A CG    1 
ATOM   392  C CD1   . PHE A 1 55  ? -19.229 -19.123 4.842   1.00 16.67 ?  61  PHE A CD1   1 
ATOM   393  C CD2   . PHE A 1 55  ? -20.289 -17.348 6.022   1.00 11.96 ?  61  PHE A CD2   1 
ATOM   394  C CE1   . PHE A 1 55  ? -18.533 -19.481 5.981   1.00 17.33 ?  61  PHE A CE1   1 
ATOM   395  C CE2   . PHE A 1 55  ? -19.601 -17.689 7.164   1.00 13.22 ?  61  PHE A CE2   1 
ATOM   396  C CZ    . PHE A 1 55  ? -18.716 -18.762 7.152   1.00 16.15 ?  61  PHE A CZ    1 
ATOM   397  N N     . ALA A 1 56  ? -24.072 -17.762 4.297   1.00 10.65 ?  62  ALA A N     1 
ATOM   398  C CA    . ALA A 1 56  ? -24.976 -17.529 5.423   1.00 10.06 ?  62  ALA A CA    1 
ATOM   399  C C     . ALA A 1 56  ? -25.648 -18.807 5.891   1.00 8.64  ?  62  ALA A C     1 
ATOM   400  O O     . ALA A 1 56  ? -25.936 -18.947 7.083   1.00 9.40  ?  62  ALA A O     1 
ATOM   401  C CB    . ALA A 1 56  ? -26.033 -16.494 5.032   1.00 11.99 ?  62  ALA A CB    1 
ATOM   402  N N     . LYS A 1 57  ? -25.896 -19.758 4.985   1.00 9.57  ?  63  LYS A N     1 
ATOM   403  C CA    . LYS A 1 57  ? -26.562 -20.997 5.386   1.00 12.34 ?  63  LYS A CA    1 
ATOM   404  C C     . LYS A 1 57  ? -25.707 -21.862 6.304   1.00 13.63 ?  63  LYS A C     1 
ATOM   405  O O     . LYS A 1 57  ? -26.237 -22.767 6.967   1.00 12.49 ?  63  LYS A O     1 
ATOM   406  C CB    . LYS A 1 57  ? -26.972 -21.804 4.152   1.00 15.69 ?  63  LYS A CB    1 
ATOM   407  C CG    . LYS A 1 57  ? -25.801 -22.330 3.330   1.00 16.64 ?  63  LYS A CG    1 
ATOM   408  C CD    . LYS A 1 57  ? -26.308 -23.169 2.162   1.00 24.52 ?  63  LYS A CD    1 
ATOM   409  C CE    . LYS A 1 57  ? -25.179 -23.581 1.225   1.00 32.50 ?  63  LYS A CE    1 
ATOM   410  N NZ    . LYS A 1 57  ? -24.727 -22.451 0.353   1.00 42.43 ?  63  LYS A NZ    1 
ATOM   411  N N     . LYS A 1 58  ? -24.402 -21.599 6.382   1.00 12.00 ?  64  LYS A N     1 
ATOM   412  C CA    . LYS A 1 58  ? -23.539 -22.261 7.352   1.00 12.23 ?  64  LYS A CA    1 
ATOM   413  C C     . LYS A 1 58  ? -23.582 -21.620 8.729   1.00 10.98 ?  64  LYS A C     1 
ATOM   414  O O     . LYS A 1 58  ? -22.931 -22.126 9.644   1.00 11.12 ?  64  LYS A O     1 
ATOM   415  C CB    . LYS A 1 58  ? -22.088 -22.265 6.835   1.00 16.94 ?  64  LYS A CB    1 
ATOM   416  C CG    . LYS A 1 58  ? -21.964 -22.909 5.444   1.00 20.50 ?  64  LYS A CG    1 
ATOM   417  C CD    . LYS A 1 58  ? -20.508 -23.107 5.020   1.00 35.36 ?  64  LYS A CD    1 
ATOM   418  C CE    . LYS A 1 58  ? -20.020 -24.532 5.313   1.00 55.08 ?  64  LYS A CE    1 
ATOM   419  N NZ    . LYS A 1 58  ? -19.763 -24.799 6.770   1.00 51.70 ?  64  LYS A NZ    1 
ATOM   420  N N     . THR A 1 59  ? -24.282 -20.501 8.898   1.00 9.77  ?  65  THR A N     1 
ATOM   421  C CA    . THR A 1 59  ? -24.275 -19.773 10.165  1.00 8.89  ?  65  THR A CA    1 
ATOM   422  C C     . THR A 1 59  ? -25.583 -19.849 10.955  1.00 9.80  ?  65  THR A C     1 
ATOM   423  O O     . THR A 1 59  ? -25.671 -19.220 12.025  1.00 9.77  ?  65  THR A O     1 
ATOM   424  C CB    . THR A 1 59  ? -23.911 -18.286 9.948   1.00 9.88  ?  65  THR A CB    1 
ATOM   425  O OG1   . THR A 1 59  ? -24.978 -17.577 9.300   1.00 10.18 ?  65  THR A OG1   1 
ATOM   426  C CG2   . THR A 1 59  ? -22.637 -18.143 9.127   1.00 8.71  ?  65  THR A CG2   1 
ATOM   427  N N     . PHE A 1 60  ? -26.600 -20.570 10.471  1.00 9.39  ?  66  PHE A N     1 
ATOM   428  C CA    . PHE A 1 60  ? -27.866 -20.710 11.196  1.00 11.44 ?  66  PHE A CA    1 
ATOM   429  C C     . PHE A 1 60  ? -28.177 -22.193 11.336  1.00 11.48 ?  66  PHE A C     1 
ATOM   430  O O     . PHE A 1 60  ? -28.126 -22.929 10.343  1.00 12.71 ?  66  PHE A O     1 
ATOM   431  C CB    . PHE A 1 60  ? -29.023 -19.983 10.478  1.00 10.63 ?  66  PHE A CB    1 
ATOM   432  C CG    . PHE A 1 60  ? -28.959 -18.474 10.583  1.00 9.27  ?  66  PHE A CG    1 
ATOM   433  C CD1   . PHE A 1 60  ? -29.449 -17.814 11.702  1.00 9.47  ?  66  PHE A CD1   1 
ATOM   434  C CD2   . PHE A 1 60  ? -28.415 -17.720 9.563   1.00 9.43  ?  66  PHE A CD2   1 
ATOM   435  C CE1   . PHE A 1 60  ? -29.385 -16.424 11.795  1.00 9.53  ?  66  PHE A CE1   1 
ATOM   436  C CE2   . PHE A 1 60  ? -28.349 -16.332 9.654   1.00 9.39  ?  66  PHE A CE2   1 
ATOM   437  C CZ    . PHE A 1 60  ? -28.844 -15.691 10.767  1.00 10.50 ?  66  PHE A CZ    1 
ATOM   438  N N     . ILE A 1 61  ? -28.508 -22.632 12.555  1.00 10.98 ?  67  ILE A N     1 
ATOM   439  C CA    . ILE A 1 61  ? -28.713 -24.053 12.857  1.00 10.86 ?  67  ILE A CA    1 
ATOM   440  C C     . ILE A 1 61  ? -30.052 -24.222 13.573  1.00 13.00 ?  67  ILE A C     1 
ATOM   441  O O     . ILE A 1 61  ? -30.243 -23.676 14.663  1.00 12.20 ?  67  ILE A O     1 
ATOM   442  C CB    . ILE A 1 61  ? -27.582 -24.635 13.726  1.00 11.50 ?  67  ILE A CB    1 
ATOM   443  C CG1   . ILE A 1 61  ? -26.203 -24.275 13.155  1.00 9.94  ?  67  ILE A CG1   1 
ATOM   444  C CG2   . ILE A 1 61  ? -27.797 -26.144 13.888  1.00 11.69 ?  67  ILE A CG2   1 
ATOM   445  C CD1   . ILE A 1 61  ? -25.012 -24.758 13.998  1.00 11.71 ?  67  ILE A CD1   1 
ATOM   446  N N     . SER A 1 62  ? -30.963 -24.996 12.975  1.00 14.82 ?  68  SER A N     1 
ATOM   447  C CA    . SER A 1 62  ? -32.306 -25.194 13.536  1.00 15.11 ?  68  SER A CA    1 
ATOM   448  C C     . SER A 1 62  ? -32.281 -25.721 14.973  1.00 12.72 ?  68  SER A C     1 
ATOM   449  O O     . SER A 1 62  ? -31.689 -26.770 15.239  1.00 14.54 ?  68  SER A O     1 
ATOM   450  C CB    . SER A 1 62  ? -33.078 -26.196 12.680  1.00 18.00 ?  68  SER A CB    1 
ATOM   451  O OG    . SER A 1 62  ? -34.220 -26.659 13.403  1.00 18.47 ?  68  SER A OG    1 
ATOM   452  N N     . TYR A 1 63  ? -32.994 -25.038 15.883  1.00 12.46 ?  69  TYR A N     1 
ATOM   453  C CA    . TYR A 1 63  ? -33.086 -25.532 17.259  1.00 14.30 ?  69  TYR A CA    1 
ATOM   454  C C     . TYR A 1 63  ? -33.920 -26.798 17.330  1.00 16.60 ?  69  TYR A C     1 
ATOM   455  O O     . TYR A 1 63  ? -33.583 -27.732 18.073  1.00 17.09 ?  69  TYR A O     1 
ATOM   456  C CB    . TYR A 1 63  ? -33.738 -24.515 18.187  1.00 13.55 ?  69  TYR A CB    1 
ATOM   457  C CG    . TYR A 1 63  ? -32.981 -23.244 18.447  1.00 14.43 ?  69  TYR A CG    1 
ATOM   458  C CD1   . TYR A 1 63  ? -31.765 -23.254 19.125  1.00 10.75 ?  69  TYR A CD1   1 
ATOM   459  C CD2   . TYR A 1 63  ? -33.514 -22.027 18.058  1.00 12.84 ?  69  TYR A CD2   1 
ATOM   460  C CE1   . TYR A 1 63  ? -31.094 -22.065 19.381  1.00 11.57 ?  69  TYR A CE1   1 
ATOM   461  C CE2   . TYR A 1 63  ? -32.862 -20.848 18.300  1.00 12.61 ?  69  TYR A CE2   1 
ATOM   462  C CZ    . TYR A 1 63  ? -31.647 -20.871 18.951  1.00 11.40 ?  69  TYR A CZ    1 
ATOM   463  O OH    . TYR A 1 63  ? -31.024 -19.675 19.184  1.00 11.59 ?  69  TYR A OH    1 
ATOM   464  N N     . SER A 1 64  ? -35.042 -26.827 16.605  1.00 17.03 ?  70  SER A N     1 
ATOM   465  C CA    . SER A 1 64  ? -35.969 -27.945 16.760  1.00 17.60 ?  70  SER A CA    1 
ATOM   466  C C     . SER A 1 64  ? -35.332 -29.243 16.295  1.00 17.87 ?  70  SER A C     1 
ATOM   467  O O     . SER A 1 64  ? -35.607 -30.300 16.866  1.00 20.73 ?  70  SER A O     1 
ATOM   468  C CB    . SER A 1 64  ? -37.274 -27.684 15.998  1.00 19.86 ?  70  SER A CB    1 
ATOM   469  O OG    . SER A 1 64  ? -37.031 -27.622 14.598  1.00 25.72 ?  70  SER A OG    1 
ATOM   470  N N     . VAL A 1 65  ? -34.448 -29.183 15.296  1.00 18.20 ?  71  VAL A N     1 
ATOM   471  C CA    . VAL A 1 65  ? -33.837 -30.413 14.797  1.00 15.51 ?  71  VAL A CA    1 
ATOM   472  C C     . VAL A 1 65  ? -32.991 -31.067 15.881  1.00 19.86 ?  71  VAL A C     1 
ATOM   473  O O     . VAL A 1 65  ? -32.977 -32.299 16.028  1.00 19.13 ?  71  VAL A O     1 
ATOM   474  C CB    . VAL A 1 65  ? -33.032 -30.131 13.517  1.00 19.47 ?  71  VAL A CB    1 
ATOM   475  C CG1   . VAL A 1 65  ? -32.082 -31.292 13.218  1.00 19.41 ?  71  VAL A CG1   1 
ATOM   476  C CG2   . VAL A 1 65  ? -33.982 -29.893 12.350  1.00 15.75 ?  71  VAL A CG2   1 
ATOM   477  N N     . THR A 1 66  ? -32.308 -30.258 16.690  1.00 16.78 ?  72  THR A N     1 
ATOM   478  C CA    . THR A 1 66  ? -31.441 -30.787 17.735  1.00 18.83 ?  72  THR A CA    1 
ATOM   479  C C     . THR A 1 66  ? -32.200 -31.104 19.009  1.00 17.30 ?  72  THR A C     1 
ATOM   480  O O     . THR A 1 66  ? -31.964 -32.150 19.624  1.00 17.68 ?  72  THR A O     1 
ATOM   481  C CB    . THR A 1 66  ? -30.334 -29.781 18.064  1.00 19.20 ?  72  THR A CB    1 
ATOM   482  O OG1   . THR A 1 66  ? -29.501 -29.607 16.910  1.00 16.87 ?  72  THR A OG1   1 
ATOM   483  C CG2   . THR A 1 66  ? -29.504 -30.257 19.255  1.00 16.07 ?  72  THR A CG2   1 
ATOM   484  N N     . PHE A 1 67  ? -33.109 -30.213 19.409  1.00 15.13 ?  73  PHE A N     1 
ATOM   485  C CA    . PHE A 1 67  ? -33.706 -30.269 20.735  1.00 18.48 ?  73  PHE A CA    1 
ATOM   486  C C     . PHE A 1 67  ? -35.180 -30.673 20.766  1.00 18.76 ?  73  PHE A C     1 
ATOM   487  O O     . PHE A 1 67  ? -35.676 -31.006 21.846  1.00 18.80 ?  73  PHE A O     1 
ATOM   488  C CB    . PHE A 1 67  ? -33.545 -28.913 21.433  1.00 16.28 ?  73  PHE A CB    1 
ATOM   489  C CG    . PHE A 1 67  ? -32.120 -28.525 21.657  1.00 14.92 ?  73  PHE A CG    1 
ATOM   490  C CD1   . PHE A 1 67  ? -31.312 -29.280 22.493  1.00 14.31 ?  73  PHE A CD1   1 
ATOM   491  C CD2   . PHE A 1 67  ? -31.590 -27.391 21.063  1.00 15.03 ?  73  PHE A CD2   1 
ATOM   492  C CE1   . PHE A 1 67  ? -29.985 -28.932 22.718  1.00 16.20 ?  73  PHE A CE1   1 
ATOM   493  C CE2   . PHE A 1 67  ? -30.266 -27.034 21.294  1.00 14.75 ?  73  PHE A CE2   1 
ATOM   494  C CZ    . PHE A 1 67  ? -29.465 -27.810 22.121  1.00 12.35 ?  73  PHE A CZ    1 
ATOM   495  N N     . LYS A 1 68  ? -35.892 -30.634 19.642  1.00 18.51 ?  74  LYS A N     1 
ATOM   496  C CA    . LYS A 1 68  ? -37.256 -31.204 19.535  1.00 18.44 ?  74  LYS A CA    1 
ATOM   497  C C     . LYS A 1 68  ? -38.153 -30.559 20.592  1.00 23.24 ?  74  LYS A C     1 
ATOM   498  O O     . LYS A 1 68  ? -38.208 -29.321 20.667  1.00 19.24 ?  74  LYS A O     1 
ATOM   499  C CB    . LYS A 1 68  ? -37.143 -32.720 19.598  1.00 24.01 ?  74  LYS A CB    1 
ATOM   500  C CG    . LYS A 1 68  ? -36.333 -33.317 18.445  1.00 24.99 ?  74  LYS A CG    1 
ATOM   501  C CD    . LYS A 1 68  ? -37.093 -33.131 17.129  1.00 35.24 ?  74  LYS A CD    1 
ATOM   502  C CE    . LYS A 1 68  ? -36.325 -33.663 15.924  1.00 47.31 ?  74  LYS A CE    1 
ATOM   503  N NZ    . LYS A 1 68  ? -36.993 -33.311 14.635  1.00 50.90 ?  74  LYS A NZ    1 
ATOM   504  N N     . ASP A 1 69  ? -38.876 -31.333 21.418  1.00 20.91 ?  75  ASP A N     1 
ATOM   505  C CA    . ASP A 1 69  ? -39.808 -30.718 22.357  1.00 22.89 ?  75  ASP A CA    1 
ATOM   506  C C     . ASP A 1 69  ? -39.130 -30.045 23.534  1.00 19.29 ?  75  ASP A C     1 
ATOM   507  O O     . ASP A 1 69  ? -39.833 -29.453 24.358  1.00 22.21 ?  75  ASP A O     1 
ATOM   508  C CB    . ASP A 1 69  ? -40.809 -31.756 22.879  1.00 29.11 ?  75  ASP A CB    1 
ATOM   509  C CG    . ASP A 1 69  ? -41.952 -32.007 21.906  1.00 38.37 ?  75  ASP A CG    1 
ATOM   510  O OD1   . ASP A 1 69  ? -42.118 -31.212 20.949  1.00 33.42 ?  75  ASP A OD1   1 
ATOM   511  O OD2   . ASP A 1 69  ? -42.686 -33.004 22.105  1.00 44.94 -1 75  ASP A OD2   1 
ATOM   512  N N     . ASN A 1 70  ? -37.809 -30.120 23.656  1.00 18.49 ?  76  ASN A N     1 
ATOM   513  C CA    . ASN A 1 70  ? -37.123 -29.332 24.670  1.00 17.93 ?  76  ASN A CA    1 
ATOM   514  C C     . ASN A 1 70  ? -36.865 -27.901 24.223  1.00 18.89 ?  76  ASN A C     1 
ATOM   515  O O     . ASN A 1 70  ? -36.218 -27.143 24.952  1.00 16.76 ?  76  ASN A O     1 
ATOM   516  C CB    . ASN A 1 70  ? -35.817 -30.011 25.048  1.00 20.24 ?  76  ASN A CB    1 
ATOM   517  C CG    . ASN A 1 70  ? -36.051 -31.284 25.831  1.00 21.28 ?  76  ASN A CG    1 
ATOM   518  O OD1   . ASN A 1 70  ? -36.799 -31.283 26.810  1.00 27.15 ?  76  ASN A OD1   1 
ATOM   519  N ND2   . ASN A 1 70  ? -35.429 -32.364 25.409  1.00 18.62 ?  76  ASN A ND2   1 
ATOM   520  N N     . PHE A 1 71  ? -37.350 -27.522 23.048  1.00 19.06 ?  77  PHE A N     1 
ATOM   521  C CA    . PHE A 1 71  ? -37.195 -26.169 22.541  1.00 17.23 ?  77  PHE A CA    1 
ATOM   522  C C     . PHE A 1 71  ? -38.557 -25.535 22.321  1.00 19.58 ?  77  PHE A C     1 
ATOM   523  O O     . PHE A 1 71  ? -39.462 -26.172 21.780  1.00 19.01 ?  77  PHE A O     1 
ATOM   524  C CB    . PHE A 1 71  ? -36.441 -26.132 21.228  1.00 16.50 ?  77  PHE A CB    1 
ATOM   525  C CG    . PHE A 1 71  ? -36.471 -24.781 20.592  1.00 17.74 ?  77  PHE A CG    1 
ATOM   526  C CD1   . PHE A 1 71  ? -35.762 -23.730 21.164  1.00 15.52 ?  77  PHE A CD1   1 
ATOM   527  C CD2   . PHE A 1 71  ? -37.244 -24.543 19.459  1.00 17.96 ?  77  PHE A CD2   1 
ATOM   528  C CE1   . PHE A 1 71  ? -35.792 -22.460 20.593  1.00 17.33 ?  77  PHE A CE1   1 
ATOM   529  C CE2   . PHE A 1 71  ? -37.287 -23.272 18.885  1.00 18.98 ?  77  PHE A CE2   1 
ATOM   530  C CZ    . PHE A 1 71  ? -36.563 -22.237 19.454  1.00 16.81 ?  77  PHE A CZ    1 
ATOM   531  N N     . ARG A 1 72  ? -38.679 -24.269 22.715  1.00 19.64 ?  78  ARG A N     1 
ATOM   532  C CA    . ARG A 1 72  ? -39.883 -23.475 22.506  1.00 19.87 ?  78  ARG A CA    1 
ATOM   533  C C     . ARG A 1 72  ? -39.460 -22.117 21.977  1.00 20.05 ?  78  ARG A C     1 
ATOM   534  O O     . ARG A 1 72  ? -38.717 -21.404 22.649  1.00 19.19 ?  78  ARG A O     1 
ATOM   535  C CB    . ARG A 1 72  ? -40.665 -23.300 23.812  1.00 24.47 ?  78  ARG A CB    1 
ATOM   536  C CG    . ARG A 1 72  ? -41.950 -22.493 23.662  1.00 27.77 ?  78  ARG A CG    1 
ATOM   537  C CD    . ARG A 1 72  ? -42.948 -23.246 22.801  1.00 32.83 ?  78  ARG A CD    1 
ATOM   538  N N     . GLN A 1 73  ? -39.948 -21.742 20.799  1.00 19.80 ?  79  GLN A N     1 
ATOM   539  C CA    . GLN A 1 73  ? -39.694 -20.400 20.278  1.00 20.80 ?  79  GLN A CA    1 
ATOM   540  C C     . GLN A 1 73  ? -40.594 -19.378 20.967  1.00 22.56 ?  79  GLN A C     1 
ATOM   541  O O     . GLN A 1 73  ? -41.780 -19.636 21.205  1.00 26.18 ?  79  GLN A O     1 
ATOM   542  C CB    . GLN A 1 73  ? -39.908 -20.372 18.768  1.00 22.75 ?  79  GLN A CB    1 
ATOM   543  C CG    . GLN A 1 73  ? -39.678 -19.005 18.136  1.00 24.76 ?  79  GLN A CG    1 
ATOM   544  C CD    . GLN A 1 73  ? -39.683 -19.063 16.610  1.00 28.71 ?  79  GLN A CD    1 
ATOM   545  O OE1   . GLN A 1 73  ? -40.126 -20.056 16.014  1.00 31.66 ?  79  GLN A OE1   1 
ATOM   546  N NE2   . GLN A 1 73  ? -39.177 -18.003 15.969  1.00 28.38 ?  79  GLN A NE2   1 
ATOM   547  N N     . GLY A 1 74  ? -40.027 -18.234 21.333  1.00 19.65 ?  80  GLY A N     1 
ATOM   548  C CA    . GLY A 1 74  ? -40.844 -17.191 21.930  1.00 25.42 ?  80  GLY A CA    1 
ATOM   549  C C     . GLY A 1 74  ? -39.996 -16.085 22.509  1.00 25.35 ?  80  GLY A C     1 
ATOM   550  O O     . GLY A 1 74  ? -38.777 -16.209 22.660  1.00 20.49 ?  80  GLY A O     1 
ATOM   551  N N     . LEU A 1 75  ? -40.675 -14.995 22.862  1.00 23.78 ?  81  LEU A N     1 
ATOM   552  C CA    . LEU A 1 75  ? -40.039 -13.795 23.389  1.00 25.88 ?  81  LEU A CA    1 
ATOM   553  C C     . LEU A 1 75  ? -40.326 -13.703 24.881  1.00 27.33 ?  81  LEU A C     1 
ATOM   554  O O     . LEU A 1 75  ? -41.489 -13.644 25.291  1.00 31.23 ?  81  LEU A O     1 
ATOM   555  C CB    . LEU A 1 75  ? -40.545 -12.551 22.656  1.00 29.45 ?  81  LEU A CB    1 
ATOM   556  C CG    . LEU A 1 75  ? -39.946 -11.214 23.092  1.00 31.94 ?  81  LEU A CG    1 
ATOM   557  C CD1   . LEU A 1 75  ? -38.480 -11.192 22.736  1.00 28.25 ?  81  LEU A CD1   1 
ATOM   558  C CD2   . LEU A 1 75  ? -40.673 -10.042 22.447  1.00 32.94 ?  81  LEU A CD2   1 
ATOM   559  N N     . VAL A 1 76  ? -39.282 -13.706 25.694  1.00 25.38 ?  82  VAL A N     1 
ATOM   560  C CA    . VAL A 1 76  ? -39.477 -13.617 27.135  1.00 28.57 ?  82  VAL A CA    1 
ATOM   561  C C     . VAL A 1 76  ? -39.627 -12.149 27.509  1.00 29.95 ?  82  VAL A C     1 
ATOM   562  O O     . VAL A 1 76  ? -38.789 -11.317 27.143  1.00 27.59 ?  82  VAL A O     1 
ATOM   563  C CB    . VAL A 1 76  ? -38.313 -14.280 27.889  1.00 31.54 ?  82  VAL A CB    1 
ATOM   564  C CG1   . VAL A 1 76  ? -38.490 -14.114 29.388  1.00 28.00 ?  82  VAL A CG1   1 
ATOM   565  C CG2   . VAL A 1 76  ? -38.216 -15.766 27.506  1.00 28.11 ?  82  VAL A CG2   1 
ATOM   566  N N     . VAL A 1 77  ? -40.703 -11.826 28.228  1.00 32.61 ?  83  VAL A N     1 
ATOM   567  C CA    . VAL A 1 77  ? -41.011 -10.444 28.582  1.00 35.54 ?  83  VAL A CA    1 
ATOM   568  C C     . VAL A 1 77  ? -40.832 -10.154 30.069  1.00 35.97 ?  83  VAL A C     1 
ATOM   569  O O     . VAL A 1 77  ? -40.703 -8.977  30.439  1.00 37.76 ?  83  VAL A O     1 
ATOM   570  C CB    . VAL A 1 77  ? -42.435 -10.054 28.136  1.00 33.26 ?  83  VAL A CB    1 
ATOM   571  C CG1   . VAL A 1 77  ? -42.551 -10.104 26.620  1.00 33.99 ?  83  VAL A CG1   1 
ATOM   572  C CG2   . VAL A 1 77  ? -43.471 -10.972 28.780  1.00 35.05 ?  83  VAL A CG2   1 
ATOM   573  N N     . GLY A 1 78  ? -40.834 -11.164 30.925  1.00 34.28 ?  84  GLY A N     1 
ATOM   574  C CA    . GLY A 1 78  ? -40.557 -10.946 32.333  1.00 35.52 ?  84  GLY A CA    1 
ATOM   575  C C     . GLY A 1 78  ? -40.284 -12.259 33.032  1.00 35.00 ?  84  GLY A C     1 
ATOM   576  O O     . GLY A 1 78  ? -40.515 -13.342 32.491  1.00 32.08 ?  84  GLY A O     1 
ATOM   577  N N     . ILE A 1 79  ? -39.765 -12.141 34.250  1.00 35.11 ?  85  ILE A N     1 
ATOM   578  C CA    . ILE A 1 79  ? -39.542 -13.275 35.137  1.00 38.79 ?  85  ILE A CA    1 
ATOM   579  C C     . ILE A 1 79  ? -40.331 -13.028 36.420  1.00 43.71 ?  85  ILE A C     1 
ATOM   580  O O     . ILE A 1 79  ? -40.179 -11.977 37.053  1.00 43.40 ?  85  ILE A O     1 
ATOM   581  C CB    . ILE A 1 79  ? -38.044 -13.474 35.437  1.00 40.19 ?  85  ILE A CB    1 
ATOM   582  C CG1   . ILE A 1 79  ? -37.238 -13.663 34.136  1.00 39.72 ?  85  ILE A CG1   1 
ATOM   583  C CG2   . ILE A 1 79  ? -37.841 -14.641 36.398  1.00 40.68 ?  85  ILE A CG2   1 
ATOM   584  C CD1   . ILE A 1 79  ? -37.692 -14.843 33.271  1.00 37.52 ?  85  ILE A CD1   1 
ATOM   585  N N     . ASP A 1 80  ? -41.180 -13.987 36.789  1.00 41.30 ?  86  ASP A N     1 
ATOM   586  C CA    . ASP A 1 80  ? -41.991 -13.931 38.010  1.00 43.80 ?  86  ASP A CA    1 
ATOM   587  C C     . ASP A 1 80  ? -41.229 -14.668 39.108  1.00 45.42 ?  86  ASP A C     1 
ATOM   588  O O     . ASP A 1 80  ? -41.355 -15.882 39.268  1.00 44.92 ?  86  ASP A O     1 
ATOM   589  C CB    . ASP A 1 80  ? -43.362 -14.546 37.756  1.00 45.93 ?  86  ASP A CB    1 
ATOM   590  C CG    . ASP A 1 80  ? -44.287 -14.483 38.972  1.00 55.43 ?  86  ASP A CG    1 
ATOM   591  O OD1   . ASP A 1 80  ? -43.816 -14.339 40.130  1.00 50.55 ?  86  ASP A OD1   1 
ATOM   592  O OD2   . ASP A 1 80  ? -45.510 -14.602 38.752  1.00 54.30 -1 86  ASP A OD2   1 
ATOM   593  N N     . LEU A 1 81  ? -40.439 -13.921 39.885  1.00 45.36 ?  87  LEU A N     1 
ATOM   594  C CA    . LEU A 1 81  ? -39.572 -14.554 40.877  1.00 47.54 ?  87  LEU A CA    1 
ATOM   595  C C     . LEU A 1 81  ? -40.352 -15.138 42.047  1.00 48.78 ?  87  LEU A C     1 
ATOM   596  O O     . LEU A 1 81  ? -39.878 -16.083 42.686  1.00 44.92 ?  87  LEU A O     1 
ATOM   597  C CB    . LEU A 1 81  ? -38.542 -13.555 41.394  1.00 47.75 ?  87  LEU A CB    1 
ATOM   598  C CG    . LEU A 1 81  ? -37.368 -13.310 40.459  1.00 46.07 ?  87  LEU A CG    1 
ATOM   599  C CD1   . LEU A 1 81  ? -36.383 -12.353 41.109  1.00 49.05 ?  87  LEU A CD1   1 
ATOM   600  C CD2   . LEU A 1 81  ? -36.707 -14.639 40.127  1.00 44.84 ?  87  LEU A CD2   1 
ATOM   601  N N     . LYS A 1 82  ? -41.526 -14.582 42.358  1.00 50.92 ?  88  LYS A N     1 
ATOM   602  C CA    . LYS A 1 82  ? -42.304 -15.083 43.487  1.00 53.12 ?  88  LYS A CA    1 
ATOM   603  C C     . LYS A 1 82  ? -42.879 -16.462 43.184  1.00 51.86 ?  88  LYS A C     1 
ATOM   604  O O     . LYS A 1 82  ? -42.795 -17.376 44.014  1.00 52.67 ?  88  LYS A O     1 
ATOM   605  C CB    . LYS A 1 82  ? -43.416 -14.092 43.839  1.00 53.06 ?  88  LYS A CB    1 
ATOM   606  N N     . ASN A 1 83  ? -43.453 -16.636 41.994  1.00 50.86 ?  89  ASN A N     1 
ATOM   607  C CA    . ASN A 1 83  ? -44.026 -17.908 41.575  1.00 50.09 ?  89  ASN A CA    1 
ATOM   608  C C     . ASN A 1 83  ? -43.095 -18.714 40.676  1.00 46.62 ?  89  ASN A C     1 
ATOM   609  O O     . ASN A 1 83  ? -43.535 -19.705 40.084  1.00 44.39 ?  89  ASN A O     1 
ATOM   610  C CB    . ASN A 1 83  ? -45.359 -17.674 40.867  1.00 48.49 ?  89  ASN A CB    1 
ATOM   611  C CG    . ASN A 1 83  ? -46.339 -16.903 41.725  1.00 56.38 ?  89  ASN A CG    1 
ATOM   612  O OD1   . ASN A 1 83  ? -46.837 -17.411 42.736  1.00 51.41 ?  89  ASN A OD1   1 
ATOM   613  N ND2   . ASN A 1 83  ? -46.627 -15.669 41.325  1.00 54.68 ?  89  ASN A ND2   1 
ATOM   614  N N     . GLN A 1 84  ? -41.826 -18.308 40.563  1.00 44.03 ?  90  GLN A N     1 
ATOM   615  C CA    . GLN A 1 84  ? -40.812 -18.998 39.770  1.00 40.41 ?  90  GLN A CA    1 
ATOM   616  C C     . GLN A 1 84  ? -41.339 -19.369 38.388  1.00 35.93 ?  90  GLN A C     1 
ATOM   617  O O     . GLN A 1 84  ? -41.512 -20.551 38.071  1.00 33.98 ?  90  GLN A O     1 
ATOM   618  C CB    . GLN A 1 84  ? -40.305 -20.229 40.525  1.00 34.77 ?  90  GLN A CB    1 
ATOM   619  C CG    . GLN A 1 84  ? -39.740 -19.885 41.909  1.00 39.52 ?  90  GLN A CG    1 
ATOM   620  C CD    . GLN A 1 84  ? -38.278 -19.457 41.889  1.00 34.26 ?  90  GLN A CD    1 
ATOM   621  O OE1   . GLN A 1 84  ? -37.374 -20.291 41.782  1.00 35.04 ?  90  GLN A OE1   1 
ATOM   622  N NE2   . GLN A 1 84  ? -38.036 -18.155 42.021  1.00 40.17 ?  90  GLN A NE2   1 
ATOM   623  N N     . MET A 1 85  ? -41.573 -18.356 37.556  1.00 36.55 ?  91  MET A N     1 
ATOM   624  C CA    . MET A 1 85  ? -42.226 -18.514 36.266  1.00 36.78 ?  91  MET A CA    1 
ATOM   625  C C     . MET A 1 85  ? -41.545 -17.624 35.232  1.00 36.85 ?  91  MET A C     1 
ATOM   626  O O     . MET A 1 85  ? -41.205 -16.476 35.526  1.00 35.63 ?  91  MET A O     1 
ATOM   627  C CB    . MET A 1 85  ? -43.703 -18.140 36.370  1.00 38.69 ?  91  MET A CB    1 
ATOM   628  C CG    . MET A 1 85  ? -44.623 -18.934 35.481  1.00 45.10 ?  91  MET A CG    1 
ATOM   629  S SD    . MET A 1 85  ? -45.102 -20.510 36.216  1.00 51.87 ?  91  MET A SD    1 
ATOM   630  C CE    . MET A 1 85  ? -46.185 -21.195 34.958  1.00 41.48 ?  91  MET A CE    1 
ATOM   631  N N     . VAL A 1 86  ? -41.356 -18.146 34.023  1.00 34.95 ?  92  VAL A N     1 
ATOM   632  C CA    . VAL A 1 86  ? -40.801 -17.374 32.914  1.00 37.04 ?  92  VAL A CA    1 
ATOM   633  C C     . VAL A 1 86  ? -41.961 -16.916 32.042  1.00 36.22 ?  92  VAL A C     1 
ATOM   634  O O     . VAL A 1 86  ? -42.683 -17.744 31.472  1.00 36.71 ?  92  VAL A O     1 
ATOM   635  C CB    . VAL A 1 86  ? -39.780 -18.190 32.101  1.00 29.94 ?  92  VAL A CB    1 
ATOM   636  C CG1   . VAL A 1 86  ? -39.454 -17.478 30.804  1.00 31.81 ?  92  VAL A CG1   1 
ATOM   637  C CG2   . VAL A 1 86  ? -38.518 -18.395 32.902  1.00 32.14 ?  92  VAL A CG2   1 
ATOM   638  N N     . LEU A 1 87  ? -42.135 -15.596 31.927  1.00 34.05 ?  93  LEU A N     1 
ATOM   639  C CA    . LEU A 1 87  ? -43.300 -15.020 31.263  1.00 36.16 ?  93  LEU A CA    1 
ATOM   640  C C     . LEU A 1 87  ? -42.981 -14.768 29.795  1.00 38.06 ?  93  LEU A C     1 
ATOM   641  O O     . LEU A 1 87  ? -42.031 -14.042 29.479  1.00 34.88 ?  93  LEU A O     1 
ATOM   642  C CB    . LEU A 1 87  ? -43.732 -13.719 31.947  1.00 37.19 ?  93  LEU A CB    1 
ATOM   643  C CG    . LEU A 1 87  ? -43.946 -13.760 33.471  1.00 43.27 ?  93  LEU A CG    1 
ATOM   644  C CD1   . LEU A 1 87  ? -44.552 -12.454 33.989  1.00 43.14 ?  93  LEU A CD1   1 
ATOM   645  C CD2   . LEU A 1 87  ? -44.801 -14.952 33.883  1.00 38.06 ?  93  LEU A CD2   1 
ATOM   646  N N     . LEU A 1 88  ? -43.771 -15.363 28.905  1.00 34.86 ?  94  LEU A N     1 
ATOM   647  C CA    . LEU A 1 88  ? -43.606 -15.178 27.472  1.00 35.36 ?  94  LEU A CA    1 
ATOM   648  C C     . LEU A 1 88  ? -44.576 -14.125 26.959  1.00 38.55 ?  94  LEU A C     1 
ATOM   649  O O     . LEU A 1 88  ? -45.659 -13.924 27.517  1.00 38.20 ?  94  LEU A O     1 
ATOM   650  C CB    . LEU A 1 88  ? -43.851 -16.480 26.702  1.00 38.02 ?  94  LEU A CB    1 
ATOM   651  C CG    . LEU A 1 88  ? -42.952 -17.667 27.022  1.00 39.39 ?  94  LEU A CG    1 
ATOM   652  C CD1   . LEU A 1 88  ? -43.243 -18.837 26.080  1.00 38.35 ?  94  LEU A CD1   1 
ATOM   653  C CD2   . LEU A 1 88  ? -41.510 -17.225 26.918  1.00 33.50 ?  94  LEU A CD2   1 
ATOM   654  N N     . GLN A 1 89  ? -44.177 -13.459 25.878  1.00 35.71 ?  95  GLN A N     1 
ATOM   655  C CA    . GLN A 1 89  ? -45.122 -12.644 25.129  1.00 40.98 ?  95  GLN A CA    1 
ATOM   656  C C     . GLN A 1 89  ? -46.227 -13.528 24.566  1.00 42.20 ?  95  GLN A C     1 
ATOM   657  O O     . GLN A 1 89  ? -45.967 -14.606 24.024  1.00 35.66 ?  95  GLN A O     1 
ATOM   658  C CB    . GLN A 1 89  ? -44.410 -11.896 24.001  1.00 39.13 ?  95  GLN A CB    1 
ATOM   659  C CG    . GLN A 1 89  ? -45.340 -11.361 22.935  1.00 42.66 ?  95  GLN A CG    1 
ATOM   660  C CD    . GLN A 1 89  ? -44.616 -10.515 21.913  1.00 48.72 ?  95  GLN A CD    1 
ATOM   661  O OE1   . GLN A 1 89  ? -44.436 -10.925 20.765  1.00 54.23 ?  95  GLN A OE1   1 
ATOM   662  N NE2   . GLN A 1 89  ? -44.195 -9.326  22.323  1.00 45.24 ?  95  GLN A NE2   1 
ATOM   663  N N     . GLY A 1 90  ? -47.472 -13.059 24.700  1.00 42.89 ?  96  GLY A N     1 
ATOM   664  C CA    . GLY A 1 90  ? -48.645 -13.848 24.402  1.00 40.96 ?  96  GLY A CA    1 
ATOM   665  C C     . GLY A 1 90  ? -49.361 -14.380 25.626  1.00 48.08 ?  96  GLY A C     1 
ATOM   666  O O     . GLY A 1 90  ? -50.491 -14.871 25.502  1.00 46.86 ?  96  GLY A O     1 
ATOM   667  N N     . GLY A 1 91  ? -48.734 -14.313 26.800  1.00 44.58 ?  97  GLY A N     1 
ATOM   668  C CA    . GLY A 1 91  ? -49.364 -14.693 28.039  1.00 43.74 ?  97  GLY A CA    1 
ATOM   669  C C     . GLY A 1 91  ? -48.889 -16.006 28.626  1.00 48.57 ?  97  GLY A C     1 
ATOM   670  O O     . GLY A 1 91  ? -49.102 -16.240 29.822  1.00 44.46 ?  97  GLY A O     1 
ATOM   671  N N     . GLU A 1 92  ? -48.249 -16.862 27.828  1.00 46.03 ?  98  GLU A N     1 
ATOM   672  C CA    . GLU A 1 92  ? -47.834 -18.169 28.321  1.00 44.05 ?  98  GLU A CA    1 
ATOM   673  C C     . GLU A 1 92  ? -46.731 -18.036 29.364  1.00 43.88 ?  98  GLU A C     1 
ATOM   674  O O     . GLU A 1 92  ? -45.958 -17.072 29.374  1.00 41.30 ?  98  GLU A O     1 
ATOM   675  C CB    . GLU A 1 92  ? -47.370 -19.060 27.170  1.00 46.37 ?  98  GLU A CB    1 
ATOM   676  C CG    . GLU A 1 92  ? -48.445 -19.260 26.113  1.00 51.01 ?  98  GLU A CG    1 
ATOM   677  C CD    . GLU A 1 92  ? -48.481 -20.669 25.552  1.00 60.28 ?  98  GLU A CD    1 
ATOM   678  O OE1   . GLU A 1 92  ? -47.417 -21.206 25.173  1.00 59.39 ?  98  GLU A OE1   1 
ATOM   679  O OE2   . GLU A 1 92  ? -49.588 -21.243 25.493  1.00 69.82 -1 98  GLU A OE2   1 
ATOM   680  N N     . ALA A 1 93  ? -46.670 -19.016 30.259  1.00 41.02 ?  99  ALA A N     1 
ATOM   681  C CA    . ALA A 1 93  ? -45.711 -18.992 31.350  1.00 42.09 ?  99  ALA A CA    1 
ATOM   682  C C     . ALA A 1 93  ? -45.015 -20.343 31.460  1.00 43.17 ?  99  ALA A C     1 
ATOM   683  O O     . ALA A 1 93  ? -45.630 -21.389 31.223  1.00 43.66 ?  99  ALA A O     1 
ATOM   684  C CB    . ALA A 1 93  ? -46.409 -18.620 32.654  1.00 40.36 ?  99  ALA A CB    1 
ATOM   685  N N     . LEU A 1 94  ? -43.730 -20.316 31.807  1.00 38.70 ?  100 LEU A N     1 
ATOM   686  C CA    . LEU A 1 94  ? -42.935 -21.534 31.976  1.00 34.32 ?  100 LEU A CA    1 
ATOM   687  C C     . LEU A 1 94  ? -42.436 -21.668 33.408  1.00 34.07 ?  100 LEU A C     1 
ATOM   688  O O     . LEU A 1 94  ? -41.613 -20.847 33.854  1.00 32.89 ?  100 LEU A O     1 
ATOM   689  C CB    . LEU A 1 94  ? -41.761 -21.533 30.997  1.00 34.60 ?  100 LEU A CB    1 
ATOM   690  C CG    . LEU A 1 94  ? -42.224 -21.551 29.543  1.00 36.76 ?  100 LEU A CG    1 
ATOM   691  C CD1   . LEU A 1 94  ? -41.061 -21.542 28.580  1.00 35.39 ?  100 LEU A CD1   1 
ATOM   692  C CD2   . LEU A 1 94  ? -43.036 -22.780 29.332  1.00 41.28 ?  100 LEU A CD2   1 
ATOM   693  N N     . PRO A 1 95  ? -42.882 -22.665 34.168  1.00 37.14 ?  101 PRO A N     1 
ATOM   694  C CA    . PRO A 1 95  ? -42.371 -22.834 35.533  1.00 33.81 ?  101 PRO A CA    1 
ATOM   695  C C     . PRO A 1 95  ? -40.966 -23.416 35.540  1.00 29.28 ?  101 PRO A C     1 
ATOM   696  O O     . PRO A 1 95  ? -40.587 -24.196 34.666  1.00 29.86 ?  101 PRO A O     1 
ATOM   697  C CB    . PRO A 1 95  ? -43.374 -23.812 36.162  1.00 37.71 ?  101 PRO A CB    1 
ATOM   698  C CG    . PRO A 1 95  ? -43.889 -24.613 34.991  1.00 36.68 ?  101 PRO A CG    1 
ATOM   699  C CD    . PRO A 1 95  ? -43.908 -23.666 33.818  1.00 36.34 ?  101 PRO A CD    1 
ATOM   700  N N     . PHE A 1 96  ? -40.191 -23.047 36.557  1.00 29.56 ?  102 PHE A N     1 
ATOM   701  C CA    . PHE A 1 96  ? -38.825 -23.537 36.640  1.00 30.04 ?  102 PHE A CA    1 
ATOM   702  C C     . PHE A 1 96  ? -38.429 -23.836 38.077  1.00 30.53 ?  102 PHE A C     1 
ATOM   703  O O     . PHE A 1 96  ? -38.827 -23.131 39.007  1.00 31.06 ?  102 PHE A O     1 
ATOM   704  C CB    . PHE A 1 96  ? -37.826 -22.539 36.034  1.00 25.78 ?  102 PHE A CB    1 
ATOM   705  C CG    . PHE A 1 96  ? -37.757 -21.204 36.749  1.00 25.79 ?  102 PHE A CG    1 
ATOM   706  C CD1   . PHE A 1 96  ? -36.864 -21.000 37.797  1.00 27.00 ?  102 PHE A CD1   1 
ATOM   707  C CD2   . PHE A 1 96  ? -38.544 -20.144 36.333  1.00 28.63 ?  102 PHE A CD2   1 
ATOM   708  C CE1   . PHE A 1 96  ? -36.774 -19.770 38.428  1.00 26.94 ?  102 PHE A CE1   1 
ATOM   709  C CE2   . PHE A 1 96  ? -38.463 -18.912 36.959  1.00 30.08 ?  102 PHE A CE2   1 
ATOM   710  C CZ    . PHE A 1 96  ? -37.586 -18.730 38.012  1.00 28.96 ?  102 PHE A CZ    1 
ATOM   711  N N     . SER A 1 97  ? -37.640 -24.891 38.247  1.00 23.19 ?  103 SER A N     1 
ATOM   712  C CA    . SER A 1 97  ? -36.908 -25.074 39.486  1.00 24.51 ?  103 SER A CA    1 
ATOM   713  C C     . SER A 1 97  ? -35.590 -24.323 39.450  1.00 26.10 ?  103 SER A C     1 
ATOM   714  O O     . SER A 1 97  ? -35.111 -23.850 40.488  1.00 23.14 ?  103 SER A O     1 
ATOM   715  C CB    . SER A 1 97  ? -36.654 -26.560 39.729  1.00 23.69 ?  103 SER A CB    1 
ATOM   716  O OG    . SER A 1 97  ? -35.710 -27.057 38.797  1.00 21.96 ?  103 SER A OG    1 
ATOM   717  N N     . HIS A 1 98  ? -34.990 -24.212 38.266  1.00 21.81 ?  104 HIS A N     1 
ATOM   718  C CA    . HIS A 1 98  ? -33.740 -23.497 38.088  1.00 22.45 ?  104 HIS A CA    1 
ATOM   719  C C     . HIS A 1 98  ? -33.817 -22.724 36.788  1.00 23.02 ?  104 HIS A C     1 
ATOM   720  O O     . HIS A 1 98  ? -34.425 -23.189 35.820  1.00 17.76 ?  104 HIS A O     1 
ATOM   721  C CB    . HIS A 1 98  ? -32.547 -24.437 38.072  1.00 21.71 ?  104 HIS A CB    1 
ATOM   722  C CG    . HIS A 1 98  ? -32.411 -25.238 39.327  1.00 22.80 ?  104 HIS A CG    1 
ATOM   723  N ND1   . HIS A 1 98  ? -33.299 -26.237 39.667  1.00 22.03 ?  104 HIS A ND1   1 
ATOM   724  C CD2   . HIS A 1 98  ? -31.500 -25.184 40.323  1.00 25.41 ?  104 HIS A CD2   1 
ATOM   725  C CE1   . HIS A 1 98  ? -32.936 -26.768 40.821  1.00 24.06 ?  104 HIS A CE1   1 
ATOM   726  N NE2   . HIS A 1 98  ? -31.842 -26.153 41.237  1.00 25.46 ?  104 HIS A NE2   1 
ATOM   727  N N     . LEU A 1 99  ? -33.228 -21.533 36.794  1.00 22.14 ?  105 LEU A N     1 
ATOM   728  C CA    . LEU A 1 99  ? -33.286 -20.615 35.665  1.00 21.01 ?  105 LEU A CA    1 
ATOM   729  C C     . LEU A 1 99  ? -31.875 -20.287 35.207  1.00 19.89 ?  105 LEU A C     1 
ATOM   730  O O     . LEU A 1 99  ? -31.014 -19.916 36.021  1.00 19.48 ?  105 LEU A O     1 
ATOM   731  C CB    . LEU A 1 99  ? -34.040 -19.348 36.051  1.00 21.57 ?  105 LEU A CB    1 
ATOM   732  C CG    . LEU A 1 99  ? -34.098 -18.220 35.024  1.00 24.21 ?  105 LEU A CG    1 
ATOM   733  C CD1   . LEU A 1 99  ? -35.022 -18.590 33.864  1.00 20.91 ?  105 LEU A CD1   1 
ATOM   734  C CD2   . LEU A 1 99  ? -34.533 -16.941 35.729  1.00 24.95 ?  105 LEU A CD2   1 
ATOM   735  N N     . ILE A 1 100 ? -31.638 -20.407 33.901  1.00 19.39 ?  106 ILE A N     1 
ATOM   736  C CA    . ILE A 1 100 ? -30.370 -20.025 33.299  1.00 18.19 ?  106 ILE A CA    1 
ATOM   737  C C     . ILE A 1 100 ? -30.662 -18.881 32.351  1.00 18.24 ?  106 ILE A C     1 
ATOM   738  O O     . ILE A 1 100 ? -31.394 -19.057 31.372  1.00 18.04 ?  106 ILE A O     1 
ATOM   739  C CB    . ILE A 1 100 ? -29.699 -21.184 32.551  1.00 17.43 ?  106 ILE A CB    1 
ATOM   740  C CG1   . ILE A 1 100 ? -29.279 -22.285 33.525  1.00 17.45 ?  106 ILE A CG1   1 
ATOM   741  C CG2   . ILE A 1 100 ? -28.465 -20.670 31.789  1.00 15.58 ?  106 ILE A CG2   1 
ATOM   742  C CD1   . ILE A 1 100 ? -28.615 -23.492 32.832  1.00 15.78 ?  106 ILE A CD1   1 
ATOM   743  N N     . LEU A 1 101 ? -30.095 -17.720 32.635  1.00 16.53 ?  107 LEU A N     1 
ATOM   744  C CA    . LEU A 1 101 ? -30.286 -16.555 31.786  1.00 18.06 ?  107 LEU A CA    1 
ATOM   745  C C     . LEU A 1 101 ? -29.078 -16.424 30.867  1.00 14.31 ?  107 LEU A C     1 
ATOM   746  O O     . LEU A 1 101 ? -27.932 -16.352 31.329  1.00 16.09 ?  107 LEU A O     1 
ATOM   747  C CB    . LEU A 1 101 ? -30.502 -15.302 32.630  1.00 20.17 ?  107 LEU A CB    1 
ATOM   748  C CG    . LEU A 1 101 ? -31.842 -15.261 33.362  1.00 25.54 ?  107 LEU A CG    1 
ATOM   749  C CD1   . LEU A 1 101 ? -31.831 -14.147 34.415  1.00 29.96 ?  107 LEU A CD1   1 
ATOM   750  C CD2   . LEU A 1 101 ? -33.013 -15.104 32.405  1.00 21.46 ?  107 LEU A CD2   1 
ATOM   751  N N     . ALA A 1 102 ? -29.336 -16.419 29.564  1.00 17.19 ?  108 ALA A N     1 
ATOM   752  C CA    . ALA A 1 102 ? -28.285 -16.486 28.565  1.00 12.44 ?  108 ALA A CA    1 
ATOM   753  C C     . ALA A 1 102 ? -28.691 -15.621 27.383  1.00 17.23 ?  108 ALA A C     1 
ATOM   754  O O     . ALA A 1 102 ? -28.710 -16.061 26.233  1.00 14.92 ?  108 ALA A O     1 
ATOM   755  C CB    . ALA A 1 102 ? -28.030 -17.928 28.141  1.00 13.90 ?  108 ALA A CB    1 
ATOM   756  N N     . THR A 1 103 ? -29.028 -14.364 27.676  1.00 15.86 ?  109 THR A N     1 
ATOM   757  C CA    . THR A 1 103 ? -29.693 -13.480 26.731  1.00 17.96 ?  109 THR A CA    1 
ATOM   758  C C     . THR A 1 103 ? -28.745 -12.705 25.820  1.00 15.40 ?  109 THR A C     1 
ATOM   759  O O     . THR A 1 103 ? -29.225 -12.036 24.902  1.00 17.20 ?  109 THR A O     1 
ATOM   760  C CB    . THR A 1 103 ? -30.578 -12.491 27.494  1.00 18.12 ?  109 THR A CB    1 
ATOM   761  O OG1   . THR A 1 103 ? -29.758 -11.769 28.418  1.00 20.66 ?  109 THR A OG1   1 
ATOM   762  C CG2   . THR A 1 103 ? -31.650 -13.254 28.254  1.00 22.00 ?  109 THR A CG2   1 
ATOM   763  N N     . GLY A 1 104 ? -27.433 -12.787 26.029  1.00 16.89 ?  110 GLY A N     1 
ATOM   764  C CA    . GLY A 1 104 ? -26.508 -12.185 25.068  1.00 15.81 ?  110 GLY A CA    1 
ATOM   765  C C     . GLY A 1 104 ? -26.685 -10.682 24.925  1.00 19.09 ?  110 GLY A C     1 
ATOM   766  O O     . GLY A 1 104 ? -27.080 -9.978  25.863  1.00 18.52 ?  110 GLY A O     1 
ATOM   767  N N     . SER A 1 105 ? -26.415 -10.184 23.712  1.00 15.84 ?  111 SER A N     1 
ATOM   768  C CA    . SER A 1 105 ? -26.386 -8.756  23.431  1.00 18.70 ?  111 SER A CA    1 
ATOM   769  C C     . SER A 1 105 ? -27.165 -8.444  22.158  1.00 20.66 ?  111 SER A C     1 
ATOM   770  O O     . SER A 1 105 ? -27.396 -9.316  21.314  1.00 20.18 ?  111 SER A O     1 
ATOM   771  C CB    . SER A 1 105 ? -24.950 -8.244  23.249  1.00 19.47 ?  111 SER A CB    1 
ATOM   772  O OG    . SER A 1 105 ? -24.108 -8.601  24.321  1.00 26.33 ?  111 SER A OG    1 
ATOM   773  N N     . THR A 1 106 ? -27.559 -7.179  22.023  1.00 18.91 ?  112 THR A N     1 
ATOM   774  C CA    . THR A 1 106 ? -28.151 -6.662  20.798  1.00 18.97 ?  112 THR A CA    1 
ATOM   775  C C     . THR A 1 106 ? -27.266 -5.574  20.212  1.00 18.56 ?  112 THR A C     1 
ATOM   776  O O     . THR A 1 106 ? -26.455 -4.949  20.895  1.00 16.68 ?  112 THR A O     1 
ATOM   777  C CB    . THR A 1 106 ? -29.553 -6.057  21.010  1.00 23.16 ?  112 THR A CB    1 
ATOM   778  O OG1   . THR A 1 106 ? -29.459 -4.968  21.931  1.00 25.62 ?  112 THR A OG1   1 
ATOM   779  C CG2   . THR A 1 106 ? -30.532 -7.085  21.542  1.00 23.81 ?  112 THR A CG2   1 
ATOM   780  N N     . GLY A 1 107 ? -27.455 -5.330  18.929  1.00 17.77 ?  113 GLY A N     1 
ATOM   781  C CA    . GLY A 1 107 ? -26.686 -4.325  18.252  1.00 17.67 ?  113 GLY A CA    1 
ATOM   782  C C     . GLY A 1 107 ? -27.146 -4.303  16.823  1.00 15.82 ?  113 GLY A C     1 
ATOM   783  O O     . GLY A 1 107 ? -28.058 -5.046  16.431  1.00 15.87 ?  113 GLY A O     1 
ATOM   784  N N     . PRO A 1 108 ? -26.526 -3.448  16.020  1.00 15.54 ?  114 PRO A N     1 
ATOM   785  C CA    . PRO A 1 108 ? -26.963 -3.294  14.624  1.00 16.42 ?  114 PRO A CA    1 
ATOM   786  C C     . PRO A 1 108 ? -26.655 -4.518  13.771  1.00 14.76 ?  114 PRO A C     1 
ATOM   787  O O     . PRO A 1 108 ? -25.650 -5.208  13.969  1.00 13.41 ?  114 PRO A O     1 
ATOM   788  C CB    . PRO A 1 108 ? -26.181 -2.067  14.130  1.00 14.92 ?  114 PRO A CB    1 
ATOM   789  C CG    . PRO A 1 108 ? -24.994 -1.949  15.049  1.00 17.03 ?  114 PRO A CG    1 
ATOM   790  C CD    . PRO A 1 108 ? -25.395 -2.574  16.378  1.00 16.21 ?  114 PRO A CD    1 
ATOM   791  N N     . PHE A 1 109 ? -27.565 -4.795  12.844  1.00 11.87 ?  115 PHE A N     1 
ATOM   792  C CA    . PHE A 1 109 ? -27.266 -5.681  11.728  1.00 15.87 ?  115 PHE A CA    1 
ATOM   793  C C     . PHE A 1 109 ? -26.140 -5.069  10.901  1.00 13.84 ?  115 PHE A C     1 
ATOM   794  O O     . PHE A 1 109 ? -26.098 -3.845  10.739  1.00 12.89 ?  115 PHE A O     1 
ATOM   795  C CB    . PHE A 1 109 ? -28.525 -5.861  10.868  1.00 14.78 ?  115 PHE A CB    1 
ATOM   796  C CG    . PHE A 1 109 ? -28.394 -6.889  9.786   1.00 14.48 ?  115 PHE A CG    1 
ATOM   797  C CD1   . PHE A 1 109 ? -28.650 -8.223  10.054  1.00 13.41 ?  115 PHE A CD1   1 
ATOM   798  C CD2   . PHE A 1 109 ? -28.042 -6.519  8.503   1.00 17.82 ?  115 PHE A CD2   1 
ATOM   799  C CE1   . PHE A 1 109 ? -28.531 -9.177  9.061   1.00 14.99 ?  115 PHE A CE1   1 
ATOM   800  C CE2   . PHE A 1 109 ? -27.910 -7.470  7.503   1.00 18.65 ?  115 PHE A CE2   1 
ATOM   801  C CZ    . PHE A 1 109 ? -28.169 -8.803  7.790   1.00 13.25 ?  115 PHE A CZ    1 
ATOM   802  N N     . PRO A 1 110 ? -25.223 -5.883  10.331  1.00 12.63 ?  116 PRO A N     1 
ATOM   803  C CA    . PRO A 1 110 ? -25.183 -7.362  10.274  1.00 12.09 ?  116 PRO A CA    1 
ATOM   804  C C     . PRO A 1 110 ? -24.476 -8.041  11.425  1.00 11.25 ?  116 PRO A C     1 
ATOM   805  O O     . PRO A 1 110 ? -24.538 -9.262  11.510  1.00 11.71 ?  116 PRO A O     1 
ATOM   806  C CB    . PRO A 1 110 ? -24.409 -7.626  8.978   1.00 13.14 ?  116 PRO A CB    1 
ATOM   807  C CG    . PRO A 1 110 ? -23.403 -6.504  8.956   1.00 14.18 ?  116 PRO A CG    1 
ATOM   808  C CD    . PRO A 1 110 ? -24.134 -5.290  9.536   1.00 13.01 ?  116 PRO A CD    1 
ATOM   809  N N     . GLY A 1 111 ? -23.793 -7.311  12.310  1.00 13.16 ?  117 GLY A N     1 
ATOM   810  C CA    . GLY A 1 111 ? -23.008 -7.954  13.359  1.00 10.62 ?  117 GLY A CA    1 
ATOM   811  C C     . GLY A 1 111 ? -23.838 -8.714  14.375  1.00 13.79 ?  117 GLY A C     1 
ATOM   812  O O     . GLY A 1 111 ? -23.324 -9.648  15.002  1.00 14.09 ?  117 GLY A O     1 
ATOM   813  N N     . LYS A 1 112 ? -25.106 -8.334  14.548  1.00 12.94 ?  118 LYS A N     1 
ATOM   814  C CA    . LYS A 1 112 ? -26.061 -9.042  15.398  1.00 15.73 ?  118 LYS A CA    1 
ATOM   815  C C     . LYS A 1 112 ? -27.368 -9.229  14.641  1.00 17.23 ?  118 LYS A C     1 
ATOM   816  O O     . LYS A 1 112 ? -27.755 -8.391  13.818  1.00 15.54 ?  118 LYS A O     1 
ATOM   817  C CB    . LYS A 1 112 ? -26.359 -8.281  16.713  1.00 17.10 ?  118 LYS A CB    1 
ATOM   818  C CG    . LYS A 1 112 ? -25.150 -8.038  17.593  1.00 17.60 ?  118 LYS A CG    1 
ATOM   819  C CD    . LYS A 1 112 ? -24.650 -9.343  18.253  1.00 22.62 ?  118 LYS A CD    1 
ATOM   820  C CE    . LYS A 1 112 ? -23.303 -9.137  18.957  1.00 24.05 ?  118 LYS A CE    1 
ATOM   821  N NZ    . LYS A 1 112 ? -22.604 -10.407 19.420  1.00 20.68 ?  118 LYS A NZ    1 
ATOM   822  N N     . PHE A 1 113 ? -28.069 -10.318 14.954  1.00 14.58 ?  119 PHE A N     1 
ATOM   823  C CA    . PHE A 1 113 ? -29.337 -10.619 14.293  1.00 16.42 ?  119 PHE A CA    1 
ATOM   824  C C     . PHE A 1 113 ? -30.293 -11.152 15.355  1.00 20.14 ?  119 PHE A C     1 
ATOM   825  O O     . PHE A 1 113 ? -30.177 -12.303 15.783  1.00 20.06 ?  119 PHE A O     1 
ATOM   826  C CB    . PHE A 1 113 ? -29.149 -11.629 13.169  1.00 13.46 ?  119 PHE A CB    1 
ATOM   827  C CG    . PHE A 1 113 ? -30.410 -11.944 12.457  1.00 16.97 ?  119 PHE A CG    1 
ATOM   828  C CD1   . PHE A 1 113 ? -30.854 -11.130 11.426  1.00 18.24 ?  119 PHE A CD1   1 
ATOM   829  C CD2   . PHE A 1 113 ? -31.169 -13.051 12.827  1.00 17.41 ?  119 PHE A CD2   1 
ATOM   830  C CE1   . PHE A 1 113 ? -32.034 -11.402 10.776  1.00 20.42 ?  119 PHE A CE1   1 
ATOM   831  C CE2   . PHE A 1 113 ? -32.345 -13.334 12.182  1.00 20.71 ?  119 PHE A CE2   1 
ATOM   832  C CZ    . PHE A 1 113 ? -32.781 -12.511 11.154  1.00 19.88 ?  119 PHE A CZ    1 
ATOM   833  N N     . ASN A 1 114 ? -31.233 -10.321 15.782  1.00 20.49 ?  120 ASN A N     1 
ATOM   834  C CA    . ASN A 1 114 ? -32.195 -10.731 16.803  1.00 25.77 ?  120 ASN A CA    1 
ATOM   835  C C     . ASN A 1 114 ? -33.603 -10.352 16.357  1.00 28.04 ?  120 ASN A C     1 
ATOM   836  O O     . ASN A 1 114 ? -34.314 -9.573  16.990  1.00 34.12 ?  120 ASN A O     1 
ATOM   837  C CB    . ASN A 1 114 ? -31.845 -10.123 18.157  1.00 25.38 ?  120 ASN A CB    1 
ATOM   838  C CG    . ASN A 1 114 ? -30.572 -10.695 18.726  1.00 25.94 ?  120 ASN A CG    1 
ATOM   839  O OD1   . ASN A 1 114 ? -30.501 -11.900 19.014  1.00 25.62 ?  120 ASN A OD1   1 
ATOM   840  N ND2   . ASN A 1 114 ? -29.545 -9.844  18.888  1.00 22.61 ?  120 ASN A ND2   1 
ATOM   841  N N     . GLU A 1 115 ? -34.000 -10.916 15.230  1.00 30.01 ?  121 GLU A N     1 
ATOM   842  C CA    . GLU A 1 115 ? -35.327 -10.723 14.677  1.00 29.52 ?  121 GLU A CA    1 
ATOM   843  C C     . GLU A 1 115 ? -36.112 -12.008 14.863  1.00 31.70 ?  121 GLU A C     1 
ATOM   844  O O     . GLU A 1 115 ? -35.559 -13.107 14.757  1.00 29.43 ?  121 GLU A O     1 
ATOM   845  C CB    . GLU A 1 115 ? -35.253 -10.346 13.193  1.00 29.19 ?  121 GLU A CB    1 
ATOM   846  C CG    . GLU A 1 115 ? -34.767 -8.924  12.948  1.00 33.66 ?  121 GLU A CG    1 
ATOM   847  N N     . VAL A 1 116 ? -37.393 -11.879 15.182  1.00 27.28 ?  122 VAL A N     1 
ATOM   848  C CA    . VAL A 1 116 ? -38.246 -13.053 15.131  1.00 34.10 ?  122 VAL A CA    1 
ATOM   849  C C     . VAL A 1 116 ? -38.447 -13.395 13.665  1.00 37.36 ?  122 VAL A C     1 
ATOM   850  O O     . VAL A 1 116 ? -38.940 -12.577 12.881  1.00 34.88 ?  122 VAL A O     1 
ATOM   851  C CB    . VAL A 1 116 ? -39.572 -12.817 15.860  1.00 36.29 ?  122 VAL A CB    1 
ATOM   852  C CG1   . VAL A 1 116 ? -40.479 -14.021 15.687  1.00 33.05 ?  122 VAL A CG1   1 
ATOM   853  C CG2   . VAL A 1 116 ? -39.298 -12.560 17.338  1.00 34.71 ?  122 VAL A CG2   1 
ATOM   854  N N     . SER A 1 117 ? -38.023 -14.590 13.284  1.00 35.46 ?  123 SER A N     1 
ATOM   855  C CA    . SER A 1 117 ? -37.819 -14.885 11.878  1.00 38.92 ?  123 SER A CA    1 
ATOM   856  C C     . SER A 1 117 ? -37.711 -16.387 11.711  1.00 33.60 ?  123 SER A C     1 
ATOM   857  O O     . SER A 1 117 ? -37.360 -17.120 12.646  1.00 33.46 ?  123 SER A O     1 
ATOM   858  C CB    . SER A 1 117 ? -36.540 -14.229 11.353  1.00 47.69 ?  123 SER A CB    1 
ATOM   859  O OG    . SER A 1 117 ? -35.418 -14.805 12.020  1.00 35.87 ?  123 SER A OG    1 
ATOM   860  N N     . SER A 1 118 ? -37.976 -16.824 10.497  1.00 24.70 ?  124 SER A N     1 
ATOM   861  C CA    . SER A 1 118 ? -37.696 -18.194 10.131  1.00 23.92 ?  124 SER A CA    1 
ATOM   862  C C     . SER A 1 118 ? -36.238 -18.312 9.708   1.00 17.93 ?  124 SER A C     1 
ATOM   863  O O     . SER A 1 118 ? -35.571 -17.317 9.400   1.00 16.37 ?  124 SER A O     1 
ATOM   864  C CB    . SER A 1 118 ? -38.607 -18.640 8.993   1.00 19.15 ?  124 SER A CB    1 
ATOM   865  O OG    . SER A 1 118 ? -38.354 -17.832 7.864   1.00 17.35 ?  124 SER A OG    1 
ATOM   866  N N     . GLN A 1 119 ? -35.768 -19.556 9.655   1.00 15.32 ?  125 GLN A N     1 
ATOM   867  C CA    . GLN A 1 119 ? -34.389 -19.812 9.246   1.00 17.63 ?  125 GLN A CA    1 
ATOM   868  C C     . GLN A 1 119 ? -34.117 -19.296 7.835   1.00 17.48 ?  125 GLN A C     1 
ATOM   869  O O     . GLN A 1 119 ? -33.050 -18.729 7.574   1.00 14.06 ?  125 GLN A O     1 
ATOM   870  C CB    . GLN A 1 119 ? -34.078 -21.309 9.362   1.00 19.14 ?  125 GLN A CB    1 
ATOM   871  C CG    . GLN A 1 119 ? -32.661 -21.705 8.899   1.00 18.41 ?  125 GLN A CG    1 
ATOM   872  C CD    . GLN A 1 119 ? -32.165 -23.022 9.499   1.00 24.58 ?  125 GLN A CD    1 
ATOM   873  O OE1   . GLN A 1 119 ? -32.485 -23.363 10.630  1.00 28.00 ?  125 GLN A OE1   1 
ATOM   874  N NE2   . GLN A 1 119 ? -31.369 -23.754 8.740   1.00 31.17 ?  125 GLN A NE2   1 
ATOM   875  N N     . GLN A 1 120 ? -35.071 -19.453 6.904   1.00 14.31 ?  126 GLN A N     1 
ATOM   876  C CA    . GLN A 1 120 ? -34.753 -19.024 5.543   1.00 16.07 ?  126 GLN A CA    1 
ATOM   877  C C     . GLN A 1 120 ? -34.812 -17.507 5.399   1.00 14.47 ?  126 GLN A C     1 
ATOM   878  O O     . GLN A 1 120 ? -34.042 -16.934 4.621   1.00 12.09 ?  126 GLN A O     1 
ATOM   879  C CB    . GLN A 1 120 ? -35.662 -19.725 4.525   1.00 20.93 ?  126 GLN A CB    1 
ATOM   880  C CG    . GLN A 1 120 ? -35.323 -21.233 4.315   1.00 22.83 ?  126 GLN A CG    1 
ATOM   881  C CD    . GLN A 1 120 ? -33.797 -21.562 4.288   1.00 25.76 ?  126 GLN A CD    1 
ATOM   882  O OE1   . GLN A 1 120 ? -33.048 -21.087 3.415   1.00 23.62 ?  126 GLN A OE1   1 
ATOM   883  N NE2   . GLN A 1 120 ? -33.348 -22.394 5.247   1.00 23.04 ?  126 GLN A NE2   1 
ATOM   884  N N     . ALA A 1 121 ? -35.670 -16.829 6.166   1.00 12.99 ?  127 ALA A N     1 
ATOM   885  C CA    . ALA A 1 121 ? -35.648 -15.371 6.137   1.00 14.69 ?  127 ALA A CA    1 
ATOM   886  C C     . ALA A 1 121 ? -34.336 -14.832 6.703   1.00 13.18 ?  127 ALA A C     1 
ATOM   887  O O     . ALA A 1 121 ? -33.771 -13.871 6.166   1.00 14.75 ?  127 ALA A O     1 
ATOM   888  C CB    . ALA A 1 121 ? -36.844 -14.807 6.905   1.00 15.74 ?  127 ALA A CB    1 
ATOM   889  N N     . ALA A 1 122 ? -33.832 -15.458 7.768   1.00 12.84 ?  128 ALA A N     1 
ATOM   890  C CA    . ALA A 1 122 ? -32.556 -15.050 8.367   1.00 11.96 ?  128 ALA A CA    1 
ATOM   891  C C     . ALA A 1 122 ? -31.400 -15.209 7.386   1.00 10.83 ?  128 ALA A C     1 
ATOM   892  O O     . ALA A 1 122 ? -30.570 -14.304 7.224   1.00 11.88 ?  128 ALA A O     1 
ATOM   893  C CB    . ALA A 1 122 ? -32.314 -15.879 9.632   1.00 13.16 ?  128 ALA A CB    1 
ATOM   894  N N     . ILE A 1 123 ? -31.318 -16.373 6.736   1.00 10.25 ?  129 ILE A N     1 
ATOM   895  C CA    . ILE A 1 123 ? -30.284 -16.602 5.727   1.00 11.85 ?  129 ILE A CA    1 
ATOM   896  C C     . ILE A 1 123 ? -30.414 -15.597 4.592   1.00 13.21 ?  129 ILE A C     1 
ATOM   897  O O     . ILE A 1 123 ? -29.415 -15.033 4.126   1.00 11.89 ?  129 ILE A O     1 
ATOM   898  C CB    . ILE A 1 123 ? -30.367 -18.051 5.204   1.00 11.69 ?  129 ILE A CB    1 
ATOM   899  C CG1   . ILE A 1 123 ? -29.966 -19.047 6.294   1.00 13.71 ?  129 ILE A CG1   1 
ATOM   900  C CG2   . ILE A 1 123 ? -29.539 -18.212 3.921   1.00 13.66 ?  129 ILE A CG2   1 
ATOM   901  C CD1   . ILE A 1 123 ? -30.347 -20.470 5.960   1.00 13.03 ?  129 ILE A CD1   1 
ATOM   902  N N     . GLN A 1 124 ? -31.651 -15.347 4.133   1.00 11.08 ?  130 GLN A N     1 
ATOM   903  C CA    . GLN A 1 124 ? -31.870 -14.368 3.067   1.00 13.77 ?  130 GLN A CA    1 
ATOM   904  C C     . GLN A 1 124 ? -31.460 -12.950 3.471   1.00 14.65 ?  130 GLN A C     1 
ATOM   905  O O     . GLN A 1 124 ? -31.002 -12.175 2.619   1.00 13.08 ?  130 GLN A O     1 
ATOM   906  C CB    . GLN A 1 124 ? -33.337 -14.360 2.632   1.00 16.94 ?  130 GLN A CB    1 
ATOM   907  C CG    . GLN A 1 124 ? -33.567 -13.548 1.345   1.00 19.23 ?  130 GLN A CG    1 
ATOM   908  C CD    . GLN A 1 124 ? -32.891 -14.176 0.143   1.00 22.45 ?  130 GLN A CD    1 
ATOM   909  O OE1   . GLN A 1 124 ? -33.070 -15.358 -0.134  1.00 25.03 ?  130 GLN A OE1   1 
ATOM   910  N NE2   . GLN A 1 124 ? -32.092 -13.392 -0.563  1.00 21.27 ?  130 GLN A NE2   1 
ATOM   911  N N     . ALA A 1 125 ? -31.645 -12.575 4.743   1.00 12.45 ?  131 ALA A N     1 
ATOM   912  C CA    . ALA A 1 125 ? -31.209 -11.246 5.173   1.00 13.59 ?  131 ALA A CA    1 
ATOM   913  C C     . ALA A 1 125 ? -29.713 -11.071 4.949   1.00 10.89 ?  131 ALA A C     1 
ATOM   914  O O     . ALA A 1 125 ? -29.264 -10.009 4.508   1.00 11.03 ?  131 ALA A O     1 
ATOM   915  C CB    . ALA A 1 125 ? -31.547 -11.017 6.651   1.00 15.81 ?  131 ALA A CB    1 
ATOM   916  N N     . TYR A 1 126 ? -28.922 -12.113 5.243   1.00 11.21 ?  132 TYR A N     1 
ATOM   917  C CA    . TYR A 1 126 ? -27.490 -12.042 4.979   1.00 10.63 ?  132 TYR A CA    1 
ATOM   918  C C     . TYR A 1 126 ? -27.195 -12.122 3.482   1.00 12.25 ?  132 TYR A C     1 
ATOM   919  O O     . TYR A 1 126 ? -26.330 -11.393 2.986   1.00 11.80 ?  132 TYR A O     1 
ATOM   920  C CB    . TYR A 1 126 ? -26.754 -13.127 5.782   1.00 9.80  ?  132 TYR A CB    1 
ATOM   921  C CG    . TYR A 1 126 ? -26.614 -12.658 7.210   1.00 9.08  ?  132 TYR A CG    1 
ATOM   922  C CD1   . TYR A 1 126 ? -25.538 -11.856 7.588   1.00 9.76  ?  132 TYR A CD1   1 
ATOM   923  C CD2   . TYR A 1 126 ? -27.603 -12.914 8.145   1.00 10.48 ?  132 TYR A CD2   1 
ATOM   924  C CE1   . TYR A 1 126 ? -25.430 -11.360 8.881   1.00 8.76  ?  132 TYR A CE1   1 
ATOM   925  C CE2   . TYR A 1 126 ? -27.504 -12.428 9.455   1.00 9.58  ?  132 TYR A CE2   1 
ATOM   926  C CZ    . TYR A 1 126 ? -26.426 -11.646 9.805   1.00 10.48 ?  132 TYR A CZ    1 
ATOM   927  O OH    . TYR A 1 126 ? -26.341 -11.156 11.094  1.00 11.75 ?  132 TYR A OH    1 
ATOM   928  N N     . GLU A 1 127 ? -27.912 -12.974 2.729   1.00 12.00 ?  133 GLU A N     1 
ATOM   929  C CA    . GLU A 1 127 ? -27.675 -12.994 1.282   1.00 14.14 ?  133 GLU A CA    1 
ATOM   930  C C     . GLU A 1 127 ? -28.033 -11.656 0.640   1.00 14.88 ?  133 GLU A C     1 
ATOM   931  O O     . GLU A 1 127 ? -27.367 -11.229 -0.314  1.00 13.55 ?  133 GLU A O     1 
ATOM   932  C CB    . GLU A 1 127 ? -28.450 -14.135 0.615   1.00 13.70 ?  133 GLU A CB    1 
ATOM   933  C CG    . GLU A 1 127 ? -27.916 -15.547 0.940   1.00 19.00 ?  133 GLU A CG    1 
ATOM   934  C CD    . GLU A 1 127 ? -26.472 -15.811 0.435   1.00 22.79 ?  133 GLU A CD    1 
ATOM   935  O OE1   . GLU A 1 127 ? -26.000 -15.172 -0.555  1.00 20.85 ?  133 GLU A OE1   1 
ATOM   936  O OE2   . GLU A 1 127 ? -25.803 -16.675 1.050   1.00 22.80 -1 133 GLU A OE2   1 
ATOM   937  N N     . ASP A 1 128 ? -29.060 -10.966 1.153   1.00 12.99 ?  134 ASP A N     1 
ATOM   938  C CA    . ASP A 1 128 ? -29.371 -9.638  0.626   1.00 14.42 ?  134 ASP A CA    1 
ATOM   939  C C     . ASP A 1 128 ? -28.265 -8.650  0.946   1.00 14.63 ?  134 ASP A C     1 
ATOM   940  O O     . ASP A 1 128 ? -27.955 -7.770  0.131   1.00 15.28 ?  134 ASP A O     1 
ATOM   941  C CB    . ASP A 1 128 ? -30.697 -9.139  1.192   1.00 17.51 ?  134 ASP A CB    1 
ATOM   942  C CG    . ASP A 1 128 ? -31.888 -9.892  0.622   1.00 23.16 ?  134 ASP A CG    1 
ATOM   943  O OD1   . ASP A 1 128 ? -31.706 -10.614 -0.390  1.00 25.13 ?  134 ASP A OD1   1 
ATOM   944  O OD2   . ASP A 1 128 ? -33.002 -9.764  1.184   1.00 27.27 -1 134 ASP A OD2   1 
ATOM   945  N N     . MET A 1 129 ? -27.681 -8.770  2.140   1.00 13.02 ?  135 MET A N     1 
ATOM   946  C CA    . MET A 1 129 ? -26.559 -7.918  2.513   1.00 13.51 ?  135 MET A CA    1 
ATOM   947  C C     . MET A 1 129 ? -25.389 -8.126  1.564   1.00 10.83 ?  135 MET A C     1 
ATOM   948  O O     . MET A 1 129 ? -24.750 -7.163  1.126   1.00 11.12 ?  135 MET A O     1 
ATOM   949  C CB    . MET A 1 129 ? -26.164 -8.217  3.963   1.00 14.95 ?  135 MET A CB    1 
ATOM   950  C CG    . MET A 1 129 ? -25.074 -7.325  4.525   1.00 15.73 ?  135 MET A CG    1 
ATOM   951  S SD    . MET A 1 129 ? -25.672 -5.615  4.722   1.00 25.13 ?  135 MET A SD    1 
ATOM   952  C CE    . MET A 1 129 ? -24.145 -4.704  4.613   1.00 21.84 ?  135 MET A CE    1 
ATOM   953  N N     . VAL A 1 130 ? -25.082 -9.383  1.238   1.00 11.67 ?  136 VAL A N     1 
ATOM   954  C CA    . VAL A 1 130 ? -24.019 -9.660  0.268   1.00 10.96 ?  136 VAL A CA    1 
ATOM   955  C C     . VAL A 1 130 ? -24.295 -8.931  -1.036  1.00 10.92 ?  136 VAL A C     1 
ATOM   956  O O     . VAL A 1 130 ? -23.405 -8.299  -1.617  1.00 10.65 ?  136 VAL A O     1 
ATOM   957  C CB    . VAL A 1 130 ? -23.877 -11.177 0.031   1.00 12.35 ?  136 VAL A CB    1 
ATOM   958  C CG1   . VAL A 1 130 ? -22.799 -11.438 -1.038  1.00 12.85 ?  136 VAL A CG1   1 
ATOM   959  C CG2   . VAL A 1 130 ? -23.521 -11.893 1.341   1.00 11.81 ?  136 VAL A CG2   1 
ATOM   960  N N     . ARG A 1 131 ? -25.543 -8.992  -1.508  1.00 12.73 ?  137 ARG A N     1 
ATOM   961  C CA    . ARG A 1 131 ? -25.897 -8.305  -2.751  1.00 15.18 ?  137 ARG A CA    1 
ATOM   962  C C     . ARG A 1 131 ? -25.731 -6.789  -2.643  1.00 13.87 ?  137 ARG A C     1 
ATOM   963  O O     . ARG A 1 131 ? -25.308 -6.148  -3.607  1.00 13.57 ?  137 ARG A O     1 
ATOM   964  C CB    . ARG A 1 131 ? -27.322 -8.672  -3.156  1.00 16.28 ?  137 ARG A CB    1 
ATOM   965  C CG    . ARG A 1 131 ? -27.414 -10.065 -3.804  1.00 22.29 ?  137 ARG A CG    1 
ATOM   966  C CD    . ARG A 1 131 ? -28.853 -10.432 -4.196  1.00 39.87 ?  137 ARG A CD    1 
ATOM   967  N NE    . ARG A 1 131 ? -29.606 -11.003 -3.084  1.00 31.90 ?  137 ARG A NE    1 
ATOM   968  N N     . GLN A 1 132 ? -26.052 -6.190  -1.488  1.00 14.52 ?  138 GLN A N     1 
ATOM   969  C CA    . GLN A 1 132 ? -25.827 -4.747  -1.333  1.00 12.78 ?  138 GLN A CA    1 
ATOM   970  C C     . GLN A 1 132 ? -24.342 -4.419  -1.427  1.00 13.57 ?  138 GLN A C     1 
ATOM   971  O O     . GLN A 1 132 ? -23.952 -3.441  -2.075  1.00 11.93 ?  138 GLN A O     1 
ATOM   972  C CB    . GLN A 1 132 ? -26.359 -4.236  0.012   1.00 14.08 ?  138 GLN A CB    1 
ATOM   973  C CG    . GLN A 1 132 ? -27.857 -4.484  0.304   1.00 16.10 ?  138 GLN A CG    1 
ATOM   974  C CD    . GLN A 1 132 ? -28.772 -3.978  -0.789  1.00 20.01 ?  138 GLN A CD    1 
ATOM   975  O OE1   . GLN A 1 132 ? -28.555 -2.910  -1.366  1.00 17.16 ?  138 GLN A OE1   1 
ATOM   976  N NE2   . GLN A 1 132 ? -29.802 -4.764  -1.099  1.00 26.96 ?  138 GLN A NE2   1 
ATOM   977  N N     . VAL A 1 133 ? -23.505 -5.206  -0.744  1.00 12.11 ?  139 VAL A N     1 
ATOM   978  C CA    . VAL A 1 133 ? -22.065 -4.985  -0.813  1.00 12.38 ?  139 VAL A CA    1 
ATOM   979  C C     . VAL A 1 133 ? -21.583 -5.145  -2.251  1.00 11.04 ?  139 VAL A C     1 
ATOM   980  O O     . VAL A 1 133 ? -20.801 -4.333  -2.752  1.00 10.41 ?  139 VAL A O     1 
ATOM   981  C CB    . VAL A 1 133 ? -21.328 -5.937  0.149   1.00 9.67  ?  139 VAL A CB    1 
ATOM   982  C CG1   . VAL A 1 133 ? -19.797 -5.895  -0.105  1.00 11.47 ?  139 VAL A CG1   1 
ATOM   983  C CG2   . VAL A 1 133 ? -21.641 -5.598  1.607   1.00 9.14  ?  139 VAL A CG2   1 
ATOM   984  N N     . GLN A 1 134 ? -22.058 -6.181  -2.944  1.00 10.43 ?  140 GLN A N     1 
ATOM   985  C CA    . GLN A 1 134 ? -21.603 -6.425  -4.315  1.00 13.24 ?  140 GLN A CA    1 
ATOM   986  C C     . GLN A 1 134 ? -21.994 -5.290  -5.251  1.00 13.65 ?  140 GLN A C     1 
ATOM   987  O O     . GLN A 1 134 ? -21.242 -4.959  -6.175  1.00 12.88 ?  140 GLN A O     1 
ATOM   988  C CB    . GLN A 1 134 ? -22.155 -7.765  -4.823  1.00 14.57 ?  140 GLN A CB    1 
ATOM   989  C CG    . GLN A 1 134 ? -21.436 -8.927  -4.130  1.00 15.29 ?  140 GLN A CG    1 
ATOM   990  C CD    . GLN A 1 134 ? -21.943 -10.299 -4.485  1.00 18.77 ?  140 GLN A CD    1 
ATOM   991  O OE1   . GLN A 1 134 ? -23.086 -10.467 -4.889  1.00 16.70 ?  140 GLN A OE1   1 
ATOM   992  N NE2   . GLN A 1 134 ? -21.091 -11.312 -4.280  1.00 21.10 ?  140 GLN A NE2   1 
ATOM   993  N N     . ARG A 1 135 ? -23.145 -4.669  -5.021  1.00 12.97 ?  141 ARG A N     1 
ATOM   994  C CA    . ARG A 1 135 ? -23.557 -3.569  -5.891  1.00 15.80 ?  141 ARG A CA    1 
ATOM   995  C C     . ARG A 1 135 ? -22.774 -2.290  -5.648  1.00 16.26 ?  141 ARG A C     1 
ATOM   996  O O     . ARG A 1 135 ? -22.778 -1.409  -6.518  1.00 15.29 ?  141 ARG A O     1 
ATOM   997  C CB    . ARG A 1 135 ? -25.042 -3.264  -5.691  1.00 19.45 ?  141 ARG A CB    1 
ATOM   998  C CG    . ARG A 1 135 ? -25.998 -4.335  -6.147  1.00 28.32 ?  141 ARG A CG    1 
ATOM   999  C CD    . ARG A 1 135 ? -27.285 -3.648  -6.569  1.00 50.96 ?  141 ARG A CD    1 
ATOM   1000 N NE    . ARG A 1 135 ? -26.989 -2.661  -7.601  1.00 63.13 ?  141 ARG A NE    1 
ATOM   1001 C CZ    . ARG A 1 135 ? -27.815 -1.705  -8.001  1.00 59.76 ?  141 ARG A CZ    1 
ATOM   1002 N NH1   . ARG A 1 135 ? -29.019 -1.563  -7.467  1.00 57.72 ?  141 ARG A NH1   1 
ATOM   1003 N NH2   . ARG A 1 135 ? -27.422 -0.868  -8.960  1.00 47.99 ?  141 ARG A NH2   1 
ATOM   1004 N N     . SER A 1 136 ? -22.115 -2.156  -4.494  1.00 12.58 ?  142 SER A N     1 
ATOM   1005 C CA    . SER A 1 136 ? -21.599 -0.878  -4.021  1.00 13.37 ?  142 SER A CA    1 
ATOM   1006 C C     . SER A 1 136 ? -20.098 -0.778  -4.272  1.00 14.35 ?  142 SER A C     1 
ATOM   1007 O O     . SER A 1 136 ? -19.318 -1.537  -3.687  1.00 15.01 ?  142 SER A O     1 
ATOM   1008 C CB    . SER A 1 136 ? -21.893 -0.707  -2.526  1.00 10.65 ?  142 SER A CB    1 
ATOM   1009 O OG    . SER A 1 136 ? -23.281 -0.844  -2.251  1.00 11.51 ?  142 SER A OG    1 
ATOM   1010 N N     . ARG A 1 137 ? -19.690 0.187   -5.103  1.00 13.39 ?  143 ARG A N     1 
ATOM   1011 C CA    . ARG A 1 137 ? -18.263 0.427   -5.298  1.00 13.64 ?  143 ARG A CA    1 
ATOM   1012 C C     . ARG A 1 137 ? -17.629 1.125   -4.095  1.00 14.09 ?  143 ARG A C     1 
ATOM   1013 O O     . ARG A 1 137 ? -16.465 0.869   -3.766  1.00 14.41 ?  143 ARG A O     1 
ATOM   1014 C CB    . ARG A 1 137 ? -18.040 1.264   -6.561  1.00 16.95 ?  143 ARG A CB    1 
ATOM   1015 C CG    . ARG A 1 137 ? -16.599 1.735   -6.741  1.00 17.90 ?  143 ARG A CG    1 
ATOM   1016 C CD    . ARG A 1 137 ? -15.709 0.623   -7.237  1.00 20.04 ?  143 ARG A CD    1 
ATOM   1017 N NE    . ARG A 1 137 ? -16.010 0.269   -8.624  1.00 21.40 ?  143 ARG A NE    1 
ATOM   1018 C CZ    . ARG A 1 137 ? -15.302 -0.605  -9.328  1.00 23.88 ?  143 ARG A CZ    1 
ATOM   1019 N NH1   . ARG A 1 137 ? -14.254 -1.223  -8.807  1.00 18.85 ?  143 ARG A NH1   1 
ATOM   1020 N NH2   . ARG A 1 137 ? -15.665 -0.881  -10.575 1.00 21.57 ?  143 ARG A NH2   1 
ATOM   1021 N N     . PHE A 1 138 ? -18.352 2.047   -3.461  1.00 12.65 ?  144 PHE A N     1 
ATOM   1022 C CA    . PHE A 1 138 ? -17.859 2.806   -2.312  1.00 11.44 ?  144 PHE A CA    1 
ATOM   1023 C C     . PHE A 1 138 ? -18.648 2.407   -1.068  1.00 10.24 ?  144 PHE A C     1 
ATOM   1024 O O     . PHE A 1 138 ? -19.881 2.401   -1.084  1.00 9.80  ?  144 PHE A O     1 
ATOM   1025 C CB    . PHE A 1 138 ? -17.998 4.323   -2.546  1.00 11.25 ?  144 PHE A CB    1 
ATOM   1026 C CG    . PHE A 1 138 ? -17.212 4.830   -3.721  1.00 13.87 ?  144 PHE A CG    1 
ATOM   1027 C CD1   . PHE A 1 138 ? -17.718 4.741   -5.005  1.00 14.76 ?  144 PHE A CD1   1 
ATOM   1028 C CD2   . PHE A 1 138 ? -15.970 5.408   -3.539  1.00 17.48 ?  144 PHE A CD2   1 
ATOM   1029 C CE1   . PHE A 1 138 ? -16.991 5.200   -6.085  1.00 18.59 ?  144 PHE A CE1   1 
ATOM   1030 C CE2   . PHE A 1 138 ? -15.240 5.872   -4.619  1.00 17.49 ?  144 PHE A CE2   1 
ATOM   1031 C CZ    . PHE A 1 138 ? -15.745 5.773   -5.881  1.00 18.51 ?  144 PHE A CZ    1 
ATOM   1032 N N     . ILE A 1 139 ? -17.950 2.090   0.017   1.00 8.91  ?  145 ILE A N     1 
ATOM   1033 C CA    . ILE A 1 139 ? -18.601 1.605   1.228   1.00 8.77  ?  145 ILE A CA    1 
ATOM   1034 C C     . ILE A 1 139 ? -17.983 2.300   2.437   1.00 8.64  ?  145 ILE A C     1 
ATOM   1035 O O     . ILE A 1 139 ? -16.757 2.449   2.520   1.00 9.47  ?  145 ILE A O     1 
ATOM   1036 C CB    . ILE A 1 139 ? -18.468 0.067   1.362   1.00 9.10  ?  145 ILE A CB    1 
ATOM   1037 C CG1   . ILE A 1 139 ? -19.066 -0.631  0.136   1.00 9.98  ?  145 ILE A CG1   1 
ATOM   1038 C CG2   . ILE A 1 139 ? -19.128 -0.414  2.638   1.00 9.72  ?  145 ILE A CG2   1 
ATOM   1039 C CD1   . ILE A 1 139 ? -18.731 -2.127  0.033   1.00 11.36 ?  145 ILE A CD1   1 
ATOM   1040 N N     . VAL A 1 140 ? -18.827 2.729   3.370   1.00 8.07  ?  146 VAL A N     1 
ATOM   1041 C CA    . VAL A 1 140 ? -18.382 3.294   4.643   1.00 7.89  ?  146 VAL A CA    1 
ATOM   1042 C C     . VAL A 1 140 ? -18.770 2.346   5.768   1.00 7.93  ?  146 VAL A C     1 
ATOM   1043 O O     . VAL A 1 140 ? -19.935 1.947   5.877   1.00 8.69  ?  146 VAL A O     1 
ATOM   1044 C CB    . VAL A 1 140 ? -18.988 4.690   4.892   1.00 10.04 ?  146 VAL A CB    1 
ATOM   1045 C CG1   . VAL A 1 140 ? -18.777 5.114   6.355   1.00 9.11  ?  146 VAL A CG1   1 
ATOM   1046 C CG2   . VAL A 1 140 ? -18.330 5.699   3.946   1.00 11.93 ?  146 VAL A CG2   1 
ATOM   1047 N N     . VAL A 1 141 ? -17.798 1.996   6.607   1.00 7.75  ?  147 VAL A N     1 
ATOM   1048 C CA    . VAL A 1 141 ? -18.039 1.296   7.864   1.00 8.04  ?  147 VAL A CA    1 
ATOM   1049 C C     . VAL A 1 141 ? -17.908 2.301   9.002   1.00 8.24  ?  147 VAL A C     1 
ATOM   1050 O O     . VAL A 1 141 ? -16.883 2.998   9.114   1.00 11.61 ?  147 VAL A O     1 
ATOM   1051 C CB    . VAL A 1 141 ? -17.048 0.129   8.044   1.00 8.75  ?  147 VAL A CB    1 
ATOM   1052 C CG1   . VAL A 1 141 ? -17.267 -0.563  9.392   1.00 9.71  ?  147 VAL A CG1   1 
ATOM   1053 C CG2   . VAL A 1 141 ? -17.166 -0.862  6.863   1.00 7.34  ?  147 VAL A CG2   1 
ATOM   1054 N N     . VAL A 1 142 ? -18.933 2.392   9.844   1.00 8.35  ?  148 VAL A N     1 
ATOM   1055 C CA    . VAL A 1 142 ? -18.957 3.342   10.960  1.00 10.12 ?  148 VAL A CA    1 
ATOM   1056 C C     . VAL A 1 142 ? -18.666 2.586   12.250  1.00 12.28 ?  148 VAL A C     1 
ATOM   1057 O O     . VAL A 1 142 ? -19.430 1.696   12.642  1.00 11.19 ?  148 VAL A O     1 
ATOM   1058 C CB    . VAL A 1 142 ? -20.300 4.081   11.072  1.00 11.02 ?  148 VAL A CB    1 
ATOM   1059 C CG1   . VAL A 1 142 ? -20.227 5.125   12.192  1.00 12.15 ?  148 VAL A CG1   1 
ATOM   1060 C CG2   . VAL A 1 142 ? -20.673 4.769   9.767   1.00 12.64 ?  148 VAL A CG2   1 
ATOM   1061 N N     . GLY A 1 143 ? -17.562 2.943   12.905  1.00 11.59 ?  149 GLY A N     1 
ATOM   1062 C CA    . GLY A 1 143 ? -17.199 2.400   14.200  1.00 11.50 ?  149 GLY A CA    1 
ATOM   1063 C C     . GLY A 1 143 ? -16.033 1.447   14.059  1.00 13.58 ?  149 GLY A C     1 
ATOM   1064 O O     . GLY A 1 143 ? -16.138 0.452   13.343  1.00 13.63 ?  149 GLY A O     1 
ATOM   1065 N N     . GLY A 1 144 ? -14.915 1.757   14.708  1.00 13.87 ?  150 GLY A N     1 
ATOM   1066 C CA    . GLY A 1 144 ? -13.688 1.004   14.546  1.00 12.95 ?  150 GLY A CA    1 
ATOM   1067 C C     . GLY A 1 144 ? -13.314 0.228   15.792  1.00 14.55 ?  150 GLY A C     1 
ATOM   1068 O O     . GLY A 1 144 ? -12.134 0.133   16.146  1.00 16.32 ?  150 GLY A O     1 
ATOM   1069 N N     . GLY A 1 145 ? -14.318 -0.301  16.478  1.00 13.13 ?  151 GLY A N     1 
ATOM   1070 C CA    . GLY A 1 145 ? -14.102 -1.328  17.467  1.00 14.33 ?  151 GLY A CA    1 
ATOM   1071 C C     . GLY A 1 145 ? -13.718 -2.608  16.758  1.00 14.42 ?  151 GLY A C     1 
ATOM   1072 O O     . GLY A 1 145 ? -13.441 -2.634  15.559  1.00 11.67 ?  151 GLY A O     1 
ATOM   1073 N N     . SER A 1 146 ? -13.729 -3.705  17.512  1.00 15.05 ?  152 SER A N     1 
ATOM   1074 C CA    . SER A 1 146 ? -13.301 -4.960  16.903  1.00 14.56 ?  152 SER A CA    1 
ATOM   1075 C C     . SER A 1 146 ? -14.246 -5.410  15.780  1.00 15.28 ?  152 SER A C     1 
ATOM   1076 O O     . SER A 1 146 ? -13.785 -5.987  14.790  1.00 13.15 ?  152 SER A O     1 
ATOM   1077 C CB    . SER A 1 146 ? -13.152 -6.044  17.978  1.00 20.76 ?  152 SER A CB    1 
ATOM   1078 O OG    . SER A 1 146 ? -14.363 -6.252  18.681  1.00 24.81 ?  152 SER A OG    1 
ATOM   1079 N N     . ALA A 1 147 ? -15.552 -5.151  15.888  1.00 12.16 ?  153 ALA A N     1 
ATOM   1080 C CA    . ALA A 1 147 ? -16.450 -5.515  14.789  1.00 12.16 ?  153 ALA A CA    1 
ATOM   1081 C C     . ALA A 1 147 ? -16.153 -4.708  13.525  1.00 11.70 ?  153 ALA A C     1 
ATOM   1082 O O     . ALA A 1 147 ? -16.076 -5.268  12.420  1.00 10.28 ?  153 ALA A O     1 
ATOM   1083 C CB    . ALA A 1 147 ? -17.911 -5.319  15.206  1.00 12.28 ?  153 ALA A CB    1 
ATOM   1084 N N     . GLY A 1 148 ? -15.977 -3.393  13.660  1.00 10.12 ?  154 GLY A N     1 
ATOM   1085 C CA    . GLY A 1 148 ? -15.795 -2.572  12.483  1.00 10.85 ?  154 GLY A CA    1 
ATOM   1086 C C     . GLY A 1 148 ? -14.501 -2.859  11.747  1.00 9.46  ?  154 GLY A C     1 
ATOM   1087 O O     . GLY A 1 148 ? -14.463 -2.833  10.513  1.00 8.14  ?  154 GLY A O     1 
ATOM   1088 N N     . VAL A 1 149 ? -13.413 -3.108  12.484  1.00 9.54  ?  155 VAL A N     1 
ATOM   1089 C CA    . VAL A 1 149 ? -12.158 -3.427  11.809  1.00 9.11  ?  155 VAL A CA    1 
ATOM   1090 C C     . VAL A 1 149 ? -12.268 -4.759  11.084  1.00 10.10 ?  155 VAL A C     1 
ATOM   1091 O O     . VAL A 1 149 ? -11.762 -4.904  9.965   1.00 9.46  ?  155 VAL A O     1 
ATOM   1092 C CB    . VAL A 1 149 ? -10.961 -3.406  12.785  1.00 11.09 ?  155 VAL A CB    1 
ATOM   1093 C CG1   . VAL A 1 149 ? -10.864 -2.050  13.429  1.00 11.17 ?  155 VAL A CG1   1 
ATOM   1094 C CG2   . VAL A 1 149 ? -11.040 -4.529  13.834  1.00 12.05 ?  155 VAL A CG2   1 
ATOM   1095 N N     . GLU A 1 150 ? -12.971 -5.731  11.675  1.00 8.66  ?  156 GLU A N     1 
ATOM   1096 C CA    . GLU A 1 150 ? -13.195 -6.983  10.960  1.00 10.58 ?  156 GLU A CA    1 
ATOM   1097 C C     . GLU A 1 150 ? -14.072 -6.775  9.734   1.00 11.78 ?  156 GLU A C     1 
ATOM   1098 O O     . GLU A 1 150 ? -13.785 -7.335  8.665   1.00 9.48  ?  156 GLU A O     1 
ATOM   1099 C CB    . GLU A 1 150 ? -13.811 -8.033  11.888  1.00 11.84 ?  156 GLU A CB    1 
ATOM   1100 C CG    . GLU A 1 150 ? -12.834 -8.545  12.944  1.00 15.82 ?  156 GLU A CG    1 
ATOM   1101 C CD    . GLU A 1 150 ? -13.369 -9.737  13.741  1.00 22.50 ?  156 GLU A CD    1 
ATOM   1102 O OE1   . GLU A 1 150 ? -14.607 -9.937  13.759  1.00 23.67 ?  156 GLU A OE1   1 
ATOM   1103 O OE2   . GLU A 1 150 ? -12.552 -10.476 14.345  1.00 16.96 -1 156 GLU A OE2   1 
ATOM   1104 N N     . MET A 1 151 ? -15.135 -5.966  9.859   1.00 7.65  ?  157 MET A N     1 
ATOM   1105 C CA    . MET A 1 151 ? -16.025 -5.707  8.719   1.00 9.43  ?  157 MET A CA    1 
ATOM   1106 C C     . MET A 1 151 ? -15.273 -5.080  7.558   1.00 8.65  ?  157 MET A C     1 
ATOM   1107 O O     . MET A 1 151 ? -15.380 -5.534  6.409   1.00 9.60  ?  157 MET A O     1 
ATOM   1108 C CB    . MET A 1 151 ? -17.185 -4.799  9.138   1.00 9.81  ?  157 MET A CB    1 
ATOM   1109 C CG    . MET A 1 151 ? -18.215 -4.521  8.022   1.00 8.73  ?  157 MET A CG    1 
ATOM   1110 S SD    . MET A 1 151 ? -19.341 -5.911  7.741   1.00 14.90 ?  157 MET A SD    1 
ATOM   1111 C CE    . MET A 1 151 ? -18.629 -6.672  6.311   1.00 12.05 ?  157 MET A CE    1 
ATOM   1112 N N     . ALA A 1 152 ? -14.525 -4.013  7.829   1.00 10.08 ?  158 ALA A N     1 
ATOM   1113 C CA    . ALA A 1 152 ? -13.752 -3.362  6.779   1.00 8.90  ?  158 ALA A CA    1 
ATOM   1114 C C     . ALA A 1 152 ? -12.746 -4.318  6.148   1.00 10.57 ?  158 ALA A C     1 
ATOM   1115 O O     . ALA A 1 152 ? -12.573 -4.337  4.923   1.00 9.58  ?  158 ALA A O     1 
ATOM   1116 C CB    . ALA A 1 152 ? -13.042 -2.129  7.349   1.00 8.74  ?  158 ALA A CB    1 
ATOM   1117 N N     . ALA A 1 153 ? -12.085 -5.139  6.961   1.00 8.81  ?  159 ALA A N     1 
ATOM   1118 C CA    . ALA A 1 153 ? -11.101 -6.060  6.405   1.00 11.23 ?  159 ALA A CA    1 
ATOM   1119 C C     . ALA A 1 153 ? -11.761 -7.130  5.559   1.00 8.36  ?  159 ALA A C     1 
ATOM   1120 O O     . ALA A 1 153 ? -11.200 -7.533  4.536   1.00 10.07 ?  159 ALA A O     1 
ATOM   1121 C CB    . ALA A 1 153 ? -10.281 -6.716  7.527   1.00 13.86 ?  159 ALA A CB    1 
ATOM   1122 N N     . GLU A 1 154 ? -12.932 -7.623  5.979   1.00 8.11  ?  160 GLU A N     1 
ATOM   1123 C CA    . GLU A 1 154 ? -13.613 -8.650  5.198   1.00 7.36  ?  160 GLU A CA    1 
ATOM   1124 C C     . GLU A 1 154 ? -13.973 -8.126  3.826   1.00 8.64  ?  160 GLU A C     1 
ATOM   1125 O O     . GLU A 1 154 ? -13.760 -8.812  2.822   1.00 8.89  ?  160 GLU A O     1 
ATOM   1126 C CB    . GLU A 1 154 ? -14.885 -9.147  5.893   1.00 9.94  ?  160 GLU A CB    1 
ATOM   1127 C CG    . GLU A 1 154 ? -14.664 -10.034 7.096   1.00 11.85 ?  160 GLU A CG    1 
ATOM   1128 C CD    . GLU A 1 154 ? -14.188 -11.452 6.742   1.00 15.82 ?  160 GLU A CD    1 
ATOM   1129 O OE1   . GLU A 1 154 ? -14.479 -11.934 5.614   1.00 13.66 ?  160 GLU A OE1   1 
ATOM   1130 O OE2   . GLU A 1 154 ? -13.569 -12.094 7.638   1.00 15.40 -1 160 GLU A OE2   1 
ATOM   1131 N N     . ILE A 1 155 ? -14.517 -6.909  3.764   1.00 7.05  ?  161 ILE A N     1 
ATOM   1132 C CA    . ILE A 1 155 ? -14.904 -6.339  2.471   1.00 8.41  ?  161 ILE A CA    1 
ATOM   1133 C C     . ILE A 1 155 ? -13.691 -6.204  1.563   1.00 7.99  ?  161 ILE A C     1 
ATOM   1134 O O     . ILE A 1 155 ? -13.727 -6.619  0.400   1.00 7.82  ?  161 ILE A O     1 
ATOM   1135 C CB    . ILE A 1 155 ? -15.612 -4.985  2.665   1.00 7.83  ?  161 ILE A CB    1 
ATOM   1136 C CG1   . ILE A 1 155 ? -16.896 -5.179  3.488   1.00 7.48  ?  161 ILE A CG1   1 
ATOM   1137 C CG2   . ILE A 1 155 ? -15.913 -4.355  1.299   1.00 8.42  ?  161 ILE A CG2   1 
ATOM   1138 C CD1   . ILE A 1 155 ? -17.514 -3.859  4.004   1.00 8.88  ?  161 ILE A CD1   1 
ATOM   1139 N N     . LYS A 1 156 ? -12.601 -5.599  2.063   1.00 7.06  ?  162 LYS A N     1 
ATOM   1140 C CA    . LYS A 1 156 ? -11.457 -5.363  1.175   1.00 9.59  ?  162 LYS A CA    1 
ATOM   1141 C C     . LYS A 1 156 ? -10.720 -6.653  0.812   1.00 10.16 ?  162 LYS A C     1 
ATOM   1142 O O     . LYS A 1 156 ? -10.067 -6.702  -0.242  1.00 10.40 ?  162 LYS A O     1 
ATOM   1143 C CB    . LYS A 1 156 ? -10.454 -4.381  1.794   1.00 12.11 ?  162 LYS A CB    1 
ATOM   1144 C CG    . LYS A 1 156 ? -10.711 -2.926  1.491   1.00 17.01 ?  162 LYS A CG    1 
ATOM   1145 C CD    . LYS A 1 156 ? -10.651 -2.629  -0.003  1.00 14.10 ?  162 LYS A CD    1 
ATOM   1146 C CE    . LYS A 1 156 ? -9.348  -1.972  -0.419  1.00 15.70 ?  162 LYS A CE    1 
ATOM   1147 N NZ    . LYS A 1 156 ? -9.460  -1.339  -1.757  1.00 13.87 ?  162 LYS A NZ    1 
ATOM   1148 N N     . THR A 1 157 ? -10.808 -7.691  1.646   1.00 9.33  ?  163 THR A N     1 
ATOM   1149 C CA    . THR A 1 157 ? -10.191 -8.972  1.284   1.00 8.74  ?  163 THR A CA    1 
ATOM   1150 C C     . THR A 1 157 ? -10.985 -9.695  0.207   1.00 10.58 ?  163 THR A C     1 
ATOM   1151 O O     . THR A 1 157 ? -10.396 -10.273 -0.721  1.00 9.50  ?  163 THR A O     1 
ATOM   1152 C CB    . THR A 1 157 ? -10.060 -9.869  2.521   1.00 9.78  ?  163 THR A CB    1 
ATOM   1153 O OG1   . THR A 1 157 ? -9.309  -9.184  3.532   1.00 9.76  ?  163 THR A OG1   1 
ATOM   1154 C CG2   . THR A 1 157 ? -9.364  -11.183 2.159   1.00 10.67 ?  163 THR A CG2   1 
ATOM   1155 N N     . GLU A 1 158 ? -12.314 -9.708  0.323   1.00 7.87  ?  164 GLU A N     1 
ATOM   1156 C CA    . GLU A 1 158 ? -13.141 -10.355 -0.689  1.00 10.08 ?  164 GLU A CA    1 
ATOM   1157 C C     . GLU A 1 158 ? -13.256 -9.524  -1.966  1.00 11.47 ?  164 GLU A C     1 
ATOM   1158 O O     . GLU A 1 158 ? -13.395 -10.089 -3.060  1.00 10.37 ?  164 GLU A O     1 
ATOM   1159 C CB    . GLU A 1 158 ? -14.540 -10.630 -0.127  1.00 9.77  ?  164 GLU A CB    1 
ATOM   1160 C CG    . GLU A 1 158 ? -14.526 -11.592 1.030   1.00 12.17 ?  164 GLU A CG    1 
ATOM   1161 C CD    . GLU A 1 158 ? -13.859 -12.926 0.658   1.00 17.77 ?  164 GLU A CD    1 
ATOM   1162 O OE1   . GLU A 1 158 ? -14.459 -13.651 -0.152  1.00 18.94 ?  164 GLU A OE1   1 
ATOM   1163 O OE2   . GLU A 1 158 ? -12.732 -13.226 1.144   1.00 15.33 -1 164 GLU A OE2   1 
ATOM   1164 N N     . TYR A 1 159 ? -13.207 -8.196  -1.855  1.00 8.86  ?  165 TYR A N     1 
ATOM   1165 C CA    . TYR A 1 159 ? -13.441 -7.289  -2.982  1.00 9.15  ?  165 TYR A CA    1 
ATOM   1166 C C     . TYR A 1 159 ? -12.370 -6.213  -2.999  1.00 9.41  ?  165 TYR A C     1 
ATOM   1167 O O     . TYR A 1 159 ? -12.636 -5.054  -2.663  1.00 9.10  ?  165 TYR A O     1 
ATOM   1168 C CB    . TYR A 1 159 ? -14.818 -6.635  -2.900  1.00 10.12 ?  165 TYR A CB    1 
ATOM   1169 C CG    . TYR A 1 159 ? -15.944 -7.617  -2.750  1.00 10.70 ?  165 TYR A CG    1 
ATOM   1170 C CD1   . TYR A 1 159 ? -16.474 -8.253  -3.857  1.00 12.70 ?  165 TYR A CD1   1 
ATOM   1171 C CD2   . TYR A 1 159 ? -16.476 -7.908  -1.501  1.00 9.86  ?  165 TYR A CD2   1 
ATOM   1172 C CE1   . TYR A 1 159 ? -17.491 -9.165  -3.740  1.00 11.79 ?  165 TYR A CE1   1 
ATOM   1173 C CE2   . TYR A 1 159 ? -17.519 -8.826  -1.370  1.00 12.19 ?  165 TYR A CE2   1 
ATOM   1174 C CZ    . TYR A 1 159 ? -18.011 -9.446  -2.497  1.00 15.73 ?  165 TYR A CZ    1 
ATOM   1175 O OH    . TYR A 1 159 ? -19.034 -10.364 -2.383  1.00 14.57 ?  165 TYR A OH    1 
ATOM   1176 N N     . PRO A 1 160 ? -11.144 -6.558  -3.376  1.00 9.04  ?  166 PRO A N     1 
ATOM   1177 C CA    . PRO A 1 160 ? -10.068 -5.550  -3.321  1.00 13.20 ?  166 PRO A CA    1 
ATOM   1178 C C     . PRO A 1 160 ? -10.333 -4.354  -4.205  1.00 12.42 ?  166 PRO A C     1 
ATOM   1179 O O     . PRO A 1 160 ? -9.775  -3.275  -3.950  1.00 10.60 ?  166 PRO A O     1 
ATOM   1180 C CB    . PRO A 1 160 ? -8.821  -6.326  -3.772  1.00 14.45 ?  166 PRO A CB    1 
ATOM   1181 C CG    . PRO A 1 160 ? -9.336  -7.601  -4.377  1.00 15.46 ?  166 PRO A CG    1 
ATOM   1182 C CD    . PRO A 1 160 ? -10.636 -7.903  -3.698  1.00 10.97 ?  166 PRO A CD    1 
ATOM   1183 N N     . GLU A 1 161 ? -11.200 -4.496  -5.211  1.00 9.54  ?  167 GLU A N     1 
ATOM   1184 C CA    . GLU A 1 161 ? -11.472 -3.389  -6.119  1.00 14.03 ?  167 GLU A CA    1 
ATOM   1185 C C     . GLU A 1 161 ? -12.436 -2.349  -5.540  1.00 15.46 ?  167 GLU A C     1 
ATOM   1186 O O     . GLU A 1 161 ? -12.621 -1.298  -6.156  1.00 13.87 ?  167 GLU A O     1 
ATOM   1187 C CB    . GLU A 1 161 ? -12.016 -3.936  -7.447  1.00 16.45 ?  167 GLU A CB    1 
ATOM   1188 C CG    . GLU A 1 161 ? -13.467 -4.406  -7.377  1.00 16.59 ?  167 GLU A CG    1 
ATOM   1189 C CD    . GLU A 1 161 ? -13.647 -5.829  -6.812  1.00 17.18 ?  167 GLU A CD    1 
ATOM   1190 O OE1   . GLU A 1 161 ? -12.669 -6.426  -6.287  1.00 12.34 ?  167 GLU A OE1   1 
ATOM   1191 O OE2   . GLU A 1 161 ? -14.789 -6.362  -6.924  1.00 11.18 -1 167 GLU A OE2   1 
ATOM   1192 N N     . LYS A 1 162 ? -13.059 -2.606  -4.396  1.00 10.68 ?  168 LYS A N     1 
ATOM   1193 C CA    . LYS A 1 162 ? -13.967 -1.632  -3.801  1.00 12.16 ?  168 LYS A CA    1 
ATOM   1194 C C     . LYS A 1 162 ? -13.189 -0.619  -2.949  1.00 16.72 ?  168 LYS A C     1 
ATOM   1195 O O     . LYS A 1 162 ? -12.062 -0.862  -2.512  1.00 13.50 ?  168 LYS A O     1 
ATOM   1196 C CB    . LYS A 1 162 ? -15.035 -2.335  -2.966  1.00 12.32 ?  168 LYS A CB    1 
ATOM   1197 C CG    . LYS A 1 162 ? -16.027 -3.159  -3.809  1.00 11.09 ?  168 LYS A CG    1 
ATOM   1198 C CD    . LYS A 1 162 ? -17.075 -3.817  -2.942  1.00 12.95 ?  168 LYS A CD    1 
ATOM   1199 C CE    . LYS A 1 162 ? -17.880 -4.781  -3.765  1.00 10.42 ?  168 LYS A CE    1 
ATOM   1200 N NZ    . LYS A 1 162 ? -18.668 -4.018  -4.822  1.00 13.06 ?  168 LYS A NZ    1 
ATOM   1201 N N     . GLU A 1 163 ? -13.801 0.539   -2.734  1.00 12.66 ?  169 GLU A N     1 
ATOM   1202 C CA    . GLU A 1 163 ? -13.219 1.599   -1.923  1.00 16.39 ?  169 GLU A CA    1 
ATOM   1203 C C     . GLU A 1 163 ? -13.887 1.564   -0.561  1.00 16.72 ?  169 GLU A C     1 
ATOM   1204 O O     . GLU A 1 163 ? -15.100 1.756   -0.465  1.00 13.36 ?  169 GLU A O     1 
ATOM   1205 C CB    . GLU A 1 163 ? -13.419 2.973   -2.572  1.00 18.15 ?  169 GLU A CB    1 
ATOM   1206 C CG    . GLU A 1 163 ? -12.748 3.099   -3.929  1.00 27.41 ?  169 GLU A CG    1 
ATOM   1207 C CD    . GLU A 1 163 ? -11.239 3.051   -3.816  1.00 53.14 ?  169 GLU A CD    1 
ATOM   1208 O OE1   . GLU A 1 163 ? -10.701 3.499   -2.777  1.00 67.92 ?  169 GLU A OE1   1 
ATOM   1209 O OE2   . GLU A 1 163 ? -10.588 2.549   -4.757  1.00 65.27 -1 169 GLU A OE2   1 
ATOM   1210 N N     . VAL A 1 164 ? -13.109 1.320   0.486   1.00 12.37 ?  170 VAL A N     1 
ATOM   1211 C CA    . VAL A 1 164 ? -13.664 1.133   1.820   1.00 11.52 ?  170 VAL A CA    1 
ATOM   1212 C C     . VAL A 1 164 ? -13.072 2.171   2.754   1.00 14.35 ?  170 VAL A C     1 
ATOM   1213 O O     . VAL A 1 164 ? -11.846 2.311   2.847   1.00 11.18 ?  170 VAL A O     1 
ATOM   1214 C CB    . VAL A 1 164 ? -13.394 -0.283  2.353   1.00 12.90 ?  170 VAL A CB    1 
ATOM   1215 C CG1   . VAL A 1 164 ? -13.974 -0.415  3.766   1.00 13.00 ?  170 VAL A CG1   1 
ATOM   1216 C CG2   . VAL A 1 164 ? -13.969 -1.330  1.384   1.00 11.27 ?  170 VAL A CG2   1 
ATOM   1217 N N     . THR A 1 165 ? -13.938 2.876   3.469   1.00 10.15 ?  171 THR A N     1 
ATOM   1218 C CA    . THR A 1 165 ? -13.528 3.844   4.469   1.00 11.58 ?  171 THR A CA    1 
ATOM   1219 C C     . THR A 1 165 ? -14.108 3.413   5.805   1.00 11.90 ?  171 THR A C     1 
ATOM   1220 O O     . THR A 1 165 ? -15.301 3.082   5.894   1.00 10.68 ?  171 THR A O     1 
ATOM   1221 C CB    . THR A 1 165 ? -14.004 5.264   4.112   1.00 13.90 ?  171 THR A CB    1 
ATOM   1222 O OG1   . THR A 1 165 ? -13.391 5.673   2.879   1.00 15.41 ?  171 THR A OG1   1 
ATOM   1223 C CG2   . THR A 1 165 ? -13.637 6.249   5.217   1.00 13.79 ?  171 THR A CG2   1 
ATOM   1224 N N     . LEU A 1 166 ? -13.260 3.378   6.823   1.00 9.86  ?  172 LEU A N     1 
ATOM   1225 C CA    . LEU A 1 166 ? -13.680 3.085   8.188   1.00 11.19 ?  172 LEU A CA    1 
ATOM   1226 C C     . LEU A 1 166 ? -13.585 4.377   8.989   1.00 12.68 ?  172 LEU A C     1 
ATOM   1227 O O     . LEU A 1 166 ? -12.518 4.997   9.034   1.00 12.20 ?  172 LEU A O     1 
ATOM   1228 C CB    . LEU A 1 166 ? -12.794 1.991   8.797   1.00 10.60 ?  172 LEU A CB    1 
ATOM   1229 C CG    . LEU A 1 166 ? -12.986 1.674   10.276  1.00 11.14 ?  172 LEU A CG    1 
ATOM   1230 C CD1   . LEU A 1 166 ? -14.352 1.055   10.488  1.00 13.02 ?  172 LEU A CD1   1 
ATOM   1231 C CD2   . LEU A 1 166 ? -11.892 0.694   10.729  1.00 13.77 ?  172 LEU A CD2   1 
ATOM   1232 N N     . ILE A 1 167 ? -14.694 4.800   9.589   1.00 10.63 ?  173 ILE A N     1 
ATOM   1233 C CA    . ILE A 1 167 ? -14.740 6.034   10.371  1.00 11.78 ?  173 ILE A CA    1 
ATOM   1234 C C     . ILE A 1 167 ? -14.885 5.659   11.839  1.00 13.26 ?  173 ILE A C     1 
ATOM   1235 O O     . ILE A 1 167 ? -15.836 4.965   12.220  1.00 11.14 ?  173 ILE A O     1 
ATOM   1236 C CB    . ILE A 1 167 ? -15.876 6.961   9.922   1.00 12.92 ?  173 ILE A CB    1 
ATOM   1237 C CG1   . ILE A 1 167 ? -15.815 7.175   8.419   1.00 11.15 ?  173 ILE A CG1   1 
ATOM   1238 C CG2   . ILE A 1 167 ? -15.767 8.321   10.681  1.00 13.44 ?  173 ILE A CG2   1 
ATOM   1239 C CD1   . ILE A 1 167 ? -16.981 7.982   7.826   1.00 15.51 ?  173 ILE A CD1   1 
ATOM   1240 N N     . HIS A 1 168 ? -13.969 6.145   12.663  1.00 15.10 ?  174 HIS A N     1 
ATOM   1241 C CA    . HIS A 1 168 ? -13.902 5.743   14.061  1.00 14.04 ?  174 HIS A CA    1 
ATOM   1242 C C     . HIS A 1 168 ? -13.711 6.974   14.939  1.00 16.70 ?  174 HIS A C     1 
ATOM   1243 O O     . HIS A 1 168 ? -12.908 7.851   14.618  1.00 16.66 ?  174 HIS A O     1 
ATOM   1244 C CB    . HIS A 1 168 ? -12.741 4.775   14.275  1.00 13.86 ?  174 HIS A CB    1 
ATOM   1245 C CG    . HIS A 1 168 ? -12.650 4.249   15.672  1.00 16.36 ?  174 HIS A CG    1 
ATOM   1246 N ND1   . HIS A 1 168 ? -13.752 3.814   16.373  1.00 14.47 ?  174 HIS A ND1   1 
ATOM   1247 C CD2   . HIS A 1 168 ? -11.588 4.074   16.492  1.00 17.26 ?  174 HIS A CD2   1 
ATOM   1248 C CE1   . HIS A 1 168 ? -13.377 3.405   17.570  1.00 17.30 ?  174 HIS A CE1   1 
ATOM   1249 N NE2   . HIS A 1 168 ? -12.069 3.538   17.664  1.00 18.10 ?  174 HIS A NE2   1 
ATOM   1250 N N     . SER A 1 169 ? -14.418 7.015   16.070  1.00 17.69 ?  175 SER A N     1 
ATOM   1251 C CA    . SER A 1 169 ? -14.400 8.212   16.911  1.00 18.38 ?  175 SER A CA    1 
ATOM   1252 C C     . SER A 1 169 ? -13.172 8.316   17.803  1.00 19.05 ?  175 SER A C     1 
ATOM   1253 O O     . SER A 1 169 ? -12.934 9.385   18.377  1.00 20.60 ?  175 SER A O     1 
ATOM   1254 C CB    . SER A 1 169 ? -15.664 8.267   17.775  1.00 20.27 ?  175 SER A CB    1 
ATOM   1255 O OG    . SER A 1 169 ? -15.805 7.077   18.535  1.00 22.76 ?  175 SER A OG    1 
ATOM   1256 N N     . GLN A 1 170 ? -12.379 7.263   17.935  1.00 21.02 ?  176 GLN A N     1 
ATOM   1257 C CA    . GLN A 1 170 ? -11.240 7.286   18.841  1.00 21.92 ?  176 GLN A CA    1 
ATOM   1258 C C     . GLN A 1 170 ? -9.945  7.358   18.043  1.00 22.02 ?  176 GLN A C     1 
ATOM   1259 O O     . GLN A 1 170 ? -9.936  7.232   16.819  1.00 20.42 ?  176 GLN A O     1 
ATOM   1260 C CB    . GLN A 1 170 ? -11.250 6.057   19.757  1.00 23.01 ?  176 GLN A CB    1 
ATOM   1261 C CG    . GLN A 1 170 ? -12.595 5.775   20.416  1.00 24.48 ?  176 GLN A CG    1 
ATOM   1262 C CD    . GLN A 1 170 ? -13.053 6.915   21.316  1.00 33.93 ?  176 GLN A CD    1 
ATOM   1263 O OE1   . GLN A 1 170 ? -12.233 7.686   21.820  1.00 36.33 ?  176 GLN A OE1   1 
ATOM   1264 N NE2   . GLN A 1 170 ? -14.364 7.032   21.512  1.00 50.18 ?  176 GLN A NE2   1 
ATOM   1265 N N     . VAL A 1 171 ? -8.833  7.539   18.757  1.00 23.12 ?  177 VAL A N     1 
ATOM   1266 C CA    . VAL A 1 171 ? -7.539  7.625   18.084  1.00 24.93 ?  177 VAL A CA    1 
ATOM   1267 C C     . VAL A 1 171 ? -7.040  6.245   17.660  1.00 22.74 ?  177 VAL A C     1 
ATOM   1268 O O     . VAL A 1 171 ? -6.431  6.094   16.597  1.00 25.84 ?  177 VAL A O     1 
ATOM   1269 C CB    . VAL A 1 171 ? -6.509  8.336   18.987  1.00 28.41 ?  177 VAL A CB    1 
ATOM   1270 C CG1   . VAL A 1 171 ? -5.295  8.744   18.164  1.00 30.58 ?  177 VAL A CG1   1 
ATOM   1271 C CG2   . VAL A 1 171 ? -7.141  9.559   19.672  1.00 28.37 ?  177 VAL A CG2   1 
ATOM   1272 N N     . ALA A 1 172 ? -7.261  5.227   18.485  1.00 22.96 ?  178 ALA A N     1 
ATOM   1273 C CA    . ALA A 1 172 ? -6.792  3.872   18.217  1.00 23.54 ?  178 ALA A CA    1 
ATOM   1274 C C     . ALA A 1 172 ? -7.969  2.927   17.994  1.00 22.82 ?  178 ALA A C     1 
ATOM   1275 O O     . ALA A 1 172 ? -9.089  3.161   18.461  1.00 20.74 ?  178 ALA A O     1 
ATOM   1276 C CB    . ALA A 1 172 ? -5.915  3.355   19.366  1.00 21.20 ?  178 ALA A CB    1 
ATOM   1277 N N     . LEU A 1 173 ? -7.689  1.816   17.315  1.00 23.15 ?  179 LEU A N     1 
ATOM   1278 C CA    . LEU A 1 173 ? -8.711  0.884   16.867  1.00 19.07 ?  179 LEU A CA    1 
ATOM   1279 C C     . LEU A 1 173 ? -8.896  -0.273  17.838  1.00 22.80 ?  179 LEU A C     1 
ATOM   1280 O O     . LEU A 1 173 ? -7.990  -0.627  18.595  1.00 22.83 ?  179 LEU A O     1 
ATOM   1281 C CB    . LEU A 1 173 ? -8.344  0.338   15.489  1.00 17.86 ?  179 LEU A CB    1 
ATOM   1282 C CG    . LEU A 1 173 ? -8.331  1.380   14.377  1.00 19.40 ?  179 LEU A CG    1 
ATOM   1283 C CD1   . LEU A 1 173 ? -7.642  0.804   13.142  1.00 17.74 ?  179 LEU A CD1   1 
ATOM   1284 C CD2   . LEU A 1 173 ? -9.752  1.821   14.040  1.00 18.05 ?  179 LEU A CD2   1 
ATOM   1285 N N     . ALA A 1 174 ? -10.088 -0.874  17.789  1.00 21.98 ?  180 ALA A N     1 
ATOM   1286 C CA    . ALA A 1 174 ? -10.432 -2.056  18.574  1.00 22.86 ?  180 ALA A CA    1 
ATOM   1287 C C     . ALA A 1 174 ? -10.324 -1.802  20.077  1.00 28.02 ?  180 ALA A C     1 
ATOM   1288 O O     . ALA A 1 174 ? -10.135 -0.659  20.516  1.00 27.78 ?  180 ALA A O     1 
ATOM   1289 C CB    . ALA A 1 174 ? -9.568  -3.249  18.151  1.00 21.88 ?  180 ALA A CB    1 
ATOM   1290 N N     . ASP A 1 175 ? -10.457 -2.864  20.871  1.00 28.73 ?  181 ASP A N     1 
ATOM   1291 C CA    . ASP A 1 175 ? -10.734 -2.725  22.296  1.00 31.29 ?  181 ASP A CA    1 
ATOM   1292 C C     . ASP A 1 175 ? -9.578  -2.093  23.054  1.00 30.64 ?  181 ASP A C     1 
ATOM   1293 O O     . ASP A 1 175 ? -8.410  -2.428  22.840  1.00 27.35 ?  181 ASP A O     1 
ATOM   1294 C CB    . ASP A 1 175 ? -11.045 -4.088  22.911  1.00 35.92 ?  181 ASP A CB    1 
ATOM   1295 C CG    . ASP A 1 175 ? -12.444 -4.549  22.610  1.00 41.62 ?  181 ASP A CG    1 
ATOM   1296 O OD1   . ASP A 1 175 ? -12.744 -4.822  21.427  1.00 78.61 ?  181 ASP A OD1   1 
ATOM   1297 O OD2   . ASP A 1 175 ? -13.244 -4.634  23.564  1.00 41.70 -1 181 ASP A OD2   1 
ATOM   1298 N N     . LYS A 1 176 ? -9.923  -1.199  23.982  1.00 30.34 ?  182 LYS A N     1 
ATOM   1299 C CA    . LYS A 1 176 ? -8.910  -0.568  24.816  1.00 32.79 ?  182 LYS A CA    1 
ATOM   1300 C C     . LYS A 1 176 ? -8.170  -1.587  25.675  1.00 34.05 ?  182 LYS A C     1 
ATOM   1301 O O     . LYS A 1 176 ? -7.007  -1.366  26.029  1.00 34.27 ?  182 LYS A O     1 
ATOM   1302 C CB    . LYS A 1 176 ? -9.556  0.507   25.692  1.00 35.00 ?  182 LYS A CB    1 
ATOM   1303 N N     . GLU A 1 177 ? -8.813  -2.713  26.008  1.00 35.54 ?  183 GLU A N     1 
ATOM   1304 C CA    . GLU A 1 177 ? -8.164  -3.705  26.862  1.00 37.59 ?  183 GLU A CA    1 
ATOM   1305 C C     . GLU A 1 177 ? -7.040  -4.442  26.150  1.00 32.18 ?  183 GLU A C     1 
ATOM   1306 O O     . GLU A 1 177 ? -6.219  -5.081  26.815  1.00 29.60 ?  183 GLU A O     1 
ATOM   1307 C CB    . GLU A 1 177 ? -9.174  -4.733  27.379  1.00 39.59 ?  183 GLU A CB    1 
ATOM   1308 C CG    . GLU A 1 177 ? -10.216 -4.183  28.333  1.00 48.00 ?  183 GLU A CG    1 
ATOM   1309 C CD    . GLU A 1 177 ? -11.392 -3.553  27.607  1.00 55.58 ?  183 GLU A CD    1 
ATOM   1310 O OE1   . GLU A 1 177 ? -11.290 -3.326  26.377  1.00 55.46 ?  183 GLU A OE1   1 
ATOM   1311 O OE2   . GLU A 1 177 ? -12.422 -3.288  28.265  1.00 63.88 -1 183 GLU A OE2   1 
ATOM   1312 N N     . LEU A 1 178 ? -6.992  -4.390  24.825  1.00 27.29 ?  184 LEU A N     1 
ATOM   1313 C CA    . LEU A 1 178 ? -5.980  -5.139  24.105  1.00 24.32 ?  184 LEU A CA    1 
ATOM   1314 C C     . LEU A 1 178 ? -4.596  -4.547  24.332  1.00 23.90 ?  184 LEU A C     1 
ATOM   1315 O O     . LEU A 1 178 ? -4.435  -3.350  24.592  1.00 23.45 ?  184 LEU A O     1 
ATOM   1316 C CB    . LEU A 1 178 ? -6.279  -5.143  22.612  1.00 23.88 ?  184 LEU A CB    1 
ATOM   1317 C CG    . LEU A 1 178 ? -7.569  -5.832  22.190  1.00 21.98 ?  184 LEU A CG    1 
ATOM   1318 C CD1   . LEU A 1 178 ? -7.904  -5.452  20.748  1.00 20.79 ?  184 LEU A CD1   1 
ATOM   1319 C CD2   . LEU A 1 178 ? -7.444  -7.330  22.327  1.00 23.01 ?  184 LEU A CD2   1 
ATOM   1320 N N     . LEU A 1 179 ? -3.590  -5.408  24.205  1.00 21.17 ?  185 LEU A N     1 
ATOM   1321 C CA    . LEU A 1 179 ? -2.206  -4.968  24.148  1.00 21.55 ?  185 LEU A CA    1 
ATOM   1322 C C     . LEU A 1 179 ? -2.053  -3.857  23.112  1.00 23.09 ?  185 LEU A C     1 
ATOM   1323 O O     . LEU A 1 179 ? -2.581  -3.981  22.000  1.00 21.64 ?  185 LEU A O     1 
ATOM   1324 C CB    . LEU A 1 179 ? -1.296  -6.138  23.769  1.00 20.99 ?  185 LEU A CB    1 
ATOM   1325 C CG    . LEU A 1 179 ? -1.136  -7.316  24.724  1.00 26.11 ?  185 LEU A CG    1 
ATOM   1326 C CD1   . LEU A 1 179 ? -0.450  -8.484  24.020  1.00 24.33 ?  185 LEU A CD1   1 
ATOM   1327 C CD2   . LEU A 1 179 ? -0.341  -6.889  25.956  1.00 27.27 ?  185 LEU A CD2   1 
ATOM   1328 N N     . PRO A 1 180 ? -1.338  -2.776  23.421  1.00 23.19 ?  186 PRO A N     1 
ATOM   1329 C CA    . PRO A 1 180 ? -1.061  -1.765  22.381  1.00 21.76 ?  186 PRO A CA    1 
ATOM   1330 C C     . PRO A 1 180 ? -0.455  -2.343  21.106  1.00 22.41 ?  186 PRO A C     1 
ATOM   1331 O O     . PRO A 1 180 ? -0.770  -1.858  20.010  1.00 23.38 ?  186 PRO A O     1 
ATOM   1332 C CB    . PRO A 1 180 ? -0.101  -0.804  23.092  1.00 24.29 ?  186 PRO A CB    1 
ATOM   1333 C CG    . PRO A 1 180 ? -0.541  -0.884  24.535  1.00 20.21 ?  186 PRO A CG    1 
ATOM   1334 C CD    . PRO A 1 180 ? -0.895  -2.330  24.760  1.00 20.80 ?  186 PRO A CD    1 
ATOM   1335 N N     . SER A 1 181 ? 0.390   -3.374  21.211  1.00 19.40 ?  187 SER A N     1 
ATOM   1336 C CA    . SER A 1 181 ? 0.973   -3.999  20.022  1.00 19.28 ?  187 SER A CA    1 
ATOM   1337 C C     . SER A 1 181 ? -0.103  -4.578  19.111  1.00 20.67 ?  187 SER A C     1 
ATOM   1338 O O     . SER A 1 181 ? 0.011   -4.523  17.877  1.00 20.20 ?  187 SER A O     1 
ATOM   1339 C CB    . SER A 1 181 ? 1.947   -5.100  20.433  1.00 20.77 ?  187 SER A CB    1 
ATOM   1340 O OG    . SER A 1 181 ? 1.275   -6.116  21.166  1.00 21.62 ?  187 SER A OG    1 
ATOM   1341 N N     . VAL A 1 182 ? -1.142  -5.166  19.702  1.00 21.35 ?  188 VAL A N     1 
ATOM   1342 C CA    . VAL A 1 182 ? -2.232  -5.714  18.906  1.00 19.43 ?  188 VAL A CA    1 
ATOM   1343 C C     . VAL A 1 182 ? -2.979  -4.593  18.197  1.00 18.66 ?  188 VAL A C     1 
ATOM   1344 O O     . VAL A 1 182 ? -3.288  -4.686  17.004  1.00 15.77 ?  188 VAL A O     1 
ATOM   1345 C CB    . VAL A 1 182 ? -3.172  -6.546  19.794  1.00 19.56 ?  188 VAL A CB    1 
ATOM   1346 C CG1   . VAL A 1 182 ? -4.481  -6.855  19.058  1.00 17.62 ?  188 VAL A CG1   1 
ATOM   1347 C CG2   . VAL A 1 182 ? -2.481  -7.823  20.236  1.00 19.94 ?  188 VAL A CG2   1 
ATOM   1348 N N     . ARG A 1 183 ? -3.298  -3.531  18.932  1.00 18.28 ?  189 ARG A N     1 
ATOM   1349 C CA    . ARG A 1 183 ? -4.083  -2.441  18.363  1.00 18.79 ?  189 ARG A CA    1 
ATOM   1350 C C     . ARG A 1 183 ? -3.339  -1.749  17.232  1.00 18.87 ?  189 ARG A C     1 
ATOM   1351 O O     . ARG A 1 183 ? -3.945  -1.352  16.228  1.00 17.60 ?  189 ARG A O     1 
ATOM   1352 C CB    . ARG A 1 183 ? -4.443  -1.440  19.457  1.00 19.60 ?  189 ARG A CB    1 
ATOM   1353 C CG    . ARG A 1 183 ? -5.292  -2.027  20.568  1.00 19.30 ?  189 ARG A CG    1 
ATOM   1354 C CD    . ARG A 1 183 ? -5.632  -0.956  21.573  1.00 22.84 ?  189 ARG A CD    1 
ATOM   1355 N NE    . ARG A 1 183 ? -6.813  -0.199  21.185  1.00 24.18 ?  189 ARG A NE    1 
ATOM   1356 C CZ    . ARG A 1 183 ? -7.209  0.916   21.781  1.00 28.64 ?  189 ARG A CZ    1 
ATOM   1357 N NH1   . ARG A 1 183 ? -6.497  1.466   22.750  1.00 29.37 ?  189 ARG A NH1   1 
ATOM   1358 N NH2   . ARG A 1 183 ? -8.356  1.482   21.411  1.00 22.73 ?  189 ARG A NH2   1 
ATOM   1359 N N     . GLN A 1 184 ? -2.024  -1.599  17.368  1.00 20.30 ?  190 GLN A N     1 
ATOM   1360 C CA    . GLN A 1 184 ? -1.258  -0.964  16.300  1.00 21.94 ?  190 GLN A CA    1 
ATOM   1361 C C     . GLN A 1 184 ? -1.152  -1.868  15.075  1.00 20.40 ?  190 GLN A C     1 
ATOM   1362 O O     . GLN A 1 184 ? -1.191  -1.386  13.935  1.00 17.95 ?  190 GLN A O     1 
ATOM   1363 C CB    . GLN A 1 184 ? 0.130   -0.575  16.811  1.00 22.72 ?  190 GLN A CB    1 
ATOM   1364 C CG    . GLN A 1 184 ? 1.006   0.109   15.757  1.00 27.36 ?  190 GLN A CG    1 
ATOM   1365 C CD    . GLN A 1 184 ? 0.400   1.397   15.217  1.00 30.33 ?  190 GLN A CD    1 
ATOM   1366 O OE1   . GLN A 1 184 ? -0.392  2.061   15.888  1.00 33.43 ?  190 GLN A OE1   1 
ATOM   1367 N NE2   . GLN A 1 184 ? 0.784   1.761   14.006  1.00 29.08 ?  190 GLN A NE2   1 
ATOM   1368 N N     . GLU A 1 185 ? -1.000  -3.181  15.284  1.00 17.99 ?  191 GLU A N     1 
ATOM   1369 C CA    . GLU A 1 185 ? -0.931  -4.083  14.139  1.00 19.25 ?  191 GLU A CA    1 
ATOM   1370 C C     . GLU A 1 185 ? -2.260  -4.129  13.385  1.00 18.93 ?  191 GLU A C     1 
ATOM   1371 O O     . GLU A 1 185 ? -2.264  -4.233  12.153  1.00 16.37 ?  191 GLU A O     1 
ATOM   1372 C CB    . GLU A 1 185 ? -0.503  -5.482  14.589  1.00 20.46 ?  191 GLU A CB    1 
ATOM   1373 C CG    . GLU A 1 185 ? -0.230  -6.480  13.460  1.00 24.85 ?  191 GLU A CG    1 
ATOM   1374 C CD    . GLU A 1 185 ? 0.953   -6.078  12.575  1.00 35.45 ?  191 GLU A CD    1 
ATOM   1375 O OE1   . GLU A 1 185 ? 1.688   -5.132  12.942  1.00 34.50 ?  191 GLU A OE1   1 
ATOM   1376 O OE2   . GLU A 1 185 ? 1.150   -6.714  11.513  1.00 43.84 -1 191 GLU A OE2   1 
ATOM   1377 N N     . VAL A 1 186 ? -3.390  -4.038  14.100  1.00 15.59 ?  192 VAL A N     1 
ATOM   1378 C CA    . VAL A 1 186 ? -4.696  -3.946  13.435  1.00 15.66 ?  192 VAL A CA    1 
ATOM   1379 C C     . VAL A 1 186 ? -4.714  -2.761  12.478  1.00 15.26 ?  192 VAL A C     1 
ATOM   1380 O O     . VAL A 1 186 ? -5.159  -2.864  11.327  1.00 14.13 ?  192 VAL A O     1 
ATOM   1381 C CB    . VAL A 1 186 ? -5.825  -3.824  14.474  1.00 14.86 ?  192 VAL A CB    1 
ATOM   1382 C CG1   . VAL A 1 186 ? -7.142  -3.489  13.769  1.00 15.37 ?  192 VAL A CG1   1 
ATOM   1383 C CG2   . VAL A 1 186 ? -5.970  -5.121  15.259  1.00 13.86 ?  192 VAL A CG2   1 
ATOM   1384 N N     . LYS A 1 187 ? -4.232  -1.611  12.947  1.00 13.87 ?  193 LYS A N     1 
ATOM   1385 C CA    . LYS A 1 187 ? -4.175  -0.433  12.082  1.00 15.94 ?  193 LYS A CA    1 
ATOM   1386 C C     . LYS A 1 187 ? -3.306  -0.686  10.854  1.00 17.78 ?  193 LYS A C     1 
ATOM   1387 O O     . LYS A 1 187 ? -3.680  -0.314  9.734   1.00 14.12 ?  193 LYS A O     1 
ATOM   1388 C CB    . LYS A 1 187 ? -3.661  0.770   12.880  1.00 17.24 ?  193 LYS A CB    1 
ATOM   1389 C CG    . LYS A 1 187 ? -3.601  2.081   12.104  1.00 16.91 ?  193 LYS A CG    1 
ATOM   1390 C CD    . LYS A 1 187 ? -3.228  3.216   13.054  1.00 20.62 ?  193 LYS A CD    1 
ATOM   1391 C CE    . LYS A 1 187 ? -3.200  4.567   12.349  1.00 25.32 ?  193 LYS A CE    1 
ATOM   1392 N NZ    . LYS A 1 187 ? -2.776  5.643   13.302  1.00 30.28 ?  193 LYS A NZ    1 
ATOM   1393 N N     . GLU A 1 188 ? -2.139  -1.306  11.038  1.00 18.65 ?  194 GLU A N     1 
ATOM   1394 C CA    . GLU A 1 188 ? -1.222  -1.481  9.911   1.00 20.75 ?  194 GLU A CA    1 
ATOM   1395 C C     . GLU A 1 188 ? -1.788  -2.440  8.877   1.00 21.45 ?  194 GLU A C     1 
ATOM   1396 O O     . GLU A 1 188 ? -1.589  -2.250  7.671   1.00 17.06 ?  194 GLU A O     1 
ATOM   1397 C CB    . GLU A 1 188 ? 0.136   -1.984  10.397  1.00 25.12 ?  194 GLU A CB    1 
ATOM   1398 C CG    . GLU A 1 188 ? 0.918   -0.941  11.189  1.00 29.17 ?  194 GLU A CG    1 
ATOM   1399 C CD    . GLU A 1 188 ? 1.172   0.319   10.379  1.00 42.19 ?  194 GLU A CD    1 
ATOM   1400 O OE1   . GLU A 1 188 ? 1.425   0.208   9.157   1.00 50.21 ?  194 GLU A OE1   1 
ATOM   1401 O OE2   . GLU A 1 188 ? 1.108   1.424   10.963  1.00 61.67 -1 194 GLU A OE2   1 
ATOM   1402 N N     . ILE A 1 189 ? -2.455  -3.500  9.335   1.00 15.27 ?  195 ILE A N     1 
ATOM   1403 C CA    . ILE A 1 189 ? -3.047  -4.456  8.403   1.00 15.62 ?  195 ILE A CA    1 
ATOM   1404 C C     . ILE A 1 189 ? -4.120  -3.774  7.572   1.00 16.54 ?  195 ILE A C     1 
ATOM   1405 O O     . ILE A 1 189 ? -4.162  -3.921  6.344   1.00 14.58 ?  195 ILE A O     1 
ATOM   1406 C CB    . ILE A 1 189 ? -3.602  -5.666  9.173   1.00 16.80 ?  195 ILE A CB    1 
ATOM   1407 C CG1   . ILE A 1 189 ? -2.438  -6.465  9.777   1.00 17.78 ?  195 ILE A CG1   1 
ATOM   1408 C CG2   . ILE A 1 189 ? -4.463  -6.544  8.261   1.00 17.46 ?  195 ILE A CG2   1 
ATOM   1409 C CD1   . ILE A 1 189 ? -2.850  -7.405  10.910  1.00 21.61 ?  195 ILE A CD1   1 
ATOM   1410 N N     . LEU A 1 190 ? -5.009  -3.013  8.227   1.00 13.49 ?  196 LEU A N     1 
ATOM   1411 C CA    . LEU A 1 190 ? -6.053  -2.305  7.484   1.00 16.11 ?  196 LEU A CA    1 
ATOM   1412 C C     . LEU A 1 190 ? -5.452  -1.382  6.432   1.00 16.16 ?  196 LEU A C     1 
ATOM   1413 O O     . LEU A 1 190 ? -5.890  -1.373  5.275   1.00 13.36 ?  196 LEU A O     1 
ATOM   1414 C CB    . LEU A 1 190 ? -6.945  -1.506  8.436   1.00 13.24 ?  196 LEU A CB    1 
ATOM   1415 C CG    . LEU A 1 190 ? -7.890  -2.368  9.268   1.00 13.67 ?  196 LEU A CG    1 
ATOM   1416 C CD1   . LEU A 1 190 ? -8.750  -1.486  10.176  1.00 15.33 ?  196 LEU A CD1   1 
ATOM   1417 C CD2   . LEU A 1 190 ? -8.775  -3.156  8.350   1.00 14.10 ?  196 LEU A CD2   1 
ATOM   1418 N N     . LEU A 1 191 ? -4.448  -0.590  6.817   1.00 15.94 ?  197 LEU A N     1 
ATOM   1419 C CA    . LEU A 1 191 ? -3.838  0.329   5.855   1.00 16.41 ?  197 LEU A CA    1 
ATOM   1420 C C     . LEU A 1 191 ? -3.208  -0.428  4.686   1.00 19.46 ?  197 LEU A C     1 
ATOM   1421 O O     . LEU A 1 191 ? -3.371  -0.032  3.527   1.00 16.90 ?  197 LEU A O     1 
ATOM   1422 C CB    . LEU A 1 191 ? -2.798  1.207   6.552   1.00 16.52 ?  197 LEU A CB    1 
ATOM   1423 C CG    . LEU A 1 191 ? -3.389  2.254   7.524   1.00 17.37 ?  197 LEU A CG    1 
ATOM   1424 C CD1   . LEU A 1 191 ? -2.334  2.925   8.407   1.00 18.67 ?  197 LEU A CD1   1 
ATOM   1425 C CD2   . LEU A 1 191 ? -4.222  3.320   6.749   1.00 13.81 ?  197 LEU A CD2   1 
ATOM   1426 N N     . ARG A 1 192 ? -2.500  -1.529  4.968   1.00 14.32 ?  198 ARG A N     1 
ATOM   1427 C CA    . ARG A 1 192 ? -1.899  -2.320  3.890   1.00 17.93 ?  198 ARG A CA    1 
ATOM   1428 C C     . ARG A 1 192 ? -2.948  -2.944  2.971   1.00 21.23 ?  198 ARG A C     1 
ATOM   1429 O O     . ARG A 1 192 ? -2.666  -3.191  1.793   1.00 20.79 ?  198 ARG A O     1 
ATOM   1430 C CB    . ARG A 1 192 ? -1.011  -3.430  4.455   1.00 20.21 ?  198 ARG A CB    1 
ATOM   1431 C CG    . ARG A 1 192 ? 0.260   -3.011  5.205   1.00 27.95 ?  198 ARG A CG    1 
ATOM   1432 C CD    . ARG A 1 192 ? 1.035   -4.283  5.656   1.00 33.64 ?  198 ARG A CD    1 
ATOM   1433 N NE    . ARG A 1 192 ? 1.800   -4.117  6.891   1.00 44.70 ?  198 ARG A NE    1 
ATOM   1434 C CZ    . ARG A 1 192 ? 1.545   -4.751  8.031   1.00 45.14 ?  198 ARG A CZ    1 
ATOM   1435 N NH1   . ARG A 1 192 ? 0.572   -5.643  8.125   1.00 42.21 ?  198 ARG A NH1   1 
ATOM   1436 N NH2   . ARG A 1 192 ? 2.284   -4.483  9.105   1.00 55.37 ?  198 ARG A NH2   1 
ATOM   1437 N N     . LYS A 1 193 ? -4.140  -3.249  3.490   1.00 14.36 ?  199 LYS A N     1 
ATOM   1438 C CA    . LYS A 1 193 ? -5.228  -3.735  2.645   1.00 16.75 ?  199 LYS A CA    1 
ATOM   1439 C C     . LYS A 1 193 ? -5.856  -2.638  1.796   1.00 16.70 ?  199 LYS A C     1 
ATOM   1440 O O     . LYS A 1 193 ? -6.653  -2.957  0.905   1.00 17.48 ?  199 LYS A O     1 
ATOM   1441 C CB    . LYS A 1 193 ? -6.326  -4.389  3.496   1.00 14.47 ?  199 LYS A CB    1 
ATOM   1442 C CG    . LYS A 1 193 ? -5.926  -5.727  4.116   1.00 16.31 ?  199 LYS A CG    1 
ATOM   1443 C CD    . LYS A 1 193 ? -7.140  -6.420  4.707   1.00 17.11 ?  199 LYS A CD    1 
ATOM   1444 C CE    . LYS A 1 193 ? -6.803  -7.783  5.297   1.00 12.80 ?  199 LYS A CE    1 
ATOM   1445 N NZ    . LYS A 1 193 ? -6.525  -8.875  4.304   1.00 10.80 ?  199 LYS A NZ    1 
ATOM   1446 N N     . GLY A 1 194 ? -5.520  -1.375  2.043   1.00 14.29 ?  200 GLY A N     1 
ATOM   1447 C CA    . GLY A 1 194 ? -6.098  -0.278  1.288   1.00 16.97 ?  200 GLY A CA    1 
ATOM   1448 C C     . GLY A 1 194 ? -7.339  0.343   1.896   1.00 14.97 ?  200 GLY A C     1 
ATOM   1449 O O     . GLY A 1 194 ? -7.970  1.183   1.242   1.00 12.74 ?  200 GLY A O     1 
ATOM   1450 N N     . VAL A 1 195 ? -7.720  -0.050  3.116   1.00 11.36 ?  201 VAL A N     1 
ATOM   1451 C CA    . VAL A 1 195 ? -8.826  0.608   3.802   1.00 11.02 ?  201 VAL A CA    1 
ATOM   1452 C C     . VAL A 1 195 ? -8.396  2.025   4.141   1.00 15.30 ?  201 VAL A C     1 
ATOM   1453 O O     . VAL A 1 195 ? -7.287  2.241   4.641   1.00 14.21 ?  201 VAL A O     1 
ATOM   1454 C CB    . VAL A 1 195 ? -9.223  -0.170  5.071   1.00 10.99 ?  201 VAL A CB    1 
ATOM   1455 C CG1   . VAL A 1 195 ? -10.386 0.523   5.803   1.00 13.26 ?  201 VAL A CG1   1 
ATOM   1456 C CG2   . VAL A 1 195 ? -9.600  -1.588  4.727   1.00 11.06 ?  201 VAL A CG2   1 
ATOM   1457 N N     . GLN A 1 196 ? -9.256  3.000   3.837   1.00 12.44 ?  202 GLN A N     1 
ATOM   1458 C CA    . GLN A 1 196 ? -9.041  4.380   4.258   1.00 16.49 ?  202 GLN A CA    1 
ATOM   1459 C C     . GLN A 1 196 ? -9.527  4.546   5.689   1.00 18.01 ?  202 GLN A C     1 
ATOM   1460 O O     . GLN A 1 196 ? -10.647 4.148   6.014   1.00 14.88 ?  202 GLN A O     1 
ATOM   1461 C CB    . GLN A 1 196 ? -9.805  5.339   3.348   1.00 17.34 ?  202 GLN A CB    1 
ATOM   1462 C CG    . GLN A 1 196 ? -9.484  5.180   1.880   1.00 25.19 ?  202 GLN A CG    1 
ATOM   1463 C CD    . GLN A 1 196 ? -8.636  6.328   1.387   1.00 49.11 ?  202 GLN A CD    1 
ATOM   1464 O OE1   . GLN A 1 196 ? -9.159  7.364   0.971   1.00 64.90 ?  202 GLN A OE1   1 
ATOM   1465 N NE2   . GLN A 1 196 ? -7.318  6.166   1.461   1.00 56.38 ?  202 GLN A NE2   1 
ATOM   1466 N N     . LEU A 1 197 ? -8.697  5.132   6.541   1.00 15.99 ?  203 LEU A N     1 
ATOM   1467 C CA    . LEU A 1 197 ? -9.041  5.308   7.945   1.00 13.78 ?  203 LEU A CA    1 
ATOM   1468 C C     . LEU A 1 197 ? -9.325  6.780   8.220   1.00 18.86 ?  203 LEU A C     1 
ATOM   1469 O O     . LEU A 1 197 ? -8.538  7.653   7.849   1.00 18.34 ?  203 LEU A O     1 
ATOM   1470 C CB    . LEU A 1 197 ? -7.931  4.794   8.860   1.00 17.47 ?  203 LEU A CB    1 
ATOM   1471 C CG    . LEU A 1 197 ? -7.575  3.311   8.730   1.00 16.67 ?  203 LEU A CG    1 
ATOM   1472 C CD1   . LEU A 1 197 ? -6.485  2.950   9.723   1.00 18.12 ?  203 LEU A CD1   1 
ATOM   1473 C CD2   . LEU A 1 197 ? -8.803  2.412   8.960   1.00 15.33 ?  203 LEU A CD2   1 
ATOM   1474 N N     . LEU A 1 198 ? -10.464 7.051   8.842   1.00 15.37 ?  204 LEU A N     1 
ATOM   1475 C CA    . LEU A 1 198 ? -10.808 8.375   9.352   1.00 18.83 ?  204 LEU A CA    1 
ATOM   1476 C C     . LEU A 1 198 ? -10.944 8.244   10.860  1.00 19.97 ?  204 LEU A C     1 
ATOM   1477 O O     . LEU A 1 198 ? -12.029 7.930   11.354  1.00 17.70 ?  204 LEU A O     1 
ATOM   1478 C CB    . LEU A 1 198 ? -12.083 8.879   8.737   1.00 20.03 ?  204 LEU A CB    1 
ATOM   1479 C CG    . LEU A 1 198 ? -12.016 9.682   7.455   1.00 26.11 ?  204 LEU A CG    1 
ATOM   1480 C CD1   . LEU A 1 198 ? -13.404 10.259  7.227   1.00 26.04 ?  204 LEU A CD1   1 
ATOM   1481 C CD2   . LEU A 1 198 ? -10.985 10.800  7.580   1.00 30.24 ?  204 LEU A CD2   1 
ATOM   1482 N N     . LEU A 1 199 ? -9.848  8.483   11.586  1.00 19.75 ?  205 LEU A N     1 
ATOM   1483 C CA    . LEU A 1 199 ? -9.814  8.315   13.032  1.00 18.57 ?  205 LEU A CA    1 
ATOM   1484 C C     . LEU A 1 199 ? -10.079 9.639   13.748  1.00 21.89 ?  205 LEU A C     1 
ATOM   1485 O O     . LEU A 1 199 ? -9.929  10.725  13.181  1.00 23.41 ?  205 LEU A O     1 
ATOM   1486 C CB    . LEU A 1 199 ? -8.469  7.740   13.484  1.00 21.33 ?  205 LEU A CB    1 
ATOM   1487 C CG    . LEU A 1 199 ? -8.105  6.412   12.816  1.00 20.09 ?  205 LEU A CG    1 
ATOM   1488 C CD1   . LEU A 1 199 ? -6.738  5.921   13.250  1.00 23.84 ?  205 LEU A CD1   1 
ATOM   1489 C CD2   . LEU A 1 199 ? -9.176  5.375   13.119  1.00 21.94 ?  205 LEU A CD2   1 
ATOM   1490 N N     . SER A 1 200 ? -10.484 9.524   15.014  1.00 21.05 ?  206 SER A N     1 
ATOM   1491 C CA    . SER A 1 200 ? -10.904 10.665  15.831  1.00 19.81 ?  206 SER A CA    1 
ATOM   1492 C C     . SER A 1 200 ? -11.997 11.477  15.146  1.00 23.93 ?  206 SER A C     1 
ATOM   1493 O O     . SER A 1 200 ? -11.982 12.710  15.167  1.00 23.10 ?  206 SER A O     1 
ATOM   1494 C CB    . SER A 1 200 ? -9.719  11.566  16.183  1.00 22.82 ?  206 SER A CB    1 
ATOM   1495 O OG    . SER A 1 200 ? -8.757  10.858  16.940  1.00 26.52 ?  206 SER A OG    1 
ATOM   1496 N N     . GLU A 1 201 ? -12.960 10.786  14.530  1.00 18.86 ?  207 GLU A N     1 
ATOM   1497 C CA    . GLU A 1 201 ? -14.092 11.461  13.902  1.00 22.27 ?  207 GLU A CA    1 
ATOM   1498 C C     . GLU A 1 201 ? -15.362 10.688  14.200  1.00 19.76 ?  207 GLU A C     1 
ATOM   1499 O O     . GLU A 1 201 ? -15.375 9.456   14.139  1.00 16.46 ?  207 GLU A O     1 
ATOM   1500 C CB    . GLU A 1 201 ? -13.916 11.605  12.374  1.00 25.91 ?  207 GLU A CB    1 
ATOM   1501 C CG    . GLU A 1 201 ? -12.568 12.186  11.965  1.00 30.31 ?  207 GLU A CG    1 
ATOM   1502 C CD    . GLU A 1 201 ? -12.665 13.244  10.882  1.00 41.72 ?  207 GLU A CD    1 
ATOM   1503 O OE1   . GLU A 1 201 ? -13.764 13.805  10.692  1.00 37.15 ?  207 GLU A OE1   1 
ATOM   1504 O OE2   . GLU A 1 201 ? -11.636 13.520  10.227  1.00 44.41 -1 207 GLU A OE2   1 
ATOM   1505 N N     . ARG A 1 202 ? -16.432 11.413  14.495  1.00 18.65 ?  208 ARG A N     1 
ATOM   1506 C CA    . ARG A 1 202 ? -17.722 10.812  14.804  1.00 20.77 ?  208 ARG A CA    1 
ATOM   1507 C C     . ARG A 1 202 ? -18.697 11.112  13.668  1.00 19.52 ?  208 ARG A C     1 
ATOM   1508 O O     . ARG A 1 202 ? -18.905 12.278  13.309  1.00 19.10 ?  208 ARG A O     1 
ATOM   1509 C CB    . ARG A 1 202 ? -18.272 11.324  16.142  1.00 21.88 ?  208 ARG A CB    1 
ATOM   1510 C CG    . ARG A 1 202 ? -19.593 10.650  16.518  1.00 22.92 ?  208 ARG A CG    1 
ATOM   1511 C CD    . ARG A 1 202 ? -20.035 10.939  17.952  1.00 27.24 ?  208 ARG A CD    1 
ATOM   1512 N NE    . ARG A 1 202 ? -19.078 10.433  18.932  1.00 29.49 ?  208 ARG A NE    1 
ATOM   1513 C CZ    . ARG A 1 202 ? -19.058 9.190   19.401  1.00 30.13 ?  208 ARG A CZ    1 
ATOM   1514 N NH1   . ARG A 1 202 ? -19.936 8.283   19.000  1.00 24.37 ?  208 ARG A NH1   1 
ATOM   1515 N NH2   . ARG A 1 202 ? -18.137 8.851   20.306  1.00 30.28 ?  208 ARG A NH2   1 
ATOM   1516 N N     . VAL A 1 203 ? -19.273 10.063  13.085  1.00 17.20 ?  209 VAL A N     1 
ATOM   1517 C CA    . VAL A 1 203 ? -20.301 10.289  12.082  1.00 17.81 ?  209 VAL A CA    1 
ATOM   1518 C C     . VAL A 1 203 ? -21.480 10.955  12.769  1.00 19.13 ?  209 VAL A C     1 
ATOM   1519 O O     . VAL A 1 203 ? -21.965 10.482  13.804  1.00 17.43 ?  209 VAL A O     1 
ATOM   1520 C CB    . VAL A 1 203 ? -20.702 8.979   11.388  1.00 15.87 ?  209 VAL A CB    1 
ATOM   1521 C CG1   . VAL A 1 203 ? -21.911 9.221   10.496  1.00 17.33 ?  209 VAL A CG1   1 
ATOM   1522 C CG2   . VAL A 1 203 ? -19.533 8.453   10.533  1.00 13.24 ?  209 VAL A CG2   1 
ATOM   1523 N N     . SER A 1 204 ? -21.931 12.074  12.209  1.00 19.50 ?  210 SER A N     1 
ATOM   1524 C CA    . SER A 1 204 ? -22.866 12.949  12.896  1.00 22.65 ?  210 SER A CA    1 
ATOM   1525 C C     . SER A 1 204 ? -24.264 12.981  12.296  1.00 27.84 ?  210 SER A C     1 
ATOM   1526 O O     . SER A 1 204 ? -25.158 13.571  12.913  1.00 29.00 ?  210 SER A O     1 
ATOM   1527 C CB    . SER A 1 204 ? -22.311 14.380  12.925  1.00 23.25 ?  210 SER A CB    1 
ATOM   1528 O OG    . SER A 1 204 ? -21.933 14.770  11.613  1.00 24.81 ?  210 SER A OG    1 
ATOM   1529 N N     . ASN A 1 205 ? -24.493 12.383  11.129  1.00 21.70 ?  211 ASN A N     1 
ATOM   1530 C CA    . ASN A 1 205 ? -25.823 12.439  10.533  1.00 25.80 ?  211 ASN A CA    1 
ATOM   1531 C C     . ASN A 1 205 ? -26.447 11.050  10.411  1.00 26.07 ?  211 ASN A C     1 
ATOM   1532 O O     . ASN A 1 205 ? -27.142 10.755  9.436   1.00 27.85 ?  211 ASN A O     1 
ATOM   1533 C CB    . ASN A 1 205 ? -25.798 13.169  9.180   1.00 25.50 ?  211 ASN A CB    1 
ATOM   1534 C CG    . ASN A 1 205 ? -24.939 12.469  8.112   1.00 26.85 ?  211 ASN A CG    1 
ATOM   1535 O OD1   . ASN A 1 205 ? -23.996 11.726  8.409   1.00 23.09 ?  211 ASN A OD1   1 
ATOM   1536 N ND2   . ASN A 1 205 ? -25.265 12.730  6.851   1.00 24.81 ?  211 ASN A ND2   1 
ATOM   1537 N N     . LEU A 1 206 ? -26.249 10.198  11.433  1.00 26.31 ?  212 LEU A N     1 
ATOM   1538 C CA    . LEU A 1 206 ? -26.690 8.802   11.353  1.00 28.46 ?  212 LEU A CA    1 
ATOM   1539 C C     . LEU A 1 206 ? -28.196 8.677   11.143  1.00 29.59 ?  212 LEU A C     1 
ATOM   1540 O O     . LEU A 1 206 ? -28.649 7.746   10.467  1.00 28.78 ?  212 LEU A O     1 
ATOM   1541 C CB    . LEU A 1 206 ? -26.291 8.032   12.615  1.00 27.60 ?  212 LEU A CB    1 
ATOM   1542 C CG    . LEU A 1 206 ? -24.846 7.544   12.698  1.00 25.90 ?  212 LEU A CG    1 
ATOM   1543 C CD1   . LEU A 1 206 ? -24.636 6.724   13.959  1.00 32.79 ?  212 LEU A CD1   1 
ATOM   1544 C CD2   . LEU A 1 206 ? -24.483 6.743   11.464  1.00 26.04 ?  212 LEU A CD2   1 
ATOM   1545 N N     . GLU A 1 207 ? -28.986 9.595   11.714  1.00 31.83 ?  213 GLU A N     1 
ATOM   1546 C CA    . GLU A 1 207 ? -30.433 9.544   11.523  1.00 32.49 ?  213 GLU A CA    1 
ATOM   1547 C C     . GLU A 1 207 ? -30.819 9.716   10.058  1.00 33.84 ?  213 GLU A C     1 
ATOM   1548 O O     . GLU A 1 207 ? -31.829 9.159   9.613   1.00 37.17 ?  213 GLU A O     1 
ATOM   1549 C CB    . GLU A 1 207 ? -31.112 10.615  12.376  1.00 37.84 ?  213 GLU A CB    1 
ATOM   1550 C CG    . GLU A 1 207 ? -30.671 12.034  12.038  1.00 37.87 ?  213 GLU A CG    1 
ATOM   1551 N N     . GLU A 1 208 ? -30.032 10.469  9.296   1.00 31.19 ?  214 GLU A N     1 
ATOM   1552 C CA    . GLU A 1 208 ? -30.354 10.796  7.916   1.00 30.04 ?  214 GLU A CA    1 
ATOM   1553 C C     . GLU A 1 208 ? -29.828 9.771   6.919   1.00 27.58 ?  214 GLU A C     1 
ATOM   1554 O O     . GLU A 1 208 ? -30.039 9.940   5.712   1.00 28.15 ?  214 GLU A O     1 
ATOM   1555 C CB    . GLU A 1 208 ? -29.795 12.181  7.573   1.00 32.61 ?  214 GLU A CB    1 
ATOM   1556 N N     . LEU A 1 209 ? -29.146 8.705   7.391   1.00 27.08 ?  215 LEU A N     1 
ATOM   1557 C CA    . LEU A 1 209 ? -28.440 7.808   6.477   1.00 23.41 ?  215 LEU A CA    1 
ATOM   1558 C C     . LEU A 1 209 ? -29.256 6.558   6.202   1.00 19.63 ?  215 LEU A C     1 
ATOM   1559 O O     . LEU A 1 209 ? -29.759 5.932   7.146   1.00 21.00 ?  215 LEU A O     1 
ATOM   1560 C CB    . LEU A 1 209 ? -27.081 7.402   7.056   1.00 21.35 ?  215 LEU A CB    1 
ATOM   1561 C CG    . LEU A 1 209 ? -26.002 8.477   7.224   1.00 23.30 ?  215 LEU A CG    1 
ATOM   1562 C CD1   . LEU A 1 209 ? -24.751 7.891   7.865   1.00 22.88 ?  215 LEU A CD1   1 
ATOM   1563 C CD2   . LEU A 1 209 ? -25.671 9.099   5.899   1.00 21.14 ?  215 LEU A CD2   1 
ATOM   1564 N N     . PRO A 1 210 ? -29.408 6.169   4.938   1.00 20.61 ?  216 PRO A N     1 
ATOM   1565 C CA    . PRO A 1 210 ? -29.883 4.812   4.639   1.00 20.14 ?  216 PRO A CA    1 
ATOM   1566 C C     . PRO A 1 210 ? -28.802 3.815   5.027   1.00 20.85 ?  216 PRO A C     1 
ATOM   1567 O O     . PRO A 1 210 ? -27.627 4.006   4.689   1.00 17.85 ?  216 PRO A O     1 
ATOM   1568 C CB    . PRO A 1 210 ? -30.112 4.838   3.122   1.00 23.05 ?  216 PRO A CB    1 
ATOM   1569 C CG    . PRO A 1 210 ? -29.982 6.293   2.710   1.00 26.55 ?  216 PRO A CG    1 
ATOM   1570 C CD    . PRO A 1 210 ? -29.097 6.933   3.724   1.00 22.16 ?  216 PRO A CD    1 
ATOM   1571 N N     . LEU A 1 211 ? -29.200 2.754   5.729   1.00 18.86 ?  217 LEU A N     1 
ATOM   1572 C CA    . LEU A 1 211 ? -28.278 1.769   6.285   1.00 18.22 ?  217 LEU A CA    1 
ATOM   1573 C C     . LEU A 1 211 ? -28.437 0.422   5.592   1.00 19.21 ?  217 LEU A C     1 
ATOM   1574 O O     . LEU A 1 211 ? -29.560 -0.008  5.297   1.00 18.18 ?  217 LEU A O     1 
ATOM   1575 C CB    . LEU A 1 211 ? -28.520 1.597   7.791   1.00 17.72 ?  217 LEU A CB    1 
ATOM   1576 C CG    . LEU A 1 211 ? -28.383 2.869   8.631   1.00 20.01 ?  217 LEU A CG    1 
ATOM   1577 C CD1   . LEU A 1 211 ? -28.740 2.602   10.092  1.00 20.40 ?  217 LEU A CD1   1 
ATOM   1578 C CD2   . LEU A 1 211 ? -26.980 3.428   8.507   1.00 20.41 ?  217 LEU A CD2   1 
ATOM   1579 N N     . ASN A 1 212 ? -27.307 -0.245  5.331   1.00 14.82 ?  218 ASN A N     1 
ATOM   1580 C CA    . ASN A 1 212 ? -27.305 -1.597  4.764   1.00 14.91 ?  218 ASN A CA    1 
ATOM   1581 C C     . ASN A 1 212 ? -28.025 -1.670  3.419   1.00 16.77 ?  218 ASN A C     1 
ATOM   1582 O O     . ASN A 1 212 ? -28.594 -2.708  3.067   1.00 18.71 ?  218 ASN A O     1 
ATOM   1583 C CB    . ASN A 1 212 ? -27.932 -2.602  5.734   1.00 19.20 ?  218 ASN A CB    1 
ATOM   1584 C CG    . ASN A 1 212 ? -27.230 -2.643  7.072   1.00 17.04 ?  218 ASN A CG    1 
ATOM   1585 O OD1   . ASN A 1 212 ? -26.021 -2.469  7.154   1.00 14.80 ?  218 ASN A OD1   1 
ATOM   1586 N ND2   . ASN A 1 212 ? -27.995 -2.871  8.138   1.00 18.36 ?  218 ASN A ND2   1 
ATOM   1587 N N     . GLU A 1 213 ? -27.988 -0.596  2.638   1.00 14.92 ?  219 GLU A N     1 
ATOM   1588 C CA    . GLU A 1 213 ? -28.720 -0.561  1.377   1.00 16.46 ?  219 GLU A CA    1 
ATOM   1589 C C     . GLU A 1 213 ? -27.926 0.238   0.357   1.00 13.73 ?  219 GLU A C     1 
ATOM   1590 O O     . GLU A 1 213 ? -27.526 1.373   0.635   1.00 15.56 ?  219 GLU A O     1 
ATOM   1591 C CB    . GLU A 1 213 ? -30.114 0.059   1.582   1.00 20.09 ?  219 GLU A CB    1 
ATOM   1592 C CG    . GLU A 1 213 ? -30.855 0.417   0.287   1.00 23.48 ?  219 GLU A CG    1 
ATOM   1593 N N     . TYR A 1 214 ? -27.714 -0.346  -0.821  1.00 13.33 ?  220 TYR A N     1 
ATOM   1594 C CA    . TYR A 1 214 ? -27.060 0.383   -1.896  1.00 12.56 ?  220 TYR A CA    1 
ATOM   1595 C C     . TYR A 1 214 ? -27.870 1.614   -2.289  1.00 16.11 ?  220 TYR A C     1 
ATOM   1596 O O     . TYR A 1 214 ? -29.088 1.541   -2.467  1.00 13.52 ?  220 TYR A O     1 
ATOM   1597 C CB    . TYR A 1 214 ? -26.874 -0.515  -3.117  1.00 12.88 ?  220 TYR A CB    1 
ATOM   1598 C CG    . TYR A 1 214 ? -26.521 0.267   -4.361  1.00 17.03 ?  220 TYR A CG    1 
ATOM   1599 C CD1   . TYR A 1 214 ? -25.207 0.644   -4.611  1.00 15.30 ?  220 TYR A CD1   1 
ATOM   1600 C CD2   . TYR A 1 214 ? -27.505 0.655   -5.275  1.00 18.35 ?  220 TYR A CD2   1 
ATOM   1601 C CE1   . TYR A 1 214 ? -24.880 1.371   -5.731  1.00 16.92 ?  220 TYR A CE1   1 
ATOM   1602 C CE2   . TYR A 1 214 ? -27.185 1.387   -6.393  1.00 19.66 ?  220 TYR A CE2   1 
ATOM   1603 C CZ    . TYR A 1 214 ? -25.877 1.747   -6.617  1.00 18.88 ?  220 TYR A CZ    1 
ATOM   1604 O OH    . TYR A 1 214 ? -25.527 2.474   -7.726  1.00 21.37 ?  220 TYR A OH    1 
ATOM   1605 N N     . ARG A 1 215 ? -27.191 2.741   -2.426  1.00 13.19 ?  221 ARG A N     1 
ATOM   1606 C CA    . ARG A 1 215 ? -27.759 3.931   -3.055  1.00 14.34 ?  221 ARG A CA    1 
ATOM   1607 C C     . ARG A 1 215 ? -26.744 4.482   -4.036  1.00 15.32 ?  221 ARG A C     1 
ATOM   1608 O O     . ARG A 1 215 ? -25.533 4.355   -3.826  1.00 13.69 ?  221 ARG A O     1 
ATOM   1609 C CB    . ARG A 1 215 ? -28.097 5.035   -2.039  1.00 16.94 ?  221 ARG A CB    1 
ATOM   1610 C CG    . ARG A 1 215 ? -29.138 4.682   -1.018  1.00 21.21 ?  221 ARG A CG    1 
ATOM   1611 C CD    . ARG A 1 215 ? -30.502 4.551   -1.664  1.00 25.21 ?  221 ARG A CD    1 
ATOM   1612 N NE    . ARG A 1 215 ? -31.506 4.190   -0.673  1.00 31.70 ?  221 ARG A NE    1 
ATOM   1613 C CZ    . ARG A 1 215 ? -32.203 5.068   0.035   1.00 42.04 ?  221 ARG A CZ    1 
ATOM   1614 N NH1   . ARG A 1 215 ? -32.092 6.372   -0.175  1.00 38.35 ?  221 ARG A NH1   1 
ATOM   1615 N NH2   . ARG A 1 215 ? -33.029 4.628   0.981   1.00 51.92 ?  221 ARG A NH2   1 
ATOM   1616 N N     . GLU A 1 216 ? -27.240 5.121   -5.112  1.00 14.75 ?  222 GLU A N     1 
ATOM   1617 C CA    . GLU A 1 216 ? -26.328 5.751   -6.048  1.00 17.71 ?  222 GLU A CA    1 
ATOM   1618 C C     . GLU A 1 216 ? -25.468 6.809   -5.368  1.00 15.30 ?  222 GLU A C     1 
ATOM   1619 O O     . GLU A 1 216 ? -24.309 7.000   -5.745  1.00 11.82 ?  222 GLU A O     1 
ATOM   1620 C CB    . GLU A 1 216 ? -27.116 6.367   -7.210  1.00 20.39 ?  222 GLU A CB    1 
ATOM   1621 C CG    . GLU A 1 216 ? -27.372 5.408   -8.356  1.00 31.17 ?  222 GLU A CG    1 
ATOM   1622 C CD    . GLU A 1 216 ? -26.121 5.142   -9.175  1.00 36.85 ?  222 GLU A CD    1 
ATOM   1623 N N     . TYR A 1 217 ? -26.001 7.482   -4.355  1.00 14.07 ?  223 TYR A N     1 
ATOM   1624 C CA    . TYR A 1 217 ? -25.254 8.525   -3.663  1.00 13.48 ?  223 TYR A CA    1 
ATOM   1625 C C     . TYR A 1 217 ? -25.772 8.684   -2.244  1.00 16.61 ?  223 TYR A C     1 
ATOM   1626 O O     . TYR A 1 217 ? -26.965 8.924   -2.048  1.00 16.72 ?  223 TYR A O     1 
ATOM   1627 C CB    . TYR A 1 217 ? -25.363 9.863   -4.410  1.00 15.34 ?  223 TYR A CB    1 
ATOM   1628 C CG    . TYR A 1 217 ? -24.634 10.964  -3.698  1.00 15.51 ?  223 TYR A CG    1 
ATOM   1629 C CD1   . TYR A 1 217 ? -25.284 11.743  -2.753  1.00 17.26 ?  223 TYR A CD1   1 
ATOM   1630 C CD2   . TYR A 1 217 ? -23.300 11.220  -3.954  1.00 17.30 ?  223 TYR A CD2   1 
ATOM   1631 C CE1   . TYR A 1 217 ? -24.637 12.746  -2.094  1.00 17.73 ?  223 TYR A CE1   1 
ATOM   1632 C CE2   . TYR A 1 217 ? -22.639 12.241  -3.285  1.00 17.88 ?  223 TYR A CE2   1 
ATOM   1633 C CZ    . TYR A 1 217 ? -23.318 12.981  -2.347  1.00 19.83 ?  223 TYR A CZ    1 
ATOM   1634 O OH    . TYR A 1 217 ? -22.693 14.001  -1.665  1.00 25.23 ?  223 TYR A OH    1 
ATOM   1635 N N     . ILE A 1 218 ? -24.865 8.571   -1.268  1.00 13.70 ?  224 ILE A N     1 
ATOM   1636 C CA    . ILE A 1 218 ? -25.107 8.859   0.148   1.00 14.90 ?  224 ILE A CA    1 
ATOM   1637 C C     . ILE A 1 218 ? -23.983 9.775   0.624   1.00 15.15 ?  224 ILE A C     1 
ATOM   1638 O O     . ILE A 1 218 ? -22.813 9.536   0.307   1.00 13.96 ?  224 ILE A O     1 
ATOM   1639 C CB    . ILE A 1 218 ? -25.125 7.574   1.013   1.00 12.01 ?  224 ILE A CB    1 
ATOM   1640 C CG1   . ILE A 1 218 ? -26.151 6.571   0.482   1.00 14.97 ?  224 ILE A CG1   1 
ATOM   1641 C CG2   . ILE A 1 218 ? -25.411 7.905   2.498   1.00 13.18 ?  224 ILE A CG2   1 
ATOM   1642 C CD1   . ILE A 1 218 ? -26.075 5.177   1.170   1.00 12.76 ?  224 ILE A CD1   1 
ATOM   1643 N N     . LYS A 1 219 ? -24.322 10.823  1.379   1.00 13.66 ?  225 LYS A N     1 
ATOM   1644 C CA    . LYS A 1 219 ? -23.309 11.714  1.952   1.00 14.99 ?  225 LYS A CA    1 
ATOM   1645 C C     . LYS A 1 219 ? -23.217 11.444  3.447   1.00 17.23 ?  225 LYS A C     1 
ATOM   1646 O O     . LYS A 1 219 ? -24.189 11.654  4.183   1.00 18.38 ?  225 LYS A O     1 
ATOM   1647 C CB    . LYS A 1 219 ? -23.623 13.191  1.710   1.00 17.91 ?  225 LYS A CB    1 
ATOM   1648 C CG    . LYS A 1 219 ? -22.661 14.128  2.441   1.00 21.42 ?  225 LYS A CG    1 
ATOM   1649 C CD    . LYS A 1 219 ? -23.161 15.582  2.424   1.00 28.48 ?  225 LYS A CD    1 
ATOM   1650 N N     . VAL A 1 220 ? -22.059 10.961  3.888   1.00 15.87 ?  226 VAL A N     1 
ATOM   1651 C CA    . VAL A 1 220 ? -21.773 10.754  5.302   1.00 15.45 ?  226 VAL A CA    1 
ATOM   1652 C C     . VAL A 1 220 ? -21.062 11.998  5.819   1.00 17.97 ?  226 VAL A C     1 
ATOM   1653 O O     . VAL A 1 220 ? -20.128 12.484  5.176   1.00 18.85 ?  226 VAL A O     1 
ATOM   1654 C CB    . VAL A 1 220 ? -20.910 9.489   5.500   1.00 14.73 ?  226 VAL A CB    1 
ATOM   1655 C CG1   . VAL A 1 220 ? -20.492 9.352   6.937   1.00 13.65 ?  226 VAL A CG1   1 
ATOM   1656 C CG2   . VAL A 1 220 ? -21.695 8.239   5.057   1.00 11.62 ?  226 VAL A CG2   1 
ATOM   1657 N N     . GLN A 1 221 ? -21.493 12.517  6.975   1.00 20.05 ?  227 GLN A N     1 
ATOM   1658 C CA    . GLN A 1 221 ? -20.878 13.698  7.580   1.00 23.12 ?  227 GLN A CA    1 
ATOM   1659 C C     . GLN A 1 221 ? -20.314 13.366  8.952   1.00 18.49 ?  227 GLN A C     1 
ATOM   1660 O O     . GLN A 1 221 ? -20.865 12.533  9.671   1.00 19.48 ?  227 GLN A O     1 
ATOM   1661 C CB    . GLN A 1 221 ? -21.877 14.845  7.752   1.00 24.61 ?  227 GLN A CB    1 
ATOM   1662 C CG    . GLN A 1 221 ? -22.611 15.242  6.504   1.00 32.26 ?  227 GLN A CG    1 
ATOM   1663 C CD    . GLN A 1 221 ? -23.460 16.485  6.709   1.00 41.92 ?  227 GLN A CD    1 
ATOM   1664 O OE1   . GLN A 1 221 ? -24.240 16.572  7.663   1.00 41.47 ?  227 GLN A OE1   1 
ATOM   1665 N NE2   . GLN A 1 221 ? -23.304 17.460  5.817   1.00 57.10 ?  227 GLN A NE2   1 
ATOM   1666 N N     . THR A 1 222 ? -19.216 14.035  9.318   1.00 21.85 ?  228 THR A N     1 
ATOM   1667 C CA    . THR A 1 222 ? -18.628 13.885  10.644  1.00 20.11 ?  228 THR A CA    1 
ATOM   1668 C C     . THR A 1 222 ? -18.707 15.184  11.441  1.00 23.98 ?  228 THR A C     1 
ATOM   1669 O O     . THR A 1 222 ? -18.887 16.276  10.892  1.00 23.67 ?  228 THR A O     1 
ATOM   1670 C CB    . THR A 1 222 ? -17.164 13.426  10.576  1.00 24.58 ?  228 THR A CB    1 
ATOM   1671 O OG1   . THR A 1 222 ? -16.318 14.523  10.208  1.00 27.12 ?  228 THR A OG1   1 
ATOM   1672 C CG2   . THR A 1 222 ? -17.000 12.274  9.571   1.00 21.50 ?  228 THR A CG2   1 
ATOM   1673 N N     . ASP A 1 223 ? -18.548 15.047  12.762  1.00 23.66 ?  229 ASP A N     1 
ATOM   1674 C CA    . ASP A 1 223 ? -18.560 16.216  13.639  1.00 28.41 ?  229 ASP A CA    1 
ATOM   1675 C C     . ASP A 1 223 ? -17.444 17.209  13.317  1.00 30.19 ?  229 ASP A C     1 
ATOM   1676 O O     . ASP A 1 223 ? -17.585 18.400  13.623  1.00 30.17 ?  229 ASP A O     1 
ATOM   1677 C CB    . ASP A 1 223 ? -18.480 15.776  15.108  1.00 26.15 ?  229 ASP A CB    1 
ATOM   1678 C CG    . ASP A 1 223 ? -17.159 15.053  15.459  1.00 31.55 ?  229 ASP A CG    1 
ATOM   1679 O OD1   . ASP A 1 223 ? -16.512 14.458  14.561  1.00 26.92 ?  229 ASP A OD1   1 
ATOM   1680 O OD2   . ASP A 1 223 ? -16.779 15.067  16.656  1.00 35.34 -1 229 ASP A OD2   1 
ATOM   1681 N N     . LYS A 1 224 ? -16.350 16.763  12.702  1.00 27.10 ?  230 LYS A N     1 
ATOM   1682 C CA    . LYS A 1 224 ? -15.282 17.669  12.296  1.00 29.13 ?  230 LYS A CA    1 
ATOM   1683 C C     . LYS A 1 224 ? -15.509 18.267  10.903  1.00 33.41 ?  230 LYS A C     1 
ATOM   1684 O O     . LYS A 1 224 ? -14.603 18.910  10.362  1.00 31.43 ?  230 LYS A O     1 
ATOM   1685 C CB    . LYS A 1 224 ? -13.927 16.953  12.353  1.00 29.90 ?  230 LYS A CB    1 
ATOM   1686 N N     . GLY A 1 225 ? -16.691 18.076  10.316  1.00 25.59 ?  231 GLY A N     1 
ATOM   1687 C CA    . GLY A 1 225 ? -16.985 18.635  9.013   1.00 28.92 ?  231 GLY A CA    1 
ATOM   1688 C C     . GLY A 1 225 ? -16.454 17.860  7.823   1.00 27.98 ?  231 GLY A C     1 
ATOM   1689 O O     . GLY A 1 225 ? -16.589 18.330  6.690   1.00 23.99 ?  231 GLY A O     1 
ATOM   1690 N N     . THR A 1 226 ? -15.848 16.693  8.034   1.00 26.80 ?  232 THR A N     1 
ATOM   1691 C CA    . THR A 1 226 ? -15.462 15.850  6.910   1.00 24.34 ?  232 THR A CA    1 
ATOM   1692 C C     . THR A 1 226 ? -16.712 15.284  6.246   1.00 24.26 ?  232 THR A C     1 
ATOM   1693 O O     . THR A 1 226 ? -17.684 14.935  6.920   1.00 24.07 ?  232 THR A O     1 
ATOM   1694 C CB    . THR A 1 226 ? -14.552 14.707  7.381   1.00 25.76 ?  232 THR A CB    1 
ATOM   1695 O OG1   . THR A 1 226 ? -13.494 15.241  8.181   1.00 29.48 ?  232 THR A OG1   1 
ATOM   1696 C CG2   . THR A 1 226 ? -13.941 13.987  6.198   1.00 24.63 ?  232 THR A CG2   1 
ATOM   1697 N N     . GLU A 1 227 ? -16.689 15.197  4.916   1.00 22.42 ?  233 GLU A N     1 
ATOM   1698 C CA    . GLU A 1 227 ? -17.802 14.658  4.147   1.00 21.95 ?  233 GLU A CA    1 
ATOM   1699 C C     . GLU A 1 227 ? -17.279 13.536  3.265   1.00 21.04 ?  233 GLU A C     1 
ATOM   1700 O O     . GLU A 1 227 ? -16.287 13.719  2.559   1.00 19.04 ?  233 GLU A O     1 
ATOM   1701 C CB    . GLU A 1 227 ? -18.476 15.750  3.295   1.00 24.99 ?  233 GLU A CB    1 
ATOM   1702 C CG    . GLU A 1 227 ? -19.361 16.704  4.103   1.00 30.95 ?  233 GLU A CG    1 
ATOM   1703 C CD    . GLU A 1 227 ? -19.920 17.867  3.273   1.00 41.40 ?  233 GLU A CD    1 
ATOM   1704 O OE1   . GLU A 1 227 ? -19.181 18.425  2.435   1.00 38.68 ?  233 GLU A OE1   1 
ATOM   1705 O OE2   . GLU A 1 227 ? -21.103 18.220  3.461   1.00 47.27 -1 233 GLU A OE2   1 
ATOM   1706 N N     . VAL A 1 228 ? -17.939 12.379  3.316   1.00 19.31 ?  234 VAL A N     1 
ATOM   1707 C CA    . VAL A 1 228 ? -17.556 11.219  2.520   1.00 16.64 ?  234 VAL A CA    1 
ATOM   1708 C C     . VAL A 1 228 ? -18.768 10.791  1.705   1.00 16.97 ?  234 VAL A C     1 
ATOM   1709 O O     . VAL A 1 228 ? -19.822 10.489  2.277   1.00 16.95 ?  234 VAL A O     1 
ATOM   1710 C CB    . VAL A 1 228 ? -17.074 10.050  3.400   1.00 18.15 ?  234 VAL A CB    1 
ATOM   1711 C CG1   . VAL A 1 228 ? -16.621 8.884   2.533   1.00 17.56 ?  234 VAL A CG1   1 
ATOM   1712 C CG2   . VAL A 1 228 ? -15.951 10.487  4.317   1.00 21.36 ?  234 VAL A CG2   1 
ATOM   1713 N N     . ALA A 1 229 ? -18.620 10.749  0.386   1.00 13.18 ?  235 ALA A N     1 
ATOM   1714 C CA    . ALA A 1 229 ? -19.668 10.203  -0.476  1.00 14.87 ?  235 ALA A CA    1 
ATOM   1715 C C     . ALA A 1 229 ? -19.498 8.691   -0.617  1.00 14.63 ?  235 ALA A C     1 
ATOM   1716 O O     . ALA A 1 229 ? -18.374 8.191   -0.728  1.00 15.58 ?  235 ALA A O     1 
ATOM   1717 C CB    . ALA A 1 229 ? -19.626 10.867  -1.853  1.00 15.19 ?  235 ALA A CB    1 
ATOM   1718 N N     . THR A 1 230 ? -20.613 7.953   -0.606  1.00 11.03 ?  236 THR A N     1 
ATOM   1719 C CA    . THR A 1 230 ? -20.510 6.500   -0.606  1.00 12.13 ?  236 THR A CA    1 
ATOM   1720 C C     . THR A 1 230 ? -21.755 5.907   -1.259  1.00 12.51 ?  236 THR A C     1 
ATOM   1721 O O     . THR A 1 230 ? -22.736 6.606   -1.538  1.00 13.36 ?  236 THR A O     1 
ATOM   1722 C CB    . THR A 1 230 ? -20.293 5.978   0.837   1.00 12.27 ?  236 THR A CB    1 
ATOM   1723 O OG1   . THR A 1 230 ? -19.972 4.572   0.835   1.00 13.27 ?  236 THR A OG1   1 
ATOM   1724 C CG2   . THR A 1 230 ? -21.527 6.227   1.683   1.00 11.00 ?  236 THR A CG2   1 
ATOM   1725 N N     . ASN A 1 231 ? -21.700 4.598   -1.529  1.00 10.79 ?  237 ASN A N     1 
ATOM   1726 C CA    . ASN A 1 231 ? -22.890 3.871   -1.965  1.00 10.42 ?  237 ASN A CA    1 
ATOM   1727 C C     . ASN A 1 231 ? -23.558 3.098   -0.839  1.00 11.38 ?  237 ASN A C     1 
ATOM   1728 O O     . ASN A 1 231 ? -24.710 2.683   -0.996  1.00 11.95 ?  237 ASN A O     1 
ATOM   1729 C CB    . ASN A 1 231 ? -22.553 2.877   -3.091  1.00 12.86 ?  237 ASN A CB    1 
ATOM   1730 C CG    . ASN A 1 231 ? -21.980 3.551   -4.322  1.00 13.20 ?  237 ASN A CG    1 
ATOM   1731 O OD1   . ASN A 1 231 ? -20.874 3.234   -4.740  1.00 12.08 ?  237 ASN A OD1   1 
ATOM   1732 N ND2   . ASN A 1 231 ? -22.739 4.481   -4.925  1.00 13.98 ?  237 ASN A ND2   1 
ATOM   1733 N N     . LEU A 1 232 ? -22.869 2.867   0.276   1.00 10.46 ?  238 LEU A N     1 
ATOM   1734 C CA    . LEU A 1 232 ? -23.347 1.909   1.269   1.00 10.44 ?  238 LEU A CA    1 
ATOM   1735 C C     . LEU A 1 232 ? -22.810 2.307   2.632   1.00 10.68 ?  238 LEU A C     1 
ATOM   1736 O O     . LEU A 1 232 ? -21.627 2.614   2.751   1.00 10.83 ?  238 LEU A O     1 
ATOM   1737 C CB    . LEU A 1 232 ? -22.875 0.496   0.918   1.00 10.36 ?  238 LEU A CB    1 
ATOM   1738 C CG    . LEU A 1 232 ? -23.329 -0.614  1.869   1.00 10.70 ?  238 LEU A CG    1 
ATOM   1739 C CD1   . LEU A 1 232 ? -24.840 -0.838  1.809   1.00 12.22 ?  238 LEU A CD1   1 
ATOM   1740 C CD2   . LEU A 1 232 ? -22.613 -1.884  1.515   1.00 11.47 ?  238 LEU A CD2   1 
ATOM   1741 N N     . VAL A 1 233 ? -23.658 2.274   3.658   1.00 10.72 ?  239 VAL A N     1 
ATOM   1742 C CA    . VAL A 1 233 ? -23.244 2.562   5.028   1.00 10.95 ?  239 VAL A CA    1 
ATOM   1743 C C     . VAL A 1 233 ? -23.560 1.350   5.898   1.00 11.00 ?  239 VAL A C     1 
ATOM   1744 O O     . VAL A 1 233 ? -24.710 0.883   5.928   1.00 11.42 ?  239 VAL A O     1 
ATOM   1745 C CB    . VAL A 1 233 ? -23.950 3.809   5.594   1.00 11.65 ?  239 VAL A CB    1 
ATOM   1746 C CG1   . VAL A 1 233 ? -23.461 4.072   7.021   1.00 12.12 ?  239 VAL A CG1   1 
ATOM   1747 C CG2   . VAL A 1 233 ? -23.711 5.007   4.726   1.00 12.96 ?  239 VAL A CG2   1 
ATOM   1748 N N     . ILE A 1 234 ? -22.552 0.869   6.632   1.00 11.12 ?  240 ILE A N     1 
ATOM   1749 C CA    . ILE A 1 234 ? -22.679 -0.244  7.572   1.00 11.18 ?  240 ILE A CA    1 
ATOM   1750 C C     . ILE A 1 234 ? -22.272 0.221   8.963   1.00 11.45 ?  240 ILE A C     1 
ATOM   1751 O O     . ILE A 1 234 ? -21.179 0.764   9.142   1.00 12.07 ?  240 ILE A O     1 
ATOM   1752 C CB    . ILE A 1 234 ? -21.797 -1.429  7.156   1.00 11.14 ?  240 ILE A CB    1 
ATOM   1753 C CG1   . ILE A 1 234 ? -22.099 -1.831  5.711   1.00 10.89 ?  240 ILE A CG1   1 
ATOM   1754 C CG2   . ILE A 1 234 ? -21.979 -2.597  8.133   1.00 11.21 ?  240 ILE A CG2   1 
ATOM   1755 C CD1   . ILE A 1 234 ? -21.058 -2.841  5.149   1.00 10.86 ?  240 ILE A CD1   1 
ATOM   1756 N N     . LEU A 1 235 ? -23.129 -0.026  9.944   1.00 11.90 ?  241 LEU A N     1 
ATOM   1757 C CA    . LEU A 1 235 ? -22.898 0.399   11.318  1.00 11.78 ?  241 LEU A CA    1 
ATOM   1758 C C     . LEU A 1 235 ? -22.296 -0.744  12.120  1.00 12.95 ?  241 LEU A C     1 
ATOM   1759 O O     . LEU A 1 235 ? -22.912 -1.813  12.244  1.00 14.32 ?  241 LEU A O     1 
ATOM   1760 C CB    . LEU A 1 235 ? -24.202 0.845   11.975  1.00 15.74 ?  241 LEU A CB    1 
ATOM   1761 C CG    . LEU A 1 235 ? -24.959 1.994   11.332  1.00 16.36 ?  241 LEU A CG    1 
ATOM   1762 C CD1   . LEU A 1 235 ? -25.990 2.461   12.361  1.00 20.96 ?  241 LEU A CD1   1 
ATOM   1763 C CD2   . LEU A 1 235 ? -24.027 3.122   10.955  1.00 14.67 ?  241 LEU A CD2   1 
ATOM   1764 N N     . CYS A 1 236 ? -21.102 -0.514  12.669  1.00 12.43 ?  242 CYS A N     1 
ATOM   1765 C CA    . CYS A 1 236 ? -20.528 -1.371  13.694  1.00 12.29 ?  242 CYS A CA    1 
ATOM   1766 C C     . CYS A 1 236 ? -20.269 -0.540  14.946  1.00 13.22 ?  242 CYS A C     1 
ATOM   1767 O O     . CYS A 1 236 ? -19.146 -0.504  15.456  1.00 12.74 ?  242 CYS A O     1 
ATOM   1768 C CB    . CYS A 1 236 ? -19.236 -2.015  13.194  1.00 12.28 ?  242 CYS A CB    1 
ATOM   1769 S SG    . CYS A 1 236 ? -19.511 -3.040  11.698  1.00 18.00 ?  242 CYS A SG    1 
ATOM   1770 N N     . THR A 1 237 ? -21.317 0.115   15.449  1.00 12.60 ?  243 THR A N     1 
ATOM   1771 C CA    . THR A 1 237 ? -21.183 1.186   16.429  1.00 13.54 ?  243 THR A CA    1 
ATOM   1772 C C     . THR A 1 237 ? -21.313 0.706   17.864  1.00 15.51 ?  243 THR A C     1 
ATOM   1773 O O     . THR A 1 237 ? -21.237 1.533   18.777  1.00 15.09 ?  243 THR A O     1 
ATOM   1774 C CB    . THR A 1 237 ? -22.219 2.279   16.148  1.00 14.03 ?  243 THR A CB    1 
ATOM   1775 O OG1   . THR A 1 237 ? -23.480 1.664   15.843  1.00 15.44 ?  243 THR A OG1   1 
ATOM   1776 C CG2   . THR A 1 237 ? -21.783 3.125   14.949  1.00 14.65 ?  243 THR A CG2   1 
ATOM   1777 N N     . GLY A 1 238 ? -21.467 -0.586  18.103  1.00 13.05 ?  244 GLY A N     1 
ATOM   1778 C CA    . GLY A 1 238 ? -21.439 -1.119  19.451  1.00 14.79 ?  244 GLY A CA    1 
ATOM   1779 C C     . GLY A 1 238 ? -22.689 -1.903  19.793  1.00 14.93 ?  244 GLY A C     1 
ATOM   1780 O O     . GLY A 1 238 ? -23.697 -1.887  19.081  1.00 15.07 ?  244 GLY A O     1 
ATOM   1781 N N     . ILE A 1 239 ? -22.618 -2.591  20.929  1.00 15.80 ?  245 ILE A N     1 
ATOM   1782 C CA    . ILE A 1 239 ? -23.695 -3.457  21.369  1.00 17.13 ?  245 ILE A CA    1 
ATOM   1783 C C     . ILE A 1 239 ? -24.090 -3.090  22.794  1.00 20.85 ?  245 ILE A C     1 
ATOM   1784 O O     . ILE A 1 239 ? -23.391 -2.349  23.487  1.00 19.72 ?  245 ILE A O     1 
ATOM   1785 C CB    . ILE A 1 239 ? -23.307 -4.951  21.272  1.00 18.50 ?  245 ILE A CB    1 
ATOM   1786 C CG1   . ILE A 1 239 ? -22.153 -5.299  22.213  1.00 20.84 ?  245 ILE A CG1   1 
ATOM   1787 C CG2   . ILE A 1 239 ? -22.927 -5.308  19.835  1.00 17.72 ?  245 ILE A CG2   1 
ATOM   1788 C CD1   . ILE A 1 239 ? -21.807 -6.804  22.192  1.00 25.22 ?  245 ILE A CD1   1 
ATOM   1789 N N     . LYS A 1 240 ? -25.252 -3.595  23.201  1.00 17.75 ?  246 LYS A N     1 
ATOM   1790 C CA    . LYS A 1 240 ? -25.809 -3.427  24.536  1.00 21.43 ?  246 LYS A CA    1 
ATOM   1791 C C     . LYS A 1 240 ? -26.209 -4.799  25.051  1.00 23.64 ?  246 LYS A C     1 
ATOM   1792 O O     . LYS A 1 240 ? -26.766 -5.608  24.305  1.00 19.57 ?  246 LYS A O     1 
ATOM   1793 C CB    . LYS A 1 240 ? -27.047 -2.516  24.536  1.00 23.93 ?  246 LYS A CB    1 
ATOM   1794 C CG    . LYS A 1 240 ? -26.769 -1.058  24.178  1.00 35.40 ?  246 LYS A CG    1 
ATOM   1795 C CD    . LYS A 1 240 ? -28.056 -0.271  23.974  1.00 50.42 ?  246 LYS A CD    1 
ATOM   1796 N N     . ILE A 1 241 ? -25.934 -5.067  26.330  1.00 24.45 ?  247 ILE A N     1 
ATOM   1797 C CA    . ILE A 1 241 ? -26.395 -6.325  26.903  1.00 23.85 ?  247 ILE A CA    1 
ATOM   1798 C C     . ILE A 1 241 ? -27.910 -6.379  26.783  1.00 22.98 ?  247 ILE A C     1 
ATOM   1799 O O     . ILE A 1 241 ? -28.604 -5.377  26.992  1.00 23.05 ?  247 ILE A O     1 
ATOM   1800 C CB    . ILE A 1 241 ? -25.924 -6.465  28.358  1.00 26.54 ?  247 ILE A CB    1 
ATOM   1801 C CG1   . ILE A 1 241 ? -24.436 -6.804  28.382  1.00 29.38 ?  247 ILE A CG1   1 
ATOM   1802 C CG2   . ILE A 1 241 ? -26.701 -7.549  29.066  1.00 25.67 ?  247 ILE A CG2   1 
ATOM   1803 C CD1   . ILE A 1 241 ? -23.819 -6.742  29.756  1.00 37.43 ?  247 ILE A CD1   1 
ATOM   1804 N N     . ASN A 1 242 ? -28.434 -7.536  26.382  1.00 23.23 ?  248 ASN A N     1 
ATOM   1805 C CA    . ASN A 1 242 ? -29.870 -7.672  26.158  1.00 23.59 ?  248 ASN A CA    1 
ATOM   1806 C C     . ASN A 1 242 ? -30.519 -8.056  27.484  1.00 28.38 ?  248 ASN A C     1 
ATOM   1807 O O     . ASN A 1 242 ? -30.561 -9.235  27.856  1.00 24.05 ?  248 ASN A O     1 
ATOM   1808 C CB    . ASN A 1 242 ? -30.158 -8.700  25.073  1.00 26.09 ?  248 ASN A CB    1 
ATOM   1809 C CG    . ASN A 1 242 ? -31.599 -8.697  24.649  1.00 26.11 ?  248 ASN A CG    1 
ATOM   1810 O OD1   . ASN A 1 242 ? -32.456 -8.142  25.336  1.00 30.88 ?  248 ASN A OD1   1 
ATOM   1811 N ND2   . ASN A 1 242 ? -31.879 -9.306  23.506  1.00 28.52 ?  248 ASN A ND2   1 
ATOM   1812 N N     . SER A 1 243 ? -31.033 -7.059  28.202  1.00 27.81 ?  249 SER A N     1 
ATOM   1813 C CA    . SER A 1 243 ? -31.620 -7.275  29.519  1.00 31.21 ?  249 SER A CA    1 
ATOM   1814 C C     . SER A 1 243 ? -33.142 -7.300  29.495  1.00 32.42 ?  249 SER A C     1 
ATOM   1815 O O     . SER A 1 243 ? -33.760 -7.253  30.562  1.00 36.52 ?  249 SER A O     1 
ATOM   1816 C CB    . SER A 1 243 ? -31.146 -6.195  30.490  1.00 35.07 ?  249 SER A CB    1 
ATOM   1817 O OG    . SER A 1 243 ? -31.716 -4.937  30.152  1.00 36.01 ?  249 SER A OG    1 
ATOM   1818 N N     . SER A 1 244 ? -33.761 -7.398  28.314  1.00 30.85 ?  250 SER A N     1 
ATOM   1819 C CA    . SER A 1 244 ? -35.210 -7.236  28.229  1.00 34.13 ?  250 SER A CA    1 
ATOM   1820 C C     . SER A 1 244 ? -35.932 -8.268  29.082  1.00 35.19 ?  250 SER A C     1 
ATOM   1821 O O     . SER A 1 244 ? -36.860 -7.932  29.826  1.00 40.80 ?  250 SER A O     1 
ATOM   1822 C CB    . SER A 1 244 ? -35.679 -7.311  26.773  1.00 30.68 ?  250 SER A CB    1 
ATOM   1823 O OG    . SER A 1 244 ? -35.292 -8.506  26.130  1.00 33.28 ?  250 SER A OG    1 
ATOM   1824 N N     . ALA A 1 245 ? -35.489 -9.525  29.019  1.00 35.46 ?  251 ALA A N     1 
ATOM   1825 C CA    . ALA A 1 245 ? -36.211 -10.606 29.688  1.00 35.66 ?  251 ALA A CA    1 
ATOM   1826 C C     . ALA A 1 245 ? -36.192 -10.478 31.207  1.00 35.10 ?  251 ALA A C     1 
ATOM   1827 O O     . ALA A 1 245 ? -37.092 -10.986 31.878  1.00 35.00 ?  251 ALA A O     1 
ATOM   1828 C CB    . ALA A 1 245 ? -35.623 -11.955 29.268  1.00 32.95 ?  251 ALA A CB    1 
ATOM   1829 N N     . TYR A 1 246 ? -35.192 -9.818  31.775  1.00 37.47 ?  252 TYR A N     1 
ATOM   1830 C CA    . TYR A 1 246 ? -34.986 -9.909  33.209  1.00 40.33 ?  252 TYR A CA    1 
ATOM   1831 C C     . TYR A 1 246 ? -34.780 -8.577  33.922  1.00 40.65 ?  252 TYR A C     1 
ATOM   1832 O O     . TYR A 1 246 ? -34.557 -8.588  35.140  1.00 37.32 ?  252 TYR A O     1 
ATOM   1833 C CB    . TYR A 1 246 ? -33.783 -10.822 33.501  1.00 37.03 ?  252 TYR A CB    1 
ATOM   1834 C CG    . TYR A 1 246 ? -32.466 -10.312 32.943  1.00 37.03 ?  252 TYR A CG    1 
ATOM   1835 C CD1   . TYR A 1 246 ? -31.750 -9.322  33.606  1.00 36.39 ?  252 TYR A CD1   1 
ATOM   1836 C CD2   . TYR A 1 246 ? -31.933 -10.824 31.759  1.00 33.66 ?  252 TYR A CD2   1 
ATOM   1837 C CE1   . TYR A 1 246 ? -30.561 -8.852  33.115  1.00 35.48 ?  252 TYR A CE1   1 
ATOM   1838 C CE2   . TYR A 1 246 ? -30.734 -10.351 31.258  1.00 32.90 ?  252 TYR A CE2   1 
ATOM   1839 C CZ    . TYR A 1 246 ? -30.053 -9.363  31.946  1.00 34.52 ?  252 TYR A CZ    1 
ATOM   1840 O OH    . TYR A 1 246 ? -28.857 -8.871  31.490  1.00 33.10 ?  252 TYR A OH    1 
ATOM   1841 N N     . ARG A 1 247 ? -34.837 -7.436  33.220  1.00 40.17 ?  253 ARG A N     1 
ATOM   1842 C CA    . ARG A 1 247 ? -34.391 -6.187  33.840  1.00 38.40 ?  253 ARG A CA    1 
ATOM   1843 C C     . ARG A 1 247 ? -35.287 -5.802  35.015  1.00 40.24 ?  253 ARG A C     1 
ATOM   1844 O O     . ARG A 1 247 ? -34.787 -5.477  36.096  1.00 41.31 ?  253 ARG A O     1 
ATOM   1845 C CB    . ARG A 1 247 ? -34.306 -5.051  32.809  1.00 39.53 ?  253 ARG A CB    1 
ATOM   1846 C CG    . ARG A 1 247 ? -35.613 -4.606  32.165  1.00 38.91 ?  253 ARG A CG    1 
ATOM   1847 N N     . LYS A 1 248 ? -36.610 -5.854  34.835  1.00 35.55 ?  254 LYS A N     1 
ATOM   1848 C CA    . LYS A 1 248 ? -37.517 -5.496  35.922  1.00 44.19 ?  254 LYS A CA    1 
ATOM   1849 C C     . LYS A 1 248 ? -37.309 -6.416  37.120  1.00 45.93 ?  254 LYS A C     1 
ATOM   1850 O O     . LYS A 1 248 ? -36.983 -5.962  38.223  1.00 43.57 ?  254 LYS A O     1 
ATOM   1851 C CB    . LYS A 1 248 ? -38.973 -5.552  35.443  1.00 42.89 ?  254 LYS A CB    1 
ATOM   1852 N N     . ALA A 1 249 ? -37.440 -7.726  36.899  1.00 42.46 ?  255 ALA A N     1 
ATOM   1853 C CA    . ALA A 1 249 ? -37.423 -8.682  37.998  1.00 42.85 ?  255 ALA A CA    1 
ATOM   1854 C C     . ALA A 1 249 ? -36.142 -8.579  38.818  1.00 46.99 ?  255 ALA A C     1 
ATOM   1855 O O     . ALA A 1 249 ? -36.171 -8.715  40.048  1.00 50.65 ?  255 ALA A O     1 
ATOM   1856 C CB    . ALA A 1 249 ? -37.605 -10.096 37.448  1.00 43.07 ?  255 ALA A CB    1 
ATOM   1857 N N     . PHE A 1 250 ? -35.011 -8.318  38.166  1.00 45.05 ?  256 PHE A N     1 
ATOM   1858 C CA    . PHE A 1 250 ? -33.713 -8.354  38.830  1.00 47.44 ?  256 PHE A CA    1 
ATOM   1859 C C     . PHE A 1 250 ? -33.057 -6.979  38.900  1.00 47.63 ?  256 PHE A C     1 
ATOM   1860 O O     . PHE A 1 250 ? -31.828 -6.886  38.975  1.00 49.94 ?  256 PHE A O     1 
ATOM   1861 C CB    . PHE A 1 250 ? -32.781 -9.341  38.129  1.00 47.09 ?  256 PHE A CB    1 
ATOM   1862 C CG    . PHE A 1 250 ? -33.290 -10.756 38.107  1.00 45.68 ?  256 PHE A CG    1 
ATOM   1863 C CD1   . PHE A 1 250 ? -34.238 -11.150 37.180  1.00 41.96 ?  256 PHE A CD1   1 
ATOM   1864 C CD2   . PHE A 1 250 ? -32.812 -11.694 39.011  1.00 46.34 ?  256 PHE A CD2   1 
ATOM   1865 C CE1   . PHE A 1 250 ? -34.707 -12.449 37.157  1.00 44.04 ?  256 PHE A CE1   1 
ATOM   1866 C CE2   . PHE A 1 250 ? -33.276 -13.000 38.984  1.00 42.03 ?  256 PHE A CE2   1 
ATOM   1867 C CZ    . PHE A 1 250 ? -34.225 -13.371 38.055  1.00 38.23 ?  256 PHE A CZ    1 
ATOM   1868 N N     . GLU A 1 251 ? -33.864 -5.911  38.889  1.00 48.30 ?  257 GLU A N     1 
ATOM   1869 C CA    . GLU A 1 251 ? -33.318 -4.553  38.840  1.00 49.29 ?  257 GLU A CA    1 
ATOM   1870 C C     . GLU A 1 251 ? -32.281 -4.313  39.934  1.00 55.82 ?  257 GLU A C     1 
ATOM   1871 O O     . GLU A 1 251 ? -31.228 -3.719  39.675  1.00 54.22 ?  257 GLU A O     1 
ATOM   1872 C CB    . GLU A 1 251 ? -34.449 -3.528  38.932  1.00 46.97 ?  257 GLU A CB    1 
ATOM   1873 C CG    . GLU A 1 251 ? -35.451 -3.792  40.043  1.00 55.17 ?  257 GLU A CG    1 
ATOM   1874 N N     . SER A 1 252 ? -32.536 -4.801  41.152  1.00 52.80 ?  258 SER A N     1 
ATOM   1875 C CA    . SER A 1 252 ? -31.586 -4.597  42.241  1.00 54.74 ?  258 SER A CA    1 
ATOM   1876 C C     . SER A 1 252 ? -30.273 -5.344  42.040  1.00 58.21 ?  258 SER A C     1 
ATOM   1877 O O     . SER A 1 252 ? -29.288 -5.025  42.713  1.00 53.19 ?  258 SER A O     1 
ATOM   1878 C CB    . SER A 1 252 ? -32.211 -5.024  43.568  1.00 57.40 ?  258 SER A CB    1 
ATOM   1879 O OG    . SER A 1 252 ? -31.881 -6.367  43.877  1.00 56.82 ?  258 SER A OG    1 
ATOM   1880 N N     . ARG A 1 253 ? -30.223 -6.312  41.128  1.00 58.01 ?  259 ARG A N     1 
ATOM   1881 C CA    . ARG A 1 253 ? -29.063 -7.180  40.974  1.00 60.51 ?  259 ARG A CA    1 
ATOM   1882 C C     . ARG A 1 253 ? -28.210 -6.843  39.760  1.00 55.42 ?  259 ARG A C     1 
ATOM   1883 O O     . ARG A 1 253 ? -27.176 -7.492  39.542  1.00 48.46 ?  259 ARG A O     1 
ATOM   1884 C CB    . ARG A 1 253 ? -29.523 -8.636  40.889  1.00 58.65 ?  259 ARG A CB    1 
ATOM   1885 C CG    . ARG A 1 253 ? -30.424 -9.026  42.036  1.00 55.56 ?  259 ARG A CG    1 
ATOM   1886 C CD    . ARG A 1 253 ? -29.699 -8.866  43.360  1.00 55.45 ?  259 ARG A CD    1 
ATOM   1887 N NE    . ARG A 1 253 ? -30.501 -9.382  44.458  1.00 55.36 ?  259 ARG A NE    1 
ATOM   1888 C CZ    . ARG A 1 253 ? -30.071 -9.512  45.705  1.00 54.81 ?  259 ARG A CZ    1 
ATOM   1889 N NH1   . ARG A 1 253 ? -28.842 -9.165  46.054  1.00 53.73 ?  259 ARG A NH1   1 
ATOM   1890 N NH2   . ARG A 1 253 ? -30.895 -10.006 46.624  1.00 50.92 ?  259 ARG A NH2   1 
ATOM   1891 N N     . LEU A 1 254 ? -28.603 -5.833  38.989  1.00 56.65 ?  260 LEU A N     1 
ATOM   1892 C CA    . LEU A 1 254 ? -27.966 -5.517  37.720  1.00 53.48 ?  260 LEU A CA    1 
ATOM   1893 C C     . LEU A 1 254 ? -26.735 -4.647  37.918  1.00 54.41 ?  260 LEU A C     1 
ATOM   1894 O O     . LEU A 1 254 ? -26.760 -3.672  38.673  1.00 55.19 ?  260 LEU A O     1 
ATOM   1895 C CB    . LEU A 1 254 ? -28.959 -4.800  36.814  1.00 46.02 ?  260 LEU A CB    1 
ATOM   1896 C CG    . LEU A 1 254 ? -30.254 -5.541  36.514  1.00 47.01 ?  260 LEU A CG    1 
ATOM   1897 C CD1   . LEU A 1 254 ? -31.200 -4.685  35.697  1.00 46.90 ?  260 LEU A CD1   1 
ATOM   1898 C CD2   . LEU A 1 254 ? -29.939 -6.830  35.795  1.00 48.35 ?  260 LEU A CD2   1 
ATOM   1899 N N     . ALA A 1 255 ? -25.649 -5.011  37.242  1.00 50.81 ?  261 ALA A N     1 
ATOM   1900 C CA    . ALA A 1 255 ? -24.503 -4.123  37.166  1.00 53.49 ?  261 ALA A CA    1 
ATOM   1901 C C     . ALA A 1 255 ? -24.880 -2.890  36.357  1.00 53.96 ?  261 ALA A C     1 
ATOM   1902 O O     . ALA A 1 255 ? -25.989 -2.785  35.823  1.00 49.77 ?  261 ALA A O     1 
ATOM   1903 C CB    . ALA A 1 255 ? -23.306 -4.841  36.547  1.00 49.86 ?  261 ALA A CB    1 
ATOM   1904 N N     . SER A 1 256 ? -23.956 -1.931  36.274  1.00 56.60 ?  262 SER A N     1 
ATOM   1905 C CA    . SER A 1 256 ? -24.195 -0.803  35.380  1.00 52.01 ?  262 SER A CA    1 
ATOM   1906 C C     . SER A 1 256 ? -24.356 -1.297  33.942  1.00 52.47 ?  262 SER A C     1 
ATOM   1907 O O     . SER A 1 256 ? -25.344 -0.973  33.272  1.00 49.96 ?  262 SER A O     1 
ATOM   1908 C CB    . SER A 1 256 ? -23.079 0.245   35.510  1.00 54.09 ?  262 SER A CB    1 
ATOM   1909 O OG    . SER A 1 256 ? -21.856 -0.192  34.946  1.00 53.63 ?  262 SER A OG    1 
ATOM   1910 N N     . SER A 1 257 ? -23.452 -2.177  33.493  1.00 47.08 ?  263 SER A N     1 
ATOM   1911 C CA    . SER A 1 257 ? -23.473 -2.677  32.120  1.00 46.93 ?  263 SER A CA    1 
ATOM   1912 C C     . SER A 1 257 ? -24.785 -3.349  31.724  1.00 40.55 ?  263 SER A C     1 
ATOM   1913 O O     . SER A 1 257 ? -24.969 -3.635  30.536  1.00 42.16 ?  263 SER A O     1 
ATOM   1914 C CB    . SER A 1 257 ? -22.314 -3.658  31.897  1.00 47.38 ?  263 SER A CB    1 
ATOM   1915 O OG    . SER A 1 257 ? -22.587 -4.952  32.422  1.00 38.62 ?  263 SER A OG    1 
ATOM   1916 N N     . GLY A 1 258 ? -25.697 -3.595  32.661  1.00 43.40 ?  264 GLY A N     1 
ATOM   1917 C CA    . GLY A 1 258 ? -26.922 -4.325  32.388  1.00 40.48 ?  264 GLY A CA    1 
ATOM   1918 C C     . GLY A 1 258 ? -26.814 -5.818  32.619  1.00 37.66 ?  264 GLY A C     1 
ATOM   1919 O O     . GLY A 1 258 ? -27.827 -6.527  32.550  1.00 28.74 ?  264 GLY A O     1 
ATOM   1920 N N     . ALA A 1 259 ? -25.610 -6.310  32.876  1.00 37.21 ?  265 ALA A N     1 
ATOM   1921 C CA    . ALA A 1 259 ? -25.390 -7.683  33.274  1.00 37.52 ?  265 ALA A CA    1 
ATOM   1922 C C     . ALA A 1 259 ? -25.954 -7.923  34.683  1.00 39.61 ?  265 ALA A C     1 
ATOM   1923 O O     . ALA A 1 259 ? -26.380 -6.999  35.382  1.00 38.26 ?  265 ALA A O     1 
ATOM   1924 C CB    . ALA A 1 259 ? -23.898 -7.996  33.201  1.00 37.27 ?  265 ALA A CB    1 
ATOM   1925 N N     . LEU A 1 260 ? -25.989 -9.191  35.081  1.00 40.94 ?  266 LEU A N     1 
ATOM   1926 C CA    . LEU A 1 260 ? -26.419 -9.605  36.413  1.00 32.76 ?  266 LEU A CA    1 
ATOM   1927 C C     . LEU A 1 260 ? -25.179 -9.918  37.244  1.00 38.17 ?  266 LEU A C     1 
ATOM   1928 O O     . LEU A 1 260 ? -24.260 -10.588 36.761  1.00 32.69 ?  266 LEU A O     1 
ATOM   1929 C CB    . LEU A 1 260 ? -27.319 -10.835 36.309  1.00 35.28 ?  266 LEU A CB    1 
ATOM   1930 C CG    . LEU A 1 260 ? -28.563 -10.677 35.431  1.00 32.75 ?  266 LEU A CG    1 
ATOM   1931 C CD1   . LEU A 1 260 ? -28.716 -11.823 34.460  1.00 34.34 ?  266 LEU A CD1   1 
ATOM   1932 C CD2   . LEU A 1 260 ? -29.800 -10.567 36.281  1.00 38.28 ?  266 LEU A CD2   1 
ATOM   1933 N N     . ARG A 1 261 ? -25.137 -9.435  38.481  1.00 36.39 ?  267 ARG A N     1 
ATOM   1934 C CA    . ARG A 1 261 ? -24.011 -9.778  39.339  1.00 40.98 ?  267 ARG A CA    1 
ATOM   1935 C C     . ARG A 1 261 ? -24.094 -11.247 39.769  1.00 32.67 ?  267 ARG A C     1 
ATOM   1936 O O     . ARG A 1 261 ? -25.177 -11.800 39.956  1.00 33.62 ?  267 ARG A O     1 
ATOM   1937 C CB    . ARG A 1 261 ? -23.964 -8.839  40.544  1.00 41.32 ?  267 ARG A CB    1 
ATOM   1938 C CG    . ARG A 1 261 ? -23.654 -7.386  40.155  1.00 49.41 ?  267 ARG A CG    1 
ATOM   1939 C CD    . ARG A 1 261 ? -23.540 -6.461  41.365  1.00 57.47 ?  267 ARG A CD    1 
ATOM   1940 N NE    . ARG A 1 261 ? -24.813 -6.305  42.058  1.00 63.15 ?  267 ARG A NE    1 
ATOM   1941 C CZ    . ARG A 1 261 ? -25.724 -5.386  41.763  1.00 65.78 ?  267 ARG A CZ    1 
ATOM   1942 N NH1   . ARG A 1 261 ? -25.532 -4.510  40.791  1.00 72.81 ?  267 ARG A NH1   1 
ATOM   1943 N NH2   . ARG A 1 261 ? -26.855 -5.346  42.462  1.00 68.34 ?  267 ARG A NH2   1 
ATOM   1944 N N     . VAL A 1 262 ? -22.924 -11.883 39.894  1.00 33.64 ?  268 VAL A N     1 
ATOM   1945 C CA    . VAL A 1 262 ? -22.811 -13.326 40.101  1.00 34.32 ?  268 VAL A CA    1 
ATOM   1946 C C     . VAL A 1 262 ? -21.548 -13.618 40.913  1.00 35.91 ?  268 VAL A C     1 
ATOM   1947 O O     . VAL A 1 262 ? -20.626 -12.798 40.978  1.00 32.00 ?  268 VAL A O     1 
ATOM   1948 C CB    . VAL A 1 262 ? -22.757 -14.091 38.748  1.00 34.58 ?  268 VAL A CB    1 
ATOM   1949 C CG1   . VAL A 1 262 ? -24.070 -13.981 37.982  1.00 31.10 ?  268 VAL A CG1   1 
ATOM   1950 C CG2   . VAL A 1 262 ? -21.619 -13.549 37.891  1.00 35.49 ?  268 VAL A CG2   1 
ATOM   1951 N N     . ASN A 1 263 ? -21.487 -14.816 41.518  1.00 30.88 ?  269 ASN A N     1 
ATOM   1952 C CA    . ASN A 1 263 ? -20.278 -15.225 42.222  1.00 29.42 ?  269 ASN A CA    1 
ATOM   1953 C C     . ASN A 1 263 ? -19.422 -16.083 41.291  1.00 34.76 ?  269 ASN A C     1 
ATOM   1954 O O     . ASN A 1 263 ? -19.697 -16.207 40.089  1.00 32.60 ?  269 ASN A O     1 
ATOM   1955 C CB    . ASN A 1 263 ? -20.593 -15.974 43.523  1.00 33.50 ?  269 ASN A CB    1 
ATOM   1956 C CG    . ASN A 1 263 ? -21.268 -17.329 43.281  1.00 34.45 ?  269 ASN A CG    1 
ATOM   1957 O OD1   . ASN A 1 263 ? -21.241 -17.883 42.164  1.00 29.92 ?  269 ASN A OD1   1 
ATOM   1958 N ND2   . ASN A 1 263 ? -21.966 -17.814 44.306  1.00 30.66 ?  269 ASN A ND2   1 
ATOM   1959 N N     . GLU A 1 264 ? -18.377 -16.709 41.844  1.00 30.56 ?  270 GLU A N     1 
ATOM   1960 C CA    . GLU A 1 264 ? -17.498 -17.547 41.028  1.00 38.67 ?  270 GLU A CA    1 
ATOM   1961 C C     . GLU A 1 264 ? -18.167 -18.843 40.561  1.00 36.29 ?  270 GLU A C     1 
ATOM   1962 O O     . GLU A 1 264 ? -17.597 -19.543 39.710  1.00 33.99 ?  270 GLU A O     1 
ATOM   1963 C CB    . GLU A 1 264 ? -16.205 -17.865 41.796  1.00 39.40 ?  270 GLU A CB    1 
ATOM   1964 C CG    . GLU A 1 264 ? -16.383 -18.750 43.032  1.00 43.62 ?  270 GLU A CG    1 
ATOM   1965 C CD    . GLU A 1 264 ? -16.765 -17.979 44.298  1.00 46.48 ?  270 GLU A CD    1 
ATOM   1966 O OE1   . GLU A 1 264 ? -17.137 -16.784 44.208  1.00 44.02 ?  270 GLU A OE1   1 
ATOM   1967 O OE2   . GLU A 1 264 ? -16.690 -18.584 45.392  1.00 53.30 -1 270 GLU A OE2   1 
ATOM   1968 N N     . HIS A 1 265 ? -19.341 -19.181 41.105  1.00 31.99 ?  271 HIS A N     1 
ATOM   1969 C CA    . HIS A 1 265 ? -20.155 -20.305 40.646  1.00 31.01 ?  271 HIS A CA    1 
ATOM   1970 C C     . HIS A 1 265 ? -21.215 -19.889 39.637  1.00 30.05 ?  271 HIS A C     1 
ATOM   1971 O O     . HIS A 1 265 ? -22.006 -20.738 39.209  1.00 26.46 ?  271 HIS A O     1 
ATOM   1972 C CB    . HIS A 1 265 ? -20.854 -20.982 41.830  1.00 35.40 ?  271 HIS A CB    1 
ATOM   1973 C CG    . HIS A 1 265 ? -19.980 -21.160 43.026  1.00 37.00 ?  271 HIS A CG    1 
ATOM   1974 N ND1   . HIS A 1 265 ? -18.801 -21.873 42.982  1.00 38.35 ?  271 HIS A ND1   1 
ATOM   1975 C CD2   . HIS A 1 265 ? -20.114 -20.723 44.302  1.00 37.40 ?  271 HIS A CD2   1 
ATOM   1976 C CE1   . HIS A 1 265 ? -18.245 -21.868 44.182  1.00 40.87 ?  271 HIS A CE1   1 
ATOM   1977 N NE2   . HIS A 1 265 ? -19.022 -21.178 45.000  1.00 35.44 ?  271 HIS A NE2   1 
ATOM   1978 N N     . LEU A 1 266 ? -21.269 -18.603 39.285  1.00 28.10 ?  272 LEU A N     1 
ATOM   1979 C CA    . LEU A 1 266 ? -22.178 -18.011 38.305  1.00 31.72 ?  272 LEU A CA    1 
ATOM   1980 C C     . LEU A 1 266 ? -23.630 -17.969 38.760  1.00 27.37 ?  272 LEU A C     1 
ATOM   1981 O O     . LEU A 1 266 ? -24.510 -17.749 37.933  1.00 22.75 ?  272 LEU A O     1 
ATOM   1982 C CB    . LEU A 1 266 ? -22.110 -18.727 36.955  1.00 25.80 ?  272 LEU A CB    1 
ATOM   1983 C CG    . LEU A 1 266 ? -20.725 -18.670 36.323  1.00 31.85 ?  272 LEU A CG    1 
ATOM   1984 C CD1   . LEU A 1 266 ? -20.676 -19.577 35.131  1.00 27.62 ?  272 LEU A CD1   1 
ATOM   1985 C CD2   . LEU A 1 266 ? -20.396 -17.235 35.932  1.00 29.88 ?  272 LEU A CD2   1 
ATOM   1986 N N     . GLN A 1 267 ? -23.923 -18.203 40.039  1.00 25.30 ?  273 GLN A N     1 
ATOM   1987 C CA    . GLN A 1 267 ? -25.286 -17.955 40.493  1.00 24.42 ?  273 GLN A CA    1 
ATOM   1988 C C     . GLN A 1 267 ? -25.489 -16.460 40.645  1.00 29.23 ?  273 GLN A C     1 
ATOM   1989 O O     . GLN A 1 267 ? -24.567 -15.738 41.039  1.00 30.18 ?  273 GLN A O     1 
ATOM   1990 C CB    . GLN A 1 267 ? -25.588 -18.623 41.837  1.00 31.80 ?  273 GLN A CB    1 
ATOM   1991 C CG    . GLN A 1 267 ? -25.267 -20.095 42.012  1.00 29.41 ?  273 GLN A CG    1 
ATOM   1992 C CD    . GLN A 1 267 ? -25.539 -20.510 43.447  1.00 37.36 ?  273 GLN A CD    1 
ATOM   1993 O OE1   . GLN A 1 267 ? -25.978 -19.689 44.261  1.00 42.40 ?  273 GLN A OE1   1 
ATOM   1994 N NE2   . GLN A 1 267 ? -25.294 -21.774 43.763  1.00 32.92 ?  273 GLN A NE2   1 
ATOM   1995 N N     . VAL A 1 268 ? -26.699 -15.986 40.352  1.00 27.75 ?  274 VAL A N     1 
ATOM   1996 C CA    . VAL A 1 268 ? -26.974 -14.564 40.495  1.00 30.14 ?  274 VAL A CA    1 
ATOM   1997 C C     . VAL A 1 268 ? -27.036 -14.225 41.977  1.00 38.89 ?  274 VAL A C     1 
ATOM   1998 O O     . VAL A 1 268 ? -27.688 -14.929 42.757  1.00 39.34 ?  274 VAL A O     1 
ATOM   1999 C CB    . VAL A 1 268 ? -28.273 -14.199 39.765  1.00 32.31 ?  274 VAL A CB    1 
ATOM   2000 C CG1   . VAL A 1 268 ? -28.649 -12.751 40.018  1.00 37.26 ?  274 VAL A CG1   1 
ATOM   2001 C CG2   . VAL A 1 268 ? -28.114 -14.458 38.252  1.00 29.25 ?  274 VAL A CG2   1 
ATOM   2002 N N     . GLU A 1 269 ? -26.329 -13.166 42.385  1.00 40.10 ?  275 GLU A N     1 
ATOM   2003 C CA    . GLU A 1 269 ? -26.343 -12.786 43.794  1.00 42.42 ?  275 GLU A CA    1 
ATOM   2004 C C     . GLU A 1 269 ? -27.778 -12.522 44.234  1.00 45.27 ?  275 GLU A C     1 
ATOM   2005 O O     . GLU A 1 269 ? -28.564 -11.910 43.504  1.00 39.13 ?  275 GLU A O     1 
ATOM   2006 C CB    . GLU A 1 269 ? -25.466 -11.554 44.049  1.00 43.97 ?  275 GLU A CB    1 
ATOM   2007 C CG    . GLU A 1 269 ? -26.038 -10.247 43.521  1.00 51.05 ?  275 GLU A CG    1 
ATOM   2008 C CD    . GLU A 1 269 ? -25.458 -9.018  44.209  1.00 54.65 ?  275 GLU A CD    1 
ATOM   2009 O OE1   . GLU A 1 269 ? -24.220 -8.973  44.407  1.00 49.59 ?  275 GLU A OE1   1 
ATOM   2010 O OE2   . GLU A 1 269 ? -26.251 -8.105  44.559  1.00 48.17 -1 275 GLU A OE2   1 
ATOM   2011 N N     . GLY A 1 270 ? -28.126 -13.026 45.422  1.00 47.18 ?  276 GLY A N     1 
ATOM   2012 C CA    . GLY A 1 270 ? -29.495 -13.040 45.897  1.00 48.02 ?  276 GLY A CA    1 
ATOM   2013 C C     . GLY A 1 270 ? -30.291 -14.280 45.536  1.00 50.44 ?  276 GLY A C     1 
ATOM   2014 O O     . GLY A 1 270 ? -31.468 -14.375 45.913  1.00 50.84 ?  276 GLY A O     1 
ATOM   2015 N N     . HIS A 1 271 ? -29.698 -15.232 44.816  1.00 45.78 ?  277 HIS A N     1 
ATOM   2016 C CA    . HIS A 1 271 ? -30.410 -16.440 44.418  1.00 44.13 ?  277 HIS A CA    1 
ATOM   2017 C C     . HIS A 1 271 ? -29.430 -17.607 44.373  1.00 45.46 ?  277 HIS A C     1 
ATOM   2018 O O     . HIS A 1 271 ? -28.244 -17.432 44.082  1.00 44.44 ?  277 HIS A O     1 
ATOM   2019 C CB    . HIS A 1 271 ? -31.105 -16.267 43.060  1.00 44.18 ?  277 HIS A CB    1 
ATOM   2020 C CG    . HIS A 1 271 ? -32.209 -15.251 43.063  1.00 46.96 ?  277 HIS A CG    1 
ATOM   2021 N ND1   . HIS A 1 271 ? -31.983 -13.898 42.909  1.00 46.33 ?  277 HIS A ND1   1 
ATOM   2022 C CD2   . HIS A 1 271 ? -33.550 -15.394 43.188  1.00 44.42 ?  277 HIS A CD2   1 
ATOM   2023 C CE1   . HIS A 1 271 ? -33.138 -13.255 42.942  1.00 46.62 ?  277 HIS A CE1   1 
ATOM   2024 N NE2   . HIS A 1 271 ? -34.104 -14.140 43.111  1.00 48.82 ?  277 HIS A NE2   1 
ATOM   2025 N N     . SER A 1 272 ? -29.932 -18.803 44.684  1.00 41.22 ?  278 SER A N     1 
ATOM   2026 C CA    . SER A 1 272 ? -29.116 -20.007 44.625  1.00 36.94 ?  278 SER A CA    1 
ATOM   2027 C C     . SER A 1 272 ? -29.413 -20.864 43.404  1.00 32.79 ?  278 SER A C     1 
ATOM   2028 O O     . SER A 1 272 ? -28.574 -21.689 43.022  1.00 32.13 ?  278 SER A O     1 
ATOM   2029 C CB    . SER A 1 272 ? -29.324 -20.856 45.883  1.00 39.53 ?  278 SER A CB    1 
ATOM   2030 O OG    . SER A 1 272 ? -30.703 -21.118 46.068  1.00 43.36 ?  278 SER A OG    1 
ATOM   2031 N N     . ASN A 1 273 ? -30.578 -20.678 42.789  1.00 24.60 ?  279 ASN A N     1 
ATOM   2032 C CA    . ASN A 1 273 ? -31.030 -21.484 41.663  1.00 29.56 ?  279 ASN A CA    1 
ATOM   2033 C C     . ASN A 1 273 ? -31.152 -20.688 40.370  1.00 28.10 ?  279 ASN A C     1 
ATOM   2034 O O     . ASN A 1 273 ? -31.799 -21.163 39.435  1.00 22.28 ?  279 ASN A O     1 
ATOM   2035 C CB    . ASN A 1 273 ? -32.391 -22.079 41.978  1.00 28.67 ?  279 ASN A CB    1 
ATOM   2036 C CG    . ASN A 1 273 ? -33.411 -21.008 42.131  1.00 30.16 ?  279 ASN A CG    1 
ATOM   2037 O OD1   . ASN A 1 273 ? -33.062 -19.879 42.525  1.00 28.76 ?  279 ASN A OD1   1 
ATOM   2038 N ND2   . ASN A 1 273 ? -34.659 -21.305 41.780  1.00 28.84 ?  279 ASN A ND2   1 
ATOM   2039 N N     . VAL A 1 274 ? -30.617 -19.469 40.316  1.00 26.68 ?  280 VAL A N     1 
ATOM   2040 C CA    . VAL A 1 274 ? -30.614 -18.659 39.099  1.00 24.32 ?  280 VAL A CA    1 
ATOM   2041 C C     . VAL A 1 274 ? -29.173 -18.410 38.698  1.00 26.36 ?  280 VAL A C     1 
ATOM   2042 O O     . VAL A 1 274 ? -28.348 -17.991 39.529  1.00 21.89 ?  280 VAL A O     1 
ATOM   2043 C CB    . VAL A 1 274 ? -31.365 -17.330 39.277  1.00 24.31 ?  280 VAL A CB    1 
ATOM   2044 C CG1   . VAL A 1 274 ? -31.264 -16.497 38.009  1.00 24.82 ?  280 VAL A CG1   1 
ATOM   2045 C CG2   . VAL A 1 274 ? -32.819 -17.595 39.618  1.00 30.11 ?  280 VAL A CG2   1 
ATOM   2046 N N     . TYR A 1 275 ? -28.872 -18.671 37.426  1.00 23.23 ?  281 TYR A N     1 
ATOM   2047 C CA    . TYR A 1 275 ? -27.537 -18.522 36.890  1.00 22.05 ?  281 TYR A CA    1 
ATOM   2048 C C     . TYR A 1 275 ? -27.583 -17.545 35.726  1.00 20.40 ?  281 TYR A C     1 
ATOM   2049 O O     . TYR A 1 275 ? -28.582 -17.463 35.015  1.00 17.99 ?  281 TYR A O     1 
ATOM   2050 C CB    . TYR A 1 275 ? -26.994 -19.878 36.445  1.00 20.12 ?  281 TYR A CB    1 
ATOM   2051 C CG    . TYR A 1 275 ? -26.856 -20.853 37.603  1.00 24.38 ?  281 TYR A CG    1 
ATOM   2052 C CD1   . TYR A 1 275 ? -27.964 -21.517 38.122  1.00 25.42 ?  281 TYR A CD1   1 
ATOM   2053 C CD2   . TYR A 1 275 ? -25.616 -21.090 38.184  1.00 24.29 ?  281 TYR A CD2   1 
ATOM   2054 C CE1   . TYR A 1 275 ? -27.829 -22.398 39.196  1.00 24.36 ?  281 TYR A CE1   1 
ATOM   2055 C CE2   . TYR A 1 275 ? -25.474 -21.964 39.252  1.00 25.44 ?  281 TYR A CE2   1 
ATOM   2056 C CZ    . TYR A 1 275 ? -26.582 -22.618 39.746  1.00 28.11 ?  281 TYR A CZ    1 
ATOM   2057 O OH    . TYR A 1 275 ? -26.416 -23.487 40.807  1.00 28.78 ?  281 TYR A OH    1 
ATOM   2058 N N     . ALA A 1 276 ? -26.506 -16.793 35.554  1.00 21.53 ?  282 ALA A N     1 
ATOM   2059 C CA    . ALA A 1 276 ? -26.302 -15.996 34.353  1.00 17.77 ?  282 ALA A CA    1 
ATOM   2060 C C     . ALA A 1 276 ? -25.020 -16.453 33.691  1.00 19.16 ?  282 ALA A C     1 
ATOM   2061 O O     . ALA A 1 276 ? -24.016 -16.716 34.367  1.00 21.73 ?  282 ALA A O     1 
ATOM   2062 C CB    . ALA A 1 276 ? -26.238 -14.490 34.662  1.00 20.18 ?  282 ALA A CB    1 
ATOM   2063 N N     . ILE A 1 277 ? -25.066 -16.570 32.366  1.00 17.24 ?  283 ILE A N     1 
ATOM   2064 C CA    . ILE A 1 277 ? -23.965 -17.115 31.595  1.00 15.98 ?  283 ILE A CA    1 
ATOM   2065 C C     . ILE A 1 277 ? -23.804 -16.264 30.347  1.00 17.40 ?  283 ILE A C     1 
ATOM   2066 O O     . ILE A 1 277 ? -24.778 -15.724 29.815  1.00 17.31 ?  283 ILE A O     1 
ATOM   2067 C CB    . ILE A 1 277 ? -24.187 -18.599 31.221  1.00 16.65 ?  283 ILE A CB    1 
ATOM   2068 C CG1   . ILE A 1 277 ? -25.390 -18.772 30.300  1.00 15.44 ?  283 ILE A CG1   1 
ATOM   2069 C CG2   . ILE A 1 277 ? -24.390 -19.453 32.487  1.00 16.05 ?  283 ILE A CG2   1 
ATOM   2070 C CD1   . ILE A 1 277 ? -25.468 -20.194 29.703  1.00 15.32 ?  283 ILE A CD1   1 
ATOM   2071 N N     . GLY A 1 278 ? -22.565 -16.159 29.874  1.00 18.07 ?  284 GLY A N     1 
ATOM   2072 C CA    . GLY A 1 278 ? -22.326 -15.466 28.619  1.00 18.80 ?  284 GLY A CA    1 
ATOM   2073 C C     . GLY A 1 278 ? -22.372 -13.957 28.791  1.00 21.66 ?  284 GLY A C     1 
ATOM   2074 O O     . GLY A 1 278 ? -22.040 -13.422 29.852  1.00 20.67 ?  284 GLY A O     1 
ATOM   2075 N N     . ASP A 1 279 ? -22.788 -13.262 27.720  1.00 17.50 ?  285 ASP A N     1 
ATOM   2076 C CA    . ASP A 1 279 ? -22.692 -11.800 27.707  1.00 18.91 ?  285 ASP A CA    1 
ATOM   2077 C C     . ASP A 1 279 ? -23.489 -11.155 28.835  1.00 25.24 ?  285 ASP A C     1 
ATOM   2078 O O     . ASP A 1 279 ? -23.079 -10.115 29.364  1.00 25.76 ?  285 ASP A O     1 
ATOM   2079 C CB    . ASP A 1 279 ? -23.163 -11.238 26.364  1.00 20.67 ?  285 ASP A CB    1 
ATOM   2080 C CG    . ASP A 1 279 ? -22.152 -11.457 25.240  1.00 22.44 ?  285 ASP A CG    1 
ATOM   2081 O OD1   . ASP A 1 279 ? -21.160 -12.206 25.447  1.00 21.13 ?  285 ASP A OD1   1 
ATOM   2082 O OD2   . ASP A 1 279 ? -22.367 -10.894 24.129  1.00 20.32 -1 285 ASP A OD2   1 
ATOM   2083 N N     . CYS A 1 280 ? -24.621 -11.742 29.219  1.00 23.39 ?  286 CYS A N     1 
ATOM   2084 C CA    . CYS A 1 280 ? -25.435 -11.136 30.265  1.00 25.84 ?  286 CYS A CA    1 
ATOM   2085 C C     . CYS A 1 280 ? -24.901 -11.400 31.667  1.00 27.31 ?  286 CYS A C     1 
ATOM   2086 O O     . CYS A 1 280 ? -25.486 -10.896 32.628  1.00 28.76 ?  286 CYS A O     1 
ATOM   2087 C CB    . CYS A 1 280 ? -26.885 -11.616 30.170  1.00 21.13 ?  286 CYS A CB    1 
ATOM   2088 S SG    . CYS A 1 280 ? -27.153 -13.332 30.756  1.00 23.37 ?  286 CYS A SG    1 
ATOM   2089 N N     . ALA A 1 281 ? -23.808 -12.151 31.811  1.00 26.30 ?  287 ALA A N     1 
ATOM   2090 C CA    . ALA A 1 281 ? -23.164 -12.341 33.110  1.00 29.94 ?  287 ALA A CA    1 
ATOM   2091 C C     . ALA A 1 281 ? -22.088 -11.281 33.356  1.00 36.23 ?  287 ALA A C     1 
ATOM   2092 O O     . ALA A 1 281 ? -21.236 -11.029 32.500  1.00 33.87 ?  287 ALA A O     1 
ATOM   2093 C CB    . ALA A 1 281 ? -22.544 -13.731 33.224  1.00 25.64 ?  287 ALA A CB    1 
ATOM   2094 N N     . ASP A 1 282 ? -22.119 -10.677 34.551  1.00 43.08 ?  288 ASP A N     1 
ATOM   2095 C CA    . ASP A 1 282 ? -21.128 -9.682  34.949  1.00 40.53 ?  288 ASP A CA    1 
ATOM   2096 C C     . ASP A 1 282 ? -19.788 -10.345 35.243  1.00 48.34 ?  288 ASP A C     1 
ATOM   2097 O O     . ASP A 1 282 ? -19.289 -10.308 36.374  1.00 48.91 ?  288 ASP A O     1 
ATOM   2098 C CB    . ASP A 1 282 ? -21.605 -8.893  36.168  1.00 40.52 ?  288 ASP A CB    1 
ATOM   2099 C CG    . ASP A 1 282 ? -20.656 -7.755  36.536  1.00 53.98 ?  288 ASP A CG    1 
ATOM   2100 O OD1   . ASP A 1 282 ? -20.237 -7.005  35.621  1.00 50.53 ?  288 ASP A OD1   1 
ATOM   2101 O OD2   . ASP A 1 282 ? -20.331 -7.615  37.741  1.00 51.93 -1 288 ASP A OD2   1 
ATOM   2102 N N     . VAL A 1 283 ? -19.203 -10.970 34.223  1.00 50.92 ?  289 VAL A N     1 
ATOM   2103 C CA    . VAL A 1 283 ? -17.910 -11.612 34.396  1.00 53.45 ?  289 VAL A CA    1 
ATOM   2104 C C     . VAL A 1 283 ? -16.828 -10.572 34.638  1.00 59.98 ?  289 VAL A C     1 
ATOM   2105 O O     . VAL A 1 283 ? -15.834 -10.853 35.321  1.00 64.19 ?  289 VAL A O     1 
ATOM   2106 C CB    . VAL A 1 283 ? -17.590 -12.490 33.170  1.00 51.56 ?  289 VAL A CB    1 
ATOM   2107 N N     . ARG A 1 284 ? -17.007 -9.360  34.095  1.00 57.34 ?  290 ARG A N     1 
ATOM   2108 C CA    . ARG A 1 284 ? -15.982 -8.318  34.011  1.00 64.85 ?  290 ARG A CA    1 
ATOM   2109 C C     . ARG A 1 284 ? -14.876 -8.739  33.041  1.00 66.03 ?  290 ARG A C     1 
ATOM   2110 O O     . ARG A 1 284 ? -14.019 -7.930  32.674  1.00 66.84 ?  290 ARG A O     1 
ATOM   2111 C CB    . ARG A 1 284 ? -15.412 -7.974  35.394  1.00 63.29 ?  290 ARG A CB    1 
ATOM   2112 N N     . THR A 1 285 ? -14.894 -10.006 32.624  1.00 63.86 ?  291 THR A N     1 
ATOM   2113 C CA    . THR A 1 285 ? -14.099 -10.494 31.511  1.00 63.02 ?  291 THR A CA    1 
ATOM   2114 C C     . THR A 1 285 ? -14.692 -9.946  30.212  1.00 59.48 ?  291 THR A C     1 
ATOM   2115 O O     . THR A 1 285 ? -15.803 -9.410  30.210  1.00 57.49 ?  291 THR A O     1 
ATOM   2116 C CB    . THR A 1 285 ? -14.087 -12.026 31.521  1.00 57.83 ?  291 THR A CB    1 
ATOM   2117 N N     . PRO A 1 286 ? -13.980 -10.049 29.087  1.00 60.50 ?  292 PRO A N     1 
ATOM   2118 C CA    . PRO A 1 286 ? -14.583 -9.649  27.809  1.00 52.40 ?  292 PRO A CA    1 
ATOM   2119 C C     . PRO A 1 286 ? -15.755 -10.555 27.469  1.00 41.36 ?  292 PRO A C     1 
ATOM   2120 O O     . PRO A 1 286 ? -15.856 -11.696 27.929  1.00 40.98 ?  292 PRO A O     1 
ATOM   2121 C CB    . PRO A 1 286 ? -13.444 -9.831  26.806  1.00 47.38 ?  292 PRO A CB    1 
ATOM   2122 C CG    . PRO A 1 286 ? -12.679 -10.966 27.390  1.00 48.36 ?  292 PRO A CG    1 
ATOM   2123 C CD    . PRO A 1 286 ? -12.649 -10.647 28.866  1.00 57.33 ?  292 PRO A CD    1 
ATOM   2124 N N     . LYS A 1 287 ? -16.660 -10.035 26.654  1.00 34.68 ?  293 LYS A N     1 
ATOM   2125 C CA    . LYS A 1 287 ? -17.847 -10.798 26.290  1.00 28.61 ?  293 LYS A CA    1 
ATOM   2126 C C     . LYS A 1 287 ? -17.487 -11.650 25.079  1.00 22.33 ?  293 LYS A C     1 
ATOM   2127 O O     . LYS A 1 287 ? -17.263 -11.121 23.989  1.00 22.63 ?  293 LYS A O     1 
ATOM   2128 C CB    . LYS A 1 287 ? -19.022 -9.864  26.023  1.00 30.75 ?  293 LYS A CB    1 
ATOM   2129 C CG    . LYS A 1 287 ? -19.357 -8.958  27.216  1.00 34.17 ?  293 LYS A CG    1 
ATOM   2130 C CD    . LYS A 1 287 ? -19.342 -9.727  28.535  1.00 36.78 ?  293 LYS A CD    1 
ATOM   2131 N N     . MET A 1 288 ? -17.425 -12.970 25.272  1.00 20.68 ?  294 MET A N     1 
ATOM   2132 C CA    . MET A 1 288 ? -16.869 -13.892 24.291  1.00 16.60 ?  294 MET A CA    1 
ATOM   2133 C C     . MET A 1 288 ? -17.759 -15.121 24.151  1.00 15.76 ?  294 MET A C     1 
ATOM   2134 O O     . MET A 1 288 ? -18.306 -15.612 25.143  1.00 15.89 ?  294 MET A O     1 
ATOM   2135 C CB    . MET A 1 288 ? -15.467 -14.357 24.704  1.00 20.35 ?  294 MET A CB    1 
ATOM   2136 C CG    . MET A 1 288 ? -14.413 -13.257 24.730  1.00 22.24 ?  294 MET A CG    1 
ATOM   2137 S SD    . MET A 1 288 ? -14.105 -12.688 23.044  1.00 31.08 ?  294 MET A SD    1 
ATOM   2138 C CE    . MET A 1 288 ? -12.451 -12.097 23.250  1.00 52.95 ?  294 MET A CE    1 
ATOM   2139 N N     . ALA A 1 289 ? -17.856 -15.641 22.925  1.00 13.30 ?  295 ALA A N     1 
ATOM   2140 C CA    . ALA A 1 289 ? -18.613 -16.872 22.700  1.00 14.75 ?  295 ALA A CA    1 
ATOM   2141 C C     . ALA A 1 289 ? -18.022 -18.042 23.485  1.00 14.52 ?  295 ALA A C     1 
ATOM   2142 O O     . ALA A 1 289 ? -18.757 -18.856 24.061  1.00 10.94 ?  295 ALA A O     1 
ATOM   2143 C CB    . ALA A 1 289 ? -18.633 -17.204 21.205  1.00 13.13 ?  295 ALA A CB    1 
ATOM   2144 N N     . TYR A 1 290 ? -16.691 -18.158 23.510  1.00 15.95 ?  296 TYR A N     1 
ATOM   2145 C CA    . TYR A 1 290 ? -16.113 -19.336 24.153  1.00 15.34 ?  296 TYR A CA    1 
ATOM   2146 C C     . TYR A 1 290 ? -16.317 -19.298 25.664  1.00 17.80 ?  296 TYR A C     1 
ATOM   2147 O O     . TYR A 1 290 ? -16.440 -20.354 26.297  1.00 18.45 ?  296 TYR A O     1 
ATOM   2148 C CB    . TYR A 1 290 ? -14.632 -19.466 23.793  1.00 18.68 ?  296 TYR A CB    1 
ATOM   2149 C CG    . TYR A 1 290 ? -13.680 -18.638 24.627  1.00 17.34 ?  296 TYR A CG    1 
ATOM   2150 C CD1   . TYR A 1 290 ? -13.102 -19.156 25.787  1.00 22.76 ?  296 TYR A CD1   1 
ATOM   2151 C CD2   . TYR A 1 290 ? -13.326 -17.352 24.238  1.00 17.97 ?  296 TYR A CD2   1 
ATOM   2152 C CE1   . TYR A 1 290 ? -12.229 -18.401 26.536  1.00 21.46 ?  296 TYR A CE1   1 
ATOM   2153 C CE2   . TYR A 1 290 ? -12.444 -16.599 24.980  1.00 16.66 ?  296 TYR A CE2   1 
ATOM   2154 C CZ    . TYR A 1 290 ? -11.899 -17.131 26.121  1.00 18.32 ?  296 TYR A CZ    1 
ATOM   2155 O OH    . TYR A 1 290 ? -11.034 -16.377 26.859  1.00 18.66 ?  296 TYR A OH    1 
ATOM   2156 N N     . LEU A 1 291 ? -16.375 -18.103 26.248  1.00 13.45 ?  297 LEU A N     1 
ATOM   2157 C CA    . LEU A 1 291 ? -16.645 -17.988 27.677  1.00 17.29 ?  297 LEU A CA    1 
ATOM   2158 C C     . LEU A 1 291 ? -18.096 -18.313 27.995  1.00 16.41 ?  297 LEU A C     1 
ATOM   2159 O O     . LEU A 1 291 ? -18.387 -18.896 29.042  1.00 15.40 ?  297 LEU A O     1 
ATOM   2160 C CB    . LEU A 1 291 ? -16.307 -16.580 28.160  1.00 17.39 ?  297 LEU A CB    1 
ATOM   2161 C CG    . LEU A 1 291 ? -14.824 -16.232 28.246  1.00 22.74 ?  297 LEU A CG    1 
ATOM   2162 C CD1   . LEU A 1 291 ? -14.652 -14.768 28.634  1.00 22.61 ?  297 LEU A CD1   1 
ATOM   2163 C CD2   . LEU A 1 291 ? -14.136 -17.150 29.248  1.00 19.62 ?  297 LEU A CD2   1 
ATOM   2164 N N     . ALA A 1 292 ? -19.026 -17.921 27.118  1.00 14.72 ?  298 ALA A N     1 
ATOM   2165 C CA    . ALA A 1 292 ? -20.419 -18.319 27.293  1.00 13.47 ?  298 ALA A CA    1 
ATOM   2166 C C     . ALA A 1 292 ? -20.548 -19.833 27.384  1.00 13.87 ?  298 ALA A C     1 
ATOM   2167 O O     . ALA A 1 292 ? -21.300 -20.349 28.215  1.00 15.33 ?  298 ALA A O     1 
ATOM   2168 C CB    . ALA A 1 292 ? -21.277 -17.782 26.137  1.00 13.30 ?  298 ALA A CB    1 
ATOM   2169 N N     . GLY A 1 293 ? -19.833 -20.556 26.527  1.00 13.68 ?  299 GLY A N     1 
ATOM   2170 C CA    . GLY A 1 293 ? -19.860 -22.007 26.594  1.00 13.14 ?  299 GLY A CA    1 
ATOM   2171 C C     . GLY A 1 293 ? -19.304 -22.547 27.901  1.00 19.41 ?  299 GLY A C     1 
ATOM   2172 O O     . GLY A 1 293 ? -19.868 -23.474 28.484  1.00 19.42 ?  299 GLY A O     1 
ATOM   2173 N N     . LEU A 1 294 ? -18.184 -21.985 28.376  1.00 19.97 ?  300 LEU A N     1 
ATOM   2174 C CA    . LEU A 1 294 ? -17.630 -22.421 29.660  1.00 22.06 ?  300 LEU A CA    1 
ATOM   2175 C C     . LEU A 1 294 ? -18.568 -22.107 30.810  1.00 18.91 ?  300 LEU A C     1 
ATOM   2176 O O     . LEU A 1 294 ? -18.711 -22.914 31.736  1.00 22.34 ?  300 LEU A O     1 
ATOM   2177 C CB    . LEU A 1 294 ? -16.279 -21.754 29.926  1.00 21.68 ?  300 LEU A CB    1 
ATOM   2178 C CG    . LEU A 1 294 ? -15.116 -22.086 29.007  1.00 28.80 ?  300 LEU A CG    1 
ATOM   2179 C CD1   . LEU A 1 294 ? -13.834 -21.432 29.554  1.00 32.57 ?  300 LEU A CD1   1 
ATOM   2180 C CD2   . LEU A 1 294 ? -14.952 -23.595 28.863  1.00 30.49 ?  300 LEU A CD2   1 
ATOM   2181 N N     . HIS A 1 295 ? -19.162 -20.911 30.809  1.00 17.23 ?  301 HIS A N     1 
ATOM   2182 C CA    . HIS A 1 295 ? -20.143 -20.572 31.829  1.00 18.69 ?  301 HIS A CA    1 
ATOM   2183 C C     . HIS A 1 295 ? -21.296 -21.565 31.851  1.00 18.74 ?  301 HIS A C     1 
ATOM   2184 O O     . HIS A 1 295 ? -21.792 -21.929 32.922  1.00 19.60 ?  301 HIS A O     1 
ATOM   2185 C CB    . HIS A 1 295 ? -20.703 -19.176 31.604  1.00 18.38 ?  301 HIS A CB    1 
ATOM   2186 C CG    . HIS A 1 295 ? -19.698 -18.079 31.745  1.00 21.47 ?  301 HIS A CG    1 
ATOM   2187 N ND1   . HIS A 1 295 ? -19.956 -16.783 31.338  1.00 20.94 ?  301 HIS A ND1   1 
ATOM   2188 C CD2   . HIS A 1 295 ? -18.436 -18.079 32.235  1.00 25.05 ?  301 HIS A CD2   1 
ATOM   2189 C CE1   . HIS A 1 295 ? -18.895 -16.032 31.582  1.00 22.73 ?  301 HIS A CE1   1 
ATOM   2190 N NE2   . HIS A 1 295 ? -17.958 -16.794 32.120  1.00 24.30 ?  301 HIS A NE2   1 
ATOM   2191 N N     . ALA A 1 296 ? -21.771 -21.980 30.678  1.00 18.14 ?  302 ALA A N     1 
ATOM   2192 C CA    . ALA A 1 296 ? -22.889 -22.916 30.640  1.00 17.18 ?  302 ALA A CA    1 
ATOM   2193 C C     . ALA A 1 296 ? -22.513 -24.224 31.307  1.00 20.31 ?  302 ALA A C     1 
ATOM   2194 O O     . ALA A 1 296 ? -23.310 -24.804 32.063  1.00 18.50 ?  302 ALA A O     1 
ATOM   2195 C CB    . ALA A 1 296 ? -23.325 -23.169 29.195  1.00 12.79 ?  302 ALA A CB    1 
ATOM   2196 N N     . ASN A 1 297 ? -21.298 -24.709 31.043  1.00 21.98 ?  303 ASN A N     1 
ATOM   2197 C CA    . ASN A 1 297 ? -20.864 -25.949 31.669  1.00 23.72 ?  303 ASN A CA    1 
ATOM   2198 C C     . ASN A 1 297 ? -20.793 -25.790 33.179  1.00 23.02 ?  303 ASN A C     1 
ATOM   2199 O O     . ASN A 1 297 ? -21.156 -26.704 33.922  1.00 20.57 ?  303 ASN A O     1 
ATOM   2200 C CB    . ASN A 1 297 ? -19.509 -26.379 31.112  1.00 27.34 ?  303 ASN A CB    1 
ATOM   2201 C CG    . ASN A 1 297 ? -19.608 -26.956 29.702  1.00 39.76 ?  303 ASN A CG    1 
ATOM   2202 O OD1   . ASN A 1 297 ? -20.635 -27.518 29.319  1.00 39.07 ?  303 ASN A OD1   1 
ATOM   2203 N ND2   . ASN A 1 297 ? -18.542 -26.825 28.934  1.00 58.14 ?  303 ASN A ND2   1 
ATOM   2204 N N     . ILE A 1 298 ? -20.329 -24.633 33.647  1.00 20.60 ?  304 ILE A N     1 
ATOM   2205 C CA    . ILE A 1 298 ? -20.287 -24.378 35.081  1.00 22.34 ?  304 ILE A CA    1 
ATOM   2206 C C     . ILE A 1 298 ? -21.695 -24.309 35.655  1.00 23.17 ?  304 ILE A C     1 
ATOM   2207 O O     . ILE A 1 298 ? -21.962 -24.898 36.719  1.00 24.09 ?  304 ILE A O     1 
ATOM   2208 C CB    . ILE A 1 298 ? -19.491 -23.095 35.378  1.00 26.87 ?  304 ILE A CB    1 
ATOM   2209 C CG1   . ILE A 1 298 ? -17.998 -23.339 35.147  1.00 27.86 ?  304 ILE A CG1   1 
ATOM   2210 C CG2   . ILE A 1 298 ? -19.769 -22.599 36.779  1.00 26.21 ?  304 ILE A CG2   1 
ATOM   2211 C CD1   . ILE A 1 298 ? -17.181 -22.070 35.128  1.00 28.92 ?  304 ILE A CD1   1 
ATOM   2212 N N     . ALA A 1 299 ? -22.626 -23.640 34.943  1.00 21.64 ?  305 ALA A N     1 
ATOM   2213 C CA    . ALA A 1 299 ? -23.995 -23.453 35.437  1.00 18.11 ?  305 ALA A CA    1 
ATOM   2214 C C     . ALA A 1 299 ? -24.736 -24.783 35.556  1.00 20.87 ?  305 ALA A C     1 
ATOM   2215 O O     . ALA A 1 299 ? -25.361 -25.074 36.588  1.00 19.24 ?  305 ALA A O     1 
ATOM   2216 C CB    . ALA A 1 299 ? -24.779 -22.495 34.542  1.00 22.10 ?  305 ALA A CB    1 
ATOM   2217 N N     . VAL A 1 300 ? -24.681 -25.606 34.512  1.00 16.77 ?  306 VAL A N     1 
ATOM   2218 C CA    . VAL A 1 300 ? -25.381 -26.884 34.557  1.00 18.67 ?  306 VAL A CA    1 
ATOM   2219 C C     . VAL A 1 300 ? -24.779 -27.777 35.634  1.00 20.22 ?  306 VAL A C     1 
ATOM   2220 O O     . VAL A 1 300 ? -25.497 -28.444 36.393  1.00 21.38 ?  306 VAL A O     1 
ATOM   2221 C CB    . VAL A 1 300 ? -25.352 -27.551 33.172  1.00 19.18 ?  306 VAL A CB    1 
ATOM   2222 C CG1   . VAL A 1 300 ? -25.821 -29.002 33.257  1.00 18.34 ?  306 VAL A CG1   1 
ATOM   2223 C CG2   . VAL A 1 300 ? -26.200 -26.726 32.189  1.00 14.55 ?  306 VAL A CG2   1 
ATOM   2224 N N     . ALA A 1 301 ? -23.451 -27.768 35.739  1.00 20.67 ?  307 ALA A N     1 
ATOM   2225 C CA    . ALA A 1 301 ? -22.766 -28.595 36.732  1.00 23.63 ?  307 ALA A CA    1 
ATOM   2226 C C     . ALA A 1 301 ? -23.163 -28.222 38.154  1.00 26.16 ?  307 ALA A C     1 
ATOM   2227 O O     . ALA A 1 301 ? -23.343 -29.108 39.000  1.00 23.49 ?  307 ALA A O     1 
ATOM   2228 C CB    . ALA A 1 301 ? -21.252 -28.492 36.544  1.00 26.84 ?  307 ALA A CB    1 
ATOM   2229 N N     . ASN A 1 302 ? -23.311 -26.926 38.455  1.00 22.66 ?  308 ASN A N     1 
ATOM   2230 C CA    . ASN A 1 302 ? -23.650 -26.619 39.840  1.00 23.98 ?  308 ASN A CA    1 
ATOM   2231 C C     . ASN A 1 302 ? -25.130 -26.794 40.126  1.00 26.27 ?  308 ASN A C     1 
ATOM   2232 O O     . ASN A 1 302 ? -25.483 -26.994 41.286  1.00 28.28 ?  308 ASN A O     1 
ATOM   2233 C CB    . ASN A 1 302 ? -23.250 -25.202 40.254  1.00 29.77 ?  308 ASN A CB    1 
ATOM   2234 C CG    . ASN A 1 302 ? -21.780 -24.929 40.095  1.00 30.00 ?  308 ASN A CG    1 
ATOM   2235 O OD1   . ASN A 1 302 ? -20.945 -25.823 40.248  1.00 31.21 ?  308 ASN A OD1   1 
ATOM   2236 N ND2   . ASN A 1 302 ? -21.444 -23.665 39.837  1.00 28.86 ?  308 ASN A ND2   1 
ATOM   2237 N N     . ILE A 1 303 ? -26.010 -26.735 39.119  1.00 22.10 ?  309 ILE A N     1 
ATOM   2238 C CA    . ILE A 1 303 ? -27.386 -27.193 39.341  1.00 24.61 ?  309 ILE A CA    1 
ATOM   2239 C C     . ILE A 1 303 ? -27.375 -28.646 39.819  1.00 26.36 ?  309 ILE A C     1 
ATOM   2240 O O     . ILE A 1 303 ? -27.965 -28.987 40.855  1.00 30.00 ?  309 ILE A O     1 
ATOM   2241 C CB    . ILE A 1 303 ? -28.249 -27.020 38.073  1.00 23.76 ?  309 ILE A CB    1 
ATOM   2242 C CG1   . ILE A 1 303 ? -28.428 -25.540 37.710  1.00 21.80 ?  309 ILE A CG1   1 
ATOM   2243 C CG2   . ILE A 1 303 ? -29.607 -27.672 38.261  1.00 21.91 ?  309 ILE A CG2   1 
ATOM   2244 C CD1   . ILE A 1 303 ? -29.235 -25.300 36.410  1.00 19.99 ?  309 ILE A CD1   1 
ATOM   2245 N N     . VAL A 1 304 ? -26.638 -29.509 39.111  1.00 23.25 ?  310 VAL A N     1 
ATOM   2246 C CA    . VAL A 1 304 ? -26.528 -30.913 39.514  1.00 23.10 ?  310 VAL A CA    1 
ATOM   2247 C C     . VAL A 1 304 ? -25.763 -31.047 40.831  1.00 27.95 ?  310 VAL A C     1 
ATOM   2248 O O     . VAL A 1 304 ? -26.211 -31.737 41.756  1.00 28.34 ?  310 VAL A O     1 
ATOM   2249 C CB    . VAL A 1 304 ? -25.871 -31.740 38.397  1.00 25.85 ?  310 VAL A CB    1 
ATOM   2250 C CG1   . VAL A 1 304 ? -25.603 -33.159 38.878  1.00 28.55 ?  310 VAL A CG1   1 
ATOM   2251 C CG2   . VAL A 1 304 ? -26.760 -31.752 37.175  1.00 24.35 ?  310 VAL A CG2   1 
ATOM   2252 N N     . ASN A 1 305 ? -24.583 -30.419 40.926  1.00 26.77 ?  311 ASN A N     1 
ATOM   2253 C CA    . ASN A 1 305 ? -23.825 -30.464 42.177  1.00 30.45 ?  311 ASN A CA    1 
ATOM   2254 C C     . ASN A 1 305 ? -24.681 -30.028 43.352  1.00 33.53 ?  311 ASN A C     1 
ATOM   2255 O O     . ASN A 1 305 ? -24.587 -30.603 44.445  1.00 35.22 ?  311 ASN A O     1 
ATOM   2256 C CB    . ASN A 1 305 ? -22.590 -29.569 42.110  1.00 30.30 ?  311 ASN A CB    1 
ATOM   2257 C CG    . ASN A 1 305 ? -21.434 -30.218 41.411  1.00 37.80 ?  311 ASN A CG    1 
ATOM   2258 O OD1   . ASN A 1 305 ? -21.359 -31.439 41.309  1.00 40.05 ?  311 ASN A OD1   1 
ATOM   2259 N ND2   . ASN A 1 305 ? -20.507 -29.396 40.925  1.00 38.11 ?  311 ASN A ND2   1 
ATOM   2260 N N     . SER A 1 306 ? -25.519 -29.007 43.150  1.00 28.46 ?  312 SER A N     1 
ATOM   2261 C CA    . SER A 1 306 ? -26.304 -28.489 44.263  1.00 32.85 ?  312 SER A CA    1 
ATOM   2262 C C     . SER A 1 306 ? -27.353 -29.495 44.712  1.00 36.77 ?  312 SER A C     1 
ATOM   2263 O O     . SER A 1 306 ? -27.653 -29.578 45.906  1.00 40.15 ?  312 SER A O     1 
ATOM   2264 C CB    . SER A 1 306 ? -26.965 -27.160 43.902  1.00 31.01 ?  312 SER A CB    1 
ATOM   2265 O OG    . SER A 1 306 ? -28.140 -27.362 43.147  1.00 33.18 ?  312 SER A OG    1 
ATOM   2266 N N     . VAL A 1 307 ? -27.925 -30.262 43.775  1.00 30.38 ?  313 VAL A N     1 
ATOM   2267 C CA    . VAL A 1 307 ? -28.883 -31.308 44.144  1.00 34.94 ?  313 VAL A CA    1 
ATOM   2268 C C     . VAL A 1 307 ? -28.173 -32.483 44.828  1.00 35.06 ?  313 VAL A C     1 
ATOM   2269 O O     . VAL A 1 307 ? -28.734 -33.112 45.734  1.00 33.77 ?  313 VAL A O     1 
ATOM   2270 C CB    . VAL A 1 307 ? -29.693 -31.752 42.906  1.00 34.21 ?  313 VAL A CB    1 
ATOM   2271 C CG1   . VAL A 1 307 ? -30.567 -32.955 43.222  1.00 35.25 ?  313 VAL A CG1   1 
ATOM   2272 C CG2   . VAL A 1 307 ? -30.579 -30.609 42.414  1.00 32.48 ?  313 VAL A CG2   1 
ATOM   2273 N N     . LYS A 1 308 ? -26.920 -32.756 44.472  1.00 35.00 ?  314 LYS A N     1 
ATOM   2274 C CA    . LYS A 1 308 ? -26.146 -33.813 45.112  1.00 38.45 ?  314 LYS A CA    1 
ATOM   2275 C C     . LYS A 1 308 ? -25.403 -33.338 46.380  1.00 42.24 ?  314 LYS A C     1 
ATOM   2276 O O     . LYS A 1 308 ? -24.529 -34.070 46.870  1.00 40.87 ?  314 LYS A O     1 
ATOM   2277 C CB    . LYS A 1 308 ? -25.153 -34.403 44.106  1.00 37.62 ?  314 LYS A CB    1 
ATOM   2278 C CG    . LYS A 1 308 ? -25.826 -35.076 42.911  1.00 35.29 ?  314 LYS A CG    1 
ATOM   2279 C CD    . LYS A 1 308 ? -24.804 -35.629 41.930  1.00 35.14 ?  314 LYS A CD    1 
ATOM   2280 C CE    . LYS A 1 308 ? -25.457 -36.481 40.853  1.00 38.30 ?  314 LYS A CE    1 
ATOM   2281 N NZ    . LYS A 1 308 ? -24.462 -37.062 39.911  1.00 36.92 ?  314 LYS A NZ    1 
ATOM   2282 N N     . GLN A 1 309 ? -25.757 -32.166 46.921  1.00 42.05 ?  315 GLN A N     1 
ATOM   2283 C CA    . GLN A 1 309 ? -25.061 -31.529 48.050  1.00 45.28 ?  315 GLN A CA    1 
ATOM   2284 C C     . GLN A 1 309 ? -23.541 -31.637 47.902  1.00 46.19 ?  315 GLN A C     1 
ATOM   2285 O O     . GLN A 1 309 ? -22.820 -31.974 48.845  1.00 45.10 ?  315 GLN A O     1 
ATOM   2286 C CB    . GLN A 1 309 ? -25.495 -32.112 49.412  1.00 46.71 ?  315 GLN A CB    1 
ATOM   2287 C CG    . GLN A 1 309 ? -27.016 -32.272 49.694  1.00 47.60 ?  315 GLN A CG    1 
ATOM   2288 C CD    . GLN A 1 309 ? -27.795 -30.956 49.901  1.00 55.24 ?  315 GLN A CD    1 
ATOM   2289 O OE1   . GLN A 1 309 ? -28.528 -30.503 49.012  1.00 63.16 ?  315 GLN A OE1   1 
ATOM   2290 N NE2   . GLN A 1 309 ? -27.656 -30.360 51.075  1.00 57.96 ?  315 GLN A NE2   1 
ATOM   2291 N N     . ARG A 1 310 ? -23.053 -31.348 46.704  1.00 42.37 ?  316 ARG A N     1 
ATOM   2292 C CA    . ARG A 1 310 ? -21.632 -31.363 46.373  1.00 41.64 ?  316 ARG A CA    1 
ATOM   2293 C C     . ARG A 1 310 ? -21.091 -29.936 46.281  1.00 43.73 ?  316 ARG A C     1 
ATOM   2294 O O     . ARG A 1 310 ? -21.851 -28.969 46.226  1.00 43.19 ?  316 ARG A O     1 
ATOM   2295 C CB    . ARG A 1 310 ? -21.410 -32.115 45.052  1.00 44.20 ?  316 ARG A CB    1 
ATOM   2296 C CG    . ARG A 1 310 ? -21.682 -33.616 45.122  1.00 42.54 ?  316 ARG A CG    1 
ATOM   2297 N N     . PRO A 1 311 ? -19.765 -29.771 46.294  1.00 45.63 ?  317 PRO A N     1 
ATOM   2298 C CA    . PRO A 1 311 ? -19.199 -28.419 46.174  1.00 44.03 ?  317 PRO A CA    1 
ATOM   2299 C C     . PRO A 1 311 ? -19.218 -27.939 44.734  1.00 39.00 ?  317 PRO A C     1 
ATOM   2300 O O     . PRO A 1 311 ? -19.063 -28.714 43.787  1.00 37.16 ?  317 PRO A O     1 
ATOM   2301 C CB    . PRO A 1 311 ? -17.755 -28.586 46.676  1.00 48.98 ?  317 PRO A CB    1 
ATOM   2302 C CG    . PRO A 1 311 ? -17.667 -29.976 47.230  1.00 51.16 ?  317 PRO A CG    1 
ATOM   2303 C CD    . PRO A 1 311 ? -18.713 -30.770 46.523  1.00 45.86 ?  317 PRO A CD    1 
ATOM   2304 N N     . LEU A 1 312 ? -19.387 -26.629 44.586  1.00 36.10 ?  318 LEU A N     1 
ATOM   2305 C CA    . LEU A 1 312 ? -19.653 -26.038 43.284  1.00 32.99 ?  318 LEU A CA    1 
ATOM   2306 C C     . LEU A 1 312 ? -18.364 -25.752 42.516  1.00 39.81 ?  318 LEU A C     1 
ATOM   2307 O O     . LEU A 1 312 ? -17.311 -25.463 43.097  1.00 30.55 ?  318 LEU A O     1 
ATOM   2308 C CB    . LEU A 1 312 ? -20.462 -24.753 43.448  1.00 32.06 ?  318 LEU A CB    1 
ATOM   2309 C CG    . LEU A 1 312 ? -21.774 -24.968 44.207  1.00 29.67 ?  318 LEU A CG    1 
ATOM   2310 C CD1   . LEU A 1 312 ? -22.648 -23.734 44.207  1.00 26.24 ?  318 LEU A CD1   1 
ATOM   2311 C CD2   . LEU A 1 312 ? -22.536 -26.157 43.648  1.00 29.58 ?  318 LEU A CD2   1 
ATOM   2312 N N     . GLN A 1 313 ? -18.461 -25.852 41.190  1.00 32.21 ?  319 GLN A N     1 
ATOM   2313 C CA    . GLN A 1 313 ? -17.363 -25.470 40.317  1.00 36.01 ?  319 GLN A CA    1 
ATOM   2314 C C     . GLN A 1 313 ? -17.220 -23.953 40.276  1.00 34.45 ?  319 GLN A C     1 
ATOM   2315 O O     . GLN A 1 313 ? -18.194 -23.209 40.436  1.00 29.77 ?  319 GLN A O     1 
ATOM   2316 C CB    . GLN A 1 313 ? -17.589 -26.002 38.904  1.00 35.80 ?  319 GLN A CB    1 
ATOM   2317 C CG    . GLN A 1 313 ? -17.716 -27.497 38.810  1.00 38.36 ?  319 GLN A CG    1 
ATOM   2318 C CD    . GLN A 1 313 ? -17.568 -27.986 37.389  1.00 44.94 ?  319 GLN A CD    1 
ATOM   2319 O OE1   . GLN A 1 313 ? -17.337 -27.193 36.475  1.00 43.19 ?  319 GLN A OE1   1 
ATOM   2320 N NE2   . GLN A 1 313 ? -17.626 -29.301 37.202  1.00 44.06 ?  319 GLN A NE2   1 
ATOM   2321 N N     . ALA A 1 314 ? -15.990 -23.495 40.033  1.00 37.58 ?  320 ALA A N     1 
ATOM   2322 C CA    . ALA A 1 314 ? -15.677 -22.075 40.100  1.00 35.29 ?  320 ALA A CA    1 
ATOM   2323 C C     . ALA A 1 314 ? -15.029 -21.589 38.812  1.00 37.91 ?  320 ALA A C     1 
ATOM   2324 O O     . ALA A 1 314 ? -14.113 -22.228 38.281  1.00 40.00 ?  320 ALA A O     1 
ATOM   2325 C CB    . ALA A 1 314 ? -14.758 -21.779 41.279  1.00 36.90 ?  320 ALA A CB    1 
ATOM   2326 N N     . TYR A 1 315 ? -15.497 -20.439 38.338  1.00 34.28 ?  321 TYR A N     1 
ATOM   2327 C CA    . TYR A 1 315 ? -14.954 -19.782 37.153  1.00 39.95 ?  321 TYR A CA    1 
ATOM   2328 C C     . TYR A 1 315 ? -13.824 -18.849 37.570  1.00 39.47 ?  321 TYR A C     1 
ATOM   2329 O O     . TYR A 1 315 ? -14.050 -17.914 38.341  1.00 38.21 ?  321 TYR A O     1 
ATOM   2330 C CB    . TYR A 1 315 ? -16.052 -19.001 36.429  1.00 37.21 ?  321 TYR A CB    1 
ATOM   2331 C CG    . TYR A 1 315 ? -15.547 -18.078 35.343  1.00 38.19 ?  321 TYR A CG    1 
ATOM   2332 C CD1   . TYR A 1 315 ? -14.815 -18.573 34.264  1.00 40.94 ?  321 TYR A CD1   1 
ATOM   2333 C CD2   . TYR A 1 315 ? -15.816 -16.711 35.385  1.00 38.89 ?  321 TYR A CD2   1 
ATOM   2334 C CE1   . TYR A 1 315 ? -14.350 -17.727 33.255  1.00 39.97 ?  321 TYR A CE1   1 
ATOM   2335 C CE2   . TYR A 1 315 ? -15.361 -15.856 34.383  1.00 44.71 ?  321 TYR A CE2   1 
ATOM   2336 C CZ    . TYR A 1 315 ? -14.626 -16.369 33.321  1.00 43.02 ?  321 TYR A CZ    1 
ATOM   2337 O OH    . TYR A 1 315 ? -14.170 -15.516 32.335  1.00 42.35 ?  321 TYR A OH    1 
ATOM   2338 N N     . LYS A 1 316 ? -12.618 -19.095 37.065  1.00 39.38 ?  322 LYS A N     1 
ATOM   2339 C CA    . LYS A 1 316 ? -11.477 -18.236 37.386  1.00 38.67 ?  322 LYS A CA    1 
ATOM   2340 C C     . LYS A 1 316 ? -10.839 -17.690 36.119  1.00 42.50 ?  322 LYS A C     1 
ATOM   2341 O O     . LYS A 1 316 ? -10.176 -18.450 35.387  1.00 40.98 ?  322 LYS A O     1 
ATOM   2342 C CB    . LYS A 1 316 ? -10.437 -18.985 38.216  1.00 39.77 ?  322 LYS A CB    1 
ATOM   2343 C CG    . LYS A 1 316 ? -9.565  -18.043 39.035  1.00 38.97 ?  322 LYS A CG    1 
ATOM   2344 C CD    . LYS A 1 316 ? -8.101  -18.277 38.758  1.00 42.12 ?  322 LYS A CD    1 
ATOM   2345 C CE    . LYS A 1 316 ? -7.241  -17.086 39.155  1.00 46.91 ?  322 LYS A CE    1 
ATOM   2346 N NZ    . LYS A 1 316 ? -7.324  -16.800 40.606  1.00 52.44 ?  322 LYS A NZ    1 
ATOM   2347 N N     . PRO A 1 317 ? -10.986 -16.396 35.830  1.00 40.68 ?  323 PRO A N     1 
ATOM   2348 C CA    . PRO A 1 317 ? -10.395 -15.830 34.609  1.00 41.43 ?  323 PRO A CA    1 
ATOM   2349 C C     . PRO A 1 317 ? -8.873  -15.920 34.597  1.00 39.42 ?  323 PRO A C     1 
ATOM   2350 O O     . PRO A 1 317 ? -8.211  -16.051 35.630  1.00 37.82 ?  323 PRO A O     1 
ATOM   2351 C CB    . PRO A 1 317 ? -10.850 -14.363 34.635  1.00 40.29 ?  323 PRO A CB    1 
ATOM   2352 C CG    . PRO A 1 317 ? -12.032 -14.336 35.579  1.00 43.30 ?  323 PRO A CG    1 
ATOM   2353 C CD    . PRO A 1 317 ? -11.771 -15.405 36.589  1.00 41.49 ?  323 PRO A CD    1 
ATOM   2354 N N     . GLY A 1 318 ? -8.324  -15.850 33.386  1.00 33.13 ?  324 GLY A N     1 
ATOM   2355 C CA    . GLY A 1 318 ? -6.898  -15.702 33.171  1.00 28.36 ?  324 GLY A CA    1 
ATOM   2356 C C     . GLY A 1 318 ? -6.637  -14.484 32.307  1.00 27.80 ?  324 GLY A C     1 
ATOM   2357 O O     . GLY A 1 318 ? -7.489  -13.604 32.213  1.00 18.70 ?  324 GLY A O     1 
ATOM   2358 N N     . ALA A 1 319 ? -5.473  -14.398 31.676  1.00 24.39 ?  325 ALA A N     1 
ATOM   2359 C CA    . ALA A 1 319 ? -5.214  -13.214 30.881  1.00 25.16 ?  325 ALA A CA    1 
ATOM   2360 C C     . ALA A 1 319 ? -6.133  -13.187 29.654  1.00 23.46 ?  325 ALA A C     1 
ATOM   2361 O O     . ALA A 1 319 ? -6.803  -14.168 29.318  1.00 23.92 ?  325 ALA A O     1 
ATOM   2362 C CB    . ALA A 1 319 ? -3.738  -13.157 30.492  1.00 28.79 ?  325 ALA A CB    1 
ATOM   2363 N N     . LEU A 1 320 ? -6.194  -12.025 29.017  1.00 23.63 ?  326 LEU A N     1 
ATOM   2364 C CA    . LEU A 1 320 ? -7.149  -11.790 27.935  1.00 24.85 ?  326 LEU A CA    1 
ATOM   2365 C C     . LEU A 1 320 ? -6.763  -12.577 26.680  1.00 21.31 ?  326 LEU A C     1 
ATOM   2366 O O     . LEU A 1 320 ? -5.620  -12.495 26.215  1.00 19.49 ?  326 LEU A O     1 
ATOM   2367 C CB    . LEU A 1 320 ? -7.212  -10.293 27.641  1.00 25.62 ?  326 LEU A CB    1 
ATOM   2368 C CG    . LEU A 1 320 ? -8.069  -9.768  26.491  1.00 23.25 ?  326 LEU A CG    1 
ATOM   2369 C CD1   . LEU A 1 320 ? -9.498  -10.206 26.689  1.00 22.06 ?  326 LEU A CD1   1 
ATOM   2370 C CD2   . LEU A 1 320 ? -7.969  -8.252  26.418  1.00 26.97 ?  326 LEU A CD2   1 
ATOM   2371 N N     . THR A 1 321 ? -7.696  -13.380 26.167  1.00 17.74 ?  327 THR A N     1 
ATOM   2372 C CA    . THR A 1 321 ? -7.597  -13.957 24.827  1.00 17.87 ?  327 THR A CA    1 
ATOM   2373 C C     . THR A 1 321 ? -8.545  -13.187 23.921  1.00 17.55 ?  327 THR A C     1 
ATOM   2374 O O     . THR A 1 321 ? -9.725  -13.046 24.240  1.00 13.56 ?  327 THR A O     1 
ATOM   2375 C CB    . THR A 1 321 ? -7.977  -15.443 24.793  1.00 19.99 ?  327 THR A CB    1 
ATOM   2376 O OG1   . THR A 1 321 ? -6.979  -16.232 25.459  1.00 21.58 ?  327 THR A OG1   1 
ATOM   2377 C CG2   . THR A 1 321 ? -8.088  -15.924 23.354  1.00 17.10 ?  327 THR A CG2   1 
ATOM   2378 N N     . PHE A 1 322 ? -8.045  -12.718 22.787  1.00 14.08 ?  328 PHE A N     1 
ATOM   2379 C CA    . PHE A 1 322 ? -8.877  -11.903 21.897  1.00 14.54 ?  328 PHE A CA    1 
ATOM   2380 C C     . PHE A 1 322 ? -8.243  -11.966 20.523  1.00 13.84 ?  328 PHE A C     1 
ATOM   2381 O O     . PHE A 1 322 ? -7.124  -11.479 20.349  1.00 12.91 ?  328 PHE A O     1 
ATOM   2382 C CB    . PHE A 1 322 ? -8.936  -10.451 22.400  1.00 15.76 ?  328 PHE A CB    1 
ATOM   2383 C CG    . PHE A 1 322 ? -10.094 -9.651  21.852  1.00 19.62 ?  328 PHE A CG    1 
ATOM   2384 C CD1   . PHE A 1 322 ? -10.153 -9.308  20.517  1.00 19.17 ?  328 PHE A CD1   1 
ATOM   2385 C CD2   . PHE A 1 322 ? -11.105 -9.214  22.691  1.00 22.48 ?  328 PHE A CD2   1 
ATOM   2386 C CE1   . PHE A 1 322 ? -11.215 -8.573  20.024  1.00 21.16 ?  328 PHE A CE1   1 
ATOM   2387 C CE2   . PHE A 1 322 ? -12.178 -8.480  22.199  1.00 28.75 ?  328 PHE A CE2   1 
ATOM   2388 C CZ    . PHE A 1 322 ? -12.222 -8.151  20.865  1.00 22.25 ?  328 PHE A CZ    1 
ATOM   2389 N N     . LEU A 1 323 ? -8.945  -12.547 19.561  1.00 11.12 ?  329 LEU A N     1 
ATOM   2390 C CA    . LEU A 1 323 ? -8.421  -12.766 18.217  1.00 12.26 ?  329 LEU A CA    1 
ATOM   2391 C C     . LEU A 1 323 ? -9.234  -11.951 17.224  1.00 12.60 ?  329 LEU A C     1 
ATOM   2392 O O     . LEU A 1 323 ? -10.461 -12.049 17.204  1.00 12.37 ?  329 LEU A O     1 
ATOM   2393 C CB    . LEU A 1 323 ? -8.500  -14.244 17.841  1.00 10.90 ?  329 LEU A CB    1 
ATOM   2394 C CG    . LEU A 1 323 ? -7.707  -15.179 18.763  1.00 12.53 ?  329 LEU A CG    1 
ATOM   2395 C CD1   . LEU A 1 323 ? -7.868  -16.625 18.313  1.00 15.04 ?  329 LEU A CD1   1 
ATOM   2396 C CD2   . LEU A 1 323 ? -6.223  -14.781 18.790  1.00 12.83 ?  329 LEU A CD2   1 
ATOM   2397 N N     . LEU A 1 324 ? -8.566  -11.174 16.388  1.00 11.00 ?  330 LEU A N     1 
ATOM   2398 C CA    . LEU A 1 324 ? -9.260  -10.388 15.371  1.00 12.05 ?  330 LEU A CA    1 
ATOM   2399 C C     . LEU A 1 324 ? -8.947  -10.962 14.003  1.00 11.18 ?  330 LEU A C     1 
ATOM   2400 O O     . LEU A 1 324 ? -7.800  -10.916 13.566  1.00 12.81 ?  330 LEU A O     1 
ATOM   2401 C CB    . LEU A 1 324 ? -8.834  -8.923  15.427  1.00 12.35 ?  330 LEU A CB    1 
ATOM   2402 C CG    . LEU A 1 324 ? -9.179  -8.235  16.740  1.00 17.07 ?  330 LEU A CG    1 
ATOM   2403 C CD1   . LEU A 1 324 ? -7.936  -8.050  17.613  1.00 18.49 ?  330 LEU A CD1   1 
ATOM   2404 C CD2   . LEU A 1 324 ? -9.851  -6.898  16.425  1.00 20.10 ?  330 LEU A CD2   1 
ATOM   2405 N N     . SER A 1 325 ? -9.958  -11.480 13.315  1.00 12.25 ?  331 SER A N     1 
ATOM   2406 C CA    . SER A 1 325 ? -9.718  -11.860 11.933  1.00 11.56 ?  331 SER A CA    1 
ATOM   2407 C C     . SER A 1 325 ? -9.677  -10.594 11.081  1.00 17.31 ?  331 SER A C     1 
ATOM   2408 O O     . SER A 1 325 ? -10.373 -9.613  11.350  1.00 19.61 ?  331 SER A O     1 
ATOM   2409 C CB    . SER A 1 325 ? -10.808 -12.798 11.433  1.00 16.27 ?  331 SER A CB    1 
ATOM   2410 O OG    . SER A 1 325 ? -12.020 -12.078 11.392  1.00 27.55 ?  331 SER A OG    1 
ATOM   2411 N N     . MET A 1 326 ? -8.819  -10.595 10.091  1.00 12.59 ?  332 MET A N     1 
ATOM   2412 C CA    . MET A 1 326 ? -8.655  -9.448  9.204   1.00 11.88 ?  332 MET A CA    1 
ATOM   2413 C C     . MET A 1 326 ? -8.851  -9.961  7.782   1.00 11.31 ?  332 MET A C     1 
ATOM   2414 O O     . MET A 1 326 ? -7.894  -10.043 7.004   1.00 12.80 ?  332 MET A O     1 
ATOM   2415 C CB    . MET A 1 326 ? -7.270  -8.807  9.388   1.00 15.62 ?  332 MET A CB    1 
ATOM   2416 C CG    . MET A 1 326 ? -6.993  -8.231  10.763  1.00 19.01 ?  332 MET A CG    1 
ATOM   2417 S SD    . MET A 1 326 ? -7.440  -6.491  10.801  1.00 32.27 ?  332 MET A SD    1 
ATOM   2418 C CE    . MET A 1 326 ? -9.030  -6.692  11.576  1.00 13.92 ?  332 MET A CE    1 
ATOM   2419 N N     . GLY A 1 327 ? -10.073 -10.376 7.465   1.00 9.33  ?  333 GLY A N     1 
ATOM   2420 C CA    . GLY A 1 327 ? -10.307 -11.150 6.261   1.00 9.14  ?  333 GLY A CA    1 
ATOM   2421 C C     . GLY A 1 327 ? -9.826  -12.583 6.430   1.00 10.27 ?  333 GLY A C     1 
ATOM   2422 O O     . GLY A 1 327 ? -9.222  -12.967 7.438   1.00 10.50 ?  333 GLY A O     1 
ATOM   2423 N N     . ARG A 1 328 ? -10.108 -13.398 5.420   1.00 8.91  ?  334 ARG A N     1 
ATOM   2424 C CA    . ARG A 1 328 ? -9.808  -14.821 5.568   1.00 9.24  ?  334 ARG A CA    1 
ATOM   2425 C C     . ARG A 1 328 ? -8.314  -15.130 5.548   1.00 10.13 ?  334 ARG A C     1 
ATOM   2426 O O     . ARG A 1 328 ? -7.924  -16.248 5.913   1.00 9.94  ?  334 ARG A O     1 
ATOM   2427 C CB    . ARG A 1 328 ? -10.513 -15.619 4.473   1.00 9.26  ?  334 ARG A CB    1 
ATOM   2428 C CG    . ARG A 1 328 ? -9.942  -15.450 3.067   1.00 12.27 ?  334 ARG A CG    1 
ATOM   2429 C CD    . ARG A 1 328 ? -10.671 -16.320 2.033   1.00 13.17 ?  334 ARG A CD    1 
ATOM   2430 N NE    . ARG A 1 328 ? -12.063 -15.910 1.832   1.00 14.31 ?  334 ARG A NE    1 
ATOM   2431 C CZ    . ARG A 1 328 ? -13.123 -16.593 2.252   1.00 17.70 ?  334 ARG A CZ    1 
ATOM   2432 N NH1   . ARG A 1 328 ? -12.996 -17.744 2.905   1.00 16.78 ?  334 ARG A NH1   1 
ATOM   2433 N NH2   . ARG A 1 328 ? -14.345 -16.118 2.001   1.00 14.94 ?  334 ARG A NH2   1 
ATOM   2434 N N     . ASN A 1 329 ? -7.468  -14.184 5.143   1.00 9.74  ?  335 ASN A N     1 
ATOM   2435 C CA    . ASN A 1 329 ? -6.045  -14.468 4.986   1.00 10.57 ?  335 ASN A CA    1 
ATOM   2436 C C     . ASN A 1 329 ? -5.157  -13.755 6.010   1.00 13.98 ?  335 ASN A C     1 
ATOM   2437 O O     . ASN A 1 329 ? -3.935  -13.763 5.852   1.00 10.83 ?  335 ASN A O     1 
ATOM   2438 C CB    . ASN A 1 329 ? -5.590  -14.100 3.567   1.00 11.09 ?  335 ASN A CB    1 
ATOM   2439 C CG    . ASN A 1 329 ? -5.727  -12.615 3.285   1.00 14.26 ?  335 ASN A CG    1 
ATOM   2440 O OD1   . ASN A 1 329 ? -6.303  -11.881 4.075   1.00 10.42 ?  335 ASN A OD1   1 
ATOM   2441 N ND2   . ASN A 1 329 ? -5.221  -12.169 2.138   1.00 15.46 ?  335 ASN A ND2   1 
ATOM   2442 N N     . ASP A 1 330 ? -5.717  -13.153 7.054   1.00 10.71 ?  336 ASP A N     1 
ATOM   2443 C CA    . ASP A 1 330 ? -4.905  -12.305 7.930   1.00 11.87 ?  336 ASP A CA    1 
ATOM   2444 C C     . ASP A 1 330 ? -5.594  -12.193 9.282   1.00 11.99 ?  336 ASP A C     1 
ATOM   2445 O O     . ASP A 1 330 ? -6.720  -12.655 9.470   1.00 11.05 ?  336 ASP A O     1 
ATOM   2446 C CB    . ASP A 1 330 ? -4.696  -10.909 7.312   1.00 13.91 ?  336 ASP A CB    1 
ATOM   2447 C CG    . ASP A 1 330 ? -3.274  -10.344 7.548   1.00 18.66 ?  336 ASP A CG    1 
ATOM   2448 O OD1   . ASP A 1 330 ? -2.622  -10.732 8.542   1.00 17.08 ?  336 ASP A OD1   1 
ATOM   2449 O OD2   . ASP A 1 330 ? -2.808  -9.502  6.728   1.00 16.51 -1 336 ASP A OD2   1 
ATOM   2450 N N     . GLY A 1 331 ? -4.914  -11.550 10.216  1.00 14.69 ?  337 GLY A N     1 
ATOM   2451 C CA    . GLY A 1 331 ? -5.472  -11.354 11.540  1.00 13.33 ?  337 GLY A CA    1 
ATOM   2452 C C     . GLY A 1 331 ? -4.373  -11.092 12.540  1.00 10.89 ?  337 GLY A C     1 
ATOM   2453 O O     . GLY A 1 331 ? -3.190  -11.215 12.245  1.00 12.85 ?  337 GLY A O     1 
ATOM   2454 N N     . VAL A 1 332 ? -4.780  -10.702 13.744  1.00 10.45 ?  338 VAL A N     1 
ATOM   2455 C CA    . VAL A 1 332 ? -3.820  -10.511 14.827  1.00 10.03 ?  338 VAL A CA    1 
ATOM   2456 C C     . VAL A 1 332 ? -4.585  -10.593 16.136  1.00 10.93 ?  338 VAL A C     1 
ATOM   2457 O O     . VAL A 1 332 ? -5.804  -10.508 16.161  1.00 10.15 ?  338 VAL A O     1 
ATOM   2458 C CB    . VAL A 1 332 ? -3.051  -9.176  14.660  1.00 15.84 ?  338 VAL A CB    1 
ATOM   2459 C CG1   . VAL A 1 332 ? -3.983  -7.986  14.792  1.00 13.02 ?  338 VAL A CG1   1 
ATOM   2460 C CG2   . VAL A 1 332 ? -1.897  -9.097  15.666  1.00 15.83 ?  338 VAL A CG2   1 
ATOM   2461 N N     . GLY A 1 333 ? -3.879  -10.816 17.235  1.00 13.40 ?  339 GLY A N     1 
ATOM   2462 C CA    . GLY A 1 333 ? -4.584  -10.860 18.495  1.00 11.94 ?  339 GLY A CA    1 
ATOM   2463 C C     . GLY A 1 333 ? -3.671  -11.244 19.629  1.00 14.64 ?  339 GLY A C     1 
ATOM   2464 O O     . GLY A 1 333 ? -2.451  -11.085 19.543  1.00 14.65 ?  339 GLY A O     1 
ATOM   2465 N N     . GLN A 1 334 ? -4.285  -11.744 20.693  1.00 12.86 ?  340 GLN A N     1 
ATOM   2466 C CA    . GLN A 1 334 ? -3.551  -12.207 21.862  1.00 16.63 ?  340 GLN A CA    1 
ATOM   2467 C C     . GLN A 1 334 ? -4.227  -13.444 22.442  1.00 18.63 ?  340 GLN A C     1 
ATOM   2468 O O     . GLN A 1 334 ? -5.457  -13.548 22.445  1.00 14.88 ?  340 GLN A O     1 
ATOM   2469 C CB    . GLN A 1 334 ? -3.446  -11.106 22.922  1.00 16.33 ?  340 GLN A CB    1 
ATOM   2470 C CG    . GLN A 1 334 ? -4.752  -10.524 23.390  1.00 16.98 ?  340 GLN A CG    1 
ATOM   2471 C CD    . GLN A 1 334 ? -4.513  -9.281  24.242  1.00 22.03 ?  340 GLN A CD    1 
ATOM   2472 O OE1   . GLN A 1 334 ? -4.284  -8.190  23.718  1.00 22.95 ?  340 GLN A OE1   1 
ATOM   2473 N NE2   . GLN A 1 334 ? -4.520  -9.455  25.556  1.00 22.09 ?  340 GLN A NE2   1 
ATOM   2474 N N     . ILE A 1 335 ? -3.418  -14.392 22.909  1.00 17.19 ?  341 ILE A N     1 
ATOM   2475 C CA    . ILE A 1 335 ? -3.916  -15.609 23.541  1.00 21.15 ?  341 ILE A CA    1 
ATOM   2476 C C     . ILE A 1 335 ? -3.420  -15.607 24.976  1.00 22.94 ?  341 ILE A C     1 
ATOM   2477 O O     . ILE A 1 335 ? -2.205  -15.573 25.216  1.00 25.09 ?  341 ILE A O     1 
ATOM   2478 C CB    . ILE A 1 335 ? -3.473  -16.878 22.795  1.00 21.55 ?  341 ILE A CB    1 
ATOM   2479 C CG1   . ILE A 1 335 ? -4.180  -16.973 21.437  1.00 19.83 ?  341 ILE A CG1   1 
ATOM   2480 C CG2   . ILE A 1 335 ? -3.769  -18.127 23.630  1.00 25.14 ?  341 ILE A CG2   1 
ATOM   2481 C CD1   . ILE A 1 335 ? -3.742  -18.162 20.613  1.00 21.90 ?  341 ILE A CD1   1 
ATOM   2482 N N     . SER A 1 336 ? -4.362  -15.627 25.923  1.00 22.26 ?  342 SER A N     1 
ATOM   2483 C CA    . SER A 1 336 ? -4.129  -15.362 27.341  1.00 26.72 ?  342 SER A CA    1 
ATOM   2484 C C     . SER A 1 336 ? -2.989  -14.377 27.598  1.00 28.31 ?  342 SER A C     1 
ATOM   2485 O O     . SER A 1 336 ? -2.003  -14.712 28.262  1.00 27.34 ?  342 SER A O     1 
ATOM   2486 C CB    . SER A 1 336 ? -3.869  -16.669 28.100  1.00 31.17 ?  342 SER A CB    1 
ATOM   2487 O OG    . SER A 1 336 ? -2.874  -17.427 27.448  1.00 35.57 ?  342 SER A OG    1 
ATOM   2488 N N     . GLY A 1 337 ? -3.119  -13.160 27.087  1.00 25.77 ?  343 GLY A N     1 
ATOM   2489 C CA    . GLY A 1 337 ? -2.268  -12.066 27.501  1.00 26.03 ?  343 GLY A CA    1 
ATOM   2490 C C     . GLY A 1 337 ? -0.985  -11.878 26.730  1.00 27.11 ?  343 GLY A C     1 
ATOM   2491 O O     . GLY A 1 337 ? -0.256  -10.920 27.007  1.00 29.84 ?  343 GLY A O     1 
ATOM   2492 N N     . PHE A 1 338 ? -0.673  -12.726 25.765  1.00 24.39 ?  344 PHE A N     1 
ATOM   2493 C CA    . PHE A 1 338 ? 0.481   -12.437 24.935  1.00 28.04 ?  344 PHE A CA    1 
ATOM   2494 C C     . PHE A 1 338 ? 0.117   -12.394 23.457  1.00 23.77 ?  344 PHE A C     1 
ATOM   2495 O O     . PHE A 1 338 ? -0.806  -13.073 22.989  1.00 21.15 ?  344 PHE A O     1 
ATOM   2496 C CB    . PHE A 1 338 ? 1.604   -13.431 25.165  1.00 31.00 ?  344 PHE A CB    1 
ATOM   2497 C CG    . PHE A 1 338 ? 1.160   -14.840 25.162  1.00 32.21 ?  344 PHE A CG    1 
ATOM   2498 C CD1   . PHE A 1 338 ? 0.962   -15.511 23.967  1.00 29.07 ?  344 PHE A CD1   1 
ATOM   2499 C CD2   . PHE A 1 338 ? 0.951   -15.505 26.357  1.00 27.45 ?  344 PHE A CD2   1 
ATOM   2500 C CE1   . PHE A 1 338 ? 0.552   -16.826 23.967  1.00 31.39 ?  344 PHE A CE1   1 
ATOM   2501 C CE2   . PHE A 1 338 ? 0.543   -16.809 26.368  1.00 30.39 ?  344 PHE A CE2   1 
ATOM   2502 C CZ    . PHE A 1 338 ? 0.347   -17.482 25.179  1.00 32.21 ?  344 PHE A CZ    1 
ATOM   2503 N N     . TYR A 1 339 ? 0.902   -11.607 22.736  1.00 22.66 ?  345 TYR A N     1 
ATOM   2504 C CA    . TYR A 1 339 ? 0.690   -11.362 21.318  1.00 19.78 ?  345 TYR A CA    1 
ATOM   2505 C C     . TYR A 1 339 ? 0.790   -12.644 20.507  1.00 19.34 ?  345 TYR A C     1 
ATOM   2506 O O     . TYR A 1 339 ? 1.726   -13.429 20.673  1.00 17.22 ?  345 TYR A O     1 
ATOM   2507 C CB    . TYR A 1 339 ? 1.741   -10.373 20.842  1.00 19.40 ?  345 TYR A CB    1 
ATOM   2508 C CG    . TYR A 1 339 ? 1.663   -9.959  19.395  1.00 20.46 ?  345 TYR A CG    1 
ATOM   2509 C CD1   . TYR A 1 339 ? 2.319   -10.673 18.397  1.00 20.11 ?  345 TYR A CD1   1 
ATOM   2510 C CD2   . TYR A 1 339 ? 0.967   -8.819  19.033  1.00 20.41 ?  345 TYR A CD2   1 
ATOM   2511 C CE1   . TYR A 1 339 ? 2.262   -10.254 17.062  1.00 20.86 ?  345 TYR A CE1   1 
ATOM   2512 C CE2   . TYR A 1 339 ? 0.916   -8.391  17.718  1.00 23.32 ?  345 TYR A CE2   1 
ATOM   2513 C CZ    . TYR A 1 339 ? 1.557   -9.111  16.739  1.00 23.29 ?  345 TYR A CZ    1 
ATOM   2514 O OH    . TYR A 1 339 ? 1.477   -8.653  15.435  1.00 24.96 ?  345 TYR A OH    1 
ATOM   2515 N N     . VAL A 1 340 ? -0.155  -12.835 19.591  1.00 16.86 ?  346 VAL A N     1 
ATOM   2516 C CA    . VAL A 1 340 ? -0.021  -13.886 18.599  1.00 16.62 ?  346 VAL A CA    1 
ATOM   2517 C C     . VAL A 1 340 ? -0.177  -13.248 17.227  1.00 16.99 ?  346 VAL A C     1 
ATOM   2518 O O     . VAL A 1 340 ? -0.943  -12.293 17.042  1.00 16.96 ?  346 VAL A O     1 
ATOM   2519 C CB    . VAL A 1 340 ? -1.028  -15.033 18.812  1.00 18.94 ?  346 VAL A CB    1 
ATOM   2520 C CG1   . VAL A 1 340 ? -0.748  -15.732 20.146  1.00 18.91 ?  346 VAL A CG1   1 
ATOM   2521 C CG2   . VAL A 1 340 ? -2.439  -14.517 18.769  1.00 16.78 ?  346 VAL A CG2   1 
ATOM   2522 N N     . GLY A 1 341 ? 0.567   -13.774 16.269  1.00 18.30 ?  347 GLY A N     1 
ATOM   2523 C CA    . GLY A 1 341 ? 0.731   -13.141 14.979  1.00 17.62 ?  347 GLY A CA    1 
ATOM   2524 C C     . GLY A 1 341 ? -0.286  -13.550 13.935  1.00 17.72 ?  347 GLY A C     1 
ATOM   2525 O O     . GLY A 1 341 ? -1.319  -14.156 14.224  1.00 17.59 ?  347 GLY A O     1 
ATOM   2526 N N     . ARG A 1 342 ? 0.043   -13.241 12.686  1.00 15.87 ?  348 ARG A N     1 
ATOM   2527 C CA    . ARG A 1 342 ? -0.932  -13.313 11.605  1.00 15.79 ?  348 ARG A CA    1 
ATOM   2528 C C     . ARG A 1 342 ? -1.151  -14.745 11.140  1.00 15.75 ?  348 ARG A C     1 
ATOM   2529 O O     . ARG A 1 342 ? -2.294  -15.152 10.895  1.00 13.41 ?  348 ARG A O     1 
ATOM   2530 C CB    . ARG A 1 342 ? -0.475  -12.404 10.464  1.00 14.13 ?  348 ARG A CB    1 
ATOM   2531 C CG    . ARG A 1 342 ? -0.244  -10.983 10.971  1.00 18.32 ?  348 ARG A CG    1 
ATOM   2532 C CD    . ARG A 1 342 ? 0.654   -10.179 10.071  1.00 18.03 ?  348 ARG A CD    1 
ATOM   2533 N NE    . ARG A 1 342 ? -0.000  -9.823  8.816   1.00 14.77 ?  348 ARG A NE    1 
ATOM   2534 C CZ    . ARG A 1 342 ? 0.588   -9.092  7.880   1.00 18.65 ?  348 ARG A CZ    1 
ATOM   2535 N NH1   . ARG A 1 342 ? 1.824   -8.649  8.035   1.00 19.21 ?  348 ARG A NH1   1 
ATOM   2536 N NH2   . ARG A 1 342 ? -0.081  -8.787  6.768   1.00 17.43 ?  348 ARG A NH2   1 
ATOM   2537 N N     . LEU A 1 343 ? -0.078  -15.527 11.023  1.00 13.44 ?  349 LEU A N     1 
ATOM   2538 C CA    . LEU A 1 343 ? -0.237  -16.939 10.694  1.00 15.41 ?  349 LEU A CA    1 
ATOM   2539 C C     . LEU A 1 343 ? -1.080  -17.650 11.743  1.00 16.46 ?  349 LEU A C     1 
ATOM   2540 O O     . LEU A 1 343 ? -2.007  -18.401 11.410  1.00 13.89 ?  349 LEU A O     1 
ATOM   2541 C CB    . LEU A 1 343 ? 1.135   -17.600 10.572  1.00 18.46 ?  349 LEU A CB    1 
ATOM   2542 C CG    . LEU A 1 343 ? 1.096   -19.122 10.410  1.00 20.42 ?  349 LEU A CG    1 
ATOM   2543 C CD1   . LEU A 1 343 ? 0.307   -19.507 9.183   1.00 23.48 ?  349 LEU A CD1   1 
ATOM   2544 C CD2   . LEU A 1 343 ? 2.508   -19.651 10.316  1.00 32.61 ?  349 LEU A CD2   1 
ATOM   2545 N N     . MET A 1 344 ? -0.778  -17.409 13.026  1.00 12.94 ?  350 MET A N     1 
ATOM   2546 C CA    . MET A 1 344 ? -1.526  -18.047 14.107  1.00 14.93 ?  350 MET A CA    1 
ATOM   2547 C C     . MET A 1 344 ? -3.009  -17.683 14.048  1.00 13.93 ?  350 MET A C     1 
ATOM   2548 O O     . MET A 1 344 ? -3.880  -18.551 14.154  1.00 12.60 ?  350 MET A O     1 
ATOM   2549 C CB    . MET A 1 344 ? -0.919  -17.643 15.454  1.00 16.89 ?  350 MET A CB    1 
ATOM   2550 C CG    . MET A 1 344 ? -1.585  -18.280 16.654  1.00 18.35 ?  350 MET A CG    1 
ATOM   2551 S SD    . MET A 1 344 ? -1.575  -20.086 16.515  1.00 31.01 ?  350 MET A SD    1 
ATOM   2552 C CE    . MET A 1 344 ? -2.401  -20.568 18.045  1.00 35.44 ?  350 MET A CE    1 
ATOM   2553 N N     . VAL A 1 345 ? -3.323  -16.402 13.891  1.00 11.74 ?  351 VAL A N     1 
ATOM   2554 C CA    . VAL A 1 345 ? -4.734  -16.022 13.900  1.00 11.45 ?  351 VAL A CA    1 
ATOM   2555 C C     . VAL A 1 345 ? -5.432  -16.518 12.641  1.00 11.29 ?  351 VAL A C     1 
ATOM   2556 O O     . VAL A 1 345 ? -6.582  -16.980 12.695  1.00 11.03 ?  351 VAL A O     1 
ATOM   2557 C CB    . VAL A 1 345 ? -4.880  -14.503 14.079  1.00 13.26 ?  351 VAL A CB    1 
ATOM   2558 C CG1   . VAL A 1 345 ? -6.364  -14.090 13.996  1.00 11.15 ?  351 VAL A CG1   1 
ATOM   2559 C CG2   . VAL A 1 345 ? -4.286  -14.086 15.435  1.00 14.17 ?  351 VAL A CG2   1 
ATOM   2560 N N     . ARG A 1 346 ? -4.755  -16.440 11.489  1.00 10.73 ?  352 ARG A N     1 
ATOM   2561 C CA    . ARG A 1 346 ? -5.369  -16.956 10.264  1.00 11.24 ?  352 ARG A CA    1 
ATOM   2562 C C     . ARG A 1 346 ? -5.775  -18.422 10.423  1.00 10.95 ?  352 ARG A C     1 
ATOM   2563 O O     . ARG A 1 346 ? -6.902  -18.810 10.087  1.00 11.83 ?  352 ARG A O     1 
ATOM   2564 C CB    . ARG A 1 346 ? -4.424  -16.774 9.068   1.00 13.07 ?  352 ARG A CB    1 
ATOM   2565 C CG    . ARG A 1 346 ? -4.949  -17.434 7.810   1.00 11.83 ?  352 ARG A CG    1 
ATOM   2566 C CD    . ARG A 1 346 ? -4.125  -17.078 6.589   1.00 13.11 ?  352 ARG A CD    1 
ATOM   2567 N NE    . ARG A 1 346 ? -2.761  -17.574 6.715   1.00 13.35 ?  352 ARG A NE    1 
ATOM   2568 C CZ    . ARG A 1 346 ? -1.679  -16.808 6.737   1.00 15.16 ?  352 ARG A CZ    1 
ATOM   2569 N NH1   . ARG A 1 346 ? -1.760  -15.492 6.634   1.00 11.87 ?  352 ARG A NH1   1 
ATOM   2570 N NH2   . ARG A 1 346 ? -0.485  -17.381 6.883   1.00 13.21 ?  352 ARG A NH2   1 
ATOM   2571 N N     . LEU A 1 347 ? -4.882  -19.249 10.966  1.00 11.44 ?  353 LEU A N     1 
ATOM   2572 C CA    . LEU A 1 347 ? -5.196  -20.664 11.119  1.00 12.95 ?  353 LEU A CA    1 
ATOM   2573 C C     . LEU A 1 347 ? -6.235  -20.900 12.213  1.00 13.85 ?  353 LEU A C     1 
ATOM   2574 O O     . LEU A 1 347 ? -7.126  -21.747 12.058  1.00 15.67 ?  353 LEU A O     1 
ATOM   2575 C CB    . LEU A 1 347 ? -3.929  -21.465 11.434  1.00 15.65 ?  353 LEU A CB    1 
ATOM   2576 C CG    . LEU A 1 347 ? -2.889  -21.509 10.305  1.00 21.40 ?  353 LEU A CG    1 
ATOM   2577 C CD1   . LEU A 1 347 ? -1.663  -22.335 10.722  1.00 25.95 ?  353 LEU A CD1   1 
ATOM   2578 C CD2   . LEU A 1 347 ? -3.509  -22.056 9.029   1.00 25.04 ?  353 LEU A CD2   1 
ATOM   2579 N N     . THR A 1 348 ? -6.139  -20.173 13.322  1.00 11.36 ?  354 THR A N     1 
ATOM   2580 C CA    . THR A 1 348 ? -7.012  -20.450 14.459  1.00 13.30 ?  354 THR A CA    1 
ATOM   2581 C C     . THR A 1 348 ? -8.428  -19.941 14.223  1.00 12.55 ?  354 THR A C     1 
ATOM   2582 O O     . THR A 1 348 ? -9.406  -20.627 14.559  1.00 11.04 ?  354 THR A O     1 
ATOM   2583 C CB    . THR A 1 348 ? -6.430  -19.815 15.721  1.00 14.71 ?  354 THR A CB    1 
ATOM   2584 O OG1   . THR A 1 348 ? -5.105  -20.313 15.926  1.00 15.11 ?  354 THR A OG1   1 
ATOM   2585 C CG2   . THR A 1 348 ? -7.257  -20.148 16.929  1.00 14.92 ?  354 THR A CG2   1 
ATOM   2586 N N     . LYS A 1 349 ? -8.560  -18.746 13.654  1.00 10.80 ?  355 LYS A N     1 
ATOM   2587 C CA    . LYS A 1 349 ? -9.855  -18.088 13.538  1.00 10.02 ?  355 LYS A CA    1 
ATOM   2588 C C     . LYS A 1 349 ? -10.230 -17.702 12.112  1.00 9.74  ?  355 LYS A C     1 
ATOM   2589 O O     . LYS A 1 349 ? -11.352 -17.983 11.685  1.00 10.02 ?  355 LYS A O     1 
ATOM   2590 C CB    . LYS A 1 349 ? -9.893  -16.829 14.408  1.00 10.03 ?  355 LYS A CB    1 
ATOM   2591 C CG    . LYS A 1 349 ? -11.237 -16.140 14.315  1.00 12.70 ?  355 LYS A CG    1 
ATOM   2592 C CD    . LYS A 1 349 ? -11.292 -14.831 15.087  1.00 13.21 ?  355 LYS A CD    1 
ATOM   2593 C CE    . LYS A 1 349 ? -12.711 -14.260 14.977  1.00 15.68 ?  355 LYS A CE    1 
ATOM   2594 N NZ    . LYS A 1 349 ? -12.871 -13.028 15.792  1.00 17.96 ?  355 LYS A NZ    1 
ATOM   2595 N N     . SER A 1 350 ? -9.339  -17.035 11.366  1.00 9.79  ?  356 SER A N     1 
ATOM   2596 C CA    . SER A 1 350 ? -9.791  -16.332 10.163  1.00 9.54  ?  356 SER A CA    1 
ATOM   2597 C C     . SER A 1 350 ? -10.332 -17.273 9.101   1.00 9.60  ?  356 SER A C     1 
ATOM   2598 O O     . SER A 1 350 ? -11.259 -16.903 8.376   1.00 9.44  ?  356 SER A O     1 
ATOM   2599 C CB    . SER A 1 350 ? -8.668  -15.493 9.555   1.00 9.76  ?  356 SER A CB    1 
ATOM   2600 O OG    . SER A 1 350 ? -8.103  -14.633 10.520  1.00 11.29 ?  356 SER A OG    1 
ATOM   2601 N N     . ARG A 1 351 ? -9.780  -18.485 8.985   1.00 11.15 ?  357 ARG A N     1 
ATOM   2602 C CA    . ARG A 1 351 ? -10.163 -19.346 7.869   1.00 15.30 ?  357 ARG A CA    1 
ATOM   2603 C C     . ARG A 1 351 ? -11.583 -19.854 8.026   1.00 16.47 ?  357 ARG A C     1 
ATOM   2604 O O     . ARG A 1 351 ? -12.378 -19.806 7.070   1.00 11.61 ?  357 ARG A O     1 
ATOM   2605 C CB    . ARG A 1 351 ? -9.197  -20.527 7.750   1.00 22.05 ?  357 ARG A CB    1 
ATOM   2606 C CG    . ARG A 1 351 ? -7.858  -20.140 7.152   1.00 26.00 ?  357 ARG A CG    1 
ATOM   2607 C CD    . ARG A 1 351 ? -6.934  -21.343 6.920   1.00 40.66 ?  357 ARG A CD    1 
ATOM   2608 N NE    . ARG A 1 351 ? -7.421  -22.261 5.895   1.00 55.78 ?  357 ARG A NE    1 
ATOM   2609 C CZ    . ARG A 1 351 ? -8.149  -23.344 6.138   1.00 65.28 ?  357 ARG A CZ    1 
ATOM   2610 N NH1   . ARG A 1 351 ? -8.516  -23.674 7.367   1.00 62.29 ?  357 ARG A NH1   1 
ATOM   2611 N NH2   . ARG A 1 351 ? -8.518  -24.120 5.122   1.00 64.02 ?  357 ARG A NH2   1 
ATOM   2612 N N     . ASP A 1 352 ? -11.919 -20.332 9.234   1.00 11.08 ?  358 ASP A N     1 
ATOM   2613 C CA    . ASP A 1 352 ? -13.170 -21.029 9.482   1.00 15.88 ?  358 ASP A CA    1 
ATOM   2614 C C     . ASP A 1 352 ? -14.094 -20.326 10.463  1.00 12.89 ?  358 ASP A C     1 
ATOM   2615 O O     . ASP A 1 352 ? -15.264 -20.715 10.545  1.00 9.79  ?  358 ASP A O     1 
ATOM   2616 C CB    . ASP A 1 352 ? -12.902 -22.443 10.015  1.00 17.52 ?  358 ASP A CB    1 
ATOM   2617 N N     . LEU A 1 353 ? -13.608 -19.315 11.193  1.00 9.78  ?  359 LEU A N     1 
ATOM   2618 C CA    . LEU A 1 353 ? -14.392 -18.527 12.158  1.00 10.54 ?  359 LEU A CA    1 
ATOM   2619 C C     . LEU A 1 353 ? -15.131 -19.420 13.157  1.00 10.76 ?  359 LEU A C     1 
ATOM   2620 O O     . LEU A 1 353 ? -16.215 -19.082 13.619  1.00 10.20 ?  359 LEU A O     1 
ATOM   2621 C CB    . LEU A 1 353 ? -15.363 -17.573 11.437  1.00 9.54  ?  359 LEU A CB    1 
ATOM   2622 C CG    . LEU A 1 353 ? -14.673 -16.506 10.585  1.00 10.15 ?  359 LEU A CG    1 
ATOM   2623 C CD1   . LEU A 1 353 ? -15.669 -15.868 9.610   1.00 11.41 ?  359 LEU A CD1   1 
ATOM   2624 C CD2   . LEU A 1 353 ? -14.019 -15.424 11.459  1.00 11.42 ?  359 LEU A CD2   1 
ATOM   2625 N N     . PHE A 1 354 ? -14.538 -20.560 13.507  1.00 9.80  ?  360 PHE A N     1 
ATOM   2626 C CA    . PHE A 1 354 ? -15.057 -21.507 14.497  1.00 11.17 ?  360 PHE A CA    1 
ATOM   2627 C C     . PHE A 1 354 ? -16.415 -22.114 14.118  1.00 13.49 ?  360 PHE A C     1 
ATOM   2628 O O     . PHE A 1 354 ? -17.085 -22.716 14.976  1.00 11.53 ?  360 PHE A O     1 
ATOM   2629 C CB    . PHE A 1 354 ? -15.147 -20.860 15.893  1.00 12.03 ?  360 PHE A CB    1 
ATOM   2630 C CG    . PHE A 1 354 ? -13.891 -20.157 16.312  1.00 12.91 ?  360 PHE A CG    1 
ATOM   2631 C CD1   . PHE A 1 354 ? -12.716 -20.871 16.496  1.00 11.77 ?  360 PHE A CD1   1 
ATOM   2632 C CD2   . PHE A 1 354 ? -13.885 -18.788 16.534  1.00 13.17 ?  360 PHE A CD2   1 
ATOM   2633 C CE1   . PHE A 1 354 ? -11.540 -20.229 16.892  1.00 12.38 ?  360 PHE A CE1   1 
ATOM   2634 C CE2   . PHE A 1 354 ? -12.712 -18.124 16.931  1.00 13.17 ?  360 PHE A CE2   1 
ATOM   2635 C CZ    . PHE A 1 354 ? -11.537 -18.844 17.112  1.00 14.37 ?  360 PHE A CZ    1 
ATOM   2636 N N     . VAL A 1 355 ? -16.823 -22.014 12.853  1.00 12.14 ?  361 VAL A N     1 
ATOM   2637 C CA    . VAL A 1 355 ? -18.162 -22.446 12.454  1.00 11.84 ?  361 VAL A CA    1 
ATOM   2638 C C     . VAL A 1 355 ? -18.383 -23.924 12.779  1.00 16.41 ?  361 VAL A C     1 
ATOM   2639 O O     . VAL A 1 355 ? -19.448 -24.311 13.284  1.00 13.38 ?  361 VAL A O     1 
ATOM   2640 C CB    . VAL A 1 355 ? -18.393 -22.141 10.959  1.00 13.81 ?  361 VAL A CB    1 
ATOM   2641 C CG1   . VAL A 1 355 ? -19.678 -22.794 10.462  1.00 15.32 ?  361 VAL A CG1   1 
ATOM   2642 C CG2   . VAL A 1 355 ? -18.462 -20.620 10.734  1.00 13.06 ?  361 VAL A CG2   1 
ATOM   2643 N N     . SER A 1 356 ? -17.389 -24.772 12.517  1.00 16.96 ?  362 SER A N     1 
ATOM   2644 C CA    . SER A 1 356 ? -17.608 -26.206 12.706  1.00 17.62 ?  362 SER A CA    1 
ATOM   2645 C C     . SER A 1 356 ? -17.936 -26.554 14.160  1.00 17.70 ?  362 SER A C     1 
ATOM   2646 O O     . SER A 1 356 ? -18.635 -27.545 14.416  1.00 17.28 ?  362 SER A O     1 
ATOM   2647 C CB    . SER A 1 356 ? -16.381 -26.990 12.240  1.00 21.44 ?  362 SER A CB    1 
ATOM   2648 O OG    . SER A 1 356 ? -15.290 -26.740 13.103  1.00 25.32 ?  362 SER A OG    1 
ATOM   2649 N N     . THR A 1 357 ? -17.448 -25.765 15.126  1.00 14.40 ?  363 THR A N     1 
ATOM   2650 C CA    . THR A 1 357 ? -17.703 -26.087 16.534  1.00 16.04 ?  363 THR A CA    1 
ATOM   2651 C C     . THR A 1 357 ? -19.193 -26.004 16.881  1.00 16.88 ?  363 THR A C     1 
ATOM   2652 O O     . THR A 1 357 ? -19.667 -26.742 17.743  1.00 15.05 ?  363 THR A O     1 
ATOM   2653 C CB    . THR A 1 357 ? -16.890 -25.166 17.460  1.00 19.58 ?  363 THR A CB    1 
ATOM   2654 O OG1   . THR A 1 357 ? -17.359 -23.812 17.339  1.00 18.46 ?  363 THR A OG1   1 
ATOM   2655 C CG2   . THR A 1 357 ? -15.392 -25.204 17.105  1.00 19.44 ?  363 THR A CG2   1 
ATOM   2656 N N     . SER A 1 358 ? -19.947 -25.126 16.229  1.00 10.87 ?  364 SER A N     1 
ATOM   2657 C CA    . SER A 1 358 ? -21.361 -25.006 16.560  1.00 13.52 ?  364 SER A CA    1 
ATOM   2658 C C     . SER A 1 358 ? -22.161 -26.147 15.953  1.00 15.10 ?  364 SER A C     1 
ATOM   2659 O O     . SER A 1 358 ? -23.072 -26.682 16.600  1.00 14.88 ?  364 SER A O     1 
ATOM   2660 C CB    . SER A 1 358 ? -21.910 -23.650 16.092  1.00 13.91 ?  364 SER A CB    1 
ATOM   2661 O OG    . SER A 1 358 ? -21.399 -22.607 16.907  1.00 11.87 ?  364 SER A OG    1 
ATOM   2662 N N     . TRP A 1 359 ? -21.831 -26.533 14.717  1.00 14.84 ?  365 TRP A N     1 
ATOM   2663 C CA    . TRP A 1 359 ? -22.475 -27.696 14.108  1.00 14.97 ?  365 TRP A CA    1 
ATOM   2664 C C     . TRP A 1 359 ? -22.189 -28.958 14.917  1.00 17.08 ?  365 TRP A C     1 
ATOM   2665 O O     . TRP A 1 359 ? -23.072 -29.808 15.093  1.00 15.27 ?  365 TRP A O     1 
ATOM   2666 C CB    . TRP A 1 359 ? -22.014 -27.838 12.654  1.00 14.86 ?  365 TRP A CB    1 
ATOM   2667 C CG    . TRP A 1 359 ? -22.595 -26.736 11.765  1.00 15.46 ?  365 TRP A CG    1 
ATOM   2668 C CD1   . TRP A 1 359 ? -21.980 -25.564 11.382  1.00 15.21 ?  365 TRP A CD1   1 
ATOM   2669 C CD2   . TRP A 1 359 ? -23.917 -26.690 11.213  1.00 14.59 ?  365 TRP A CD2   1 
ATOM   2670 N NE1   . TRP A 1 359 ? -22.837 -24.808 10.611  1.00 14.00 ?  365 TRP A NE1   1 
ATOM   2671 C CE2   . TRP A 1 359 ? -24.033 -25.473 10.496  1.00 14.62 ?  365 TRP A CE2   1 
ATOM   2672 C CE3   . TRP A 1 359 ? -25.008 -27.566 11.242  1.00 14.25 ?  365 TRP A CE3   1 
ATOM   2673 C CZ2   . TRP A 1 359 ? -25.195 -25.120 9.812   1.00 13.36 ?  365 TRP A CZ2   1 
ATOM   2674 C CZ3   . TRP A 1 359 ? -26.161 -27.211 10.577  1.00 12.80 ?  365 TRP A CZ3   1 
ATOM   2675 C CH2   . TRP A 1 359 ? -26.251 -25.991 9.871   1.00 14.11 ?  365 TRP A CH2   1 
ATOM   2676 N N     . LYS A 1 360 ? -20.975 -29.071 15.467  1.00 14.73 ?  366 LYS A N     1 
ATOM   2677 C CA    . LYS A 1 360 ? -20.659 -30.203 16.340  1.00 18.29 ?  366 LYS A CA    1 
ATOM   2678 C C     . LYS A 1 360 ? -21.514 -30.189 17.607  1.00 17.76 ?  366 LYS A C     1 
ATOM   2679 O O     . LYS A 1 360 ? -22.145 -31.192 17.953  1.00 17.84 ?  366 LYS A O     1 
ATOM   2680 C CB    . LYS A 1 360 ? -19.170 -30.199 16.692  1.00 16.88 ?  366 LYS A CB    1 
ATOM   2681 C CG    . LYS A 1 360 ? -18.776 -31.350 17.627  1.00 23.25 ?  366 LYS A CG    1 
ATOM   2682 N N     . THR A 1 361 ? -21.545 -29.059 18.319  1.00 15.03 ?  367 THR A N     1 
ATOM   2683 C CA    . THR A 1 361 ? -22.378 -28.953 19.515  1.00 16.29 ?  367 THR A CA    1 
ATOM   2684 C C     . THR A 1 361 ? -23.827 -29.353 19.231  1.00 18.62 ?  367 THR A C     1 
ATOM   2685 O O     . THR A 1 361 ? -24.434 -30.103 20.003  1.00 18.38 ?  367 THR A O     1 
ATOM   2686 C CB    . THR A 1 361 ? -22.288 -27.525 20.072  1.00 16.23 ?  367 THR A CB    1 
ATOM   2687 O OG1   . THR A 1 361 ? -20.950 -27.296 20.553  1.00 16.21 ?  367 THR A OG1   1 
ATOM   2688 C CG2   . THR A 1 361 ? -23.258 -27.301 21.225  1.00 16.29 ?  367 THR A CG2   1 
ATOM   2689 N N     . MET A 1 362 ? -24.392 -28.875 18.117  1.00 15.72 ?  368 MET A N     1 
ATOM   2690 C CA    . MET A 1 362 ? -25.783 -29.119 17.744  1.00 17.37 ?  368 MET A CA    1 
ATOM   2691 C C     . MET A 1 362 ? -25.999 -30.490 17.128  1.00 17.69 ?  368 MET A C     1 
ATOM   2692 O O     . MET A 1 362 ? -27.149 -30.848 16.838  1.00 17.54 ?  368 MET A O     1 
ATOM   2693 C CB    . MET A 1 362 ? -26.250 -28.038 16.755  1.00 15.13 ?  368 MET A CB    1 
ATOM   2694 C CG    . MET A 1 362 ? -26.278 -26.631 17.389  1.00 12.61 ?  368 MET A CG    1 
ATOM   2695 S SD    . MET A 1 362 ? -27.526 -26.505 18.699  1.00 18.17 ?  368 MET A SD    1 
ATOM   2696 C CE    . MET A 1 362 ? -28.970 -26.261 17.677  1.00 15.52 ?  368 MET A CE    1 
ATOM   2697 N N     . ARG A 1 363 ? -24.920 -31.240 16.899  1.00 15.37 ?  369 ARG A N     1 
ATOM   2698 C CA    . ARG A 1 363 ? -24.988 -32.586 16.319  1.00 22.05 ?  369 ARG A CA    1 
ATOM   2699 C C     . ARG A 1 363 ? -25.729 -32.573 14.981  1.00 23.89 ?  369 ARG A C     1 
ATOM   2700 O O     . ARG A 1 363 ? -26.559 -33.437 14.687  1.00 21.64 ?  369 ARG A O     1 
ATOM   2701 C CB    . ARG A 1 363 ? -25.608 -33.573 17.320  1.00 24.84 ?  369 ARG A CB    1 
ATOM   2702 C CG    . ARG A 1 363 ? -24.667 -33.868 18.508  1.00 27.11 ?  369 ARG A CG    1 
ATOM   2703 C CD    . ARG A 1 363 ? -25.385 -34.402 19.736  1.00 32.69 ?  369 ARG A CD    1 
ATOM   2704 N NE    . ARG A 1 363 ? -25.821 -35.785 19.582  1.00 42.00 ?  369 ARG A NE    1 
ATOM   2705 N N     . GLN A 1 364 ? -25.415 -31.574 14.152  1.00 18.36 ?  370 GLN A N     1 
ATOM   2706 C CA    . GLN A 1 364 ? -25.981 -31.447 12.824  1.00 18.74 ?  370 GLN A CA    1 
ATOM   2707 C C     . GLN A 1 364 ? -24.853 -31.233 11.824  1.00 20.31 ?  370 GLN A C     1 
ATOM   2708 O O     . GLN A 1 364 ? -23.728 -30.880 12.188  1.00 18.59 ?  370 GLN A O     1 
ATOM   2709 C CB    . GLN A 1 364 ? -26.986 -30.287 12.736  1.00 17.22 ?  370 GLN A CB    1 
ATOM   2710 C CG    . GLN A 1 364 ? -28.300 -30.493 13.470  1.00 15.32 ?  370 GLN A CG    1 
ATOM   2711 C CD    . GLN A 1 364 ? -29.238 -29.327 13.260  1.00 17.38 ?  370 GLN A CD    1 
ATOM   2712 O OE1   . GLN A 1 364 ? -29.424 -28.875 12.127  1.00 15.23 ?  370 GLN A OE1   1 
ATOM   2713 N NE2   . GLN A 1 364 ? -29.808 -28.807 14.342  1.00 14.91 ?  370 GLN A NE2   1 
ATOM   2714 N N     . SER A 1 365 ? -25.169 -31.464 10.562  1.00 21.23 ?  371 SER A N     1 
ATOM   2715 C CA    . SER A 1 365 ? -24.216 -31.252 9.489   1.00 21.77 ?  371 SER A CA    1 
ATOM   2716 C C     . SER A 1 365 ? -24.617 -30.050 8.644   1.00 19.52 ?  371 SER A C     1 
ATOM   2717 O O     . SER A 1 365 ? -25.800 -29.895 8.293   1.00 19.86 ?  371 SER A O     1 
ATOM   2718 C CB    . SER A 1 365 ? -24.110 -32.491 8.595   1.00 26.15 ?  371 SER A CB    1 
ATOM   2719 O OG    . SER A 1 365 ? -23.510 -33.555 9.317   1.00 28.64 ?  371 SER A OG    1 
ATOM   2720 N N     . PRO A 1 366 ? -23.666 -29.184 8.295   1.00 20.85 ?  372 PRO A N     1 
ATOM   2721 C CA    . PRO A 1 366 ? -24.033 -27.957 7.588   1.00 21.20 ?  372 PRO A CA    1 
ATOM   2722 C C     . PRO A 1 366 ? -24.514 -28.268 6.187   1.00 25.72 ?  372 PRO A C     1 
ATOM   2723 O O     . PRO A 1 366 ? -24.121 -29.281 5.583   1.00 26.33 ?  372 PRO A O     1 
ATOM   2724 C CB    . PRO A 1 366 ? -22.727 -27.139 7.583   1.00 23.75 ?  372 PRO A CB    1 
ATOM   2725 C CG    . PRO A 1 366 ? -21.644 -28.084 7.916   1.00 21.57 ?  372 PRO A CG    1 
ATOM   2726 C CD    . PRO A 1 366 ? -22.237 -29.232 8.658   1.00 18.59 ?  372 PRO A CD    1 
ATOM   2727 N N     . PRO A 1 367 ? -25.424 -27.454 5.638   1.00 24.71 ?  373 PRO A N     1 
ATOM   2728 C CA    . PRO A 1 367 ? -25.913 -27.679 4.278   1.00 28.09 ?  373 PRO A CA    1 
ATOM   2729 C C     . PRO A 1 367 ? -24.892 -27.201 3.243   1.00 37.06 ?  373 PRO A C     1 
ATOM   2730 O O     . PRO A 1 367 ? -23.984 -26.428 3.569   1.00 40.12 ?  373 PRO A O     1 
ATOM   2731 C CB    . PRO A 1 367 ? -27.198 -26.848 4.233   1.00 26.83 ?  373 PRO A CB    1 
ATOM   2732 C CG    . PRO A 1 367 ? -26.940 -25.718 5.185   1.00 24.24 ?  373 PRO A CG    1 
ATOM   2733 C CD    . PRO A 1 367 ? -26.101 -26.316 6.293   1.00 22.35 ?  373 PRO A CD    1 
ATOM   2734 O OXT   . PRO A 1 367 ? -24.937 -27.573 2.066   1.00 48.50 -1 373 PRO A OXT   1 
HETATM 2735 N N1    . 6FA B 2 .   ? -16.390 -14.535 20.748  1.00 12.40 ?  401 6FA A N1    1 
HETATM 2736 C C2    . 6FA B 2 .   ? -15.371 -15.413 20.894  1.00 15.55 ?  401 6FA A C2    1 
HETATM 2737 O O2    . 6FA B 2 .   ? -15.294 -16.139 21.886  1.00 13.88 ?  401 6FA A O2    1 
HETATM 2738 N N3    . 6FA B 2 .   ? -14.376 -15.522 19.985  1.00 14.71 ?  401 6FA A N3    1 
HETATM 2739 C C4    . 6FA B 2 .   ? -14.350 -14.758 18.851  1.00 13.82 ?  401 6FA A C4    1 
HETATM 2740 O O4    . 6FA B 2 .   ? -13.417 -14.874 18.075  1.00 12.89 ?  401 6FA A O4    1 
HETATM 2741 C C4A   . 6FA B 2 .   ? -15.424 -13.879 18.624  1.00 14.36 ?  401 6FA A C4A   1 
HETATM 2742 N N5    . 6FA B 2 .   ? -15.434 -13.176 17.521  1.00 16.03 ?  401 6FA A N5    1 
HETATM 2743 C C5A   . 6FA B 2 .   ? -16.491 -12.384 17.289  1.00 13.35 ?  401 6FA A C5A   1 
HETATM 2744 C C6    . 6FA B 2 .   ? -16.518 -11.681 16.045  1.00 18.44 ?  401 6FA A C6    1 
HETATM 2745 O O6    . 6FA B 2 .   ? -15.486 -11.871 15.179  1.00 15.81 ?  401 6FA A O6    1 
HETATM 2746 C C7    . 6FA B 2 .   ? -17.595 -10.879 15.739  1.00 17.32 ?  401 6FA A C7    1 
HETATM 2747 C C7M   . 6FA B 2 .   ? -17.637 -10.153 14.419  1.00 17.58 ?  401 6FA A C7M   1 
HETATM 2748 C C8    . 6FA B 2 .   ? -18.643 -10.715 16.662  1.00 19.22 ?  401 6FA A C8    1 
HETATM 2749 C C8M   . 6FA B 2 .   ? -19.793 -9.805  16.324  1.00 18.20 ?  401 6FA A C8M   1 
HETATM 2750 C C9    . 6FA B 2 .   ? -18.597 -11.353 17.901  1.00 16.61 ?  401 6FA A C9    1 
HETATM 2751 C C9A   . 6FA B 2 .   ? -17.539 -12.219 18.227  1.00 16.34 ?  401 6FA A C9A   1 
HETATM 2752 N N10   . 6FA B 2 .   ? -17.480 -12.937 19.425  1.00 14.35 ?  401 6FA A N10   1 
HETATM 2753 C C10   . 6FA B 2 .   ? -16.431 -13.813 19.647  1.00 14.13 ?  401 6FA A C10   1 
HETATM 2754 C "C1'" . 6FA B 2 .   ? -18.492 -12.721 20.481  1.00 15.20 ?  401 6FA A "C1'" 1 
HETATM 2755 C "C2'" . 6FA B 2 .   ? -19.672 -13.633 20.495  1.00 13.90 ?  401 6FA A "C2'" 1 
HETATM 2756 O "O2'" . 6FA B 2 .   ? -20.410 -13.347 19.328  1.00 13.08 ?  401 6FA A "O2'" 1 
HETATM 2757 C "C3'" . 6FA B 2 .   ? -20.542 -13.298 21.711  1.00 11.60 ?  401 6FA A "C3'" 1 
HETATM 2758 O "O3'" . 6FA B 2 .   ? -19.729 -13.085 22.878  1.00 12.30 ?  401 6FA A "O3'" 1 
HETATM 2759 C "C4'" . 6FA B 2 .   ? -21.541 -14.420 22.006  1.00 13.57 ?  401 6FA A "C4'" 1 
HETATM 2760 O "O4'" . 6FA B 2 .   ? -22.539 -14.441 20.986  1.00 12.15 ?  401 6FA A "O4'" 1 
HETATM 2761 C "C5'" . 6FA B 2 .   ? -22.231 -14.290 23.340  1.00 13.60 ?  401 6FA A "C5'" 1 
HETATM 2762 O "O5'" . 6FA B 2 .   ? -23.004 -15.527 23.460  1.00 12.27 ?  401 6FA A "O5'" 1 
HETATM 2763 P P     . 6FA B 2 .   ? -24.302 -15.544 24.385  1.00 11.09 ?  401 6FA A P     1 
HETATM 2764 O O1P   . 6FA B 2 .   ? -24.813 -16.952 24.440  1.00 13.19 -1 401 6FA A O1P   1 
HETATM 2765 O O2P   . 6FA B 2 .   ? -24.017 -14.797 25.654  1.00 13.57 ?  401 6FA A O2P   1 
HETATM 2766 O O3P   . 6FA B 2 .   ? -25.335 -14.646 23.595  1.00 12.69 ?  401 6FA A O3P   1 
HETATM 2767 P PA    . 6FA B 2 .   ? -25.833 -14.638 22.070  1.00 14.80 ?  401 6FA A PA    1 
HETATM 2768 O O1A   . 6FA B 2 .   ? -26.031 -13.206 21.711  1.00 14.93 -1 401 6FA A O1A   1 
HETATM 2769 O O2A   . 6FA B 2 .   ? -24.943 -15.515 21.272  1.00 13.03 ?  401 6FA A O2A   1 
HETATM 2770 O O5B   . 6FA B 2 .   ? -27.257 -15.340 22.189  1.00 12.02 ?  401 6FA A O5B   1 
HETATM 2771 C C5B   . 6FA B 2 .   ? -28.299 -14.754 22.998  1.00 13.61 ?  401 6FA A C5B   1 
HETATM 2772 C C4B   . 6FA B 2 .   ? -29.619 -15.290 22.500  1.00 13.08 ?  401 6FA A C4B   1 
HETATM 2773 O O4B   . 6FA B 2 .   ? -30.665 -14.871 23.410  1.00 15.23 ?  401 6FA A O4B   1 
HETATM 2774 C C3B   . 6FA B 2 .   ? -30.064 -14.784 21.116  1.00 13.76 ?  401 6FA A C3B   1 
HETATM 2775 O O3B   . 6FA B 2 .   ? -30.428 -15.879 20.288  1.00 14.82 ?  401 6FA A O3B   1 
HETATM 2776 C C2B   . 6FA B 2 .   ? -31.298 -13.932 21.427  1.00 17.09 ?  401 6FA A C2B   1 
HETATM 2777 O O2B   . 6FA B 2 .   ? -32.213 -13.869 20.355  1.00 19.65 ?  401 6FA A O2B   1 
HETATM 2778 C C1B   . 6FA B 2 .   ? -31.833 -14.645 22.664  1.00 17.01 ?  401 6FA A C1B   1 
HETATM 2779 N N9A   . 6FA B 2 .   ? -32.705 -13.806 23.471  1.00 17.69 ?  401 6FA A N9A   1 
HETATM 2780 C C8A   . 6FA B 2 .   ? -32.310 -12.674 24.133  1.00 21.20 ?  401 6FA A C8A   1 
HETATM 2781 N N7A   . 6FA B 2 .   ? -33.280 -12.089 24.782  1.00 24.37 ?  401 6FA A N7A   1 
HETATM 2782 C C5X   . 6FA B 2 .   ? -34.387 -12.888 24.543  1.00 22.01 ?  401 6FA A C5X   1 
HETATM 2783 C C6A   . 6FA B 2 .   ? -35.723 -12.788 24.969  1.00 25.55 ?  401 6FA A C6A   1 
HETATM 2784 N N6A   . 6FA B 2 .   ? -36.170 -11.802 25.748  1.00 25.45 ?  401 6FA A N6A   1 
HETATM 2785 N N1A   . 6FA B 2 .   ? -36.582 -13.750 24.552  1.00 22.00 ?  401 6FA A N1A   1 
HETATM 2786 C C2A   . 6FA B 2 .   ? -36.113 -14.735 23.771  1.00 21.78 ?  401 6FA A C2A   1 
HETATM 2787 N N3A   . 6FA B 2 .   ? -34.879 -14.923 23.309  1.00 19.26 ?  401 6FA A N3A   1 
HETATM 2788 C C4X   . 6FA B 2 .   ? -34.049 -13.955 23.735  1.00 18.74 ?  401 6FA A C4X   1 
HETATM 2789 P PA    . NDP C 3 .   ? -17.385 -1.426  20.374  1.00 18.99 ?  402 NDP A PA    1 
HETATM 2790 O O1A   . NDP C 3 .   ? -18.286 -0.644  21.271  1.00 18.41 -1 402 NDP A O1A   1 
HETATM 2791 O O2A   . NDP C 3 .   ? -16.256 -2.217  20.971  1.00 21.30 ?  402 NDP A O2A   1 
HETATM 2792 O O5B   . NDP C 3 .   ? -16.716 -0.454  19.234  1.00 16.72 ?  402 NDP A O5B   1 
HETATM 2793 C C5B   . NDP C 3 .   ? -17.729 0.391   18.713  1.00 14.81 ?  402 NDP A C5B   1 
HETATM 2794 C C4B   . NDP C 3 .   ? -17.016 1.698   18.365  1.00 16.65 ?  402 NDP A C4B   1 
HETATM 2795 O O4B   . NDP C 3 .   ? -17.810 2.506   17.492  1.00 14.61 ?  402 NDP A O4B   1 
HETATM 2796 C C3B   . NDP C 3 .   ? -16.798 2.447   19.694  1.00 16.99 ?  402 NDP A C3B   1 
HETATM 2797 O O3B   . NDP C 3 .   ? -15.424 2.740   19.882  1.00 19.00 ?  402 NDP A O3B   1 
HETATM 2798 C C2B   . NDP C 3 .   ? -17.573 3.765   19.462  1.00 19.11 ?  402 NDP A C2B   1 
HETATM 2799 O O2B   . NDP C 3 .   ? -16.952 4.834   19.963  1.00 19.55 ?  402 NDP A O2B   1 
HETATM 2800 C C1B   . NDP C 3 .   ? -17.564 3.830   17.894  1.00 16.39 ?  402 NDP A C1B   1 
HETATM 2801 N N9A   . NDP C 3 .   ? -18.657 4.667   17.394  1.00 15.99 ?  402 NDP A N9A   1 
HETATM 2802 C C8A   . NDP C 3 .   ? -19.999 4.675   17.810  1.00 17.82 ?  402 NDP A C8A   1 
HETATM 2803 N N7A   . NDP C 3 .   ? -20.756 5.576   17.136  1.00 20.18 ?  402 NDP A N7A   1 
HETATM 2804 C C5A   . NDP C 3 .   ? -19.849 6.162   16.232  1.00 15.29 ?  402 NDP A C5A   1 
HETATM 2805 C C6A   . NDP C 3 .   ? -20.019 7.158   15.269  1.00 16.05 ?  402 NDP A C6A   1 
HETATM 2806 N N6A   . NDP C 3 .   ? -21.246 7.751   15.089  1.00 16.77 ?  402 NDP A N6A   1 
HETATM 2807 N N1A   . NDP C 3 .   ? -18.992 7.558   14.491  1.00 14.54 ?  402 NDP A N1A   1 
HETATM 2808 C C2A   . NDP C 3 .   ? -17.788 6.949   14.724  1.00 14.52 ?  402 NDP A C2A   1 
HETATM 2809 N N3A   . NDP C 3 .   ? -17.464 5.991   15.617  1.00 15.55 ?  402 NDP A N3A   1 
HETATM 2810 C C4A   . NDP C 3 .   ? -18.548 5.612   16.374  1.00 15.08 ?  402 NDP A C4A   1 
HETATM 2811 O O3    . NDP C 3 .   ? -18.553 -2.429  19.732  1.00 15.43 ?  402 NDP A O3    1 
HETATM 2812 P PN    . NDP C 3 .   ? -18.045 -3.739  18.891  1.00 17.63 ?  402 NDP A PN    1 
HETATM 2813 O O1N   . NDP C 3 .   ? -19.289 -4.371  18.422  1.00 14.86 -1 402 NDP A O1N   1 
HETATM 2814 O O2N   . NDP C 3 .   ? -16.828 -3.562  18.016  1.00 17.29 ?  402 NDP A O2N   1 
HETATM 2815 O O5D   . NDP C 3 .   ? -17.469 -4.934  20.070  1.00 22.33 ?  402 NDP A O5D   1 
HETATM 2816 C C5D   . NDP C 3 .   ? -18.429 -5.110  21.056  1.00 22.47 ?  402 NDP A C5D   1 
HETATM 2817 C C4D   . NDP C 3 .   ? -18.009 -6.317  21.935  1.00 24.90 ?  402 NDP A C4D   1 
HETATM 2818 O O4D   . NDP C 3 .   ? -18.233 -7.549  21.213  1.00 26.07 ?  402 NDP A O4D   1 
HETATM 2819 C C3D   . NDP C 3 .   ? -16.488 -6.280  22.189  1.00 28.81 ?  402 NDP A C3D   1 
HETATM 2820 O O3D   . NDP C 3 .   ? -16.252 -5.576  23.352  1.00 32.49 ?  402 NDP A O3D   1 
HETATM 2821 C C2D   . NDP C 3 .   ? -16.147 -7.773  22.379  1.00 30.44 ?  402 NDP A C2D   1 
HETATM 2822 O O2D   . NDP C 3 .   ? -16.472 -8.252  23.658  1.00 35.26 ?  402 NDP A O2D   1 
HETATM 2823 C C1D   . NDP C 3 .   ? -17.117 -8.454  21.388  1.00 26.97 ?  402 NDP A C1D   1 
HETATM 2824 N N1N   . NDP C 3 .   ? -16.437 -8.730  20.071  1.00 27.48 ?  402 NDP A N1N   1 
HETATM 2825 C C2N   . NDP C 3 .   ? -15.385 -9.636  20.002  1.00 26.90 ?  402 NDP A C2N   1 
HETATM 2826 C C3N   . NDP C 3 .   ? -14.718 -9.856  18.821  1.00 23.71 ?  402 NDP A C3N   1 
HETATM 2827 C C7N   . NDP C 3 .   ? -13.608 -10.814 18.851  1.00 25.33 ?  402 NDP A C7N   1 
HETATM 2828 O O7N   . NDP C 3 .   ? -13.358 -11.603 19.787  1.00 23.38 ?  402 NDP A O7N   1 
HETATM 2829 N N7N   . NDP C 3 .   ? -12.760 -10.797 17.730  1.00 23.31 ?  402 NDP A N7N   1 
HETATM 2830 C C4N   . NDP C 3 .   ? -15.063 -9.148  17.536  1.00 22.23 ?  402 NDP A C4N   1 
HETATM 2831 C C5N   . NDP C 3 .   ? -16.279 -8.298  17.693  1.00 24.30 ?  402 NDP A C5N   1 
HETATM 2832 C C6N   . NDP C 3 .   ? -16.887 -8.119  18.886  1.00 27.01 ?  402 NDP A C6N   1 
HETATM 2833 P P2B   . NDP C 3 .   ? -17.841 5.560   21.339  1.00 25.91 ?  402 NDP A P2B   1 
HETATM 2834 O O1X   . NDP C 3 .   ? -17.905 4.355   22.227  1.00 30.10 ?  402 NDP A O1X   1 
HETATM 2835 O O2X   . NDP C 3 .   ? -19.149 6.052   20.717  1.00 27.06 -1 402 NDP A O2X   1 
HETATM 2836 O O3X   . NDP C 3 .   ? -16.795 6.591   21.639  1.00 33.02 ?  402 NDP A O3X   1 
HETATM 2837 S S     . SO4 D 4 .   ? 3.578   -13.116 11.714  1.00 28.31 ?  403 SO4 A S     1 
HETATM 2838 O O1    . SO4 D 4 .   ? 3.949   -12.525 10.436  1.00 27.71 ?  403 SO4 A O1    1 
HETATM 2839 O O2    . SO4 D 4 .   ? 2.929   -14.427 11.474  1.00 19.88 ?  403 SO4 A O2    1 
HETATM 2840 O O3    . SO4 D 4 .   ? 4.793   -13.321 12.520  1.00 34.91 -1 403 SO4 A O3    1 
HETATM 2841 O O4    . SO4 D 4 .   ? 2.726   -12.183 12.440  1.00 23.22 ?  403 SO4 A O4    1 
HETATM 2842 O O     . HOH E 5 .   ? -30.374 -11.605 43.271  1.00 49.63 ?  501 HOH A O     1 
HETATM 2843 O O     . HOH E 5 .   ? -28.014 -31.106 47.148  1.00 45.97 ?  502 HOH A O     1 
HETATM 2844 O O     . HOH E 5 .   ? -31.932 -19.493 45.714  1.00 45.39 ?  503 HOH A O     1 
HETATM 2845 O O     . HOH E 5 .   ? -23.511 -16.841 42.465  1.00 40.47 ?  504 HOH A O     1 
HETATM 2846 O O     . HOH E 5 .   ? -14.460 -4.165  20.362  1.00 26.87 ?  505 HOH A O     1 
HETATM 2847 O O     . HOH E 5 .   ? -37.556 -6.580  33.042  1.00 42.62 ?  506 HOH A O     1 
HETATM 2848 O O     . HOH E 5 .   ? -41.273 -29.797 37.293  1.00 32.01 ?  507 HOH A O     1 
HETATM 2849 O O     . HOH E 5 .   ? -27.002 -0.957  35.075  1.00 42.71 ?  508 HOH A O     1 
HETATM 2850 O O     . HOH E 5 .   ? -9.977  0.344   -4.881  1.00 38.24 ?  509 HOH A O     1 
HETATM 2851 O O     . HOH E 5 .   ? -34.465 -33.272 23.508  1.00 42.37 ?  510 HOH A O     1 
HETATM 2852 O O     . HOH E 5 .   ? -6.499  11.184  16.245  1.00 43.29 ?  511 HOH A O     1 
HETATM 2853 O O     . HOH E 5 .   ? -0.451  -9.292  28.780  1.00 45.18 ?  512 HOH A O     1 
HETATM 2854 O O     . HOH E 5 .   ? -9.138  1.667   -2.553  1.00 40.57 ?  513 HOH A O     1 
HETATM 2855 O O     . HOH E 5 .   ? -6.461  -16.685 42.871  1.00 38.97 ?  514 HOH A O     1 
HETATM 2856 O O     . HOH E 5 .   ? -26.127 -13.190 -1.982  1.00 20.36 ?  515 HOH A O     1 
HETATM 2857 O O     . HOH E 5 .   ? -30.217 -7.096  -1.799  1.00 31.87 ?  516 HOH A O     1 
HETATM 2858 O O     . HOH E 5 .   ? 3.346   -7.852  11.605  1.00 36.72 ?  517 HOH A O     1 
HETATM 2859 O O     . HOH E 5 .   ? -8.411  -26.360 6.179   1.00 46.50 ?  518 HOH A O     1 
HETATM 2860 O O     . HOH E 5 .   ? -17.701 -23.411 6.807   1.00 33.54 ?  519 HOH A O     1 
HETATM 2861 O O     . HOH E 5 .   ? -10.812 -13.893 26.721  1.00 24.57 ?  520 HOH A O     1 
HETATM 2862 O O     . HOH E 5 .   ? -38.030 -9.060  41.687  1.00 43.16 ?  521 HOH A O     1 
HETATM 2863 O O     . HOH E 5 .   ? -34.693 -17.217 0.314   1.00 27.40 ?  522 HOH A O     1 
HETATM 2864 O O     . HOH E 5 .   ? -38.389 -22.591 41.690  1.00 32.35 ?  523 HOH A O     1 
HETATM 2865 O O     . HOH E 5 .   ? -6.268  -4.689  -0.902  1.00 25.97 ?  524 HOH A O     1 
HETATM 2866 O O     . HOH E 5 .   ? -28.488 -24.416 41.946  1.00 28.07 ?  525 HOH A O     1 
HETATM 2867 O O     . HOH E 5 .   ? 3.128   -9.996  13.673  1.00 28.53 ?  526 HOH A O     1 
HETATM 2868 O O     . HOH E 5 .   ? 2.392   -2.908  13.962  1.00 30.70 ?  527 HOH A O     1 
HETATM 2869 O O     . HOH E 5 .   ? -33.927 -18.063 12.574  1.00 21.23 ?  528 HOH A O     1 
HETATM 2870 O O     . HOH E 5 .   ? -16.176 8.851   -1.839  1.00 29.67 ?  529 HOH A O     1 
HETATM 2871 O O     . HOH E 5 .   ? -36.299 -26.265 11.980  1.00 30.93 ?  530 HOH A O     1 
HETATM 2872 O O     . HOH E 5 .   ? -43.903 -15.580 22.879  1.00 34.22 ?  531 HOH A O     1 
HETATM 2873 O O     . HOH E 5 .   ? -39.097 -27.880 18.747  1.00 22.52 ?  532 HOH A O     1 
HETATM 2874 O O     . HOH E 5 .   ? -7.504  -6.733  -0.067  1.00 18.47 ?  533 HOH A O     1 
HETATM 2875 O O     . HOH E 5 .   ? -27.582 0.000   32.453  0.50 31.21 ?  534 HOH A O     1 
HETATM 2876 O O     . HOH E 5 .   ? -20.689 -24.727 20.598  1.00 16.54 ?  535 HOH A O     1 
HETATM 2877 O O     . HOH E 5 .   ? -29.927 -38.086 34.918  1.00 25.70 ?  536 HOH A O     1 
HETATM 2878 O O     . HOH E 5 .   ? -25.463 -1.578  9.581   1.00 16.11 ?  537 HOH A O     1 
HETATM 2879 O O     . HOH E 5 .   ? -23.012 2.866   -8.381  1.00 23.52 ?  538 HOH A O     1 
HETATM 2880 O O     . HOH E 5 .   ? -24.336 -12.710 -4.115  1.00 21.18 ?  539 HOH A O     1 
HETATM 2881 O O     . HOH E 5 .   ? -20.039 -13.938 27.085  1.00 21.22 ?  540 HOH A O     1 
HETATM 2882 O O     . HOH E 5 .   ? -35.917 -33.765 37.807  1.00 34.96 ?  541 HOH A O     1 
HETATM 2883 O O     . HOH E 5 .   ? -24.616 -9.487  -6.801  1.00 27.17 ?  542 HOH A O     1 
HETATM 2884 O O     . HOH E 5 .   ? -30.573 6.073   9.782   1.00 31.59 ?  543 HOH A O     1 
HETATM 2885 O O     . HOH E 5 .   ? -27.343 -11.744 19.946  1.00 29.66 ?  544 HOH A O     1 
HETATM 2886 O O     . HOH E 5 .   ? -29.719 -7.372  17.974  1.00 22.66 ?  545 HOH A O     1 
HETATM 2887 O O     . HOH E 5 .   ? -26.423 -18.996 2.149   1.00 16.48 ?  546 HOH A O     1 
HETATM 2888 O O     . HOH E 5 .   ? -26.816 -33.515 24.107  1.00 23.89 ?  547 HOH A O     1 
HETATM 2889 O O     . HOH E 5 .   ? -16.749 -13.194 -1.396  1.00 19.11 ?  548 HOH A O     1 
HETATM 2890 O O     . HOH E 5 .   ? -15.112 -24.047 11.379  1.00 28.03 ?  549 HOH A O     1 
HETATM 2891 O O     . HOH E 5 .   ? 4.426   -16.437 10.619  1.00 40.09 ?  550 HOH A O     1 
HETATM 2892 O O     . HOH E 5 .   ? -27.137 -18.148 24.869  1.00 11.21 ?  551 HOH A O     1 
HETATM 2893 O O     . HOH E 5 .   ? -12.423 -10.236 9.141   1.00 20.23 ?  552 HOH A O     1 
HETATM 2894 O O     . HOH E 5 .   ? -36.358 -24.590 15.165  1.00 16.75 ?  553 HOH A O     1 
HETATM 2895 O O     . HOH E 5 .   ? -20.252 -1.878  22.563  1.00 19.84 ?  554 HOH A O     1 
HETATM 2896 O O     . HOH E 5 .   ? -47.492 -16.606 25.293  1.00 44.43 ?  555 HOH A O     1 
HETATM 2897 O O     . HOH E 5 .   ? -3.861  -8.459  4.517   1.00 17.89 ?  556 HOH A O     1 
HETATM 2898 O O     . HOH E 5 .   ? -19.584 20.822  1.340   1.00 33.73 ?  557 HOH A O     1 
HETATM 2899 O O     . HOH E 5 .   ? -30.562 -26.611 43.979  1.00 37.82 ?  558 HOH A O     1 
HETATM 2900 O O     . HOH E 5 .   ? -37.521 -28.650 42.574  1.00 28.13 ?  559 HOH A O     1 
HETATM 2901 O O     . HOH E 5 .   ? -18.830 -29.640 12.766  1.00 19.18 ?  560 HOH A O     1 
HETATM 2902 O O     . HOH E 5 .   ? -25.664 -14.281 27.743  1.00 15.31 ?  561 HOH A O     1 
HETATM 2903 O O     . HOH E 5 .   ? -6.776  -23.474 10.042  1.00 34.38 ?  562 HOH A O     1 
HETATM 2904 O O     . HOH E 5 .   ? -29.570 -30.221 9.815   1.00 19.76 ?  563 HOH A O     1 
HETATM 2905 O O     . HOH E 5 .   ? -16.744 -20.897 2.466   1.00 36.00 ?  564 HOH A O     1 
HETATM 2906 O O     . HOH E 5 .   ? -21.226 -31.725 12.687  1.00 25.27 ?  565 HOH A O     1 
HETATM 2907 O O     . HOH E 5 .   ? -32.475 -36.208 26.941  1.00 29.78 ?  566 HOH A O     1 
HETATM 2908 O O     . HOH E 5 .   ? -22.779 5.600   -7.460  1.00 38.75 ?  567 HOH A O     1 
HETATM 2909 O O     . HOH E 5 .   ? -26.449 2.190   3.087   1.00 11.98 ?  568 HOH A O     1 
HETATM 2910 O O     . HOH E 5 .   ? -8.909  9.090   5.598   1.00 31.47 ?  569 HOH A O     1 
HETATM 2911 O O     . HOH E 5 .   ? -15.288 -18.575 4.307   1.00 24.51 ?  570 HOH A O     1 
HETATM 2912 O O     . HOH E 5 .   ? -19.869 -7.006  18.225  1.00 22.58 ?  571 HOH A O     1 
HETATM 2913 O O     . HOH E 5 .   ? -11.238 -19.223 4.334   1.00 19.88 ?  572 HOH A O     1 
HETATM 2914 O O     . HOH E 5 .   ? -48.570 -20.932 30.061  1.00 44.08 ?  573 HOH A O     1 
HETATM 2915 O O     . HOH E 5 .   ? -16.845 -1.864  15.878  1.00 12.52 ?  574 HOH A O     1 
HETATM 2916 O O     . HOH E 5 .   ? -19.848 -19.806 0.298   1.00 23.64 ?  575 HOH A O     1 
HETATM 2917 O O     . HOH E 5 .   ? -46.558 -14.335 30.038  1.00 43.38 ?  576 HOH A O     1 
HETATM 2918 O O     . HOH E 5 .   ? -11.067 0.305   -7.692  1.00 31.40 ?  577 HOH A O     1 
HETATM 2919 O O     . HOH E 5 .   ? -24.221 -11.183 21.721  1.00 22.52 ?  578 HOH A O     1 
HETATM 2920 O O     . HOH E 5 .   ? 4.047   -13.227 22.068  1.00 31.35 ?  579 HOH A O     1 
HETATM 2921 O O     . HOH E 5 .   ? -7.406  -16.659 28.108  1.00 28.91 ?  580 HOH A O     1 
HETATM 2922 O O     . HOH E 5 .   ? -31.468 -21.496 48.648  1.00 42.71 ?  581 HOH A O     1 
HETATM 2923 O O     . HOH E 5 .   ? -23.240 -32.032 21.499  1.00 27.88 ?  582 HOH A O     1 
HETATM 2924 O O     . HOH E 5 .   ? -29.593 -10.879 22.467  1.00 16.19 ?  583 HOH A O     1 
HETATM 2925 O O     . HOH E 5 .   ? -10.355 1.346   -0.064  1.00 17.18 ?  584 HOH A O     1 
HETATM 2926 O O     . HOH E 5 .   ? -17.230 -5.237  -7.404  1.00 21.98 ?  585 HOH A O     1 
HETATM 2927 O O     . HOH E 5 .   ? -23.750 -15.108 2.897   1.00 10.08 ?  586 HOH A O     1 
HETATM 2928 O O     . HOH E 5 .   ? -25.491 3.520   15.827  1.00 29.46 ?  587 HOH A O     1 
HETATM 2929 O O     . HOH E 5 .   ? -19.055 -17.567 -2.628  1.00 25.96 ?  588 HOH A O     1 
HETATM 2930 O O     . HOH E 5 .   ? -3.894  5.205   15.762  1.00 39.81 ?  589 HOH A O     1 
HETATM 2931 O O     . HOH E 5 .   ? -31.018 -4.557  24.150  1.00 30.28 ?  590 HOH A O     1 
HETATM 2932 O O     . HOH E 5 .   ? -8.091  -18.617 4.538   1.00 24.06 ?  591 HOH A O     1 
HETATM 2933 O O     . HOH E 5 .   ? -40.219 -15.819 7.891   1.00 24.19 ?  592 HOH A O     1 
HETATM 2934 O O     . HOH E 5 .   ? -29.680 -6.699  14.802  1.00 21.97 ?  593 HOH A O     1 
HETATM 2935 O O     . HOH E 5 .   ? -24.593 0.518   18.102  1.00 20.70 ?  594 HOH A O     1 
HETATM 2936 O O     . HOH E 5 .   ? -28.237 -28.725 7.799   1.00 19.57 ?  595 HOH A O     1 
HETATM 2937 O O     . HOH E 5 .   ? -21.261 -33.691 17.222  1.00 31.12 ?  596 HOH A O     1 
HETATM 2938 O O     . HOH E 5 .   ? -5.078  2.209   3.002   1.00 21.98 ?  597 HOH A O     1 
HETATM 2939 O O     . HOH E 5 .   ? -27.909 -33.445 20.784  1.00 32.24 ?  598 HOH A O     1 
HETATM 2940 O O     . HOH E 5 .   ? -41.158 -22.560 16.512  1.00 34.93 ?  599 HOH A O     1 
HETATM 2941 O O     . HOH E 5 .   ? -28.900 -33.593 16.139  1.00 43.16 ?  600 HOH A O     1 
HETATM 2942 O O     . HOH E 5 .   ? -24.782 -14.748 9.639   1.00 9.20  ?  601 HOH A O     1 
HETATM 2943 O O     . HOH E 5 .   ? -26.147 -16.327 18.925  1.00 12.67 ?  602 HOH A O     1 
HETATM 2944 O O     . HOH E 5 .   ? -28.767 -23.582 7.719   1.00 16.74 ?  603 HOH A O     1 
HETATM 2945 O O     . HOH E 5 .   ? -22.391 -28.337 26.093  1.00 32.43 ?  604 HOH A O     1 
HETATM 2946 O O     . HOH E 5 .   ? -32.172 0.799   4.835   1.00 32.84 ?  605 HOH A O     1 
HETATM 2947 O O     . HOH E 5 .   ? -29.372 9.287   -0.714  1.00 35.59 ?  606 HOH A O     1 
HETATM 2948 O O     . HOH E 5 .   ? -19.509 -22.993 18.903  1.00 17.85 ?  607 HOH A O     1 
HETATM 2949 O O     . HOH E 5 .   ? -9.262  -23.162 15.691  1.00 21.29 ?  608 HOH A O     1 
HETATM 2950 O O     . HOH E 5 .   ? -15.277 -28.428 15.317  1.00 26.83 ?  609 HOH A O     1 
HETATM 2951 O O     . HOH E 5 .   ? 3.504   -14.852 19.071  1.00 34.18 ?  610 HOH A O     1 
HETATM 2952 O O     . HOH E 5 .   ? -21.593 1.028   -7.183  1.00 21.62 ?  611 HOH A O     1 
HETATM 2953 O O     . HOH E 5 .   ? -12.399 8.237   2.376   1.00 24.89 ?  612 HOH A O     1 
HETATM 2954 O O     . HOH E 5 .   ? 3.213   -7.147  22.896  1.00 28.21 ?  613 HOH A O     1 
HETATM 2955 O O     . HOH E 5 .   ? -30.402 -26.559 10.726  1.00 20.42 ?  614 HOH A O     1 
HETATM 2956 O O     . HOH E 5 .   ? -20.147 -9.308  20.179  1.00 22.21 ?  615 HOH A O     1 
HETATM 2957 O O     . HOH E 5 .   ? -14.311 11.819  18.292  1.00 40.03 ?  616 HOH A O     1 
HETATM 2958 O O     . HOH E 5 .   ? -27.477 14.389  6.410   1.00 33.02 ?  617 HOH A O     1 
HETATM 2959 O O     . HOH E 5 .   ? -9.551  -17.776 28.779  1.00 24.79 ?  618 HOH A O     1 
HETATM 2960 O O     . HOH E 5 .   ? -44.420 -29.644 38.977  1.00 35.16 ?  619 HOH A O     1 
HETATM 2961 O O     . HOH E 5 .   ? -27.331 -27.735 47.994  1.00 42.16 ?  620 HOH A O     1 
HETATM 2962 O O     . HOH E 5 .   ? -12.380 -17.526 40.561  1.00 40.48 ?  621 HOH A O     1 
HETATM 2963 O O     . HOH E 5 .   ? -4.914  1.288   16.371  1.00 21.41 ?  622 HOH A O     1 
HETATM 2964 O O     . HOH E 5 .   ? -47.196 -29.388 40.179  1.00 24.74 ?  623 HOH A O     1 
HETATM 2965 O O     . HOH E 5 .   ? -33.275 -18.403 2.334   1.00 23.55 ?  624 HOH A O     1 
HETATM 2966 O O     . HOH E 5 .   ? -21.401 -23.124 22.807  1.00 14.73 ?  625 HOH A O     1 
HETATM 2967 O O     . HOH E 5 .   ? -21.961 -10.506 43.677  1.00 35.13 ?  626 HOH A O     1 
HETATM 2968 O O     . HOH E 5 .   ? -29.901 -5.201  3.336   1.00 33.58 ?  627 HOH A O     1 
HETATM 2969 O O     . HOH E 5 .   ? -12.157 -12.341 3.768   1.00 11.96 ?  628 HOH A O     1 
HETATM 2970 O O     . HOH E 5 .   ? -20.220 4.561   -7.155  1.00 27.88 ?  629 HOH A O     1 
HETATM 2971 O O     . HOH E 5 .   ? -27.740 -32.491 9.952   1.00 22.55 ?  630 HOH A O     1 
HETATM 2972 O O     . HOH E 5 .   ? -26.711 -31.182 21.309  1.00 26.66 ?  631 HOH A O     1 
HETATM 2973 O O     . HOH E 5 .   ? -34.676 -30.477 44.194  1.00 29.50 ?  632 HOH A O     1 
HETATM 2974 O O     . HOH E 5 .   ? -23.569 5.737   17.488  1.00 29.92 ?  633 HOH A O     1 
HETATM 2975 O O     . HOH E 5 .   ? -22.879 -4.616  12.736  1.00 17.27 ?  634 HOH A O     1 
HETATM 2976 O O     . HOH E 5 .   ? -41.898 -35.536 44.084  1.00 19.90 ?  635 HOH A O     1 
HETATM 2977 O O     . HOH E 5 .   ? -10.631 -13.859 -0.682  1.00 19.73 ?  636 HOH A O     1 
HETATM 2978 O O     . HOH E 5 .   ? -17.577 -2.669  -7.090  1.00 17.19 ?  637 HOH A O     1 
HETATM 2979 O O     . HOH E 5 .   ? -11.794 -21.514 13.268  1.00 12.42 ?  638 HOH A O     1 
HETATM 2980 O O     . HOH E 5 .   ? -19.827 1.719   21.730  1.00 29.72 ?  639 HOH A O     1 
HETATM 2981 O O     . HOH E 5 .   ? -29.730 -2.958  12.514  1.00 23.09 ?  640 HOH A O     1 
HETATM 2982 O O     . HOH E 5 .   ? -27.131 -16.989 -2.458  1.00 31.07 ?  641 HOH A O     1 
HETATM 2983 O O     . HOH E 5 .   ? -20.268 -7.006  32.754  1.00 41.66 ?  642 HOH A O     1 
HETATM 2984 O O     . HOH E 5 .   ? -19.231 -12.935 29.543  1.00 31.01 ?  643 HOH A O     1 
HETATM 2985 O O     . HOH E 5 .   ? -24.067 16.385  10.582  1.00 31.90 ?  644 HOH A O     1 
HETATM 2986 O O     . HOH E 5 .   ? -4.889  -9.804  30.278  1.00 31.28 ?  645 HOH A O     1 
HETATM 2987 O O     . HOH E 5 .   ? 2.540   -3.843  16.697  1.00 27.88 ?  646 HOH A O     1 
HETATM 2988 O O     . HOH E 5 .   ? -28.418 -17.751 18.464  1.00 12.89 ?  647 HOH A O     1 
HETATM 2989 O O     . HOH E 5 .   ? -10.417 15.114  15.368  1.00 35.84 ?  648 HOH A O     1 
HETATM 2990 O O     . HOH E 5 .   ? -42.056 -27.798 34.323  1.00 41.56 ?  649 HOH A O     1 
HETATM 2991 O O     . HOH E 5 .   ? -42.442 -22.890 39.463  1.00 38.21 ?  650 HOH A O     1 
HETATM 2992 O O     . HOH E 5 .   ? -18.851 -14.299 -2.715  1.00 20.39 ?  651 HOH A O     1 
HETATM 2993 O O     . HOH E 5 .   ? -24.073 -1.195  -9.087  1.00 32.46 ?  652 HOH A O     1 
HETATM 2994 O O     . HOH E 5 .   ? -28.662 -2.495  20.661  1.00 30.65 ?  653 HOH A O     1 
HETATM 2995 O O     . HOH E 5 .   ? -30.570 -21.843 2.128   1.00 24.86 ?  654 HOH A O     1 
HETATM 2996 O O     . HOH E 5 .   ? -17.071 5.898   0.465   1.00 23.43 ?  655 HOH A O     1 
HETATM 2997 O O     . HOH E 5 .   ? -17.583 -12.743 10.557  1.00 10.88 ?  656 HOH A O     1 
HETATM 2998 O O     . HOH E 5 .   ? -4.021  -6.933  27.186  1.00 30.50 ?  657 HOH A O     1 
HETATM 2999 O O     . HOH E 5 .   ? -9.914  -21.039 11.205  1.00 14.82 ?  658 HOH A O     1 
HETATM 3000 O O     . HOH E 5 .   ? -33.320 -10.535 27.231  1.00 29.90 ?  659 HOH A O     1 
HETATM 3001 O O     . HOH E 5 .   ? -14.955 4.883   0.566   1.00 20.01 ?  660 HOH A O     1 
HETATM 3002 O O     . HOH E 5 .   ? -26.420 -36.314 14.312  1.00 44.33 ?  661 HOH A O     1 
HETATM 3003 O O     . HOH E 5 .   ? -19.164 -6.910  -6.737  1.00 21.49 ?  662 HOH A O     1 
HETATM 3004 O O     . HOH E 5 .   ? -6.296  -8.761  1.410   1.00 20.42 ?  663 HOH A O     1 
HETATM 3005 O O     . HOH E 5 .   ? -10.070 -16.229 31.094  1.00 34.18 ?  664 HOH A O     1 
HETATM 3006 O O     . HOH E 5 .   ? -26.923 -12.493 16.505  1.00 17.32 ?  665 HOH A O     1 
HETATM 3007 O O     . HOH E 5 .   ? -27.542 -8.218  48.478  1.00 41.31 ?  666 HOH A O     1 
HETATM 3008 O O     . HOH E 5 .   ? -25.013 10.675  14.023  1.00 31.69 ?  667 HOH A O     1 
HETATM 3009 O O     . HOH E 5 .   ? -16.386 -21.452 7.963   1.00 19.76 ?  668 HOH A O     1 
HETATM 3010 O O     . HOH E 5 .   ? -11.512 1.870   20.091  1.00 23.97 ?  669 HOH A O     1 
HETATM 3011 O O     . HOH E 5 .   ? -41.860 -27.662 23.255  1.00 31.48 ?  670 HOH A O     1 
HETATM 3012 O O     . HOH E 5 .   ? -14.610 16.742  3.562   1.00 26.60 ?  671 HOH A O     1 
HETATM 3013 O O     . HOH E 5 .   ? 4.056   -9.644  9.939   1.00 27.29 ?  672 HOH A O     1 
HETATM 3014 O O     . HOH E 5 .   ? -23.506 -15.143 43.700  1.00 34.41 ?  673 HOH A O     1 
HETATM 3015 O O     . HOH E 5 .   ? -32.783 -41.602 32.748  1.00 37.38 ?  674 HOH A O     1 
HETATM 3016 O O     . HOH E 5 .   ? -16.344 -24.972 45.819  1.00 37.80 ?  675 HOH A O     1 
HETATM 3017 O O     . HOH E 5 .   ? -23.517 10.716  16.280  1.00 27.27 ?  676 HOH A O     1 
HETATM 3018 O O     . HOH E 5 .   ? -40.569 -15.902 18.945  1.00 29.21 ?  677 HOH A O     1 
HETATM 3019 O O     . HOH E 5 .   ? -30.544 -7.372  4.643   1.00 20.90 ?  678 HOH A O     1 
HETATM 3020 O O     . HOH E 5 .   ? -20.758 -33.106 10.231  1.00 35.00 ?  679 HOH A O     1 
HETATM 3021 O O     . HOH E 5 .   ? -31.776 -7.916  14.189  1.00 28.03 ?  680 HOH A O     1 
HETATM 3022 O O     . HOH E 5 .   ? -1.670  -20.233 6.118   1.00 21.85 ?  681 HOH A O     1 
HETATM 3023 O O     . HOH E 5 .   ? -25.535 -22.920 46.459  1.00 33.39 ?  682 HOH A O     1 
HETATM 3024 O O     . HOH E 5 .   ? -9.176  8.257   21.587  1.00 32.17 ?  683 HOH A O     1 
HETATM 3025 O O     . HOH E 5 .   ? -12.695 -12.940 -3.220  1.00 19.70 ?  684 HOH A O     1 
HETATM 3026 O O     . HOH E 5 .   ? -20.825 -16.711 46.781  1.00 32.75 ?  685 HOH A O     1 
HETATM 3027 O O     . HOH E 5 .   ? -6.133  6.067   5.444   1.00 18.43 ?  686 HOH A O     1 
HETATM 3028 O O     . HOH E 5 .   ? -14.501 -20.559 45.517  1.00 45.10 ?  687 HOH A O     1 
HETATM 3029 O O     . HOH E 5 .   ? -11.359 -14.100 20.269  1.00 18.51 ?  688 HOH A O     1 
HETATM 3030 O O     . HOH E 5 .   ? -27.708 -3.493  29.427  1.00 34.65 ?  689 HOH A O     1 
HETATM 3031 O O     . HOH E 5 .   ? -15.152 -19.556 6.072   1.00 27.80 ?  690 HOH A O     1 
HETATM 3032 O O     . HOH E 5 .   ? -31.265 -17.576 0.635   1.00 44.12 ?  691 HOH A O     1 
HETATM 3033 O O     . HOH E 5 .   ? 1.704   -15.982 13.800  1.00 22.30 ?  692 HOH A O     1 
HETATM 3034 O O     . HOH E 5 .   ? -37.663 -20.892 7.016   1.00 23.80 ?  693 HOH A O     1 
HETATM 3035 O O     . HOH E 5 .   ? -30.905 -3.450  8.129   1.00 31.98 ?  694 HOH A O     1 
HETATM 3036 O O     . HOH E 5 .   ? -17.797 -28.078 19.631  1.00 23.75 ?  695 HOH A O     1 
HETATM 3037 O O     . HOH E 5 .   ? -2.564  -6.095  5.090   1.00 19.61 ?  696 HOH A O     1 
HETATM 3038 O O     . HOH E 5 .   ? -22.191 -31.786 38.404  1.00 34.59 ?  697 HOH A O     1 
HETATM 3039 O O     . HOH E 5 .   ? -8.140  -1.254  -5.403  1.00 26.63 ?  698 HOH A O     1 
HETATM 3040 O O     . HOH E 5 .   ? -21.330 3.810   20.700  1.00 30.23 ?  699 HOH A O     1 
HETATM 3041 O O     . HOH E 5 .   ? -2.814  2.480   17.591  1.00 33.48 ?  700 HOH A O     1 
HETATM 3042 O O     . HOH E 5 .   ? -27.219 11.566  1.417   1.00 23.75 ?  701 HOH A O     1 
HETATM 3043 O O     . HOH E 5 .   ? -39.373 -28.103 44.865  1.00 34.25 ?  702 HOH A O     1 
HETATM 3044 O O     . HOH E 5 .   ? -23.910 -3.175  27.767  1.00 34.02 ?  703 HOH A O     1 
HETATM 3045 O O     . HOH E 5 .   ? -41.555 -25.512 43.336  1.00 35.13 ?  704 HOH A O     1 
HETATM 3046 O O     . HOH E 5 .   ? -19.051 -21.696 23.136  1.00 19.16 ?  705 HOH A O     1 
HETATM 3047 O O     . HOH E 5 .   ? -22.680 8.349   17.772  1.00 31.16 ?  706 HOH A O     1 
HETATM 3048 O O     . HOH E 5 .   ? -20.203 -10.232 39.239  1.00 37.26 ?  707 HOH A O     1 
HETATM 3049 O O     . HOH E 5 .   ? -41.594 -23.665 19.167  1.00 28.19 ?  708 HOH A O     1 
HETATM 3050 O O     . HOH E 5 .   ? -30.243 5.080   -5.378  1.00 23.54 ?  709 HOH A O     1 
HETATM 3051 O O     . HOH E 5 .   ? -21.279 -3.119  16.476  1.00 15.06 ?  710 HOH A O     1 
HETATM 3052 O O     . HOH E 5 .   ? -23.276 -4.969  15.815  1.00 21.65 ?  711 HOH A O     1 
HETATM 3053 O O     . HOH E 5 .   ? -36.354 -24.339 43.203  1.00 34.88 ?  712 HOH A O     1 
HETATM 3054 O O     . HOH E 5 .   ? -36.456 -33.585 28.747  1.00 31.02 ?  713 HOH A O     1 
HETATM 3055 O O     . HOH E 5 .   ? -15.591 -12.059 -3.755  1.00 22.88 ?  714 HOH A O     1 
HETATM 3056 O O     . HOH E 5 .   ? -27.078 12.128  3.321   1.00 30.13 ?  715 HOH A O     1 
HETATM 3057 O O     . HOH E 5 .   ? -21.700 -29.518 32.865  1.00 32.52 ?  716 HOH A O     1 
HETATM 3058 O O     . HOH E 5 .   ? 3.067   -9.916  24.096  1.00 32.04 ?  717 HOH A O     1 
HETATM 3059 O O     . HOH E 5 .   ? 2.115   -16.189 17.350  1.00 27.15 ?  718 HOH A O     1 
HETATM 3060 O O     . HOH E 5 .   ? -19.135 -11.683 -6.611  1.00 43.02 ?  719 HOH A O     1 
HETATM 3061 O O     . HOH E 5 .   ? -40.052 -31.878 35.839  1.00 26.22 ?  720 HOH A O     1 
HETATM 3062 O O     . HOH E 5 .   ? -29.053 8.021   -4.398  1.00 20.44 ?  721 HOH A O     1 
HETATM 3063 O O     . HOH E 5 .   ? 0.338   -3.244  1.009   1.00 32.43 ?  722 HOH A O     1 
HETATM 3064 O O     . HOH E 5 .   ? -17.945 -12.361 39.461  1.00 40.46 ?  723 HOH A O     1 
HETATM 3065 O O     . HOH E 5 .   ? -15.953 11.662  -0.940  1.00 24.00 ?  724 HOH A O     1 
HETATM 3066 O O     . HOH E 5 .   ? -42.607 -27.893 45.868  1.00 26.70 ?  725 HOH A O     1 
HETATM 3067 O O     . HOH E 5 .   ? -8.998  -17.780 43.050  1.00 31.77 ?  726 HOH A O     1 
HETATM 3068 O O     . HOH E 5 .   ? -21.953 -7.304  16.543  1.00 22.09 ?  727 HOH A O     1 
HETATM 3069 O O     . HOH E 5 .   ? -19.867 -9.933  41.965  1.00 36.01 ?  728 HOH A O     1 
HETATM 3070 O O     . HOH E 5 .   ? -19.257 13.301  20.159  1.00 32.60 ?  729 HOH A O     1 
HETATM 3071 O O     . HOH E 5 .   ? -3.325  -8.845  28.381  1.00 52.19 ?  730 HOH A O     1 
HETATM 3072 O O     . HOH E 5 .   ? -44.164 -17.640 21.552  1.00 32.29 ?  731 HOH A O     1 
HETATM 3073 O O     . HOH E 5 .   ? -33.635 -5.852  23.559  1.00 37.90 ?  732 HOH A O     1 
HETATM 3074 O O     . HOH E 5 .   ? -15.028 -11.629 10.643  1.00 29.94 ?  733 HOH A O     1 
HETATM 3075 O O     . HOH E 5 .   ? -32.259 2.540   6.444   1.00 31.43 ?  734 HOH A O     1 
HETATM 3076 O O     . HOH E 5 .   ? -25.733 -14.453 46.918  1.00 34.50 ?  735 HOH A O     1 
HETATM 3077 O O     . HOH E 5 .   ? 3.829   -11.696 23.947  1.00 46.75 ?  736 HOH A O     1 
HETATM 3078 O O     . HOH E 5 .   ? -13.687 -25.676 40.321  1.00 32.84 ?  737 HOH A O     1 
HETATM 3079 O O     . HOH E 5 .   ? 1.799   -4.121  23.979  1.00 23.97 ?  738 HOH A O     1 
HETATM 3080 O O     . HOH E 5 .   ? -30.480 -24.008 44.696  1.00 36.23 ?  739 HOH A O     1 
HETATM 3081 O O     . HOH E 5 .   ? -29.475 -26.296 8.200   1.00 21.64 ?  740 HOH A O     1 
HETATM 3082 O O     . HOH E 5 .   ? -28.098 -13.906 18.241  1.00 21.34 ?  741 HOH A O     1 
HETATM 3083 O O     . HOH E 5 .   ? -30.476 -23.907 5.636   1.00 24.66 ?  742 HOH A O     1 
HETATM 3084 O O     . HOH E 5 .   ? -27.162 -20.953 -1.168  1.00 34.94 ?  743 HOH A O     1 
HETATM 3085 O O     . HOH E 5 .   ? -25.256 -16.697 45.278  1.00 40.80 ?  744 HOH A O     1 
HETATM 3086 O O     . HOH E 5 .   ? -26.553 -1.171  20.483  1.00 24.46 ?  745 HOH A O     1 
HETATM 3087 O O     . HOH E 5 .   ? -3.363  -5.825  0.000   0.50 28.96 ?  746 HOH A O     1 
HETATM 3088 O O     . HOH E 5 .   ? -11.735 -23.251 7.769   1.00 35.91 ?  747 HOH A O     1 
HETATM 3089 O O     . HOH E 5 .   ? -13.827 0.076   20.910  1.00 27.76 ?  748 HOH A O     1 
HETATM 3090 O O     . HOH E 5 .   ? 3.651   -6.315  16.202  1.00 43.55 ?  749 HOH A O     1 
HETATM 3091 O O     . HOH E 5 .   ? -19.838 -14.078 -5.669  1.00 33.56 ?  750 HOH A O     1 
HETATM 3092 O O     . HOH E 5 .   ? -32.591 -4.875  25.852  1.00 39.47 ?  751 HOH A O     1 
HETATM 3093 O O     . HOH E 5 .   ? -33.176 -7.867  3.911   1.00 31.41 ?  752 HOH A O     1 
HETATM 3094 O O     . HOH E 5 .   ? -18.921 1.232   -9.917  1.00 32.09 ?  753 HOH A O     1 
HETATM 3095 O O     . HOH E 5 .   ? -21.216 -7.100  -8.752  1.00 33.07 ?  754 HOH A O     1 
HETATM 3096 O O     . HOH E 5 .   ? -16.149 -17.461 -1.679  1.00 44.90 ?  755 HOH A O     1 
HETATM 3097 O O     . HOH E 5 .   ? -18.316 -26.375 9.410   1.00 26.60 ?  756 HOH A O     1 
HETATM 3098 O O     . HOH E 5 .   ? -2.062  1.289   20.031  1.00 34.47 ?  757 HOH A O     1 
HETATM 3099 O O     . HOH E 5 .   ? -24.470 -34.000 22.934  1.00 53.03 ?  758 HOH A O     1 
HETATM 3100 O O     . HOH E 5 .   ? -31.684 -26.453 6.602   1.00 32.55 ?  759 HOH A O     1 
HETATM 3101 O O     . HOH E 5 .   ? -34.007 -33.950 28.173  1.00 30.04 ?  760 HOH A O     1 
HETATM 3102 O O     . HOH E 5 .   ? -28.057 -0.952  11.089  1.00 25.69 ?  761 HOH A O     1 
HETATM 3103 O O     . HOH E 5 .   ? -23.729 -6.195  -8.411  1.00 25.58 ?  762 HOH A O     1 
HETATM 3104 O O     . HOH E 5 .   ? -4.382  -20.486 5.289   1.00 45.48 ?  763 HOH A O     1 
HETATM 3105 O O     . HOH E 5 .   ? -19.749 -1.520  -8.426  1.00 27.07 ?  764 HOH A O     1 
HETATM 3106 O O     . HOH E 5 .   ? -12.759 -24.238 13.606  1.00 31.49 ?  765 HOH A O     1 
HETATM 3107 O O     . HOH E 5 .   ? -24.353 -18.482 47.259  1.00 42.67 ?  766 HOH A O     1 
HETATM 3108 O O     . HOH E 5 .   ? -11.843 -16.299 -1.773  1.00 26.20 ?  767 HOH A O     1 
HETATM 3109 O O     . HOH E 5 .   ? -19.958 -9.392  -7.154  1.00 27.60 ?  768 HOH A O     1 
HETATM 3110 O O     . HOH E 5 .   ? -29.229 -1.060  16.605  1.00 37.15 ?  769 HOH A O     1 
HETATM 3111 O O     . HOH E 5 .   ? -29.154 -34.459 18.689  1.00 33.49 ?  770 HOH A O     1 
HETATM 3112 O O     . HOH E 5 .   ? -1.928  0.103   0.119   1.00 33.95 ?  771 HOH A O     1 
HETATM 3113 O O     . HOH E 5 .   ? -42.565 -16.989 17.069  1.00 43.89 ?  772 HOH A O     1 
HETATM 3114 O O     . HOH E 5 .   ? -12.102 -18.676 -0.666  1.00 26.92 ?  773 HOH A O     1 
HETATM 3115 O O     . HOH E 5 .   ? -32.892 -27.134 9.315   1.00 29.83 ?  774 HOH A O     1 
HETATM 3116 O O     . HOH E 5 .   ? -27.457 -36.333 24.257  1.00 30.67 ?  775 HOH A O     1 
HETATM 3117 O O     . HOH E 5 .   ? -29.004 -34.258 11.812  1.00 35.04 ?  776 HOH A O     1 
HETATM 3118 O O     . HOH E 5 .   ? -34.944 -3.953  27.029  1.00 43.22 ?  777 HOH A O     1 
HETATM 3119 O O     . HOH E 5 .   ? -4.356  4.793   3.564   1.00 33.71 ?  778 HOH A O     1 
HETATM 3120 O O     . HOH E 5 .   ? -16.146 -25.334 8.868   1.00 36.10 ?  779 HOH A O     1 
HETATM 3121 O O     . HOH E 5 .   ? -0.290  -11.846 30.799  1.00 31.73 ?  780 HOH A O     1 
HETATM 3122 O O     . HOH E 5 .   ? -8.040  -13.926 0.000   0.50 20.94 ?  781 HOH A O     1 
HETATM 3123 O O     . HOH E 5 .   ? -22.138 -12.765 44.837  1.00 34.33 ?  782 HOH A O     1 
HETATM 3124 O O     . HOH E 5 .   ? -13.648 -23.543 6.582   1.00 36.32 ?  783 HOH A O     1 
HETATM 3125 O O     . HOH E 5 .   ? -34.727 -28.028 43.253  1.00 39.87 ?  784 HOH A O     1 
HETATM 3126 O O     . HOH E 5 .   ? -13.192 3.299   -7.722  1.00 37.27 ?  785 HOH A O     1 
HETATM 3127 O O     . HOH E 5 .   ? -19.591 -3.583  24.705  1.00 31.98 ?  786 HOH A O     1 
HETATM 3128 O O     . HOH E 5 .   ? -29.191 9.505   1.681   1.00 47.07 ?  787 HOH A O     1 
HETATM 3129 O O     . HOH E 5 .   ? -39.198 -24.120 15.577  1.00 41.08 ?  788 HOH A O     1 
HETATM 3130 O O     . HOH E 5 .   ? -51.080 -20.012 29.212  1.00 43.52 ?  789 HOH A O     1 
HETATM 3131 O O     . HOH E 5 .   ? -43.185 -25.241 45.297  1.00 36.90 ?  790 HOH A O     1 
HETATM 3132 O O     . HOH E 5 .   ? -38.045 -28.182 47.102  1.00 30.20 ?  791 HOH A O     1 
HETATM 3133 O O     . HOH E 5 .   ? -29.911 -23.966 3.316   1.00 26.10 ?  792 HOH A O     1 
HETATM 3134 O O     . HOH E 5 .   ? -32.364 -6.103  18.622  1.00 36.08 ?  793 HOH A O     1 
HETATM 3135 O O     . HOH E 5 .   ? -13.834 -27.845 39.035  1.00 39.64 ?  794 HOH A O     1 
HETATM 3136 O O     . HOH E 5 .   ? -27.333 0.659   17.689  1.00 41.54 ?  795 HOH A O     1 
HETATM 3137 O O     . HOH E 5 .   ? -31.552 -4.246  11.019  1.00 28.50 ?  796 HOH A O     1 
HETATM 3138 O O     . HOH E 5 .   ? -22.363 -31.585 33.746  1.00 42.28 ?  797 HOH A O     1 
HETATM 3139 O O     . HOH E 5 .   ? -5.767  -23.607 18.887  1.00 42.50 ?  798 HOH A O     1 
HETATM 3140 O O     . HOH E 5 .   ? -31.899 -31.051 9.080   1.00 28.18 ?  799 HOH A O     1 
HETATM 3141 O O     . HOH E 5 .   ? -19.079 3.399   -9.625  1.00 37.99 ?  800 HOH A O     1 
HETATM 3142 O O     . HOH E 5 .   ? -28.808 -20.048 0.976   1.00 24.40 ?  801 HOH A O     1 
HETATM 3143 O O     . HOH E 5 .   ? -15.398 -28.454 18.497  1.00 37.31 ?  802 HOH A O     1 
HETATM 3144 O O     . HOH E 5 .   ? -15.057 4.789   -9.523  1.00 36.31 ?  803 HOH A O     1 
HETATM 3145 O O     . HOH E 5 .   ? -23.183 13.075  17.547  1.00 27.45 ?  804 HOH A O     1 
HETATM 3146 O O     . HOH E 5 .   ? 5.165   -6.977  18.073  1.00 44.54 ?  805 HOH A O     1 
HETATM 3147 O O     . HOH E 5 .   ? 5.612   -10.015 23.045  1.00 48.48 ?  806 HOH A O     1 
HETATM 3148 O O     . HOH E 5 .   ? -34.432 -28.815 8.758   1.00 37.22 ?  807 HOH A O     1 
HETATM 3149 O O     . HOH E 5 .   ? -32.260 -5.479  9.470   1.00 40.87 ?  808 HOH A O     1 
HETATM 3150 O O     . HOH E 5 .   ? -29.062 0.591   13.343  1.00 33.27 ?  809 HOH A O     1 
HETATM 3151 O O     . HOH E 5 .   ? -44.129 -16.007 17.166  1.00 57.20 ?  810 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   . PRO A 1   ? 0.4005 0.4572 0.4247 -0.0270 0.0677  0.0731  7   PRO A N   
2    C CA  . PRO A 1   ? 0.3684 0.4160 0.3847 -0.0292 0.0668  0.0698  7   PRO A CA  
3    C C   . PRO A 1   ? 0.3252 0.3737 0.3413 -0.0339 0.0612  0.0676  7   PRO A C   
4    O O   . PRO A 1   ? 0.2702 0.3266 0.2924 -0.0365 0.0593  0.0692  7   PRO A O   
5    C CB  . PRO A 1   ? 0.3953 0.4438 0.4124 -0.0293 0.0706  0.0716  7   PRO A CB  
6    C CG  . PRO A 1   ? 0.3860 0.4461 0.4130 -0.0290 0.0713  0.0756  7   PRO A CG  
7    C CD  . PRO A 1   ? 0.4874 0.5509 0.5177 -0.0261 0.0711  0.0768  7   PRO A CD  
8    N N   . HIS A 2   ? 0.3325 0.3730 0.3417 -0.0350 0.0586  0.0639  8   HIS A N   
9    C CA  . HIS A 2   ? 0.2879 0.3289 0.2968 -0.0393 0.0534  0.0618  8   HIS A CA  
10   C C   . HIS A 2   ? 0.2867 0.3239 0.2919 -0.0426 0.0529  0.0603  8   HIS A C   
11   O O   . HIS A 2   ? 0.2124 0.2511 0.2181 -0.0465 0.0488  0.0590  8   HIS A O   
12   C CB  . HIS A 2   ? 0.3578 0.3926 0.3617 -0.0392 0.0504  0.0587  8   HIS A CB  
13   C CG  . HIS A 2   ? 0.4342 0.4736 0.4423 -0.0367 0.0500  0.0602  8   HIS A CG  
14   N ND1 . HIS A 2   ? 0.3923 0.4393 0.4063 -0.0385 0.0462  0.0611  8   HIS A ND1 
15   C CD2 . HIS A 2   ? 0.4470 0.4847 0.4545 -0.0325 0.0530  0.0610  8   HIS A CD2 
16   C CE1 . HIS A 2   ? 0.4484 0.4981 0.4650 -0.0355 0.0469  0.0623  8   HIS A CE1 
17   N NE2 . HIS A 2   ? 0.4947 0.5390 0.5076 -0.0318 0.0510  0.0623  8   HIS A NE2 
18   N N   . MET A 3   ? 0.2421 0.2741 0.2433 -0.0410 0.0571  0.0604  9   MET A N   
19   C CA  . MET A 3   ? 0.2020 0.2300 0.1994 -0.0436 0.0573  0.0591  9   MET A CA  
20   C C   . MET A 3   ? 0.1998 0.2213 0.1912 -0.0470 0.0530  0.0552  9   MET A C   
21   O O   . MET A 3   ? 0.2176 0.2403 0.2093 -0.0507 0.0505  0.0544  9   MET A O   
22   C CB  . MET A 3   ? 0.1762 0.2133 0.1808 -0.0458 0.0573  0.0618  9   MET A CB  
23   C CG  . MET A 3   ? 0.1754 0.2187 0.1859 -0.0425 0.0619  0.0658  9   MET A CG  
24   S SD  . MET A 3   ? 0.2728 0.3260 0.2915 -0.0448 0.0626  0.0691  9   MET A SD  
25   C CE  . MET A 3   ? 0.5523 0.6111 0.5770 -0.0400 0.0671  0.0726  9   MET A CE  
26   N N   . GLY A 4   ? 0.2165 0.2309 0.2025 -0.0455 0.0521  0.0527  10  GLY A N   
27   C CA  . GLY A 4   ? 0.2213 0.2288 0.2012 -0.0482 0.0484  0.0489  10  GLY A CA  
28   C C   . GLY A 4   ? 0.2537 0.2650 0.2365 -0.0506 0.0433  0.0480  10  GLY A C   
29   O O   . GLY A 4   ? 0.2786 0.2836 0.2562 -0.0521 0.0403  0.0449  10  GLY A O   
30   N N   . ALA A 5   ? 0.2042 0.2256 0.1951 -0.0511 0.0422  0.0507  11  ALA A N   
31   C CA  . ALA A 5   ? 0.2412 0.2665 0.2349 -0.0533 0.0374  0.0500  11  ALA A CA  
32   C C   . ALA A 5   ? 0.2572 0.2794 0.2491 -0.0505 0.0369  0.0491  11  ALA A C   
33   O O   . ALA A 5   ? 0.2491 0.2694 0.2402 -0.0466 0.0405  0.0500  11  ALA A O   
34   C CB  . ALA A 5   ? 0.2130 0.2499 0.2159 -0.0544 0.0364  0.0533  11  ALA A CB  
35   N N   . LEU A 6   ? 0.2620 0.2833 0.2530 -0.0527 0.0325  0.0471  12  LEU A N   
36   C CA  . LEU A 6   ? 0.2753 0.2940 0.2649 -0.0504 0.0315  0.0460  12  LEU A CA  
37   C C   . LEU A 6   ? 0.2701 0.2983 0.2674 -0.0495 0.0305  0.0487  12  LEU A C   
38   O O   . LEU A 6   ? 0.2425 0.2779 0.2450 -0.0522 0.0278  0.0499  12  LEU A O   
39   C CB  . LEU A 6   ? 0.2511 0.2635 0.2355 -0.0531 0.0273  0.0424  12  LEU A CB  
40   C CG  . LEU A 6   ? 0.3126 0.3145 0.2887 -0.0540 0.0275  0.0391  12  LEU A CG  
41   C CD1 . LEU A 6   ? 0.2974 0.2946 0.2698 -0.0563 0.0230  0.0360  12  LEU A CD1 
42   C CD2 . LEU A 6   ? 0.3381 0.3333 0.3097 -0.0499 0.0317  0.0388  12  LEU A CD2 
43   N N   . HIS A 7   ? 0.2491 0.2771 0.2470 -0.0455 0.0327  0.0497  13  HIS A N   
44   C CA  . HIS A 7   ? 0.2751 0.3103 0.2790 -0.0445 0.0311  0.0515  13  HIS A CA  
45   C C   . HIS A 7   ? 0.2692 0.2988 0.2695 -0.0412 0.0320  0.0502  13  HIS A C   
46   O O   . HIS A 7   ? 0.2598 0.2870 0.2588 -0.0375 0.0361  0.0511  13  HIS A O   
47   C CB  . HIS A 7   ? 0.3309 0.3757 0.3425 -0.0428 0.0337  0.0556  13  HIS A CB  
48   C CG  . HIS A 7   ? 0.4820 0.5351 0.5002 -0.0426 0.0313  0.0574  13  HIS A CG  
49   N ND1 . HIS A 7   ? 0.6139 0.6702 0.6353 -0.0387 0.0333  0.0594  13  HIS A ND1 
50   C CD2 . HIS A 7   ? 0.5751 0.6335 0.5968 -0.0457 0.0268  0.0574  13  HIS A CD2 
51   C CE1 . HIS A 7   ? 0.6532 0.7166 0.6800 -0.0395 0.0303  0.0606  13  HIS A CE1 
52   N NE2 . HIS A 7   ? 0.5838 0.6485 0.6108 -0.0437 0.0263  0.0594  13  HIS A NE2 
53   N N   . VAL A 8   ? 0.2205 0.2477 0.2190 -0.0425 0.0282  0.0481  14  VAL A N   
54   C CA  . VAL A 8   ? 0.2275 0.2487 0.2222 -0.0397 0.0286  0.0465  14  VAL A CA  
55   C C   . VAL A 8   ? 0.2388 0.2672 0.2395 -0.0375 0.0283  0.0488  14  VAL A C   
56   O O   . VAL A 8   ? 0.2192 0.2548 0.2250 -0.0395 0.0252  0.0500  14  VAL A O   
57   C CB  . VAL A 8   ? 0.1929 0.2070 0.1820 -0.0423 0.0247  0.0428  14  VAL A CB  
58   C CG1 . VAL A 8   ? 0.1811 0.1884 0.1661 -0.0393 0.0254  0.0411  14  VAL A CG1 
59   C CG2 . VAL A 8   ? 0.1899 0.1975 0.1735 -0.0447 0.0249  0.0406  14  VAL A CG2 
60   N N   . VAL A 9   ? 0.2041 0.2307 0.2042 -0.0334 0.0315  0.0496  15  VAL A N   
61   C CA  . VAL A 9   ? 0.2342 0.2664 0.2391 -0.0310 0.0312  0.0514  15  VAL A CA  
62   C C   . VAL A 9   ? 0.1988 0.2238 0.1989 -0.0295 0.0302  0.0489  15  VAL A C   
63   O O   . VAL A 9   ? 0.1991 0.2158 0.1934 -0.0278 0.0324  0.0471  15  VAL A O   
64   C CB  . VAL A 9   ? 0.2455 0.2827 0.2547 -0.0272 0.0357  0.0548  15  VAL A CB  
65   C CG1 . VAL A 9   ? 0.2429 0.2853 0.2566 -0.0246 0.0354  0.0565  15  VAL A CG1 
66   C CG2 . VAL A 9   ? 0.2780 0.3228 0.2925 -0.0289 0.0364  0.0574  15  VAL A CG2 
67   N N   . ILE A 10  ? 0.1896 0.2176 0.1921 -0.0303 0.0267  0.0487  16  ILE A N   
68   C CA  . ILE A 10  ? 0.1812 0.2034 0.1801 -0.0289 0.0255  0.0465  16  ILE A CA  
69   C C   . ILE A 10  ? 0.1887 0.2164 0.1923 -0.0253 0.0269  0.0490  16  ILE A C   
70   O O   . ILE A 10  ? 0.1775 0.2138 0.1873 -0.0259 0.0253  0.0513  16  ILE A O   
71   C CB  . ILE A 10  ? 0.1776 0.1987 0.1753 -0.0326 0.0203  0.0443  16  ILE A CB  
72   C CG1 . ILE A 10  ? 0.1506 0.1671 0.1442 -0.0364 0.0187  0.0421  16  ILE A CG1 
73   C CG2 . ILE A 10  ? 0.1589 0.1736 0.1528 -0.0310 0.0193  0.0421  16  ILE A CG2 
74   C CD1 . ILE A 10  ? 0.1723 0.1898 0.1661 -0.0403 0.0135  0.0405  16  ILE A CD1 
75   N N   . VAL A 11  ? 0.2163 0.2390 0.2171 -0.0216 0.0299  0.0486  17  VAL A N   
76   C CA  . VAL A 11  ? 0.1913 0.2183 0.1961 -0.0179 0.0315  0.0508  17  VAL A CA  
77   C C   . VAL A 11  ? 0.1540 0.1766 0.1561 -0.0176 0.0289  0.0486  17  VAL A C   
78   O O   . VAL A 11  ? 0.1885 0.2024 0.1848 -0.0164 0.0298  0.0461  17  VAL A O   
79   C CB  . VAL A 11  ? 0.2365 0.2617 0.2404 -0.0138 0.0367  0.0521  17  VAL A CB  
80   C CG1 . VAL A 11  ? 0.2319 0.2617 0.2400 -0.0100 0.0382  0.0544  17  VAL A CG1 
81   C CG2 . VAL A 11  ? 0.2498 0.2794 0.2564 -0.0143 0.0392  0.0544  17  VAL A CG2 
82   N N   . GLY A 12  ? 0.1819 0.2105 0.1883 -0.0186 0.0257  0.0494  18  GLY A N   
83   C CA  . GLY A 12  ? 0.1731 0.1983 0.1777 -0.0183 0.0231  0.0477  18  GLY A CA  
84   C C   . GLY A 12  ? 0.1657 0.1903 0.1692 -0.0227 0.0182  0.0457  18  GLY A C   
85   O O   . GLY A 12  ? 0.1685 0.1877 0.1677 -0.0254 0.0172  0.0434  18  GLY A O   
86   N N   . GLY A 13  ? 0.1487 0.1786 0.1560 -0.0233 0.0152  0.0465  19  GLY A N   
87   C CA  . GLY A 13  ? 0.1149 0.1444 0.1214 -0.0273 0.0105  0.0448  19  GLY A CA  
88   C C   . GLY A 13  ? 0.1299 0.1539 0.1331 -0.0270 0.0083  0.0425  19  GLY A C   
89   O O   . GLY A 13  ? 0.1539 0.1814 0.1595 -0.0281 0.0050  0.0428  19  GLY A O   
90   N N   . GLY A 14  ? 0.1438 0.1590 0.1415 -0.0253 0.0101  0.0403  20  GLY A N   
91   C CA  . GLY A 14  ? 0.1194 0.1283 0.1136 -0.0250 0.0082  0.0379  20  GLY A CA  
92   C C   . GLY A 14  ? 0.1244 0.1272 0.1138 -0.0289 0.0052  0.0348  20  GLY A C   
93   O O   . GLY A 14  ? 0.1314 0.1367 0.1216 -0.0323 0.0035  0.0348  20  GLY A O   
94   N N   . PHE A 15  ? 0.1287 0.1233 0.1134 -0.0284 0.0045  0.0321  21  PHE A N   
95   C CA  . PHE A 15  ? 0.1257 0.1137 0.1056 -0.0319 0.0018  0.0291  21  PHE A CA  
96   C C   . PHE A 15  ? 0.1645 0.1498 0.1417 -0.0334 0.0034  0.0284  21  PHE A C   
97   O O   . PHE A 15  ? 0.1466 0.1316 0.1226 -0.0372 0.0010  0.0273  21  PHE A O   
98   C CB  . PHE A 15  ? 0.1553 0.1346 0.1306 -0.0305 0.0016  0.0264  21  PHE A CB  
99   C CG  . PHE A 15  ? 0.1548 0.1358 0.1319 -0.0302 -0.0010 0.0264  21  PHE A CG  
100  C CD1 . PHE A 15  ? 0.1605 0.1405 0.1367 -0.0337 -0.0052 0.0249  21  PHE A CD1 
101  C CD2 . PHE A 15  ? 0.1542 0.1375 0.1339 -0.0265 0.0007  0.0280  21  PHE A CD2 
102  C CE1 . PHE A 15  ? 0.1489 0.1303 0.1267 -0.0334 -0.0076 0.0249  21  PHE A CE1 
103  C CE2 . PHE A 15  ? 0.1324 0.1171 0.1137 -0.0261 -0.0017 0.0280  21  PHE A CE2 
104  C CZ  . PHE A 15  ? 0.1449 0.1286 0.1252 -0.0296 -0.0058 0.0265  21  PHE A CZ  
105  N N   . GLY A 16  ? 0.1285 0.1118 0.1046 -0.0304 0.0075  0.0291  22  GLY A N   
106  C CA  . GLY A 16  ? 0.1663 0.1469 0.1396 -0.0316 0.0092  0.0285  22  GLY A CA  
107  C C   . GLY A 16  ? 0.1383 0.1272 0.1161 -0.0336 0.0090  0.0309  22  GLY A C   
108  O O   . GLY A 16  ? 0.1567 0.1445 0.1329 -0.0369 0.0076  0.0299  22  GLY A O   
109  N N   . GLY A 17  ? 0.1408 0.1381 0.1246 -0.0317 0.0103  0.0340  23  GLY A N   
110  C CA  . GLY A 17  ? 0.1451 0.1505 0.1336 -0.0333 0.0104  0.0365  23  GLY A CA  
111  C C   . GLY A 17  ? 0.1452 0.1541 0.1353 -0.0377 0.0060  0.0360  23  GLY A C   
112  O O   . GLY A 17  ? 0.1609 0.1723 0.1518 -0.0403 0.0056  0.0364  23  GLY A O   
113  N N   . ILE A 18  ? 0.1430 0.1525 0.1338 -0.0385 0.0026  0.0353  24  ILE A N   
114  C CA  . ILE A 18  ? 0.1272 0.1401 0.1195 -0.0427 -0.0016 0.0350  24  ILE A CA  
115  C C   . ILE A 18  ? 0.1377 0.1433 0.1244 -0.0460 -0.0032 0.0319  24  ILE A C   
116  O O   . ILE A 18  ? 0.1398 0.1480 0.1273 -0.0497 -0.0056 0.0318  24  ILE A O   
117  C CB  . ILE A 18  ? 0.1121 0.1277 0.1067 -0.0429 -0.0048 0.0351  24  ILE A CB  
118  C CG1 . ILE A 18  ? 0.1231 0.1302 0.1127 -0.0422 -0.0059 0.0322  24  ILE A CG1 
119  C CG2 . ILE A 18  ? 0.1275 0.1510 0.1280 -0.0397 -0.0032 0.0383  24  ILE A CG2 
120  C CD1 . ILE A 18  ? 0.1285 0.1374 0.1194 -0.0435 -0.0099 0.0318  24  ILE A CD1 
121  N N   . ALA A 19  ? 0.1360 0.1325 0.1170 -0.0449 -0.0022 0.0294  25  ALA A N   
122  C CA  . ALA A 19  ? 0.1313 0.1208 0.1069 -0.0479 -0.0035 0.0266  25  ALA A CA  
123  C C   . ALA A 19  ? 0.1670 0.1575 0.1424 -0.0488 -0.0014 0.0273  25  ALA A C   
124  O O   . ALA A 19  ? 0.1562 0.1462 0.1303 -0.0525 -0.0033 0.0263  25  ALA A O   
125  C CB  . ALA A 19  ? 0.1616 0.1411 0.1313 -0.0462 -0.0027 0.0238  25  ALA A CB  
126  N N   . ALA A 20  ? 0.1374 0.1290 0.1138 -0.0456 0.0028  0.0290  26  ALA A N   
127  C CA  . ALA A 20  ? 0.1596 0.1522 0.1359 -0.0462 0.0052  0.0299  26  ALA A CA  
128  C C   . ALA A 20  ? 0.1428 0.1446 0.1247 -0.0487 0.0038  0.0321  26  ALA A C   
129  O O   . ALA A 20  ? 0.1421 0.1437 0.1229 -0.0516 0.0033  0.0317  26  ALA A O   
130  C CB  . ALA A 20  ? 0.1276 0.1198 0.1041 -0.0420 0.0100  0.0315  26  ALA A CB  
131  N N   . ALA A 21  ? 0.1626 0.1724 0.1504 -0.0477 0.0031  0.0346  27  ALA A N   
132  C CA  . ALA A 21  ? 0.1319 0.1508 0.1253 -0.0501 0.0016  0.0368  27  ALA A CA  
133  C C   . ALA A 21  ? 0.1386 0.1568 0.1308 -0.0547 -0.0029 0.0351  27  ALA A C   
134  O O   . ALA A 21  ? 0.1410 0.1631 0.1351 -0.0575 -0.0037 0.0358  27  ALA A O   
135  C CB  . ALA A 21  ? 0.1306 0.1577 0.1304 -0.0480 0.0014  0.0396  27  ALA A CB  
136  N N   . SER A 22  ? 0.1274 0.1412 0.1168 -0.0554 -0.0057 0.0329  28  SER A N   
137  C CA  . SER A 22  ? 0.1743 0.1871 0.1622 -0.0597 -0.0100 0.0311  28  SER A CA  
138  C C   . SER A 22  ? 0.1950 0.2024 0.1784 -0.0617 -0.0097 0.0289  28  SER A C   
139  O O   . SER A 22  ? 0.1983 0.2079 0.1822 -0.0626 -0.0121 0.0276  28  SER A O   
140  C CB  . SER A 22  ? 0.2235 0.2312 0.2085 -0.0597 -0.0126 0.0289  28  SER A CB  
141  O OG  . SER A 22  ? 0.3308 0.3368 0.3134 -0.0600 -0.0162 0.0257  28  SER A OG  
142  N N   . GLN A 23  ? 0.1967 0.1968 0.1752 -0.0604 -0.0069 0.0278  29  GLN A N   
143  C CA  . GLN A 23  ? 0.2072 0.2018 0.1812 -0.0613 -0.0067 0.0252  29  GLN A CA  
144  C C   . GLN A 23  ? 0.2041 0.2036 0.1808 -0.0624 -0.0044 0.0275  29  GLN A C   
145  O O   . GLN A 23  ? 0.2255 0.2251 0.2015 -0.0635 -0.0060 0.0258  29  GLN A O   
146  C CB  . GLN A 23  ? 0.2276 0.2123 0.1953 -0.0598 -0.0046 0.0231  29  GLN A CB  
147  C CG  . GLN A 23  ? 0.3474 0.3270 0.3124 -0.0583 -0.0070 0.0203  29  GLN A CG  
148  N N   . LEU A 24  ? 0.1677 0.1717 0.1480 -0.0600 -0.0009 0.0306  30  LEU A N   
149  C CA  . LEU A 24  ? 0.1523 0.1619 0.1360 -0.0605 0.0013  0.0328  30  LEU A CA  
150  C C   . LEU A 24  ? 0.1693 0.1871 0.1582 -0.0638 -0.0018 0.0343  30  LEU A C   
151  O O   . LEU A 24  ? 0.1639 0.1834 0.1535 -0.0652 -0.0020 0.0341  30  LEU A O   
152  C CB  . LEU A 24  ? 0.1687 0.1821 0.1558 -0.0563 0.0054  0.0356  30  LEU A CB  
153  C CG  . LEU A 24  ? 0.1926 0.1978 0.1744 -0.0530 0.0090  0.0343  30  LEU A CG  
154  C CD1 . LEU A 24  ? 0.1690 0.1779 0.1542 -0.0487 0.0122  0.0368  30  LEU A CD1 
155  C CD2 . LEU A 24  ? 0.2007 0.2024 0.1792 -0.0538 0.0114  0.0339  30  LEU A CD2 
156  N N   . GLN A 25  ? 0.1653 0.1878 0.1579 -0.0639 -0.0045 0.0351  31  GLN A N   
157  C CA  . GLN A 25  ? 0.1717 0.2008 0.1684 -0.0651 -0.0079 0.0352  31  GLN A CA  
158  C C   . GLN A 25  ? 0.2165 0.2406 0.2087 -0.0659 -0.0110 0.0312  31  GLN A C   
159  O O   . GLN A 25  ? 0.2193 0.2468 0.2132 -0.0667 -0.0121 0.0312  31  GLN A O   
160  C CB  . GLN A 25  ? 0.1632 0.1965 0.1633 -0.0645 -0.0103 0.0361  31  GLN A CB  
161  C CG  . GLN A 25  ? 0.2346 0.2754 0.2394 -0.0651 -0.0132 0.0369  31  GLN A CG  
162  C CD  . GLN A 25  ? 0.2723 0.3164 0.2797 -0.0642 -0.0156 0.0377  31  GLN A CD  
163  O OE1 . GLN A 25  ? 0.3148 0.3535 0.3182 -0.0636 -0.0176 0.0353  31  GLN A OE1 
164  N NE2 . GLN A 25  ? 0.2479 0.3009 0.2620 -0.0639 -0.0151 0.0412  31  GLN A NE2 
165  N N   . ALA A 26  ? 0.2105 0.2265 0.1968 -0.0651 -0.0122 0.0279  32  ALA A N   
166  C CA  . ALA A 26  ? 0.2261 0.2376 0.2079 -0.0647 -0.0146 0.0245  32  ALA A CA  
167  C C   . ALA A 26  ? 0.2753 0.2845 0.2550 -0.0656 -0.0128 0.0238  32  ALA A C   
168  O O   . ALA A 26  ? 0.2902 0.2988 0.2682 -0.0657 -0.0143 0.0222  32  ALA A O   
169  C CB  . ALA A 26  ? 0.2944 0.2983 0.2708 -0.0629 -0.0157 0.0214  32  ALA A CB  
170  N N   . LEU A 27  ? 0.2424 0.2497 0.2217 -0.0659 -0.0092 0.0251  33  LEU A N   
171  C CA  . LEU A 27  ? 0.2368 0.2416 0.2139 -0.0666 -0.0071 0.0246  33  LEU A CA  
172  C C   . LEU A 27  ? 0.2368 0.2493 0.2194 -0.0678 -0.0057 0.0277  33  LEU A C   
173  O O   . LEU A 27  ? 0.2484 0.2595 0.2296 -0.0684 -0.0039 0.0275  33  LEU A O   
174  C CB  . LEU A 27  ? 0.2366 0.2351 0.2099 -0.0658 -0.0034 0.0247  33  LEU A CB  
175  C CG  . LEU A 27  ? 0.3088 0.2983 0.2760 -0.0643 -0.0042 0.0214  33  LEU A CG  
176  C CD1 . LEU A 27  ? 0.3018 0.2860 0.2660 -0.0632 0.0000  0.0224  33  LEU A CD1 
177  C CD2 . LEU A 27  ? 0.3382 0.3230 0.3008 -0.0641 -0.0063 0.0178  33  LEU A CD2 
178  N N   . ASN A 28  ? 0.2053 0.2259 0.1940 -0.0680 -0.0063 0.0304  34  ASN A N   
179  C CA  . ASN A 28  ? 0.2234 0.2522 0.2181 -0.0687 -0.0049 0.0336  34  ASN A CA  
180  C C   . ASN A 28  ? 0.2567 0.2855 0.2519 -0.0680 0.0002  0.0362  34  ASN A C   
181  O O   . ASN A 28  ? 0.2271 0.2594 0.2248 -0.0685 0.0021  0.0377  34  ASN A O   
182  C CB  . ASN A 28  ? 0.2498 0.2797 0.2444 -0.0699 -0.0071 0.0322  34  ASN A CB  
183  C CG  . ASN A 28  ? 0.3186 0.3579 0.3201 -0.0704 -0.0074 0.0350  34  ASN A CG  
184  O OD1 . ASN A 28  ? 0.3930 0.4384 0.3995 -0.0698 -0.0072 0.0376  34  ASN A OD1 
185  N ND2 . ASN A 28  ? 0.3364 0.3770 0.3384 -0.0714 -0.0078 0.0346  34  ASN A ND2 
186  N N   . VAL A 29  ? 0.1988 0.2237 0.1915 -0.0665 0.0027  0.0367  35  VAL A N   
187  C CA  . VAL A 29  ? 0.2019 0.2263 0.1943 -0.0645 0.0079  0.0390  35  VAL A CA  
188  C C   . VAL A 29  ? 0.2305 0.2635 0.2299 -0.0618 0.0094  0.0425  35  VAL A C   
189  O O   . VAL A 29  ? 0.1884 0.2232 0.1896 -0.0607 0.0077  0.0426  35  VAL A O   
190  C CB  . VAL A 29  ? 0.2445 0.2588 0.2299 -0.0620 0.0096  0.0366  35  VAL A CB  
191  C CG1 . VAL A 29  ? 0.2097 0.2234 0.1952 -0.0579 0.0148  0.0384  35  VAL A CG1 
192  C CG2 . VAL A 29  ? 0.2037 0.2095 0.1822 -0.0646 0.0084  0.0334  35  VAL A CG2 
193  N N   . PRO A 30  ? 0.1893 0.2278 0.1930 -0.0607 0.0124  0.0453  36  PRO A N   
194  C CA  . PRO A 30  ? 0.2011 0.2479 0.2116 -0.0580 0.0139  0.0486  36  PRO A CA  
195  C C   . PRO A 30  ? 0.2135 0.2566 0.2221 -0.0538 0.0161  0.0484  36  PRO A C   
196  O O   . PRO A 30  ? 0.1644 0.2000 0.1676 -0.0518 0.0189  0.0470  36  PRO A O   
197  C CB  . PRO A 30  ? 0.2595 0.3106 0.2733 -0.0575 0.0175  0.0511  36  PRO A CB  
198  C CG  . PRO A 30  ? 0.2479 0.2962 0.2589 -0.0614 0.0161  0.0495  36  PRO A CG  
199  C CD  . PRO A 30  ? 0.2160 0.2541 0.2189 -0.0621 0.0145  0.0456  36  PRO A CD  
200  N N   . PHE A 31  ? 0.1991 0.2474 0.2120 -0.0524 0.0147  0.0498  37  PHE A N   
201  C CA  . PHE A 31  ? 0.1910 0.2360 0.2023 -0.0484 0.0167  0.0497  37  PHE A CA  
202  C C   . PHE A 31  ? 0.2015 0.2551 0.2196 -0.0467 0.0160  0.0523  37  PHE A C   
203  O O   . PHE A 31  ? 0.1747 0.2356 0.1979 -0.0490 0.0132  0.0537  37  PHE A O   
204  C CB  . PHE A 31  ? 0.1891 0.2252 0.1937 -0.0489 0.0144  0.0461  37  PHE A CB  
205  C CG  . PHE A 31  ? 0.1679 0.2067 0.1744 -0.0509 0.0098  0.0454  37  PHE A CG  
206  C CD1 . PHE A 31  ? 0.1675 0.2078 0.1742 -0.0552 0.0060  0.0444  37  PHE A CD1 
207  C CD2 . PHE A 31  ? 0.1697 0.2096 0.1777 -0.0483 0.0093  0.0458  37  PHE A CD2 
208  C CE1 . PHE A 31  ? 0.1710 0.2137 0.1793 -0.0571 0.0017  0.0438  37  PHE A CE1 
209  C CE2 . PHE A 31  ? 0.1525 0.1948 0.1621 -0.0501 0.0051  0.0453  37  PHE A CE2 
210  C CZ  . PHE A 31  ? 0.1600 0.2037 0.1698 -0.0544 0.0013  0.0443  37  PHE A CZ  
211  N N   . MET A 32  ? 0.1735 0.2260 0.1916 -0.0426 0.0186  0.0531  38  MET A N   
212  C CA  . MET A 32  ? 0.1908 0.2501 0.2144 -0.0405 0.0180  0.0553  38  MET A CA  
213  C C   . MET A 32  ? 0.1711 0.2244 0.1908 -0.0378 0.0182  0.0537  38  MET A C   
214  O O   . MET A 32  ? 0.1961 0.2429 0.2115 -0.0352 0.0215  0.0527  38  MET A O   
215  C CB  . MET A 32  ? 0.2286 0.2949 0.2580 -0.0377 0.0219  0.0590  38  MET A CB  
216  C CG  . MET A 32  ? 0.2727 0.3473 0.3087 -0.0359 0.0211  0.0617  38  MET A CG  
217  S SD  . MET A 32  ? 0.3460 0.4298 0.3882 -0.0400 0.0161  0.0628  38  MET A SD  
218  C CE  . MET A 32  ? 0.3880 0.4761 0.4333 -0.0420 0.0181  0.0647  38  MET A CE  
219  N N   . LEU A 33  ? 0.1598 0.2150 0.1810 -0.0385 0.0147  0.0532  39  LEU A N   
220  C CA  . LEU A 33  ? 0.1747 0.2255 0.1932 -0.0358 0.0148  0.0520  39  LEU A CA  
221  C C   . LEU A 33  ? 0.1668 0.2248 0.1913 -0.0324 0.0163  0.0551  39  LEU A C   
222  O O   . LEU A 33  ? 0.1520 0.2184 0.1824 -0.0335 0.0143  0.0572  39  LEU A O   
223  C CB  . LEU A 33  ? 0.1604 0.2085 0.1767 -0.0384 0.0100  0.0496  39  LEU A CB  
224  C CG  . LEU A 33  ? 0.1941 0.2392 0.2090 -0.0359 0.0094  0.0487  39  LEU A CG  
225  C CD1 . LEU A 33  ? 0.1647 0.2003 0.1733 -0.0335 0.0122  0.0466  39  LEU A CD1 
226  C CD2 . LEU A 33  ? 0.1509 0.1952 0.1648 -0.0389 0.0045  0.0469  39  LEU A CD2 
227  N N   . VAL A 34  ? 0.1845 0.2393 0.2074 -0.0284 0.0199  0.0555  40  VAL A N   
228  C CA  . VAL A 34  ? 0.1892 0.2502 0.2173 -0.0248 0.0218  0.0584  40  VAL A CA  
229  C C   . VAL A 34  ? 0.1660 0.2229 0.1916 -0.0226 0.0210  0.0570  40  VAL A C   
230  O O   . VAL A 34  ? 0.1942 0.2423 0.2138 -0.0216 0.0220  0.0545  40  VAL A O   
231  C CB  . VAL A 34  ? 0.1862 0.2476 0.2151 -0.0215 0.0271  0.0603  40  VAL A CB  
232  C CG1 . VAL A 34  ? 0.2109 0.2796 0.2458 -0.0180 0.0288  0.0635  40  VAL A CG1 
233  C CG2 . VAL A 34  ? 0.2252 0.2898 0.2559 -0.0237 0.0280  0.0615  40  VAL A CG2 
234  N N   . ASP A 35  ? 0.1736 0.2368 0.2040 -0.0219 0.0191  0.0586  41  ASP A N   
235  C CA  . ASP A 35  ? 0.1755 0.2361 0.2046 -0.0192 0.0188  0.0579  41  ASP A CA  
236  C C   . ASP A 35  ? 0.1869 0.2561 0.2226 -0.0166 0.0195  0.0612  41  ASP A C   
237  O O   . ASP A 35  ? 0.1915 0.2691 0.2329 -0.0181 0.0181  0.0634  41  ASP A O   
238  C CB  . ASP A 35  ? 0.1574 0.2145 0.1837 -0.0219 0.0142  0.0553  41  ASP A CB  
239  C CG  . ASP A 35  ? 0.1680 0.2195 0.1911 -0.0192 0.0145  0.0538  41  ASP A CG  
240  O OD1 . ASP A 35  ? 0.1796 0.2225 0.1969 -0.0184 0.0161  0.0515  41  ASP A OD1 
241  O OD2 . ASP A 35  ? 0.1727 0.2285 0.1991 -0.0178 0.0132  0.0550  41  ASP A OD2 
242  N N   . MET A 36  ? 0.1987 0.2659 0.2337 -0.0127 0.0216  0.0615  42  MET A N   
243  C CA  . MET A 36  ? 0.2053 0.2804 0.2465 -0.0100 0.0224  0.0646  42  MET A CA  
244  C C   . MET A 36  ? 0.2103 0.2901 0.2544 -0.0117 0.0178  0.0648  42  MET A C   
245  O O   . MET A 36  ? 0.2213 0.3096 0.2715 -0.0109 0.0174  0.0676  42  MET A O   
246  C CB  . MET A 36  ? 0.2307 0.3021 0.2701 -0.0053 0.0260  0.0648  42  MET A CB  
247  C CG  . MET A 36  ? 0.2520 0.3165 0.2868 -0.0046 0.0243  0.0621  42  MET A CG  
248  S SD  . MET A 36  ? 0.3161 0.3768 0.3493 0.0010  0.0287  0.0625  42  MET A SD  
249  C CE  . MET A 36  ? 0.2720 0.3250 0.2999 0.0018  0.0328  0.0612  42  MET A CE  
250  N N   . LYS A 37  ? 0.1643 0.2386 0.2042 -0.0141 0.0144  0.0619  43  LYS A N   
251  C CA  . LYS A 37  ? 0.1857 0.2638 0.2278 -0.0159 0.0100  0.0618  43  LYS A CA  
252  C C   . LYS A 37  ? 0.1870 0.2690 0.2310 -0.0204 0.0066  0.0618  43  LYS A C   
253  O O   . LYS A 37  ? 0.1569 0.2371 0.1993 -0.0225 0.0073  0.0611  43  LYS A O   
254  C CB  . LYS A 37  ? 0.1614 0.2315 0.1981 -0.0161 0.0079  0.0587  43  LYS A CB  
255  C CG  . LYS A 37  ? 0.2014 0.2652 0.2346 -0.0122 0.0110  0.0578  43  LYS A CG  
256  C CD  . LYS A 37  ? 0.1854 0.2418 0.2136 -0.0130 0.0084  0.0547  43  LYS A CD  
257  C CE  . LYS A 37  ? 0.1805 0.2271 0.2020 -0.0143 0.0091  0.0515  43  LYS A CE  
258  N NZ  . LYS A 37  ? 0.1414 0.1883 0.1621 -0.0183 0.0077  0.0508  43  LYS A NZ  
259  N N   . ASP A 38  ? 0.1553 0.2426 0.2026 -0.0220 0.0027  0.0625  44  ASP A N   
260  C CA  . ASP A 38  ? 0.1871 0.2774 0.2356 -0.0266 -0.0010 0.0622  44  ASP A CA  
261  C C   . ASP A 38  ? 0.1554 0.2385 0.1983 -0.0296 -0.0044 0.0587  44  ASP A C   
262  O O   . ASP A 38  ? 0.1305 0.2150 0.1735 -0.0336 -0.0075 0.0580  44  ASP A O   
263  C CB  . ASP A 38  ? 0.1778 0.2780 0.2330 -0.0272 -0.0036 0.0648  44  ASP A CB  
264  C CG  . ASP A 38  ? 0.2826 0.3824 0.3373 -0.0271 -0.0071 0.0641  44  ASP A CG  
265  O OD1 . ASP A 38  ? 0.2815 0.3737 0.3310 -0.0263 -0.0074 0.0616  44  ASP A OD1 
266  O OD2 . ASP A 38  ? 0.2284 0.3358 0.2881 -0.0277 -0.0096 0.0660  44  ASP A OD2 
267  N N   . SER A 39  ? 0.1663 0.2417 0.2042 -0.0279 -0.0038 0.0565  45  SER A N   
268  C CA  . SER A 39  ? 0.1286 0.1970 0.1612 -0.0307 -0.0069 0.0532  45  SER A CA  
269  C C   . SER A 39  ? 0.1338 0.1922 0.1602 -0.0289 -0.0046 0.0506  45  SER A C   
270  O O   . SER A 39  ? 0.1367 0.1935 0.1627 -0.0250 -0.0013 0.0513  45  SER A O   
271  C CB  . SER A 39  ? 0.1937 0.2641 0.2275 -0.0310 -0.0106 0.0532  45  SER A CB  
272  O OG  . SER A 39  ? 0.2635 0.3355 0.2992 -0.0269 -0.0088 0.0546  45  SER A OG  
273  N N   . PHE A 40  ? 0.1117 0.1635 0.1331 -0.0319 -0.0064 0.0477  46  PHE A N   
274  C CA  . PHE A 40  ? 0.1034 0.1451 0.1184 -0.0309 -0.0052 0.0448  46  PHE A CA  
275  C C   . PHE A 40  ? 0.0977 0.1366 0.1116 -0.0290 -0.0064 0.0440  46  PHE A C   
276  O O   . PHE A 40  ? 0.1004 0.1425 0.1161 -0.0304 -0.0097 0.0442  46  PHE A O   
277  C CB  . PHE A 40  ? 0.1151 0.1513 0.1256 -0.0350 -0.0075 0.0421  46  PHE A CB  
278  C CG  . PHE A 40  ? 0.1224 0.1483 0.1265 -0.0347 -0.0076 0.0388  46  PHE A CG  
279  C CD1 . PHE A 40  ? 0.1170 0.1365 0.1173 -0.0329 -0.0042 0.0377  46  PHE A CD1 
280  C CD2 . PHE A 40  ? 0.1111 0.1338 0.1132 -0.0362 -0.0110 0.0370  46  PHE A CD2 
281  C CE1 . PHE A 40  ? 0.1381 0.1482 0.1326 -0.0325 -0.0043 0.0347  46  PHE A CE1 
282  C CE2 . PHE A 40  ? 0.1094 0.1227 0.1058 -0.0359 -0.0110 0.0340  46  PHE A CE2 
283  C CZ  . PHE A 40  ? 0.1209 0.1281 0.1137 -0.0341 -0.0078 0.0329  46  PHE A CZ  
284  N N   . HIS A 41  ? 0.0999 0.1328 0.1106 -0.0258 -0.0035 0.0430  47  HIS A N   
285  C CA  . HIS A 41  ? 0.1038 0.1333 0.1131 -0.0236 -0.0042 0.0421  47  HIS A CA  
286  C C   . HIS A 41  ? 0.1243 0.1435 0.1271 -0.0246 -0.0048 0.0386  47  HIS A C   
287  O O   . HIS A 41  ? 0.1095 0.1229 0.1088 -0.0233 -0.0020 0.0374  47  HIS A O   
288  C CB  . HIS A 41  ? 0.1009 0.1319 0.1121 -0.0188 -0.0004 0.0439  47  HIS A CB  
289  C CG  . HIS A 41  ? 0.1001 0.1284 0.1104 -0.0165 -0.0010 0.0433  47  HIS A CG  
290  N ND1 . HIS A 41  ? 0.1330 0.1585 0.1426 -0.0123 0.0024  0.0436  47  HIS A ND1 
291  C CD2 . HIS A 41  ? 0.1086 0.1368 0.1189 -0.0177 -0.0045 0.0425  47  HIS A CD2 
292  C CE1 . HIS A 41  ? 0.1219 0.1457 0.1310 -0.0110 0.0010  0.0430  47  HIS A CE1 
293  N NE2 . HIS A 41  ? 0.1147 0.1400 0.1241 -0.0142 -0.0031 0.0423  47  HIS A NE2 
294  N N   . HIS A 42  ? 0.1092 0.1260 0.1104 -0.0267 -0.0085 0.0369  48  HIS A N   
295  C CA  . HIS A 42  ? 0.1142 0.1212 0.1095 -0.0276 -0.0093 0.0335  48  HIS A CA  
296  C C   . HIS A 42  ? 0.1283 0.1316 0.1225 -0.0235 -0.0073 0.0333  48  HIS A C   
297  O O   . HIS A 42  ? 0.1234 0.1258 0.1177 -0.0230 -0.0092 0.0328  48  HIS A O   
298  C CB  . HIS A 42  ? 0.1057 0.1118 0.0999 -0.0314 -0.0139 0.0320  48  HIS A CB  
299  C CG  . HIS A 42  ? 0.1371 0.1335 0.1254 -0.0328 -0.0150 0.0286  48  HIS A CG  
300  N ND1 . HIS A 42  ? 0.1421 0.1345 0.1271 -0.0359 -0.0157 0.0268  48  HIS A ND1 
301  C CD2 . HIS A 42  ? 0.1475 0.1374 0.1328 -0.0316 -0.0155 0.0267  48  HIS A CD2 
302  C CE1 . HIS A 42  ? 0.1652 0.1490 0.1454 -0.0365 -0.0166 0.0239  48  HIS A CE1 
303  N NE2 . HIS A 42  ? 0.1328 0.1150 0.1131 -0.0339 -0.0165 0.0238  48  HIS A NE2 
304  N N   . ASN A 43  ? 0.1022 0.1033 0.0956 -0.0205 -0.0033 0.0337  49  ASN A N   
305  C CA  . ASN A 43  ? 0.1339 0.1335 0.1275 -0.0162 -0.0010 0.0342  49  ASN A CA  
306  C C   . ASN A 43  ? 0.1378 0.1282 0.1266 -0.0158 -0.0017 0.0313  49  ASN A C   
307  O O   . ASN A 43  ? 0.1281 0.1169 0.1171 -0.0126 -0.0004 0.0314  49  ASN A O   
308  C CB  . ASN A 43  ? 0.1496 0.1501 0.1440 -0.0129 0.0037  0.0357  49  ASN A CB  
309  C CG  . ASN A 43  ? 0.1625 0.1565 0.1524 -0.0139 0.0054  0.0339  49  ASN A CG  
310  O OD1 . ASN A 43  ? 0.2004 0.1879 0.1861 -0.0164 0.0035  0.0311  49  ASN A OD1 
311  N ND2 . ASN A 43  ? 0.2110 0.2070 0.2020 -0.0120 0.0090  0.0355  49  ASN A ND2 
312  N N   . VAL A 44  ? 0.1232 0.1075 0.1078 -0.0190 -0.0036 0.0286  50  VAL A N   
313  C CA  . VAL A 44  ? 0.1431 0.1190 0.1234 -0.0191 -0.0049 0.0258  50  VAL A CA  
314  C C   . VAL A 44  ? 0.1520 0.1302 0.1343 -0.0189 -0.0074 0.0262  50  VAL A C   
315  O O   . VAL A 44  ? 0.1631 0.1360 0.1434 -0.0172 -0.0074 0.0248  50  VAL A O   
316  C CB  . VAL A 44  ? 0.1549 0.1249 0.1310 -0.0230 -0.0070 0.0230  50  VAL A CB  
317  C CG1 . VAL A 44  ? 0.1906 0.1524 0.1626 -0.0233 -0.0086 0.0202  50  VAL A CG1 
318  C CG2 . VAL A 44  ? 0.1629 0.1297 0.1364 -0.0227 -0.0041 0.0225  50  VAL A CG2 
319  N N   . ALA A 45  ? 0.1238 0.1099 0.1102 -0.0204 -0.0096 0.0281  51  ALA A N   
320  C CA  . ALA A 45  ? 0.1110 0.0997 0.0994 -0.0203 -0.0123 0.0286  51  ALA A CA  
321  C C   . ALA A 45  ? 0.1252 0.1205 0.1181 -0.0168 -0.0106 0.0315  51  ALA A C   
322  O O   . ALA A 45  ? 0.1271 0.1262 0.1224 -0.0168 -0.0128 0.0324  51  ALA A O   
323  C CB  . ALA A 45  ? 0.1060 0.0985 0.0955 -0.0246 -0.0163 0.0287  51  ALA A CB  
324  N N   . ALA A 46  ? 0.1088 0.1057 0.1030 -0.0137 -0.0067 0.0330  52  ALA A N   
325  C CA  . ALA A 46  ? 0.1249 0.1289 0.1238 -0.0104 -0.0050 0.0359  52  ALA A CA  
326  C C   . ALA A 46  ? 0.1147 0.1164 0.1134 -0.0076 -0.0050 0.0357  52  ALA A C   
327  O O   . ALA A 46  ? 0.1079 0.1158 0.1105 -0.0059 -0.0053 0.0379  52  ALA A O   
328  C CB  . ALA A 46  ? 0.1190 0.1241 0.1188 -0.0077 -0.0007 0.0373  52  ALA A CB  
329  N N   . LEU A 47  ? 0.1192 0.1120 0.1134 -0.0069 -0.0045 0.0331  53  LEU A N   
330  C CA  . LEU A 47  ? 0.1178 0.1083 0.1118 -0.0041 -0.0043 0.0329  53  LEU A CA  
331  C C   . LEU A 47  ? 0.1297 0.1211 0.1241 -0.0062 -0.0084 0.0325  53  LEU A C   
332  O O   . LEU A 47  ? 0.1490 0.1439 0.1459 -0.0042 -0.0088 0.0339  53  LEU A O   
333  C CB  . LEU A 47  ? 0.1362 0.1168 0.1254 -0.0026 -0.0023 0.0304  53  LEU A CB  
334  C CG  . LEU A 47  ? 0.1550 0.1334 0.1429 -0.0006 0.0017  0.0304  53  LEU A CG  
335  C CD1 . LEU A 47  ? 0.1890 0.1579 0.1725 0.0012  0.0034  0.0280  53  LEU A CD1 
336  C CD2 . LEU A 47  ? 0.1523 0.1379 0.1446 0.0028  0.0046  0.0336  53  LEU A CD2 
337  N N   . ARG A 48  ? 0.1209 0.1097 0.1130 -0.0103 -0.0115 0.0306  54  ARG A N   
338  C CA  . ARG A 48  ? 0.1226 0.1133 0.1154 -0.0126 -0.0155 0.0305  54  ARG A CA  
339  C C   . ARG A 48  ? 0.1151 0.1160 0.1131 -0.0128 -0.0167 0.0335  54  ARG A C   
340  O O   . ARG A 48  ? 0.1300 0.1337 0.1296 -0.0125 -0.0188 0.0343  54  ARG A O   
341  C CB  . ARG A 48  ? 0.1467 0.1332 0.1362 -0.0171 -0.0183 0.0281  54  ARG A CB  
342  C CG  . ARG A 48  ? 0.1888 0.1766 0.1784 -0.0202 -0.0227 0.0277  54  ARG A CG  
343  C CD  . ARG A 48  ? 0.1979 0.1790 0.1846 -0.0199 -0.0241 0.0257  54  ARG A CD  
344  N NE  . ARG A 48  ? 0.1699 0.1419 0.1523 -0.0191 -0.0224 0.0232  54  ARG A NE  
345  C CZ  . ARG A 48  ? 0.1951 0.1608 0.1737 -0.0220 -0.0237 0.0206  54  ARG A CZ  
346  N NH1 . ARG A 48  ? 0.1464 0.1136 0.1246 -0.0261 -0.0268 0.0201  54  ARG A NH1 
347  N NH2 . ARG A 48  ? 0.1475 0.1052 0.1225 -0.0208 -0.0219 0.0185  54  ARG A NH2 
348  N N   . ALA A 49  ? 0.1066 0.1130 0.1072 -0.0132 -0.0153 0.0352  55  ALA A N   
349  C CA  . ALA A 49  ? 0.0909 0.1071 0.0968 -0.0131 -0.0162 0.0382  55  ALA A CA  
350  C C   . ALA A 49  ? 0.1171 0.1370 0.1260 -0.0087 -0.0139 0.0404  55  ALA A C   
351  O O   . ALA A 49  ? 0.1146 0.1424 0.1279 -0.0083 -0.0150 0.0429  55  ALA A O   
352  C CB  . ALA A 49  ? 0.1168 0.1377 0.1247 -0.0146 -0.0151 0.0394  55  ALA A CB  
353  N N   . SER A 50  ? 0.1194 0.1339 0.1262 -0.0054 -0.0110 0.0396  56  SER A N   
354  C CA  . SER A 50  ? 0.1345 0.1516 0.1438 -0.0011 -0.0089 0.0414  56  SER A CA  
355  C C   . SER A 50  ? 0.1282 0.1430 0.1366 -0.0002 -0.0109 0.0407  56  SER A C   
356  O O   . SER A 50  ? 0.1146 0.1319 0.1251 0.0033  -0.0094 0.0424  56  SER A O   
357  C CB  . SER A 50  ? 0.1312 0.1436 0.1386 0.0023  -0.0045 0.0409  56  SER A CB  
358  O OG  . SER A 50  ? 0.1361 0.1520 0.1452 0.0023  -0.0021 0.0423  56  SER A OG  
359  N N   . VAL A 51  ? 0.1255 0.1354 0.1307 -0.0031 -0.0140 0.0385  57  VAL A N   
360  C CA  . VAL A 51  ? 0.1430 0.1497 0.1469 -0.0022 -0.0157 0.0376  57  VAL A CA  
361  C C   . VAL A 51  ? 0.1821 0.1910 0.1863 -0.0057 -0.0202 0.0374  57  VAL A C   
362  O O   . VAL A 51  ? 0.1753 0.1834 0.1793 -0.0049 -0.0218 0.0373  57  VAL A O   
363  C CB  . VAL A 51  ? 0.1487 0.1453 0.1479 -0.0015 -0.0146 0.0347  57  VAL A CB  
364  C CG1 . VAL A 51  ? 0.1667 0.1607 0.1655 0.0025  -0.0101 0.0350  57  VAL A CG1 
365  C CG2 . VAL A 51  ? 0.1600 0.1510 0.1554 -0.0055 -0.0162 0.0321  57  VAL A CG2 
366  N N   . GLU A 52  ? 0.1293 0.1407 0.1338 -0.0095 -0.0222 0.0372  58  GLU A N   
367  C CA  . GLU A 52  ? 0.1756 0.1880 0.1797 -0.0132 -0.0266 0.0367  58  GLU A CA  
368  C C   . GLU A 52  ? 0.1414 0.1636 0.1502 -0.0145 -0.0283 0.0393  58  GLU A C   
369  O O   . GLU A 52  ? 0.1391 0.1649 0.1494 -0.0158 -0.0275 0.0401  58  GLU A O   
370  C CB  . GLU A 52  ? 0.1673 0.1737 0.1674 -0.0170 -0.0281 0.0339  58  GLU A CB  
371  C CG  . GLU A 52  ? 0.2095 0.2170 0.2091 -0.0210 -0.0327 0.0333  58  GLU A CG  
372  C CD  . GLU A 52  ? 0.2852 0.2873 0.2811 -0.0250 -0.0343 0.0308  58  GLU A CD  
373  O OE1 . GLU A 52  ? 0.2536 0.2494 0.2464 -0.0247 -0.0322 0.0290  58  GLU A OE1 
374  O OE2 . GLU A 52  ? 0.3219 0.3259 0.3178 -0.0286 -0.0378 0.0306  58  GLU A OE2 
375  N N   . THR A 53  ? 0.1489 0.1751 0.1597 -0.0140 -0.0305 0.0406  59  THR A N   
376  C CA  . THR A 53  ? 0.1472 0.1827 0.1625 -0.0152 -0.0325 0.0431  59  THR A CA  
377  C C   . THR A 53  ? 0.1619 0.1983 0.1766 -0.0200 -0.0352 0.0422  59  THR A C   
378  O O   . THR A 53  ? 0.1650 0.1957 0.1759 -0.0227 -0.0374 0.0399  59  THR A O   
379  C CB  . THR A 53  ? 0.1886 0.2268 0.2052 -0.0143 -0.0350 0.0442  59  THR A CB  
380  O OG1 . THR A 53  ? 0.2092 0.2464 0.2263 -0.0098 -0.0324 0.0450  59  THR A OG1 
381  C CG2 . THR A 53  ? 0.2123 0.2604 0.2338 -0.0154 -0.0370 0.0469  59  THR A CG2 
382  N N   . GLY A 54  ? 0.1374 0.1808 0.1558 -0.0210 -0.0348 0.0441  60  GLY A N   
383  C CA  . GLY A 54  ? 0.1839 0.2294 0.2024 -0.0254 -0.0374 0.0437  60  GLY A CA  
384  C C   . GLY A 54  ? 0.1776 0.2178 0.1929 -0.0274 -0.0360 0.0417  60  GLY A C   
385  O O   . GLY A 54  ? 0.1755 0.2171 0.1907 -0.0312 -0.0380 0.0413  60  GLY A O   
386  N N   . PHE A 55  ? 0.1325 0.1666 0.1451 -0.0251 -0.0328 0.0404  61  PHE A N   
387  C CA  . PHE A 55  ? 0.1562 0.1844 0.1652 -0.0268 -0.0316 0.0383  61  PHE A CA  
388  C C   . PHE A 55  ? 0.1174 0.1498 0.1289 -0.0265 -0.0289 0.0397  61  PHE A C   
389  O O   . PHE A 55  ? 0.1226 0.1527 0.1322 -0.0291 -0.0288 0.0385  61  PHE A O   
390  C CB  . PHE A 55  ? 0.1352 0.1545 0.1400 -0.0245 -0.0294 0.0361  61  PHE A CB  
391  C CG  . PHE A 55  ? 0.1410 0.1533 0.1416 -0.0264 -0.0286 0.0336  61  PHE A CG  
392  C CD1 . PHE A 55  ? 0.2094 0.2173 0.2067 -0.0302 -0.0316 0.0314  61  PHE A CD1 
393  C CD2 . PHE A 55  ? 0.1481 0.1583 0.1480 -0.0244 -0.0248 0.0335  61  PHE A CD2 
394  C CE1 . PHE A 55  ? 0.2212 0.2227 0.2146 -0.0320 -0.0310 0.0290  61  PHE A CE1 
395  C CE2 . PHE A 55  ? 0.1676 0.1712 0.1634 -0.0262 -0.0241 0.0312  61  PHE A CE2 
396  C CZ  . PHE A 55  ? 0.2072 0.2066 0.1999 -0.0300 -0.0273 0.0289  61  PHE A CZ  
397  N N   . ALA A 56  ? 0.1169 0.1551 0.1325 -0.0232 -0.0265 0.0423  62  ALA A N   
398  C CA  . ALA A 56  ? 0.1078 0.1490 0.1253 -0.0223 -0.0232 0.0437  62  ALA A CA  
399  C C   . ALA A 56  ? 0.0877 0.1335 0.1070 -0.0261 -0.0249 0.0443  62  ALA A C   
400  O O   . ALA A 56  ? 0.0978 0.1429 0.1166 -0.0266 -0.0228 0.0441  62  ALA A O   
401  C CB  . ALA A 56  ? 0.1285 0.1762 0.1507 -0.0183 -0.0208 0.0467  62  ALA A CB  
402  N N   . LYS A 57  ? 0.0973 0.1477 0.1187 -0.0288 -0.0288 0.0449  63  LYS A N   
403  C CA  . LYS A 57  ? 0.1301 0.1852 0.1534 -0.0325 -0.0305 0.0455  63  LYS A CA  
404  C C   . LYS A 57  ? 0.1502 0.1987 0.1689 -0.0358 -0.0313 0.0427  63  LYS A C   
405  O O   . LYS A 57  ? 0.1345 0.1858 0.1542 -0.0386 -0.0317 0.0431  63  LYS A O   
406  C CB  . LYS A 57  ? 0.1696 0.2307 0.1959 -0.0346 -0.0346 0.0467  63  LYS A CB  
407  C CG  . LYS A 57  ? 0.1846 0.2404 0.2070 -0.0366 -0.0381 0.0444  63  LYS A CG  
408  C CD  . LYS A 57  ? 0.2839 0.3409 0.3069 -0.0369 -0.0386 0.0440  63  LYS A CD  
409  C CE  . LYS A 57  ? 0.3894 0.4379 0.4074 -0.0369 -0.0390 0.0407  63  LYS A CE  
410  N NZ  . LYS A 57  ? 0.5154 0.5632 0.5337 -0.0342 -0.0392 0.0411  63  LYS A NZ  
411  N N   . LYS A 58  ? 0.1343 0.1740 0.1478 -0.0357 -0.0313 0.0400  64  LYS A N   
412  C CA  . LYS A 58  ? 0.1410 0.1738 0.1499 -0.0384 -0.0316 0.0373  64  LYS A CA  
413  C C   . LYS A 58  ? 0.1269 0.1562 0.1341 -0.0366 -0.0275 0.0369  64  LYS A C   
414  O O   . LYS A 58  ? 0.1319 0.1555 0.1352 -0.0387 -0.0274 0.0347  64  LYS A O   
415  C CB  . LYS A 58  ? 0.2049 0.2297 0.2090 -0.0391 -0.0335 0.0346  64  LYS A CB  
416  C CG  . LYS A 58  ? 0.2487 0.2761 0.2539 -0.0406 -0.0373 0.0348  64  LYS A CG  
417  C CD  . LYS A 58  ? 0.4422 0.4594 0.4418 -0.0399 -0.0369 0.0314  64  LYS A CD  
418  C CE  . LYS A 58  ? 0.6951 0.7069 0.6906 -0.0406 -0.0356 0.0289  64  LYS A CE  
419  N NZ  . LYS A 58  ? 0.6543 0.6628 0.6471 -0.0418 -0.0346 0.0277  64  LYS A NZ  
420  N N   . THR A 59  ? 0.1099 0.1419 0.1196 -0.0327 -0.0241 0.0388  65  THR A N   
421  C CA  . THR A 59  ? 0.1007 0.1288 0.1085 -0.0306 -0.0201 0.0383  65  THR A CA  
422  C C   . THR A 59  ? 0.1088 0.1433 0.1203 -0.0302 -0.0177 0.0406  65  THR A C   
423  O O   . THR A 59  ? 0.1098 0.1413 0.1199 -0.0283 -0.0141 0.0405  65  THR A O   
424  C CB  . THR A 59  ? 0.1146 0.1393 0.1215 -0.0262 -0.0173 0.0383  65  THR A CB  
425  O OG1 . THR A 59  ? 0.1142 0.1464 0.1262 -0.0232 -0.0160 0.0413  65  THR A OG1 
426  C CG2 . THR A 59  ? 0.1030 0.1215 0.1065 -0.0263 -0.0195 0.0361  65  THR A CG2 
427  N N   . PHE A 60  ? 0.0992 0.1421 0.1154 -0.0319 -0.0194 0.0428  66  PHE A N   
428  C CA  . PHE A 60  ? 0.1218 0.1710 0.1419 -0.0317 -0.0173 0.0452  66  PHE A CA  
429  C C   . PHE A 60  ? 0.1208 0.1733 0.1419 -0.0362 -0.0202 0.0451  66  PHE A C   
430  O O   . PHE A 60  ? 0.1350 0.1904 0.1574 -0.0385 -0.0239 0.0452  66  PHE A O   
431  C CB  . PHE A 60  ? 0.1068 0.1643 0.1328 -0.0287 -0.0161 0.0485  66  PHE A CB  
432  C CG  . PHE A 60  ? 0.0905 0.1457 0.1160 -0.0239 -0.0124 0.0490  66  PHE A CG  
433  C CD1 . PHE A 60  ? 0.0932 0.1477 0.1188 -0.0217 -0.0082 0.0498  66  PHE A CD1 
434  C CD2 . PHE A 60  ? 0.0933 0.1467 0.1182 -0.0217 -0.0131 0.0487  66  PHE A CD2 
435  C CE1 . PHE A 60  ? 0.0950 0.1472 0.1200 -0.0173 -0.0048 0.0502  66  PHE A CE1 
436  C CE2 . PHE A 60  ? 0.0937 0.1449 0.1182 -0.0174 -0.0097 0.0492  66  PHE A CE2 
437  C CZ  . PHE A 60  ? 0.1079 0.1585 0.1325 -0.0152 -0.0056 0.0499  66  PHE A CZ  
438  N N   . ILE A 61  ? 0.1150 0.1668 0.1354 -0.0375 -0.0184 0.0449  67  ILE A N   
439  C CA  . ILE A 61  ? 0.1127 0.1666 0.1334 -0.0419 -0.0208 0.0446  67  ILE A CA  
440  C C   . ILE A 61  ? 0.1360 0.1967 0.1612 -0.0417 -0.0185 0.0471  67  ILE A C   
441  O O   . ILE A 61  ? 0.1271 0.1853 0.1511 -0.0398 -0.0148 0.0472  67  ILE A O   
442  C CB  . ILE A 61  ? 0.1258 0.1709 0.1404 -0.0443 -0.0213 0.0413  67  ILE A CB  
443  C CG1 . ILE A 61  ? 0.1100 0.1476 0.1200 -0.0439 -0.0229 0.0387  67  ILE A CG1 
444  C CG2 . ILE A 61  ? 0.1271 0.1748 0.1423 -0.0489 -0.0241 0.0410  67  ILE A CG2 
445  C CD1 . ILE A 61  ? 0.1376 0.1661 0.1414 -0.0461 -0.0233 0.0354  67  ILE A CD1 
446  N N   . SER A 62  ? 0.1547 0.2236 0.1848 -0.0436 -0.0208 0.0491  68  SER A N   
447  C CA  . SER A 62  ? 0.1543 0.2304 0.1893 -0.0435 -0.0188 0.0518  68  SER A CA  
448  C C   . SER A 62  ? 0.1261 0.1986 0.1585 -0.0451 -0.0168 0.0508  68  SER A C   
449  O O   . SER A 62  ? 0.1512 0.2205 0.1807 -0.0487 -0.0192 0.0488  68  SER A O   
450  C CB  . SER A 62  ? 0.1865 0.2709 0.2265 -0.0463 -0.0224 0.0535  68  SER A CB  
451  O OG  . SER A 62  ? 0.1891 0.2794 0.2332 -0.0471 -0.0208 0.0556  68  SER A OG  
452  N N   . TYR A 63  ? 0.1219 0.1957 0.1558 -0.0425 -0.0126 0.0523  69  TYR A N   
453  C CA  . TYR A 63  ? 0.1470 0.2179 0.1786 -0.0439 -0.0105 0.0516  69  TYR A CA  
454  C C   . TYR A 63  ? 0.1727 0.2501 0.2081 -0.0474 -0.0124 0.0529  69  TYR A C   
455  O O   . TYR A 63  ? 0.1808 0.2550 0.2134 -0.0504 -0.0131 0.0513  69  TYR A O   
456  C CB  . TYR A 63  ? 0.1372 0.2082 0.1696 -0.0402 -0.0055 0.0531  69  TYR A CB  
457  C CG  . TYR A 63  ? 0.1520 0.2160 0.1803 -0.0366 -0.0029 0.0518  69  TYR A CG  
458  C CD1 . TYR A 63  ? 0.1110 0.1652 0.1325 -0.0373 -0.0027 0.0486  69  TYR A CD1 
459  C CD2 . TYR A 63  ? 0.1299 0.1968 0.1611 -0.0324 -0.0004 0.0539  69  TYR A CD2 
460  C CE1 . TYR A 63  ? 0.1246 0.1724 0.1425 -0.0339 -0.0002 0.0474  69  TYR A CE1 
461  C CE2 . TYR A 63  ? 0.1303 0.1909 0.1579 -0.0291 0.0021  0.0527  69  TYR A CE2 
462  C CZ  . TYR A 63  ? 0.1204 0.1715 0.1414 -0.0299 0.0022  0.0495  69  TYR A CZ  
463  O OH  . TYR A 63  ? 0.1260 0.1708 0.1435 -0.0265 0.0047  0.0485  69  TYR A OH  
464  N N   . SER A 64  ? 0.1727 0.2594 0.2148 -0.0469 -0.0130 0.0559  70  SER A N   
465  C CA  . SER A 64  ? 0.1764 0.2698 0.2227 -0.0499 -0.0143 0.0574  70  SER A CA  
466  C C   . SER A 64  ? 0.1809 0.2730 0.2253 -0.0545 -0.0189 0.0555  70  SER A C   
467  O O   . SER A 64  ? 0.2169 0.3095 0.2611 -0.0571 -0.0195 0.0550  70  SER A O   
468  C CB  . SER A 64  ? 0.1990 0.3027 0.2530 -0.0485 -0.0143 0.0610  70  SER A CB  
469  O OG  . SER A 64  ? 0.2720 0.3780 0.3273 -0.0486 -0.0177 0.0611  70  SER A OG  
470  N N   . VAL A 65  ? 0.1867 0.2759 0.2288 -0.0549 -0.0219 0.0539  71  VAL A N   
471  C CA  . VAL A 65  ? 0.1559 0.2401 0.1930 -0.0566 -0.0256 0.0508  71  VAL A CA  
472  C C   . VAL A 65  ? 0.2159 0.2919 0.2468 -0.0583 -0.0252 0.0478  71  VAL A C   
473  O O   . VAL A 65  ? 0.2085 0.2818 0.2363 -0.0592 -0.0266 0.0459  71  VAL A O   
474  C CB  . VAL A 65  ? 0.2080 0.2890 0.2426 -0.0555 -0.0281 0.0495  71  VAL A CB  
475  C CG1 . VAL A 65  ? 0.2127 0.2850 0.2399 -0.0562 -0.0303 0.0457  71  VAL A CG1 
476  C CG2 . VAL A 65  ? 0.1568 0.2452 0.1966 -0.0540 -0.0292 0.0520  71  VAL A CG2 
477  N N   . THR A 66  ? 0.1789 0.2507 0.2078 -0.0584 -0.0229 0.0473  72  THR A N   
478  C CA  . THR A 66  ? 0.2098 0.2732 0.2323 -0.0597 -0.0224 0.0442  72  THR A CA  
479  C C   . THR A 66  ? 0.1893 0.2546 0.2132 -0.0606 -0.0196 0.0454  72  THR A C   
480  O O   . THR A 66  ? 0.1968 0.2581 0.2170 -0.0617 -0.0204 0.0431  72  THR A O   
481  C CB  . THR A 66  ? 0.2184 0.2744 0.2366 -0.0587 -0.0208 0.0428  72  THR A CB  
482  O OG1 . THR A 66  ? 0.1902 0.2438 0.2068 -0.0584 -0.0237 0.0414  72  THR A OG1 
483  C CG2 . THR A 66  ? 0.1836 0.2313 0.1958 -0.0603 -0.0201 0.0400  72  THR A CG2 
484  N N   . PHE A 67  ? 0.1590 0.2289 0.1870 -0.0583 -0.0159 0.0483  73  PHE A N   
485  C CA  . PHE A 67  ? 0.2015 0.2712 0.2295 -0.0579 -0.0124 0.0491  73  PHE A CA  
486  C C   . PHE A 67  ? 0.1995 0.2788 0.2344 -0.0583 -0.0116 0.0523  73  PHE A C   
487  O O   . PHE A 67  ? 0.2000 0.2795 0.2350 -0.0588 -0.0092 0.0529  73  PHE A O   
488  C CB  . PHE A 67  ? 0.1760 0.2409 0.2015 -0.0536 -0.0080 0.0490  73  PHE A CB  
489  C CG  . PHE A 67  ? 0.1646 0.2194 0.1830 -0.0532 -0.0083 0.0457  73  PHE A CG  
490  C CD1 . PHE A 67  ? 0.1609 0.2089 0.1739 -0.0558 -0.0089 0.0430  73  PHE A CD1 
491  C CD2 . PHE A 67  ? 0.1673 0.2193 0.1845 -0.0500 -0.0077 0.0453  73  PHE A CD2 
492  C CE1 . PHE A 67  ? 0.1901 0.2287 0.1967 -0.0555 -0.0092 0.0400  73  PHE A CE1 
493  C CE2 . PHE A 67  ? 0.1690 0.2116 0.1798 -0.0497 -0.0079 0.0422  73  PHE A CE2 
494  C CZ  . PHE A 67  ? 0.1425 0.1785 0.1481 -0.0524 -0.0087 0.0396  73  PHE A CZ  
495  N N   . LYS A 68  ? 0.1918 0.2790 0.2324 -0.0580 -0.0134 0.0546  74  LYS A N   
496  C CA  . LYS A 68  ? 0.1859 0.2820 0.2329 -0.0585 -0.0135 0.0572  74  LYS A CA  
497  C C   . LYS A 68  ? 0.2449 0.3435 0.2945 -0.0563 -0.0085 0.0596  74  LYS A C   
498  O O   . LYS A 68  ? 0.1948 0.2920 0.2442 -0.0523 -0.0056 0.0604  74  LYS A O   
499  C CB  . LYS A 68  ? 0.2585 0.3516 0.3022 -0.0607 -0.0166 0.0545  74  LYS A CB  
500  C CG  . LYS A 68  ? 0.2736 0.3626 0.3133 -0.0611 -0.0210 0.0518  74  LYS A CG  
501  C CD  . LYS A 68  ? 0.3996 0.4954 0.4441 -0.0598 -0.0227 0.0539  74  LYS A CD  
502  C CE  . LYS A 68  ? 0.5554 0.6466 0.5956 -0.0597 -0.0263 0.0515  74  LYS A CE  
503  N NZ  . LYS A 68  ? 0.5976 0.6946 0.6420 -0.0583 -0.0276 0.0536  74  LYS A NZ  
504  N N   . ASP A 69  ? 0.2139 0.3152 0.2655 -0.0580 -0.0074 0.0605  75  ASP A N   
505  C CA  . ASP A 69  ? 0.2374 0.3410 0.2915 -0.0554 -0.0026 0.0628  75  ASP A CA  
506  C C   . ASP A 69  ? 0.1969 0.2915 0.2447 -0.0533 0.0010  0.0610  75  ASP A C   
507  O O   . ASP A 69  ? 0.2331 0.3287 0.2822 -0.0507 0.0052  0.0627  75  ASP A O   
508  C CB  . ASP A 69  ? 0.3133 0.4217 0.3709 -0.0573 -0.0025 0.0640  75  ASP A CB  
509  C CG  . ASP A 69  ? 0.4255 0.5426 0.4898 -0.0567 -0.0045 0.0662  75  ASP A CG  
510  O OD1 . ASP A 69  ? 0.3604 0.4816 0.4279 -0.0548 -0.0050 0.0678  75  ASP A OD1 
511  O OD2 . ASP A 69  ? 0.5072 0.6269 0.5733 -0.0580 -0.0055 0.0662  75  ASP A OD2 
512  N N   . ASN A 70  ? 0.1919 0.2779 0.2329 -0.0543 -0.0004 0.0576  76  ASN A N   
513  C CA  . ASN A 70  ? 0.1897 0.2669 0.2246 -0.0519 0.0029  0.0559  76  ASN A CA  
514  C C   . ASN A 70  ? 0.2027 0.2781 0.2370 -0.0477 0.0046  0.0562  76  ASN A C   
515  O O   . ASN A 70  ? 0.1800 0.2478 0.2091 -0.0455 0.0072  0.0546  76  ASN A O   
516  C CB  . ASN A 70  ? 0.2242 0.2928 0.2521 -0.0547 0.0008  0.0522  76  ASN A CB  
517  C CG  . ASN A 70  ? 0.2375 0.3064 0.2649 -0.0583 0.0002  0.0518  76  ASN A CG  
518  O OD1 . ASN A 70  ? 0.3109 0.3810 0.3394 -0.0575 0.0036  0.0532  76  ASN A OD1 
519  N ND2 . ASN A 70  ? 0.2047 0.2724 0.2304 -0.0622 -0.0038 0.0500  76  ASN A ND2 
520  N N   . PHE A 71  ? 0.2010 0.2830 0.2404 -0.0465 0.0032  0.0581  77  PHE A N   
521  C CA  . PHE A 71  ? 0.1781 0.2591 0.2174 -0.0425 0.0048  0.0586  77  PHE A CA  
522  C C   . PHE A 71  ? 0.2028 0.2923 0.2490 -0.0397 0.0073  0.0624  77  PHE A C   
523  O O   . PHE A 71  ? 0.1908 0.2887 0.2430 -0.0413 0.0056  0.0645  77  PHE A O   
524  C CB  . PHE A 71  ? 0.1693 0.2497 0.2080 -0.0431 0.0009  0.0574  77  PHE A CB  
525  C CG  . PHE A 71  ? 0.1843 0.2654 0.2243 -0.0390 0.0024  0.0584  77  PHE A CG  
526  C CD1 . PHE A 71  ? 0.1604 0.2339 0.1955 -0.0360 0.0053  0.0569  77  PHE A CD1 
527  C CD2 . PHE A 71  ? 0.1824 0.2717 0.2284 -0.0380 0.0011  0.0609  77  PHE A CD2 
528  C CE1 . PHE A 71  ? 0.1828 0.2567 0.2189 -0.0320 0.0069  0.0579  77  PHE A CE1 
529  C CE2 . PHE A 71  ? 0.1948 0.2846 0.2419 -0.0340 0.0027  0.0619  77  PHE A CE2 
530  C CZ  . PHE A 71  ? 0.1715 0.2537 0.2137 -0.0310 0.0056  0.0604  77  PHE A CZ  
531  N N   . ARG A 72  ? 0.2044 0.2918 0.2499 -0.0355 0.0112  0.0631  78  ARG A N   
532  C CA  . ARG A 72  ? 0.2029 0.2977 0.2545 -0.0323 0.0139  0.0666  78  ARG A CA  
533  C C   . ARG A 72  ? 0.2065 0.2986 0.2567 -0.0283 0.0152  0.0665  78  ARG A C   
534  O O   . ARG A 72  ? 0.2001 0.2843 0.2448 -0.0264 0.0176  0.0647  78  ARG A O   
535  C CB  . ARG A 72  ? 0.2609 0.3558 0.3131 -0.0309 0.0185  0.0681  78  ARG A CB  
536  C CG  . ARG A 72  ? 0.2980 0.4006 0.3566 -0.0275 0.0216  0.0719  78  ARG A CG  
537  C CD  . ARG A 72  ? 0.3560 0.4690 0.4222 -0.0295 0.0189  0.0744  78  ARG A CD  
538  N N   . GLN A 73  ? 0.1995 0.2982 0.2547 -0.0271 0.0138  0.0684  79  GLN A N   
539  C CA  . GLN A 73  ? 0.2128 0.3099 0.2675 -0.0231 0.0153  0.0687  79  GLN A CA  
540  C C   . GLN A 73  ? 0.2337 0.3329 0.2907 -0.0191 0.0204  0.0712  79  GLN A C   
541  O O   . GLN A 73  ? 0.2753 0.3817 0.3378 -0.0191 0.0218  0.0740  79  GLN A O   
542  C CB  . GLN A 73  ? 0.2340 0.3374 0.2931 -0.0231 0.0120  0.0700  79  GLN A CB  
543  C CG  . GLN A 73  ? 0.2599 0.3621 0.3188 -0.0190 0.0134  0.0704  79  GLN A CG  
544  C CD  . GLN A 73  ? 0.3072 0.4143 0.3694 -0.0194 0.0096  0.0711  79  GLN A CD  
545  O OE1 . GLN A 73  ? 0.3414 0.4544 0.4072 -0.0223 0.0062  0.0719  79  GLN A OE1 
546  N NE2 . GLN A 73  ? 0.3044 0.4090 0.3651 -0.0163 0.0100  0.0706  79  GLN A NE2 
547  N N   . GLY A 74  ? 0.2002 0.2931 0.2532 -0.0157 0.0233  0.0702  80  GLY A N   
548  C CA  . GLY A 74  ? 0.2721 0.3667 0.3271 -0.0117 0.0282  0.0725  80  GLY A CA  
549  C C   . GLY A 74  ? 0.2762 0.3618 0.3251 -0.0087 0.0312  0.0707  80  GLY A C   
550  O O   . GLY A 74  ? 0.2194 0.2969 0.2623 -0.0099 0.0297  0.0674  80  GLY A O   
551  N N   . LEU A 75  ? 0.2552 0.3424 0.3060 -0.0047 0.0355  0.0728  81  LEU A N   
552  C CA  . LEU A 75  ? 0.2860 0.3655 0.3318 -0.0012 0.0388  0.0715  81  LEU A CA  
553  C C   . LEU A 75  ? 0.3065 0.3822 0.3496 -0.0003 0.0429  0.0716  81  LEU A C   
554  O O   . LEU A 75  ? 0.3526 0.4340 0.4001 0.0008  0.0457  0.0745  81  LEU A O   
555  C CB  . LEU A 75  ? 0.3286 0.4122 0.3781 0.0030  0.0407  0.0738  81  LEU A CB  
556  C CG  . LEU A 75  ? 0.3642 0.4404 0.4089 0.0069  0.0441  0.0727  81  LEU A CG  
557  C CD1 . LEU A 75  ? 0.3222 0.3903 0.3610 0.0058  0.0414  0.0691  81  LEU A CD1 
558  C CD2 . LEU A 75  ? 0.3736 0.4551 0.4229 0.0110  0.0464  0.0755  81  LEU A CD2 
559  N N   . VAL A 76  ? 0.2874 0.3534 0.3233 -0.0009 0.0434  0.0685  82  VAL A N   
560  C CA  . VAL A 76  ? 0.3305 0.3920 0.3631 -0.0001 0.0473  0.0684  82  VAL A CA  
561  C C   . VAL A 76  ? 0.3493 0.4081 0.3807 0.0047  0.0518  0.0693  82  VAL A C   
562  O O   . VAL A 76  ? 0.3222 0.3759 0.3503 0.0066  0.0517  0.0677  82  VAL A O   
563  C CB  . VAL A 76  ? 0.3735 0.4258 0.3989 -0.0029 0.0458  0.0647  82  VAL A CB  
564  C CG1 . VAL A 76  ? 0.3317 0.3790 0.3533 -0.0018 0.0500  0.0645  82  VAL A CG1 
565  C CG2 . VAL A 76  ? 0.3287 0.3841 0.3555 -0.0077 0.0414  0.0639  82  VAL A CG2 
566  N N   . VAL A 77  ? 0.3808 0.4431 0.4150 0.0068  0.0559  0.0720  83  VAL A N   
567  C CA  . VAL A 77  ? 0.4186 0.4792 0.4523 0.0115  0.0605  0.0734  83  VAL A CA  
568  C C   . VAL A 77  ? 0.4286 0.4815 0.4566 0.0127  0.0644  0.0723  83  VAL A C   
569  O O   . VAL A 77  ? 0.4536 0.5022 0.4790 0.0164  0.0679  0.0724  83  VAL A O   
570  C CB  . VAL A 77  ? 0.3837 0.4545 0.4254 0.0137  0.0625  0.0776  83  VAL A CB  
571  C CG1 . VAL A 77  ? 0.3890 0.4666 0.4357 0.0132  0.0589  0.0786  83  VAL A CG1 
572  C CG2 . VAL A 77  ? 0.4034 0.4796 0.4488 0.0118  0.0635  0.0796  83  VAL A CG2 
573  N N   . GLY A 78  ? 0.4085 0.4595 0.4345 0.0098  0.0641  0.0714  84  GLY A N   
574  C CA  . GLY A 78  ? 0.4289 0.4718 0.4488 0.0108  0.0675  0.0701  84  GLY A CA  
575  C C   . GLY A 78  ? 0.4240 0.4644 0.4413 0.0067  0.0657  0.0684  84  GLY A C   
576  O O   . GLY A 78  ? 0.3840 0.4299 0.4049 0.0033  0.0623  0.0688  84  GLY A O   
577  N N   . ILE A 79  ? 0.4306 0.4622 0.4412 0.0072  0.0679  0.0665  85  ILE A N   
578  C CA  . ILE A 79  ? 0.4794 0.5076 0.4867 0.0038  0.0671  0.0650  85  ILE A CA  
579  C C   . ILE A 79  ? 0.5425 0.5695 0.5488 0.0058  0.0721  0.0666  85  ILE A C   
580  O O   . ILE A 79  ? 0.5417 0.5631 0.5443 0.0092  0.0757  0.0664  85  ILE A O   
581  C CB  . ILE A 79  ? 0.5033 0.5212 0.5026 0.0021  0.0647  0.0607  85  ILE A CB  
582  C CG1 . ILE A 79  ? 0.4966 0.5156 0.4969 0.0003  0.0599  0.0591  85  ILE A CG1 
583  C CG2 . ILE A 79  ? 0.5118 0.5261 0.5076 -0.0012 0.0640  0.0592  85  ILE A CG2 
584  C CD1 . ILE A 79  ? 0.4641 0.4914 0.4700 -0.0033 0.0560  0.0602  85  ILE A CD1 
585  N N   . ASP A 80  ? 0.5091 0.5412 0.5188 0.0037  0.0723  0.0683  86  ASP A N   
586  C CA  . ASP A 80  ? 0.5411 0.5727 0.5504 0.0052  0.0769  0.0700  86  ASP A CA  
587  C C   . ASP A 80  ? 0.5669 0.5899 0.5690 0.0028  0.0765  0.0671  86  ASP A C   
588  O O   . ASP A 80  ? 0.5595 0.5846 0.5626 -0.0007 0.0744  0.0668  86  ASP A O   
589  C CB  . ASP A 80  ? 0.5618 0.6041 0.5793 0.0043  0.0773  0.0736  86  ASP A CB  
590  C CG  . ASP A 80  ? 0.6821 0.7244 0.6997 0.0059  0.0822  0.0757  86  ASP A CG  
591  O OD1 . ASP A 80  ? 0.6254 0.6590 0.6362 0.0066  0.0846  0.0740  86  ASP A OD1 
592  O OD2 . ASP A 80  ? 0.6624 0.7136 0.6873 0.0065  0.0837  0.0792  86  ASP A OD2 
593  N N   . LEU A 81  ? 0.5719 0.5850 0.5666 0.0049  0.0785  0.0649  87  LEU A N   
594  C CA  . LEU A 81  ? 0.6050 0.6092 0.5923 0.0027  0.0778  0.0617  87  LEU A CA  
595  C C   . LEU A 81  ? 0.6207 0.6251 0.6077 0.0023  0.0809  0.0631  87  LEU A C   
596  O O   . LEU A 81  ? 0.5746 0.5746 0.5575 -0.0007 0.0794  0.0610  87  LEU A O   
597  C CB  . LEU A 81  ? 0.6136 0.6073 0.5933 0.0052  0.0793  0.0591  87  LEU A CB  
598  C CG  . LEU A 81  ? 0.5940 0.5846 0.5717 0.0044  0.0754  0.0565  87  LEU A CG  
599  C CD1 . LEU A 81  ? 0.6379 0.6177 0.6080 0.0068  0.0770  0.0539  87  LEU A CD1 
600  C CD2 . LEU A 81  ? 0.5787 0.5691 0.5557 -0.0004 0.0704  0.0543  87  LEU A CD2 
601  N N   . LYS A 82  ? 0.6449 0.6540 0.6359 0.0052  0.0852  0.0665  88  LYS A N   
602  C CA  . LYS A 82  ? 0.6728 0.6820 0.6635 0.0050  0.0884  0.0679  88  LYS A CA  
603  C C   . LYS A 82  ? 0.6526 0.6693 0.6486 0.0011  0.0858  0.0690  88  LYS A C   
604  O O   . LYS A 82  ? 0.6648 0.6785 0.6579 -0.0013 0.0857  0.0680  88  LYS A O   
605  C CB  . LYS A 82  ? 0.6698 0.6822 0.6639 0.0091  0.0923  0.0703  88  LYS A CB  
606  N N   . ASN A 83  ? 0.6342 0.6605 0.6379 0.0003  0.0835  0.0710  89  ASN A N   
607  C CA  . ASN A 83  ? 0.6199 0.6539 0.6293 -0.0034 0.0808  0.0722  89  ASN A CA  
608  C C   . ASN A 83  ? 0.5762 0.6101 0.5849 -0.0072 0.0750  0.0696  89  ASN A C   
609  O O   . ASN A 83  ? 0.5439 0.5850 0.5579 -0.0103 0.0721  0.0706  89  ASN A O   
610  C CB  . ASN A 83  ? 0.5927 0.6381 0.6115 -0.0020 0.0820  0.0764  89  ASN A CB  
611  C CG  . ASN A 83  ? 0.6923 0.7378 0.7120 0.0017  0.0869  0.0784  89  ASN A CG  
612  O OD1 . ASN A 83  ? 0.6301 0.6743 0.6488 0.0012  0.0887  0.0784  89  ASN A OD1 
613  N ND2 . ASN A 83  ? 0.6697 0.7166 0.6913 0.0055  0.0886  0.0795  89  ASN A ND2 
614  N N   . GLN A 84  ? 0.5482 0.5742 0.5507 -0.0071 0.0732  0.0663  90  GLN A N   
615  C CA  . GLN A 84  ? 0.5033 0.5278 0.5042 -0.0105 0.0678  0.0636  90  GLN A CA  
616  C C   . GLN A 84  ? 0.4405 0.4752 0.4493 -0.0120 0.0646  0.0655  90  GLN A C   
617  O O   . GLN A 84  ? 0.4135 0.4526 0.4251 -0.0157 0.0615  0.0655  90  GLN A O   
618  C CB  . GLN A 84  ? 0.4349 0.4548 0.4315 -0.0143 0.0661  0.0613  90  GLN A CB  
619  C CG  . GLN A 84  ? 0.5013 0.5106 0.4896 -0.0129 0.0691  0.0593  90  GLN A CG  
620  C CD  . GLN A 84  ? 0.4402 0.4400 0.4213 -0.0128 0.0672  0.0555  90  GLN A CD  
621  O OE1 . GLN A 84  ? 0.4525 0.4486 0.4302 -0.0162 0.0634  0.0528  90  GLN A OE1 
622  N NE2 . GLN A 84  ? 0.5175 0.5130 0.4959 -0.0090 0.0698  0.0554  90  GLN A NE2 
623  N N   . MET A 85  ? 0.4461 0.4844 0.4583 -0.0091 0.0651  0.0669  91  MET A N   
624  C CA  . MET A 85  ? 0.4429 0.4913 0.4631 -0.0098 0.0627  0.0692  91  MET A CA  
625  C C   . MET A 85  ? 0.4443 0.4916 0.4640 -0.0080 0.0609  0.0682  91  MET A C   
626  O O   . MET A 85  ? 0.4319 0.4739 0.4480 -0.0046 0.0637  0.0677  91  MET A O   
627  C CB  . MET A 85  ? 0.4622 0.5188 0.4892 -0.0074 0.0664  0.0734  91  MET A CB  
628  C CG  . MET A 85  ? 0.5370 0.6045 0.5723 -0.0096 0.0639  0.0759  91  MET A CG  
629  S SD  . MET A 85  ? 0.6215 0.6913 0.6580 -0.0138 0.0631  0.0761  91  MET A SD  
630  C CE  . MET A 85  ? 0.4819 0.5651 0.5289 -0.0158 0.0601  0.0793  91  MET A CE  
631  N N   . VAL A 86  ? 0.4175 0.4697 0.4406 -0.0104 0.0565  0.0680  92  VAL A N   
632  C CA  . VAL A 86  ? 0.4438 0.4960 0.4674 -0.0089 0.0546  0.0674  92  VAL A CA  
633  C C   . VAL A 86  ? 0.4273 0.4898 0.4591 -0.0069 0.0553  0.0711  92  VAL A C   
634  O O   . VAL A 86  ? 0.4289 0.4995 0.4665 -0.0092 0.0532  0.0729  92  VAL A O   
635  C CB  . VAL A 86  ? 0.3552 0.4056 0.3769 -0.0125 0.0491  0.0647  92  VAL A CB  
636  C CG1 . VAL A 86  ? 0.3774 0.4300 0.4011 -0.0111 0.0471  0.0647  92  VAL A CG1 
637  C CG2 . VAL A 86  ? 0.3895 0.4291 0.4027 -0.0138 0.0486  0.0609  92  VAL A CG2 
638  N N   . LEU A 87  ? 0.3999 0.4618 0.4320 -0.0027 0.0583  0.0723  93  LEU A N   
639  C CA  . LEU A 87  ? 0.4211 0.4923 0.4607 -0.0002 0.0599  0.0760  93  LEU A CA  
640  C C   . LEU A 87  ? 0.4430 0.5178 0.4854 -0.0002 0.0563  0.0759  93  LEU A C   
641  O O   . LEU A 87  ? 0.4060 0.4750 0.4443 0.0012  0.0557  0.0739  93  LEU A O   
642  C CB  . LEU A 87  ? 0.4351 0.5041 0.4738 0.0045  0.0653  0.0776  93  LEU A CB  
643  C CG  . LEU A 87  ? 0.5151 0.5790 0.5499 0.0052  0.0694  0.0775  93  LEU A CG  
644  C CD1 . LEU A 87  ? 0.5135 0.5768 0.5486 0.0100  0.0748  0.0796  93  LEU A CD1 
645  C CD2 . LEU A 87  ? 0.4460 0.5154 0.4847 0.0023  0.0691  0.0791  93  LEU A CD2 
646  N N   . LEU A 88  ? 0.3969 0.4812 0.4464 -0.0018 0.0539  0.0781  94  LEU A N   
647  C CA  . LEU A 88  ? 0.4006 0.4893 0.4534 -0.0019 0.0504  0.0784  94  LEU A CA  
648  C C   . LEU A 88  ? 0.4370 0.5323 0.4955 0.0020  0.0530  0.0818  94  LEU A C   
649  O O   . LEU A 88  ? 0.4298 0.5295 0.4920 0.0037  0.0565  0.0846  94  LEU A O   
650  C CB  . LEU A 88  ? 0.4308 0.5260 0.4878 -0.0061 0.0458  0.0787  94  LEU A CB  
651  C CG  . LEU A 88  ? 0.4514 0.5414 0.5037 -0.0104 0.0426  0.0756  94  LEU A CG  
652  C CD1 . LEU A 88  ? 0.4344 0.5315 0.4914 -0.0142 0.0379  0.0761  94  LEU A CD1 
653  C CD2 . LEU A 88  ? 0.3824 0.4630 0.4275 -0.0101 0.0413  0.0720  94  LEU A CD2 
654  N N   . GLN A 89  ? 0.4006 0.4966 0.4597 0.0035  0.0513  0.0815  95  GLN A N   
655  C CA  . GLN A 89  ? 0.4627 0.5664 0.5281 0.0066  0.0527  0.0848  95  GLN A CA  
656  C C   . GLN A 89  ? 0.4720 0.5862 0.5452 0.0045  0.0506  0.0876  95  GLN A C   
657  O O   . GLN A 89  ? 0.3882 0.5044 0.4623 0.0006  0.0463  0.0865  95  GLN A O   
658  C CB  . GLN A 89  ? 0.4400 0.5423 0.5044 0.0082  0.0507  0.0838  95  GLN A CB  
659  C CG  . GLN A 89  ? 0.4792 0.5907 0.5509 0.0104  0.0505  0.0870  95  GLN A CG  
660  C CD  . GLN A 89  ? 0.5572 0.6666 0.6274 0.0123  0.0491  0.0860  95  GLN A CD  
661  O OE1 . GLN A 89  ? 0.6250 0.7380 0.6975 0.0106  0.0450  0.0857  95  GLN A OE1 
662  N NE2 . GLN A 89  ? 0.5164 0.6198 0.5827 0.0159  0.0525  0.0853  95  GLN A NE2 
663  N N   . GLY A 90  ? 0.4765 0.5976 0.5556 0.0069  0.0538  0.0911  96  GLY A N   
664  C CA  . GLY A 90  ? 0.4463 0.5772 0.5330 0.0051  0.0527  0.0940  96  GLY A CA  
665  C C   . GLY A 90  ? 0.5358 0.6675 0.6234 0.0043  0.0557  0.0953  96  GLY A C   
666  O O   . GLY A 90  ? 0.5153 0.6555 0.6098 0.0035  0.0557  0.0982  96  GLY A O   
667  N N   . GLY A 91  ? 0.4967 0.6196 0.5776 0.0045  0.0581  0.0931  97  GLY A N   
668  C CA  . GLY A 91  ? 0.4862 0.6087 0.5671 0.0042  0.0615  0.0942  97  GLY A CA  
669  C C   . GLY A 91  ? 0.5495 0.6686 0.6271 -0.0002 0.0592  0.0919  97  GLY A C   
670  O O   . GLY A 91  ? 0.4994 0.6153 0.5747 -0.0002 0.0623  0.0919  97  GLY A O   
671  N N   . GLU A 92  ? 0.5175 0.6369 0.5946 -0.0037 0.0541  0.0900  98  GLU A N   
672  C CA  . GLU A 92  ? 0.4942 0.6109 0.5685 -0.0080 0.0518  0.0879  98  GLU A CA  
673  C C   . GLU A 92  ? 0.4989 0.6042 0.5641 -0.0080 0.0532  0.0846  98  GLU A C   
674  O O   . GLU A 92  ? 0.4700 0.5689 0.5304 -0.0054 0.0544  0.0830  98  GLU A O   
675  C CB  . GLU A 92  ? 0.5222 0.6418 0.5979 -0.0116 0.0459  0.0866  98  GLU A CB  
676  C CG  . GLU A 92  ? 0.5742 0.7051 0.6588 -0.0119 0.0441  0.0899  98  GLU A CG  
677  C CD  . GLU A 92  ? 0.6893 0.8245 0.7765 -0.0166 0.0393  0.0894  98  GLU A CD  
678  O OE1 . GLU A 92  ? 0.6811 0.8115 0.7638 -0.0192 0.0356  0.0864  98  GLU A OE1 
679  O OE2 . GLU A 92  ? 0.8053 0.9486 0.8991 -0.0178 0.0392  0.0921  98  GLU A OE2 
680  N N   . ALA A 93  ? 0.4644 0.5671 0.5273 -0.0107 0.0533  0.0836  99  ALA A N   
681  C CA  . ALA A 93  ? 0.4842 0.5763 0.5387 -0.0109 0.0547  0.0805  99  ALA A CA  
682  C C   . ALA A 93  ? 0.4999 0.5891 0.5513 -0.0157 0.0509  0.0779  99  ALA A C   
683  O O   . ALA A 93  ? 0.5024 0.5981 0.5585 -0.0186 0.0488  0.0791  99  ALA A O   
684  C CB  . ALA A 93  ? 0.4630 0.5536 0.5168 -0.0086 0.0601  0.0821  99  ALA A CB  
685  N N   . LEU A 94  ? 0.4490 0.5286 0.4926 -0.0164 0.0498  0.0743  100 LEU A N   
686  C CA  . LEU A 94  ? 0.3961 0.4719 0.4359 -0.0207 0.0463  0.0715  100 LEU A CA  
687  C C   . LEU A 94  ? 0.3983 0.4652 0.4312 -0.0208 0.0489  0.0695  100 LEU A C   
688  O O   . LEU A 94  ? 0.3881 0.4467 0.4148 -0.0187 0.0505  0.0675  100 LEU A O   
689  C CB  . LEU A 94  ? 0.4017 0.4741 0.4386 -0.0220 0.0420  0.0688  100 LEU A CB  
690  C CG  . LEU A 94  ? 0.4240 0.5051 0.4676 -0.0223 0.0390  0.0706  100 LEU A CG  
691  C CD1 . LEU A 94  ? 0.4089 0.4864 0.4494 -0.0235 0.0349  0.0680  100 LEU A CD1 
692  C CD2 . LEU A 94  ? 0.4769 0.5657 0.5259 -0.0257 0.0369  0.0722  100 LEU A CD2 
693  N N   . PRO A 95  ? 0.4366 0.5046 0.4699 -0.0233 0.0493  0.0698  101 PRO A N   
694  C CA  . PRO A 95  ? 0.3997 0.4589 0.4260 -0.0235 0.0516  0.0678  101 PRO A CA  
695  C C   . PRO A 95  ? 0.3472 0.3985 0.3668 -0.0264 0.0480  0.0638  101 PRO A C   
696  O O   . PRO A 95  ? 0.3532 0.4070 0.3743 -0.0295 0.0436  0.0628  101 PRO A O   
697  C CB  . PRO A 95  ? 0.4462 0.5103 0.4762 -0.0255 0.0528  0.0698  101 PRO A CB  
698  C CG  . PRO A 95  ? 0.4277 0.5013 0.4648 -0.0282 0.0489  0.0712  101 PRO A CG  
699  C CD  . PRO A 95  ? 0.4210 0.4984 0.4614 -0.0258 0.0479  0.0722  101 PRO A CD  
700  N N   . PHE A 96  ? 0.3565 0.3980 0.3685 -0.0253 0.0501  0.0614  102 PHE A N   
701  C CA  . PHE A 96  ? 0.3675 0.4009 0.3729 -0.0278 0.0469  0.0575  102 PHE A CA  
702  C C   . PHE A 96  ? 0.3787 0.4039 0.3774 -0.0282 0.0491  0.0557  102 PHE A C   
703  O O   . PHE A 96  ? 0.3869 0.4093 0.3838 -0.0253 0.0535  0.0567  102 PHE A O   
704  C CB  . PHE A 96  ? 0.3163 0.3447 0.3184 -0.0258 0.0459  0.0557  102 PHE A CB  
705  C CG  . PHE A 96  ? 0.3196 0.3424 0.3180 -0.0214 0.0503  0.0558  102 PHE A CG  
706  C CD1 . PHE A 96  ? 0.3410 0.3534 0.3315 -0.0209 0.0517  0.0530  102 PHE A CD1 
707  C CD2 . PHE A 96  ? 0.3524 0.3802 0.3554 -0.0177 0.0530  0.0585  102 PHE A CD2 
708  C CE1 . PHE A 96  ? 0.3432 0.3503 0.3302 -0.0169 0.0556  0.0530  102 PHE A CE1 
709  C CE2 . PHE A 96  ? 0.3735 0.3961 0.3731 -0.0136 0.0570  0.0586  102 PHE A CE2 
710  C CZ  . PHE A 96  ? 0.3655 0.3777 0.3571 -0.0133 0.0583  0.0558  102 PHE A CZ  
711  N N   . SER A 97  ? 0.2884 0.3096 0.2833 -0.0320 0.0459  0.0531  103 SER A N   
712  C CA  . SER A 97  ? 0.3108 0.3224 0.2980 -0.0324 0.0472  0.0505  103 SER A CA  
713  C C   . SER A 97  ? 0.3362 0.3387 0.3169 -0.0312 0.0463  0.0474  103 SER A C   
714  O O   . SER A 97  ? 0.3036 0.2977 0.2780 -0.0295 0.0488  0.0458  103 SER A O   
715  C CB  . SER A 97  ? 0.3010 0.3122 0.2870 -0.0370 0.0443  0.0490  103 SER A CB  
716  O OG  . SER A 97  ? 0.2797 0.2899 0.2648 -0.0398 0.0394  0.0468  103 SER A OG  
717  N N   . HIS A 98  ? 0.2809 0.2848 0.2629 -0.0319 0.0427  0.0465  104 HIS A N   
718  C CA  . HIS A 98  ? 0.2935 0.2895 0.2701 -0.0308 0.0416  0.0436  104 HIS A CA  
719  C C   . HIS A 98  ? 0.2977 0.2985 0.2787 -0.0290 0.0404  0.0448  104 HIS A C   
720  O O   . HIS A 98  ? 0.2261 0.2355 0.2134 -0.0304 0.0383  0.0467  104 HIS A O   
721  C CB  . HIS A 98  ? 0.2876 0.2778 0.2594 -0.0346 0.0375  0.0402  104 HIS A CB  
722  C CG  . HIS A 98  ? 0.3046 0.2897 0.2718 -0.0365 0.0385  0.0389  104 HIS A CG  
723  N ND1 . HIS A 98  ? 0.2921 0.2826 0.2625 -0.0386 0.0388  0.0405  104 HIS A ND1 
724  C CD2 . HIS A 98  ? 0.3436 0.3188 0.3032 -0.0365 0.0391  0.0361  104 HIS A CD2 
725  C CE1 . HIS A 98  ? 0.3218 0.3058 0.2867 -0.0399 0.0397  0.0388  104 HIS A CE1 
726  N NE2 . HIS A 98  ? 0.3448 0.3194 0.3030 -0.0386 0.0398  0.0361  104 HIS A NE2 
727  N N   . LEU A 99  ? 0.2893 0.2847 0.2670 -0.0258 0.0419  0.0438  105 LEU A N   
728  C CA  . LEU A 99  ? 0.2726 0.2717 0.2539 -0.0235 0.0414  0.0450  105 LEU A CA  
729  C C   . LEU A 99  ? 0.2623 0.2543 0.2389 -0.0238 0.0388  0.0417  105 LEU A C   
730  O O   . LEU A 99  ? 0.2625 0.2452 0.2324 -0.0230 0.0398  0.0393  105 LEU A O   
731  C CB  . LEU A 99  ? 0.2789 0.2790 0.2616 -0.0189 0.0463  0.0472  105 LEU A CB  
732  C CG  . LEU A 99  ? 0.3102 0.3134 0.2961 -0.0158 0.0465  0.0484  105 LEU A CG  
733  C CD1 . LEU A 99  ? 0.2621 0.2763 0.2561 -0.0167 0.0447  0.0512  105 LEU A CD1 
734  C CD2 . LEU A 99  ? 0.3209 0.3216 0.3055 -0.0113 0.0516  0.0497  105 LEU A CD2 
735  N N   . ILE A 100 ? 0.2535 0.2496 0.2334 -0.0249 0.0353  0.0418  106 ILE A N   
736  C CA  . ILE A 100 ? 0.2415 0.2318 0.2178 -0.0249 0.0328  0.0391  106 ILE A CA  
737  C C   . ILE A 100 ? 0.2395 0.2337 0.2196 -0.0215 0.0337  0.0408  106 ILE A C   
738  O O   . ILE A 100 ? 0.2321 0.2350 0.2185 -0.0218 0.0324  0.0431  106 ILE A O   
739  C CB  . ILE A 100 ? 0.2316 0.2226 0.2080 -0.0292 0.0277  0.0374  106 ILE A CB  
740  C CG1 . ILE A 100 ? 0.2350 0.2212 0.2070 -0.0325 0.0267  0.0353  106 ILE A CG1 
741  C CG2 . ILE A 100 ? 0.2109 0.1966 0.1843 -0.0288 0.0253  0.0350  106 ILE A CG2 
742  C CD1 . ILE A 100 ? 0.2136 0.2003 0.1855 -0.0369 0.0217  0.0336  106 ILE A CD1 
743  N N   . LEU A 101 ? 0.2213 0.2091 0.1976 -0.0183 0.0359  0.0398  107 LEU A N   
744  C CA  . LEU A 101 ? 0.2388 0.2294 0.2181 -0.0149 0.0370  0.0412  107 LEU A CA  
745  C C   . LEU A 101 ? 0.1932 0.1800 0.1705 -0.0157 0.0335  0.0388  107 LEU A C   
746  O O   . LEU A 101 ? 0.2208 0.1986 0.1919 -0.0162 0.0328  0.0357  107 LEU A O   
747  C CB  . LEU A 101 ? 0.2676 0.2542 0.2445 -0.0106 0.0418  0.0418  107 LEU A CB  
748  C CG  . LEU A 101 ? 0.3329 0.3245 0.3130 -0.0092 0.0456  0.0448  107 LEU A CG  
749  C CD1 . LEU A 101 ? 0.3924 0.3778 0.3683 -0.0054 0.0503  0.0447  107 LEU A CD1 
750  C CD2 . LEU A 101 ? 0.2749 0.2774 0.2630 -0.0081 0.0459  0.0484  107 LEU A CD2 
751  N N   . ALA A 102 ? 0.2258 0.2192 0.2081 -0.0158 0.0313  0.0401  108 ALA A N   
752  C CA  . ALA A 102 ? 0.1669 0.1578 0.1479 -0.0170 0.0275  0.0381  108 ALA A CA  
753  C C   . ALA A 102 ? 0.2241 0.2206 0.2099 -0.0143 0.0277  0.0402  108 ALA A C   
754  O O   . ALA A 102 ? 0.1919 0.1935 0.1813 -0.0159 0.0244  0.0407  108 ALA A O   
755  C CB  . ALA A 102 ? 0.1845 0.1776 0.1662 -0.0217 0.0232  0.0371  108 ALA A CB  
756  N N   . THR A 103 ? 0.2071 0.2027 0.1930 -0.0102 0.0316  0.0413  109 THR A N   
757  C CA  . THR A 103 ? 0.2298 0.2318 0.2208 -0.0071 0.0326  0.0439  109 THR A CA  
758  C C   . THR A 103 ? 0.1991 0.1975 0.1886 -0.0056 0.0312  0.0424  109 THR A C   
759  O O   . THR A 103 ? 0.2187 0.2224 0.2124 -0.0033 0.0316  0.0444  109 THR A O   
760  C CB  . THR A 103 ? 0.2312 0.2343 0.2232 -0.0033 0.0377  0.0461  109 THR A CB  
761  O OG1 . THR A 103 ? 0.2687 0.2620 0.2543 -0.0015 0.0400  0.0438  109 THR A OG1 
762  C CG2 . THR A 103 ? 0.2778 0.2857 0.2722 -0.0046 0.0391  0.0480  109 THR A CG2 
763  N N   . GLY A 104 ? 0.2228 0.2124 0.2066 -0.0068 0.0296  0.0391  110 GLY A N   
764  C CA  . GLY A 104 ? 0.2105 0.1971 0.1933 -0.0058 0.0278  0.0377  110 GLY A CA  
765  C C   . GLY A 104 ? 0.2520 0.2379 0.2354 -0.0011 0.0312  0.0388  110 GLY A C   
766  O O   . GLY A 104 ? 0.2459 0.2297 0.2279 0.0015  0.0351  0.0395  110 GLY A O   
767  N N   . SER A 105 ? 0.2095 0.1974 0.1951 0.0001  0.0297  0.0391  111 SER A N   
768  C CA  . SER A 105 ? 0.2460 0.2326 0.2319 0.0045  0.0324  0.0399  111 SER A CA  
769  C C   . SER A 105 ? 0.2659 0.2612 0.2579 0.0060  0.0318  0.0426  111 SER A C   
770  O O   . SER A 105 ? 0.2567 0.2578 0.2521 0.0034  0.0285  0.0433  111 SER A O   
771  C CB  . SER A 105 ? 0.2604 0.2381 0.2414 0.0050  0.0314  0.0368  111 SER A CB  
772  O OG  . SER A 105 ? 0.3520 0.3212 0.3271 0.0033  0.0313  0.0340  111 SER A OG  
773  N N   . THR A 106 ? 0.2429 0.2393 0.2364 0.0102  0.0351  0.0442  112 THR A N   
774  C CA  . THR A 106 ? 0.2395 0.2430 0.2383 0.0122  0.0348  0.0466  112 THR A CA  
775  C C   . THR A 106 ? 0.2367 0.2351 0.2334 0.0149  0.0352  0.0453  112 THR A C   
776  O O   . THR A 106 ? 0.2174 0.2075 0.2091 0.0162  0.0369  0.0432  112 THR A O   
777  C CB  . THR A 106 ? 0.2886 0.2993 0.2921 0.0151  0.0384  0.0501  112 THR A CB  
778  O OG1 . THR A 106 ? 0.3227 0.3278 0.3229 0.0185  0.0427  0.0498  112 THR A OG1 
779  C CG2 . THR A 106 ? 0.2941 0.3104 0.3003 0.0127  0.0383  0.0517  112 THR A CG2 
780  N N   . GLY A 107 ? 0.2237 0.2273 0.2242 0.0158  0.0336  0.0466  113 GLY A N   
781  C CA  . GLY A 107 ? 0.2242 0.2237 0.2233 0.0184  0.0339  0.0457  113 GLY A CA  
782  C C   . GLY A 107 ? 0.1966 0.2036 0.2007 0.0189  0.0318  0.0476  113 GLY A C   
783  O O   . GLY A 107 ? 0.1931 0.2082 0.2017 0.0173  0.0304  0.0497  113 GLY A O   
784  N N   . PRO A 108 ? 0.1941 0.1986 0.1976 0.0212  0.0318  0.0470  114 PRO A N   
785  C CA  . PRO A 108 ? 0.2015 0.2128 0.2097 0.0221  0.0301  0.0490  114 PRO A CA  
786  C C   . PRO A 108 ? 0.1793 0.1931 0.1885 0.0182  0.0252  0.0483  114 PRO A C   
787  O O   . PRO A 108 ? 0.1655 0.1734 0.1708 0.0153  0.0228  0.0455  114 PRO A O   
788  C CB  . PRO A 108 ? 0.1848 0.1910 0.1910 0.0255  0.0314  0.0480  114 PRO A CB  
789  C CG  . PRO A 108 ? 0.2171 0.2128 0.2171 0.0248  0.0320  0.0447  114 PRO A CG  
790  C CD  . PRO A 108 ? 0.2075 0.2025 0.2060 0.0230  0.0332  0.0445  114 PRO A CD  
791  N N   . PHE A 109 ? 0.1379 0.1605 0.1524 0.0181  0.0237  0.0508  115 PHE A N   
792  C CA  . PHE A 109 ? 0.1874 0.2126 0.2031 0.0153  0.0192  0.0504  115 PHE A CA  
793  C C   . PHE A 109 ? 0.1644 0.1840 0.1775 0.0166  0.0181  0.0486  115 PHE A C   
794  O O   . PHE A 109 ? 0.1528 0.1709 0.1659 0.0204  0.0208  0.0492  115 PHE A O   
795  C CB  . PHE A 109 ? 0.1679 0.2037 0.1900 0.0157  0.0183  0.0538  115 PHE A CB  
796  C CG  . PHE A 109 ? 0.1623 0.2017 0.1861 0.0126  0.0136  0.0536  115 PHE A CG  
797  C CD1 . PHE A 109 ? 0.1477 0.1897 0.1721 0.0084  0.0110  0.0534  115 PHE A CD1 
798  C CD2 . PHE A 109 ? 0.2042 0.2443 0.2288 0.0138  0.0118  0.0537  115 PHE A CD2 
799  C CE1 . PHE A 109 ? 0.1662 0.2114 0.1920 0.0055  0.0066  0.0533  115 PHE A CE1 
800  C CE2 . PHE A 109 ? 0.2132 0.2563 0.2391 0.0109  0.0074  0.0536  115 PHE A CE2 
801  C CZ  . PHE A 109 ? 0.1438 0.1895 0.1703 0.0067  0.0048  0.0534  115 PHE A CZ  
802  N N   . PRO A 110 ? 0.1508 0.1674 0.1618 0.0135  0.0142  0.0465  116 PRO A N   
803  C CA  . PRO A 110 ? 0.1433 0.1617 0.1543 0.0089  0.0104  0.0458  116 PRO A CA  
804  C C   . PRO A 110 ? 0.1365 0.1482 0.1429 0.0060  0.0102  0.0432  116 PRO A C   
805  O O   . PRO A 110 ? 0.1416 0.1551 0.1482 0.0022  0.0074  0.0427  116 PRO A O   
806  C CB  . PRO A 110 ? 0.1571 0.1744 0.1677 0.0078  0.0068  0.0447  116 PRO A CB  
807  C CG  . PRO A 110 ? 0.1740 0.1836 0.1811 0.0107  0.0086  0.0430  116 PRO A CG  
808  C CD  . PRO A 110 ? 0.1583 0.1693 0.1668 0.0148  0.0133  0.0448  116 PRO A CD  
809  N N   . GLY A 111 ? 0.1646 0.1686 0.1669 0.0077  0.0128  0.0414  117 GLY A N   
810  C CA  . GLY A 111 ? 0.1364 0.1334 0.1339 0.0050  0.0123  0.0387  117 GLY A CA  
811  C C   . GLY A 111 ? 0.1751 0.1753 0.1735 0.0031  0.0131  0.0396  117 GLY A C   
812  O O   . GLY A 111 ? 0.1812 0.1777 0.1766 -0.0003 0.0115  0.0376  117 GLY A O   
813  N N   . LYS A 112 ? 0.1607 0.1678 0.1632 0.0051  0.0157  0.0425  118 LYS A N   
814  C CA  . LYS A 112 ? 0.1940 0.2055 0.1983 0.0035  0.0165  0.0439  118 LYS A CA  
815  C C   . LYS A 112 ? 0.2073 0.2295 0.2181 0.0038  0.0161  0.0473  118 LYS A C   
816  O O   . LYS A 112 ? 0.1835 0.2094 0.1973 0.0068  0.0169  0.0490  118 LYS A O   
817  C CB  . LYS A 112 ? 0.2131 0.2213 0.2154 0.0059  0.0211  0.0441  118 LYS A CB  
818  C CG  . LYS A 112 ? 0.2250 0.2226 0.2209 0.0058  0.0219  0.0408  118 LYS A CG  
819  C CD  . LYS A 112 ? 0.2908 0.2850 0.2836 0.0013  0.0194  0.0387  118 LYS A CD  
820  C CE  . LYS A 112 ? 0.3148 0.2981 0.3010 0.0010  0.0196  0.0353  118 LYS A CE  
821  N NZ  . LYS A 112 ? 0.2745 0.2539 0.2575 -0.0034 0.0166  0.0328  118 LYS A NZ  
822  N N   . PHE A 113 ? 0.1713 0.1984 0.1843 0.0009  0.0148  0.0482  119 PHE A N   
823  C CA  . PHE A 113 ? 0.1891 0.2265 0.2084 0.0008  0.0141  0.0514  119 PHE A CA  
824  C C   . PHE A 113 ? 0.2344 0.2753 0.2554 -0.0003 0.0159  0.0528  119 PHE A C   
825  O O   . PHE A 113 ? 0.2339 0.2744 0.2538 -0.0040 0.0139  0.0518  119 PHE A O   
826  C CB  . PHE A 113 ? 0.1498 0.1907 0.1708 -0.0024 0.0092  0.0512  119 PHE A CB  
827  C CG  . PHE A 113 ? 0.1887 0.2400 0.2161 -0.0025 0.0083  0.0544  119 PHE A CG  
828  C CD1 . PHE A 113 ? 0.2020 0.2580 0.2331 0.0004  0.0086  0.0564  119 PHE A CD1 
829  C CD2 . PHE A 113 ? 0.1917 0.2481 0.2217 -0.0056 0.0071  0.0554  119 PHE A CD2 
830  C CE1 . PHE A 113 ? 0.2244 0.2900 0.2615 0.0004  0.0076  0.0594  119 PHE A CE1 
831  C CE2 . PHE A 113 ? 0.2282 0.2943 0.2644 -0.0057 0.0061  0.0584  119 PHE A CE2 
832  C CZ  . PHE A 113 ? 0.2150 0.2858 0.2547 -0.0027 0.0064  0.0604  119 PHE A CZ  
833  N N   . ASN A 114 ? 0.2367 0.2812 0.2605 0.0030  0.0198  0.0552  120 ASN A N   
834  C CA  . ASN A 114 ? 0.3019 0.3498 0.3275 0.0023  0.0219  0.0568  120 ASN A CA  
835  C C   . ASN A 114 ? 0.3251 0.3828 0.3574 0.0045  0.0235  0.0606  120 ASN A C   
836  O O   . ASN A 114 ? 0.4012 0.4604 0.4350 0.0074  0.0275  0.0624  120 ASN A O   
837  C CB  . ASN A 114 ? 0.3009 0.3414 0.3218 0.0040  0.0258  0.0554  120 ASN A CB  
838  C CG  . ASN A 114 ? 0.3131 0.3446 0.3277 0.0013  0.0241  0.0518  120 ASN A CG  
839  O OD1 . ASN A 114 ? 0.3093 0.3410 0.3232 -0.0025 0.0217  0.0509  120 ASN A OD1 
840  N ND2 . ASN A 114 ? 0.2754 0.2987 0.2852 0.0033  0.0252  0.0496  120 ASN A ND2 
841  N N   . GLU A 115 ? 0.3463 0.4109 0.3830 0.0029  0.0201  0.0619  121 GLU A N   
842  C CA  . GLU A 115 ? 0.3346 0.4090 0.3781 0.0045  0.0208  0.0655  121 GLU A CA  
843  C C   . GLU A 115 ? 0.3589 0.4395 0.4059 0.0009  0.0188  0.0667  121 GLU A C   
844  O O   . GLU A 115 ? 0.3314 0.4102 0.3765 -0.0030 0.0154  0.0648  121 GLU A O   
845  C CB  . GLU A 115 ? 0.3283 0.4062 0.3744 0.0057  0.0184  0.0663  121 GLU A CB  
846  C CG  . GLU A 115 ? 0.3871 0.4608 0.4311 0.0099  0.0209  0.0659  121 GLU A CG  
847  N N   . VAL A 116 ? 0.2990 0.3866 0.3510 0.0021  0.0212  0.0698  122 VAL A N   
848  C CA  . VAL A 116 ? 0.3814 0.4762 0.4378 -0.0011 0.0191  0.0713  122 VAL A CA  
849  C C   . VAL A 116 ? 0.4194 0.5204 0.4798 -0.0021 0.0151  0.0723  122 VAL A C   
850  O O   . VAL A 116 ? 0.3853 0.4908 0.4493 0.0009  0.0157  0.0743  122 VAL A O   
851  C CB  . VAL A 116 ? 0.4058 0.5065 0.4667 0.0006  0.0228  0.0744  122 VAL A CB  
852  C CG1 . VAL A 116 ? 0.3603 0.4690 0.4264 -0.0027 0.0203  0.0761  122 VAL A CG1 
853  C CG2 . VAL A 116 ? 0.3896 0.4835 0.4460 0.0013  0.0266  0.0731  122 VAL A CG2 
854  N N   . SER A 117 ? 0.3957 0.4966 0.4552 -0.0062 0.0108  0.0708  123 SER A N   
855  C CA  . SER A 117 ? 0.4378 0.5418 0.4991 -0.0073 0.0067  0.0709  123 SER A CA  
856  C C   . SER A 117 ? 0.3699 0.4755 0.4313 -0.0122 0.0025  0.0699  123 SER A C   
857  O O   . SER A 117 ? 0.3704 0.4720 0.4287 -0.0148 0.0026  0.0682  123 SER A O   
858  C CB  . SER A 117 ? 0.5532 0.6496 0.6094 -0.0059 0.0059  0.0684  123 SER A CB  
859  O OG  . SER A 117 ? 0.4082 0.4963 0.4583 -0.0085 0.0050  0.0650  123 SER A OG  
860  N N   . SER A 118 ? 0.2542 0.3654 0.3190 -0.0134 -0.0012 0.0709  124 SER A N   
861  C CA  . SER A 118 ? 0.2442 0.3562 0.3086 -0.0180 -0.0056 0.0697  124 SER A CA  
862  C C   . SER A 118 ? 0.1730 0.2769 0.2314 -0.0192 -0.0080 0.0664  124 SER A C   
863  O O   . SER A 118 ? 0.1557 0.2549 0.2114 -0.0163 -0.0068 0.0654  124 SER A O   
864  C CB  . SER A 118 ? 0.1786 0.3000 0.2492 -0.0189 -0.0086 0.0722  124 SER A CB  
865  O OG  . SER A 118 ? 0.1555 0.2773 0.2265 -0.0163 -0.0095 0.0725  124 SER A OG  
866  N N   . GLN A 119 ? 0.1411 0.2434 0.1976 -0.0235 -0.0115 0.0646  125 GLN A N   
867  C CA  . GLN A 119 ? 0.1747 0.2695 0.2256 -0.0250 -0.0141 0.0615  125 GLN A CA  
868  C C   . GLN A 119 ? 0.1721 0.2681 0.2238 -0.0234 -0.0162 0.0618  125 GLN A C   
869  O O   . GLN A 119 ? 0.1326 0.2217 0.1800 -0.0221 -0.0162 0.0598  125 GLN A O   
870  C CB  . GLN A 119 ? 0.1946 0.2887 0.2440 -0.0300 -0.0177 0.0599  125 GLN A CB  
871  C CG  . GLN A 119 ? 0.1897 0.2763 0.2336 -0.0320 -0.0207 0.0567  125 GLN A CG  
872  C CD  . GLN A 119 ? 0.2699 0.3533 0.3108 -0.0366 -0.0228 0.0546  125 GLN A CD  
873  O OE1 . GLN A 119 ? 0.3135 0.3964 0.3540 -0.0375 -0.0209 0.0546  125 GLN A OE1 
874  N NE2 . GLN A 119 ? 0.3549 0.4358 0.3935 -0.0393 -0.0268 0.0529  125 GLN A NE2 
875  N N   . GLN A 120 ? 0.1272 0.2318 0.1846 -0.0233 -0.0180 0.0644  126 GLN A N   
876  C CA  . GLN A 120 ? 0.1492 0.2545 0.2069 -0.0219 -0.0203 0.0646  126 GLN A CA  
877  C C   . GLN A 120 ? 0.1292 0.2335 0.1872 -0.0169 -0.0168 0.0656  126 GLN A C   
878  O O   . GLN A 120 ? 0.1010 0.2016 0.1566 -0.0153 -0.0176 0.0645  126 GLN A O   
879  C CB  . GLN A 120 ? 0.2060 0.3202 0.2691 -0.0235 -0.0237 0.0668  126 GLN A CB  
880  C CG  . GLN A 120 ? 0.2306 0.3446 0.2924 -0.0286 -0.0281 0.0654  126 GLN A CG  
881  C CD  . GLN A 120 ? 0.2731 0.3776 0.3281 -0.0304 -0.0298 0.0617  126 GLN A CD  
882  O OE1 . GLN A 120 ? 0.2479 0.3490 0.3006 -0.0291 -0.0310 0.0607  126 GLN A OE1 
883  N NE2 . GLN A 120 ? 0.2411 0.3414 0.2929 -0.0335 -0.0299 0.0598  126 GLN A NE2 
884  N N   . ALA A 121 ? 0.1085 0.2159 0.1693 -0.0144 -0.0129 0.0675  127 ALA A N   
885  C CA  . ALA A 121 ? 0.1307 0.2363 0.1913 -0.0096 -0.0093 0.0683  127 ALA A CA  
886  C C   . ALA A 121 ? 0.1172 0.2124 0.1712 -0.0087 -0.0077 0.0652  127 ALA A C   
887  O O   . ALA A 121 ? 0.1389 0.2306 0.1911 -0.0058 -0.0069 0.0647  127 ALA A O   
888  C CB  . ALA A 121 ? 0.1408 0.2517 0.2056 -0.0072 -0.0054 0.0710  127 ALA A CB  
889  N N   . ALA A 122 ? 0.1159 0.2059 0.1662 -0.0112 -0.0073 0.0631  128 ALA A N   
890  C CA  . ALA A 122 ? 0.1103 0.1901 0.1541 -0.0107 -0.0059 0.0601  128 ALA A CA  
891  C C   . ALA A 122 ? 0.0987 0.1738 0.1391 -0.0117 -0.0093 0.0579  128 ALA A C   
892  O O   . ALA A 122 ? 0.1150 0.1841 0.1522 -0.0093 -0.0080 0.0565  128 ALA A O   
893  C CB  . ALA A 122 ? 0.1278 0.2037 0.1686 -0.0136 -0.0055 0.0584  128 ALA A CB  
894  N N   . ILE A 123 ? 0.0903 0.1677 0.1314 -0.0154 -0.0135 0.0575  129 ILE A N   
895  C CA  . ILE A 123 ? 0.1129 0.1863 0.1510 -0.0165 -0.0169 0.0556  129 ILE A CA  
896  C C   . ILE A 123 ? 0.1286 0.2044 0.1688 -0.0130 -0.0167 0.0570  129 ILE A C   
897  O O   . ILE A 123 ? 0.1152 0.1849 0.1519 -0.0116 -0.0169 0.0553  129 ILE A O   
898  C CB  . ILE A 123 ? 0.1094 0.1861 0.1485 -0.0210 -0.0214 0.0553  129 ILE A CB  
899  C CG1 . ILE A 123 ? 0.1374 0.2101 0.1734 -0.0246 -0.0218 0.0534  129 ILE A CG1 
900  C CG2 . ILE A 123 ? 0.1358 0.2102 0.1731 -0.0217 -0.0250 0.0541  129 ILE A CG2 
901  C CD1 . ILE A 123 ? 0.1265 0.2039 0.1645 -0.0289 -0.0257 0.0537  129 ILE A CD1 
902  N N   . GLN A 124 ? 0.0968 0.1813 0.1427 -0.0114 -0.0163 0.0601  130 GLN A N   
903  C CA  . GLN A 124 ? 0.1293 0.2165 0.1774 -0.0079 -0.0159 0.0617  130 GLN A CA  
904  C C   . GLN A 124 ? 0.1429 0.2249 0.1888 -0.0036 -0.0118 0.0613  130 GLN A C   
905  O O   . GLN A 124 ? 0.1239 0.2041 0.1690 -0.0011 -0.0119 0.0611  130 GLN A O   
906  C CB  . GLN A 124 ? 0.1638 0.2614 0.2186 -0.0070 -0.0160 0.0653  130 GLN A CB  
907  C CG  . GLN A 124 ? 0.1908 0.2919 0.2481 -0.0039 -0.0166 0.0669  130 GLN A CG  
908  C CD  . GLN A 124 ? 0.2325 0.3323 0.2881 -0.0059 -0.0211 0.0657  130 GLN A CD  
909  O OE1 . GLN A 124 ? 0.2639 0.3666 0.3205 -0.0096 -0.0246 0.0656  130 GLN A OE1 
910  N NE2 . GLN A 124 ? 0.2200 0.3152 0.2730 -0.0036 -0.0210 0.0647  130 GLN A NE2 
911  N N   . ALA A 125 ? 0.1160 0.1960 0.1611 -0.0026 -0.0081 0.0612  131 ALA A N   
912  C CA  . ALA A 125 ? 0.1330 0.2076 0.1756 0.0013  -0.0042 0.0606  131 ALA A CA  
913  C C   . ALA A 125 ? 0.1039 0.1692 0.1407 0.0011  -0.0052 0.0574  131 ALA A C   
914  O O   . ALA A 125 ? 0.1070 0.1692 0.1427 0.0043  -0.0037 0.0572  131 ALA A O   
915  C CB  . ALA A 125 ? 0.1620 0.2349 0.2038 0.0020  -0.0003 0.0607  131 ALA A CB  
916  N N   . TYR A 126 ? 0.1107 0.1714 0.1440 -0.0028 -0.0078 0.0550  132 TYR A N   
917  C CA  . TYR A 126 ? 0.1079 0.1600 0.1360 -0.0033 -0.0091 0.0520  132 TYR A CA  
918  C C   . TYR A 126 ? 0.1276 0.1813 0.1565 -0.0033 -0.0124 0.0522  132 TYR A C   
919  O O   . TYR A 126 ? 0.1245 0.1729 0.1508 -0.0014 -0.0120 0.0509  132 TYR A O   
920  C CB  . TYR A 126 ? 0.1005 0.1473 0.1246 -0.0074 -0.0107 0.0494  132 TYR A CB  
921  C CG  . TYR A 126 ? 0.0939 0.1358 0.1154 -0.0063 -0.0070 0.0484  132 TYR A CG  
922  C CD1 . TYR A 126 ? 0.1069 0.1402 0.1239 -0.0045 -0.0051 0.0462  132 TYR A CD1 
923  C CD2 . TYR A 126 ? 0.1094 0.1556 0.1333 -0.0067 -0.0051 0.0500  132 TYR A CD2 
924  C CE1 . TYR A 126 ? 0.0965 0.1253 0.1110 -0.0033 -0.0016 0.0454  132 TYR A CE1 
925  C CE2 . TYR A 126 ? 0.1003 0.1420 0.1217 -0.0055 -0.0014 0.0492  132 TYR A CE2 
926  C CZ  . TYR A 126 ? 0.1162 0.1491 0.1328 -0.0037 0.0002  0.0469  132 TYR A CZ  
927  O OH  . TYR A 126 ? 0.1347 0.1630 0.1487 -0.0025 0.0037  0.0462  132 TYR A OH  
928  N N   . GLU A 127 ? 0.1209 0.1818 0.1534 -0.0055 -0.0155 0.0538  133 GLU A N   
929  C CA  . GLU A 127 ? 0.1472 0.2097 0.1805 -0.0052 -0.0185 0.0541  133 GLU A CA  
930  C C   . GLU A 127 ? 0.1551 0.2198 0.1906 -0.0005 -0.0162 0.0559  133 GLU A C   
931  O O   . GLU A 127 ? 0.1397 0.2015 0.1737 0.0009  -0.0173 0.0552  133 GLU A O   
932  C CB  . GLU A 127 ? 0.1379 0.2079 0.1748 -0.0083 -0.0222 0.0556  133 GLU A CB  
933  C CG  . GLU A 127 ? 0.2067 0.2741 0.2410 -0.0132 -0.0254 0.0536  133 GLU A CG  
934  C CD  . GLU A 127 ? 0.2592 0.3186 0.2883 -0.0146 -0.0277 0.0507  133 GLU A CD  
935  O OE1 . GLU A 127 ? 0.2354 0.2930 0.2638 -0.0125 -0.0283 0.0505  133 GLU A OE1 
936  O OE2 . GLU A 127 ? 0.2618 0.3166 0.2877 -0.0179 -0.0290 0.0485  133 GLU A OE2 
937  N N   . ASP A 128 ? 0.1284 0.1978 0.1674 0.0021  -0.0129 0.0582  134 ASP A N   
938  C CA  . ASP A 128 ? 0.1453 0.2164 0.1862 0.0068  -0.0104 0.0599  134 ASP A CA  
939  C C   . ASP A 128 ? 0.1525 0.2146 0.1887 0.0092  -0.0078 0.0577  134 ASP A C   
940  O O   . ASP A 128 ? 0.1613 0.2221 0.1973 0.0122  -0.0073 0.0580  134 ASP A O   
941  C CB  . ASP A 128 ? 0.1806 0.2585 0.2261 0.0089  -0.0072 0.0628  134 ASP A CB  
942  C CG  . ASP A 128 ? 0.2471 0.3348 0.2981 0.0073  -0.0097 0.0654  134 ASP A CG  
943  O OD1 . ASP A 128 ? 0.2714 0.3608 0.3227 0.0052  -0.0137 0.0652  134 ASP A OD1 
944  O OD2 . ASP A 128 ? 0.2959 0.3895 0.3509 0.0082  -0.0075 0.0677  134 ASP A OD2 
945  N N   . MET A 129 ? 0.1353 0.1913 0.1679 0.0081  -0.0062 0.0557  135 MET A N   
946  C CA  . MET A 129 ? 0.1462 0.1931 0.1742 0.0100  -0.0040 0.0534  135 MET A CA  
947  C C   . MET A 129 ? 0.1149 0.1567 0.1398 0.0090  -0.0070 0.0513  135 MET A C   
948  O O   . MET A 129 ? 0.1206 0.1581 0.1438 0.0119  -0.0057 0.0507  135 MET A O   
949  C CB  . MET A 129 ? 0.1673 0.2088 0.1919 0.0084  -0.0024 0.0515  135 MET A CB  
950  C CG  . MET A 129 ? 0.1819 0.2141 0.2018 0.0104  0.0001  0.0492  135 MET A CG  
951  S SD  . MET A 129 ? 0.2999 0.3333 0.3217 0.0161  0.0052  0.0511  135 MET A SD  
952  C CE  . MET A 129 ? 0.2635 0.2863 0.2800 0.0181  0.0062  0.0483  135 MET A CE  
953  N N   . VAL A 130 ? 0.1259 0.1678 0.1499 0.0050  -0.0110 0.0503  136 VAL A N   
954  C CA  . VAL A 130 ? 0.1192 0.1567 0.1404 0.0038  -0.0140 0.0485  136 VAL A CA  
955  C C   . VAL A 130 ? 0.1167 0.1577 0.1404 0.0069  -0.0143 0.0502  136 VAL A C   
956  O O   . VAL A 130 ? 0.1160 0.1516 0.1371 0.0086  -0.0142 0.0490  136 VAL A O   
957  C CB  . VAL A 130 ? 0.1366 0.1752 0.1573 -0.0010 -0.0183 0.0476  136 VAL A CB  
958  C CG1 . VAL A 130 ? 0.1454 0.1794 0.1633 -0.0020 -0.0214 0.0459  136 VAL A CG1 
959  C CG2 . VAL A 130 ? 0.1321 0.1667 0.1501 -0.0040 -0.0179 0.0457  136 VAL A CG2 
960  N N   . ARG A 131 ? 0.1350 0.1850 0.1636 0.0075  -0.0147 0.0531  137 ARG A N   
961  C CA  . ARG A 131 ? 0.1639 0.2178 0.1951 0.0105  -0.0151 0.0550  137 ARG A CA  
962  C C   . ARG A 131 ? 0.1485 0.1994 0.1792 0.0152  -0.0110 0.0553  137 ARG A C   
963  O O   . ARG A 131 ? 0.1454 0.1946 0.1754 0.0175  -0.0113 0.0553  137 ARG A O   
964  C CB  . ARG A 131 ? 0.1725 0.2367 0.2093 0.0102  -0.0162 0.0581  137 ARG A CB  
965  C CG  . ARG A 131 ? 0.2474 0.3148 0.2848 0.0060  -0.0209 0.0580  137 ARG A CG  
966  C CD  . ARG A 131 ? 0.4647 0.5425 0.5078 0.0058  -0.0221 0.0611  137 ARG A CD  
967  N NE  . ARG A 131 ? 0.3619 0.4432 0.4071 0.0038  -0.0211 0.0618  137 ARG A NE  
968  N N   . GLN A 132 ? 0.1570 0.2071 0.1878 0.0168  -0.0072 0.0556  138 GLN A N   
969  C CA  . GLN A 132 ? 0.1363 0.1830 0.1663 0.0213  -0.0033 0.0557  138 GLN A CA  
970  C C   . GLN A 132 ? 0.1513 0.1882 0.1761 0.0215  -0.0034 0.0527  138 GLN A C   
971  O O   . GLN A 132 ? 0.1315 0.1661 0.1558 0.0247  -0.0022 0.0527  138 GLN A O   
972  C CB  . GLN A 132 ? 0.1527 0.1994 0.1831 0.0227  0.0007  0.0562  138 GLN A CB  
973  C CG  . GLN A 132 ? 0.1734 0.2294 0.2090 0.0226  0.0015  0.0593  138 GLN A CG  
974  C CD  . GLN A 132 ? 0.2188 0.2824 0.2590 0.0252  0.0013  0.0622  138 GLN A CD  
975  O OE1 . GLN A 132 ? 0.1832 0.2454 0.2233 0.0288  0.0029  0.0626  138 GLN A OE1 
976  N NE2 . GLN A 132 ? 0.3027 0.3746 0.3472 0.0234  -0.0009 0.0643  138 GLN A NE2 
977  N N   . VAL A 133 ? 0.1360 0.1671 0.1571 0.0182  -0.0047 0.0501  139 VAL A N   
978  C CA  . VAL A 133 ? 0.1441 0.1659 0.1604 0.0181  -0.0050 0.0472  139 VAL A CA  
979  C C   . VAL A 133 ? 0.1271 0.1488 0.1434 0.0180  -0.0081 0.0471  139 VAL A C   
980  O O   . VAL A 133 ? 0.1214 0.1382 0.1357 0.0204  -0.0072 0.0461  139 VAL A O   
981  C CB  . VAL A 133 ? 0.1128 0.1291 0.1255 0.0142  -0.0063 0.0446  139 VAL A CB  
982  C CG1 . VAL A 133 ? 0.1403 0.1473 0.1483 0.0136  -0.0074 0.0416  139 VAL A CG1 
983  C CG2 . VAL A 133 ? 0.1068 0.1216 0.1189 0.0149  -0.0028 0.0444  139 VAL A CG2 
984  N N   . GLN A 134 ? 0.1170 0.1442 0.1352 0.0153  -0.0117 0.0480  140 GLN A N   
985  C CA  . GLN A 134 ? 0.1528 0.1798 0.1706 0.0149  -0.0148 0.0479  140 GLN A CA  
986  C C   . GLN A 134 ? 0.1562 0.1861 0.1764 0.0193  -0.0132 0.0498  140 GLN A C   
987  O O   . GLN A 134 ? 0.1482 0.1744 0.1666 0.0205  -0.0142 0.0491  140 GLN A O   
988  C CB  . GLN A 134 ? 0.1671 0.1999 0.1868 0.0112  -0.0188 0.0487  140 GLN A CB  
989  C CG  . GLN A 134 ? 0.1788 0.2070 0.1953 0.0068  -0.0209 0.0463  140 GLN A CG  
990  C CD  . GLN A 134 ? 0.2205 0.2540 0.2386 0.0028  -0.0248 0.0469  140 GLN A CD  
991  O OE1 . GLN A 134 ? 0.1902 0.2319 0.2125 0.0030  -0.0255 0.0494  140 GLN A OE1 
992  N NE2 . GLN A 134 ? 0.2528 0.2815 0.2675 -0.0010 -0.0273 0.0445  140 GLN A NE2 
993  N N   . ARG A 135 ? 0.1442 0.1804 0.1682 0.0218  -0.0108 0.0524  141 ARG A N   
994  C CA  . ARG A 135 ? 0.1783 0.2174 0.2045 0.0260  -0.0092 0.0543  141 ARG A CA  
995  C C   . ARG A 135 ? 0.1872 0.2195 0.2109 0.0296  -0.0057 0.0531  141 ARG A C   
996  O O   . ARG A 135 ? 0.1746 0.2074 0.1991 0.0329  -0.0048 0.0541  141 ARG A O   
997  C CB  . ARG A 135 ? 0.2199 0.2679 0.2511 0.0277  -0.0075 0.0575  141 ARG A CB  
998  C CG  . ARG A 135 ? 0.3284 0.3846 0.3632 0.0250  -0.0108 0.0593  141 ARG A CG  
999  C CD  . ARG A 135 ? 0.6106 0.6751 0.6505 0.0282  -0.0093 0.0626  141 ARG A CD  
1000 N NE  . ARG A 135 ? 0.7652 0.8285 0.8049 0.0318  -0.0086 0.0631  141 ARG A NE  
1001 C CZ  . ARG A 135 ? 0.7203 0.7877 0.7627 0.0349  -0.0062 0.0646  141 ARG A CZ  
1002 N NH1 . ARG A 135 ? 0.6906 0.7651 0.7374 0.0360  -0.0045 0.0674  141 ARG A NH1 
1003 N NH2 . ARG A 135 ? 0.5728 0.6369 0.6135 0.0369  -0.0054 0.0632  141 ARG A NH2 
1004 N N   . SER A 136 ? 0.1439 0.1697 0.1645 0.0290  -0.0037 0.0510  142 SER A N   
1005 C CA  . SER A 136 ? 0.1563 0.1765 0.1750 0.0326  0.0002  0.0502  142 SER A CA  
1006 C C   . SER A 136 ? 0.1734 0.1843 0.1876 0.0321  -0.0006 0.0473  142 SER A C   
1007 O O   . SER A 136 ? 0.1845 0.1903 0.1956 0.0289  -0.0021 0.0450  142 SER A O   
1008 C CB  . SER A 136 ? 0.1225 0.1415 0.1407 0.0325  0.0032  0.0499  142 SER A CB  
1009 O OG  . SER A 136 ? 0.1291 0.1567 0.1516 0.0327  0.0040  0.0526  142 SER A OG  
1010 N N   . ARG A 137 ? 0.1621 0.1708 0.1760 0.0355  0.0005  0.0475  143 ARG A N   
1011 C CA  . ARG A 137 ? 0.1696 0.1693 0.1793 0.0350  0.0002  0.0442  143 ARG A CA  
1012 C C   . ARG A 137 ? 0.1785 0.1713 0.1855 0.0360  0.0034  0.0422  143 ARG A C   
1013 O O   . ARG A 137 ? 0.1863 0.1716 0.1896 0.0341  0.0026  0.0393  143 ARG A O   
1014 C CB  . ARG A 137 ? 0.2115 0.2110 0.2214 0.0365  0.0004  0.0429  143 ARG A CB  
1015 C CG  . ARG A 137 ? 0.2279 0.2186 0.2338 0.0358  0.0006  0.0389  143 ARG A CG  
1016 C CD  . ARG A 137 ? 0.2569 0.2439 0.2604 0.0325  -0.0033 0.0372  143 ARG A CD  
1017 N NE  . ARG A 137 ? 0.2724 0.2634 0.2772 0.0320  -0.0059 0.0379  143 ARG A NE  
1018 C CZ  . ARG A 137 ? 0.3054 0.2936 0.3082 0.0294  -0.0093 0.0364  143 ARG A CZ  
1019 N NH1 . ARG A 137 ? 0.2450 0.2268 0.2445 0.0270  -0.0106 0.0342  143 ARG A NH1 
1020 N NH2 . ARG A 137 ? 0.2747 0.2666 0.2785 0.0292  -0.0114 0.0370  143 ARG A NH2 
1021 N N   . PHE A 138 ? 0.1589 0.1540 0.1676 0.0389  0.0071  0.0436  144 PHE A N   
1022 C CA  . PHE A 138 ? 0.1464 0.1355 0.1526 0.0399  0.0104  0.0417  144 PHE A CA  
1023 C C   . PHE A 138 ? 0.1302 0.1218 0.1373 0.0396  0.0118  0.0435  144 PHE A C   
1024 O O   . PHE A 138 ? 0.1207 0.1202 0.1315 0.0404  0.0125  0.0461  144 PHE A O   
1025 C CB  . PHE A 138 ? 0.1438 0.1331 0.1505 0.0429  0.0138  0.0411  144 PHE A CB  
1026 C CG  . PHE A 138 ? 0.1782 0.1652 0.1838 0.0425  0.0127  0.0387  144 PHE A CG  
1027 C CD1 . PHE A 138 ? 0.1869 0.1790 0.1948 0.0429  0.0111  0.0402  144 PHE A CD1 
1028 C CD2 . PHE A 138 ? 0.2273 0.2073 0.2296 0.0415  0.0132  0.0350  144 PHE A CD2 
1029 C CE1 . PHE A 138 ? 0.2366 0.2264 0.2434 0.0426  0.0101  0.0381  144 PHE A CE1 
1030 C CE2 . PHE A 138 ? 0.2283 0.2066 0.2298 0.0410  0.0121  0.0330  144 PHE A CE2 
1031 C CZ  . PHE A 138 ? 0.2389 0.2217 0.2425 0.0416  0.0107  0.0345  144 PHE A CZ  
1032 N N   . ILE A 139 ? 0.1164 0.1018 0.1201 0.0376  0.0122  0.0411  145 ILE A N   
1033 C CA  . ILE A 139 ? 0.1139 0.1014 0.1179 0.0359  0.0131  0.0414  145 ILE A CA  
1034 C C   . ILE A 139 ? 0.1159 0.0959 0.1165 0.0371  0.0162  0.0396  145 ILE A C   
1035 O O   . ILE A 139 ? 0.1303 0.1023 0.1273 0.0367  0.0159  0.0370  145 ILE A O   
1036 C CB  . ILE A 139 ? 0.1180 0.1064 0.1212 0.0309  0.0092  0.0404  145 ILE A CB  
1037 C CG1 . ILE A 139 ? 0.1257 0.1213 0.1322 0.0297  0.0060  0.0422  145 ILE A CG1 
1038 C CG2 . ILE A 139 ? 0.1252 0.1155 0.1286 0.0292  0.0104  0.0407  145 ILE A CG2 
1039 C CD1 . ILE A 139 ? 0.1437 0.1392 0.1490 0.0248  0.0018  0.0409  145 ILE A CD1 
1040 N N   . VAL A 140 ? 0.1074 0.0900 0.1092 0.0386  0.0193  0.0409  146 VAL A N   
1041 C CA  . VAL A 140 ? 0.1084 0.0844 0.1069 0.0395  0.0223  0.0392  146 VAL A CA  
1042 C C   . VAL A 140 ? 0.1089 0.0858 0.1067 0.0363  0.0218  0.0389  146 VAL A C   
1043 O O   . VAL A 140 ? 0.1148 0.0993 0.1159 0.0358  0.0219  0.0412  146 VAL A O   
1044 C CB  . VAL A 140 ? 0.1348 0.1120 0.1347 0.0442  0.0268  0.0410  146 VAL A CB  
1045 C CG1 . VAL A 140 ? 0.1260 0.0975 0.1228 0.0447  0.0298  0.0396  146 VAL A CG1 
1046 C CG2 . VAL A 140 ? 0.1596 0.1347 0.1591 0.0459  0.0271  0.0395  146 VAL A CG2 
1047 N N   . VAL A 141 ? 0.1105 0.0798 0.1040 0.0342  0.0213  0.0360  147 VAL A N   
1048 C CA  . VAL A 141 ? 0.1150 0.0835 0.1070 0.0317  0.0216  0.0354  147 VAL A CA  
1049 C C   . VAL A 141 ? 0.1202 0.0833 0.1097 0.0344  0.0257  0.0347  147 VAL A C   
1050 O O   . VAL A 141 ? 0.1664 0.1219 0.1527 0.0357  0.0266  0.0327  147 VAL A O   
1051 C CB  . VAL A 141 ? 0.1267 0.0902 0.1155 0.0274  0.0181  0.0326  147 VAL A CB  
1052 C CG1 . VAL A 141 ? 0.1399 0.1022 0.1268 0.0249  0.0185  0.0318  147 VAL A CG1 
1053 C CG2 . VAL A 141 ? 0.1064 0.0749 0.0974 0.0248  0.0140  0.0333  147 VAL A CG2 
1054 N N   . VAL A 142 ? 0.1198 0.0869 0.1106 0.0351  0.0281  0.0364  148 VAL A N   
1055 C CA  . VAL A 142 ? 0.1443 0.1070 0.1330 0.0377  0.0322  0.0360  148 VAL A CA  
1056 C C   . VAL A 142 ? 0.1744 0.1327 0.1596 0.0348  0.0319  0.0341  148 VAL A C   
1057 O O   . VAL A 142 ? 0.1584 0.1216 0.1451 0.0325  0.0311  0.0352  148 VAL A O   
1058 C CB  . VAL A 142 ? 0.1522 0.1218 0.1446 0.0410  0.0356  0.0392  148 VAL A CB  
1059 C CG1 . VAL A 142 ? 0.1692 0.1334 0.1589 0.0438  0.0399  0.0387  148 VAL A CG1 
1060 C CG2 . VAL A 142 ? 0.1698 0.1445 0.1660 0.0438  0.0358  0.0413  148 VAL A CG2 
1061 N N   . GLY A 143 ? 0.1702 0.1192 0.1508 0.0349  0.0325  0.0314  149 GLY A N   
1062 C CA  . GLY A 143 ? 0.1722 0.1160 0.1489 0.0326  0.0326  0.0294  149 GLY A CA  
1063 C C   . GLY A 143 ? 0.2012 0.1397 0.1750 0.0288  0.0288  0.0266  149 GLY A C   
1064 O O   . GLY A 143 ? 0.1998 0.1425 0.1755 0.0260  0.0255  0.0269  149 GLY A O   
1065 N N   . GLY A 144 ? 0.2096 0.1388 0.1788 0.0287  0.0292  0.0238  150 GLY A N   
1066 C CA  . GLY A 144 ? 0.1998 0.1253 0.1669 0.0250  0.0253  0.0204  150 GLY A CA  
1067 C C   . GLY A 144 ? 0.2227 0.1440 0.1862 0.0219  0.0245  0.0183  150 GLY A C   
1068 O O   . GLY A 144 ? 0.2462 0.1656 0.2082 0.0193  0.0221  0.0144  150 GLY A O   
1069 N N   . GLY A 145 ? 0.2040 0.1273 0.1675 0.0216  0.0259  0.0204  151 GLY A N   
1070 C CA  . GLY A 145 ? 0.2211 0.1416 0.1818 0.0182  0.0245  0.0188  151 GLY A CA  
1071 C C   . GLY A 145 ? 0.2214 0.1438 0.1828 0.0141  0.0201  0.0180  151 GLY A C   
1072 O O   . GLY A 145 ? 0.1853 0.1096 0.1487 0.0141  0.0181  0.0183  151 GLY A O   
1073 N N   . SER A 146 ? 0.2302 0.1519 0.1898 0.0107  0.0186  0.0171  152 SER A N   
1074 C CA  . SER A 146 ? 0.2235 0.1464 0.1834 0.0067  0.0143  0.0162  152 SER A CA  
1075 C C   . SER A 146 ? 0.2277 0.1603 0.1927 0.0063  0.0128  0.0189  152 SER A C   
1076 O O   . SER A 146 ? 0.2001 0.1336 0.1660 0.0044  0.0096  0.0184  152 SER A O   
1077 C CB  . SER A 146 ? 0.3039 0.2241 0.2608 0.0031  0.0131  0.0147  152 SER A CB  
1078 O OG  . SER A 146 ? 0.3528 0.2785 0.3114 0.0033  0.0150  0.0167  152 SER A OG  
1079 N N   . ALA A 147 ? 0.1846 0.1244 0.1531 0.0080  0.0150  0.0217  153 ALA A N   
1080 C CA  . ALA A 147 ? 0.1799 0.1289 0.1534 0.0077  0.0136  0.0243  153 ALA A CA  
1081 C C   . ALA A 147 ? 0.1732 0.1229 0.1485 0.0102  0.0133  0.0249  153 ALA A C   
1082 O O   . ALA A 147 ? 0.1533 0.1065 0.1307 0.0087  0.0103  0.0253  153 ALA A O   
1083 C CB  . ALA A 147 ? 0.1777 0.1342 0.1547 0.0093  0.0162  0.0272  153 ALA A CB  
1084 N N   . GLY A 148 ? 0.1545 0.1009 0.1291 0.0141  0.0165  0.0249  154 GLY A N   
1085 C CA  . GLY A 148 ? 0.1628 0.1103 0.1393 0.0168  0.0166  0.0257  154 GLY A CA  
1086 C C   . GLY A 148 ? 0.1477 0.0898 0.1221 0.0152  0.0135  0.0233  154 GLY A C   
1087 O O   . GLY A 148 ? 0.1291 0.0743 0.1058 0.0156  0.0119  0.0242  154 GLY A O   
1088 N N   . VAL A 149 ? 0.1530 0.0867 0.1229 0.0135  0.0128  0.0204  155 VAL A N   
1089 C CA  . VAL A 149 ? 0.1499 0.0784 0.1179 0.0118  0.0099  0.0182  155 VAL A CA  
1090 C C   . VAL A 149 ? 0.1605 0.0934 0.1300 0.0081  0.0059  0.0185  155 VAL A C   
1091 O O   . VAL A 149 ? 0.1521 0.0850 0.1223 0.0076  0.0036  0.0182  155 VAL A O   
1092 C CB  . VAL A 149 ? 0.1776 0.1009 0.1429 0.0101  0.0093  0.0141  155 VAL A CB  
1093 C CG1 . VAL A 149 ? 0.1788 0.1016 0.1442 0.0131  0.0125  0.0133  155 VAL A CG1 
1094 C CG2 . VAL A 149 ? 0.1913 0.1126 0.1540 0.0068  0.0083  0.0133  155 VAL A CG2 
1095 N N   . GLU A 150 ? 0.1407 0.0776 0.1108 0.0054  0.0051  0.0191  156 GLU A N   
1096 C CA  . GLU A 150 ? 0.1628 0.1047 0.1347 0.0019  0.0014  0.0196  156 GLU A CA  
1097 C C   . GLU A 150 ? 0.1737 0.1238 0.1502 0.0035  0.0010  0.0224  156 GLU A C   
1098 O O   . GLU A 150 ? 0.1436 0.0953 0.1211 0.0020  -0.0021 0.0224  156 GLU A O   
1099 C CB  . GLU A 150 ? 0.1779 0.1225 0.1496 -0.0011 0.0008  0.0198  156 GLU A CB  
1100 C CG  . GLU A 150 ? 0.2326 0.1690 0.1994 -0.0036 0.0001  0.0168  156 GLU A CG  
1101 C CD  . GLU A 150 ? 0.3164 0.2555 0.2830 -0.0070 -0.0010 0.0169  156 GLU A CD  
1102 O OE1 . GLU A 150 ? 0.3275 0.2744 0.2975 -0.0068 -0.0002 0.0194  156 GLU A OE1 
1103 O OE2 . GLU A 150 ? 0.2493 0.1828 0.2123 -0.0099 -0.0027 0.0145  156 GLU A OE2 
1104 N N   . MET A 151 ? 0.1187 0.0739 0.0981 0.0067  0.0040  0.0249  157 MET A N   
1105 C CA  . MET A 151 ? 0.1369 0.1002 0.1210 0.0084  0.0038  0.0276  157 MET A CA  
1106 C C   . MET A 151 ? 0.1280 0.0887 0.1120 0.0102  0.0030  0.0272  157 MET A C   
1107 O O   . MET A 151 ? 0.1380 0.1027 0.1240 0.0093  0.0004  0.0280  157 MET A O   
1108 C CB  . MET A 151 ? 0.1392 0.1074 0.1261 0.0119  0.0076  0.0301  157 MET A CB  
1109 C CG  . MET A 151 ? 0.1210 0.0980 0.1129 0.0137  0.0075  0.0332  157 MET A CG  
1110 S SD  . MET A 151 ? 0.1946 0.1812 0.1904 0.0102  0.0046  0.0352  157 MET A SD  
1111 C CE  . MET A 151 ? 0.1585 0.1451 0.1542 0.0079  0.0000  0.0344  157 MET A CE  
1112 N N   . ALA A 152 ? 0.1492 0.1032 0.1307 0.0129  0.0054  0.0258  158 ALA A N   
1113 C CA  . ALA A 152 ? 0.1353 0.0863 0.1166 0.0148  0.0049  0.0253  158 ALA A CA  
1114 C C   . ALA A 152 ? 0.1583 0.1058 0.1377 0.0115  0.0009  0.0233  158 ALA A C   
1115 O O   . ALA A 152 ? 0.1446 0.0939 0.1254 0.0118  -0.0009 0.0239  158 ALA A O   
1116 C CB  . ALA A 152 ? 0.1367 0.0803 0.1153 0.0179  0.0080  0.0239  158 ALA A CB  
1117 N N   . ALA A 153 ? 0.1387 0.0813 0.1149 0.0082  -0.0006 0.0211  159 ALA A N   
1118 C CA  . ALA A 153 ? 0.1712 0.1102 0.1455 0.0050  -0.0043 0.0192  159 ALA A CA  
1119 C C   . ALA A 153 ? 0.1314 0.0778 0.1084 0.0025  -0.0074 0.0207  159 ALA A C   
1120 O O   . ALA A 153 ? 0.1533 0.0990 0.1302 0.0013  -0.0101 0.0202  159 ALA A O   
1121 C CB  . ALA A 153 ? 0.2078 0.1405 0.1783 0.0020  -0.0050 0.0164  159 ALA A CB  
1122 N N   . GLU A 154 ? 0.1251 0.0784 0.1045 0.0015  -0.0072 0.0225  160 GLU A N   
1123 C CA  . GLU A 154 ? 0.1123 0.0728 0.0945 -0.0009 -0.0102 0.0241  160 GLU A CA  
1124 C C   . GLU A 154 ? 0.1260 0.0911 0.1113 0.0015  -0.0106 0.0260  160 GLU A C   
1125 O O   . GLU A 154 ? 0.1284 0.0951 0.1142 -0.0004 -0.0138 0.0260  160 GLU A O   
1126 C CB  . GLU A 154 ? 0.1419 0.1093 0.1266 -0.0020 -0.0095 0.0259  160 GLU A CB  
1127 C CG  . GLU A 154 ? 0.1679 0.1322 0.1499 -0.0053 -0.0100 0.0243  160 GLU A CG  
1128 C CD  . GLU A 154 ? 0.2188 0.1827 0.1996 -0.0098 -0.0142 0.0230  160 GLU A CD  
1129 O OE1 . GLU A 154 ? 0.1890 0.1578 0.1723 -0.0107 -0.0168 0.0242  160 GLU A OE1 
1130 O OE2 . GLU A 154 ? 0.2163 0.1751 0.1938 -0.0124 -0.0149 0.0209  160 GLU A OE2 
1131 N N   . ILE A 155 ? 0.1045 0.0716 0.0917 0.0056  -0.0074 0.0276  161 ILE A N   
1132 C CA  . ILE A 155 ? 0.1192 0.0908 0.1094 0.0081  -0.0076 0.0296  161 ILE A CA  
1133 C C   . ILE A 155 ? 0.1167 0.0824 0.1046 0.0083  -0.0093 0.0279  161 ILE A C   
1134 O O   . ILE A 155 ? 0.1130 0.0818 0.1023 0.0075  -0.0119 0.0286  161 ILE A O   
1135 C CB  . ILE A 155 ? 0.1104 0.0844 0.1026 0.0127  -0.0035 0.0314  161 ILE A CB  
1136 C CG1 . ILE A 155 ? 0.1029 0.0834 0.0978 0.0125  -0.0019 0.0334  161 ILE A CG1 
1137 C CG2 . ILE A 155 ? 0.1156 0.0936 0.1106 0.0155  -0.0037 0.0333  161 ILE A CG2 
1138 C CD1 . ILE A 155 ? 0.1199 0.1014 0.1161 0.0168  0.0026  0.0349  161 ILE A CD1 
1139 N N   . LYS A 156 ? 0.1088 0.0661 0.0933 0.0092  -0.0078 0.0256  162 LYS A N   
1140 C CA  . LYS A 156 ? 0.1433 0.0950 0.1260 0.0097  -0.0091 0.0241  162 LYS A CA  
1141 C C   . LYS A 156 ? 0.1520 0.1014 0.1328 0.0055  -0.0131 0.0225  162 LYS A C   
1142 O O   . LYS A 156 ? 0.1549 0.1044 0.1361 0.0054  -0.0141 0.0213  162 LYS A O   
1143 C CB  . LYS A 156 ? 0.1786 0.1226 0.1589 0.0117  -0.0064 0.0219  162 LYS A CB  
1144 C CG  . LYS A 156 ? 0.2394 0.1851 0.2220 0.0159  -0.0033 0.0228  162 LYS A CG  
1145 C CD  . LYS A 156 ? 0.2005 0.1495 0.1856 0.0171  -0.0045 0.0235  162 LYS A CD  
1146 C CE  . LYS A 156 ? 0.2205 0.1686 0.2074 0.0162  -0.0042 0.0200  162 LYS A CE  
1147 N NZ  . LYS A 156 ? 0.1957 0.1466 0.1847 0.0180  -0.0046 0.0209  162 LYS A NZ  
1148 N N   . THR A 157 ? 0.1418 0.0913 0.1214 0.0019  -0.0145 0.0216  163 THR A N   
1149 C CA  . THR A 157 ? 0.1350 0.0837 0.1133 -0.0022 -0.0181 0.0199  163 THR A CA  
1150 C C   . THR A 157 ? 0.1551 0.1107 0.1361 -0.0035 -0.0211 0.0223  163 THR A C   
1151 O O   . THR A 157 ? 0.1415 0.0972 0.1222 -0.0050 -0.0234 0.0209  163 THR A O   
1152 C CB  . THR A 157 ? 0.1495 0.0964 0.1259 -0.0055 -0.0186 0.0182  163 THR A CB  
1153 O OG1 . THR A 157 ? 0.1509 0.0939 0.1259 -0.0041 -0.0154 0.0154  163 THR A OG1 
1154 C CG2 . THR A 157 ? 0.1604 0.1089 0.1363 -0.0093 -0.0216 0.0154  163 THR A CG2 
1155 N N   . GLU A 158 ? 0.1170 0.0806 0.1014 -0.0028 -0.0203 0.0247  164 GLU A N   
1156 C CA  . GLU A 158 ? 0.1414 0.1127 0.1289 -0.0039 -0.0228 0.0268  164 GLU A CA  
1157 C C   . GLU A 158 ? 0.1577 0.1311 0.1470 -0.0006 -0.0225 0.0283  164 GLU A C   
1158 O O   . GLU A 158 ? 0.1423 0.1190 0.1327 -0.0017 -0.0254 0.0291  164 GLU A O   
1159 C CB  . GLU A 158 ? 0.1337 0.1130 0.1245 -0.0043 -0.0220 0.0290  164 GLU A CB  
1160 C CG  . GLU A 158 ? 0.1650 0.1431 0.1542 -0.0078 -0.0226 0.0277  164 GLU A CG  
1161 C CD  . GLU A 158 ? 0.2374 0.2135 0.2245 -0.0122 -0.0267 0.0262  164 GLU A CD  
1162 O OE1 . GLU A 158 ? 0.2493 0.2314 0.2388 -0.0137 -0.0293 0.0276  164 GLU A OE1 
1163 O OE2 . GLU A 158 ? 0.2102 0.1787 0.1935 -0.0139 -0.0273 0.0235  164 GLU A OE2 
1164 N N   . TYR A 159 ? 0.1150 0.0827 0.1391 0.0210  -0.0169 0.0186  165 TYR A N   
1165 C CA  . TYR A 159 ? 0.1189 0.0856 0.1430 0.0244  -0.0143 0.0198  165 TYR A CA  
1166 C C   . TYR A 159 ? 0.1239 0.0848 0.1487 0.0231  -0.0140 0.0209  165 TYR A C   
1167 O O   . TYR A 159 ? 0.1226 0.0787 0.1445 0.0237  -0.0127 0.0204  165 TYR A O   
1168 C CB  . TYR A 159 ? 0.1329 0.0987 0.1529 0.0274  -0.0124 0.0186  165 TYR A CB  
1169 C CG  . TYR A 159 ? 0.1388 0.1099 0.1577 0.0287  -0.0128 0.0173  165 TYR A CG  
1170 C CD1 . TYR A 159 ? 0.1617 0.1383 0.1823 0.0316  -0.0119 0.0180  165 TYR A CD1 
1171 C CD2 . TYR A 159 ? 0.1294 0.0998 0.1453 0.0269  -0.0140 0.0153  165 TYR A CD2 
1172 C CE1 . TYR A 159 ? 0.1491 0.1304 0.1687 0.0327  -0.0122 0.0168  165 TYR A CE1 
1173 C CE2 . TYR A 159 ? 0.1577 0.1330 0.1726 0.0280  -0.0144 0.0141  165 TYR A CE2 
1174 C CZ  . TYR A 159 ? 0.2001 0.1808 0.2169 0.0309  -0.0135 0.0149  165 TYR A CZ  
1175 O OH  . TYR A 159 ? 0.1841 0.1696 0.1999 0.0320  -0.0138 0.0137  165 TYR A OH  
1176 N N   . PRO A 160 ? 0.1177 0.0791 0.1465 0.0212  -0.0150 0.0224  166 PRO A N   
1177 C CA  . PRO A 160 ? 0.1721 0.1279 0.2016 0.0196  -0.0148 0.0234  166 PRO A CA  
1178 C C   . PRO A 160 ? 0.1634 0.1166 0.1920 0.0228  -0.0121 0.0244  166 PRO A C   
1179 O O   . PRO A 160 ? 0.1425 0.0901 0.1703 0.0219  -0.0115 0.0247  166 PRO A O   
1180 C CB  . PRO A 160 ? 0.1855 0.1437 0.2198 0.0176  -0.0163 0.0250  166 PRO A CB  
1181 C CG  . PRO A 160 ? 0.1954 0.1605 0.2316 0.0190  -0.0168 0.0251  166 PRO A CG  
1182 C CD  . PRO A 160 ? 0.1391 0.1058 0.1717 0.0200  -0.0168 0.0231  166 PRO A CD  
1183 N N   . GLU A 161 ? 0.1256 0.0825 0.1542 0.0266  -0.0104 0.0249  167 GLU A N   
1184 C CA  . GLU A 161 ? 0.1834 0.1382 0.2113 0.0298  -0.0078 0.0259  167 GLU A CA  
1185 C C   . GLU A 161 ? 0.2046 0.1553 0.2277 0.0313  -0.0063 0.0245  167 GLU A C   
1186 O O   . GLU A 161 ? 0.1856 0.1336 0.2078 0.0337  -0.0041 0.0252  167 GLU A O   
1187 C CB  . GLU A 161 ? 0.2118 0.1727 0.2404 0.0328  -0.0066 0.0262  167 GLU A CB  
1188 C CG  . GLU A 161 ? 0.2131 0.1776 0.2396 0.0353  -0.0060 0.0250  167 GLU A CG  
1189 C CD  . GLU A 161 ? 0.2186 0.1875 0.2467 0.0339  -0.0082 0.0245  167 GLU A CD  
1190 O OE1 . GLU A 161 ? 0.1566 0.1254 0.1869 0.0305  -0.0103 0.0246  167 GLU A OE1 
1191 O OE2 . GLU A 161 ? 0.1417 0.1147 0.1682 0.0360  -0.0077 0.0234  167 GLU A OE2 
1192 N N   . LYS A 162 ? 0.1451 0.0954 0.1653 0.0299  -0.0073 0.0225  168 LYS A N   
1193 C CA  . LYS A 162 ? 0.1666 0.1131 0.1823 0.0311  -0.0059 0.0211  168 LYS A CA  
1194 C C   . LYS A 162 ? 0.2272 0.1668 0.2415 0.0285  -0.0063 0.0208  168 LYS A C   
1195 O O   . LYS A 162 ? 0.1861 0.1243 0.2025 0.0251  -0.0081 0.0212  168 LYS A O   
1196 C CB  . LYS A 162 ? 0.1687 0.1178 0.1816 0.0310  -0.0068 0.0190  168 LYS A CB  
1197 C CG  . LYS A 162 ? 0.1508 0.1063 0.1643 0.0342  -0.0061 0.0191  168 LYS A CG  
1198 C CD  . LYS A 162 ? 0.1745 0.1324 0.1852 0.0340  -0.0069 0.0170  168 LYS A CD  
1199 C CE  . LYS A 162 ? 0.1397 0.1043 0.1517 0.0367  -0.0065 0.0172  168 LYS A CE  
1200 N NZ  . LYS A 162 ? 0.1735 0.1384 0.1844 0.0410  -0.0037 0.0179  168 LYS A NZ  
1201 N N   . GLU A 163 ? 0.1783 0.1136 0.1891 0.0300  -0.0045 0.0202  169 GLU A N   
1202 C CA  . GLU A 163 ? 0.2283 0.1570 0.2374 0.0279  -0.0045 0.0198  169 GLU A CA  
1203 C C   . GLU A 163 ? 0.2343 0.1613 0.2395 0.0263  -0.0055 0.0175  169 GLU A C   
1204 O O   . GLU A 163 ? 0.1926 0.1203 0.1947 0.0287  -0.0043 0.0164  169 GLU A O   
1205 C CB  . GLU A 163 ? 0.2524 0.1771 0.2601 0.0306  -0.0018 0.0206  169 GLU A CB  
1206 C CG  . GLU A 163 ? 0.3681 0.2940 0.3794 0.0323  -0.0008 0.0229  169 GLU A CG  
1207 C CD  . GLU A 163 ? 0.6936 0.6174 0.7082 0.0289  -0.0023 0.0240  169 GLU A CD  
1208 O OE1 . GLU A 163 ? 0.8827 0.8019 0.8959 0.0259  -0.0033 0.0232  169 GLU A OE1 
1209 O OE2 . GLU A 163 ? 0.8450 0.7718 0.8634 0.0293  -0.0024 0.0257  169 GLU A OE2 
1210 N N   . VAL A 164 ? 0.1799 0.1048 0.1854 0.0223  -0.0076 0.0168  170 VAL A N   
1211 C CA  . VAL A 164 ? 0.1706 0.0944 0.1728 0.0204  -0.0089 0.0146  170 VAL A CA  
1212 C C   . VAL A 164 ? 0.2094 0.1263 0.2097 0.0179  -0.0091 0.0141  170 VAL A C   
1213 O O   . VAL A 164 ? 0.1692 0.0838 0.1718 0.0154  -0.0101 0.0150  170 VAL A O   
1214 C CB  . VAL A 164 ? 0.1860 0.1140 0.1900 0.0178  -0.0115 0.0141  170 VAL A CB  
1215 C CG1 . VAL A 164 ? 0.1890 0.1156 0.1894 0.0159  -0.0127 0.0118  170 VAL A CG1 
1216 C CG2 . VAL A 164 ? 0.1623 0.0973 0.1684 0.0203  -0.0113 0.0147  170 VAL A CG2 
1217 N N   . THR A 165 ? 0.1586 0.0725 0.1546 0.0186  -0.0082 0.0125  171 THR A N   
1218 C CA  . THR A 165 ? 0.1796 0.0870 0.1733 0.0163  -0.0084 0.0116  171 THR A CA  
1219 C C   . THR A 165 ? 0.1847 0.0921 0.1753 0.0144  -0.0099 0.0094  171 THR A C   
1220 O O   . THR A 165 ? 0.1692 0.0793 0.1575 0.0164  -0.0094 0.0083  171 THR A O   
1221 C CB  . THR A 165 ? 0.2113 0.1143 0.2024 0.0190  -0.0057 0.0118  171 THR A CB  
1222 O OG1 . THR A 165 ? 0.2295 0.1324 0.2235 0.0207  -0.0044 0.0139  171 THR A OG1 
1223 C CG2 . THR A 165 ? 0.2131 0.1094 0.2015 0.0165  -0.0060 0.0108  171 THR A CG2 
1224 N N   . LEU A 166 ? 0.1599 0.0643 0.1506 0.0104  -0.0119 0.0088  172 LEU A N   
1225 C CA  . LEU A 166 ? 0.1780 0.0815 0.1657 0.0082  -0.0134 0.0067  172 LEU A CA  
1226 C C   . LEU A 166 ? 0.2002 0.0968 0.1848 0.0071  -0.0127 0.0058  172 LEU A C   
1227 O O   . LEU A 166 ? 0.1950 0.0876 0.1809 0.0052  -0.0129 0.0067  172 LEU A O   
1228 C CB  . LEU A 166 ? 0.1689 0.0746 0.1592 0.0044  -0.0163 0.0066  172 LEU A CB  
1229 C CG  . LEU A 166 ? 0.1771 0.0814 0.1647 0.0014  -0.0181 0.0046  172 LEU A CG  
1230 C CD1 . LEU A 166 ? 0.2005 0.1086 0.1856 0.0033  -0.0179 0.0032  172 LEU A CD1 
1231 C CD2 . LEU A 166 ? 0.2089 0.1149 0.1995 -0.0023 -0.0209 0.0049  172 LEU A CD2 
1232 N N   . ILE A 167 ? 0.1762 0.0713 0.1565 0.0084  -0.0118 0.0042  173 ILE A N   
1233 C CA  . ILE A 167 ? 0.1940 0.0827 0.1710 0.0076  -0.0109 0.0032  173 ILE A CA  
1234 C C   . ILE A 167 ? 0.2139 0.1015 0.1884 0.0045  -0.0129 0.0011  173 ILE A C   
1235 O O   . ILE A 167 ? 0.1865 0.0774 0.1593 0.0052  -0.0134 -0.0002 173 ILE A O   
1236 C CB  . ILE A 167 ? 0.2100 0.0972 0.1839 0.0115  -0.0082 0.0029  173 ILE A CB  
1237 C CG1 . ILE A 167 ? 0.1860 0.0752 0.1624 0.0147  -0.0063 0.0049  173 ILE A CG1 
1238 C CG2 . ILE A 167 ? 0.2200 0.1001 0.1907 0.0105  -0.0073 0.0020  173 ILE A CG2 
1239 C CD1 . ILE A 167 ? 0.2424 0.1309 0.2161 0.0189  -0.0035 0.0047  173 ILE A CD1 
1240 N N   . HIS A 168 ? 0.2388 0.1218 0.2131 0.0012  -0.0140 0.0008  174 HIS A N   
1241 C CA  . HIS A 168 ? 0.2264 0.1083 0.1989 -0.0022 -0.0162 -0.0009 174 HIS A CA  
1242 C C   . HIS A 168 ? 0.2634 0.1384 0.2328 -0.0037 -0.0157 -0.0019 174 HIS A C   
1243 O O   . HIS A 168 ? 0.2638 0.1348 0.2343 -0.0041 -0.0149 -0.0008 174 HIS A O   
1244 C CB  . HIS A 168 ? 0.2223 0.1062 0.1983 -0.0056 -0.0188 -0.0002 174 HIS A CB  
1245 C CG  . HIS A 168 ? 0.2547 0.1380 0.2291 -0.0091 -0.0211 -0.0020 174 HIS A CG  
1246 N ND1 . HIS A 168 ? 0.2312 0.1163 0.2025 -0.0086 -0.0214 -0.0038 174 HIS A ND1 
1247 C CD2 . HIS A 168 ? 0.2664 0.1476 0.2419 -0.0131 -0.0232 -0.0021 174 HIS A CD2 
1248 C CE1 . HIS A 168 ? 0.2675 0.1517 0.2380 -0.0121 -0.0236 -0.0050 174 HIS A CE1 
1249 N NE2 . HIS A 168 ? 0.2776 0.1594 0.2506 -0.0149 -0.0248 -0.0040 174 HIS A NE2 
1250 N N   . SER A 169 ? 0.2776 0.1512 0.2433 -0.0046 -0.0162 -0.0039 175 SER A N   
1251 C CA  . SER A 169 ? 0.2896 0.1567 0.2520 -0.0057 -0.0156 -0.0050 175 SER A CA  
1252 C C   . SER A 169 ? 0.2990 0.1625 0.2623 -0.0101 -0.0176 -0.0052 175 SER A C   
1253 O O   . SER A 169 ? 0.3213 0.1791 0.2824 -0.0112 -0.0170 -0.0058 175 SER A O   
1254 C CB  . SER A 169 ? 0.3152 0.1819 0.2730 -0.0050 -0.0153 -0.0072 175 SER A CB  
1255 O OG  . SER A 169 ? 0.3455 0.2159 0.3034 -0.0070 -0.0176 -0.0083 175 SER A OG  
1256 N N   . GLN A 170 ? 0.3219 0.1885 0.2883 -0.0126 -0.0199 -0.0047 176 GLN A N   
1257 C CA  . GLN A 170 ? 0.3341 0.1976 0.3012 -0.0169 -0.0220 -0.0050 176 GLN A CA  
1258 C C   . GLN A 170 ? 0.3340 0.1971 0.3054 -0.0178 -0.0222 -0.0029 176 GLN A C   
1259 O O   . GLN A 170 ? 0.3120 0.1778 0.2859 -0.0152 -0.0210 -0.0013 176 GLN A O   
1260 C CB  . GLN A 170 ? 0.3468 0.2136 0.3139 -0.0195 -0.0246 -0.0061 176 GLN A CB  
1261 C CG  . GLN A 170 ? 0.3661 0.2345 0.3295 -0.0183 -0.0244 -0.0081 176 GLN A CG  
1262 C CD  . GLN A 170 ? 0.4892 0.3518 0.4481 -0.0186 -0.0235 -0.0096 176 GLN A CD  
1263 O OE1 . GLN A 170 ? 0.5209 0.3794 0.4799 -0.0208 -0.0236 -0.0096 176 GLN A OE1 
1264 N NE2 . GLN A 170 ? 0.6960 0.5593 0.6514 -0.0163 -0.0223 -0.0110 176 GLN A NE2 
1265 N N   . VAL A 171 ? 0.3470 0.2109 0.3206 -0.0208 -0.0228 -0.0030 177 VAL A N   
1266 C CA  . VAL A 171 ? 0.3678 0.2335 0.3460 -0.0216 -0.0224 -0.0011 177 VAL A CA  
1267 C C   . VAL A 171 ? 0.3369 0.2085 0.3188 -0.0224 -0.0241 -0.0002 177 VAL A C   
1268 O O   . VAL A 171 ? 0.3744 0.2476 0.3596 -0.0215 -0.0237 0.0016  177 VAL A O   
1269 C CB  . VAL A 171 ? 0.4119 0.2767 0.3910 -0.0242 -0.0222 -0.0016 177 VAL A CB  
1270 C CG1 . VAL A 171 ? 0.4378 0.3031 0.4208 -0.0244 -0.0212 0.0002  177 VAL A CG1 
1271 C CG2 . VAL A 171 ? 0.4144 0.2739 0.3895 -0.0238 -0.0209 -0.0030 177 VAL A CG2 
1272 N N   . ALA A 172 ? 0.3387 0.2136 0.3200 -0.0241 -0.0260 -0.0013 178 ALA A N   
1273 C CA  . ALA A 172 ? 0.3430 0.2238 0.3277 -0.0250 -0.0277 -0.0006 178 ALA A CA  
1274 C C   . ALA A 172 ? 0.3338 0.2163 0.3170 -0.0235 -0.0287 -0.0011 178 ALA A C   
1275 O O   . ALA A 172 ? 0.3098 0.1894 0.2888 -0.0226 -0.0286 -0.0026 178 ALA A O   
1276 C CB  . ALA A 172 ? 0.3117 0.1960 0.2977 -0.0282 -0.0290 -0.0013 178 ALA A CB  
1277 N N   . LEU A 173 ? 0.3354 0.2225 0.3219 -0.0234 -0.0298 0.0000  179 LEU A N   
1278 C CA  . LEU A 173 ? 0.2828 0.1728 0.2688 -0.0215 -0.0305 -0.0002 179 LEU A CA  
1279 C C   . LEU A 173 ? 0.3292 0.2226 0.3147 -0.0238 -0.0328 -0.0015 179 LEU A C   
1280 O O   . LEU A 173 ? 0.3279 0.2244 0.3150 -0.0264 -0.0335 -0.0017 179 LEU A O   
1281 C CB  . LEU A 173 ? 0.2646 0.1589 0.2549 -0.0197 -0.0300 0.0019  179 LEU A CB  
1282 C CG  . LEU A 173 ? 0.2847 0.1768 0.2755 -0.0168 -0.0274 0.0033  179 LEU A CG  
1283 C CD1 . LEU A 173 ? 0.2609 0.1568 0.2564 -0.0159 -0.0274 0.0054  179 LEU A CD1 
1284 C CD2 . LEU A 173 ? 0.2685 0.1612 0.2561 -0.0130 -0.0251 0.0025  179 LEU A CD2 
1285 N N   . ALA A 174 ? 0.3181 0.2151 0.3019 -0.0218 -0.0324 -0.0024 180 ALA A N   
1286 C CA  . ALA A 174 ? 0.3282 0.2288 0.3114 -0.0234 -0.0345 -0.0036 180 ALA A CA  
1287 C C   . ALA A 174 ? 0.3954 0.2934 0.3759 -0.0263 -0.0355 -0.0054 180 ALA A C   
1288 O O   . ALA A 174 ? 0.3943 0.2881 0.3730 -0.0266 -0.0343 -0.0057 180 ALA A O   
1289 C CB  . ALA A 174 ? 0.3128 0.2179 0.3006 -0.0249 -0.0363 -0.0023 180 ALA A CB  
1290 N N   . ASP A 175 ? 0.4028 0.3056 0.3834 -0.0277 -0.0369 -0.0063 181 ASP A N   
1291 C CA  . ASP A 175 ? 0.4362 0.3388 0.4139 -0.0292 -0.0370 -0.0080 181 ASP A CA  
1292 C C   . ASP A 175 ? 0.4277 0.3297 0.4066 -0.0312 -0.0365 -0.0077 181 ASP A C   
1293 O O   . ASP A 175 ? 0.3840 0.2888 0.3665 -0.0322 -0.0367 -0.0064 181 ASP A O   
1294 C CB  . ASP A 175 ? 0.4927 0.4012 0.4709 -0.0300 -0.0383 -0.0087 181 ASP A CB  
1295 C CG  . ASP A 175 ? 0.5658 0.4743 0.5413 -0.0283 -0.0388 -0.0098 181 ASP A CG  
1296 O OD1 . ASP A 175 ? 1.0337 0.9427 1.0105 -0.0264 -0.0388 -0.0090 181 ASP A OD1 
1297 O OD2 . ASP A 175 ? 0.5677 0.4765 0.5401 -0.0285 -0.0389 -0.0115 181 ASP A OD2 
1298 N N   . LYS A 176 ? 0.4264 0.3246 0.4019 -0.0317 -0.0358 -0.0091 182 LYS A N   
1299 C CA  . LYS A 176 ? 0.4573 0.3548 0.4337 -0.0335 -0.0353 -0.0091 182 LYS A CA  
1300 C C   . LYS A 176 ? 0.4707 0.3737 0.4493 -0.0354 -0.0363 -0.0090 182 LYS A C   
1301 O O   . LYS A 176 ? 0.4726 0.3763 0.4532 -0.0367 -0.0361 -0.0085 182 LYS A O   
1302 C CB  . LYS A 176 ? 0.4882 0.3809 0.4606 -0.0336 -0.0345 -0.0106 182 LYS A CB  
1303 N N   . GLU A 177 ? 0.4884 0.3955 0.4665 -0.0352 -0.0373 -0.0096 183 GLU A N   
1304 C CA  . GLU A 177 ? 0.5120 0.4243 0.4921 -0.0366 -0.0380 -0.0096 183 GLU A CA  
1305 C C   . GLU A 177 ? 0.4407 0.3569 0.4249 -0.0369 -0.0383 -0.0079 183 GLU A C   
1306 O O   . GLU A 177 ? 0.4063 0.3260 0.3922 -0.0379 -0.0386 -0.0076 183 GLU A O   
1307 C CB  . GLU A 177 ? 0.5366 0.4524 0.5152 -0.0362 -0.0387 -0.0105 183 GLU A CB  
1308 C CG  . GLU A 177 ? 0.6454 0.5585 0.6199 -0.0362 -0.0384 -0.0124 183 GLU A CG  
1309 C CD  . GLU A 177 ? 0.7439 0.6527 0.7153 -0.0345 -0.0380 -0.0130 183 GLU A CD  
1310 O OE1 . GLU A 177 ? 0.7426 0.6497 0.7151 -0.0334 -0.0379 -0.0120 183 GLU A OE1 
1311 O OE2 . GLU A 177 ? 0.8507 0.7579 0.8185 -0.0341 -0.0378 -0.0146 183 GLU A OE2 
1312 N N   . LEU A 178 ? 0.3785 0.2940 0.3643 -0.0357 -0.0383 -0.0067 184 LEU A N   
1313 C CA  . LEU A 178 ? 0.3383 0.2577 0.3280 -0.0358 -0.0386 -0.0051 184 LEU A CA  
1314 C C   . LEU A 178 ? 0.3327 0.2512 0.3242 -0.0370 -0.0380 -0.0044 184 LEU A C   
1315 O O   . LEU A 178 ? 0.3289 0.2429 0.3191 -0.0374 -0.0372 -0.0048 184 LEU A O   
1316 C CB  . LEU A 178 ? 0.3326 0.2512 0.3237 -0.0342 -0.0386 -0.0039 184 LEU A CB  
1317 C CG  . LEU A 178 ? 0.3084 0.2283 0.2983 -0.0328 -0.0393 -0.0044 184 LEU A CG  
1318 C CD1 . LEU A 178 ? 0.2939 0.2113 0.2846 -0.0309 -0.0390 -0.0034 184 LEU A CD1 
1319 C CD2 . LEU A 178 ? 0.3187 0.2450 0.3105 -0.0330 -0.0402 -0.0041 184 LEU A CD2 
1320 N N   . LEU A 179 ? 0.2957 0.2185 0.2902 -0.0375 -0.0384 -0.0034 185 LEU A N   
1321 C CA  . LEU A 179 ? 0.2999 0.2224 0.2966 -0.0383 -0.0379 -0.0026 185 LEU A CA  
1322 C C   . LEU A 179 ? 0.3206 0.2389 0.3178 -0.0376 -0.0370 -0.0017 185 LEU A C   
1323 O O   . LEU A 179 ? 0.3021 0.2202 0.3000 -0.0362 -0.0370 -0.0010 185 LEU A O   
1324 C CB  . LEU A 179 ? 0.2900 0.2176 0.2898 -0.0383 -0.0384 -0.0014 185 LEU A CB  
1325 C CG  . LEU A 179 ? 0.3533 0.2854 0.3532 -0.0389 -0.0389 -0.0018 185 LEU A CG  
1326 C CD1 . LEU A 179 ? 0.3283 0.2651 0.3311 -0.0383 -0.0393 -0.0005 185 LEU A CD1 
1327 C CD2 . LEU A 179 ? 0.3685 0.2997 0.3678 -0.0403 -0.0386 -0.0026 185 LEU A CD2 
1328 N N   . PRO A 180 ? 0.3230 0.2380 0.3201 -0.0384 -0.0361 -0.0019 186 PRO A N   
1329 C CA  . PRO A 180 ? 0.3059 0.2172 0.3039 -0.0377 -0.0350 -0.0009 186 PRO A CA  
1330 C C   . PRO A 180 ? 0.3120 0.2261 0.3133 -0.0368 -0.0351 0.0008  186 PRO A C   
1331 O O   . PRO A 180 ? 0.3249 0.2368 0.3268 -0.0354 -0.0344 0.0017  186 PRO A O   
1332 C CB  . PRO A 180 ? 0.3388 0.2476 0.3366 -0.0390 -0.0342 -0.0013 186 PRO A CB  
1333 C CG  . PRO A 180 ? 0.2879 0.1967 0.2833 -0.0401 -0.0347 -0.0029 186 PRO A CG  
1334 C CD  . PRO A 180 ? 0.2935 0.2075 0.2893 -0.0400 -0.0359 -0.0030 186 PRO A CD  
1335 N N   . SER A 181 ? 0.2715 0.1904 0.2751 -0.0374 -0.0359 0.0014  187 SER A N   
1336 C CA  . SER A 181 ? 0.2679 0.1899 0.2747 -0.0366 -0.0360 0.0030  187 SER A CA  
1337 C C   . SER A 181 ? 0.2851 0.2082 0.2921 -0.0350 -0.0365 0.0035  187 SER A C   
1338 O O   . SER A 181 ? 0.2784 0.2015 0.2874 -0.0338 -0.0362 0.0048  187 SER A O   
1339 C CB  . SER A 181 ? 0.2845 0.2115 0.2931 -0.0374 -0.0368 0.0033  187 SER A CB  
1340 O OG  . SER A 181 ? 0.2947 0.2247 0.3021 -0.0375 -0.0377 0.0025  187 SER A OG  
1341 N N   . VAL A 182 ? 0.2940 0.2182 0.2990 -0.0349 -0.0373 0.0024  188 VAL A N   
1342 C CA  . VAL A 182 ? 0.2693 0.1944 0.2743 -0.0333 -0.0379 0.0027  188 VAL A CA  
1343 C C   . VAL A 182 ? 0.2618 0.1816 0.2654 -0.0320 -0.0369 0.0028  188 VAL A C   
1344 O O   . VAL A 182 ? 0.2247 0.1446 0.2300 -0.0304 -0.0367 0.0039  188 VAL A O   
1345 C CB  . VAL A 182 ? 0.2710 0.1983 0.2738 -0.0336 -0.0388 0.0013  188 VAL A CB  
1346 C CG1 . VAL A 182 ? 0.2467 0.1738 0.2488 -0.0320 -0.0393 0.0012  188 VAL A CG1 
1347 C CG2 . VAL A 182 ? 0.2734 0.2064 0.2780 -0.0343 -0.0395 0.0016  188 VAL A CG2 
1348 N N   . ARG A 183 ? 0.2595 0.1747 0.2602 -0.0324 -0.0362 0.0016  189 ARG A N   
1349 C CA  . ARG A 183 ? 0.2685 0.1783 0.2672 -0.0309 -0.0350 0.0016  189 ARG A CA  
1350 C C   . ARG A 183 ? 0.2692 0.1773 0.2704 -0.0299 -0.0338 0.0033  189 ARG A C   
1351 O O   . ARG A 183 ? 0.2540 0.1597 0.2552 -0.0278 -0.0330 0.0041  189 ARG A O   
1352 C CB  . ARG A 183 ? 0.2814 0.1868 0.2766 -0.0316 -0.0344 0.0000  189 ARG A CB  
1353 C CG  . ARG A 183 ? 0.2780 0.1847 0.2704 -0.0324 -0.0354 -0.0017 189 ARG A CG  
1354 C CD  . ARG A 183 ? 0.3256 0.2278 0.3145 -0.0330 -0.0347 -0.0031 189 ARG A CD  
1355 N NE  . ARG A 183 ? 0.3453 0.2426 0.3310 -0.0311 -0.0339 -0.0037 189 ARG A NE  
1356 C CZ  . ARG A 183 ? 0.4044 0.2968 0.3869 -0.0311 -0.0329 -0.0048 189 ARG A CZ  
1357 N NH1 . ARG A 183 ? 0.4140 0.3056 0.3963 -0.0329 -0.0326 -0.0054 189 ARG A NH1 
1358 N NH2 . ARG A 183 ? 0.3321 0.2203 0.3114 -0.0291 -0.0322 -0.0054 189 ARG A NH2 
1359 N N   . GLN A 184 ? 0.2862 0.1956 0.2896 -0.0312 -0.0335 0.0039  190 GLN A N   
1360 C CA  . GLN A 184 ? 0.3066 0.2146 0.3123 -0.0304 -0.0322 0.0054  190 GLN A CA  
1361 C C   . GLN A 184 ? 0.2847 0.1967 0.2936 -0.0291 -0.0327 0.0070  190 GLN A C   
1362 O O   . GLN A 184 ? 0.2538 0.1642 0.2640 -0.0273 -0.0315 0.0083  190 GLN A O   
1363 C CB  . GLN A 184 ? 0.3161 0.2244 0.3229 -0.0322 -0.0318 0.0055  190 GLN A CB  
1364 C CG  . GLN A 184 ? 0.3744 0.2815 0.3836 -0.0314 -0.0305 0.0070  190 GLN A CG  
1365 C CD  . GLN A 184 ? 0.4145 0.3160 0.4220 -0.0298 -0.0287 0.0073  190 GLN A CD  
1366 O OE1 . GLN A 184 ? 0.4561 0.3538 0.4605 -0.0297 -0.0283 0.0061  190 GLN A OE1 
1367 N NE2 . GLN A 184 ? 0.3981 0.2991 0.4078 -0.0283 -0.0275 0.0088  190 GLN A NE2 
1368 N N   . GLU A 185 ? 0.2520 0.1693 0.2624 -0.0298 -0.0342 0.0069  191 GLU A N   
1369 C CA  . GLU A 185 ? 0.2655 0.1867 0.2791 -0.0286 -0.0347 0.0084  191 GLU A CA  
1370 C C   . GLU A 185 ? 0.2622 0.1821 0.2751 -0.0264 -0.0346 0.0086  191 GLU A C   
1371 O O   . GLU A 185 ? 0.2286 0.1493 0.2439 -0.0246 -0.0341 0.0101  191 GLU A O   
1372 C CB  . GLU A 185 ? 0.2785 0.2056 0.2935 -0.0297 -0.0362 0.0082  191 GLU A CB  
1373 C CG  . GLU A 185 ? 0.3313 0.2630 0.3499 -0.0287 -0.0368 0.0097  191 GLU A CG  
1374 C CD  . GLU A 185 ? 0.4646 0.3965 0.4860 -0.0284 -0.0359 0.0112  191 GLU A CD  
1375 O OE1 . GLU A 185 ? 0.4538 0.3827 0.4745 -0.0293 -0.0349 0.0110  191 GLU A OE1 
1376 O OE2 . GLU A 185 ? 0.5687 0.5039 0.5932 -0.0273 -0.0361 0.0125  191 GLU A OE2 
1377 N N   . VAL A 186 ? 0.2217 0.1394 0.2312 -0.0263 -0.0350 0.0071  192 VAL A N   
1378 C CA  . VAL A 186 ? 0.2238 0.1393 0.2321 -0.0239 -0.0347 0.0072  192 VAL A CA  
1379 C C   . VAL A 186 ? 0.2201 0.1313 0.2285 -0.0217 -0.0327 0.0084  192 VAL A C   
1380 O O   . VAL A 186 ? 0.2051 0.1166 0.2150 -0.0191 -0.0321 0.0097  192 VAL A O   
1381 C CB  . VAL A 186 ? 0.2160 0.1289 0.2198 -0.0241 -0.0352 0.0052  192 VAL A CB  
1382 C CG1 . VAL A 186 ? 0.2236 0.1349 0.2255 -0.0208 -0.0340 0.0051  192 VAL A CG1 
1383 C CG2 . VAL A 186 ? 0.2015 0.1195 0.2055 -0.0257 -0.0371 0.0042  192 VAL A CG2 
1384 N N   . LYS A 187 ? 0.2044 0.1115 0.2111 -0.0225 -0.0315 0.0080  193 LYS A N   
1385 C CA  . LYS A 187 ? 0.2318 0.1350 0.2387 -0.0204 -0.0294 0.0091  193 LYS A CA  
1386 C C   . LYS A 187 ? 0.2528 0.1590 0.2639 -0.0195 -0.0288 0.0112  193 LYS A C   
1387 O O   . LYS A 187 ? 0.2064 0.1116 0.2184 -0.0168 -0.0275 0.0125  193 LYS A O   
1388 C CB  . LYS A 187 ? 0.2505 0.1494 0.2552 -0.0218 -0.0284 0.0083  193 LYS A CB  
1389 C CG  . LYS A 187 ? 0.2479 0.1424 0.2523 -0.0198 -0.0261 0.0093  193 LYS A CG  
1390 C CD  . LYS A 187 ? 0.2970 0.1872 0.2990 -0.0214 -0.0252 0.0082  193 LYS A CD  
1391 C CE  . LYS A 187 ? 0.3583 0.2439 0.3597 -0.0195 -0.0228 0.0091  193 LYS A CE  
1392 N NZ  . LYS A 187 ? 0.4231 0.3048 0.4226 -0.0212 -0.0220 0.0080  193 LYS A NZ  
1393 N N   . GLU A 188 ? 0.2616 0.1718 0.2753 -0.0217 -0.0297 0.0115  194 GLU A N   
1394 C CA  . GLU A 188 ? 0.2860 0.1989 0.3035 -0.0210 -0.0291 0.0133  194 GLU A CA  
1395 C C   . GLU A 188 ? 0.2928 0.2095 0.3127 -0.0190 -0.0296 0.0144  194 GLU A C   
1396 O O   . GLU A 188 ? 0.2362 0.1536 0.2584 -0.0170 -0.0284 0.0160  194 GLU A O   
1397 C CB  . GLU A 188 ? 0.3396 0.2559 0.3589 -0.0236 -0.0301 0.0132  194 GLU A CB  
1398 C CG  . GLU A 188 ? 0.3926 0.3055 0.4103 -0.0252 -0.0292 0.0124  194 GLU A CG  
1399 C CD  . GLU A 188 ? 0.5589 0.4677 0.5767 -0.0238 -0.0271 0.0134  194 GLU A CD  
1400 O OE1 . GLU A 188 ? 0.6590 0.5694 0.6793 -0.0222 -0.0264 0.0150  194 GLU A OE1 
1401 O OE2 . GLU A 188 ? 0.8079 0.7121 0.8232 -0.0242 -0.0260 0.0127  194 GLU A OE2 
1402 N N   . ILE A 189 ? 0.2137 0.1331 0.2332 -0.0195 -0.0313 0.0136  195 ILE A N   
1403 C CA  . ILE A 189 ? 0.2162 0.1393 0.2380 -0.0176 -0.0319 0.0146  195 ILE A CA  
1404 C C   . ILE A 189 ? 0.2291 0.1494 0.2497 -0.0140 -0.0302 0.0153  195 ILE A C   
1405 O O   . ILE A 189 ? 0.2025 0.1257 0.2255 -0.0114 -0.0289 0.0168  195 ILE A O   
1406 C CB  . ILE A 189 ? 0.2303 0.1567 0.2515 -0.0189 -0.0340 0.0134  195 ILE A CB  
1407 C CG1 . ILE A 189 ? 0.2406 0.1713 0.2635 -0.0217 -0.0353 0.0131  195 ILE A CG1 
1408 C CG2 . ILE A 189 ? 0.2367 0.1671 0.2595 -0.0164 -0.0340 0.0141  195 ILE A CG2 
1409 C CD1 . ILE A 189 ? 0.2888 0.2220 0.3100 -0.0234 -0.0371 0.0115  195 ILE A CD1 
1410 N N   . LEU A 190 ? 0.1931 0.1102 0.2094 -0.0131 -0.0291 0.0137  196 LEU A N   
1411 C CA  . LEU A 190 ? 0.2269 0.1439 0.2411 -0.0091 -0.0264 0.0138  196 LEU A CA  
1412 C C   . LEU A 190 ? 0.2278 0.1423 0.2439 -0.0075 -0.0246 0.0156  196 LEU A C   
1413 O O   . LEU A 190 ? 0.1911 0.1083 0.2083 -0.0042 -0.0229 0.0167  196 LEU A O   
1414 C CB  . LEU A 190 ? 0.1936 0.1066 0.2028 -0.0088 -0.0257 0.0119  196 LEU A CB  
1415 C CG  . LEU A 190 ? 0.1988 0.1149 0.2057 -0.0092 -0.0268 0.0100  196 LEU A CG  
1416 C CD1 . LEU A 190 ? 0.2229 0.1348 0.2248 -0.0088 -0.0260 0.0082  196 LEU A CD1 
1417 C CD2 . LEU A 190 ? 0.2020 0.1240 0.2097 -0.0060 -0.0260 0.0104  196 LEU A CD2 
1418 N N   . LEU A 191 ? 0.2266 0.1360 0.2431 -0.0098 -0.0250 0.0160  197 LEU A N   
1419 C CA  . LEU A 191 ? 0.2327 0.1401 0.2507 -0.0084 -0.0230 0.0176  197 LEU A CA  
1420 C C   . LEU A 191 ? 0.2681 0.1808 0.2904 -0.0076 -0.0229 0.0193  197 LEU A C   
1421 O O   . LEU A 191 ? 0.2352 0.1483 0.2587 -0.0046 -0.0211 0.0207  197 LEU A O   
1422 C CB  . LEU A 191 ? 0.2354 0.1397 0.2525 -0.0110 -0.0226 0.0170  197 LEU A CB  
1423 C CG  . LEU A 191 ? 0.2497 0.1481 0.2624 -0.0114 -0.0220 0.0155  197 LEU A CG  
1424 C CD1 . LEU A 191 ? 0.2671 0.1633 0.2791 -0.0144 -0.0219 0.0147  197 LEU A CD1 
1425 C CD2 . LEU A 191 ? 0.2063 0.1009 0.2173 -0.0077 -0.0196 0.0161  197 LEU A CD2 
1426 N N   . ARG A 192 ? 0.2007 0.1178 0.2254 -0.0100 -0.0248 0.0192  198 ARG A N   
1427 C CA  . ARG A 192 ? 0.2434 0.1657 0.2721 -0.0094 -0.0249 0.0207  198 ARG A CA  
1428 C C   . ARG A 192 ? 0.2839 0.2091 0.3138 -0.0061 -0.0245 0.0217  198 ARG A C   
1429 O O   . ARG A 192 ? 0.2762 0.2049 0.3090 -0.0043 -0.0236 0.0231  198 ARG A O   
1430 C CB  . ARG A 192 ? 0.2702 0.1967 0.3009 -0.0125 -0.0271 0.0203  198 ARG A CB  
1431 C CG  . ARG A 192 ? 0.3688 0.2941 0.3991 -0.0155 -0.0274 0.0196  198 ARG A CG  
1432 C CD  . ARG A 192 ? 0.4385 0.3689 0.4709 -0.0179 -0.0295 0.0192  198 ARG A CD  
1433 N NE  . ARG A 192 ? 0.5794 0.5088 0.6102 -0.0207 -0.0303 0.0179  198 ARG A NE  
1434 C CZ  . ARG A 192 ? 0.5851 0.5156 0.6144 -0.0224 -0.0319 0.0165  198 ARG A CZ  
1435 N NH1 . ARG A 192 ? 0.5474 0.4801 0.5765 -0.0219 -0.0331 0.0162  198 ARG A NH1 
1436 N NH2 . ARG A 192 ? 0.7155 0.6450 0.7433 -0.0246 -0.0322 0.0155  198 ARG A NH2 
1437 N N   . LYS A 193 ? 0.1976 0.1234 0.2248 -0.0051 -0.0248 0.0203  199 LYS A N   
1438 C CA  . LYS A 193 ? 0.2262 0.1570 0.2532 -0.0014 -0.0235 0.0204  199 LYS A CA  
1439 C C   . LYS A 193 ? 0.2267 0.1555 0.2521 0.0023  -0.0206 0.0210  199 LYS A C   
1440 O O   . LYS A 193 ? 0.2352 0.1680 0.2609 0.0056  -0.0193 0.0214  199 LYS A O   
1441 C CB  . LYS A 193 ? 0.1976 0.1307 0.2216 -0.0014 -0.0243 0.0184  199 LYS A CB  
1442 C CG  . LYS A 193 ? 0.2191 0.1558 0.2449 -0.0043 -0.0270 0.0179  199 LYS A CG  
1443 C CD  . LYS A 193 ? 0.2290 0.1689 0.2521 -0.0036 -0.0274 0.0161  199 LYS A CD  
1444 C CE  . LYS A 193 ? 0.1726 0.1163 0.1974 -0.0064 -0.0301 0.0157  199 LYS A CE  
1445 N NZ  . LYS A 193 ? 0.1439 0.0935 0.1728 -0.0055 -0.0305 0.0170  199 LYS A NZ  
1446 N N   . GLY A 194 ? 0.1987 0.1215 0.2225 0.0019  -0.0196 0.0210  200 GLY A N   
1447 C CA  . GLY A 194 ? 0.2340 0.1545 0.2561 0.0054  -0.0168 0.0216  200 GLY A CA  
1448 C C   . GLY A 194 ? 0.2110 0.1295 0.2284 0.0070  -0.0156 0.0198  200 GLY A C   
1449 O O   . GLY A 194 ? 0.1837 0.1008 0.1995 0.0102  -0.0132 0.0202  200 GLY A O   
1450 N N   . VAL A 195 ? 0.1662 0.0844 0.1811 0.0049  -0.0171 0.0179  201 VAL A N   
1451 C CA  . VAL A 195 ? 0.1643 0.0800 0.1745 0.0061  -0.0161 0.0162  201 VAL A CA  
1452 C C   . VAL A 195 ? 0.2214 0.1301 0.2298 0.0054  -0.0150 0.0162  201 VAL A C   
1453 O O   . VAL A 195 ? 0.2082 0.1137 0.2179 0.0023  -0.0163 0.0165  201 VAL A O   
1454 C CB  . VAL A 195 ? 0.1642 0.0811 0.1724 0.0037  -0.0181 0.0142  201 VAL A CB  
1455 C CG1 . VAL A 195 ? 0.1954 0.1096 0.1987 0.0049  -0.0170 0.0124  201 VAL A CG1 
1456 C CG2 . VAL A 195 ? 0.1621 0.0858 0.1722 0.0043  -0.0192 0.0143  201 VAL A CG2 
1457 N N   . GLN A 196 ? 0.1869 0.0934 0.1925 0.0084  -0.0126 0.0159  202 GLN A N   
1458 C CA  . GLN A 196 ? 0.2412 0.1409 0.2444 0.0080  -0.0115 0.0156  202 GLN A CA  
1459 C C   . GLN A 196 ? 0.2626 0.1597 0.2620 0.0060  -0.0124 0.0134  202 GLN A C   
1460 O O   . GLN A 196 ? 0.2231 0.1225 0.2199 0.0073  -0.0123 0.0121  202 GLN A O   
1461 C CB  . GLN A 196 ? 0.2529 0.1515 0.2546 0.0121  -0.0085 0.0163  202 GLN A CB  
1462 C CG  . GLN A 196 ? 0.3500 0.2516 0.3553 0.0145  -0.0074 0.0184  202 GLN A CG  
1463 C CD  . GLN A 196 ? 0.6543 0.5511 0.6606 0.0146  -0.0060 0.0198  202 GLN A CD  
1464 O OE1 . GLN A 196 ? 0.8558 0.7498 0.8601 0.0172  -0.0037 0.0200  202 GLN A OE1 
1465 N NE2 . GLN A 196 ? 0.7457 0.6413 0.7551 0.0116  -0.0075 0.0208  202 GLN A NE2 
1466 N N   . LEU A 197 ? 0.2389 0.1309 0.2377 0.0029  -0.0134 0.0130  203 LEU A N   
1467 C CA  . LEU A 197 ? 0.2131 0.1021 0.2083 0.0007  -0.0144 0.0109  203 LEU A CA  
1468 C C   . LEU A 197 ? 0.2806 0.1635 0.2725 0.0016  -0.0125 0.0104  203 LEU A C   
1469 O O   . LEU A 197 ? 0.2750 0.1540 0.2680 0.0013  -0.0116 0.0115  203 LEU A O   
1470 C CB  . LEU A 197 ? 0.2596 0.1477 0.2564 -0.0038 -0.0171 0.0106  203 LEU A CB  
1471 C CG  . LEU A 197 ? 0.2465 0.1404 0.2466 -0.0052 -0.0192 0.0111  203 LEU A CG  
1472 C CD1 . LEU A 197 ? 0.2650 0.1572 0.2662 -0.0097 -0.0218 0.0107  203 LEU A CD1 
1473 C CD2 . LEU A 197 ? 0.2285 0.1271 0.2267 -0.0038 -0.0196 0.0098  203 LEU A CD2 
1474 N N   . LEU A 198 ? 0.2381 0.1201 0.2259 0.0028  -0.0118 0.0087  204 LEU A N   
1475 C CA  . LEU A 198 ? 0.2851 0.1612 0.2692 0.0032  -0.0103 0.0078  204 LEU A CA  
1476 C C   . LEU A 198 ? 0.3012 0.1751 0.2824 0.0002  -0.0120 0.0057  204 LEU A C   
1477 O O   . LEU A 198 ? 0.2729 0.1485 0.2512 0.0011  -0.0120 0.0042  204 LEU A O   
1478 C CB  . LEU A 198 ? 0.3008 0.1776 0.2825 0.0075  -0.0078 0.0076  204 LEU A CB  
1479 C CG  . LEU A 198 ? 0.3778 0.2536 0.3607 0.0106  -0.0053 0.0093  204 LEU A CG  
1480 C CD1 . LEU A 198 ? 0.3781 0.2538 0.3575 0.0143  -0.0030 0.0086  204 LEU A CD1 
1481 C CD2 . LEU A 198 ? 0.4321 0.3017 0.4154 0.0089  -0.0048 0.0101  204 LEU A CD2 
1482 N N   . LEU A 199 ? 0.2994 0.1696 0.2814 -0.0035 -0.0135 0.0056  205 LEU A N   
1483 C CA  . LEU A 199 ? 0.2859 0.1541 0.2655 -0.0068 -0.0154 0.0037  205 LEU A CA  
1484 C C   . LEU A 199 ? 0.3314 0.1932 0.3072 -0.0070 -0.0142 0.0026  205 LEU A C   
1485 O O   . LEU A 199 ? 0.3519 0.2101 0.3275 -0.0054 -0.0122 0.0034  205 LEU A O   
1486 C CB  . LEU A 199 ? 0.3198 0.1880 0.3026 -0.0108 -0.0179 0.0042  205 LEU A CB  
1487 C CG  . LEU A 199 ? 0.3008 0.1751 0.2875 -0.0109 -0.0193 0.0054  205 LEU A CG  
1488 C CD1 . LEU A 199 ? 0.3471 0.2218 0.3369 -0.0148 -0.0215 0.0059  205 LEU A CD1 
1489 C CD2 . LEU A 199 ? 0.3230 0.2023 0.3083 -0.0100 -0.0200 0.0041  205 LEU A CD2 
1490 N N   . SER A 200 ? 0.3222 0.1826 0.2949 -0.0089 -0.0154 0.0006  206 SER A N   
1491 C CA  . SER A 200 ? 0.3098 0.1645 0.2784 -0.0091 -0.0144 -0.0009 206 SER A CA  
1492 C C   . SER A 200 ? 0.3630 0.2170 0.3293 -0.0049 -0.0115 -0.0008 206 SER A C   
1493 O O   . SER A 200 ? 0.3548 0.2037 0.3193 -0.0042 -0.0098 -0.0008 206 SER A O   
1494 C CB  . SER A 200 ? 0.3495 0.1987 0.3188 -0.0117 -0.0146 -0.0004 206 SER A CB  
1495 O OG  . SER A 200 ? 0.3942 0.2469 0.3665 -0.0154 -0.0167 -0.0007 206 SER A OG  
1496 N N   . GLU A 201 ? 0.2971 0.1563 0.2633 -0.0020 -0.0108 -0.0007 207 GLU A N   
1497 C CA  . GLU A 201 ? 0.3411 0.2000 0.3049 0.0021  -0.0082 -0.0008 207 GLU A CA  
1498 C C   . GLU A 201 ? 0.3087 0.1719 0.2703 0.0036  -0.0084 -0.0022 207 GLU A C   
1499 O O   . GLU A 201 ? 0.2644 0.1328 0.2280 0.0030  -0.0100 -0.0022 207 GLU A O   
1500 C CB  . GLU A 201 ? 0.3856 0.2465 0.3524 0.0051  -0.0064 0.0014  207 GLU A CB  
1501 C CG  . GLU A 201 ? 0.4414 0.2990 0.4112 0.0036  -0.0064 0.0030  207 GLU A CG  
1502 C CD  . GLU A 201 ? 0.5866 0.4420 0.5565 0.0068  -0.0037 0.0044  207 GLU A CD  
1503 O OE1 . GLU A 201 ? 0.5299 0.3847 0.4969 0.0099  -0.0017 0.0038  207 GLU A OE1 
1504 O OE2 . GLU A 201 ? 0.6201 0.4743 0.5931 0.0063  -0.0035 0.0061  207 GLU A OE2 
1505 N N   . ARG A 202 ? 0.2967 0.1576 0.2543 0.0056  -0.0067 -0.0035 208 ARG A N   
1506 C CA  . ARG A 202 ? 0.3232 0.1877 0.2783 0.0072  -0.0067 -0.0049 208 ARG A CA  
1507 C C   . ARG A 202 ? 0.3068 0.1735 0.2614 0.0119  -0.0041 -0.0042 208 ARG A C   
1508 O O   . ARG A 202 ? 0.3032 0.1661 0.2564 0.0139  -0.0020 -0.0038 208 ARG A O   
1509 C CB  . ARG A 202 ? 0.3400 0.2006 0.2907 0.0058  -0.0070 -0.0071 208 ARG A CB  
1510 C CG  . ARG A 202 ? 0.3528 0.2172 0.3009 0.0073  -0.0070 -0.0087 208 ARG A CG  
1511 C CD  . ARG A 202 ? 0.4100 0.2710 0.3540 0.0053  -0.0078 -0.0109 208 ARG A CD  
1512 N NE  . ARG A 202 ? 0.4384 0.2985 0.3834 0.0009  -0.0105 -0.0115 208 ARG A NE  
1513 C CZ  . ARG A 202 ? 0.4449 0.3091 0.3909 -0.0009 -0.0126 -0.0120 208 ARG A CZ  
1514 N NH1 . ARG A 202 ? 0.3700 0.2398 0.3162 0.0012  -0.0126 -0.0122 208 ARG A NH1 
1515 N NH2 . ARG A 202 ? 0.4470 0.3097 0.3938 -0.0050 -0.0150 -0.0125 208 ARG A NH2 
1516 N N   . VAL A 203 ? 0.2748 0.1477 0.2309 0.0137  -0.0044 -0.0039 209 VAL A N   
1517 C CA  . VAL A 203 ? 0.2820 0.1573 0.2374 0.0181  -0.0020 -0.0034 209 VAL A CA  
1518 C C   . VAL A 203 ? 0.3012 0.1740 0.2517 0.0195  -0.0008 -0.0052 209 VAL A C   
1519 O O   . VAL A 203 ? 0.2803 0.1536 0.2285 0.0179  -0.0021 -0.0070 209 VAL A O   
1520 C CB  . VAL A 203 ? 0.2543 0.1368 0.2119 0.0195  -0.0027 -0.0029 209 VAL A CB  
1521 C CG1 . VAL A 203 ? 0.2725 0.1574 0.2288 0.0241  -0.0003 -0.0027 209 VAL A CG1 
1522 C CG2 . VAL A 203 ? 0.2185 0.1033 0.1811 0.0186  -0.0035 -0.0009 209 VAL A CG2 
1523 N N   . SER A 204 ? 0.3073 0.1772 0.2562 0.0224  0.0017  -0.0048 210 SER A N   
1524 C CA  . SER A 204 ? 0.3501 0.2162 0.2944 0.0234  0.0030  -0.0064 210 SER A CA  
1525 C C   . SER A 204 ? 0.4154 0.2845 0.3578 0.0277  0.0050  -0.0068 210 SER A C   
1526 O O   . SER A 204 ? 0.4323 0.2990 0.3707 0.0286  0.0060  -0.0083 210 SER A O   
1527 C CB  . SER A 204 ? 0.3602 0.2196 0.3035 0.0232  0.0045  -0.0060 210 SER A CB  
1528 O OG  . SER A 204 ? 0.3789 0.2387 0.3249 0.0255  0.0061  -0.0039 210 SER A OG  
1529 N N   . ASN A 205 ? 0.3351 0.2093 0.2800 0.0303  0.0057  -0.0054 211 ASN A N   
1530 C CA  . ASN A 205 ? 0.3868 0.2638 0.3298 0.0344  0.0076  -0.0057 211 ASN A CA  
1531 C C   . ASN A 205 ? 0.3876 0.2714 0.3316 0.0349  0.0064  -0.0062 211 ASN A C   
1532 O O   . ASN A 205 ? 0.4084 0.2965 0.3532 0.0383  0.0077  -0.0055 211 ASN A O   
1533 C CB  . ASN A 205 ? 0.3826 0.2592 0.3270 0.0378  0.0100  -0.0038 211 ASN A CB  
1534 C CG  . ASN A 205 ? 0.3969 0.2773 0.3461 0.0378  0.0094  -0.0018 211 ASN A CG  
1535 O OD1 . ASN A 205 ? 0.3479 0.2295 0.2998 0.0347  0.0072  -0.0015 211 ASN A OD1 
1536 N ND2 . ASN A 205 ? 0.3700 0.2523 0.3204 0.0414  0.0114  -0.0004 211 ASN A ND2 
1537 N N   . LEU A 206 ? 0.3903 0.2754 0.3341 0.0317  0.0040  -0.0074 212 LEU A N   
1538 C CA  . LEU A 206 ? 0.4149 0.3065 0.3600 0.0318  0.0026  -0.0078 212 LEU A CA  
1539 C C   . LEU A 206 ? 0.4290 0.3237 0.3715 0.0353  0.0040  -0.0088 212 LEU A C   
1540 O O   . LEU A 206 ? 0.4163 0.3168 0.3605 0.0370  0.0039  -0.0084 212 LEU A O   
1541 C CB  . LEU A 206 ? 0.4041 0.2958 0.3489 0.0277  -0.0001 -0.0092 212 LEU A CB  
1542 C CG  . LEU A 206 ? 0.3813 0.2728 0.3298 0.0242  -0.0022 -0.0081 212 LEU A CG  
1543 C CD1 . LEU A 206 ? 0.4686 0.3607 0.4164 0.0205  -0.0048 -0.0096 212 LEU A CD1 
1544 C CD2 . LEU A 206 ? 0.3800 0.2767 0.3327 0.0256  -0.0023 -0.0063 212 LEU A CD2 
1545 N N   . GLU A 207 ? 0.4601 0.3510 0.3985 0.0363  0.0054  -0.0101 213 GLU A N   
1546 C CA  . GLU A 207 ? 0.4683 0.3619 0.4042 0.0397  0.0068  -0.0111 213 GLU A CA  
1547 C C   . GLU A 207 ? 0.4839 0.3804 0.4214 0.0438  0.0090  -0.0095 213 GLU A C   
1548 O O   . GLU A 207 ? 0.5248 0.4259 0.4617 0.0464  0.0096  -0.0098 213 GLU A O   
1549 C CB  . GLU A 207 ? 0.5394 0.4278 0.4706 0.0400  0.0080  -0.0127 213 GLU A CB  
1550 C CG  . GLU A 207 ? 0.5418 0.4244 0.4725 0.0408  0.0099  -0.0117 213 GLU A CG  
1551 N N   . GLU A 208 ? 0.4507 0.3444 0.3900 0.0444  0.0101  -0.0078 214 GLU A N   
1552 C CA  . GLU A 208 ? 0.4350 0.3306 0.3756 0.0483  0.0122  -0.0062 214 GLU A CA  
1553 C C   . GLU A 208 ? 0.4005 0.3016 0.3456 0.0486  0.0114  -0.0046 214 GLU A C   
1554 O O   . GLU A 208 ? 0.4065 0.3098 0.3531 0.0518  0.0131  -0.0032 214 GLU A O   
1555 C CB  . GLU A 208 ? 0.4696 0.3594 0.4100 0.0489  0.0140  -0.0051 214 GLU A CB  
1556 N N   . LEU A 209 ? 0.4142 0.2804 0.3344 0.0188  0.0283  0.0402  215 LEU A N   
1557 C CA  . LEU A 209 ? 0.3645 0.2369 0.2880 0.0208  0.0259  0.0420  215 LEU A CA  
1558 C C   . LEU A 209 ? 0.3175 0.1905 0.2379 0.0218  0.0279  0.0398  215 LEU A C   
1559 O O   . LEU A 209 ? 0.3392 0.2064 0.2524 0.0193  0.0292  0.0376  215 LEU A O   
1560 C CB  . LEU A 209 ? 0.3395 0.2108 0.2611 0.0184  0.0218  0.0442  215 LEU A CB  
1561 C CG  . LEU A 209 ? 0.3627 0.2345 0.2881 0.0175  0.0190  0.0470  215 LEU A CG  
1562 C CD1 . LEU A 209 ? 0.3586 0.2293 0.2814 0.0151  0.0156  0.0489  215 LEU A CD1 
1563 C CD2 . LEU A 209 ? 0.3302 0.2092 0.2640 0.0207  0.0180  0.0489  215 LEU A CD2 
1564 N N   . PRO A 210 ? 0.3259 0.2058 0.2514 0.0253  0.0283  0.0402  216 PRO A N   
1565 C CA  . PRO A 210 ? 0.3204 0.2015 0.2434 0.0261  0.0292  0.0387  216 PRO A CA  
1566 C C   . PRO A 210 ? 0.3305 0.2109 0.2507 0.0243  0.0256  0.0400  216 PRO A C   
1567 O O   . PRO A 210 ? 0.2902 0.1740 0.2142 0.0244  0.0223  0.0427  216 PRO A O   
1568 C CB  . PRO A 210 ? 0.3521 0.2417 0.2822 0.0304  0.0303  0.0392  216 PRO A CB  
1569 C CG  . PRO A 210 ? 0.3936 0.2858 0.3294 0.0317  0.0307  0.0405  216 PRO A CG  
1570 C CD  . PRO A 210 ? 0.3404 0.2275 0.2741 0.0285  0.0279  0.0420  216 PRO A CD  
1571 N N   . LEU A 211 ? 0.3090 0.1850 0.2226 0.0224  0.0262  0.0381  217 LEU A N   
1572 C CA  . LEU A 211 ? 0.3027 0.1770 0.2126 0.0202  0.0232  0.0390  217 LEU A CA  
1573 C C   . LEU A 211 ? 0.3139 0.1918 0.2243 0.0219  0.0230  0.0385  217 LEU A C   
1574 O O   . LEU A 211 ? 0.3013 0.1791 0.2105 0.0233  0.0259  0.0362  217 LEU A O   
1575 C CB  . LEU A 211 ? 0.3021 0.1679 0.2032 0.0161  0.0239  0.0372  217 LEU A CB  
1576 C CG  . LEU A 211 ? 0.3331 0.1945 0.2327 0.0140  0.0242  0.0374  217 LEU A CG  
1577 C CD1 . LEU A 211 ? 0.3440 0.1970 0.2341 0.0100  0.0254  0.0350  217 LEU A CD1 
1578 C CD2 . LEU A 211 ? 0.3358 0.2001 0.2398 0.0138  0.0206  0.0408  217 LEU A CD2 
1579 N N   . ASN A 212 ? 0.2567 0.1377 0.1688 0.0217  0.0196  0.0405  218 ASN A N   
1580 C CA  . ASN A 212 ? 0.2567 0.1408 0.1690 0.0229  0.0189  0.0401  218 ASN A CA  
1581 C C   . ASN A 212 ? 0.2764 0.1667 0.1940 0.0270  0.0211  0.0394  218 ASN A C   
1582 O O   . ASN A 212 ? 0.3009 0.1923 0.2175 0.0281  0.0221  0.0379  218 ASN A O   
1583 C CB  . ASN A 212 ? 0.3159 0.1936 0.2203 0.0205  0.0200  0.0377  218 ASN A CB  
1584 C CG  . ASN A 212 ? 0.2925 0.1641 0.1909 0.0165  0.0182  0.0380  218 ASN A CG  
1585 O OD1 . ASN A 212 ? 0.2629 0.1361 0.1632 0.0157  0.0152  0.0404  218 ASN A OD1 
1586 N ND2 . ASN A 212 ? 0.3141 0.1786 0.2049 0.0139  0.0202  0.0354  218 ASN A ND2 
1587 N N   . GLU A 213 ? 0.2495 0.1443 0.1730 0.0292  0.0218  0.0404  219 GLU A N   
1588 C CA  . GLU A 213 ? 0.2653 0.1664 0.1937 0.0331  0.0244  0.0396  219 GLU A CA  
1589 C C   . GLU A 213 ? 0.2260 0.1340 0.1616 0.0353  0.0233  0.0418  219 GLU A C   
1590 O O   . GLU A 213 ? 0.2491 0.1559 0.1863 0.0344  0.0225  0.0431  219 GLU A O   
1591 C CB  . GLU A 213 ? 0.3127 0.2111 0.2396 0.0337  0.0286  0.0373  219 GLU A CB  
1592 C CG  . GLU A 213 ? 0.3514 0.2569 0.2840 0.0377  0.0316  0.0369  219 GLU A CG  
1593 N N   . TYR A 214 ? 0.2172 0.1322 0.1571 0.0379  0.0233  0.0422  220 TYR A N   
1594 C CA  . TYR A 214 ? 0.2029 0.1250 0.1495 0.0401  0.0230  0.0440  220 TYR A CA  
1595 C C   . TYR A 214 ? 0.2461 0.1702 0.1959 0.0419  0.0263  0.0436  220 TYR A C   
1596 O O   . TYR A 214 ? 0.2134 0.1378 0.1626 0.0433  0.0297  0.0417  220 TYR A O   
1597 C CB  . TYR A 214 ? 0.2033 0.1327 0.1533 0.0427  0.0233  0.0440  220 TYR A CB  
1598 C CG  . TYR A 214 ? 0.2509 0.1884 0.2078 0.0453  0.0245  0.0455  220 TYR A CG  
1599 C CD1 . TYR A 214 ? 0.2271 0.1670 0.1870 0.0448  0.0218  0.0477  220 TYR A CD1 
1600 C CD2 . TYR A 214 ? 0.2647 0.2076 0.2249 0.0480  0.0286  0.0447  220 TYR A CD2 
1601 C CE1 . TYR A 214 ? 0.2432 0.1904 0.2092 0.0470  0.0231  0.0491  220 TYR A CE1 
1602 C CE2 . TYR A 214 ? 0.2768 0.2272 0.2429 0.0500  0.0299  0.0463  220 TYR A CE2 
1603 C CZ  . TYR A 214 ? 0.2653 0.2178 0.2344 0.0495  0.0273  0.0484  220 TYR A CZ  
1604 O OH  . TYR A 214 ? 0.2923 0.2523 0.2672 0.0513  0.0288  0.0501  220 TYR A OH  
1605 N N   . ARG A 215 ? 0.2073 0.1329 0.1608 0.0419  0.0252  0.0455  221 ARG A N   
1606 C CA  . ARG A 215 ? 0.2191 0.1485 0.1773 0.0439  0.0281  0.0456  221 ARG A CA  
1607 C C   . ARG A 215 ? 0.2271 0.1635 0.1915 0.0453  0.0270  0.0480  221 ARG A C   
1608 O O   . ARG A 215 ? 0.2067 0.1423 0.1710 0.0439  0.0235  0.0496  221 ARG A O   
1609 C CB  . ARG A 215 ? 0.2549 0.1778 0.2110 0.0420  0.0284  0.0454  221 ARG A CB  
1610 C CG  . ARG A 215 ? 0.3135 0.2292 0.2633 0.0403  0.0301  0.0430  221 ARG A CG  
1611 C CD  . ARG A 215 ? 0.3627 0.2814 0.3136 0.0427  0.0345  0.0411  221 ARG A CD  
1612 N NE  . ARG A 215 ? 0.4494 0.3610 0.3940 0.0410  0.0363  0.0386  221 ARG A NE  
1613 C CZ  . ARG A 215 ? 0.5827 0.4893 0.5255 0.0397  0.0383  0.0375  221 ARG A CZ  
1614 N NH1 . ARG A 215 ? 0.5340 0.4422 0.4811 0.0403  0.0387  0.0386  221 ARG A NH1 
1615 N NH2 . ARG A 215 ? 0.7122 0.6120 0.6486 0.0378  0.0399  0.0352  221 ARG A NH2 
1616 N N   . GLU A 216 ? 0.2159 0.1591 0.1856 0.0479  0.0302  0.0483  222 GLU A N   
1617 C CA  . GLU A 216 ? 0.2492 0.1990 0.2248 0.0491  0.0297  0.0506  222 GLU A CA  
1618 C C   . GLU A 216 ? 0.2197 0.1656 0.1959 0.0473  0.0270  0.0522  222 GLU A C   
1619 O O   . GLU A 216 ? 0.1737 0.1226 0.1528 0.0472  0.0248  0.0542  222 GLU A O   
1620 C CB  . GLU A 216 ? 0.2790 0.2361 0.2596 0.0516  0.0339  0.0509  222 GLU A CB  
1621 C CG  . GLU A 216 ? 0.4128 0.3768 0.3946 0.0534  0.0359  0.0507  222 GLU A CG  
1622 C CD  . GLU A 216 ? 0.4817 0.4514 0.4669 0.0539  0.0343  0.0527  222 GLU A CD  
1623 N N   . TYR A 217 ? 0.2074 0.1466 0.1807 0.0458  0.0270  0.0514  223 TYR A N   
1624 C CA  . TYR A 217 ? 0.2012 0.1363 0.1748 0.0439  0.0245  0.0529  223 TYR A CA  
1625 C C   . TYR A 217 ? 0.2459 0.1716 0.2136 0.0412  0.0239  0.0515  223 TYR A C   
1626 O O   . TYR A 217 ? 0.2483 0.1721 0.2148 0.0417  0.0270  0.0497  223 TYR A O   
1627 C CB  . TYR A 217 ? 0.2209 0.1610 0.2010 0.0457  0.0265  0.0541  223 TYR A CB  
1628 C CG  . TYR A 217 ? 0.2244 0.1600 0.2047 0.0439  0.0239  0.0555  223 TYR A CG  
1629 C CD1 . TYR A 217 ? 0.2496 0.1787 0.2276 0.0424  0.0245  0.0545  223 TYR A CD1 
1630 C CD2 . TYR A 217 ? 0.2455 0.1834 0.2284 0.0435  0.0210  0.0577  223 TYR A CD2 
1631 C CE1 . TYR A 217 ? 0.2570 0.1818 0.2350 0.0407  0.0221  0.0558  223 TYR A CE1 
1632 C CE2 . TYR A 217 ? 0.2544 0.1879 0.2372 0.0417  0.0186  0.0590  223 TYR A CE2 
1633 C CZ  . TYR A 217 ? 0.2821 0.2090 0.2624 0.0403  0.0190  0.0581  223 TYR A CZ  
1634 O OH  . TYR A 217 ? 0.3520 0.2744 0.3322 0.0385  0.0166  0.0593  223 TYR A OH  
1635 N N   . ILE A 218 ? 0.2122 0.1321 0.1761 0.0382  0.0200  0.0525  224 ILE A N   
1636 C CA  . ILE A 218 ? 0.2322 0.1433 0.1905 0.0350  0.0191  0.0518  224 ILE A CA  
1637 C C   . ILE A 218 ? 0.2359 0.1446 0.1953 0.0330  0.0157  0.0541  224 ILE A C   
1638 O O   . ILE A 218 ? 0.2195 0.1307 0.1804 0.0327  0.0127  0.0560  224 ILE A O   
1639 C CB  . ILE A 218 ? 0.1995 0.1058 0.1512 0.0325  0.0180  0.0509  224 ILE A CB  
1640 C CG1 . ILE A 218 ? 0.2365 0.1452 0.1872 0.0346  0.0210  0.0486  224 ILE A CG1 
1641 C CG2 . ILE A 218 ? 0.2191 0.1167 0.1651 0.0290  0.0178  0.0501  224 ILE A CG2 
1642 C CD1 . ILE A 218 ? 0.2117 0.1168 0.1564 0.0325  0.0197  0.0477  224 ILE A CD1 
1643 N N   . LYS A 219 ? 0.2189 0.1227 0.1775 0.0315  0.0162  0.0540  225 LYS A N   
1644 C CA  . LYS A 219 ? 0.2366 0.1374 0.1957 0.0294  0.0129  0.0561  225 LYS A CA  
1645 C C   . LYS A 219 ? 0.2695 0.1626 0.2225 0.0253  0.0115  0.0559  225 LYS A C   
1646 O O   . LYS A 219 ? 0.2868 0.1752 0.2364 0.0243  0.0141  0.0540  225 LYS A O   
1647 C CB  . LYS A 219 ? 0.2719 0.1732 0.2354 0.0306  0.0144  0.0563  225 LYS A CB  
1648 C CG  . LYS A 219 ? 0.3178 0.2149 0.2812 0.0281  0.0109  0.0583  225 LYS A CG  
1649 C CD  . LYS A 219 ? 0.4065 0.3025 0.3733 0.0289  0.0126  0.0580  225 LYS A CD  
1650 N N   . VAL A 220 ? 0.2530 0.1453 0.2045 0.0231  0.0078  0.0578  226 VAL A N   
1651 C CA  . VAL A 220 ? 0.2514 0.1377 0.1978 0.0193  0.0068  0.0582  226 VAL A CA  
1652 C C   . VAL A 220 ? 0.2833 0.1674 0.2320 0.0177  0.0047  0.0603  226 VAL A C   
1653 O O   . VAL A 220 ? 0.2919 0.1793 0.2450 0.0184  0.0019  0.0624  226 VAL A O   
1654 C CB  . VAL A 220 ? 0.2426 0.1301 0.1868 0.0180  0.0045  0.0593  226 VAL A CB  
1655 C CG1 . VAL A 220 ? 0.2324 0.1146 0.1717 0.0147  0.0040  0.0598  226 VAL A CG1 
1656 C CG2 . VAL A 220 ? 0.2036 0.0927 0.1452 0.0196  0.0066  0.0571  226 VAL A CG2 
1657 N N   . GLN A 221 ? 0.3128 0.1909 0.2581 0.0155  0.0063  0.0593  227 GLN A N   
1658 C CA  . GLN A 221 ? 0.3519 0.2274 0.2993 0.0137  0.0046  0.0611  227 GLN A CA  
1659 C C   . GLN A 221 ? 0.2964 0.1673 0.2388 0.0106  0.0043  0.0616  227 GLN A C   
1660 O O   . GLN A 221 ? 0.3127 0.1797 0.2480 0.0094  0.0065  0.0592  227 GLN A O   
1661 C CB  . GLN A 221 ? 0.3716 0.2438 0.3197 0.0141  0.0072  0.0593  227 GLN A CB  
1662 C CG  . GLN A 221 ? 0.4657 0.3420 0.4179 0.0177  0.0089  0.0583  227 GLN A CG  
1663 C CD  . GLN A 221 ? 0.5886 0.4618 0.5424 0.0180  0.0113  0.0568  227 GLN A CD  
1664 O OE1 . GLN A 221 ? 0.5861 0.4538 0.5356 0.0162  0.0138  0.0547  227 GLN A OE1 
1665 N NE2 . GLN A 221 ? 0.7778 0.6545 0.7373 0.0203  0.0108  0.0577  227 GLN A NE2 
1666 N N   . THR A 222 ? 0.3379 0.2090 0.2833 0.0094  0.0019  0.0644  228 THR A N   
1667 C CA  . THR A 222 ? 0.3193 0.1855 0.2593 0.0068  0.0022  0.0645  228 THR A CA  
1668 C C   . THR A 222 ? 0.3698 0.2312 0.3100 0.0053  0.0029  0.0643  228 THR A C   
1669 O O   . THR A 222 ? 0.3632 0.2263 0.3098 0.0064  0.0022  0.0653  228 THR A O   
1670 C CB  . THR A 222 ? 0.3738 0.2439 0.3161 0.0067  -0.0004 0.0676  228 THR A CB  
1671 O OG1 . THR A 222 ? 0.4022 0.2757 0.3526 0.0072  -0.0026 0.0710  228 THR A OG1 
1672 C CG2 . THR A 222 ? 0.3322 0.2083 0.2764 0.0084  -0.0016 0.0682  228 THR A CG2 
1673 N N   . ASP A 223 ? 0.3707 0.2254 0.3030 0.0027  0.0039  0.0627  229 ASP A N   
1674 C CA  . ASP A 223 ? 0.4328 0.2822 0.3643 0.0009  0.0045  0.0623  229 ASP A CA  
1675 C C   . ASP A 223 ? 0.4513 0.3044 0.3914 0.0018  0.0022  0.0662  229 ASP A C   
1676 O O   . ASP A 223 ? 0.4509 0.3015 0.3940 0.0012  0.0024  0.0664  229 ASP A O   
1677 C CB  . ASP A 223 ? 0.4108 0.2521 0.3309 -0.0025 0.0054  0.0596  229 ASP A CB  
1678 C CG  . ASP A 223 ? 0.4800 0.3218 0.3969 -0.0033 0.0030  0.0611  229 ASP A CG  
1679 O OD1 . ASP A 223 ? 0.4175 0.2660 0.3393 -0.0012 0.0015  0.0635  229 ASP A OD1 
1680 O OD2 . ASP A 223 ? 0.5327 0.3682 0.4417 -0.0062 0.0027  0.0596  229 ASP A OD2 
1681 N N   . LYS A 224 ? 0.4087 0.2678 0.3531 0.0031  0.0000  0.0694  230 LYS A N   
1682 C CA  . LYS A 224 ? 0.4300 0.2935 0.3833 0.0042  -0.0019 0.0734  230 LYS A CA  
1683 C C   . LYS A 224 ? 0.4787 0.3493 0.4415 0.0060  -0.0042 0.0745  230 LYS A C   
1684 O O   . LYS A 224 ? 0.4495 0.3257 0.4190 0.0067  -0.0066 0.0762  230 LYS A O   
1685 C CB  . LYS A 224 ? 0.4393 0.3054 0.3915 0.0047  -0.0028 0.0755  230 LYS A CB  
1686 N N   . GLY A 225 ? 0.3804 0.2500 0.3418 0.0066  -0.0039 0.0724  231 GLY A N   
1687 C CA  . GLY A 225 ? 0.4205 0.2931 0.3851 0.0083  -0.0065 0.0715  231 GLY A CA  
1688 C C   . GLY A 225 ? 0.4069 0.2846 0.3714 0.0099  -0.0090 0.0715  231 GLY A C   
1689 O O   . GLY A 225 ? 0.3568 0.2342 0.3204 0.0123  -0.0101 0.0703  231 GLY A O   
1690 N N   . THR A 226 ? 0.3910 0.2721 0.3552 0.0093  -0.0090 0.0727  232 THR A N   
1691 C CA  . THR A 226 ? 0.3589 0.2438 0.3221 0.0107  -0.0112 0.0722  232 THR A CA  
1692 C C   . THR A 226 ? 0.3591 0.2431 0.3196 0.0130  -0.0087 0.0703  232 THR A C   
1693 O O   . THR A 226 ? 0.3583 0.2399 0.3165 0.0125  -0.0052 0.0689  232 THR A O   
1694 C CB  . THR A 226 ? 0.3751 0.2644 0.3393 0.0098  -0.0110 0.0741  232 THR A CB  
1695 O OG1 . THR A 226 ? 0.4205 0.3113 0.3885 0.0090  -0.0104 0.0767  232 THR A OG1 
1696 C CG2 . THR A 226 ? 0.3600 0.2525 0.3232 0.0107  -0.0143 0.0734  232 THR A CG2 
1697 N N   . GLU A 227 ? 0.3351 0.2215 0.2954 0.0161  -0.0090 0.0693  233 GLU A N   
1698 C CA  . GLU A 227 ? 0.3279 0.2176 0.2885 0.0191  -0.0051 0.0669  233 GLU A CA  
1699 C C   . GLU A 227 ? 0.3147 0.2092 0.2753 0.0207  -0.0058 0.0669  233 GLU A C   
1700 O O   . GLU A 227 ? 0.2884 0.1851 0.2500 0.0220  -0.0077 0.0679  233 GLU A O   
1701 C CB  . GLU A 227 ? 0.3645 0.2563 0.3288 0.0225  -0.0022 0.0657  233 GLU A CB  
1702 C CG  . GLU A 227 ? 0.4416 0.3287 0.4058 0.0213  -0.0004 0.0648  233 GLU A CG  
1703 C CD  . GLU A 227 ? 0.5713 0.4612 0.5403 0.0246  0.0024  0.0641  233 GLU A CD  
1704 O OE1 . GLU A 227 ? 0.5343 0.4282 0.5070 0.0267  0.0017  0.0654  233 GLU A OE1 
1705 O OE2 . GLU A 227 ? 0.6460 0.5346 0.6155 0.0251  0.0057  0.0623  233 GLU A OE2 
1706 N N   . VAL A 228 ? 0.2930 0.1888 0.2518 0.0208  -0.0040 0.0657  234 VAL A N   
1707 C CA  . VAL A 228 ? 0.2577 0.1580 0.2165 0.0223  -0.0045 0.0655  234 VAL A CA  
1708 C C   . VAL A 228 ? 0.2601 0.1643 0.2202 0.0255  -0.0002 0.0632  234 VAL A C   
1709 O O   . VAL A 228 ? 0.2616 0.1632 0.2192 0.0250  0.0022  0.0615  234 VAL A O   
1710 C CB  . VAL A 228 ? 0.2783 0.1770 0.2341 0.0191  -0.0065 0.0665  234 VAL A CB  
1711 C CG1 . VAL A 228 ? 0.2694 0.1724 0.2252 0.0206  -0.0073 0.0662  234 VAL A CG1 
1712 C CG2 . VAL A 228 ? 0.3196 0.2161 0.2759 0.0158  -0.0099 0.0694  234 VAL A CG2 
1713 N N   . ALA A 229 ? 0.2084 0.1194 0.1729 0.0290  0.0012  0.0631  235 ALA A N   
1714 C CA  . ALA A 229 ? 0.2273 0.1436 0.1940 0.0321  0.0052  0.0613  235 ALA A CA  
1715 C C   . ALA A 229 ? 0.2246 0.1423 0.1888 0.0318  0.0045  0.0607  235 ALA A C   
1716 O O   . ALA A 229 ? 0.2366 0.1551 0.2004 0.0309  0.0015  0.0620  235 ALA A O   
1717 C CB  . ALA A 229 ? 0.2262 0.1508 0.2000 0.0358  0.0077  0.0619  235 ALA A CB  
1718 N N   . THR A 230 ? 0.1798 0.0974 0.1420 0.0326  0.0072  0.0587  236 THR A N   
1719 C CA  . THR A 230 ? 0.1944 0.1125 0.1538 0.0322  0.0064  0.0580  236 THR A CA  
1720 C C   . THR A 230 ? 0.1980 0.1195 0.1580 0.0349  0.0105  0.0558  236 THR A C   
1721 O O   . THR A 230 ? 0.2076 0.1303 0.1696 0.0366  0.0138  0.0547  236 THR A O   
1722 C CB  . THR A 230 ? 0.2006 0.1115 0.1540 0.0281  0.0040  0.0583  236 THR A CB  
1723 O OG1 . THR A 230 ? 0.2138 0.1255 0.1649 0.0274  0.0028  0.0581  236 THR A OG1 
1724 C CG2 . THR A 230 ? 0.1874 0.0933 0.1372 0.0272  0.0068  0.0564  236 THR A CG2 
1725 N N   . ASN A 231 ? 0.1761 0.0993 0.1345 0.0352  0.0102  0.0551  237 ASN A N   
1726 C CA  . ASN A 231 ? 0.1709 0.0962 0.1288 0.0372  0.0136  0.0528  237 ASN A CA  
1727 C C   . ASN A 231 ? 0.1875 0.1060 0.1387 0.0349  0.0137  0.0512  237 ASN A C   
1728 O O   . ASN A 231 ? 0.1952 0.1139 0.1451 0.0363  0.0168  0.0491  237 ASN A O   
1729 C CB  . ASN A 231 ? 0.1987 0.1308 0.1593 0.0394  0.0139  0.0528  237 ASN A CB  
1730 C CG  . ASN A 231 ? 0.1981 0.1380 0.1654 0.0419  0.0147  0.0543  237 ASN A CG  
1731 O OD1 . ASN A 231 ? 0.1824 0.1251 0.1514 0.0418  0.0126  0.0557  237 ASN A OD1 
1732 N ND2 . ASN A 231 ? 0.2054 0.1491 0.1766 0.0440  0.0182  0.0541  237 ASN A ND2 
1733 N N   . LEU A 232 ? 0.1791 0.0920 0.1262 0.0314  0.0106  0.0521  238 LEU A N   
1734 C CA  . LEU A 232 ? 0.1828 0.0903 0.1236 0.0292  0.0109  0.0507  238 LEU A CA  
1735 C C   . LEU A 232 ? 0.1892 0.0904 0.1261 0.0254  0.0089  0.0518  238 LEU A C   
1736 O O   . LEU A 232 ? 0.1902 0.0923 0.1290 0.0241  0.0058  0.0543  238 LEU A O   
1737 C CB  . LEU A 232 ? 0.1811 0.0911 0.1213 0.0293  0.0093  0.0508  238 LEU A CB  
1738 C CG  . LEU A 232 ? 0.1893 0.0941 0.1231 0.0272  0.0096  0.0492  238 LEU A CG  
1739 C CD1 . LEU A 232 ? 0.2099 0.1131 0.1412 0.0287  0.0135  0.0463  238 LEU A CD1 
1740 C CD2 . LEU A 232 ? 0.1981 0.1056 0.1321 0.0272  0.0074  0.0499  238 LEU A CD2 
1741 N N   . VAL A 233 ? 0.1936 0.0887 0.1248 0.0237  0.0109  0.0500  239 VAL A N   
1742 C CA  . VAL A 233 ? 0.2002 0.0891 0.1266 0.0202  0.0099  0.0505  239 VAL A CA  
1743 C C   . VAL A 233 ? 0.2049 0.0891 0.1240 0.0182  0.0105  0.0486  239 VAL A C   
1744 O O   . VAL A 233 ? 0.2120 0.0940 0.1278 0.0187  0.0132  0.0460  239 VAL A O   
1745 C CB  . VAL A 233 ? 0.2109 0.0955 0.1361 0.0195  0.0121  0.0495  239 VAL A CB  
1746 C CG1 . VAL A 233 ? 0.2209 0.0991 0.1407 0.0158  0.0112  0.0498  239 VAL A CG1 
1747 C CG2 . VAL A 233 ? 0.2237 0.1128 0.1560 0.0216  0.0117  0.0511  239 VAL A CG2 
1748 N N   . ILE A 234 ? 0.2081 0.0903 0.1243 0.0158  0.0080  0.0499  240 ILE A N   
1749 C CA  . ILE A 234 ? 0.2131 0.0902 0.1217 0.0135  0.0082  0.0481  240 ILE A CA  
1750 C C   . ILE A 234 ? 0.2207 0.0911 0.1233 0.0101  0.0078  0.0478  240 ILE A C   
1751 O O   . ILE A 234 ? 0.2274 0.0989 0.1322 0.0093  0.0056  0.0502  240 ILE A O   
1752 C CB  . ILE A 234 ? 0.2108 0.0917 0.1209 0.0138  0.0057  0.0494  240 ILE A CB  
1753 C CG1 . ILE A 234 ? 0.2032 0.0910 0.1195 0.0171  0.0059  0.0496  240 ILE A CG1 
1754 C CG2 . ILE A 234 ? 0.2163 0.0915 0.1182 0.0113  0.0058  0.0473  240 ILE A CG2 
1755 C CD1 . ILE A 234 ? 0.2003 0.0928 0.1195 0.0176  0.0031  0.0513  240 ILE A CD1 
1756 N N   . LEU A 235 ? 0.2314 0.0948 0.1260 0.0079  0.0099  0.0449  241 LEU A N   
1757 C CA  . LEU A 235 ? 0.2346 0.0909 0.1222 0.0044  0.0098  0.0439  241 LEU A CA  
1758 C C   . LEU A 235 ? 0.2527 0.1054 0.1337 0.0018  0.0080  0.0432  241 LEU A C   
1759 O O   . LEU A 235 ? 0.2721 0.1229 0.1490 0.0013  0.0089  0.0411  241 LEU A O   
1760 C CB  . LEU A 235 ? 0.2885 0.1388 0.1708 0.0031  0.0132  0.0408  241 LEU A CB  
1761 C CG  . LEU A 235 ? 0.2938 0.1464 0.1814 0.0053  0.0155  0.0410  241 LEU A CG  
1762 C CD1 . LEU A 235 ? 0.3568 0.2020 0.2375 0.0028  0.0186  0.0379  241 LEU A CD1 
1763 C CD2 . LEU A 235 ? 0.2688 0.1252 0.1632 0.0063  0.0135  0.0441  241 LEU A CD2 
1764 N N   . CYS A 236 ? 0.2469 0.0986 0.1269 0.0002  0.0055  0.0447  242 CYS A N   
1765 C CA  . CYS A 236 ? 0.2493 0.0960 0.1216 -0.0029 0.0039  0.0436  242 CYS A CA  
1766 C C   . CYS A 236 ? 0.2653 0.1054 0.1315 -0.0062 0.0038  0.0427  242 CYS A C   
1767 O O   . CYS A 236 ? 0.2602 0.0992 0.1248 -0.0077 0.0013  0.0438  242 CYS A O   
1768 C CB  . CYS A 236 ? 0.2463 0.0978 0.1225 -0.0020 0.0008  0.0460  242 CYS A CB  
1769 S SG  . CYS A 236 ? 0.3136 0.1731 0.1971 0.0017  0.0009  0.0470  242 CYS A SG  
1770 N N   . THR A 237 ? 0.2601 0.0959 0.1228 -0.0072 0.0065  0.0406  243 THR A N   
1771 C CA  . THR A 237 ? 0.2750 0.1055 0.1338 -0.0097 0.0068  0.0401  243 THR A CA  
1772 C C   . THR A 237 ? 0.3064 0.1289 0.1542 -0.0140 0.0069  0.0372  243 THR A C   
1773 O O   . THR A 237 ? 0.3041 0.1217 0.1476 -0.0164 0.0072  0.0365  243 THR A O   
1774 C CB  . THR A 237 ? 0.2802 0.1109 0.1420 -0.0084 0.0099  0.0395  243 THR A CB  
1775 O OG1 . THR A 237 ? 0.2987 0.1290 0.1590 -0.0076 0.0126  0.0372  243 THR A OG1 
1776 C CG2 . THR A 237 ? 0.2820 0.1201 0.1547 -0.0048 0.0091  0.0428  243 THR A CG2 
1777 N N   . GLY A 238 ? 0.2773 0.0981 0.1204 -0.0152 0.0065  0.0357  244 GLY A N   
1778 C CA  . GLY A 238 ? 0.3052 0.1186 0.1380 -0.0194 0.0061  0.0332  244 GLY A CA  
1779 C C   . GLY A 238 ? 0.3101 0.1199 0.1373 -0.0207 0.0087  0.0301  244 GLY A C   
1780 O O   . GLY A 238 ? 0.3099 0.1221 0.1406 -0.0185 0.0113  0.0295  244 GLY A O   
1781 N N   . ILE A 239 ? 0.3260 0.1299 0.1444 -0.0245 0.0081  0.0281  245 ILE A N   
1782 C CA  . ILE A 239 ? 0.3461 0.1461 0.1585 -0.0262 0.0103  0.0251  245 ILE A CA  
1783 C C   . ILE A 239 ? 0.3990 0.1913 0.2020 -0.0305 0.0116  0.0224  245 ILE A C   
1784 O O   . ILE A 239 ? 0.3864 0.1761 0.1869 -0.0324 0.0103  0.0229  245 ILE A O   
1785 C CB  . ILE A 239 ? 0.3636 0.1645 0.1748 -0.0266 0.0081  0.0252  245 ILE A CB  
1786 C CG1 . ILE A 239 ? 0.3962 0.1937 0.2021 -0.0298 0.0049  0.0254  245 ILE A CG1 
1787 C CG2 . ILE A 239 ? 0.3479 0.1567 0.1685 -0.0223 0.0069  0.0278  245 ILE A CG2 
1788 C CD1 . ILE A 239 ? 0.4520 0.2498 0.2563 -0.0305 0.0028  0.0253  245 ILE A CD1 
1789 N N   . LYS A 240 ? 0.3625 0.1514 0.1605 -0.0320 0.0145  0.0196  246 LYS A N   
1790 C CA  . LYS A 240 ? 0.4146 0.1962 0.2033 -0.0363 0.0163  0.0166  246 LYS A CA  
1791 C C   . LYS A 240 ? 0.4456 0.2241 0.2284 -0.0386 0.0164  0.0146  246 LYS A C   
1792 O O   . LYS A 240 ? 0.3920 0.1735 0.1780 -0.0366 0.0172  0.0145  246 LYS A O   
1793 C CB  . LYS A 240 ? 0.4468 0.2271 0.2355 -0.0359 0.0205  0.0148  246 LYS A CB  
1794 C CG  . LYS A 240 ? 0.5895 0.3720 0.3835 -0.0341 0.0208  0.0164  246 LYS A CG  
1795 C CD  . LYS A 240 ? 0.7794 0.5615 0.5747 -0.0333 0.0251  0.0147  246 LYS A CD  
1796 N N   . ILE A 241 ? 0.4606 0.2333 0.2350 -0.0428 0.0155  0.0130  247 ILE A N   
1797 C CA  . ILE A 241 ? 0.4561 0.2254 0.2247 -0.0454 0.0158  0.0110  247 ILE A CA  
1798 C C   . ILE A 241 ? 0.4457 0.2140 0.2134 -0.0451 0.0201  0.0085  247 ILE A C   
1799 O O   . ILE A 241 ? 0.4474 0.2141 0.2142 -0.0454 0.0231  0.0072  247 ILE A O   
1800 C CB  . ILE A 241 ? 0.4953 0.2582 0.2547 -0.0502 0.0145  0.0095  247 ILE A CB  
1801 C CG1 . ILE A 241 ? 0.5306 0.2948 0.2910 -0.0503 0.0100  0.0119  247 ILE A CG1 
1802 C CG2 . ILE A 241 ? 0.4879 0.2466 0.2408 -0.0531 0.0159  0.0070  247 ILE A CG2 
1803 C CD1 . ILE A 241 ? 0.6372 0.3956 0.3893 -0.0548 0.0083  0.0108  247 ILE A CD1 
1804 N N   . ASN A 242 ? 0.4482 0.2177 0.2167 -0.0444 0.0205  0.0080  248 ASN A N   
1805 C CA  . ASN A 242 ? 0.4530 0.2220 0.2214 -0.0438 0.0246  0.0058  248 ASN A CA  
1806 C C   . ASN A 242 ? 0.5189 0.2812 0.2780 -0.0485 0.0264  0.0026  248 ASN A C   
1807 O O   . ASN A 242 ? 0.4659 0.2263 0.2215 -0.0504 0.0254  0.0019  248 ASN A O   
1808 C CB  . ASN A 242 ? 0.4812 0.2550 0.2552 -0.0408 0.0243  0.0067  248 ASN A CB  
1809 C CG  . ASN A 242 ? 0.4809 0.2551 0.2562 -0.0395 0.0284  0.0047  248 ASN A CG  
1810 O OD1 . ASN A 242 ? 0.5441 0.3143 0.3149 -0.0416 0.0316  0.0021  248 ASN A OD1 
1811 N ND2 . ASN A 242 ? 0.5077 0.2868 0.2893 -0.0360 0.0285  0.0058  248 ASN A ND2 
1812 N N   . SER A 243 ? 0.5143 0.2729 0.2693 -0.0505 0.0290  0.0007  249 SER A N   
1813 C CA  . SER A 243 ? 0.5625 0.3147 0.3086 -0.0551 0.0308  -0.0024 249 SER A CA  
1814 C C   . SER A 243 ? 0.5785 0.3296 0.3237 -0.0554 0.0354  -0.0053 249 SER A C   
1815 O O   . SER A 243 ? 0.6345 0.3803 0.3727 -0.0591 0.0376  -0.0080 249 SER A O   
1816 C CB  . SER A 243 ? 0.6143 0.3627 0.3556 -0.0578 0.0306  -0.0029 249 SER A CB  
1817 O OG  . SER A 243 ? 0.6247 0.3744 0.3690 -0.0561 0.0335  -0.0033 249 SER A OG  
1818 N N   . SER A 244 ? 0.5548 0.3105 0.3069 -0.0515 0.0370  -0.0047 250 SER A N   
1819 C CA  . SER A 244 ? 0.5967 0.3516 0.3485 -0.0515 0.0416  -0.0074 250 SER A CA  
1820 C C   . SER A 244 ? 0.6122 0.3647 0.3601 -0.0547 0.0427  -0.0092 250 SER A C   
1821 O O   . SER A 244 ? 0.6832 0.4359 0.4313 -0.0567 0.0456  -0.0106 250 SER A O   
1822 C CB  . SER A 244 ? 0.5482 0.3091 0.3086 -0.0467 0.0426  -0.0062 250 SER A CB  
1823 O OG  . SER A 244 ? 0.5790 0.3428 0.3425 -0.0449 0.0401  -0.0045 250 SER A OG  
1824 N N   . ALA A 245 ? 0.6164 0.3682 0.3627 -0.0552 0.0402  -0.0086 251 ALA A N   
1825 C CA  . ALA A 245 ? 0.6194 0.3709 0.3645 -0.0576 0.0411  -0.0095 251 ALA A CA  
1826 C C   . ALA A 245 ? 0.6153 0.3634 0.3550 -0.0622 0.0412  -0.0104 251 ALA A C   
1827 O O   . ALA A 245 ? 0.6141 0.3621 0.3534 -0.0644 0.0432  -0.0115 251 ALA A O   
1828 C CB  . ALA A 245 ? 0.5855 0.3368 0.3297 -0.0572 0.0380  -0.0085 251 ALA A CB  
1829 N N   . TYR A 246 ? 0.6476 0.3928 0.3833 -0.0638 0.0391  -0.0099 252 TYR A N   
1830 C CA  . TYR A 246 ? 0.6869 0.4286 0.4170 -0.0681 0.0386  -0.0104 252 TYR A CA  
1831 C C   . TYR A 246 ? 0.6922 0.4323 0.4201 -0.0696 0.0394  -0.0109 252 TYR A C   
1832 O O   . TYR A 246 ? 0.6525 0.3896 0.3757 -0.0732 0.0389  -0.0113 252 TYR A O   
1833 C CB  . TYR A 246 ? 0.6473 0.3866 0.3732 -0.0697 0.0343  -0.0092 252 TYR A CB  
1834 C CG  . TYR A 246 ? 0.6477 0.3863 0.3730 -0.0680 0.0309  -0.0078 252 TYR A CG  
1835 C CD1 . TYR A 246 ? 0.6415 0.3777 0.3635 -0.0696 0.0299  -0.0076 252 TYR A CD1 
1836 C CD2 . TYR A 246 ? 0.6024 0.3442 0.3321 -0.0647 0.0287  -0.0061 252 TYR A CD2 
1837 C CE1 . TYR A 246 ? 0.6292 0.3663 0.3526 -0.0679 0.0267  -0.0057 252 TYR A CE1 
1838 C CE2 . TYR A 246 ? 0.5904 0.3354 0.3242 -0.0625 0.0254  -0.0033 252 TYR A CE2 
1839 C CZ  . TYR A 246 ? 0.6128 0.3554 0.3434 -0.0642 0.0245  -0.0031 252 TYR A CZ  
1840 O OH  . TYR A 246 ? 0.5924 0.3381 0.3271 -0.0622 0.0213  -0.0004 252 TYR A OH  
1841 N N   . ARG A 247 ? 0.6845 0.4262 0.4156 -0.0670 0.0407  -0.0107 253 ARG A N   
1842 C CA  . ARG A 247 ? 0.6637 0.4033 0.3921 -0.0683 0.0407  -0.0109 253 ARG A CA  
1843 C C   . ARG A 247 ? 0.6879 0.4264 0.4144 -0.0715 0.0438  -0.0125 253 ARG A C   
1844 O O   . ARG A 247 ? 0.7044 0.4394 0.4257 -0.0746 0.0429  -0.0127 253 ARG A O   
1845 C CB  . ARG A 247 ? 0.6761 0.4176 0.4083 -0.0648 0.0416  -0.0104 253 ARG A CB  
1846 C CG  . ARG A 247 ? 0.6652 0.4102 0.4031 -0.0625 0.0458  -0.0113 253 ARG A CG  
1847 N N   . LYS A 248 ? 0.6275 0.3670 0.3562 -0.0713 0.0477  -0.0139 254 LYS A N   
1848 C CA  . LYS A 248 ? 0.7392 0.4757 0.4642 -0.0749 0.0511  -0.0158 254 LYS A CA  
1849 C C   . LYS A 248 ? 0.7637 0.4975 0.4838 -0.0787 0.0496  -0.0161 254 LYS A C   
1850 O O   . LYS A 248 ? 0.7368 0.4670 0.4516 -0.0820 0.0495  -0.0165 254 LYS A O   
1851 C CB  . LYS A 248 ? 0.7206 0.4592 0.4496 -0.0738 0.0552  -0.0172 254 LYS A CB  
1852 N N   . ALA A 249 ? 0.7186 0.4542 0.4404 -0.0783 0.0484  -0.0156 255 ALA A N   
1853 C CA  . ALA A 249 ? 0.7258 0.4591 0.4434 -0.0819 0.0475  -0.0160 255 ALA A CA  
1854 C C   . ALA A 249 ? 0.7806 0.5112 0.4935 -0.0839 0.0441  -0.0150 255 ALA A C   
1855 O O   . ALA A 249 ? 0.8298 0.5570 0.5376 -0.0878 0.0444  -0.0157 255 ALA A O   
1856 C CB  . ALA A 249 ? 0.7267 0.4626 0.4473 -0.0805 0.0463  -0.0153 255 ALA A CB  
1857 N N   . PHE A 250 ? 0.7556 0.4869 0.4694 -0.0817 0.0409  -0.0134 256 PHE A N   
1858 C CA  . PHE A 250 ? 0.7885 0.5167 0.4973 -0.0838 0.0374  -0.0124 256 PHE A CA  
1859 C C   . PHE A 250 ? 0.7915 0.5188 0.4995 -0.0834 0.0368  -0.0121 256 PHE A C   
1860 O O   . PHE A 250 ? 0.8223 0.5477 0.5275 -0.0837 0.0334  -0.0108 256 PHE A O   
1861 C CB  . PHE A 250 ? 0.7841 0.5123 0.4928 -0.0825 0.0336  -0.0109 256 PHE A CB  
1862 C CG  . PHE A 250 ? 0.7660 0.4946 0.4749 -0.0831 0.0337  -0.0110 256 PHE A CG  
1863 C CD1 . PHE A 250 ? 0.7163 0.4481 0.4300 -0.0805 0.0359  -0.0114 256 PHE A CD1 
1864 C CD2 . PHE A 250 ? 0.7768 0.5028 0.4811 -0.0863 0.0317  -0.0107 256 PHE A CD2 
1865 C CE1 . PHE A 250 ? 0.7424 0.4746 0.4562 -0.0812 0.0360  -0.0116 256 PHE A CE1 
1866 C CE2 . PHE A 250 ? 0.7222 0.4483 0.4264 -0.0870 0.0318  -0.0108 256 PHE A CE2 
1867 C CZ  . PHE A 250 ? 0.6715 0.4007 0.3804 -0.0844 0.0339  -0.0113 256 PHE A CZ  
1868 N N   . GLU A 251 ? 0.7995 0.5271 0.5087 -0.0830 0.0403  -0.0132 257 GLU A N   
1869 C CA  . GLU A 251 ? 0.8131 0.5391 0.5208 -0.0825 0.0402  -0.0130 257 GLU A CA  
1870 C C   . GLU A 251 ? 0.8987 0.6213 0.6010 -0.0856 0.0376  -0.0125 257 GLU A C   
1871 O O   . GLU A 251 ? 0.8785 0.6009 0.5807 -0.0844 0.0349  -0.0112 257 GLU A O   
1872 C CB  . GLU A 251 ? 0.7841 0.5089 0.4915 -0.0831 0.0449  -0.0147 257 GLU A CB  
1873 C CG  . GLU A 251 ? 0.8901 0.6123 0.5939 -0.0869 0.0480  -0.0166 257 GLU A CG  
1874 N N   . SER A 252 ? 0.8628 0.5826 0.5606 -0.0894 0.0382  -0.0134 258 SER A N   
1875 C CA  . SER A 252 ? 0.8903 0.6067 0.5827 -0.0924 0.0358  -0.0129 258 SER A CA  
1876 C C   . SER A 252 ? 0.9339 0.6512 0.6267 -0.0916 0.0310  -0.0110 258 SER A C   
1877 O O   . SER A 252 ? 0.8724 0.5872 0.5614 -0.0934 0.0285  -0.0104 258 SER A O   
1878 C CB  . SER A 252 ? 0.9268 0.6399 0.6143 -0.0967 0.0377  -0.0143 258 SER A CB  
1879 O OG  . SER A 252 ? 0.9192 0.6330 0.6065 -0.0977 0.0353  -0.0136 258 SER A OG  
1880 N N   . ARG A 253 ? 0.9299 0.6490 0.6252 -0.0896 0.0297  -0.0103 259 ARG A N   
1881 C CA  . ARG A 253 ? 0.9624 0.6805 0.6561 -0.0898 0.0254  -0.0088 259 ARG A CA  
1882 C C   . ARG A 253 ? 0.8966 0.6161 0.5931 -0.0865 0.0229  -0.0074 259 ARG A C   
1883 O O   . ARG A 253 ? 0.8089 0.5279 0.5044 -0.0864 0.0191  -0.0061 259 ARG A O   
1884 C CB  . ARG A 253 ? 0.9385 0.6573 0.6327 -0.0903 0.0254  -0.0089 259 ARG A CB  
1885 C CG  . ARG A 253 ? 0.9008 0.6180 0.5922 -0.0936 0.0280  -0.0103 259 ARG A CG  
1886 C CD  . ARG A 253 ? 0.9025 0.6162 0.5883 -0.0973 0.0264  -0.0102 259 ARG A CD  
1887 N NE  . ARG A 253 ? 0.9029 0.6149 0.5858 -0.1006 0.0286  -0.0114 259 ARG A NE  
1888 C CZ  . ARG A 253 ? 0.8987 0.6074 0.5765 -0.1043 0.0277  -0.0114 259 ARG A CZ  
1889 N NH1 . ARG A 253 ? 0.8865 0.5935 0.5616 -0.1051 0.0245  -0.0104 259 ARG A NH1 
1890 N NH2 . ARG A 253 ? 0.8507 0.5580 0.5260 -0.1072 0.0299  -0.0126 259 ARG A NH2 
1891 N N   . LEU A 254 ? 0.9105 0.6317 0.6102 -0.0838 0.0248  -0.0077 260 LEU A N   
1892 C CA  . LEU A 254 ? 0.8689 0.5916 0.5716 -0.0803 0.0229  -0.0065 260 LEU A CA  
1893 C C   . LEU A 254 ? 0.8822 0.6028 0.5824 -0.0808 0.0199  -0.0055 260 LEU A C   
1894 O O   . LEU A 254 ? 0.8934 0.6123 0.5913 -0.0824 0.0211  -0.0060 260 LEU A O   
1895 C CB  . LEU A 254 ? 0.7720 0.4974 0.4793 -0.0773 0.0264  -0.0072 260 LEU A CB  
1896 C CG  . LEU A 254 ? 0.7826 0.5105 0.4932 -0.0765 0.0296  -0.0082 260 LEU A CG  
1897 C CD1 . LEU A 254 ? 0.7786 0.5092 0.4940 -0.0736 0.0332  -0.0089 260 LEU A CD1 
1898 C CD2 . LEU A 254 ? 0.7986 0.5277 0.5107 -0.0751 0.0273  -0.0074 260 LEU A CD2 
1899 N N   . ALA A 255 ? 0.8346 0.5577 0.5382 -0.0789 0.0161  -0.0031 261 ALA A N   
1900 C CA  . ALA A 255 ? 0.8676 0.5918 0.5732 -0.0779 0.0134  -0.0009 261 ALA A CA  
1901 C C   . ALA A 255 ? 0.8703 0.5980 0.5819 -0.0746 0.0156  -0.0001 261 ALA A C   
1902 O O   . ALA A 255 ? 0.8158 0.5451 0.5301 -0.0729 0.0190  -0.0012 261 ALA A O   
1903 C CB  . ALA A 255 ? 0.8188 0.5467 0.5289 -0.0761 0.0091  0.0019  261 ALA A CB  
1904 N N   . SER A 256 ? 0.9026 0.6314 0.6165 -0.0736 0.0136  0.0018  262 SER A N   
1905 C CA  . SER A 256 ? 0.8408 0.5736 0.5619 -0.0701 0.0151  0.0032  262 SER A CA  
1906 C C   . SER A 256 ? 0.8415 0.5806 0.5715 -0.0656 0.0150  0.0050  262 SER A C   
1907 O O   . SER A 256 ? 0.8077 0.5491 0.5417 -0.0634 0.0182  0.0045  262 SER A O   
1908 C CB  . SER A 256 ? 0.8665 0.5996 0.5891 -0.0698 0.0126  0.0053  262 SER A CB  
1909 O OG  . SER A 256 ? 0.8580 0.5946 0.5852 -0.0680 0.0085  0.0081  262 SER A OG  
1910 N N   . SER A 257 ? 0.7715 0.5132 0.5043 -0.0645 0.0115  0.0070  263 SER A N   
1911 C CA  . SER A 257 ? 0.7646 0.5126 0.5060 -0.0603 0.0109  0.0089  263 SER A CA  
1912 C C   . SER A 257 ? 0.6834 0.4320 0.4253 -0.0595 0.0142  0.0071  263 SER A C   
1913 O O   . SER A 257 ? 0.6996 0.4535 0.4488 -0.0558 0.0144  0.0086  263 SER A O   
1914 C CB  . SER A 257 ? 0.7691 0.5190 0.5120 -0.0600 0.0067  0.0108  263 SER A CB  
1915 O OG  . SER A 257 ? 0.6608 0.4080 0.3986 -0.0625 0.0065  0.0092  263 SER A OG  
1916 N N   . GLY A 258 ? 0.7236 0.4672 0.4581 -0.0628 0.0169  0.0040  264 GLY A N   
1917 C CA  . GLY A 258 ? 0.6866 0.4303 0.4210 -0.0625 0.0199  0.0022  264 GLY A CA  
1918 C C   . GLY A 258 ? 0.6523 0.3949 0.3838 -0.0640 0.0182  0.0017  264 GLY A C   
1919 O O   . GLY A 258 ? 0.5399 0.2818 0.2704 -0.0643 0.0206  0.0000  264 GLY A O   
1920 N N   . ALA A 259 ? 0.6470 0.3894 0.3775 -0.0650 0.0142  0.0033  265 ALA A N   
1921 C CA  . ALA A 259 ? 0.6526 0.3932 0.3796 -0.0671 0.0124  0.0029  265 ALA A CA  
1922 C C   . ALA A 259 ? 0.6846 0.4185 0.4021 -0.0720 0.0140  0.0000  265 ALA A C   
1923 O O   . ALA A 259 ? 0.6700 0.4005 0.3834 -0.0739 0.0162  -0.0017 265 ALA A O   
1924 C CB  . ALA A 259 ? 0.6484 0.3907 0.3771 -0.0669 0.0077  0.0054  265 ALA A CB  
1925 N N   . LEU A 260 ? 0.7030 0.4351 0.4173 -0.0741 0.0130  -0.0007 266 LEU A N   
1926 C CA  . LEU A 260 ? 0.6044 0.3303 0.3100 -0.0789 0.0141  -0.0032 266 LEU A CA  
1927 C C   . LEU A 260 ? 0.6752 0.3984 0.3765 -0.0817 0.0102  -0.0023 266 LEU A C   
1928 O O   . LEU A 260 ? 0.6038 0.3298 0.3085 -0.0803 0.0068  -0.0002 266 LEU A O   
1929 C CB  . LEU A 260 ? 0.6363 0.3623 0.3418 -0.0793 0.0156  -0.0042 266 LEU A CB  
1930 C CG  . LEU A 260 ? 0.6017 0.3306 0.3119 -0.0764 0.0193  -0.0051 266 LEU A CG  
1931 C CD1 . LEU A 260 ? 0.6190 0.3517 0.3340 -0.0738 0.0185  -0.0040 266 LEU A CD1 
1932 C CD2 . LEU A 260 ? 0.6722 0.4007 0.3814 -0.0784 0.0233  -0.0067 266 LEU A CD2 
1933 N N   . ARG A 261 ? 0.6556 0.3753 0.3519 -0.0850 0.0108  -0.0032 267 ARG A N   
1934 C CA  . ARG A 261 ? 0.7157 0.4330 0.4081 -0.0878 0.0074  -0.0024 267 ARG A CA  
1935 C C   . ARG A 261 ? 0.6111 0.3280 0.3020 -0.0898 0.0065  -0.0023 267 ARG A C   
1936 O O   . ARG A 261 ? 0.6231 0.3403 0.3141 -0.0903 0.0093  -0.0033 267 ARG A O   
1937 C CB  . ARG A 261 ? 0.7223 0.4370 0.4108 -0.0905 0.0084  -0.0030 267 ARG A CB  
1938 C CG  . ARG A 261 ? 0.8243 0.5391 0.5138 -0.0888 0.0086  -0.0028 267 ARG A CG  
1939 C CD  . ARG A 261 ? 0.9287 0.6407 0.6142 -0.0916 0.0094  -0.0034 267 ARG A CD  
1940 N NE  . ARG A 261 ? 1.0010 0.7128 0.6857 -0.0930 0.0137  -0.0050 267 ARG A NE  
1941 C CZ  . ARG A 261 ? 1.0332 0.7461 0.7200 -0.0916 0.0172  -0.0060 267 ARG A CZ  
1942 N NH1 . ARG A 261 ? 1.1209 0.8351 0.8105 -0.0887 0.0171  -0.0055 267 ARG A NH1 
1943 N NH2 . ARG A 261 ? 1.0659 0.7786 0.7520 -0.0933 0.0209  -0.0076 267 ARG A NH2 
1944 N N   . VAL A 262 ? 0.6242 0.3403 0.3138 -0.0907 0.0024  -0.0010 268 VAL A N   
1945 C CA  . VAL A 262 ? 0.6332 0.3491 0.3218 -0.0921 0.0009  -0.0006 268 VAL A CA  
1946 C C   . VAL A 262 ? 0.6551 0.3689 0.3404 -0.0948 -0.0028 0.0005  268 VAL A C   
1947 O O   . VAL A 262 ? 0.6060 0.3192 0.2908 -0.0947 -0.0048 0.0011  268 VAL A O   
1948 C CB  . VAL A 262 ? 0.6340 0.3528 0.3270 -0.0890 -0.0004 0.0001  268 VAL A CB  
1949 C CG1 . VAL A 262 ? 0.5881 0.3091 0.2845 -0.0865 0.0034  -0.0009 268 VAL A CG1 
1950 C CG2 . VAL A 262 ? 0.6421 0.3653 0.3411 -0.0858 -0.0033 0.0026  268 VAL A CG2 
1951 N N   . ASN A 263 ? 0.5925 0.3052 0.2755 -0.0971 -0.0038 0.0006  269 ASN A N   
1952 C CA  . ASN A 263 ? 0.5756 0.2865 0.2557 -0.0995 -0.0074 0.0017  269 ASN A CA  
1953 C C   . ASN A 263 ? 0.6414 0.3545 0.3247 -0.0978 -0.0110 0.0031  269 ASN A C   
1954 O O   . ASN A 263 ? 0.6118 0.3276 0.2993 -0.0946 -0.0108 0.0032  269 ASN A O   
1955 C CB  . ASN A 263 ? 0.6298 0.3380 0.3053 -0.1033 -0.0066 0.0012  269 ASN A CB  
1956 C CG  . ASN A 263 ? 0.6413 0.3502 0.3174 -0.1035 -0.0059 0.0010  269 ASN A CG  
1957 O OD1 . ASN A 263 ? 0.5818 0.2934 0.2618 -0.1009 -0.0069 0.0016  269 ASN A OD1 
1958 N ND2 . ASN A 263 ? 0.5954 0.3021 0.2676 -0.1065 -0.0038 0.0002  269 ASN A ND2 
1959 N N   . GLU A 264 ? 0.5893 0.3012 0.2706 -0.0998 -0.0143 0.0041  270 GLU A N   
1960 C CA  . GLU A 264 ? 0.6903 0.4042 0.3746 -0.0985 -0.0179 0.0055  270 GLU A CA  
1961 C C   . GLU A 264 ? 0.6593 0.3745 0.3450 -0.0979 -0.0173 0.0053  270 GLU A C   
1962 O O   . GLU A 264 ? 0.6273 0.3462 0.3179 -0.0957 -0.0196 0.0069  270 GLU A O   
1963 C CB  . GLU A 264 ? 0.7009 0.4132 0.3828 -0.1010 -0.0216 0.0066  270 GLU A CB  
1964 C CG  . GLU A 264 ? 0.7568 0.4664 0.4341 -0.1047 -0.0212 0.0064  270 GLU A CG  
1965 C CD  . GLU A 264 ? 0.7957 0.5022 0.4683 -0.1074 -0.0189 0.0054  270 GLU A CD  
1966 O OE1 . GLU A 264 ? 0.7643 0.4708 0.4373 -0.1063 -0.0169 0.0047  270 GLU A OE1 
1967 O OE2 . GLU A 264 ? 0.8843 0.5883 0.5527 -0.1106 -0.0191 0.0054  270 GLU A OE2 
1968 N N   . HIS A 265 ? 0.6060 0.3200 0.2895 -0.0993 -0.0140 0.0041  271 HIS A N   
1969 C CA  . HIS A 265 ? 0.5927 0.3078 0.2776 -0.0986 -0.0128 0.0038  271 HIS A CA  
1970 C C   . HIS A 265 ? 0.5786 0.2961 0.2672 -0.0954 -0.0098 0.0029  271 HIS A C   
1971 O O   . HIS A 265 ? 0.5323 0.2508 0.2222 -0.0946 -0.0084 0.0026  271 HIS A O   
1972 C CB  . HIS A 265 ? 0.6507 0.3632 0.3310 -0.1021 -0.0109 0.0030  271 HIS A CB  
1973 C CG  . HIS A 265 ? 0.6735 0.3831 0.3494 -0.1056 -0.0131 0.0036  271 HIS A CG  
1974 N ND1 . HIS A 265 ? 0.6903 0.4003 0.3665 -0.1062 -0.0171 0.0051  271 HIS A ND1 
1975 C CD2 . HIS A 265 ? 0.6810 0.3876 0.3522 -0.1087 -0.0118 0.0030  271 HIS A CD2 
1976 C CE1 . HIS A 265 ? 0.7247 0.4318 0.3965 -0.1095 -0.0181 0.0053  271 HIS A CE1 
1977 N NE2 . HIS A 265 ? 0.6577 0.3627 0.3263 -0.1111 -0.0150 0.0041  271 HIS A NE2 
1978 N N   . LEU A 266 ? 0.5531 0.2712 0.2432 -0.0936 -0.0086 0.0026  272 LEU A N   
1979 C CA  . LEU A 266 ? 0.5961 0.3177 0.2913 -0.0899 -0.0056 0.0023  272 LEU A CA  
1980 C C   . LEU A 266 ? 0.5425 0.2622 0.2351 -0.0912 -0.0013 0.0003  272 LEU A C   
1981 O O   . LEU A 266 ? 0.4823 0.2040 0.1782 -0.0886 0.0012  -0.0004 272 LEU A O   
1982 C CB  . LEU A 266 ? 0.5166 0.2442 0.2196 -0.0858 -0.0066 0.0041  272 LEU A CB  
1983 C CG  . LEU A 266 ? 0.5904 0.3216 0.2982 -0.0837 -0.0104 0.0065  272 LEU A CG  
1984 C CD1 . LEU A 266 ? 0.5326 0.2693 0.2474 -0.0802 -0.0114 0.0081  272 LEU A CD1 
1985 C CD2 . LEU A 266 ? 0.5638 0.2969 0.2746 -0.0815 -0.0101 0.0071  272 LEU A CD2 
1986 N N   . GLN A 267 ? 0.5188 0.2357 0.2069 -0.0948 -0.0002 -0.0003 273 GLN A N   
1987 C CA  . GLN A 267 ? 0.5081 0.2244 0.1953 -0.0956 0.0042  -0.0019 273 GLN A CA  
1988 C C   . GLN A 267 ? 0.5691 0.2852 0.2564 -0.0950 0.0063  -0.0026 273 GLN A C   
1989 O O   . GLN A 267 ? 0.5821 0.2969 0.2678 -0.0958 0.0043  -0.0020 273 GLN A O   
1990 C CB  . GLN A 267 ? 0.6042 0.3176 0.2864 -0.0998 0.0050  -0.0024 273 GLN A CB  
1991 C CG  . GLN A 267 ? 0.5747 0.2873 0.2553 -0.1013 0.0027  -0.0017 273 GLN A CG  
1992 C CD  . GLN A 267 ? 0.6783 0.3876 0.3535 -0.1056 0.0037  -0.0023 273 GLN A CD  
1993 O OE1 . GLN A 267 ? 0.7436 0.4512 0.4163 -0.1073 0.0060  -0.0033 273 GLN A OE1 
1994 N NE2 . GLN A 267 ? 0.6232 0.3314 0.2962 -0.1075 0.0019  -0.0016 273 GLN A NE2 
1995 N N   . VAL A 268 ? 0.5492 0.2665 0.2387 -0.0937 0.0102  -0.0039 274 VAL A N   
1996 C CA  . VAL A 268 ? 0.5794 0.2967 0.2692 -0.0931 0.0123  -0.0046 274 VAL A CA  
1997 C C   . VAL A 268 ? 0.6929 0.4070 0.3777 -0.0970 0.0133  -0.0053 274 VAL A C   
1998 O O   . VAL A 268 ? 0.7000 0.4126 0.3823 -0.0996 0.0149  -0.0061 274 VAL A O   
1999 C CB  . VAL A 268 ? 0.6046 0.3244 0.2985 -0.0906 0.0163  -0.0057 274 VAL A CB  
2000 C CG1 . VAL A 268 ? 0.6674 0.3870 0.3615 -0.0904 0.0188  -0.0066 274 VAL A CG1 
2001 C CG2 . VAL A 268 ? 0.5633 0.2862 0.2621 -0.0866 0.0151  -0.0049 274 VAL A CG2 
2002 N N   . GLU A 269 ? 0.7092 0.4220 0.3925 -0.0976 0.0123  -0.0051 275 GLU A N   
2003 C CA  . GLU A 269 ? 0.7411 0.4509 0.4196 -0.1012 0.0132  -0.0057 275 GLU A CA  
2004 C C   . GLU A 269 ? 0.7773 0.4870 0.4557 -0.1022 0.0178  -0.0075 275 GLU A C   
2005 O O   . GLU A 269 ? 0.6975 0.4095 0.3798 -0.0997 0.0204  -0.0082 275 GLU A O   
2006 C CB  . GLU A 269 ? 0.7615 0.4702 0.4389 -0.1013 0.0118  -0.0052 275 GLU A CB  
2007 C CG  . GLU A 269 ? 0.8498 0.5600 0.5300 -0.0989 0.0145  -0.0060 275 GLU A CG  
2008 C CD  . GLU A 269 ? 0.8967 0.6051 0.5745 -0.1002 0.0140  -0.0060 275 GLU A CD  
2009 O OE1 . GLU A 269 ? 0.8337 0.5408 0.5097 -0.1008 0.0105  -0.0048 275 GLU A OE1 
2010 O OE2 . GLU A 269 ? 0.8148 0.5230 0.4925 -0.1005 0.0173  -0.0072 275 GLU A OE2 
2011 N N   . GLY A 270 ? 0.8038 0.5109 0.4780 -0.1058 0.0188  -0.0081 276 GLY A N   
2012 C CA  . GLY A 270 ? 0.8146 0.5215 0.4885 -0.1072 0.0229  -0.0098 276 GLY A CA  
2013 C C   . GLY A 270 ? 0.8445 0.5525 0.5197 -0.1070 0.0240  -0.0101 276 GLY A C   
2014 O O   . GLY A 270 ? 0.8496 0.5575 0.5246 -0.1081 0.0274  -0.0115 276 GLY A O   
2015 N N   . HIS A 271 ? 0.7847 0.4937 0.4611 -0.1055 0.0211  -0.0089 277 HIS A N   
2016 C CA  . HIS A 271 ? 0.7630 0.4731 0.4407 -0.1052 0.0219  -0.0091 277 HIS A CA  
2017 C C   . HIS A 271 ? 0.7808 0.4900 0.4567 -0.1060 0.0180  -0.0076 277 HIS A C   
2018 O O   . HIS A 271 ? 0.7676 0.4769 0.4438 -0.1050 0.0146  -0.0063 277 HIS A O   
2019 C CB  . HIS A 271 ? 0.7604 0.4743 0.4441 -0.1011 0.0236  -0.0093 277 HIS A CB  
2020 C CG  . HIS A 271 ? 0.7944 0.5094 0.4803 -0.1004 0.0278  -0.0108 277 HIS A CG  
2021 N ND1 . HIS A 271 ? 0.7859 0.5015 0.4731 -0.0990 0.0283  -0.0110 277 HIS A ND1 
2022 C CD2 . HIS A 271 ? 0.7616 0.4773 0.4487 -0.1008 0.0315  -0.0123 277 HIS A CD2 
2023 C CE1 . HIS A 271 ? 0.7883 0.5051 0.4777 -0.0987 0.0322  -0.0124 277 HIS A CE1 
2024 N NE2 . HIS A 271 ? 0.8162 0.5332 0.5056 -0.0998 0.0342  -0.0132 277 HIS A NE2 
2025 N N   . SER A 272 ? 0.7279 0.4362 0.4021 -0.1077 0.0185  -0.0078 278 SER A N   
2026 C CA  . SER A 272 ? 0.6744 0.3821 0.3472 -0.1085 0.0149  -0.0065 278 SER A CA  
2027 C C   . SER A 272 ? 0.6194 0.3300 0.2965 -0.1055 0.0145  -0.0061 278 SER A C   
2028 O O   . SER A 272 ? 0.6108 0.3217 0.2881 -0.1051 0.0112  -0.0048 278 SER A O   
2029 C CB  . SER A 272 ? 0.7101 0.4144 0.3774 -0.1128 0.0152  -0.0068 278 SER A CB  
2030 O OG  . SER A 272 ? 0.7586 0.4629 0.4259 -0.1136 0.0190  -0.0082 278 SER A OG  
2031 N N   . ASN A 273 ? 0.5138 0.2265 0.1943 -0.1035 0.0179  -0.0072 279 ASN A N   
2032 C CA  . ASN A 273 ? 0.5744 0.2897 0.2589 -0.1008 0.0180  -0.0069 279 ASN A CA  
2033 C C   . ASN A 273 ? 0.5529 0.2717 0.2431 -0.0964 0.0187  -0.0069 279 ASN A C   
2034 O O   . ASN A 273 ? 0.4771 0.1984 0.1711 -0.0939 0.0198  -0.0070 279 ASN A O   
2035 C CB  . ASN A 273 ? 0.5635 0.2786 0.2474 -0.1021 0.0215  -0.0082 279 ASN A CB  
2036 C CG  . ASN A 273 ? 0.5816 0.2973 0.2670 -0.1017 0.0255  -0.0097 279 ASN A CG  
2037 O OD1 . ASN A 273 ? 0.5644 0.2794 0.2490 -0.1021 0.0257  -0.0099 279 ASN A OD1 
2038 N ND2 . ASN A 273 ? 0.5636 0.2809 0.2515 -0.1009 0.0287  -0.0108 279 ASN A ND2 
2039 N N   . VAL A 274 ? 0.5346 0.2537 0.2255 -0.0954 0.0183  -0.0067 280 VAL A N   
2040 C CA  . VAL A 274 ? 0.5019 0.2241 0.1979 -0.0913 0.0187  -0.0065 280 VAL A CA  
2041 C C   . VAL A 274 ? 0.5277 0.2499 0.2239 -0.0902 0.0146  -0.0050 280 VAL A C   
2042 O O   . VAL A 274 ? 0.4730 0.1929 0.1657 -0.0924 0.0129  -0.0046 280 VAL A O   
2043 C CB  . VAL A 274 ? 0.5013 0.2239 0.1984 -0.0908 0.0222  -0.0078 280 VAL A CB  
2044 C CG1 . VAL A 274 ? 0.5051 0.2307 0.2073 -0.0866 0.0224  -0.0074 280 VAL A CG1 
2045 C CG2 . VAL A 274 ? 0.5746 0.2974 0.2721 -0.0918 0.0263  -0.0093 280 VAL A CG2 
2046 N N   . TYR A 275 ? 0.4857 0.2106 0.1861 -0.0868 0.0131  -0.0042 281 TYR A N   
2047 C CA  . TYR A 275 ? 0.4704 0.1958 0.1717 -0.0854 0.0091  -0.0028 281 TYR A CA  
2048 C C   . TYR A 275 ? 0.4467 0.1753 0.1532 -0.0813 0.0099  -0.0024 281 TYR A C   
2049 O O   . TYR A 275 ? 0.4142 0.1450 0.1242 -0.0789 0.0128  -0.0031 281 TYR A O   
2050 C CB  . TYR A 275 ? 0.4452 0.1717 0.1476 -0.0850 0.0061  -0.0015 281 TYR A CB  
2051 C CG  . TYR A 275 ? 0.5020 0.2252 0.1991 -0.0891 0.0051  -0.0016 281 TYR A CG  
2052 C CD1 . TYR A 275 ? 0.5159 0.2383 0.2115 -0.0909 0.0079  -0.0027 281 TYR A CD1 
2053 C CD2 . TYR A 275 ? 0.5024 0.2239 0.1967 -0.0912 0.0014  -0.0005 281 TYR A CD2 
2054 C CE1 . TYR A 275 ? 0.5050 0.2247 0.1959 -0.0946 0.0070  -0.0026 281 TYR A CE1 
2055 C CE2 . TYR A 275 ? 0.5192 0.2382 0.2092 -0.0948 0.0005  -0.0004 281 TYR A CE2 
2056 C CZ  . TYR A 275 ? 0.5540 0.2720 0.2422 -0.0965 0.0033  -0.0014 281 TYR A CZ  
2057 O OH  . TYR A 275 ? 0.5648 0.2801 0.2484 -0.1002 0.0023  -0.0013 281 TYR A OH  
2058 N N   . ALA A 276 ? 0.4599 0.1899 0.1682 -0.0801 0.0075  -0.0009 282 ALA A N   
2059 C CA  . ALA A 276 ? 0.4080 0.1433 0.1237 -0.0756 0.0075  0.0007  282 ALA A CA  
2060 C C   . ALA A 276 ? 0.4228 0.1620 0.1432 -0.0735 0.0034  0.0034  282 ALA A C   
2061 O O   . ALA A 276 ? 0.4571 0.1942 0.1743 -0.0759 0.0004  0.0041  282 ALA A O   
2062 C CB  . ALA A 276 ? 0.4395 0.1733 0.1539 -0.0757 0.0088  0.0001  282 ALA A CB  
2063 N N   . ILE A 277 ? 0.3939 0.1389 0.1222 -0.0691 0.0033  0.0050  283 ILE A N   
2064 C CA  . ILE A 277 ? 0.3746 0.1241 0.1083 -0.0668 -0.0003 0.0075  283 ILE A CA  
2065 C C   . ILE A 277 ? 0.3880 0.1433 0.1298 -0.0621 0.0000  0.0092  283 ILE A C   
2066 O O   . ILE A 277 ? 0.3855 0.1423 0.1299 -0.0600 0.0031  0.0085  283 ILE A O   
2067 C CB  . ILE A 277 ? 0.3821 0.1331 0.1173 -0.0664 -0.0010 0.0079  283 ILE A CB  
2068 C CG1 . ILE A 277 ? 0.3643 0.1185 0.1039 -0.0634 0.0020  0.0074  283 ILE A CG1 
2069 C CG2 . ILE A 277 ? 0.3791 0.1245 0.1064 -0.0712 -0.0012 0.0063  283 ILE A CG2 
2070 C CD1 . ILE A 277 ? 0.3608 0.1177 0.1034 -0.0622 0.0009  0.0082  283 ILE A CD1 
2071 N N   . GLY A 278 ? 0.3940 0.1526 0.1399 -0.0605 -0.0033 0.0115  284 GLY A N   
2072 C CA  . GLY A 278 ? 0.3985 0.1632 0.1527 -0.0560 -0.0033 0.0134  284 GLY A CA  
2073 C C   . GLY A 278 ? 0.4350 0.1989 0.1890 -0.0557 -0.0019 0.0132  284 GLY A C   
2074 O O   . GLY A 278 ? 0.4261 0.1853 0.1741 -0.0589 -0.0023 0.0123  284 GLY A O   
2075 N N   . ASP A 279 ? 0.3785 0.1471 0.1392 -0.0517 -0.0001 0.0141  285 ASP A N   
2076 C CA  . ASP A 279 ? 0.3959 0.1647 0.1579 -0.0508 0.0009  0.0145  285 ASP A CA  
2077 C C   . ASP A 279 ? 0.4806 0.2433 0.2351 -0.0542 0.0036  0.0118  285 ASP A C   
2078 O O   . ASP A 279 ? 0.4885 0.2492 0.2409 -0.0553 0.0034  0.0119  285 ASP A O   
2079 C CB  . ASP A 279 ? 0.4133 0.1882 0.1839 -0.0461 0.0026  0.0158  285 ASP A CB  
2080 C CG  . ASP A 279 ? 0.4309 0.2123 0.2095 -0.0426 -0.0002 0.0187  285 ASP A CG  
2081 O OD1 . ASP A 279 ? 0.4146 0.1960 0.1924 -0.0438 -0.0034 0.0197  285 ASP A OD1 
2082 O OD2 . ASP A 279 ? 0.3998 0.1865 0.1859 -0.0387 0.0009  0.0201  285 ASP A OD2 
2083 N N   . CYS A 280 ? 0.4594 0.2192 0.2100 -0.0558 0.0062  0.0095  286 CYS A N   
2084 C CA  . CYS A 280 ? 0.4947 0.2489 0.2383 -0.0590 0.0091  0.0069  286 CYS A CA  
2085 C C   . CYS A 280 ? 0.5181 0.2664 0.2533 -0.0638 0.0075  0.0058  286 CYS A C   
2086 O O   . CYS A 280 ? 0.5402 0.2836 0.2691 -0.0667 0.0097  0.0036  286 CYS A O   
2087 C CB  . CYS A 280 ? 0.4357 0.1890 0.1783 -0.0590 0.0128  0.0047  286 CYS A CB  
2088 S SG  . CYS A 280 ? 0.4666 0.2170 0.2044 -0.0619 0.0121  0.0036  286 CYS A SG  
2089 N N   . ALA A 281 ? 0.5054 0.2539 0.2402 -0.0646 0.0037  0.0072  287 ALA A N   
2090 C CA  . ALA A 281 ? 0.5557 0.2989 0.2830 -0.0691 0.0018  0.0064  287 ALA A CA  
2091 C C   . ALA A 281 ? 0.6354 0.3785 0.3627 -0.0692 -0.0003 0.0077  287 ALA A C   
2092 O O   . ALA A 281 ? 0.6019 0.3496 0.3355 -0.0662 -0.0025 0.0101  287 ALA A O   
2093 C CB  . ALA A 281 ? 0.5015 0.2448 0.2280 -0.0703 -0.0011 0.0072  287 ALA A CB  
2094 N N   . ASP A 282 ? 0.7264 0.4640 0.4465 -0.0728 0.0004  0.0060  288 ASP A N   
2095 C CA  . ASP A 282 ? 0.6948 0.4313 0.4139 -0.0735 -0.0016 0.0070  288 ASP A CA  
2096 C C   . ASP A 282 ? 0.7941 0.5304 0.5123 -0.0749 -0.0059 0.0084  288 ASP A C   
2097 O O   . ASP A 282 ? 0.8051 0.5366 0.5167 -0.0786 -0.0073 0.0076  288 ASP A O   
2098 C CB  . ASP A 282 ? 0.6992 0.4298 0.4106 -0.0771 0.0005  0.0046  288 ASP A CB  
2099 C CG  . ASP A 282 ? 0.8702 0.6000 0.5809 -0.0776 -0.0012 0.0056  288 ASP A CG  
2100 O OD1 . ASP A 282 ? 0.8228 0.5571 0.5402 -0.0741 -0.0019 0.0076  288 ASP A OD1 
2101 O OD2 . ASP A 282 ? 0.8484 0.5730 0.5518 -0.0815 -0.0020 0.0044  288 ASP A OD2 
2102 N N   . VAL A 283 ? 0.8228 0.5643 0.5477 -0.0719 -0.0081 0.0106  289 VAL A N   
2103 C CA  . VAL A 283 ? 0.8547 0.5965 0.5795 -0.0730 -0.0122 0.0120  289 VAL A CA  
2104 C C   . VAL A 283 ? 0.9375 0.6791 0.6625 -0.0732 -0.0143 0.0132  289 VAL A C   
2105 O O   . VAL A 283 ? 0.9926 0.7319 0.7143 -0.0757 -0.0173 0.0135  289 VAL A O   
2106 C CB  . VAL A 283 ? 0.8263 0.5741 0.5587 -0.0695 -0.0137 0.0139  289 VAL A CB  
2107 N N   . ARG A 284 ? 0.9019 0.6459 0.6310 -0.0706 -0.0128 0.0139  290 ARG A N   
2108 C CA  . ARG A 284 ? 0.9956 0.7410 0.7272 -0.0698 -0.0148 0.0156  290 ARG A CA  
2109 C C   . ARG A 284 ? 1.0063 0.7574 0.7453 -0.0670 -0.0180 0.0183  290 ARG A C   
2110 O O   . ARG A 284 ? 1.0143 0.7679 0.7573 -0.0654 -0.0196 0.0202  290 ARG A O   
2111 C CB  . ARG A 284 ? 0.9806 0.7200 0.7041 -0.0741 -0.0162 0.0145  290 ARG A CB  
2112 N N   . THR A 285 ? 0.9777 0.7306 0.7183 -0.0665 -0.0189 0.0185  291 THR A N   
2113 C CA  . THR A 285 ? 0.9623 0.7213 0.7107 -0.0633 -0.0212 0.0209  291 THR A CA  
2114 C C   . THR A 285 ? 0.9128 0.6777 0.6695 -0.0587 -0.0190 0.0222  291 THR A C   
2115 O O   . THR A 285 ? 0.8883 0.6521 0.6441 -0.0582 -0.0157 0.0209  291 THR A O   
2116 C CB  . THR A 285 ? 0.8970 0.6558 0.6443 -0.0644 -0.0223 0.0206  291 THR A CB  
2117 N N   . PRO A 286 ? 0.9209 0.6920 0.6858 -0.0553 -0.0206 0.0246  292 PRO A N   
2118 C CA  . PRO A 286 ? 0.8137 0.5906 0.5865 -0.0509 -0.0185 0.0258  292 PRO A CA  
2119 C C   . PRO A 286 ? 0.6738 0.4512 0.4466 -0.0501 -0.0162 0.0245  292 PRO A C   
2120 O O   . PRO A 286 ? 0.6712 0.4460 0.4398 -0.0522 -0.0169 0.0233  292 PRO A O   
2121 C CB  . PRO A 286 ? 0.7454 0.5286 0.5261 -0.0480 -0.0212 0.0285  292 PRO A CB  
2122 C CG  . PRO A 286 ? 0.7600 0.5408 0.5367 -0.0508 -0.0241 0.0282  292 PRO A CG  
2123 C CD  . PRO A 286 ? 0.8791 0.6526 0.6466 -0.0553 -0.0243 0.0263  292 PRO A CD  
2124 N N   . LYS A 287 ? 0.5866 0.3671 0.3641 -0.0470 -0.0133 0.0246  293 LYS A N   
2125 C CA  . LYS A 287 ? 0.5095 0.2905 0.2871 -0.0461 -0.0108 0.0234  293 LYS A CA  
2126 C C   . LYS A 287 ? 0.4253 0.2126 0.2104 -0.0428 -0.0122 0.0252  293 LYS A C   
2127 O O   . LYS A 287 ? 0.4245 0.2177 0.2175 -0.0390 -0.0121 0.0272  293 LYS A O   
2128 C CB  . LYS A 287 ? 0.5361 0.3172 0.3149 -0.0446 -0.0071 0.0225  293 LYS A CB  
2129 C CG  . LYS A 287 ? 0.5840 0.3589 0.3555 -0.0479 -0.0056 0.0206  293 LYS A CG  
2130 C CD  . LYS A 287 ? 0.6222 0.3907 0.3844 -0.0526 -0.0064 0.0185  293 LYS A CD  
2131 N N   . MET A 288 ? 0.4056 0.1919 0.1884 -0.0442 -0.0134 0.0246  294 MET A N   
2132 C CA  . MET A 288 ? 0.3501 0.1418 0.1390 -0.0417 -0.0153 0.0264  294 MET A CA  
2133 C C   . MET A 288 ? 0.3400 0.1312 0.1276 -0.0418 -0.0141 0.0251  294 MET A C   
2134 O O   . MET A 288 ? 0.3459 0.1314 0.1262 -0.0452 -0.0134 0.0230  294 MET A O   
2135 C CB  . MET A 288 ? 0.3982 0.1891 0.1857 -0.0436 -0.0191 0.0274  294 MET A CB  
2136 C CG  . MET A 288 ? 0.4211 0.2133 0.2108 -0.0433 -0.0208 0.0289  294 MET A CG  
2137 S SD  . MET A 288 ? 0.5260 0.3273 0.3275 -0.0377 -0.0205 0.0318  294 MET A SD  
2138 C CE  . MET A 288 ? 0.8023 0.6044 0.6051 -0.0384 -0.0239 0.0337  294 MET A CE  
2139 N N   . ALA A 289 ? 0.1782 0.1842 0.1430 -0.0509 -0.0444 0.0377  295 ALA A N   
2140 C CA  . ALA A 289 ? 0.1987 0.2010 0.1607 -0.0510 -0.0454 0.0371  295 ALA A CA  
2141 C C   . ALA A 289 ? 0.1971 0.1953 0.1592 -0.0523 -0.0496 0.0393  295 ALA A C   
2142 O O   . ALA A 289 ? 0.1537 0.1484 0.1135 -0.0542 -0.0503 0.0395  295 ALA A O   
2143 C CB  . ALA A 289 ? 0.1780 0.1813 0.1395 -0.0476 -0.0451 0.0358  295 ALA A CB  
2144 N N   . TYR A 290 ? 0.2140 0.2126 0.1793 -0.0514 -0.0526 0.0411  296 TYR A N   
2145 C CA  . TYR A 290 ? 0.2075 0.2021 0.1734 -0.0524 -0.0567 0.0431  296 TYR A CA  
2146 C C   . TYR A 290 ? 0.2397 0.2320 0.2045 -0.0558 -0.0571 0.0442  296 TYR A C   
2147 O O   . TYR A 290 ? 0.2498 0.2380 0.2133 -0.0573 -0.0596 0.0453  296 TYR A O   
2148 C CB  . TYR A 290 ? 0.2479 0.2436 0.2184 -0.0504 -0.0598 0.0448  296 TYR A CB  
2149 C CG  . TYR A 290 ? 0.2291 0.2266 0.2030 -0.0515 -0.0606 0.0464  296 TYR A CG  
2150 C CD1 . TYR A 290 ? 0.2986 0.2929 0.2734 -0.0535 -0.0636 0.0483  296 TYR A CD1 
2151 C CD2 . TYR A 290 ? 0.2347 0.2369 0.2110 -0.0504 -0.0584 0.0461  296 TYR A CD2 
2152 C CE1 . TYR A 290 ? 0.2806 0.2763 0.2585 -0.0543 -0.0644 0.0498  296 TYR A CE1 
2153 C CE2 . TYR A 290 ? 0.2165 0.2202 0.1961 -0.0513 -0.0592 0.0476  296 TYR A CE2 
2154 C CZ  . TYR A 290 ? 0.2384 0.2388 0.2187 -0.0532 -0.0623 0.0494  296 TYR A CZ  
2155 O OH  . TYR A 290 ? 0.2414 0.2429 0.2247 -0.0540 -0.0632 0.0509  296 TYR A OH  
2156 N N   . LEU A 291 ? 0.1838 0.1785 0.1489 -0.0569 -0.0548 0.0441  297 LEU A N   
2157 C CA  . LEU A 291 ? 0.2335 0.2261 0.1972 -0.0599 -0.0550 0.0450  297 LEU A CA  
2158 C C   . LEU A 291 ? 0.2242 0.2149 0.1843 -0.0617 -0.0529 0.0440  297 LEU A C   
2159 O O   . LEU A 291 ? 0.2132 0.2004 0.1715 -0.0646 -0.0546 0.0455  297 LEU A O   
2160 C CB  . LEU A 291 ? 0.2334 0.2290 0.1985 -0.0604 -0.0531 0.0451  297 LEU A CB  
2161 C CG  . LEU A 291 ? 0.2993 0.2962 0.2684 -0.0595 -0.0557 0.0468  297 LEU A CG  
2162 C CD1 . LEU A 291 ? 0.2964 0.2964 0.2665 -0.0599 -0.0534 0.0466  297 LEU A CD1 
2163 C CD2 . LEU A 291 ? 0.2610 0.2539 0.2306 -0.0609 -0.0597 0.0490  297 LEU A CD2 
2164 N N   . ALA A 292 ? 0.2025 0.1952 0.1614 -0.0610 -0.0499 0.0422  298 ALA A N   
2165 C CA  . ALA A 292 ? 0.1884 0.1791 0.1442 -0.0637 -0.0487 0.0419  298 ALA A CA  
2166 C C   . ALA A 292 ? 0.1954 0.1818 0.1499 -0.0637 -0.0515 0.0426  298 ALA A C   
2167 O O   . ALA A 292 ? 0.2157 0.1990 0.1679 -0.0670 -0.0522 0.0437  298 ALA A O   
2168 C CB  . ALA A 292 ? 0.1856 0.1790 0.1409 -0.0622 -0.0453 0.0397  298 ALA A CB  
2169 N N   . GLY A 293 ? 0.1926 0.1787 0.1483 -0.0604 -0.0534 0.0420  299 GLY A N   
2170 C CA  . GLY A 293 ? 0.1877 0.1694 0.1422 -0.0609 -0.0566 0.0431  299 GLY A CA  
2171 C C   . GLY A 293 ? 0.2680 0.2466 0.2228 -0.0633 -0.0596 0.0454  299 GLY A C   
2172 O O   . GLY A 293 ? 0.2700 0.2450 0.2229 -0.0652 -0.0610 0.0462  299 GLY A O   
2173 N N   . LEU A 294 ? 0.2740 0.2538 0.2312 -0.0632 -0.0609 0.0465  300 LEU A N   
2174 C CA  . LEU A 294 ? 0.3012 0.2781 0.2587 -0.0654 -0.0637 0.0487  300 LEU A CA  
2175 C C   . LEU A 294 ? 0.2625 0.2384 0.2174 -0.0687 -0.0622 0.0491  300 LEU A C   
2176 O O   . LEU A 294 ? 0.3078 0.2799 0.2612 -0.0710 -0.0644 0.0506  300 LEU A O   
2177 C CB  . LEU A 294 ? 0.2947 0.2734 0.2556 -0.0647 -0.0652 0.0498  300 LEU A CB  
2178 C CG  . LEU A 294 ? 0.3835 0.3630 0.3479 -0.0620 -0.0677 0.0503  300 LEU A CG  
2179 C CD1 . LEU A 294 ? 0.4295 0.4105 0.3977 -0.0619 -0.0694 0.0518  300 LEU A CD1 
2180 C CD2 . LEU A 294 ? 0.4063 0.3817 0.3706 -0.0618 -0.0712 0.0511  300 LEU A CD2 
2181 N N   . HIS A 295 ? 0.2406 0.2193 0.1948 -0.0698 -0.0590 0.0484  301 HIS A N   
2182 C CA  . HIS A 295 ? 0.2604 0.2379 0.2120 -0.0738 -0.0578 0.0492  301 HIS A CA  
2183 C C   . HIS A 295 ? 0.2627 0.2376 0.2118 -0.0752 -0.0579 0.0491  301 HIS A C   
2184 O O   . HIS A 295 ? 0.2747 0.2481 0.2220 -0.0767 -0.0585 0.0495  301 HIS A O   
2185 C CB  . HIS A 295 ? 0.2550 0.2367 0.2066 -0.0738 -0.0539 0.0477  301 HIS A CB  
2186 C CG  . HIS A 295 ? 0.2926 0.2767 0.2464 -0.0732 -0.0537 0.0482  301 HIS A CG  
2187 N ND1 . HIS A 295 ? 0.2842 0.2726 0.2388 -0.0721 -0.0504 0.0466  301 HIS A ND1 
2188 C CD2 . HIS A 295 ? 0.3375 0.3210 0.2933 -0.0724 -0.0563 0.0495  301 HIS A CD2 
2189 C CE1 . HIS A 295 ? 0.3058 0.2955 0.2624 -0.0718 -0.0511 0.0476  301 HIS A CE1 
2190 N NE2 . HIS A 295 ? 0.3263 0.3133 0.2838 -0.0716 -0.0546 0.0491  301 HIS A NE2 
2191 N N   . ALA A 296 ? 0.2550 0.2302 0.2039 -0.0735 -0.0570 0.0477  302 ALA A N   
2192 C CA  . ALA A 296 ? 0.2446 0.2171 0.1911 -0.0749 -0.0571 0.0476  302 ALA A CA  
2193 C C   . ALA A 296 ? 0.2859 0.2538 0.2318 -0.0760 -0.0609 0.0494  302 ALA A C   
2194 O O   . ALA A 296 ? 0.2641 0.2306 0.2082 -0.0772 -0.0612 0.0496  302 ALA A O   
2195 C CB  . ALA A 296 ? 0.1887 0.1621 0.1352 -0.0723 -0.0558 0.0458  302 ALA A CB  
2196 N N   . ASN A 297 ? 0.3066 0.2740 0.2546 -0.0733 -0.0634 0.0496  303 ASN A N   
2197 C CA  . ASN A 297 ? 0.3300 0.2933 0.2779 -0.0740 -0.0671 0.0512  303 ASN A CA  
2198 C C   . ASN A 297 ? 0.3221 0.2836 0.2690 -0.0775 -0.0683 0.0531  303 ASN A C   
2199 O O   . ASN A 297 ? 0.2926 0.2510 0.2379 -0.0792 -0.0701 0.0541  303 ASN A O   
2200 C CB  . ASN A 297 ? 0.3751 0.3381 0.3256 -0.0712 -0.0698 0.0514  303 ASN A CB  
2201 C CG  . ASN A 297 ? 0.5323 0.4952 0.4831 -0.0686 -0.0702 0.0501  303 ASN A CG  
2202 O OD1 . ASN A 297 ? 0.5249 0.4862 0.4734 -0.0690 -0.0694 0.0494  303 ASN A OD1 
2203 N ND2 . ASN A 297 ? 0.7637 0.7281 0.7171 -0.0659 -0.0715 0.0499  303 ASN A ND2 
2204 N N   . ILE A 298 ? 0.2903 0.2543 0.2381 -0.0780 -0.0671 0.0534  304 ILE A N   
2205 C CA  . ILE A 298 ? 0.3128 0.2765 0.2596 -0.0796 -0.0677 0.0542  304 ILE A CA  
2206 C C   . ILE A 298 ? 0.3238 0.2884 0.2679 -0.0807 -0.0655 0.0531  304 ILE A C   
2207 O O   . ILE A 298 ? 0.3368 0.2992 0.2793 -0.0823 -0.0670 0.0540  304 ILE A O   
2208 C CB  . ILE A 298 ? 0.3687 0.3350 0.3171 -0.0793 -0.0669 0.0544  304 ILE A CB  
2209 C CG1 . ILE A 298 ? 0.3805 0.3459 0.3320 -0.0778 -0.0698 0.0555  304 ILE A CG1 
2210 C CG2 . ILE A 298 ? 0.3608 0.3274 0.3075 -0.0809 -0.0666 0.0546  304 ILE A CG2 
2211 C CD1 . ILE A 298 ? 0.3921 0.3609 0.3458 -0.0765 -0.0688 0.0553  304 ILE A CD1 
2212 N N   . ALA A 299 ? 0.3035 0.2713 0.2473 -0.0799 -0.0620 0.0512  305 ALA A N   
2213 C CA  . ALA A 299 ? 0.2591 0.2282 0.2009 -0.0807 -0.0597 0.0501  305 ALA A CA  
2214 C C   . ALA A 299 ? 0.2955 0.2616 0.2357 -0.0816 -0.0612 0.0505  305 ALA A C   
2215 O O   . ALA A 299 ? 0.2757 0.2410 0.2143 -0.0831 -0.0616 0.0509  305 ALA A O   
2216 C CB  . ALA A 299 ? 0.3082 0.2812 0.2504 -0.0794 -0.0558 0.0479  305 ALA A CB  
2217 N N   . VAL A 300 ? 0.2441 0.2084 0.1847 -0.0806 -0.0622 0.0505  306 VAL A N   
2218 C CA  . VAL A 300 ? 0.2696 0.2310 0.2088 -0.0814 -0.0637 0.0509  306 VAL A CA  
2219 C C   . VAL A 300 ? 0.2905 0.2484 0.2292 -0.0828 -0.0672 0.0529  306 VAL A C   
2220 O O   . VAL A 300 ? 0.3062 0.2628 0.2434 -0.0842 -0.0679 0.0533  306 VAL A O   
2221 C CB  . VAL A 300 ? 0.2765 0.2362 0.2160 -0.0800 -0.0643 0.0506  306 VAL A CB  
2222 C CG1 . VAL A 300 ? 0.2676 0.2234 0.2059 -0.0807 -0.0667 0.0514  306 VAL A CG1 
2223 C CG2 . VAL A 300 ? 0.2168 0.1798 0.1563 -0.0789 -0.0606 0.0486  306 VAL A CG2 
2224 N N   . ALA A 301 ? 0.2962 0.2528 0.2365 -0.0825 -0.0694 0.0540  307 ALA A N   
2225 C CA  . ALA A 301 ? 0.3348 0.2881 0.2750 -0.0837 -0.0730 0.0559  307 ALA A CA  
2226 C C   . ALA A 301 ? 0.3672 0.3211 0.3058 -0.0855 -0.0726 0.0563  307 ALA A C   
2227 O O   . ALA A 301 ? 0.3346 0.2860 0.2720 -0.0869 -0.0747 0.0573  307 ALA A O   
2228 C CB  . ALA A 301 ? 0.3750 0.3273 0.3177 -0.0829 -0.0753 0.0569  307 ALA A CB  
2229 N N   . ASN A 302 ? 0.3218 0.2790 0.2603 -0.0855 -0.0701 0.0554  308 ASN A N   
2230 C CA  . ASN A 302 ? 0.3390 0.2964 0.2759 -0.0873 -0.0702 0.0559  308 ASN A CA  
2231 C C   . ASN A 302 ? 0.3682 0.3266 0.3032 -0.0882 -0.0683 0.0549  308 ASN A C   
2232 O O   . ASN A 302 ? 0.3945 0.3520 0.3279 -0.0900 -0.0693 0.0556  308 ASN A O   
2233 C CB  . ASN A 302 ? 0.4112 0.3713 0.3485 -0.0873 -0.0686 0.0554  308 ASN A CB  
2234 C CG  . ASN A 302 ? 0.4137 0.3730 0.3530 -0.0865 -0.0704 0.0565  308 ASN A CG  
2235 O OD1 . ASN A 302 ? 0.4299 0.3860 0.3700 -0.0867 -0.0737 0.0580  308 ASN A OD1 
2236 N ND2 . ASN A 302 ? 0.3980 0.3603 0.3384 -0.0856 -0.0685 0.0557  308 ASN A ND2 
2237 N N   . ILE A 303 ? 0.3147 0.2749 0.2499 -0.0871 -0.0659 0.0534  309 ILE A N   
2238 C CA  . ILE A 303 ? 0.3470 0.3075 0.2807 -0.0880 -0.0649 0.0529  309 ILE A CA  
2239 C C   . ILE A 303 ? 0.3708 0.3274 0.3035 -0.0892 -0.0682 0.0544  309 ILE A C   
2240 O O   . ILE A 303 ? 0.4176 0.3736 0.3489 -0.0909 -0.0689 0.0550  309 ILE A O   
2241 C CB  . ILE A 303 ? 0.3353 0.2978 0.2695 -0.0865 -0.0622 0.0511  309 ILE A CB  
2242 C CG1 . ILE A 303 ? 0.3089 0.2755 0.2440 -0.0854 -0.0588 0.0494  309 ILE A CG1 
2243 C CG2 . ILE A 303 ? 0.3124 0.2748 0.2454 -0.0874 -0.0618 0.0508  309 ILE A CG2 
2244 C CD1 . ILE A 303 ? 0.2850 0.2537 0.2208 -0.0838 -0.0561 0.0477  309 ILE A CD1 
2245 N N   . VAL A 304 ? 0.3319 0.2859 0.2656 -0.0883 -0.0704 0.0552  310 VAL A N   
2246 C CA  . VAL A 304 ? 0.3315 0.2816 0.2646 -0.0893 -0.0736 0.0566  310 VAL A CA  
2247 C C   . VAL A 304 ? 0.3937 0.3419 0.3263 -0.0909 -0.0762 0.0582  310 VAL A C   
2248 O O   . VAL A 304 ? 0.3996 0.3462 0.3308 -0.0926 -0.0777 0.0591  310 VAL A O   
2249 C CB  . VAL A 304 ? 0.3668 0.3143 0.3012 -0.0879 -0.0755 0.0569  310 VAL A CB  
2250 C CG1 . VAL A 304 ? 0.4025 0.3458 0.3365 -0.0888 -0.0791 0.0585  310 VAL A CG1 
2251 C CG2 . VAL A 304 ? 0.3474 0.2961 0.2818 -0.0866 -0.0733 0.0555  310 VAL A CG2 
2252 N N   . ASN A 305 ? 0.3783 0.3266 0.3121 -0.0904 -0.0769 0.0587  311 ASN A N   
2253 C CA  . ASN A 305 ? 0.4257 0.3722 0.3590 -0.0918 -0.0793 0.0602  311 ASN A CA  
2254 C C   . ASN A 305 ? 0.4651 0.4128 0.3962 -0.0937 -0.0783 0.0601  311 ASN A C   
2255 O O   . ASN A 305 ? 0.4877 0.4331 0.4175 -0.0954 -0.0807 0.0614  311 ASN A O   
2256 C CB  . ASN A 305 ? 0.4230 0.3702 0.3580 -0.0910 -0.0796 0.0605  311 ASN A CB  
2257 C CG  . ASN A 305 ? 0.5180 0.4629 0.4554 -0.0897 -0.0822 0.0613  311 ASN A CG  
2258 O OD1 . ASN A 305 ? 0.5474 0.4893 0.4848 -0.0898 -0.0846 0.0621  311 ASN A OD1 
2259 N ND2 . ASN A 305 ? 0.5208 0.4670 0.4601 -0.0885 -0.0819 0.0612  311 ASN A ND2 
2260 N N   . SER A 306 ? 0.3998 0.3511 0.3305 -0.0934 -0.0749 0.0586  312 SER A N   
2261 C CA  . SER A 306 ? 0.4557 0.4082 0.3844 -0.0951 -0.0739 0.0584  312 SER A CA  
2262 C C   . SER A 306 ? 0.5062 0.4576 0.4334 -0.0965 -0.0747 0.0588  312 SER A C   
2263 O O   . SER A 306 ? 0.5499 0.5004 0.4752 -0.0985 -0.0758 0.0596  312 SER A O   
2264 C CB  . SER A 306 ? 0.4308 0.3875 0.3598 -0.0943 -0.0701 0.0566  312 SER A CB  
2265 O OG  . SER A 306 ? 0.4577 0.4161 0.3868 -0.0936 -0.0680 0.0552  312 SER A OG  
2266 N N   . VAL A 307 ? 0.4252 0.3763 0.3530 -0.0956 -0.0743 0.0583  313 VAL A N   
2267 C CA  . VAL A 307 ? 0.4838 0.4336 0.4103 -0.0969 -0.0753 0.0588  313 VAL A CA  
2268 C C   . VAL A 307 ? 0.4867 0.4325 0.4128 -0.0981 -0.0793 0.0608  313 VAL A C   
2269 O O   . VAL A 307 ? 0.4714 0.4159 0.3959 -0.0999 -0.0807 0.0617  313 VAL A O   
2270 C CB  . VAL A 307 ? 0.4740 0.4246 0.4014 -0.0955 -0.0738 0.0577  313 VAL A CB  
2271 C CG1 . VAL A 307 ? 0.4880 0.4369 0.4144 -0.0968 -0.0753 0.0584  313 VAL A CG1 
2272 C CG2 . VAL A 307 ? 0.4506 0.4053 0.3783 -0.0947 -0.0700 0.0558  313 VAL A CG2 
2273 N N   . LYS A 308 ? 0.4863 0.4299 0.4137 -0.0971 -0.0812 0.0615  314 LYS A N   
2274 C CA  . LYS A 308 ? 0.5313 0.4710 0.4586 -0.0981 -0.0851 0.0633  314 LYS A CA  
2275 C C   . LYS A 308 ? 0.5800 0.5188 0.5063 -0.0995 -0.0866 0.0644  314 LYS A C   
2276 O O   . LYS A 308 ? 0.5636 0.4991 0.4901 -0.1001 -0.0899 0.0659  314 LYS A O   
2277 C CB  . LYS A 308 ? 0.5207 0.4584 0.4502 -0.0963 -0.0867 0.0636  314 LYS A CB  
2278 C CG  . LYS A 308 ? 0.4910 0.4286 0.4211 -0.0950 -0.0859 0.0627  314 LYS A CG  
2279 C CD  . LYS A 308 ? 0.4892 0.4245 0.4214 -0.0933 -0.0877 0.0630  314 LYS A CD  
2280 C CE  . LYS A 308 ? 0.5295 0.4637 0.4619 -0.0923 -0.0876 0.0624  314 LYS A CE  
2281 N NZ  . LYS A 308 ? 0.5124 0.4439 0.4465 -0.0910 -0.0900 0.0628  314 LYS A NZ  
2282 N N   . GLN A 309 ? 0.5771 0.5184 0.5023 -0.1002 -0.0845 0.0637  315 GLN A N   
2283 C CA  . GLN A 309 ? 0.6186 0.5592 0.5427 -0.1014 -0.0858 0.0647  315 GLN A CA  
2284 C C   . GLN A 309 ? 0.6303 0.5685 0.5562 -0.1005 -0.0882 0.0656  315 GLN A C   
2285 O O   . GLN A 309 ? 0.6176 0.5531 0.5428 -0.1017 -0.0912 0.0671  315 GLN A O   
2286 C CB  . GLN A 309 ? 0.6383 0.5767 0.5598 -0.1040 -0.0879 0.0660  315 GLN A CB  
2287 C CG  . GLN A 309 ? 0.6496 0.5898 0.5693 -0.1052 -0.0864 0.0654  315 GLN A CG  
2288 C CD  . GLN A 309 ? 0.7454 0.6892 0.6642 -0.1055 -0.0832 0.0641  315 GLN A CD  
2289 O OE1 . GLN A 309 ? 0.8444 0.7913 0.7643 -0.1042 -0.0802 0.0624  315 GLN A OE1 
2290 N NE2 . GLN A 309 ? 0.7808 0.7240 0.6975 -0.1072 -0.0840 0.0647  315 GLN A NE2 
2291 N N   . ARG A 310 ? 0.5807 0.5202 0.5090 -0.0984 -0.0871 0.0648  316 ARG A N   
2292 C CA  . ARG A 310 ? 0.5712 0.5091 0.5018 -0.0972 -0.0891 0.0656  316 ARG A CA  
2293 C C   . ARG A 310 ? 0.5966 0.5370 0.5280 -0.0964 -0.0874 0.0650  316 ARG A C   
2294 O O   . ARG A 310 ? 0.5890 0.5325 0.5195 -0.0964 -0.0843 0.0637  316 ARG A O   
2295 C CB  . ARG A 310 ? 0.6031 0.5404 0.5358 -0.0953 -0.0894 0.0652  316 ARG A CB  
2296 C CG  . ARG A 310 ? 0.5833 0.5175 0.5156 -0.0959 -0.0918 0.0660  316 ARG A CG  
2297 N N   . PRO A 311 ? 0.6205 0.5595 0.5537 -0.0958 -0.0895 0.0659  317 PRO A N   
2298 C CA  . PRO A 311 ? 0.5991 0.5405 0.5334 -0.0951 -0.0880 0.0654  317 PRO A CA  
2299 C C   . PRO A 311 ? 0.5337 0.4780 0.4702 -0.0929 -0.0854 0.0641  317 PRO A C   
2300 O O   . PRO A 311 ? 0.5101 0.4536 0.4482 -0.0916 -0.0860 0.0640  317 PRO A O   
2301 C CB  . PRO A 311 ? 0.6622 0.6007 0.5981 -0.0952 -0.0916 0.0671  317 PRO A CB  
2302 C CG  . PRO A 311 ? 0.6913 0.6259 0.6265 -0.0962 -0.0948 0.0684  317 PRO A CG  
2303 C CD  . PRO A 311 ? 0.6242 0.5594 0.5588 -0.0959 -0.0934 0.0675  317 PRO A CD  
2304 N N   . LEU A 312 ? 0.4959 0.4434 0.4324 -0.0924 -0.0826 0.0630  318 LEU A N   
2305 C CA  . LEU A 312 ? 0.4548 0.4056 0.3929 -0.0905 -0.0796 0.0615  318 LEU A CA  
2306 C C   . LEU A 312 ? 0.5401 0.4911 0.4814 -0.0888 -0.0807 0.0619  318 LEU A C   
2307 O O   . LEU A 312 ? 0.4229 0.3727 0.3653 -0.0891 -0.0829 0.0631  318 LEU A O   
2308 C CB  . LEU A 312 ? 0.4423 0.3967 0.3791 -0.0906 -0.0761 0.0600  318 LEU A CB  
2309 C CG  . LEU A 312 ? 0.4130 0.3675 0.3469 -0.0922 -0.0750 0.0595  318 LEU A CG  
2310 C CD1 . LEU A 312 ? 0.3685 0.3268 0.3017 -0.0921 -0.0713 0.0578  318 LEU A CD1 
2311 C CD2 . LEU A 312 ? 0.4122 0.3658 0.3459 -0.0921 -0.0751 0.0592  318 LEU A CD2 
2312 N N   . GLN A 313 ? 0.4428 0.3953 0.3857 -0.0871 -0.0793 0.0610  319 GLN A N   
2313 C CA  . GLN A 313 ? 0.4896 0.4429 0.4358 -0.0854 -0.0799 0.0612  319 GLN A CA  
2314 C C   . GLN A 313 ? 0.4685 0.4254 0.4153 -0.0849 -0.0774 0.0605  319 GLN A C   
2315 O O   . GLN A 313 ? 0.4089 0.3683 0.3538 -0.0853 -0.0743 0.0591  319 GLN A O   
2316 C CB  . GLN A 313 ? 0.4863 0.4401 0.4338 -0.0838 -0.0791 0.0604  319 GLN A CB  
2317 C CG  . GLN A 313 ? 0.5201 0.4702 0.4672 -0.0841 -0.0816 0.0610  319 GLN A CG  
2318 C CD  . GLN A 313 ? 0.6029 0.5530 0.5517 -0.0820 -0.0816 0.0603  319 GLN A CD  
2319 O OE1 . GLN A 313 ? 0.5789 0.5326 0.5294 -0.0796 -0.0795 0.0590  319 GLN A OE1 
2320 N NE2 . GLN A 313 ? 0.5930 0.5397 0.5416 -0.0822 -0.0841 0.0610  319 GLN A NE2 
2321 N N   . ALA A 314 ? 0.5070 0.4641 0.4567 -0.0840 -0.0788 0.0613  320 ALA A N   
2322 C CA  . ALA A 314 ? 0.4768 0.4369 0.4273 -0.0836 -0.0770 0.0609  320 ALA A CA  
2323 C C   . ALA A 314 ? 0.5078 0.4708 0.4617 -0.0811 -0.0759 0.0603  320 ALA A C   
2324 O O   . ALA A 314 ? 0.5333 0.4961 0.4902 -0.0787 -0.0780 0.0603  320 ALA A O   
2325 C CB  . ALA A 314 ? 0.4976 0.4558 0.4485 -0.0848 -0.0797 0.0625  320 ALA A CB  
2326 N N   . TYR A 315 ? 0.4607 0.4272 0.4145 -0.0808 -0.0726 0.0591  321 TYR A N   
2327 C CA  . TYR A 315 ? 0.5301 0.5006 0.4870 -0.0776 -0.0709 0.0578  321 TYR A CA  
2328 C C   . TYR A 315 ? 0.5228 0.4947 0.4822 -0.0768 -0.0719 0.0585  321 TYR A C   
2329 O O   . TYR A 315 ? 0.5073 0.4794 0.4650 -0.0788 -0.0710 0.0589  321 TYR A O   
2330 C CB  . TYR A 315 ? 0.4949 0.4685 0.4504 -0.0778 -0.0668 0.0561  321 TYR A CB  
2331 C CG  . TYR A 315 ? 0.5049 0.4830 0.4633 -0.0748 -0.0648 0.0548  321 TYR A CG  
2332 C CD1 . TYR A 315 ? 0.5382 0.5176 0.4997 -0.0713 -0.0656 0.0540  321 TYR A CD1 
2333 C CD2 . TYR A 315 ? 0.5129 0.4938 0.4710 -0.0754 -0.0620 0.0542  321 TYR A CD2 
2334 C CE1 . TYR A 315 ? 0.5236 0.5073 0.4880 -0.0685 -0.0638 0.0527  321 TYR A CE1 
2335 C CE2 . TYR A 315 ? 0.5843 0.5694 0.5452 -0.0726 -0.0601 0.0530  321 TYR A CE2 
2336 C CZ  . TYR A 315 ? 0.5613 0.5479 0.5254 -0.0692 -0.0611 0.0522  321 TYR A CZ  
2337 O OH  . TYR A 315 ? 0.5505 0.5413 0.5174 -0.0664 -0.0592 0.0510  321 TYR A OH  
2338 N N   . LYS A 316 ? 0.5200 0.4928 0.4834 -0.0740 -0.0739 0.0586  322 LYS A N   
2339 C CA  . LYS A 316 ? 0.5094 0.4837 0.4760 -0.0731 -0.0750 0.0592  322 LYS A CA  
2340 C C   . LYS A 316 ? 0.5552 0.5337 0.5259 -0.0702 -0.0741 0.0585  322 LYS A C   
2341 O O   . LYS A 316 ? 0.5350 0.5132 0.5088 -0.0688 -0.0763 0.0591  322 LYS A O   
2342 C CB  . LYS A 316 ? 0.5239 0.4949 0.4923 -0.0736 -0.0794 0.0611  322 LYS A CB  
2343 C CG  . LYS A 316 ? 0.5131 0.4844 0.4830 -0.0738 -0.0807 0.0620  322 LYS A CG  
2344 C CD  . LYS A 316 ? 0.5513 0.5226 0.5267 -0.0724 -0.0842 0.0635  322 LYS A CD  
2345 C CE  . LYS A 316 ? 0.6104 0.5835 0.5885 -0.0720 -0.0847 0.0640  322 LYS A CE  
2346 N NZ  . LYS A 316 ? 0.6825 0.6527 0.6574 -0.0740 -0.0857 0.0646  322 LYS A NZ  
2347 N N   . PRO A 317 ? 0.5309 0.5130 0.5020 -0.0695 -0.0711 0.0574  323 PRO A N   
2348 C CA  . PRO A 317 ? 0.5377 0.5238 0.5128 -0.0670 -0.0703 0.0569  323 PRO A CA  
2349 C C   . PRO A 317 ? 0.5104 0.4966 0.4909 -0.0659 -0.0740 0.0587  323 PRO A C   
2350 O O   . PRO A 317 ? 0.4907 0.4744 0.4720 -0.0671 -0.0768 0.0602  323 PRO A O   
2351 C CB  . PRO A 317 ? 0.5226 0.5118 0.4965 -0.0670 -0.0666 0.0557  323 PRO A CB  
2352 C CG  . PRO A 317 ? 0.5634 0.5500 0.5320 -0.0703 -0.0654 0.0558  323 PRO A CG  
2353 C CD  . PRO A 317 ? 0.5423 0.5243 0.5098 -0.0720 -0.0690 0.0574  323 PRO A CD  
2354 N N   . GLY A 318 ? 0.4281 0.4176 0.4130 -0.0636 -0.0739 0.0586  324 GLY A N   
2355 C CA  . GLY A 318 ? 0.3650 0.3559 0.3565 -0.0621 -0.0767 0.0602  324 GLY A CA  
2356 C C   . GLY A 318 ? 0.3552 0.3513 0.3499 -0.0603 -0.0743 0.0595  324 GLY A C   
2357 O O   . GLY A 318 ? 0.2404 0.2383 0.2317 -0.0607 -0.0707 0.0580  324 GLY A O   
2358 N N   . ALA A 319 ? 0.3088 0.3074 0.3105 -0.0582 -0.0761 0.0607  325 ALA A N   
2359 C CA  . ALA A 319 ? 0.3157 0.3194 0.3209 -0.0565 -0.0738 0.0603  325 ALA A CA  
2360 C C   . ALA A 319 ? 0.2940 0.3005 0.2970 -0.0551 -0.0704 0.0584  325 ALA A C   
2361 O O   . ALA A 319 ? 0.3015 0.3060 0.3014 -0.0551 -0.0704 0.0576  325 ALA A O   
2362 C CB  . ALA A 319 ? 0.3579 0.3638 0.3720 -0.0545 -0.0764 0.0622  325 ALA A CB  
2363 N N   . LEU A 320 ? 0.2941 0.3050 0.2986 -0.0540 -0.0676 0.0576  326 LEU A N   
2364 C CA  . LEU A 320 ? 0.3095 0.3233 0.3114 -0.0529 -0.0639 0.0556  326 LEU A CA  
2365 C C   . LEU A 320 ? 0.2627 0.2783 0.2687 -0.0500 -0.0649 0.0560  326 LEU A C   
2366 O O   . LEU A 320 ? 0.2363 0.2545 0.2498 -0.0479 -0.0666 0.0576  326 LEU A O   
2367 C CB  . LEU A 320 ? 0.3176 0.3356 0.3203 -0.0524 -0.0608 0.0549  326 LEU A CB  
2368 C CG  . LEU A 320 ? 0.2870 0.3087 0.2878 -0.0511 -0.0568 0.0529  326 LEU A CG  
2369 C CD1 . LEU A 320 ? 0.2753 0.2941 0.2687 -0.0526 -0.0546 0.0509  326 LEU A CD1 
2370 C CD2 . LEU A 320 ? 0.3324 0.3579 0.3345 -0.0509 -0.0541 0.0526  326 LEU A CD2 
2371 N N   . THR A 321 ? 0.2195 0.2335 0.2210 -0.0498 -0.0640 0.0545  327 THR A N   
2372 C CA  . THR A 321 ? 0.2197 0.2357 0.2237 -0.0468 -0.0640 0.0543  327 THR A CA  
2373 C C   . THR A 321 ? 0.2155 0.2350 0.2164 -0.0459 -0.0597 0.0522  327 THR A C   
2374 O O   . THR A 321 ? 0.1676 0.1854 0.1621 -0.0477 -0.0573 0.0502  327 THR A O   
2375 C CB  . THR A 321 ? 0.2490 0.2606 0.2501 -0.0468 -0.0661 0.0541  327 THR A CB  
2376 O OG1 . THR A 321 ? 0.2688 0.2775 0.2736 -0.0471 -0.0702 0.0562  327 THR A OG1 
2377 C CG2 . THR A 321 ? 0.2114 0.2248 0.2135 -0.0433 -0.0655 0.0535  327 THR A CG2 
2378 N N   . PHE A 322 ? 0.1683 0.1926 0.1741 -0.0428 -0.0587 0.0526  328 PHE A N   
2379 C CA  . PHE A 322 ? 0.1737 0.2017 0.1768 -0.0418 -0.0545 0.0507  328 PHE A CA  
2380 C C   . PHE A 322 ? 0.1616 0.1939 0.1704 -0.0375 -0.0544 0.0517  328 PHE A C   
2381 O O   . PHE A 322 ? 0.1460 0.1819 0.1628 -0.0357 -0.0551 0.0538  328 PHE A O   
2382 C CB  . PHE A 322 ? 0.1883 0.2190 0.1914 -0.0435 -0.0520 0.0503  328 PHE A CB  
2383 C CG  . PHE A 322 ? 0.2381 0.2710 0.2364 -0.0436 -0.0475 0.0477  328 PHE A CG  
2384 C CD1 . PHE A 322 ? 0.2303 0.2678 0.2304 -0.0407 -0.0453 0.0472  328 PHE A CD1 
2385 C CD2 . PHE A 322 ? 0.2771 0.3075 0.2696 -0.0465 -0.0453 0.0460  328 PHE A CD2 
2386 C CE1 . PHE A 322 ? 0.2563 0.2956 0.2520 -0.0409 -0.0411 0.0448  328 PHE A CE1 
2387 C CE2 . PHE A 322 ? 0.3570 0.3893 0.3460 -0.0465 -0.0410 0.0436  328 PHE A CE2 
2388 C CZ  . PHE A 322 ? 0.2728 0.3095 0.2632 -0.0439 -0.0389 0.0428  328 PHE A CZ  
2389 N N   . LEU A 323 ? 0.1284 0.1603 0.1336 -0.0355 -0.0533 0.0504  329 LEU A N   
2390 C CA  . LEU A 323 ? 0.1403 0.1753 0.1502 -0.0306 -0.0530 0.0517  329 LEU A CA  
2391 C C   . LEU A 323 ? 0.1443 0.1833 0.1510 -0.0292 -0.0486 0.0499  329 LEU A C   
2392 O O   . LEU A 323 ? 0.1449 0.1814 0.1437 -0.0309 -0.0467 0.0471  329 LEU A O   
2393 C CB  . LEU A 323 ? 0.1252 0.1556 0.1332 -0.0288 -0.0555 0.0518  329 LEU A CB  
2394 C CG  . LEU A 323 ? 0.1463 0.1725 0.1573 -0.0300 -0.0598 0.0535  329 LEU A CG  
2395 C CD1 . LEU A 323 ? 0.1805 0.2020 0.1891 -0.0281 -0.0620 0.0534  329 LEU A CD1 
2396 C CD2 . LEU A 323 ? 0.1454 0.1752 0.1670 -0.0279 -0.0611 0.0564  329 LEU A CD2 
2397 N N   . LEU A 324 ? 0.1198 0.1649 0.1331 -0.0257 -0.0467 0.0515  330 LEU A N   
2398 C CA  . LEU A 324 ? 0.1327 0.1821 0.1433 -0.0238 -0.0423 0.0501  330 LEU A CA  
2399 C C   . LEU A 324 ? 0.1207 0.1698 0.1341 -0.0175 -0.0396 0.0499  330 LEU A C   
2400 O O   . LEU A 324 ? 0.1378 0.1887 0.1603 -0.0134 -0.0384 0.0514  330 LEU A O   
2401 C CB  . LEU A 324 ? 0.1325 0.1883 0.1484 -0.0241 -0.0397 0.0508  330 LEU A CB  
2402 C CG  . LEU A 324 ? 0.1940 0.2479 0.2066 -0.0295 -0.0399 0.0494  330 LEU A CG  
2403 C CD1 . LEU A 324 ? 0.2095 0.2635 0.2297 -0.0304 -0.0428 0.0518  330 LEU A CD1 
2404 C CD2 . LEU A 324 ? 0.2319 0.2900 0.2419 -0.0302 -0.0353 0.0475  330 LEU A CD2 
2405 N N   . SER A 325 ? 0.1378 0.1839 0.1436 -0.0165 -0.0379 0.0474  331 SER A N   
2406 C CA  . SER A 325 ? 0.1288 0.1740 0.1366 -0.0100 -0.0339 0.0461  331 SER A CA  
2407 C C   . SER A 325 ? 0.1987 0.2495 0.2094 -0.0070 -0.0276 0.0449  331 SER A C   
2408 O O   . SER A 325 ? 0.2281 0.2820 0.2351 -0.0102 -0.0260 0.0439  331 SER A O   
2409 C CB  . SER A 325 ? 0.1931 0.2331 0.1918 -0.0096 -0.0341 0.0438  331 SER A CB  
2410 O OG  . SER A 325 ? 0.3380 0.3797 0.3293 -0.0124 -0.0318 0.0415  331 SER A OG  
2411 N N   . MET A 326 ? 0.1363 0.1883 0.1538 -0.0010 -0.0241 0.0453  332 MET A N   
2412 C CA  . MET A 326 ? 0.1243 0.1815 0.1455 0.0025  -0.0179 0.0444  332 MET A CA  
2413 C C   . MET A 326 ? 0.1185 0.1734 0.1376 0.0088  -0.0138 0.0423  332 MET A C   
2414 O O   . MET A 326 ? 0.1347 0.1906 0.1610 0.0145  -0.0111 0.0433  332 MET A O   
2415 C CB  . MET A 326 ? 0.1662 0.2280 0.1993 0.0042  -0.0173 0.0472  332 MET A CB  
2416 C CG  . MET A 326 ? 0.2075 0.2716 0.2432 -0.0016 -0.0214 0.0493  332 MET A CG  
2417 S SD  . MET A 326 ? 0.3733 0.4440 0.4087 -0.0038 -0.0174 0.0482  332 MET A SD  
2418 C CE  . MET A 326 ? 0.1465 0.2139 0.1684 -0.0102 -0.0203 0.0461  332 MET A CE  
2419 N N   . GLY A 327 ? 0.0980 0.1494 0.1072 0.0078  -0.0136 0.0396  333 GLY A N   
2420 C CA  . GLY A 327 ? 0.0979 0.1454 0.1040 0.0133  -0.0113 0.0377  333 GLY A CA  
2421 C C   . GLY A 327 ? 0.1139 0.1557 0.1208 0.0146  -0.0157 0.0389  333 GLY A C   
2422 O O   . GLY A 327 ? 0.1157 0.1569 0.1264 0.0116  -0.0203 0.0414  333 GLY A O   
2423 N N   . ARG A 328 ? 0.0993 0.1367 0.1024 0.0192  -0.0143 0.0371  334 ARG A N   
2424 C CA  . ARG A 328 ? 0.1057 0.1371 0.1084 0.0202  -0.0187 0.0379  334 ARG A CA  
2425 C C   . ARG A 328 ? 0.1134 0.1454 0.1261 0.0239  -0.0192 0.0408  334 ARG A C   
2426 O O   . ARG A 328 ? 0.1122 0.1398 0.1257 0.0239  -0.0235 0.0421  334 ARG A O   
2427 C CB  . ARG A 328 ? 0.1100 0.1361 0.1056 0.0243  -0.0173 0.0350  334 ARG A CB  
2428 C CG  . ARG A 328 ? 0.1468 0.1736 0.1458 0.0323  -0.0117 0.0342  334 ARG A CG  
2429 C CD  . ARG A 328 ? 0.1628 0.1836 0.1542 0.0362  -0.0110 0.0313  334 ARG A CD  
2430 N NE  . ARG A 328 ? 0.1802 0.2009 0.1628 0.0336  -0.0097 0.0283  334 ARG A NE  
2431 C CZ  . ARG A 328 ? 0.2272 0.2435 0.2018 0.0294  -0.0136 0.0269  334 ARG A CZ  
2432 N NH1 . ARG A 328 ? 0.2174 0.2289 0.1914 0.0273  -0.0192 0.0281  334 ARG A NH1 
2433 N NH2 . ARG A 328 ? 0.1945 0.2112 0.1618 0.0274  -0.0119 0.0243  334 ARG A NH2 
2434 N N   . ASN A 329 ? 0.1040 0.1414 0.1247 0.0271  -0.0150 0.0420  335 ASN A N   
2435 C CA  . ASN A 329 ? 0.1108 0.1490 0.1416 0.0313  -0.0148 0.0447  335 ASN A CA  
2436 C C   . ASN A 329 ? 0.1495 0.1927 0.1891 0.0279  -0.0167 0.0479  335 ASN A C   
2437 O O   . ASN A 329 ? 0.1058 0.1508 0.1549 0.0314  -0.0159 0.0503  335 ASN A O   
2438 C CB  . ASN A 329 ? 0.1156 0.1557 0.1500 0.0390  -0.0083 0.0440  335 ASN A CB  
2439 C CG  . ASN A 329 ? 0.1529 0.1995 0.1894 0.0389  -0.0032 0.0435  335 ASN A CG  
2440 O OD1 . ASN A 329 ? 0.1041 0.1535 0.1382 0.0332  -0.0044 0.0432  335 ASN A OD1 
2441 N ND2 . ASN A 329 ? 0.1659 0.2148 0.2067 0.0454  0.0027  0.0434  335 ASN A ND2 
2442 N N   . ASP A 330 ? 0.1083 0.1535 0.1450 0.0213  -0.0193 0.0479  336 ASP A N   
2443 C CA  . ASP A 330 ? 0.1186 0.1688 0.1635 0.0184  -0.0205 0.0506  336 ASP A CA  
2444 C C   . ASP A 330 ? 0.1221 0.1718 0.1616 0.0106  -0.0255 0.0507  336 ASP A C   
2445 O O   . ASP A 330 ? 0.1146 0.1607 0.1445 0.0076  -0.0272 0.0487  336 ASP A O   
2446 C CB  . ASP A 330 ? 0.1407 0.1974 0.1903 0.0206  -0.0145 0.0504  336 ASP A CB  
2447 C CG  . ASP A 330 ? 0.1951 0.2564 0.2575 0.0222  -0.0141 0.0537  336 ASP A CG  
2448 O OD1 . ASP A 330 ? 0.1739 0.2344 0.2407 0.0193  -0.0192 0.0562  336 ASP A OD1 
2449 O OD2 . ASP A 330 ? 0.1644 0.2302 0.2327 0.0264  -0.0087 0.0539  336 ASP A OD2 
2450 N N   . GLY A 331 ? 0.1531 0.2063 0.1990 0.0074  -0.0277 0.0531  337 GLY A N   
2451 C CA  . GLY A 331 ? 0.1374 0.1903 0.1787 0.0003  -0.0324 0.0535  337 GLY A CA  
2452 C C   . GLY A 331 ? 0.1028 0.1580 0.1528 -0.0019 -0.0361 0.0567  337 GLY A C   
2453 O O   . GLY A 331 ? 0.1241 0.1805 0.1836 0.0019  -0.0356 0.0588  337 GLY A O   
2454 N N   . VAL A 332 ? 0.0983 0.1539 0.1448 -0.0081 -0.0399 0.0572  338 VAL A N   
2455 C CA  . VAL A 332 ? 0.0902 0.1471 0.1437 -0.0108 -0.0443 0.0602  338 VAL A CA  
2456 C C   . VAL A 332 ? 0.1052 0.1595 0.1507 -0.0177 -0.0490 0.0598  338 VAL A C   
2457 O O   . VAL A 332 ? 0.0990 0.1519 0.1349 -0.0202 -0.0480 0.0574  338 VAL A O   
2458 C CB  . VAL A 332 ? 0.1586 0.2220 0.2213 -0.0095 -0.0411 0.0613  338 VAL A CB  
2459 C CG1 . VAL A 332 ? 0.1236 0.1903 0.1807 -0.0127 -0.0386 0.0594  338 VAL A CG1 
2460 C CG2 . VAL A 332 ? 0.1555 0.2194 0.2265 -0.0115 -0.0454 0.0642  338 VAL A CG2 
2461 N N   . GLY A 333 ? 0.1365 0.1879 0.1847 -0.0204 -0.0525 0.0608  339 GLY A N   
2462 C CA  . GLY A 333 ? 0.1224 0.1693 0.1620 -0.0262 -0.0545 0.0590  339 GLY A CA  
2463 C C   . GLY A 333 ? 0.1564 0.2000 0.1997 -0.0283 -0.0583 0.0605  339 GLY A C   
2464 O O   . GLY A 333 ? 0.1526 0.1984 0.2055 -0.0260 -0.0590 0.0627  339 GLY A O   
2465 N N   . GLN A 334 ? 0.1384 0.1765 0.1739 -0.0324 -0.0604 0.0593  340 GLN A N   
2466 C CA  . GLN A 334 ? 0.1868 0.2209 0.2241 -0.0346 -0.0640 0.0606  340 GLN A CA  
2467 C C   . GLN A 334 ? 0.2167 0.2446 0.2467 -0.0368 -0.0663 0.0597  340 GLN A C   
2468 O O   . GLN A 334 ? 0.1726 0.1987 0.1942 -0.0384 -0.0646 0.0575  340 GLN A O   
2469 C CB  . GLN A 334 ? 0.1832 0.2175 0.2197 -0.0378 -0.0637 0.0605  340 GLN A CB  
2470 C CG  . GLN A 334 ? 0.1951 0.2280 0.2220 -0.0409 -0.0611 0.0581  340 GLN A CG  
2471 C CD  . GLN A 334 ? 0.2587 0.2924 0.2859 -0.0429 -0.0603 0.0582  340 GLN A CD  
2472 O OE1 . GLN A 334 ? 0.2676 0.3060 0.2984 -0.0416 -0.0580 0.0583  340 GLN A OE1 
2473 N NE2 . GLN A 334 ? 0.2622 0.2912 0.2858 -0.0457 -0.0624 0.0584  340 GLN A NE2 
2474 N N   . ILE A 335 ? 0.1983 0.2230 0.2318 -0.0366 -0.0699 0.0613  341 ILE A N   
2475 C CA  . ILE A 335 ? 0.2525 0.2712 0.2800 -0.0386 -0.0723 0.0607  341 ILE A CA  
2476 C C   . ILE A 335 ? 0.2761 0.2917 0.3038 -0.0418 -0.0749 0.0618  341 ILE A C   
2477 O O   . ILE A 335 ? 0.3006 0.3170 0.3358 -0.0409 -0.0771 0.0638  341 ILE A O   
2478 C CB  . ILE A 335 ? 0.2570 0.2741 0.2877 -0.0353 -0.0744 0.0616  341 ILE A CB  
2479 C CG1 . ILE A 335 ? 0.2353 0.2544 0.2637 -0.0322 -0.0718 0.0604  341 ILE A CG1 
2480 C CG2 . ILE A 335 ? 0.3062 0.3171 0.3320 -0.0378 -0.0774 0.0614  341 ILE A CG2 
2481 C CD1 . ILE A 335 ? 0.2613 0.2784 0.2925 -0.0281 -0.0734 0.0613  341 ILE A CD1 
2482 N N   . SER A 336 ? 0.2713 0.2833 0.2910 -0.0454 -0.0745 0.0604  342 SER A N   
2483 C CA  . SER A 336 ? 0.3293 0.3384 0.3475 -0.0484 -0.0760 0.0612  342 SER A CA  
2484 C C   . SER A 336 ? 0.3462 0.3582 0.3713 -0.0479 -0.0766 0.0627  342 SER A C   
2485 O O   . SER A 336 ? 0.3331 0.3433 0.3626 -0.0482 -0.0799 0.0645  342 SER A O   
2486 C CB  . SER A 336 ? 0.3877 0.3915 0.4050 -0.0497 -0.0797 0.0622  342 SER A CB  
2487 O OG  . SER A 336 ? 0.4410 0.4454 0.4652 -0.0469 -0.0822 0.0637  342 SER A OG  
2488 N N   . GLY A 337 ? 0.3120 0.3286 0.3384 -0.0471 -0.0736 0.0621  343 GLY A N   
2489 C CA  . GLY A 337 ? 0.3129 0.3317 0.3443 -0.0472 -0.0737 0.0632  343 GLY A CA  
2490 C C   . GLY A 337 ? 0.3217 0.3446 0.3639 -0.0440 -0.0745 0.0651  343 GLY A C   
2491 O O   . GLY A 337 ? 0.3538 0.3789 0.4009 -0.0440 -0.0744 0.0660  343 GLY A O   
2492 N N   . PHE A 338 ? 0.2852 0.3094 0.3319 -0.0411 -0.0750 0.0657  344 PHE A N   
2493 C CA  . PHE A 338 ? 0.3263 0.3551 0.3840 -0.0375 -0.0747 0.0675  344 PHE A CA  
2494 C C   . PHE A 338 ? 0.2702 0.3033 0.3297 -0.0339 -0.0716 0.0669  344 PHE A C   
2495 O O   . PHE A 338 ? 0.2396 0.2711 0.2928 -0.0335 -0.0710 0.0655  344 PHE A O   
2496 C CB  . PHE A 338 ? 0.3624 0.3889 0.4266 -0.0364 -0.0783 0.0695  344 PHE A CB  
2497 C CG  . PHE A 338 ? 0.3807 0.4029 0.4402 -0.0365 -0.0803 0.0691  344 PHE A CG  
2498 C CD1 . PHE A 338 ? 0.3401 0.3636 0.4008 -0.0329 -0.0791 0.0688  344 PHE A CD1 
2499 C CD2 . PHE A 338 ? 0.3241 0.3408 0.3781 -0.0399 -0.0832 0.0690  344 PHE A CD2 
2500 C CE1 . PHE A 338 ? 0.3725 0.3915 0.4286 -0.0330 -0.0811 0.0683  344 PHE A CE1 
2501 C CE2 . PHE A 338 ? 0.3641 0.3767 0.4140 -0.0401 -0.0850 0.0686  344 PHE A CE2 
2502 C CZ  . PHE A 338 ? 0.3864 0.4001 0.4373 -0.0367 -0.0841 0.0682  344 PHE A CZ  
2503 N N   . TYR A 339 ? 0.2514 0.2898 0.3198 -0.0308 -0.0695 0.0681  345 TYR A N   
2504 C CA  . TYR A 339 ? 0.2124 0.2555 0.2837 -0.0267 -0.0658 0.0678  345 TYR A CA  
2505 C C   . TYR A 339 ? 0.2068 0.2484 0.2796 -0.0231 -0.0665 0.0683  345 TYR A C   
2506 O O   . TYR A 339 ? 0.1789 0.2184 0.2571 -0.0217 -0.0689 0.0699  345 TYR A O   
2507 C CB  . TYR A 339 ? 0.2022 0.2506 0.2843 -0.0240 -0.0635 0.0693  345 TYR A CB  
2508 C CG  . TYR A 339 ? 0.2124 0.2661 0.2988 -0.0192 -0.0588 0.0693  345 TYR A CG  
2509 C CD1 . TYR A 339 ? 0.2054 0.2600 0.2986 -0.0139 -0.0575 0.0705  345 TYR A CD1 
2510 C CD2 . TYR A 339 ? 0.2113 0.2690 0.2951 -0.0197 -0.0552 0.0679  345 TYR A CD2 
2511 C CE1 . TYR A 339 ? 0.2121 0.2713 0.3092 -0.0090 -0.0524 0.0704  345 TYR A CE1 
2512 C CE2 . TYR A 339 ? 0.2451 0.3077 0.3331 -0.0151 -0.0505 0.0679  345 TYR A CE2 
2513 C CZ  . TYR A 339 ? 0.2424 0.3056 0.3369 -0.0097 -0.0490 0.0691  345 TYR A CZ  
2514 O OH  . TYR A 339 ? 0.2610 0.3285 0.3589 -0.0048 -0.0435 0.0688  345 TYR A OH  
2515 N N   . VAL A 340 ? 0.1769 0.2193 0.2446 -0.0213 -0.0642 0.0669  346 VAL A N   
2516 C CA  . VAL A 340 ? 0.1735 0.2147 0.2431 -0.0167 -0.0639 0.0674  346 VAL A CA  
2517 C C   . VAL A 340 ? 0.1755 0.2218 0.2483 -0.0119 -0.0590 0.0673  346 VAL A C   
2518 O O   . VAL A 340 ? 0.1752 0.2248 0.2443 -0.0132 -0.0564 0.0661  346 VAL A O   
2519 C CB  . VAL A 340 ? 0.2083 0.2437 0.2677 -0.0186 -0.0662 0.0659  346 VAL A CB  
2520 C CG1 . VAL A 340 ? 0.2102 0.2406 0.2675 -0.0227 -0.0706 0.0662  346 VAL A CG1 
2521 C CG2 . VAL A 340 ? 0.1840 0.2198 0.2337 -0.0213 -0.0643 0.0634  346 VAL A CG2 
2522 N N   . GLY A 341 ? 0.1897 0.2364 0.2692 -0.0061 -0.0573 0.0686  347 GLY A N   
2523 C CA  . GLY A 341 ? 0.1777 0.2292 0.2625 -0.0007 -0.0518 0.0687  347 GLY A CA  
2524 C C   . GLY A 341 ? 0.1820 0.2320 0.2595 0.0023  -0.0489 0.0668  347 GLY A C   
2525 O O   . GLY A 341 ? 0.1850 0.2308 0.2524 -0.0007 -0.0511 0.0650  347 GLY A O   
2526 N N   . ARG A 342 ? 0.1562 0.2087 0.2381 0.0082  -0.0431 0.0662  348 ARG A N   
2527 C CA  . ARG A 342 ? 0.1582 0.2094 0.2323 0.0110  -0.0384 0.0630  348 ARG A CA  
2528 C C   . ARG A 342 ? 0.1614 0.2063 0.2307 0.0137  -0.0398 0.0622  348 ARG A C   
2529 O O   . ARG A 342 ? 0.1364 0.1778 0.1955 0.0127  -0.0396 0.0595  348 ARG A O   
2530 C CB  . ARG A 342 ? 0.1334 0.1895 0.2138 0.0164  -0.0316 0.0629  348 ARG A CB  
2531 C CG  . ARG A 342 ? 0.1827 0.2451 0.2682 0.0135  -0.0305 0.0638  348 ARG A CG  
2532 C CD  . ARG A 342 ? 0.1739 0.2415 0.2696 0.0189  -0.0250 0.0650  348 ARG A CD  
2533 N NE  . ARG A 342 ? 0.1338 0.2023 0.2251 0.0230  -0.0186 0.0624  348 ARG A NE  
2534 C CZ  . ARG A 342 ? 0.1791 0.2520 0.2775 0.0280  -0.0128 0.0630  348 ARG A CZ  
2535 N NH1 . ARG A 342 ? 0.1830 0.2571 0.2898 0.0282  -0.0120 0.0642  348 ARG A NH1 
2536 N NH2 . ARG A 342 ? 0.1651 0.2385 0.2586 0.0316  -0.0072 0.0604  348 ARG A NH2 
2537 N N   . LEU A 343 ? 0.1304 0.1735 0.2068 0.0172  -0.0414 0.0644  349 LEU A N   
2538 C CA  . LEU A 343 ? 0.1589 0.1957 0.2309 0.0195  -0.0434 0.0637  349 LEU A CA  
2539 C C   . LEU A 343 ? 0.1767 0.2089 0.2400 0.0134  -0.0493 0.0631  349 LEU A C   
2540 O O   . LEU A 343 ? 0.1486 0.1761 0.2030 0.0134  -0.0497 0.0609  349 LEU A O   
2541 C CB  . LEU A 343 ? 0.1946 0.2306 0.2763 0.0236  -0.0446 0.0666  349 LEU A CB  
2542 C CG  . LEU A 343 ? 0.2230 0.2521 0.3008 0.0255  -0.0477 0.0663  349 LEU A CG  
2543 C CD1 . LEU A 343 ? 0.2652 0.2913 0.3357 0.0298  -0.0436 0.0633  349 LEU A CD1 
2544 C CD2 . LEU A 343 ? 0.3746 0.4031 0.4613 0.0291  -0.0477 0.0681  349 LEU A CD2 
2545 N N   . MET A 344 ? 0.1309 0.1642 0.1966 0.0081  -0.0539 0.0651  350 MET A N   
2546 C CA  . MET A 344 ? 0.1602 0.1893 0.2180 0.0022  -0.0596 0.0649  350 MET A CA  
2547 C C   . MET A 344 ? 0.1513 0.1799 0.1982 -0.0010 -0.0581 0.0619  350 MET A C   
2548 O O   . MET A 344 ? 0.1389 0.1625 0.1774 -0.0027 -0.0603 0.0605  350 MET A O   
2549 C CB  . MET A 344 ? 0.1832 0.2137 0.2449 -0.0028 -0.0630 0.0664  350 MET A CB  
2550 C CG  . MET A 344 ? 0.2061 0.2317 0.2594 -0.0088 -0.0674 0.0653  350 MET A CG  
2551 S SD  . MET A 344 ? 0.3700 0.3882 0.4200 -0.0071 -0.0706 0.0651  350 MET A SD  
2552 C CE  . MET A 344 ? 0.4307 0.4443 0.4716 -0.0147 -0.0747 0.0637  350 MET A CE  
2553 N N   . VAL A 345 ? 0.1218 0.1555 0.1688 -0.0019 -0.0543 0.0610  351 VAL A N   
2554 C CA  . VAL A 345 ? 0.1216 0.1550 0.1584 -0.0052 -0.0529 0.0583  351 VAL A CA  
2555 C C   . VAL A 345 ? 0.1224 0.1530 0.1536 -0.0009 -0.0492 0.0555  351 VAL A C   
2556 O O   . VAL A 345 ? 0.1234 0.1505 0.1452 -0.0033 -0.0503 0.0535  351 VAL A O   
2557 C CB  . VAL A 345 ? 0.1420 0.1815 0.1803 -0.0072 -0.0500 0.0580  351 VAL A CB  
2558 C CG1 . VAL A 345 ? 0.1188 0.1582 0.1465 -0.0103 -0.0481 0.0551  351 VAL A CG1 
2559 C CG2 . VAL A 345 ? 0.1515 0.1929 0.1940 -0.0119 -0.0545 0.0606  351 VAL A CG2 
2560 N N   . ARG A 346 ? 0.1128 0.1449 0.1498 0.0056  -0.0447 0.0554  352 ARG A N   
2561 C CA  . ARG A 346 ? 0.1221 0.1512 0.1537 0.0100  -0.0413 0.0527  352 ARG A CA  
2562 C C   . ARG A 346 ? 0.1228 0.1447 0.1485 0.0094  -0.0457 0.0522  352 ARG A C   
2563 O O   . ARG A 346 ? 0.1380 0.1566 0.1549 0.0087  -0.0455 0.0497  352 ARG A O   
2564 C CB  . ARG A 346 ? 0.1420 0.1732 0.1813 0.0175  -0.0363 0.0531  352 ARG A CB  
2565 C CG  . ARG A 346 ? 0.1295 0.1566 0.1632 0.0226  -0.0333 0.0505  352 ARG A CG  
2566 C CD  . ARG A 346 ? 0.1426 0.1723 0.1830 0.0301  -0.0276 0.0507  352 ARG A CD  
2567 N NE  . ARG A 346 ? 0.1426 0.1722 0.1925 0.0330  -0.0292 0.0538  352 ARG A NE  
2568 C CZ  . ARG A 346 ? 0.1603 0.1951 0.2206 0.0348  -0.0271 0.0562  352 ARG A CZ  
2569 N NH1 . ARG A 346 ? 0.1159 0.1566 0.1786 0.0340  -0.0232 0.0560  352 ARG A NH1 
2570 N NH2 . ARG A 346 ? 0.1331 0.1673 0.2017 0.0373  -0.0289 0.0590  352 ARG A NH2 
2571 N N   . LEU A 347 ? 0.1282 0.1477 0.1589 0.0096  -0.0499 0.0547  353 LEU A N   
2572 C CA  . LEU A 347 ? 0.1512 0.1639 0.1769 0.0092  -0.0542 0.0545  353 LEU A CA  
2573 C C   . LEU A 347 ? 0.1661 0.1764 0.1837 0.0021  -0.0587 0.0541  353 LEU A C   
2574 O O   . LEU A 347 ? 0.1934 0.1987 0.2033 0.0013  -0.0603 0.0524  353 LEU A O   
2575 C CB  . LEU A 347 ? 0.1835 0.1943 0.2169 0.0112  -0.0575 0.0573  353 LEU A CB  
2576 C CG  . LEU A 347 ? 0.2533 0.2653 0.2944 0.0188  -0.0534 0.0579  353 LEU A CG  
2577 C CD1 . LEU A 347 ? 0.3090 0.3191 0.3577 0.0203  -0.0571 0.0609  353 LEU A CD1 
2578 C CD2 . LEU A 347 ? 0.3027 0.3109 0.3378 0.0237  -0.0501 0.0551  353 LEU A CD2 
2579 N N   . THR A 348 ? 0.1329 0.1465 0.1521 -0.0030 -0.0608 0.0556  354 THR A N   
2580 C CA  . THR A 348 ? 0.1607 0.1719 0.1727 -0.0096 -0.0652 0.0557  354 THR A CA  
2581 C C   . THR A 348 ? 0.1541 0.1658 0.1571 -0.0120 -0.0627 0.0529  354 THR A C   
2582 O O   . THR A 348 ? 0.1389 0.1462 0.1343 -0.0150 -0.0638 0.0508  354 THR A O   
2583 C CB  . THR A 348 ? 0.1762 0.1901 0.1924 -0.0139 -0.0664 0.0567  354 THR A CB  
2584 O OG1 . THR A 348 ? 0.1787 0.1920 0.2033 -0.0117 -0.0687 0.0591  354 THR A OG1 
2585 C CG2 . THR A 348 ? 0.1825 0.1929 0.1916 -0.0201 -0.0682 0.0550  354 THR A CG2 
2586 N N   . LYS A 349 ? 0.1298 0.1467 0.1340 -0.0106 -0.0577 0.0517  355 LYS A N   
2587 C CA  . LYS A 349 ? 0.1220 0.1403 0.1184 -0.0133 -0.0553 0.0493  355 LYS A CA  
2588 C C   . LYS A 349 ? 0.1185 0.1380 0.1135 -0.0083 -0.0493 0.0466  355 LYS A C   
2589 O O   . LYS A 349 ? 0.1255 0.1425 0.1126 -0.0088 -0.0485 0.0442  355 LYS A O   
2590 C CB  . LYS A 349 ? 0.1201 0.1433 0.1176 -0.0177 -0.0545 0.0497  355 LYS A CB  
2591 C CG  . LYS A 349 ? 0.1562 0.1804 0.1459 -0.0203 -0.0510 0.0465  355 LYS A CG  
2592 C CD  . LYS A 349 ? 0.1609 0.1893 0.1519 -0.0238 -0.0489 0.0460  355 LYS A CD  
2593 C CE  . LYS A 349 ? 0.1946 0.2230 0.1780 -0.0260 -0.0450 0.0425  355 LYS A CE  
2594 N NZ  . LYS A 349 ? 0.2222 0.2537 0.2065 -0.0294 -0.0428 0.0418  355 LYS A NZ  
2595 N N   . SER A 350 ? 0.1154 0.1389 0.1178 -0.0036 -0.0451 0.0469  356 SER A N   
2596 C CA  . SER A 350 ? 0.1120 0.1379 0.1126 0.0002  -0.0390 0.0444  356 SER A CA  
2597 C C   . SER A 350 ? 0.1162 0.1370 0.1116 0.0043  -0.0379 0.0420  356 SER A C   
2598 O O   . SER A 350 ? 0.1160 0.1371 0.1056 0.0053  -0.0344 0.0393  356 SER A O   
2599 C CB  . SER A 350 ? 0.1099 0.1409 0.1200 0.0049  -0.0347 0.0454  356 SER A CB  
2600 O OG  . SER A 350 ? 0.1259 0.1615 0.1414 0.0013  -0.0360 0.0476  356 SER A OG  
2601 N N   . ARG A 351 ? 0.1369 0.1529 0.1340 0.0069  -0.0408 0.0430  357 ARG A N   
2602 C CA  . ARG A 351 ? 0.1925 0.2036 0.1853 0.0117  -0.0394 0.0408  357 ARG A CA  
2603 C C   . ARG A 351 ? 0.2120 0.2190 0.1947 0.0080  -0.0416 0.0386  357 ARG A C   
2604 O O   . ARG A 351 ? 0.1527 0.1584 0.1299 0.0104  -0.0385 0.0358  357 ARG A O   
2605 C CB  . ARG A 351 ? 0.2780 0.2847 0.2752 0.0152  -0.0422 0.0424  357 ARG A CB  
2606 C CG  . ARG A 351 ? 0.3236 0.3337 0.3306 0.0209  -0.0388 0.0440  357 ARG A CG  
2607 C CD  . ARG A 351 ? 0.5095 0.5151 0.5205 0.0251  -0.0412 0.0455  357 ARG A CD  
2608 N NE  . ARG A 351 ? 0.7048 0.7047 0.7100 0.0295  -0.0404 0.0431  357 ARG A NE  
2609 C CZ  . ARG A 351 ? 0.8294 0.8231 0.8277 0.0273  -0.0446 0.0421  357 ARG A CZ  
2610 N NH1 . ARG A 351 ? 0.7927 0.7852 0.7888 0.0208  -0.0498 0.0433  357 ARG A NH1 
2611 N NH2 . ARG A 351 ? 0.8168 0.8053 0.8104 0.0319  -0.0437 0.0399  357 ARG A NH2 
2612 N N   . ASP A 352 ? 0.1453 0.1503 0.1253 0.0020  -0.0469 0.0400  358 ASP A N   
2613 C CA  . ASP A 352 ? 0.2106 0.2110 0.1817 -0.0016 -0.0498 0.0385  358 ASP A CA  
2614 C C   . ASP A 352 ? 0.1734 0.1764 0.1398 -0.0084 -0.0509 0.0385  358 ASP A C   
2615 O O   . ASP A 352 ? 0.1378 0.1378 0.0966 -0.0112 -0.0522 0.0371  358 ASP A O   
2616 C CB  . ASP A 352 ? 0.2335 0.2279 0.2044 -0.0025 -0.0555 0.0400  358 ASP A CB  
2617 N N   . LEU A 353 ? 0.1309 0.1392 0.1016 -0.0110 -0.0503 0.0402  359 LEU A N   
2618 C CA  . LEU A 353 ? 0.1407 0.1516 0.1083 -0.0168 -0.0495 0.0392  359 LEU A CA  
2619 C C   . LEU A 353 ? 0.1462 0.1521 0.1105 -0.0210 -0.0515 0.0377  359 LEU A C   
2620 O O   . LEU A 353 ? 0.1402 0.1462 0.1011 -0.0243 -0.0491 0.0354  359 LEU A O   
2621 C CB  . LEU A 353 ? 0.1284 0.1423 0.0915 -0.0164 -0.0446 0.0365  359 LEU A CB  
2622 C CG  . LEU A 353 ? 0.1328 0.1523 0.1005 -0.0123 -0.0405 0.0371  359 LEU A CG  
2623 C CD1 . LEU A 353 ? 0.1500 0.1711 0.1124 -0.0107 -0.0356 0.0339  359 LEU A CD1 
2624 C CD2 . LEU A 353 ? 0.1452 0.1703 0.1183 -0.0151 -0.0404 0.0392  359 LEU A CD2 
2625 N N   . PHE A 354 ? 0.1348 0.1366 0.1011 -0.0208 -0.0556 0.0394  360 PHE A N   
2626 C CA  . PHE A 354 ? 0.1544 0.1517 0.1185 -0.0246 -0.0578 0.0388  360 PHE A CA  
2627 C C   . PHE A 354 ? 0.1869 0.1807 0.1448 -0.0251 -0.0567 0.0361  360 PHE A C   
2628 O O   . PHE A 354 ? 0.1637 0.1544 0.1198 -0.0287 -0.0576 0.0356  360 PHE A O   
2629 C CB  . PHE A 354 ? 0.1641 0.1633 0.1298 -0.0294 -0.0571 0.0391  360 PHE A CB  
2630 C CG  . PHE A 354 ? 0.1719 0.1748 0.1438 -0.0293 -0.0580 0.0415  360 PHE A CG  
2631 C CD1 . PHE A 354 ? 0.1564 0.1577 0.1332 -0.0278 -0.0618 0.0441  360 PHE A CD1 
2632 C CD2 . PHE A 354 ? 0.1731 0.1809 0.1465 -0.0305 -0.0550 0.0413  360 PHE A CD2 
2633 C CE1 . PHE A 354 ? 0.1607 0.1655 0.1441 -0.0275 -0.0626 0.0464  360 PHE A CE1 
2634 C CE2 . PHE A 354 ? 0.1697 0.1811 0.1494 -0.0304 -0.0559 0.0436  360 PHE A CE2 
2635 C CZ  . PHE A 354 ? 0.1838 0.1937 0.1687 -0.0289 -0.0597 0.0462  360 PHE A CZ  
2636 N N   . VAL A 355 ? 0.1710 0.1647 0.1257 -0.0215 -0.0549 0.0346  361 VAL A N   
2637 C CA  . VAL A 355 ? 0.1699 0.1609 0.1192 -0.0220 -0.0535 0.0318  361 VAL A CA  
2638 C C   . VAL A 355 ? 0.2303 0.2152 0.1781 -0.0231 -0.0572 0.0321  361 VAL A C   
2639 O O   . VAL A 355 ? 0.1933 0.1762 0.1388 -0.0262 -0.0567 0.0308  361 VAL A O   
2640 C CB  . VAL A 355 ? 0.1957 0.1873 0.1417 -0.0174 -0.0513 0.0303  361 VAL A CB  
2641 C CG1 . VAL A 355 ? 0.2177 0.2056 0.1586 -0.0174 -0.0506 0.0275  361 VAL A CG1 
2642 C CG2 . VAL A 355 ? 0.1840 0.1817 0.1307 -0.0172 -0.0469 0.0295  361 VAL A CG2 
2643 N N   . SER A 356 ? 0.2376 0.2194 0.1875 -0.0203 -0.0609 0.0340  362 SER A N   
2644 C CA  . SER A 356 ? 0.2484 0.2242 0.1968 -0.0209 -0.0644 0.0340  362 SER A CA  
2645 C C   . SER A 356 ? 0.2495 0.2243 0.1988 -0.0264 -0.0655 0.0348  362 SER A C   
2646 O O   . SER A 356 ? 0.2465 0.2169 0.1934 -0.0281 -0.0671 0.0342  362 SER A O   
2647 C CB  . SER A 356 ? 0.2968 0.2696 0.2482 -0.0167 -0.0680 0.0360  362 SER A CB  
2648 O OG  . SER A 356 ? 0.3433 0.3184 0.3004 -0.0179 -0.0694 0.0386  362 SER A OG  
2649 N N   . THR A 357 ? 0.2053 0.1838 0.1580 -0.0289 -0.0648 0.0361  363 THR A N   
2650 C CA  . THR A 357 ? 0.2264 0.2033 0.1797 -0.0337 -0.0658 0.0370  363 THR A CA  
2651 C C   . THR A 357 ? 0.2385 0.2148 0.1881 -0.0367 -0.0631 0.0353  363 THR A C   
2652 O O   . THR A 357 ? 0.2167 0.1898 0.1654 -0.0397 -0.0645 0.0359  363 THR A O   
2653 C CB  . THR A 357 ? 0.2686 0.2493 0.2259 -0.0355 -0.0653 0.0387  363 THR A CB  
2654 O OG1 . THR A 357 ? 0.2529 0.2385 0.2098 -0.0360 -0.0611 0.0373  363 THR A OG1 
2655 C CG2 . THR A 357 ? 0.2648 0.2467 0.2270 -0.0323 -0.0679 0.0407  363 THR A CG2 
2656 N N   . SER A 358 ? 0.1619 0.1414 0.1097 -0.0357 -0.0593 0.0332  364 SER A N   
2657 C CA  . SER A 358 ? 0.1965 0.1756 0.1417 -0.0383 -0.0566 0.0317  364 SER A CA  
2658 C C   . SER A 358 ? 0.2191 0.1936 0.1611 -0.0375 -0.0581 0.0307  364 SER A C   
2659 O O   . SER A 358 ? 0.2175 0.1896 0.1583 -0.0404 -0.0582 0.0308  364 SER A O   
2660 C CB  . SER A 358 ? 0.1999 0.1839 0.1448 -0.0375 -0.0519 0.0298  364 SER A CB  
2661 O OG  . SER A 358 ? 0.1718 0.1595 0.1196 -0.0391 -0.0505 0.0308  364 SER A OG  
2662 N N   . TRP A 359 ? 0.2166 0.1898 0.1573 -0.0335 -0.0592 0.0298  365 TRP A N   
2663 C CA  . TRP A 359 ? 0.2211 0.1892 0.1587 -0.0326 -0.0612 0.0288  365 TRP A CA  
2664 C C   . TRP A 359 ? 0.2491 0.2123 0.1875 -0.0347 -0.0654 0.0308  365 TRP A C   
2665 O O   . TRP A 359 ? 0.2282 0.1876 0.1645 -0.0364 -0.0664 0.0305  365 TRP A O   
2666 C CB  . TRP A 359 ? 0.2204 0.1876 0.1564 -0.0274 -0.0618 0.0277  365 TRP A CB  
2667 C CG  . TRP A 359 ? 0.2274 0.1986 0.1616 -0.0254 -0.0575 0.0254  365 TRP A CG  
2668 C CD1 . TRP A 359 ? 0.2220 0.1982 0.1576 -0.0234 -0.0550 0.0254  365 TRP A CD1 
2669 C CD2 . TRP A 359 ? 0.2174 0.1884 0.1487 -0.0254 -0.0551 0.0230  365 TRP A CD2 
2670 N NE1 . TRP A 359 ? 0.2066 0.1854 0.1399 -0.0220 -0.0511 0.0229  365 TRP A NE1 
2671 C CE2 . TRP A 359 ? 0.2164 0.1921 0.1472 -0.0232 -0.0511 0.0214  365 TRP A CE2 
2672 C CE3 . TRP A 359 ? 0.2150 0.1821 0.1442 -0.0270 -0.0559 0.0222  365 TRP A CE3 
2673 C CZ2 . TRP A 359 ? 0.2008 0.1775 0.1294 -0.0225 -0.0479 0.0189  365 TRP A CZ2 
2674 C CZ3 . TRP A 359 ? 0.1970 0.1652 0.1242 -0.0264 -0.0529 0.0198  365 TRP A CZ3 
2675 C CH2 . TRP A 359 ? 0.2120 0.1851 0.1390 -0.0241 -0.0489 0.0181  365 TRP A CH2 
2676 N N   . LYS A 360 ? 0.2183 0.1816 0.1597 -0.0347 -0.0678 0.0328  366 LYS A N   
2677 C CA  . LYS A 360 ? 0.2645 0.2233 0.2069 -0.0369 -0.0716 0.0347  366 LYS A CA  
2678 C C   . LYS A 360 ? 0.2581 0.2167 0.2001 -0.0418 -0.0705 0.0355  366 LYS A C   
2679 O O   . LYS A 360 ? 0.2611 0.2154 0.2015 -0.0437 -0.0724 0.0359  366 LYS A O   
2680 C CB  . LYS A 360 ? 0.2451 0.2047 0.1916 -0.0358 -0.0741 0.0368  366 LYS A CB  
2681 C CG  . LYS A 360 ? 0.3269 0.2820 0.2747 -0.0380 -0.0781 0.0388  366 LYS A CG  
2682 N N   . THR A 361 ? 0.2216 0.1846 0.1650 -0.0437 -0.0676 0.0358  367 THR A N   
2683 C CA  . THR A 361 ? 0.2377 0.2005 0.1805 -0.0479 -0.0663 0.0366  367 THR A CA  
2684 C C   . THR A 361 ? 0.2689 0.2298 0.2088 -0.0489 -0.0649 0.0353  367 THR A C   
2685 O O   . THR A 361 ? 0.2673 0.2249 0.2062 -0.0518 -0.0662 0.0365  367 THR A O   
2686 C CB  . THR A 361 ? 0.2347 0.2028 0.1792 -0.0491 -0.0628 0.0365  367 THR A CB  
2687 O OG1 . THR A 361 ? 0.2330 0.2022 0.1805 -0.0488 -0.0647 0.0382  367 THR A OG1 
2688 C CG2 . THR A 361 ? 0.2357 0.2037 0.1794 -0.0529 -0.0610 0.0371  367 THR A CG2 
2689 N N   . MET A 362 ? 0.2321 0.1949 0.1705 -0.0464 -0.0624 0.0330  368 MET A N   
2690 C CA  . MET A 362 ? 0.2541 0.2157 0.1901 -0.0470 -0.0608 0.0317  368 MET A CA  
2691 C C   . MET A 362 ? 0.2607 0.2167 0.1946 -0.0460 -0.0642 0.0315  368 MET A C   
2692 O O   . MET A 362 ? 0.2601 0.2143 0.1920 -0.0466 -0.0635 0.0306  368 MET A O   
2693 C CB  . MET A 362 ? 0.2245 0.1903 0.1599 -0.0446 -0.0569 0.0292  368 MET A CB  
2694 C CG  . MET A 362 ? 0.1902 0.1613 0.1276 -0.0458 -0.0531 0.0292  368 MET A CG  
2695 S SD  . MET A 362 ? 0.2606 0.2315 0.1982 -0.0504 -0.0512 0.0302  368 MET A SD  
2696 C CE  . MET A 362 ? 0.2274 0.1990 0.1632 -0.0491 -0.0482 0.0278  368 MET A CE  
2697 N N   . ARG A 363 ? 0.2321 0.1853 0.1667 -0.0442 -0.0680 0.0323  369 ARG A N   
2698 C CA  . ARG A 363 ? 0.3193 0.2665 0.2521 -0.0429 -0.0717 0.0321  369 ARG A CA  
2699 C C   . ARG A 363 ? 0.3436 0.2903 0.2737 -0.0400 -0.0704 0.0296  369 ARG A C   
2700 O O   . ARG A 363 ? 0.3172 0.2597 0.2452 -0.0404 -0.0718 0.0290  369 ARG A O   
2701 C CB  . ARG A 363 ? 0.3561 0.2992 0.2884 -0.0468 -0.0738 0.0339  369 ARG A CB  
2702 C CG  . ARG A 363 ? 0.3844 0.3266 0.3191 -0.0489 -0.0761 0.0364  369 ARG A CG  
2703 C CD  . ARG A 363 ? 0.4560 0.3958 0.3902 -0.0533 -0.0768 0.0383  369 ARG A CD  
2704 N NE  . ARG A 363 ? 0.5764 0.5103 0.5091 -0.0538 -0.0802 0.0388  369 ARG A NE  
2705 N N   . GLN A 364 ? 0.2721 0.2230 0.2023 -0.0369 -0.0678 0.0280  370 GLN A N   
2706 C CA  . GLN A 364 ? 0.2779 0.2286 0.2054 -0.0337 -0.0664 0.0254  370 GLN A CA  
2707 C C   . GLN A 364 ? 0.2977 0.2488 0.2251 -0.0289 -0.0672 0.0248  370 GLN A C   
2708 O O   . GLN A 364 ? 0.2744 0.2275 0.2043 -0.0284 -0.0678 0.0263  370 GLN A O   
2709 C CB  . GLN A 364 ? 0.2571 0.2128 0.1844 -0.0345 -0.0614 0.0239  370 GLN A CB  
2710 C CG  . GLN A 364 ? 0.2334 0.1883 0.1604 -0.0384 -0.0603 0.0243  370 GLN A CG  
2711 C CD  . GLN A 364 ? 0.2577 0.2176 0.1850 -0.0385 -0.0555 0.0227  370 GLN A CD  
2712 O OE1 . GLN A 364 ? 0.2304 0.1919 0.1564 -0.0353 -0.0537 0.0205  370 GLN A OE1 
2713 N NE2 . GLN A 364 ? 0.2251 0.1872 0.1540 -0.0420 -0.0534 0.0239  370 GLN A NE2 
2714 N N   . SER A 365 ? 0.3111 0.2600 0.2355 -0.0253 -0.0672 0.0227  371 SER A N   
2715 C CA  . SER A 365 ? 0.3184 0.2670 0.2419 -0.0201 -0.0676 0.0221  371 SER A CA  
2716 C C   . SER A 365 ? 0.2889 0.2421 0.2109 -0.0180 -0.0632 0.0200  371 SER A C   
2717 O O   . SER A 365 ? 0.2935 0.2473 0.2136 -0.0187 -0.0609 0.0181  371 SER A O   
2718 C CB  . SER A 365 ? 0.3772 0.3185 0.2980 -0.0166 -0.0713 0.0212  371 SER A CB  
2719 O OG  . SER A 365 ? 0.4094 0.3466 0.3321 -0.0179 -0.0755 0.0232  371 SER A OG  
2720 N N   . PRO A 366 ? 0.3041 0.2609 0.2272 -0.0152 -0.0618 0.0205  372 PRO A N   
2721 C CA  . PRO A 366 ? 0.3074 0.2691 0.2292 -0.0135 -0.0572 0.0186  372 PRO A CA  
2722 C C   . PRO A 366 ? 0.3672 0.3253 0.2846 -0.0092 -0.0569 0.0161  372 PRO A C   
2723 O O   . PRO A 366 ? 0.3778 0.3295 0.2931 -0.0059 -0.0603 0.0159  372 PRO A O   
2724 C CB  . PRO A 366 ? 0.3377 0.3029 0.2619 -0.0112 -0.0567 0.0204  372 PRO A CB  
2725 C CG  . PRO A 366 ? 0.3107 0.2718 0.2370 -0.0102 -0.0612 0.0227  372 PRO A CG  
2726 C CD  . PRO A 366 ? 0.2743 0.2313 0.2005 -0.0139 -0.0641 0.0230  372 PRO A CD  
2727 N N   . PRO A 367 ? 0.3538 0.3154 0.2697 -0.0090 -0.0527 0.0138  373 PRO A N   
2728 C CA  . PRO A 367 ? 0.3991 0.3573 0.3108 -0.0048 -0.0520 0.0112  373 PRO A CA  
2729 C C   . PRO A 367 ? 0.5137 0.4711 0.4232 0.0013  -0.0511 0.0108  373 PRO A C   
2730 O O   . PRO A 367 ? 0.5504 0.5118 0.4622 0.0018  -0.0501 0.0125  373 PRO A O   
2731 C CB  . PRO A 367 ? 0.3812 0.3447 0.2936 -0.0072 -0.0476 0.0093  373 PRO A CB  
2732 C CG  . PRO A 367 ? 0.3447 0.3152 0.2609 -0.0100 -0.0448 0.0107  373 PRO A CG  
2733 C CD  . PRO A 367 ? 0.3206 0.2892 0.2392 -0.0124 -0.0485 0.0135  373 PRO A CD  
2734 O OXT . PRO A 367 ? 0.6616 0.6141 0.5671 0.0064  -0.0512 0.0087  373 PRO A OXT 
# 
